data_9EIX
# 
_entry.id   9EIX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EIX         pdb_00009eix 10.2210/pdb9eix/pdb 
WWPDB D_1000290522 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EIX 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-27 
_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_contact_author.id                 2 
_pdbx_contact_author.email              ret6@cornell.edu 
_pdbx_contact_author.name_first         Robert 
_pdbx_contact_author.name_last          Thorne 
_pdbx_contact_author.name_mi            E 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7489-8074 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McLeod, M.J.'    1 0000-0001-5540-916X 
'Barwell, S.A.E.' 2 0000-0002-5703-5525 
'Holyoak, T.'     3 0000-0002-7329-1115 
'Thorne, R.E.'    4 0000-0002-7489-8074 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'A structural perspective on the temperature dependent activity of enzymes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2025.02.013 
_citation.pdbx_database_id_PubMed   40120576 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McLeod, M.J.'    1 ? 
primary 'Barwell, S.A.E.' 2 ? 
primary 'Holyoak, T.'     3 ? 
primary 'Thorne, R.E.'    4 ? 
# 
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 'Phosphoenolpyruvate carboxykinase, cytosolic [GTP]' 69499.664 1  4.1.1.32 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                                 54.938    3  ?        ? ? ? 
3 non-polymer syn '2-PHOSPHOGLYCOLIC ACID'                             156.031   1  ?        ? ? ? 
4 non-polymer syn "GUANOSINE-5'-DIPHOSPHATE"                           443.201   1  ?        ? ? ? 
5 water       nat water                                                18.015    15 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        PEPCK-C 
# 
_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       
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_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 'MANGANESE (II) ION'       MN  
3 '2-PHOSPHOGLYCOLIC ACID'   PGA 
4 "GUANOSINE-5'-DIPHOSPHATE" GDP 
5 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   PRO n 
1 4   GLN n 
1 5   LEU n 
1 6   HIS n 
1 7   ASN n 
1 8   GLY n 
1 9   LEU n 
1 10  ASP n 
1 11  PHE n 
1 12  SER n 
1 13  ALA n 
1 14  LYS n 
1 15  VAL n 
1 16  ILE n 
1 17  GLN n 
1 18  GLY n 
1 19  SER n 
1 20  LEU n 
1 21  ASP n 
1 22  SER n 
1 23  LEU n 
1 24  PRO n 
1 25  GLN n 
1 26  GLU n 
1 27  VAL n 
1 28  ARG n 
1 29  LYS n 
1 30  PHE n 
1 31  VAL n 
1 32  GLU n 
1 33  GLY n 
1 34  ASN n 
1 35  ALA n 
1 36  GLN n 
1 37  LEU n 
1 38  CYS n 
1 39  GLN n 
1 40  PRO n 
1 41  GLU n 
1 42  TYR n 
1 43  ILE n 
1 44  HIS n 
1 45  ILE n 
1 46  CYS n 
1 47  ASP n 
1 48  GLY n 
1 49  SER n 
1 50  GLU n 
1 51  GLU n 
1 52  GLU n 
1 53  TYR n 
1 54  GLY n 
1 55  ARG n 
1 56  LEU n 
1 57  LEU n 
1 58  ALA n 
1 59  HIS n 
1 60  MET n 
1 61  GLN n 
1 62  GLU n 
1 63  GLU n 
1 64  GLY n 
1 65  VAL n 
1 66  ILE n 
1 67  ARG n 
1 68  LYS n 
1 69  LEU n 
1 70  LYS n 
1 71  LYS n 
1 72  TYR n 
1 73  ASP n 
1 74  ASN n 
1 75  CYS n 
1 76  TRP n 
1 77  LEU n 
1 78  ALA n 
1 79  LEU n 
1 80  THR n 
1 81  ASP n 
1 82  PRO n 
1 83  ARG n 
1 84  ASP n 
1 85  VAL n 
1 86  ALA n 
1 87  ARG n 
1 88  ILE n 
1 89  GLU n 
1 90  SER n 
1 91  LYS n 
1 92  THR n 
1 93  VAL n 
1 94  ILE n 
1 95  ILE n 
1 96  THR n 
1 97  GLN n 
1 98  GLU n 
1 99  GLN n 
1 100 ARG n 
1 101 ASP n 
1 102 THR n 
1 103 VAL n 
1 104 PRO n 
1 105 ILE n 
1 106 PRO n 
1 107 LYS n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 SER n 
1 112 GLN n 
1 113 LEU n 
1 114 GLY n 
1 115 ARG n 
1 116 TRP n 
1 117 MET n 
1 118 SER n 
1 119 GLU n 
1 120 GLU n 
1 121 ASP n 
1 122 PHE n 
1 123 GLU n 
1 124 LYS n 
1 125 ALA n 
1 126 PHE n 
1 127 ASN n 
1 128 ALA n 
1 129 ARG n 
1 130 PHE n 
1 131 PRO n 
1 132 GLY n 
1 133 CYS n 
1 134 MET n 
1 135 LYS n 
1 136 GLY n 
1 137 ARG n 
1 138 THR n 
1 139 MET n 
1 140 TYR n 
1 141 VAL n 
1 142 ILE n 
1 143 PRO n 
1 144 PHE n 
1 145 SER n 
1 146 MET n 
1 147 GLY n 
1 148 PRO n 
1 149 LEU n 
1 150 GLY n 
1 151 SER n 
1 152 PRO n 
1 153 LEU n 
1 154 ALA n 
1 155 LYS n 
1 156 ILE n 
1 157 GLY n 
1 158 ILE n 
1 159 GLU n 
1 160 LEU n 
1 161 THR n 
1 162 ASP n 
1 163 SER n 
1 164 PRO n 
1 165 TYR n 
1 166 VAL n 
1 167 VAL n 
1 168 ALA n 
1 169 SER n 
1 170 MET n 
1 171 ARG n 
1 172 ILE n 
1 173 MET n 
1 174 THR n 
1 175 ARG n 
1 176 MET n 
1 177 GLY n 
1 178 THR n 
1 179 SER n 
1 180 VAL n 
1 181 LEU n 
1 182 GLU n 
1 183 ALA n 
1 184 LEU n 
1 185 GLY n 
1 186 ASP n 
1 187 GLY n 
1 188 GLU n 
1 189 PHE n 
1 190 ILE n 
1 191 LYS n 
1 192 CYS n 
1 193 LEU n 
1 194 HIS n 
1 195 SER n 
1 196 VAL n 
1 197 GLY n 
1 198 CYS n 
1 199 PRO n 
1 200 LEU n 
1 201 PRO n 
1 202 LEU n 
1 203 LYS n 
1 204 LYS n 
1 205 PRO n 
1 206 LEU n 
1 207 VAL n 
1 208 ASN n 
1 209 ASN n 
1 210 TRP n 
1 211 ALA n 
1 212 CYS n 
1 213 ASN n 
1 214 PRO n 
1 215 GLU n 
1 216 LEU n 
1 217 THR n 
1 218 LEU n 
1 219 ILE n 
1 220 ALA n 
1 221 HIS n 
1 222 LEU n 
1 223 PRO n 
1 224 ASP n 
1 225 ARG n 
1 226 ARG n 
1 227 GLU n 
1 228 ILE n 
1 229 ILE n 
1 230 SER n 
1 231 PHE n 
1 232 GLY n 
1 233 SER n 
1 234 GLY n 
1 235 TYR n 
1 236 GLY n 
1 237 GLY n 
1 238 ASN n 
1 239 SER n 
1 240 LEU n 
1 241 LEU n 
1 242 GLY n 
1 243 LYS n 
1 244 LYS n 
1 245 CYS n 
1 246 PHE n 
1 247 ALA n 
1 248 LEU n 
1 249 ARG n 
1 250 ILE n 
1 251 ALA n 
1 252 SER n 
1 253 ARG n 
1 254 LEU n 
1 255 ALA n 
1 256 LYS n 
1 257 GLU n 
1 258 GLU n 
1 259 GLY n 
1 260 TRP n 
1 261 LEU n 
1 262 ALA n 
1 263 GLU n 
1 264 HIS n 
1 265 MET n 
1 266 LEU n 
1 267 ILE n 
1 268 LEU n 
1 269 GLY n 
1 270 ILE n 
1 271 THR n 
1 272 ASN n 
1 273 PRO n 
1 274 GLU n 
1 275 GLY n 
1 276 LYS n 
1 277 LYS n 
1 278 LYS n 
1 279 TYR n 
1 280 LEU n 
1 281 ALA n 
1 282 ALA n 
1 283 ALA n 
1 284 PHE n 
1 285 PRO n 
1 286 SER n 
1 287 ALA n 
1 288 CYS n 
1 289 GLY n 
1 290 LYS n 
1 291 THR n 
1 292 ASN n 
1 293 LEU n 
1 294 ALA n 
1 295 MET n 
1 296 MET n 
1 297 ASN n 
1 298 PRO n 
1 299 THR n 
1 300 LEU n 
1 301 PRO n 
1 302 GLY n 
1 303 TRP n 
1 304 LYS n 
1 305 VAL n 
1 306 GLU n 
1 307 CYS n 
1 308 VAL n 
1 309 GLY n 
1 310 ASP n 
1 311 ASP n 
1 312 ILE n 
1 313 ALA n 
1 314 TRP n 
1 315 MET n 
1 316 LYS n 
1 317 PHE n 
1 318 ASP n 
1 319 ALA n 
1 320 GLN n 
1 321 GLY n 
1 322 ASN n 
1 323 LEU n 
1 324 ARG n 
1 325 ALA n 
1 326 ILE n 
1 327 ASN n 
1 328 PRO n 
1 329 GLU n 
1 330 ASN n 
1 331 GLY n 
1 332 PHE n 
1 333 PHE n 
1 334 GLY n 
1 335 VAL n 
1 336 ALA n 
1 337 PRO n 
1 338 GLY n 
1 339 THR n 
1 340 SER n 
1 341 VAL n 
1 342 LYS n 
1 343 THR n 
1 344 ASN n 
1 345 PRO n 
1 346 ASN n 
1 347 ALA n 
1 348 ILE n 
1 349 LYS n 
1 350 THR n 
1 351 ILE n 
1 352 GLN n 
1 353 LYS n 
1 354 ASN n 
1 355 THR n 
1 356 ILE n 
1 357 PHE n 
1 358 THR n 
1 359 ASN n 
1 360 VAL n 
1 361 ALA n 
1 362 GLU n 
1 363 THR n 
1 364 SER n 
1 365 ASP n 
1 366 GLY n 
1 367 GLY n 
1 368 VAL n 
1 369 TYR n 
1 370 TRP n 
1 371 GLU n 
1 372 GLY n 
1 373 ILE n 
1 374 ASP n 
1 375 GLU n 
1 376 PRO n 
1 377 LEU n 
1 378 ALA n 
1 379 PRO n 
1 380 GLY n 
1 381 VAL n 
1 382 THR n 
1 383 ILE n 
1 384 THR n 
1 385 SER n 
1 386 TRP n 
1 387 LYS n 
1 388 ASN n 
1 389 LYS n 
1 390 GLU n 
1 391 TRP n 
1 392 ARG n 
1 393 PRO n 
1 394 GLN n 
1 395 ASP n 
1 396 GLU n 
1 397 GLU n 
1 398 PRO n 
1 399 CYS n 
1 400 ALA n 
1 401 HIS n 
1 402 PRO n 
1 403 ASN n 
1 404 SER n 
1 405 ARG n 
1 406 PHE n 
1 407 CYS n 
1 408 THR n 
1 409 PRO n 
1 410 ALA n 
1 411 SER n 
1 412 GLN n 
1 413 CYS n 
1 414 PRO n 
1 415 ILE n 
1 416 ILE n 
1 417 ASP n 
1 418 PRO n 
1 419 ALA n 
1 420 TRP n 
1 421 GLU n 
1 422 SER n 
1 423 PRO n 
1 424 GLU n 
1 425 GLY n 
1 426 VAL n 
1 427 PRO n 
1 428 ILE n 
1 429 GLU n 
1 430 GLY n 
1 431 ILE n 
1 432 ILE n 
1 433 PHE n 
1 434 GLY n 
1 435 GLY n 
1 436 ARG n 
1 437 ARG n 
1 438 PRO n 
1 439 ALA n 
1 440 GLY n 
1 441 VAL n 
1 442 PRO n 
1 443 LEU n 
1 444 VAL n 
1 445 TYR n 
1 446 GLU n 
1 447 ALA n 
1 448 LEU n 
1 449 SER n 
1 450 TRP n 
1 451 GLN n 
1 452 HIS n 
1 453 GLY n 
1 454 VAL n 
1 455 PHE n 
1 456 VAL n 
1 457 GLY n 
1 458 ALA n 
1 459 ALA n 
1 460 MET n 
1 461 ARG n 
1 462 SER n 
1 463 GLU n 
1 464 ALA n 
1 465 THR n 
1 466 ALA n 
1 467 ALA n 
1 468 ALA n 
1 469 GLU n 
1 470 HIS n 
1 471 LYS n 
1 472 GLY n 
1 473 LYS n 
1 474 VAL n 
1 475 ILE n 
1 476 MET n 
1 477 HIS n 
1 478 ASP n 
1 479 PRO n 
1 480 PHE n 
1 481 ALA n 
1 482 MET n 
1 483 ARG n 
1 484 PRO n 
1 485 PHE n 
1 486 PHE n 
1 487 GLY n 
1 488 TYR n 
1 489 ASN n 
1 490 PHE n 
1 491 GLY n 
1 492 LYS n 
1 493 TYR n 
1 494 LEU n 
1 495 ALA n 
1 496 HIS n 
1 497 TRP n 
1 498 LEU n 
1 499 SER n 
1 500 MET n 
1 501 ALA n 
1 502 HIS n 
1 503 ARG n 
1 504 PRO n 
1 505 ALA n 
1 506 ALA n 
1 507 LYS n 
1 508 LEU n 
1 509 PRO n 
1 510 LYS n 
1 511 ILE n 
1 512 PHE n 
1 513 HIS n 
1 514 VAL n 
1 515 ASN n 
1 516 TRP n 
1 517 PHE n 
1 518 ARG n 
1 519 LYS n 
1 520 ASP n 
1 521 LYS n 
1 522 ASN n 
1 523 GLY n 
1 524 LYS n 
1 525 PHE n 
1 526 LEU n 
1 527 TRP n 
1 528 PRO n 
1 529 GLY n 
1 530 PHE n 
1 531 GLY n 
1 532 GLU n 
1 533 ASN n 
1 534 SER n 
1 535 ARG n 
1 536 VAL n 
1 537 LEU n 
1 538 GLU n 
1 539 TRP n 
1 540 MET n 
1 541 PHE n 
1 542 GLY n 
1 543 ARG n 
1 544 ILE n 
1 545 GLU n 
1 546 GLY n 
1 547 GLU n 
1 548 ASP n 
1 549 SER n 
1 550 ALA n 
1 551 LYS n 
1 552 LEU n 
1 553 THR n 
1 554 PRO n 
1 555 ILE n 
1 556 GLY n 
1 557 TYR n 
1 558 VAL n 
1 559 PRO n 
1 560 LYS n 
1 561 GLU n 
1 562 ASP n 
1 563 ALA n 
1 564 LEU n 
1 565 ASN n 
1 566 LEU n 
1 567 LYS n 
1 568 GLY n 
1 569 LEU n 
1 570 GLY n 
1 571 ASP n 
1 572 VAL n 
1 573 ASN n 
1 574 VAL n 
1 575 GLU n 
1 576 GLU n 
1 577 LEU n 
1 578 PHE n 
1 579 GLY n 
1 580 ILE n 
1 581 SER n 
1 582 LYS n 
1 583 GLU n 
1 584 PHE n 
1 585 TRP n 
1 586 GLU n 
1 587 LYS n 
1 588 GLU n 
1 589 VAL n 
1 590 GLU n 
1 591 GLU n 
1 592 ILE n 
1 593 ASP n 
1 594 LYS n 
1 595 TYR n 
1 596 LEU n 
1 597 GLU n 
1 598 ASP n 
1 599 GLN n 
1 600 VAL n 
1 601 ASN n 
1 602 ALA n 
1 603 ASP n 
1 604 LEU n 
1 605 PRO n 
1 606 TYR n 
1 607 GLU n 
1 608 ILE n 
1 609 GLU n 
1 610 ARG n 
1 611 GLU n 
1 612 LEU n 
1 613 ARG n 
1 614 ALA n 
1 615 LEU n 
1 616 LYS n 
1 617 GLN n 
1 618 ARG n 
1 619 ILE n 
1 620 SER n 
1 621 GLN n 
1 622 MET 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                   622 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Pck1 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_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 
GDP 'RNA linking'       n "GUANOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O11 P2' 443.201 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                      ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'     149.211 
MN  non-polymer         . 'MANGANESE (II) ION'       ? 'Mn 2'              54.938  
PGA non-polymer         . '2-PHOSPHOGLYCOLIC ACID'   ? 'C2 H5 O6 P'        156.031 
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   PRO 2   2   ?   ?   ?   A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   GLN 4   4   4   GLN GLN A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   HIS 6   6   6   HIS HIS A . n 
A 1 7   ASN 7   7   7   ASN ASN A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  LYS 14  14  14  LYS LYS A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  SER 19  19  19  SER SER A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  VAL 27  27  27  VAL VAL A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  ASN 34  34  34  ASN ASN A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  CYS 46  46  46  CYS CYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  TYR 53  53  53  TYR TYR A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  HIS 59  59  59  HIS HIS A . n 
A 1 60  MET 60  60  60  MET MET A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  ASP 73  73  73  ASP ASP A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  CYS 75  75  75  CYS CYS A . n 
A 1 76  TRP 76  76  76  TRP TRP A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  PRO 82  82  82  PRO PRO A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  ILE 88  88  88  ILE ILE A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  GLU 98  98  98  GLU GLU A . n 
A 1 99  GLN 99  99  99  GLN GLN A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 TRP 116 116 116 TRP TRP A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 CYS 133 133 133 CYS CYS A . n 
A 1 134 MET 134 134 134 MET MET A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 ARG 137 137 137 ARG ARG A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 MET 139 139 139 MET MET A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 MET 146 146 146 MET MET A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 MET 170 170 170 MET MET A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 ARG 175 175 175 ARG ARG A . n 
A 1 176 MET 176 176 176 MET MET A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 ASP 186 186 186 ASP ASP A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ILE 190 190 190 ILE ILE A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 CYS 192 192 192 CYS CYS A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 HIS 194 194 194 HIS HIS A . n 
A 1 195 SER 195 195 195 SER SER A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 CYS 198 198 198 CYS CYS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 TRP 210 210 210 TRP TRP A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 CYS 212 212 212 CYS CYS A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 GLU 215 215 215 GLU GLU A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 ILE 228 228 228 ILE ILE A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 SER 230 230 230 SER SER 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 SER 233 233 233 SER SER A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 GLY 237 237 237 GLY GLY A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 CYS 245 245 245 CYS CYS A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 GLU 257 257 257 GLU GLU A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 TRP 260 260 260 TRP TRP A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 MET 265 265 265 MET MET A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 PRO 273 273 273 PRO PRO A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 PRO 285 285 285 PRO PRO A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 CYS 288 288 288 CYS CYS A . n 
A 1 289 GLY 289 289 289 GLY GLY A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 THR 291 291 291 THR THR A . n 
A 1 292 ASN 292 292 292 ASN ASN A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 MET 296 296 296 MET MET A . n 
A 1 297 ASN 297 297 297 ASN ASN A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 CYS 307 307 307 CYS CYS A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 ASP 311 311 311 ASP ASP A . n 
A 1 312 ILE 312 312 312 ILE ILE A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 TRP 314 314 314 TRP TRP A . n 
A 1 315 MET 315 315 315 MET MET A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 GLN 320 320 320 GLN GLN A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 LEU 323 323 323 LEU LEU A . n 
A 1 324 ARG 324 324 324 ARG ARG A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 PRO 328 328 328 PRO PRO A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 ASN 330 330 330 ASN ASN A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 PHE 332 332 332 PHE PHE A . n 
A 1 333 PHE 333 333 333 PHE PHE A . n 
A 1 334 GLY 334 334 334 GLY GLY A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 ALA 336 336 336 ALA ALA A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 THR 339 339 339 THR THR A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 LYS 342 342 342 LYS LYS A . n 
A 1 343 THR 343 343 343 THR THR A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 ASN 346 346 346 ASN ASN A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 ILE 348 348 348 ILE ILE A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 THR 350 350 350 THR THR A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 GLN 352 352 352 GLN GLN A . n 
A 1 353 LYS 353 353 353 LYS LYS A . n 
A 1 354 ASN 354 354 354 ASN ASN A . n 
A 1 355 THR 355 355 355 THR THR A . n 
A 1 356 ILE 356 356 356 ILE ILE A . n 
A 1 357 PHE 357 357 357 PHE PHE A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 ASN 359 359 359 ASN ASN A . n 
A 1 360 VAL 360 360 360 VAL VAL A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 THR 363 363 363 THR THR A . n 
A 1 364 SER 364 364 364 SER SER A . n 
A 1 365 ASP 365 365 365 ASP ASP A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 TYR 369 369 369 TYR TYR A . n 
A 1 370 TRP 370 370 370 TRP TRP A . n 
A 1 371 GLU 371 371 371 GLU GLU A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 ILE 373 373 373 ILE ILE A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 GLU 375 375 375 GLU GLU A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 LEU 377 377 377 LEU LEU A . n 
A 1 378 ALA 378 378 378 ALA ALA A . n 
A 1 379 PRO 379 379 379 PRO PRO A . n 
A 1 380 GLY 380 380 380 GLY GLY A . n 
A 1 381 VAL 381 381 381 VAL VAL A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 ILE 383 383 383 ILE ILE A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 SER 385 385 385 SER SER A . n 
A 1 386 TRP 386 386 386 TRP TRP A . n 
A 1 387 LYS 387 387 387 LYS LYS A . n 
A 1 388 ASN 388 388 388 ASN ASN A . n 
A 1 389 LYS 389 389 389 LYS LYS A . n 
A 1 390 GLU 390 390 390 GLU GLU A . n 
A 1 391 TRP 391 391 391 TRP TRP A . n 
A 1 392 ARG 392 392 392 ARG ARG A . n 
A 1 393 PRO 393 393 393 PRO PRO A . n 
A 1 394 GLN 394 394 394 GLN GLN A . n 
A 1 395 ASP 395 395 395 ASP ASP A . n 
A 1 396 GLU 396 396 396 GLU GLU A . n 
A 1 397 GLU 397 397 397 GLU GLU A . n 
A 1 398 PRO 398 398 398 PRO PRO A . n 
A 1 399 CYS 399 399 399 CYS CYS A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 HIS 401 401 401 HIS HIS A . n 
A 1 402 PRO 402 402 402 PRO PRO A . n 
A 1 403 ASN 403 403 403 ASN ASN A . n 
A 1 404 SER 404 404 404 SER SER A . n 
A 1 405 ARG 405 405 405 ARG ARG A . n 
A 1 406 PHE 406 406 406 PHE PHE A . n 
A 1 407 CYS 407 407 407 CYS CYS A . n 
A 1 408 THR 408 408 408 THR THR A . n 
A 1 409 PRO 409 409 409 PRO PRO A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 SER 411 411 411 SER SER A . n 
A 1 412 GLN 412 412 412 GLN GLN A . n 
A 1 413 CYS 413 413 413 CYS CYS A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 ILE 415 415 415 ILE ILE A . n 
A 1 416 ILE 416 416 416 ILE ILE A . n 
A 1 417 ASP 417 417 417 ASP ASP A . n 
A 1 418 PRO 418 418 418 PRO PRO A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 TRP 420 420 420 TRP TRP A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 SER 422 422 422 SER SER A . n 
A 1 423 PRO 423 423 423 PRO PRO A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 GLY 425 425 425 GLY GLY A . n 
A 1 426 VAL 426 426 426 VAL VAL A . n 
A 1 427 PRO 427 427 427 PRO PRO A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 GLU 429 429 429 GLU GLU A . n 
A 1 430 GLY 430 430 430 GLY GLY A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ILE 432 432 432 ILE ILE A . n 
A 1 433 PHE 433 433 433 PHE PHE A . n 
A 1 434 GLY 434 434 434 GLY GLY A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 ARG 436 436 436 ARG ARG A . n 
A 1 437 ARG 437 437 437 ARG ARG A . n 
A 1 438 PRO 438 438 438 PRO PRO A . n 
A 1 439 ALA 439 439 439 ALA ALA A . n 
A 1 440 GLY 440 440 440 GLY GLY A . n 
A 1 441 VAL 441 441 441 VAL VAL A . n 
A 1 442 PRO 442 442 442 PRO PRO A . n 
A 1 443 LEU 443 443 443 LEU LEU A . n 
A 1 444 VAL 444 444 444 VAL VAL A . n 
A 1 445 TYR 445 445 445 TYR TYR A . n 
A 1 446 GLU 446 446 446 GLU GLU A . n 
A 1 447 ALA 447 447 447 ALA ALA A . n 
A 1 448 LEU 448 448 448 LEU LEU A . n 
A 1 449 SER 449 449 449 SER SER A . n 
A 1 450 TRP 450 450 450 TRP TRP A . n 
A 1 451 GLN 451 451 451 GLN GLN A . n 
A 1 452 HIS 452 452 452 HIS HIS A . n 
A 1 453 GLY 453 453 453 GLY GLY A . n 
A 1 454 VAL 454 454 454 VAL VAL A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 VAL 456 456 456 VAL VAL A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 ALA 459 459 459 ALA ALA A . n 
A 1 460 MET 460 460 460 MET MET A . n 
A 1 461 ARG 461 461 461 ARG ARG A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 GLU 463 463 463 GLU GLU A . n 
A 1 464 ALA 464 464 464 ALA ALA A . n 
A 1 465 THR 465 465 465 THR THR A . n 
A 1 466 ALA 466 466 466 ALA ALA A . n 
A 1 467 ALA 467 467 467 ALA ALA A . n 
A 1 468 ALA 468 468 468 ALA ALA A . n 
A 1 469 GLU 469 469 469 GLU GLU A . n 
A 1 470 HIS 470 470 470 HIS HIS A . n 
A 1 471 LYS 471 471 471 LYS LYS A . n 
A 1 472 GLY 472 472 472 GLY GLY A . n 
A 1 473 LYS 473 473 473 LYS LYS A . n 
A 1 474 VAL 474 474 474 VAL VAL A . n 
A 1 475 ILE 475 475 475 ILE ILE A . n 
A 1 476 MET 476 476 476 MET MET A . n 
A 1 477 HIS 477 477 477 HIS HIS A . n 
A 1 478 ASP 478 478 478 ASP ASP A . n 
A 1 479 PRO 479 479 479 PRO PRO A . n 
A 1 480 PHE 480 480 480 PHE PHE A . n 
A 1 481 ALA 481 481 481 ALA ALA A . n 
A 1 482 MET 482 482 482 MET MET A . n 
A 1 483 ARG 483 483 483 ARG ARG A . n 
A 1 484 PRO 484 484 484 PRO PRO A . n 
A 1 485 PHE 485 485 485 PHE PHE A . n 
A 1 486 PHE 486 486 486 PHE PHE A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 TYR 488 488 488 TYR TYR A . n 
A 1 489 ASN 489 489 489 ASN ASN A . n 
A 1 490 PHE 490 490 490 PHE PHE A . n 
A 1 491 GLY 491 491 491 GLY GLY A . n 
A 1 492 LYS 492 492 492 LYS LYS A . n 
A 1 493 TYR 493 493 493 TYR TYR A . n 
A 1 494 LEU 494 494 494 LEU LEU A . n 
A 1 495 ALA 495 495 495 ALA ALA A . n 
A 1 496 HIS 496 496 496 HIS HIS A . n 
A 1 497 TRP 497 497 497 TRP TRP A . n 
A 1 498 LEU 498 498 498 LEU LEU A . n 
A 1 499 SER 499 499 499 SER SER A . n 
A 1 500 MET 500 500 500 MET MET A . n 
A 1 501 ALA 501 501 501 ALA ALA A . n 
A 1 502 HIS 502 502 502 HIS HIS A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 PRO 504 504 504 PRO PRO A . n 
A 1 505 ALA 505 505 505 ALA ALA A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 LYS 507 507 507 LYS LYS A . n 
A 1 508 LEU 508 508 508 LEU LEU A . n 
A 1 509 PRO 509 509 509 PRO PRO A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 ILE 511 511 511 ILE ILE A . n 
A 1 512 PHE 512 512 512 PHE PHE A . n 
A 1 513 HIS 513 513 513 HIS HIS A . n 
A 1 514 VAL 514 514 514 VAL VAL A . n 
A 1 515 ASN 515 515 515 ASN ASN A . n 
A 1 516 TRP 516 516 516 TRP TRP A . n 
A 1 517 PHE 517 517 517 PHE PHE A . n 
A 1 518 ARG 518 518 518 ARG ARG A . n 
A 1 519 LYS 519 519 519 LYS LYS A . n 
A 1 520 ASP 520 520 520 ASP ASP A . n 
A 1 521 LYS 521 521 521 LYS LYS A . n 
A 1 522 ASN 522 522 522 ASN ASN A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 LYS 524 524 524 LYS LYS A . n 
A 1 525 PHE 525 525 525 PHE PHE A . n 
A 1 526 LEU 526 526 526 LEU LEU A . n 
A 1 527 TRP 527 527 527 TRP TRP A . n 
A 1 528 PRO 528 528 528 PRO PRO A . n 
A 1 529 GLY 529 529 529 GLY GLY A . n 
A 1 530 PHE 530 530 530 PHE PHE A . n 
A 1 531 GLY 531 531 531 GLY GLY A . n 
A 1 532 GLU 532 532 532 GLU GLU A . n 
A 1 533 ASN 533 533 533 ASN ASN A . n 
A 1 534 SER 534 534 534 SER SER A . n 
A 1 535 ARG 535 535 535 ARG ARG A . n 
A 1 536 VAL 536 536 536 VAL VAL A . n 
A 1 537 LEU 537 537 537 LEU LEU A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 TRP 539 539 539 TRP TRP A . n 
A 1 540 MET 540 540 540 MET MET A . n 
A 1 541 PHE 541 541 541 PHE PHE A . n 
A 1 542 GLY 542 542 542 GLY GLY A . n 
A 1 543 ARG 543 543 543 ARG ARG A . n 
A 1 544 ILE 544 544 544 ILE ILE A . n 
A 1 545 GLU 545 545 545 GLU GLU A . n 
A 1 546 GLY 546 546 546 GLY GLY A . n 
A 1 547 GLU 547 547 547 GLU GLU A . n 
A 1 548 ASP 548 548 548 ASP ASP A . n 
A 1 549 SER 549 549 549 SER SER A . n 
A 1 550 ALA 550 550 550 ALA ALA A . n 
A 1 551 LYS 551 551 551 LYS LYS A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 THR 553 553 553 THR THR A . n 
A 1 554 PRO 554 554 554 PRO PRO A . n 
A 1 555 ILE 555 555 555 ILE ILE A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 TYR 557 557 557 TYR TYR A . n 
A 1 558 VAL 558 558 558 VAL VAL A . n 
A 1 559 PRO 559 559 559 PRO PRO A . n 
A 1 560 LYS 560 560 560 LYS LYS A . n 
A 1 561 GLU 561 561 561 GLU GLU A . n 
A 1 562 ASP 562 562 562 ASP ASP A . n 
A 1 563 ALA 563 563 563 ALA ALA A . n 
A 1 564 LEU 564 564 564 LEU LEU A . n 
A 1 565 ASN 565 565 565 ASN ASN A . n 
A 1 566 LEU 566 566 566 LEU LEU A . n 
A 1 567 LYS 567 567 567 LYS LYS A . n 
A 1 568 GLY 568 568 568 GLY GLY A . n 
A 1 569 LEU 569 569 569 LEU LEU A . n 
A 1 570 GLY 570 570 570 GLY GLY A . n 
A 1 571 ASP 571 571 571 ASP ASP A . n 
A 1 572 VAL 572 572 572 VAL VAL A . n 
A 1 573 ASN 573 573 573 ASN ASN A . n 
A 1 574 VAL 574 574 574 VAL VAL A . n 
A 1 575 GLU 575 575 575 GLU GLU A . n 
A 1 576 GLU 576 576 576 GLU GLU A . n 
A 1 577 LEU 577 577 577 LEU LEU A . n 
A 1 578 PHE 578 578 578 PHE PHE A . n 
A 1 579 GLY 579 579 579 GLY GLY A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 SER 581 581 581 SER SER A . n 
A 1 582 LYS 582 582 582 LYS LYS A . n 
A 1 583 GLU 583 583 583 GLU GLU A . n 
A 1 584 PHE 584 584 584 PHE PHE A . n 
A 1 585 TRP 585 585 585 TRP TRP A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 LYS 587 587 587 LYS LYS A . n 
A 1 588 GLU 588 588 588 GLU GLU A . n 
A 1 589 VAL 589 589 589 VAL VAL A . n 
A 1 590 GLU 590 590 590 GLU GLU A . n 
A 1 591 GLU 591 591 591 GLU GLU A . n 
A 1 592 ILE 592 592 592 ILE ILE A . n 
A 1 593 ASP 593 593 593 ASP ASP A . n 
A 1 594 LYS 594 594 594 LYS LYS A . n 
A 1 595 TYR 595 595 595 TYR TYR A . n 
A 1 596 LEU 596 596 596 LEU LEU A . n 
A 1 597 GLU 597 597 597 GLU GLU A . n 
A 1 598 ASP 598 598 598 ASP ASP A . n 
A 1 599 GLN 599 599 599 GLN GLN A . n 
A 1 600 VAL 600 600 600 VAL VAL A . n 
A 1 601 ASN 601 601 601 ASN ASN A . n 
A 1 602 ALA 602 602 602 ALA ALA A . n 
A 1 603 ASP 603 603 603 ASP ASP A . n 
A 1 604 LEU 604 604 604 LEU LEU A . n 
A 1 605 PRO 605 605 605 PRO PRO A . n 
A 1 606 TYR 606 606 606 TYR TYR A . n 
A 1 607 GLU 607 607 607 GLU GLU A . n 
A 1 608 ILE 608 608 608 ILE ILE A . n 
A 1 609 GLU 609 609 609 GLU GLU A . n 
A 1 610 ARG 610 610 610 ARG ARG A . n 
A 1 611 GLU 611 611 611 GLU GLU A . n 
A 1 612 LEU 612 612 612 LEU LEU A . n 
A 1 613 ARG 613 613 613 ARG ARG A . n 
A 1 614 ALA 614 614 614 ALA ALA A . n 
A 1 615 LEU 615 615 615 LEU LEU A . n 
A 1 616 LYS 616 616 616 LYS LYS A . n 
A 1 617 GLN 617 617 617 GLN GLN A . n 
A 1 618 ARG 618 618 618 ARG ARG A . n 
A 1 619 ILE 619 619 619 ILE ILE A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 GLN 621 621 621 GLN GLN A . n 
A 1 622 MET 622 622 622 MET MET A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 GDP ? ? GDP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PGA ? ? PGA ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 MN  1  701 700 MN  MN  A . 
C 2 MN  1  702 701 MN  MN  A . 
D 2 MN  1  703 702 MN  MN  A . 
E 3 PGA 1  704 800 PGA PGA A . 
F 4 GDP 1  705 900 GDP GDP A . 
G 5 HOH 1  801 803 HOH HOH A . 
G 5 HOH 2  802 802 HOH HOH A . 
G 5 HOH 3  803 801 HOH HOH A . 
G 5 HOH 4  804 5   HOH HOH A . 
G 5 HOH 5  805 3   HOH HOH A . 
G 5 HOH 6  806 12  HOH HOH A . 
G 5 HOH 7  807 10  HOH HOH A . 
G 5 HOH 8  808 1   HOH HOH A . 
G 5 HOH 9  809 2   HOH HOH A . 
G 5 HOH 10 810 4   HOH HOH A . 
G 5 HOH 11 811 6   HOH HOH A . 
G 5 HOH 12 812 9   HOH HOH A . 
G 5 HOH 13 813 11  HOH HOH A . 
G 5 HOH 14 814 7   HOH HOH A . 
G 5 HOH 15 815 8   HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A PRO 379 ? CG ? A PRO 379 CG 
2 1 Y 1 A PRO 379 ? CD ? A PRO 379 CD 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.21.2_5419: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.52 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.416 
_cell.length_a_esd                 ? 
_cell.length_b                     120.893 
_cell.length_b_esd                 ? 
_cell.length_c                     60.826 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9EIX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9EIX 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.97 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M HEPES pH 7.5, 0.5 uL of 100 mM MnCl2, 100 mM GDP, and 18-28% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     293 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.1271 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CHESS BEAMLINE 7B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1271 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   7B2 
_diffrn_source.pdbx_synchrotron_site       CHESS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EIX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               120.95 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     23314 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.95 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.57 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.168 
_reflns.pdbx_Rpim_I_all                                0.065 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.155 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.4200 
_reflns_shell.d_res_low                                     2.4600 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.2000 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1155 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.94 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               2.017 
_reflns_shell.pdbx_Rpim_I_all                               0.758 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.623 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.867 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EIX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.42 
_refine.ls_d_res_low                             56.59 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     23181 
_refine.ls_number_reflns_R_free                  1160 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.31 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2265 
_refine.ls_R_factor_R_free                       0.2710 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2242 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 33.20 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.44 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4867 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               4922 
_refine_hist.d_res_high                       2.42 
_refine_hist.d_res_low                        56.59 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.001 ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.397 ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.026 ? 1896 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.039 ? 717  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.002 ? 893  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.42 2.53  . . 161 2679 97.00  . . . . 0.3401 . . . . . . . . . . . 0.4149 
'X-RAY DIFFRACTION' 2.53 2.66  . . 160 2724 100.00 . . . . 0.3194 . . . . . . . . . . . 0.3583 
'X-RAY DIFFRACTION' 2.66 2.83  . . 123 2767 100.00 . . . . 0.3004 . . . . . . . . . . . 0.3481 
'X-RAY DIFFRACTION' 2.83 3.05  . . 131 2768 100.00 . . . . 0.2932 . . . . . . . . . . . 0.3287 
'X-RAY DIFFRACTION' 3.05 3.35  . . 121 2759 100.00 . . . . 0.2612 . . . . . . . . . . . 0.3235 
'X-RAY DIFFRACTION' 3.35 3.84  . . 154 2790 100.00 . . . . 0.2283 . . . . . . . . . . . 0.2965 
'X-RAY DIFFRACTION' 3.84 4.84  . . 146 2741 100.00 . . . . 0.1880 . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 4.84 56.59 . . 164 2793 100.00 . . . . 0.1769 . . . . . . . . . . . 0.2269 
# 
_struct.entry_id                     9EIX 
_struct.title                        'Rat cytosolic PEPCK in complex with GDP and phosphoglycolic acid (293K)' 
_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        9EIX 
_struct_keywords.text            'Inhibitor complex, Metabolic enzyme, Multi-temperature, Ambient temperature, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PCKGC_RAT 
_struct_ref.pdbx_db_accession          P07379 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALT
DPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIEL
TDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ
GNLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLAPGVTITSWKNKEWRPQDEEPCA
HPNSRFCTPASQCPIIDPAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPF
AMRPFFGYNFGKYLAHWLSMAHRPAAKLPKIFHVNWFRKDKNGKFLWPGFGENSRVLEWMFGRIEGEDSAKLTPIGYVPK
EDALNLKGLGDVNVEELFGISKEFWEKEVEEIDKYLEDQVNADLPYEIERELRALKQRISQM
;
_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              9EIX 
_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                 622 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P07379 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  622 
_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       622 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 10  ? ALA A 13  ? ASP A 10  ALA A 13  5 ? 4  
HELX_P HELX_P2  AA2 PRO A 24  ? GLN A 39  ? PRO A 24  GLN A 39  1 ? 16 
HELX_P HELX_P3  AA3 SER A 49  ? GLU A 63  ? SER A 49  GLU A 63  1 ? 15 
HELX_P HELX_P4  AA4 GLU A 98  ? VAL A 103 ? GLU A 98  VAL A 103 1 ? 6  
HELX_P HELX_P5  AA5 SER A 118 ? ASN A 127 ? SER A 118 ASN A 127 1 ? 10 
HELX_P HELX_P6  AA6 SER A 163 ? THR A 174 ? SER A 163 THR A 174 1 ? 12 
HELX_P HELX_P7  AA7 THR A 178 ? GLY A 185 ? THR A 178 GLY A 185 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 206 ? TRP A 210 ? LEU A 206 TRP A 210 5 ? 5  
HELX_P HELX_P9  AA9 ASN A 213 ? THR A 217 ? ASN A 213 THR A 217 5 ? 5  
HELX_P HELX_P10 AB1 TYR A 235 ? SER A 239 ? TYR A 235 SER A 239 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P12 AB3 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P13 AB4 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P14 AB5 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P15 AB6 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P16 AB7 PRO A 479 ? PHE A 486 ? PRO A 479 PHE A 486 5 ? 8  
HELX_P HELX_P17 AB8 ASN A 489 ? SER A 499 ? ASN A 489 SER A 499 1 ? 11 
HELX_P HELX_P18 AB9 MET A 500 ? HIS A 502 ? MET A 500 HIS A 502 5 ? 3  
HELX_P HELX_P19 AC1 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P20 AC2 ASN A 533 ? GLY A 546 ? ASN A 533 GLY A 546 1 ? 14 
HELX_P HELX_P21 AC3 ASN A 573 ? PHE A 578 ? ASN A 573 PHE A 578 1 ? 6  
HELX_P HELX_P22 AC4 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P23 AC5 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P24 AC6 PRO A 605 ? GLN A 621 ? PRO A 605 GLN A 621 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A LYS 244 NZ  ? ? ? 1_555 B MN  . MN  ? ? A LYS 244 A MN  701 1_555 ? ? ? ? ? ? ? 2.658 ? ? 
metalc2  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 B MN  . MN  ? ? A HIS 264 A MN  701 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc3  metalc ? ? A THR 291 OG1 ? ? ? 1_555 C MN  . MN  ? ? A THR 291 A MN  702 1_555 ? ? ? ? ? ? ? 2.532 ? ? 
metalc4  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 B MN  . MN  ? ? A ASP 311 A MN  701 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc5  metalc ? ? A HIS 502 NE2 ? ? ? 1_555 D MN  . MN  ? ? A HIS 502 A MN  703 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc6  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O4P B ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.580 ? ? 
metalc7  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O1P A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc8  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O3P B ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.757 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . P   A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.521 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O4P A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.495 ? ? 
metalc11 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 802 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc12 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 803 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc13 metalc ? ? C MN  .   MN  ? ? ? 1_555 E PGA . O3P A ? A MN  702 A PGA 704 1_555 ? ? ? ? ? ? ? 2.552 ? ? 
metalc14 metalc ? ? C MN  .   MN  ? ? ? 1_555 E PGA . O4P A ? A MN  702 A PGA 704 1_555 ? ? ? ? ? ? ? 2.707 ? ? 
metalc15 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GDP . O3B ? ? A MN  702 A GDP 705 1_555 ? ? ? ? ? ? ? 2.434 ? ? 
metalc16 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 807 1_555 ? ? ? ? ? ? ? 2.492 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 89.2  ? 
2  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 89.5  ? 
3  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 78.7  ? 
4  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P B E PGA .   ? A PGA 704 ? 1_555 75.8  ? 
5  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P B E PGA .   ? A PGA 704 ? 1_555 127.4 ? 
6  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P B E PGA .   ? A PGA 704 ? 1_555 148.9 ? 
7  NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 103.0 ? 
8  NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 162.3 ? 
9  OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 113.7 ? 
10 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O1P A E PGA .   ? A PGA 704 ? 1_555 46.4  ? 
11 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O3P B E PGA .   ? A PGA 704 ? 1_555 84.1  ? 
12 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O3P B E PGA .   ? A PGA 704 ? 1_555 172.0 ? 
13 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O3P B E PGA .   ? A PGA 704 ? 1_555 96.9  ? 
14 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O3P B E PGA .   ? A PGA 704 ? 1_555 55.0  ? 
15 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O3P B E PGA .   ? A PGA 704 ? 1_555 25.6  ? 
16 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 P   A E PGA .   ? A PGA 704 ? 1_555 142.3 ? 
17 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 P   A E PGA .   ? A PGA 704 ? 1_555 128.1 ? 
18 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 P   A E PGA .   ? A PGA 704 ? 1_555 102.1 ? 
19 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 P   A E PGA .   ? A PGA 704 ? 1_555 76.0  ? 
20 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 P   A E PGA .   ? A PGA 704 ? 1_555 39.5  ? 
21 O3P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 P   A E PGA .   ? A PGA 704 ? 1_555 59.2  ? 
22 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 147.9 ? 
23 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 108.6 ? 
24 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 69.0  ? 
25 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 110.2 ? 
26 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 67.2  ? 
27 O3P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 75.5  ? 
28 P   A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 35.0  ? 
29 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 154.3 ? 
30 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 96.7  ? 
31 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 116.2 ? 
32 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 80.8  ? 
33 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 66.9  ? 
34 O3P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 91.3  ? 
35 P   A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 35.8  ? 
36 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 52.3  ? 
37 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 72.1  ? 
38 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 99.3  ? 
39 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 161.6 ? 
40 O4P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 28.1  ? 
41 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 73.0  ? 
42 O3P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 82.8  ? 
43 P   A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 93.6  ? 
44 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 128.0 ? 
45 O   ? G HOH .   ? A HOH 802 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 82.2  ? 
46 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3P A E PGA .   ? A PGA 704 ? 1_555 147.9 ? 
47 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 144.5 ? 
48 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O4P A E PGA .   ? A PGA 704 ? 1_555 55.9  ? 
49 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3B ? F GDP .   ? A GDP 705 ? 1_555 65.6  ? 
50 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3B ? F GDP .   ? A GDP 705 ? 1_555 87.2  ? 
51 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3B ? F GDP .   ? A GDP 705 ? 1_555 104.3 ? 
52 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 807 ? 1_555 79.6  ? 
53 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 807 ? 1_555 72.5  ? 
54 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 807 ? 1_555 127.7 ? 
55 O3B ? F GDP .   ? A GDP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 807 ? 1_555 62.0  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           200 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            200 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    201 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     201 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 7 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA1 8 9 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA1 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA1 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA1 4 LYS A 155 ? THR A 161 ? LYS A 155 THR A 161 
AA1 5 ILE A 190 ? SER A 195 ? ILE A 190 SER A 195 
AA1 6 GLU A 227 ? PHE A 231 ? GLU A 227 PHE A 231 
AA1 7 LEU A 218 ? LEU A 222 ? LEU A 218 LEU A 222 
AA1 8 THR A 92  ? ILE A 95  ? THR A 92  ILE A 95  
AA1 9 TRP A 116 ? MET A 117 ? TRP A 116 MET A 117 
AA2 1 VAL A 15  ? GLN A 17  ? VAL A 15  GLN A 17  
AA2 2 TYR A 42  ? ILE A 45  ? TYR A 42  ILE A 45  
AA2 3 THR A 138 ? MET A 146 ? THR A 138 MET A 146 
AA2 4 ARG A 175 ? MET A 176 ? ARG A 175 MET A 176 
AA3 1 ILE A 66  ? LYS A 68  ? ILE A 66  LYS A 68  
AA3 2 ASP A 73  ? ALA A 78  ? ASP A 73  ALA A 78  
AA3 3 LYS A 353 ? THR A 358 ? LYS A 353 THR A 358 
AA3 4 ARG A 405 ? PRO A 409 ? ARG A 405 PRO A 409 
AA3 5 GLY A 331 ? VAL A 335 ? GLY A 331 VAL A 335 
AA4 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA4 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA4 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA4 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA4 5 LYS A 277 ? ALA A 283 ? LYS A 277 ALA A 283 
AA4 6 LEU A 266 ? THR A 271 ? LEU A 266 THR A 271 
AA4 7 LYS A 304 ? GLY A 309 ? LYS A 304 GLY A 309 
AA5 1 LEU A 261 ? GLU A 263 ? LEU A 261 GLU A 263 
AA5 2 ALA A 313 ? PHE A 317 ? ALA A 313 PHE A 317 
AA5 3 LEU A 323 ? ILE A 326 ? LEU A 323 ILE A 326 
AA5 4 VAL A 426 ? GLY A 434 ? VAL A 426 GLY A 434 
AA5 5 LYS A 510 ? VAL A 514 ? LYS A 510 VAL A 514 
AA5 6 VAL A 444 ? GLU A 446 ? VAL A 444 GLU A 446 
AA6 1 VAL A 368 ? TYR A 369 ? VAL A 368 TYR A 369 
AA6 2 ALA A 361 ? THR A 363 ? ALA A 361 THR A 363 
AA6 3 ILE A 383 ? THR A 384 ? ILE A 383 THR A 384 
AA6 4 GLU A 390 ? TRP A 391 ? GLU A 390 TRP A 391 
AA7 1 ARG A 461 ? GLU A 463 ? ARG A 461 GLU A 463 
AA7 2 ILE A 475 ? HIS A 477 ? ILE A 475 HIS A 477 
AA8 1 ALA A 550 ? LEU A 552 ? ALA A 550 LEU A 552 
AA8 2 TYR A 557 ? PRO A 559 ? TYR A 557 PRO A 559 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 16  ? N ILE A 16  O ILE A 43  ? O ILE A 43  
AA1 2 3 N TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
AA1 3 4 N TYR A 140 ? N TYR A 140 O THR A 161 ? O THR A 161 
AA1 4 5 N LEU A 160 ? N LEU A 160 O HIS A 194 ? O HIS A 194 
AA1 5 6 N LYS A 191 ? N LYS A 191 O ILE A 228 ? O ILE A 228 
AA1 6 7 O ILE A 229 ? O ILE A 229 N ALA A 220 ? N ALA A 220 
AA1 7 8 O HIS A 221 ? O HIS A 221 N ILE A 95  ? N ILE A 95  
AA1 8 9 N ILE A 94  ? N ILE A 94  O MET A 117 ? O MET A 117 
AA2 1 2 N ILE A 16  ? N ILE A 16  O ILE A 43  ? O ILE A 43  
AA2 2 3 N TYR A 42  ? N TYR A 42  O MET A 139 ? O MET A 139 
AA2 3 4 N SER A 145 ? N SER A 145 O ARG A 175 ? O ARG A 175 
AA3 1 2 N ARG A 67  ? N ARG A 67  O LEU A 77  ? O LEU A 77  
AA3 2 3 N TRP A 76  ? N TRP A 76  O PHE A 357 ? O PHE A 357 
AA3 3 4 N ILE A 356 ? N ILE A 356 O CYS A 407 ? O CYS A 407 
AA3 4 5 O THR A 408 ? O THR A 408 N PHE A 332 ? N PHE A 332 
AA4 1 2 N LEU A 261 ? N LEU A 261 O MET A 315 ? O MET A 315 
AA4 2 3 N LYS A 316 ? N LYS A 316 O ARG A 324 ? O ARG A 324 
AA4 3 4 N LEU A 323 ? N LEU A 323 O ILE A 428 ? O ILE A 428 
AA4 4 5 O ILE A 432 ? O ILE A 432 N ALA A 283 ? N ALA A 283 
AA4 5 6 O LEU A 280 ? O LEU A 280 N LEU A 268 ? N LEU A 268 
AA4 6 7 N GLY A 269 ? N GLY A 269 O GLU A 306 ? O GLU A 306 
AA5 1 2 N LEU A 261 ? N LEU A 261 O MET A 315 ? O MET A 315 
AA5 2 3 N LYS A 316 ? N LYS A 316 O ARG A 324 ? O ARG A 324 
AA5 3 4 N LEU A 323 ? N LEU A 323 O ILE A 428 ? O ILE A 428 
AA5 4 5 N PHE A 433 ? N PHE A 433 O PHE A 512 ? O PHE A 512 
AA5 5 6 O HIS A 513 ? O HIS A 513 N TYR A 445 ? N TYR A 445 
AA6 1 2 O TYR A 369 ? O TYR A 369 N ALA A 361 ? N ALA A 361 
AA6 2 3 N GLU A 362 ? N GLU A 362 O THR A 384 ? O THR A 384 
AA6 3 4 N ILE A 383 ? N ILE A 383 O TRP A 391 ? O TRP A 391 
AA7 1 2 N SER A 462 ? N SER A 462 O MET A 476 ? O MET A 476 
AA8 1 2 N LYS A 551 ? N LYS A 551 O VAL A 558 ? O VAL A 558 
# 
_pdbx_entry_details.entry_id                   9EIX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 11  ? ? -88.90  30.78   
2  1 ASN A 74  ? ? 60.12   65.22   
3  1 LYS A 91  ? ? -99.53  34.83   
4  1 SER A 108 ? ? 71.14   -61.92  
5  1 LEU A 113 ? ? -88.18  33.25   
6  1 ARG A 129 ? ? -134.32 -61.12  
7  1 PRO A 131 ? ? -48.26  98.43   
8  1 LYS A 243 ? ? -87.50  -70.10  
9  1 LEU A 248 ? ? -123.52 -64.06  
10 1 TRP A 260 ? ? -114.58 -164.55 
11 1 ASP A 311 ? ? -150.38 -69.70  
12 1 LYS A 316 ? ? -173.64 145.27  
13 1 PRO A 418 ? ? -73.17  21.43   
14 1 THR A 465 ? ? -104.02 -147.48 
15 1 ALA A 468 ? ? -102.44 -143.01 
16 1 LYS A 473 ? ? -104.68 72.74   
17 1 ASP A 478 ? ? -153.53 78.30   
18 1 PHE A 480 ? ? 58.23   15.25   
19 1 ASN A 515 ? ? -166.43 93.39   
20 1 ASP A 520 ? ? -100.79 -162.19 
21 1 PHE A 530 ? ? 58.89   -112.13 
22 1 ASP A 548 ? ? -103.29 76.80   
23 1 LEU A 569 ? ? -95.43  -83.51  
24 1 ASN A 601 ? ? 59.18   -116.71 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -2.2022 11.3167  -6.3221 0.4120 ? -0.0738 ? -0.0499 ? 0.5129 ? 0.0935  ? 0.4544 ? 0.4750 ? -0.3983 
? 0.0299  ? 2.1472 ? -0.5559 ? 1.3662 ? -0.1098 ? 0.0142  ? 0.1182  ? -0.4358 ? 0.2606 ? 0.3700  ? 0.0721  ? -0.4467 ? -0.0002 ? 
2 'X-RAY DIFFRACTION' ? refined 8.4627  4.4071   11.1272 0.2556 ? -0.0862 ? 0.0354  ? 0.2684 ? 0.0278  ? 0.2759 ? 1.1114 ? 0.1537  
? -0.4565 ? 2.1967 ? -0.7413 ? 1.3385 ? 0.0319  ? 0.0273  ? -0.1553 ? 0.1502  ? 0.1484 ? -0.2197 ? -0.0177 ? -0.0054 ? 0.2937  ? 
3 'X-RAY DIFFRACTION' ? refined 2.6337  -16.1370 18.9136 0.3756 ? -0.0148 ? -0.0211 ? 0.3524 ? -0.0269 ? 0.4361 ? 1.6192 ? 1.0507  
? -0.5536 ? 2.4826 ? -0.2889 ? 0.3107 ? -0.0570 ? -0.0808 ? 0.0542  ? 0.3068  ? 0.1520 ? -0.0149 ? 0.0516  ? -0.0278 ? 0.0002  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 222 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 223 through 427 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 428 through 622 )
;
# 
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 PRO 2 ? A PRO 2 
# 
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  
GDP PB     P  N N 88  
GDP O1B    O  N N 89  
GDP O2B    O  N N 90  
GDP O3B    O  N N 91  
GDP O3A    O  N N 92  
GDP PA     P  N N 93  
GDP O1A    O  N N 94  
GDP O2A    O  N N 95  
GDP "O5'"  O  N N 96  
GDP "C5'"  C  N N 97  
GDP "C4'"  C  N R 98  
GDP "O4'"  O  N N 99  
GDP "C3'"  C  N S 100 
GDP "O3'"  O  N N 101 
GDP "C2'"  C  N R 102 
GDP "O2'"  O  N N 103 
GDP "C1'"  C  N R 104 
GDP N9     N  Y N 105 
GDP C8     C  Y N 106 
GDP N7     N  Y N 107 
GDP C5     C  Y N 108 
GDP C6     C  N N 109 
GDP O6     O  N N 110 
GDP N1     N  N N 111 
GDP C2     C  N N 112 
GDP N2     N  N N 113 
GDP N3     N  N N 114 
GDP C4     C  Y N 115 
GDP HOB2   H  N N 116 
GDP HOB3   H  N N 117 
GDP HOA2   H  N N 118 
GDP "H5'"  H  N N 119 
GDP "H5''" H  N N 120 
GDP "H4'"  H  N N 121 
GDP "H3'"  H  N N 122 
GDP "HO3'" H  N N 123 
GDP "H2'"  H  N N 124 
GDP "HO2'" H  N N 125 
GDP "H1'"  H  N N 126 
GDP H8     H  N N 127 
GDP HN1    H  N N 128 
GDP HN21   H  N N 129 
GDP HN22   H  N N 130 
GLN N      N  N N 131 
GLN CA     C  N S 132 
GLN C      C  N N 133 
GLN O      O  N N 134 
GLN CB     C  N N 135 
GLN CG     C  N N 136 
GLN CD     C  N N 137 
GLN OE1    O  N N 138 
GLN NE2    N  N N 139 
GLN OXT    O  N N 140 
GLN H      H  N N 141 
GLN H2     H  N N 142 
GLN HA     H  N N 143 
GLN HB2    H  N N 144 
GLN HB3    H  N N 145 
GLN HG2    H  N N 146 
GLN HG3    H  N N 147 
GLN HE21   H  N N 148 
GLN HE22   H  N N 149 
GLN HXT    H  N N 150 
GLU N      N  N N 151 
GLU CA     C  N S 152 
GLU C      C  N N 153 
GLU O      O  N N 154 
GLU CB     C  N N 155 
GLU CG     C  N N 156 
GLU CD     C  N N 157 
GLU OE1    O  N N 158 
GLU OE2    O  N N 159 
GLU OXT    O  N N 160 
GLU H      H  N N 161 
GLU H2     H  N N 162 
GLU HA     H  N N 163 
GLU HB2    H  N N 164 
GLU HB3    H  N N 165 
GLU HG2    H  N N 166 
GLU HG3    H  N N 167 
GLU HE2    H  N N 168 
GLU HXT    H  N N 169 
GLY N      N  N N 170 
GLY CA     C  N N 171 
GLY C      C  N N 172 
GLY O      O  N N 173 
GLY OXT    O  N N 174 
GLY H      H  N N 175 
GLY H2     H  N N 176 
GLY HA2    H  N N 177 
GLY HA3    H  N N 178 
GLY HXT    H  N N 179 
HIS N      N  N N 180 
HIS CA     C  N S 181 
HIS C      C  N N 182 
HIS O      O  N N 183 
HIS CB     C  N N 184 
HIS CG     C  Y N 185 
HIS ND1    N  Y N 186 
HIS CD2    C  Y N 187 
HIS CE1    C  Y N 188 
HIS NE2    N  Y N 189 
HIS OXT    O  N N 190 
HIS H      H  N N 191 
HIS H2     H  N N 192 
HIS HA     H  N N 193 
HIS HB2    H  N N 194 
HIS HB3    H  N N 195 
HIS HD1    H  N N 196 
HIS HD2    H  N N 197 
HIS HE1    H  N N 198 
HIS HE2    H  N N 199 
HIS HXT    H  N N 200 
HOH O      O  N N 201 
HOH H1     H  N N 202 
HOH H2     H  N N 203 
ILE N      N  N N 204 
ILE CA     C  N S 205 
ILE C      C  N N 206 
ILE O      O  N N 207 
ILE CB     C  N S 208 
ILE CG1    C  N N 209 
ILE CG2    C  N N 210 
ILE CD1    C  N N 211 
ILE OXT    O  N N 212 
ILE H      H  N N 213 
ILE H2     H  N N 214 
ILE HA     H  N N 215 
ILE HB     H  N N 216 
ILE HG12   H  N N 217 
ILE HG13   H  N N 218 
ILE HG21   H  N N 219 
ILE HG22   H  N N 220 
ILE HG23   H  N N 221 
ILE HD11   H  N N 222 
ILE HD12   H  N N 223 
ILE HD13   H  N N 224 
ILE HXT    H  N N 225 
LEU N      N  N N 226 
LEU CA     C  N S 227 
LEU C      C  N N 228 
LEU O      O  N N 229 
LEU CB     C  N N 230 
LEU CG     C  N N 231 
LEU CD1    C  N N 232 
LEU CD2    C  N N 233 
LEU OXT    O  N N 234 
LEU H      H  N N 235 
LEU H2     H  N N 236 
LEU HA     H  N N 237 
LEU HB2    H  N N 238 
LEU HB3    H  N N 239 
LEU HG     H  N N 240 
LEU HD11   H  N N 241 
LEU HD12   H  N N 242 
LEU HD13   H  N N 243 
LEU HD21   H  N N 244 
LEU HD22   H  N N 245 
LEU HD23   H  N N 246 
LEU HXT    H  N N 247 
LYS N      N  N N 248 
LYS CA     C  N S 249 
LYS C      C  N N 250 
LYS O      O  N N 251 
LYS CB     C  N N 252 
LYS CG     C  N N 253 
LYS CD     C  N N 254 
LYS CE     C  N N 255 
LYS NZ     N  N N 256 
LYS OXT    O  N N 257 
LYS H      H  N N 258 
LYS H2     H  N N 259 
LYS HA     H  N N 260 
LYS HB2    H  N N 261 
LYS HB3    H  N N 262 
LYS HG2    H  N N 263 
LYS HG3    H  N N 264 
LYS HD2    H  N N 265 
LYS HD3    H  N N 266 
LYS HE2    H  N N 267 
LYS HE3    H  N N 268 
LYS HZ1    H  N N 269 
LYS HZ2    H  N N 270 
LYS HZ3    H  N N 271 
LYS HXT    H  N N 272 
MET N      N  N N 273 
MET CA     C  N S 274 
MET C      C  N N 275 
MET O      O  N N 276 
MET CB     C  N N 277 
MET CG     C  N N 278 
MET SD     S  N N 279 
MET CE     C  N N 280 
MET OXT    O  N N 281 
MET H      H  N N 282 
MET H2     H  N N 283 
MET HA     H  N N 284 
MET HB2    H  N N 285 
MET HB3    H  N N 286 
MET HG2    H  N N 287 
MET HG3    H  N N 288 
MET HE1    H  N N 289 
MET HE2    H  N N 290 
MET HE3    H  N N 291 
MET HXT    H  N N 292 
MN  MN     MN N N 293 
PGA P      P  N N 294 
PGA O1P    O  N N 295 
PGA O2P    O  N N 296 
PGA O3P    O  N N 297 
PGA O4P    O  N N 298 
PGA C2     C  N N 299 
PGA C1     C  N N 300 
PGA O1     O  N N 301 
PGA O2     O  N N 302 
PGA HOP3   H  N N 303 
PGA HOP4   H  N N 304 
PGA H21    H  N N 305 
PGA H22    H  N N 306 
PGA HO2    H  N N 307 
PHE N      N  N N 308 
PHE CA     C  N S 309 
PHE C      C  N N 310 
PHE O      O  N N 311 
PHE CB     C  N N 312 
PHE CG     C  Y N 313 
PHE CD1    C  Y N 314 
PHE CD2    C  Y N 315 
PHE CE1    C  Y N 316 
PHE CE2    C  Y N 317 
PHE CZ     C  Y N 318 
PHE OXT    O  N N 319 
PHE H      H  N N 320 
PHE H2     H  N N 321 
PHE HA     H  N N 322 
PHE HB2    H  N N 323 
PHE HB3    H  N N 324 
PHE HD1    H  N N 325 
PHE HD2    H  N N 326 
PHE HE1    H  N N 327 
PHE HE2    H  N N 328 
PHE HZ     H  N N 329 
PHE HXT    H  N N 330 
PRO N      N  N N 331 
PRO CA     C  N S 332 
PRO C      C  N N 333 
PRO O      O  N N 334 
PRO CB     C  N N 335 
PRO CG     C  N N 336 
PRO CD     C  N N 337 
PRO OXT    O  N N 338 
PRO H      H  N N 339 
PRO HA     H  N N 340 
PRO HB2    H  N N 341 
PRO HB3    H  N N 342 
PRO HG2    H  N N 343 
PRO HG3    H  N N 344 
PRO HD2    H  N N 345 
PRO HD3    H  N N 346 
PRO HXT    H  N N 347 
SER N      N  N N 348 
SER CA     C  N S 349 
SER C      C  N N 350 
SER O      O  N N 351 
SER CB     C  N N 352 
SER OG     O  N N 353 
SER OXT    O  N N 354 
SER H      H  N N 355 
SER H2     H  N N 356 
SER HA     H  N N 357 
SER HB2    H  N N 358 
SER HB3    H  N N 359 
SER HG     H  N N 360 
SER HXT    H  N N 361 
THR N      N  N N 362 
THR CA     C  N S 363 
THR C      C  N N 364 
THR O      O  N N 365 
THR CB     C  N R 366 
THR OG1    O  N N 367 
THR CG2    C  N N 368 
THR OXT    O  N N 369 
THR H      H  N N 370 
THR H2     H  N N 371 
THR HA     H  N N 372 
THR HB     H  N N 373 
THR HG1    H  N N 374 
THR HG21   H  N N 375 
THR HG22   H  N N 376 
THR HG23   H  N N 377 
THR HXT    H  N N 378 
TRP N      N  N N 379 
TRP CA     C  N S 380 
TRP C      C  N N 381 
TRP O      O  N N 382 
TRP CB     C  N N 383 
TRP CG     C  Y N 384 
TRP CD1    C  Y N 385 
TRP CD2    C  Y N 386 
TRP NE1    N  Y N 387 
TRP CE2    C  Y N 388 
TRP CE3    C  Y N 389 
TRP CZ2    C  Y N 390 
TRP CZ3    C  Y N 391 
TRP CH2    C  Y N 392 
TRP OXT    O  N N 393 
TRP H      H  N N 394 
TRP H2     H  N N 395 
TRP HA     H  N N 396 
TRP HB2    H  N N 397 
TRP HB3    H  N N 398 
TRP HD1    H  N N 399 
TRP HE1    H  N N 400 
TRP HE3    H  N N 401 
TRP HZ2    H  N N 402 
TRP HZ3    H  N N 403 
TRP HH2    H  N N 404 
TRP HXT    H  N N 405 
TYR N      N  N N 406 
TYR CA     C  N S 407 
TYR C      C  N N 408 
TYR O      O  N N 409 
TYR CB     C  N N 410 
TYR CG     C  Y N 411 
TYR CD1    C  Y N 412 
TYR CD2    C  Y N 413 
TYR CE1    C  Y N 414 
TYR CE2    C  Y N 415 
TYR CZ     C  Y N 416 
TYR OH     O  N N 417 
TYR OXT    O  N N 418 
TYR H      H  N N 419 
TYR H2     H  N N 420 
TYR HA     H  N N 421 
TYR HB2    H  N N 422 
TYR HB3    H  N N 423 
TYR HD1    H  N N 424 
TYR HD2    H  N N 425 
TYR HE1    H  N N 426 
TYR HE2    H  N N 427 
TYR HH     H  N N 428 
TYR HXT    H  N N 429 
VAL N      N  N N 430 
VAL CA     C  N S 431 
VAL C      C  N N 432 
VAL O      O  N N 433 
VAL CB     C  N N 434 
VAL CG1    C  N N 435 
VAL CG2    C  N N 436 
VAL OXT    O  N N 437 
VAL H      H  N N 438 
VAL H2     H  N N 439 
VAL HA     H  N N 440 
VAL HB     H  N N 441 
VAL HG11   H  N N 442 
VAL HG12   H  N N 443 
VAL HG13   H  N N 444 
VAL HG21   H  N N 445 
VAL HG22   H  N N 446 
VAL HG23   H  N N 447 
VAL HXT    H  N N 448 
# 
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  
GDP PB    O1B    doub N N 83  
GDP PB    O2B    sing N N 84  
GDP PB    O3B    sing N N 85  
GDP PB    O3A    sing N N 86  
GDP O2B   HOB2   sing N N 87  
GDP O3B   HOB3   sing N N 88  
GDP O3A   PA     sing N N 89  
GDP PA    O1A    doub N N 90  
GDP PA    O2A    sing N N 91  
GDP PA    "O5'"  sing N N 92  
GDP O2A   HOA2   sing N N 93  
GDP "O5'" "C5'"  sing N N 94  
GDP "C5'" "C4'"  sing N N 95  
GDP "C5'" "H5'"  sing N N 96  
GDP "C5'" "H5''" sing N N 97  
GDP "C4'" "O4'"  sing N N 98  
GDP "C4'" "C3'"  sing N N 99  
GDP "C4'" "H4'"  sing N N 100 
GDP "O4'" "C1'"  sing N N 101 
GDP "C3'" "O3'"  sing N N 102 
GDP "C3'" "C2'"  sing N N 103 
GDP "C3'" "H3'"  sing N N 104 
GDP "O3'" "HO3'" sing N N 105 
GDP "C2'" "O2'"  sing N N 106 
GDP "C2'" "C1'"  sing N N 107 
GDP "C2'" "H2'"  sing N N 108 
GDP "O2'" "HO2'" sing N N 109 
GDP "C1'" N9     sing N N 110 
GDP "C1'" "H1'"  sing N N 111 
GDP N9    C8     sing Y N 112 
GDP N9    C4     sing Y N 113 
GDP C8    N7     doub Y N 114 
GDP C8    H8     sing N N 115 
GDP N7    C5     sing Y N 116 
GDP C5    C6     sing N N 117 
GDP C5    C4     doub Y N 118 
GDP C6    O6     doub N N 119 
GDP C6    N1     sing N N 120 
GDP N1    C2     sing N N 121 
GDP N1    HN1    sing N N 122 
GDP C2    N2     sing N N 123 
GDP C2    N3     doub N N 124 
GDP N2    HN21   sing N N 125 
GDP N2    HN22   sing N N 126 
GDP N3    C4     sing N N 127 
GLN N     CA     sing N N 128 
GLN N     H      sing N N 129 
GLN N     H2     sing N N 130 
GLN CA    C      sing N N 131 
GLN CA    CB     sing N N 132 
GLN CA    HA     sing N N 133 
GLN C     O      doub N N 134 
GLN C     OXT    sing N N 135 
GLN CB    CG     sing N N 136 
GLN CB    HB2    sing N N 137 
GLN CB    HB3    sing N N 138 
GLN CG    CD     sing N N 139 
GLN CG    HG2    sing N N 140 
GLN CG    HG3    sing N N 141 
GLN CD    OE1    doub N N 142 
GLN CD    NE2    sing N N 143 
GLN NE2   HE21   sing N N 144 
GLN NE2   HE22   sing N N 145 
GLN OXT   HXT    sing N N 146 
GLU N     CA     sing N N 147 
GLU N     H      sing N N 148 
GLU N     H2     sing N N 149 
GLU CA    C      sing N N 150 
GLU CA    CB     sing N N 151 
GLU CA    HA     sing N N 152 
GLU C     O      doub N N 153 
GLU C     OXT    sing N N 154 
GLU CB    CG     sing N N 155 
GLU CB    HB2    sing N N 156 
GLU CB    HB3    sing N N 157 
GLU CG    CD     sing N N 158 
GLU CG    HG2    sing N N 159 
GLU CG    HG3    sing N N 160 
GLU CD    OE1    doub N N 161 
GLU CD    OE2    sing N N 162 
GLU OE2   HE2    sing N N 163 
GLU OXT   HXT    sing N N 164 
GLY N     CA     sing N N 165 
GLY N     H      sing N N 166 
GLY N     H2     sing N N 167 
GLY CA    C      sing N N 168 
GLY CA    HA2    sing N N 169 
GLY CA    HA3    sing N N 170 
GLY C     O      doub N N 171 
GLY C     OXT    sing N N 172 
GLY OXT   HXT    sing N N 173 
HIS N     CA     sing N N 174 
HIS N     H      sing N N 175 
HIS N     H2     sing N N 176 
HIS CA    C      sing N N 177 
HIS CA    CB     sing N N 178 
HIS CA    HA     sing N N 179 
HIS C     O      doub N N 180 
HIS C     OXT    sing N N 181 
HIS CB    CG     sing N N 182 
HIS CB    HB2    sing N N 183 
HIS CB    HB3    sing N N 184 
HIS CG    ND1    sing Y N 185 
HIS CG    CD2    doub Y N 186 
HIS ND1   CE1    doub Y N 187 
HIS ND1   HD1    sing N N 188 
HIS CD2   NE2    sing Y N 189 
HIS CD2   HD2    sing N N 190 
HIS CE1   NE2    sing Y N 191 
HIS CE1   HE1    sing N N 192 
HIS NE2   HE2    sing N N 193 
HIS OXT   HXT    sing N N 194 
HOH O     H1     sing N N 195 
HOH O     H2     sing N N 196 
ILE N     CA     sing N N 197 
ILE N     H      sing N N 198 
ILE N     H2     sing N N 199 
ILE CA    C      sing N N 200 
ILE CA    CB     sing N N 201 
ILE CA    HA     sing N N 202 
ILE C     O      doub N N 203 
ILE C     OXT    sing N N 204 
ILE CB    CG1    sing N N 205 
ILE CB    CG2    sing N N 206 
ILE CB    HB     sing N N 207 
ILE CG1   CD1    sing N N 208 
ILE CG1   HG12   sing N N 209 
ILE CG1   HG13   sing N N 210 
ILE CG2   HG21   sing N N 211 
ILE CG2   HG22   sing N N 212 
ILE CG2   HG23   sing N N 213 
ILE CD1   HD11   sing N N 214 
ILE CD1   HD12   sing N N 215 
ILE CD1   HD13   sing N N 216 
ILE OXT   HXT    sing N N 217 
LEU N     CA     sing N N 218 
LEU N     H      sing N N 219 
LEU N     H2     sing N N 220 
LEU CA    C      sing N N 221 
LEU CA    CB     sing N N 222 
LEU CA    HA     sing N N 223 
LEU C     O      doub N N 224 
LEU C     OXT    sing N N 225 
LEU CB    CG     sing N N 226 
LEU CB    HB2    sing N N 227 
LEU CB    HB3    sing N N 228 
LEU CG    CD1    sing N N 229 
LEU CG    CD2    sing N N 230 
LEU CG    HG     sing N N 231 
LEU CD1   HD11   sing N N 232 
LEU CD1   HD12   sing N N 233 
LEU CD1   HD13   sing N N 234 
LEU CD2   HD21   sing N N 235 
LEU CD2   HD22   sing N N 236 
LEU CD2   HD23   sing N N 237 
LEU OXT   HXT    sing N N 238 
LYS N     CA     sing N N 239 
LYS N     H      sing N N 240 
LYS N     H2     sing N N 241 
LYS CA    C      sing N N 242 
LYS CA    CB     sing N N 243 
LYS CA    HA     sing N N 244 
LYS C     O      doub N N 245 
LYS C     OXT    sing N N 246 
LYS CB    CG     sing N N 247 
LYS CB    HB2    sing N N 248 
LYS CB    HB3    sing N N 249 
LYS CG    CD     sing N N 250 
LYS CG    HG2    sing N N 251 
LYS CG    HG3    sing N N 252 
LYS CD    CE     sing N N 253 
LYS CD    HD2    sing N N 254 
LYS CD    HD3    sing N N 255 
LYS CE    NZ     sing N N 256 
LYS CE    HE2    sing N N 257 
LYS CE    HE3    sing N N 258 
LYS NZ    HZ1    sing N N 259 
LYS NZ    HZ2    sing N N 260 
LYS NZ    HZ3    sing N N 261 
LYS OXT   HXT    sing N N 262 
MET N     CA     sing N N 263 
MET N     H      sing N N 264 
MET N     H2     sing N N 265 
MET CA    C      sing N N 266 
MET CA    CB     sing N N 267 
MET CA    HA     sing N N 268 
MET C     O      doub N N 269 
MET C     OXT    sing N N 270 
MET CB    CG     sing N N 271 
MET CB    HB2    sing N N 272 
MET CB    HB3    sing N N 273 
MET CG    SD     sing N N 274 
MET CG    HG2    sing N N 275 
MET CG    HG3    sing N N 276 
MET SD    CE     sing N N 277 
MET CE    HE1    sing N N 278 
MET CE    HE2    sing N N 279 
MET CE    HE3    sing N N 280 
MET OXT   HXT    sing N N 281 
PGA P     O1P    sing N N 282 
PGA P     O2P    doub N N 283 
PGA P     O3P    sing N N 284 
PGA P     O4P    sing N N 285 
PGA O1P   C2     sing N N 286 
PGA O3P   HOP3   sing N N 287 
PGA O4P   HOP4   sing N N 288 
PGA C2    C1     sing N N 289 
PGA C2    H21    sing N N 290 
PGA C2    H22    sing N N 291 
PGA C1    O1     doub N N 292 
PGA C1    O2     sing N N 293 
PGA O2    HO2    sing N N 294 
PHE N     CA     sing N N 295 
PHE N     H      sing N N 296 
PHE N     H2     sing N N 297 
PHE CA    C      sing N N 298 
PHE CA    CB     sing N N 299 
PHE CA    HA     sing N N 300 
PHE C     O      doub N N 301 
PHE C     OXT    sing N N 302 
PHE CB    CG     sing N N 303 
PHE CB    HB2    sing N N 304 
PHE CB    HB3    sing N N 305 
PHE CG    CD1    doub Y N 306 
PHE CG    CD2    sing Y N 307 
PHE CD1   CE1    sing Y N 308 
PHE CD1   HD1    sing N N 309 
PHE CD2   CE2    doub Y N 310 
PHE CD2   HD2    sing N N 311 
PHE CE1   CZ     doub Y N 312 
PHE CE1   HE1    sing N N 313 
PHE CE2   CZ     sing Y N 314 
PHE CE2   HE2    sing N N 315 
PHE CZ    HZ     sing N N 316 
PHE OXT   HXT    sing N N 317 
PRO N     CA     sing N N 318 
PRO N     CD     sing N N 319 
PRO N     H      sing N N 320 
PRO CA    C      sing N N 321 
PRO CA    CB     sing N N 322 
PRO CA    HA     sing N N 323 
PRO C     O      doub N N 324 
PRO C     OXT    sing N N 325 
PRO CB    CG     sing N N 326 
PRO CB    HB2    sing N N 327 
PRO CB    HB3    sing N N 328 
PRO CG    CD     sing N N 329 
PRO CG    HG2    sing N N 330 
PRO CG    HG3    sing N N 331 
PRO CD    HD2    sing N N 332 
PRO CD    HD3    sing N N 333 
PRO OXT   HXT    sing N N 334 
SER N     CA     sing N N 335 
SER N     H      sing N N 336 
SER N     H2     sing N N 337 
SER CA    C      sing N N 338 
SER CA    CB     sing N N 339 
SER CA    HA     sing N N 340 
SER C     O      doub N N 341 
SER C     OXT    sing N N 342 
SER CB    OG     sing N N 343 
SER CB    HB2    sing N N 344 
SER CB    HB3    sing N N 345 
SER OG    HG     sing N N 346 
SER OXT   HXT    sing N N 347 
THR N     CA     sing N N 348 
THR N     H      sing N N 349 
THR N     H2     sing N N 350 
THR CA    C      sing N N 351 
THR CA    CB     sing N N 352 
THR CA    HA     sing N N 353 
THR C     O      doub N N 354 
THR C     OXT    sing N N 355 
THR CB    OG1    sing N N 356 
THR CB    CG2    sing N N 357 
THR CB    HB     sing N N 358 
THR OG1   HG1    sing N N 359 
THR CG2   HG21   sing N N 360 
THR CG2   HG22   sing N N 361 
THR CG2   HG23   sing N N 362 
THR OXT   HXT    sing N N 363 
TRP N     CA     sing N N 364 
TRP N     H      sing N N 365 
TRP N     H2     sing N N 366 
TRP CA    C      sing N N 367 
TRP CA    CB     sing N N 368 
TRP CA    HA     sing N N 369 
TRP C     O      doub N N 370 
TRP C     OXT    sing N N 371 
TRP CB    CG     sing N N 372 
TRP CB    HB2    sing N N 373 
TRP CB    HB3    sing N N 374 
TRP CG    CD1    doub Y N 375 
TRP CG    CD2    sing Y N 376 
TRP CD1   NE1    sing Y N 377 
TRP CD1   HD1    sing N N 378 
TRP CD2   CE2    doub Y N 379 
TRP CD2   CE3    sing Y N 380 
TRP NE1   CE2    sing Y N 381 
TRP NE1   HE1    sing N N 382 
TRP CE2   CZ2    sing Y N 383 
TRP CE3   CZ3    doub Y N 384 
TRP CE3   HE3    sing N N 385 
TRP CZ2   CH2    doub Y N 386 
TRP CZ2   HZ2    sing N N 387 
TRP CZ3   CH2    sing Y N 388 
TRP CZ3   HZ3    sing N N 389 
TRP CH2   HH2    sing N N 390 
TRP OXT   HXT    sing N N 391 
TYR N     CA     sing N N 392 
TYR N     H      sing N N 393 
TYR N     H2     sing N N 394 
TYR CA    C      sing N N 395 
TYR CA    CB     sing N N 396 
TYR CA    HA     sing N N 397 
TYR C     O      doub N N 398 
TYR C     OXT    sing N N 399 
TYR CB    CG     sing N N 400 
TYR CB    HB2    sing N N 401 
TYR CB    HB3    sing N N 402 
TYR CG    CD1    doub Y N 403 
TYR CG    CD2    sing Y N 404 
TYR CD1   CE1    sing Y N 405 
TYR CD1   HD1    sing N N 406 
TYR CD2   CE2    doub Y N 407 
TYR CD2   HD2    sing N N 408 
TYR CE1   CZ     doub Y N 409 
TYR CE1   HE1    sing N N 410 
TYR CE2   CZ     sing Y N 411 
TYR CE2   HE2    sing N N 412 
TYR CZ    OH     sing N N 413 
TYR OH    HH     sing N N 414 
TYR OXT   HXT    sing N N 415 
VAL N     CA     sing N N 416 
VAL N     H      sing N N 417 
VAL N     H2     sing N N 418 
VAL CA    C      sing N N 419 
VAL CA    CB     sing N N 420 
VAL CA    HA     sing N N 421 
VAL C     O      doub N N 422 
VAL C     OXT    sing N N 423 
VAL CB    CG1    sing N N 424 
VAL CB    CG2    sing N N 425 
VAL CB    HB     sing N N 426 
VAL CG1   HG11   sing N N 427 
VAL CG1   HG12   sing N N 428 
VAL CG1   HG13   sing N N 429 
VAL CG2   HG21   sing N N 430 
VAL CG2   HG22   sing N N 431 
VAL CG2   HG23   sing N N 432 
VAL OXT   HXT    sing N N 433 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)'                                         'United States' DBI-2210041     1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 5R01GM127528-02 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3DT2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EIX 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.022018 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008681 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008272 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.017672 
_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  
H  
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . PRO A 1 3   ? -2.850  15.636  -34.922 1.00 115.87 ? 3   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? -3.515  14.469  -34.332 1.00 116.55 ? 3   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? -4.790  14.835  -33.577 1.00 115.84 ? 3   PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? -5.212  14.096  -32.688 1.00 107.52 ? 3   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? -2.456  13.915  -33.377 1.00 111.79 ? 3   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? -1.164  14.312  -33.998 1.00 115.48 ? 3   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? -1.408  15.659  -34.622 1.00 119.69 ? 3   PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? -5.392  15.967  -33.933 1.00 99.98  ? 4   GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? -6.622  16.410  -33.293 1.00 98.98  ? 4   GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? -7.278  17.468  -34.167 1.00 100.93 ? 4   GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? -6.632  18.084  -35.019 1.00 95.60  ? 4   GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? -6.360  16.959  -31.886 1.00 106.32 ? 4   GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? -5.442  18.171  -31.854 1.00 105.78 ? 4   GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? -5.281  18.744  -30.459 1.00 114.72 ? 4   GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? -5.910  18.280  -29.508 1.00 116.04 ? 4   GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? -4.435  19.760  -30.331 1.00 119.38 ? 4   GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? -8.576  17.668  -33.943 1.00 93.80  ? 5   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? -9.336  18.669  -34.681 1.00 97.25  ? 5   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? -9.339  20.023  -33.983 1.00 111.79 ? 5   LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? -9.282  21.062  -34.648 1.00 102.84 ? 5   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? -10.775 18.188  -34.893 1.00 93.27  ? 5   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? -10.961 16.987  -35.822 1.00 77.79  ? 5   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? -12.425 16.579  -35.886 1.00 76.27  ? 5   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? -10.428 17.299  -37.211 1.00 75.91  ? 5   LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? -9.406  20.030  -32.653 1.00 139.90 ? 6   HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? -9.380  21.256  -31.871 1.00 143.29 ? 6   HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? -8.375  21.112  -30.737 1.00 148.95 ? 6   HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? -8.085  20.003  -30.280 1.00 143.89 ? 6   HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? -10.766 21.594  -31.302 1.00 138.38 ? 6   HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? -11.814 21.812  -32.349 1.00 132.29 ? 6   HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? -12.241 20.810  -33.194 1.00 128.84 ? 6   HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? -12.520 22.916  -32.688 1.00 127.59 ? 6   HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? -13.165 21.288  -34.008 1.00 124.65 ? 6   HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? -13.353 22.563  -33.722 1.00 121.40 ? 6   HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? -7.843  22.249  -30.287 1.00 178.16 ? 7   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? -6.856  22.272  -29.207 1.00 174.26 ? 7   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? -7.562  22.056  -27.868 1.00 171.02 ? 7   ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? -7.672  22.946  -27.022 1.00 170.05 ? 7   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? -6.072  23.577  -29.226 1.00 180.46 ? 7   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? -5.128  23.672  -30.408 1.00 184.80 ? 7   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? -3.951  23.323  -30.306 1.00 179.63 ? 7   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? -5.639  24.144  -31.538 1.00 192.32 ? 7   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? -8.047  20.831  -27.686 1.00 136.71 ? 8   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? -8.705  20.451  -26.452 1.00 120.73 ? 8   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? -8.067  19.241  -25.803 1.00 115.46 ? 8   GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? -8.435  18.854  -24.690 1.00 112.69 ? 8   GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? -7.101  18.634  -26.495 1.00 112.29 ? 9   LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? -6.415  17.453  -25.999 1.00 102.76 ? 9   LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? -4.923  17.658  -25.778 1.00 102.96 ? 9   LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? -4.285  16.793  -25.167 1.00 106.21 ? 9   LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? -6.615  16.273  -26.963 1.00 105.25 ? 9   LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? -8.061  15.952  -27.348 1.00 103.59 ? 9   LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? -8.120  14.740  -28.267 1.00 100.13 ? 9   LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? -8.915  15.733  -26.109 1.00 100.42 ? 9   LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? -4.351  18.763  -26.249 1.00 100.97 ? 10  ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? -2.924  19.042  -26.103 1.00 97.56  ? 10  ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? -2.744  19.994  -24.925 1.00 84.92  ? 10  ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? -2.984  21.198  -25.043 1.00 81.97  ? 10  ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? -2.351  19.626  -27.390 1.00 96.53  ? 10  ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? -0.845  19.798  -27.333 1.00 85.19  ? 10  ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? -0.235  19.389  -26.324 1.00 85.15  ? 10  ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? -0.271  20.343  -28.300 1.00 87.77  ? 10  ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? -2.317  19.447  -23.784 1.00 86.87  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? -2.084  20.227  -22.574 1.00 84.91  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? -0.666  20.780  -22.493 1.00 72.37  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? -0.131  20.945  -21.388 1.00 69.18  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? -2.395  19.381  -21.338 1.00 82.88  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? -3.864  19.215  -21.070 1.00 85.15  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? -4.626  18.338  -21.824 1.00 84.59  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? -4.481  19.933  -20.059 1.00 81.32  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? -5.978  18.184  -21.577 1.00 87.51  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? -5.832  19.783  -19.807 1.00 73.62  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? -6.581  18.908  -20.567 1.00 84.51  ? 11  PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? -0.040  21.074  -23.635 1.00 72.16  ? 12  SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? 1.317   21.609  -23.612 1.00 70.20  ? 12  SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? 1.354   23.033  -23.073 1.00 75.05  ? 12  SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? 2.364   23.447  -22.492 1.00 68.25  ? 12  SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? 1.926   21.557  -25.013 1.00 71.73  ? 12  SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? 2.010   20.224  -25.484 1.00 85.85  ? 12  SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? 0.275   23.792  -23.253 1.00 75.38  ? 13  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? 0.212   25.175  -22.797 1.00 57.13  ? 13  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? -0.128  25.301  -21.317 1.00 59.93  ? 13  ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? -0.453  26.405  -20.865 1.00 67.22  ? 13  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? -0.807  25.956  -23.631 1.00 57.50  ? 13  ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? -0.064  24.207  -20.554 1.00 66.71  ? 14  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? -0.356  24.241  -19.127 1.00 65.17  ? 14  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? 0.769   23.657  -18.281 1.00 58.83  ? 14  LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? 0.576   23.446  -17.078 1.00 59.36  ? 14  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? -1.665  23.501  -18.824 1.00 64.51  ? 14  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? -2.914  24.207  -19.325 1.00 68.31  ? 14  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? -4.171  23.462  -18.898 1.00 74.47  ? 14  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? -5.428  24.213  -19.306 1.00 85.00  ? 14  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? -5.517  24.394  -20.781 1.00 88.64  ? 14  LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? 1.932   23.393  -18.868 1.00 53.39  ? 15  VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? 3.057   22.809  -18.146 1.00 60.17  ? 15  VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? 3.905   23.947  -17.588 1.00 56.91  ? 15  VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? 4.573   24.663  -18.339 1.00 54.46  ? 15  VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? 3.886   21.887  -19.047 1.00 63.34  ? 15  VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? 5.066   21.315  -18.276 1.00 52.70  ? 15  VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? 3.016   20.771  -19.606 1.00 54.22  ? 15  VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? 3.879   24.115  -16.264 1.00 51.78  ? 16  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? 4.688   25.151  -15.632 1.00 58.47  ? 16  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? 6.122   24.695  -15.398 1.00 54.28  ? 16  ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? 7.001   25.534  -15.165 1.00 55.26  ? 16  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? 4.061   25.602  -14.302 1.00 55.05  ? 16  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? 4.039   24.445  -13.302 1.00 43.85  ? 16  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? 2.657   26.138  -14.532 1.00 55.17  ? 16  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? 3.447   24.812  -11.959 1.00 45.27  ? 16  ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? 6.382   23.390  -15.452 1.00 52.54  ? 17  GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? 7.734   22.868  -15.298 1.00 53.25  ? 17  GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? 7.813   21.517  -15.990 1.00 51.13  ? 17  GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? 6.913   20.687  -15.833 1.00 52.13  ? 17  GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? 8.117   22.735  -13.819 1.00 52.79  ? 17  GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? 9.447   22.032  -13.593 1.00 52.31  ? 17  GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? 9.771   21.844  -12.124 1.00 53.70  ? 17  GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? 9.204   22.513  -11.260 1.00 64.59  ? 17  GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? 10.685  20.927  -11.833 1.00 48.45  ? 17  GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? 8.880   21.304  -16.747 1.00 48.22  ? 18  GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? 9.078   20.056  -17.456 1.00 52.65  ? 18  GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? 8.656   20.141  -18.908 1.00 62.60  ? 18  GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? 8.445   21.216  -19.478 1.00 67.06  ? 18  GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? 8.532   18.963  -19.514 1.00 64.26  ? 19  SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? 8.154   18.856  -20.916 1.00 66.09  ? 19  SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? 7.488   17.511  -21.153 1.00 75.43  ? 19  SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? 8.070   16.466  -20.846 1.00 81.93  ? 19  SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? 9.374   19.013  -21.831 1.00 71.29  ? 19  SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? 9.021   18.823  -23.189 1.00 83.13  ? 19  SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? 6.269   17.541  -21.697 1.00 75.61  ? 20  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? 5.587   16.303  -22.054 1.00 82.18  ? 20  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? 6.311   15.548  -23.159 1.00 88.37  ? 20  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? 6.100   14.339  -23.309 1.00 86.74  ? 20  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? 4.147   16.597  -22.481 1.00 72.36  ? 20  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? 3.234   17.224  -21.426 1.00 75.70  ? 20  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? 1.842   17.459  -21.992 1.00 76.15  ? 20  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? 3.170   16.351  -20.183 1.00 68.70  ? 20  LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? 7.158   16.230  -23.933 1.00 85.37  ? 21  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? 7.901   15.555  -24.991 1.00 97.96  ? 21  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? 8.987   14.656  -24.414 1.00 103.02 ? 21  ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? 9.254   13.573  -24.949 1.00 106.17 ? 21  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? 8.508   16.586  -25.942 1.00 108.73 ? 21  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? 7.501   17.627  -26.393 1.00 111.20 ? 21  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? 6.300   17.297  -26.483 1.00 101.36 ? 21  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? 7.912   18.778  -26.655 1.00 114.86 ? 21  ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? 9.622   15.086  -23.322 1.00 94.07  ? 22  SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? 10.677  14.299  -22.697 1.00 92.81  ? 22  SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? 10.150  13.063  -21.981 1.00 96.78  ? 22  SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? 10.952  12.215  -21.575 1.00 101.88 ? 22  SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? 11.465  15.168  -21.714 1.00 93.64  ? 22  SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? 10.611  15.727  -20.731 1.00 92.68  ? 22  SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? 8.834   12.938  -21.815 1.00 87.51  ? 23  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? 8.270   11.779  -21.146 1.00 89.97  ? 23  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? 8.164   10.597  -22.108 1.00 93.26  ? 23  LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? 7.958   10.781  -23.310 1.00 97.57  ? 23  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? 6.890   12.103  -20.586 1.00 82.04  ? 23  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? 6.818   13.070  -19.404 1.00 74.80  ? 23  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? 5.372   13.294  -18.990 1.00 74.74  ? 23  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? 7.637   12.549  -18.235 1.00 68.40  ? 23  LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? 8.305   9.375   -21.600 1.00 89.80  ? 24  PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? 8.093   8.194   -22.444 1.00 95.98  ? 24  PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? 6.692   8.190   -23.037 1.00 95.50  ? 24  PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? 5.810   8.957   -22.645 1.00 90.66  ? 24  PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? 8.301   7.022   -21.479 1.00 98.27  ? 24  PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? 9.167   7.581   -20.394 1.00 94.85  ? 24  PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? 8.749   9.015   -20.243 1.00 85.42  ? 24  PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? 6.490   7.299   -24.006 1.00 105.51 ? 25  GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? 5.216   7.230   -24.710 1.00 109.22 ? 25  GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? 4.076   6.893   -23.757 1.00 102.66 ? 25  GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? 3.184   7.717   -23.530 1.00 100.14 ? 25  GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? 5.287   6.203   -25.842 1.00 124.67 ? 25  GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? 3.989   6.044   -26.615 1.00 129.82 ? 25  GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? 4.134   5.136   -27.820 1.00 142.02 ? 25  GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? 5.245   4.854   -28.270 1.00 154.66 ? 25  GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? 3.008   4.671   -28.348 1.00 143.75 ? 25  GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? 4.095   5.684   -23.190 1.00 112.97 ? 26  GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? 3.019   5.268   -22.298 1.00 114.30 ? 26  GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? 2.924   6.141   -21.054 1.00 102.85 ? 26  GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? 1.855   6.202   -20.436 1.00 99.39  ? 26  GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? 3.207   3.804   -21.896 1.00 122.56 ? 26  GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? 2.980   2.818   -23.031 1.00 130.06 ? 26  GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? 1.546   2.823   -23.527 1.00 131.77 ? 26  GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? 0.666   3.330   -22.799 1.00 125.78 ? 26  GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? 1.300   2.323   -24.644 1.00 134.12 ? 26  GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? 4.009   6.814   -20.670 1.00 95.73  ? 27  VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? 3.957   7.689   -19.504 1.00 84.43  ? 27  VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? 3.189   8.964   -19.827 1.00 84.84  ? 27  VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? 2.404   9.457   -19.007 1.00 80.71  ? 27  VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? 5.379   7.996   -18.999 1.00 86.00  ? 27  VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? 5.326   8.956   -17.820 1.00 71.56  ? 27  VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? 6.093   6.709   -18.613 1.00 75.20  ? 27  VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? 3.396   9.518   -21.024 1.00 77.89  ? 28  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? 2.693   10.741  -21.396 1.00 71.96  ? 28  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? 1.204   10.487  -21.589 1.00 76.97  ? 28  ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? 0.371   11.297  -21.166 1.00 81.21  ? 28  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? 3.303   11.340  -22.662 1.00 78.46  ? 28  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? 2.593   12.597  -23.141 1.00 82.05  ? 28  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? 3.325   13.259  -24.297 1.00 90.99  ? 28  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? 2.648   14.473  -24.736 1.00 88.47  ? 28  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? 3.120   15.307  -25.653 1.00 81.95  ? 28  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? 4.280   15.092  -26.251 1.00 85.41  ? 28  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? 2.411   16.385  -25.976 1.00 85.77  ? 28  ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? 0.847   9.369   -22.226 1.00 84.33  ? 29  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? -0.565  9.053   -22.417 1.00 82.21  ? 29  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? -1.294  8.962   -21.083 1.00 73.02  ? 29  LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? -2.456  9.371   -20.972 1.00 68.04  ? 29  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? -0.714  7.748   -23.201 1.00 87.24  ? 29  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? -0.294  7.844   -24.658 1.00 88.91  ? 29  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? -0.640  6.572   -25.415 1.00 103.07 ? 29  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? -0.352  6.717   -26.900 1.00 115.85 ? 29  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? -0.760  5.507   -27.666 1.00 110.63 ? 29  LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? -0.627  8.430   -20.057 1.00 78.92  ? 30  PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? -1.253  8.327   -18.743 1.00 72.25  ? 30  PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? -1.500  9.699   -18.128 1.00 70.12  ? 30  PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? -2.459  9.871   -17.367 1.00 68.33  ? 30  PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? -0.388  7.471   -17.817 1.00 70.39  ? 30  PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? -0.870  7.435   -16.394 1.00 68.22  ? 30  PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? -2.120  6.925   -16.085 1.00 69.49  ? 30  PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? -0.067  7.897   -15.364 1.00 69.55  ? 30  PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? -2.564  6.887   -14.777 1.00 64.92  ? 30  PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? -0.505  7.860   -14.053 1.00 66.07  ? 30  PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? -1.756  7.354   -13.760 1.00 67.00  ? 30  PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? -0.659  10.681  -18.447 1.00 70.29  ? 31  VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? -0.815  12.016  -17.876 1.00 70.57  ? 31  VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? -1.939  12.773  -18.575 1.00 73.50  ? 31  VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? -2.910  13.202  -17.941 1.00 69.69  ? 31  VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? 0.514   12.790  -17.946 1.00 72.80  ? 31  VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? 0.336   14.200  -17.402 1.00 66.34  ? 31  VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? 1.599   12.050  -17.179 1.00 65.36  ? 31  VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? -1.823  12.948  -19.894 1.00 75.46  ? 32  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? -2.844  13.683  -20.633 1.00 78.14  ? 32  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? -4.205  13.005  -20.573 1.00 79.40  ? 32  GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? -5.227  13.676  -20.754 1.00 79.58  ? 32  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? -2.417  13.865  -22.091 1.00 79.22  ? 32  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? -1.403  14.977  -22.307 1.00 87.32  ? 32  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? -1.176  15.279  -23.775 1.00 90.67  ? 32  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? -1.520  14.425  -24.618 1.00 94.26  ? 32  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? -0.660  16.373  -24.085 1.00 86.23  ? 32  GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? -4.245  11.694  -20.328 1.00 74.87  ? 33  GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? -5.528  11.019  -20.209 1.00 68.13  ? 33  GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? -6.340  11.528  -19.034 1.00 66.26  ? 33  GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? -7.497  11.927  -19.187 1.00 70.42  ? 33  GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? -5.741  11.523  -17.842 1.00 63.66  ? 34  ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? -6.428  12.012  -16.655 1.00 56.35  ? 34  ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? -6.512  13.531  -16.610 1.00 67.65  ? 34  ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? -7.408  14.069  -15.951 1.00 74.71  ? 34  ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? -5.733  11.494  -15.394 1.00 69.62  ? 34  ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? -5.659  9.981   -15.352 1.00 61.48  ? 34  ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? -6.536  9.319   -14.797 1.00 53.06  ? 34  ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? -4.609  9.424   -15.943 1.00 67.17  ? 34  ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? -5.602  14.233  -17.290 1.00 64.31  ? 35  ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? -5.699  15.687  -17.359 1.00 70.55  ? 35  ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? -6.986  16.115  -18.051 1.00 72.89  ? 35  ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? -7.643  17.072  -17.625 1.00 76.95  ? 35  ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? -4.482  16.264  -18.080 1.00 74.42  ? 35  ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? -7.363  15.415  -19.124 1.00 78.86  ? 36  GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? -8.627  15.706  -19.791 1.00 80.92  ? 36  GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? -9.817  15.370  -18.903 1.00 78.93  ? 36  GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? -10.877 15.995  -19.025 1.00 78.65  ? 36  GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? -8.717  14.936  -21.108 1.00 88.08  ? 36  GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? -7.556  15.183  -22.058 1.00 94.74  ? 36  GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? -7.634  14.328  -23.309 1.00 104.79 ? 36  GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? -8.586  13.570  -23.499 1.00 111.55 ? 36  GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? -6.629  14.445  -24.169 1.00 107.81 ? 36  GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? -9.664  14.392  -18.007 1.00 74.98  ? 37  LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? -10.763 14.000  -17.132 1.00 72.44  ? 37  LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? -10.852 14.896  -15.903 1.00 77.36  ? 37  LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? -11.947 15.330  -15.526 1.00 63.39  ? 37  LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? -10.602 12.538  -16.714 1.00 77.46  ? 37  LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? -11.628 11.998  -15.715 1.00 80.55  ? 37  LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? -13.035 12.089  -16.286 1.00 67.97  ? 37  LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? -11.294 10.566  -15.326 1.00 78.13  ? 37  LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? -9.717  15.183  -15.265 1.00 75.20  ? 38  CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? -9.701  16.012  -14.067 1.00 69.99  ? 38  CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? -9.647  17.503  -14.371 1.00 66.25  ? 38  CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? -10.045 18.307  -13.520 1.00 63.33  ? 38  CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? -8.513  15.630  -13.178 1.00 72.07  ? 38  CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? -8.520  13.907  -12.628 1.00 65.73  ? 38  CYS A SG    1 
ATOM   277  N  N     . GLN A 1 39  ? -9.168  17.887  -15.553 1.00 63.70  ? 39  GLN A N     1 
ATOM   278  C  CA    . GLN A 1 39  ? -9.089  19.287  -15.952 1.00 78.05  ? 39  GLN A CA    1 
ATOM   279  C  C     . GLN A 1 39  ? -8.323  20.110  -14.923 1.00 73.45  ? 39  GLN A C     1 
ATOM   280  O  O     . GLN A 1 39  ? -8.918  20.938  -14.222 1.00 71.74  ? 39  GLN A O     1 
ATOM   281  C  CB    . GLN A 1 39  ? -10.488 19.873  -16.154 1.00 70.37  ? 39  GLN A CB    1 
ATOM   282  C  CG    . GLN A 1 39  ? -11.162 19.449  -17.447 1.00 73.83  ? 39  GLN A CG    1 
ATOM   283  C  CD    . GLN A 1 39  ? -12.423 20.242  -17.730 1.00 81.62  ? 39  GLN A CD    1 
ATOM   284  O  OE1   . GLN A 1 39  ? -12.993 20.865  -16.834 1.00 79.49  ? 39  GLN A OE1   1 
ATOM   285  N  NE2   . GLN A 1 39  ? -12.861 20.228  -18.984 1.00 85.39  ? 39  GLN A NE2   1 
ATOM   286  N  N     . PRO A 1 40  ? -7.014  19.913  -14.799 1.00 71.75  ? 40  PRO A N     1 
ATOM   287  C  CA    . PRO A 1 40  ? -6.226  20.751  -13.894 1.00 71.51  ? 40  PRO A CA    1 
ATOM   288  C  C     . PRO A 1 40  ? -5.879  22.087  -14.530 1.00 69.67  ? 40  PRO A C     1 
ATOM   289  O  O     . PRO A 1 40  ? -5.778  22.219  -15.752 1.00 70.64  ? 40  PRO A O     1 
ATOM   290  C  CB    . PRO A 1 40  ? -4.967  19.912  -13.651 1.00 62.58  ? 40  PRO A CB    1 
ATOM   291  C  CG    . PRO A 1 40  ? -4.806  19.139  -14.917 1.00 60.93  ? 40  PRO A CG    1 
ATOM   292  C  CD    . PRO A 1 40  ? -6.203  18.848  -15.415 1.00 71.19  ? 40  PRO A CD    1 
ATOM   293  N  N     . GLU A 1 41  ? -5.700  23.094  -13.671 1.00 71.04  ? 41  GLU A N     1 
ATOM   294  C  CA    . GLU A 1 41  ? -5.309  24.410  -14.163 1.00 68.11  ? 41  GLU A CA    1 
ATOM   295  C  C     . GLU A 1 41  ? -3.885  24.393  -14.704 1.00 66.41  ? 41  GLU A C     1 
ATOM   296  O  O     . GLU A 1 41  ? -3.590  25.039  -15.716 1.00 69.31  ? 41  GLU A O     1 
ATOM   297  C  CB    . GLU A 1 41  ? -5.451  25.451  -13.053 1.00 67.40  ? 41  GLU A CB    1 
ATOM   298  C  CG    . GLU A 1 41  ? -5.372  26.892  -13.535 1.00 63.71  ? 41  GLU A CG    1 
ATOM   299  C  CD    . GLU A 1 41  ? -6.621  27.327  -14.279 1.00 77.64  ? 41  GLU A CD    1 
ATOM   300  O  OE1   . GLU A 1 41  ? -7.690  26.723  -14.051 1.00 89.55  ? 41  GLU A OE1   1 
ATOM   301  O  OE2   . GLU A 1 41  ? -6.533  28.272  -15.092 1.00 78.80  ? 41  GLU A OE2   1 
ATOM   302  N  N     . TYR A 1 42  ? -2.991  23.657  -14.046 1.00 59.68  ? 42  TYR A N     1 
ATOM   303  C  CA    . TYR A 1 42  ? -1.603  23.554  -14.469 1.00 64.65  ? 42  TYR A CA    1 
ATOM   304  C  C     . TYR A 1 42  ? -1.128  22.120  -14.287 1.00 58.88  ? 42  TYR A C     1 
ATOM   305  O  O     . TYR A 1 42  ? -1.752  21.319  -13.586 1.00 59.53  ? 42  TYR A O     1 
ATOM   306  C  CB    . TYR A 1 42  ? -0.694  24.510  -13.682 1.00 55.42  ? 42  TYR A CB    1 
ATOM   307  C  CG    . TYR A 1 42  ? -1.275  25.892  -13.485 1.00 59.36  ? 42  TYR A CG    1 
ATOM   308  C  CD1   . TYR A 1 42  ? -1.289  26.816  -14.521 1.00 56.60  ? 42  TYR A CD1   1 
ATOM   309  C  CD2   . TYR A 1 42  ? -1.806  26.274  -12.260 1.00 56.46  ? 42  TYR A CD2   1 
ATOM   310  C  CE1   . TYR A 1 42  ? -1.819  28.079  -14.344 1.00 57.69  ? 42  TYR A CE1   1 
ATOM   311  C  CE2   . TYR A 1 42  ? -2.337  27.535  -12.073 1.00 52.74  ? 42  TYR A CE2   1 
ATOM   312  C  CZ    . TYR A 1 42  ? -2.341  28.434  -13.118 1.00 60.71  ? 42  TYR A CZ    1 
ATOM   313  O  OH    . TYR A 1 42  ? -2.870  29.691  -12.937 1.00 57.47  ? 42  TYR A OH    1 
ATOM   314  N  N     . ILE A 1 43  ? -0.007  21.803  -14.932 1.00 50.69  ? 43  ILE A N     1 
ATOM   315  C  CA    . ILE A 1 43  ? 0.642   20.504  -14.809 1.00 58.29  ? 43  ILE A CA    1 
ATOM   316  C  C     . ILE A 1 43  ? 2.089   20.737  -14.403 1.00 56.80  ? 43  ILE A C     1 
ATOM   317  O  O     . ILE A 1 43  ? 2.795   21.532  -15.034 1.00 54.12  ? 43  ILE A O     1 
ATOM   318  C  CB    . ILE A 1 43  ? 0.567   19.694  -16.118 1.00 53.46  ? 43  ILE A CB    1 
ATOM   319  C  CG1   . ILE A 1 43  ? -0.890  19.407  -16.486 1.00 42.71  ? 43  ILE A CG1   1 
ATOM   320  C  CG2   . ILE A 1 43  ? 1.354   18.399  -15.987 1.00 45.12  ? 43  ILE A CG2   1 
ATOM   321  C  CD1   . ILE A 1 43  ? -1.051  18.613  -17.764 1.00 54.16  ? 43  ILE A CD1   1 
ATOM   322  N  N     . HIS A 1 44  ? 2.529   20.047  -13.352 1.00 41.67  ? 44  HIS A N     1 
ATOM   323  C  CA    . HIS A 1 44  ? 3.864   20.234  -12.786 1.00 53.50  ? 44  HIS A CA    1 
ATOM   324  C  C     . HIS A 1 44  ? 4.571   18.883  -12.749 1.00 40.80  ? 44  HIS A C     1 
ATOM   325  O  O     . HIS A 1 44  ? 4.289   18.051  -11.881 1.00 46.47  ? 44  HIS A O     1 
ATOM   326  C  CB    . HIS A 1 44  ? 3.781   20.856  -11.395 1.00 50.11  ? 44  HIS A CB    1 
ATOM   327  C  CG    . HIS A 1 44  ? 5.111   21.226  -10.816 1.00 55.17  ? 44  HIS A CG    1 
ATOM   328  N  ND1   . HIS A 1 44  ? 5.887   20.336  -10.104 1.00 53.95  ? 44  HIS A ND1   1 
ATOM   329  C  CD2   . HIS A 1 44  ? 5.800   22.391  -10.839 1.00 58.91  ? 44  HIS A CD2   1 
ATOM   330  C  CE1   . HIS A 1 44  ? 6.998   20.937  -9.716  1.00 45.07  ? 44  HIS A CE1   1 
ATOM   331  N  NE2   . HIS A 1 44  ? 6.970   22.184  -10.149 1.00 59.41  ? 44  HIS A NE2   1 
ATOM   332  N  N     . ILE A 1 45  ? 5.486   18.666  -13.689 1.00 38.82  ? 45  ILE A N     1 
ATOM   333  C  CA    . ILE A 1 45  ? 6.279   17.442  -13.723 1.00 47.95  ? 45  ILE A CA    1 
ATOM   334  C  C     . ILE A 1 45  ? 7.440   17.595  -12.748 1.00 41.56  ? 45  ILE A C     1 
ATOM   335  O  O     . ILE A 1 45  ? 8.276   18.493  -12.898 1.00 50.32  ? 45  ILE A O     1 
ATOM   336  C  CB    . ILE A 1 45  ? 6.781   17.146  -15.143 1.00 51.50  ? 45  ILE A CB    1 
ATOM   337  C  CG1   . ILE A 1 45  ? 5.622   17.204  -16.140 1.00 48.85  ? 45  ILE A CG1   1 
ATOM   338  C  CG2   . ILE A 1 45  ? 7.455   15.783  -15.196 1.00 44.86  ? 45  ILE A CG2   1 
ATOM   339  C  CD1   . ILE A 1 45  ? 6.037   16.965  -17.575 1.00 55.88  ? 45  ILE A CD1   1 
ATOM   340  N  N     . CYS A 1 46  ? 7.494   16.720  -11.749 1.00 42.29  ? 46  CYS A N     1 
ATOM   341  C  CA    . CYS A 1 46  ? 8.463   16.857  -10.672 1.00 47.92  ? 46  CYS A CA    1 
ATOM   342  C  C     . CYS A 1 46  ? 9.850   16.396  -11.106 1.00 44.32  ? 46  CYS A C     1 
ATOM   343  O  O     . CYS A 1 46  ? 10.002  15.490  -11.930 1.00 47.77  ? 46  CYS A O     1 
ATOM   344  C  CB    . CYS A 1 46  ? 8.019   16.059  -9.445  1.00 33.80  ? 46  CYS A CB    1 
ATOM   345  S  SG    . CYS A 1 46  ? 6.525   16.684  -8.646  1.00 45.60  ? 46  CYS A SG    1 
ATOM   346  N  N     . ASP A 1 47  ? 10.870  17.040  -10.534 1.00 50.42  ? 47  ASP A N     1 
ATOM   347  C  CA    . ASP A 1 47  ? 12.255  16.631  -10.715 1.00 40.41  ? 47  ASP A CA    1 
ATOM   348  C  C     . ASP A 1 47  ? 12.961  16.301  -9.408  1.00 47.56  ? 47  ASP A C     1 
ATOM   349  O  O     . ASP A 1 47  ? 14.111  15.849  -9.446  1.00 51.52  ? 47  ASP A O     1 
ATOM   350  C  CB    . ASP A 1 47  ? 13.051  17.719  -11.456 1.00 41.43  ? 47  ASP A CB    1 
ATOM   351  C  CG    . ASP A 1 47  ? 13.162  19.008  -10.663 1.00 37.79  ? 47  ASP A CG    1 
ATOM   352  O  OD1   . ASP A 1 47  ? 12.575  19.094  -9.564  1.00 37.95  ? 47  ASP A OD1   1 
ATOM   353  O  OD2   . ASP A 1 47  ? 13.842  19.939  -11.142 1.00 41.06  ? 47  ASP A OD2   1 
ATOM   354  N  N     . GLY A 1 48  ? 12.317  16.518  -8.262  1.00 38.51  ? 48  GLY A N     1 
ATOM   355  C  CA    . GLY A 1 48  ? 12.887  16.155  -6.981  1.00 51.70  ? 48  GLY A CA    1 
ATOM   356  C  C     . GLY A 1 48  ? 14.055  16.995  -6.521  1.00 49.00  ? 48  GLY A C     1 
ATOM   357  O  O     . GLY A 1 48  ? 14.677  16.658  -5.509  1.00 52.42  ? 48  GLY A O     1 
ATOM   358  N  N     . SER A 1 49  ? 14.372  18.080  -7.221  1.00 45.18  ? 49  SER A N     1 
ATOM   359  C  CA    . SER A 1 49  ? 15.517  18.897  -6.852  1.00 61.55  ? 49  SER A CA    1 
ATOM   360  C  C     . SER A 1 49  ? 15.234  19.689  -5.577  1.00 66.99  ? 49  SER A C     1 
ATOM   361  O  O     . SER A 1 49  ? 14.083  19.930  -5.200  1.00 67.30  ? 49  SER A O     1 
ATOM   362  C  CB    . SER A 1 49  ? 15.881  19.853  -7.988  1.00 49.51  ? 49  SER A CB    1 
ATOM   363  O  OG    . SER A 1 49  ? 14.826  20.762  -8.247  1.00 48.99  ? 49  SER A OG    1 
ATOM   364  N  N     . GLU A 1 50  ? 16.315  20.094  -4.906  1.00 68.75  ? 50  GLU A N     1 
ATOM   365  C  CA    . GLU A 1 50  ? 16.176  20.927  -3.715  1.00 70.07  ? 50  GLU A CA    1 
ATOM   366  C  C     . GLU A 1 50  ? 15.477  22.239  -4.042  1.00 74.30  ? 50  GLU A C     1 
ATOM   367  O  O     . GLU A 1 50  ? 14.684  22.747  -3.239  1.00 73.81  ? 50  GLU A O     1 
ATOM   368  C  CB    . GLU A 1 50  ? 17.550  21.190  -3.096  1.00 80.49  ? 50  GLU A CB    1 
ATOM   369  C  CG    . GLU A 1 50  ? 18.209  19.963  -2.483  1.00 91.03  ? 50  GLU A CG    1 
ATOM   370  C  CD    . GLU A 1 50  ? 17.659  19.630  -1.109  1.00 96.65  ? 50  GLU A CD    1 
ATOM   371  O  OE1   . GLU A 1 50  ? 16.952  20.481  -0.528  1.00 94.86  ? 50  GLU A OE1   1 
ATOM   372  O  OE2   . GLU A 1 50  ? 17.937  18.520  -0.609  1.00 88.77  ? 50  GLU A OE2   1 
ATOM   373  N  N     . GLU A 1 51  ? 15.760  22.807  -5.216  1.00 73.37  ? 51  GLU A N     1 
ATOM   374  C  CA    . GLU A 1 51  ? 15.094  24.039  -5.623  1.00 73.94  ? 51  GLU A CA    1 
ATOM   375  C  C     . GLU A 1 51  ? 13.587  23.842  -5.719  1.00 69.76  ? 51  GLU A C     1 
ATOM   376  O  O     . GLU A 1 51  ? 12.810  24.717  -5.321  1.00 66.40  ? 51  GLU A O     1 
ATOM   377  C  CB    . GLU A 1 51  ? 15.660  24.520  -6.959  1.00 83.43  ? 51  GLU A CB    1 
ATOM   378  C  CG    . GLU A 1 51  ? 17.172  24.684  -6.966  1.00 113.39 ? 51  GLU A CG    1 
ATOM   379  C  CD    . GLU A 1 51  ? 17.723  24.954  -8.352  1.00 143.14 ? 51  GLU A CD    1 
ATOM   380  O  OE1   . GLU A 1 51  ? 16.954  24.842  -9.330  1.00 144.86 ? 51  GLU A OE1   1 
ATOM   381  O  OE2   . GLU A 1 51  ? 18.924  25.279  -8.464  1.00 152.44 ? 51  GLU A OE2   1 
ATOM   382  N  N     . GLU A 1 52  ? 13.156  22.694  -6.247  1.00 72.83  ? 52  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 52  ? 11.728  22.410  -6.342  1.00 64.20  ? 52  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 52  ? 11.111  22.202  -4.964  1.00 64.10  ? 52  GLU A C     1 
ATOM   385  O  O     . GLU A 1 52  ? 9.994   22.662  -4.703  1.00 50.60  ? 52  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 52  ? 11.500  21.186  -7.229  1.00 50.09  ? 52  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 52  ? 10.173  20.483  -7.002  1.00 52.79  ? 52  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 52  ? 9.977   19.302  -7.933  1.00 52.05  ? 52  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 52  ? 9.817   19.524  -9.152  1.00 48.50  ? 52  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 52  ? 9.997   18.151  -7.448  1.00 54.24  ? 52  GLU A OE2   1 
ATOM   391  N  N     . TYR A 1 53  ? 11.823  21.512  -4.070  1.00 62.27  ? 53  TYR A N     1 
ATOM   392  C  CA    . TYR A 1 53  ? 11.289  21.277  -2.732  1.00 55.38  ? 53  TYR A CA    1 
ATOM   393  C  C     . TYR A 1 53  ? 11.160  22.580  -1.952  1.00 66.71  ? 53  TYR A C     1 
ATOM   394  O  O     . TYR A 1 53  ? 10.153  22.803  -1.269  1.00 63.75  ? 53  TYR A O     1 
ATOM   395  C  CB    . TYR A 1 53  ? 12.173  20.282  -1.981  1.00 61.00  ? 53  TYR A CB    1 
ATOM   396  C  CG    . TYR A 1 53  ? 11.648  19.907  -0.614  1.00 60.14  ? 53  TYR A CG    1 
ATOM   397  C  CD1   . TYR A 1 53  ? 10.520  19.109  -0.478  1.00 54.38  ? 53  TYR A CD1   1 
ATOM   398  C  CD2   . TYR A 1 53  ? 12.286  20.343  0.539   1.00 55.44  ? 53  TYR A CD2   1 
ATOM   399  C  CE1   . TYR A 1 53  ? 10.037  18.762  0.769   1.00 48.92  ? 53  TYR A CE1   1 
ATOM   400  C  CE2   . TYR A 1 53  ? 11.810  20.000  1.791   1.00 54.59  ? 53  TYR A CE2   1 
ATOM   401  C  CZ    . TYR A 1 53  ? 10.686  19.209  1.900   1.00 56.10  ? 53  TYR A CZ    1 
ATOM   402  O  OH    . TYR A 1 53  ? 10.208  18.865  3.143   1.00 52.79  ? 53  TYR A OH    1 
ATOM   403  N  N     . GLY A 1 54  ? 12.166  23.452  -2.041  1.00 68.66  ? 54  GLY A N     1 
ATOM   404  C  CA    . GLY A 1 54  ? 12.071  24.739  -1.372  1.00 73.55  ? 54  GLY A CA    1 
ATOM   405  C  C     . GLY A 1 54  ? 10.947  25.596  -1.920  1.00 80.85  ? 54  GLY A C     1 
ATOM   406  O  O     . GLY A 1 54  ? 10.227  26.253  -1.164  1.00 80.21  ? 54  GLY A O     1 
ATOM   407  N  N     . ARG A 1 55  ? 10.781  25.602  -3.245  1.00 92.50  ? 55  ARG A N     1 
ATOM   408  C  CA    . ARG A 1 55  ? 9.684   26.351  -3.849  1.00 95.50  ? 55  ARG A CA    1 
ATOM   409  C  C     . ARG A 1 55  ? 8.337   25.706  -3.552  1.00 87.47  ? 55  ARG A C     1 
ATOM   410  O  O     . ARG A 1 55  ? 7.308   26.392  -3.553  1.00 87.03  ? 55  ARG A O     1 
ATOM   411  C  CB    . ARG A 1 55  ? 9.905   26.470  -5.356  1.00 95.00  ? 55  ARG A CB    1 
ATOM   412  C  CG    . ARG A 1 55  ? 8.807   27.208  -6.099  1.00 108.35 ? 55  ARG A CG    1 
ATOM   413  C  CD    . ARG A 1 55  ? 9.197   27.439  -7.550  1.00 110.50 ? 55  ARG A CD    1 
ATOM   414  N  NE    . ARG A 1 55  ? 9.655   26.211  -8.190  1.00 112.49 ? 55  ARG A NE    1 
ATOM   415  C  CZ    . ARG A 1 55  ? 8.866   25.361  -8.833  1.00 114.64 ? 55  ARG A CZ    1 
ATOM   416  N  NH1   . ARG A 1 55  ? 7.566   25.575  -8.947  1.00 108.81 ? 55  ARG A NH1   1 
ATOM   417  N  NH2   . ARG A 1 55  ? 9.396   24.268  -9.374  1.00 103.64 ? 55  ARG A NH2   1 
ATOM   418  N  N     . LEU A 1 56  ? 8.320   24.396  -3.294  1.00 79.12  ? 56  LEU A N     1 
ATOM   419  C  CA    . LEU A 1 56  ? 7.073   23.726  -2.943  1.00 74.76  ? 56  LEU A CA    1 
ATOM   420  C  C     . LEU A 1 56  ? 6.629   24.075  -1.529  1.00 76.80  ? 56  LEU A C     1 
ATOM   421  O  O     . LEU A 1 56  ? 5.425   24.109  -1.248  1.00 74.40  ? 56  LEU A O     1 
ATOM   422  C  CB    . LEU A 1 56  ? 7.231   22.213  -3.094  1.00 68.33  ? 56  LEU A CB    1 
ATOM   423  C  CG    . LEU A 1 56  ? 5.986   21.354  -2.864  1.00 55.17  ? 56  LEU A CG    1 
ATOM   424  C  CD1   . LEU A 1 56  ? 4.974   21.562  -3.980  1.00 73.53  ? 56  LEU A CD1   1 
ATOM   425  C  CD2   . LEU A 1 56  ? 6.361   19.885  -2.738  1.00 62.29  ? 56  LEU A CD2   1 
ATOM   426  N  N     . LEU A 1 57  ? 7.580   24.335  -0.628  1.00 83.45  ? 57  LEU A N     1 
ATOM   427  C  CA    . LEU A 1 57  ? 7.224   24.694  0.741   1.00 80.95  ? 57  LEU A CA    1 
ATOM   428  C  C     . LEU A 1 57  ? 6.632   26.096  0.811   1.00 83.97  ? 57  LEU A C     1 
ATOM   429  O  O     . LEU A 1 57  ? 5.697   26.343  1.582   1.00 85.85  ? 57  LEU A O     1 
ATOM   430  C  CB    . LEU A 1 57  ? 8.451   24.587  1.648   1.00 72.10  ? 57  LEU A CB    1 
ATOM   431  C  CG    . LEU A 1 57  ? 8.944   23.177  1.979   1.00 64.99  ? 57  LEU A CG    1 
ATOM   432  C  CD1   . LEU A 1 57  ? 10.226  23.235  2.796   1.00 62.03  ? 57  LEU A CD1   1 
ATOM   433  C  CD2   . LEU A 1 57  ? 7.868   22.401  2.722   1.00 60.55  ? 57  LEU A CD2   1 
ATOM   434  N  N     . ALA A 1 58  ? 7.163   27.028  0.015   1.00 97.25  ? 58  ALA A N     1 
ATOM   435  C  CA    . ALA A 1 58  ? 6.672   28.401  0.057   1.00 95.74  ? 58  ALA A CA    1 
ATOM   436  C  C     . ALA A 1 58  ? 5.199   28.475  -0.325  1.00 91.80  ? 58  ALA A C     1 
ATOM   437  O  O     . ALA A 1 58  ? 4.438   29.260  0.253   1.00 93.53  ? 58  ALA A O     1 
ATOM   438  C  CB    . ALA A 1 58  ? 7.511   29.288  -0.862  1.00 93.75  ? 58  ALA A CB    1 
ATOM   439  N  N     . HIS A 1 59  ? 4.777   27.665  -1.298  1.00 84.10  ? 59  HIS A N     1 
ATOM   440  C  CA    . HIS A 1 59  ? 3.382   27.689  -1.726  1.00 78.37  ? 59  HIS A CA    1 
ATOM   441  C  C     . HIS A 1 59  ? 2.455   27.266  -0.593  1.00 81.95  ? 59  HIS A C     1 
ATOM   442  O  O     . HIS A 1 59  ? 1.464   27.944  -0.299  1.00 83.19  ? 59  HIS A O     1 
ATOM   443  C  CB    . HIS A 1 59  ? 3.192   26.786  -2.946  1.00 83.84  ? 59  HIS A CB    1 
ATOM   444  C  CG    . HIS A 1 59  ? 1.824   26.869  -3.550  1.00 87.14  ? 59  HIS A CG    1 
ATOM   445  N  ND1   . HIS A 1 59  ? 1.192   25.780  -4.112  1.00 84.05  ? 59  HIS A ND1   1 
ATOM   446  C  CD2   . HIS A 1 59  ? 0.971   27.911  -3.685  1.00 82.96  ? 59  HIS A CD2   1 
ATOM   447  C  CE1   . HIS A 1 59  ? 0.006   26.148  -4.564  1.00 88.53  ? 59  HIS A CE1   1 
ATOM   448  N  NE2   . HIS A 1 59  ? -0.153  27.436  -4.318  1.00 92.31  ? 59  HIS A NE2   1 
ATOM   449  N  N     . MET A 1 60  ? 2.764   26.141  0.057   1.00 85.59  ? 60  MET A N     1 
ATOM   450  C  CA    . MET A 1 60  ? 1.922   25.668  1.151   1.00 76.17  ? 60  MET A CA    1 
ATOM   451  C  C     . MET A 1 60  ? 1.891   26.668  2.299   1.00 76.60  ? 60  MET A C     1 
ATOM   452  O  O     . MET A 1 60  ? 0.840   26.885  2.915   1.00 70.86  ? 60  MET A O     1 
ATOM   453  C  CB    . MET A 1 60  ? 2.409   24.303  1.639   1.00 71.71  ? 60  MET A CB    1 
ATOM   454  C  CG    . MET A 1 60  ? 2.196   23.175  0.643   1.00 69.74  ? 60  MET A CG    1 
ATOM   455  S  SD    . MET A 1 60  ? 2.681   21.564  1.292   1.00 65.48  ? 60  MET A SD    1 
ATOM   456  C  CE    . MET A 1 60  ? 4.447   21.793  1.482   1.00 70.41  ? 60  MET A CE    1 
ATOM   457  N  N     . GLN A 1 61  ? 3.033   27.289  2.604   1.00 74.68  ? 61  GLN A N     1 
ATOM   458  C  CA    . GLN A 1 61  ? 3.070   28.264  3.688   1.00 80.39  ? 61  GLN A CA    1 
ATOM   459  C  C     . GLN A 1 61  ? 2.260   29.507  3.340   1.00 87.55  ? 61  GLN A C     1 
ATOM   460  O  O     . GLN A 1 61  ? 1.536   30.041  4.189   1.00 89.40  ? 61  GLN A O     1 
ATOM   461  C  CB    . GLN A 1 61  ? 4.516   28.640  4.012   1.00 80.69  ? 61  GLN A CB    1 
ATOM   462  C  CG    . GLN A 1 61  ? 4.658   29.557  5.217   1.00 76.52  ? 61  GLN A CG    1 
ATOM   463  C  CD    . GLN A 1 61  ? 6.095   29.962  5.475   1.00 82.49  ? 61  GLN A CD    1 
ATOM   464  O  OE1   . GLN A 1 61  ? 6.957   29.823  4.607   1.00 89.38  ? 61  GLN A OE1   1 
ATOM   465  N  NE2   . GLN A 1 61  ? 6.362   30.464  6.675   1.00 86.12  ? 61  GLN A NE2   1 
ATOM   466  N  N     . GLU A 1 62  ? 2.368   29.982  2.098   1.00 90.65  ? 62  GLU A N     1 
ATOM   467  C  CA    . GLU A 1 62  ? 1.598   31.140  1.663   1.00 92.50  ? 62  GLU A CA    1 
ATOM   468  C  C     . GLU A 1 62  ? 0.127   30.817  1.438   1.00 86.37  ? 62  GLU A C     1 
ATOM   469  O  O     . GLU A 1 62  ? -0.662  31.738  1.199   1.00 93.04  ? 62  GLU A O     1 
ATOM   470  C  CB    . GLU A 1 62  ? 2.210   31.721  0.386   1.00 92.26  ? 62  GLU A CB    1 
ATOM   471  C  CG    . GLU A 1 62  ? 3.629   32.238  0.570   1.00 84.65  ? 62  GLU A CG    1 
ATOM   472  C  CD    . GLU A 1 62  ? 4.275   32.660  -0.735  1.00 76.95  ? 62  GLU A CD    1 
ATOM   473  O  OE1   . GLU A 1 62  ? 3.683   32.405  -1.804  1.00 74.36  ? 62  GLU A OE1   1 
ATOM   474  O  OE2   . GLU A 1 62  ? 5.378   33.246  -0.689  1.00 75.48  ? 62  GLU A OE2   1 
ATOM   475  N  N     . GLU A 1 63  ? -0.258  29.544  1.508   1.00 85.03  ? 63  GLU A N     1 
ATOM   476  C  CA    . GLU A 1 63  ? -1.649  29.129  1.400   1.00 81.43  ? 63  GLU A CA    1 
ATOM   477  C  C     . GLU A 1 63  ? -2.260  28.762  2.745   1.00 82.07  ? 63  GLU A C     1 
ATOM   478  O  O     . GLU A 1 63  ? -3.411  28.318  2.789   1.00 82.89  ? 63  GLU A O     1 
ATOM   479  C  CB    . GLU A 1 63  ? -1.774  27.943  0.436   1.00 83.93  ? 63  GLU A CB    1 
ATOM   480  C  CG    . GLU A 1 63  ? -1.568  28.299  -1.030  1.00 88.85  ? 63  GLU A CG    1 
ATOM   481  C  CD    . GLU A 1 63  ? -2.768  29.002  -1.636  1.00 95.13  ? 63  GLU A CD    1 
ATOM   482  O  OE1   . GLU A 1 63  ? -3.757  29.227  -0.907  1.00 103.20 ? 63  GLU A OE1   1 
ATOM   483  O  OE2   . GLU A 1 63  ? -2.724  29.325  -2.842  1.00 95.28  ? 63  GLU A OE2   1 
ATOM   484  N  N     . GLY A 1 64  ? -1.519  28.932  3.839   1.00 84.18  ? 64  GLY A N     1 
ATOM   485  C  CA    . GLY A 1 64  ? -2.046  28.624  5.153   1.00 83.69  ? 64  GLY A CA    1 
ATOM   486  C  C     . GLY A 1 64  ? -2.161  27.151  5.467   1.00 85.62  ? 64  GLY A C     1 
ATOM   487  O  O     . GLY A 1 64  ? -2.953  26.774  6.334   1.00 87.91  ? 64  GLY A O     1 
ATOM   488  N  N     . VAL A 1 65  ? -1.392  26.303  4.791   1.00 87.74  ? 65  VAL A N     1 
ATOM   489  C  CA    . VAL A 1 65  ? -1.454  24.863  5.025   1.00 86.35  ? 65  VAL A CA    1 
ATOM   490  C  C     . VAL A 1 65  ? -0.509  24.441  6.141   1.00 84.27  ? 65  VAL A C     1 
ATOM   491  O  O     . VAL A 1 65  ? -0.909  23.747  7.080   1.00 80.79  ? 65  VAL A O     1 
ATOM   492  C  CB    . VAL A 1 65  ? -1.155  24.101  3.717   1.00 84.45  ? 65  VAL A CB    1 
ATOM   493  C  CG1   . VAL A 1 65  ? -1.156  22.601  3.967   1.00 73.41  ? 65  VAL A CG1   1 
ATOM   494  C  CG2   . VAL A 1 65  ? -2.170  24.468  2.646   1.00 91.51  ? 65  VAL A CG2   1 
ATOM   495  N  N     . ILE A 1 66  ? 0.757   24.849  6.062   1.00 81.75  ? 66  ILE A N     1 
ATOM   496  C  CA    . ILE A 1 66  ? 1.761   24.459  7.040   1.00 71.78  ? 66  ILE A CA    1 
ATOM   497  C  C     . ILE A 1 66  ? 2.373   25.709  7.659   1.00 77.40  ? 66  ILE A C     1 
ATOM   498  O  O     . ILE A 1 66  ? 2.331   26.803  7.091   1.00 79.08  ? 66  ILE A O     1 
ATOM   499  C  CB    . ILE A 1 66  ? 2.862   23.572  6.422   1.00 64.27  ? 66  ILE A CB    1 
ATOM   500  C  CG1   . ILE A 1 66  ? 3.678   24.368  5.402   1.00 63.12  ? 66  ILE A CG1   1 
ATOM   501  C  CG2   . ILE A 1 66  ? 2.251   22.338  5.776   1.00 70.07  ? 66  ILE A CG2   1 
ATOM   502  C  CD1   . ILE A 1 66  ? 4.837   23.596  4.812   1.00 75.22  ? 66  ILE A CD1   1 
ATOM   503  N  N     . ARG A 1 67  ? 2.947   25.527  8.844   1.00 79.58  ? 67  ARG A N     1 
ATOM   504  C  CA    . ARG A 1 67  ? 3.665   26.574  9.550   1.00 75.81  ? 67  ARG A CA    1 
ATOM   505  C  C     . ARG A 1 67  ? 5.121   26.160  9.718   1.00 73.72  ? 67  ARG A C     1 
ATOM   506  O  O     . ARG A 1 67  ? 5.469   24.981  9.608   1.00 73.60  ? 67  ARG A O     1 
ATOM   507  C  CB    . ARG A 1 67  ? 3.033   26.859  10.919  1.00 84.01  ? 67  ARG A CB    1 
ATOM   508  C  CG    . ARG A 1 67  ? 1.538   27.132  10.862  1.00 94.93  ? 67  ARG A CG    1 
ATOM   509  C  CD    . ARG A 1 67  ? 0.963   27.388  12.246  1.00 111.41 ? 67  ARG A CD    1 
ATOM   510  N  NE    . ARG A 1 67  ? 1.510   28.595  12.853  1.00 121.36 ? 67  ARG A NE    1 
ATOM   511  C  CZ    . ARG A 1 67  ? 1.116   29.092  14.018  1.00 125.49 ? 67  ARG A CZ    1 
ATOM   512  N  NH1   . ARG A 1 67  ? 0.169   28.508  14.734  1.00 130.38 ? 67  ARG A NH1   1 
ATOM   513  N  NH2   . ARG A 1 67  ? 1.686   30.203  14.475  1.00 124.59 ? 67  ARG A NH2   1 
ATOM   514  N  N     . LYS A 1 68  ? 5.975   27.143  9.984   1.00 78.17  ? 68  LYS A N     1 
ATOM   515  C  CA    . LYS A 1 68  ? 7.405   26.912  10.132  1.00 68.21  ? 68  LYS A CA    1 
ATOM   516  C  C     . LYS A 1 68  ? 7.759   26.806  11.610  1.00 73.30  ? 68  LYS A C     1 
ATOM   517  O  O     . LYS A 1 68  ? 7.384   27.672  12.407  1.00 65.27  ? 68  LYS A O     1 
ATOM   518  C  CB    . LYS A 1 68  ? 8.213   28.031  9.473   1.00 69.00  ? 68  LYS A CB    1 
ATOM   519  C  CG    . LYS A 1 68  ? 9.688   27.700  9.296   1.00 65.14  ? 68  LYS A CG    1 
ATOM   520  C  CD    . LYS A 1 68  ? 10.427  28.810  8.567   1.00 64.54  ? 68  LYS A CD    1 
ATOM   521  C  CE    . LYS A 1 68  ? 11.839  28.382  8.197   1.00 67.63  ? 68  LYS A CE    1 
ATOM   522  N  NZ    . LYS A 1 68  ? 12.635  27.981  9.390   1.00 79.50  ? 68  LYS A NZ    1 
ATOM   523  N  N     . LEU A 1 69  ? 8.477   25.744  11.967  1.00 70.11  ? 69  LEU A N     1 
ATOM   524  C  CA    . LEU A 1 69  ? 8.932   25.525  13.338  1.00 72.32  ? 69  LEU A CA    1 
ATOM   525  C  C     . LEU A 1 69  ? 10.315  26.150  13.475  1.00 81.40  ? 69  LEU A C     1 
ATOM   526  O  O     . LEU A 1 69  ? 11.325  25.542  13.113  1.00 72.07  ? 69  LEU A O     1 
ATOM   527  C  CB    . LEU A 1 69  ? 8.944   24.037  13.668  1.00 67.88  ? 69  LEU A CB    1 
ATOM   528  C  CG    . LEU A 1 69  ? 7.587   23.335  13.565  1.00 67.23  ? 69  LEU A CG    1 
ATOM   529  C  CD1   . LEU A 1 69  ? 7.746   21.826  13.671  1.00 58.90  ? 69  LEU A CD1   1 
ATOM   530  C  CD2   . LEU A 1 69  ? 6.635   23.853  14.633  1.00 68.25  ? 69  LEU A CD2   1 
ATOM   531  N  N     . LYS A 1 70  ? 10.360  27.374  14.006  1.00 81.44  ? 70  LYS A N     1 
ATOM   532  C  CA    . LYS A 1 70  ? 11.601  28.138  14.030  1.00 82.62  ? 70  LYS A CA    1 
ATOM   533  C  C     . LYS A 1 70  ? 12.649  27.542  14.962  1.00 85.66  ? 70  LYS A C     1 
ATOM   534  O  O     . LYS A 1 70  ? 13.841  27.813  14.780  1.00 93.34  ? 70  LYS A O     1 
ATOM   535  C  CB    . LYS A 1 70  ? 11.318  29.586  14.431  1.00 82.44  ? 70  LYS A CB    1 
ATOM   536  C  CG    . LYS A 1 70  ? 10.438  30.341  13.448  1.00 99.89  ? 70  LYS A CG    1 
ATOM   537  C  CD    . LYS A 1 70  ? 10.265  31.793  13.862  1.00 112.95 ? 70  LYS A CD    1 
ATOM   538  C  CE    . LYS A 1 70  ? 9.439   32.563  12.843  1.00 112.31 ? 70  LYS A CE    1 
ATOM   539  N  NZ    . LYS A 1 70  ? 9.287   33.996  13.217  1.00 111.00 ? 70  LYS A NZ    1 
ATOM   540  N  N     . LYS A 1 71  ? 12.244  26.743  15.951  1.00 77.98  ? 71  LYS A N     1 
ATOM   541  C  CA    . LYS A 1 71  ? 13.214  26.218  16.905  1.00 67.90  ? 71  LYS A CA    1 
ATOM   542  C  C     . LYS A 1 71  ? 14.107  25.143  16.299  1.00 64.52  ? 71  LYS A C     1 
ATOM   543  O  O     . LYS A 1 71  ? 15.179  24.867  16.848  1.00 70.65  ? 71  LYS A O     1 
ATOM   544  C  CB    . LYS A 1 71  ? 12.503  25.664  18.140  1.00 72.59  ? 71  LYS A CB    1 
ATOM   545  C  CG    . LYS A 1 71  ? 13.457  25.195  19.229  1.00 67.83  ? 71  LYS A CG    1 
ATOM   546  C  CD    . LYS A 1 71  ? 12.739  24.963  20.548  1.00 75.81  ? 71  LYS A CD    1 
ATOM   547  C  CE    . LYS A 1 71  ? 13.734  24.705  21.669  1.00 79.25  ? 71  LYS A CE    1 
ATOM   548  N  NZ    . LYS A 1 71  ? 13.070  24.607  22.997  1.00 96.34  ? 71  LYS A NZ    1 
ATOM   549  N  N     . TYR A 1 72  ? 13.700  24.537  15.188  1.00 64.07  ? 72  TYR A N     1 
ATOM   550  C  CA    . TYR A 1 72  ? 14.463  23.473  14.557  1.00 60.07  ? 72  TYR A CA    1 
ATOM   551  C  C     . TYR A 1 72  ? 14.820  23.863  13.128  1.00 63.90  ? 72  TYR A C     1 
ATOM   552  O  O     . TYR A 1 72  ? 14.224  24.768  12.538  1.00 76.61  ? 72  TYR A O     1 
ATOM   553  C  CB    . TYR A 1 72  ? 13.686  22.151  14.569  1.00 64.29  ? 72  TYR A CB    1 
ATOM   554  C  CG    . TYR A 1 72  ? 13.035  21.850  15.900  1.00 67.10  ? 72  TYR A CG    1 
ATOM   555  C  CD1   . TYR A 1 72  ? 13.799  21.518  17.011  1.00 63.48  ? 72  TYR A CD1   1 
ATOM   556  C  CD2   . TYR A 1 72  ? 11.655  21.899  16.046  1.00 65.15  ? 72  TYR A CD2   1 
ATOM   557  C  CE1   . TYR A 1 72  ? 13.207  21.244  18.230  1.00 66.21  ? 72  TYR A CE1   1 
ATOM   558  C  CE2   . TYR A 1 72  ? 11.054  21.626  17.260  1.00 69.25  ? 72  TYR A CE2   1 
ATOM   559  C  CZ    . TYR A 1 72  ? 11.834  21.299  18.348  1.00 63.97  ? 72  TYR A CZ    1 
ATOM   560  O  OH    . TYR A 1 72  ? 11.239  21.027  19.559  1.00 68.55  ? 72  TYR A OH    1 
ATOM   561  N  N     . ASP A 1 73  ? 15.808  23.162  12.576  1.00 64.93  ? 73  ASP A N     1 
ATOM   562  C  CA    . ASP A 1 73  ? 16.338  23.473  11.250  1.00 65.97  ? 73  ASP A CA    1 
ATOM   563  C  C     . ASP A 1 73  ? 15.455  22.822  10.194  1.00 63.16  ? 73  ASP A C     1 
ATOM   564  O  O     . ASP A 1 73  ? 15.508  21.609  9.980   1.00 63.84  ? 73  ASP A O     1 
ATOM   565  C  CB    . ASP A 1 73  ? 17.783  23.001  11.128  1.00 72.08  ? 73  ASP A CB    1 
ATOM   566  C  CG    . ASP A 1 73  ? 18.357  23.232  9.743   1.00 79.07  ? 73  ASP A CG    1 
ATOM   567  O  OD1   . ASP A 1 73  ? 18.594  24.404  9.382   1.00 88.13  ? 73  ASP A OD1   1 
ATOM   568  O  OD2   . ASP A 1 73  ? 18.575  22.241  9.015   1.00 75.51  ? 73  ASP A OD2   1 
ATOM   569  N  N     . ASN A 1 74  ? 14.638  23.635  9.525   1.00 68.40  ? 74  ASN A N     1 
ATOM   570  C  CA    . ASN A 1 74  ? 13.802  23.191  8.411   1.00 64.12  ? 74  ASN A CA    1 
ATOM   571  C  C     . ASN A 1 74  ? 12.829  22.096  8.860   1.00 58.48  ? 74  ASN A C     1 
ATOM   572  O  O     . ASN A 1 74  ? 12.889  20.942  8.431   1.00 52.40  ? 74  ASN A O     1 
ATOM   573  C  CB    . ASN A 1 74  ? 14.670  22.717  7.240   1.00 57.61  ? 74  ASN A CB    1 
ATOM   574  C  CG    . ASN A 1 74  ? 13.870  22.506  5.971   1.00 70.51  ? 74  ASN A CG    1 
ATOM   575  O  OD1   . ASN A 1 74  ? 12.853  23.161  5.749   1.00 73.21  ? 74  ASN A OD1   1 
ATOM   576  N  ND2   . ASN A 1 74  ? 14.327  21.584  5.130   1.00 70.33  ? 74  ASN A ND2   1 
ATOM   577  N  N     . CYS A 1 75  ? 11.923  22.500  9.746   1.00 59.97  ? 75  CYS A N     1 
ATOM   578  C  CA    . CYS A 1 75  ? 10.850  21.642  10.226  1.00 49.48  ? 75  CYS A CA    1 
ATOM   579  C  C     . CYS A 1 75  ? 9.534   22.399  10.134  1.00 54.65  ? 75  CYS A C     1 
ATOM   580  O  O     . CYS A 1 75  ? 9.483   23.604  10.395  1.00 61.35  ? 75  CYS A O     1 
ATOM   581  C  CB    . CYS A 1 75  ? 11.098  21.178  11.667  1.00 59.54  ? 75  CYS A CB    1 
ATOM   582  S  SG    . CYS A 1 75  ? 12.509  20.063  11.856  1.00 54.73  ? 75  CYS A SG    1 
ATOM   583  N  N     . TRP A 1 76  ? 8.473   21.689  9.760   1.00 59.51  ? 76  TRP A N     1 
ATOM   584  C  CA    . TRP A 1 76  ? 7.190   22.316  9.485   1.00 60.85  ? 76  TRP A CA    1 
ATOM   585  C  C     . TRP A 1 76  ? 6.072   21.508  10.126  1.00 43.44  ? 76  TRP A C     1 
ATOM   586  O  O     . TRP A 1 76  ? 6.142   20.280  10.214  1.00 57.03  ? 76  TRP A O     1 
ATOM   587  C  CB    . TRP A 1 76  ? 6.949   22.444  7.975   1.00 62.21  ? 76  TRP A CB    1 
ATOM   588  C  CG    . TRP A 1 76  ? 8.107   23.052  7.243   1.00 58.28  ? 76  TRP A CG    1 
ATOM   589  C  CD1   . TRP A 1 76  ? 9.247   22.419  6.842   1.00 50.41  ? 76  TRP A CD1   1 
ATOM   590  C  CD2   . TRP A 1 76  ? 8.239   24.417  6.826   1.00 64.83  ? 76  TRP A CD2   1 
ATOM   591  N  NE1   . TRP A 1 76  ? 10.081  23.303  6.202   1.00 58.82  ? 76  TRP A NE1   1 
ATOM   592  C  CE2   . TRP A 1 76  ? 9.484   24.536  6.178   1.00 58.65  ? 76  TRP A CE2   1 
ATOM   593  C  CE3   . TRP A 1 76  ? 7.424   25.548  6.936   1.00 71.59  ? 76  TRP A CE3   1 
ATOM   594  C  CZ2   . TRP A 1 76  ? 9.935   25.741  5.644   1.00 61.69  ? 76  TRP A CZ2   1 
ATOM   595  C  CZ3   . TRP A 1 76  ? 7.874   26.744  6.404   1.00 66.25  ? 76  TRP A CZ3   1 
ATOM   596  C  CH2   . TRP A 1 76  ? 9.117   26.831  5.766   1.00 59.86  ? 76  TRP A CH2   1 
ATOM   597  N  N     . LEU A 1 77  ? 5.038   22.215  10.573  1.00 56.53  ? 77  LEU A N     1 
ATOM   598  C  CA    . LEU A 1 77  ? 3.854   21.608  11.160  1.00 56.16  ? 77  LEU A CA    1 
ATOM   599  C  C     . LEU A 1 77  ? 2.669   21.776  10.219  1.00 62.21  ? 77  LEU A C     1 
ATOM   600  O  O     . LEU A 1 77  ? 2.538   22.804  9.547   1.00 64.01  ? 77  LEU A O     1 
ATOM   601  C  CB    . LEU A 1 77  ? 3.531   22.231  12.521  1.00 50.67  ? 77  LEU A CB    1 
ATOM   602  C  CG    . LEU A 1 77  ? 2.229   21.774  13.183  1.00 51.19  ? 77  LEU A CG    1 
ATOM   603  C  CD1   . LEU A 1 77  ? 2.254   20.276  13.445  1.00 70.24  ? 77  LEU A CD1   1 
ATOM   604  C  CD2   . LEU A 1 77  ? 1.979   22.544  14.470  1.00 58.48  ? 77  LEU A CD2   1 
ATOM   605  N  N     . ALA A 1 78  ? 1.808   20.762  10.174  1.00 59.70  ? 78  ALA A N     1 
ATOM   606  C  CA    . ALA A 1 78  ? 0.623   20.774  9.328   1.00 55.92  ? 78  ALA A CA    1 
ATOM   607  C  C     . ALA A 1 78  ? -0.568  20.278  10.131  1.00 65.94  ? 78  ALA A C     1 
ATOM   608  O  O     . ALA A 1 78  ? -0.502  19.211  10.750  1.00 72.03  ? 78  ALA A O     1 
ATOM   609  C  CB    . ALA A 1 78  ? 0.821   19.908  8.080   1.00 46.31  ? 78  ALA A CB    1 
ATOM   610  N  N     . LEU A 1 79  ? -1.649  21.052  10.122  1.00 73.92  ? 79  LEU A N     1 
ATOM   611  C  CA    . LEU A 1 79  ? -2.884  20.701  10.812  1.00 73.66  ? 79  LEU A CA    1 
ATOM   612  C  C     . LEU A 1 79  ? -3.940  20.352  9.773   1.00 82.59  ? 79  LEU A C     1 
ATOM   613  O  O     . LEU A 1 79  ? -4.231  21.159  8.883   1.00 81.81  ? 79  LEU A O     1 
ATOM   614  C  CB    . LEU A 1 79  ? -3.357  21.847  11.706  1.00 78.99  ? 79  LEU A CB    1 
ATOM   615  C  CG    . LEU A 1 79  ? -2.375  22.274  12.799  1.00 78.89  ? 79  LEU A CG    1 
ATOM   616  C  CD1   . LEU A 1 79  ? -2.980  23.354  13.682  1.00 89.45  ? 79  LEU A CD1   1 
ATOM   617  C  CD2   . LEU A 1 79  ? -1.942  21.075  13.630  1.00 77.95  ? 79  LEU A CD2   1 
ATOM   618  N  N     . THR A 1 80  ? -4.508  19.156  9.888   1.00 91.82  ? 80  THR A N     1 
ATOM   619  C  CA    . THR A 1 80  ? -5.451  18.640  8.911   1.00 93.08  ? 80  THR A CA    1 
ATOM   620  C  C     . THR A 1 80  ? -6.882  18.782  9.423   1.00 94.69  ? 80  THR A C     1 
ATOM   621  O  O     . THR A 1 80  ? -7.136  19.258  10.531  1.00 95.98  ? 80  THR A O     1 
ATOM   622  C  CB    . THR A 1 80  ? -5.136  17.178  8.586   1.00 92.73  ? 80  THR A CB    1 
ATOM   623  O  OG1   . THR A 1 80  ? -5.399  16.364  9.736   1.00 93.65  ? 80  THR A OG1   1 
ATOM   624  C  CG2   . THR A 1 80  ? -3.676  17.024  8.190   1.00 91.77  ? 80  THR A CG2   1 
ATOM   625  N  N     . ASP A 1 81  ? -7.829  18.360  8.592   1.00 85.68  ? 81  ASP A N     1 
ATOM   626  C  CA    . ASP A 1 81  ? -9.225  18.349  8.999   1.00 81.16  ? 81  ASP A CA    1 
ATOM   627  C  C     . ASP A 1 81  ? -9.449  17.250  10.036  1.00 79.71  ? 81  ASP A C     1 
ATOM   628  O  O     . ASP A 1 81  ? -8.917  16.144  9.894   1.00 84.10  ? 81  ASP A O     1 
ATOM   629  C  CB    . ASP A 1 81  ? -10.131 18.132  7.785   1.00 76.46  ? 81  ASP A CB    1 
ATOM   630  C  CG    . ASP A 1 81  ? -11.605 18.271  8.118   1.00 81.50  ? 81  ASP A CG    1 
ATOM   631  O  OD1   . ASP A 1 81  ? -12.094 17.547  9.011   1.00 84.46  ? 81  ASP A OD1   1 
ATOM   632  O  OD2   . ASP A 1 81  ? -12.279 19.109  7.482   1.00 74.79  ? 81  ASP A OD2   1 
ATOM   633  N  N     . PRO A 1 82  ? -10.225 17.520  11.088  1.00 75.10  ? 82  PRO A N     1 
ATOM   634  C  CA    . PRO A 1 82  ? -10.402 16.509  12.144  1.00 76.48  ? 82  PRO A CA    1 
ATOM   635  C  C     . PRO A 1 82  ? -11.011 15.208  11.653  1.00 86.21  ? 82  PRO A C     1 
ATOM   636  O  O     . PRO A 1 82  ? -10.867 14.182  12.330  1.00 86.11  ? 82  PRO A O     1 
ATOM   637  C  CB    . PRO A 1 82  ? -11.321 17.213  13.154  1.00 74.98  ? 82  PRO A CB    1 
ATOM   638  C  CG    . PRO A 1 82  ? -12.002 18.290  12.368  1.00 78.87  ? 82  PRO A CG    1 
ATOM   639  C  CD    . PRO A 1 82  ? -10.993 18.746  11.359  1.00 80.25  ? 82  PRO A CD    1 
ATOM   640  N  N     . ARG A 1 83  ? -11.683 15.210  10.503  1.00 94.44  ? 83  ARG A N     1 
ATOM   641  C  CA    . ARG A 1 83  ? -12.291 14.002  9.961   1.00 89.31  ? 83  ARG A CA    1 
ATOM   642  C  C     . ARG A 1 83  ? -11.341 13.192  9.089   1.00 90.43  ? 83  ARG A C     1 
ATOM   643  O  O     . ARG A 1 83  ? -11.653 12.040  8.767   1.00 94.43  ? 83  ARG A O     1 
ATOM   644  C  CB    . ARG A 1 83  ? -13.543 14.363  9.154   1.00 84.83  ? 83  ARG A CB    1 
ATOM   645  C  CG    . ARG A 1 83  ? -14.660 14.970  9.988   1.00 92.64  ? 83  ARG A CG    1 
ATOM   646  C  CD    . ARG A 1 83  ? -15.709 15.629  9.109   1.00 96.96  ? 83  ARG A CD    1 
ATOM   647  N  NE    . ARG A 1 83  ? -15.150 16.737  8.343   1.00 88.96  ? 83  ARG A NE    1 
ATOM   648  C  CZ    . ARG A 1 83  ? -15.854 17.529  7.547   1.00 99.65  ? 83  ARG A CZ    1 
ATOM   649  N  NH1   . ARG A 1 83  ? -17.157 17.366  7.385   1.00 107.93 ? 83  ARG A NH1   1 
ATOM   650  N  NH2   . ARG A 1 83  ? -15.235 18.510  6.896   1.00 103.34 ? 83  ARG A NH2   1 
ATOM   651  N  N     . ASP A 1 84  ? -10.200 13.758  8.703   1.00 84.21  ? 84  ASP A N     1 
ATOM   652  C  CA    . ASP A 1 84  ? -9.199  13.082  7.878   1.00 82.74  ? 84  ASP A CA    1 
ATOM   653  C  C     . ASP A 1 84  ? -7.911  13.008  8.693   1.00 86.00  ? 84  ASP A C     1 
ATOM   654  O  O     . ASP A 1 84  ? -7.010  13.835  8.536   1.00 80.68  ? 84  ASP A O     1 
ATOM   655  C  CB    . ASP A 1 84  ? -8.997  13.826  6.549   1.00 68.15  ? 84  ASP A CB    1 
ATOM   656  C  CG    . ASP A 1 84  ? -8.059  13.097  5.609   1.00 75.34  ? 84  ASP A CG    1 
ATOM   657  O  OD1   . ASP A 1 84  ? -7.661  11.957  5.928   1.00 85.17  ? 84  ASP A OD1   1 
ATOM   658  O  OD2   . ASP A 1 84  ? -7.718  13.667  4.551   1.00 76.82  ? 84  ASP A OD2   1 
ATOM   659  N  N     . VAL A 1 85  ? -7.827  12.005  9.566   1.00 73.73  ? 85  VAL A N     1 
ATOM   660  C  CA    . VAL A 1 85  ? -6.715  11.903  10.505  1.00 81.58  ? 85  VAL A CA    1 
ATOM   661  C  C     . VAL A 1 85  ? -6.197  10.473  10.579  1.00 83.84  ? 85  VAL A C     1 
ATOM   662  O  O     . VAL A 1 85  ? -5.104  10.226  11.102  1.00 88.43  ? 85  VAL A O     1 
ATOM   663  C  CB    . VAL A 1 85  ? -7.131  12.403  11.901  1.00 80.03  ? 85  VAL A CB    1 
ATOM   664  C  CG1   . VAL A 1 85  ? -7.437  13.892  11.862  1.00 78.96  ? 85  VAL A CG1   1 
ATOM   665  C  CG2   . VAL A 1 85  ? -8.336  11.622  12.403  1.00 74.70  ? 85  VAL A CG2   1 
ATOM   666  N  N     . ALA A 1 86  ? -6.970  9.521   10.062  1.00 83.19  ? 86  ALA A N     1 
ATOM   667  C  CA    . ALA A 1 86  ? -6.618  8.110   10.140  1.00 86.08  ? 86  ALA A CA    1 
ATOM   668  C  C     . ALA A 1 86  ? -6.761  7.467   8.766   1.00 86.11  ? 86  ALA A C     1 
ATOM   669  O  O     . ALA A 1 86  ? -7.114  8.119   7.779   1.00 87.62  ? 86  ALA A O     1 
ATOM   670  C  CB    . ALA A 1 86  ? -7.482  7.381   11.178  1.00 93.10  ? 86  ALA A CB    1 
ATOM   671  N  N     . ARG A 1 87  ? -6.477  6.167   8.711   1.00 86.68  ? 87  ARG A N     1 
ATOM   672  C  CA    . ARG A 1 87  ? -6.558  5.382   7.485   1.00 80.32  ? 87  ARG A CA    1 
ATOM   673  C  C     . ARG A 1 87  ? -7.876  4.616   7.491   1.00 86.50  ? 87  ARG A C     1 
ATOM   674  O  O     . ARG A 1 87  ? -8.053  3.678   8.276   1.00 96.46  ? 87  ARG A O     1 
ATOM   675  C  CB    . ARG A 1 87  ? -5.362  4.439   7.373   1.00 81.46  ? 87  ARG A CB    1 
ATOM   676  C  CG    . ARG A 1 87  ? -5.436  3.452   6.221   1.00 84.09  ? 87  ARG A CG    1 
ATOM   677  C  CD    . ARG A 1 87  ? -4.162  2.627   6.132   1.00 70.82  ? 87  ARG A CD    1 
ATOM   678  N  NE    . ARG A 1 87  ? -3.717  2.175   7.445   1.00 69.16  ? 87  ARG A NE    1 
ATOM   679  C  CZ    . ARG A 1 87  ? -4.188  1.104   8.069   1.00 72.05  ? 87  ARG A CZ    1 
ATOM   680  N  NH1   . ARG A 1 87  ? -5.130  0.348   7.528   1.00 69.17  ? 87  ARG A NH1   1 
ATOM   681  N  NH2   . ARG A 1 87  ? -3.705  0.786   9.266   1.00 69.09  ? 87  ARG A NH2   1 
ATOM   682  N  N     . ILE A 1 88  ? -8.796  5.016   6.617   1.00 91.67  ? 88  ILE A N     1 
ATOM   683  C  CA    . ILE A 1 88  ? -10.139 4.446   6.582   1.00 89.11  ? 88  ILE A CA    1 
ATOM   684  C  C     . ILE A 1 88  ? -10.062 3.054   5.964   1.00 90.62  ? 88  ILE A C     1 
ATOM   685  O  O     . ILE A 1 88  ? -9.890  2.910   4.752   1.00 86.87  ? 88  ILE A O     1 
ATOM   686  C  CB    . ILE A 1 88  ? -11.107 5.344   5.804   1.00 85.03  ? 88  ILE A CB    1 
ATOM   687  C  CG1   . ILE A 1 88  ? -11.082 6.766   6.369   1.00 85.00  ? 88  ILE A CG1   1 
ATOM   688  C  CG2   . ILE A 1 88  ? -12.517 4.775   5.851   1.00 87.61  ? 88  ILE A CG2   1 
ATOM   689  C  CD1   . ILE A 1 88  ? -11.957 7.739   5.613   1.00 74.43  ? 88  ILE A CD1   1 
ATOM   690  N  N     . GLU A 1 89  ? -10.199 2.023   6.800   1.00 91.56  ? 89  GLU A N     1 
ATOM   691  C  CA    . GLU A 1 89  ? -10.186 0.652   6.304   1.00 89.07  ? 89  GLU A CA    1 
ATOM   692  C  C     . GLU A 1 89  ? -11.525 0.247   5.702   1.00 92.89  ? 89  GLU A C     1 
ATOM   693  O  O     . GLU A 1 89  ? -11.565 -0.605  4.808   1.00 88.64  ? 89  GLU A O     1 
ATOM   694  C  CB    . GLU A 1 89  ? -9.810  -0.312  7.432   1.00 98.90  ? 89  GLU A CB    1 
ATOM   695  C  CG    . GLU A 1 89  ? -9.895  -1.780  7.048   1.00 93.93  ? 89  GLU A CG    1 
ATOM   696  C  CD    . GLU A 1 89  ? -9.560  -2.704  8.203   1.00 90.92  ? 89  GLU A CD    1 
ATOM   697  O  OE1   . GLU A 1 89  ? -9.095  -2.207  9.250   1.00 90.86  ? 89  GLU A OE1   1 
ATOM   698  O  OE2   . GLU A 1 89  ? -9.765  -3.928  8.064   1.00 88.75  ? 89  GLU A OE2   1 
ATOM   699  N  N     . SER A 1 90  ? -12.624 0.843   6.171   1.00 97.67  ? 90  SER A N     1 
ATOM   700  C  CA    . SER A 1 90  ? -13.939 0.471   5.661   1.00 93.44  ? 90  SER A CA    1 
ATOM   701  C  C     . SER A 1 90  ? -14.140 0.930   4.223   1.00 91.96  ? 90  SER A C     1 
ATOM   702  O  O     . SER A 1 90  ? -14.882 0.290   3.468   1.00 88.47  ? 90  SER A O     1 
ATOM   703  C  CB    . SER A 1 90  ? -15.033 1.049   6.559   1.00 91.29  ? 90  SER A CB    1 
ATOM   704  O  OG    . SER A 1 90  ? -14.939 2.461   6.634   1.00 93.70  ? 90  SER A OG    1 
ATOM   705  N  N     . LYS A 1 91  ? -13.495 2.027   3.824   1.00 89.50  ? 91  LYS A N     1 
ATOM   706  C  CA    . LYS A 1 91  ? -13.638 2.584   2.484   1.00 80.07  ? 91  LYS A CA    1 
ATOM   707  C  C     . LYS A 1 91  ? -12.483 2.192   1.567   1.00 77.49  ? 91  LYS A C     1 
ATOM   708  O  O     . LYS A 1 91  ? -12.072 2.982   0.710   1.00 73.49  ? 91  LYS A O     1 
ATOM   709  C  CB    . LYS A 1 91  ? -13.770 4.105   2.558   1.00 76.99  ? 91  LYS A CB    1 
ATOM   710  C  CG    . LYS A 1 91  ? -15.040 4.576   3.249   1.00 82.08  ? 91  LYS A CG    1 
ATOM   711  C  CD    . LYS A 1 91  ? -15.086 6.090   3.362   1.00 85.98  ? 91  LYS A CD    1 
ATOM   712  C  CE    . LYS A 1 91  ? -16.424 6.560   3.910   1.00 100.94 ? 91  LYS A CE    1 
ATOM   713  N  NZ    . LYS A 1 91  ? -16.748 5.923   5.217   1.00 105.32 ? 91  LYS A NZ    1 
ATOM   714  N  N     . THR A 1 92  ? -11.953 0.983   1.728   1.00 76.45  ? 92  THR A N     1 
ATOM   715  C  CA    . THR A 1 92  ? -10.879 0.466   0.891   1.00 78.11  ? 92  THR A CA    1 
ATOM   716  C  C     . THR A 1 92  ? -11.353 -0.815  0.221   1.00 72.44  ? 92  THR A C     1 
ATOM   717  O  O     . THR A 1 92  ? -11.835 -1.731  0.897   1.00 77.99  ? 92  THR A O     1 
ATOM   718  C  CB    . THR A 1 92  ? -9.613  0.201   1.711   1.00 78.58  ? 92  THR A CB    1 
ATOM   719  O  OG1   . THR A 1 92  ? -9.221  1.401   2.390   1.00 76.25  ? 92  THR A OG1   1 
ATOM   720  C  CG2   . THR A 1 92  ? -8.479  -0.255  0.804   1.00 67.98  ? 92  THR A CG2   1 
ATOM   721  N  N     . VAL A 1 93  ? -11.217 -0.878  -1.104  1.00 70.71  ? 93  VAL A N     1 
ATOM   722  C  CA    . VAL A 1 93  ? -11.719 -1.999  -1.885  1.00 73.70  ? 93  VAL A CA    1 
ATOM   723  C  C     . VAL A 1 93  ? -10.644 -2.468  -2.856  1.00 68.26  ? 93  VAL A C     1 
ATOM   724  O  O     . VAL A 1 93  ? -9.748  -1.715  -3.246  1.00 73.55  ? 93  VAL A O     1 
ATOM   725  C  CB    . VAL A 1 93  ? -13.009 -1.637  -2.653  1.00 70.67  ? 93  VAL A CB    1 
ATOM   726  C  CG1   . VAL A 1 93  ? -14.108 -1.237  -1.682  1.00 72.98  ? 93  VAL A CG1   1 
ATOM   727  C  CG2   . VAL A 1 93  ? -12.737 -0.521  -3.649  1.00 64.33  ? 93  VAL A CG2   1 
ATOM   728  N  N     . ILE A 1 94  ? -10.748 -3.737  -3.243  1.00 65.37  ? 94  ILE A N     1 
ATOM   729  C  CA    . ILE A 1 94  ? -9.865  -4.353  -4.225  1.00 68.16  ? 94  ILE A CA    1 
ATOM   730  C  C     . ILE A 1 94  ? -10.717 -4.804  -5.402  1.00 76.65  ? 94  ILE A C     1 
ATOM   731  O  O     . ILE A 1 94  ? -11.738 -5.476  -5.213  1.00 79.07  ? 94  ILE A O     1 
ATOM   732  C  CB    . ILE A 1 94  ? -9.083  -5.537  -3.627  1.00 64.67  ? 94  ILE A CB    1 
ATOM   733  C  CG1   . ILE A 1 94  ? -8.197  -5.063  -2.474  1.00 74.95  ? 94  ILE A CG1   1 
ATOM   734  C  CG2   . ILE A 1 94  ? -8.252  -6.224  -4.700  1.00 66.94  ? 94  ILE A CG2   1 
ATOM   735  C  CD1   . ILE A 1 94  ? -7.393  -6.169  -1.827  1.00 73.18  ? 94  ILE A CD1   1 
ATOM   736  N  N     . ILE A 1 95  ? -10.299 -4.438  -6.609  1.00 75.48  ? 95  ILE A N     1 
ATOM   737  C  CA    . ILE A 1 95  ? -11.080 -4.671  -7.818  1.00 73.09  ? 95  ILE A CA    1 
ATOM   738  C  C     . ILE A 1 95  ? -10.457 -5.853  -8.554  1.00 80.43  ? 95  ILE A C     1 
ATOM   739  O  O     . ILE A 1 95  ? -9.418  -5.720  -9.207  1.00 75.91  ? 95  ILE A O     1 
ATOM   740  C  CB    . ILE A 1 95  ? -11.141 -3.423  -8.702  1.00 75.61  ? 95  ILE A CB    1 
ATOM   741  C  CG1   . ILE A 1 95  ? -11.557 -2.206  -7.874  1.00 75.21  ? 95  ILE A CG1   1 
ATOM   742  C  CG2   . ILE A 1 95  ? -12.109 -3.636  -9.855  1.00 87.01  ? 95  ILE A CG2   1 
ATOM   743  C  CD1   . ILE A 1 95  ? -12.893 -2.363  -7.184  1.00 82.43  ? 95  ILE A CD1   1 
ATOM   744  N  N     . THR A 1 96  ? -11.097 -7.015  -8.450  1.00 87.50  ? 96  THR A N     1 
ATOM   745  C  CA    . THR A 1 96  ? -10.725 -8.195  -9.214  1.00 97.71  ? 96  THR A CA    1 
ATOM   746  C  C     . THR A 1 96  ? -11.976 -8.782  -9.854  1.00 106.98 ? 96  THR A C     1 
ATOM   747  O  O     . THR A 1 96  ? -13.103 -8.469  -9.462  1.00 104.70 ? 96  THR A O     1 
ATOM   748  C  CB    . THR A 1 96  ? -10.035 -9.254  -8.342  1.00 93.31  ? 96  THR A CB    1 
ATOM   749  O  OG1   . THR A 1 96  ? -10.947 -9.717  -7.337  1.00 101.90 ? 96  THR A OG1   1 
ATOM   750  C  CG2   . THR A 1 96  ? -8.799  -8.671  -7.671  1.00 89.79  ? 96  THR A CG2   1 
ATOM   751  N  N     . GLN A 1 97  ? -11.766 -9.641  -10.853 1.00 107.07 ? 97  GLN A N     1 
ATOM   752  C  CA    . GLN A 1 97  ? -12.898 -10.228 -11.563 1.00 119.01 ? 97  GLN A CA    1 
ATOM   753  C  C     . GLN A 1 97  ? -13.662 -11.200 -10.672 1.00 123.42 ? 97  GLN A C     1 
ATOM   754  O  O     . GLN A 1 97  ? -14.896 -11.157 -10.604 1.00 115.75 ? 97  GLN A O     1 
ATOM   755  C  CB    . GLN A 1 97  ? -12.419 -10.925 -12.836 1.00 120.14 ? 97  GLN A CB    1 
ATOM   756  C  CG    . GLN A 1 97  ? -13.540 -11.551 -13.650 1.00 125.73 ? 97  GLN A CG    1 
ATOM   757  C  CD    . GLN A 1 97  ? -13.060 -12.116 -14.972 1.00 124.13 ? 97  GLN A CD    1 
ATOM   758  O  OE1   . GLN A 1 97  ? -11.919 -11.896 -15.378 1.00 128.31 ? 97  GLN A OE1   1 
ATOM   759  N  NE2   . GLN A 1 97  ? -13.933 -12.850 -15.653 1.00 117.94 ? 97  GLN A NE2   1 
ATOM   760  N  N     . GLU A 1 98  ? -12.947 -12.083 -9.982  1.00 134.70 ? 98  GLU A N     1 
ATOM   761  C  CA    . GLU A 1 98  ? -13.549 -13.077 -9.104  1.00 135.46 ? 98  GLU A CA    1 
ATOM   762  C  C     . GLU A 1 98  ? -13.327 -12.680 -7.652  1.00 131.87 ? 98  GLU A C     1 
ATOM   763  O  O     . GLU A 1 98  ? -12.217 -12.292 -7.271  1.00 126.27 ? 98  GLU A O     1 
ATOM   764  C  CB    . GLU A 1 98  ? -12.965 -14.467 -9.368  1.00 136.30 ? 98  GLU A CB    1 
ATOM   765  C  CG    . GLU A 1 98  ? -13.309 -15.035 -10.737 1.00 146.88 ? 98  GLU A CG    1 
ATOM   766  C  CD    . GLU A 1 98  ? -14.787 -15.340 -10.887 1.00 157.98 ? 98  GLU A CD    1 
ATOM   767  O  OE1   . GLU A 1 98  ? -15.477 -15.457 -9.852  1.00 161.24 ? 98  GLU A OE1   1 
ATOM   768  O  OE2   . GLU A 1 98  ? -15.259 -15.459 -12.037 1.00 162.34 ? 98  GLU A OE2   1 
ATOM   769  N  N     . GLN A 1 99  ? -14.386 -12.777 -6.844  1.00 138.18 ? 99  GLN A N     1 
ATOM   770  C  CA    . GLN A 1 99  ? -14.261 -12.449 -5.428  1.00 135.36 ? 99  GLN A CA    1 
ATOM   771  C  C     . GLN A 1 99  ? -13.324 -13.412 -4.712  1.00 127.42 ? 99  GLN A C     1 
ATOM   772  O  O     . GLN A 1 99  ? -12.684 -13.035 -3.724  1.00 125.23 ? 99  GLN A O     1 
ATOM   773  C  CB    . GLN A 1 99  ? -15.637 -12.456 -4.762  1.00 135.99 ? 99  GLN A CB    1 
ATOM   774  C  CG    . GLN A 1 99  ? -15.609 -12.131 -3.276  1.00 136.93 ? 99  GLN A CG    1 
ATOM   775  C  CD    . GLN A 1 99  ? -16.980 -12.219 -2.633  1.00 147.28 ? 99  GLN A CD    1 
ATOM   776  O  OE1   . GLN A 1 99  ? -17.949 -12.638 -3.266  1.00 156.75 ? 99  GLN A OE1   1 
ATOM   777  N  NE2   . GLN A 1 99  ? -17.068 -11.822 -1.368  1.00 148.66 ? 99  GLN A NE2   1 
ATOM   778  N  N     . ARG A 1 100 ? -13.228 -14.653 -5.193  1.00 119.51 ? 100 ARG A N     1 
ATOM   779  C  CA    . ARG A 1 100 ? -12.360 -15.633 -4.551  1.00 112.50 ? 100 ARG A CA    1 
ATOM   780  C  C     . ARG A 1 100 ? -10.891 -15.247 -4.646  1.00 102.54 ? 100 ARG A C     1 
ATOM   781  O  O     . ARG A 1 100 ? -10.089 -15.694 -3.819  1.00 96.72  ? 100 ARG A O     1 
ATOM   782  C  CB    . ARG A 1 100 ? -12.587 -17.014 -5.169  1.00 114.87 ? 100 ARG A CB    1 
ATOM   783  C  CG    . ARG A 1 100 ? -12.014 -18.164 -4.356  1.00 115.81 ? 100 ARG A CG    1 
ATOM   784  C  CD    . ARG A 1 100 ? -12.467 -19.505 -4.911  1.00 121.50 ? 100 ARG A CD    1 
ATOM   785  N  NE    . ARG A 1 100 ? -12.091 -20.614 -4.042  1.00 119.83 ? 100 ARG A NE    1 
ATOM   786  C  CZ    . ARG A 1 100 ? -12.441 -21.876 -4.247  1.00 130.91 ? 100 ARG A CZ    1 
ATOM   787  N  NH1   . ARG A 1 100 ? -13.177 -22.229 -5.288  1.00 135.22 ? 100 ARG A NH1   1 
ATOM   788  N  NH2   . ARG A 1 100 ? -12.044 -22.808 -3.385  1.00 130.52 ? 100 ARG A NH2   1 
ATOM   789  N  N     . ASP A 1 101 ? -10.520 -14.428 -5.633  1.00 104.13 ? 101 ASP A N     1 
ATOM   790  C  CA    . ASP A 1 101 ? -9.137  -13.973 -5.733  1.00 101.15 ? 101 ASP A CA    1 
ATOM   791  C  C     . ASP A 1 101 ? -8.797  -12.994 -4.617  1.00 90.78  ? 101 ASP A C     1 
ATOM   792  O  O     . ASP A 1 101 ? -7.685  -13.021 -4.077  1.00 82.72  ? 101 ASP A O     1 
ATOM   793  C  CB    . ASP A 1 101 ? -8.890  -13.332 -7.099  1.00 98.01  ? 101 ASP A CB    1 
ATOM   794  C  CG    . ASP A 1 101 ? -9.024  -14.319 -8.241  1.00 109.85 ? 101 ASP A CG    1 
ATOM   795  O  OD1   . ASP A 1 101 ? -8.734  -15.515 -8.032  1.00 111.43 ? 101 ASP A OD1   1 
ATOM   796  O  OD2   . ASP A 1 101 ? -9.417  -13.897 -9.349  1.00 117.40 ? 101 ASP A OD2   1 
ATOM   797  N  N     . THR A 1 102 ? -9.741  -12.124 -4.256  1.00 92.02  ? 102 THR A N     1 
ATOM   798  C  CA    . THR A 1 102 ? -9.484  -11.118 -3.230  1.00 87.75  ? 102 THR A CA    1 
ATOM   799  C  C     . THR A 1 102 ? -9.617  -11.705 -1.828  1.00 88.65  ? 102 THR A C     1 
ATOM   800  O  O     . THR A 1 102 ? -8.674  -11.658 -1.031  1.00 82.82  ? 102 THR A O     1 
ATOM   801  C  CB    . THR A 1 102 ? -10.435 -9.931  -3.407  1.00 86.87  ? 102 THR A CB    1 
ATOM   802  O  OG1   . THR A 1 102 ? -10.169 -9.283  -4.658  1.00 89.34  ? 102 THR A OG1   1 
ATOM   803  C  CG2   . THR A 1 102 ? -10.255 -8.930  -2.275  1.00 77.36  ? 102 THR A CG2   1 
ATOM   804  N  N     . VAL A 1 103 ? -10.783 -12.260 -1.511  1.00 87.32  ? 103 VAL A N     1 
ATOM   805  C  CA    . VAL A 1 103 ? -11.048 -12.778 -0.172  1.00 83.44  ? 103 VAL A CA    1 
ATOM   806  C  C     . VAL A 1 103 ? -11.578 -14.204 -0.265  1.00 93.38  ? 103 VAL A C     1 
ATOM   807  O  O     . VAL A 1 103 ? -12.287 -14.541 -1.224  1.00 95.96  ? 103 VAL A O     1 
ATOM   808  C  CB    . VAL A 1 103 ? -12.039 -11.879 0.585   1.00 80.77  ? 103 VAL A CB    1 
ATOM   809  C  CG1   . VAL A 1 103 ? -11.442 -10.498 0.804   1.00 87.51  ? 103 VAL A CG1   1 
ATOM   810  C  CG2   . VAL A 1 103 ? -13.354 -11.783 -0.176  1.00 89.74  ? 103 VAL A CG2   1 
ATOM   811  N  N     . PRO A 1 104 ? -11.257 -15.071 0.695   1.00 89.76  ? 104 PRO A N     1 
ATOM   812  C  CA    . PRO A 1 104 ? -11.855 -16.413 0.706   1.00 87.63  ? 104 PRO A CA    1 
ATOM   813  C  C     . PRO A 1 104 ? -13.348 -16.330 0.990   1.00 90.48  ? 104 PRO A C     1 
ATOM   814  O  O     . PRO A 1 104 ? -13.781 -15.641 1.916   1.00 85.01  ? 104 PRO A O     1 
ATOM   815  C  CB    . PRO A 1 104 ? -11.104 -17.132 1.835   1.00 81.06  ? 104 PRO A CB    1 
ATOM   816  C  CG    . PRO A 1 104 ? -9.859  -16.320 2.057   1.00 80.99  ? 104 PRO A CG    1 
ATOM   817  C  CD    . PRO A 1 104 ? -10.244 -14.907 1.750   1.00 82.68  ? 104 PRO A CD    1 
ATOM   818  N  N     . ILE A 1 105 ? -14.134 -17.037 0.183   1.00 87.88  ? 105 ILE A N     1 
ATOM   819  C  CA    . ILE A 1 105 ? -15.587 -17.044 0.334   1.00 84.50  ? 105 ILE A CA    1 
ATOM   820  C  C     . ILE A 1 105 ? -15.932 -17.582 1.718   1.00 83.56  ? 105 ILE A C     1 
ATOM   821  O  O     . ILE A 1 105 ? -15.669 -18.757 2.010   1.00 84.03  ? 105 ILE A O     1 
ATOM   822  C  CB    . ILE A 1 105 ? -16.261 -17.866 -0.774  1.00 90.17  ? 105 ILE A CB    1 
ATOM   823  C  CG1   . ILE A 1 105 ? -16.040 -17.200 -2.134  1.00 89.34  ? 105 ILE A CG1   1 
ATOM   824  C  CG2   . ILE A 1 105 ? -17.747 -18.024 -0.491  1.00 92.89  ? 105 ILE A CG2   1 
ATOM   825  C  CD1   . ILE A 1 105 ? -16.575 -15.786 -2.213  1.00 98.79  ? 105 ILE A CD1   1 
ATOM   826  N  N     . PRO A 1 106 ? -16.518 -16.770 2.593   1.00 84.93  ? 106 PRO A N     1 
ATOM   827  C  CA    . PRO A 1 106 ? -16.743 -17.204 3.976   1.00 86.02  ? 106 PRO A CA    1 
ATOM   828  C  C     . PRO A 1 106 ? -17.895 -18.193 4.076   1.00 92.94  ? 106 PRO A C     1 
ATOM   829  O  O     . PRO A 1 106 ? -18.650 -18.428 3.131   1.00 102.45 ? 106 PRO A O     1 
ATOM   830  C  CB    . PRO A 1 106 ? -17.072 -15.900 4.716   1.00 85.19  ? 106 PRO A CB    1 
ATOM   831  C  CG    . PRO A 1 106 ? -16.740 -14.786 3.750   1.00 91.25  ? 106 PRO A CG    1 
ATOM   832  C  CD    . PRO A 1 106 ? -16.913 -15.369 2.387   1.00 83.39  ? 106 PRO A CD    1 
ATOM   833  N  N     . LYS A 1 107 ? -18.016 -18.781 5.265   1.00 102.85 ? 107 LYS A N     1 
ATOM   834  C  CA    . LYS A 1 107 ? -19.140 -19.641 5.615   1.00 111.30 ? 107 LYS A CA    1 
ATOM   835  C  C     . LYS A 1 107 ? -20.108 -18.826 6.465   1.00 125.77 ? 107 LYS A C     1 
ATOM   836  O  O     . LYS A 1 107 ? -19.838 -18.560 7.641   1.00 125.80 ? 107 LYS A O     1 
ATOM   837  C  CB    . LYS A 1 107 ? -18.673 -20.889 6.362   1.00 108.48 ? 107 LYS A CB    1 
ATOM   838  C  CG    . LYS A 1 107 ? -19.815 -21.709 6.951   1.00 112.95 ? 107 LYS A CG    1 
ATOM   839  C  CD    . LYS A 1 107 ? -19.317 -22.819 7.868   1.00 109.22 ? 107 LYS A CD    1 
ATOM   840  C  CE    . LYS A 1 107 ? -18.770 -24.005 7.087   1.00 106.29 ? 107 LYS A CE    1 
ATOM   841  N  NZ    . LYS A 1 107 ? -17.514 -23.681 6.359   1.00 108.54 ? 107 LYS A NZ    1 
ATOM   842  N  N     . SER A 1 108 ? -21.227 -18.421 5.866   1.00 175.86 ? 108 SER A N     1 
ATOM   843  C  CA    . SER A 1 108 ? -22.247 -17.652 6.570   1.00 178.97 ? 108 SER A CA    1 
ATOM   844  C  C     . SER A 1 108 ? -21.777 -16.231 6.857   1.00 173.97 ? 108 SER A C     1 
ATOM   845  O  O     . SER A 1 108 ? -22.376 -15.264 6.375   1.00 175.43 ? 108 SER A O     1 
ATOM   846  C  CB    . SER A 1 108 ? -22.640 -18.351 7.874   1.00 181.72 ? 108 SER A CB    1 
ATOM   847  O  OG    . SER A 1 108 ? -23.154 -19.648 7.627   1.00 186.90 ? 108 SER A OG    1 
ATOM   848  N  N     . GLY A 1 109 ? -20.710 -16.094 7.638   1.00 131.55 ? 109 GLY A N     1 
ATOM   849  C  CA    . GLY A 1 109 ? -20.238 -14.792 8.055   1.00 124.74 ? 109 GLY A CA    1 
ATOM   850  C  C     . GLY A 1 109 ? -19.688 -13.962 6.908   1.00 114.30 ? 109 GLY A C     1 
ATOM   851  O  O     . GLY A 1 109 ? -19.630 -14.377 5.749   1.00 114.46 ? 109 GLY A O     1 
ATOM   852  N  N     . GLN A 1 110 ? -19.277 -12.747 7.256   1.00 106.42 ? 110 GLN A N     1 
ATOM   853  C  CA    . GLN A 1 110 ? -18.688 -11.805 6.317   1.00 98.05  ? 110 GLN A CA    1 
ATOM   854  C  C     . GLN A 1 110 ? -17.167 -11.908 6.360   1.00 92.76  ? 110 GLN A C     1 
ATOM   855  O  O     . GLN A 1 110 ? -16.578 -12.350 7.348   1.00 92.89  ? 110 GLN A O     1 
ATOM   856  C  CB    . GLN A 1 110 ? -19.131 -10.374 6.636   1.00 94.83  ? 110 GLN A CB    1 
ATOM   857  C  CG    . GLN A 1 110 ? -18.789 -9.349  5.563   1.00 96.15  ? 110 GLN A CG    1 
ATOM   858  C  CD    . GLN A 1 110 ? -19.639 -9.498  4.314   1.00 102.23 ? 110 GLN A CD    1 
ATOM   859  O  OE1   . GLN A 1 110 ? -19.675 -10.562 3.696   1.00 102.29 ? 110 GLN A OE1   1 
ATOM   860  N  NE2   . GLN A 1 110 ? -20.332 -8.429  3.939   1.00 104.13 ? 110 GLN A NE2   1 
ATOM   861  N  N     . SER A 1 111 ? -16.535 -11.484 5.269   1.00 79.85  ? 111 SER A N     1 
ATOM   862  C  CA    . SER A 1 111 ? -15.090 -11.615 5.107   1.00 77.73  ? 111 SER A CA    1 
ATOM   863  C  C     . SER A 1 111 ? -14.394 -10.408 5.727   1.00 72.75  ? 111 SER A C     1 
ATOM   864  O  O     . SER A 1 111 ? -14.538 -9.280  5.243   1.00 69.03  ? 111 SER A O     1 
ATOM   865  C  CB    . SER A 1 111 ? -14.730 -11.754 3.630   1.00 73.34  ? 111 SER A CB    1 
ATOM   866  O  OG    . SER A 1 111 ? -13.329 -11.879 3.455   1.00 76.85  ? 111 SER A OG    1 
ATOM   867  N  N     . GLN A 1 112 ? -13.634 -10.645 6.798   1.00 68.55  ? 112 GLN A N     1 
ATOM   868  C  CA    . GLN A 1 112 ? -12.786 -9.610  7.376   1.00 66.26  ? 112 GLN A CA    1 
ATOM   869  C  C     . GLN A 1 112 ? -11.460 -9.462  6.645   1.00 65.83  ? 112 GLN A C     1 
ATOM   870  O  O     . GLN A 1 112 ? -10.738 -8.491  6.894   1.00 61.53  ? 112 GLN A O     1 
ATOM   871  C  CB    . GLN A 1 112 ? -12.509 -9.909  8.853   1.00 73.25  ? 112 GLN A CB    1 
ATOM   872  C  CG    . GLN A 1 112 ? -13.750 -10.014 9.725   1.00 69.88  ? 112 GLN A CG    1 
ATOM   873  C  CD    . GLN A 1 112 ? -13.414 -10.180 11.197  1.00 57.10  ? 112 GLN A CD    1 
ATOM   874  O  OE1   . GLN A 1 112 ? -12.271 -9.981  11.611  1.00 66.25  ? 112 GLN A OE1   1 
ATOM   875  N  NE2   . GLN A 1 112 ? -14.411 -10.546 11.996  1.00 56.15  ? 112 GLN A NE2   1 
ATOM   876  N  N     . LEU A 1 113 ? -11.126 -10.394 5.756   1.00 73.15  ? 113 LEU A N     1 
ATOM   877  C  CA    . LEU A 1 113 ? -9.820  -10.407 5.111   1.00 65.34  ? 113 LEU A CA    1 
ATOM   878  C  C     . LEU A 1 113 ? -9.825  -9.560  3.846   1.00 64.51  ? 113 LEU A C     1 
ATOM   879  O  O     . LEU A 1 113 ? -9.129  -9.875  2.875   1.00 66.52  ? 113 LEU A O     1 
ATOM   880  C  CB    . LEU A 1 113 ? -9.405  -11.844 4.796   1.00 63.36  ? 113 LEU A CB    1 
ATOM   881  C  CG    . LEU A 1 113 ? -9.550  -12.845 5.946   1.00 58.37  ? 113 LEU A CG    1 
ATOM   882  C  CD1   . LEU A 1 113 ? -9.200  -14.249 5.479   1.00 58.76  ? 113 LEU A CD1   1 
ATOM   883  C  CD2   . LEU A 1 113 ? -8.690  -12.439 7.135   1.00 63.30  ? 113 LEU A CD2   1 
ATOM   884  N  N     . GLY A 1 114 ? -10.606 -8.483  3.850   1.00 80.20  ? 114 GLY A N     1 
ATOM   885  C  CA    . GLY A 1 114 ? -10.651 -7.590  2.712   1.00 88.80  ? 114 GLY A CA    1 
ATOM   886  C  C     . GLY A 1 114 ? -12.052 -7.329  2.201   1.00 86.00  ? 114 GLY A C     1 
ATOM   887  O  O     . GLY A 1 114 ? -12.973 -8.115  2.443   1.00 87.75  ? 114 GLY A O     1 
ATOM   888  N  N     . ARG A 1 115 ? -12.219 -6.220  1.487   1.00 80.13  ? 115 ARG A N     1 
ATOM   889  C  CA    . ARG A 1 115 ? -13.496 -5.831  0.904   1.00 87.65  ? 115 ARG A CA    1 
ATOM   890  C  C     . ARG A 1 115 ? -13.369 -5.856  -0.612  1.00 82.38  ? 115 ARG A C     1 
ATOM   891  O  O     . ARG A 1 115 ? -12.561 -5.115  -1.182  1.00 83.59  ? 115 ARG A O     1 
ATOM   892  C  CB    . ARG A 1 115 ? -13.920 -4.444  1.388   1.00 90.96  ? 115 ARG A CB    1 
ATOM   893  C  CG    . ARG A 1 115 ? -15.287 -4.003  0.889   1.00 97.24  ? 115 ARG A CG    1 
ATOM   894  C  CD    . ARG A 1 115 ? -15.619 -2.595  1.356   1.00 107.13 ? 115 ARG A CD    1 
ATOM   895  N  NE    . ARG A 1 115 ? -15.537 -2.468  2.806   1.00 111.69 ? 115 ARG A NE    1 
ATOM   896  C  CZ    . ARG A 1 115 ? -16.544 -2.699  3.637   1.00 113.28 ? 115 ARG A CZ    1 
ATOM   897  N  NH1   . ARG A 1 115 ? -17.732 -3.078  3.194   1.00 99.68  ? 115 ARG A NH1   1 
ATOM   898  N  NH2   . ARG A 1 115 ? -16.354 -2.545  4.944   1.00 111.73 ? 115 ARG A NH2   1 
ATOM   899  N  N     . TRP A 1 116 ? -14.168 -6.697  -1.259  1.00 91.37  ? 116 TRP A N     1 
ATOM   900  C  CA    . TRP A 1 116 ? -14.125 -6.862  -2.704  1.00 92.97  ? 116 TRP A CA    1 
ATOM   901  C  C     . TRP A 1 116 ? -15.256 -6.082  -3.363  1.00 94.89  ? 116 TRP A C     1 
ATOM   902  O  O     . TRP A 1 116 ? -16.361 -5.988  -2.821  1.00 92.93  ? 116 TRP A O     1 
ATOM   903  C  CB    . TRP A 1 116 ? -14.219 -8.340  -3.087  1.00 97.66  ? 116 TRP A CB    1 
ATOM   904  C  CG    . TRP A 1 116 ? -14.205 -8.573  -4.567  1.00 101.71 ? 116 TRP A CG    1 
ATOM   905  C  CD1   . TRP A 1 116 ? -13.111 -8.608  -5.381  1.00 101.04 ? 116 TRP A CD1   1 
ATOM   906  C  CD2   . TRP A 1 116 ? -15.340 -8.805  -5.411  1.00 107.08 ? 116 TRP A CD2   1 
ATOM   907  N  NE1   . TRP A 1 116 ? -13.493 -8.846  -6.679  1.00 96.07  ? 116 TRP A NE1   1 
ATOM   908  C  CE2   . TRP A 1 116 ? -14.857 -8.972  -6.724  1.00 107.21 ? 116 TRP A CE2   1 
ATOM   909  C  CE3   . TRP A 1 116 ? -16.717 -8.889  -5.183  1.00 110.62 ? 116 TRP A CE3   1 
ATOM   910  C  CZ2   . TRP A 1 116 ? -15.702 -9.216  -7.805  1.00 113.61 ? 116 TRP A CZ2   1 
ATOM   911  C  CZ3   . TRP A 1 116 ? -17.554 -9.132  -6.258  1.00 114.82 ? 116 TRP A CZ3   1 
ATOM   912  C  CH2   . TRP A 1 116 ? -17.043 -9.293  -7.552  1.00 114.30 ? 116 TRP A CH2   1 
ATOM   913  N  N     . MET A 1 117 ? -14.970 -5.527  -4.539  1.00 95.82  ? 117 MET A N     1 
ATOM   914  C  CA    . MET A 1 117 ? -15.941 -4.764  -5.308  1.00 100.45 ? 117 MET A CA    1 
ATOM   915  C  C     . MET A 1 117 ? -15.753 -5.067  -6.787  1.00 105.75 ? 117 MET A C     1 
ATOM   916  O  O     . MET A 1 117 ? -14.622 -5.182  -7.266  1.00 98.80  ? 117 MET A O     1 
ATOM   917  C  CB    . MET A 1 117 ? -15.799 -3.258  -5.051  1.00 96.22  ? 117 MET A CB    1 
ATOM   918  C  CG    . MET A 1 117 ? -16.808 -2.397  -5.795  1.00 101.20 ? 117 MET A CG    1 
ATOM   919  S  SD    . MET A 1 117 ? -16.633 -0.641  -5.420  1.00 78.50  ? 117 MET A SD    1 
ATOM   920  C  CE    . MET A 1 117 ? -17.010 -0.629  -3.669  1.00 86.48  ? 117 MET A CE    1 
ATOM   921  N  N     . SER A 1 118 ? -16.866 -5.194  -7.505  1.00 124.33 ? 118 SER A N     1 
ATOM   922  C  CA    . SER A 1 118 ? -16.822 -5.562  -8.911  1.00 128.92 ? 118 SER A CA    1 
ATOM   923  C  C     . SER A 1 118 ? -16.418 -4.369  -9.774  1.00 129.67 ? 118 SER A C     1 
ATOM   924  O  O     . SER A 1 118 ? -16.467 -3.212  -9.350  1.00 127.01 ? 118 SER A O     1 
ATOM   925  C  CB    . SER A 1 118 ? -18.178 -6.104  -9.365  1.00 128.24 ? 118 SER A CB    1 
ATOM   926  O  OG    . SER A 1 118 ? -19.208 -5.157  -9.140  1.00 128.83 ? 118 SER A OG    1 
ATOM   927  N  N     . GLU A 1 119 ? -16.012 -4.671  -11.011 1.00 116.57 ? 119 GLU A N     1 
ATOM   928  C  CA    . GLU A 1 119 ? -15.606 -3.612  -11.930 1.00 116.04 ? 119 GLU A CA    1 
ATOM   929  C  C     . GLU A 1 119 ? -16.785 -2.727  -12.317 1.00 116.16 ? 119 GLU A C     1 
ATOM   930  O  O     . GLU A 1 119 ? -16.625 -1.515  -12.497 1.00 111.31 ? 119 GLU A O     1 
ATOM   931  C  CB    . GLU A 1 119 ? -14.959 -4.210  -13.179 1.00 120.16 ? 119 GLU A CB    1 
ATOM   932  C  CG    . GLU A 1 119 ? -13.668 -4.977  -12.922 1.00 119.75 ? 119 GLU A CG    1 
ATOM   933  C  CD    . GLU A 1 119 ? -13.912 -6.407  -12.479 1.00 121.16 ? 119 GLU A CD    1 
ATOM   934  O  OE1   . GLU A 1 119 ? -15.080 -6.760  -12.211 1.00 119.70 ? 119 GLU A OE1   1 
ATOM   935  O  OE2   . GLU A 1 119 ? -12.935 -7.181  -12.404 1.00 120.20 ? 119 GLU A OE2   1 
ATOM   936  N  N     . GLU A 1 120 ? -17.976 -3.314  -12.454 1.00 115.63 ? 120 GLU A N     1 
ATOM   937  C  CA    . GLU A 1 120 ? -19.151 -2.528  -12.815 1.00 111.24 ? 120 GLU A CA    1 
ATOM   938  C  C     . GLU A 1 120 ? -19.504 -1.533  -11.716 1.00 109.87 ? 120 GLU A C     1 
ATOM   939  O  O     . GLU A 1 120 ? -19.779 -0.359  -11.991 1.00 102.22 ? 120 GLU A O     1 
ATOM   940  C  CB    . GLU A 1 120 ? -20.335 -3.451  -13.109 1.00 111.95 ? 120 GLU A CB    1 
ATOM   941  C  CG    . GLU A 1 120 ? -20.133 -4.370  -14.306 1.00 117.57 ? 120 GLU A CG    1 
ATOM   942  C  CD    . GLU A 1 120 ? -19.228 -5.548  -13.997 1.00 119.07 ? 120 GLU A CD    1 
ATOM   943  O  OE1   . GLU A 1 120 ? -19.068 -5.880  -12.804 1.00 115.96 ? 120 GLU A OE1   1 
ATOM   944  O  OE2   . GLU A 1 120 ? -18.675 -6.140  -14.947 1.00 121.11 ? 120 GLU A OE2   1 
ATOM   945  N  N     . ASP A 1 121 ? -19.501 -1.986  -10.461 1.00 119.11 ? 121 ASP A N     1 
ATOM   946  C  CA    . ASP A 1 121 ? -19.789 -1.085  -9.350  1.00 117.12 ? 121 ASP A CA    1 
ATOM   947  C  C     . ASP A 1 121 ? -18.696 -0.039  -9.177  1.00 112.85 ? 121 ASP A C     1 
ATOM   948  O  O     . ASP A 1 121 ? -18.972 1.073   -8.711  1.00 109.80 ? 121 ASP A O     1 
ATOM   949  C  CB    . ASP A 1 121 ? -19.969 -1.885  -8.060  1.00 124.13 ? 121 ASP A CB    1 
ATOM   950  C  CG    . ASP A 1 121 ? -21.093 -2.898  -8.156  1.00 122.20 ? 121 ASP A CG    1 
ATOM   951  O  OD1   . ASP A 1 121 ? -22.077 -2.630  -8.878  1.00 121.55 ? 121 ASP A OD1   1 
ATOM   952  O  OD2   . ASP A 1 121 ? -20.993 -3.962  -7.510  1.00 120.04 ? 121 ASP A OD2   1 
ATOM   953  N  N     . PHE A 1 122 ? -17.456 -0.370  -9.544  1.00 106.33 ? 122 PHE A N     1 
ATOM   954  C  CA    . PHE A 1 122 ? -16.365 0.591   -9.410  1.00 101.24 ? 122 PHE A CA    1 
ATOM   955  C  C     . PHE A 1 122 ? -16.439 1.667   -10.486 1.00 101.44 ? 122 PHE A C     1 
ATOM   956  O  O     . PHE A 1 122 ? -16.166 2.843   -10.215 1.00 93.58  ? 122 PHE A O     1 
ATOM   957  C  CB    . PHE A 1 122 ? -15.019 -0.132  -9.461  1.00 94.75  ? 122 PHE A CB    1 
ATOM   958  C  CG    . PHE A 1 122 ? -13.841 0.790   -9.594  1.00 97.71  ? 122 PHE A CG    1 
ATOM   959  C  CD1   . PHE A 1 122 ? -13.477 1.626   -8.551  1.00 90.66  ? 122 PHE A CD1   1 
ATOM   960  C  CD2   . PHE A 1 122 ? -13.095 0.817   -10.759 1.00 93.61  ? 122 PHE A CD2   1 
ATOM   961  C  CE1   . PHE A 1 122 ? -12.393 2.475   -8.672  1.00 78.85  ? 122 PHE A CE1   1 
ATOM   962  C  CE2   . PHE A 1 122 ? -12.009 1.662   -10.885 1.00 85.40  ? 122 PHE A CE2   1 
ATOM   963  C  CZ    . PHE A 1 122 ? -11.658 2.492   -9.840  1.00 79.21  ? 122 PHE A CZ    1 
ATOM   964  N  N     . GLU A 1 123 ? -16.804 1.287   -11.712 1.00 102.29 ? 123 GLU A N     1 
ATOM   965  C  CA    . GLU A 1 123 ? -16.919 2.272   -12.782 1.00 93.60  ? 123 GLU A CA    1 
ATOM   966  C  C     . GLU A 1 123 ? -18.024 3.281   -12.497 1.00 86.21  ? 123 GLU A C     1 
ATOM   967  O  O     . GLU A 1 123 ? -17.922 4.444   -12.901 1.00 82.00  ? 123 GLU A O     1 
ATOM   968  C  CB    . GLU A 1 123 ? -17.168 1.570   -14.117 1.00 94.26  ? 123 GLU A CB    1 
ATOM   969  C  CG    . GLU A 1 123 ? -17.263 2.511   -15.307 1.00 94.88  ? 123 GLU A CG    1 
ATOM   970  C  CD    . GLU A 1 123 ? -17.456 1.774   -16.617 1.00 118.50 ? 123 GLU A CD    1 
ATOM   971  O  OE1   . GLU A 1 123 ? -17.408 0.525   -16.611 1.00 131.38 ? 123 GLU A OE1   1 
ATOM   972  O  OE2   . GLU A 1 123 ? -17.655 2.441   -17.654 1.00 111.75 ? 123 GLU A OE2   1 
ATOM   973  N  N     . LYS A 1 124 ? -19.083 2.857   -11.803 1.00 97.15  ? 124 LYS A N     1 
ATOM   974  C  CA    . LYS A 1 124 ? -20.164 3.777   -11.469 1.00 91.30  ? 124 LYS A CA    1 
ATOM   975  C  C     . LYS A 1 124 ? -19.707 4.821   -10.458 1.00 85.99  ? 124 LYS A C     1 
ATOM   976  O  O     . LYS A 1 124 ? -20.052 6.003   -10.577 1.00 86.74  ? 124 LYS A O     1 
ATOM   977  C  CB    . LYS A 1 124 ? -21.364 2.997   -10.934 1.00 94.65  ? 124 LYS A CB    1 
ATOM   978  C  CG    . LYS A 1 124 ? -21.858 1.911   -11.875 1.00 96.92  ? 124 LYS A CG    1 
ATOM   979  C  CD    . LYS A 1 124 ? -22.804 0.953   -11.171 1.00 110.40 ? 124 LYS A CD    1 
ATOM   980  C  CE    . LYS A 1 124 ? -23.191 -0.201  -12.081 1.00 105.03 ? 124 LYS A CE    1 
ATOM   981  N  NZ    . LYS A 1 124 ? -23.970 -1.245  -11.360 1.00 104.17 ? 124 LYS A NZ    1 
ATOM   982  N  N     . ALA A 1 125 ? -18.930 4.405   -9.456  1.00 97.49  ? 125 ALA A N     1 
ATOM   983  C  CA    . ALA A 1 125 ? -18.426 5.346   -8.463  1.00 90.98  ? 125 ALA A CA    1 
ATOM   984  C  C     . ALA A 1 125 ? -17.250 6.157   -8.988  1.00 82.02  ? 125 ALA A C     1 
ATOM   985  O  O     . ALA A 1 125 ? -17.057 7.303   -8.569  1.00 81.78  ? 125 ALA A O     1 
ATOM   986  C  CB    . ALA A 1 125 ? -18.023 4.602   -7.189  1.00 92.69  ? 125 ALA A CB    1 
ATOM   987  N  N     . PHE A 1 126 ? -16.458 5.586   -9.899  1.00 82.66  ? 126 PHE A N     1 
ATOM   988  C  CA    . PHE A 1 126 ? -15.315 6.311   -10.444 1.00 80.45  ? 126 PHE A CA    1 
ATOM   989  C  C     . PHE A 1 126 ? -15.766 7.525   -11.245 1.00 82.83  ? 126 PHE A C     1 
ATOM   990  O  O     . PHE A 1 126 ? -15.220 8.624   -11.093 1.00 81.21  ? 126 PHE A O     1 
ATOM   991  C  CB    . PHE A 1 126 ? -14.467 5.376   -11.307 1.00 84.62  ? 126 PHE A CB    1 
ATOM   992  C  CG    . PHE A 1 126 ? -13.282 6.045   -11.943 1.00 83.17  ? 126 PHE A CG    1 
ATOM   993  C  CD1   . PHE A 1 126 ? -12.110 6.233   -11.229 1.00 79.20  ? 126 PHE A CD1   1 
ATOM   994  C  CD2   . PHE A 1 126 ? -13.338 6.483   -13.256 1.00 84.14  ? 126 PHE A CD2   1 
ATOM   995  C  CE1   . PHE A 1 126 ? -11.017 6.847   -11.812 1.00 78.63  ? 126 PHE A CE1   1 
ATOM   996  C  CE2   . PHE A 1 126 ? -12.248 7.098   -13.844 1.00 92.58  ? 126 PHE A CE2   1 
ATOM   997  C  CZ    . PHE A 1 126 ? -11.087 7.280   -13.121 1.00 74.39  ? 126 PHE A CZ    1 
ATOM   998  N  N     . ASN A 1 127 ? -16.769 7.346   -12.106 1.00 82.40  ? 127 ASN A N     1 
ATOM   999  C  CA    . ASN A 1 127 ? -17.276 8.439   -12.927 1.00 79.00  ? 127 ASN A CA    1 
ATOM   1000 C  C     . ASN A 1 127 ? -18.125 9.429   -12.143 1.00 78.26  ? 127 ASN A C     1 
ATOM   1001 O  O     . ASN A 1 127 ? -18.602 10.406  -12.730 1.00 81.89  ? 127 ASN A O     1 
ATOM   1002 C  CB    . ASN A 1 127 ? -18.084 7.880   -14.099 1.00 74.73  ? 127 ASN A CB    1 
ATOM   1003 C  CG    . ASN A 1 127 ? -17.242 7.041   -15.040 1.00 76.84  ? 127 ASN A CG    1 
ATOM   1004 O  OD1   . ASN A 1 127 ? -16.075 7.345   -15.287 1.00 72.23  ? 127 ASN A OD1   1 
ATOM   1005 N  ND2   . ASN A 1 127 ? -17.832 5.975   -15.570 1.00 87.93  ? 127 ASN A ND2   1 
ATOM   1006 N  N     . ALA A 1 128 ? -18.328 9.209   -10.845 1.00 78.81  ? 128 ALA A N     1 
ATOM   1007 C  CA    . ALA A 1 128 ? -19.115 10.107  -10.012 1.00 78.67  ? 128 ALA A CA    1 
ATOM   1008 C  C     . ALA A 1 128 ? -18.254 10.937  -9.069  1.00 76.10  ? 128 ALA A C     1 
ATOM   1009 O  O     . ALA A 1 128 ? -18.791 11.584  -8.164  1.00 69.09  ? 128 ALA A O     1 
ATOM   1010 C  CB    . ALA A 1 128 ? -20.152 9.315   -9.213  1.00 72.28  ? 128 ALA A CB    1 
ATOM   1011 N  N     . ARG A 1 129 ? -16.935 10.939  -9.259  1.00 81.68  ? 129 ARG A N     1 
ATOM   1012 C  CA    . ARG A 1 129 ? -16.041 11.650  -8.353  1.00 80.83  ? 129 ARG A CA    1 
ATOM   1013 C  C     . ARG A 1 129 ? -15.002 12.466  -9.113  1.00 80.92  ? 129 ARG A C     1 
ATOM   1014 O  O     . ARG A 1 129 ? -14.949 13.694  -8.986  1.00 82.05  ? 129 ARG A O     1 
ATOM   1015 C  CB    . ARG A 1 129 ? -15.337 10.666  -7.415  1.00 74.95  ? 129 ARG A CB    1 
ATOM   1016 C  CG    . ARG A 1 129 ? -16.255 9.661   -6.738  1.00 67.96  ? 129 ARG A CG    1 
ATOM   1017 C  CD    . ARG A 1 129 ? -15.445 8.620   -5.977  1.00 75.46  ? 129 ARG A CD    1 
ATOM   1018 N  NE    . ARG A 1 129 ? -16.265 7.507   -5.511  1.00 84.30  ? 129 ARG A NE    1 
ATOM   1019 C  CZ    . ARG A 1 129 ? -16.741 7.389   -4.279  1.00 83.31  ? 129 ARG A CZ    1 
ATOM   1020 N  NH1   . ARG A 1 129 ? -16.496 8.300   -3.352  1.00 77.70  ? 129 ARG A NH1   1 
ATOM   1021 N  NH2   . ARG A 1 129 ? -17.479 6.327   -3.968  1.00 87.41  ? 129 ARG A NH2   1 
ATOM   1022 N  N     . PHE A 1 130 ? -14.173 11.789  -9.904  1.00 78.22  ? 130 PHE A N     1 
ATOM   1023 C  CA    . PHE A 1 130 ? -13.003 12.392  -10.532 1.00 84.99  ? 130 PHE A CA    1 
ATOM   1024 C  C     . PHE A 1 130 ? -13.352 13.418  -11.606 1.00 88.16  ? 130 PHE A C     1 
ATOM   1025 O  O     . PHE A 1 130 ? -12.709 14.474  -11.671 1.00 92.28  ? 130 PHE A O     1 
ATOM   1026 C  CB    . PHE A 1 130 ? -12.108 11.301  -11.123 1.00 84.49  ? 130 PHE A CB    1 
ATOM   1027 C  CG    . PHE A 1 130 ? -11.273 10.588  -10.099 1.00 87.85  ? 130 PHE A CG    1 
ATOM   1028 C  CD1   . PHE A 1 130 ? -11.773 9.491   -9.417  1.00 84.44  ? 130 PHE A CD1   1 
ATOM   1029 C  CD2   . PHE A 1 130 ? -9.988  11.020  -9.812  1.00 82.61  ? 130 PHE A CD2   1 
ATOM   1030 C  CE1   . PHE A 1 130 ? -11.006 8.837   -8.471  1.00 79.46  ? 130 PHE A CE1   1 
ATOM   1031 C  CE2   . PHE A 1 130 ? -9.217  10.370  -8.869  1.00 80.13  ? 130 PHE A CE2   1 
ATOM   1032 C  CZ    . PHE A 1 130 ? -9.726  9.277   -8.197  1.00 80.06  ? 130 PHE A CZ    1 
ATOM   1033 N  N     . PRO A 1 131 ? -14.338 13.152  -12.478 1.00 87.62  ? 131 PRO A N     1 
ATOM   1034 C  CA    . PRO A 1 131 ? -14.655 14.119  -13.540 1.00 83.81  ? 131 PRO A CA    1 
ATOM   1035 C  C     . PRO A 1 131 ? -14.798 15.548  -13.035 1.00 80.20  ? 131 PRO A C     1 
ATOM   1036 O  O     . PRO A 1 131 ? -15.852 15.931  -12.519 1.00 75.34  ? 131 PRO A O     1 
ATOM   1037 C  CB    . PRO A 1 131 ? -15.978 13.588  -14.104 1.00 83.81  ? 131 PRO A CB    1 
ATOM   1038 C  CG    . PRO A 1 131 ? -15.891 12.119  -13.893 1.00 83.40  ? 131 PRO A CG    1 
ATOM   1039 C  CD    . PRO A 1 131 ? -15.158 11.932  -12.587 1.00 82.33  ? 131 PRO A CD    1 
ATOM   1040 N  N     . GLY A 1 132 ? -13.737 16.339  -13.181 1.00 83.97  ? 132 GLY A N     1 
ATOM   1041 C  CA    . GLY A 1 132 ? -13.761 17.731  -12.781 1.00 76.88  ? 132 GLY A CA    1 
ATOM   1042 C  C     . GLY A 1 132 ? -13.288 18.013  -11.374 1.00 74.32  ? 132 GLY A C     1 
ATOM   1043 O  O     . GLY A 1 132 ? -13.554 19.103  -10.856 1.00 77.08  ? 132 GLY A O     1 
ATOM   1044 N  N     . CYS A 1 133 ? -12.587 17.071  -10.739 1.00 70.17  ? 133 CYS A N     1 
ATOM   1045 C  CA    . CYS A 1 133 ? -12.168 17.260  -9.354  1.00 73.64  ? 133 CYS A CA    1 
ATOM   1046 C  C     . CYS A 1 133 ? -10.976 18.200  -9.227  1.00 74.63  ? 133 CYS A C     1 
ATOM   1047 O  O     . CYS A 1 133 ? -10.813 18.842  -8.184  1.00 79.22  ? 133 CYS A O     1 
ATOM   1048 C  CB    . CYS A 1 133 ? -11.839 15.910  -8.715  1.00 70.50  ? 133 CYS A CB    1 
ATOM   1049 S  SG    . CYS A 1 133 ? -10.545 14.974  -9.563  1.00 73.06  ? 133 CYS A SG    1 
ATOM   1050 N  N     . MET A 1 134 ? -10.134 18.296  -10.258 1.00 77.88  ? 134 MET A N     1 
ATOM   1051 C  CA    . MET A 1 134 ? -8.965  19.166  -10.229 1.00 75.39  ? 134 MET A CA    1 
ATOM   1052 C  C     . MET A 1 134 ? -9.216  20.507  -10.912 1.00 78.59  ? 134 MET A C     1 
ATOM   1053 O  O     . MET A 1 134 ? -8.263  21.165  -11.343 1.00 76.25  ? 134 MET A O     1 
ATOM   1054 C  CB    . MET A 1 134 ? -7.765  18.465  -10.868 1.00 72.89  ? 134 MET A CB    1 
ATOM   1055 C  CG    . MET A 1 134 ? -7.310  17.214  -10.134 1.00 66.71  ? 134 MET A CG    1 
ATOM   1056 S  SD    . MET A 1 134 ? -5.762  16.559  -10.786 1.00 52.66  ? 134 MET A SD    1 
ATOM   1057 C  CE    . MET A 1 134 ? -5.575  15.079  -9.794  1.00 59.20  ? 134 MET A CE    1 
ATOM   1058 N  N     . LYS A 1 135 ? -10.476 20.926  -11.014 1.00 88.84  ? 135 LYS A N     1 
ATOM   1059 C  CA    . LYS A 1 135 ? -10.809 22.199  -11.641 1.00 91.29  ? 135 LYS A CA    1 
ATOM   1060 C  C     . LYS A 1 135 ? -10.176 23.360  -10.885 1.00 90.00  ? 135 LYS A C     1 
ATOM   1061 O  O     . LYS A 1 135 ? -10.573 23.665  -9.756  1.00 92.31  ? 135 LYS A O     1 
ATOM   1062 C  CB    . LYS A 1 135 ? -12.328 22.375  -11.713 1.00 102.78 ? 135 LYS A CB    1 
ATOM   1063 C  CG    . LYS A 1 135 ? -12.780 23.693  -12.320 1.00 122.85 ? 135 LYS A CG    1 
ATOM   1064 C  CD    . LYS A 1 135 ? -14.298 23.806  -12.307 1.00 127.09 ? 135 LYS A CD    1 
ATOM   1065 C  CE    . LYS A 1 135 ? -14.764 25.153  -12.837 1.00 135.23 ? 135 LYS A CE    1 
ATOM   1066 N  NZ    . LYS A 1 135 ? -14.379 25.358  -14.260 1.00 140.99 ? 135 LYS A NZ    1 
ATOM   1067 N  N     . GLY A 1 136 ? -9.190  24.009  -11.497 1.00 80.79  ? 136 GLY A N     1 
ATOM   1068 C  CA    . GLY A 1 136 ? -8.534  25.148  -10.889 1.00 75.52  ? 136 GLY A CA    1 
ATOM   1069 C  C     . GLY A 1 136 ? -7.323  24.831  -10.041 1.00 76.42  ? 136 GLY A C     1 
ATOM   1070 O  O     . GLY A 1 136 ? -6.784  25.741  -9.401  1.00 69.93  ? 136 GLY A O     1 
ATOM   1071 N  N     . ARG A 1 137 ? -6.878  23.579  -10.013 1.00 70.95  ? 137 ARG A N     1 
ATOM   1072 C  CA    . ARG A 1 137 ? -5.722  23.171  -9.229  1.00 57.81  ? 137 ARG A CA    1 
ATOM   1073 C  C     . ARG A 1 137 ? -4.598  22.716  -10.151 1.00 65.43  ? 137 ARG A C     1 
ATOM   1074 O  O     . ARG A 1 137 ? -4.755  22.627  -11.372 1.00 69.45  ? 137 ARG A O     1 
ATOM   1075 C  CB    . ARG A 1 137 ? -6.095  22.054  -8.248  1.00 56.32  ? 137 ARG A CB    1 
ATOM   1076 C  CG    . ARG A 1 137 ? -7.143  22.451  -7.224  1.00 64.65  ? 137 ARG A CG    1 
ATOM   1077 C  CD    . ARG A 1 137 ? -7.382  21.336  -6.219  1.00 68.78  ? 137 ARG A CD    1 
ATOM   1078 N  NE    . ARG A 1 137 ? -8.359  21.716  -5.206  1.00 75.31  ? 137 ARG A NE    1 
ATOM   1079 C  CZ    . ARG A 1 137 ? -8.065  22.367  -4.089  1.00 72.43  ? 137 ARG A CZ    1 
ATOM   1080 N  NH1   . ARG A 1 137 ? -6.826  22.737  -3.810  1.00 79.28  ? 137 ARG A NH1   1 
ATOM   1081 N  NH2   . ARG A 1 137 ? -9.039  22.655  -3.230  1.00 73.71  ? 137 ARG A NH2   1 
ATOM   1082 N  N     . THR A 1 138 ? -3.451  22.427  -9.544  1.00 58.78  ? 138 THR A N     1 
ATOM   1083 C  CA    . THR A 1 138 ? -2.275  21.968  -10.267 1.00 58.37  ? 138 THR A CA    1 
ATOM   1084 C  C     . THR A 1 138 ? -2.121  20.462  -10.104 1.00 52.88  ? 138 THR A C     1 
ATOM   1085 O  O     . THR A 1 138 ? -2.265  19.928  -9.000  1.00 49.46  ? 138 THR A O     1 
ATOM   1086 C  CB    . THR A 1 138 ? -1.011  22.674  -9.768  1.00 55.03  ? 138 THR A CB    1 
ATOM   1087 O  OG1   . THR A 1 138 ? -1.149  24.090  -9.942  1.00 72.04  ? 138 THR A OG1   1 
ATOM   1088 C  CG2   . THR A 1 138 ? 0.206   22.191  -10.541 1.00 43.78  ? 138 THR A CG2   1 
ATOM   1089 N  N     . MET A 1 139 ? -1.828  19.784  -11.210 1.00 48.82  ? 139 MET A N     1 
ATOM   1090 C  CA    . MET A 1 139 ? -1.613  18.341  -11.223 1.00 52.24  ? 139 MET A CA    1 
ATOM   1091 C  C     . MET A 1 139 ? -0.112  18.075  -11.225 1.00 47.85  ? 139 MET A C     1 
ATOM   1092 O  O     . MET A 1 139 ? 0.574   18.363  -12.211 1.00 52.21  ? 139 MET A O     1 
ATOM   1093 C  CB    . MET A 1 139 ? -2.282  17.700  -12.437 1.00 44.69  ? 139 MET A CB    1 
ATOM   1094 C  CG    . MET A 1 139 ? -1.869  16.256  -12.671 1.00 51.30  ? 139 MET A CG    1 
ATOM   1095 S  SD    . MET A 1 139 ? -2.485  15.580  -14.225 1.00 54.36  ? 139 MET A SD    1 
ATOM   1096 C  CE    . MET A 1 139 ? -4.248  15.565  -13.914 1.00 56.85  ? 139 MET A CE    1 
ATOM   1097 N  N     . TYR A 1 140 ? 0.394   17.528  -10.123 1.00 46.02  ? 140 TYR A N     1 
ATOM   1098 C  CA    . TYR A 1 140 ? 1.804   17.185  -10.010 1.00 43.14  ? 140 TYR A CA    1 
ATOM   1099 C  C     . TYR A 1 140 ? 2.028   15.760  -10.501 1.00 43.60  ? 140 TYR A C     1 
ATOM   1100 O  O     . TYR A 1 140 ? 1.301   14.841  -10.111 1.00 52.00  ? 140 TYR A O     1 
ATOM   1101 C  CB    . TYR A 1 140 ? 2.284   17.321  -8.564  1.00 49.48  ? 140 TYR A CB    1 
ATOM   1102 C  CG    . TYR A 1 140 ? 2.078   18.693  -7.964  1.00 49.30  ? 140 TYR A CG    1 
ATOM   1103 C  CD1   . TYR A 1 140 ? 2.968   19.726  -8.222  1.00 45.78  ? 140 TYR A CD1   1 
ATOM   1104 C  CD2   . TYR A 1 140 ? 0.998   18.951  -7.130  1.00 47.04  ? 140 TYR A CD2   1 
ATOM   1105 C  CE1   . TYR A 1 140 ? 2.785   20.981  -7.673  1.00 51.28  ? 140 TYR A CE1   1 
ATOM   1106 C  CE2   . TYR A 1 140 ? 0.807   20.202  -6.575  1.00 50.74  ? 140 TYR A CE2   1 
ATOM   1107 C  CZ    . TYR A 1 140 ? 1.703   21.213  -6.850  1.00 55.73  ? 140 TYR A CZ    1 
ATOM   1108 O  OH    . TYR A 1 140 ? 1.515   22.460  -6.299  1.00 59.75  ? 140 TYR A OH    1 
ATOM   1109 N  N     . VAL A 1 141 ? 3.030   15.583  -11.355 1.00 46.14  ? 141 VAL A N     1 
ATOM   1110 C  CA    . VAL A 1 141 ? 3.432   14.268  -11.841 1.00 48.77  ? 141 VAL A CA    1 
ATOM   1111 C  C     . VAL A 1 141 ? 4.623   13.821  -11.003 1.00 47.41  ? 141 VAL A C     1 
ATOM   1112 O  O     . VAL A 1 141 ? 5.709   14.404  -11.090 1.00 43.33  ? 141 VAL A O     1 
ATOM   1113 C  CB    . VAL A 1 141 ? 3.773   14.295  -13.336 1.00 45.10  ? 141 VAL A CB    1 
ATOM   1114 C  CG1   . VAL A 1 141 ? 4.080   12.893  -13.833 1.00 45.66  ? 141 VAL A CG1   1 
ATOM   1115 C  CG2   . VAL A 1 141 ? 2.630   14.911  -14.128 1.00 51.76  ? 141 VAL A CG2   1 
ATOM   1116 N  N     . ILE A 1 142 ? 4.425   12.787  -10.190 1.00 50.54  ? 142 ILE A N     1 
ATOM   1117 C  CA    . ILE A 1 142 ? 5.434   12.354  -9.226  1.00 48.82  ? 142 ILE A CA    1 
ATOM   1118 C  C     . ILE A 1 142 ? 6.046   11.031  -9.669  1.00 44.02  ? 142 ILE A C     1 
ATOM   1119 O  O     . ILE A 1 142 ? 5.406   9.978   -9.535  1.00 54.57  ? 142 ILE A O     1 
ATOM   1120 C  CB    . ILE A 1 142 ? 4.835   12.229  -7.817  1.00 44.85  ? 142 ILE A CB    1 
ATOM   1121 C  CG1   . ILE A 1 142 ? 4.195   13.551  -7.390  1.00 44.93  ? 142 ILE A CG1   1 
ATOM   1122 C  CG2   . ILE A 1 142 ? 5.904   11.804  -6.822  1.00 49.61  ? 142 ILE A CG2   1 
ATOM   1123 C  CD1   . ILE A 1 142 ? 3.467   13.478  -6.067  1.00 45.09  ? 142 ILE A CD1   1 
ATOM   1124 N  N     . PRO A 1 143 ? 7.273   11.031  -10.196 1.00 48.08  ? 143 PRO A N     1 
ATOM   1125 C  CA    . PRO A 1 143 ? 7.939   9.764   -10.516 1.00 55.01  ? 143 PRO A CA    1 
ATOM   1126 C  C     . PRO A 1 143 ? 8.843   9.297   -9.386  1.00 63.16  ? 143 PRO A C     1 
ATOM   1127 O  O     . PRO A 1 143 ? 9.885   9.907   -9.126  1.00 64.13  ? 143 PRO A O     1 
ATOM   1128 C  CB    . PRO A 1 143 ? 8.741   10.106  -11.778 1.00 45.13  ? 143 PRO A CB    1 
ATOM   1129 C  CG    . PRO A 1 143 ? 8.948   11.623  -11.716 1.00 51.85  ? 143 PRO A CG    1 
ATOM   1130 C  CD    . PRO A 1 143 ? 8.089   12.186  -10.602 1.00 46.88  ? 143 PRO A CD    1 
ATOM   1131 N  N     . PHE A 1 144 ? 8.457   8.222   -8.711  1.00 57.60  ? 144 PHE A N     1 
ATOM   1132 C  CA    . PHE A 1 144 ? 9.192   7.699   -7.568  1.00 59.45  ? 144 PHE A CA    1 
ATOM   1133 C  C     . PHE A 1 144 ? 9.702   6.293   -7.877  1.00 60.10  ? 144 PHE A C     1 
ATOM   1134 O  O     . PHE A 1 144 ? 9.418   5.719   -8.931  1.00 64.02  ? 144 PHE A O     1 
ATOM   1135 C  CB    . PHE A 1 144 ? 8.316   7.702   -6.311  1.00 55.22  ? 144 PHE A CB    1 
ATOM   1136 C  CG    . PHE A 1 144 ? 7.097   6.831   -6.418  1.00 57.65  ? 144 PHE A CG    1 
ATOM   1137 C  CD1   . PHE A 1 144 ? 5.920   7.325   -6.954  1.00 60.36  ? 144 PHE A CD1   1 
ATOM   1138 C  CD2   . PHE A 1 144 ? 7.127   5.519   -5.977  1.00 59.31  ? 144 PHE A CD2   1 
ATOM   1139 C  CE1   . PHE A 1 144 ? 4.797   6.526   -7.051  1.00 55.81  ? 144 PHE A CE1   1 
ATOM   1140 C  CE2   . PHE A 1 144 ? 6.008   4.715   -6.071  1.00 56.43  ? 144 PHE A CE2   1 
ATOM   1141 C  CZ    . PHE A 1 144 ? 4.841   5.219   -6.609  1.00 65.32  ? 144 PHE A CZ    1 
ATOM   1142 N  N     . SER A 1 145 ? 10.466  5.741   -6.936  1.00 74.30  ? 145 SER A N     1 
ATOM   1143 C  CA    . SER A 1 145 ? 11.036  4.407   -7.090  1.00 55.48  ? 145 SER A CA    1 
ATOM   1144 C  C     . SER A 1 145 ? 11.069  3.732   -5.729  1.00 62.27  ? 145 SER A C     1 
ATOM   1145 O  O     . SER A 1 145 ? 11.751  4.209   -4.817  1.00 67.02  ? 145 SER A O     1 
ATOM   1146 C  CB    . SER A 1 145 ? 12.440  4.473   -7.695  1.00 61.78  ? 145 SER A CB    1 
ATOM   1147 O  OG    . SER A 1 145 ? 13.031  3.187   -7.758  1.00 59.90  ? 145 SER A OG    1 
ATOM   1148 N  N     . MET A 1 146 ? 10.336  2.631   -5.594  1.00 60.92  ? 146 MET A N     1 
ATOM   1149 C  CA    . MET A 1 146 ? 10.319  1.859   -4.354  1.00 59.29  ? 146 MET A CA    1 
ATOM   1150 C  C     . MET A 1 146 ? 11.524  0.928   -4.355  1.00 65.13  ? 146 MET A C     1 
ATOM   1151 O  O     . MET A 1 146 ? 11.538  -0.091  -5.050  1.00 59.80  ? 146 MET A O     1 
ATOM   1152 C  CB    . MET A 1 146 ? 9.014   1.083   -4.220  1.00 52.68  ? 146 MET A CB    1 
ATOM   1153 C  CG    . MET A 1 146 ? 7.773   1.957   -4.205  1.00 52.63  ? 146 MET A CG    1 
ATOM   1154 S  SD    . MET A 1 146 ? 7.783   3.161   -2.864  1.00 59.81  ? 146 MET A SD    1 
ATOM   1155 C  CE    . MET A 1 146 ? 7.879   2.079   -1.440  1.00 58.60  ? 146 MET A CE    1 
ATOM   1156 N  N     . GLY A 1 147 ? 12.541  1.278   -3.574  1.00 71.05  ? 147 GLY A N     1 
ATOM   1157 C  CA    . GLY A 1 147 ? 13.768  0.521   -3.533  1.00 71.93  ? 147 GLY A CA    1 
ATOM   1158 C  C     . GLY A 1 147 ? 14.887  1.226   -4.272  1.00 80.86  ? 147 GLY A C     1 
ATOM   1159 O  O     . GLY A 1 147 ? 14.666  2.203   -4.994  1.00 79.54  ? 147 GLY A O     1 
ATOM   1160 N  N     . PRO A 1 148 ? 16.117  0.746   -4.099  1.00 91.37  ? 148 PRO A N     1 
ATOM   1161 C  CA    . PRO A 1 148 ? 17.250  1.369   -4.794  1.00 97.02  ? 148 PRO A CA    1 
ATOM   1162 C  C     . PRO A 1 148 ? 17.086  1.279   -6.304  1.00 107.89 ? 148 PRO A C     1 
ATOM   1163 O  O     . PRO A 1 148 ? 16.621  0.271   -6.840  1.00 112.13 ? 148 PRO A O     1 
ATOM   1164 C  CB    . PRO A 1 148 ? 18.456  0.556   -4.307  1.00 88.99  ? 148 PRO A CB    1 
ATOM   1165 C  CG    . PRO A 1 148 ? 18.007  -0.061  -3.019  1.00 83.16  ? 148 PRO A CG    1 
ATOM   1166 C  CD    . PRO A 1 148 ? 16.546  -0.338  -3.200  1.00 86.78  ? 148 PRO A CD    1 
ATOM   1167 N  N     . LEU A 1 149 ? 17.473  2.353   -6.990  1.00 113.42 ? 149 LEU A N     1 
ATOM   1168 C  CA    . LEU A 1 149 ? 17.393  2.378   -8.444  1.00 119.97 ? 149 LEU A CA    1 
ATOM   1169 C  C     . LEU A 1 149 ? 18.320  1.330   -9.046  1.00 130.10 ? 149 LEU A C     1 
ATOM   1170 O  O     . LEU A 1 149 ? 19.485  1.213   -8.653  1.00 133.29 ? 149 LEU A O     1 
ATOM   1171 C  CB    . LEU A 1 149 ? 17.749  3.768   -8.972  1.00 114.91 ? 149 LEU A CB    1 
ATOM   1172 C  CG    . LEU A 1 149 ? 16.664  4.839   -8.857  1.00 113.27 ? 149 LEU A CG    1 
ATOM   1173 C  CD1   . LEU A 1 149 ? 17.175  6.177   -9.368  1.00 106.55 ? 149 LEU A CD1   1 
ATOM   1174 C  CD2   . LEU A 1 149 ? 15.418  4.413   -9.617  1.00 108.17 ? 149 LEU A CD2   1 
ATOM   1175 N  N     . GLY A 1 150 ? 17.797  0.567   -10.004 1.00 125.52 ? 150 GLY A N     1 
ATOM   1176 C  CA    . GLY A 1 150 ? 18.558  -0.472  -10.662 1.00 123.12 ? 150 GLY A CA    1 
ATOM   1177 C  C     . GLY A 1 150 ? 18.720  -1.753  -9.876  1.00 130.89 ? 150 GLY A C     1 
ATOM   1178 O  O     . GLY A 1 150 ? 19.199  -2.747  -10.437 1.00 135.41 ? 150 GLY A O     1 
ATOM   1179 N  N     . SER A 1 151 ? 18.340  -1.771  -8.603  1.00 147.30 ? 151 SER A N     1 
ATOM   1180 C  CA    . SER A 1 151 ? 18.471  -2.965  -7.787  1.00 146.04 ? 151 SER A CA    1 
ATOM   1181 C  C     . SER A 1 151 ? 17.382  -3.977  -8.130  1.00 149.49 ? 151 SER A C     1 
ATOM   1182 O  O     . SER A 1 151 ? 16.368  -3.633  -8.744  1.00 148.73 ? 151 SER A O     1 
ATOM   1183 C  CB    . SER A 1 151 ? 18.399  -2.601  -6.308  1.00 142.15 ? 151 SER A CB    1 
ATOM   1184 O  OG    . SER A 1 151 ? 17.171  -1.965  -6.000  1.00 141.17 ? 151 SER A OG    1 
ATOM   1185 N  N     . PRO A 1 152 ? 17.570  -5.236  -7.746  1.00 144.86 ? 152 PRO A N     1 
ATOM   1186 C  CA    . PRO A 1 152 ? 16.543  -6.247  -8.015  1.00 143.30 ? 152 PRO A CA    1 
ATOM   1187 C  C     . PRO A 1 152 ? 15.291  -6.003  -7.188  1.00 135.40 ? 152 PRO A C     1 
ATOM   1188 O  O     . PRO A 1 152 ? 15.341  -5.456  -6.084  1.00 131.77 ? 152 PRO A O     1 
ATOM   1189 C  CB    . PRO A 1 152 ? 17.226  -7.561  -7.619  1.00 145.67 ? 152 PRO A CB    1 
ATOM   1190 C  CG    . PRO A 1 152 ? 18.257  -7.157  -6.618  1.00 146.24 ? 152 PRO A CG    1 
ATOM   1191 C  CD    . PRO A 1 152 ? 18.740  -5.802  -7.052  1.00 146.57 ? 152 PRO A CD    1 
ATOM   1192 N  N     . LEU A 1 153 ? 14.153  -6.421  -7.744  1.00 120.64 ? 153 LEU A N     1 
ATOM   1193 C  CA    . LEU A 1 153 ? 12.851  -6.223  -7.109  1.00 109.71 ? 153 LEU A CA    1 
ATOM   1194 C  C     . LEU A 1 153 ? 12.563  -4.745  -6.861  1.00 97.60  ? 153 LEU A C     1 
ATOM   1195 O  O     . LEU A 1 153 ? 11.838  -4.389  -5.930  1.00 90.88  ? 153 LEU A O     1 
ATOM   1196 C  CB    . LEU A 1 153 ? 12.742  -7.013  -5.801  1.00 108.60 ? 153 LEU A CB    1 
ATOM   1197 C  CG    . LEU A 1 153 ? 12.744  -8.537  -5.923  1.00 95.86  ? 153 LEU A CG    1 
ATOM   1198 C  CD1   . LEU A 1 153 ? 12.484  -9.182  -4.570  1.00 74.99  ? 153 LEU A CD1   1 
ATOM   1199 C  CD2   . LEU A 1 153 ? 11.718  -8.996  -6.948  1.00 86.04  ? 153 LEU A CD2   1 
ATOM   1200 N  N     . ALA A 1 154 ? 13.131  -3.876  -7.691  1.00 101.04 ? 154 ALA A N     1 
ATOM   1201 C  CA    . ALA A 1 154 ? 12.912  -2.439  -7.599  1.00 96.27  ? 154 ALA A CA    1 
ATOM   1202 C  C     . ALA A 1 154 ? 11.808  -2.046  -8.572  1.00 86.52  ? 154 ALA A C     1 
ATOM   1203 O  O     . ALA A 1 154 ? 11.900  -2.334  -9.770  1.00 82.57  ? 154 ALA A O     1 
ATOM   1204 C  CB    . ALA A 1 154 ? 14.196  -1.668  -7.898  1.00 95.45  ? 154 ALA A CB    1 
ATOM   1205 N  N     . LYS A 1 155 ? 10.769  -1.394  -8.058  1.00 74.82  ? 155 LYS A N     1 
ATOM   1206 C  CA    . LYS A 1 155 ? 9.611   -1.014  -8.851  1.00 74.32  ? 155 LYS A CA    1 
ATOM   1207 C  C     . LYS A 1 155 ? 9.505   0.502   -8.933  1.00 70.26  ? 155 LYS A C     1 
ATOM   1208 O  O     . LYS A 1 155 ? 9.843   1.219   -7.986  1.00 68.86  ? 155 LYS A O     1 
ATOM   1209 C  CB    . LYS A 1 155 ? 8.321   -1.599  -8.263  1.00 73.63  ? 155 LYS A CB    1 
ATOM   1210 C  CG    . LYS A 1 155 ? 8.363   -3.105  -8.059  1.00 79.38  ? 155 LYS A CG    1 
ATOM   1211 C  CD    . LYS A 1 155 ? 8.724   -3.826  -9.348  1.00 80.89  ? 155 LYS A CD    1 
ATOM   1212 C  CE    . LYS A 1 155 ? 8.816   -5.328  -9.137  1.00 89.38  ? 155 LYS A CE    1 
ATOM   1213 N  NZ    . LYS A 1 155 ? 9.170   -6.043  -10.394 1.00 100.75 ? 155 LYS A NZ    1 
ATOM   1214 N  N     . ILE A 1 156 ? 9.028   0.984   -10.078 1.00 78.01  ? 156 ILE A N     1 
ATOM   1215 C  CA    . ILE A 1 156 ? 8.875   2.409   -10.342 1.00 71.79  ? 156 ILE A CA    1 
ATOM   1216 C  C     . ILE A 1 156 ? 7.401   2.710   -10.563 1.00 67.72  ? 156 ILE A C     1 
ATOM   1217 O  O     . ILE A 1 156 ? 6.683   1.925   -11.192 1.00 63.86  ? 156 ILE A O     1 
ATOM   1218 C  CB    . ILE A 1 156 ? 9.712   2.856   -11.559 1.00 67.83  ? 156 ILE A CB    1 
ATOM   1219 C  CG1   . ILE A 1 156 ? 11.204  2.651   -11.283 1.00 70.16  ? 156 ILE A CG1   1 
ATOM   1220 C  CG2   . ILE A 1 156 ? 9.419   4.308   -11.905 1.00 69.33  ? 156 ILE A CG2   1 
ATOM   1221 C  CD1   . ILE A 1 156 ? 12.099  3.083   -12.423 1.00 71.56  ? 156 ILE A CD1   1 
ATOM   1222 N  N     . GLY A 1 157 ? 6.952   3.854   -10.047 1.00 67.76  ? 157 GLY A N     1 
ATOM   1223 C  CA    . GLY A 1 157 ? 5.565   4.246   -10.178 1.00 66.61  ? 157 GLY A CA    1 
ATOM   1224 C  C     . GLY A 1 157 ? 5.442   5.709   -10.555 1.00 56.96  ? 157 GLY A C     1 
ATOM   1225 O  O     . GLY A 1 157 ? 6.382   6.496   -10.418 1.00 58.79  ? 157 GLY A O     1 
ATOM   1226 N  N     . ILE A 1 158 ? 4.253   6.060   -11.038 1.00 62.10  ? 158 ILE A N     1 
ATOM   1227 C  CA    . ILE A 1 158 ? 3.922   7.423   -11.437 1.00 53.81  ? 158 ILE A CA    1 
ATOM   1228 C  C     . ILE A 1 158 ? 2.627   7.800   -10.731 1.00 51.94  ? 158 ILE A C     1 
ATOM   1229 O  O     . ILE A 1 158 ? 1.565   7.243   -11.038 1.00 61.28  ? 158 ILE A O     1 
ATOM   1230 C  CB    . ILE A 1 158 ? 3.774   7.566   -12.958 1.00 57.36  ? 158 ILE A CB    1 
ATOM   1231 C  CG1   . ILE A 1 158 ? 5.079   7.191   -13.664 1.00 59.25  ? 158 ILE A CG1   1 
ATOM   1232 C  CG2   . ILE A 1 158 ? 3.357   8.984   -13.321 1.00 51.77  ? 158 ILE A CG2   1 
ATOM   1233 C  CD1   . ILE A 1 158 ? 6.233   8.118   -13.353 1.00 62.95  ? 158 ILE A CD1   1 
ATOM   1234 N  N     . GLU A 1 159 ? 2.708   8.736   -9.790  1.00 47.21  ? 159 GLU A N     1 
ATOM   1235 C  CA    . GLU A 1 159 ? 1.547   9.199   -9.043  1.00 48.09  ? 159 GLU A CA    1 
ATOM   1236 C  C     . GLU A 1 159 ? 1.186   10.614  -9.472  1.00 53.43  ? 159 GLU A C     1 
ATOM   1237 O  O     . GLU A 1 159 ? 2.029   11.517  -9.429  1.00 51.27  ? 159 GLU A O     1 
ATOM   1238 C  CB    . GLU A 1 159 ? 1.801   9.162   -7.534  1.00 50.49  ? 159 GLU A CB    1 
ATOM   1239 C  CG    . GLU A 1 159 ? 0.664   9.764   -6.719  1.00 40.27  ? 159 GLU A CG    1 
ATOM   1240 C  CD    . GLU A 1 159 ? 0.866   9.615   -5.226  1.00 53.82  ? 159 GLU A CD    1 
ATOM   1241 O  OE1   . GLU A 1 159 ? 1.798   8.889   -4.819  1.00 55.83  ? 159 GLU A OE1   1 
ATOM   1242 O  OE2   . GLU A 1 159 ? 0.091   10.224  -4.457  1.00 42.20  ? 159 GLU A OE2   1 
ATOM   1243 N  N     . LEU A 1 160 ? -0.066  10.800  -9.879  1.00 57.23  ? 160 LEU A N     1 
ATOM   1244 C  CA    . LEU A 1 160 ? -0.606  12.113  -10.201 1.00 47.49  ? 160 LEU A CA    1 
ATOM   1245 C  C     . LEU A 1 160 ? -1.476  12.583  -9.044  1.00 44.30  ? 160 LEU A C     1 
ATOM   1246 O  O     . LEU A 1 160 ? -2.360  11.850  -8.589  1.00 50.88  ? 160 LEU A O     1 
ATOM   1247 C  CB    . LEU A 1 160 ? -1.422  12.067  -11.494 1.00 45.58  ? 160 LEU A CB    1 
ATOM   1248 C  CG    . LEU A 1 160 ? -0.743  11.436  -12.712 1.00 42.40  ? 160 LEU A CG    1 
ATOM   1249 C  CD1   . LEU A 1 160 ? -1.641  11.534  -13.935 1.00 59.10  ? 160 LEU A CD1   1 
ATOM   1250 C  CD2   . LEU A 1 160 ? 0.606   12.084  -12.977 1.00 58.35  ? 160 LEU A CD2   1 
ATOM   1251 N  N     . THR A 1 161 ? -1.222  13.799  -8.568  1.00 41.37  ? 161 THR A N     1 
ATOM   1252 C  CA    . THR A 1 161 ? -1.964  14.337  -7.438  1.00 49.71  ? 161 THR A CA    1 
ATOM   1253 C  C     . THR A 1 161 ? -2.077  15.847  -7.585  1.00 51.75  ? 161 THR A C     1 
ATOM   1254 O  O     . THR A 1 161 ? -1.382  16.471  -8.391  1.00 48.56  ? 161 THR A O     1 
ATOM   1255 C  CB    . THR A 1 161 ? -1.301  13.973  -6.105  1.00 44.58  ? 161 THR A CB    1 
ATOM   1256 O  OG1   . THR A 1 161 ? -2.090  14.481  -5.021  1.00 51.42  ? 161 THR A OG1   1 
ATOM   1257 C  CG2   . THR A 1 161 ? 0.097   14.566  -6.027  1.00 43.10  ? 161 THR A CG2   1 
ATOM   1258 N  N     . ASP A 1 162 ? -2.972  16.430  -6.788  1.00 52.25  ? 162 ASP A N     1 
ATOM   1259 C  CA    . ASP A 1 162 ? -3.177  17.873  -6.761  1.00 57.14  ? 162 ASP A CA    1 
ATOM   1260 C  C     . ASP A 1 162 ? -2.858  18.476  -5.399  1.00 56.01  ? 162 ASP A C     1 
ATOM   1261 O  O     . ASP A 1 162 ? -3.212  19.634  -5.147  1.00 54.69  ? 162 ASP A O     1 
ATOM   1262 C  CB    . ASP A 1 162 ? -4.616  18.212  -7.162  1.00 62.42  ? 162 ASP A CB    1 
ATOM   1263 C  CG    . ASP A 1 162 ? -5.644  17.497  -6.306  1.00 64.17  ? 162 ASP A CG    1 
ATOM   1264 O  OD1   . ASP A 1 162 ? -5.242  16.750  -5.389  1.00 56.55  ? 162 ASP A OD1   1 
ATOM   1265 O  OD2   . ASP A 1 162 ? -6.855  17.681  -6.551  1.00 65.41  ? 162 ASP A OD2   1 
ATOM   1266 N  N     . SER A 1 163 ? -2.199  17.725  -4.518  1.00 48.52  ? 163 SER A N     1 
ATOM   1267 C  CA    . SER A 1 163 ? -1.887  18.192  -3.176  1.00 49.67  ? 163 SER A CA    1 
ATOM   1268 C  C     . SER A 1 163 ? -0.384  18.350  -3.022  1.00 57.40  ? 163 SER A C     1 
ATOM   1269 O  O     . SER A 1 163 ? 0.347   17.350  -3.095  1.00 57.78  ? 163 SER A O     1 
ATOM   1270 C  CB    . SER A 1 163 ? -2.428  17.219  -2.129  1.00 47.18  ? 163 SER A CB    1 
ATOM   1271 O  OG    . SER A 1 163 ? -2.040  17.605  -0.822  1.00 50.98  ? 163 SER A OG    1 
ATOM   1272 N  N     . PRO A 1 164 ? 0.125   19.566  -2.815  1.00 54.63  ? 164 PRO A N     1 
ATOM   1273 C  CA    . PRO A 1 164 ? 1.565   19.717  -2.553  1.00 53.70  ? 164 PRO A CA    1 
ATOM   1274 C  C     . PRO A 1 164 ? 2.005   19.060  -1.259  1.00 57.07  ? 164 PRO A C     1 
ATOM   1275 O  O     . PRO A 1 164 ? 3.188   18.721  -1.123  1.00 55.35  ? 164 PRO A O     1 
ATOM   1276 C  CB    . PRO A 1 164 ? 1.756   21.239  -2.508  1.00 50.28  ? 164 PRO A CB    1 
ATOM   1277 C  CG    . PRO A 1 164 ? 0.414   21.774  -2.133  1.00 53.30  ? 164 PRO A CG    1 
ATOM   1278 C  CD    . PRO A 1 164 ? -0.587  20.854  -2.772  1.00 52.17  ? 164 PRO A CD    1 
ATOM   1279 N  N     . TYR A 1 165 ? 1.093   18.872  -0.302  1.00 49.49  ? 165 TYR A N     1 
ATOM   1280 C  CA    . TYR A 1 165 ? 1.433   18.137  0.911   1.00 51.96  ? 165 TYR A CA    1 
ATOM   1281 C  C     . TYR A 1 165 ? 1.801   16.693  0.599   1.00 53.40  ? 165 TYR A C     1 
ATOM   1282 O  O     . TYR A 1 165 ? 2.566   16.072  1.345   1.00 61.34  ? 165 TYR A O     1 
ATOM   1283 C  CB    . TYR A 1 165 ? 0.268   18.194  1.899   1.00 48.81  ? 165 TYR A CB    1 
ATOM   1284 C  CG    . TYR A 1 165 ? 0.459   17.346  3.136   1.00 58.62  ? 165 TYR A CG    1 
ATOM   1285 C  CD1   . TYR A 1 165 ? 1.199   17.813  4.214   1.00 54.40  ? 165 TYR A CD1   1 
ATOM   1286 C  CD2   . TYR A 1 165 ? -0.108  16.082  3.229   1.00 60.02  ? 165 TYR A CD2   1 
ATOM   1287 C  CE1   . TYR A 1 165 ? 1.374   17.042  5.348   1.00 53.74  ? 165 TYR A CE1   1 
ATOM   1288 C  CE2   . TYR A 1 165 ? 0.061   15.305  4.358   1.00 58.46  ? 165 TYR A CE2   1 
ATOM   1289 C  CZ    . TYR A 1 165 ? 0.802   15.789  5.415   1.00 55.04  ? 165 TYR A CZ    1 
ATOM   1290 O  OH    . TYR A 1 165 ? 0.972   15.017  6.542   1.00 47.39  ? 165 TYR A OH    1 
ATOM   1291 N  N     . VAL A 1 166 ? 1.267   16.143  -0.492  1.00 55.89  ? 166 VAL A N     1 
ATOM   1292 C  CA    . VAL A 1 166 ? 1.638   14.795  -0.905  1.00 50.41  ? 166 VAL A CA    1 
ATOM   1293 C  C     . VAL A 1 166 ? 2.987   14.801  -1.613  1.00 46.92  ? 166 VAL A C     1 
ATOM   1294 O  O     . VAL A 1 166 ? 3.804   13.894  -1.423  1.00 59.90  ? 166 VAL A O     1 
ATOM   1295 C  CB    . VAL A 1 166 ? 0.537   14.189  -1.795  1.00 52.73  ? 166 VAL A CB    1 
ATOM   1296 C  CG1   . VAL A 1 166 ? 0.954   12.815  -2.296  1.00 50.46  ? 166 VAL A CG1   1 
ATOM   1297 C  CG2   . VAL A 1 166 ? -0.777  14.110  -1.034  1.00 51.97  ? 166 VAL A CG2   1 
ATOM   1298 N  N     . VAL A 1 167 ? 3.242   15.821  -2.436  1.00 51.36  ? 167 VAL A N     1 
ATOM   1299 C  CA    . VAL A 1 167 ? 4.507   15.891  -3.162  1.00 52.83  ? 167 VAL A CA    1 
ATOM   1300 C  C     . VAL A 1 167 ? 5.672   16.023  -2.190  1.00 50.16  ? 167 VAL A C     1 
ATOM   1301 O  O     . VAL A 1 167 ? 6.721   15.390  -2.365  1.00 45.18  ? 167 VAL A O     1 
ATOM   1302 C  CB    . VAL A 1 167 ? 4.478   17.052  -4.173  1.00 53.35  ? 167 VAL A CB    1 
ATOM   1303 C  CG1   . VAL A 1 167 ? 5.737   17.044  -5.026  1.00 45.65  ? 167 VAL A CG1   1 
ATOM   1304 C  CG2   . VAL A 1 167 ? 3.231   16.971  -5.041  1.00 55.90  ? 167 VAL A CG2   1 
ATOM   1305 N  N     . ALA A 1 168 ? 5.510   16.845  -1.152  1.00 56.06  ? 168 ALA A N     1 
ATOM   1306 C  CA    . ALA A 1 168 ? 6.584   17.026  -0.181  1.00 46.84  ? 168 ALA A CA    1 
ATOM   1307 C  C     . ALA A 1 168 ? 6.858   15.740  0.588   1.00 51.71  ? 168 ALA A C     1 
ATOM   1308 O  O     . ALA A 1 168 ? 8.019   15.400  0.845   1.00 44.43  ? 168 ALA A O     1 
ATOM   1309 C  CB    . ALA A 1 168 ? 6.238   18.164  0.778   1.00 46.85  ? 168 ALA A CB    1 
ATOM   1310 N  N     . SER A 1 169 ? 5.805   15.011  0.962   1.00 51.79  ? 169 SER A N     1 
ATOM   1311 C  CA    . SER A 1 169 ? 5.994   13.771  1.709   1.00 45.92  ? 169 SER A CA    1 
ATOM   1312 C  C     . SER A 1 169 ? 6.573   12.674  0.825   1.00 48.86  ? 169 SER A C     1 
ATOM   1313 O  O     . SER A 1 169 ? 7.468   11.934  1.251   1.00 42.35  ? 169 SER A O     1 
ATOM   1314 C  CB    . SER A 1 169 ? 4.671   13.322  2.326   1.00 39.70  ? 169 SER A CB    1 
ATOM   1315 O  OG    . SER A 1 169 ? 4.197   14.272  3.263   1.00 47.82  ? 169 SER A OG    1 
ATOM   1316 N  N     . MET A 1 170 ? 6.074   12.550  -0.408  1.00 46.27  ? 170 MET A N     1 
ATOM   1317 C  CA    . MET A 1 170 ? 6.592   11.530  -1.314  1.00 43.28  ? 170 MET A CA    1 
ATOM   1318 C  C     . MET A 1 170 ? 8.086   11.700  -1.554  1.00 40.13  ? 170 MET A C     1 
ATOM   1319 O  O     . MET A 1 170 ? 8.790   10.715  -1.807  1.00 42.05  ? 170 MET A O     1 
ATOM   1320 C  CB    . MET A 1 170 ? 5.830   11.565  -2.638  1.00 38.00  ? 170 MET A CB    1 
ATOM   1321 C  CG    . MET A 1 170 ? 4.391   11.085  -2.534  1.00 54.59  ? 170 MET A CG    1 
ATOM   1322 S  SD    . MET A 1 170 ? 4.265   9.319   -2.186  1.00 46.85  ? 170 MET A SD    1 
ATOM   1323 C  CE    . MET A 1 170 ? 4.934   8.630   -3.697  1.00 37.84  ? 170 MET A CE    1 
ATOM   1324 N  N     . ARG A 1 171 ? 8.588   12.934  -1.486  1.00 50.99  ? 171 ARG A N     1 
ATOM   1325 C  CA    . ARG A 1 171 ? 10.025  13.148  -1.612  1.00 44.19  ? 171 ARG A CA    1 
ATOM   1326 C  C     . ARG A 1 171 ? 10.776  12.603  -0.405  1.00 41.24  ? 171 ARG A C     1 
ATOM   1327 O  O     . ARG A 1 171 ? 11.944  12.215  -0.525  1.00 47.85  ? 171 ARG A O     1 
ATOM   1328 C  CB    . ARG A 1 171 ? 10.322  14.637  -1.795  1.00 47.59  ? 171 ARG A CB    1 
ATOM   1329 C  CG    . ARG A 1 171 ? 11.790  14.956  -2.029  1.00 56.69  ? 171 ARG A CG    1 
ATOM   1330 C  CD    . ARG A 1 171 ? 12.008  16.447  -2.239  1.00 55.47  ? 171 ARG A CD    1 
ATOM   1331 N  NE    . ARG A 1 171 ? 13.393  16.757  -2.574  1.00 56.40  ? 171 ARG A NE    1 
ATOM   1332 C  CZ    . ARG A 1 171 ? 14.329  17.067  -1.687  1.00 64.23  ? 171 ARG A CZ    1 
ATOM   1333 N  NH1   . ARG A 1 171 ? 14.064  17.121  -0.392  1.00 61.30  ? 171 ARG A NH1   1 
ATOM   1334 N  NH2   . ARG A 1 171 ? 15.562  17.331  -2.110  1.00 64.64  ? 171 ARG A NH2   1 
ATOM   1335 N  N     . ILE A 1 172 ? 10.125  12.557  0.757   1.00 42.31  ? 172 ILE A N     1 
ATOM   1336 C  CA    . ILE A 1 172 ? 10.780  12.063  1.963   1.00 43.29  ? 172 ILE A CA    1 
ATOM   1337 C  C     . ILE A 1 172 ? 10.714  10.542  2.035   1.00 43.84  ? 172 ILE A C     1 
ATOM   1338 O  O     . ILE A 1 172 ? 11.683  9.886   2.431   1.00 42.97  ? 172 ILE A O     1 
ATOM   1339 C  CB    . ILE A 1 172 ? 10.154  12.714  3.209   1.00 40.54  ? 172 ILE A CB    1 
ATOM   1340 C  CG1   . ILE A 1 172 ? 10.339  14.233  3.174   1.00 33.43  ? 172 ILE A CG1   1 
ATOM   1341 C  CG2   . ILE A 1 172 ? 10.755  12.129  4.479   1.00 39.37  ? 172 ILE A CG2   1 
ATOM   1342 C  CD1   . ILE A 1 172 ? 9.764   14.948  4.379   1.00 30.25  ? 172 ILE A CD1   1 
ATOM   1343 N  N     . MET A 1 173 ? 9.578   9.956   1.652   1.00 39.38  ? 173 MET A N     1 
ATOM   1344 C  CA    . MET A 1 173 ? 9.353   8.530   1.854   1.00 40.49  ? 173 MET A CA    1 
ATOM   1345 C  C     . MET A 1 173 ? 9.854   7.661   0.710   1.00 36.20  ? 173 MET A C     1 
ATOM   1346 O  O     . MET A 1 173 ? 10.057  6.459   0.913   1.00 35.60  ? 173 MET A O     1 
ATOM   1347 C  CB    . MET A 1 173 ? 7.862   8.255   2.072   1.00 38.12  ? 173 MET A CB    1 
ATOM   1348 C  CG    . MET A 1 173 ? 7.309   8.828   3.364   1.00 41.50  ? 173 MET A CG    1 
ATOM   1349 S  SD    . MET A 1 173 ? 8.126   8.159   4.825   1.00 41.51  ? 173 MET A SD    1 
ATOM   1350 C  CE    . MET A 1 173 ? 7.769   6.412   4.651   1.00 51.49  ? 173 MET A CE    1 
ATOM   1351 N  N     . THR A 1 174 ? 10.062  8.227   -0.476  1.00 36.32  ? 174 THR A N     1 
ATOM   1352 C  CA    . THR A 1 174 ? 10.476  7.453   -1.640  1.00 35.87  ? 174 THR A CA    1 
ATOM   1353 C  C     . THR A 1 174 ? 11.666  8.123   -2.317  1.00 44.02  ? 174 THR A C     1 
ATOM   1354 O  O     . THR A 1 174 ? 12.182  9.144   -1.856  1.00 46.49  ? 174 THR A O     1 
ATOM   1355 C  CB    . THR A 1 174 ? 9.323   7.291   -2.638  1.00 52.38  ? 174 THR A CB    1 
ATOM   1356 O  OG1   . THR A 1 174 ? 9.005   8.566   -3.212  1.00 44.97  ? 174 THR A OG1   1 
ATOM   1357 C  CG2   . THR A 1 174 ? 8.087   6.729   -1.944  1.00 39.77  ? 174 THR A CG2   1 
ATOM   1358 N  N     . ARG A 1 175 ? 12.107  7.523   -3.423  1.00 49.26  ? 175 ARG A N     1 
ATOM   1359 C  CA    . ARG A 1 175 ? 13.134  8.095   -4.291  1.00 50.47  ? 175 ARG A CA    1 
ATOM   1360 C  C     . ARG A 1 175 ? 12.423  8.678   -5.507  1.00 57.43  ? 175 ARG A C     1 
ATOM   1361 O  O     . ARG A 1 175 ? 12.062  7.952   -6.437  1.00 54.96  ? 175 ARG A O     1 
ATOM   1362 C  CB    . ARG A 1 175 ? 14.165  7.047   -4.699  1.00 49.65  ? 175 ARG A CB    1 
ATOM   1363 C  CG    . ARG A 1 175 ? 15.122  6.618   -3.598  1.00 52.43  ? 175 ARG A CG    1 
ATOM   1364 C  CD    . ARG A 1 175 ? 14.581  5.448   -2.793  1.00 56.40  ? 175 ARG A CD    1 
ATOM   1365 N  NE    . ARG A 1 175 ? 15.636  4.795   -2.027  1.00 63.11  ? 175 ARG A NE    1 
ATOM   1366 C  CZ    . ARG A 1 175 ? 15.455  3.737   -1.249  1.00 61.62  ? 175 ARG A CZ    1 
ATOM   1367 N  NH1   . ARG A 1 175 ? 14.262  3.185   -1.100  1.00 65.58  ? 175 ARG A NH1   1 
ATOM   1368 N  NH2   . ARG A 1 175 ? 16.497  3.219   -0.604  1.00 59.32  ? 175 ARG A NH2   1 
ATOM   1369 N  N     . MET A 1 176 ? 12.222  9.992   -5.501  1.00 57.89  ? 176 MET A N     1 
ATOM   1370 C  CA    . MET A 1 176 ? 11.481  10.678  -6.549  1.00 57.72  ? 176 MET A CA    1 
ATOM   1371 C  C     . MET A 1 176 ? 12.348  11.763  -7.172  1.00 53.11  ? 176 MET A C     1 
ATOM   1372 O  O     . MET A 1 176 ? 13.106  12.444  -6.474  1.00 63.20  ? 176 MET A O     1 
ATOM   1373 C  CB    . MET A 1 176 ? 10.183  11.284  -5.997  1.00 57.12  ? 176 MET A CB    1 
ATOM   1374 C  CG    . MET A 1 176 ? 9.443   12.186  -6.972  1.00 56.97  ? 176 MET A CG    1 
ATOM   1375 S  SD    . MET A 1 176 ? 9.801   13.932  -6.703  1.00 48.93  ? 176 MET A SD    1 
ATOM   1376 C  CE    . MET A 1 176 ? 9.144   14.160  -5.052  1.00 43.18  ? 176 MET A CE    1 
ATOM   1377 N  N     . GLY A 1 177 ? 12.235  11.916  -8.484  1.00 56.02  ? 177 GLY A N     1 
ATOM   1378 C  CA    . GLY A 1 177 ? 13.002  12.918  -9.191  1.00 49.50  ? 177 GLY A CA    1 
ATOM   1379 C  C     . GLY A 1 177 ? 13.053  12.609  -10.675 1.00 56.02  ? 177 GLY A C     1 
ATOM   1380 O  O     . GLY A 1 177 ? 12.346  11.734  -11.174 1.00 59.40  ? 177 GLY A O     1 
ATOM   1381 N  N     . THR A 1 178 ? 13.915  13.358  -11.368 1.00 59.23  ? 178 THR A N     1 
ATOM   1382 C  CA    . THR A 1 178 ? 14.065  13.172  -12.808 1.00 61.01  ? 178 THR A CA    1 
ATOM   1383 C  C     . THR A 1 178 ? 14.822  11.888  -13.126 1.00 68.59  ? 178 THR A C     1 
ATOM   1384 O  O     . THR A 1 178 ? 14.490  11.188  -14.090 1.00 65.44  ? 178 THR A O     1 
ATOM   1385 C  CB    . THR A 1 178 ? 14.780  14.375  -13.423 1.00 47.88  ? 178 THR A CB    1 
ATOM   1386 O  OG1   . THR A 1 178 ? 13.982  15.552  -13.243 1.00 53.37  ? 178 THR A OG1   1 
ATOM   1387 C  CG2   . THR A 1 178 ? 15.019  14.152  -14.909 1.00 51.79  ? 178 THR A CG2   1 
ATOM   1388 N  N     . SER A 1 179 ? 15.840  11.561  -12.326 1.00 66.72  ? 179 SER A N     1 
ATOM   1389 C  CA    . SER A 1 179 ? 16.635  10.365  -12.581 1.00 68.39  ? 179 SER A CA    1 
ATOM   1390 C  C     . SER A 1 179 ? 15.796  9.095   -12.564 1.00 71.64  ? 179 SER A C     1 
ATOM   1391 O  O     . SER A 1 179 ? 16.235  8.070   -13.097 1.00 77.69  ? 179 SER A O     1 
ATOM   1392 C  CB    . SER A 1 179 ? 17.765  10.262  -11.555 1.00 65.20  ? 179 SER A CB    1 
ATOM   1393 O  OG    . SER A 1 179 ? 17.262  10.335  -10.232 1.00 64.39  ? 179 SER A OG    1 
ATOM   1394 N  N     . VAL A 1 180 ? 14.604  9.134   -11.964 1.00 75.30  ? 180 VAL A N     1 
ATOM   1395 C  CA    . VAL A 1 180 ? 13.742  7.956   -11.966 1.00 70.25  ? 180 VAL A CA    1 
ATOM   1396 C  C     . VAL A 1 180 ? 13.138  7.735   -13.347 1.00 69.38  ? 180 VAL A C     1 
ATOM   1397 O  O     . VAL A 1 180 ? 12.899  6.590   -13.751 1.00 76.38  ? 180 VAL A O     1 
ATOM   1398 C  CB    . VAL A 1 180 ? 12.651  8.088   -10.888 1.00 59.99  ? 180 VAL A CB    1 
ATOM   1399 C  CG1   . VAL A 1 180 ? 11.816  6.819   -10.822 1.00 69.45  ? 180 VAL A CG1   1 
ATOM   1400 C  CG2   . VAL A 1 180 ? 13.276  8.393   -9.536  1.00 62.68  ? 180 VAL A CG2   1 
ATOM   1401 N  N     . LEU A 1 181 ? 12.881  8.812   -14.091 1.00 67.67  ? 181 LEU A N     1 
ATOM   1402 C  CA    . LEU A 1 181 ? 12.344  8.666   -15.440 1.00 72.89  ? 181 LEU A CA    1 
ATOM   1403 C  C     . LEU A 1 181 ? 13.366  8.032   -16.376 1.00 81.44  ? 181 LEU A C     1 
ATOM   1404 O  O     . LEU A 1 181 ? 13.013  7.189   -17.209 1.00 83.16  ? 181 LEU A O     1 
ATOM   1405 C  CB    . LEU A 1 181 ? 11.894  10.024  -15.978 1.00 66.14  ? 181 LEU A CB    1 
ATOM   1406 C  CG    . LEU A 1 181 ? 10.649  10.635  -15.333 1.00 65.74  ? 181 LEU A CG    1 
ATOM   1407 C  CD1   . LEU A 1 181 ? 10.385  12.025  -15.888 1.00 61.46  ? 181 LEU A CD1   1 
ATOM   1408 C  CD2   . LEU A 1 181 ? 9.443   9.733   -15.545 1.00 72.80  ? 181 LEU A CD2   1 
ATOM   1409 N  N     . GLU A 1 182 ? 14.636  8.425   -16.256 1.00 97.03  ? 182 GLU A N     1 
ATOM   1410 C  CA    . GLU A 1 182 ? 15.670  7.841   -17.103 1.00 98.97  ? 182 GLU A CA    1 
ATOM   1411 C  C     . GLU A 1 182 ? 15.846  6.355   -16.826 1.00 96.82  ? 182 GLU A C     1 
ATOM   1412 O  O     . GLU A 1 182 ? 16.167  5.586   -17.740 1.00 102.30 ? 182 GLU A O     1 
ATOM   1413 C  CB    . GLU A 1 182 ? 16.993  8.581   -16.903 1.00 109.61 ? 182 GLU A CB    1 
ATOM   1414 C  CG    . GLU A 1 182 ? 16.921  10.069  -17.199 1.00 113.74 ? 182 GLU A CG    1 
ATOM   1415 C  CD    . GLU A 1 182 ? 18.244  10.774  -16.972 1.00 129.23 ? 182 GLU A CD    1 
ATOM   1416 O  OE1   . GLU A 1 182 ? 19.227  10.094  -16.609 1.00 138.22 ? 182 GLU A OE1   1 
ATOM   1417 O  OE2   . GLU A 1 182 ? 18.300  12.008  -17.155 1.00 133.05 ? 182 GLU A OE2   1 
ATOM   1418 N  N     . ALA A 1 183 ? 15.642  5.930   -15.577 1.00 85.46  ? 183 ALA A N     1 
ATOM   1419 C  CA    . ALA A 1 183 ? 15.781  4.515   -15.249 1.00 78.72  ? 183 ALA A CA    1 
ATOM   1420 C  C     . ALA A 1 183 ? 14.608  3.704   -15.785 1.00 79.05  ? 183 ALA A C     1 
ATOM   1421 O  O     . ALA A 1 183 ? 14.784  2.560   -16.218 1.00 88.14  ? 183 ALA A O     1 
ATOM   1422 C  CB    . ALA A 1 183 ? 15.913  4.338   -13.737 1.00 80.58  ? 183 ALA A CB    1 
ATOM   1423 N  N     . LEU A 1 184 ? 13.404  4.280   -15.765 1.00 80.94  ? 184 LEU A N     1 
ATOM   1424 C  CA    . LEU A 1 184 ? 12.231  3.561   -16.252 1.00 85.49  ? 184 LEU A CA    1 
ATOM   1425 C  C     . LEU A 1 184 ? 12.332  3.289   -17.748 1.00 88.17  ? 184 LEU A C     1 
ATOM   1426 O  O     . LEU A 1 184 ? 12.205  2.141   -18.191 1.00 87.38  ? 184 LEU A O     1 
ATOM   1427 C  CB    . LEU A 1 184 ? 10.962  4.351   -15.932 1.00 81.43  ? 184 LEU A CB    1 
ATOM   1428 C  CG    . LEU A 1 184 ? 9.651   3.760   -16.456 1.00 80.83  ? 184 LEU A CG    1 
ATOM   1429 C  CD1   . LEU A 1 184 ? 9.401   2.386   -15.852 1.00 84.61  ? 184 LEU A CD1   1 
ATOM   1430 C  CD2   . LEU A 1 184 ? 8.485   4.695   -16.176 1.00 67.27  ? 184 LEU A CD2   1 
ATOM   1431 N  N     . GLY A 1 185 ? 12.561  4.332   -18.542 1.00 89.34  ? 185 GLY A N     1 
ATOM   1432 C  CA    . GLY A 1 185 ? 12.635  4.179   -19.981 1.00 95.81  ? 185 GLY A CA    1 
ATOM   1433 C  C     . GLY A 1 185 ? 11.328  3.707   -20.585 1.00 106.75 ? 185 GLY A C     1 
ATOM   1434 O  O     . GLY A 1 185 ? 10.353  4.463   -20.639 1.00 105.32 ? 185 GLY A O     1 
ATOM   1435 N  N     . ASP A 1 186 ? 11.296  2.456   -21.043 1.00 124.17 ? 186 ASP A N     1 
ATOM   1436 C  CA    . ASP A 1 186 ? 10.096  1.857   -21.615 1.00 126.86 ? 186 ASP A CA    1 
ATOM   1437 C  C     . ASP A 1 186 ? 9.626   0.659   -20.796 1.00 121.63 ? 186 ASP A C     1 
ATOM   1438 O  O     . ASP A 1 186 ? 9.004   -0.262  -21.329 1.00 129.25 ? 186 ASP A O     1 
ATOM   1439 C  CB    . ASP A 1 186 ? 10.331  1.455   -23.070 1.00 137.73 ? 186 ASP A CB    1 
ATOM   1440 C  CG    . ASP A 1 186 ? 10.517  2.652   -23.982 1.00 146.36 ? 186 ASP A CG    1 
ATOM   1441 O  OD1   . ASP A 1 186 ? 9.937   3.719   -23.689 1.00 142.11 ? 186 ASP A OD1   1 
ATOM   1442 O  OD2   . ASP A 1 186 ? 11.240  2.525   -24.992 1.00 155.68 ? 186 ASP A OD2   1 
ATOM   1443 N  N     . GLY A 1 187 ? 9.920   0.660   -19.494 1.00 109.59 ? 187 GLY A N     1 
ATOM   1444 C  CA    . GLY A 1 187 ? 9.475   -0.405  -18.622 1.00 106.76 ? 187 GLY A CA    1 
ATOM   1445 C  C     . GLY A 1 187 ? 8.114   -0.127  -18.010 1.00 105.36 ? 187 GLY A C     1 
ATOM   1446 O  O     . GLY A 1 187 ? 7.587   0.983   -18.072 1.00 101.54 ? 187 GLY A O     1 
ATOM   1447 N  N     . GLU A 1 188 ? 7.542   -1.167  -17.411 1.00 114.19 ? 188 GLU A N     1 
ATOM   1448 C  CA    . GLU A 1 188 ? 6.236   -1.039  -16.786 1.00 111.20 ? 188 GLU A CA    1 
ATOM   1449 C  C     . GLU A 1 188 ? 6.315   -0.138  -15.555 1.00 100.92 ? 188 GLU A C     1 
ATOM   1450 O  O     . GLU A 1 188 ? 7.374   0.045   -14.948 1.00 96.57  ? 188 GLU A O     1 
ATOM   1451 C  CB    . GLU A 1 188 ? 5.687   -2.411  -16.397 1.00 115.47 ? 188 GLU A CB    1 
ATOM   1452 C  CG    . GLU A 1 188 ? 5.467   -3.347  -17.573 1.00 127.15 ? 188 GLU A CG    1 
ATOM   1453 C  CD    . GLU A 1 188 ? 4.803   -4.647  -17.166 1.00 142.11 ? 188 GLU A CD    1 
ATOM   1454 O  OE1   . GLU A 1 188 ? 4.455   -4.790  -15.975 1.00 141.81 ? 188 GLU A OE1   1 
ATOM   1455 O  OE2   . GLU A 1 188 ? 4.627   -5.525  -18.036 1.00 148.85 ? 188 GLU A OE2   1 
ATOM   1456 N  N     . PHE A 1 189 ? 5.167   0.430   -15.192 1.00 83.65  ? 189 PHE A N     1 
ATOM   1457 C  CA    . PHE A 1 189 ? 5.077   1.302   -14.031 1.00 78.29  ? 189 PHE A CA    1 
ATOM   1458 C  C     . PHE A 1 189 ? 3.656   1.262   -13.490 1.00 75.66  ? 189 PHE A C     1 
ATOM   1459 O  O     . PHE A 1 189 ? 2.693   1.206   -14.259 1.00 79.72  ? 189 PHE A O     1 
ATOM   1460 C  CB    . PHE A 1 189 ? 5.473   2.743   -14.376 1.00 82.27  ? 189 PHE A CB    1 
ATOM   1461 C  CG    . PHE A 1 189 ? 4.551   3.408   -15.360 1.00 71.37  ? 189 PHE A CG    1 
ATOM   1462 C  CD1   . PHE A 1 189 ? 4.747   3.260   -16.723 1.00 74.28  ? 189 PHE A CD1   1 
ATOM   1463 C  CD2   . PHE A 1 189 ? 3.491   4.186   -14.922 1.00 64.81  ? 189 PHE A CD2   1 
ATOM   1464 C  CE1   . PHE A 1 189 ? 3.901   3.872   -17.630 1.00 75.20  ? 189 PHE A CE1   1 
ATOM   1465 C  CE2   . PHE A 1 189 ? 2.643   4.800   -15.824 1.00 71.04  ? 189 PHE A CE2   1 
ATOM   1466 C  CZ    . PHE A 1 189 ? 2.848   4.643   -17.180 1.00 69.94  ? 189 PHE A CZ    1 
ATOM   1467 N  N     . ILE A 1 190 ? 3.535   1.289   -12.163 1.00 69.71  ? 190 ILE A N     1 
ATOM   1468 C  CA    . ILE A 1 190 ? 2.222   1.297   -11.532 1.00 69.15  ? 190 ILE A CA    1 
ATOM   1469 C  C     . ILE A 1 190 ? 1.594   2.673   -11.702 1.00 70.90  ? 190 ILE A C     1 
ATOM   1470 O  O     . ILE A 1 190 ? 2.229   3.702   -11.437 1.00 72.96  ? 190 ILE A O     1 
ATOM   1471 C  CB    . ILE A 1 190 ? 2.330   0.910   -10.050 1.00 75.62  ? 190 ILE A CB    1 
ATOM   1472 C  CG1   . ILE A 1 190 ? 3.073   -0.420  -9.900  1.00 78.56  ? 190 ILE A CG1   1 
ATOM   1473 C  CG2   . ILE A 1 190 ? 0.948   0.824   -9.422  1.00 75.10  ? 190 ILE A CG2   1 
ATOM   1474 C  CD1   . ILE A 1 190 ? 2.413   -1.575  -10.620 1.00 83.29  ? 190 ILE A CD1   1 
ATOM   1475 N  N     . LYS A 1 191 ? 0.341   2.697   -12.148 1.00 67.56  ? 191 LYS A N     1 
ATOM   1476 C  CA    . LYS A 1 191 ? -0.368  3.942   -12.423 1.00 63.90  ? 191 LYS A CA    1 
ATOM   1477 C  C     . LYS A 1 191 ? -1.121  4.367   -11.167 1.00 60.88  ? 191 LYS A C     1 
ATOM   1478 O  O     . LYS A 1 191 ? -2.077  3.704   -10.753 1.00 64.60  ? 191 LYS A O     1 
ATOM   1479 C  CB    . LYS A 1 191 ? -1.315  3.765   -13.606 1.00 66.76  ? 191 LYS A CB    1 
ATOM   1480 C  CG    . LYS A 1 191 ? -0.631  3.235   -14.857 1.00 68.42  ? 191 LYS A CG    1 
ATOM   1481 C  CD    . LYS A 1 191 ? -1.637  2.870   -15.936 1.00 72.67  ? 191 LYS A CD    1 
ATOM   1482 C  CE    . LYS A 1 191 ? -0.945  2.252   -17.141 1.00 78.78  ? 191 LYS A CE    1 
ATOM   1483 N  NZ    . LYS A 1 191 ? -1.916  1.818   -18.183 1.00 86.42  ? 191 LYS A NZ    1 
ATOM   1484 N  N     . CYS A 1 192 ? -0.691  5.472   -10.564 1.00 55.21  ? 192 CYS A N     1 
ATOM   1485 C  CA    . CYS A 1 192 ? -1.300  6.003   -9.354  1.00 55.86  ? 192 CYS A CA    1 
ATOM   1486 C  C     . CYS A 1 192 ? -2.019  7.308   -9.665  1.00 56.76  ? 192 CYS A C     1 
ATOM   1487 O  O     . CYS A 1 192 ? -1.525  8.130   -10.443 1.00 54.68  ? 192 CYS A O     1 
ATOM   1488 C  CB    . CYS A 1 192 ? -0.248  6.233   -8.265  1.00 59.34  ? 192 CYS A CB    1 
ATOM   1489 S  SG    . CYS A 1 192 ? 0.689   4.757   -7.804  1.00 49.28  ? 192 CYS A SG    1 
ATOM   1490 N  N     . LEU A 1 193 ? -3.187  7.493   -9.052  1.00 56.57  ? 193 LEU A N     1 
ATOM   1491 C  CA    . LEU A 1 193 ? -3.992  8.693   -9.250  1.00 55.25  ? 193 LEU A CA    1 
ATOM   1492 C  C     . LEU A 1 193 ? -4.609  9.090   -7.919  1.00 50.04  ? 193 LEU A C     1 
ATOM   1493 O  O     . LEU A 1 193 ? -5.331  8.297   -7.309  1.00 53.33  ? 193 LEU A O     1 
ATOM   1494 C  CB    . LEU A 1 193 ? -5.083  8.462   -10.301 1.00 54.76  ? 193 LEU A CB    1 
ATOM   1495 C  CG    . LEU A 1 193 ? -6.032  9.635   -10.562 1.00 58.54  ? 193 LEU A CG    1 
ATOM   1496 C  CD1   . LEU A 1 193 ? -5.266  10.844  -11.079 1.00 55.93  ? 193 LEU A CD1   1 
ATOM   1497 C  CD2   . LEU A 1 193 ? -7.132  9.234   -11.534 1.00 69.26  ? 193 LEU A CD2   1 
ATOM   1498 N  N     . HIS A 1 194 ? -4.327  10.312  -7.473  1.00 50.87  ? 194 HIS A N     1 
ATOM   1499 C  CA    . HIS A 1 194 ? -4.850  10.827  -6.217  1.00 53.14  ? 194 HIS A CA    1 
ATOM   1500 C  C     . HIS A 1 194 ? -5.435  12.215  -6.431  1.00 46.12  ? 194 HIS A C     1 
ATOM   1501 O  O     . HIS A 1 194 ? -4.891  13.017  -7.196  1.00 47.44  ? 194 HIS A O     1 
ATOM   1502 C  CB    . HIS A 1 194 ? -3.764  10.885  -5.137  1.00 38.00  ? 194 HIS A CB    1 
ATOM   1503 C  CG    . HIS A 1 194 ? -4.214  11.535  -3.865  1.00 39.80  ? 194 HIS A CG    1 
ATOM   1504 N  ND1   . HIS A 1 194 ? -3.945  12.854  -3.567  1.00 42.47  ? 194 HIS A ND1   1 
ATOM   1505 C  CD2   . HIS A 1 194 ? -4.921  11.049  -2.817  1.00 53.71  ? 194 HIS A CD2   1 
ATOM   1506 C  CE1   . HIS A 1 194 ? -4.463  13.151  -2.389  1.00 52.58  ? 194 HIS A CE1   1 
ATOM   1507 N  NE2   . HIS A 1 194 ? -5.061  12.074  -1.913  1.00 59.69  ? 194 HIS A NE2   1 
ATOM   1508 N  N     . SER A 1 195 ? -6.544  12.491  -5.749  1.00 39.91  ? 195 SER A N     1 
ATOM   1509 C  CA    . SER A 1 195 ? -7.191  13.792  -5.817  1.00 53.13  ? 195 SER A CA    1 
ATOM   1510 C  C     . SER A 1 195 ? -7.926  14.045  -4.510  1.00 56.69  ? 195 SER A C     1 
ATOM   1511 O  O     . SER A 1 195 ? -8.566  13.141  -3.965  1.00 61.74  ? 195 SER A O     1 
ATOM   1512 C  CB    . SER A 1 195 ? -8.162  13.877  -7.000  1.00 55.09  ? 195 SER A CB    1 
ATOM   1513 O  OG    . SER A 1 195 ? -8.751  15.163  -7.084  1.00 59.57  ? 195 SER A OG    1 
ATOM   1514 N  N     . VAL A 1 196 ? -7.828  15.279  -4.011  1.00 57.08  ? 196 VAL A N     1 
ATOM   1515 C  CA    . VAL A 1 196 ? -8.491  15.631  -2.760  1.00 54.00  ? 196 VAL A CA    1 
ATOM   1516 C  C     . VAL A 1 196 ? -9.995  15.799  -2.931  1.00 64.62  ? 196 VAL A C     1 
ATOM   1517 O  O     . VAL A 1 196 ? -10.735 15.719  -1.942  1.00 70.63  ? 196 VAL A O     1 
ATOM   1518 C  CB    . VAL A 1 196 ? -7.889  16.915  -2.166  1.00 66.99  ? 196 VAL A CB    1 
ATOM   1519 C  CG1   . VAL A 1 196 ? -6.406  16.723  -1.882  1.00 43.84  ? 196 VAL A CG1   1 
ATOM   1520 C  CG2   . VAL A 1 196 ? -8.111  18.088  -3.108  1.00 57.90  ? 196 VAL A CG2   1 
ATOM   1521 N  N     . GLY A 1 197 ? -10.468 16.032  -4.152  1.00 58.07  ? 197 GLY A N     1 
ATOM   1522 C  CA    . GLY A 1 197 ? -11.891 16.177  -4.383  1.00 69.02  ? 197 GLY A CA    1 
ATOM   1523 C  C     . GLY A 1 197 ? -12.467 17.521  -4.005  1.00 71.95  ? 197 GLY A C     1 
ATOM   1524 O  O     . GLY A 1 197 ? -13.628 17.594  -3.588  1.00 68.42  ? 197 GLY A O     1 
ATOM   1525 N  N     . CYS A 1 198 ? -11.689 18.594  -4.134  1.00 68.15  ? 198 CYS A N     1 
ATOM   1526 C  CA    . CYS A 1 198 ? -12.144 19.951  -3.835  1.00 70.19  ? 198 CYS A CA    1 
ATOM   1527 C  C     . CYS A 1 198 ? -11.729 20.876  -4.971  1.00 72.84  ? 198 CYS A C     1 
ATOM   1528 O  O     . CYS A 1 198 ? -10.803 21.684  -4.830  1.00 74.64  ? 198 CYS A O     1 
ATOM   1529 C  CB    . CYS A 1 198 ? -11.587 20.439  -2.497  1.00 66.76  ? 198 CYS A CB    1 
ATOM   1530 S  SG    . CYS A 1 198 ? -12.302 19.624  -1.052  1.00 77.10  ? 198 CYS A SG    1 
ATOM   1531 N  N     . PRO A 1 199 ? -12.396 20.781  -6.118  1.00 76.93  ? 199 PRO A N     1 
ATOM   1532 C  CA    . PRO A 1 199 ? -12.073 21.675  -7.233  1.00 83.61  ? 199 PRO A CA    1 
ATOM   1533 C  C     . PRO A 1 199 ? -12.478 23.109  -6.929  1.00 89.34  ? 199 PRO A C     1 
ATOM   1534 O  O     . PRO A 1 199 ? -13.283 23.386  -6.038  1.00 88.40  ? 199 PRO A O     1 
ATOM   1535 C  CB    . PRO A 1 199 ? -12.889 21.102  -8.396  1.00 86.73  ? 199 PRO A CB    1 
ATOM   1536 C  CG    . PRO A 1 199 ? -14.036 20.412  -7.735  1.00 78.99  ? 199 PRO A CG    1 
ATOM   1537 C  CD    . PRO A 1 199 ? -13.490 19.852  -6.449  1.00 76.16  ? 199 PRO A CD    1 
ATOM   1538 N  N     . LEU A 1 200 ? -11.899 24.029  -7.695  1.00 87.92  ? 200 LEU A N     1 
ATOM   1539 C  CA    . LEU A 1 200 ? -12.241 25.429  -7.495  1.00 90.81  ? 200 LEU A CA    1 
ATOM   1540 C  C     . LEU A 1 200 ? -13.293 25.871  -8.505  1.00 99.05  ? 200 LEU A C     1 
ATOM   1541 O  O     . LEU A 1 200 ? -13.248 25.457  -9.669  1.00 104.99 ? 200 LEU A O     1 
ATOM   1542 C  CB    . LEU A 1 200 ? -11.000 26.313  -7.634  1.00 88.01  ? 200 LEU A CB    1 
ATOM   1543 C  CG    . LEU A 1 200 ? -9.777  25.875  -6.823  1.00 81.63  ? 200 LEU A CG    1 
ATOM   1544 C  CD1   . LEU A 1 200 ? -8.641  26.877  -6.970  1.00 82.90  ? 200 LEU A CD1   1 
ATOM   1545 C  CD2   . LEU A 1 200 ? -10.139 25.676  -5.359  1.00 82.43  ? 200 LEU A CD2   1 
ATOM   1546 N  N     . PRO A 1 201 ? -14.254 26.711  -8.100  1.00 97.50  ? 201 PRO A N     1 
ATOM   1547 C  CA    . PRO A 1 201 ? -14.420 27.315  -6.769  1.00 101.79 ? 201 PRO A CA    1 
ATOM   1548 C  C     . PRO A 1 201 ? -14.872 26.307  -5.718  1.00 106.40 ? 201 PRO A C     1 
ATOM   1549 O  O     . PRO A 1 201 ? -15.530 25.319  -6.033  1.00 110.17 ? 201 PRO A O     1 
ATOM   1550 C  CB    . PRO A 1 201 ? -15.480 28.396  -7.019  1.00 101.38 ? 201 PRO A CB    1 
ATOM   1551 C  CG    . PRO A 1 201 ? -16.315 27.832  -8.129  1.00 101.31 ? 201 PRO A CG    1 
ATOM   1552 C  CD    . PRO A 1 201 ? -15.335 27.110  -9.019  1.00 95.37  ? 201 PRO A CD    1 
ATOM   1553 N  N     . LEU A 1 202 ? -14.532 26.543  -4.454  1.00 117.59 ? 202 LEU A N     1 
ATOM   1554 C  CA    . LEU A 1 202 ? -14.878 25.621  -3.382  1.00 126.53 ? 202 LEU A CA    1 
ATOM   1555 C  C     . LEU A 1 202 ? -16.354 25.748  -3.027  1.00 137.22 ? 202 LEU A C     1 
ATOM   1556 O  O     . LEU A 1 202 ? -16.839 26.845  -2.731  1.00 139.82 ? 202 LEU A O     1 
ATOM   1557 C  CB    . LEU A 1 202 ? -14.014 25.890  -2.150  1.00 125.42 ? 202 LEU A CB    1 
ATOM   1558 C  CG    . LEU A 1 202 ? -12.509 25.663  -2.300  1.00 115.91 ? 202 LEU A CG    1 
ATOM   1559 C  CD1   . LEU A 1 202 ? -11.770 26.117  -1.050  1.00 112.01 ? 202 LEU A CD1   1 
ATOM   1560 C  CD2   . LEU A 1 202 ? -12.215 24.200  -2.595  1.00 102.97 ? 202 LEU A CD2   1 
ATOM   1561 N  N     . LYS A 1 203 ? -17.067 24.623  -3.059  1.00 145.75 ? 203 LYS A N     1 
ATOM   1562 C  CA    . LYS A 1 203 ? -18.464 24.592  -2.652  1.00 153.24 ? 203 LYS A CA    1 
ATOM   1563 C  C     . LYS A 1 203 ? -18.639 24.335  -1.163  1.00 157.14 ? 203 LYS A C     1 
ATOM   1564 O  O     . LYS A 1 203 ? -19.710 24.628  -0.618  1.00 158.34 ? 203 LYS A O     1 
ATOM   1565 C  CB    . LYS A 1 203 ? -19.223 23.523  -3.446  1.00 157.15 ? 203 LYS A CB    1 
ATOM   1566 C  CG    . LYS A 1 203 ? -19.165 23.714  -4.953  1.00 157.62 ? 203 LYS A CG    1 
ATOM   1567 C  CD    . LYS A 1 203 ? -19.859 22.577  -5.684  1.00 164.36 ? 203 LYS A CD    1 
ATOM   1568 C  CE    . LYS A 1 203 ? -19.796 22.770  -7.191  1.00 159.51 ? 203 LYS A CE    1 
ATOM   1569 N  NZ    . LYS A 1 203 ? -18.392 22.851  -7.683  1.00 144.06 ? 203 LYS A NZ    1 
ATOM   1570 N  N     . LYS A 1 204 ? -17.619 23.800  -0.497  1.00 156.65 ? 204 LYS A N     1 
ATOM   1571 C  CA    . LYS A 1 204 ? -17.658 23.538  0.937   1.00 147.40 ? 204 LYS A CA    1 
ATOM   1572 C  C     . LYS A 1 204 ? -16.488 24.246  1.606   1.00 139.36 ? 204 LYS A C     1 
ATOM   1573 O  O     . LYS A 1 204 ? -15.332 24.033  1.200   1.00 129.97 ? 204 LYS A O     1 
ATOM   1574 C  CB    . LYS A 1 204 ? -17.599 22.034  1.222   1.00 149.50 ? 204 LYS A CB    1 
ATOM   1575 C  CG    . LYS A 1 204 ? -18.686 21.216  0.548   1.00 154.88 ? 204 LYS A CG    1 
ATOM   1576 C  CD    . LYS A 1 204 ? -18.502 19.734  0.838   1.00 151.67 ? 204 LYS A CD    1 
ATOM   1577 C  CE    . LYS A 1 204 ? -19.550 18.891  0.132   1.00 147.23 ? 204 LYS A CE    1 
ATOM   1578 N  NZ    . LYS A 1 204 ? -19.350 17.439  0.394   1.00 137.82 ? 204 LYS A NZ    1 
ATOM   1579 N  N     . PRO A 1 205 ? -16.721 25.089  2.610   1.00 131.09 ? 205 PRO A N     1 
ATOM   1580 C  CA    . PRO A 1 205 ? -15.596 25.720  3.309   1.00 120.20 ? 205 PRO A CA    1 
ATOM   1581 C  C     . PRO A 1 205 ? -14.673 24.672  3.916   1.00 110.51 ? 205 PRO A C     1 
ATOM   1582 O  O     . PRO A 1 205 ? -15.123 23.690  4.509   1.00 105.91 ? 205 PRO A O     1 
ATOM   1583 C  CB    . PRO A 1 205 ? -16.278 26.568  4.389   1.00 114.79 ? 205 PRO A CB    1 
ATOM   1584 C  CG    . PRO A 1 205 ? -17.650 26.819  3.857   1.00 117.68 ? 205 PRO A CG    1 
ATOM   1585 C  CD    . PRO A 1 205 ? -18.021 25.578  3.098   1.00 127.47 ? 205 PRO A CD    1 
ATOM   1586 N  N     . LEU A 1 206 ? -13.370 24.892  3.760   1.00 106.71 ? 206 LEU A N     1 
ATOM   1587 C  CA    . LEU A 1 206 ? -12.365 23.944  4.220   1.00 96.72  ? 206 LEU A CA    1 
ATOM   1588 C  C     . LEU A 1 206 ? -11.980 24.227  5.666   1.00 91.75  ? 206 LEU A C     1 
ATOM   1589 O  O     . LEU A 1 206 ? -11.892 25.385  6.085   1.00 95.61  ? 206 LEU A O     1 
ATOM   1590 C  CB    . LEU A 1 206 ? -11.123 24.004  3.329   1.00 85.25  ? 206 LEU A CB    1 
ATOM   1591 C  CG    . LEU A 1 206 ? -11.343 23.730  1.839   1.00 78.84  ? 206 LEU A CG    1 
ATOM   1592 C  CD1   . LEU A 1 206 ? -10.034 23.844  1.073   1.00 85.68  ? 206 LEU A CD1   1 
ATOM   1593 C  CD2   . LEU A 1 206 ? -11.973 22.362  1.629   1.00 78.80  ? 206 LEU A CD2   1 
ATOM   1594 N  N     . VAL A 1 207 ? -11.748 23.159  6.423   1.00 91.42  ? 207 VAL A N     1 
ATOM   1595 C  CA    . VAL A 1 207 ? -11.348 23.261  7.822   1.00 91.83  ? 207 VAL A CA    1 
ATOM   1596 C  C     . VAL A 1 207 ? -9.828  23.227  7.900   1.00 92.24  ? 207 VAL A C     1 
ATOM   1597 O  O     . VAL A 1 207 ? -9.190  22.311  7.366   1.00 91.13  ? 207 VAL A O     1 
ATOM   1598 C  CB    . VAL A 1 207 ? -11.970 22.130  8.657   1.00 86.85  ? 207 VAL A CB    1 
ATOM   1599 C  CG1   . VAL A 1 207 ? -11.562 22.261  10.117  1.00 86.30  ? 207 VAL A CG1   1 
ATOM   1600 C  CG2   . VAL A 1 207 ? -13.485 22.137  8.517   1.00 90.01  ? 207 VAL A CG2   1 
ATOM   1601 N  N     . ASN A 1 208 ? -9.246  24.224  8.568   1.00 94.56  ? 208 ASN A N     1 
ATOM   1602 C  CA    . ASN A 1 208 ? -7.793  24.354  8.672   1.00 89.14  ? 208 ASN A CA    1 
ATOM   1603 C  C     . ASN A 1 208 ? -7.132  24.398  7.298   1.00 87.16  ? 208 ASN A C     1 
ATOM   1604 O  O     . ASN A 1 208 ? -5.990  23.964  7.133   1.00 95.66  ? 208 ASN A O     1 
ATOM   1605 C  CB    . ASN A 1 208 ? -7.191  23.226  9.516   1.00 90.93  ? 208 ASN A CB    1 
ATOM   1606 C  CG    . ASN A 1 208 ? -7.142  23.564  10.992  1.00 92.42  ? 208 ASN A CG    1 
ATOM   1607 O  OD1   . ASN A 1 208 ? -6.955  24.721  11.370  1.00 96.78  ? 208 ASN A OD1   1 
ATOM   1608 N  ND2   . ASN A 1 208 ? -7.307  22.553  11.837  1.00 90.95  ? 208 ASN A ND2   1 
ATOM   1609 N  N     . ASN A 1 209 ? -7.845  24.922  6.303   1.00 93.63  ? 209 ASN A N     1 
ATOM   1610 C  CA    . ASN A 1 209 ? -7.363  24.983  4.926   1.00 89.50  ? 209 ASN A CA    1 
ATOM   1611 C  C     . ASN A 1 209 ? -6.996  23.606  4.385   1.00 87.06  ? 209 ASN A C     1 
ATOM   1612 O  O     . ASN A 1 209 ? -6.194  23.494  3.453   1.00 90.68  ? 209 ASN A O     1 
ATOM   1613 C  CB    . ASN A 1 209 ? -6.168  25.934  4.798   1.00 88.73  ? 209 ASN A CB    1 
ATOM   1614 C  CG    . ASN A 1 209 ? -6.520  27.363  5.162   1.00 92.32  ? 209 ASN A CG    1 
ATOM   1615 O  OD1   . ASN A 1 209 ? -7.651  27.806  4.962   1.00 96.78  ? 209 ASN A OD1   1 
ATOM   1616 N  ND2   . ASN A 1 209 ? -5.549  28.093  5.698   1.00 97.68  ? 209 ASN A ND2   1 
ATOM   1617 N  N     . TRP A 1 210 ? -7.573  22.550  4.955   1.00 83.90  ? 210 TRP A N     1 
ATOM   1618 C  CA    . TRP A 1 210 ? -7.278  21.176  4.560   1.00 78.34  ? 210 TRP A CA    1 
ATOM   1619 C  C     . TRP A 1 210 ? -8.368  20.717  3.597   1.00 70.63  ? 210 TRP A C     1 
ATOM   1620 O  O     . TRP A 1 210 ? -9.493  20.423  4.008   1.00 73.00  ? 210 TRP A O     1 
ATOM   1621 C  CB    . TRP A 1 210 ? -7.189  20.268  5.782   1.00 75.45  ? 210 TRP A CB    1 
ATOM   1622 C  CG    . TRP A 1 210 ? -6.654  18.906  5.474   1.00 75.47  ? 210 TRP A CG    1 
ATOM   1623 C  CD1   . TRP A 1 210 ? -7.373  17.759  5.305   1.00 75.92  ? 210 TRP A CD1   1 
ATOM   1624 C  CD2   . TRP A 1 210 ? -5.279  18.548  5.291   1.00 79.75  ? 210 TRP A CD2   1 
ATOM   1625 N  NE1   . TRP A 1 210 ? -6.531  16.708  5.032   1.00 68.67  ? 210 TRP A NE1   1 
ATOM   1626 C  CE2   . TRP A 1 210 ? -5.240  17.167  5.017   1.00 78.87  ? 210 TRP A CE2   1 
ATOM   1627 C  CE3   . TRP A 1 210 ? -4.078  19.262  5.334   1.00 63.90  ? 210 TRP A CE3   1 
ATOM   1628 C  CZ2   . TRP A 1 210 ? -4.047  16.486  4.787   1.00 67.26  ? 210 TRP A CZ2   1 
ATOM   1629 C  CZ3   . TRP A 1 210 ? -2.895  18.585  5.105   1.00 60.99  ? 210 TRP A CZ3   1 
ATOM   1630 C  CH2   . TRP A 1 210 ? -2.888  17.211  4.835   1.00 67.56  ? 210 TRP A CH2   1 
ATOM   1631 N  N     . ALA A 1 211 ? -8.029  20.658  2.312   1.00 67.79  ? 211 ALA A N     1 
ATOM   1632 C  CA    . ALA A 1 211 ? -8.983  20.226  1.298   1.00 64.77  ? 211 ALA A CA    1 
ATOM   1633 C  C     . ALA A 1 211 ? -9.210  18.724  1.406   1.00 73.66  ? 211 ALA A C     1 
ATOM   1634 O  O     . ALA A 1 211 ? -8.259  17.938  1.343   1.00 73.24  ? 211 ALA A O     1 
ATOM   1635 C  CB    . ALA A 1 211 ? -8.477  20.595  -0.094  1.00 55.98  ? 211 ALA A CB    1 
ATOM   1636 N  N     . CYS A 1 212 ? -10.468 18.324  1.571   1.00 68.31  ? 212 CYS A N     1 
ATOM   1637 C  CA    . CYS A 1 212 ? -10.813 16.914  1.687   1.00 69.83  ? 212 CYS A CA    1 
ATOM   1638 C  C     . CYS A 1 212 ? -12.306 16.758  1.441   1.00 69.42  ? 212 CYS A C     1 
ATOM   1639 O  O     . CYS A 1 212 ? -13.055 17.736  1.393   1.00 69.44  ? 212 CYS A O     1 
ATOM   1640 C  CB    . CYS A 1 212 ? -10.418 16.353  3.057   1.00 67.57  ? 212 CYS A CB    1 
ATOM   1641 S  SG    . CYS A 1 212 ? -11.252 17.139  4.456   1.00 74.50  ? 212 CYS A SG    1 
ATOM   1642 N  N     . ASN A 1 213 ? -12.727 15.505  1.283   1.00 69.44  ? 213 ASN A N     1 
ATOM   1643 C  CA    . ASN A 1 213 ? -14.137 15.176  1.063   1.00 79.85  ? 213 ASN A CA    1 
ATOM   1644 C  C     . ASN A 1 213 ? -14.435 13.855  1.752   1.00 77.61  ? 213 ASN A C     1 
ATOM   1645 O  O     . ASN A 1 213 ? -14.407 12.785  1.133   1.00 78.80  ? 213 ASN A O     1 
ATOM   1646 C  CB    . ASN A 1 213 ? -14.464 15.106  -0.429  1.00 81.18  ? 213 ASN A CB    1 
ATOM   1647 C  CG    . ASN A 1 213 ? -15.953 15.158  -0.701  1.00 80.94  ? 213 ASN A CG    1 
ATOM   1648 O  OD1   . ASN A 1 213 ? -16.758 14.671  0.092   1.00 82.43  ? 213 ASN A OD1   1 
ATOM   1649 N  ND2   . ASN A 1 213 ? -16.328 15.758  -1.825  1.00 88.63  ? 213 ASN A ND2   1 
ATOM   1650 N  N     . PRO A 1 214 ? -14.725 13.892  3.055   1.00 83.24  ? 214 PRO A N     1 
ATOM   1651 C  CA    . PRO A 1 214 ? -14.937 12.634  3.790   1.00 82.70  ? 214 PRO A CA    1 
ATOM   1652 C  C     . PRO A 1 214 ? -16.117 11.824  3.284   1.00 88.88  ? 214 PRO A C     1 
ATOM   1653 O  O     . PRO A 1 214 ? -16.078 10.589  3.344   1.00 77.20  ? 214 PRO A O     1 
ATOM   1654 C  CB    . PRO A 1 214 ? -15.157 13.106  5.235   1.00 78.99  ? 214 PRO A CB    1 
ATOM   1655 C  CG    . PRO A 1 214 ? -14.569 14.484  5.289   1.00 87.11  ? 214 PRO A CG    1 
ATOM   1656 C  CD    . PRO A 1 214 ? -14.805 15.069  3.934   1.00 86.93  ? 214 PRO A CD    1 
ATOM   1657 N  N     . GLU A 1 215 ? -17.169 12.479  2.787   1.00 100.44 ? 215 GLU A N     1 
ATOM   1658 C  CA    . GLU A 1 215 ? -18.354 11.745  2.357   1.00 97.40  ? 215 GLU A CA    1 
ATOM   1659 C  C     . GLU A 1 215 ? -18.066 10.851  1.157   1.00 91.01  ? 215 GLU A C     1 
ATOM   1660 O  O     . GLU A 1 215 ? -18.714 9.810   0.994   1.00 89.78  ? 215 GLU A O     1 
ATOM   1661 C  CB    . GLU A 1 215 ? -19.490 12.715  2.028   1.00 99.92  ? 215 GLU A CB    1 
ATOM   1662 C  CG    . GLU A 1 215 ? -19.933 13.592  3.191   1.00 111.79 ? 215 GLU A CG    1 
ATOM   1663 C  CD    . GLU A 1 215 ? -19.033 14.795  3.396   1.00 112.63 ? 215 GLU A CD    1 
ATOM   1664 O  OE1   . GLU A 1 215 ? -18.072 14.962  2.616   1.00 107.38 ? 215 GLU A OE1   1 
ATOM   1665 O  OE2   . GLU A 1 215 ? -19.288 15.577  4.337   1.00 114.28 ? 215 GLU A OE2   1 
ATOM   1666 N  N     . LEU A 1 216 ? -17.106 11.230  0.314   1.00 84.40  ? 216 LEU A N     1 
ATOM   1667 C  CA    . LEU A 1 216 ? -16.821 10.509  -0.921  1.00 77.23  ? 216 LEU A CA    1 
ATOM   1668 C  C     . LEU A 1 216 ? -15.447 9.845   -0.908  1.00 79.57  ? 216 LEU A C     1 
ATOM   1669 O  O     . LEU A 1 216 ? -14.913 9.517   -1.973  1.00 73.28  ? 216 LEU A O     1 
ATOM   1670 C  CB    . LEU A 1 216 ? -16.940 11.452  -2.118  1.00 64.48  ? 216 LEU A CB    1 
ATOM   1671 C  CG    . LEU A 1 216 ? -18.227 12.275  -2.209  1.00 79.36  ? 216 LEU A CG    1 
ATOM   1672 C  CD1   . LEU A 1 216 ? -18.223 13.140  -3.461  1.00 64.96  ? 216 LEU A CD1   1 
ATOM   1673 C  CD2   . LEU A 1 216 ? -19.452 11.375  -2.177  1.00 72.84  ? 216 LEU A CD2   1 
ATOM   1674 N  N     . THR A 1 217 ? -14.866 9.637   0.270   1.00 74.09  ? 217 THR A N     1 
ATOM   1675 C  CA    . THR A 1 217 ? -13.547 9.023   0.354   1.00 73.19  ? 217 THR A CA    1 
ATOM   1676 C  C     . THR A 1 217 ? -13.600 7.582   -0.143  1.00 74.21  ? 217 THR A C     1 
ATOM   1677 O  O     . THR A 1 217 ? -14.448 6.795   0.288   1.00 71.55  ? 217 THR A O     1 
ATOM   1678 C  CB    . THR A 1 217 ? -13.028 9.067   1.790   1.00 80.66  ? 217 THR A CB    1 
ATOM   1679 O  OG1   . THR A 1 217 ? -12.910 10.430  2.216   1.00 75.60  ? 217 THR A OG1   1 
ATOM   1680 C  CG2   . THR A 1 217 ? -11.666 8.394   1.884   1.00 70.72  ? 217 THR A CG2   1 
ATOM   1681 N  N     . LEU A 1 218 ? -12.689 7.239   -1.051  1.00 71.27  ? 218 LEU A N     1 
ATOM   1682 C  CA    . LEU A 1 218 ? -12.630 5.897   -1.616  1.00 72.56  ? 218 LEU A CA    1 
ATOM   1683 C  C     . LEU A 1 218 ? -11.199 5.590   -2.028  1.00 70.91  ? 218 LEU A C     1 
ATOM   1684 O  O     . LEU A 1 218 ? -10.559 6.400   -2.704  1.00 66.78  ? 218 LEU A O     1 
ATOM   1685 C  CB    . LEU A 1 218 ? -13.568 5.761   -2.821  1.00 73.28  ? 218 LEU A CB    1 
ATOM   1686 C  CG    . LEU A 1 218 ? -13.511 4.426   -3.568  1.00 75.65  ? 218 LEU A CG    1 
ATOM   1687 C  CD1   . LEU A 1 218 ? -14.040 3.295   -2.699  1.00 74.29  ? 218 LEU A CD1   1 
ATOM   1688 C  CD2   . LEU A 1 218 ? -14.277 4.505   -4.881  1.00 77.40  ? 218 LEU A CD2   1 
ATOM   1689 N  N     . ILE A 1 219 ? -10.707 4.424   -1.619  1.00 74.24  ? 219 ILE A N     1 
ATOM   1690 C  CA    . ILE A 1 219 ? -9.385  3.936   -2.000  1.00 64.27  ? 219 ILE A CA    1 
ATOM   1691 C  C     . ILE A 1 219 ? -9.587  2.591   -2.681  1.00 64.24  ? 219 ILE A C     1 
ATOM   1692 O  O     . ILE A 1 219 ? -10.016 1.622   -2.041  1.00 72.46  ? 219 ILE A O     1 
ATOM   1693 C  CB    . ILE A 1 219 ? -8.439  3.811   -0.797  1.00 68.07  ? 219 ILE A CB    1 
ATOM   1694 C  CG1   . ILE A 1 219 ? -8.260  5.163   -0.101  1.00 60.21  ? 219 ILE A CG1   1 
ATOM   1695 C  CG2   . ILE A 1 219 ? -7.092  3.257   -1.236  1.00 61.46  ? 219 ILE A CG2   1 
ATOM   1696 C  CD1   . ILE A 1 219 ? -9.409  5.551   0.807   1.00 64.13  ? 219 ILE A CD1   1 
ATOM   1697 N  N     . ALA A 1 220 ? -9.284  2.526   -3.975  1.00 63.52  ? 220 ALA A N     1 
ATOM   1698 C  CA    . ALA A 1 220 ? -9.505  1.331   -4.772  1.00 65.09  ? 220 ALA A CA    1 
ATOM   1699 C  C     . ALA A 1 220 ? -8.184  0.808   -5.320  1.00 61.97  ? 220 ALA A C     1 
ATOM   1700 O  O     . ALA A 1 220 ? -7.244  1.571   -5.557  1.00 61.04  ? 220 ALA A O     1 
ATOM   1701 C  CB    . ALA A 1 220 ? -10.473 1.605   -5.929  1.00 66.83  ? 220 ALA A CB    1 
ATOM   1702 N  N     . HIS A 1 221 ? -8.128  -0.507  -5.521  1.00 61.12  ? 221 HIS A N     1 
ATOM   1703 C  CA    . HIS A 1 221 ? -6.953  -1.176  -6.063  1.00 67.66  ? 221 HIS A CA    1 
ATOM   1704 C  C     . HIS A 1 221 ? -7.381  -2.078  -7.210  1.00 63.22  ? 221 HIS A C     1 
ATOM   1705 O  O     . HIS A 1 221 ? -8.357  -2.824  -7.085  1.00 54.70  ? 221 HIS A O     1 
ATOM   1706 C  CB    . HIS A 1 221 ? -6.232  -1.997  -4.987  1.00 56.16  ? 221 HIS A CB    1 
ATOM   1707 C  CG    . HIS A 1 221 ? -5.783  -1.191  -3.809  1.00 67.55  ? 221 HIS A CG    1 
ATOM   1708 N  ND1   . HIS A 1 221 ? -6.663  -0.657  -2.893  1.00 71.59  ? 221 HIS A ND1   1 
ATOM   1709 C  CD2   . HIS A 1 221 ? -4.545  -0.829  -3.397  1.00 56.55  ? 221 HIS A CD2   1 
ATOM   1710 C  CE1   . HIS A 1 221 ? -5.986  0.000   -1.967  1.00 60.82  ? 221 HIS A CE1   1 
ATOM   1711 N  NE2   . HIS A 1 221 ? -4.699  -0.089  -2.250  1.00 53.44  ? 221 HIS A NE2   1 
ATOM   1712 N  N     . LEU A 1 222 ? -6.652  -2.007  -8.325  1.00 66.05  ? 222 LEU A N     1 
ATOM   1713 C  CA    . LEU A 1 222 ? -6.900  -2.843  -9.499  1.00 67.89  ? 222 LEU A CA    1 
ATOM   1714 C  C     . LEU A 1 222 ? -5.619  -3.594  -9.836  1.00 65.80  ? 222 LEU A C     1 
ATOM   1715 O  O     . LEU A 1 222 ? -4.797  -3.115  -10.634 1.00 65.45  ? 222 LEU A O     1 
ATOM   1716 C  CB    . LEU A 1 222 ? -7.377  -2.008  -10.686 1.00 68.17  ? 222 LEU A CB    1 
ATOM   1717 C  CG    . LEU A 1 222 ? -8.734  -1.312  -10.553 1.00 68.32  ? 222 LEU A CG    1 
ATOM   1718 C  CD1   . LEU A 1 222 ? -8.632  -0.079  -9.665  1.00 72.41  ? 222 LEU A CD1   1 
ATOM   1719 C  CD2   . LEU A 1 222 ? -9.290  -0.952  -11.923 1.00 76.18  ? 222 LEU A CD2   1 
ATOM   1720 N  N     . PRO A 1 223 ? -5.405  -4.775  -9.254  1.00 68.26  ? 223 PRO A N     1 
ATOM   1721 C  CA    . PRO A 1 223 ? -4.175  -5.522  -9.559  1.00 66.34  ? 223 PRO A CA    1 
ATOM   1722 C  C     . PRO A 1 223 ? -4.079  -5.959  -11.008 1.00 85.64  ? 223 PRO A C     1 
ATOM   1723 O  O     . PRO A 1 223 ? -2.971  -6.026  -11.554 1.00 91.82  ? 223 PRO A O     1 
ATOM   1724 C  CB    . PRO A 1 223 ? -4.254  -6.725  -8.607  1.00 74.16  ? 223 PRO A CB    1 
ATOM   1725 C  CG    . PRO A 1 223 ? -5.711  -6.887  -8.325  1.00 79.89  ? 223 PRO A CG    1 
ATOM   1726 C  CD    . PRO A 1 223 ? -6.277  -5.497  -8.311  1.00 74.15  ? 223 PRO A CD    1 
ATOM   1727 N  N     . ASP A 1 224 ? -5.209  -6.257  -11.654 1.00 95.93  ? 224 ASP A N     1 
ATOM   1728 C  CA    . ASP A 1 224 ? -5.169  -6.702  -13.042 1.00 102.64 ? 224 ASP A CA    1 
ATOM   1729 C  C     . ASP A 1 224 ? -4.670  -5.605  -13.973 1.00 100.63 ? 224 ASP A C     1 
ATOM   1730 O  O     . ASP A 1 224 ? -4.069  -5.902  -15.012 1.00 102.39 ? 224 ASP A O     1 
ATOM   1731 C  CB    . ASP A 1 224 ? -6.553  -7.181  -13.480 1.00 110.91 ? 224 ASP A CB    1 
ATOM   1732 C  CG    . ASP A 1 224 ? -7.099  -8.276  -12.585 1.00 112.25 ? 224 ASP A CG    1 
ATOM   1733 O  OD1   . ASP A 1 224 ? -6.290  -8.995  -11.962 1.00 110.48 ? 224 ASP A OD1   1 
ATOM   1734 O  OD2   . ASP A 1 224 ? -8.338  -8.418  -12.504 1.00 111.91 ? 224 ASP A OD2   1 
ATOM   1735 N  N     . ARG A 1 225 ? -4.907  -4.341  -13.625 1.00 88.21  ? 225 ARG A N     1 
ATOM   1736 C  CA    . ARG A 1 225 ? -4.469  -3.215  -14.437 1.00 86.25  ? 225 ARG A CA    1 
ATOM   1737 C  C     . ARG A 1 225 ? -3.194  -2.561  -13.922 1.00 82.17  ? 225 ARG A C     1 
ATOM   1738 O  O     . ARG A 1 225 ? -2.670  -1.660  -14.586 1.00 83.68  ? 225 ARG A O     1 
ATOM   1739 C  CB    . ARG A 1 225 ? -5.574  -2.154  -14.518 1.00 88.51  ? 225 ARG A CB    1 
ATOM   1740 C  CG    . ARG A 1 225 ? -6.849  -2.615  -15.200 1.00 95.11  ? 225 ARG A CG    1 
ATOM   1741 C  CD    . ARG A 1 225 ? -7.837  -1.466  -15.312 1.00 99.80  ? 225 ARG A CD    1 
ATOM   1742 N  NE    . ARG A 1 225 ? -9.088  -1.868  -15.942 1.00 112.15 ? 225 ARG A NE    1 
ATOM   1743 C  CZ    . ARG A 1 225 ? -10.098 -1.044  -16.190 1.00 127.97 ? 225 ARG A CZ    1 
ATOM   1744 N  NH1   . ARG A 1 225 ? -10.034 0.240   -15.878 1.00 126.61 ? 225 ARG A NH1   1 
ATOM   1745 N  NH2   . ARG A 1 225 ? -11.197 -1.520  -16.766 1.00 142.72 ? 225 ARG A NH2   1 
ATOM   1746 N  N     . ARG A 1 226 ? -2.685  -2.984  -12.766 1.00 80.03  ? 226 ARG A N     1 
ATOM   1747 C  CA    . ARG A 1 226 ? -1.508  -2.360  -12.166 1.00 73.76  ? 226 ARG A CA    1 
ATOM   1748 C  C     . ARG A 1 226 ? -1.776  -0.891  -11.846 1.00 69.44  ? 226 ARG A C     1 
ATOM   1749 O  O     . ARG A 1 226 ? -0.937  -0.021  -12.084 1.00 72.45  ? 226 ARG A O     1 
ATOM   1750 C  CB    . ARG A 1 226 ? -0.284  -2.499  -13.075 1.00 79.33  ? 226 ARG A CB    1 
ATOM   1751 C  CG    . ARG A 1 226 ? 0.063   -3.927  -13.464 1.00 86.96  ? 226 ARG A CG    1 
ATOM   1752 C  CD    . ARG A 1 226 ? 0.446   -4.761  -12.253 1.00 98.33  ? 226 ARG A CD    1 
ATOM   1753 N  NE    . ARG A 1 226 ? 1.161   -5.974  -12.633 1.00 104.38 ? 226 ARG A NE    1 
ATOM   1754 C  CZ    . ARG A 1 226 ? 0.579   -7.127  -12.935 1.00 100.29 ? 226 ARG A CZ    1 
ATOM   1755 N  NH1   . ARG A 1 226 ? -0.736  -7.265  -12.910 1.00 105.80 ? 226 ARG A NH1   1 
ATOM   1756 N  NH2   . ARG A 1 226 ? 1.337   -8.167  -13.273 1.00 109.85 ? 226 ARG A NH2   1 
ATOM   1757 N  N     . GLU A 1 227 ? -2.960  -0.611  -11.303 1.00 65.59  ? 227 GLU A N     1 
ATOM   1758 C  CA    . GLU A 1 227 ? -3.397  0.753   -11.047 1.00 61.67  ? 227 GLU A CA    1 
ATOM   1759 C  C     . GLU A 1 227 ? -3.846  0.901   -9.600  1.00 59.78  ? 227 GLU A C     1 
ATOM   1760 O  O     . GLU A 1 227 ? -4.300  -0.057  -8.970  1.00 57.31  ? 227 GLU A O     1 
ATOM   1761 C  CB    . GLU A 1 227 ? -4.543  1.161   -11.984 1.00 69.45  ? 227 GLU A CB    1 
ATOM   1762 C  CG    . GLU A 1 227 ? -4.198  1.093   -13.463 1.00 74.74  ? 227 GLU A CG    1 
ATOM   1763 C  CD    . GLU A 1 227 ? -5.377  1.441   -14.350 1.00 77.80  ? 227 GLU A CD    1 
ATOM   1764 O  OE1   . GLU A 1 227 ? -6.492  1.621   -13.817 1.00 70.60  ? 227 GLU A OE1   1 
ATOM   1765 O  OE2   . GLU A 1 227 ? -5.189  1.534   -15.581 1.00 80.91  ? 227 GLU A OE2   1 
ATOM   1766 N  N     . ILE A 1 228 ? -3.714  2.121   -9.085  1.00 63.35  ? 228 ILE A N     1 
ATOM   1767 C  CA    . ILE A 1 228 ? -4.164  2.476   -7.743  1.00 63.12  ? 228 ILE A CA    1 
ATOM   1768 C  C     . ILE A 1 228 ? -4.876  3.817   -7.829  1.00 63.11  ? 228 ILE A C     1 
ATOM   1769 O  O     . ILE A 1 228 ? -4.320  4.787   -8.355  1.00 52.06  ? 228 ILE A O     1 
ATOM   1770 C  CB    . ILE A 1 228 ? -2.997  2.546   -6.739  1.00 53.29  ? 228 ILE A CB    1 
ATOM   1771 C  CG1   . ILE A 1 228 ? -2.241  1.217   -6.705  1.00 62.06  ? 228 ILE A CG1   1 
ATOM   1772 C  CG2   . ILE A 1 228 ? -3.509  2.906   -5.353  1.00 52.56  ? 228 ILE A CG2   1 
ATOM   1773 C  CD1   . ILE A 1 228 ? -1.064  1.208   -5.754  1.00 63.28  ? 228 ILE A CD1   1 
ATOM   1774 N  N     . ILE A 1 229 ? -6.104  3.876   -7.316  1.00 63.29  ? 229 ILE A N     1 
ATOM   1775 C  CA    . ILE A 1 229 ? -6.940  5.067   -7.412  1.00 61.39  ? 229 ILE A CA    1 
ATOM   1776 C  C     . ILE A 1 229 ? -7.461  5.408   -6.024  1.00 65.68  ? 229 ILE A C     1 
ATOM   1777 O  O     . ILE A 1 229 ? -8.173  4.604   -5.409  1.00 67.27  ? 229 ILE A O     1 
ATOM   1778 C  CB    . ILE A 1 229 ? -8.108  4.872   -8.394  1.00 70.40  ? 229 ILE A CB    1 
ATOM   1779 C  CG1   . ILE A 1 229 ? -7.578  4.631   -9.809  1.00 65.29  ? 229 ILE A CG1   1 
ATOM   1780 C  CG2   . ILE A 1 229 ? -9.035  6.075   -8.362  1.00 70.85  ? 229 ILE A CG2   1 
ATOM   1781 C  CD1   . ILE A 1 229 ? -8.663  4.410   -10.838 1.00 75.95  ? 229 ILE A CD1   1 
ATOM   1782 N  N     . SER A 1 230 ? -7.112  6.594   -5.534  1.00 75.54  ? 230 SER A N     1 
ATOM   1783 C  CA    . SER A 1 230 ? -7.592  7.102   -4.258  1.00 71.24  ? 230 SER A CA    1 
ATOM   1784 C  C     . SER A 1 230 ? -8.252  8.457   -4.470  1.00 51.77  ? 230 SER A C     1 
ATOM   1785 O  O     . SER A 1 230 ? -7.879  9.212   -5.373  1.00 52.32  ? 230 SER A O     1 
ATOM   1786 C  CB    . SER A 1 230 ? -6.453  7.230   -3.238  1.00 62.22  ? 230 SER A CB    1 
ATOM   1787 O  OG    . SER A 1 230 ? -6.922  7.777   -2.017  1.00 64.77  ? 230 SER A OG    1 
ATOM   1788 N  N     . PHE A 1 231 ? -9.236  8.763   -3.627  1.00 59.04  ? 231 PHE A N     1 
ATOM   1789 C  CA    . PHE A 1 231 ? -9.997  9.996   -3.764  1.00 64.11  ? 231 PHE A CA    1 
ATOM   1790 C  C     . PHE A 1 231 ? -10.570 10.395  -2.413  1.00 64.35  ? 231 PHE A C     1 
ATOM   1791 O  O     . PHE A 1 231 ? -10.972 9.537   -1.622  1.00 62.71  ? 231 PHE A O     1 
ATOM   1792 C  CB    . PHE A 1 231 ? -11.125 9.839   -4.791  1.00 62.56  ? 231 PHE A CB    1 
ATOM   1793 C  CG    . PHE A 1 231 ? -11.972 11.070  -4.957  1.00 67.31  ? 231 PHE A CG    1 
ATOM   1794 C  CD1   . PHE A 1 231 ? -13.087 11.273  -4.162  1.00 69.53  ? 231 PHE A CD1   1 
ATOM   1795 C  CD2   . PHE A 1 231 ? -11.654 12.021  -5.912  1.00 74.98  ? 231 PHE A CD2   1 
ATOM   1796 C  CE1   . PHE A 1 231 ? -13.867 12.404  -4.312  1.00 67.31  ? 231 PHE A CE1   1 
ATOM   1797 C  CE2   . PHE A 1 231 ? -12.431 13.154  -6.067  1.00 67.70  ? 231 PHE A CE2   1 
ATOM   1798 C  CZ    . PHE A 1 231 ? -13.539 13.344  -5.266  1.00 62.94  ? 231 PHE A CZ    1 
ATOM   1799 N  N     . GLY A 1 232 ? -10.606 11.702  -2.159  1.00 61.32  ? 232 GLY A N     1 
ATOM   1800 C  CA    . GLY A 1 232 ? -11.236 12.227  -0.964  1.00 68.68  ? 232 GLY A CA    1 
ATOM   1801 C  C     . GLY A 1 232 ? -10.284 12.505  0.180   1.00 72.97  ? 232 GLY A C     1 
ATOM   1802 O  O     . GLY A 1 232 ? -10.268 13.613  0.727   1.00 76.13  ? 232 GLY A O     1 
ATOM   1803 N  N     . SER A 1 233 ? -9.487  11.510  0.554   1.00 78.63  ? 233 SER A N     1 
ATOM   1804 C  CA    . SER A 1 233 ? -8.599  11.621  1.700   1.00 70.91  ? 233 SER A CA    1 
ATOM   1805 C  C     . SER A 1 233 ? -7.284  12.280  1.285   1.00 69.69  ? 233 SER A C     1 
ATOM   1806 O  O     . SER A 1 233 ? -7.122  12.748  0.155   1.00 68.53  ? 233 SER A O     1 
ATOM   1807 C  CB    . SER A 1 233 ? -8.371  10.246  2.323   1.00 69.16  ? 233 SER A CB    1 
ATOM   1808 O  OG    . SER A 1 233 ? -7.495  10.327  3.434   1.00 74.73  ? 233 SER A OG    1 
ATOM   1809 N  N     . GLY A 1 234 ? -6.329  12.320  2.209   1.00 79.48  ? 234 GLY A N     1 
ATOM   1810 C  CA    . GLY A 1 234 ? -5.029  12.906  1.951   1.00 81.58  ? 234 GLY A CA    1 
ATOM   1811 C  C     . GLY A 1 234 ? -4.111  12.797  3.151   1.00 82.90  ? 234 GLY A C     1 
ATOM   1812 O  O     . GLY A 1 234 ? -3.283  13.679  3.393   1.00 84.14  ? 234 GLY A O     1 
ATOM   1813 N  N     A TYR A 1 235 ? -4.227  11.698  3.896   0.66 94.15  ? 235 TYR A N     1 
ATOM   1814 N  N     B TYR A 1 235 ? -4.278  11.729  3.925   0.34 92.02  ? 235 TYR A N     1 
ATOM   1815 C  CA    A TYR A 1 235 ? -3.465  11.492  5.124   0.66 96.23  ? 235 TYR A CA    1 
ATOM   1816 C  CA    B TYR A 1 235 ? -3.465  11.468  5.104   0.34 94.20  ? 235 TYR A CA    1 
ATOM   1817 C  C     A TYR A 1 235 ? -2.763  10.142  5.057   0.66 91.20  ? 235 TYR A C     1 
ATOM   1818 C  C     B TYR A 1 235 ? -2.738  10.146  4.929   0.34 91.14  ? 235 TYR A C     1 
ATOM   1819 O  O     A TYR A 1 235 ? -3.417  9.110   4.873   0.66 89.73  ? 235 TYR A O     1 
ATOM   1820 O  O     B TYR A 1 235 ? -3.350  9.142   4.550   0.34 89.36  ? 235 TYR A O     1 
ATOM   1821 C  CB    A TYR A 1 235 ? -4.381  11.564  6.350   0.66 92.29  ? 235 TYR A CB    1 
ATOM   1822 C  CB    B TYR A 1 235 ? -4.315  11.425  6.376   0.34 92.35  ? 235 TYR A CB    1 
ATOM   1823 C  CG    A TYR A 1 235 ? -3.653  11.682  7.670   0.66 90.94  ? 235 TYR A CG    1 
ATOM   1824 C  CG    B TYR A 1 235 ? -3.729  10.529  7.444   0.34 92.33  ? 235 TYR A CG    1 
ATOM   1825 C  CD1   A TYR A 1 235 ? -3.191  10.554  8.335   0.66 91.02  ? 235 TYR A CD1   1 
ATOM   1826 C  CD1   B TYR A 1 235 ? -2.713  10.979  8.276   0.34 90.40  ? 235 TYR A CD1   1 
ATOM   1827 C  CD2   A TYR A 1 235 ? -3.439  12.922  8.258   0.66 88.22  ? 235 TYR A CD2   1 
ATOM   1828 C  CD2   B TYR A 1 235 ? -4.184  9.226   7.612   0.34 90.45  ? 235 TYR A CD2   1 
ATOM   1829 C  CE1   A TYR A 1 235 ? -2.529  10.658  9.544   0.66 90.63  ? 235 TYR A CE1   1 
ATOM   1830 C  CE1   B TYR A 1 235 ? -2.170  10.160  9.248   0.34 90.28  ? 235 TYR A CE1   1 
ATOM   1831 C  CE2   A TYR A 1 235 ? -2.778  13.036  9.466   0.66 89.36  ? 235 TYR A CE2   1 
ATOM   1832 C  CE2   B TYR A 1 235 ? -3.647  8.401   8.581   0.34 87.90  ? 235 TYR A CE2   1 
ATOM   1833 C  CZ    A TYR A 1 235 ? -2.326  11.902  10.105  0.66 87.94  ? 235 TYR A CZ    1 
ATOM   1834 C  CZ    B TYR A 1 235 ? -2.641  8.873   9.396   0.34 87.98  ? 235 TYR A CZ    1 
ATOM   1835 O  OH    A TYR A 1 235 ? -1.668  12.011  11.308  0.66 83.84  ? 235 TYR A OH    1 
ATOM   1836 O  OH    B TYR A 1 235 ? -2.105  8.053   10.363  0.34 88.83  ? 235 TYR A OH    1 
ATOM   1837 N  N     . GLY A 1 236 ? -1.438  10.153  5.211   1.00 98.54  ? 236 GLY A N     1 
ATOM   1838 C  CA    . GLY A 1 236 ? -0.640  8.940   5.228   1.00 87.77  ? 236 GLY A CA    1 
ATOM   1839 C  C     . GLY A 1 236 ? -0.933  7.922   4.146   1.00 82.76  ? 236 GLY A C     1 
ATOM   1840 O  O     . GLY A 1 236 ? -0.797  8.210   2.953   1.00 77.03  ? 236 GLY A O     1 
ATOM   1841 N  N     . GLY A 1 237 ? -1.338  6.721   4.559   1.00 83.96  ? 237 GLY A N     1 
ATOM   1842 C  CA    . GLY A 1 237 ? -1.580  5.629   3.632   1.00 83.91  ? 237 GLY A CA    1 
ATOM   1843 C  C     . GLY A 1 237 ? -2.649  5.905   2.594   1.00 89.59  ? 237 GLY A C     1 
ATOM   1844 O  O     . GLY A 1 237 ? -2.732  5.164   1.608   1.00 92.94  ? 237 GLY A O     1 
ATOM   1845 N  N     . ASN A 1 238 ? -3.467  6.941   2.787   1.00 83.28  ? 238 ASN A N     1 
ATOM   1846 C  CA    . ASN A 1 238 ? -4.499  7.252   1.803   1.00 80.86  ? 238 ASN A CA    1 
ATOM   1847 C  C     . ASN A 1 238 ? -3.930  8.027   0.620   1.00 79.25  ? 238 ASN A C     1 
ATOM   1848 O  O     . ASN A 1 238 ? -4.310  7.776   -0.529  1.00 72.89  ? 238 ASN A O     1 
ATOM   1849 C  CB    . ASN A 1 238 ? -5.635  8.040   2.456   1.00 81.18  ? 238 ASN A CB    1 
ATOM   1850 C  CG    . ASN A 1 238 ? -6.292  7.283   3.594   1.00 80.08  ? 238 ASN A CG    1 
ATOM   1851 O  OD1   . ASN A 1 238 ? -6.697  7.875   4.594   1.00 78.90  ? 238 ASN A OD1   1 
ATOM   1852 N  ND2   . ASN A 1 238 ? -6.397  5.967   3.449   1.00 77.07  ? 238 ASN A ND2   1 
ATOM   1853 N  N     . SER A 1 239 ? -3.024  8.968   0.880   1.00 76.72  ? 239 SER A N     1 
ATOM   1854 C  CA    . SER A 1 239 ? -2.436  9.800   -0.163  1.00 68.14  ? 239 SER A CA    1 
ATOM   1855 C  C     . SER A 1 239 ? -1.060  9.322   -0.605  1.00 68.89  ? 239 SER A C     1 
ATOM   1856 O  O     . SER A 1 239 ? -0.730  9.418   -1.791  1.00 63.63  ? 239 SER A O     1 
ATOM   1857 C  CB    . SER A 1 239 ? -2.343  11.253  0.314   1.00 71.34  ? 239 SER A CB    1 
ATOM   1858 O  OG    . SER A 1 239 ? -1.690  11.336  1.569   1.00 82.12  ? 239 SER A OG    1 
ATOM   1859 N  N     . LEU A 1 240 ? -0.245  8.813   0.320   1.00 69.81  ? 240 LEU A N     1 
ATOM   1860 C  CA    . LEU A 1 240 ? 1.072   8.269   -0.015  1.00 62.62  ? 240 LEU A CA    1 
ATOM   1861 C  C     . LEU A 1 240 ? 0.874   6.855   -0.555  1.00 65.17  ? 240 LEU A C     1 
ATOM   1862 O  O     . LEU A 1 240 ? 1.044   5.851   0.141   1.00 71.86  ? 240 LEU A O     1 
ATOM   1863 C  CB    . LEU A 1 240 ? 1.990   8.290   1.200   1.00 66.06  ? 240 LEU A CB    1 
ATOM   1864 C  CG    . LEU A 1 240 ? 2.132   9.635   1.918   1.00 63.07  ? 240 LEU A CG    1 
ATOM   1865 C  CD1   . LEU A 1 240 ? 3.137   9.537   3.058   1.00 58.76  ? 240 LEU A CD1   1 
ATOM   1866 C  CD2   . LEU A 1 240 ? 2.526   10.732  0.941   1.00 51.11  ? 240 LEU A CD2   1 
ATOM   1867 N  N     . LEU A 1 241 ? 0.503   6.784   -1.836  1.00 68.43  ? 241 LEU A N     1 
ATOM   1868 C  CA    . LEU A 1 241 ? 0.151   5.506   -2.444  1.00 68.12  ? 241 LEU A CA    1 
ATOM   1869 C  C     . LEU A 1 241 ? 1.321   4.533   -2.490  1.00 55.57  ? 241 LEU A C     1 
ATOM   1870 O  O     . LEU A 1 241 ? 1.099   3.321   -2.578  1.00 68.23  ? 241 LEU A O     1 
ATOM   1871 C  CB    . LEU A 1 241 ? -0.393  5.727   -3.857  1.00 53.34  ? 241 LEU A CB    1 
ATOM   1872 C  CG    . LEU A 1 241 ? -1.638  6.609   -3.972  1.00 52.71  ? 241 LEU A CG    1 
ATOM   1873 C  CD1   . LEU A 1 241 ? -2.154  6.629   -5.403  1.00 51.91  ? 241 LEU A CD1   1 
ATOM   1874 C  CD2   . LEU A 1 241 ? -2.721  6.142   -3.013  1.00 58.54  ? 241 LEU A CD2   1 
ATOM   1875 N  N     . GLY A 1 242 ? 2.559   5.029   -2.437  1.00 56.50  ? 242 GLY A N     1 
ATOM   1876 C  CA    . GLY A 1 242 ? 3.709   4.146   -2.517  1.00 71.96  ? 242 GLY A CA    1 
ATOM   1877 C  C     . GLY A 1 242 ? 3.976   3.352   -1.255  1.00 66.69  ? 242 GLY A C     1 
ATOM   1878 O  O     . GLY A 1 242 ? 4.739   2.382   -1.297  1.00 70.02  ? 242 GLY A O     1 
ATOM   1879 N  N     . LYS A 1 243 ? 3.360   3.735   -0.137  1.00 64.91  ? 243 LYS A N     1 
ATOM   1880 C  CA    . LYS A 1 243 ? 3.636   3.091   1.154   1.00 63.12  ? 243 LYS A CA    1 
ATOM   1881 C  C     . LYS A 1 243 ? 2.742   1.870   1.359   1.00 68.75  ? 243 LYS A C     1 
ATOM   1882 O  O     . LYS A 1 243 ? 3.216   0.731   1.330   1.00 69.27  ? 243 LYS A O     1 
ATOM   1883 C  CB    . LYS A 1 243 ? 3.468   4.103   2.290   1.00 63.12  ? 243 LYS A CB    1 
ATOM   1884 C  CG    . LYS A 1 243 ? 3.814   3.558   3.665   1.00 58.47  ? 243 LYS A CG    1 
ATOM   1885 C  CD    . LYS A 1 243 ? 3.725   4.642   4.728   1.00 56.52  ? 243 LYS A CD    1 
ATOM   1886 C  CE    . LYS A 1 243 ? 4.084   4.097   6.102   1.00 50.56  ? 243 LYS A CE    1 
ATOM   1887 N  NZ    . LYS A 1 243 ? 5.453   3.514   6.128   1.00 57.06  ? 243 LYS A NZ    1 
ATOM   1888 N  N     . LYS A 1 244 ? 1.446   2.099   1.567   1.00 69.85  ? 244 LYS A N     1 
ATOM   1889 C  CA    . LYS A 1 244 ? 0.513   1.018   1.865   1.00 59.33  ? 244 LYS A CA    1 
ATOM   1890 C  C     . LYS A 1 244 ? -0.066  0.385   0.603   1.00 62.35  ? 244 LYS A C     1 
ATOM   1891 O  O     . LYS A 1 244 ? 0.001   -0.836  0.431   1.00 60.14  ? 244 LYS A O     1 
ATOM   1892 C  CB    . LYS A 1 244 ? -0.619  1.533   2.758   1.00 62.13  ? 244 LYS A CB    1 
ATOM   1893 C  CG    . LYS A 1 244 ? -0.172  1.984   4.139   1.00 63.30  ? 244 LYS A CG    1 
ATOM   1894 C  CD    . LYS A 1 244 ? 0.386   0.824   4.947   1.00 54.80  ? 244 LYS A CD    1 
ATOM   1895 C  CE    . LYS A 1 244 ? 0.774   1.265   6.349   1.00 64.33  ? 244 LYS A CE    1 
ATOM   1896 N  NZ    . LYS A 1 244 ? 1.331   0.142   7.152   1.00 59.27  ? 244 LYS A NZ    1 
ATOM   1897 N  N     . CYS A 1 245 ? -0.636  1.201   -0.287  1.00 62.39  ? 245 CYS A N     1 
ATOM   1898 C  CA    . CYS A 1 245 ? -1.323  0.656   -1.454  1.00 59.84  ? 245 CYS A CA    1 
ATOM   1899 C  C     . CYS A 1 245 ? -0.359  -0.074  -2.382  1.00 66.78  ? 245 CYS A C     1 
ATOM   1900 O  O     . CYS A 1 245 ? -0.705  -1.115  -2.953  1.00 59.39  ? 245 CYS A O     1 
ATOM   1901 C  CB    . CYS A 1 245 ? -2.045  1.775   -2.205  1.00 49.40  ? 245 CYS A CB    1 
ATOM   1902 S  SG    . CYS A 1 245 ? -3.280  2.657   -1.223  1.00 41.02  ? 245 CYS A SG    1 
ATOM   1903 N  N     . PHE A 1 246 ? 0.854   0.453   -2.546  1.00 68.20  ? 246 PHE A N     1 
ATOM   1904 C  CA    . PHE A 1 246 ? 1.815   -0.110  -3.491  1.00 71.59  ? 246 PHE A CA    1 
ATOM   1905 C  C     . PHE A 1 246 ? 2.703   -1.168  -2.838  1.00 71.68  ? 246 PHE A C     1 
ATOM   1906 O  O     . PHE A 1 246 ? 2.756   -2.313  -3.299  1.00 69.60  ? 246 PHE A O     1 
ATOM   1907 C  CB    . PHE A 1 246 ? 2.670   1.013   -4.092  1.00 75.63  ? 246 PHE A CB    1 
ATOM   1908 C  CG    . PHE A 1 246 ? 3.578   0.564   -5.207  1.00 77.95  ? 246 PHE A CG    1 
ATOM   1909 C  CD1   . PHE A 1 246 ? 3.416   -0.677  -5.802  1.00 76.94  ? 246 PHE A CD1   1 
ATOM   1910 C  CD2   . PHE A 1 246 ? 4.599   1.386   -5.657  1.00 79.60  ? 246 PHE A CD2   1 
ATOM   1911 C  CE1   . PHE A 1 246 ? 4.252   -1.088  -6.823  1.00 83.95  ? 246 PHE A CE1   1 
ATOM   1912 C  CE2   . PHE A 1 246 ? 5.438   0.981   -6.678  1.00 81.33  ? 246 PHE A CE2   1 
ATOM   1913 C  CZ    . PHE A 1 246 ? 5.264   -0.258  -7.262  1.00 87.29  ? 246 PHE A CZ    1 
ATOM   1914 N  N     . ALA A 1 247 ? 3.404   -0.797  -1.766  1.00 74.25  ? 247 ALA A N     1 
ATOM   1915 C  CA    . ALA A 1 247 ? 4.428   -1.661  -1.192  1.00 70.01  ? 247 ALA A CA    1 
ATOM   1916 C  C     . ALA A 1 247 ? 3.864   -2.873  -0.462  1.00 70.14  ? 247 ALA A C     1 
ATOM   1917 O  O     . ALA A 1 247 ? 4.636   -3.774  -0.118  1.00 73.62  ? 247 ALA A O     1 
ATOM   1918 C  CB    . ALA A 1 247 ? 5.315   -0.857  -0.240  1.00 74.98  ? 247 ALA A CB    1 
ATOM   1919 N  N     . LEU A 1 248 ? 2.555   -2.926  -0.213  1.00 64.76  ? 248 LEU A N     1 
ATOM   1920 C  CA    . LEU A 1 248 ? 1.964   -4.047  0.512   1.00 57.10  ? 248 LEU A CA    1 
ATOM   1921 C  C     . LEU A 1 248 ? 0.857   -4.732  -0.278  1.00 68.02  ? 248 LEU A C     1 
ATOM   1922 O  O     . LEU A 1 248 ? 0.999   -5.908  -0.629  1.00 66.33  ? 248 LEU A O     1 
ATOM   1923 C  CB    . LEU A 1 248 ? 1.441   -3.579  1.877   1.00 49.90  ? 248 LEU A CB    1 
ATOM   1924 C  CG    . LEU A 1 248 ? 2.488   -3.467  2.987   1.00 52.68  ? 248 LEU A CG    1 
ATOM   1925 C  CD1   . LEU A 1 248 ? 1.825   -3.182  4.325   1.00 37.98  ? 248 LEU A CD1   1 
ATOM   1926 C  CD2   . LEU A 1 248 ? 3.324   -4.735  3.059   1.00 52.81  ? 248 LEU A CD2   1 
ATOM   1927 N  N     . ARG A 1 249 ? -0.245  -4.039  -0.566  1.00 56.74  ? 249 ARG A N     1 
ATOM   1928 C  CA    . ARG A 1 249 ? -1.371  -4.684  -1.234  1.00 61.07  ? 249 ARG A CA    1 
ATOM   1929 C  C     . ARG A 1 249 ? -0.987  -5.146  -2.635  1.00 66.21  ? 249 ARG A C     1 
ATOM   1930 O  O     . ARG A 1 249 ? -1.061  -6.339  -2.954  1.00 65.40  ? 249 ARG A O     1 
ATOM   1931 C  CB    . ARG A 1 249 ? -2.567  -3.731  -1.282  1.00 55.73  ? 249 ARG A CB    1 
ATOM   1932 C  CG    . ARG A 1 249 ? -3.076  -3.312  0.089   1.00 56.31  ? 249 ARG A CG    1 
ATOM   1933 C  CD    . ARG A 1 249 ? -4.393  -2.559  -0.014  1.00 55.52  ? 249 ARG A CD    1 
ATOM   1934 N  NE    . ARG A 1 249 ? -4.862  -2.104  1.289   1.00 58.57  ? 249 ARG A NE    1 
ATOM   1935 C  CZ    . ARG A 1 249 ? -4.641  -0.893  1.784   1.00 53.04  ? 249 ARG A CZ    1 
ATOM   1936 N  NH1   . ARG A 1 249 ? -3.968  0.019   1.102   1.00 57.01  ? 249 ARG A NH1   1 
ATOM   1937 N  NH2   . ARG A 1 249 ? -5.110  -0.590  2.991   1.00 57.67  ? 249 ARG A NH2   1 
ATOM   1938 N  N     . ILE A 1 250 ? -0.574  -4.210  -3.491  1.00 66.53  ? 250 ILE A N     1 
ATOM   1939 C  CA    . ILE A 1 250 ? -0.213  -4.571  -4.859  1.00 60.61  ? 250 ILE A CA    1 
ATOM   1940 C  C     . ILE A 1 250 ? 1.050   -5.424  -4.874  1.00 66.60  ? 250 ILE A C     1 
ATOM   1941 O  O     . ILE A 1 250 ? 1.164   -6.375  -5.657  1.00 63.00  ? 250 ILE A O     1 
ATOM   1942 C  CB    . ILE A 1 250 ? -0.051  -3.307  -5.721  1.00 63.44  ? 250 ILE A CB    1 
ATOM   1943 C  CG1   . ILE A 1 250 ? -1.344  -2.489  -5.718  1.00 63.72  ? 250 ILE A CG1   1 
ATOM   1944 C  CG2   . ILE A 1 250 ? 0.339   -3.680  -7.143  1.00 65.13  ? 250 ILE A CG2   1 
ATOM   1945 C  CD1   . ILE A 1 250 ? -2.519  -3.200  -6.352  1.00 68.62  ? 250 ILE A CD1   1 
ATOM   1946 N  N     . ALA A 1 251 ? 2.018   -5.100  -4.012  1.00 69.83  ? 251 ALA A N     1 
ATOM   1947 C  CA    . ALA A 1 251 ? 3.261   -5.864  -3.980  1.00 67.09  ? 251 ALA A CA    1 
ATOM   1948 C  C     . ALA A 1 251 ? 3.019   -7.318  -3.601  1.00 61.22  ? 251 ALA A C     1 
ATOM   1949 O  O     . ALA A 1 251 ? 3.720   -8.212  -4.089  1.00 64.69  ? 251 ALA A O     1 
ATOM   1950 C  CB    . ALA A 1 251 ? 4.251   -5.219  -3.010  1.00 64.19  ? 251 ALA A CB    1 
ATOM   1951 N  N     . SER A 1 252 ? 2.037   -7.578  -2.734  1.00 60.06  ? 252 SER A N     1 
ATOM   1952 C  CA    . SER A 1 252 ? 1.728   -8.955  -2.364  1.00 67.03  ? 252 SER A CA    1 
ATOM   1953 C  C     . SER A 1 252 ? 1.223   -9.745  -3.565  1.00 67.01  ? 252 SER A C     1 
ATOM   1954 O  O     . SER A 1 252 ? 1.593   -10.910 -3.751  1.00 60.77  ? 252 SER A O     1 
ATOM   1955 C  CB    . SER A 1 252 ? 0.700   -8.977  -1.233  1.00 66.90  ? 252 SER A CB    1 
ATOM   1956 O  OG    . SER A 1 252 ? -0.500  -8.332  -1.621  1.00 66.00  ? 252 SER A OG    1 
ATOM   1957 N  N     . ARG A 1 253 ? 0.374   -9.129  -4.389  1.00 68.38  ? 253 ARG A N     1 
ATOM   1958 C  CA    . ARG A 1 253 ? -0.106  -9.795  -5.596  1.00 61.26  ? 253 ARG A CA    1 
ATOM   1959 C  C     . ARG A 1 253 ? 1.054   -10.148 -6.519  1.00 67.81  ? 253 ARG A C     1 
ATOM   1960 O  O     . ARG A 1 253 ? 1.146   -11.274 -7.020  1.00 80.98  ? 253 ARG A O     1 
ATOM   1961 C  CB    . ARG A 1 253 ? -1.121  -8.905  -6.313  1.00 73.46  ? 253 ARG A CB    1 
ATOM   1962 C  CG    . ARG A 1 253 ? -1.712  -9.511  -7.578  1.00 78.58  ? 253 ARG A CG    1 
ATOM   1963 C  CD    . ARG A 1 253 ? -2.517  -10.763 -7.273  1.00 79.76  ? 253 ARG A CD    1 
ATOM   1964 N  NE    . ARG A 1 253 ? -3.266  -11.222 -8.437  1.00 97.02  ? 253 ARG A NE    1 
ATOM   1965 C  CZ    . ARG A 1 253 ? -4.518  -10.878 -8.704  1.00 99.91  ? 253 ARG A CZ    1 
ATOM   1966 N  NH1   . ARG A 1 253 ? -5.201  -10.076 -7.903  1.00 99.05  ? 253 ARG A NH1   1 
ATOM   1967 N  NH2   . ARG A 1 253 ? -5.101  -11.351 -9.803  1.00 98.54  ? 253 ARG A NH2   1 
ATOM   1968 N  N     . LEU A 1 254 ? 1.955   -9.191  -6.753  1.00 73.15  ? 254 LEU A N     1 
ATOM   1969 C  CA    . LEU A 1 254 ? 3.127   -9.467  -7.577  1.00 76.89  ? 254 LEU A CA    1 
ATOM   1970 C  C     . LEU A 1 254 ? 4.028   -10.505 -6.919  1.00 73.55  ? 254 LEU A C     1 
ATOM   1971 O  O     . LEU A 1 254 ? 4.589   -11.372 -7.600  1.00 81.60  ? 254 LEU A O     1 
ATOM   1972 C  CB    . LEU A 1 254 ? 3.900   -8.176  -7.842  1.00 72.57  ? 254 LEU A CB    1 
ATOM   1973 C  CG    . LEU A 1 254 ? 3.177   -7.095  -8.648  1.00 80.85  ? 254 LEU A CG    1 
ATOM   1974 C  CD1   . LEU A 1 254 ? 4.040   -5.848  -8.773  1.00 71.53  ? 254 LEU A CD1   1 
ATOM   1975 C  CD2   . LEU A 1 254 ? 2.790   -7.623  -10.021 1.00 80.09  ? 254 LEU A CD2   1 
ATOM   1976 N  N     . ALA A 1 255 ? 4.181   -10.432 -5.595  1.00 72.99  ? 255 ALA A N     1 
ATOM   1977 C  CA    . ALA A 1 255 ? 5.009   -11.407 -4.893  1.00 80.54  ? 255 ALA A CA    1 
ATOM   1978 C  C     . ALA A 1 255 ? 4.467   -12.820 -5.072  1.00 73.90  ? 255 ALA A C     1 
ATOM   1979 O  O     . ALA A 1 255 ? 5.238   -13.773 -5.233  1.00 77.43  ? 255 ALA A O     1 
ATOM   1980 C  CB    . ALA A 1 255 ? 5.100   -11.049 -3.410  1.00 68.09  ? 255 ALA A CB    1 
ATOM   1981 N  N     . LYS A 1 256 ? 3.142   -12.974 -5.046  1.00 76.06  ? 256 LYS A N     1 
ATOM   1982 C  CA    . LYS A 1 256 ? 2.549   -14.290 -5.264  1.00 75.19  ? 256 LYS A CA    1 
ATOM   1983 C  C     . LYS A 1 256 ? 2.790   -14.774 -6.688  1.00 79.66  ? 256 LYS A C     1 
ATOM   1984 O  O     . LYS A 1 256 ? 3.043   -15.963 -6.912  1.00 75.59  ? 256 LYS A O     1 
ATOM   1985 C  CB    . LYS A 1 256 ? 1.052   -14.247 -4.955  1.00 69.83  ? 256 LYS A CB    1 
ATOM   1986 C  CG    . LYS A 1 256 ? 0.321   -15.553 -5.219  1.00 74.24  ? 256 LYS A CG    1 
ATOM   1987 C  CD    . LYS A 1 256 ? 0.888   -16.685 -4.379  1.00 68.10  ? 256 LYS A CD    1 
ATOM   1988 C  CE    . LYS A 1 256 ? 0.092   -17.965 -4.574  1.00 71.57  ? 256 LYS A CE    1 
ATOM   1989 N  NZ    . LYS A 1 256 ? 0.067   -18.394 -6.000  1.00 68.41  ? 256 LYS A NZ    1 
ATOM   1990 N  N     . GLU A 1 257 ? 2.721   -13.865 -7.663  1.00 92.79  ? 257 GLU A N     1 
ATOM   1991 C  CA    . GLU A 1 257 ? 2.933   -14.253 -9.053  1.00 96.78  ? 257 GLU A CA    1 
ATOM   1992 C  C     . GLU A 1 257 ? 4.402   -14.548 -9.329  1.00 94.20  ? 257 GLU A C     1 
ATOM   1993 O  O     . GLU A 1 257 ? 4.727   -15.520 -10.021 1.00 98.39  ? 257 GLU A O     1 
ATOM   1994 C  CB    . GLU A 1 257 ? 2.428   -13.152 -9.985  1.00 105.34 ? 257 GLU A CB    1 
ATOM   1995 C  CG    . GLU A 1 257 ? 0.983   -12.747 -9.751  1.00 107.70 ? 257 GLU A CG    1 
ATOM   1996 C  CD    . GLU A 1 257 ? 0.604   -11.489 -10.507 1.00 108.61 ? 257 GLU A CD    1 
ATOM   1997 O  OE1   . GLU A 1 257 ? 1.494   -10.886 -11.143 1.00 103.99 ? 257 GLU A OE1   1 
ATOM   1998 O  OE2   . GLU A 1 257 ? -0.582  -11.101 -10.463 1.00 97.94  ? 257 GLU A OE2   1 
ATOM   1999 N  N     . GLU A 1 258 ? 5.302   -13.723 -8.796  1.00 88.37  ? 258 GLU A N     1 
ATOM   2000 C  CA    . GLU A 1 258 ? 6.722   -13.835 -9.105  1.00 87.13  ? 258 GLU A CA    1 
ATOM   2001 C  C     . GLU A 1 258 ? 7.472   -14.749 -8.145  1.00 87.55  ? 258 GLU A C     1 
ATOM   2002 O  O     . GLU A 1 258 ? 8.486   -15.340 -8.533  1.00 92.93  ? 258 GLU A O     1 
ATOM   2003 C  CB    . GLU A 1 258 ? 7.364   -12.445 -9.109  1.00 89.51  ? 258 GLU A CB    1 
ATOM   2004 C  CG    . GLU A 1 258 ? 6.692   -11.475 -10.069 1.00 89.68  ? 258 GLU A CG    1 
ATOM   2005 C  CD    . GLU A 1 258 ? 7.278   -10.080 -10.005 1.00 97.27  ? 258 GLU A CD    1 
ATOM   2006 O  OE1   . GLU A 1 258 ? 8.407   -9.930  -9.492  1.00 96.98  ? 258 GLU A OE1   1 
ATOM   2007 O  OE2   . GLU A 1 258 ? 6.607   -9.132  -10.465 1.00 97.97  ? 258 GLU A OE2   1 
ATOM   2008 N  N     . GLY A 1 259 ? 7.010   -14.876 -6.910  1.00 82.40  ? 259 GLY A N     1 
ATOM   2009 C  CA    . GLY A 1 259 ? 7.585   -15.801 -5.963  1.00 78.90  ? 259 GLY A CA    1 
ATOM   2010 C  C     . GLY A 1 259 ? 8.383   -15.204 -4.813  1.00 77.30  ? 259 GLY A C     1 
ATOM   2011 O  O     . GLY A 1 259 ? 9.210   -15.916 -4.230  1.00 82.93  ? 259 GLY A O     1 
ATOM   2012 N  N     . TRP A 1 260 ? 8.167   -13.935 -4.473  1.00 70.23  ? 260 TRP A N     1 
ATOM   2013 C  CA    . TRP A 1 260 ? 8.815   -13.312 -3.333  1.00 68.43  ? 260 TRP A CA    1 
ATOM   2014 C  C     . TRP A 1 260 ? 7.758   -12.956 -2.283  1.00 63.55  ? 260 TRP A C     1 
ATOM   2015 O  O     . TRP A 1 260 ? 6.624   -13.453 -2.334  1.00 57.42  ? 260 TRP A O     1 
ATOM   2016 C  CB    . TRP A 1 260 ? 9.637   -12.107 -3.804  1.00 72.24  ? 260 TRP A CB    1 
ATOM   2017 C  CG    . TRP A 1 260 ? 8.901   -11.161 -4.706  1.00 74.52  ? 260 TRP A CG    1 
ATOM   2018 C  CD1   . TRP A 1 260 ? 8.566   -11.366 -6.013  1.00 74.41  ? 260 TRP A CD1   1 
ATOM   2019 C  CD2   . TRP A 1 260 ? 8.432   -9.848  -4.374  1.00 66.74  ? 260 TRP A CD2   1 
ATOM   2020 N  NE1   . TRP A 1 260 ? 7.906   -10.270 -6.511  1.00 72.29  ? 260 TRP A NE1   1 
ATOM   2021 C  CE2   . TRP A 1 260 ? 7.812   -9.323  -5.525  1.00 71.96  ? 260 TRP A CE2   1 
ATOM   2022 C  CE3   . TRP A 1 260 ? 8.471   -9.068  -3.214  1.00 62.72  ? 260 TRP A CE3   1 
ATOM   2023 C  CZ2   . TRP A 1 260 ? 7.235   -8.055  -5.550  1.00 71.25  ? 260 TRP A CZ2   1 
ATOM   2024 C  CZ3   . TRP A 1 260 ? 7.898   -7.809  -3.241  1.00 66.27  ? 260 TRP A CZ3   1 
ATOM   2025 C  CH2   . TRP A 1 260 ? 7.289   -7.315  -4.401  1.00 67.25  ? 260 TRP A CH2   1 
ATOM   2026 N  N     . LEU A 1 261 ? 8.129   -12.104 -1.329  1.00 68.83  ? 261 LEU A N     1 
ATOM   2027 C  CA    . LEU A 1 261 ? 7.258   -11.773 -0.211  1.00 48.02  ? 261 LEU A CA    1 
ATOM   2028 C  C     . LEU A 1 261 ? 7.240   -10.270 0.024   1.00 63.53  ? 261 LEU A C     1 
ATOM   2029 O  O     . LEU A 1 261 ? 8.266   -9.596  -0.111  1.00 78.98  ? 261 LEU A O     1 
ATOM   2030 C  CB    . LEU A 1 261 ? 7.704   -12.490 1.070   1.00 47.03  ? 261 LEU A CB    1 
ATOM   2031 C  CG    . LEU A 1 261 ? 7.654   -14.019 1.047   1.00 43.24  ? 261 LEU A CG    1 
ATOM   2032 C  CD1   . LEU A 1 261 ? 8.159   -14.595 2.360   1.00 43.14  ? 261 LEU A CD1   1 
ATOM   2033 C  CD2   . LEU A 1 261 ? 6.243   -14.505 0.753   1.00 67.21  ? 261 LEU A CD2   1 
ATOM   2034 N  N     . ALA A 1 262 ? 6.063   -9.755  0.375   1.00 58.65  ? 262 ALA A N     1 
ATOM   2035 C  CA    . ALA A 1 262 ? 5.879   -8.360  0.766   1.00 55.89  ? 262 ALA A CA    1 
ATOM   2036 C  C     . ALA A 1 262 ? 5.083   -8.354  2.064   1.00 54.61  ? 262 ALA A C     1 
ATOM   2037 O  O     . ALA A 1 262 ? 3.893   -8.686  2.066   1.00 58.37  ? 262 ALA A O     1 
ATOM   2038 C  CB    . ALA A 1 262 ? 5.163   -7.564  -0.325  1.00 54.98  ? 262 ALA A CB    1 
ATOM   2039 N  N     . GLU A 1 263 ? 5.735   -7.984  3.164   1.00 48.45  ? 263 GLU A N     1 
ATOM   2040 C  CA    . GLU A 1 263 ? 5.149   -8.115  4.488   1.00 47.76  ? 263 GLU A CA    1 
ATOM   2041 C  C     . GLU A 1 263 ? 5.188   -6.784  5.226   1.00 42.72  ? 263 GLU A C     1 
ATOM   2042 O  O     . GLU A 1 263 ? 5.898   -5.851  4.843   1.00 47.49  ? 263 GLU A O     1 
ATOM   2043 C  CB    . GLU A 1 263 ? 5.872   -9.189  5.313   1.00 43.57  ? 263 GLU A CB    1 
ATOM   2044 C  CG    . GLU A 1 263 ? 5.784   -10.582 4.715   1.00 51.50  ? 263 GLU A CG    1 
ATOM   2045 C  CD    . GLU A 1 263 ? 4.362   -11.105 4.671   1.00 52.48  ? 263 GLU A CD    1 
ATOM   2046 O  OE1   . GLU A 1 263 ? 3.575   -10.767 5.581   1.00 51.94  ? 263 GLU A OE1   1 
ATOM   2047 O  OE2   . GLU A 1 263 ? 4.029   -11.847 3.724   1.00 58.88  ? 263 GLU A OE2   1 
ATOM   2048 N  N     . HIS A 1 264 ? 4.407   -6.719  6.302   1.00 50.71  ? 264 HIS A N     1 
ATOM   2049 C  CA    . HIS A 1 264 ? 4.338   -5.537  7.157   1.00 53.83  ? 264 HIS A CA    1 
ATOM   2050 C  C     . HIS A 1 264 ? 5.223   -5.752  8.385   1.00 47.52  ? 264 HIS A C     1 
ATOM   2051 O  O     . HIS A 1 264 ? 4.761   -5.895  9.518   1.00 41.15  ? 264 HIS A O     1 
ATOM   2052 C  CB    . HIS A 1 264 ? 2.887   -5.256  7.544   1.00 50.06  ? 264 HIS A CB    1 
ATOM   2053 C  CG    . HIS A 1 264 ? 2.706   -4.026  8.376   1.00 41.78  ? 264 HIS A CG    1 
ATOM   2054 N  ND1   . HIS A 1 264 ? 1.643   -3.864  9.239   1.00 35.20  ? 264 HIS A ND1   1 
ATOM   2055 C  CD2   . HIS A 1 264 ? 3.444   -2.895  8.473   1.00 43.27  ? 264 HIS A CD2   1 
ATOM   2056 C  CE1   . HIS A 1 264 ? 1.737   -2.689  9.835   1.00 46.88  ? 264 HIS A CE1   1 
ATOM   2057 N  NE2   . HIS A 1 264 ? 2.821   -2.081  9.388   1.00 57.80  ? 264 HIS A NE2   1 
ATOM   2058 N  N     . MET A 1 265 ? 6.530   -5.777  8.131   1.00 47.20  ? 265 MET A N     1 
ATOM   2059 C  CA    . MET A 1 265 ? 7.515   -6.088  9.155   1.00 44.88  ? 265 MET A CA    1 
ATOM   2060 C  C     . MET A 1 265 ? 8.626   -5.048  9.152   1.00 49.05  ? 265 MET A C     1 
ATOM   2061 O  O     . MET A 1 265 ? 8.850   -4.343  8.165   1.00 50.16  ? 265 MET A O     1 
ATOM   2062 C  CB    . MET A 1 265 ? 8.126   -7.480  8.945   1.00 43.18  ? 265 MET A CB    1 
ATOM   2063 C  CG    . MET A 1 265 ? 7.115   -8.606  8.844   1.00 45.81  ? 265 MET A CG    1 
ATOM   2064 S  SD    . MET A 1 265 ? 7.900   -10.166 8.396   1.00 37.09  ? 265 MET A SD    1 
ATOM   2065 C  CE    . MET A 1 265 ? 6.478   -11.252 8.317   1.00 48.78  ? 265 MET A CE    1 
ATOM   2066 N  N     . LEU A 1 266 ? 9.325   -4.970  10.279  1.00 50.86  ? 266 LEU A N     1 
ATOM   2067 C  CA    . LEU A 1 266 ? 10.528  -4.165  10.397  1.00 43.31  ? 266 LEU A CA    1 
ATOM   2068 C  C     . LEU A 1 266 ? 11.759  -5.029  10.132  1.00 45.25  ? 266 LEU A C     1 
ATOM   2069 O  O     . LEU A 1 266 ? 11.692  -6.259  10.090  1.00 44.71  ? 266 LEU A O     1 
ATOM   2070 C  CB    . LEU A 1 266 ? 10.607  -3.518  11.782  1.00 39.81  ? 266 LEU A CB    1 
ATOM   2071 C  CG    . LEU A 1 266 ? 10.681  -4.451  12.996  1.00 41.39  ? 266 LEU A CG    1 
ATOM   2072 C  CD1   . LEU A 1 266 ? 12.090  -4.993  13.200  1.00 36.30  ? 266 LEU A CD1   1 
ATOM   2073 C  CD2   . LEU A 1 266 ? 10.191  -3.749  14.252  1.00 37.90  ? 266 LEU A CD2   1 
ATOM   2074 N  N     . ILE A 1 267 ? 12.899  -4.367  9.950   1.00 43.33  ? 267 ILE A N     1 
ATOM   2075 C  CA    . ILE A 1 267 ? 14.171  -5.041  9.713   1.00 43.20  ? 267 ILE A CA    1 
ATOM   2076 C  C     . ILE A 1 267 ? 15.222  -4.375  10.588  1.00 48.18  ? 267 ILE A C     1 
ATOM   2077 O  O     . ILE A 1 267 ? 15.484  -3.175  10.443  1.00 45.27  ? 267 ILE A O     1 
ATOM   2078 C  CB    . ILE A 1 267 ? 14.588  -4.990  8.234   1.00 43.85  ? 267 ILE A CB    1 
ATOM   2079 C  CG1   . ILE A 1 267 ? 13.425  -5.414  7.336   1.00 49.03  ? 267 ILE A CG1   1 
ATOM   2080 C  CG2   . ILE A 1 267 ? 15.796  -5.882  7.992   1.00 46.64  ? 267 ILE A CG2   1 
ATOM   2081 C  CD1   . ILE A 1 267 ? 13.735  -5.326  5.856   1.00 48.79  ? 267 ILE A CD1   1 
ATOM   2082 N  N     . LEU A 1 268 ? 15.822  -5.147  11.491  1.00 44.16  ? 268 LEU A N     1 
ATOM   2083 C  CA    . LEU A 1 268 ? 16.836  -4.622  12.392  1.00 51.73  ? 268 LEU A CA    1 
ATOM   2084 C  C     . LEU A 1 268 ? 17.969  -5.626  12.531  1.00 54.10  ? 268 LEU A C     1 
ATOM   2085 O  O     . LEU A 1 268 ? 17.732  -6.832  12.648  1.00 49.80  ? 268 LEU A O     1 
ATOM   2086 C  CB    . LEU A 1 268 ? 16.246  -4.295  13.774  1.00 40.81  ? 268 LEU A CB    1 
ATOM   2087 C  CG    . LEU A 1 268 ? 15.731  -5.438  14.654  1.00 36.86  ? 268 LEU A CG    1 
ATOM   2088 C  CD1   . LEU A 1 268 ? 16.872  -6.165  15.354  1.00 43.10  ? 268 LEU A CD1   1 
ATOM   2089 C  CD2   . LEU A 1 268 ? 14.728  -4.917  15.671  1.00 41.88  ? 268 LEU A CD2   1 
ATOM   2090 N  N     . GLY A 1 269 ? 19.197  -5.120  12.513  1.00 55.98  ? 269 GLY A N     1 
ATOM   2091 C  CA    . GLY A 1 269 ? 20.378  -5.928  12.769  1.00 53.39  ? 269 GLY A CA    1 
ATOM   2092 C  C     . GLY A 1 269 ? 20.882  -5.690  14.180  1.00 42.06  ? 269 GLY A C     1 
ATOM   2093 O  O     . GLY A 1 269 ? 20.844  -4.566  14.683  1.00 52.94  ? 269 GLY A O     1 
ATOM   2094 N  N     . ILE A 1 270 ? 21.353  -6.760  14.815  1.00 44.36  ? 270 ILE A N     1 
ATOM   2095 C  CA    . ILE A 1 270 ? 21.819  -6.715  16.195  1.00 49.78  ? 270 ILE A CA    1 
ATOM   2096 C  C     . ILE A 1 270 ? 23.194  -7.362  16.272  1.00 48.78  ? 270 ILE A C     1 
ATOM   2097 O  O     . ILE A 1 270 ? 23.440  -8.399  15.647  1.00 46.23  ? 270 ILE A O     1 
ATOM   2098 C  CB    . ILE A 1 270 ? 20.830  -7.415  17.151  1.00 45.24  ? 270 ILE A CB    1 
ATOM   2099 C  CG1   . ILE A 1 270 ? 21.340  -7.345  18.591  1.00 60.75  ? 270 ILE A CG1   1 
ATOM   2100 C  CG2   . ILE A 1 270 ? 20.607  -8.856  16.724  1.00 48.59  ? 270 ILE A CG2   1 
ATOM   2101 C  CD1   . ILE A 1 270 ? 20.384  -7.929  19.607  1.00 58.52  ? 270 ILE A CD1   1 
ATOM   2102 N  N     . THR A 1 271 ? 24.089  -6.747  17.042  1.00 56.15  ? 271 THR A N     1 
ATOM   2103 C  CA    . THR A 1 271 ? 25.451  -7.228  17.216  1.00 49.05  ? 271 THR A CA    1 
ATOM   2104 C  C     . THR A 1 271 ? 25.702  -7.523  18.688  1.00 53.83  ? 271 THR A C     1 
ATOM   2105 O  O     . THR A 1 271 ? 25.292  -6.754  19.563  1.00 46.66  ? 271 THR A O     1 
ATOM   2106 C  CB    . THR A 1 271 ? 26.471  -6.203  16.708  1.00 58.68  ? 271 THR A CB    1 
ATOM   2107 O  OG1   . THR A 1 271 ? 26.140  -5.821  15.367  1.00 61.66  ? 271 THR A OG1   1 
ATOM   2108 C  CG2   . THR A 1 271 ? 27.875  -6.792  16.730  1.00 64.13  ? 271 THR A CG2   1 
ATOM   2109 N  N     . ASN A 1 272 ? 26.375  -8.632  18.955  1.00 57.57  ? 272 ASN A N     1 
ATOM   2110 C  CA    . ASN A 1 272 ? 26.654  -9.093  20.305  1.00 51.54  ? 272 ASN A CA    1 
ATOM   2111 C  C     . ASN A 1 272 ? 28.068  -8.724  20.718  1.00 58.90  ? 272 ASN A C     1 
ATOM   2112 O  O     . ASN A 1 272 ? 28.905  -8.358  19.887  1.00 58.19  ? 272 ASN A O     1 
ATOM   2113 C  CB    . ASN A 1 272 ? 26.456  -10.607 20.393  1.00 56.72  ? 272 ASN A CB    1 
ATOM   2114 C  CG    . ASN A 1 272 ? 27.467  -11.375 19.564  1.00 61.78  ? 272 ASN A CG    1 
ATOM   2115 O  OD1   . ASN A 1 272 ? 28.053  -10.838 18.625  1.00 70.37  ? 272 ASN A OD1   1 
ATOM   2116 N  ND2   . ASN A 1 272 ? 27.676  -12.642 19.908  1.00 63.72  ? 272 ASN A ND2   1 
ATOM   2117 N  N     . PRO A 1 273 ? 28.377  -8.810  22.014  1.00 60.24  ? 273 PRO A N     1 
ATOM   2118 C  CA    . PRO A 1 273 ? 29.735  -8.470  22.469  1.00 66.94  ? 273 PRO A CA    1 
ATOM   2119 C  C     . PRO A 1 273 ? 30.815  -9.371  21.897  1.00 64.56  ? 273 PRO A C     1 
ATOM   2120 O  O     . PRO A 1 273 ? 31.994  -9.000  21.943  1.00 64.09  ? 273 PRO A O     1 
ATOM   2121 C  CB    . PRO A 1 273 ? 29.640  -8.612  23.995  1.00 59.39  ? 273 PRO A CB    1 
ATOM   2122 C  CG    . PRO A 1 273 ? 28.178  -8.491  24.302  1.00 64.75  ? 273 PRO A CG    1 
ATOM   2123 C  CD    . PRO A 1 273 ? 27.474  -9.112  23.137  1.00 54.68  ? 273 PRO A CD    1 
ATOM   2124 N  N     . GLU A 1 274 ? 30.458  -10.539 21.364  1.00 66.32  ? 274 GLU A N     1 
ATOM   2125 C  CA    . GLU A 1 274 ? 31.448  -11.463 20.825  1.00 63.10  ? 274 GLU A CA    1 
ATOM   2126 C  C     . GLU A 1 274 ? 31.851  -11.140 19.392  1.00 66.79  ? 274 GLU A C     1 
ATOM   2127 O  O     . GLU A 1 274 ? 32.830  -11.711 18.900  1.00 61.73  ? 274 GLU A O     1 
ATOM   2128 C  CB    . GLU A 1 274 ? 30.921  -12.899 20.899  1.00 62.13  ? 274 GLU A CB    1 
ATOM   2129 C  CG    . GLU A 1 274 ? 30.618  -13.371 22.312  1.00 60.82  ? 274 GLU A CG    1 
ATOM   2130 C  CD    . GLU A 1 274 ? 31.847  -13.384 23.199  1.00 64.19  ? 274 GLU A CD    1 
ATOM   2131 O  OE1   . GLU A 1 274 ? 32.969  -13.497 22.662  1.00 68.11  ? 274 GLU A OE1   1 
ATOM   2132 O  OE2   . GLU A 1 274 ? 31.691  -13.278 24.434  1.00 64.14  ? 274 GLU A OE2   1 
ATOM   2133 N  N     . GLY A 1 275 ? 31.131  -10.253 18.716  1.00 68.63  ? 275 GLY A N     1 
ATOM   2134 C  CA    . GLY A 1 275 ? 31.473  -9.859  17.367  1.00 65.75  ? 275 GLY A CA    1 
ATOM   2135 C  C     . GLY A 1 275 ? 30.606  -10.434 16.268  1.00 66.21  ? 275 GLY A C     1 
ATOM   2136 O  O     . GLY A 1 275 ? 31.007  -10.374 15.100  1.00 66.75  ? 275 GLY A O     1 
ATOM   2137 N  N     . LYS A 1 276 ? 29.443  -10.986 16.598  1.00 73.19  ? 276 LYS A N     1 
ATOM   2138 C  CA    . LYS A 1 276 ? 28.528  -11.544 15.615  1.00 66.20  ? 276 LYS A CA    1 
ATOM   2139 C  C     . LYS A 1 276 ? 27.328  -10.620 15.441  1.00 65.82  ? 276 LYS A C     1 
ATOM   2140 O  O     . LYS A 1 276 ? 26.889  -9.961  16.389  1.00 68.11  ? 276 LYS A O     1 
ATOM   2141 C  CB    . LYS A 1 276 ? 28.052  -12.939 16.033  1.00 70.28  ? 276 LYS A CB    1 
ATOM   2142 C  CG    . LYS A 1 276 ? 29.139  -13.828 16.623  1.00 70.16  ? 276 LYS A CG    1 
ATOM   2143 C  CD    . LYS A 1 276 ? 30.285  -14.047 15.649  1.00 71.38  ? 276 LYS A CD    1 
ATOM   2144 C  CE    . LYS A 1 276 ? 31.265  -15.083 16.180  1.00 75.61  ? 276 LYS A CE    1 
ATOM   2145 N  NZ    . LYS A 1 276 ? 31.810  -14.710 17.515  1.00 76.95  ? 276 LYS A NZ    1 
ATOM   2146 N  N     . LYS A 1 277 ? 26.800  -10.574 14.220  1.00 57.08  ? 277 LYS A N     1 
ATOM   2147 C  CA    . LYS A 1 277 ? 25.653  -9.735  13.898  1.00 59.25  ? 277 LYS A CA    1 
ATOM   2148 C  C     . LYS A 1 277 ? 24.648  -10.538 13.087  1.00 53.00  ? 277 LYS A C     1 
ATOM   2149 O  O     . LYS A 1 277 ? 25.026  -11.244 12.146  1.00 56.43  ? 277 LYS A O     1 
ATOM   2150 C  CB    . LYS A 1 277 ? 26.077  -8.482  13.124  1.00 51.27  ? 277 LYS A CB    1 
ATOM   2151 C  CG    . LYS A 1 277 ? 24.929  -7.529  12.827  1.00 51.16  ? 277 LYS A CG    1 
ATOM   2152 C  CD    . LYS A 1 277 ? 25.396  -6.325  12.027  1.00 49.45  ? 277 LYS A CD    1 
ATOM   2153 C  CE    . LYS A 1 277 ? 24.247  -5.367  11.755  1.00 57.83  ? 277 LYS A CE    1 
ATOM   2154 N  NZ    . LYS A 1 277 ? 24.681  -4.191  10.953  1.00 63.67  ? 277 LYS A NZ    1 
ATOM   2155 N  N     . LYS A 1 278 ? 23.373  -10.423 13.451  1.00 55.33  ? 278 LYS A N     1 
ATOM   2156 C  CA    . LYS A 1 278 ? 22.290  -11.105 12.761  1.00 57.74  ? 278 LYS A CA    1 
ATOM   2157 C  C     . LYS A 1 278 ? 21.155  -10.123 12.507  1.00 58.23  ? 278 LYS A C     1 
ATOM   2158 O  O     . LYS A 1 278 ? 21.006  -9.117  13.207  1.00 45.81  ? 278 LYS A O     1 
ATOM   2159 C  CB    . LYS A 1 278 ? 21.779  -12.309 13.566  1.00 53.73  ? 278 LYS A CB    1 
ATOM   2160 C  CG    . LYS A 1 278 ? 22.854  -13.328 13.911  1.00 58.84  ? 278 LYS A CG    1 
ATOM   2161 C  CD    . LYS A 1 278 ? 22.286  -14.484 14.720  1.00 61.09  ? 278 LYS A CD    1 
ATOM   2162 C  CE    . LYS A 1 278 ? 23.367  -15.490 15.082  1.00 67.42  ? 278 LYS A CE    1 
ATOM   2163 N  NZ    . LYS A 1 278 ? 24.025  -16.058 13.872  1.00 58.88  ? 278 LYS A NZ    1 
ATOM   2164 N  N     . TYR A 1 279 ? 20.351  -10.426 11.492  1.00 55.11  ? 279 TYR A N     1 
ATOM   2165 C  CA    . TYR A 1 279 ? 19.218  -9.597  11.106  1.00 52.51  ? 279 TYR A CA    1 
ATOM   2166 C  C     . TYR A 1 279 ? 17.913  -10.289 11.475  1.00 48.46  ? 279 TYR A C     1 
ATOM   2167 O  O     . TYR A 1 279 ? 17.754  -11.495 11.259  1.00 58.71  ? 279 TYR A O     1 
ATOM   2168 C  CB    . TYR A 1 279 ? 19.243  -9.293  9.605   1.00 52.31  ? 279 TYR A CB    1 
ATOM   2169 C  CG    . TYR A 1 279 ? 20.315  -8.308  9.197   1.00 47.33  ? 279 TYR A CG    1 
ATOM   2170 C  CD1   . TYR A 1 279 ? 20.082  -6.940  9.248   1.00 48.08  ? 279 TYR A CD1   1 
ATOM   2171 C  CD2   . TYR A 1 279 ? 21.559  -8.745  8.761   1.00 51.95  ? 279 TYR A CD2   1 
ATOM   2172 C  CE1   . TYR A 1 279 ? 21.056  -6.035  8.876   1.00 42.69  ? 279 TYR A CE1   1 
ATOM   2173 C  CE2   . TYR A 1 279 ? 22.541  -7.845  8.386   1.00 51.66  ? 279 TYR A CE2   1 
ATOM   2174 C  CZ    . TYR A 1 279 ? 22.284  -6.493  8.446   1.00 49.03  ? 279 TYR A CZ    1 
ATOM   2175 O  OH    . TYR A 1 279 ? 23.257  -5.594  8.075   1.00 56.62  ? 279 TYR A OH    1 
ATOM   2176 N  N     . LEU A 1 280 ? 16.982  -9.518  12.030  1.00 43.33  ? 280 LEU A N     1 
ATOM   2177 C  CA    . LEU A 1 280 ? 15.694  -10.034 12.464  1.00 45.64  ? 280 LEU A CA    1 
ATOM   2178 C  C     . LEU A 1 280 ? 14.573  -9.238  11.812  1.00 43.81  ? 280 LEU A C     1 
ATOM   2179 O  O     . LEU A 1 280 ? 14.784  -8.146  11.276  1.00 43.23  ? 280 LEU A O     1 
ATOM   2180 C  CB    . LEU A 1 280 ? 15.552  -9.981  13.992  1.00 44.35  ? 280 LEU A CB    1 
ATOM   2181 C  CG    . LEU A 1 280 ? 16.640  -10.678 14.811  1.00 53.65  ? 280 LEU A CG    1 
ATOM   2182 C  CD1   . LEU A 1 280 ? 16.345  -10.570 16.300  1.00 49.11  ? 280 LEU A CD1   1 
ATOM   2183 C  CD2   . LEU A 1 280 ? 16.780  -12.133 14.393  1.00 55.45  ? 280 LEU A CD2   1 
ATOM   2184 N  N     . ALA A 1 281 ? 13.369  -9.804  11.867  1.00 48.04  ? 281 ALA A N     1 
ATOM   2185 C  CA    . ALA A 1 281 ? 12.172  -9.158  11.351  1.00 40.49  ? 281 ALA A CA    1 
ATOM   2186 C  C     . ALA A 1 281 ? 11.042  -9.339  12.354  1.00 36.48  ? 281 ALA A C     1 
ATOM   2187 O  O     . ALA A 1 281 ? 10.930  -10.389 12.993  1.00 35.83  ? 281 ALA A O     1 
ATOM   2188 C  CB    . ALA A 1 281 ? 11.768  -9.727  9.985   1.00 38.61  ? 281 ALA A CB    1 
ATOM   2189 N  N     . ALA A 1 282 ? 10.211  -8.309  12.492  1.00 40.83  ? 282 ALA A N     1 
ATOM   2190 C  CA    . ALA A 1 282 ? 9.108   -8.319  13.443  1.00 42.09  ? 282 ALA A CA    1 
ATOM   2191 C  C     . ALA A 1 282 ? 7.842   -7.831  12.756  1.00 35.08  ? 282 ALA A C     1 
ATOM   2192 O  O     . ALA A 1 282 ? 7.844   -6.769  12.126  1.00 39.47  ? 282 ALA A O     1 
ATOM   2193 C  CB    . ALA A 1 282 ? 9.418   -7.444  14.661  1.00 41.63  ? 282 ALA A CB    1 
ATOM   2194 N  N     . ALA A 1 283 ? 6.767   -8.603  12.884  1.00 48.46  ? 283 ALA A N     1 
ATOM   2195 C  CA    . ALA A 1 283 ? 5.468   -8.264  12.310  1.00 41.86  ? 283 ALA A CA    1 
ATOM   2196 C  C     . ALA A 1 283 ? 4.533   -7.880  13.453  1.00 33.80  ? 283 ALA A C     1 
ATOM   2197 O  O     . ALA A 1 283 ? 3.961   -8.747  14.119  1.00 30.04  ? 283 ALA A O     1 
ATOM   2198 C  CB    . ALA A 1 283 ? 4.909   -9.426  11.495  1.00 42.09  ? 283 ALA A CB    1 
ATOM   2199 N  N     . PHE A 1 284 ? 4.384   -6.576  13.678  1.00 47.29  ? 284 PHE A N     1 
ATOM   2200 C  CA    . PHE A 1 284 ? 3.500   -6.059  14.706  1.00 49.30  ? 284 PHE A CA    1 
ATOM   2201 C  C     . PHE A 1 284 ? 2.400   -5.215  14.077  1.00 63.87  ? 284 PHE A C     1 
ATOM   2202 O  O     . PHE A 1 284 ? 2.646   -4.517  13.086  1.00 50.01  ? 284 PHE A O     1 
ATOM   2203 C  CB    . PHE A 1 284 ? 4.269   -5.205  15.726  1.00 46.77  ? 284 PHE A CB    1 
ATOM   2204 C  CG    . PHE A 1 284 ? 5.385   -5.934  16.417  1.00 42.12  ? 284 PHE A CG    1 
ATOM   2205 C  CD1   . PHE A 1 284 ? 5.323   -7.304  16.611  1.00 33.73  ? 284 PHE A CD1   1 
ATOM   2206 C  CD2   . PHE A 1 284 ? 6.498   -5.245  16.871  1.00 41.72  ? 284 PHE A CD2   1 
ATOM   2207 C  CE1   . PHE A 1 284 ? 6.353   -7.974  17.248  1.00 45.19  ? 284 PHE A CE1   1 
ATOM   2208 C  CE2   . PHE A 1 284 ? 7.531   -5.908  17.507  1.00 33.43  ? 284 PHE A CE2   1 
ATOM   2209 C  CZ    . PHE A 1 284 ? 7.459   -7.273  17.697  1.00 33.96  ? 284 PHE A CZ    1 
ATOM   2210 N  N     . PRO A 1 285 ? 1.184   -5.256  14.617  1.00 79.54  ? 285 PRO A N     1 
ATOM   2211 C  CA    . PRO A 1 285 ? 0.122   -4.383  14.104  1.00 79.06  ? 285 PRO A CA    1 
ATOM   2212 C  C     . PRO A 1 285 ? 0.489   -2.918  14.277  1.00 84.04  ? 285 PRO A C     1 
ATOM   2213 O  O     . PRO A 1 285 ? 1.493   -2.560  14.897  1.00 86.60  ? 285 PRO A O     1 
ATOM   2214 C  CB    . PRO A 1 285 ? -1.096  -4.762  14.953  1.00 73.96  ? 285 PRO A CB    1 
ATOM   2215 C  CG    . PRO A 1 285 ? -0.793  -6.130  15.465  1.00 79.82  ? 285 PRO A CG    1 
ATOM   2216 C  CD    . PRO A 1 285 ? 0.693   -6.168  15.663  1.00 75.85  ? 285 PRO A CD    1 
ATOM   2217 N  N     . SER A 1 286 ? -0.353  -2.056  13.713  1.00 70.25  ? 286 SER A N     1 
ATOM   2218 C  CA    . SER A 1 286 ? -0.130  -0.621  13.820  1.00 63.20  ? 286 SER A CA    1 
ATOM   2219 C  C     . SER A 1 286 ? -0.222  -0.173  15.273  1.00 62.03  ? 286 SER A C     1 
ATOM   2220 O  O     . SER A 1 286 ? -1.108  -0.599  16.019  1.00 60.06  ? 286 SER A O     1 
ATOM   2221 C  CB    . SER A 1 286 ? -1.146  0.137   12.965  1.00 73.19  ? 286 SER A CB    1 
ATOM   2222 O  OG    . SER A 1 286 ? -1.013  -0.204  11.596  1.00 74.18  ? 286 SER A OG    1 
ATOM   2223 N  N     . ALA A 1 287 ? 0.708   0.694   15.674  1.00 60.57  ? 287 ALA A N     1 
ATOM   2224 C  CA    . ALA A 1 287 ? 0.753   1.214   17.039  1.00 62.15  ? 287 ALA A CA    1 
ATOM   2225 C  C     . ALA A 1 287 ? 0.931   0.082   18.050  1.00 61.62  ? 287 ALA A C     1 
ATOM   2226 O  O     . ALA A 1 287 ? 0.228   0.001   19.059  1.00 65.00  ? 287 ALA A O     1 
ATOM   2227 C  CB    . ALA A 1 287 ? -0.496  2.040   17.351  1.00 70.81  ? 287 ALA A CB    1 
ATOM   2228 N  N     . CYS A 1 288 ? 1.888   -0.805  17.768  1.00 60.98  ? 288 CYS A N     1 
ATOM   2229 C  CA    . CYS A 1 288 ? 2.166   -1.936  18.641  1.00 58.27  ? 288 CYS A CA    1 
ATOM   2230 C  C     . CYS A 1 288 ? 3.635   -2.096  19.008  1.00 55.93  ? 288 CYS A C     1 
ATOM   2231 O  O     . CYS A 1 288 ? 3.945   -2.947  19.851  1.00 54.88  ? 288 CYS A O     1 
ATOM   2232 C  CB    . CYS A 1 288 ? 1.666   -3.243  18.006  1.00 60.01  ? 288 CYS A CB    1 
ATOM   2233 S  SG    . CYS A 1 288 ? -0.136  -3.386  17.938  1.00 61.61  ? 288 CYS A SG    1 
ATOM   2234 N  N     . GLY A 1 289 ? 4.543   -1.326  18.413  1.00 51.93  ? 289 GLY A N     1 
ATOM   2235 C  CA    . GLY A 1 289 ? 5.924   -1.333  18.854  1.00 54.54  ? 289 GLY A CA    1 
ATOM   2236 C  C     . GLY A 1 289 ? 6.962   -1.658  17.798  1.00 54.65  ? 289 GLY A C     1 
ATOM   2237 O  O     . GLY A 1 289 ? 8.050   -2.139  18.131  1.00 54.18  ? 289 GLY A O     1 
ATOM   2238 N  N     . LYS A 1 290 ? 6.654   -1.398  16.526  1.00 40.57  ? 290 LYS A N     1 
ATOM   2239 C  CA    . LYS A 1 290 ? 7.636   -1.655  15.477  1.00 40.90  ? 290 LYS A CA    1 
ATOM   2240 C  C     . LYS A 1 290 ? 8.703   -0.567  15.425  1.00 60.70  ? 290 LYS A C     1 
ATOM   2241 O  O     . LYS A 1 290 ? 9.896   -0.871  15.308  1.00 59.80  ? 290 LYS A O     1 
ATOM   2242 C  CB    . LYS A 1 290 ? 6.946   -1.782  14.117  1.00 52.16  ? 290 LYS A CB    1 
ATOM   2243 C  CG    . LYS A 1 290 ? 6.070   -3.014  13.968  1.00 47.66  ? 290 LYS A CG    1 
ATOM   2244 C  CD    . LYS A 1 290 ? 5.713   -3.260  12.510  1.00 48.83  ? 290 LYS A CD    1 
ATOM   2245 C  CE    . LYS A 1 290 ? 4.986   -2.069  11.905  1.00 51.60  ? 290 LYS A CE    1 
ATOM   2246 N  NZ    . LYS A 1 290 ? 3.688   -1.806  12.587  1.00 53.77  ? 290 LYS A NZ    1 
ATOM   2247 N  N     . THR A 1 291 ? 8.296   0.701   15.513  1.00 46.85  ? 291 THR A N     1 
ATOM   2248 C  CA    . THR A 1 291 ? 9.255   1.794   15.385  1.00 57.88  ? 291 THR A CA    1 
ATOM   2249 C  C     . THR A 1 291 ? 10.191  1.861   16.585  1.00 55.51  ? 291 THR A C     1 
ATOM   2250 O  O     . THR A 1 291 ? 11.406  2.025   16.421  1.00 53.24  ? 291 THR A O     1 
ATOM   2251 C  CB    . THR A 1 291 ? 8.520   3.122   15.206  1.00 60.04  ? 291 THR A CB    1 
ATOM   2252 O  OG1   . THR A 1 291 ? 7.754   3.086   13.996  1.00 45.40  ? 291 THR A OG1   1 
ATOM   2253 C  CG2   . THR A 1 291 ? 9.515   4.274   15.136  1.00 56.16  ? 291 THR A CG2   1 
ATOM   2254 N  N     . ASN A 1 292 ? 9.649   1.741   17.799  1.00 63.58  ? 292 ASN A N     1 
ATOM   2255 C  CA    . ASN A 1 292 ? 10.490  1.785   18.990  1.00 63.86  ? 292 ASN A CA    1 
ATOM   2256 C  C     . ASN A 1 292 ? 11.468  0.620   19.049  1.00 64.23  ? 292 ASN A C     1 
ATOM   2257 O  O     . ASN A 1 292 ? 12.504  0.729   19.715  1.00 64.50  ? 292 ASN A O     1 
ATOM   2258 C  CB    . ASN A 1 292 ? 9.622   1.802   20.250  1.00 57.85  ? 292 ASN A CB    1 
ATOM   2259 C  CG    . ASN A 1 292 ? 8.828   3.085   20.395  1.00 62.58  ? 292 ASN A CG    1 
ATOM   2260 O  OD1   . ASN A 1 292 ? 9.303   4.061   20.975  1.00 71.79  ? 292 ASN A OD1   1 
ATOM   2261 N  ND2   . ASN A 1 292 ? 7.609   3.089   19.868  1.00 69.07  ? 292 ASN A ND2   1 
ATOM   2262 N  N     . LEU A 1 293 ? 11.169  -0.487  18.368  1.00 63.46  ? 293 LEU A N     1 
ATOM   2263 C  CA    . LEU A 1 293 ? 12.055  -1.646  18.403  1.00 51.20  ? 293 LEU A CA    1 
ATOM   2264 C  C     . LEU A 1 293 ? 13.206  -1.504  17.411  1.00 54.51  ? 293 LEU A C     1 
ATOM   2265 O  O     . LEU A 1 293 ? 14.345  -1.870  17.723  1.00 47.19  ? 293 LEU A O     1 
ATOM   2266 C  CB    . LEU A 1 293 ? 11.258  -2.920  18.121  1.00 42.16  ? 293 LEU A CB    1 
ATOM   2267 C  CG    . LEU A 1 293 ? 12.017  -4.247  18.166  1.00 49.91  ? 293 LEU A CG    1 
ATOM   2268 C  CD1   . LEU A 1 293 ? 12.529  -4.532  19.570  1.00 54.97  ? 293 LEU A CD1   1 
ATOM   2269 C  CD2   . LEU A 1 293 ? 11.138  -5.386  17.671  1.00 40.61  ? 293 LEU A CD2   1 
ATOM   2270 N  N     . ALA A 1 294 ? 12.929  -0.974  16.217  1.00 52.12  ? 294 ALA A N     1 
ATOM   2271 C  CA    . ALA A 1 294 ? 13.962  -0.825  15.198  1.00 48.57  ? 294 ALA A CA    1 
ATOM   2272 C  C     . ALA A 1 294 ? 14.960  0.274   15.534  1.00 49.59  ? 294 ALA A C     1 
ATOM   2273 O  O     . ALA A 1 294 ? 16.081  0.258   15.013  1.00 56.19  ? 294 ALA A O     1 
ATOM   2274 C  CB    . ALA A 1 294 ? 13.321  -0.547  13.837  1.00 47.63  ? 294 ALA A CB    1 
ATOM   2275 N  N     . MET A 1 295 ? 14.581  1.228   16.380  1.00 52.00  ? 295 MET A N     1 
ATOM   2276 C  CA    . MET A 1 295 ? 15.461  2.298   16.830  1.00 55.99  ? 295 MET A CA    1 
ATOM   2277 C  C     . MET A 1 295 ? 15.713  2.189   18.328  1.00 55.10  ? 295 MET A C     1 
ATOM   2278 O  O     . MET A 1 295 ? 15.744  3.189   19.049  1.00 57.62  ? 295 MET A O     1 
ATOM   2279 C  CB    . MET A 1 295 ? 14.881  3.667   16.483  1.00 51.99  ? 295 MET A CB    1 
ATOM   2280 C  CG    . MET A 1 295 ? 14.550  3.851   15.014  1.00 56.77  ? 295 MET A CG    1 
ATOM   2281 S  SD    . MET A 1 295 ? 13.793  5.452   14.676  1.00 42.54  ? 295 MET A SD    1 
ATOM   2282 C  CE    . MET A 1 295 ? 13.468  5.310   12.920  1.00 46.12  ? 295 MET A CE    1 
ATOM   2283 N  N     . MET A 1 296 ? 15.903  0.965   18.811  1.00 52.72  ? 296 MET A N     1 
ATOM   2284 C  CA    . MET A 1 296 ? 16.038  0.724   20.239  1.00 56.42  ? 296 MET A CA    1 
ATOM   2285 C  C     . MET A 1 296 ? 17.420  1.127   20.740  1.00 52.55  ? 296 MET A C     1 
ATOM   2286 O  O     . MET A 1 296 ? 18.430  0.934   20.056  1.00 46.48  ? 296 MET A O     1 
ATOM   2287 C  CB    . MET A 1 296 ? 15.780  -0.750  20.553  1.00 55.44  ? 296 MET A CB    1 
ATOM   2288 C  CG    . MET A 1 296 ? 15.962  -1.112  22.018  1.00 50.35  ? 296 MET A CG    1 
ATOM   2289 S  SD    . MET A 1 296 ? 15.728  -2.869  22.346  1.00 48.63  ? 296 MET A SD    1 
ATOM   2290 C  CE    . MET A 1 296 ? 17.026  -3.577  21.336  1.00 50.29  ? 296 MET A CE    1 
ATOM   2291 N  N     . ASN A 1 297 ? 17.455  1.702   21.944  1.00 50.68  ? 297 ASN A N     1 
ATOM   2292 C  CA    . ASN A 1 297 ? 18.688  1.946   22.687  1.00 52.20  ? 297 ASN A CA    1 
ATOM   2293 C  C     . ASN A 1 297 ? 18.771  0.904   23.792  1.00 50.75  ? 297 ASN A C     1 
ATOM   2294 O  O     . ASN A 1 297 ? 18.250  1.119   24.897  1.00 47.87  ? 297 ASN A O     1 
ATOM   2295 C  CB    . ASN A 1 297 ? 18.723  3.362   23.268  1.00 55.11  ? 297 ASN A CB    1 
ATOM   2296 C  CG    . ASN A 1 297 ? 20.091  3.734   23.815  1.00 50.08  ? 297 ASN A CG    1 
ATOM   2297 O  OD1   . ASN A 1 297 ? 21.118  3.308   23.288  1.00 51.96  ? 297 ASN A OD1   1 
ATOM   2298 N  ND2   . ASN A 1 297 ? 20.108  4.526   24.881  1.00 58.89  ? 297 ASN A ND2   1 
ATOM   2299 N  N     . PRO A 1 298 ? 19.406  -0.241  23.548  1.00 46.58  ? 298 PRO A N     1 
ATOM   2300 C  CA    . PRO A 1 298 ? 19.380  -1.325  24.535  1.00 51.76  ? 298 PRO A CA    1 
ATOM   2301 C  C     . PRO A 1 298 ? 20.059  -0.930  25.838  1.00 45.80  ? 298 PRO A C     1 
ATOM   2302 O  O     . PRO A 1 298 ? 20.897  -0.027  25.893  1.00 59.28  ? 298 PRO A O     1 
ATOM   2303 C  CB    . PRO A 1 298 ? 20.133  -2.463  23.836  1.00 50.59  ? 298 PRO A CB    1 
ATOM   2304 C  CG    . PRO A 1 298 ? 20.990  -1.782  22.824  1.00 50.94  ? 298 PRO A CG    1 
ATOM   2305 C  CD    . PRO A 1 298 ? 20.207  -0.589  22.363  1.00 45.08  ? 298 PRO A CD    1 
ATOM   2306 N  N     . THR A 1 299 ? 19.677  -1.633  26.903  1.00 52.03  ? 299 THR A N     1 
ATOM   2307 C  CA    . THR A 1 299 ? 20.229  -1.421  28.232  1.00 42.00  ? 299 THR A CA    1 
ATOM   2308 C  C     . THR A 1 299 ? 21.289  -2.453  28.597  1.00 54.21  ? 299 THR A C     1 
ATOM   2309 O  O     . THR A 1 299 ? 21.733  -2.491  29.749  1.00 58.90  ? 299 THR A O     1 
ATOM   2310 C  CB    . THR A 1 299 ? 19.111  -1.432  29.277  1.00 46.79  ? 299 THR A CB    1 
ATOM   2311 O  OG1   . THR A 1 299 ? 18.442  -2.699  29.252  1.00 53.38  ? 299 THR A OG1   1 
ATOM   2312 C  CG2   . THR A 1 299 ? 18.104  -0.329  28.987  1.00 57.35  ? 299 THR A CG2   1 
ATOM   2313 N  N     . LEU A 1 300 ? 21.700  -3.297  27.643  1.00 51.29  ? 300 LEU A N     1 
ATOM   2314 C  CA    . LEU A 1 300 ? 22.744  -4.283  27.893  1.00 49.86  ? 300 LEU A CA    1 
ATOM   2315 C  C     . LEU A 1 300 ? 24.048  -3.830  27.261  1.00 55.97  ? 300 LEU A C     1 
ATOM   2316 O  O     . LEU A 1 300 ? 24.058  -3.455  26.079  1.00 46.96  ? 300 LEU A O     1 
ATOM   2317 C  CB    . LEU A 1 300 ? 22.347  -5.647  27.333  1.00 46.40  ? 300 LEU A CB    1 
ATOM   2318 C  CG    . LEU A 1 300 ? 21.160  -6.349  27.995  1.00 55.57  ? 300 LEU A CG    1 
ATOM   2319 C  CD1   . LEU A 1 300 ? 20.964  -7.738  27.406  1.00 61.74  ? 300 LEU A CD1   1 
ATOM   2320 C  CD2   . LEU A 1 300 ? 21.351  -6.422  29.501  1.00 51.52  ? 300 LEU A CD2   1 
ATOM   2321 N  N     . PRO A 1 301 ? 25.157  -3.845  27.998  1.00 44.82  ? 301 PRO A N     1 
ATOM   2322 C  CA    . PRO A 1 301 ? 26.433  -3.427  27.409  1.00 45.78  ? 301 PRO A CA    1 
ATOM   2323 C  C     . PRO A 1 301 ? 26.945  -4.458  26.416  1.00 45.82  ? 301 PRO A C     1 
ATOM   2324 O  O     . PRO A 1 301 ? 26.775  -5.665  26.600  1.00 61.86  ? 301 PRO A O     1 
ATOM   2325 C  CB    . PRO A 1 301 ? 27.361  -3.309  28.623  1.00 65.30  ? 301 PRO A CB    1 
ATOM   2326 C  CG    . PRO A 1 301 ? 26.789  -4.269  29.614  1.00 60.21  ? 301 PRO A CG    1 
ATOM   2327 C  CD    . PRO A 1 301 ? 25.296  -4.229  29.414  1.00 57.48  ? 301 PRO A CD    1 
ATOM   2328 N  N     . GLY A 1 302 ? 27.579  -3.966  25.353  1.00 58.49  ? 302 GLY A N     1 
ATOM   2329 C  CA    . GLY A 1 302 ? 28.125  -4.823  24.324  1.00 63.21  ? 302 GLY A CA    1 
ATOM   2330 C  C     . GLY A 1 302 ? 27.168  -5.191  23.212  1.00 63.13  ? 302 GLY A C     1 
ATOM   2331 O  O     . GLY A 1 302 ? 27.568  -5.912  22.288  1.00 65.43  ? 302 GLY A O     1 
ATOM   2332 N  N     . TRP A 1 303 ? 25.923  -4.728  23.267  1.00 51.50  ? 303 TRP A N     1 
ATOM   2333 C  CA    . TRP A 1 303 ? 24.933  -4.995  22.234  1.00 52.67  ? 303 TRP A CA    1 
ATOM   2334 C  C     . TRP A 1 303 ? 24.661  -3.724  21.441  1.00 52.11  ? 303 TRP A C     1 
ATOM   2335 O  O     . TRP A 1 303 ? 24.584  -2.630  22.009  1.00 49.59  ? 303 TRP A O     1 
ATOM   2336 C  CB    . TRP A 1 303 ? 23.631  -5.523  22.842  1.00 56.37  ? 303 TRP A CB    1 
ATOM   2337 C  CG    . TRP A 1 303 ? 23.760  -6.891  23.442  1.00 52.66  ? 303 TRP A CG    1 
ATOM   2338 C  CD1   . TRP A 1 303 ? 24.133  -7.196  24.719  1.00 56.03  ? 303 TRP A CD1   1 
ATOM   2339 C  CD2   . TRP A 1 303 ? 23.512  -8.142  22.787  1.00 54.16  ? 303 TRP A CD2   1 
ATOM   2340 N  NE1   . TRP A 1 303 ? 24.134  -8.558  24.900  1.00 52.65  ? 303 TRP A NE1   1 
ATOM   2341 C  CE2   . TRP A 1 303 ? 23.757  -9.162  23.729  1.00 59.94  ? 303 TRP A CE2   1 
ATOM   2342 C  CE3   . TRP A 1 303 ? 23.108  -8.498  21.497  1.00 53.89  ? 303 TRP A CE3   1 
ATOM   2343 C  CZ2   . TRP A 1 303 ? 23.611  -10.513 23.420  1.00 58.68  ? 303 TRP A CZ2   1 
ATOM   2344 C  CZ3   . TRP A 1 303 ? 22.964  -9.840  21.193  1.00 54.03  ? 303 TRP A CZ3   1 
ATOM   2345 C  CH2   . TRP A 1 303 ? 23.214  -10.831 22.150  1.00 47.77  ? 303 TRP A CH2   1 
ATOM   2346 N  N     . LYS A 1 304 ? 24.518  -3.874  20.126  1.00 53.35  ? 304 LYS A N     1 
ATOM   2347 C  CA    . LYS A 1 304 ? 24.289  -2.752  19.226  1.00 56.30  ? 304 LYS A CA    1 
ATOM   2348 C  C     . LYS A 1 304 ? 23.165  -3.108  18.266  1.00 51.25  ? 304 LYS A C     1 
ATOM   2349 O  O     . LYS A 1 304 ? 23.234  -4.131  17.577  1.00 47.32  ? 304 LYS A O     1 
ATOM   2350 C  CB    . LYS A 1 304 ? 25.562  -2.397  18.451  1.00 47.45  ? 304 LYS A CB    1 
ATOM   2351 C  CG    . LYS A 1 304 ? 25.436  -1.167  17.569  1.00 53.88  ? 304 LYS A CG    1 
ATOM   2352 C  CD    . LYS A 1 304 ? 26.742  -0.876  16.848  1.00 74.61  ? 304 LYS A CD    1 
ATOM   2353 C  CE    . LYS A 1 304 ? 26.631  0.364   15.976  1.00 80.95  ? 304 LYS A CE    1 
ATOM   2354 N  NZ    . LYS A 1 304 ? 27.898  0.639   15.243  1.00 77.31  ? 304 LYS A NZ    1 
ATOM   2355 N  N     . VAL A 1 305 ? 22.137  -2.265  18.221  1.00 58.74  ? 305 VAL A N     1 
ATOM   2356 C  CA    . VAL A 1 305 ? 20.973  -2.473  17.366  1.00 53.49  ? 305 VAL A CA    1 
ATOM   2357 C  C     . VAL A 1 305 ? 20.932  -1.349  16.341  1.00 55.87  ? 305 VAL A C     1 
ATOM   2358 O  O     . VAL A 1 305 ? 20.921  -0.167  16.707  1.00 60.11  ? 305 VAL A O     1 
ATOM   2359 C  CB    . VAL A 1 305 ? 19.669  -2.523  18.177  1.00 56.49  ? 305 VAL A CB    1 
ATOM   2360 C  CG1   . VAL A 1 305 ? 18.473  -2.668  17.248  1.00 55.61  ? 305 VAL A CG1   1 
ATOM   2361 C  CG2   . VAL A 1 305 ? 19.712  -3.664  19.180  1.00 54.04  ? 305 VAL A CG2   1 
ATOM   2362 N  N     . GLU A 1 306 ? 20.907  -1.717  15.063  1.00 61.53  ? 306 GLU A N     1 
ATOM   2363 C  CA    . GLU A 1 306 ? 20.823  -0.766  13.967  1.00 64.29  ? 306 GLU A CA    1 
ATOM   2364 C  C     . GLU A 1 306 ? 19.516  -0.970  13.212  1.00 60.83  ? 306 GLU A C     1 
ATOM   2365 O  O     . GLU A 1 306 ? 18.913  -2.046  13.250  1.00 65.65  ? 306 GLU A O     1 
ATOM   2366 C  CB    . GLU A 1 306 ? 22.022  -0.906  13.020  1.00 64.93  ? 306 GLU A CB    1 
ATOM   2367 C  CG    . GLU A 1 306 ? 23.353  -0.561  13.671  1.00 65.63  ? 306 GLU A CG    1 
ATOM   2368 C  CD    . GLU A 1 306 ? 24.541  -0.862  12.780  1.00 76.36  ? 306 GLU A CD    1 
ATOM   2369 O  OE1   . GLU A 1 306 ? 24.395  -1.679  11.846  1.00 80.57  ? 306 GLU A OE1   1 
ATOM   2370 O  OE2   . GLU A 1 306 ? 25.622  -0.282  13.014  1.00 77.25  ? 306 GLU A OE2   1 
ATOM   2371 N  N     . CYS A 1 307 ? 19.080  0.081   12.523  1.00 51.71  ? 307 CYS A N     1 
ATOM   2372 C  CA    . CYS A 1 307 ? 17.773  0.113   11.883  1.00 52.03  ? 307 CYS A CA    1 
ATOM   2373 C  C     . CYS A 1 307 ? 17.908  0.027   10.369  1.00 55.79  ? 307 CYS A C     1 
ATOM   2374 O  O     . CYS A 1 307 ? 18.783  0.664   9.774   1.00 50.94  ? 307 CYS A O     1 
ATOM   2375 C  CB    . CYS A 1 307 ? 17.014  1.388   12.261  1.00 56.82  ? 307 CYS A CB    1 
ATOM   2376 S  SG    . CYS A 1 307 ? 15.360  1.509   11.544  1.00 57.78  ? 307 CYS A SG    1 
ATOM   2377 N  N     . VAL A 1 308 ? 17.030  -0.766  9.751   1.00 48.61  ? 308 VAL A N     1 
ATOM   2378 C  CA    . VAL A 1 308 ? 16.933  -0.863  8.303   1.00 51.99  ? 308 VAL A CA    1 
ATOM   2379 C  C     . VAL A 1 308 ? 15.554  -0.453  7.804   1.00 54.30  ? 308 VAL A C     1 
ATOM   2380 O  O     . VAL A 1 308 ? 15.429  0.155   6.735   1.00 51.81  ? 308 VAL A O     1 
ATOM   2381 C  CB    . VAL A 1 308 ? 17.283  -2.285  7.814   1.00 55.29  ? 308 VAL A CB    1 
ATOM   2382 C  CG1   . VAL A 1 308 ? 17.297  -2.336  6.294   1.00 45.78  ? 308 VAL A CG1   1 
ATOM   2383 C  CG2   . VAL A 1 308 ? 18.620  -2.732  8.385   1.00 46.26  ? 308 VAL A CG2   1 
ATOM   2384 N  N     . GLY A 1 309 ? 14.508  -0.773  8.562   1.00 51.71  ? 309 GLY A N     1 
ATOM   2385 C  CA    . GLY A 1 309 ? 13.155  -0.390  8.210   1.00 39.03  ? 309 GLY A CA    1 
ATOM   2386 C  C     . GLY A 1 309 ? 12.246  -0.542  9.406   1.00 41.02  ? 309 GLY A C     1 
ATOM   2387 O  O     . GLY A 1 309 ? 12.575  -1.232  10.377  1.00 50.73  ? 309 GLY A O     1 
ATOM   2388 N  N     . ASP A 1 310 ? 11.086  0.114   9.330   1.00 34.88  ? 310 ASP A N     1 
ATOM   2389 C  CA    . ASP A 1 310 ? 10.130  0.089   10.430  1.00 37.96  ? 310 ASP A CA    1 
ATOM   2390 C  C     . ASP A 1 310 ? 8.708   -0.229  9.981   1.00 48.12  ? 310 ASP A C     1 
ATOM   2391 O  O     . ASP A 1 310 ? 7.785   -0.145  10.799  1.00 51.34  ? 310 ASP A O     1 
ATOM   2392 C  CB    . ASP A 1 310 ? 10.139  1.426   11.183  1.00 46.55  ? 310 ASP A CB    1 
ATOM   2393 C  CG    . ASP A 1 310 ? 9.465   2.539   10.404  1.00 46.98  ? 310 ASP A CG    1 
ATOM   2394 O  OD1   . ASP A 1 310 ? 9.643   2.596   9.169   1.00 39.03  ? 310 ASP A OD1   1 
ATOM   2395 O  OD2   . ASP A 1 310 ? 8.750   3.353   11.026  1.00 47.07  ? 310 ASP A OD2   1 
ATOM   2396 N  N     . ASP A 1 311 ? 8.501   -0.595  8.717   1.00 46.81  ? 311 ASP A N     1 
ATOM   2397 C  CA    . ASP A 1 311 ? 7.143   -0.826  8.238   1.00 49.43  ? 311 ASP A CA    1 
ATOM   2398 C  C     . ASP A 1 311 ? 7.098   -1.865  7.124   1.00 44.81  ? 311 ASP A C     1 
ATOM   2399 O  O     . ASP A 1 311 ? 6.592   -2.974  7.325   1.00 47.29  ? 311 ASP A O     1 
ATOM   2400 C  CB    . ASP A 1 311 ? 6.524   0.490   7.764   1.00 47.54  ? 311 ASP A CB    1 
ATOM   2401 C  CG    . ASP A 1 311 ? 5.020   0.407   7.625   1.00 54.53  ? 311 ASP A CG    1 
ATOM   2402 O  OD1   . ASP A 1 311 ? 4.347   0.115   8.636   1.00 56.37  ? 311 ASP A OD1   1 
ATOM   2403 O  OD2   . ASP A 1 311 ? 4.511   0.637   6.509   1.00 59.12  ? 311 ASP A OD2   1 
ATOM   2404 N  N     . ILE A 1 312 ? 7.616   -1.521  5.950   1.00 47.49  ? 312 ILE A N     1 
ATOM   2405 C  CA    . ILE A 1 312 ? 7.545   -2.395  4.785   1.00 50.87  ? 312 ILE A CA    1 
ATOM   2406 C  C     . ILE A 1 312 ? 8.783   -3.279  4.741   1.00 63.82  ? 312 ILE A C     1 
ATOM   2407 O  O     . ILE A 1 312 ? 9.869   -2.894  5.189   1.00 51.00  ? 312 ILE A O     1 
ATOM   2408 C  CB    . ILE A 1 312 ? 7.395   -1.577  3.485   1.00 59.36  ? 312 ILE A CB    1 
ATOM   2409 C  CG1   . ILE A 1 312 ? 6.281   -0.539  3.631   1.00 53.55  ? 312 ILE A CG1   1 
ATOM   2410 C  CG2   . ILE A 1 312 ? 7.112   -2.498  2.307   1.00 51.28  ? 312 ILE A CG2   1 
ATOM   2411 C  CD1   . ILE A 1 312 ? 4.921   -1.135  3.912   1.00 45.69  ? 312 ILE A CD1   1 
ATOM   2412 N  N     . ALA A 1 313 ? 8.619   -4.479  4.188   1.00 54.57  ? 313 ALA A N     1 
ATOM   2413 C  CA    . ALA A 1 313 ? 9.721   -5.427  4.062   1.00 55.57  ? 313 ALA A CA    1 
ATOM   2414 C  C     . ALA A 1 313 ? 9.454   -6.336  2.874   1.00 53.40  ? 313 ALA A C     1 
ATOM   2415 O  O     . ALA A 1 313 ? 8.435   -7.033  2.844   1.00 48.59  ? 313 ALA A O     1 
ATOM   2416 C  CB    . ALA A 1 313 ? 9.892   -6.248  5.342   1.00 50.10  ? 313 ALA A CB    1 
ATOM   2417 N  N     . TRP A 1 314 ? 10.362  -6.326  1.902   1.00 51.09  ? 314 TRP A N     1 
ATOM   2418 C  CA    . TRP A 1 314 ? 10.288  -7.193  0.732   1.00 56.76  ? 314 TRP A CA    1 
ATOM   2419 C  C     . TRP A 1 314 ? 11.386  -8.243  0.839   1.00 62.57  ? 314 TRP A C     1 
ATOM   2420 O  O     . TRP A 1 314 ? 12.572  -7.900  0.901   1.00 69.49  ? 314 TRP A O     1 
ATOM   2421 C  CB    . TRP A 1 314 ? 10.430  -6.390  -0.562  1.00 62.71  ? 314 TRP A CB    1 
ATOM   2422 C  CG    . TRP A 1 314 ? 9.281   -5.461  -0.830  1.00 53.58  ? 314 TRP A CG    1 
ATOM   2423 C  CD1   . TRP A 1 314 ? 8.211   -5.223  -0.017  1.00 48.98  ? 314 TRP A CD1   1 
ATOM   2424 C  CD2   . TRP A 1 314 ? 9.086   -4.652  -1.996  1.00 46.05  ? 314 TRP A CD2   1 
ATOM   2425 N  NE1   . TRP A 1 314 ? 7.364   -4.313  -0.603  1.00 57.45  ? 314 TRP A NE1   1 
ATOM   2426 C  CE2   . TRP A 1 314 ? 7.878   -3.948  -1.819  1.00 52.42  ? 314 TRP A CE2   1 
ATOM   2427 C  CE3   . TRP A 1 314 ? 9.815   -4.454  -3.173  1.00 52.87  ? 314 TRP A CE3   1 
ATOM   2428 C  CZ2   . TRP A 1 314 ? 7.384   -3.061  -2.773  1.00 47.73  ? 314 TRP A CZ2   1 
ATOM   2429 C  CZ3   . TRP A 1 314 ? 9.322   -3.572  -4.119  1.00 58.03  ? 314 TRP A CZ3   1 
ATOM   2430 C  CH2   . TRP A 1 314 ? 8.119   -2.887  -3.913  1.00 51.79  ? 314 TRP A CH2   1 
ATOM   2431 N  N     . MET A 1 315 ? 10.993  -9.513  0.862   1.00 62.70  ? 315 MET A N     1 
ATOM   2432 C  CA    . MET A 1 315 ? 11.921  -10.616 1.054   1.00 61.51  ? 315 MET A CA    1 
ATOM   2433 C  C     . MET A 1 315 ? 11.833  -11.591 -0.113  1.00 61.72  ? 315 MET A C     1 
ATOM   2434 O  O     . MET A 1 315 ? 10.828  -11.655 -0.827  1.00 64.81  ? 315 MET A O     1 
ATOM   2435 C  CB    . MET A 1 315 ? 11.641  -11.352 2.370   1.00 59.16  ? 315 MET A CB    1 
ATOM   2436 C  CG    . MET A 1 315 ? 11.617  -10.450 3.592   1.00 46.51  ? 315 MET A CG    1 
ATOM   2437 S  SD    . MET A 1 315 ? 11.270  -11.356 5.112   1.00 52.33  ? 315 MET A SD    1 
ATOM   2438 C  CE    . MET A 1 315 ? 9.706   -12.124 4.699   1.00 58.21  ? 315 MET A CE    1 
ATOM   2439 N  N     . LYS A 1 316 ? 12.906  -12.358 -0.294  1.00 69.41  ? 316 LYS A N     1 
ATOM   2440 C  CA    . LYS A 1 316 ? 12.988  -13.344 -1.362  1.00 75.34  ? 316 LYS A CA    1 
ATOM   2441 C  C     . LYS A 1 316 ? 14.268  -14.146 -1.187  1.00 75.71  ? 316 LYS A C     1 
ATOM   2442 O  O     . LYS A 1 316 ? 15.292  -13.614 -0.748  1.00 76.89  ? 316 LYS A O     1 
ATOM   2443 C  CB    . LYS A 1 316 ? 12.958  -12.680 -2.745  1.00 79.26  ? 316 LYS A CB    1 
ATOM   2444 C  CG    . LYS A 1 316 ? 13.008  -13.660 -3.907  1.00 80.93  ? 316 LYS A CG    1 
ATOM   2445 C  CD    . LYS A 1 316 ? 13.011  -12.933 -5.242  1.00 83.01  ? 316 LYS A CD    1 
ATOM   2446 C  CE    . LYS A 1 316 ? 14.235  -12.043 -5.383  1.00 95.35  ? 316 LYS A CE    1 
ATOM   2447 N  NZ    . LYS A 1 316 ? 15.500  -12.824 -5.292  1.00 92.11  ? 316 LYS A NZ    1 
ATOM   2448 N  N     . PHE A 1 317 ? 14.198  -15.429 -1.532  1.00 79.69  ? 317 PHE A N     1 
ATOM   2449 C  CA    . PHE A 1 317 ? 15.359  -16.297 -1.422  1.00 85.01  ? 317 PHE A CA    1 
ATOM   2450 C  C     . PHE A 1 317 ? 16.407  -15.932 -2.471  1.00 88.09  ? 317 PHE A C     1 
ATOM   2451 O  O     . PHE A 1 317 ? 16.115  -15.301 -3.491  1.00 93.36  ? 317 PHE A O     1 
ATOM   2452 C  CB    . PHE A 1 317 ? 14.953  -17.763 -1.577  1.00 87.84  ? 317 PHE A CB    1 
ATOM   2453 C  CG    . PHE A 1 317 ? 14.176  -18.304 -0.411  1.00 86.74  ? 317 PHE A CG    1 
ATOM   2454 C  CD1   . PHE A 1 317 ? 12.800  -18.160 -0.350  1.00 89.19  ? 317 PHE A CD1   1 
ATOM   2455 C  CD2   . PHE A 1 317 ? 14.822  -18.960 0.623   1.00 80.50  ? 317 PHE A CD2   1 
ATOM   2456 C  CE1   . PHE A 1 317 ? 12.085  -18.658 0.722   1.00 79.79  ? 317 PHE A CE1   1 
ATOM   2457 C  CE2   . PHE A 1 317 ? 14.113  -19.460 1.697   1.00 73.97  ? 317 PHE A CE2   1 
ATOM   2458 C  CZ    . PHE A 1 317 ? 12.742  -19.309 1.747   1.00 74.43  ? 317 PHE A CZ    1 
ATOM   2459 N  N     . ASP A 1 318 ? 17.643  -16.338 -2.206  1.00 87.50  ? 318 ASP A N     1 
ATOM   2460 C  CA    . ASP A 1 318 ? 18.761  -16.100 -3.107  1.00 96.21  ? 318 ASP A CA    1 
ATOM   2461 C  C     . ASP A 1 318 ? 19.286  -17.439 -3.627  1.00 98.91  ? 318 ASP A C     1 
ATOM   2462 O  O     . ASP A 1 318 ? 18.716  -18.501 -3.360  1.00 92.87  ? 318 ASP A O     1 
ATOM   2463 C  CB    . ASP A 1 318 ? 19.858  -15.293 -2.406  1.00 98.40  ? 318 ASP A CB    1 
ATOM   2464 C  CG    . ASP A 1 318 ? 20.605  -16.104 -1.365  1.00 94.34  ? 318 ASP A CG    1 
ATOM   2465 O  OD1   . ASP A 1 318 ? 20.001  -17.026 -0.778  1.00 96.34  ? 318 ASP A OD1   1 
ATOM   2466 O  OD2   . ASP A 1 318 ? 21.799  -15.818 -1.135  1.00 93.14  ? 318 ASP A OD2   1 
ATOM   2467 N  N     . ALA A 1 319 ? 20.390  -17.379 -4.375  1.00 103.41 ? 319 ALA A N     1 
ATOM   2468 C  CA    . ALA A 1 319 ? 20.946  -18.592 -4.966  1.00 107.55 ? 319 ALA A CA    1 
ATOM   2469 C  C     . ALA A 1 319 ? 21.522  -19.526 -3.910  1.00 104.59 ? 319 ALA A C     1 
ATOM   2470 O  O     . ALA A 1 319 ? 21.571  -20.743 -4.124  1.00 99.66  ? 319 ALA A O     1 
ATOM   2471 C  CB    . ALA A 1 319 ? 22.017  -18.231 -5.995  1.00 111.29 ? 319 ALA A CB    1 
ATOM   2472 N  N     . GLN A 1 320 ? 21.958  -18.987 -2.775  1.00 106.21 ? 320 GLN A N     1 
ATOM   2473 C  CA    . GLN A 1 320 ? 22.579  -19.783 -1.725  1.00 96.86  ? 320 GLN A CA    1 
ATOM   2474 C  C     . GLN A 1 320 ? 21.576  -20.328 -0.717  1.00 94.88  ? 320 GLN A C     1 
ATOM   2475 O  O     . GLN A 1 320 ? 21.971  -21.072 0.186   1.00 92.21  ? 320 GLN A O     1 
ATOM   2476 C  CB    . GLN A 1 320 ? 23.641  -18.952 -0.998  1.00 98.77  ? 320 GLN A CB    1 
ATOM   2477 C  CG    . GLN A 1 320 ? 24.547  -18.160 -1.928  1.00 103.16 ? 320 GLN A CG    1 
ATOM   2478 C  CD    . GLN A 1 320 ? 25.247  -19.035 -2.950  1.00 104.45 ? 320 GLN A CD    1 
ATOM   2479 O  OE1   . GLN A 1 320 ? 25.512  -20.211 -2.702  1.00 99.47  ? 320 GLN A OE1   1 
ATOM   2480 N  NE2   . GLN A 1 320 ? 25.546  -18.463 -4.112  1.00 104.68 ? 320 GLN A NE2   1 
ATOM   2481 N  N     . GLY A 1 321 ? 20.299  -19.980 -0.845  1.00 96.47  ? 321 GLY A N     1 
ATOM   2482 C  CA    . GLY A 1 321 ? 19.287  -20.465 0.070   1.00 94.21  ? 321 GLY A CA    1 
ATOM   2483 C  C     . GLY A 1 321 ? 18.985  -19.559 1.240   1.00 90.71  ? 321 GLY A C     1 
ATOM   2484 O  O     . GLY A 1 321 ? 18.408  -20.025 2.229   1.00 91.12  ? 321 GLY A O     1 
ATOM   2485 N  N     . ASN A 1 322 ? 19.352  -18.284 1.164   1.00 93.63  ? 322 ASN A N     1 
ATOM   2486 C  CA    . ASN A 1 322 ? 19.100  -17.332 2.235   1.00 86.68  ? 322 ASN A CA    1 
ATOM   2487 C  C     . ASN A 1 322 ? 17.895  -16.463 1.896   1.00 79.67  ? 322 ASN A C     1 
ATOM   2488 O  O     . ASN A 1 322 ? 17.595  -16.212 0.726   1.00 84.48  ? 322 ASN A O     1 
ATOM   2489 C  CB    . ASN A 1 322 ? 20.325  -16.448 2.482   1.00 82.65  ? 322 ASN A CB    1 
ATOM   2490 C  CG    . ASN A 1 322 ? 21.596  -17.253 2.672   1.00 92.52  ? 322 ASN A CG    1 
ATOM   2491 O  OD1   . ASN A 1 322 ? 21.861  -17.771 3.757   1.00 101.57 ? 322 ASN A OD1   1 
ATOM   2492 N  ND2   . ASN A 1 322 ? 22.392  -17.358 1.614   1.00 92.99  ? 322 ASN A ND2   1 
ATOM   2493 N  N     . LEU A 1 323 ? 17.204  -16.006 2.938   1.00 71.54  ? 323 LEU A N     1 
ATOM   2494 C  CA    . LEU A 1 323 ? 16.033  -15.144 2.791   1.00 63.57  ? 323 LEU A CA    1 
ATOM   2495 C  C     . LEU A 1 323 ? 16.494  -13.703 2.985   1.00 75.15  ? 323 LEU A C     1 
ATOM   2496 O  O     . LEU A 1 323 ? 16.555  -13.195 4.106   1.00 68.59  ? 323 LEU A O     1 
ATOM   2497 C  CB    . LEU A 1 323 ? 14.942  -15.532 3.783   1.00 60.96  ? 323 LEU A CB    1 
ATOM   2498 C  CG    . LEU A 1 323 ? 13.597  -14.818 3.633   1.00 63.08  ? 323 LEU A CG    1 
ATOM   2499 C  CD1   . LEU A 1 323 ? 13.000  -15.081 2.259   1.00 63.57  ? 323 LEU A CD1   1 
ATOM   2500 C  CD2   . LEU A 1 323 ? 12.636  -15.247 4.731   1.00 50.58  ? 323 LEU A CD2   1 
ATOM   2501 N  N     . ARG A 1 324 ? 16.826  -13.044 1.880   1.00 64.73  ? 324 ARG A N     1 
ATOM   2502 C  CA    . ARG A 1 324 ? 17.289  -11.666 1.913   1.00 67.52  ? 324 ARG A CA    1 
ATOM   2503 C  C     . ARG A 1 324 ? 16.111  -10.703 1.835   1.00 63.54  ? 324 ARG A C     1 
ATOM   2504 O  O     . ARG A 1 324 ? 15.101  -10.976 1.181   1.00 65.42  ? 324 ARG A O     1 
ATOM   2505 C  CB    . ARG A 1 324 ? 18.267  -11.396 0.768   1.00 76.23  ? 324 ARG A CB    1 
ATOM   2506 C  CG    . ARG A 1 324 ? 19.559  -12.191 0.865   1.00 82.53  ? 324 ARG A CG    1 
ATOM   2507 C  CD    . ARG A 1 324 ? 20.544  -11.791 -0.220  1.00 97.30  ? 324 ARG A CD    1 
ATOM   2508 N  NE    . ARG A 1 324 ? 21.827  -12.465 -0.063  1.00 100.26 ? 324 ARG A NE    1 
ATOM   2509 C  CZ    . ARG A 1 324 ? 22.831  -12.001 0.669   1.00 96.39  ? 324 ARG A CZ    1 
ATOM   2510 N  NH1   . ARG A 1 324 ? 22.736  -10.857 1.327   1.00 90.35  ? 324 ARG A NH1   1 
ATOM   2511 N  NH2   . ARG A 1 324 ? 23.958  -12.703 0.743   1.00 99.73  ? 324 ARG A NH2   1 
ATOM   2512 N  N     . ALA A 1 325 ? 16.251  -9.566  2.514   1.00 62.38  ? 325 ALA A N     1 
ATOM   2513 C  CA    . ALA A 1 325 ? 15.185  -8.581  2.601   1.00 55.01  ? 325 ALA A CA    1 
ATOM   2514 C  C     . ALA A 1 325 ? 15.752  -7.185  2.391   1.00 69.67  ? 325 ALA A C     1 
ATOM   2515 O  O     . ALA A 1 325 ? 16.934  -6.931  2.641   1.00 56.67  ? 325 ALA A O     1 
ATOM   2516 C  CB    . ALA A 1 325 ? 14.462  -8.653  3.953   1.00 49.60  ? 325 ALA A CB    1 
ATOM   2517 N  N     . ILE A 1 326 ? 14.890  -6.279  1.926   1.00 60.70  ? 326 ILE A N     1 
ATOM   2518 C  CA    . ILE A 1 326 ? 15.249  -4.885  1.707   1.00 54.21  ? 326 ILE A CA    1 
ATOM   2519 C  C     . ILE A 1 326 ? 14.106  -4.004  2.189   1.00 52.78  ? 326 ILE A C     1 
ATOM   2520 O  O     . ILE A 1 326 ? 12.963  -4.445  2.325   1.00 54.68  ? 326 ILE A O     1 
ATOM   2521 C  CB    . ILE A 1 326 ? 15.558  -4.576  0.224   1.00 54.46  ? 326 ILE A CB    1 
ATOM   2522 C  CG1   . ILE A 1 326 ? 14.283  -4.677  -0.616  1.00 60.76  ? 326 ILE A CG1   1 
ATOM   2523 C  CG2   . ILE A 1 326 ? 16.630  -5.514  -0.306  1.00 67.46  ? 326 ILE A CG2   1 
ATOM   2524 C  CD1   . ILE A 1 326 ? 14.460  -4.235  -2.053  1.00 68.82  ? 326 ILE A CD1   1 
ATOM   2525 N  N     . ASN A 1 327 ? 14.433  -2.739  2.452   1.00 56.07  ? 327 ASN A N     1 
ATOM   2526 C  CA    . ASN A 1 327 ? 13.427  -1.748  2.798   1.00 50.32  ? 327 ASN A CA    1 
ATOM   2527 C  C     . ASN A 1 327 ? 13.157  -0.882  1.580   1.00 51.71  ? 327 ASN A C     1 
ATOM   2528 O  O     . ASN A 1 327 ? 13.993  -0.030  1.242   1.00 60.13  ? 327 ASN A O     1 
ATOM   2529 C  CB    . ASN A 1 327 ? 13.890  -0.887  3.971   1.00 50.41  ? 327 ASN A CB    1 
ATOM   2530 C  CG    . ASN A 1 327 ? 12.925  0.243   4.280   1.00 53.79  ? 327 ASN A CG    1 
ATOM   2531 O  OD1   . ASN A 1 327 ? 11.725  0.137   4.024   1.00 51.30  ? 327 ASN A OD1   1 
ATOM   2532 N  ND2   . ASN A 1 327 ? 13.446  1.335   4.827   1.00 51.77  ? 327 ASN A ND2   1 
ATOM   2533 N  N     . PRO A 1 328 ? 12.025  -1.052  0.890   1.00 53.20  ? 328 PRO A N     1 
ATOM   2534 C  CA    . PRO A 1 328 ? 11.764  -0.250  -0.314  1.00 49.99  ? 328 PRO A CA    1 
ATOM   2535 C  C     . PRO A 1 328 ? 11.455  1.211   -0.032  1.00 49.24  ? 328 PRO A C     1 
ATOM   2536 O  O     . PRO A 1 328 ? 11.273  1.979   -0.985  1.00 60.89  ? 328 PRO A O     1 
ATOM   2537 C  CB    . PRO A 1 328 ? 10.553  -0.956  -0.941  1.00 56.06  ? 328 PRO A CB    1 
ATOM   2538 C  CG    . PRO A 1 328 ? 9.847   -1.567  0.223   1.00 52.50  ? 328 PRO A CG    1 
ATOM   2539 C  CD    . PRO A 1 328 ? 10.928  -1.991  1.182   1.00 49.71  ? 328 PRO A CD    1 
ATOM   2540 N  N     . GLU A 1 329 ? 11.390  1.622   1.230   1.00 52.22  ? 329 GLU A N     1 
ATOM   2541 C  CA    . GLU A 1 329 ? 11.069  2.996   1.580   1.00 47.62  ? 329 GLU A CA    1 
ATOM   2542 C  C     . GLU A 1 329 ? 12.340  3.825   1.750   1.00 46.01  ? 329 GLU A C     1 
ATOM   2543 O  O     . GLU A 1 329 ? 13.459  3.308   1.774   1.00 54.37  ? 329 GLU A O     1 
ATOM   2544 C  CB    . GLU A 1 329 ? 10.223  3.039   2.852   1.00 49.52  ? 329 GLU A CB    1 
ATOM   2545 C  CG    . GLU A 1 329 ? 8.797   2.550   2.657   1.00 47.43  ? 329 GLU A CG    1 
ATOM   2546 C  CD    . GLU A 1 329 ? 7.958   2.675   3.912   1.00 48.27  ? 329 GLU A CD    1 
ATOM   2547 O  OE1   . GLU A 1 329 ? 8.478   2.384   5.009   1.00 60.95  ? 329 GLU A OE1   1 
ATOM   2548 O  OE2   . GLU A 1 329 ? 6.779   3.072   3.801   1.00 53.08  ? 329 GLU A OE2   1 
ATOM   2549 N  N     . ASN A 1 330 ? 12.149  5.140   1.872   1.00 47.49  ? 330 ASN A N     1 
ATOM   2550 C  CA    . ASN A 1 330 ? 13.253  6.081   1.972   1.00 50.05  ? 330 ASN A CA    1 
ATOM   2551 C  C     . ASN A 1 330 ? 13.210  6.949   3.221   1.00 46.83  ? 330 ASN A C     1 
ATOM   2552 O  O     . ASN A 1 330 ? 14.172  7.683   3.473   1.00 37.58  ? 330 ASN A O     1 
ATOM   2553 C  CB    . ASN A 1 330 ? 13.288  6.991   0.733   1.00 43.79  ? 330 ASN A CB    1 
ATOM   2554 C  CG    . ASN A 1 330 ? 14.609  7.715   0.577   1.00 50.67  ? 330 ASN A CG    1 
ATOM   2555 O  OD1   . ASN A 1 330 ? 15.656  7.217   0.992   1.00 57.77  ? 330 ASN A OD1   1 
ATOM   2556 N  ND2   . ASN A 1 330 ? 14.569  8.899   -0.023  1.00 47.04  ? 330 ASN A ND2   1 
ATOM   2557 N  N     . GLY A 1 331 ? 12.137  6.891   4.007   1.00 39.68  ? 331 GLY A N     1 
ATOM   2558 C  CA    . GLY A 1 331 ? 12.037  7.690   5.212   1.00 39.80  ? 331 GLY A CA    1 
ATOM   2559 C  C     . GLY A 1 331 ? 11.274  6.995   6.321   1.00 36.74  ? 331 GLY A C     1 
ATOM   2560 O  O     . GLY A 1 331 ? 11.124  5.770   6.304   1.00 48.31  ? 331 GLY A O     1 
ATOM   2561 N  N     . PHE A 1 332 ? 10.787  7.764   7.292   1.00 35.09  ? 332 PHE A N     1 
ATOM   2562 C  CA    . PHE A 1 332 ? 10.024  7.225   8.409   1.00 37.94  ? 332 PHE A CA    1 
ATOM   2563 C  C     . PHE A 1 332 ? 8.733   8.012   8.572   1.00 40.20  ? 332 PHE A C     1 
ATOM   2564 O  O     . PHE A 1 332 ? 8.712   9.234   8.402   1.00 49.76  ? 332 PHE A O     1 
ATOM   2565 C  CB    . PHE A 1 332 ? 10.831  7.265   9.713   1.00 42.69  ? 332 PHE A CB    1 
ATOM   2566 C  CG    . PHE A 1 332 ? 12.056  6.396   9.694   1.00 41.88  ? 332 PHE A CG    1 
ATOM   2567 C  CD1   . PHE A 1 332 ? 11.942  5.016   9.726   1.00 45.99  ? 332 PHE A CD1   1 
ATOM   2568 C  CD2   . PHE A 1 332 ? 13.321  6.958   9.651   1.00 52.11  ? 332 PHE A CD2   1 
ATOM   2569 C  CE1   . PHE A 1 332 ? 13.067  4.213   9.709   1.00 50.05  ? 332 PHE A CE1   1 
ATOM   2570 C  CE2   . PHE A 1 332 ? 14.449  6.160   9.636   1.00 51.13  ? 332 PHE A CE2   1 
ATOM   2571 C  CZ    . PHE A 1 332 ? 14.321  4.785   9.665   1.00 53.86  ? 332 PHE A CZ    1 
ATOM   2572 N  N     . PHE A 1 333 ? 7.650   7.295   8.909   1.00 50.56  ? 333 PHE A N     1 
ATOM   2573 C  CA    . PHE A 1 333 ? 6.318   7.871   9.064   1.00 40.63  ? 333 PHE A CA    1 
ATOM   2574 C  C     . PHE A 1 333 ? 5.669   7.213   10.287  1.00 45.86  ? 333 PHE A C     1 
ATOM   2575 O  O     . PHE A 1 333 ? 4.701   6.460   10.193  1.00 55.63  ? 333 PHE A O     1 
ATOM   2576 C  CB    . PHE A 1 333 ? 5.481   7.673   7.797   1.00 48.11  ? 333 PHE A CB    1 
ATOM   2577 C  CG    . PHE A 1 333 ? 4.189   8.441   7.790   1.00 43.70  ? 333 PHE A CG    1 
ATOM   2578 C  CD1   . PHE A 1 333 ? 4.164   9.775   7.419   1.00 47.57  ? 333 PHE A CD1   1 
ATOM   2579 C  CD2   . PHE A 1 333 ? 2.998   7.825   8.136   1.00 60.99  ? 333 PHE A CD2   1 
ATOM   2580 C  CE1   . PHE A 1 333 ? 2.978   10.484  7.404   1.00 49.20  ? 333 PHE A CE1   1 
ATOM   2581 C  CE2   . PHE A 1 333 ? 1.807   8.529   8.122   1.00 66.85  ? 333 PHE A CE2   1 
ATOM   2582 C  CZ    . PHE A 1 333 ? 1.798   9.860   7.756   1.00 58.25  ? 333 PHE A CZ    1 
ATOM   2583 N  N     . GLY A 1 334 ? 6.220   7.503   11.467  1.00 49.99  ? 334 GLY A N     1 
ATOM   2584 C  CA    . GLY A 1 334 ? 5.809   6.866   12.697  1.00 55.55  ? 334 GLY A CA    1 
ATOM   2585 C  C     . GLY A 1 334 ? 4.942   7.760   13.573  1.00 43.41  ? 334 GLY A C     1 
ATOM   2586 O  O     . GLY A 1 334 ? 4.807   8.963   13.357  1.00 48.41  ? 334 GLY A O     1 
ATOM   2587 N  N     . VAL A 1 335 ? 4.352   7.129   14.592  1.00 54.56  ? 335 VAL A N     1 
ATOM   2588 C  CA    . VAL A 1 335 ? 3.471   7.840   15.509  1.00 58.74  ? 335 VAL A CA    1 
ATOM   2589 C  C     . VAL A 1 335 ? 4.286   8.801   16.367  1.00 54.82  ? 335 VAL A C     1 
ATOM   2590 O  O     . VAL A 1 335 ? 5.449   8.542   16.705  1.00 49.14  ? 335 VAL A O     1 
ATOM   2591 C  CB    . VAL A 1 335 ? 2.684   6.846   16.383  1.00 58.09  ? 335 VAL A CB    1 
ATOM   2592 C  CG1   . VAL A 1 335 ? 1.579   7.563   17.145  1.00 56.37  ? 335 VAL A CG1   1 
ATOM   2593 C  CG2   . VAL A 1 335 ? 2.114   5.723   15.529  1.00 60.95  ? 335 VAL A CG2   1 
ATOM   2594 N  N     . ALA A 1 336 ? 3.667   9.923   16.730  1.00 57.14  ? 336 ALA A N     1 
ATOM   2595 C  CA    . ALA A 1 336 ? 4.349   10.971  17.478  1.00 51.35  ? 336 ALA A CA    1 
ATOM   2596 C  C     . ALA A 1 336 ? 4.120   10.818  18.978  1.00 54.71  ? 336 ALA A C     1 
ATOM   2597 O  O     . ALA A 1 336 ? 5.088   10.726  19.744  1.00 55.43  ? 336 ALA A O     1 
ATOM   2598 C  CB    . ALA A 1 336 ? 3.884   12.351  17.009  1.00 51.34  ? 336 ALA A CB    1 
ATOM   2599 N  N     . PRO A 1 337 ? 2.868   10.796  19.437  1.00 56.61  ? 337 PRO A N     1 
ATOM   2600 C  CA    . PRO A 1 337 ? 2.617   10.691  20.880  1.00 51.73  ? 337 PRO A CA    1 
ATOM   2601 C  C     . PRO A 1 337 ? 3.316   9.481   21.481  1.00 59.43  ? 337 PRO A C     1 
ATOM   2602 O  O     . PRO A 1 337 ? 3.339   8.396   20.896  1.00 65.47  ? 337 PRO A O     1 
ATOM   2603 C  CB    . PRO A 1 337 ? 1.093   10.563  20.965  1.00 48.78  ? 337 PRO A CB    1 
ATOM   2604 C  CG    . PRO A 1 337 ? 0.595   11.214  19.719  1.00 59.54  ? 337 PRO A CG    1 
ATOM   2605 C  CD    . PRO A 1 337 ? 1.618   10.902  18.666  1.00 60.79  ? 337 PRO A CD    1 
ATOM   2606 N  N     . GLY A 1 338 ? 3.891   9.679   22.667  1.00 56.15  ? 338 GLY A N     1 
ATOM   2607 C  CA    . GLY A 1 338 ? 4.633   8.642   23.346  1.00 55.46  ? 338 GLY A CA    1 
ATOM   2608 C  C     . GLY A 1 338 ? 6.113   8.603   23.032  1.00 56.19  ? 338 GLY A C     1 
ATOM   2609 O  O     . GLY A 1 338 ? 6.861   7.911   23.735  1.00 64.56  ? 338 GLY A O     1 
ATOM   2610 N  N     . THR A 1 339 ? 6.560   9.319   22.002  1.00 53.87  ? 339 THR A N     1 
ATOM   2611 C  CA    . THR A 1 339 ? 7.973   9.358   21.643  1.00 56.47  ? 339 THR A CA    1 
ATOM   2612 C  C     . THR A 1 339 ? 8.688   10.343  22.559  1.00 67.14  ? 339 THR A C     1 
ATOM   2613 O  O     . THR A 1 339 ? 8.474   11.556  22.467  1.00 68.97  ? 339 THR A O     1 
ATOM   2614 C  CB    . THR A 1 339 ? 8.145   9.752   20.178  1.00 54.52  ? 339 THR A CB    1 
ATOM   2615 O  OG1   . THR A 1 339 ? 7.446   8.819   19.345  1.00 59.43  ? 339 THR A OG1   1 
ATOM   2616 C  CG2   . THR A 1 339 ? 9.618   9.758   19.799  1.00 56.30  ? 339 THR A CG2   1 
ATOM   2617 N  N     . SER A 1 340 ? 9.536   9.825   23.444  1.00 70.60  ? 340 SER A N     1 
ATOM   2618 C  CA    . SER A 1 340 ? 10.289  10.638  24.388  1.00 71.84  ? 340 SER A CA    1 
ATOM   2619 C  C     . SER A 1 340 ? 11.755  10.223  24.347  1.00 75.36  ? 340 SER A C     1 
ATOM   2620 O  O     . SER A 1 340 ? 12.144  9.300   23.626  1.00 74.18  ? 340 SER A O     1 
ATOM   2621 C  CB    . SER A 1 340 ? 9.723   10.507  25.808  1.00 82.44  ? 340 SER A CB    1 
ATOM   2622 O  OG    . SER A 1 340 ? 9.841   9.177   26.282  1.00 80.10  ? 340 SER A OG    1 
ATOM   2623 N  N     . VAL A 1 341 ? 12.576  10.919  25.136  1.00 90.51  ? 341 VAL A N     1 
ATOM   2624 C  CA    . VAL A 1 341 ? 13.997  10.595  25.188  1.00 86.95  ? 341 VAL A CA    1 
ATOM   2625 C  C     . VAL A 1 341 ? 14.226  9.295   25.946  1.00 89.08  ? 341 VAL A C     1 
ATOM   2626 O  O     . VAL A 1 341 ? 15.186  8.566   25.667  1.00 90.33  ? 341 VAL A O     1 
ATOM   2627 C  CB    . VAL A 1 341 ? 14.787  11.758  25.816  1.00 97.30  ? 341 VAL A CB    1 
ATOM   2628 C  CG1   . VAL A 1 341 ? 16.280  11.469  25.775  1.00 105.21 ? 341 VAL A CG1   1 
ATOM   2629 C  CG2   . VAL A 1 341 ? 14.467  13.063  25.103  1.00 98.77  ? 341 VAL A CG2   1 
ATOM   2630 N  N     . LYS A 1 342 ? 13.357  8.977   26.908  1.00 81.34  ? 342 LYS A N     1 
ATOM   2631 C  CA    . LYS A 1 342 ? 13.529  7.766   27.701  1.00 83.68  ? 342 LYS A CA    1 
ATOM   2632 C  C     . LYS A 1 342 ? 13.058  6.520   26.963  1.00 74.52  ? 342 LYS A C     1 
ATOM   2633 O  O     . LYS A 1 342 ? 13.601  5.432   27.187  1.00 75.96  ? 342 LYS A O     1 
ATOM   2634 C  CB    . LYS A 1 342 ? 12.782  7.898   29.030  1.00 87.18  ? 342 LYS A CB    1 
ATOM   2635 C  CG    . LYS A 1 342 ? 11.276  8.047   28.881  1.00 92.53  ? 342 LYS A CG    1 
ATOM   2636 C  CD    . LYS A 1 342 ? 10.596  8.165   30.236  1.00 108.59 ? 342 LYS A CD    1 
ATOM   2637 C  CE    . LYS A 1 342 ? 9.086   8.264   30.089  1.00 113.73 ? 342 LYS A CE    1 
ATOM   2638 N  NZ    . LYS A 1 342 ? 8.511   7.056   29.435  1.00 114.63 ? 342 LYS A NZ    1 
ATOM   2639 N  N     . THR A 1 343 ? 12.062  6.652   26.088  1.00 80.86  ? 343 THR A N     1 
ATOM   2640 C  CA    . THR A 1 343 ? 11.518  5.505   25.370  1.00 64.76  ? 343 THR A CA    1 
ATOM   2641 C  C     . THR A 1 343 ? 12.217  5.279   24.034  1.00 65.57  ? 343 THR A C     1 
ATOM   2642 O  O     . THR A 1 343 ? 12.710  4.179   23.767  1.00 63.45  ? 343 THR A O     1 
ATOM   2643 C  CB    . THR A 1 343 ? 10.012  5.685   25.151  1.00 64.17  ? 343 THR A CB    1 
ATOM   2644 O  OG1   . THR A 1 343 ? 9.780   6.832   24.324  1.00 73.21  ? 343 THR A OG1   1 
ATOM   2645 C  CG2   . THR A 1 343 ? 9.299   5.875   26.483  1.00 67.46  ? 343 THR A CG2   1 
ATOM   2646 N  N     . ASN A 1 344 ? 12.271  6.306   23.186  1.00 62.84  ? 344 ASN A N     1 
ATOM   2647 C  CA    . ASN A 1 344 ? 12.869  6.210   21.855  1.00 61.59  ? 344 ASN A CA    1 
ATOM   2648 C  C     . ASN A 1 344 ? 13.819  7.384   21.665  1.00 61.45  ? 344 ASN A C     1 
ATOM   2649 O  O     . ASN A 1 344 ? 13.492  8.363   20.980  1.00 65.58  ? 344 ASN A O     1 
ATOM   2650 C  CB    . ASN A 1 344 ? 11.793  6.184   20.768  1.00 55.22  ? 344 ASN A CB    1 
ATOM   2651 C  CG    . ASN A 1 344 ? 12.335  5.751   19.420  1.00 62.73  ? 344 ASN A CG    1 
ATOM   2652 O  OD1   . ASN A 1 344 ? 13.533  5.850   19.156  1.00 54.13  ? 344 ASN A OD1   1 
ATOM   2653 N  ND2   . ASN A 1 344 ? 11.450  5.268   18.555  1.00 62.63  ? 344 ASN A ND2   1 
ATOM   2654 N  N     . PRO A 1 345 ? 15.014  7.319   22.259  1.00 62.50  ? 345 PRO A N     1 
ATOM   2655 C  CA    . PRO A 1 345 ? 15.954  8.443   22.119  1.00 58.93  ? 345 PRO A CA    1 
ATOM   2656 C  C     . PRO A 1 345 ? 16.508  8.594   20.714  1.00 57.88  ? 345 PRO A C     1 
ATOM   2657 O  O     . PRO A 1 345 ? 16.833  9.716   20.309  1.00 62.16  ? 345 PRO A O     1 
ATOM   2658 C  CB    . PRO A 1 345 ? 17.057  8.102   23.130  1.00 55.48  ? 345 PRO A CB    1 
ATOM   2659 C  CG    . PRO A 1 345 ? 17.008  6.615   23.242  1.00 57.42  ? 345 PRO A CG    1 
ATOM   2660 C  CD    . PRO A 1 345 ? 15.559  6.237   23.096  1.00 67.93  ? 345 PRO A CD    1 
ATOM   2661 N  N     . ASN A 1 346 ? 16.629  7.500   19.957  1.00 52.19  ? 346 ASN A N     1 
ATOM   2662 C  CA    . ASN A 1 346 ? 17.137  7.600   18.593  1.00 47.40  ? 346 ASN A CA    1 
ATOM   2663 C  C     . ASN A 1 346 ? 16.199  8.404   17.700  1.00 48.94  ? 346 ASN A C     1 
ATOM   2664 O  O     . ASN A 1 346 ? 16.656  9.064   16.760  1.00 60.25  ? 346 ASN A O     1 
ATOM   2665 C  CB    . ASN A 1 346 ? 17.358  6.204   18.011  1.00 55.18  ? 346 ASN A CB    1 
ATOM   2666 C  CG    . ASN A 1 346 ? 18.539  5.490   18.640  1.00 63.52  ? 346 ASN A CG    1 
ATOM   2667 O  OD1   . ASN A 1 346 ? 19.645  6.027   18.698  1.00 55.97  ? 346 ASN A OD1   1 
ATOM   2668 N  ND2   . ASN A 1 346 ? 18.307  4.275   19.123  1.00 54.70  ? 346 ASN A ND2   1 
ATOM   2669 N  N     . ALA A 1 347 ? 14.894  8.363   17.974  1.00 59.74  ? 347 ALA A N     1 
ATOM   2670 C  CA    . ALA A 1 347 ? 13.948  9.115   17.157  1.00 59.92  ? 347 ALA A CA    1 
ATOM   2671 C  C     . ALA A 1 347 ? 14.057  10.614  17.403  1.00 60.45  ? 347 ALA A C     1 
ATOM   2672 O  O     . ALA A 1 347 ? 13.840  11.409  16.481  1.00 57.10  ? 347 ALA A O     1 
ATOM   2673 C  CB    . ALA A 1 347 ? 12.522  8.635   17.426  1.00 55.59  ? 347 ALA A CB    1 
ATOM   2674 N  N     . ILE A 1 348 ? 14.393  11.019  18.629  1.00 72.48  ? 348 ILE A N     1 
ATOM   2675 C  CA    . ILE A 1 348 ? 14.500  12.442  18.938  1.00 51.63  ? 348 ILE A CA    1 
ATOM   2676 C  C     . ILE A 1 348 ? 15.627  13.078  18.135  1.00 57.22  ? 348 ILE A C     1 
ATOM   2677 O  O     . ILE A 1 348 ? 15.523  14.229  17.693  1.00 66.41  ? 348 ILE A O     1 
ATOM   2678 C  CB    . ILE A 1 348 ? 14.695  12.648  20.451  1.00 60.91  ? 348 ILE A CB    1 
ATOM   2679 C  CG1   . ILE A 1 348 ? 13.534  12.025  21.229  1.00 59.16  ? 348 ILE A CG1   1 
ATOM   2680 C  CG2   . ILE A 1 348 ? 14.825  14.128  20.775  1.00 73.15  ? 348 ILE A CG2   1 
ATOM   2681 C  CD1   . ILE A 1 348 ? 12.185  12.622  20.896  1.00 50.55  ? 348 ILE A CD1   1 
ATOM   2682 N  N     . LYS A 1 349 ? 16.723  12.342  17.934  1.00 55.49  ? 349 LYS A N     1 
ATOM   2683 C  CA    . LYS A 1 349 ? 17.850  12.875  17.180  1.00 56.96  ? 349 LYS A CA    1 
ATOM   2684 C  C     . LYS A 1 349 ? 17.539  13.026  15.697  1.00 58.76  ? 349 LYS A C     1 
ATOM   2685 O  O     . LYS A 1 349 ? 18.183  13.834  15.021  1.00 56.51  ? 349 LYS A O     1 
ATOM   2686 C  CB    . LYS A 1 349 ? 19.075  11.975  17.355  1.00 63.14  ? 349 LYS A CB    1 
ATOM   2687 C  CG    . LYS A 1 349 ? 19.513  11.776  18.796  1.00 64.27  ? 349 LYS A CG    1 
ATOM   2688 C  CD    . LYS A 1 349 ? 20.727  10.863  18.875  1.00 67.97  ? 349 LYS A CD    1 
ATOM   2689 C  CE    . LYS A 1 349 ? 21.174  10.655  20.313  1.00 87.50  ? 349 LYS A CE    1 
ATOM   2690 N  NZ    . LYS A 1 349 ? 22.378  9.783   20.398  1.00 101.10 ? 349 LYS A NZ    1 
ATOM   2691 N  N     . THR A 1 350 ? 16.567  12.275  15.181  1.00 60.90  ? 350 THR A N     1 
ATOM   2692 C  CA    . THR A 1 350 ? 16.292  12.257  13.750  1.00 58.03  ? 350 THR A CA    1 
ATOM   2693 C  C     . THR A 1 350 ? 15.263  13.296  13.324  1.00 55.14  ? 350 THR A C     1 
ATOM   2694 O  O     . THR A 1 350 ? 15.352  13.819  12.207  1.00 48.36  ? 350 THR A O     1 
ATOM   2695 C  CB    . THR A 1 350 ? 15.804  10.868  13.325  1.00 62.77  ? 350 THR A CB    1 
ATOM   2696 O  OG1   . THR A 1 350 ? 16.722  9.870   13.789  1.00 52.50  ? 350 THR A OG1   1 
ATOM   2697 C  CG2   . THR A 1 350 ? 15.694  10.782  11.809  1.00 51.15  ? 350 THR A CG2   1 
ATOM   2698 N  N     . ILE A 1 351 ? 14.297  13.613  14.184  1.00 59.87  ? 351 ILE A N     1 
ATOM   2699 C  CA    . ILE A 1 351 ? 13.169  14.456  13.801  1.00 63.56  ? 351 ILE A CA    1 
ATOM   2700 C  C     . ILE A 1 351 ? 13.449  15.917  14.125  1.00 61.83  ? 351 ILE A C     1 
ATOM   2701 O  O     . ILE A 1 351 ? 12.518  16.713  14.295  1.00 47.41  ? 351 ILE A O     1 
ATOM   2702 C  CB    . ILE A 1 351 ? 11.876  13.988  14.492  1.00 52.03  ? 351 ILE A CB    1 
ATOM   2703 C  CG1   . ILE A 1 351 ? 12.007  14.129  16.010  1.00 52.47  ? 351 ILE A CG1   1 
ATOM   2704 C  CG2   . ILE A 1 351 ? 11.558  12.550  14.111  1.00 43.86  ? 351 ILE A CG2   1 
ATOM   2705 C  CD1   . ILE A 1 351 ? 10.755  13.757  16.771  1.00 45.96  ? 351 ILE A CD1   1 
ATOM   2706 N  N     . GLN A 1 352 ? 14.725  16.286  14.207  1.00 63.27  ? 352 GLN A N     1 
ATOM   2707 C  CA    . GLN A 1 352 ? 15.110  17.652  14.536  1.00 61.50  ? 352 GLN A CA    1 
ATOM   2708 C  C     . GLN A 1 352 ? 15.521  18.471  13.320  1.00 63.18  ? 352 GLN A C     1 
ATOM   2709 O  O     . GLN A 1 352 ? 15.931  19.625  13.480  1.00 53.09  ? 352 GLN A O     1 
ATOM   2710 C  CB    . GLN A 1 352 ? 16.246  17.648  15.564  1.00 61.73  ? 352 GLN A CB    1 
ATOM   2711 C  CG    . GLN A 1 352 ? 15.808  17.257  16.967  1.00 68.70  ? 352 GLN A CG    1 
ATOM   2712 C  CD    . GLN A 1 352 ? 16.947  17.302  17.967  1.00 72.07  ? 352 GLN A CD    1 
ATOM   2713 O  OE1   . GLN A 1 352 ? 18.119  17.314  17.590  1.00 67.91  ? 352 GLN A OE1   1 
ATOM   2714 N  NE2   . GLN A 1 352 ? 16.607  17.330  19.251  1.00 84.28  ? 352 GLN A NE2   1 
ATOM   2715 N  N     . LYS A 1 353 ? 15.420  17.914  12.115  1.00 67.10  ? 353 LYS A N     1 
ATOM   2716 C  CA    . LYS A 1 353 ? 15.756  18.657  10.910  1.00 71.10  ? 353 LYS A CA    1 
ATOM   2717 C  C     . LYS A 1 353 ? 15.206  17.918  9.699   1.00 76.63  ? 353 LYS A C     1 
ATOM   2718 O  O     . LYS A 1 353 ? 15.220  16.685  9.659   1.00 74.33  ? 353 LYS A O     1 
ATOM   2719 C  CB    . LYS A 1 353 ? 17.272  18.854  10.776  1.00 71.27  ? 353 LYS A CB    1 
ATOM   2720 C  CG    . LYS A 1 353 ? 18.078  17.565  10.783  1.00 81.79  ? 353 LYS A CG    1 
ATOM   2721 C  CD    . LYS A 1 353 ? 19.571  17.854  10.725  1.00 84.49  ? 353 LYS A CD    1 
ATOM   2722 C  CE    . LYS A 1 353 ? 20.389  16.575  10.799  1.00 87.27  ? 353 LYS A CE    1 
ATOM   2723 N  NZ    . LYS A 1 353 ? 21.852  16.851  10.777  1.00 101.62 ? 353 LYS A NZ    1 
ATOM   2724 N  N     . ASN A 1 354 ? 14.720  18.683  8.720   1.00 63.49  ? 354 ASN A N     1 
ATOM   2725 C  CA    . ASN A 1 354 ? 14.167  18.121  7.488   1.00 59.50  ? 354 ASN A CA    1 
ATOM   2726 C  C     . ASN A 1 354 ? 13.006  17.174  7.785   1.00 55.60  ? 354 ASN A C     1 
ATOM   2727 O  O     . ASN A 1 354 ? 12.869  16.117  7.167   1.00 56.48  ? 354 ASN A O     1 
ATOM   2728 C  CB    . ASN A 1 354 ? 15.250  17.410  6.672   1.00 63.10  ? 354 ASN A CB    1 
ATOM   2729 C  CG    . ASN A 1 354 ? 16.429  18.311  6.357   1.00 63.99  ? 354 ASN A CG    1 
ATOM   2730 O  OD1   . ASN A 1 354 ? 16.291  19.531  6.289   1.00 68.96  ? 354 ASN A OD1   1 
ATOM   2731 N  ND2   . ASN A 1 354 ? 17.598  17.710  6.163   1.00 61.21  ? 354 ASN A ND2   1 
ATOM   2732 N  N     . THR A 1 355 ? 12.160  17.558  8.739   1.00 54.00  ? 355 THR A N     1 
ATOM   2733 C  CA    . THR A 1 355 ? 11.047  16.728  9.176   1.00 55.18  ? 355 THR A CA    1 
ATOM   2734 C  C     . THR A 1 355 ? 9.745   17.507  9.075   1.00 52.32  ? 355 THR A C     1 
ATOM   2735 O  O     . THR A 1 355 ? 9.691   18.692  9.417   1.00 43.73  ? 355 THR A O     1 
ATOM   2736 C  CB    . THR A 1 355 ? 11.248  16.239  10.615  1.00 50.62  ? 355 THR A CB    1 
ATOM   2737 O  OG1   . THR A 1 355 ? 12.455  15.472  10.698  1.00 52.30  ? 355 THR A OG1   1 
ATOM   2738 C  CG2   . THR A 1 355 ? 10.073  15.377  11.053  1.00 50.21  ? 355 THR A CG2   1 
ATOM   2739 N  N     . ILE A 1 356 ? 8.698   16.832  8.609   1.00 42.39  ? 356 ILE A N     1 
ATOM   2740 C  CA    . ILE A 1 356 ? 7.363   17.408  8.488   1.00 42.31  ? 356 ILE A CA    1 
ATOM   2741 C  C     . ILE A 1 356 ? 6.466   16.733  9.516   1.00 39.03  ? 356 ILE A C     1 
ATOM   2742 O  O     . ILE A 1 356 ? 6.277   15.511  9.477   1.00 46.81  ? 356 ILE A O     1 
ATOM   2743 C  CB    . ILE A 1 356 ? 6.796   17.241  7.070   1.00 50.13  ? 356 ILE A CB    1 
ATOM   2744 C  CG1   . ILE A 1 356 ? 7.670   17.974  6.051   1.00 44.66  ? 356 ILE A CG1   1 
ATOM   2745 C  CG2   . ILE A 1 356 ? 5.362   17.744  7.008   1.00 51.37  ? 356 ILE A CG2   1 
ATOM   2746 C  CD1   . ILE A 1 356 ? 7.185   17.838  4.623   1.00 53.66  ? 356 ILE A CD1   1 
ATOM   2747 N  N     . PHE A 1 357 ? 5.916   17.523  10.431  1.00 43.19  ? 357 PHE A N     1 
ATOM   2748 C  CA    . PHE A 1 357 ? 5.011   17.030  11.457  1.00 46.04  ? 357 PHE A CA    1 
ATOM   2749 C  C     . PHE A 1 357 ? 3.564   17.284  11.054  1.00 53.01  ? 357 PHE A C     1 
ATOM   2750 O  O     . PHE A 1 357 ? 3.264   18.166  10.245  1.00 46.05  ? 357 PHE A O     1 
ATOM   2751 C  CB    . PHE A 1 357 ? 5.306   17.692  12.806  1.00 47.79  ? 357 PHE A CB    1 
ATOM   2752 C  CG    . PHE A 1 357 ? 6.676   17.389  13.344  1.00 56.67  ? 357 PHE A CG    1 
ATOM   2753 C  CD1   . PHE A 1 357 ? 7.763   18.170  12.990  1.00 50.43  ? 357 PHE A CD1   1 
ATOM   2754 C  CD2   . PHE A 1 357 ? 6.875   16.323  14.205  1.00 57.31  ? 357 PHE A CD2   1 
ATOM   2755 C  CE1   . PHE A 1 357 ? 9.024   17.893  13.484  1.00 48.82  ? 357 PHE A CE1   1 
ATOM   2756 C  CE2   . PHE A 1 357 ? 8.133   16.041  14.703  1.00 53.36  ? 357 PHE A CE2   1 
ATOM   2757 C  CZ    . PHE A 1 357 ? 9.209   16.827  14.341  1.00 48.27  ? 357 PHE A CZ    1 
ATOM   2758 N  N     . THR A 1 358 ? 2.660   16.496  11.634  1.00 54.03  ? 358 THR A N     1 
ATOM   2759 C  CA    . THR A 1 358 ? 1.244   16.584  11.292  1.00 56.12  ? 358 THR A CA    1 
ATOM   2760 C  C     . THR A 1 358 ? 0.408   16.306  12.531  1.00 54.57  ? 358 THR A C     1 
ATOM   2761 O  O     . THR A 1 358 ? 0.549   15.247  13.151  1.00 67.68  ? 358 THR A O     1 
ATOM   2762 C  CB    . THR A 1 358 ? 0.885   15.602  10.173  1.00 47.62  ? 358 THR A CB    1 
ATOM   2763 O  OG1   . THR A 1 358 ? 1.670   15.891  9.010   1.00 41.96  ? 358 THR A OG1   1 
ATOM   2764 C  CG2   . THR A 1 358 ? -0.591  15.715  9.820   1.00 62.67  ? 358 THR A CG2   1 
ATOM   2765 N  N     . ASN A 1 359 ? -0.460  17.256  12.884  1.00 59.49  ? 359 ASN A N     1 
ATOM   2766 C  CA    . ASN A 1 359 ? -1.425  17.097  13.969  1.00 62.78  ? 359 ASN A CA    1 
ATOM   2767 C  C     . ASN A 1 359 ? -0.758  17.003  15.338  1.00 66.27  ? 359 ASN A C     1 
ATOM   2768 O  O     . ASN A 1 359 ? -1.290  16.366  16.250  1.00 69.31  ? 359 ASN A O     1 
ATOM   2769 C  CB    . ASN A 1 359 ? -2.326  15.880  13.736  1.00 65.89  ? 359 ASN A CB    1 
ATOM   2770 C  CG    . ASN A 1 359 ? -3.351  16.115  12.644  1.00 67.91  ? 359 ASN A CG    1 
ATOM   2771 O  OD1   . ASN A 1 359 ? -3.769  17.248  12.404  1.00 75.23  ? 359 ASN A OD1   1 
ATOM   2772 N  ND2   . ASN A 1 359 ? -3.765  15.043  11.979  1.00 76.79  ? 359 ASN A ND2   1 
ATOM   2773 N  N     . VAL A 1 360 ? 0.399   17.634  15.502  1.00 61.25  ? 360 VAL A N     1 
ATOM   2774 C  CA    . VAL A 1 360 ? 1.070   17.702  16.792  1.00 66.46  ? 360 VAL A CA    1 
ATOM   2775 C  C     . VAL A 1 360 ? 0.988   19.133  17.306  1.00 67.57  ? 360 VAL A C     1 
ATOM   2776 O  O     . VAL A 1 360 ? 0.761   20.084  16.552  1.00 70.98  ? 360 VAL A O     1 
ATOM   2777 C  CB    . VAL A 1 360 ? 2.536   17.227  16.718  1.00 54.62  ? 360 VAL A CB    1 
ATOM   2778 C  CG1   . VAL A 1 360 ? 2.608   15.802  16.189  1.00 51.19  ? 360 VAL A CG1   1 
ATOM   2779 C  CG2   . VAL A 1 360 ? 3.359   18.169  15.854  1.00 54.77  ? 360 VAL A CG2   1 
ATOM   2780 N  N     . ALA A 1 361 ? 1.175   19.280  18.614  1.00 73.13  ? 361 ALA A N     1 
ATOM   2781 C  CA    . ALA A 1 361 ? 1.091   20.587  19.247  1.00 72.19  ? 361 ALA A CA    1 
ATOM   2782 C  C     . ALA A 1 361 ? 2.360   21.393  19.000  1.00 71.05  ? 361 ALA A C     1 
ATOM   2783 O  O     . ALA A 1 361 ? 3.452   20.842  18.834  1.00 77.11  ? 361 ALA A O     1 
ATOM   2784 C  CB    . ALA A 1 361 ? 0.850   20.442  20.750  1.00 76.55  ? 361 ALA A CB    1 
ATOM   2785 N  N     . GLU A 1 362 ? 2.204   22.714  18.978  1.00 78.70  ? 362 GLU A N     1 
ATOM   2786 C  CA    . GLU A 1 362 ? 3.305   23.639  18.752  1.00 80.99  ? 362 GLU A CA    1 
ATOM   2787 C  C     . GLU A 1 362 ? 3.495   24.518  19.979  1.00 84.23  ? 362 GLU A C     1 
ATOM   2788 O  O     . GLU A 1 362 ? 2.523   25.018  20.554  1.00 89.56  ? 362 GLU A O     1 
ATOM   2789 C  CB    . GLU A 1 362 ? 3.051   24.514  17.519  1.00 76.15  ? 362 GLU A CB    1 
ATOM   2790 C  CG    . GLU A 1 362 ? 4.141   25.542  17.255  1.00 78.97  ? 362 GLU A CG    1 
ATOM   2791 C  CD    . GLU A 1 362 ? 3.807   26.465  16.098  1.00 95.55  ? 362 GLU A CD    1 
ATOM   2792 O  OE1   . GLU A 1 362 ? 2.724   26.300  15.498  1.00 102.45 ? 362 GLU A OE1   1 
ATOM   2793 O  OE2   . GLU A 1 362 ? 4.625   27.357  15.790  1.00 96.15  ? 362 GLU A OE2   1 
ATOM   2794 N  N     . THR A 1 363 ? 4.750   24.704  20.376  1.00 85.21  ? 363 THR A N     1 
ATOM   2795 C  CA    . THR A 1 363 ? 5.080   25.553  21.509  1.00 85.57  ? 363 THR A CA    1 
ATOM   2796 C  C     . THR A 1 363 ? 5.306   26.991  21.052  1.00 87.82  ? 363 THR A C     1 
ATOM   2797 O  O     . THR A 1 363 ? 5.545   27.266  19.873  1.00 88.42  ? 363 THR A O     1 
ATOM   2798 C  CB    . THR A 1 363 ? 6.321   25.031  22.237  1.00 75.17  ? 363 THR A CB    1 
ATOM   2799 O  OG1   . THR A 1 363 ? 7.437   25.020  21.338  1.00 81.73  ? 363 THR A OG1   1 
ATOM   2800 C  CG2   . THR A 1 363 ? 6.079   23.621  22.752  1.00 75.00  ? 363 THR A CG2   1 
ATOM   2801 N  N     . SER A 1 364 ? 5.230   27.915  22.012  1.00 81.94  ? 364 SER A N     1 
ATOM   2802 C  CA    . SER A 1 364 ? 5.345   29.333  21.684  1.00 83.90  ? 364 SER A CA    1 
ATOM   2803 C  C     . SER A 1 364 ? 6.700   29.655  21.066  1.00 80.59  ? 364 SER A C     1 
ATOM   2804 O  O     . SER A 1 364 ? 6.792   30.483  20.152  1.00 78.58  ? 364 SER A O     1 
ATOM   2805 C  CB    . SER A 1 364 ? 5.111   30.182  22.933  1.00 89.96  ? 364 SER A CB    1 
ATOM   2806 O  OG    . SER A 1 364 ? 6.118   29.950  23.903  1.00 82.97  ? 364 SER A OG    1 
ATOM   2807 N  N     . ASP A 1 365 ? 7.762   29.014  21.549  1.00 76.67  ? 365 ASP A N     1 
ATOM   2808 C  CA    . ASP A 1 365 ? 9.107   29.287  21.058  1.00 73.12  ? 365 ASP A CA    1 
ATOM   2809 C  C     . ASP A 1 365 ? 9.409   28.611  19.726  1.00 72.19  ? 365 ASP A C     1 
ATOM   2810 O  O     . ASP A 1 365 ? 10.549  28.692  19.255  1.00 71.43  ? 365 ASP A O     1 
ATOM   2811 C  CB    . ASP A 1 365 ? 10.144  28.859  22.100  1.00 74.73  ? 365 ASP A CB    1 
ATOM   2812 C  CG    . ASP A 1 365 ? 9.978   27.416  22.529  1.00 85.95  ? 365 ASP A CG    1 
ATOM   2813 O  OD1   . ASP A 1 365 ? 9.004   26.771  22.086  1.00 88.84  ? 365 ASP A OD1   1 
ATOM   2814 O  OD2   . ASP A 1 365 ? 10.822  26.926  23.307  1.00 86.47  ? 365 ASP A OD2   1 
ATOM   2815 N  N     . GLY A 1 366 ? 8.431   27.956  19.109  1.00 74.47  ? 366 GLY A N     1 
ATOM   2816 C  CA    . GLY A 1 366 ? 8.626   27.320  17.825  1.00 71.69  ? 366 GLY A CA    1 
ATOM   2817 C  C     . GLY A 1 366 ? 8.955   25.845  17.862  1.00 75.26  ? 366 GLY A C     1 
ATOM   2818 O  O     . GLY A 1 366 ? 9.384   25.301  16.838  1.00 75.89  ? 366 GLY A O     1 
ATOM   2819 N  N     . GLY A 1 367 ? 8.771   25.179  19.002  1.00 72.60  ? 367 GLY A N     1 
ATOM   2820 C  CA    . GLY A 1 367 ? 9.046   23.766  19.125  1.00 72.79  ? 367 GLY A CA    1 
ATOM   2821 C  C     . GLY A 1 367 ? 7.807   22.913  18.912  1.00 69.75  ? 367 GLY A C     1 
ATOM   2822 O  O     . GLY A 1 367 ? 6.741   23.388  18.517  1.00 71.95  ? 367 GLY A O     1 
ATOM   2823 N  N     . VAL A 1 368 ? 7.966   21.620  19.184  1.00 68.19  ? 368 VAL A N     1 
ATOM   2824 C  CA    . VAL A 1 368 ? 6.885   20.653  19.067  1.00 73.17  ? 368 VAL A CA    1 
ATOM   2825 C  C     . VAL A 1 368 ? 6.575   20.098  20.451  1.00 67.84  ? 368 VAL A C     1 
ATOM   2826 O  O     . VAL A 1 368 ? 7.396   20.152  21.370  1.00 73.90  ? 368 VAL A O     1 
ATOM   2827 C  CB    . VAL A 1 368 ? 7.224   19.512  18.086  1.00 65.80  ? 368 VAL A CB    1 
ATOM   2828 C  CG1   . VAL A 1 368 ? 7.515   20.071  16.701  1.00 60.06  ? 368 VAL A CG1   1 
ATOM   2829 C  CG2   . VAL A 1 368 ? 8.406   18.704  18.601  1.00 67.02  ? 368 VAL A CG2   1 
ATOM   2830 N  N     . TYR A 1 369 ? 5.367   19.557  20.591  1.00 60.13  ? 369 TYR A N     1 
ATOM   2831 C  CA    . TYR A 1 369 ? 4.934   19.010  21.868  1.00 67.09  ? 369 TYR A CA    1 
ATOM   2832 C  C     . TYR A 1 369 ? 3.830   17.991  21.626  1.00 69.77  ? 369 TYR A C     1 
ATOM   2833 O  O     . TYR A 1 369 ? 3.005   18.164  20.725  1.00 71.77  ? 369 TYR A O     1 
ATOM   2834 C  CB    . TYR A 1 369 ? 4.447   20.118  22.809  1.00 63.07  ? 369 TYR A CB    1 
ATOM   2835 C  CG    . TYR A 1 369 ? 4.492   19.740  24.271  1.00 67.70  ? 369 TYR A CG    1 
ATOM   2836 C  CD1   . TYR A 1 369 ? 5.677   19.821  24.990  1.00 70.17  ? 369 TYR A CD1   1 
ATOM   2837 C  CD2   . TYR A 1 369 ? 3.352   19.305  24.934  1.00 66.11  ? 369 TYR A CD2   1 
ATOM   2838 C  CE1   . TYR A 1 369 ? 5.727   19.478  26.327  1.00 68.39  ? 369 TYR A CE1   1 
ATOM   2839 C  CE2   . TYR A 1 369 ? 3.392   18.960  26.272  1.00 72.20  ? 369 TYR A CE2   1 
ATOM   2840 C  CZ    . TYR A 1 369 ? 4.582   19.049  26.963  1.00 74.36  ? 369 TYR A CZ    1 
ATOM   2841 O  OH    . TYR A 1 369 ? 4.630   18.707  28.294  1.00 77.14  ? 369 TYR A OH    1 
ATOM   2842 N  N     . TRP A 1 370 ? 3.824   16.935  22.434  1.00 60.51  ? 370 TRP A N     1 
ATOM   2843 C  CA    . TRP A 1 370 ? 2.805   15.898  22.344  1.00 64.05  ? 370 TRP A CA    1 
ATOM   2844 C  C     . TRP A 1 370 ? 2.779   15.130  23.657  1.00 66.18  ? 370 TRP A C     1 
ATOM   2845 O  O     . TRP A 1 370 ? 3.696   15.230  24.477  1.00 64.72  ? 370 TRP A O     1 
ATOM   2846 C  CB    . TRP A 1 370 ? 3.060   14.959  21.159  1.00 65.83  ? 370 TRP A CB    1 
ATOM   2847 C  CG    . TRP A 1 370 ? 4.455   14.403  21.107  1.00 62.81  ? 370 TRP A CG    1 
ATOM   2848 C  CD1   . TRP A 1 370 ? 5.016   13.510  21.973  1.00 57.57  ? 370 TRP A CD1   1 
ATOM   2849 C  CD2   . TRP A 1 370 ? 5.458   14.694  20.125  1.00 58.52  ? 370 TRP A CD2   1 
ATOM   2850 N  NE1   . TRP A 1 370 ? 6.309   13.234  21.597  1.00 53.58  ? 370 TRP A NE1   1 
ATOM   2851 C  CE2   . TRP A 1 370 ? 6.604   13.947  20.465  1.00 50.42  ? 370 TRP A CE2   1 
ATOM   2852 C  CE3   . TRP A 1 370 ? 5.499   15.516  18.995  1.00 53.15  ? 370 TRP A CE3   1 
ATOM   2853 C  CZ2   . TRP A 1 370 ? 7.777   13.998  19.715  1.00 52.52  ? 370 TRP A CZ2   1 
ATOM   2854 C  CZ3   . TRP A 1 370 ? 6.665   15.564  18.252  1.00 55.53  ? 370 TRP A CZ3   1 
ATOM   2855 C  CH2   . TRP A 1 370 ? 7.788   14.810  18.615  1.00 47.15  ? 370 TRP A CH2   1 
ATOM   2856 N  N     . GLU A 1 371 ? 1.710   14.361  23.848  1.00 68.09  ? 371 GLU A N     1 
ATOM   2857 C  CA    . GLU A 1 371 ? 1.577   13.561  25.057  1.00 61.11  ? 371 GLU A CA    1 
ATOM   2858 C  C     . GLU A 1 371 ? 2.698   12.531  25.141  1.00 63.22  ? 371 GLU A C     1 
ATOM   2859 O  O     . GLU A 1 371 ? 3.170   12.007  24.129  1.00 56.52  ? 371 GLU A O     1 
ATOM   2860 C  CB    . GLU A 1 371 ? 0.217   12.861  25.095  1.00 52.49  ? 371 GLU A CB    1 
ATOM   2861 C  CG    . GLU A 1 371 ? -0.954  13.774  25.426  1.00 67.72  ? 371 GLU A CG    1 
ATOM   2862 C  CD    . GLU A 1 371 ? -1.281  14.743  24.308  1.00 78.09  ? 371 GLU A CD    1 
ATOM   2863 O  OE1   . GLU A 1 371 ? -0.773  14.548  23.183  1.00 77.16  ? 371 GLU A OE1   1 
ATOM   2864 O  OE2   . GLU A 1 371 ? -2.046  15.698  24.554  1.00 93.16  ? 371 GLU A OE2   1 
ATOM   2865 N  N     . GLY A 1 372 ? 3.123   12.242  26.369  1.00 63.30  ? 372 GLY A N     1 
ATOM   2866 C  CA    . GLY A 1 372 ? 4.199   11.297  26.580  1.00 56.10  ? 372 GLY A CA    1 
ATOM   2867 C  C     . GLY A 1 372 ? 5.570   11.785  26.175  1.00 60.32  ? 372 GLY A C     1 
ATOM   2868 O  O     . GLY A 1 372 ? 6.518   10.994  26.179  1.00 60.73  ? 372 GLY A O     1 
ATOM   2869 N  N     . ILE A 1 373 ? 5.708   13.064  25.818  1.00 65.23  ? 373 ILE A N     1 
ATOM   2870 C  CA    . ILE A 1 373 ? 7.021   13.585  25.454  1.00 62.52  ? 373 ILE A CA    1 
ATOM   2871 C  C     . ILE A 1 373 ? 7.943   13.605  26.666  1.00 68.50  ? 373 ILE A C     1 
ATOM   2872 O  O     . ILE A 1 373 ? 9.166   13.483  26.525  1.00 72.16  ? 373 ILE A O     1 
ATOM   2873 C  CB    . ILE A 1 373 ? 6.886   14.982  24.821  1.00 56.33  ? 373 ILE A CB    1 
ATOM   2874 C  CG1   . ILE A 1 373 ? 8.220   15.429  24.221  1.00 59.59  ? 373 ILE A CG1   1 
ATOM   2875 C  CG2   . ILE A 1 373 ? 6.397   15.990  25.850  1.00 60.23  ? 373 ILE A CG2   1 
ATOM   2876 C  CD1   . ILE A 1 373 ? 8.146   16.745  23.476  1.00 67.95  ? 373 ILE A CD1   1 
ATOM   2877 N  N     . ASP A 1 374 ? 7.381   13.752  27.865  1.00 71.36  ? 374 ASP A N     1 
ATOM   2878 C  CA    . ASP A 1 374 ? 8.138   13.728  29.115  1.00 72.14  ? 374 ASP A CA    1 
ATOM   2879 C  C     . ASP A 1 374 ? 9.350   14.661  29.036  1.00 70.98  ? 374 ASP A C     1 
ATOM   2880 O  O     . ASP A 1 374 ? 10.507  14.241  29.037  1.00 74.66  ? 374 ASP A O     1 
ATOM   2881 C  CB    . ASP A 1 374 ? 8.561   12.297  29.459  1.00 75.58  ? 374 ASP A CB    1 
ATOM   2882 C  CG    . ASP A 1 374 ? 9.122   12.175  30.862  1.00 82.73  ? 374 ASP A CG    1 
ATOM   2883 O  OD1   . ASP A 1 374 ? 8.984   13.139  31.644  1.00 79.62  ? 374 ASP A OD1   1 
ATOM   2884 O  OD2   . ASP A 1 374 ? 9.703   11.116  31.182  1.00 78.54  ? 374 ASP A OD2   1 
ATOM   2885 N  N     . GLU A 1 375 ? 9.043   15.953  28.968  1.00 74.27  ? 375 GLU A N     1 
ATOM   2886 C  CA    . GLU A 1 375 ? 10.082  16.963  28.822  1.00 75.02  ? 375 GLU A CA    1 
ATOM   2887 C  C     . GLU A 1 375 ? 9.568   18.317  29.296  1.00 72.34  ? 375 GLU A C     1 
ATOM   2888 O  O     . GLU A 1 375 ? 8.620   18.862  28.717  1.00 74.35  ? 375 GLU A O     1 
ATOM   2889 C  CB    . GLU A 1 375 ? 10.547  17.035  27.367  1.00 80.22  ? 375 GLU A CB    1 
ATOM   2890 C  CG    . GLU A 1 375 ? 11.900  17.693  27.170  1.00 84.53  ? 375 GLU A CG    1 
ATOM   2891 C  CD    . GLU A 1 375 ? 12.447  17.475  25.773  1.00 92.40  ? 375 GLU A CD    1 
ATOM   2892 O  OE1   . GLU A 1 375 ? 11.719  16.910  24.931  1.00 89.84  ? 375 GLU A OE1   1 
ATOM   2893 O  OE2   . GLU A 1 375 ? 13.607  17.862  25.519  1.00 103.93 ? 375 GLU A OE2   1 
ATOM   2894 N  N     . PRO A 1 376 ? 10.159  18.886  30.344  1.00 80.55  ? 376 PRO A N     1 
ATOM   2895 C  CA    . PRO A 1 376 ? 9.664   20.165  30.862  1.00 76.20  ? 376 PRO A CA    1 
ATOM   2896 C  C     . PRO A 1 376 ? 9.938   21.308  29.898  1.00 76.42  ? 376 PRO A C     1 
ATOM   2897 O  O     . PRO A 1 376 ? 10.941  21.326  29.181  1.00 82.19  ? 376 PRO A O     1 
ATOM   2898 C  CB    . PRO A 1 376 ? 10.445  20.348  32.171  1.00 83.81  ? 376 PRO A CB    1 
ATOM   2899 C  CG    . PRO A 1 376 ? 11.007  18.992  32.492  1.00 78.85  ? 376 PRO A CG    1 
ATOM   2900 C  CD    . PRO A 1 376 ? 11.245  18.338  31.171  1.00 77.75  ? 376 PRO A CD    1 
ATOM   2901 N  N     . LEU A 1 377 ? 9.025   22.272  29.893  1.00 81.70  ? 377 LEU A N     1 
ATOM   2902 C  CA    . LEU A 1 377 ? 9.158   23.480  29.093  1.00 87.38  ? 377 LEU A CA    1 
ATOM   2903 C  C     . LEU A 1 377 ? 9.710   24.619  29.943  1.00 97.26  ? 377 LEU A C     1 
ATOM   2904 O  O     . LEU A 1 377 ? 9.596   24.625  31.171  1.00 96.53  ? 377 LEU A O     1 
ATOM   2905 C  CB    . LEU A 1 377 ? 7.811   23.885  28.489  1.00 89.56  ? 377 LEU A CB    1 
ATOM   2906 C  CG    . LEU A 1 377 ? 7.161   22.905  27.511  1.00 82.87  ? 377 LEU A CG    1 
ATOM   2907 C  CD1   . LEU A 1 377 ? 5.825   23.445  27.023  1.00 75.82  ? 377 LEU A CD1   1 
ATOM   2908 C  CD2   . LEU A 1 377 ? 8.088   22.620  26.340  1.00 91.90  ? 377 LEU A CD2   1 
ATOM   2909 N  N     . ALA A 1 378 ? 10.318  25.590  29.266  1.00 102.67 ? 378 ALA A N     1 
ATOM   2910 C  CA    . ALA A 1 378 ? 10.842  26.756  29.952  1.00 103.71 ? 378 ALA A CA    1 
ATOM   2911 C  C     . ALA A 1 378 ? 9.697   27.623  30.468  1.00 105.05 ? 378 ALA A C     1 
ATOM   2912 O  O     . ALA A 1 378 ? 8.574   27.557  29.961  1.00 99.26  ? 378 ALA A O     1 
ATOM   2913 C  CB    . ALA A 1 378 ? 11.738  27.566  29.020  1.00 99.51  ? 378 ALA A CB    1 
ATOM   2914 N  N     . PRO A 1 379 ? 9.956   28.444  31.484  1.00 96.15  ? 379 PRO A N     1 
ATOM   2915 C  CA    . PRO A 1 379 ? 8.894   29.311  32.014  1.00 83.69  ? 379 PRO A CA    1 
ATOM   2916 C  C     . PRO A 1 379 ? 8.477   30.349  30.982  1.00 78.64  ? 379 PRO A C     1 
ATOM   2917 O  O     . PRO A 1 379 ? 9.319   31.002  30.361  1.00 79.26  ? 379 PRO A O     1 
ATOM   2918 C  CB    . PRO A 1 379 ? 9.543   29.960  33.242  1.00 69.24  ? 379 PRO A CB    1 
ATOM   2919 N  N     . GLY A 1 380 ? 7.167   30.493  30.802  1.00 74.13  ? 380 GLY A N     1 
ATOM   2920 C  CA    . GLY A 1 380 ? 6.633   31.457  29.863  1.00 81.47  ? 380 GLY A CA    1 
ATOM   2921 C  C     . GLY A 1 380 ? 6.384   30.934  28.468  1.00 87.00  ? 380 GLY A C     1 
ATOM   2922 O  O     . GLY A 1 380 ? 6.217   31.737  27.544  1.00 88.62  ? 380 GLY A O     1 
ATOM   2923 N  N     . VAL A 1 381 ? 6.355   29.617  28.282  1.00 85.97  ? 381 VAL A N     1 
ATOM   2924 C  CA    . VAL A 1 381 ? 6.116   29.006  26.980  1.00 92.51  ? 381 VAL A CA    1 
ATOM   2925 C  C     . VAL A 1 381 ? 4.692   28.473  26.947  1.00 96.12  ? 381 VAL A C     1 
ATOM   2926 O  O     . VAL A 1 381 ? 4.238   27.828  27.901  1.00 88.79  ? 381 VAL A O     1 
ATOM   2927 C  CB    . VAL A 1 381 ? 7.131   27.886  26.695  1.00 89.90  ? 381 VAL A CB    1 
ATOM   2928 C  CG1   . VAL A 1 381 ? 6.838   27.233  25.354  1.00 89.68  ? 381 VAL A CG1   1 
ATOM   2929 C  CG2   . VAL A 1 381 ? 8.549   28.436  26.727  1.00 86.99  ? 381 VAL A CG2   1 
ATOM   2930 N  N     . THR A 1 382 ? 3.986   28.739  25.852  1.00 105.21 ? 382 THR A N     1 
ATOM   2931 C  CA    . THR A 1 382 ? 2.612   28.301  25.670  1.00 110.04 ? 382 THR A CA    1 
ATOM   2932 C  C     . THR A 1 382 ? 2.552   27.147  24.676  1.00 111.40 ? 382 THR A C     1 
ATOM   2933 O  O     . THR A 1 382 ? 3.504   26.881  23.937  1.00 111.56 ? 382 THR A O     1 
ATOM   2934 C  CB    . THR A 1 382 ? 1.725   29.454  25.185  1.00 117.08 ? 382 THR A CB    1 
ATOM   2935 O  OG1   . THR A 1 382 ? 2.151   29.870  23.882  1.00 115.12 ? 382 THR A OG1   1 
ATOM   2936 C  CG2   . THR A 1 382 ? 1.817   30.633  26.143  1.00 115.87 ? 382 THR A CG2   1 
ATOM   2937 N  N     . ILE A 1 383 ? 1.411   26.462  24.668  1.00 104.94 ? 383 ILE A N     1 
ATOM   2938 C  CA    . ILE A 1 383 ? 1.189   25.308  23.807  1.00 96.72  ? 383 ILE A CA    1 
ATOM   2939 C  C     . ILE A 1 383 ? -0.097  25.520  23.022  1.00 98.71  ? 383 ILE A C     1 
ATOM   2940 O  O     . ILE A 1 383 ? -1.108  25.967  23.575  1.00 105.16 ? 383 ILE A O     1 
ATOM   2941 C  CB    . ILE A 1 383 ? 1.117   23.996  24.617  1.00 97.76  ? 383 ILE A CB    1 
ATOM   2942 C  CG1   . ILE A 1 383 ? 2.397   23.799  25.431  1.00 95.30  ? 383 ILE A CG1   1 
ATOM   2943 C  CG2   . ILE A 1 383 ? 0.881   22.814  23.692  1.00 96.45  ? 383 ILE A CG2   1 
ATOM   2944 C  CD1   . ILE A 1 383 ? 2.393   22.544  26.276  1.00 94.63  ? 383 ILE A CD1   1 
ATOM   2945 N  N     . THR A 1 384 ? -0.057  25.197  21.731  1.00 92.15  ? 384 THR A N     1 
ATOM   2946 C  CA    . THR A 1 384 ? -1.217  25.280  20.852  1.00 92.60  ? 384 THR A CA    1 
ATOM   2947 C  C     . THR A 1 384 ? -1.546  23.881  20.355  1.00 87.24  ? 384 THR A C     1 
ATOM   2948 O  O     . THR A 1 384 ? -0.720  23.245  19.691  1.00 82.46  ? 384 THR A O     1 
ATOM   2949 C  CB    . THR A 1 384 ? -0.955  26.223  19.675  1.00 86.30  ? 384 THR A CB    1 
ATOM   2950 O  OG1   . THR A 1 384 ? -0.722  27.550  20.165  1.00 91.78  ? 384 THR A OG1   1 
ATOM   2951 C  CG2   . THR A 1 384 ? -2.148  26.238  18.731  1.00 81.21  ? 384 THR A CG2   1 
ATOM   2952 N  N     . SER A 1 385 ? -2.747  23.406  20.675  1.00 90.38  ? 385 SER A N     1 
ATOM   2953 C  CA    . SER A 1 385 ? -3.149  22.059  20.303  1.00 90.41  ? 385 SER A CA    1 
ATOM   2954 C  C     . SER A 1 385 ? -3.247  21.927  18.783  1.00 86.50  ? 385 SER A C     1 
ATOM   2955 O  O     . SER A 1 385 ? -3.139  22.902  18.033  1.00 86.88  ? 385 SER A O     1 
ATOM   2956 C  CB    . SER A 1 385 ? -4.485  21.701  20.952  1.00 96.15  ? 385 SER A CB    1 
ATOM   2957 O  OG    . SER A 1 385 ? -5.517  22.561  20.503  1.00 101.39 ? 385 SER A OG    1 
ATOM   2958 N  N     . TRP A 1 386 ? -3.456  20.689  18.331  1.00 81.42  ? 386 TRP A N     1 
ATOM   2959 C  CA    . TRP A 1 386 ? -3.590  20.422  16.905  1.00 82.16  ? 386 TRP A CA    1 
ATOM   2960 C  C     . TRP A 1 386 ? -4.900  20.944  16.331  1.00 85.29  ? 386 TRP A C     1 
ATOM   2961 O  O     . TRP A 1 386 ? -5.051  20.972  15.105  1.00 84.47  ? 386 TRP A O     1 
ATOM   2962 C  CB    . TRP A 1 386 ? -3.465  18.921  16.634  1.00 73.76  ? 386 TRP A CB    1 
ATOM   2963 C  CG    . TRP A 1 386 ? -4.642  18.121  17.099  1.00 76.98  ? 386 TRP A CG    1 
ATOM   2964 C  CD1   . TRP A 1 386 ? -4.898  17.700  18.371  1.00 81.57  ? 386 TRP A CD1   1 
ATOM   2965 C  CD2   . TRP A 1 386 ? -5.721  17.636  16.291  1.00 76.93  ? 386 TRP A CD2   1 
ATOM   2966 N  NE1   . TRP A 1 386 ? -6.072  16.987  18.406  1.00 84.94  ? 386 TRP A NE1   1 
ATOM   2967 C  CE2   . TRP A 1 386 ? -6.597  16.933  17.142  1.00 79.91  ? 386 TRP A CE2   1 
ATOM   2968 C  CE3   . TRP A 1 386 ? -6.033  17.730  14.931  1.00 79.11  ? 386 TRP A CE3   1 
ATOM   2969 C  CZ2   . TRP A 1 386 ? -7.763  16.327  16.678  1.00 77.08  ? 386 TRP A CZ2   1 
ATOM   2970 C  CZ3   . TRP A 1 386 ? -7.191  17.128  14.472  1.00 78.39  ? 386 TRP A CZ3   1 
ATOM   2971 C  CH2   . TRP A 1 386 ? -8.041  16.436  15.343  1.00 78.38  ? 386 TRP A CH2   1 
ATOM   2972 N  N     . LYS A 1 387 ? -5.844  21.351  17.177  1.00 86.06  ? 387 LYS A N     1 
ATOM   2973 C  CA    . LYS A 1 387 ? -7.086  21.964  16.731  1.00 90.39  ? 387 LYS A CA    1 
ATOM   2974 C  C     . LYS A 1 387 ? -6.956  23.470  16.536  1.00 99.76  ? 387 LYS A C     1 
ATOM   2975 O  O     . LYS A 1 387 ? -7.973  24.157  16.402  1.00 98.12  ? 387 LYS A O     1 
ATOM   2976 C  CB    . LYS A 1 387 ? -8.212  21.662  17.724  1.00 93.70  ? 387 LYS A CB    1 
ATOM   2977 C  CG    . LYS A 1 387 ? -8.575  20.189  17.825  1.00 85.56  ? 387 LYS A CG    1 
ATOM   2978 C  CD    . LYS A 1 387 ? -9.687  19.962  18.837  1.00 89.61  ? 387 LYS A CD    1 
ATOM   2979 C  CE    . LYS A 1 387 ? -10.094 18.499  18.895  1.00 97.37  ? 387 LYS A CE    1 
ATOM   2980 N  NZ    . LYS A 1 387 ? -10.644 18.022  17.595  1.00 94.79  ? 387 LYS A NZ    1 
ATOM   2981 N  N     . ASN A 1 388 ? -5.730  23.994  16.521  1.00 104.86 ? 388 ASN A N     1 
ATOM   2982 C  CA    . ASN A 1 388 ? -5.488  25.423  16.329  1.00 103.71 ? 388 ASN A CA    1 
ATOM   2983 C  C     . ASN A 1 388 ? -6.152  26.247  17.430  1.00 108.40 ? 388 ASN A C     1 
ATOM   2984 O  O     . ASN A 1 388 ? -6.791  27.268  17.169  1.00 116.05 ? 388 ASN A O     1 
ATOM   2985 C  CB    . ASN A 1 388 ? -5.957  25.880  14.946  1.00 105.33 ? 388 ASN A CB    1 
ATOM   2986 C  CG    . ASN A 1 388 ? -5.316  27.184  14.514  1.00 110.39 ? 388 ASN A CG    1 
ATOM   2987 O  OD1   . ASN A 1 388 ? -4.240  27.547  14.988  1.00 110.13 ? 388 ASN A OD1   1 
ATOM   2988 N  ND2   . ASN A 1 388 ? -5.975  27.896  13.607  1.00 119.84 ? 388 ASN A ND2   1 
ATOM   2989 N  N     . LYS A 1 389 ? -5.999  25.798  18.674  1.00 102.28 ? 389 LYS A N     1 
ATOM   2990 C  CA    . LYS A 1 389 ? -6.573  26.481  19.823  1.00 108.49 ? 389 LYS A CA    1 
ATOM   2991 C  C     . LYS A 1 389 ? -5.555  26.510  20.954  1.00 112.37 ? 389 LYS A C     1 
ATOM   2992 O  O     . LYS A 1 389 ? -4.603  25.725  20.982  1.00 105.88 ? 389 LYS A O     1 
ATOM   2993 C  CB    . LYS A 1 389 ? -7.866  25.805  20.302  1.00 110.64 ? 389 LYS A CB    1 
ATOM   2994 C  CG    . LYS A 1 389 ? -8.977  25.761  19.267  1.00 110.55 ? 389 LYS A CG    1 
ATOM   2995 C  CD    . LYS A 1 389 ? -10.215 25.077  19.828  1.00 109.80 ? 389 LYS A CD    1 
ATOM   2996 C  CE    . LYS A 1 389 ? -11.339 25.034  18.806  1.00 104.89 ? 389 LYS A CE    1 
ATOM   2997 N  NZ    . LYS A 1 389 ? -12.554 24.364  19.348  1.00 105.38 ? 389 LYS A NZ    1 
ATOM   2998 N  N     . GLU A 1 390 ? -5.768  27.431  21.891  1.00 118.25 ? 390 GLU A N     1 
ATOM   2999 C  CA    . GLU A 1 390 ? -4.921  27.514  23.074  1.00 122.84 ? 390 GLU A CA    1 
ATOM   3000 C  C     . GLU A 1 390 ? -5.240  26.354  24.008  1.00 133.21 ? 390 GLU A C     1 
ATOM   3001 O  O     . GLU A 1 390 ? -6.392  26.177  24.419  1.00 134.88 ? 390 GLU A O     1 
ATOM   3002 C  CB    . GLU A 1 390 ? -5.126  28.852  23.779  1.00 123.39 ? 390 GLU A CB    1 
ATOM   3003 C  CG    . GLU A 1 390 ? -4.827  30.063  22.909  1.00 122.43 ? 390 GLU A CG    1 
ATOM   3004 C  CD    . GLU A 1 390 ? -3.365  30.158  22.519  1.00 123.30 ? 390 GLU A CD    1 
ATOM   3005 O  OE1   . GLU A 1 390 ? -2.523  29.542  23.206  1.00 119.85 ? 390 GLU A OE1   1 
ATOM   3006 O  OE2   . GLU A 1 390 ? -3.057  30.847  21.524  1.00 127.74 ? 390 GLU A OE2   1 
ATOM   3007 N  N     . TRP A 1 391 ? -4.225  25.562  24.341  1.00 156.03 ? 391 TRP A N     1 
ATOM   3008 C  CA    . TRP A 1 391 ? -4.402  24.336  25.104  1.00 157.58 ? 391 TRP A CA    1 
ATOM   3009 C  C     . TRP A 1 391 ? -3.650  24.418  26.424  1.00 167.97 ? 391 TRP A C     1 
ATOM   3010 O  O     . TRP A 1 391 ? -2.542  24.961  26.487  1.00 163.13 ? 391 TRP A O     1 
ATOM   3011 C  CB    . TRP A 1 391 ? -3.920  23.122  24.301  1.00 153.01 ? 391 TRP A CB    1 
ATOM   3012 C  CG    . TRP A 1 391 ? -3.968  21.833  25.060  1.00 154.11 ? 391 TRP A CG    1 
ATOM   3013 C  CD1   . TRP A 1 391 ? -5.042  21.002  25.197  1.00 156.27 ? 391 TRP A CD1   1 
ATOM   3014 C  CD2   . TRP A 1 391 ? -2.893  21.220  25.781  1.00 156.07 ? 391 TRP A CD2   1 
ATOM   3015 N  NE1   . TRP A 1 391 ? -4.703  19.912  25.961  1.00 157.04 ? 391 TRP A NE1   1 
ATOM   3016 C  CE2   . TRP A 1 391 ? -3.389  20.021  26.332  1.00 154.68 ? 391 TRP A CE2   1 
ATOM   3017 C  CE3   . TRP A 1 391 ? -1.559  21.568  26.015  1.00 153.02 ? 391 TRP A CE3   1 
ATOM   3018 C  CZ2   . TRP A 1 391 ? -2.598  19.171  27.102  1.00 157.10 ? 391 TRP A CZ2   1 
ATOM   3019 C  CZ3   . TRP A 1 391 ? -0.776  20.723  26.781  1.00 150.34 ? 391 TRP A CZ3   1 
ATOM   3020 C  CH2   . TRP A 1 391 ? -1.298  19.538  27.315  1.00 153.73 ? 391 TRP A CH2   1 
ATOM   3021 N  N     . ARG A 1 392 ? -4.258  23.875  27.474  1.00 166.04 ? 392 ARG A N     1 
ATOM   3022 C  CA    . ARG A 1 392 ? -3.645  23.770  28.787  1.00 172.46 ? 392 ARG A CA    1 
ATOM   3023 C  C     . ARG A 1 392 ? -3.758  22.342  29.296  1.00 177.92 ? 392 ARG A C     1 
ATOM   3024 O  O     . ARG A 1 392 ? -4.719  21.636  28.972  1.00 176.32 ? 392 ARG A O     1 
ATOM   3025 C  CB    . ARG A 1 392 ? -4.300  24.725  29.795  1.00 175.06 ? 392 ARG A CB    1 
ATOM   3026 C  CG    . ARG A 1 392 ? -4.143  26.198  29.457  1.00 172.67 ? 392 ARG A CG    1 
ATOM   3027 C  CD    . ARG A 1 392 ? -4.531  27.075  30.637  1.00 172.30 ? 392 ARG A CD    1 
ATOM   3028 N  NE    . ARG A 1 392 ? -5.888  26.807  31.100  1.00 170.82 ? 392 ARG A NE    1 
ATOM   3029 C  CZ    . ARG A 1 392 ? -6.446  27.383  32.156  1.00 168.82 ? 392 ARG A CZ    1 
ATOM   3030 N  NH1   . ARG A 1 392 ? -5.791  28.271  32.886  1.00 165.55 ? 392 ARG A NH1   1 
ATOM   3031 N  NH2   . ARG A 1 392 ? -7.692  27.058  32.489  1.00 166.54 ? 392 ARG A NH2   1 
ATOM   3032 N  N     . PRO A 1 393 ? -2.790  21.889  30.098  1.00 183.56 ? 393 PRO A N     1 
ATOM   3033 C  CA    . PRO A 1 393 ? -2.835  20.513  30.615  1.00 186.87 ? 393 PRO A CA    1 
ATOM   3034 C  C     . PRO A 1 393 ? -4.015  20.229  31.531  1.00 194.01 ? 393 PRO A C     1 
ATOM   3035 O  O     . PRO A 1 393 ? -4.174  19.081  31.961  1.00 196.36 ? 393 PRO A O     1 
ATOM   3036 C  CB    . PRO A 1 393 ? -1.507  20.378  31.377  1.00 189.85 ? 393 PRO A CB    1 
ATOM   3037 C  CG    . PRO A 1 393 ? -0.632  21.472  30.841  1.00 187.68 ? 393 PRO A CG    1 
ATOM   3038 C  CD    . PRO A 1 393 ? -1.558  22.593  30.490  1.00 185.58 ? 393 PRO A CD    1 
ATOM   3039 N  N     . GLN A 1 394 ? -4.851  21.221  31.839  1.00 197.51 ? 394 GLN A N     1 
ATOM   3040 C  CA    . GLN A 1 394 ? -5.998  21.001  32.711  1.00 195.93 ? 394 GLN A CA    1 
ATOM   3041 C  C     . GLN A 1 394 ? -7.239  20.536  31.961  1.00 190.66 ? 394 GLN A C     1 
ATOM   3042 O  O     . GLN A 1 394 ? -8.133  19.943  32.578  1.00 190.04 ? 394 GLN A O     1 
ATOM   3043 C  CB    . GLN A 1 394 ? -6.338  22.278  33.490  1.00 199.68 ? 394 GLN A CB    1 
ATOM   3044 C  CG    . GLN A 1 394 ? -5.363  22.630  34.609  1.00 211.91 ? 394 GLN A CG    1 
ATOM   3045 C  CD    . GLN A 1 394 ? -4.008  23.077  34.096  1.00 210.29 ? 394 GLN A CD    1 
ATOM   3046 O  OE1   . GLN A 1 394 ? -3.854  23.399  32.918  1.00 202.28 ? 394 GLN A OE1   1 
ATOM   3047 N  NE2   . GLN A 1 394 ? -3.016  23.094  34.980  1.00 217.13 ? 394 GLN A NE2   1 
ATOM   3048 N  N     . ASP A 1 395 ? -7.319  20.793  30.658  1.00 180.71 ? 395 ASP A N     1 
ATOM   3049 C  CA    . ASP A 1 395 ? -8.467  20.388  29.864  1.00 175.31 ? 395 ASP A CA    1 
ATOM   3050 C  C     . ASP A 1 395 ? -8.371  18.903  29.513  1.00 181.81 ? 395 ASP A C     1 
ATOM   3051 O  O     . ASP A 1 395 ? -7.390  18.222  29.826  1.00 183.07 ? 395 ASP A O     1 
ATOM   3052 C  CB    . ASP A 1 395 ? -8.568  21.244  28.603  1.00 166.72 ? 395 ASP A CB    1 
ATOM   3053 C  CG    . ASP A 1 395 ? -8.572  22.729  28.906  1.00 161.24 ? 395 ASP A CG    1 
ATOM   3054 O  OD1   . ASP A 1 395 ? -9.063  23.115  29.986  1.00 162.62 ? 395 ASP A OD1   1 
ATOM   3055 O  OD2   . ASP A 1 395 ? -8.080  23.511  28.065  1.00 151.67 ? 395 ASP A OD2   1 
ATOM   3056 N  N     . GLU A 1 396 ? -9.409  18.390  28.853  1.00 205.66 ? 396 GLU A N     1 
ATOM   3057 C  CA    . GLU A 1 396 ? -9.423  16.998  28.423  1.00 202.16 ? 396 GLU A CA    1 
ATOM   3058 C  C     . GLU A 1 396 ? -8.921  16.819  26.997  1.00 196.36 ? 396 GLU A C     1 
ATOM   3059 O  O     . GLU A 1 396 ? -8.435  15.736  26.650  1.00 189.86 ? 396 GLU A O     1 
ATOM   3060 C  CB    . GLU A 1 396 ? -10.836 16.420  28.538  1.00 201.48 ? 396 GLU A CB    1 
ATOM   3061 C  CG    . GLU A 1 396 ? -10.923 14.935  28.226  1.00 195.02 ? 396 GLU A CG    1 
ATOM   3062 C  CD    . GLU A 1 396 ? -12.353 14.437  28.143  1.00 189.02 ? 396 GLU A CD    1 
ATOM   3063 O  OE1   . GLU A 1 396 ? -13.260 15.266  27.919  1.00 190.24 ? 396 GLU A OE1   1 
ATOM   3064 O  OE2   . GLU A 1 396 ? -12.570 13.217  28.301  1.00 182.13 ? 396 GLU A OE2   1 
ATOM   3065 N  N     . GLU A 1 397 ? -9.029  17.851  26.169  1.00 161.79 ? 397 GLU A N     1 
ATOM   3066 C  CA    . GLU A 1 397 ? -8.571  17.754  24.791  1.00 147.37 ? 397 GLU A CA    1 
ATOM   3067 C  C     . GLU A 1 397 ? -7.064  17.519  24.759  1.00 143.38 ? 397 GLU A C     1 
ATOM   3068 O  O     . GLU A 1 397 ? -6.308  18.287  25.371  1.00 147.40 ? 397 GLU A O     1 
ATOM   3069 C  CB    . GLU A 1 397 ? -8.921  19.027  24.022  1.00 142.26 ? 397 GLU A CB    1 
ATOM   3070 C  CG    . GLU A 1 397 ? -10.412 19.304  23.907  1.00 133.10 ? 397 GLU A CG    1 
ATOM   3071 C  CD    . GLU A 1 397 ? -11.097 18.411  22.892  1.00 129.41 ? 397 GLU A CD    1 
ATOM   3072 O  OE1   . GLU A 1 397 ? -10.391 17.674  22.173  1.00 131.51 ? 397 GLU A OE1   1 
ATOM   3073 O  OE2   . GLU A 1 397 ? -12.343 18.449  22.811  1.00 126.88 ? 397 GLU A OE2   1 
ATOM   3074 N  N     . PRO A 1 398 ? -6.588  16.482  24.072  1.00 132.91 ? 398 PRO A N     1 
ATOM   3075 C  CA    . PRO A 1 398 ? -5.139  16.283  23.959  1.00 122.99 ? 398 PRO A CA    1 
ATOM   3076 C  C     . PRO A 1 398 ? -4.521  17.296  23.008  1.00 114.54 ? 398 PRO A C     1 
ATOM   3077 O  O     . PRO A 1 398 ? -5.102  17.643  21.976  1.00 115.02 ? 398 PRO A O     1 
ATOM   3078 C  CB    . PRO A 1 398 ? -5.019  14.856  23.416  1.00 113.83 ? 398 PRO A CB    1 
ATOM   3079 C  CG    . PRO A 1 398 ? -6.289  14.646  22.658  1.00 115.98 ? 398 PRO A CG    1 
ATOM   3080 C  CD    . PRO A 1 398 ? -7.350  15.413  23.404  1.00 127.90 ? 398 PRO A CD    1 
ATOM   3081 N  N     . CYS A 1 399 ? -3.326  17.772  23.367  1.00 119.33 ? 399 CYS A N     1 
ATOM   3082 C  CA    . CYS A 1 399 ? -2.659  18.775  22.543  1.00 116.01 ? 399 CYS A CA    1 
ATOM   3083 C  C     . CYS A 1 399 ? -2.261  18.215  21.183  1.00 99.57  ? 399 CYS A C     1 
ATOM   3084 O  O     . CYS A 1 399 ? -2.158  18.971  20.210  1.00 98.79  ? 399 CYS A O     1 
ATOM   3085 C  CB    . CYS A 1 399 ? -1.432  19.325  23.269  1.00 118.96 ? 399 CYS A CB    1 
ATOM   3086 S  SG    . CYS A 1 399 ? -0.086  18.137  23.469  1.00 110.11 ? 399 CYS A SG    1 
ATOM   3087 N  N     . ALA A 1 400 ? -2.032  16.907  21.093  1.00 86.70  ? 400 ALA A N     1 
ATOM   3088 C  CA    . ALA A 1 400 ? -1.659  16.259  19.845  1.00 81.48  ? 400 ALA A CA    1 
ATOM   3089 C  C     . ALA A 1 400 ? -2.605  15.100  19.571  1.00 84.19  ? 400 ALA A C     1 
ATOM   3090 O  O     . ALA A 1 400 ? -3.046  14.414  20.498  1.00 85.22  ? 400 ALA A O     1 
ATOM   3091 C  CB    . ALA A 1 400 ? -0.210  15.758  19.883  1.00 79.50  ? 400 ALA A CB    1 
ATOM   3092 N  N     . HIS A 1 401 ? -2.915  14.889  18.297  1.00 73.38  ? 401 HIS A N     1 
ATOM   3093 C  CA    . HIS A 1 401 ? -3.825  13.816  17.929  1.00 66.22  ? 401 HIS A CA    1 
ATOM   3094 C  C     . HIS A 1 401 ? -3.161  12.461  18.163  1.00 69.91  ? 401 HIS A C     1 
ATOM   3095 O  O     . HIS A 1 401 ? -1.951  12.318  17.961  1.00 68.58  ? 401 HIS A O     1 
ATOM   3096 C  CB    . HIS A 1 401 ? -4.247  13.947  16.466  1.00 65.52  ? 401 HIS A CB    1 
ATOM   3097 C  CG    . HIS A 1 401 ? -5.285  12.954  16.047  1.00 65.88  ? 401 HIS A CG    1 
ATOM   3098 N  ND1   . HIS A 1 401 ? -4.977  11.796  15.366  1.00 66.43  ? 401 HIS A ND1   1 
ATOM   3099 C  CD2   . HIS A 1 401 ? -6.629  12.944  16.216  1.00 66.43  ? 401 HIS A CD2   1 
ATOM   3100 C  CE1   . HIS A 1 401 ? -6.086  11.117  15.132  1.00 65.75  ? 401 HIS A CE1   1 
ATOM   3101 N  NE2   . HIS A 1 401 ? -7.102  11.792  15.638  1.00 63.92  ? 401 HIS A NE2   1 
ATOM   3102 N  N     . PRO A 1 402 ? -3.922  11.451  18.595  1.00 69.37  ? 402 PRO A N     1 
ATOM   3103 C  CA    . PRO A 1 402 ? -3.310  10.131  18.823  1.00 60.26  ? 402 PRO A CA    1 
ATOM   3104 C  C     . PRO A 1 402 ? -2.586  9.588   17.604  1.00 64.54  ? 402 PRO A C     1 
ATOM   3105 O  O     . PRO A 1 402 ? -1.483  9.043   17.736  1.00 69.09  ? 402 PRO A O     1 
ATOM   3106 C  CB    . PRO A 1 402 ? -4.510  9.256   19.212  1.00 59.39  ? 402 PRO A CB    1 
ATOM   3107 C  CG    . PRO A 1 402 ? -5.511  10.216  19.764  1.00 64.53  ? 402 PRO A CG    1 
ATOM   3108 C  CD    . PRO A 1 402 ? -5.348  11.475  18.963  1.00 67.21  ? 402 PRO A CD    1 
ATOM   3109 N  N     . ASN A 1 403 ? -3.172  9.725   16.418  1.00 67.53  ? 403 ASN A N     1 
ATOM   3110 C  CA    . ASN A 1 403 ? -2.571  9.226   15.190  1.00 69.49  ? 403 ASN A CA    1 
ATOM   3111 C  C     . ASN A 1 403 ? -1.653  10.247  14.526  1.00 64.82  ? 403 ASN A C     1 
ATOM   3112 O  O     . ASN A 1 403 ? -1.246  10.041  13.377  1.00 64.28  ? 403 ASN A O     1 
ATOM   3113 C  CB    . ASN A 1 403 ? -3.662  8.788   14.210  1.00 70.89  ? 403 ASN A CB    1 
ATOM   3114 C  CG    . ASN A 1 403 ? -3.147  7.834   13.151  1.00 75.95  ? 403 ASN A CG    1 
ATOM   3115 O  OD1   . ASN A 1 403 ? -2.146  7.145   13.352  1.00 75.13  ? 403 ASN A OD1   1 
ATOM   3116 N  ND2   . ASN A 1 403 ? -3.831  7.787   12.014  1.00 90.24  ? 403 ASN A ND2   1 
ATOM   3117 N  N     . SER A 1 404 ? -1.323  11.337  15.215  1.00 66.73  ? 404 SER A N     1 
ATOM   3118 C  CA    . SER A 1 404 ? -0.394  12.314  14.662  1.00 59.16  ? 404 SER A CA    1 
ATOM   3119 C  C     . SER A 1 404 ? 0.940   11.649  14.347  1.00 60.74  ? 404 SER A C     1 
ATOM   3120 O  O     . SER A 1 404 ? 1.392   10.752  15.064  1.00 59.26  ? 404 SER A O     1 
ATOM   3121 C  CB    . SER A 1 404 ? -0.196  13.472  15.640  1.00 62.98  ? 404 SER A CB    1 
ATOM   3122 O  OG    . SER A 1 404 ? 0.250   13.006  16.901  1.00 61.68  ? 404 SER A OG    1 
ATOM   3123 N  N     . ARG A 1 405 ? 1.573   12.097  13.266  1.00 54.89  ? 405 ARG A N     1 
ATOM   3124 C  CA    . ARG A 1 405 ? 2.758   11.447  12.730  1.00 53.06  ? 405 ARG A CA    1 
ATOM   3125 C  C     . ARG A 1 405 ? 3.877   12.463  12.541  1.00 55.89  ? 405 ARG A C     1 
ATOM   3126 O  O     . ARG A 1 405 ? 3.678   13.676  12.644  1.00 47.70  ? 405 ARG A O     1 
ATOM   3127 C  CB    . ARG A 1 405 ? 2.454   10.757  11.393  1.00 53.60  ? 405 ARG A CB    1 
ATOM   3128 C  CG    . ARG A 1 405 ? 1.294   9.779   11.440  1.00 61.78  ? 405 ARG A CG    1 
ATOM   3129 C  CD    . ARG A 1 405 ? 1.752   8.393   11.853  1.00 55.16  ? 405 ARG A CD    1 
ATOM   3130 N  NE    . ARG A 1 405 ? 0.636   7.458   11.927  1.00 61.31  ? 405 ARG A NE    1 
ATOM   3131 C  CZ    . ARG A 1 405 ? 0.764   6.147   12.072  1.00 64.75  ? 405 ARG A CZ    1 
ATOM   3132 N  NH1   . ARG A 1 405 ? 1.953   5.572   12.146  1.00 63.41  ? 405 ARG A NH1   1 
ATOM   3133 N  NH2   . ARG A 1 405 ? -0.329  5.393   12.143  1.00 65.91  ? 405 ARG A NH2   1 
ATOM   3134 N  N     . PHE A 1 406 ? 5.069   11.940  12.263  1.00 61.36  ? 406 PHE A N     1 
ATOM   3135 C  CA    . PHE A 1 406 ? 6.212   12.735  11.839  1.00 44.31  ? 406 PHE A CA    1 
ATOM   3136 C  C     . PHE A 1 406 ? 6.819   12.089  10.603  1.00 45.82  ? 406 PHE A C     1 
ATOM   3137 O  O     . PHE A 1 406 ? 6.845   10.860  10.483  1.00 59.02  ? 406 PHE A O     1 
ATOM   3138 C  CB    . PHE A 1 406 ? 7.267   12.865  12.951  1.00 56.44  ? 406 PHE A CB    1 
ATOM   3139 C  CG    . PHE A 1 406 ? 7.781   11.548  13.467  1.00 40.70  ? 406 PHE A CG    1 
ATOM   3140 C  CD1   . PHE A 1 406 ? 8.789   10.871  12.800  1.00 40.04  ? 406 PHE A CD1   1 
ATOM   3141 C  CD2   . PHE A 1 406 ? 7.266   10.997  14.628  1.00 43.69  ? 406 PHE A CD2   1 
ATOM   3142 C  CE1   . PHE A 1 406 ? 9.265   9.662   13.275  1.00 30.10  ? 406 PHE A CE1   1 
ATOM   3143 C  CE2   . PHE A 1 406 ? 7.740   9.789   15.108  1.00 38.05  ? 406 PHE A CE2   1 
ATOM   3144 C  CZ    . PHE A 1 406 ? 8.740   9.121   14.430  1.00 26.73  ? 406 PHE A CZ    1 
ATOM   3145 N  N     . CYS A 1 407 ? 7.297   12.920  9.680   1.00 33.68  ? 407 CYS A N     1 
ATOM   3146 C  CA    . CYS A 1 407 ? 7.845   12.460  8.408   1.00 37.27  ? 407 CYS A CA    1 
ATOM   3147 C  C     . CYS A 1 407 ? 9.296   12.913  8.323   1.00 42.91  ? 407 CYS A C     1 
ATOM   3148 O  O     . CYS A 1 407 ? 9.569   14.102  8.125   1.00 53.94  ? 407 CYS A O     1 
ATOM   3149 C  CB    . CYS A 1 407 ? 7.023   12.999  7.237   1.00 40.54  ? 407 CYS A CB    1 
ATOM   3150 S  SG    . CYS A 1 407 ? 7.300   12.160  5.659   1.00 45.28  ? 407 CYS A SG    1 
ATOM   3151 N  N     . THR A 1 408 ? 10.223  11.971  8.471   1.00 44.24  ? 408 THR A N     1 
ATOM   3152 C  CA    . THR A 1 408 ? 11.642  12.282  8.520   1.00 43.70  ? 408 THR A CA    1 
ATOM   3153 C  C     . THR A 1 408 ? 12.429  11.353  7.608   1.00 36.82  ? 408 THR A C     1 
ATOM   3154 O  O     . THR A 1 408 ? 12.072  10.182  7.444   1.00 47.75  ? 408 THR A O     1 
ATOM   3155 C  CB    . THR A 1 408 ? 12.185  12.167  9.952   1.00 41.22  ? 408 THR A CB    1 
ATOM   3156 O  OG1   . THR A 1 408 ? 13.602  12.377  9.948   1.00 41.37  ? 408 THR A OG1   1 
ATOM   3157 C  CG2   . THR A 1 408 ? 11.881  10.793  10.527  1.00 44.62  ? 408 THR A CG2   1 
ATOM   3158 N  N     . PRO A 1 409 ? 13.509  11.850  7.007   1.00 41.29  ? 409 PRO A N     1 
ATOM   3159 C  CA    . PRO A 1 409 ? 14.313  11.005  6.118   1.00 43.18  ? 409 PRO A CA    1 
ATOM   3160 C  C     . PRO A 1 409 ? 15.053  9.924   6.890   1.00 59.81  ? 409 PRO A C     1 
ATOM   3161 O  O     . PRO A 1 409 ? 15.430  10.099  8.052   1.00 51.29  ? 409 PRO A O     1 
ATOM   3162 C  CB    . PRO A 1 409 ? 15.294  11.994  5.474   1.00 41.52  ? 409 PRO A CB    1 
ATOM   3163 C  CG    . PRO A 1 409 ? 14.711  13.358  5.730   1.00 36.69  ? 409 PRO A CG    1 
ATOM   3164 C  CD    . PRO A 1 409 ? 13.989  13.240  7.033   1.00 48.86  ? 409 PRO A CD    1 
ATOM   3165 N  N     . ALA A 1 410 ? 15.268  8.791   6.218   1.00 50.51  ? 410 ALA A N     1 
ATOM   3166 C  CA    . ALA A 1 410 ? 15.920  7.655   6.859   1.00 55.53  ? 410 ALA A CA    1 
ATOM   3167 C  C     . ALA A 1 410 ? 17.424  7.853   7.004   1.00 58.72  ? 410 ALA A C     1 
ATOM   3168 O  O     . ALA A 1 410 ? 18.036  7.263   7.901   1.00 49.95  ? 410 ALA A O     1 
ATOM   3169 C  CB    . ALA A 1 410 ? 15.636  6.373   6.075   1.00 44.96  ? 410 ALA A CB    1 
ATOM   3170 N  N     . SER A 1 411 ? 18.034  8.669   6.142   1.00 56.88  ? 411 SER A N     1 
ATOM   3171 C  CA    . SER A 1 411 ? 19.477  8.870   6.206   1.00 58.69  ? 411 SER A CA    1 
ATOM   3172 C  C     . SER A 1 411 ? 19.905  9.641   7.447   1.00 55.76  ? 411 SER A C     1 
ATOM   3173 O  O     . SER A 1 411 ? 21.072  9.554   7.843   1.00 56.93  ? 411 SER A O     1 
ATOM   3174 C  CB    . SER A 1 411 ? 19.965  9.601   4.954   1.00 63.75  ? 411 SER A CB    1 
ATOM   3175 O  OG    . SER A 1 411 ? 19.454  10.922  4.904   1.00 71.28  ? 411 SER A OG    1 
ATOM   3176 N  N     . GLN A 1 412 ? 18.994  10.390  8.068   1.00 61.05  ? 412 GLN A N     1 
ATOM   3177 C  CA    . GLN A 1 412 ? 19.331  11.192  9.236   1.00 49.49  ? 412 GLN A CA    1 
ATOM   3178 C  C     . GLN A 1 412 ? 19.307  10.398  10.535  1.00 61.38  ? 412 GLN A C     1 
ATOM   3179 O  O     . GLN A 1 412 ? 19.680  10.943  11.580  1.00 51.62  ? 412 GLN A O     1 
ATOM   3180 C  CB    . GLN A 1 412 ? 18.376  12.384  9.345   1.00 52.00  ? 412 GLN A CB    1 
ATOM   3181 C  CG    . GLN A 1 412 ? 18.408  13.314  8.143   1.00 53.73  ? 412 GLN A CG    1 
ATOM   3182 C  CD    . GLN A 1 412 ? 17.470  14.495  8.295   1.00 63.03  ? 412 GLN A CD    1 
ATOM   3183 O  OE1   . GLN A 1 412 ? 17.530  15.454  7.525   1.00 72.52  ? 412 GLN A OE1   1 
ATOM   3184 N  NE2   . GLN A 1 412 ? 16.596  14.432  9.293   1.00 58.84  ? 412 GLN A NE2   1 
ATOM   3185 N  N     . CYS A 1 413 ? 18.883  9.142   10.502  1.00 61.24  ? 413 CYS A N     1 
ATOM   3186 C  CA    . CYS A 1 413 ? 18.853  8.337   11.716  1.00 58.13  ? 413 CYS A CA    1 
ATOM   3187 C  C     . CYS A 1 413 ? 20.277  8.038   12.172  1.00 58.40  ? 413 CYS A C     1 
ATOM   3188 O  O     . CYS A 1 413 ? 21.120  7.659   11.350  1.00 55.04  ? 413 CYS A O     1 
ATOM   3189 C  CB    . CYS A 1 413 ? 18.089  7.037   11.481  1.00 49.91  ? 413 CYS A CB    1 
ATOM   3190 S  SG    . CYS A 1 413 ? 17.937  5.991   12.948  1.00 49.91  ? 413 CYS A SG    1 
ATOM   3191 N  N     . PRO A 1 414 ? 20.586  8.191   13.462  1.00 55.46  ? 414 PRO A N     1 
ATOM   3192 C  CA    . PRO A 1 414 ? 21.967  7.953   13.909  1.00 57.73  ? 414 PRO A CA    1 
ATOM   3193 C  C     . PRO A 1 414 ? 22.377  6.492   13.862  1.00 54.13  ? 414 PRO A C     1 
ATOM   3194 O  O     . PRO A 1 414 ? 23.569  6.205   13.692  1.00 47.03  ? 414 PRO A O     1 
ATOM   3195 C  CB    . PRO A 1 414 ? 21.967  8.494   15.345  1.00 58.63  ? 414 PRO A CB    1 
ATOM   3196 C  CG    . PRO A 1 414 ? 20.545  8.379   15.786  1.00 56.12  ? 414 PRO A CG    1 
ATOM   3197 C  CD    . PRO A 1 414 ? 19.712  8.635   14.561  1.00 58.00  ? 414 PRO A CD    1 
ATOM   3198 N  N     . ILE A 1 415 ? 21.437  5.559   14.002  1.00 62.96  ? 415 ILE A N     1 
ATOM   3199 C  CA    . ILE A 1 415 ? 21.772  4.139   14.052  1.00 51.10  ? 415 ILE A CA    1 
ATOM   3200 C  C     . ILE A 1 415 ? 21.299  3.440   12.785  1.00 58.35  ? 415 ILE A C     1 
ATOM   3201 O  O     . ILE A 1 415 ? 21.018  2.236   12.797  1.00 48.66  ? 415 ILE A O     1 
ATOM   3202 C  CB    . ILE A 1 415 ? 21.169  3.470   15.301  1.00 49.96  ? 415 ILE A CB    1 
ATOM   3203 C  CG1   . ILE A 1 415 ? 19.643  3.572   15.276  1.00 45.76  ? 415 ILE A CG1   1 
ATOM   3204 C  CG2   . ILE A 1 415 ? 21.734  4.097   16.566  1.00 43.96  ? 415 ILE A CG2   1 
ATOM   3205 C  CD1   . ILE A 1 415 ? 18.970  2.920   16.461  1.00 50.20  ? 415 ILE A CD1   1 
ATOM   3206 N  N     . ILE A 1 416 ? 21.209  4.185   11.682  1.00 55.91  ? 416 ILE A N     1 
ATOM   3207 C  CA    . ILE A 1 416 ? 20.823  3.582   10.413  1.00 50.91  ? 416 ILE A CA    1 
ATOM   3208 C  C     . ILE A 1 416 ? 21.859  2.541   10.019  1.00 50.37  ? 416 ILE A C     1 
ATOM   3209 O  O     . ILE A 1 416 ? 23.070  2.787   10.083  1.00 65.91  ? 416 ILE A O     1 
ATOM   3210 C  CB    . ILE A 1 416 ? 20.667  4.660   9.331   1.00 48.81  ? 416 ILE A CB    1 
ATOM   3211 C  CG1   . ILE A 1 416 ? 20.218  4.030   8.010   1.00 52.96  ? 416 ILE A CG1   1 
ATOM   3212 C  CG2   . ILE A 1 416 ? 21.968  5.424   9.148   1.00 55.86  ? 416 ILE A CG2   1 
ATOM   3213 C  CD1   . ILE A 1 416 ? 18.846  3.394   8.072   1.00 57.29  ? 416 ILE A CD1   1 
ATOM   3214 N  N     . ASP A 1 417 ? 21.387  1.367   9.613   1.00 56.31  ? 417 ASP A N     1 
ATOM   3215 C  CA    . ASP A 1 417 ? 22.297  0.284   9.274   1.00 63.23  ? 417 ASP A CA    1 
ATOM   3216 C  C     . ASP A 1 417 ? 23.020  0.594   7.965   1.00 63.60  ? 417 ASP A C     1 
ATOM   3217 O  O     . ASP A 1 417 ? 22.406  1.098   7.018   1.00 62.91  ? 417 ASP A O     1 
ATOM   3218 C  CB    . ASP A 1 417 ? 21.538  -1.038  9.162   1.00 52.55  ? 417 ASP A CB    1 
ATOM   3219 C  CG    . ASP A 1 417 ? 22.456  -2.219  8.909   1.00 53.68  ? 417 ASP A CG    1 
ATOM   3220 O  OD1   . ASP A 1 417 ? 23.080  -2.273  7.829   1.00 57.27  ? 417 ASP A OD1   1 
ATOM   3221 O  OD2   . ASP A 1 417 ? 22.562  -3.090  9.798   1.00 47.87  ? 417 ASP A OD2   1 
ATOM   3222 N  N     . PRO A 1 418 ? 24.321  0.297   7.875   1.00 63.33  ? 418 PRO A N     1 
ATOM   3223 C  CA    . PRO A 1 418 ? 25.080  0.642   6.664   1.00 61.76  ? 418 PRO A CA    1 
ATOM   3224 C  C     . PRO A 1 418 ? 24.749  -0.245  5.473   1.00 66.26  ? 418 PRO A C     1 
ATOM   3225 O  O     . PRO A 1 418 ? 25.546  -0.354  4.535   1.00 65.34  ? 418 PRO A O     1 
ATOM   3226 C  CB    . PRO A 1 418 ? 26.537  0.461   7.107   1.00 66.61  ? 418 PRO A CB    1 
ATOM   3227 C  CG    . PRO A 1 418 ? 26.467  -0.573  8.180   1.00 60.71  ? 418 PRO A CG    1 
ATOM   3228 C  CD    . PRO A 1 418 ? 25.168  -0.332  8.904   1.00 60.40  ? 418 PRO A CD    1 
ATOM   3229 N  N     . ALA A 1 419 ? 23.576  -0.885  5.498   1.00 68.06  ? 419 ALA A N     1 
ATOM   3230 C  CA    . ALA A 1 419 ? 23.142  -1.713  4.379   1.00 70.22  ? 419 ALA A CA    1 
ATOM   3231 C  C     . ALA A 1 419 ? 21.667  -1.503  4.053   1.00 71.12  ? 419 ALA A C     1 
ATOM   3232 O  O     . ALA A 1 419 ? 21.051  -2.375  3.427   1.00 68.62  ? 419 ALA A O     1 
ATOM   3233 C  CB    . ALA A 1 419 ? 23.404  -3.196  4.664   1.00 51.60  ? 419 ALA A CB    1 
ATOM   3234 N  N     . TRP A 1 420 ? 21.086  -0.372  4.456   1.00 69.06  ? 420 TRP A N     1 
ATOM   3235 C  CA    . TRP A 1 420 ? 19.672  -0.116  4.219   1.00 67.81  ? 420 TRP A CA    1 
ATOM   3236 C  C     . TRP A 1 420 ? 19.368  0.243   2.770   1.00 67.52  ? 420 TRP A C     1 
ATOM   3237 O  O     . TRP A 1 420 ? 18.192  0.271   2.392   1.00 75.91  ? 420 TRP A O     1 
ATOM   3238 C  CB    . TRP A 1 420 ? 19.178  1.000   5.143   1.00 63.76  ? 420 TRP A CB    1 
ATOM   3239 C  CG    . TRP A 1 420 ? 19.541  2.378   4.683   1.00 69.44  ? 420 TRP A CG    1 
ATOM   3240 C  CD1   . TRP A 1 420 ? 20.758  2.986   4.790   1.00 64.24  ? 420 TRP A CD1   1 
ATOM   3241 C  CD2   . TRP A 1 420 ? 18.673  3.326   4.051   1.00 69.39  ? 420 TRP A CD2   1 
ATOM   3242 N  NE1   . TRP A 1 420 ? 20.703  4.252   4.258   1.00 68.57  ? 420 TRP A NE1   1 
ATOM   3243 C  CE2   . TRP A 1 420 ? 19.433  4.485   3.799   1.00 72.06  ? 420 TRP A CE2   1 
ATOM   3244 C  CE3   . TRP A 1 420 ? 17.327  3.306   3.672   1.00 61.78  ? 420 TRP A CE3   1 
ATOM   3245 C  CZ2   . TRP A 1 420 ? 18.893  5.613   3.185   1.00 63.09  ? 420 TRP A CZ2   1 
ATOM   3246 C  CZ3   . TRP A 1 420 ? 16.793  4.427   3.064   1.00 57.20  ? 420 TRP A CZ3   1 
ATOM   3247 C  CH2   . TRP A 1 420 ? 17.574  5.564   2.826   1.00 57.07  ? 420 TRP A CH2   1 
ATOM   3248 N  N     . GLU A 1 421 ? 20.388  0.520   1.958   1.00 62.96  ? 421 GLU A N     1 
ATOM   3249 C  CA    . GLU A 1 421 ? 20.206  0.775   0.534   1.00 71.58  ? 421 GLU A CA    1 
ATOM   3250 C  C     . GLU A 1 421 ? 20.993  -0.197  -0.335  1.00 75.17  ? 421 GLU A C     1 
ATOM   3251 O  O     . GLU A 1 421 ? 21.137  0.041   -1.540  1.00 78.08  ? 421 GLU A O     1 
ATOM   3252 C  CB    . GLU A 1 421 ? 20.593  2.217   0.192   1.00 63.44  ? 421 GLU A CB    1 
ATOM   3253 C  CG    . GLU A 1 421 ? 19.578  3.254   0.644   1.00 71.91  ? 421 GLU A CG    1 
ATOM   3254 C  CD    . GLU A 1 421 ? 19.937  4.657   0.196   1.00 69.79  ? 421 GLU A CD    1 
ATOM   3255 O  OE1   . GLU A 1 421 ? 21.133  4.914   -0.056  1.00 70.46  ? 421 GLU A OE1   1 
ATOM   3256 O  OE2   . GLU A 1 421 ? 19.023  5.502   0.089   1.00 76.55  ? 421 GLU A OE2   1 
ATOM   3257 N  N     . SER A 1 422 ? 21.506  -1.280  0.240   1.00 74.92  ? 422 SER A N     1 
ATOM   3258 C  CA    . SER A 1 422 ? 22.208  -2.275  -0.554  1.00 91.99  ? 422 SER A CA    1 
ATOM   3259 C  C     . SER A 1 422 ? 21.228  -2.980  -1.490  1.00 98.88  ? 422 SER A C     1 
ATOM   3260 O  O     . SER A 1 422 ? 20.097  -3.281  -1.095  1.00 98.14  ? 422 SER A O     1 
ATOM   3261 C  CB    . SER A 1 422 ? 22.898  -3.296  0.349   1.00 96.34  ? 422 SER A CB    1 
ATOM   3262 O  OG    . SER A 1 422 ? 23.856  -2.670  1.185   1.00 92.47  ? 422 SER A OG    1 
ATOM   3263 N  N     . PRO A 1 423 ? 21.630  -3.260  -2.732  1.00 108.35 ? 423 PRO A N     1 
ATOM   3264 C  CA    . PRO A 1 423 ? 20.689  -3.871  -3.683  1.00 113.91 ? 423 PRO A CA    1 
ATOM   3265 C  C     . PRO A 1 423 ? 20.417  -5.344  -3.422  1.00 127.18 ? 423 PRO A C     1 
ATOM   3266 O  O     . PRO A 1 423 ? 19.344  -5.830  -3.804  1.00 125.29 ? 423 PRO A O     1 
ATOM   3267 C  CB    . PRO A 1 423 ? 21.380  -3.663  -5.036  1.00 114.18 ? 423 PRO A CB    1 
ATOM   3268 C  CG    . PRO A 1 423 ? 22.836  -3.638  -4.697  1.00 106.56 ? 423 PRO A CG    1 
ATOM   3269 C  CD    . PRO A 1 423 ? 22.936  -2.970  -3.349  1.00 104.85 ? 423 PRO A CD    1 
ATOM   3270 N  N     . GLU A 1 424 ? 21.339  -6.068  -2.787  1.00 158.61 ? 424 GLU A N     1 
ATOM   3271 C  CA    . GLU A 1 424 ? 21.163  -7.500  -2.573  1.00 152.28 ? 424 GLU A CA    1 
ATOM   3272 C  C     . GLU A 1 424 ? 20.320  -7.822  -1.347  1.00 149.71 ? 424 GLU A C     1 
ATOM   3273 O  O     . GLU A 1 424 ? 19.680  -8.880  -1.306  1.00 152.98 ? 424 GLU A O     1 
ATOM   3274 C  CB    . GLU A 1 424 ? 22.524  -8.193  -2.445  1.00 156.80 ? 424 GLU A CB    1 
ATOM   3275 C  CG    . GLU A 1 424 ? 23.209  -7.998  -1.099  1.00 158.71 ? 424 GLU A CG    1 
ATOM   3276 C  CD    . GLU A 1 424 ? 23.739  -6.592  -0.906  1.00 158.08 ? 424 GLU A CD    1 
ATOM   3277 O  OE1   . GLU A 1 424 ? 23.721  -5.811  -1.879  1.00 157.72 ? 424 GLU A OE1   1 
ATOM   3278 O  OE2   . GLU A 1 424 ? 24.176  -6.267  0.219   1.00 157.23 ? 424 GLU A OE2   1 
ATOM   3279 N  N     . GLY A 1 425 ? 20.303  -6.944  -0.348  1.00 111.43 ? 425 GLY A N     1 
ATOM   3280 C  CA    . GLY A 1 425 ? 19.543  -7.174  0.861   1.00 88.97  ? 425 GLY A CA    1 
ATOM   3281 C  C     . GLY A 1 425 ? 20.362  -7.839  1.954   1.00 90.30  ? 425 GLY A C     1 
ATOM   3282 O  O     . GLY A 1 425 ? 21.509  -8.250  1.767   1.00 100.54 ? 425 GLY A O     1 
ATOM   3283 N  N     . VAL A 1 426 ? 19.745  -7.945  3.127   1.00 64.00  ? 426 VAL A N     1 
ATOM   3284 C  CA    . VAL A 1 426 ? 20.398  -8.539  4.291   1.00 54.57  ? 426 VAL A CA    1 
ATOM   3285 C  C     . VAL A 1 426 ? 19.756  -9.887  4.597   1.00 77.93  ? 426 VAL A C     1 
ATOM   3286 O  O     . VAL A 1 426 ? 18.529  -10.028 4.488   1.00 68.05  ? 426 VAL A O     1 
ATOM   3287 C  CB    . VAL A 1 426 ? 20.327  -7.603  5.508   1.00 55.59  ? 426 VAL A CB    1 
ATOM   3288 C  CG1   . VAL A 1 426 ? 21.068  -6.306  5.222   1.00 57.92  ? 426 VAL A CG1   1 
ATOM   3289 C  CG2   . VAL A 1 426 ? 18.880  -7.326  5.883   1.00 66.96  ? 426 VAL A CG2   1 
ATOM   3290 N  N     . PRO A 1 427 ? 20.536  -10.902 4.979   1.00 70.32  ? 427 PRO A N     1 
ATOM   3291 C  CA    . PRO A 1 427 ? 19.961  -12.223 5.281   1.00 67.39  ? 427 PRO A CA    1 
ATOM   3292 C  C     . PRO A 1 427 ? 19.253  -12.207 6.629   1.00 64.00  ? 427 PRO A C     1 
ATOM   3293 O  O     . PRO A 1 427 ? 19.854  -11.882 7.655   1.00 66.23  ? 427 PRO A O     1 
ATOM   3294 C  CB    . PRO A 1 427 ? 21.187  -13.144 5.297   1.00 75.63  ? 427 PRO A CB    1 
ATOM   3295 C  CG    . PRO A 1 427 ? 22.310  -12.246 5.698   1.00 83.33  ? 427 PRO A CG    1 
ATOM   3296 C  CD    . PRO A 1 427 ? 22.004  -10.896 5.097   1.00 72.94  ? 427 PRO A CD    1 
ATOM   3297 N  N     . ILE A 1 428 ? 17.973  -12.564 6.623   1.00 65.22  ? 428 ILE A N     1 
ATOM   3298 C  CA    . ILE A 1 428 ? 17.161  -12.588 7.834   1.00 61.82  ? 428 ILE A CA    1 
ATOM   3299 C  C     . ILE A 1 428 ? 17.273  -13.964 8.476   1.00 63.45  ? 428 ILE A C     1 
ATOM   3300 O  O     . ILE A 1 428 ? 17.110  -14.989 7.804   1.00 61.75  ? 428 ILE A O     1 
ATOM   3301 C  CB    . ILE A 1 428 ? 15.696  -12.243 7.520   1.00 57.10  ? 428 ILE A CB    1 
ATOM   3302 C  CG1   . ILE A 1 428 ? 15.575  -10.780 7.089   1.00 56.08  ? 428 ILE A CG1   1 
ATOM   3303 C  CG2   . ILE A 1 428 ? 14.812  -12.527 8.724   1.00 46.85  ? 428 ILE A CG2   1 
ATOM   3304 C  CD1   . ILE A 1 428 ? 16.006  -9.793  8.153   1.00 46.94  ? 428 ILE A CD1   1 
ATOM   3305 N  N     . GLU A 1 429 ? 17.546  -13.988 9.781   1.00 56.93  ? 429 GLU A N     1 
ATOM   3306 C  CA    . GLU A 1 429 ? 17.704  -15.235 10.519  1.00 59.38  ? 429 GLU A CA    1 
ATOM   3307 C  C     . GLU A 1 429 ? 16.633  -15.432 11.584  1.00 55.50  ? 429 GLU A C     1 
ATOM   3308 O  O     . GLU A 1 429 ? 16.733  -16.372 12.381  1.00 53.11  ? 429 GLU A O     1 
ATOM   3309 C  CB    . GLU A 1 429 ? 19.093  -15.301 11.164  1.00 65.92  ? 429 GLU A CB    1 
ATOM   3310 C  CG    . GLU A 1 429 ? 20.245  -15.187 10.180  1.00 80.43  ? 429 GLU A CG    1 
ATOM   3311 C  CD    . GLU A 1 429 ? 21.594  -15.410 10.835  1.00 88.58  ? 429 GLU A CD    1 
ATOM   3312 O  OE1   . GLU A 1 429 ? 21.629  -15.945 11.963  1.00 79.30  ? 429 GLU A OE1   1 
ATOM   3313 O  OE2   . GLU A 1 429 ? 22.621  -15.048 10.223  1.00 98.55  ? 429 GLU A OE2   1 
ATOM   3314 N  N     . GLY A 1 430 ? 15.614  -14.577 11.623  1.00 55.32  ? 430 GLY A N     1 
ATOM   3315 C  CA    . GLY A 1 430 ? 14.566  -14.706 12.616  1.00 47.35  ? 430 GLY A CA    1 
ATOM   3316 C  C     . GLY A 1 430 ? 13.348  -13.852 12.327  1.00 44.38  ? 430 GLY A C     1 
ATOM   3317 O  O     . GLY A 1 430 ? 13.467  -12.756 11.771  1.00 45.73  ? 430 GLY A O     1 
ATOM   3318 N  N     . ILE A 1 431 ? 12.171  -14.344 12.705  1.00 40.61  ? 431 ILE A N     1 
ATOM   3319 C  CA    . ILE A 1 431 ? 10.910  -13.644 12.495  1.00 37.46  ? 431 ILE A CA    1 
ATOM   3320 C  C     . ILE A 1 431 ? 10.156  -13.599 13.816  1.00 33.21  ? 431 ILE A C     1 
ATOM   3321 O  O     . ILE A 1 431 ? 10.093  -14.598 14.540  1.00 36.57  ? 431 ILE A O     1 
ATOM   3322 C  CB    . ILE A 1 431 ? 10.061  -14.319 11.399  1.00 38.34  ? 431 ILE A CB    1 
ATOM   3323 C  CG1   . ILE A 1 431 ? 10.847  -14.388 10.087  1.00 30.57  ? 431 ILE A CG1   1 
ATOM   3324 C  CG2   . ILE A 1 431 ? 8.750   -13.574 11.202  1.00 49.48  ? 431 ILE A CG2   1 
ATOM   3325 C  CD1   . ILE A 1 431 ? 10.087  -15.037 8.951   1.00 48.02  ? 431 ILE A CD1   1 
ATOM   3326 N  N     . ILE A 1 432 ? 9.580   -12.440 14.127  1.00 31.30  ? 432 ILE A N     1 
ATOM   3327 C  CA    . ILE A 1 432 ? 8.930   -12.197 15.409  1.00 33.35  ? 432 ILE A CA    1 
ATOM   3328 C  C     . ILE A 1 432 ? 7.483   -11.793 15.160  1.00 44.67  ? 432 ILE A C     1 
ATOM   3329 O  O     . ILE A 1 432 ? 7.215   -10.878 14.373  1.00 44.35  ? 432 ILE A O     1 
ATOM   3330 C  CB    . ILE A 1 432 ? 9.663   -11.111 16.218  1.00 38.92  ? 432 ILE A CB    1 
ATOM   3331 C  CG1   . ILE A 1 432 ? 11.128  -11.500 16.430  1.00 35.58  ? 432 ILE A CG1   1 
ATOM   3332 C  CG2   . ILE A 1 432 ? 8.966   -10.880 17.551  1.00 31.93  ? 432 ILE A CG2   1 
ATOM   3333 C  CD1   . ILE A 1 432 ? 11.947  -10.438 17.129  1.00 31.37  ? 432 ILE A CD1   1 
ATOM   3334 N  N     . PHE A 1 433 ? 6.559   -12.475 15.830  1.00 34.46  ? 433 PHE A N     1 
ATOM   3335 C  CA    . PHE A 1 433 ? 5.150   -12.117 15.835  1.00 32.35  ? 433 PHE A CA    1 
ATOM   3336 C  C     . PHE A 1 433 ? 4.750   -11.621 17.218  1.00 30.30  ? 433 PHE A C     1 
ATOM   3337 O  O     . PHE A 1 433 ? 5.449   -11.847 18.210  1.00 42.23  ? 433 PHE A O     1 
ATOM   3338 C  CB    . PHE A 1 433 ? 4.268   -13.307 15.438  1.00 42.30  ? 433 PHE A CB    1 
ATOM   3339 C  CG    . PHE A 1 433 ? 4.452   -13.756 14.018  1.00 34.91  ? 433 PHE A CG    1 
ATOM   3340 C  CD1   . PHE A 1 433 ? 4.111   -12.924 12.965  1.00 36.88  ? 433 PHE A CD1   1 
ATOM   3341 C  CD2   . PHE A 1 433 ? 4.949   -15.016 13.735  1.00 32.23  ? 433 PHE A CD2   1 
ATOM   3342 C  CE1   . PHE A 1 433 ? 4.274   -13.336 11.656  1.00 33.33  ? 433 PHE A CE1   1 
ATOM   3343 C  CE2   . PHE A 1 433 ? 5.114   -15.435 12.429  1.00 30.25  ? 433 PHE A CE2   1 
ATOM   3344 C  CZ    . PHE A 1 433 ? 4.776   -14.593 11.388  1.00 34.99  ? 433 PHE A CZ    1 
ATOM   3345 N  N     . GLY A 1 434 ? 3.615   -10.943 17.277  1.00 39.28  ? 434 GLY A N     1 
ATOM   3346 C  CA    . GLY A 1 434 ? 3.104   -10.468 18.546  1.00 30.97  ? 434 GLY A CA    1 
ATOM   3347 C  C     . GLY A 1 434 ? 2.198   -9.275  18.369  1.00 31.24  ? 434 GLY A C     1 
ATOM   3348 O  O     . GLY A 1 434 ? 2.141   -8.649  17.310  1.00 34.04  ? 434 GLY A O     1 
ATOM   3349 N  N     . GLY A 1 435 ? 1.481   -8.969  19.443  1.00 31.84  ? 435 GLY A N     1 
ATOM   3350 C  CA    . GLY A 1 435 ? 0.585   -7.837  19.470  1.00 43.85  ? 435 GLY A CA    1 
ATOM   3351 C  C     . GLY A 1 435 ? 0.252   -7.457  20.895  1.00 41.42  ? 435 GLY A C     1 
ATOM   3352 O  O     . GLY A 1 435 ? 0.830   -7.980  21.850  1.00 51.91  ? 435 GLY A O     1 
ATOM   3353 N  N     . ARG A 1 436 ? -0.700  -6.536  21.029  1.00 46.34  ? 436 ARG A N     1 
ATOM   3354 C  CA    . ARG A 1 436 ? -1.133  -6.055  22.340  1.00 52.97  ? 436 ARG A CA    1 
ATOM   3355 C  C     . ARG A 1 436 ? -2.079  -7.081  22.954  1.00 59.33  ? 436 ARG A C     1 
ATOM   3356 O  O     . ARG A 1 436 ? -3.292  -7.050  22.742  1.00 67.11  ? 436 ARG A O     1 
ATOM   3357 C  CB    . ARG A 1 436 ? -1.796  -4.688  22.222  1.00 55.45  ? 436 ARG A CB    1 
ATOM   3358 C  CG    . ARG A 1 436 ? -0.840  -3.553  21.891  1.00 55.55  ? 436 ARG A CG    1 
ATOM   3359 C  CD    . ARG A 1 436 ? -1.572  -2.222  21.823  1.00 65.10  ? 436 ARG A CD    1 
ATOM   3360 N  NE    . ARG A 1 436 ? -0.660  -1.102  21.623  1.00 60.47  ? 436 ARG A NE    1 
ATOM   3361 C  CZ    . ARG A 1 436 ? -0.134  -0.381  22.604  1.00 55.41  ? 436 ARG A CZ    1 
ATOM   3362 N  NH1   . ARG A 1 436 ? -0.411  -0.633  23.872  1.00 56.51  ? 436 ARG A NH1   1 
ATOM   3363 N  NH2   . ARG A 1 436 ? 0.689   0.620   22.304  1.00 46.75  ? 436 ARG A NH2   1 
ATOM   3364 N  N     . ARG A 1 437 ? -1.514  -8.007  23.726  1.00 54.54  ? 437 ARG A N     1 
ATOM   3365 C  CA    . ARG A 1 437 ? -2.305  -8.987  24.461  1.00 55.49  ? 437 ARG A CA    1 
ATOM   3366 C  C     . ARG A 1 437 ? -2.187  -8.706  25.952  1.00 57.01  ? 437 ARG A C     1 
ATOM   3367 O  O     . ARG A 1 437 ? -1.105  -8.901  26.529  1.00 63.50  ? 437 ARG A O     1 
ATOM   3368 C  CB    . ARG A 1 437 ? -1.848  -10.412 24.145  1.00 53.25  ? 437 ARG A CB    1 
ATOM   3369 C  CG    . ARG A 1 437 ? -2.187  -10.866 22.734  1.00 50.76  ? 437 ARG A CG    1 
ATOM   3370 C  CD    . ARG A 1 437 ? -3.668  -10.678 22.439  1.00 61.53  ? 437 ARG A CD    1 
ATOM   3371 N  NE    . ARG A 1 437 ? -4.514  -11.435 23.354  1.00 55.60  ? 437 ARG A NE    1 
ATOM   3372 C  CZ    . ARG A 1 437 ? -4.992  -12.646 23.104  1.00 47.69  ? 437 ARG A CZ    1 
ATOM   3373 N  NH1   . ARG A 1 437 ? -4.727  -13.272 21.969  1.00 46.74  ? 437 ARG A NH1   1 
ATOM   3374 N  NH2   . ARG A 1 437 ? -5.755  -13.244 24.015  1.00 46.73  ? 437 ARG A NH2   1 
ATOM   3375 N  N     . PRO A 1 438 ? -3.255  -8.255  26.615  1.00 63.82  ? 438 PRO A N     1 
ATOM   3376 C  CA    . PRO A 1 438 ? -3.113  -7.829  28.015  1.00 69.61  ? 438 PRO A CA    1 
ATOM   3377 C  C     . PRO A 1 438 ? -2.931  -8.977  28.993  1.00 66.95  ? 438 PRO A C     1 
ATOM   3378 O  O     . PRO A 1 438 ? -2.325  -8.774  30.052  1.00 74.92  ? 438 PRO A O     1 
ATOM   3379 C  CB    . PRO A 1 438 ? -4.417  -7.065  28.279  1.00 69.79  ? 438 PRO A CB    1 
ATOM   3380 C  CG    . PRO A 1 438 ? -5.399  -7.679  27.338  1.00 62.51  ? 438 PRO A CG    1 
ATOM   3381 C  CD    . PRO A 1 438 ? -4.620  -8.046  26.103  1.00 62.32  ? 438 PRO A CD    1 
ATOM   3382 N  N     . ALA A 1 439 ? -3.433  -10.171 28.685  1.00 64.77  ? 439 ALA A N     1 
ATOM   3383 C  CA    . ALA A 1 439 ? -3.341  -11.286 29.616  1.00 66.87  ? 439 ALA A CA    1 
ATOM   3384 C  C     . ALA A 1 439 ? -3.397  -12.601 28.855  1.00 61.94  ? 439 ALA A C     1 
ATOM   3385 O  O     . ALA A 1 439 ? -4.099  -12.714 27.846  1.00 53.40  ? 439 ALA A O     1 
ATOM   3386 C  CB    . ALA A 1 439 ? -4.464  -11.235 30.659  1.00 64.71  ? 439 ALA A CB    1 
ATOM   3387 N  N     . GLY A 1 440 ? -2.655  -13.590 29.348  1.00 75.67  ? 440 GLY A N     1 
ATOM   3388 C  CA    . GLY A 1 440 ? -2.666  -14.915 28.759  1.00 56.54  ? 440 GLY A CA    1 
ATOM   3389 C  C     . GLY A 1 440 ? -1.392  -15.274 28.024  1.00 61.56  ? 440 GLY A C     1 
ATOM   3390 O  O     . GLY A 1 440 ? -0.741  -16.272 28.346  1.00 58.93  ? 440 GLY A O     1 
ATOM   3391 N  N     . VAL A 1 441 ? -1.026  -14.467 27.033  1.00 58.53  ? 441 VAL A N     1 
ATOM   3392 C  CA    . VAL A 1 441 ? 0.144   -14.736 26.202  1.00 60.57  ? 441 VAL A CA    1 
ATOM   3393 C  C     . VAL A 1 441 ? 1.412   -14.487 27.010  1.00 61.23  ? 441 VAL A C     1 
ATOM   3394 O  O     . VAL A 1 441 ? 1.595   -13.388 27.554  1.00 55.98  ? 441 VAL A O     1 
ATOM   3395 C  CB    . VAL A 1 441 ? 0.128   -13.879 24.926  1.00 55.67  ? 441 VAL A CB    1 
ATOM   3396 C  CG1   . VAL A 1 441 ? 1.366   -14.154 24.085  1.00 54.67  ? 441 VAL A CG1   1 
ATOM   3397 C  CG2   . VAL A 1 441 ? -1.140  -14.144 24.128  1.00 52.90  ? 441 VAL A CG2   1 
ATOM   3398 N  N     . PRO A 1 442 ? 2.308   -15.465 27.118  1.00 63.46  ? 442 PRO A N     1 
ATOM   3399 C  CA    . PRO A 1 442 ? 3.561   -15.245 27.848  1.00 62.30  ? 442 PRO A CA    1 
ATOM   3400 C  C     . PRO A 1 442 ? 4.430   -14.209 27.149  1.00 53.64  ? 442 PRO A C     1 
ATOM   3401 O  O     . PRO A 1 442 ? 4.181   -13.798 26.014  1.00 49.30  ? 442 PRO A O     1 
ATOM   3402 C  CB    . PRO A 1 442 ? 4.223   -16.626 27.853  1.00 60.04  ? 442 PRO A CB    1 
ATOM   3403 C  CG    . PRO A 1 442 ? 3.626   -17.335 26.680  1.00 50.97  ? 442 PRO A CG    1 
ATOM   3404 C  CD    . PRO A 1 442 ? 2.215   -16.830 26.573  1.00 57.31  ? 442 PRO A CD    1 
ATOM   3405 N  N     . LEU A 1 443 ? 5.479   -13.787 27.860  1.00 61.65  ? 443 LEU A N     1 
ATOM   3406 C  CA    . LEU A 1 443 ? 6.342   -12.727 27.347  1.00 54.86  ? 443 LEU A CA    1 
ATOM   3407 C  C     . LEU A 1 443 ? 6.946   -13.103 25.999  1.00 47.47  ? 443 LEU A C     1 
ATOM   3408 O  O     . LEU A 1 443 ? 6.997   -12.275 25.082  1.00 40.89  ? 443 LEU A O     1 
ATOM   3409 C  CB    . LEU A 1 443 ? 7.444   -12.412 28.358  1.00 57.53  ? 443 LEU A CB    1 
ATOM   3410 C  CG    . LEU A 1 443 ? 8.380   -11.257 27.993  1.00 52.20  ? 443 LEU A CG    1 
ATOM   3411 C  CD1   . LEU A 1 443 ? 7.614   -9.943  27.937  1.00 46.56  ? 443 LEU A CD1   1 
ATOM   3412 C  CD2   . LEU A 1 443 ? 9.537   -11.167 28.975  1.00 60.88  ? 443 LEU A CD2   1 
ATOM   3413 N  N     . VAL A 1 444 ? 7.410   -14.342 25.859  1.00 45.48  ? 444 VAL A N     1 
ATOM   3414 C  CA    . VAL A 1 444 ? 8.052   -14.782 24.625  1.00 44.02  ? 444 VAL A CA    1 
ATOM   3415 C  C     . VAL A 1 444 ? 8.094   -16.302 24.619  1.00 43.77  ? 444 VAL A C     1 
ATOM   3416 O  O     . VAL A 1 444 ? 8.387   -16.934 25.637  1.00 57.59  ? 444 VAL A O     1 
ATOM   3417 C  CB    . VAL A 1 444 ? 9.470   -14.178 24.484  1.00 46.64  ? 444 VAL A CB    1 
ATOM   3418 C  CG1   . VAL A 1 444 ? 10.352  -14.626 25.640  1.00 46.40  ? 444 VAL A CG1   1 
ATOM   3419 C  CG2   . VAL A 1 444 ? 10.087  -14.577 23.153  1.00 38.21  ? 444 VAL A CG2   1 
ATOM   3420 N  N     . TYR A 1 445 ? 7.798   -16.884 23.459  1.00 34.99  ? 445 TYR A N     1 
ATOM   3421 C  CA    . TYR A 1 445 ? 7.966   -18.315 23.252  1.00 46.14  ? 445 TYR A CA    1 
ATOM   3422 C  C     . TYR A 1 445 ? 8.380   -18.550 21.807  1.00 51.16  ? 445 TYR A C     1 
ATOM   3423 O  O     . TYR A 1 445 ? 8.355   -17.641 20.974  1.00 43.12  ? 445 TYR A O     1 
ATOM   3424 C  CB    . TYR A 1 445 ? 6.695   -19.099 23.612  1.00 42.20  ? 445 TYR A CB    1 
ATOM   3425 C  CG    . TYR A 1 445 ? 5.473   -18.778 22.777  1.00 43.53  ? 445 TYR A CG    1 
ATOM   3426 C  CD1   . TYR A 1 445 ? 4.604   -17.760 23.145  1.00 43.79  ? 445 TYR A CD1   1 
ATOM   3427 C  CD2   . TYR A 1 445 ? 5.175   -19.512 21.636  1.00 51.18  ? 445 TYR A CD2   1 
ATOM   3428 C  CE1   . TYR A 1 445 ? 3.481   -17.469 22.392  1.00 48.14  ? 445 TYR A CE1   1 
ATOM   3429 C  CE2   . TYR A 1 445 ? 4.052   -19.229 20.875  1.00 44.71  ? 445 TYR A CE2   1 
ATOM   3430 C  CZ    . TYR A 1 445 ? 3.210   -18.207 21.259  1.00 49.16  ? 445 TYR A CZ    1 
ATOM   3431 O  OH    . TYR A 1 445 ? 2.093   -17.921 20.507  1.00 40.95  ? 445 TYR A OH    1 
ATOM   3432 N  N     . GLU A 1 446 ? 8.773   -19.788 21.520  1.00 55.46  ? 446 GLU A N     1 
ATOM   3433 C  CA    . GLU A 1 446 ? 9.328   -20.163 20.227  1.00 52.96  ? 446 GLU A CA    1 
ATOM   3434 C  C     . GLU A 1 446 ? 8.488   -21.266 19.599  1.00 47.32  ? 446 GLU A C     1 
ATOM   3435 O  O     . GLU A 1 446 ? 8.006   -22.166 20.294  1.00 36.58  ? 446 GLU A O     1 
ATOM   3436 C  CB    . GLU A 1 446 ? 10.781  -20.628 20.375  1.00 46.62  ? 446 GLU A CB    1 
ATOM   3437 C  CG    . GLU A 1 446 ? 11.458  -21.008 19.071  1.00 45.99  ? 446 GLU A CG    1 
ATOM   3438 C  CD    . GLU A 1 446 ? 12.840  -21.590 19.289  1.00 49.04  ? 446 GLU A CD    1 
ATOM   3439 O  OE1   . GLU A 1 446 ? 13.215  -21.807 20.460  1.00 47.66  ? 446 GLU A OE1   1 
ATOM   3440 O  OE2   . GLU A 1 446 ? 13.552  -21.830 18.291  1.00 54.69  ? 446 GLU A OE2   1 
ATOM   3441 N  N     . ALA A 1 447 ? 8.319   -21.192 18.281  1.00 50.88  ? 447 ALA A N     1 
ATOM   3442 C  CA    . ALA A 1 447 ? 7.530   -22.182 17.567  1.00 49.59  ? 447 ALA A CA    1 
ATOM   3443 C  C     . ALA A 1 447 ? 8.220   -23.544 17.603  1.00 53.41  ? 447 ALA A C     1 
ATOM   3444 O  O     . ALA A 1 447 ? 9.391   -23.675 17.972  1.00 61.98  ? 447 ALA A O     1 
ATOM   3445 C  CB    . ALA A 1 447 ? 7.295   -21.742 16.123  1.00 44.69  ? 447 ALA A CB    1 
ATOM   3446 N  N     . LEU A 1 448 ? 7.469   -24.574 17.209  1.00 48.40  ? 448 LEU A N     1 
ATOM   3447 C  CA    . LEU A 1 448 ? 7.975   -25.939 17.191  1.00 45.62  ? 448 LEU A CA    1 
ATOM   3448 C  C     . LEU A 1 448 ? 8.433   -26.394 15.814  1.00 41.58  ? 448 LEU A C     1 
ATOM   3449 O  O     . LEU A 1 448 ? 9.217   -27.345 15.723  1.00 43.55  ? 448 LEU A O     1 
ATOM   3450 C  CB    . LEU A 1 448 ? 6.903   -26.907 17.708  1.00 36.80  ? 448 LEU A CB    1 
ATOM   3451 C  CG    . LEU A 1 448 ? 6.394   -26.642 19.127  1.00 44.79  ? 448 LEU A CG    1 
ATOM   3452 C  CD1   . LEU A 1 448 ? 5.214   -27.541 19.455  1.00 36.69  ? 448 LEU A CD1   1 
ATOM   3453 C  CD2   . LEU A 1 448 ? 7.511   -26.830 20.143  1.00 52.79  ? 448 LEU A CD2   1 
ATOM   3454 N  N     . SER A 1 449 ? 7.970   -25.747 14.751  1.00 40.55  ? 449 SER A N     1 
ATOM   3455 C  CA    . SER A 1 449 ? 8.354   -26.100 13.388  1.00 42.56  ? 449 SER A CA    1 
ATOM   3456 C  C     . SER A 1 449 ? 7.919   -24.964 12.469  1.00 42.09  ? 449 SER A C     1 
ATOM   3457 O  O     . SER A 1 449 ? 7.327   -23.974 12.910  1.00 41.87  ? 449 SER A O     1 
ATOM   3458 C  CB    . SER A 1 449 ? 7.739   -27.434 12.961  1.00 47.69  ? 449 SER A CB    1 
ATOM   3459 O  OG    . SER A 1 449 ? 6.324   -27.355 12.924  1.00 50.09  ? 449 SER A OG    1 
ATOM   3460 N  N     . TRP A 1 450 ? 8.220   -25.116 11.178  1.00 45.34  ? 450 TRP A N     1 
ATOM   3461 C  CA    . TRP A 1 450 ? 7.820   -24.103 10.208  1.00 47.50  ? 450 TRP A CA    1 
ATOM   3462 C  C     . TRP A 1 450 ? 6.306   -24.056 10.050  1.00 49.01  ? 450 TRP A C     1 
ATOM   3463 O  O     . TRP A 1 450 ? 5.727   -22.977 9.879   1.00 49.09  ? 450 TRP A O     1 
ATOM   3464 C  CB    . TRP A 1 450 ? 8.494   -24.367 8.862   1.00 50.00  ? 450 TRP A CB    1 
ATOM   3465 C  CG    . TRP A 1 450 ? 8.106   -23.387 7.799   1.00 57.15  ? 450 TRP A CG    1 
ATOM   3466 C  CD1   . TRP A 1 450 ? 7.217   -23.587 6.783   1.00 63.72  ? 450 TRP A CD1   1 
ATOM   3467 C  CD2   . TRP A 1 450 ? 8.590   -22.047 7.649   1.00 59.32  ? 450 TRP A CD2   1 
ATOM   3468 N  NE1   . TRP A 1 450 ? 7.121   -22.457 6.008   1.00 67.51  ? 450 TRP A NE1   1 
ATOM   3469 C  CE2   . TRP A 1 450 ? 7.954   -21.497 6.519   1.00 64.07  ? 450 TRP A CE2   1 
ATOM   3470 C  CE3   . TRP A 1 450 ? 9.502   -21.260 8.360   1.00 59.49  ? 450 TRP A CE3   1 
ATOM   3471 C  CZ2   . TRP A 1 450 ? 8.200   -20.196 6.083   1.00 60.21  ? 450 TRP A CZ2   1 
ATOM   3472 C  CZ3   . TRP A 1 450 ? 9.744   -19.970 7.926   1.00 56.22  ? 450 TRP A CZ3   1 
ATOM   3473 C  CH2   . TRP A 1 450 ? 9.096   -19.451 6.799   1.00 61.46  ? 450 TRP A CH2   1 
ATOM   3474 N  N     . GLN A 1 451 ? 5.647   -25.216 10.101  1.00 55.39  ? 451 GLN A N     1 
ATOM   3475 C  CA    . GLN A 1 451 ? 4.192   -25.246 9.989   1.00 42.16  ? 451 GLN A CA    1 
ATOM   3476 C  C     . GLN A 1 451 ? 3.537   -24.606 11.208  1.00 43.81  ? 451 GLN A C     1 
ATOM   3477 O  O     . GLN A 1 451 ? 2.685   -23.720 11.074  1.00 44.70  ? 451 GLN A O     1 
ATOM   3478 C  CB    . GLN A 1 451 ? 3.706   -26.684 9.803   1.00 46.10  ? 451 GLN A CB    1 
ATOM   3479 C  CG    . GLN A 1 451 ? 3.973   -27.259 8.418   1.00 53.83  ? 451 GLN A CG    1 
ATOM   3480 C  CD    . GLN A 1 451 ? 5.450   -27.448 8.132   1.00 63.65  ? 451 GLN A CD    1 
ATOM   3481 O  OE1   . GLN A 1 451 ? 6.251   -27.650 9.045   1.00 49.10  ? 451 GLN A OE1   1 
ATOM   3482 N  NE2   . GLN A 1 451 ? 5.819   -27.379 6.858   1.00 64.35  ? 451 GLN A NE2   1 
ATOM   3483 N  N     . HIS A 1 452 ? 3.924   -25.042 12.409  1.00 46.14  ? 452 HIS A N     1 
ATOM   3484 C  CA    . HIS A 1 452 ? 3.390   -24.423 13.618  1.00 35.56  ? 452 HIS A CA    1 
ATOM   3485 C  C     . HIS A 1 452 ? 3.726   -22.940 13.677  1.00 46.99  ? 452 HIS A C     1 
ATOM   3486 O  O     . HIS A 1 452 ? 2.965   -22.153 14.253  1.00 41.33  ? 452 HIS A O     1 
ATOM   3487 C  CB    . HIS A 1 452 ? 3.922   -25.140 14.859  1.00 40.47  ? 452 HIS A CB    1 
ATOM   3488 C  CG    . HIS A 1 452 ? 3.523   -24.490 16.148  1.00 47.09  ? 452 HIS A CG    1 
ATOM   3489 N  ND1   . HIS A 1 452 ? 4.408   -23.776 16.926  1.00 36.92  ? 452 HIS A ND1   1 
ATOM   3490 C  CD2   . HIS A 1 452 ? 2.332   -24.441 16.791  1.00 49.22  ? 452 HIS A CD2   1 
ATOM   3491 C  CE1   . HIS A 1 452 ? 3.781   -23.318 17.995  1.00 37.72  ? 452 HIS A CE1   1 
ATOM   3492 N  NE2   . HIS A 1 452 ? 2.520   -23.707 17.938  1.00 46.90  ? 452 HIS A NE2   1 
ATOM   3493 N  N     . GLY A 1 453 ? 4.856   -22.538 13.092  1.00 52.56  ? 453 GLY A N     1 
ATOM   3494 C  CA    . GLY A 1 453 ? 5.183   -21.123 13.041  1.00 50.56  ? 453 GLY A CA    1 
ATOM   3495 C  C     . GLY A 1 453 ? 4.192   -20.336 12.205  1.00 52.01  ? 453 GLY A C     1 
ATOM   3496 O  O     . GLY A 1 453 ? 3.708   -19.280 12.620  1.00 51.71  ? 453 GLY A O     1 
ATOM   3497 N  N     . VAL A 1 454 ? 3.876   -20.844 11.011  1.00 51.03  ? 454 VAL A N     1 
ATOM   3498 C  CA    . VAL A 1 454 ? 2.867   -20.200 10.175  1.00 42.74  ? 454 VAL A CA    1 
ATOM   3499 C  C     . VAL A 1 454 ? 1.534   -20.140 10.908  1.00 42.89  ? 454 VAL A C     1 
ATOM   3500 O  O     . VAL A 1 454 ? 0.780   -19.168 10.780  1.00 46.83  ? 454 VAL A O     1 
ATOM   3501 C  CB    . VAL A 1 454 ? 2.740   -20.933 8.827   1.00 50.87  ? 454 VAL A CB    1 
ATOM   3502 C  CG1   . VAL A 1 454 ? 1.644   -20.303 7.980   1.00 47.90  ? 454 VAL A CG1   1 
ATOM   3503 C  CG2   . VAL A 1 454 ? 4.069   -20.920 8.087   1.00 42.27  ? 454 VAL A CG2   1 
ATOM   3504 N  N     . PHE A 1 455 ? 1.222   -21.178 11.687  1.00 40.44  ? 455 PHE A N     1 
ATOM   3505 C  CA    . PHE A 1 455 ? -0.009  -21.168 12.470  1.00 39.28  ? 455 PHE A CA    1 
ATOM   3506 C  C     . PHE A 1 455 ? 0.000   -20.042 13.496  1.00 44.26  ? 455 PHE A C     1 
ATOM   3507 O  O     . PHE A 1 455 ? -1.028  -19.396 13.728  1.00 41.74  ? 455 PHE A O     1 
ATOM   3508 C  CB    . PHE A 1 455 ? -0.206  -22.519 13.157  1.00 33.14  ? 455 PHE A CB    1 
ATOM   3509 C  CG    . PHE A 1 455 ? -1.353  -22.543 14.127  1.00 45.69  ? 455 PHE A CG    1 
ATOM   3510 C  CD1   . PHE A 1 455 ? -2.658  -22.653 13.675  1.00 41.01  ? 455 PHE A CD1   1 
ATOM   3511 C  CD2   . PHE A 1 455 ? -1.127  -22.456 15.490  1.00 43.78  ? 455 PHE A CD2   1 
ATOM   3512 C  CE1   . PHE A 1 455 ? -3.715  -22.673 14.565  1.00 45.10  ? 455 PHE A CE1   1 
ATOM   3513 C  CE2   . PHE A 1 455 ? -2.181  -22.476 16.385  1.00 43.56  ? 455 PHE A CE2   1 
ATOM   3514 C  CZ    . PHE A 1 455 ? -3.476  -22.585 15.922  1.00 39.72  ? 455 PHE A CZ    1 
ATOM   3515 N  N     . VAL A 1 456 ? 1.153   -19.793 14.121  1.00 42.94  ? 456 VAL A N     1 
ATOM   3516 C  CA    . VAL A 1 456 ? 1.248   -18.718 15.105  1.00 37.44  ? 456 VAL A CA    1 
ATOM   3517 C  C     . VAL A 1 456 ? 0.904   -17.380 14.463  1.00 36.79  ? 456 VAL A C     1 
ATOM   3518 O  O     . VAL A 1 456 ? 0.137   -16.584 15.016  1.00 38.81  ? 456 VAL A O     1 
ATOM   3519 C  CB    . VAL A 1 456 ? 2.649   -18.695 15.742  1.00 46.62  ? 456 VAL A CB    1 
ATOM   3520 C  CG1   . VAL A 1 456 ? 2.798   -17.484 16.651  1.00 41.84  ? 456 VAL A CG1   1 
ATOM   3521 C  CG2   . VAL A 1 456 ? 2.901   -19.981 16.515  1.00 44.63  ? 456 VAL A CG2   1 
ATOM   3522 N  N     . GLY A 1 457 ? 1.468   -17.114 13.284  1.00 43.06  ? 457 GLY A N     1 
ATOM   3523 C  CA    . GLY A 1 457 ? 1.176   -15.862 12.606  1.00 40.44  ? 457 GLY A CA    1 
ATOM   3524 C  C     . GLY A 1 457 ? -0.285  -15.729 12.224  1.00 44.36  ? 457 GLY A C     1 
ATOM   3525 O  O     . GLY A 1 457 ? -0.856  -14.637 12.285  1.00 38.55  ? 457 GLY A O     1 
ATOM   3526 N  N     . ALA A 1 458 ? -0.913  -16.839 11.827  1.00 39.82  ? 458 ALA A N     1 
ATOM   3527 C  CA    . ALA A 1 458 ? -2.319  -16.806 11.444  1.00 38.61  ? 458 ALA A CA    1 
ATOM   3528 C  C     . ALA A 1 458 ? -3.244  -16.655 12.644  1.00 39.43  ? 458 ALA A C     1 
ATOM   3529 O  O     . ALA A 1 458 ? -4.407  -16.275 12.469  1.00 39.97  ? 458 ALA A O     1 
ATOM   3530 C  CB    . ALA A 1 458 ? -2.683  -18.072 10.665  1.00 45.67  ? 458 ALA A CB    1 
ATOM   3531 N  N     . ALA A 1 459 ? -2.758  -16.939 13.852  1.00 40.15  ? 459 ALA A N     1 
ATOM   3532 C  CA    . ALA A 1 459 ? -3.560  -16.858 15.064  1.00 38.25  ? 459 ALA A CA    1 
ATOM   3533 C  C     . ALA A 1 459 ? -3.261  -15.604 15.878  1.00 37.58  ? 459 ALA A C     1 
ATOM   3534 O  O     . ALA A 1 459 ? -3.497  -15.588 17.091  1.00 36.51  ? 459 ALA A O     1 
ATOM   3535 C  CB    . ALA A 1 459 ? -3.349  -18.108 15.918  1.00 37.12  ? 459 ALA A CB    1 
ATOM   3536 N  N     . MET A 1 460 ? -2.750  -14.557 15.237  1.00 40.65  ? 460 MET A N     1 
ATOM   3537 C  CA    . MET A 1 460 ? -2.436  -13.323 15.942  1.00 40.97  ? 460 MET A CA    1 
ATOM   3538 C  C     . MET A 1 460 ? -3.709  -12.565 16.298  1.00 48.35  ? 460 MET A C     1 
ATOM   3539 O  O     . MET A 1 460 ? -4.633  -12.451 15.487  1.00 46.15  ? 460 MET A O     1 
ATOM   3540 C  CB    . MET A 1 460 ? -1.526  -12.439 15.090  1.00 34.91  ? 460 MET A CB    1 
ATOM   3541 C  CG    . MET A 1 460 ? -0.150  -13.026 14.828  1.00 36.45  ? 460 MET A CG    1 
ATOM   3542 S  SD    . MET A 1 460 ? 0.880   -11.944 13.820  1.00 37.81  ? 460 MET A SD    1 
ATOM   3543 C  CE    . MET A 1 460 ? 0.862   -10.446 14.802  1.00 36.58  ? 460 MET A CE    1 
ATOM   3544 N  N     . ARG A 1 461 ? -3.751  -12.047 17.523  1.00 54.21  ? 461 ARG A N     1 
ATOM   3545 C  CA    . ARG A 1 461 ? -4.862  -11.233 17.992  1.00 45.03  ? 461 ARG A CA    1 
ATOM   3546 C  C     . ARG A 1 461 ? -4.313  -10.080 18.818  1.00 48.57  ? 461 ARG A C     1 
ATOM   3547 O  O     . ARG A 1 461 ? -3.232  -10.177 19.405  1.00 60.61  ? 461 ARG A O     1 
ATOM   3548 C  CB    . ARG A 1 461 ? -5.859  -12.051 18.824  1.00 41.52  ? 461 ARG A CB    1 
ATOM   3549 C  CG    . ARG A 1 461 ? -6.540  -13.175 18.057  1.00 49.26  ? 461 ARG A CG    1 
ATOM   3550 C  CD    . ARG A 1 461 ? -7.459  -13.978 18.964  1.00 39.57  ? 461 ARG A CD    1 
ATOM   3551 N  NE    . ARG A 1 461 ? -8.546  -13.166 19.498  1.00 42.58  ? 461 ARG A NE    1 
ATOM   3552 C  CZ    . ARG A 1 461 ? -9.384  -13.568 20.444  1.00 50.67  ? 461 ARG A CZ    1 
ATOM   3553 N  NH1   . ARG A 1 461 ? -9.280  -14.765 20.996  1.00 54.45  ? 461 ARG A NH1   1 
ATOM   3554 N  NH2   . ARG A 1 461 ? -10.348 -12.746 20.848  1.00 51.65  ? 461 ARG A NH2   1 
ATOM   3555 N  N     . SER A 1 462 ? -5.067  -8.985  18.857  1.00 72.59  ? 462 SER A N     1 
ATOM   3556 C  CA    . SER A 1 462 ? -4.632  -7.797  19.578  1.00 59.03  ? 462 SER A CA    1 
ATOM   3557 C  C     . SER A 1 462 ? -5.834  -6.902  19.835  1.00 70.21  ? 462 SER A C     1 
ATOM   3558 O  O     . SER A 1 462 ? -6.851  -6.978  19.141  1.00 67.79  ? 462 SER A O     1 
ATOM   3559 C  CB    . SER A 1 462 ? -3.550  -7.037  18.804  1.00 55.56  ? 462 SER A CB    1 
ATOM   3560 O  OG    . SER A 1 462 ? -3.202  -5.833  19.464  1.00 50.68  ? 462 SER A OG    1 
ATOM   3561 N  N     . GLU A 1 463 ? -5.700  -6.051  20.848  1.00 72.55  ? 463 GLU A N     1 
ATOM   3562 C  CA    . GLU A 1 463 ? -6.741  -5.092  21.180  1.00 82.81  ? 463 GLU A CA    1 
ATOM   3563 C  C     . GLU A 1 463 ? -6.703  -3.910  20.219  1.00 89.21  ? 463 GLU A C     1 
ATOM   3564 O  O     . GLU A 1 463 ? -5.643  -3.520  19.720  1.00 85.77  ? 463 GLU A O     1 
ATOM   3565 C  CB    . GLU A 1 463 ? -6.581  -4.605  22.621  1.00 82.66  ? 463 GLU A CB    1 
ATOM   3566 C  CG    . GLU A 1 463 ? -5.215  -4.009  22.925  1.00 82.13  ? 463 GLU A CG    1 
ATOM   3567 C  CD    . GLU A 1 463 ? -5.060  -3.615  24.382  1.00 90.37  ? 463 GLU A CD    1 
ATOM   3568 O  OE1   . GLU A 1 463 ? -6.021  -3.804  25.156  1.00 93.90  ? 463 GLU A OE1   1 
ATOM   3569 O  OE2   . GLU A 1 463 ? -3.976  -3.117  24.752  1.00 92.99  ? 463 GLU A OE2   1 
ATOM   3570 N  N     . ALA A 1 464 ? -7.878  -3.340  19.962  1.00 105.16 ? 464 ALA A N     1 
ATOM   3571 C  CA    . ALA A 1 464 ? -7.977  -2.220  19.037  1.00 121.00 ? 464 ALA A CA    1 
ATOM   3572 C  C     . ALA A 1 464 ? -7.225  -1.012  19.580  1.00 132.31 ? 464 ALA A C     1 
ATOM   3573 O  O     . ALA A 1 464 ? -7.402  -0.623  20.738  1.00 134.99 ? 464 ALA A O     1 
ATOM   3574 C  CB    . ALA A 1 464 ? -9.444  -1.866  18.790  1.00 128.83 ? 464 ALA A CB    1 
ATOM   3575 N  N     . THR A 1 465 ? -6.384  -0.418  18.735  1.00 150.66 ? 465 THR A N     1 
ATOM   3576 C  CA    . THR A 1 465 ? -5.595  0.742   19.132  1.00 159.15 ? 465 THR A CA    1 
ATOM   3577 C  C     . THR A 1 465 ? -6.176  2.020   18.542  1.00 167.24 ? 465 THR A C     1 
ATOM   3578 O  O     . THR A 1 465 ? -7.394  2.134   18.369  1.00 173.40 ? 465 THR A O     1 
ATOM   3579 C  CB    . THR A 1 465 ? -4.137  0.576   18.696  1.00 148.90 ? 465 THR A CB    1 
ATOM   3580 O  OG1   . THR A 1 465 ? -4.072  0.482   17.267  1.00 143.25 ? 465 THR A OG1   1 
ATOM   3581 C  CG2   . THR A 1 465 ? -3.539  -0.681  19.307  1.00 142.28 ? 465 THR A CG2   1 
ATOM   3582 N  N     . ALA A 1 466 ? -5.312  2.985   18.231  1.00 151.40 ? 466 ALA A N     1 
ATOM   3583 C  CA    . ALA A 1 466 ? -5.751  4.248   17.651  1.00 137.97 ? 466 ALA A CA    1 
ATOM   3584 C  C     . ALA A 1 466 ? -5.069  4.491   16.311  1.00 127.15 ? 466 ALA A C     1 
ATOM   3585 O  O     . ALA A 1 466 ? -4.463  5.546   16.098  1.00 114.97 ? 466 ALA A O     1 
ATOM   3586 C  CB    . ALA A 1 466 ? -5.471  5.405   18.612  1.00 131.95 ? 466 ALA A CB    1 
ATOM   3587 N  N     . ALA A 1 467 ? -5.161  3.520   15.404  1.00 124.23 ? 467 ALA A N     1 
ATOM   3588 C  CA    . ALA A 1 467 ? -4.558  3.615   14.081  1.00 108.60 ? 467 ALA A CA    1 
ATOM   3589 C  C     . ALA A 1 467 ? -5.591  3.713   12.970  1.00 112.71 ? 467 ALA A C     1 
ATOM   3590 O  O     . ALA A 1 467 ? -5.463  4.558   12.078  1.00 107.01 ? 467 ALA A O     1 
ATOM   3591 C  CB    . ALA A 1 467 ? -3.639  2.410   13.833  1.00 96.99  ? 467 ALA A CB    1 
ATOM   3592 N  N     . ALA A 1 468 ? -6.618  2.864   12.998  1.00 120.91 ? 468 ALA A N     1 
ATOM   3593 C  CA    . ALA A 1 468 ? -7.677  2.912   11.998  1.00 122.18 ? 468 ALA A CA    1 
ATOM   3594 C  C     . ALA A 1 468 ? -8.918  3.584   12.571  1.00 134.51 ? 468 ALA A C     1 
ATOM   3595 O  O     . ALA A 1 468 ? -8.809  4.537   13.349  1.00 140.89 ? 468 ALA A O     1 
ATOM   3596 C  CB    . ALA A 1 468 ? -8.010  1.504   11.498  1.00 124.10 ? 468 ALA A CB    1 
ATOM   3597 N  N     . GLU A 1 469 ? -10.102 3.096   12.197  1.00 133.56 ? 469 GLU A N     1 
ATOM   3598 C  CA    . GLU A 1 469 ? -11.361 3.633   12.699  1.00 140.76 ? 469 GLU A CA    1 
ATOM   3599 C  C     . GLU A 1 469 ? -11.997 2.730   13.752  1.00 145.42 ? 469 GLU A C     1 
ATOM   3600 O  O     . GLU A 1 469 ? -13.222 2.736   13.916  1.00 143.52 ? 469 GLU A O     1 
ATOM   3601 C  CB    . GLU A 1 469 ? -12.338 3.876   11.548  1.00 137.05 ? 469 GLU A CB    1 
ATOM   3602 C  CG    . GLU A 1 469 ? -12.771 2.622   10.802  1.00 127.09 ? 469 GLU A CG    1 
ATOM   3603 C  CD    . GLU A 1 469 ? -11.842 2.269   9.656   1.00 116.19 ? 469 GLU A CD    1 
ATOM   3604 O  OE1   . GLU A 1 469 ? -10.725 2.824   9.599   1.00 117.48 ? 469 GLU A OE1   1 
ATOM   3605 O  OE2   . GLU A 1 469 ? -12.234 1.441   8.807   1.00 102.43 ? 469 GLU A OE2   1 
ATOM   3606 N  N     . HIS A 1 470 ? -11.188 1.957   14.470  1.00 146.54 ? 470 HIS A N     1 
ATOM   3607 C  CA    . HIS A 1 470 ? -11.675 1.067   15.514  1.00 148.93 ? 470 HIS A CA    1 
ATOM   3608 C  C     . HIS A 1 470 ? -11.448 1.698   16.882  1.00 149.89 ? 470 HIS A C     1 
ATOM   3609 O  O     . HIS A 1 470 ? -10.400 2.300   17.135  1.00 152.27 ? 470 HIS A O     1 
ATOM   3610 C  CB    . HIS A 1 470 ? -10.977 -0.294  15.446  1.00 144.73 ? 470 HIS A CB    1 
ATOM   3611 C  CG    . HIS A 1 470 ? -11.082 -0.962  14.111  1.00 140.48 ? 470 HIS A CG    1 
ATOM   3612 N  ND1   . HIS A 1 470 ? -10.246 -0.656  13.058  1.00 136.45 ? 470 HIS A ND1   1 
ATOM   3613 C  CD2   . HIS A 1 470 ? -11.925 -1.919  13.656  1.00 138.10 ? 470 HIS A CD2   1 
ATOM   3614 C  CE1   . HIS A 1 470 ? -10.568 -1.398  12.013  1.00 128.75 ? 470 HIS A CE1   1 
ATOM   3615 N  NE2   . HIS A 1 470 ? -11.584 -2.172  12.349  1.00 126.62 ? 470 HIS A NE2   1 
ATOM   3616 N  N     . LYS A 1 471 ? -12.437 1.557   17.760  1.00 149.30 ? 471 LYS A N     1 
ATOM   3617 C  CA    . LYS A 1 471 ? -12.376 2.111   19.103  1.00 153.56 ? 471 LYS A CA    1 
ATOM   3618 C  C     . LYS A 1 471 ? -12.767 1.044   20.114  1.00 162.89 ? 471 LYS A C     1 
ATOM   3619 O  O     . LYS A 1 471 ? -13.372 0.024   19.775  1.00 158.48 ? 471 LYS A O     1 
ATOM   3620 C  CB    . LYS A 1 471 ? -13.290 3.336   19.253  1.00 150.61 ? 471 LYS A CB    1 
ATOM   3621 C  CG    . LYS A 1 471 ? -12.945 4.490   18.327  1.00 144.08 ? 471 LYS A CG    1 
ATOM   3622 C  CD    . LYS A 1 471 ? -13.873 5.675   18.553  1.00 131.86 ? 471 LYS A CD    1 
ATOM   3623 C  CE    . LYS A 1 471 ? -13.515 6.840   17.643  1.00 115.81 ? 471 LYS A CE    1 
ATOM   3624 N  NZ    . LYS A 1 471 ? -14.400 8.018   17.866  1.00 107.84 ? 471 LYS A NZ    1 
ATOM   3625 N  N     . GLY A 1 472 ? -12.412 1.296   21.370  1.00 186.48 ? 472 GLY A N     1 
ATOM   3626 C  CA    . GLY A 1 472 ? -12.710 0.370   22.440  1.00 187.30 ? 472 GLY A CA    1 
ATOM   3627 C  C     . GLY A 1 472 ? -11.597 -0.626  22.687  1.00 182.70 ? 472 GLY A C     1 
ATOM   3628 O  O     . GLY A 1 472 ? -10.578 -0.679  21.990  1.00 180.65 ? 472 GLY A O     1 
ATOM   3629 N  N     . LYS A 1 473 ? -11.810 -1.437  23.718  1.00 165.86 ? 473 LYS A N     1 
ATOM   3630 C  CA    . LYS A 1 473 ? -10.862 -2.468  24.126  1.00 154.38 ? 473 LYS A CA    1 
ATOM   3631 C  C     . LYS A 1 473 ? -11.392 -3.831  23.688  1.00 144.25 ? 473 LYS A C     1 
ATOM   3632 O  O     . LYS A 1 473 ? -11.848 -4.642  24.496  1.00 144.92 ? 473 LYS A O     1 
ATOM   3633 C  CB    . LYS A 1 473 ? -10.633 -2.409  25.644  1.00 159.65 ? 473 LYS A CB    1 
ATOM   3634 C  CG    . LYS A 1 473 ? -10.372 -1.009  26.182  1.00 169.41 ? 473 LYS A CG    1 
ATOM   3635 C  CD    . LYS A 1 473 ? -9.164  -0.369  25.516  1.00 169.92 ? 473 LYS A CD    1 
ATOM   3636 C  CE    . LYS A 1 473 ? -7.878  -1.094  25.880  1.00 155.67 ? 473 LYS A CE    1 
ATOM   3637 N  NZ    . LYS A 1 473 ? -6.678  -0.414  25.316  1.00 149.36 ? 473 LYS A NZ    1 
ATOM   3638 N  N     . VAL A 1 474 ? -11.329 -4.076  22.382  1.00 117.29 ? 474 VAL A N     1 
ATOM   3639 C  CA    . VAL A 1 474 ? -11.814 -5.312  21.779  1.00 97.59  ? 474 VAL A CA    1 
ATOM   3640 C  C     . VAL A 1 474 ? -10.625 -6.073  21.211  1.00 88.34  ? 474 VAL A C     1 
ATOM   3641 O  O     . VAL A 1 474 ? -9.805  -5.502  20.482  1.00 91.62  ? 474 VAL A O     1 
ATOM   3642 C  CB    . VAL A 1 474 ? -12.861 -5.036  20.685  1.00 88.50  ? 474 VAL A CB    1 
ATOM   3643 C  CG1   . VAL A 1 474 ? -13.239 -6.326  19.974  1.00 82.53  ? 474 VAL A CG1   1 
ATOM   3644 C  CG2   . VAL A 1 474 ? -14.092 -4.373  21.286  1.00 94.73  ? 474 VAL A CG2   1 
ATOM   3645 N  N     . ILE A 1 475 ? -10.532 -7.358  21.545  1.00 74.88  ? 475 ILE A N     1 
ATOM   3646 C  CA    . ILE A 1 475 ? -9.444  -8.210  21.078  1.00 71.31  ? 475 ILE A CA    1 
ATOM   3647 C  C     . ILE A 1 475 ? -9.890  -8.826  19.756  1.00 68.67  ? 475 ILE A C     1 
ATOM   3648 O  O     . ILE A 1 475 ? -10.610 -9.825  19.731  1.00 70.58  ? 475 ILE A O     1 
ATOM   3649 C  CB    . ILE A 1 475 ? -9.080  -9.282  22.106  1.00 58.28  ? 475 ILE A CB    1 
ATOM   3650 C  CG1   . ILE A 1 475 ? -8.960  -8.666  23.501  1.00 60.38  ? 475 ILE A CG1   1 
ATOM   3651 C  CG2   . ILE A 1 475 ? -7.777  -9.967  21.716  1.00 48.82  ? 475 ILE A CG2   1 
ATOM   3652 C  CD1   . ILE A 1 475 ? -8.749  -9.684  24.598  1.00 64.68  ? 475 ILE A CD1   1 
ATOM   3653 N  N     . MET A 1 476 ? -9.456  -8.230  18.651  1.00 65.69  ? 476 MET A N     1 
ATOM   3654 C  CA    . MET A 1 476 ? -9.809  -8.708  17.324  1.00 65.42  ? 476 MET A CA    1 
ATOM   3655 C  C     . MET A 1 476 ? -8.645  -9.476  16.706  1.00 57.76  ? 476 MET A C     1 
ATOM   3656 O  O     . MET A 1 476 ? -7.521  -9.476  17.214  1.00 55.60  ? 476 MET A O     1 
ATOM   3657 C  CB    . MET A 1 476 ? -10.224 -7.540  16.423  1.00 73.73  ? 476 MET A CB    1 
ATOM   3658 C  CG    . MET A 1 476 ? -9.125  -6.523  16.167  1.00 79.16  ? 476 MET A CG    1 
ATOM   3659 S  SD    . MET A 1 476 ? -9.721  -5.113  15.214  1.00 108.74 ? 476 MET A SD    1 
ATOM   3660 C  CE    . MET A 1 476 ? -10.405 -5.938  13.779  1.00 87.32  ? 476 MET A CE    1 
ATOM   3661 N  N     . HIS A 1 477 ? -8.932  -10.143 15.594  1.00 55.23  ? 477 HIS A N     1 
ATOM   3662 C  CA    . HIS A 1 477 ? -7.933  -10.943 14.902  1.00 42.74  ? 477 HIS A CA    1 
ATOM   3663 C  C     . HIS A 1 477 ? -7.153  -10.088 13.915  1.00 53.72  ? 477 HIS A C     1 
ATOM   3664 O  O     . HIS A 1 477 ? -7.695  -9.172  13.291  1.00 56.33  ? 477 HIS A O     1 
ATOM   3665 C  CB    . HIS A 1 477 ? -8.587  -12.115 14.171  1.00 55.22  ? 477 HIS A CB    1 
ATOM   3666 C  CG    . HIS A 1 477 ? -9.220  -13.114 15.086  1.00 49.95  ? 477 HIS A CG    1 
ATOM   3667 N  ND1   . HIS A 1 477 ? -10.444 -12.903 15.684  1.00 54.90  ? 477 HIS A ND1   1 
ATOM   3668 C  CD2   . HIS A 1 477 ? -8.793  -14.324 15.518  1.00 51.19  ? 477 HIS A CD2   1 
ATOM   3669 C  CE1   . HIS A 1 477 ? -10.747 -13.943 16.439  1.00 55.90  ? 477 HIS A CE1   1 
ATOM   3670 N  NE2   . HIS A 1 477 ? -9.762  -14.819 16.356  1.00 48.24  ? 477 HIS A NE2   1 
ATOM   3671 N  N     . ASP A 1 478 ? -5.866  -10.402 13.779  1.00 53.53  ? 478 ASP A N     1 
ATOM   3672 C  CA    . ASP A 1 478 ? -4.980  -9.689  12.870  1.00 52.60  ? 478 ASP A CA    1 
ATOM   3673 C  C     . ASP A 1 478 ? -3.843  -10.608 12.437  1.00 52.14  ? 478 ASP A C     1 
ATOM   3674 O  O     . ASP A 1 478 ? -2.723  -10.497 12.953  1.00 45.36  ? 478 ASP A O     1 
ATOM   3675 C  CB    . ASP A 1 478 ? -4.432  -8.426  13.535  1.00 50.51  ? 478 ASP A CB    1 
ATOM   3676 C  CG    . ASP A 1 478 ? -3.837  -7.453  12.539  1.00 45.75  ? 478 ASP A CG    1 
ATOM   3677 O  OD1   . ASP A 1 478 ? -3.424  -7.896  11.447  1.00 47.82  ? 478 ASP A OD1   1 
ATOM   3678 O  OD2   . ASP A 1 478 ? -3.787  -6.244  12.849  1.00 46.70  ? 478 ASP A OD2   1 
ATOM   3679 N  N     . PRO A 1 479 ? -4.081  -11.524 11.499  1.00 51.80  ? 479 PRO A N     1 
ATOM   3680 C  CA    . PRO A 1 479 ? -3.027  -12.476 11.120  1.00 43.26  ? 479 PRO A CA    1 
ATOM   3681 C  C     . PRO A 1 479 ? -1.877  -11.778 10.406  1.00 45.20  ? 479 PRO A C     1 
ATOM   3682 O  O     . PRO A 1 479 ? -2.086  -11.000 9.472   1.00 42.06  ? 479 PRO A O     1 
ATOM   3683 C  CB    . PRO A 1 479 ? -3.753  -13.458 10.194  1.00 45.62  ? 479 PRO A CB    1 
ATOM   3684 C  CG    . PRO A 1 479 ? -4.889  -12.668 9.633   1.00 46.62  ? 479 PRO A CG    1 
ATOM   3685 C  CD    . PRO A 1 479 ? -5.327  -11.748 10.742  1.00 43.78  ? 479 PRO A CD    1 
ATOM   3686 N  N     . PHE A 1 480 ? -0.656  -12.066 10.855  1.00 44.69  ? 480 PHE A N     1 
ATOM   3687 C  CA    . PHE A 1 480 ? 0.562   -11.521 10.261  1.00 30.62  ? 480 PHE A CA    1 
ATOM   3688 C  C     . PHE A 1 480 ? 0.585   -9.998  10.276  1.00 36.93  ? 480 PHE A C     1 
ATOM   3689 O  O     . PHE A 1 480 ? 1.391   -9.380  9.573   1.00 39.87  ? 480 PHE A O     1 
ATOM   3690 C  CB    . PHE A 1 480 ? 0.754   -12.029 8.826   1.00 38.40  ? 480 PHE A CB    1 
ATOM   3691 C  CG    . PHE A 1 480 ? 1.070   -13.496 8.735   1.00 45.27  ? 480 PHE A CG    1 
ATOM   3692 C  CD1   . PHE A 1 480 ? 0.055   -14.439 8.714   1.00 46.60  ? 480 PHE A CD1   1 
ATOM   3693 C  CD2   . PHE A 1 480 ? 2.383   -13.930 8.660   1.00 39.20  ? 480 PHE A CD2   1 
ATOM   3694 C  CE1   . PHE A 1 480 ? 0.346   -15.789 8.627   1.00 54.09  ? 480 PHE A CE1   1 
ATOM   3695 C  CE2   . PHE A 1 480 ? 2.680   -15.277 8.573   1.00 55.59  ? 480 PHE A CE2   1 
ATOM   3696 C  CZ    . PHE A 1 480 ? 1.660   -16.208 8.556   1.00 52.64  ? 480 PHE A CZ    1 
ATOM   3697 N  N     . ALA A 1 481 ? -0.287  -9.371  11.065  1.00 48.82  ? 481 ALA A N     1 
ATOM   3698 C  CA    . ALA A 1 481 ? -0.412  -7.916  11.069  1.00 52.22  ? 481 ALA A CA    1 
ATOM   3699 C  C     . ALA A 1 481 ? -0.712  -7.391  9.668   1.00 51.12  ? 481 ALA A C     1 
ATOM   3700 O  O     . ALA A 1 481 ? -0.386  -6.251  9.330   1.00 49.30  ? 481 ALA A O     1 
ATOM   3701 C  CB    . ALA A 1 481 ? 0.845   -7.255  11.637  1.00 47.83  ? 481 ALA A CB    1 
ATOM   3702 N  N     . MET A 1 482 ? -1.339  -8.232  8.844   1.00 48.96  ? 482 MET A N     1 
ATOM   3703 C  CA    . MET A 1 482 ? -1.607  -7.916  7.446   1.00 50.94  ? 482 MET A CA    1 
ATOM   3704 C  C     . MET A 1 482 ? -3.095  -7.856  7.127   1.00 51.22  ? 482 MET A C     1 
ATOM   3705 O  O     . MET A 1 482 ? -3.458  -7.733  5.951   1.00 49.83  ? 482 MET A O     1 
ATOM   3706 C  CB    . MET A 1 482 ? -0.923  -8.941  6.534   1.00 40.65  ? 482 MET A CB    1 
ATOM   3707 C  CG    . MET A 1 482 ? 0.557   -8.689  6.307   1.00 33.27  ? 482 MET A CG    1 
ATOM   3708 S  SD    . MET A 1 482 ? 0.860   -7.503  4.983   1.00 44.10  ? 482 MET A SD    1 
ATOM   3709 C  CE    . MET A 1 482 ? 0.330   -8.447  3.555   1.00 38.10  ? 482 MET A CE    1 
ATOM   3710 N  N     . ARG A 1 483 ? -3.964  -7.940  8.134   1.00 52.16  ? 483 ARG A N     1 
ATOM   3711 C  CA    . ARG A 1 483 ? -5.404  -7.932  7.883   1.00 54.75  ? 483 ARG A CA    1 
ATOM   3712 C  C     . ARG A 1 483 ? -5.852  -6.758  7.025   1.00 58.99  ? 483 ARG A C     1 
ATOM   3713 O  O     . ARG A 1 483 ? -6.590  -6.981  6.051   1.00 63.49  ? 483 ARG A O     1 
ATOM   3714 C  CB    . ARG A 1 483 ? -6.160  -7.941  9.219   1.00 51.42  ? 483 ARG A CB    1 
ATOM   3715 C  CG    . ARG A 1 483 ? -7.630  -8.310  9.083   1.00 57.13  ? 483 ARG A CG    1 
ATOM   3716 C  CD    . ARG A 1 483 ? -8.429  -7.946  10.325  1.00 58.73  ? 483 ARG A CD    1 
ATOM   3717 N  NE    . ARG A 1 483 ? -8.568  -6.503  10.477  1.00 60.48  ? 483 ARG A NE    1 
ATOM   3718 C  CZ    . ARG A 1 483 ? -7.838  -5.762  11.299  1.00 66.24  ? 483 ARG A CZ    1 
ATOM   3719 N  NH1   . ARG A 1 483 ? -6.913  -6.300  12.077  1.00 63.52  ? 483 ARG A NH1   1 
ATOM   3720 N  NH2   . ARG A 1 483 ? -8.042  -4.449  11.343  1.00 80.45  ? 483 ARG A NH2   1 
ATOM   3721 N  N     . PRO A 1 484 ? -5.468  -5.513  7.315   1.00 56.47  ? 484 PRO A N     1 
ATOM   3722 C  CA    . PRO A 1 484 ? -5.900  -4.385  6.481   1.00 60.29  ? 484 PRO A CA    1 
ATOM   3723 C  C     . PRO A 1 484 ? -5.144  -4.247  5.169   1.00 55.36  ? 484 PRO A C     1 
ATOM   3724 O  O     . PRO A 1 484 ? -5.461  -3.340  4.391   1.00 55.51  ? 484 PRO A O     1 
ATOM   3725 C  CB    . PRO A 1 484 ? -5.638  -3.164  7.385   1.00 62.05  ? 484 PRO A CB    1 
ATOM   3726 C  CG    . PRO A 1 484 ? -5.368  -3.719  8.758   1.00 52.69  ? 484 PRO A CG    1 
ATOM   3727 C  CD    . PRO A 1 484 ? -4.770  -5.063  8.528   1.00 51.72  ? 484 PRO A CD    1 
ATOM   3728 N  N     . PHE A 1 485 ? -4.161  -5.109  4.891   1.00 45.80  ? 485 PHE A N     1 
ATOM   3729 C  CA    . PHE A 1 485 ? -3.305  -4.934  3.722   1.00 48.52  ? 485 PHE A CA    1 
ATOM   3730 C  C     . PHE A 1 485 ? -3.209  -6.195  2.869   1.00 43.79  ? 485 PHE A C     1 
ATOM   3731 O  O     . PHE A 1 485 ? -2.245  -6.346  2.112   1.00 45.75  ? 485 PHE A O     1 
ATOM   3732 C  CB    . PHE A 1 485 ? -1.904  -4.484  4.145   1.00 57.77  ? 485 PHE A CB    1 
ATOM   3733 C  CG    . PHE A 1 485 ? -1.903  -3.427  5.211   1.00 49.59  ? 485 PHE A CG    1 
ATOM   3734 C  CD1   . PHE A 1 485 ? -2.292  -2.130  4.921   1.00 46.96  ? 485 PHE A CD1   1 
ATOM   3735 C  CD2   . PHE A 1 485 ? -1.510  -3.731  6.504   1.00 55.81  ? 485 PHE A CD2   1 
ATOM   3736 C  CE1   . PHE A 1 485 ? -2.292  -1.156  5.903   1.00 64.15  ? 485 PHE A CE1   1 
ATOM   3737 C  CE2   . PHE A 1 485 ? -1.507  -2.761  7.489   1.00 60.63  ? 485 PHE A CE2   1 
ATOM   3738 C  CZ    . PHE A 1 485 ? -1.898  -1.472  7.188   1.00 59.02  ? 485 PHE A CZ    1 
ATOM   3739 N  N     . PHE A 1 486 ? -4.178  -7.102  2.968   1.00 55.71  ? 486 PHE A N     1 
ATOM   3740 C  CA    . PHE A 1 486 ? -4.147  -8.307  2.149   1.00 55.46  ? 486 PHE A CA    1 
ATOM   3741 C  C     . PHE A 1 486 ? -4.508  -7.971  0.708   1.00 60.11  ? 486 PHE A C     1 
ATOM   3742 O  O     . PHE A 1 486 ? -5.512  -7.301  0.446   1.00 69.62  ? 486 PHE A O     1 
ATOM   3743 C  CB    . PHE A 1 486 ? -5.099  -9.363  2.707   1.00 54.48  ? 486 PHE A CB    1 
ATOM   3744 C  CG    . PHE A 1 486 ? -4.534  -10.131 3.867   1.00 49.11  ? 486 PHE A CG    1 
ATOM   3745 C  CD1   . PHE A 1 486 ? -3.383  -10.887 3.716   1.00 47.23  ? 486 PHE A CD1   1 
ATOM   3746 C  CD2   . PHE A 1 486 ? -5.153  -10.103 5.105   1.00 43.91  ? 486 PHE A CD2   1 
ATOM   3747 C  CE1   . PHE A 1 486 ? -2.857  -11.595 4.778   1.00 44.52  ? 486 PHE A CE1   1 
ATOM   3748 C  CE2   . PHE A 1 486 ? -4.633  -10.810 6.171   1.00 44.44  ? 486 PHE A CE2   1 
ATOM   3749 C  CZ    . PHE A 1 486 ? -3.483  -11.557 6.008   1.00 49.63  ? 486 PHE A CZ    1 
ATOM   3750 N  N     . GLY A 1 487 ? -3.686  -8.440  -0.228  1.00 62.84  ? 487 GLY A N     1 
ATOM   3751 C  CA    . GLY A 1 487 ? -3.868  -8.119  -1.629  1.00 60.74  ? 487 GLY A CA    1 
ATOM   3752 C  C     . GLY A 1 487 ? -4.634  -9.161  -2.418  1.00 70.36  ? 487 GLY A C     1 
ATOM   3753 O  O     . GLY A 1 487 ? -5.218  -8.846  -3.460  1.00 77.79  ? 487 GLY A O     1 
ATOM   3754 N  N     . TYR A 1 488 ? -4.640  -10.400 -1.944  1.00 71.28  ? 488 TYR A N     1 
ATOM   3755 C  CA    . TYR A 1 488 ? -5.346  -11.473 -2.636  1.00 72.59  ? 488 TYR A CA    1 
ATOM   3756 C  C     . TYR A 1 488 ? -5.902  -12.435 -1.589  1.00 74.92  ? 488 TYR A C     1 
ATOM   3757 O  O     . TYR A 1 488 ? -6.015  -12.091 -0.408  1.00 69.37  ? 488 TYR A O     1 
ATOM   3758 C  CB    . TYR A 1 488 ? -4.419  -12.156 -3.658  1.00 71.49  ? 488 TYR A CB    1 
ATOM   3759 C  CG    . TYR A 1 488 ? -3.195  -12.813 -3.060  1.00 75.28  ? 488 TYR A CG    1 
ATOM   3760 C  CD1   . TYR A 1 488 ? -2.034  -12.086 -2.830  1.00 71.73  ? 488 TYR A CD1   1 
ATOM   3761 C  CD2   . TYR A 1 488 ? -3.196  -14.164 -2.737  1.00 75.85  ? 488 TYR A CD2   1 
ATOM   3762 C  CE1   . TYR A 1 488 ? -0.911  -12.685 -2.289  1.00 71.85  ? 488 TYR A CE1   1 
ATOM   3763 C  CE2   . TYR A 1 488 ? -2.078  -14.771 -2.195  1.00 75.78  ? 488 TYR A CE2   1 
ATOM   3764 C  CZ    . TYR A 1 488 ? -0.939  -14.027 -1.973  1.00 68.88  ? 488 TYR A CZ    1 
ATOM   3765 O  OH    . TYR A 1 488 ? 0.176   -14.626 -1.434  1.00 71.63  ? 488 TYR A OH    1 
ATOM   3766 N  N     . ASN A 1 489 ? -6.253  -13.643 -2.025  1.00 74.66  ? 489 ASN A N     1 
ATOM   3767 C  CA    . ASN A 1 489 ? -6.896  -14.607 -1.142  1.00 74.94  ? 489 ASN A CA    1 
ATOM   3768 C  C     . ASN A 1 489 ? -5.988  -14.956 0.031   1.00 69.38  ? 489 ASN A C     1 
ATOM   3769 O  O     . ASN A 1 489 ? -4.826  -15.329 -0.156  1.00 68.03  ? 489 ASN A O     1 
ATOM   3770 C  CB    . ASN A 1 489 ? -7.262  -15.868 -1.925  1.00 78.31  ? 489 ASN A CB    1 
ATOM   3771 C  CG    . ASN A 1 489 ? -8.166  -16.799 -1.143  1.00 78.07  ? 489 ASN A CG    1 
ATOM   3772 O  OD1   . ASN A 1 489 ? -7.705  -17.571 -0.304  1.00 74.73  ? 489 ASN A OD1   1 
ATOM   3773 N  ND2   . ASN A 1 489 ? -9.464  -16.734 -1.421  1.00 79.43  ? 489 ASN A ND2   1 
ATOM   3774 N  N     . PHE A 1 490 ? -6.526  -14.836 1.247   1.00 59.03  ? 490 PHE A N     1 
ATOM   3775 C  CA    . PHE A 1 490 ? -5.748  -15.179 2.432   1.00 58.51  ? 490 PHE A CA    1 
ATOM   3776 C  C     . PHE A 1 490 ? -5.440  -16.669 2.491   1.00 62.54  ? 490 PHE A C     1 
ATOM   3777 O  O     . PHE A 1 490 ? -4.372  -17.060 2.978   1.00 61.35  ? 490 PHE A O     1 
ATOM   3778 C  CB    . PHE A 1 490 ? -6.487  -14.738 3.696   1.00 50.76  ? 490 PHE A CB    1 
ATOM   3779 C  CG    . PHE A 1 490 ? -5.822  -15.176 4.970   1.00 57.63  ? 490 PHE A CG    1 
ATOM   3780 C  CD1   . PHE A 1 490 ? -4.602  -14.641 5.350   1.00 57.68  ? 490 PHE A CD1   1 
ATOM   3781 C  CD2   . PHE A 1 490 ? -6.420  -16.117 5.792   1.00 51.89  ? 490 PHE A CD2   1 
ATOM   3782 C  CE1   . PHE A 1 490 ? -3.988  -15.041 6.523   1.00 41.93  ? 490 PHE A CE1   1 
ATOM   3783 C  CE2   . PHE A 1 490 ? -5.812  -16.520 6.966   1.00 56.70  ? 490 PHE A CE2   1 
ATOM   3784 C  CZ    . PHE A 1 490 ? -4.594  -15.981 7.332   1.00 48.72  ? 490 PHE A CZ    1 
ATOM   3785 N  N     . GLY A 1 491 ? -6.355  -17.512 2.010   1.00 65.00  ? 491 GLY A N     1 
ATOM   3786 C  CA    . GLY A 1 491 ? -6.075  -18.938 1.964   1.00 60.37  ? 491 GLY A CA    1 
ATOM   3787 C  C     . GLY A 1 491 ? -4.838  -19.253 1.146   1.00 62.44  ? 491 GLY A C     1 
ATOM   3788 O  O     . GLY A 1 491 ? -3.968  -20.015 1.576   1.00 59.02  ? 491 GLY A O     1 
ATOM   3789 N  N     . LYS A 1 492 ? -4.743  -18.668 -0.051  1.00 60.08  ? 492 LYS A N     1 
ATOM   3790 C  CA    . LYS A 1 492 ? -3.535  -18.825 -0.851  1.00 62.77  ? 492 LYS A CA    1 
ATOM   3791 C  C     . LYS A 1 492 ? -2.341  -18.154 -0.186  1.00 66.73  ? 492 LYS A C     1 
ATOM   3792 O  O     . LYS A 1 492 ? -1.195  -18.565 -0.406  1.00 59.53  ? 492 LYS A O     1 
ATOM   3793 C  CB    . LYS A 1 492 ? -3.753  -18.254 -2.253  1.00 61.55  ? 492 LYS A CB    1 
ATOM   3794 C  CG    . LYS A 1 492 ? -5.077  -18.650 -2.888  1.00 75.76  ? 492 LYS A CG    1 
ATOM   3795 C  CD    . LYS A 1 492 ? -5.226  -20.160 -2.977  1.00 76.34  ? 492 LYS A CD    1 
ATOM   3796 C  CE    . LYS A 1 492 ? -6.575  -20.544 -3.563  1.00 82.37  ? 492 LYS A CE    1 
ATOM   3797 N  NZ    . LYS A 1 492 ? -6.763  -22.020 -3.611  1.00 83.35  ? 492 LYS A NZ    1 
ATOM   3798 N  N     . TYR A 1 493 ? -2.588  -17.123 0.626   1.00 63.81  ? 493 TYR A N     1 
ATOM   3799 C  CA    . TYR A 1 493 ? -1.508  -16.474 1.361   1.00 55.05  ? 493 TYR A CA    1 
ATOM   3800 C  C     . TYR A 1 493 ? -0.849  -17.448 2.329   1.00 56.24  ? 493 TYR A C     1 
ATOM   3801 O  O     . TYR A 1 493 ? 0.380   -17.584 2.353   1.00 58.13  ? 493 TYR A O     1 
ATOM   3802 C  CB    . TYR A 1 493 ? -2.050  -15.250 2.101   1.00 51.91  ? 493 TYR A CB    1 
ATOM   3803 C  CG    . TYR A 1 493 ? -1.046  -14.551 2.991   1.00 55.11  ? 493 TYR A CG    1 
ATOM   3804 C  CD1   . TYR A 1 493 ? -0.062  -13.732 2.454   1.00 57.27  ? 493 TYR A CD1   1 
ATOM   3805 C  CD2   . TYR A 1 493 ? -1.095  -14.696 4.372   1.00 53.71  ? 493 TYR A CD2   1 
ATOM   3806 C  CE1   . TYR A 1 493 ? 0.853   -13.087 3.265   1.00 53.43  ? 493 TYR A CE1   1 
ATOM   3807 C  CE2   . TYR A 1 493 ? -0.184  -14.054 5.191   1.00 57.66  ? 493 TYR A CE2   1 
ATOM   3808 C  CZ    . TYR A 1 493 ? 0.787   -13.251 4.632   1.00 47.66  ? 493 TYR A CZ    1 
ATOM   3809 O  OH    . TYR A 1 493 ? 1.695   -12.610 5.442   1.00 52.29  ? 493 TYR A OH    1 
ATOM   3810 N  N     . LEU A 1 494 ? -1.655  -18.140 3.138   1.00 47.54  ? 494 LEU A N     1 
ATOM   3811 C  CA    . LEU A 1 494 ? -1.107  -19.146 4.042   1.00 52.85  ? 494 LEU A CA    1 
ATOM   3812 C  C     . LEU A 1 494 ? -0.358  -20.231 3.281   1.00 62.36  ? 494 LEU A C     1 
ATOM   3813 O  O     . LEU A 1 494 ? 0.633   -20.772 3.785   1.00 69.59  ? 494 LEU A O     1 
ATOM   3814 C  CB    . LEU A 1 494 ? -2.225  -19.762 4.884   1.00 53.01  ? 494 LEU A CB    1 
ATOM   3815 C  CG    . LEU A 1 494 ? -2.936  -18.832 5.869   1.00 50.71  ? 494 LEU A CG    1 
ATOM   3816 C  CD1   . LEU A 1 494 ? -4.073  -19.558 6.571   1.00 48.70  ? 494 LEU A CD1   1 
ATOM   3817 C  CD2   . LEU A 1 494 ? -1.950  -18.272 6.882   1.00 48.40  ? 494 LEU A CD2   1 
ATOM   3818 N  N     . ALA A 1 495 ? -0.812  -20.562 2.069   1.00 67.59  ? 495 ALA A N     1 
ATOM   3819 C  CA    . ALA A 1 495 ? -0.114  -21.562 1.270   1.00 63.39  ? 495 ALA A CA    1 
ATOM   3820 C  C     . ALA A 1 495 ? 1.217   -21.036 0.749   1.00 63.20  ? 495 ALA A C     1 
ATOM   3821 O  O     . ALA A 1 495 ? 2.179   -21.802 0.623   1.00 65.01  ? 495 ALA A O     1 
ATOM   3822 C  CB    . ALA A 1 495 ? -0.997  -22.018 0.109   1.00 64.31  ? 495 ALA A CB    1 
ATOM   3823 N  N     . HIS A 1 496 ? 1.292   -19.738 0.444   1.00 61.85  ? 496 HIS A N     1 
ATOM   3824 C  CA    . HIS A 1 496 ? 2.538   -19.168 -0.057  1.00 68.39  ? 496 HIS A CA    1 
ATOM   3825 C  C     . HIS A 1 496 ? 3.650   -19.262 0.979   1.00 62.82  ? 496 HIS A C     1 
ATOM   3826 O  O     . HIS A 1 496 ? 4.818   -19.447 0.621   1.00 50.83  ? 496 HIS A O     1 
ATOM   3827 C  CB    . HIS A 1 496 ? 2.316   -17.713 -0.472  1.00 68.66  ? 496 HIS A CB    1 
ATOM   3828 C  CG    . HIS A 1 496 ? 3.319   -17.208 -1.462  1.00 68.40  ? 496 HIS A CG    1 
ATOM   3829 N  ND1   . HIS A 1 496 ? 3.668   -17.914 -2.593  1.00 70.38  ? 496 HIS A ND1   1 
ATOM   3830 C  CD2   . HIS A 1 496 ? 4.040   -16.062 -1.497  1.00 64.78  ? 496 HIS A CD2   1 
ATOM   3831 C  CE1   . HIS A 1 496 ? 4.565   -17.228 -3.279  1.00 70.20  ? 496 HIS A CE1   1 
ATOM   3832 N  NE2   . HIS A 1 496 ? 4.808   -16.100 -2.636  1.00 60.48  ? 496 HIS A NE2   1 
ATOM   3833 N  N     . TRP A 1 497 ? 3.310   -19.139 2.263   1.00 56.65  ? 497 TRP A N     1 
ATOM   3834 C  CA    . TRP A 1 497 ? 4.315   -19.270 3.313   1.00 59.44  ? 497 TRP A CA    1 
ATOM   3835 C  C     . TRP A 1 497 ? 4.712   -20.726 3.515   1.00 62.45  ? 497 TRP A C     1 
ATOM   3836 O  O     . TRP A 1 497 ? 5.901   -21.045 3.634   1.00 59.83  ? 497 TRP A O     1 
ATOM   3837 C  CB    . TRP A 1 497 ? 3.794   -18.664 4.616   1.00 56.75  ? 497 TRP A CB    1 
ATOM   3838 C  CG    . TRP A 1 497 ? 3.979   -17.183 4.702   1.00 59.93  ? 497 TRP A CG    1 
ATOM   3839 C  CD1   . TRP A 1 497 ? 3.192   -16.223 4.135   1.00 58.89  ? 497 TRP A CD1   1 
ATOM   3840 C  CD2   . TRP A 1 497 ? 5.019   -16.488 5.400   1.00 54.29  ? 497 TRP A CD2   1 
ATOM   3841 N  NE1   . TRP A 1 497 ? 3.679   -14.974 4.435   1.00 52.62  ? 497 TRP A NE1   1 
ATOM   3842 C  CE2   . TRP A 1 497 ? 4.800   -15.110 5.211   1.00 61.20  ? 497 TRP A CE2   1 
ATOM   3843 C  CE3   . TRP A 1 497 ? 6.114   -16.899 6.166   1.00 55.08  ? 497 TRP A CE3   1 
ATOM   3844 C  CZ2   . TRP A 1 497 ? 5.636   -14.139 5.760   1.00 60.35  ? 497 TRP A CZ2   1 
ATOM   3845 C  CZ3   . TRP A 1 497 ? 6.943   -15.934 6.710   1.00 58.54  ? 497 TRP A CZ3   1 
ATOM   3846 C  CH2   . TRP A 1 497 ? 6.699   -14.571 6.504   1.00 58.21  ? 497 TRP A CH2   1 
ATOM   3847 N  N     . LEU A 1 498 ? 3.729   -21.627 3.564   1.00 65.93  ? 498 LEU A N     1 
ATOM   3848 C  CA    . LEU A 1 498 ? 4.031   -23.045 3.711   1.00 59.75  ? 498 LEU A CA    1 
ATOM   3849 C  C     . LEU A 1 498 ? 4.819   -23.587 2.526   1.00 72.09  ? 498 LEU A C     1 
ATOM   3850 O  O     . LEU A 1 498 ? 5.534   -24.584 2.673   1.00 78.68  ? 498 LEU A O     1 
ATOM   3851 C  CB    . LEU A 1 498 ? 2.738   -23.841 3.893   1.00 67.44  ? 498 LEU A CB    1 
ATOM   3852 C  CG    . LEU A 1 498 ? 1.923   -23.502 5.143   1.00 65.19  ? 498 LEU A CG    1 
ATOM   3853 C  CD1   . LEU A 1 498 ? 0.607   -24.261 5.146   1.00 53.49  ? 498 LEU A CD1   1 
ATOM   3854 C  CD2   . LEU A 1 498 ? 2.725   -23.804 6.401   1.00 57.64  ? 498 LEU A CD2   1 
ATOM   3855 N  N     . SER A 1 499 ? 4.708   -22.950 1.358   1.00 76.40  ? 499 SER A N     1 
ATOM   3856 C  CA    . SER A 1 499 ? 5.474   -23.384 0.197   1.00 83.45  ? 499 SER A CA    1 
ATOM   3857 C  C     . SER A 1 499 ? 6.963   -23.113 0.354   1.00 79.73  ? 499 SER A C     1 
ATOM   3858 O  O     . SER A 1 499 ? 7.772   -23.753 -0.326  1.00 86.03  ? 499 SER A O     1 
ATOM   3859 C  CB    . SER A 1 499 ? 4.951   -22.694 -1.065  1.00 86.36  ? 499 SER A CB    1 
ATOM   3860 O  OG    . SER A 1 499 ? 5.085   -21.286 -0.970  1.00 81.70  ? 499 SER A OG    1 
ATOM   3861 N  N     A MET A 1 500 ? 7.346   -22.185 1.234   0.50 81.37  ? 500 MET A N     1 
ATOM   3862 N  N     B MET A 1 500 ? 7.342   -22.177 1.228   0.50 88.02  ? 500 MET A N     1 
ATOM   3863 C  CA    A MET A 1 500 ? 8.759   -21.881 1.421   0.50 88.01  ? 500 MET A CA    1 
ATOM   3864 C  CA    B MET A 1 500 ? 8.752   -21.876 1.437   0.50 76.89  ? 500 MET A CA    1 
ATOM   3865 C  C     A MET A 1 500 ? 9.523   -23.039 2.050   0.50 85.89  ? 500 MET A C     1 
ATOM   3866 C  C     B MET A 1 500 ? 9.516   -23.064 2.004   0.50 77.96  ? 500 MET A C     1 
ATOM   3867 O  O     A MET A 1 500 ? 10.757  -23.052 1.998   0.50 87.81  ? 500 MET A O     1 
ATOM   3868 O  O     B MET A 1 500 ? 10.742  -23.125 1.862   0.50 86.78  ? 500 MET A O     1 
ATOM   3869 C  CB    A MET A 1 500 ? 8.918   -20.623 2.275   0.50 71.40  ? 500 MET A CB    1 
ATOM   3870 C  CB    B MET A 1 500 ? 8.898   -20.670 2.367   0.50 73.04  ? 500 MET A CB    1 
ATOM   3871 C  CG    A MET A 1 500 ? 8.251   -19.392 1.682   0.50 64.58  ? 500 MET A CG    1 
ATOM   3872 C  CG    B MET A 1 500 ? 8.255   -19.398 1.838   0.50 70.30  ? 500 MET A CG    1 
ATOM   3873 S  SD    A MET A 1 500 ? 8.785   -19.066 -0.009  0.50 77.17  ? 500 MET A SD    1 
ATOM   3874 S  SD    B MET A 1 500 ? 8.243   -18.062 3.049   0.50 63.53  ? 500 MET A SD    1 
ATOM   3875 C  CE    A MET A 1 500 ? 7.804   -17.620 -0.404  0.50 58.70  ? 500 MET A CE    1 
ATOM   3876 C  CE    B MET A 1 500 ? 9.991   -17.900 3.399   0.50 62.36  ? 500 MET A CE    1 
ATOM   3877 N  N     . ALA A 1 501 ? 8.823   -24.006 2.642   1.00 84.16  ? 501 ALA A N     1 
ATOM   3878 C  CA    . ALA A 1 501 ? 9.465   -25.187 3.204   1.00 82.80  ? 501 ALA A CA    1 
ATOM   3879 C  C     . ALA A 1 501 ? 9.777   -26.244 2.153   1.00 99.75  ? 501 ALA A C     1 
ATOM   3880 O  O     . ALA A 1 501 ? 10.376  -27.271 2.491   1.00 100.33 ? 501 ALA A O     1 
ATOM   3881 C  CB    . ALA A 1 501 ? 8.585   -25.793 4.300   1.00 76.90  ? 501 ALA A CB    1 
ATOM   3882 N  N     . HIS A 1 502 ? 9.389   -26.021 0.898   1.00 109.12 ? 502 HIS A N     1 
ATOM   3883 C  CA    . HIS A 1 502 ? 9.647   -26.962 -0.182  1.00 117.33 ? 502 HIS A CA    1 
ATOM   3884 C  C     . HIS A 1 502 ? 10.793  -26.536 -1.089  1.00 127.48 ? 502 HIS A C     1 
ATOM   3885 O  O     . HIS A 1 502 ? 11.249  -27.346 -1.904  1.00 144.10 ? 502 HIS A O     1 
ATOM   3886 C  CB    . HIS A 1 502 ? 8.383   -27.159 -1.030  1.00 123.83 ? 502 HIS A CB    1 
ATOM   3887 C  CG    . HIS A 1 502 ? 7.236   -27.760 -0.279  1.00 130.05 ? 502 HIS A CG    1 
ATOM   3888 N  ND1   . HIS A 1 502 ? 5.964   -27.840 -0.803  1.00 125.41 ? 502 HIS A ND1   1 
ATOM   3889 C  CD2   . HIS A 1 502 ? 7.169   -28.314 0.955   1.00 129.41 ? 502 HIS A CD2   1 
ATOM   3890 C  CE1   . HIS A 1 502 ? 5.162   -28.415 0.075   1.00 123.09 ? 502 HIS A CE1   1 
ATOM   3891 N  NE2   . HIS A 1 502 ? 5.869   -28.713 1.151   1.00 126.63 ? 502 HIS A NE2   1 
ATOM   3892 N  N     . ARG A 1 503 ? 11.266  -25.299 -0.973  1.00 124.71 ? 503 ARG A N     1 
ATOM   3893 C  CA    . ARG A 1 503 ? 12.326  -24.828 -1.851  1.00 133.04 ? 503 ARG A CA    1 
ATOM   3894 C  C     . ARG A 1 503 ? 13.636  -25.545 -1.529  1.00 136.77 ? 503 ARG A C     1 
ATOM   3895 O  O     . ARG A 1 503 ? 13.941  -25.791 -0.357  1.00 128.61 ? 503 ARG A O     1 
ATOM   3896 C  CB    . ARG A 1 503 ? 12.506  -23.316 -1.713  1.00 129.15 ? 503 ARG A CB    1 
ATOM   3897 C  CG    . ARG A 1 503 ? 11.265  -22.511 -2.073  1.00 125.13 ? 503 ARG A CG    1 
ATOM   3898 C  CD    . ARG A 1 503 ? 11.493  -21.019 -1.887  1.00 125.86 ? 503 ARG A CD    1 
ATOM   3899 N  NE    . ARG A 1 503 ? 12.463  -20.486 -2.837  1.00 138.06 ? 503 ARG A NE    1 
ATOM   3900 C  CZ    . ARG A 1 503 ? 12.144  -19.911 -3.989  1.00 145.44 ? 503 ARG A CZ    1 
ATOM   3901 N  NH1   . ARG A 1 503 ? 10.884  -19.775 -4.369  1.00 141.06 ? 503 ARG A NH1   1 
ATOM   3902 N  NH2   . ARG A 1 503 ? 13.114  -19.458 -4.778  1.00 149.00 ? 503 ARG A NH2   1 
ATOM   3903 N  N     . PRO A 1 504 ? 14.427  -25.894 -2.542  1.00 132.85 ? 504 PRO A N     1 
ATOM   3904 C  CA    . PRO A 1 504 ? 15.679  -26.615 -2.282  1.00 135.36 ? 504 PRO A CA    1 
ATOM   3905 C  C     . PRO A 1 504 ? 16.689  -25.741 -1.555  1.00 133.92 ? 504 PRO A C     1 
ATOM   3906 O  O     . PRO A 1 504 ? 16.773  -24.532 -1.784  1.00 129.47 ? 504 PRO A O     1 
ATOM   3907 C  CB    . PRO A 1 504 ? 16.175  -26.988 -3.686  1.00 134.33 ? 504 PRO A CB    1 
ATOM   3908 C  CG    . PRO A 1 504 ? 14.977  -26.843 -4.580  1.00 132.30 ? 504 PRO A CG    1 
ATOM   3909 C  CD    . PRO A 1 504 ? 14.166  -25.739 -3.981  1.00 132.49 ? 504 PRO A CD    1 
ATOM   3910 N  N     . ALA A 1 505 ? 17.462  -26.372 -0.671  1.00 139.70 ? 505 ALA A N     1 
ATOM   3911 C  CA    . ALA A 1 505 ? 18.513  -25.686 0.079   1.00 135.20 ? 505 ALA A CA    1 
ATOM   3912 C  C     . ALA A 1 505 ? 17.965  -24.459 0.802   1.00 129.43 ? 505 ALA A C     1 
ATOM   3913 O  O     . ALA A 1 505 ? 18.614  -23.414 0.885   1.00 125.29 ? 505 ALA A O     1 
ATOM   3914 C  CB    . ALA A 1 505 ? 19.679  -25.305 -0.835  1.00 133.04 ? 505 ALA A CB    1 
ATOM   3915 N  N     . ALA A 1 506 ? 16.752  -24.589 1.334   1.00 118.43 ? 506 ALA A N     1 
ATOM   3916 C  CA    . ALA A 1 506 ? 16.105  -23.484 2.026   1.00 99.05  ? 506 ALA A CA    1 
ATOM   3917 C  C     . ALA A 1 506 ? 16.619  -23.384 3.457   1.00 90.16  ? 506 ALA A C     1 
ATOM   3918 O  O     . ALA A 1 506 ? 16.667  -24.383 4.181   1.00 88.28  ? 506 ALA A O     1 
ATOM   3919 C  CB    . ALA A 1 506 ? 14.587  -23.666 2.019   1.00 96.42  ? 506 ALA A CB    1 
ATOM   3920 N  N     . LYS A 1 507 ? 17.005  -22.176 3.858   1.00 89.38  ? 507 LYS A N     1 
ATOM   3921 C  CA    . LYS A 1 507 ? 17.470  -21.894 5.214   1.00 79.18  ? 507 LYS A CA    1 
ATOM   3922 C  C     . LYS A 1 507 ? 16.371  -21.102 5.917   1.00 77.24  ? 507 LYS A C     1 
ATOM   3923 O  O     . LYS A 1 507 ? 16.410  -19.873 5.996   1.00 79.29  ? 507 LYS A O     1 
ATOM   3924 C  CB    . LYS A 1 507 ? 18.799  -21.133 5.187   1.00 78.97  ? 507 LYS A CB    1 
ATOM   3925 C  CG    . LYS A 1 507 ? 19.894  -21.826 4.389   1.00 92.96  ? 507 LYS A CG    1 
ATOM   3926 C  CD    . LYS A 1 507 ? 21.159  -20.984 4.338   1.00 103.09 ? 507 LYS A CD    1 
ATOM   3927 C  CE    . LYS A 1 507 ? 22.227  -21.641 3.479   1.00 97.80  ? 507 LYS A CE    1 
ATOM   3928 N  NZ    . LYS A 1 507 ? 23.460  -20.810 3.395   1.00 115.79 ? 507 LYS A NZ    1 
ATOM   3929 N  N     . LEU A 1 508 ? 15.380  -21.823 6.430   1.00 72.78  ? 508 LEU A N     1 
ATOM   3930 C  CA    . LEU A 1 508 ? 14.222  -21.175 7.027   1.00 67.16  ? 508 LEU A CA    1 
ATOM   3931 C  C     . LEU A 1 508 ? 14.596  -20.545 8.367   1.00 61.49  ? 508 LEU A C     1 
ATOM   3932 O  O     . LEU A 1 508 ? 15.314  -21.157 9.165   1.00 64.57  ? 508 LEU A O     1 
ATOM   3933 C  CB    . LEU A 1 508 ? 13.087  -22.179 7.218   1.00 68.44  ? 508 LEU A CB    1 
ATOM   3934 C  CG    . LEU A 1 508 ? 12.623  -22.911 5.956   1.00 61.62  ? 508 LEU A CG    1 
ATOM   3935 C  CD1   . LEU A 1 508 ? 11.489  -23.871 6.279   1.00 69.87  ? 508 LEU A CD1   1 
ATOM   3936 C  CD2   . LEU A 1 508 ? 12.203  -21.921 4.880   1.00 65.96  ? 508 LEU A CD2   1 
ATOM   3937 N  N     . PRO A 1 509 ? 14.130  -19.331 8.642   1.00 57.10  ? 509 PRO A N     1 
ATOM   3938 C  CA    . PRO A 1 509 ? 14.446  -18.683 9.917   1.00 61.16  ? 509 PRO A CA    1 
ATOM   3939 C  C     . PRO A 1 509 ? 13.516  -19.138 11.032  1.00 50.59  ? 509 PRO A C     1 
ATOM   3940 O  O     . PRO A 1 509 ? 12.412  -19.635 10.802  1.00 59.83  ? 509 PRO A O     1 
ATOM   3941 C  CB    . PRO A 1 509 ? 14.244  -17.197 9.608   1.00 51.40  ? 509 PRO A CB    1 
ATOM   3942 C  CG    . PRO A 1 509 ? 13.165  -17.196 8.574   1.00 47.60  ? 509 PRO A CG    1 
ATOM   3943 C  CD    . PRO A 1 509 ? 13.375  -18.441 7.742   1.00 56.63  ? 509 PRO A CD    1 
ATOM   3944 N  N     . LYS A 1 510 ? 13.989  -18.954 12.262  1.00 48.34  ? 510 LYS A N     1 
ATOM   3945 C  CA    . LYS A 1 510 ? 13.174  -19.262 13.426  1.00 40.36  ? 510 LYS A CA    1 
ATOM   3946 C  C     . LYS A 1 510 ? 12.025  -18.265 13.551  1.00 44.45  ? 510 LYS A C     1 
ATOM   3947 O  O     . LYS A 1 510 ? 12.023  -17.194 12.938  1.00 45.05  ? 510 LYS A O     1 
ATOM   3948 C  CB    . LYS A 1 510 ? 14.023  -19.250 14.698  1.00 42.35  ? 510 LYS A CB    1 
ATOM   3949 C  CG    . LYS A 1 510 ? 14.939  -20.454 14.846  1.00 40.66  ? 510 LYS A CG    1 
ATOM   3950 C  CD    . LYS A 1 510 ? 15.597  -20.482 16.216  1.00 44.84  ? 510 LYS A CD    1 
ATOM   3951 C  CE    . LYS A 1 510 ? 16.363  -21.777 16.434  1.00 38.07  ? 510 LYS A CE    1 
ATOM   3952 N  NZ    . LYS A 1 510 ? 15.474  -22.967 16.324  1.00 49.99  ? 510 LYS A NZ    1 
ATOM   3953 N  N     . ILE A 1 511 ? 11.036  -18.632 14.364  1.00 39.66  ? 511 ILE A N     1 
ATOM   3954 C  CA    . ILE A 1 511 ? 9.833   -17.833 14.557  1.00 35.28  ? 511 ILE A CA    1 
ATOM   3955 C  C     . ILE A 1 511 ? 9.545   -17.737 16.048  1.00 38.27  ? 511 ILE A C     1 
ATOM   3956 O  O     . ILE A 1 511 ? 9.542   -18.754 16.751  1.00 45.68  ? 511 ILE A O     1 
ATOM   3957 C  CB    . ILE A 1 511 ? 8.627   -18.433 13.809  1.00 46.77  ? 511 ILE A CB    1 
ATOM   3958 C  CG1   . ILE A 1 511 ? 8.918   -18.511 12.308  1.00 46.06  ? 511 ILE A CG1   1 
ATOM   3959 C  CG2   . ILE A 1 511 ? 7.374   -17.614 14.074  1.00 36.79  ? 511 ILE A CG2   1 
ATOM   3960 C  CD1   . ILE A 1 511 ? 7.799   -19.128 11.498  1.00 44.32  ? 511 ILE A CD1   1 
ATOM   3961 N  N     . PHE A 1 512 ? 9.300   -16.518 16.527  1.00 34.42  ? 512 PHE A N     1 
ATOM   3962 C  CA    . PHE A 1 512 ? 9.006   -16.264 17.930  1.00 38.67  ? 512 PHE A CA    1 
ATOM   3963 C  C     . PHE A 1 512 ? 7.739   -15.429 18.046  1.00 32.66  ? 512 PHE A C     1 
ATOM   3964 O  O     . PHE A 1 512 ? 7.320   -14.759 17.098  1.00 31.81  ? 512 PHE A O     1 
ATOM   3965 C  CB    . PHE A 1 512 ? 10.162  -15.535 18.635  1.00 35.03  ? 512 PHE A CB    1 
ATOM   3966 C  CG    . PHE A 1 512 ? 11.491  -16.221 18.501  1.00 43.23  ? 512 PHE A CG    1 
ATOM   3967 C  CD1   . PHE A 1 512 ? 12.300  -15.985 17.401  1.00 41.57  ? 512 PHE A CD1   1 
ATOM   3968 C  CD2   . PHE A 1 512 ? 11.939  -17.091 19.481  1.00 41.63  ? 512 PHE A CD2   1 
ATOM   3969 C  CE1   . PHE A 1 512 ? 13.526  -16.611 17.277  1.00 41.94  ? 512 PHE A CE1   1 
ATOM   3970 C  CE2   . PHE A 1 512 ? 13.164  -17.719 19.363  1.00 40.01  ? 512 PHE A CE2   1 
ATOM   3971 C  CZ    . PHE A 1 512 ? 13.958  -17.479 18.259  1.00 39.36  ? 512 PHE A CZ    1 
ATOM   3972 N  N     . HIS A 1 513 ? 7.133   -15.473 19.231  1.00 33.21  ? 513 HIS A N     1 
ATOM   3973 C  CA    . HIS A 1 513 ? 5.972   -14.655 19.556  1.00 39.47  ? 513 HIS A CA    1 
ATOM   3974 C  C     . HIS A 1 513 ? 6.223   -13.965 20.887  1.00 38.70  ? 513 HIS A C     1 
ATOM   3975 O  O     . HIS A 1 513 ? 6.532   -14.624 21.886  1.00 32.35  ? 513 HIS A O     1 
ATOM   3976 C  CB    . HIS A 1 513 ? 4.691   -15.492 19.622  1.00 34.85  ? 513 HIS A CB    1 
ATOM   3977 C  CG    . HIS A 1 513 ? 3.436   -14.674 19.657  1.00 39.54  ? 513 HIS A CG    1 
ATOM   3978 N  ND1   . HIS A 1 513 ? 2.885   -14.203 20.829  1.00 46.30  ? 513 HIS A ND1   1 
ATOM   3979 C  CD2   . HIS A 1 513 ? 2.625   -14.244 18.661  1.00 38.64  ? 513 HIS A CD2   1 
ATOM   3980 C  CE1   . HIS A 1 513 ? 1.789   -13.518 20.554  1.00 38.37  ? 513 HIS A CE1   1 
ATOM   3981 N  NE2   . HIS A 1 513 ? 1.609   -13.528 19.246  1.00 38.83  ? 513 HIS A NE2   1 
ATOM   3982 N  N     . VAL A 1 514 ? 6.095   -12.640 20.895  1.00 40.08  ? 514 VAL A N     1 
ATOM   3983 C  CA    . VAL A 1 514 ? 6.365   -11.831 22.073  1.00 39.46  ? 514 VAL A CA    1 
ATOM   3984 C  C     . VAL A 1 514 ? 5.079   -11.128 22.488  1.00 37.86  ? 514 VAL A C     1 
ATOM   3985 O  O     . VAL A 1 514 ? 4.057   -11.197 21.806  1.00 48.79  ? 514 VAL A O     1 
ATOM   3986 C  CB    . VAL A 1 514 ? 7.500   -10.815 21.834  1.00 36.21  ? 514 VAL A CB    1 
ATOM   3987 C  CG1   . VAL A 1 514 ? 8.796   -11.537 21.503  1.00 32.62  ? 514 VAL A CG1   1 
ATOM   3988 C  CG2   . VAL A 1 514 ? 7.123   -9.854  20.714  1.00 36.41  ? 514 VAL A CG2   1 
ATOM   3989 N  N     . ASN A 1 515 ? 5.145   -10.447 23.632  1.00 43.32  ? 515 ASN A N     1 
ATOM   3990 C  CA    . ASN A 1 515 ? 3.983   -9.718  24.147  1.00 42.61  ? 515 ASN A CA    1 
ATOM   3991 C  C     . ASN A 1 515 ? 4.486   -8.790  25.259  1.00 55.96  ? 515 ASN A C     1 
ATOM   3992 O  O     . ASN A 1 515 ? 4.589   -9.197  26.414  1.00 57.61  ? 515 ASN A O     1 
ATOM   3993 C  CB    . ASN A 1 515 ? 2.907   -10.660 24.648  1.00 39.60  ? 515 ASN A CB    1 
ATOM   3994 C  CG    . ASN A 1 515 ? 1.716   -9.928  25.238  1.00 45.07  ? 515 ASN A CG    1 
ATOM   3995 O  OD1   . ASN A 1 515 ? 1.421   -8.791  24.868  1.00 51.07  ? 515 ASN A OD1   1 
ATOM   3996 N  ND2   . ASN A 1 515 ? 1.023   -10.580 26.163  1.00 54.50  ? 515 ASN A ND2   1 
ATOM   3997 N  N     . TRP A 1 516 ? 4.796   -7.549  24.883  1.00 53.55  ? 516 TRP A N     1 
ATOM   3998 C  CA    . TRP A 1 516 ? 5.250   -6.556  25.845  1.00 55.77  ? 516 TRP A CA    1 
ATOM   3999 C  C     . TRP A 1 516 ? 4.122   -5.993  26.699  1.00 63.58  ? 516 TRP A C     1 
ATOM   4000 O  O     . TRP A 1 516 ? 4.401   -5.357  27.722  1.00 69.05  ? 516 TRP A O     1 
ATOM   4001 C  CB    . TRP A 1 516 ? 5.943   -5.390  25.135  1.00 53.31  ? 516 TRP A CB    1 
ATOM   4002 C  CG    . TRP A 1 516 ? 6.902   -5.771  24.046  1.00 46.59  ? 516 TRP A CG    1 
ATOM   4003 C  CD1   . TRP A 1 516 ? 7.022   -5.178  22.823  1.00 45.63  ? 516 TRP A CD1   1 
ATOM   4004 C  CD2   . TRP A 1 516 ? 7.878   -6.819  24.080  1.00 45.18  ? 516 TRP A CD2   1 
ATOM   4005 N  NE1   . TRP A 1 516 ? 8.011   -5.790  22.094  1.00 46.17  ? 516 TRP A NE1   1 
ATOM   4006 C  CE2   . TRP A 1 516 ? 8.552   -6.802  22.842  1.00 40.88  ? 516 TRP A CE2   1 
ATOM   4007 C  CE3   . TRP A 1 516 ? 8.247   -7.771  25.035  1.00 49.58  ? 516 TRP A CE3   1 
ATOM   4008 C  CZ2   . TRP A 1 516 ? 9.572   -7.699  22.535  1.00 49.36  ? 516 TRP A CZ2   1 
ATOM   4009 C  CZ3   . TRP A 1 516 ? 9.261   -8.661  24.728  1.00 53.17  ? 516 TRP A CZ3   1 
ATOM   4010 C  CH2   . TRP A 1 516 ? 9.912   -8.618  23.488  1.00 50.95  ? 516 TRP A CH2   1 
ATOM   4011 N  N     . PHE A 1 517 ? 2.864   -6.199  26.310  1.00 59.05  ? 517 PHE A N     1 
ATOM   4012 C  CA    . PHE A 1 517 ? 1.744   -5.500  26.926  1.00 68.92  ? 517 PHE A CA    1 
ATOM   4013 C  C     . PHE A 1 517 ? 0.934   -6.385  27.867  1.00 67.04  ? 517 PHE A C     1 
ATOM   4014 O  O     . PHE A 1 517 ? -0.219  -6.063  28.166  1.00 68.23  ? 517 PHE A O     1 
ATOM   4015 C  CB    . PHE A 1 517 ? 0.835   -4.909  25.848  1.00 61.96  ? 517 PHE A CB    1 
ATOM   4016 C  CG    . PHE A 1 517 ? 1.561   -4.066  24.842  1.00 57.44  ? 517 PHE A CG    1 
ATOM   4017 C  CD1   . PHE A 1 517 ? 1.880   -2.747  25.121  1.00 60.50  ? 517 PHE A CD1   1 
ATOM   4018 C  CD2   . PHE A 1 517 ? 1.925   -4.592  23.616  1.00 52.17  ? 517 PHE A CD2   1 
ATOM   4019 C  CE1   . PHE A 1 517 ? 2.550   -1.971  24.195  1.00 58.15  ? 517 PHE A CE1   1 
ATOM   4020 C  CE2   . PHE A 1 517 ? 2.594   -3.823  22.686  1.00 54.09  ? 517 PHE A CE2   1 
ATOM   4021 C  CZ    . PHE A 1 517 ? 2.907   -2.510  22.975  1.00 59.17  ? 517 PHE A CZ    1 
ATOM   4022 N  N     . ARG A 1 518 ? 1.508   -7.486  28.347  1.00 69.74  ? 518 ARG A N     1 
ATOM   4023 C  CA    . ARG A 1 518 ? 0.800   -8.327  29.305  1.00 79.38  ? 518 ARG A CA    1 
ATOM   4024 C  C     . ARG A 1 518 ? 0.771   -7.641  30.666  1.00 98.06  ? 518 ARG A C     1 
ATOM   4025 O  O     . ARG A 1 518 ? 1.823   -7.333  31.237  1.00 100.22 ? 518 ARG A O     1 
ATOM   4026 C  CB    . ARG A 1 518 ? 1.458   -9.700  29.409  1.00 71.00  ? 518 ARG A CB    1 
ATOM   4027 C  CG    . ARG A 1 518 ? 0.731   -10.643 30.356  1.00 77.21  ? 518 ARG A CG    1 
ATOM   4028 C  CD    . ARG A 1 518 ? 1.323   -12.043 30.342  1.00 71.98  ? 518 ARG A CD    1 
ATOM   4029 N  NE    . ARG A 1 518 ? 0.535   -12.963 31.154  1.00 75.91  ? 518 ARG A NE    1 
ATOM   4030 C  CZ    . ARG A 1 518 ? 0.788   -14.258 31.284  1.00 79.36  ? 518 ARG A CZ    1 
ATOM   4031 N  NH1   . ARG A 1 518 ? 1.813   -14.828 30.671  1.00 74.48  ? 518 ARG A NH1   1 
ATOM   4032 N  NH2   . ARG A 1 518 ? -0.007  -15.001 32.049  1.00 81.22  ? 518 ARG A NH2   1 
ATOM   4033 N  N     . LYS A 1 519 ? -0.430  -7.400  31.183  1.00 103.40 ? 519 LYS A N     1 
ATOM   4034 C  CA    . LYS A 1 519 ? -0.614  -6.718  32.452  1.00 120.28 ? 519 LYS A CA    1 
ATOM   4035 C  C     . LYS A 1 519 ? -0.871  -7.732  33.564  1.00 138.80 ? 519 LYS A C     1 
ATOM   4036 O  O     . LYS A 1 519 ? -0.978  -8.939  33.335  1.00 127.63 ? 519 LYS A O     1 
ATOM   4037 C  CB    . LYS A 1 519 ? -1.762  -5.711  32.354  1.00 124.92 ? 519 LYS A CB    1 
ATOM   4038 C  CG    . LYS A 1 519 ? -1.593  -4.678  31.253  1.00 108.17 ? 519 LYS A CG    1 
ATOM   4039 C  CD    . LYS A 1 519 ? -2.795  -3.750  31.181  1.00 111.72 ? 519 LYS A CD    1 
ATOM   4040 C  CE    . LYS A 1 519 ? -2.647  -2.739  30.057  1.00 107.37 ? 519 LYS A CE    1 
ATOM   4041 N  NZ    . LYS A 1 519 ? -3.829  -1.839  29.963  1.00 110.81 ? 519 LYS A NZ    1 
ATOM   4042 N  N     . ASP A 1 520 ? -0.968  -7.228  34.788  1.00 187.78 ? 520 ASP A N     1 
ATOM   4043 C  CA    . ASP A 1 520 ? -1.271  -8.036  35.955  1.00 196.46 ? 520 ASP A CA    1 
ATOM   4044 C  C     . ASP A 1 520 ? -2.750  -7.870  36.314  1.00 199.61 ? 520 ASP A C     1 
ATOM   4045 O  O     . ASP A 1 520 ? -3.556  -7.416  35.494  1.00 194.74 ? 520 ASP A O     1 
ATOM   4046 C  CB    . ASP A 1 520 ? -0.329  -7.646  37.100  1.00 201.08 ? 520 ASP A CB    1 
ATOM   4047 C  CG    . ASP A 1 520 ? -0.351  -6.158  37.391  1.00 199.83 ? 520 ASP A CG    1 
ATOM   4048 O  OD1   . ASP A 1 520 ? -1.117  -5.431  36.724  1.00 195.33 ? 520 ASP A OD1   1 
ATOM   4049 O  OD2   . ASP A 1 520 ? 0.400   -5.714  38.285  1.00 203.29 ? 520 ASP A OD2   1 
ATOM   4050 N  N     . LYS A 1 521 ? -3.117  -8.234  37.541  1.00 175.55 ? 521 LYS A N     1 
ATOM   4051 C  CA    . LYS A 1 521 ? -4.497  -8.114  37.994  1.00 169.66 ? 521 LYS A CA    1 
ATOM   4052 C  C     . LYS A 1 521 ? -4.851  -6.706  38.455  1.00 168.09 ? 521 LYS A C     1 
ATOM   4053 O  O     . LYS A 1 521 ? -5.967  -6.495  38.942  1.00 166.06 ? 521 LYS A O     1 
ATOM   4054 C  CB    . LYS A 1 521 ? -4.766  -9.111  39.124  1.00 159.97 ? 521 LYS A CB    1 
ATOM   4055 C  CG    . LYS A 1 521 ? -4.541  -10.562 38.731  1.00 154.92 ? 521 LYS A CG    1 
ATOM   4056 C  CD    . LYS A 1 521 ? -4.763  -11.498 39.908  1.00 143.71 ? 521 LYS A CD    1 
ATOM   4057 C  CE    . LYS A 1 521 ? -4.509  -12.945 39.516  1.00 139.15 ? 521 LYS A CE    1 
ATOM   4058 N  NZ    . LYS A 1 521 ? -4.686  -13.873 40.667  1.00 132.22 ? 521 LYS A NZ    1 
ATOM   4059 N  N     . ASN A 1 522 ? -3.939  -5.743  38.314  1.00 166.78 ? 522 ASN A N     1 
ATOM   4060 C  CA    . ASN A 1 522 ? -4.186  -4.371  38.729  1.00 162.74 ? 522 ASN A CA    1 
ATOM   4061 C  C     . ASN A 1 522 ? -4.127  -3.365  37.591  1.00 154.32 ? 522 ASN A C     1 
ATOM   4062 O  O     . ASN A 1 522 ? -4.564  -2.223  37.778  1.00 151.56 ? 522 ASN A O     1 
ATOM   4063 C  CB    . ASN A 1 522 ? -3.181  -3.950  39.814  1.00 167.69 ? 522 ASN A CB    1 
ATOM   4064 C  CG    . ASN A 1 522 ? -3.204  -4.869  41.019  1.00 172.01 ? 522 ASN A CG    1 
ATOM   4065 O  OD1   . ASN A 1 522 ? -4.225  -5.484  41.326  1.00 171.81 ? 522 ASN A OD1   1 
ATOM   4066 N  ND2   . ASN A 1 522 ? -2.074  -4.967  41.709  1.00 171.27 ? 522 ASN A ND2   1 
ATOM   4067 N  N     . GLY A 1 523 ? -3.607  -3.743  36.428  1.00 152.89 ? 523 GLY A N     1 
ATOM   4068 C  CA    . GLY A 1 523 ? -3.466  -2.830  35.315  1.00 138.44 ? 523 GLY A CA    1 
ATOM   4069 C  C     . GLY A 1 523 ? -2.068  -2.303  35.084  1.00 140.59 ? 523 GLY A C     1 
ATOM   4070 O  O     . GLY A 1 523 ? -1.906  -1.358  34.303  1.00 126.47 ? 523 GLY A O     1 
ATOM   4071 N  N     . LYS A 1 524 ? -1.060  -2.876  35.732  1.00 164.45 ? 524 LYS A N     1 
ATOM   4072 C  CA    . LYS A 1 524 ? 0.324   -2.445  35.584  1.00 153.67 ? 524 LYS A CA    1 
ATOM   4073 C  C     . LYS A 1 524 ? 1.068   -3.417  34.678  1.00 146.19 ? 524 LYS A C     1 
ATOM   4074 O  O     . LYS A 1 524 ? 0.958   -4.636  34.843  1.00 150.56 ? 524 LYS A O     1 
ATOM   4075 C  CB    . LYS A 1 524 ? 1.015   -2.359  36.946  1.00 160.46 ? 524 LYS A CB    1 
ATOM   4076 C  CG    . LYS A 1 524 ? 2.505   -2.072  36.869  1.00 163.50 ? 524 LYS A CG    1 
ATOM   4077 C  CD    . LYS A 1 524 ? 3.156   -2.175  38.238  1.00 162.54 ? 524 LYS A CD    1 
ATOM   4078 C  CE    . LYS A 1 524 ? 4.661   -1.983  38.150  1.00 163.15 ? 524 LYS A CE    1 
ATOM   4079 N  NZ    . LYS A 1 524 ? 5.321   -2.154  39.474  1.00 157.82 ? 524 LYS A NZ    1 
ATOM   4080 N  N     . PHE A 1 525 ? 1.823   -2.874  33.726  1.00 118.03 ? 525 PHE A N     1 
ATOM   4081 C  CA    . PHE A 1 525 ? 2.594   -3.712  32.818  1.00 106.43 ? 525 PHE A CA    1 
ATOM   4082 C  C     . PHE A 1 525 ? 3.654   -4.491  33.586  1.00 102.73 ? 525 PHE A C     1 
ATOM   4083 O  O     . PHE A 1 525 ? 4.404   -3.924  34.386  1.00 106.60 ? 525 PHE A O     1 
ATOM   4084 C  CB    . PHE A 1 525 ? 3.248   -2.854  31.734  1.00 91.60  ? 525 PHE A CB    1 
ATOM   4085 C  CG    . PHE A 1 525 ? 2.266   -2.193  30.809  1.00 92.03  ? 525 PHE A CG    1 
ATOM   4086 C  CD1   . PHE A 1 525 ? 1.690   -0.978  31.142  1.00 88.33  ? 525 PHE A CD1   1 
ATOM   4087 C  CD2   . PHE A 1 525 ? 1.922   -2.784  29.605  1.00 87.90  ? 525 PHE A CD2   1 
ATOM   4088 C  CE1   . PHE A 1 525 ? 0.787   -0.368  30.293  1.00 88.29  ? 525 PHE A CE1   1 
ATOM   4089 C  CE2   . PHE A 1 525 ? 1.020   -2.178  28.752  1.00 82.67  ? 525 PHE A CE2   1 
ATOM   4090 C  CZ    . PHE A 1 525 ? 0.452   -0.968  29.096  1.00 83.61  ? 525 PHE A CZ    1 
ATOM   4091 N  N     . LEU A 1 526 ? 3.711   -5.800  33.340  1.00 100.51 ? 526 LEU A N     1 
ATOM   4092 C  CA    . LEU A 1 526 ? 4.685   -6.659  34.000  1.00 94.77  ? 526 LEU A CA    1 
ATOM   4093 C  C     . LEU A 1 526 ? 6.075   -6.567  33.385  1.00 86.30  ? 526 LEU A C     1 
ATOM   4094 O  O     . LEU A 1 526 ? 7.018   -7.140  33.943  1.00 88.72  ? 526 LEU A O     1 
ATOM   4095 C  CB    . LEU A 1 526 ? 4.210   -8.114  33.970  1.00 86.30  ? 526 LEU A CB    1 
ATOM   4096 C  CG    . LEU A 1 526 ? 2.944   -8.440  34.766  1.00 100.62 ? 526 LEU A CG    1 
ATOM   4097 C  CD1   . LEU A 1 526 ? 2.534   -9.888  34.554  1.00 104.96 ? 526 LEU A CD1   1 
ATOM   4098 C  CD2   . LEU A 1 526 ? 3.153   -8.152  36.245  1.00 106.70 ? 526 LEU A CD2   1 
ATOM   4099 N  N     . TRP A 1 527 ? 6.228   -5.868  32.262  1.00 81.79  ? 527 TRP A N     1 
ATOM   4100 C  CA    . TRP A 1 527 ? 7.511   -5.747  31.589  1.00 75.39  ? 527 TRP A CA    1 
ATOM   4101 C  C     . TRP A 1 527 ? 7.736   -4.290  31.208  1.00 73.87  ? 527 TRP A C     1 
ATOM   4102 O  O     . TRP A 1 527 ? 6.844   -3.660  30.612  1.00 77.87  ? 527 TRP A O     1 
ATOM   4103 C  CB    . TRP A 1 527 ? 7.564   -6.646  30.346  1.00 66.55  ? 527 TRP A CB    1 
ATOM   4104 C  CG    . TRP A 1 527 ? 8.895   -6.659  29.657  1.00 56.53  ? 527 TRP A CG    1 
ATOM   4105 C  CD1   . TRP A 1 527 ? 9.222   -6.025  28.494  1.00 54.84  ? 527 TRP A CD1   1 
ATOM   4106 C  CD2   . TRP A 1 527 ? 10.079  -7.341  30.089  1.00 58.01  ? 527 TRP A CD2   1 
ATOM   4107 N  NE1   . TRP A 1 527 ? 10.536  -6.270  28.175  1.00 49.55  ? 527 TRP A NE1   1 
ATOM   4108 C  CE2   . TRP A 1 527 ? 11.084  -7.075  29.138  1.00 60.13  ? 527 TRP A CE2   1 
ATOM   4109 C  CE3   . TRP A 1 527 ? 10.387  -8.149  31.188  1.00 64.64  ? 527 TRP A CE3   1 
ATOM   4110 C  CZ2   . TRP A 1 527 ? 12.375  -7.589  29.253  1.00 57.80  ? 527 TRP A CZ2   1 
ATOM   4111 C  CZ3   . TRP A 1 527 ? 11.669  -8.658  31.300  1.00 61.10  ? 527 TRP A CZ3   1 
ATOM   4112 C  CH2   . TRP A 1 527 ? 12.647  -8.376  30.338  1.00 56.03  ? 527 TRP A CH2   1 
ATOM   4113 N  N     . PRO A 1 528 ? 8.899   -3.715  31.527  1.00 77.78  ? 528 PRO A N     1 
ATOM   4114 C  CA    . PRO A 1 528 ? 9.124   -2.299  31.186  1.00 74.63  ? 528 PRO A CA    1 
ATOM   4115 C  C     . PRO A 1 528 ? 9.115   -2.034  29.691  1.00 75.26  ? 528 PRO A C     1 
ATOM   4116 O  O     . PRO A 1 528 ? 8.550   -1.026  29.247  1.00 73.74  ? 528 PRO A O     1 
ATOM   4117 C  CB    . PRO A 1 528 ? 10.493  -2.004  31.815  1.00 75.52  ? 528 PRO A CB    1 
ATOM   4118 C  CG    . PRO A 1 528 ? 11.165  -3.336  31.899  1.00 70.11  ? 528 PRO A CG    1 
ATOM   4119 C  CD    . PRO A 1 528 ? 10.070  -4.323  32.181  1.00 71.85  ? 528 PRO A CD    1 
ATOM   4120 N  N     . GLY A 1 529 ? 9.729   -2.909  28.900  1.00 65.30  ? 529 GLY A N     1 
ATOM   4121 C  CA    . GLY A 1 529 ? 9.730   -2.752  27.463  1.00 57.73  ? 529 GLY A CA    1 
ATOM   4122 C  C     . GLY A 1 529 ? 10.738  -1.724  26.983  1.00 58.55  ? 529 GLY A C     1 
ATOM   4123 O  O     . GLY A 1 529 ? 11.638  -1.286  27.707  1.00 60.77  ? 529 GLY A O     1 
ATOM   4124 N  N     . PHE A 1 530 ? 10.571  -1.335  25.720  1.00 58.93  ? 530 PHE A N     1 
ATOM   4125 C  CA    . PHE A 1 530 ? 11.451  -0.359  25.088  1.00 52.24  ? 530 PHE A CA    1 
ATOM   4126 C  C     . PHE A 1 530 ? 12.896  -0.840  25.101  1.00 50.04  ? 530 PHE A C     1 
ATOM   4127 O  O     . PHE A 1 530 ? 13.238  -1.814  24.422  1.00 38.54  ? 530 PHE A O     1 
ATOM   4128 C  CB    . PHE A 1 530 ? 11.333  1.000   25.784  1.00 48.88  ? 530 PHE A CB    1 
ATOM   4129 C  CG    . PHE A 1 530 ? 9.940   1.562   25.784  1.00 56.38  ? 530 PHE A CG    1 
ATOM   4130 C  CD1   . PHE A 1 530 ? 9.426   2.178   24.654  1.00 53.10  ? 530 PHE A CD1   1 
ATOM   4131 C  CD2   . PHE A 1 530 ? 9.145   1.479   26.915  1.00 56.41  ? 530 PHE A CD2   1 
ATOM   4132 C  CE1   . PHE A 1 530 ? 8.144   2.696   24.652  1.00 47.54  ? 530 PHE A CE1   1 
ATOM   4133 C  CE2   . PHE A 1 530 ? 7.863   1.996   26.919  1.00 47.29  ? 530 PHE A CE2   1 
ATOM   4134 C  CZ    . PHE A 1 530 ? 7.362   2.605   25.787  1.00 45.59  ? 530 PHE A CZ    1 
ATOM   4135 N  N     . GLY A 1 531 ? 13.751  -0.164  25.871  1.00 53.18  ? 531 GLY A N     1 
ATOM   4136 C  CA    . GLY A 1 531 ? 15.151  -0.549  25.914  1.00 43.92  ? 531 GLY A CA    1 
ATOM   4137 C  C     . GLY A 1 531 ? 15.371  -1.916  26.534  1.00 48.95  ? 531 GLY A C     1 
ATOM   4138 O  O     . GLY A 1 531 ? 16.259  -2.662  26.113  1.00 49.05  ? 531 GLY A O     1 
ATOM   4139 N  N     . GLU A 1 532 ? 14.566  -2.265  27.540  1.00 56.05  ? 532 GLU A N     1 
ATOM   4140 C  CA    . GLU A 1 532 ? 14.714  -3.551  28.209  1.00 56.48  ? 532 GLU A CA    1 
ATOM   4141 C  C     . GLU A 1 532 ? 14.350  -4.728  27.315  1.00 57.09  ? 532 GLU A C     1 
ATOM   4142 O  O     . GLU A 1 532 ? 14.695  -5.866  27.653  1.00 55.68  ? 532 GLU A O     1 
ATOM   4143 C  CB    . GLU A 1 532 ? 13.860  -3.581  29.479  1.00 56.97  ? 532 GLU A CB    1 
ATOM   4144 C  CG    . GLU A 1 532 ? 14.241  -2.524  30.502  1.00 63.64  ? 532 GLU A CG    1 
ATOM   4145 C  CD    . GLU A 1 532 ? 15.653  -2.702  31.029  1.00 63.92  ? 532 GLU A CD    1 
ATOM   4146 O  OE1   . GLU A 1 532 ? 16.172  -3.837  30.975  1.00 69.18  ? 532 GLU A OE1   1 
ATOM   4147 O  OE2   . GLU A 1 532 ? 16.244  -1.706  31.495  1.00 63.71  ? 532 GLU A OE2   1 
ATOM   4148 N  N     . ASN A 1 533 ? 13.672  -4.489  26.190  1.00 48.50  ? 533 ASN A N     1 
ATOM   4149 C  CA    . ASN A 1 533 ? 13.342  -5.579  25.280  1.00 50.04  ? 533 ASN A CA    1 
ATOM   4150 C  C     . ASN A 1 533 ? 14.584  -6.278  24.746  1.00 50.48  ? 533 ASN A C     1 
ATOM   4151 O  O     . ASN A 1 533 ? 14.481  -7.402  24.242  1.00 49.34  ? 533 ASN A O     1 
ATOM   4152 C  CB    . ASN A 1 533 ? 12.492  -5.062  24.118  1.00 51.03  ? 533 ASN A CB    1 
ATOM   4153 C  CG    . ASN A 1 533 ? 11.077  -4.715  24.539  1.00 44.91  ? 533 ASN A CG    1 
ATOM   4154 O  OD1   . ASN A 1 533 ? 10.546  -5.282  25.494  1.00 47.69  ? 533 ASN A OD1   1 
ATOM   4155 N  ND2   . ASN A 1 533 ? 10.458  -3.782  23.826  1.00 45.31  ? 533 ASN A ND2   1 
ATOM   4156 N  N     . SER A 1 534 ? 15.754  -5.641  24.844  1.00 50.14  ? 534 SER A N     1 
ATOM   4157 C  CA    . SER A 1 534 ? 16.987  -6.291  24.416  1.00 46.46  ? 534 SER A CA    1 
ATOM   4158 C  C     . SER A 1 534 ? 17.258  -7.556  25.220  1.00 43.87  ? 534 SER A C     1 
ATOM   4159 O  O     . SER A 1 534 ? 17.900  -8.486  24.716  1.00 46.57  ? 534 SER A O     1 
ATOM   4160 C  CB    . SER A 1 534 ? 18.161  -5.319  24.537  1.00 47.70  ? 534 SER A CB    1 
ATOM   4161 O  OG    . SER A 1 534 ? 18.236  -4.772  25.842  1.00 55.80  ? 534 SER A OG    1 
ATOM   4162 N  N     . ARG A 1 535 ? 16.783  -7.611  26.466  1.00 44.37  ? 535 ARG A N     1 
ATOM   4163 C  CA    . ARG A 1 535 ? 16.935  -8.826  27.260  1.00 51.71  ? 535 ARG A CA    1 
ATOM   4164 C  C     . ARG A 1 535 ? 16.231  -10.005 26.600  1.00 54.20  ? 535 ARG A C     1 
ATOM   4165 O  O     . ARG A 1 535 ? 16.714  -11.141 26.663  1.00 53.28  ? 535 ARG A O     1 
ATOM   4166 C  CB    . ARG A 1 535 ? 16.397  -8.600  28.673  1.00 55.72  ? 535 ARG A CB    1 
ATOM   4167 C  CG    . ARG A 1 535 ? 17.050  -7.439  29.405  1.00 56.22  ? 535 ARG A CG    1 
ATOM   4168 C  CD    . ARG A 1 535 ? 16.440  -7.235  30.783  1.00 68.33  ? 535 ARG A CD    1 
ATOM   4169 N  NE    . ARG A 1 535 ? 16.985  -6.058  31.450  1.00 75.33  ? 535 ARG A NE    1 
ATOM   4170 C  CZ    . ARG A 1 535 ? 18.058  -6.067  32.230  1.00 75.48  ? 535 ARG A CZ    1 
ATOM   4171 N  NH1   . ARG A 1 535 ? 18.730  -7.181  32.469  1.00 80.80  ? 535 ARG A NH1   1 
ATOM   4172 N  NH2   . ARG A 1 535 ? 18.466  -4.929  32.785  1.00 74.50  ? 535 ARG A NH2   1 
ATOM   4173 N  N     . VAL A 1 536 ? 15.085  -9.755  25.964  1.00 40.76  ? 536 VAL A N     1 
ATOM   4174 C  CA    . VAL A 1 536 ? 14.396  -10.816 25.238  1.00 44.52  ? 536 VAL A CA    1 
ATOM   4175 C  C     . VAL A 1 536 ? 15.119  -11.128 23.935  1.00 43.06  ? 536 VAL A C     1 
ATOM   4176 O  O     . VAL A 1 536 ? 15.269  -12.296 23.556  1.00 43.94  ? 536 VAL A O     1 
ATOM   4177 C  CB    . VAL A 1 536 ? 12.927  -10.428 24.989  1.00 52.14  ? 536 VAL A CB    1 
ATOM   4178 C  CG1   . VAL A 1 536 ? 12.234  -11.488 24.148  1.00 42.01  ? 536 VAL A CG1   1 
ATOM   4179 C  CG2   . VAL A 1 536 ? 12.201  -10.225 26.309  1.00 48.26  ? 536 VAL A CG2   1 
ATOM   4180 N  N     . LEU A 1 537 ? 15.580  -10.093 23.228  1.00 42.22  ? 537 LEU A N     1 
ATOM   4181 C  CA    . LEU A 1 537 ? 16.273  -10.313 21.964  1.00 44.50  ? 537 LEU A CA    1 
ATOM   4182 C  C     . LEU A 1 537 ? 17.571  -11.084 22.161  1.00 48.65  ? 537 LEU A C     1 
ATOM   4183 O  O     . LEU A 1 537 ? 18.020  -11.784 21.246  1.00 43.37  ? 537 LEU A O     1 
ATOM   4184 C  CB    . LEU A 1 537 ? 16.544  -8.976  21.272  1.00 36.19  ? 537 LEU A CB    1 
ATOM   4185 C  CG    . LEU A 1 537 ? 15.304  -8.180  20.859  1.00 43.36  ? 537 LEU A CG    1 
ATOM   4186 C  CD1   . LEU A 1 537 ? 15.695  -6.943  20.065  1.00 52.36  ? 537 LEU A CD1   1 
ATOM   4187 C  CD2   . LEU A 1 537 ? 14.349  -9.053  20.061  1.00 35.97  ? 537 LEU A CD2   1 
ATOM   4188 N  N     . GLU A 1 538 ? 18.189  -10.969 23.339  1.00 46.08  ? 538 GLU A N     1 
ATOM   4189 C  CA    . GLU A 1 538 ? 19.391  -11.751 23.615  1.00 40.67  ? 538 GLU A CA    1 
ATOM   4190 C  C     . GLU A 1 538 ? 19.090  -13.244 23.596  1.00 39.23  ? 538 GLU A C     1 
ATOM   4191 O  O     . GLU A 1 538 ? 19.864  -14.035 23.044  1.00 39.25  ? 538 GLU A O     1 
ATOM   4192 C  CB    . GLU A 1 538 ? 19.987  -11.340 24.962  1.00 53.34  ? 538 GLU A CB    1 
ATOM   4193 C  CG    . GLU A 1 538 ? 21.240  -12.109 25.346  1.00 55.99  ? 538 GLU A CG    1 
ATOM   4194 C  CD    . GLU A 1 538 ? 21.762  -11.721 26.714  1.00 62.74  ? 538 GLU A CD    1 
ATOM   4195 O  OE1   . GLU A 1 538 ? 21.093  -10.920 27.401  1.00 66.56  ? 538 GLU A OE1   1 
ATOM   4196 O  OE2   . GLU A 1 538 ? 22.841  -12.215 27.104  1.00 55.75  ? 538 GLU A OE2   1 
ATOM   4197 N  N     . TRP A 1 539 ? 17.967  -13.649 24.192  1.00 42.49  ? 539 TRP A N     1 
ATOM   4198 C  CA    . TRP A 1 539 ? 17.597  -15.061 24.189  1.00 42.56  ? 539 TRP A CA    1 
ATOM   4199 C  C     . TRP A 1 539 ? 17.342  -15.561 22.772  1.00 41.19  ? 539 TRP A C     1 
ATOM   4200 O  O     . TRP A 1 539 ? 17.659  -16.710 22.444  1.00 38.44  ? 539 TRP A O     1 
ATOM   4201 C  CB    . TRP A 1 539 ? 16.368  -15.282 25.070  1.00 44.26  ? 539 TRP A CB    1 
ATOM   4202 C  CG    . TRP A 1 539 ? 15.939  -16.714 25.155  1.00 52.89  ? 539 TRP A CG    1 
ATOM   4203 C  CD1   . TRP A 1 539 ? 16.552  -17.712 25.854  1.00 51.56  ? 539 TRP A CD1   1 
ATOM   4204 C  CD2   . TRP A 1 539 ? 14.796  -17.308 24.526  1.00 54.84  ? 539 TRP A CD2   1 
ATOM   4205 N  NE1   . TRP A 1 539 ? 15.866  -18.891 25.695  1.00 60.23  ? 539 TRP A NE1   1 
ATOM   4206 C  CE2   . TRP A 1 539 ? 14.783  -18.670 24.885  1.00 59.32  ? 539 TRP A CE2   1 
ATOM   4207 C  CE3   . TRP A 1 539 ? 13.783  -16.820 23.693  1.00 45.11  ? 539 TRP A CE3   1 
ATOM   4208 C  CZ2   . TRP A 1 539 ? 13.798  -19.551 24.441  1.00 62.17  ? 539 TRP A CZ2   1 
ATOM   4209 C  CZ3   . TRP A 1 539 ? 12.807  -17.696 23.253  1.00 48.77  ? 539 TRP A CZ3   1 
ATOM   4210 C  CH2   . TRP A 1 539 ? 12.821  -19.046 23.628  1.00 56.61  ? 539 TRP A CH2   1 
ATOM   4211 N  N     . MET A 1 540 ? 16.766  -14.712 21.916  1.00 38.06  ? 540 MET A N     1 
ATOM   4212 C  CA    . MET A 1 540 ? 16.543  -15.105 20.529  1.00 41.55  ? 540 MET A CA    1 
ATOM   4213 C  C     . MET A 1 540 ? 17.857  -15.271 19.777  1.00 40.47  ? 540 MET A C     1 
ATOM   4214 O  O     . MET A 1 540 ? 17.967  -16.142 18.907  1.00 35.72  ? 540 MET A O     1 
ATOM   4215 C  CB    . MET A 1 540 ? 15.658  -14.077 19.823  1.00 34.37  ? 540 MET A CB    1 
ATOM   4216 C  CG    . MET A 1 540 ? 14.305  -13.854 20.481  1.00 34.01  ? 540 MET A CG    1 
ATOM   4217 S  SD    . MET A 1 540 ? 13.264  -12.724 19.532  1.00 36.11  ? 540 MET A SD    1 
ATOM   4218 C  CE    . MET A 1 540 ? 11.829  -12.607 20.597  1.00 42.37  ? 540 MET A CE    1 
ATOM   4219 N  N     . PHE A 1 541 ? 18.860  -14.450 20.098  1.00 42.76  ? 541 PHE A N     1 
ATOM   4220 C  CA    . PHE A 1 541 ? 20.146  -14.553 19.417  1.00 41.52  ? 541 PHE A CA    1 
ATOM   4221 C  C     . PHE A 1 541 ? 20.836  -15.873 19.739  1.00 41.32  ? 541 PHE A C     1 
ATOM   4222 O  O     . PHE A 1 541 ? 21.397  -16.521 18.847  1.00 43.43  ? 541 PHE A O     1 
ATOM   4223 C  CB    . PHE A 1 541 ? 21.036  -13.371 19.804  1.00 50.51  ? 541 PHE A CB    1 
ATOM   4224 C  CG    . PHE A 1 541 ? 22.188  -13.143 18.866  1.00 56.86  ? 541 PHE A CG    1 
ATOM   4225 C  CD1   . PHE A 1 541 ? 23.327  -13.928 18.939  1.00 57.70  ? 541 PHE A CD1   1 
ATOM   4226 C  CD2   . PHE A 1 541 ? 22.134  -12.135 17.918  1.00 46.48  ? 541 PHE A CD2   1 
ATOM   4227 C  CE1   . PHE A 1 541 ? 24.387  -13.717 18.078  1.00 62.26  ? 541 PHE A CE1   1 
ATOM   4228 C  CE2   . PHE A 1 541 ? 23.191  -11.919 17.055  1.00 49.45  ? 541 PHE A CE2   1 
ATOM   4229 C  CZ    . PHE A 1 541 ? 24.319  -12.710 17.135  1.00 67.87  ? 541 PHE A CZ    1 
ATOM   4230 N  N     . GLY A 1 542 ? 20.803  -16.289 21.007  1.00 42.99  ? 542 GLY A N     1 
ATOM   4231 C  CA    . GLY A 1 542 ? 21.444  -17.539 21.380  1.00 56.55  ? 542 GLY A CA    1 
ATOM   4232 C  C     . GLY A 1 542 ? 20.761  -18.752 20.778  1.00 51.44  ? 542 GLY A C     1 
ATOM   4233 O  O     . GLY A 1 542 ? 21.423  -19.712 20.375  1.00 49.65  ? 542 GLY A O     1 
ATOM   4234 N  N     . ARG A 1 543 ? 19.427  -18.729 20.713  1.00 48.77  ? 543 ARG A N     1 
ATOM   4235 C  CA    . ARG A 1 543 ? 18.701  -19.837 20.103  1.00 48.14  ? 543 ARG A CA    1 
ATOM   4236 C  C     . ARG A 1 543 ? 19.083  -20.020 18.640  1.00 49.42  ? 543 ARG A C     1 
ATOM   4237 O  O     . ARG A 1 543 ? 19.133  -21.153 18.149  1.00 42.92  ? 543 ARG A O     1 
ATOM   4238 C  CB    . ARG A 1 543 ? 17.194  -19.613 20.236  1.00 47.53  ? 543 ARG A CB    1 
ATOM   4239 C  CG    . ARG A 1 543 ? 16.668  -19.762 21.654  1.00 48.49  ? 543 ARG A CG    1 
ATOM   4240 C  CD    . ARG A 1 543 ? 16.806  -21.196 22.132  1.00 58.63  ? 543 ARG A CD    1 
ATOM   4241 N  NE    . ARG A 1 543 ? 16.069  -22.119 21.278  1.00 58.59  ? 543 ARG A NE    1 
ATOM   4242 C  CZ    . ARG A 1 543 ? 16.135  -23.440 21.370  1.00 58.50  ? 543 ARG A CZ    1 
ATOM   4243 N  NH1   . ARG A 1 543 ? 16.904  -24.033 22.268  1.00 74.60  ? 543 ARG A NH1   1 
ATOM   4244 N  NH2   . ARG A 1 543 ? 15.412  -24.185 20.538  1.00 59.54  ? 543 ARG A NH2   1 
ATOM   4245 N  N     . ILE A 1 544 ? 19.356  -18.923 17.931  1.00 55.76  ? 544 ILE A N     1 
ATOM   4246 C  CA    . ILE A 1 544 ? 19.743  -19.027 16.528  1.00 58.60  ? 544 ILE A CA    1 
ATOM   4247 C  C     . ILE A 1 544 ? 21.093  -19.721 16.396  1.00 58.00  ? 544 ILE A C     1 
ATOM   4248 O  O     . ILE A 1 544 ? 21.290  -20.560 15.509  1.00 52.86  ? 544 ILE A O     1 
ATOM   4249 C  CB    . ILE A 1 544 ? 19.751  -17.635 15.871  1.00 60.61  ? 544 ILE A CB    1 
ATOM   4250 C  CG1   . ILE A 1 544 ? 18.329  -17.071 15.809  1.00 54.83  ? 544 ILE A CG1   1 
ATOM   4251 C  CG2   . ILE A 1 544 ? 20.368  -17.704 14.484  1.00 65.38  ? 544 ILE A CG2   1 
ATOM   4252 C  CD1   . ILE A 1 544 ? 18.238  -15.717 15.143  1.00 55.09  ? 544 ILE A CD1   1 
ATOM   4253 N  N     . GLU A 1 545 ? 22.044  -19.385 17.271  1.00 59.13  ? 545 GLU A N     1 
ATOM   4254 C  CA    . GLU A 1 545 ? 23.336  -20.058 17.255  1.00 50.73  ? 545 GLU A CA    1 
ATOM   4255 C  C     . GLU A 1 545 ? 23.231  -21.517 17.677  1.00 57.54  ? 545 GLU A C     1 
ATOM   4256 O  O     . GLU A 1 545 ? 24.154  -22.295 17.410  1.00 65.01  ? 545 GLU A O     1 
ATOM   4257 C  CB    . GLU A 1 545 ? 24.328  -19.323 18.157  1.00 60.03  ? 545 GLU A CB    1 
ATOM   4258 C  CG    . GLU A 1 545 ? 24.752  -17.959 17.636  1.00 52.32  ? 545 GLU A CG    1 
ATOM   4259 C  CD    . GLU A 1 545 ? 25.759  -17.277 18.541  1.00 67.95  ? 545 GLU A CD    1 
ATOM   4260 O  OE1   . GLU A 1 545 ? 25.808  -17.619 19.741  1.00 73.25  ? 545 GLU A OE1   1 
ATOM   4261 O  OE2   . GLU A 1 545 ? 26.506  -16.404 18.051  1.00 63.68  ? 545 GLU A OE2   1 
ATOM   4262 N  N     . GLY A 1 546 ? 22.137  -21.904 18.329  1.00 65.08  ? 546 GLY A N     1 
ATOM   4263 C  CA    . GLY A 1 546 ? 21.931  -23.288 18.708  1.00 50.74  ? 546 GLY A CA    1 
ATOM   4264 C  C     . GLY A 1 546 ? 22.236  -23.584 20.161  1.00 60.70  ? 546 GLY A C     1 
ATOM   4265 O  O     . GLY A 1 546 ? 22.740  -24.663 20.486  1.00 67.21  ? 546 GLY A O     1 
ATOM   4266 N  N     . GLU A 1 547 ? 21.937  -22.638 21.047  1.00 62.63  ? 547 GLU A N     1 
ATOM   4267 C  CA    . GLU A 1 547 ? 22.150  -22.860 22.467  1.00 67.13  ? 547 GLU A CA    1 
ATOM   4268 C  C     . GLU A 1 547 ? 20.984  -23.640 23.068  1.00 73.83  ? 547 GLU A C     1 
ATOM   4269 O  O     . GLU A 1 547 ? 19.867  -23.648 22.543  1.00 67.73  ? 547 GLU A O     1 
ATOM   4270 C  CB    . GLU A 1 547 ? 22.335  -21.532 23.203  1.00 65.69  ? 547 GLU A CB    1 
ATOM   4271 C  CG    . GLU A 1 547 ? 23.617  -20.799 22.838  1.00 79.90  ? 547 GLU A CG    1 
ATOM   4272 C  CD    . GLU A 1 547 ? 23.883  -19.602 23.730  1.00 85.76  ? 547 GLU A CD    1 
ATOM   4273 O  OE1   . GLU A 1 547 ? 23.023  -19.288 24.580  1.00 86.32  ? 547 GLU A OE1   1 
ATOM   4274 O  OE2   . GLU A 1 547 ? 24.955  -18.978 23.584  1.00 92.53  ? 547 GLU A OE2   1 
ATOM   4275 N  N     . ASP A 1 548 ? 21.261  -24.307 24.189  1.00 81.42  ? 548 ASP A N     1 
ATOM   4276 C  CA    . ASP A 1 548 ? 20.277  -25.154 24.861  1.00 86.60  ? 548 ASP A CA    1 
ATOM   4277 C  C     . ASP A 1 548 ? 19.746  -24.405 26.081  1.00 87.89  ? 548 ASP A C     1 
ATOM   4278 O  O     . ASP A 1 548 ? 20.110  -24.677 27.225  1.00 86.86  ? 548 ASP A O     1 
ATOM   4279 C  CB    . ASP A 1 548 ? 20.895  -26.496 25.240  1.00 87.74  ? 548 ASP A CB    1 
ATOM   4280 C  CG    . ASP A 1 548 ? 19.882  -27.462 25.818  1.00 96.09  ? 548 ASP A CG    1 
ATOM   4281 O  OD1   . ASP A 1 548 ? 18.669  -27.176 25.733  1.00 98.10  ? 548 ASP A OD1   1 
ATOM   4282 O  OD2   . ASP A 1 548 ? 20.298  -28.508 26.361  1.00 105.20 ? 548 ASP A OD2   1 
ATOM   4283 N  N     . SER A 1 549 ? 18.858  -23.443 25.818  1.00 79.02  ? 549 SER A N     1 
ATOM   4284 C  CA    . SER A 1 549 ? 18.260  -22.634 26.872  1.00 74.85  ? 549 SER A CA    1 
ATOM   4285 C  C     . SER A 1 549 ? 16.739  -22.592 26.788  1.00 66.82  ? 549 SER A C     1 
ATOM   4286 O  O     . SER A 1 549 ? 16.115  -21.782 27.485  1.00 65.04  ? 549 SER A O     1 
ATOM   4287 C  CB    . SER A 1 549 ? 18.820  -21.206 26.836  1.00 67.84  ? 549 SER A CB    1 
ATOM   4288 O  OG    . SER A 1 549 ? 18.551  -20.585 25.591  1.00 72.92  ? 549 SER A OG    1 
ATOM   4289 N  N     . ALA A 1 550 ? 16.128  -23.436 25.965  1.00 69.50  ? 550 ALA A N     1 
ATOM   4290 C  CA    . ALA A 1 550 ? 14.685  -23.452 25.786  1.00 63.39  ? 550 ALA A CA    1 
ATOM   4291 C  C     . ALA A 1 550 ? 14.054  -24.582 26.591  1.00 63.96  ? 550 ALA A C     1 
ATOM   4292 O  O     . ALA A 1 550 ? 14.716  -25.545 26.987  1.00 67.52  ? 550 ALA A O     1 
ATOM   4293 C  CB    . ALA A 1 550 ? 14.325  -23.598 24.306  1.00 51.29  ? 550 ALA A CB    1 
ATOM   4294 N  N     . LYS A 1 551 ? 12.751  -24.448 26.830  1.00 61.57  ? 551 LYS A N     1 
ATOM   4295 C  CA    . LYS A 1 551 ? 11.976  -25.436 27.565  1.00 53.72  ? 551 LYS A CA    1 
ATOM   4296 C  C     . LYS A 1 551 ? 10.674  -25.700 26.823  1.00 58.06  ? 551 LYS A C     1 
ATOM   4297 O  O     . LYS A 1 551 ? 10.098  -24.790 26.219  1.00 52.40  ? 551 LYS A O     1 
ATOM   4298 C  CB    . LYS A 1 551 ? 11.694  -24.964 28.998  1.00 51.23  ? 551 LYS A CB    1 
ATOM   4299 C  CG    . LYS A 1 551 ? 11.177  -26.050 29.924  1.00 63.91  ? 551 LYS A CG    1 
ATOM   4300 C  CD    . LYS A 1 551 ? 11.152  -25.575 31.368  1.00 64.35  ? 551 LYS A CD    1 
ATOM   4301 C  CE    . LYS A 1 551 ? 10.272  -24.347 31.531  1.00 54.50  ? 551 LYS A CE    1 
ATOM   4302 N  NZ    . LYS A 1 551 ? 10.255  -23.860 32.938  1.00 80.54  ? 551 LYS A NZ    1 
ATOM   4303 N  N     . LEU A 1 552 ? 10.215  -26.949 26.868  1.00 55.89  ? 552 LEU A N     1 
ATOM   4304 C  CA    . LEU A 1 552 ? 9.065   -27.381 26.084  1.00 53.71  ? 552 LEU A CA    1 
ATOM   4305 C  C     . LEU A 1 552 ? 7.776   -27.190 26.874  1.00 52.78  ? 552 LEU A C     1 
ATOM   4306 O  O     . LEU A 1 552 ? 7.666   -27.641 28.018  1.00 46.13  ? 552 LEU A O     1 
ATOM   4307 C  CB    . LEU A 1 552 ? 9.222   -28.845 25.672  1.00 52.95  ? 552 LEU A CB    1 
ATOM   4308 C  CG    . LEU A 1 552 ? 8.103   -29.448 24.820  1.00 52.10  ? 552 LEU A CG    1 
ATOM   4309 C  CD1   . LEU A 1 552 ? 7.885   -28.627 23.559  1.00 57.25  ? 552 LEU A CD1   1 
ATOM   4310 C  CD2   . LEU A 1 552 ? 8.421   -30.894 24.473  1.00 58.28  ? 552 LEU A CD2   1 
ATOM   4311 N  N     . THR A 1 553 ? 6.808   -26.526 26.258  1.00 53.30  ? 553 THR A N     1 
ATOM   4312 C  CA    . THR A 1 553 ? 5.494   -26.279 26.830  1.00 46.51  ? 553 THR A CA    1 
ATOM   4313 C  C     . THR A 1 553 ? 4.425   -26.643 25.817  1.00 49.30  ? 553 THR A C     1 
ATOM   4314 O  O     . THR A 1 553 ? 4.713   -26.833 24.630  1.00 48.77  ? 553 THR A O     1 
ATOM   4315 C  CB    . THR A 1 553 ? 5.341   -24.808 27.252  1.00 56.67  ? 553 THR A CB    1 
ATOM   4316 O  OG1   . THR A 1 553 ? 5.478   -23.961 26.103  1.00 54.67  ? 553 THR A OG1   1 
ATOM   4317 C  CG2   . THR A 1 553 ? 6.397   -24.436 28.280  1.00 54.33  ? 553 THR A CG2   1 
ATOM   4318 N  N     . PRO A 1 554 ? 3.168   -26.752 26.253  1.00 54.73  ? 554 PRO A N     1 
ATOM   4319 C  CA    . PRO A 1 554 ? 2.096   -27.118 25.314  1.00 49.70  ? 554 PRO A CA    1 
ATOM   4320 C  C     . PRO A 1 554 ? 1.873   -26.099 24.209  1.00 53.56  ? 554 PRO A C     1 
ATOM   4321 O  O     . PRO A 1 554 ? 1.231   -26.431 23.205  1.00 47.77  ? 554 PRO A O     1 
ATOM   4322 C  CB    . PRO A 1 554 ? 0.861   -27.239 26.219  1.00 46.52  ? 554 PRO A CB    1 
ATOM   4323 C  CG    . PRO A 1 554 ? 1.412   -27.458 27.594  1.00 51.62  ? 554 PRO A CG    1 
ATOM   4324 C  CD    . PRO A 1 554 ? 2.686   -26.671 27.641  1.00 55.18  ? 554 PRO A CD    1 
ATOM   4325 N  N     . ILE A 1 555 ? 2.374   -24.874 24.357  1.00 48.91  ? 555 ILE A N     1 
ATOM   4326 C  CA    . ILE A 1 555 ? 2.183   -23.842 23.347  1.00 50.31  ? 555 ILE A CA    1 
ATOM   4327 C  C     . ILE A 1 555 ? 3.446   -23.562 22.539  1.00 54.25  ? 555 ILE A C     1 
ATOM   4328 O  O     . ILE A 1 555 ? 3.345   -22.965 21.456  1.00 49.36  ? 555 ILE A O     1 
ATOM   4329 C  CB    . ILE A 1 555 ? 1.657   -22.535 23.975  1.00 50.10  ? 555 ILE A CB    1 
ATOM   4330 C  CG1   . ILE A 1 555 ? 2.712   -21.923 24.900  1.00 49.70  ? 555 ILE A CG1   1 
ATOM   4331 C  CG2   . ILE A 1 555 ? 0.364   -22.793 24.731  1.00 50.82  ? 555 ILE A CG2   1 
ATOM   4332 C  CD1   . ILE A 1 555 ? 2.299   -20.599 25.501  1.00 52.00  ? 555 ILE A CD1   1 
ATOM   4333 N  N     . GLY A 1 556 ? 4.616   -23.964 23.018  1.00 62.00  ? 556 GLY A N     1 
ATOM   4334 C  CA    . GLY A 1 556 ? 5.849   -23.718 22.293  1.00 59.29  ? 556 GLY A CA    1 
ATOM   4335 C  C     . GLY A 1 556 ? 7.040   -23.806 23.231  1.00 54.84  ? 556 GLY A C     1 
ATOM   4336 O  O     . GLY A 1 556 ? 6.943   -24.350 24.329  1.00 60.11  ? 556 GLY A O     1 
ATOM   4337 N  N     . TYR A 1 557 ? 8.160   -23.258 22.766  1.00 55.13  ? 557 TYR A N     1 
ATOM   4338 C  CA    . TYR A 1 557 ? 9.396   -23.249 23.537  1.00 50.92  ? 557 TYR A CA    1 
ATOM   4339 C  C     . TYR A 1 557 ? 9.511   -21.934 24.297  1.00 50.54  ? 557 TYR A C     1 
ATOM   4340 O  O     . TYR A 1 557 ? 9.474   -20.857 23.693  1.00 51.58  ? 557 TYR A O     1 
ATOM   4341 C  CB    . TYR A 1 557 ? 10.609  -23.452 22.629  1.00 48.77  ? 557 TYR A CB    1 
ATOM   4342 C  CG    . TYR A 1 557 ? 10.801  -24.876 22.163  1.00 49.13  ? 557 TYR A CG    1 
ATOM   4343 C  CD1   . TYR A 1 557 ? 11.011  -25.902 23.075  1.00 53.52  ? 557 TYR A CD1   1 
ATOM   4344 C  CD2   . TYR A 1 557 ? 10.790  -25.194 20.812  1.00 48.18  ? 557 TYR A CD2   1 
ATOM   4345 C  CE1   . TYR A 1 557 ? 11.191  -27.206 22.656  1.00 50.36  ? 557 TYR A CE1   1 
ATOM   4346 C  CE2   . TYR A 1 557 ? 10.971  -26.495 20.382  1.00 58.64  ? 557 TYR A CE2   1 
ATOM   4347 C  CZ    . TYR A 1 557 ? 11.172  -27.497 21.309  1.00 42.61  ? 557 TYR A CZ    1 
ATOM   4348 O  OH    . TYR A 1 557 ? 11.353  -28.793 20.887  1.00 47.32  ? 557 TYR A OH    1 
ATOM   4349 N  N     . VAL A 1 558 ? 9.649   -22.026 25.616  1.00 51.78  ? 558 VAL A N     1 
ATOM   4350 C  CA    . VAL A 1 558 ? 9.833   -20.852 26.465  1.00 53.81  ? 558 VAL A CA    1 
ATOM   4351 C  C     . VAL A 1 558 ? 11.219  -20.923 27.096  1.00 54.59  ? 558 VAL A C     1 
ATOM   4352 O  O     . VAL A 1 558 ? 11.765  -22.023 27.265  1.00 50.83  ? 558 VAL A O     1 
ATOM   4353 C  CB    . VAL A 1 558 ? 8.737   -20.759 27.538  1.00 53.24  ? 558 VAL A CB    1 
ATOM   4354 C  CG1   . VAL A 1 558 ? 7.364   -20.676 26.887  1.00 50.10  ? 558 VAL A CG1   1 
ATOM   4355 C  CG2   . VAL A 1 558 ? 8.818   -21.950 28.481  1.00 54.03  ? 558 VAL A CG2   1 
ATOM   4356 N  N     . PRO A 1 559 ? 11.825  -19.792 27.451  1.00 57.77  ? 559 PRO A N     1 
ATOM   4357 C  CA    . PRO A 1 559 ? 13.154  -19.837 28.070  1.00 62.91  ? 559 PRO A CA    1 
ATOM   4358 C  C     . PRO A 1 559 ? 13.115  -20.564 29.406  1.00 61.58  ? 559 PRO A C     1 
ATOM   4359 O  O     . PRO A 1 559 ? 12.207  -20.368 30.216  1.00 59.91  ? 559 PRO A O     1 
ATOM   4360 C  CB    . PRO A 1 559 ? 13.516  -18.357 28.245  1.00 50.66  ? 559 PRO A CB    1 
ATOM   4361 C  CG    . PRO A 1 559 ? 12.639  -17.627 27.274  1.00 66.65  ? 559 PRO A CG    1 
ATOM   4362 C  CD    . PRO A 1 559 ? 11.365  -18.412 27.225  1.00 52.70  ? 559 PRO A CD    1 
ATOM   4363 N  N     . LYS A 1 560 ? 14.115  -21.413 29.630  1.00 68.40  ? 560 LYS A N     1 
ATOM   4364 C  CA    . LYS A 1 560 ? 14.217  -22.116 30.897  1.00 76.31  ? 560 LYS A CA    1 
ATOM   4365 C  C     . LYS A 1 560 ? 14.517  -21.131 32.026  1.00 86.62  ? 560 LYS A C     1 
ATOM   4366 O  O     . LYS A 1 560 ? 14.739  -19.936 31.809  1.00 86.34  ? 560 LYS A O     1 
ATOM   4367 C  CB    . LYS A 1 560 ? 15.297  -23.196 30.831  1.00 74.58  ? 560 LYS A CB    1 
ATOM   4368 C  CG    . LYS A 1 560 ? 15.001  -24.313 29.845  1.00 73.03  ? 560 LYS A CG    1 
ATOM   4369 C  CD    . LYS A 1 560 ? 15.980  -25.468 29.999  1.00 77.75  ? 560 LYS A CD    1 
ATOM   4370 C  CE    . LYS A 1 560 ? 17.408  -25.039 29.699  1.00 73.78  ? 560 LYS A CE    1 
ATOM   4371 N  NZ    . LYS A 1 560 ? 18.360  -26.181 29.805  1.00 76.92  ? 560 LYS A NZ    1 
ATOM   4372 N  N     . GLU A 1 561 ? 14.518  -21.651 33.250  1.00 107.23 ? 561 GLU A N     1 
ATOM   4373 C  CA    . GLU A 1 561 ? 14.813  -20.824 34.410  1.00 112.49 ? 561 GLU A CA    1 
ATOM   4374 C  C     . GLU A 1 561 ? 16.272  -20.387 34.392  1.00 109.58 ? 561 GLU A C     1 
ATOM   4375 O  O     . GLU A 1 561 ? 17.166  -21.158 34.032  1.00 111.49 ? 561 GLU A O     1 
ATOM   4376 C  CB    . GLU A 1 561 ? 14.503  -21.588 35.697  1.00 123.36 ? 561 GLU A CB    1 
ATOM   4377 C  CG    . GLU A 1 561 ? 13.065  -22.070 35.797  1.00 136.29 ? 561 GLU A CG    1 
ATOM   4378 C  CD    . GLU A 1 561 ? 12.792  -22.835 37.077  1.00 160.57 ? 561 GLU A CD    1 
ATOM   4379 O  OE1   . GLU A 1 561 ? 13.654  -22.810 37.980  1.00 167.68 ? 561 GLU A OE1   1 
ATOM   4380 O  OE2   . GLU A 1 561 ? 11.717  -23.462 37.179  1.00 165.43 ? 561 GLU A OE2   1 
ATOM   4381 N  N     . ASP A 1 562 ? 16.511  -19.135 34.784  1.00 100.97 ? 562 ASP A N     1 
ATOM   4382 C  CA    . ASP A 1 562 ? 17.853  -18.557 34.778  1.00 100.80 ? 562 ASP A CA    1 
ATOM   4383 C  C     . ASP A 1 562 ? 18.422  -18.478 33.364  1.00 92.53  ? 562 ASP A C     1 
ATOM   4384 O  O     . ASP A 1 562 ? 19.634  -18.583 33.162  1.00 87.87  ? 562 ASP A O     1 
ATOM   4385 C  CB    . ASP A 1 562 ? 18.800  -19.341 35.691  1.00 108.51 ? 562 ASP A CB    1 
ATOM   4386 C  CG    . ASP A 1 562 ? 18.382  -19.289 37.146  1.00 116.53 ? 562 ASP A CG    1 
ATOM   4387 O  OD1   . ASP A 1 562 ? 17.760  -18.284 37.551  1.00 121.68 ? 562 ASP A OD1   1 
ATOM   4388 O  OD2   . ASP A 1 562 ? 18.675  -20.252 37.885  1.00 121.24 ? 562 ASP A OD2   1 
ATOM   4389 N  N     . ALA A 1 563 ? 17.548  -18.297 32.375  1.00 88.56  ? 563 ALA A N     1 
ATOM   4390 C  CA    . ALA A 1 563 ? 17.966  -18.190 30.983  1.00 78.24  ? 563 ALA A CA    1 
ATOM   4391 C  C     . ALA A 1 563 ? 17.927  -16.766 30.451  1.00 65.83  ? 563 ALA A C     1 
ATOM   4392 O  O     . ALA A 1 563 ? 18.721  -16.427 29.568  1.00 45.36  ? 563 ALA A O     1 
ATOM   4393 C  CB    . ALA A 1 563 ? 17.088  -19.080 30.096  1.00 74.66  ? 563 ALA A CB    1 
ATOM   4394 N  N     . LEU A 1 564 ? 17.027  -15.929 30.961  1.00 67.45  ? 564 LEU A N     1 
ATOM   4395 C  CA    . LEU A 1 564 ? 16.942  -14.537 30.547  1.00 67.72  ? 564 LEU A CA    1 
ATOM   4396 C  C     . LEU A 1 564 ? 17.828  -13.669 31.429  1.00 72.25  ? 564 LEU A C     1 
ATOM   4397 O  O     . LEU A 1 564 ? 17.839  -13.813 32.655  1.00 72.19  ? 564 LEU A O     1 
ATOM   4398 C  CB    . LEU A 1 564 ? 15.497  -14.037 30.607  1.00 66.95  ? 564 LEU A CB    1 
ATOM   4399 C  CG    . LEU A 1 564 ? 14.571  -14.458 29.465  1.00 58.06  ? 564 LEU A CG    1 
ATOM   4400 C  CD1   . LEU A 1 564 ? 13.184  -13.863 29.655  1.00 62.58  ? 564 LEU A CD1   1 
ATOM   4401 C  CD2   . LEU A 1 564 ? 15.156  -14.043 28.124  1.00 52.69  ? 564 LEU A CD2   1 
ATOM   4402 N  N     . ASN A 1 565 ? 18.574  -12.766 30.794  1.00 80.97  ? 565 ASN A N     1 
ATOM   4403 C  CA    . ASN A 1 565 ? 19.427  -11.838 31.526  1.00 64.23  ? 565 ASN A CA    1 
ATOM   4404 C  C     . ASN A 1 565 ? 18.573  -10.822 32.272  1.00 73.60  ? 565 ASN A C     1 
ATOM   4405 O  O     . ASN A 1 565 ? 18.261  -9.753  31.738  1.00 78.01  ? 565 ASN A O     1 
ATOM   4406 C  CB    . ASN A 1 565 ? 20.396  -11.133 30.574  1.00 73.05  ? 565 ASN A CB    1 
ATOM   4407 C  CG    . ASN A 1 565 ? 21.492  -10.382 31.306  1.00 70.75  ? 565 ASN A CG    1 
ATOM   4408 O  OD1   . ASN A 1 565 ? 21.361  -10.064 32.488  1.00 73.00  ? 565 ASN A OD1   1 
ATOM   4409 N  ND2   . ASN A 1 565 ? 22.580  -10.092 30.603  1.00 63.69  ? 565 ASN A ND2   1 
ATOM   4410 N  N     . LEU A 1 566 ? 18.185  -11.150 33.503  1.00 82.74  ? 566 LEU A N     1 
ATOM   4411 C  CA    . LEU A 1 566 ? 17.362  -10.275 34.326  1.00 87.41  ? 566 LEU A CA    1 
ATOM   4412 C  C     . LEU A 1 566 ? 18.176  -9.505  35.357  1.00 94.63  ? 566 LEU A C     1 
ATOM   4413 O  O     . LEU A 1 566 ? 17.597  -8.918  36.277  1.00 97.74  ? 566 LEU A O     1 
ATOM   4414 C  CB    . LEU A 1 566 ? 16.267  -11.087 35.020  1.00 82.39  ? 566 LEU A CB    1 
ATOM   4415 C  CG    . LEU A 1 566 ? 15.306  -11.838 34.095  1.00 78.79  ? 566 LEU A CG    1 
ATOM   4416 C  CD1   . LEU A 1 566 ? 14.307  -12.650 34.904  1.00 79.85  ? 566 LEU A CD1   1 
ATOM   4417 C  CD2   . LEU A 1 566 ? 14.591  -10.870 33.165  1.00 73.88  ? 566 LEU A CD2   1 
ATOM   4418 N  N     . LYS A 1 567 ? 19.501  -9.495  35.227  1.00 105.81 ? 567 LYS A N     1 
ATOM   4419 C  CA    . LYS A 1 567 ? 20.336  -8.762  36.167  1.00 115.57 ? 567 LYS A CA    1 
ATOM   4420 C  C     . LYS A 1 567 ? 20.039  -7.271  36.086  1.00 113.92 ? 567 LYS A C     1 
ATOM   4421 O  O     . LYS A 1 567 ? 19.802  -6.723  35.006  1.00 114.60 ? 567 LYS A O     1 
ATOM   4422 C  CB    . LYS A 1 567 ? 21.813  -9.032  35.880  1.00 122.21 ? 567 LYS A CB    1 
ATOM   4423 C  CG    . LYS A 1 567 ? 22.177  -10.509 35.914  1.00 123.46 ? 567 LYS A CG    1 
ATOM   4424 C  CD    . LYS A 1 567 ? 23.613  -10.745 35.483  1.00 126.13 ? 567 LYS A CD    1 
ATOM   4425 C  CE    . LYS A 1 567 ? 23.938  -12.230 35.460  1.00 131.96 ? 567 LYS A CE    1 
ATOM   4426 N  NZ    . LYS A 1 567 ? 25.330  -12.490 35.002  1.00 144.83 ? 567 LYS A NZ    1 
ATOM   4427 N  N     . GLY A 1 568 ? 20.053  -6.611  37.244  1.00 119.29 ? 568 GLY A N     1 
ATOM   4428 C  CA    . GLY A 1 568 ? 19.657  -5.229  37.358  1.00 114.45 ? 568 GLY A CA    1 
ATOM   4429 C  C     . GLY A 1 568 ? 18.185  -5.034  37.662  1.00 106.89 ? 568 GLY A C     1 
ATOM   4430 O  O     . GLY A 1 568 ? 17.812  -4.024  38.267  1.00 109.08 ? 568 GLY A O     1 
ATOM   4431 N  N     . LEU A 1 569 ? 17.340  -5.979  37.251  1.00 102.88 ? 569 LEU A N     1 
ATOM   4432 C  CA    . LEU A 1 569 ? 15.922  -5.945  37.582  1.00 105.55 ? 569 LEU A CA    1 
ATOM   4433 C  C     . LEU A 1 569 ? 15.662  -6.797  38.818  1.00 107.43 ? 569 LEU A C     1 
ATOM   4434 O  O     . LEU A 1 569 ? 15.603  -6.277  39.938  1.00 111.71 ? 569 LEU A O     1 
ATOM   4435 C  CB    . LEU A 1 569 ? 15.081  -6.436  36.402  1.00 94.18  ? 569 LEU A CB    1 
ATOM   4436 C  CG    . LEU A 1 569 ? 15.284  -5.712  35.069  1.00 84.85  ? 569 LEU A CG    1 
ATOM   4437 C  CD1   . LEU A 1 569 ? 14.419  -6.331  33.981  1.00 79.11  ? 569 LEU A CD1   1 
ATOM   4438 C  CD2   . LEU A 1 569 ? 14.990  -4.227  35.210  1.00 90.22  ? 569 LEU A CD2   1 
ATOM   4439 N  N     . GLY A 1 570 ? 15.507  -8.105  38.625  1.00 104.58 ? 570 GLY A N     1 
ATOM   4440 C  CA    . GLY A 1 570 ? 15.358  -9.028  39.733  1.00 110.96 ? 570 GLY A CA    1 
ATOM   4441 C  C     . GLY A 1 570 ? 14.011  -8.971  40.423  1.00 114.48 ? 570 GLY A C     1 
ATOM   4442 O  O     . GLY A 1 570 ? 13.579  -9.953  41.036  1.00 114.02 ? 570 GLY A O     1 
ATOM   4443 N  N     . ASP A 1 571 ? 13.337  -7.828  40.334  1.00 114.46 ? 571 ASP A N     1 
ATOM   4444 C  CA    . ASP A 1 571 ? 12.046  -7.630  40.977  1.00 117.85 ? 571 ASP A CA    1 
ATOM   4445 C  C     . ASP A 1 571 ? 10.870  -7.960  40.068  1.00 123.20 ? 571 ASP A C     1 
ATOM   4446 O  O     . ASP A 1 571 ? 9.721   -7.889  40.517  1.00 128.50 ? 571 ASP A O     1 
ATOM   4447 C  CB    . ASP A 1 571 ? 11.923  -6.185  41.473  1.00 120.00 ? 571 ASP A CB    1 
ATOM   4448 C  CG    . ASP A 1 571 ? 12.171  -5.170  40.374  1.00 121.26 ? 571 ASP A CG    1 
ATOM   4449 O  OD1   . ASP A 1 571 ? 12.946  -5.475  39.444  1.00 115.00 ? 571 ASP A OD1   1 
ATOM   4450 O  OD2   . ASP A 1 571 ? 11.591  -4.065  40.441  1.00 131.23 ? 571 ASP A OD2   1 
ATOM   4451 N  N     . VAL A 1 572 ? 11.123  -8.319  38.809  1.00 121.65 ? 572 VAL A N     1 
ATOM   4452 C  CA    . VAL A 1 572 ? 10.039  -8.621  37.884  1.00 113.83 ? 572 VAL A CA    1 
ATOM   4453 C  C     . VAL A 1 572 ? 9.364   -9.923  38.291  1.00 113.43 ? 572 VAL A C     1 
ATOM   4454 O  O     . VAL A 1 572 ? 10.027  -10.911 38.634  1.00 112.66 ? 572 VAL A O     1 
ATOM   4455 C  CB    . VAL A 1 572 ? 10.569  -8.696  36.442  1.00 106.72 ? 572 VAL A CB    1 
ATOM   4456 C  CG1   . VAL A 1 572 ? 9.418   -8.860  35.461  1.00 104.83 ? 572 VAL A CG1   1 
ATOM   4457 C  CG2   . VAL A 1 572 ? 11.389  -7.457  36.113  1.00 104.06 ? 572 VAL A CG2   1 
ATOM   4458 N  N     . ASN A 1 573 ? 8.033   -9.929  38.255  1.00 111.32 ? 573 ASN A N     1 
ATOM   4459 C  CA    . ASN A 1 573 ? 7.251   -11.113 38.605  1.00 111.79 ? 573 ASN A CA    1 
ATOM   4460 C  C     . ASN A 1 573 ? 7.331   -12.102 37.450  1.00 106.51 ? 573 ASN A C     1 
ATOM   4461 O  O     . ASN A 1 573 ? 6.594   -11.993 36.467  1.00 103.01 ? 573 ASN A O     1 
ATOM   4462 C  CB    . ASN A 1 573 ? 5.808   -10.731 38.913  1.00 112.86 ? 573 ASN A CB    1 
ATOM   4463 C  CG    . ASN A 1 573 ? 4.969   -11.919 39.344  1.00 113.73 ? 573 ASN A CG    1 
ATOM   4464 O  OD1   . ASN A 1 573 ? 5.499   -12.963 39.723  1.00 113.43 ? 573 ASN A OD1   1 
ATOM   4465 N  ND2   . ASN A 1 573 ? 3.652   -11.763 39.292  1.00 117.51 ? 573 ASN A ND2   1 
ATOM   4466 N  N     . VAL A 1 574 ? 8.233   -13.079 37.568  1.00 107.48 ? 574 VAL A N     1 
ATOM   4467 C  CA    . VAL A 1 574 ? 8.436   -14.044 36.493  1.00 102.01 ? 574 VAL A CA    1 
ATOM   4468 C  C     . VAL A 1 574 ? 7.349   -15.111 36.454  1.00 102.14 ? 574 VAL A C     1 
ATOM   4469 O  O     . VAL A 1 574 ? 7.103   -15.693 35.390  1.00 94.23  ? 574 VAL A O     1 
ATOM   4470 C  CB    . VAL A 1 574 ? 9.814   -14.713 36.620  1.00 88.41  ? 574 VAL A CB    1 
ATOM   4471 C  CG1   . VAL A 1 574 ? 10.920  -13.679 36.474  1.00 84.83  ? 574 VAL A CG1   1 
ATOM   4472 C  CG2   . VAL A 1 574 ? 9.930   -15.440 37.951  1.00 96.02  ? 574 VAL A CG2   1 
ATOM   4473 N  N     . GLU A 1 575 ? 6.690   -15.386 37.581  1.00 106.89 ? 575 GLU A N     1 
ATOM   4474 C  CA    . GLU A 1 575 ? 5.656   -16.415 37.599  1.00 106.84 ? 575 GLU A CA    1 
ATOM   4475 C  C     . GLU A 1 575 ? 4.461   -16.011 36.744  1.00 99.42  ? 575 GLU A C     1 
ATOM   4476 O  O     . GLU A 1 575 ? 3.947   -16.814 35.957  1.00 96.40  ? 575 GLU A O     1 
ATOM   4477 C  CB    . GLU A 1 575 ? 5.220   -16.695 39.037  1.00 115.48 ? 575 GLU A CB    1 
ATOM   4478 C  CG    . GLU A 1 575 ? 6.325   -17.236 39.929  1.00 121.87 ? 575 GLU A CG    1 
ATOM   4479 C  CD    . GLU A 1 575 ? 6.806   -18.606 39.495  1.00 127.13 ? 575 GLU A CD    1 
ATOM   4480 O  OE1   . GLU A 1 575 ? 6.095   -19.266 38.708  1.00 128.01 ? 575 GLU A OE1   1 
ATOM   4481 O  OE2   . GLU A 1 575 ? 7.896   -19.023 39.940  1.00 131.13 ? 575 GLU A OE2   1 
ATOM   4482 N  N     . GLU A 1 576 ? 4.002   -14.766 36.886  1.00 100.03 ? 576 GLU A N     1 
ATOM   4483 C  CA    . GLU A 1 576 ? 2.851   -14.296 36.125  1.00 101.01 ? 576 GLU A CA    1 
ATOM   4484 C  C     . GLU A 1 576 ? 3.221   -13.834 34.722  1.00 91.86  ? 576 GLU A C     1 
ATOM   4485 O  O     . GLU A 1 576 ? 2.334   -13.715 33.870  1.00 90.71  ? 576 GLU A O     1 
ATOM   4486 C  CB    . GLU A 1 576 ? 2.154   -13.159 36.875  1.00 105.57 ? 576 GLU A CB    1 
ATOM   4487 C  CG    . GLU A 1 576 ? 0.837   -12.719 36.257  1.00 111.60 ? 576 GLU A CG    1 
ATOM   4488 C  CD    . GLU A 1 576 ? 0.155   -11.627 37.057  1.00 130.06 ? 576 GLU A CD    1 
ATOM   4489 O  OE1   . GLU A 1 576 ? 0.794   -11.079 37.980  1.00 125.87 ? 576 GLU A OE1   1 
ATOM   4490 O  OE2   . GLU A 1 576 ? -1.020  -11.320 36.765  1.00 147.16 ? 576 GLU A OE2   1 
ATOM   4491 N  N     . LEU A 1 577 ? 4.503   -13.574 34.462  1.00 87.18  ? 577 LEU A N     1 
ATOM   4492 C  CA    . LEU A 1 577 ? 4.936   -13.147 33.138  1.00 80.09  ? 577 LEU A CA    1 
ATOM   4493 C  C     . LEU A 1 577 ? 5.134   -14.312 32.177  1.00 81.04  ? 577 LEU A C     1 
ATOM   4494 O  O     . LEU A 1 577 ? 5.249   -14.084 30.968  1.00 74.15  ? 577 LEU A O     1 
ATOM   4495 C  CB    . LEU A 1 577 ? 6.232   -12.338 33.248  1.00 75.35  ? 577 LEU A CB    1 
ATOM   4496 C  CG    . LEU A 1 577 ? 6.691   -11.598 31.991  1.00 77.38  ? 577 LEU A CG    1 
ATOM   4497 C  CD1   . LEU A 1 577 ? 5.593   -10.677 31.479  1.00 78.07  ? 577 LEU A CD1   1 
ATOM   4498 C  CD2   . LEU A 1 577 ? 7.962   -10.813 32.272  1.00 70.51  ? 577 LEU A CD2   1 
ATOM   4499 N  N     . PHE A 1 578 ? 5.175   -15.548 32.684  1.00 89.26  ? 578 PHE A N     1 
ATOM   4500 C  CA    . PHE A 1 578 ? 5.294   -16.738 31.849  1.00 77.02  ? 578 PHE A CA    1 
ATOM   4501 C  C     . PHE A 1 578 ? 4.272   -17.804 32.233  1.00 71.06  ? 578 PHE A C     1 
ATOM   4502 O  O     . PHE A 1 578 ? 4.485   -18.987 31.952  1.00 70.40  ? 578 PHE A O     1 
ATOM   4503 C  CB    . PHE A 1 578 ? 6.709   -17.318 31.924  1.00 68.78  ? 578 PHE A CB    1 
ATOM   4504 C  CG    . PHE A 1 578 ? 7.684   -16.668 30.985  1.00 61.94  ? 578 PHE A CG    1 
ATOM   4505 C  CD1   . PHE A 1 578 ? 8.374   -15.526 31.358  1.00 70.60  ? 578 PHE A CD1   1 
ATOM   4506 C  CD2   . PHE A 1 578 ? 7.915   -17.203 29.728  1.00 52.49  ? 578 PHE A CD2   1 
ATOM   4507 C  CE1   . PHE A 1 578 ? 9.273   -14.929 30.494  1.00 63.77  ? 578 PHE A CE1   1 
ATOM   4508 C  CE2   . PHE A 1 578 ? 8.813   -16.611 28.860  1.00 48.47  ? 578 PHE A CE2   1 
ATOM   4509 C  CZ    . PHE A 1 578 ? 9.492   -15.472 29.243  1.00 66.94  ? 578 PHE A CZ    1 
ATOM   4510 N  N     . GLY A 1 579 ? 3.170   -17.410 32.868  1.00 77.76  ? 579 GLY A N     1 
ATOM   4511 C  CA    . GLY A 1 579 ? 2.167   -18.360 33.306  1.00 83.25  ? 579 GLY A CA    1 
ATOM   4512 C  C     . GLY A 1 579 ? 1.250   -18.832 32.198  1.00 80.72  ? 579 GLY A C     1 
ATOM   4513 O  O     . GLY A 1 579 ? 0.608   -18.020 31.525  1.00 80.58  ? 579 GLY A O     1 
ATOM   4514 N  N     . ILE A 1 580 ? 1.180   -20.144 32.000  1.00 80.44  ? 580 ILE A N     1 
ATOM   4515 C  CA    . ILE A 1 580 ? 0.330   -20.754 30.985  1.00 77.88  ? 580 ILE A CA    1 
ATOM   4516 C  C     . ILE A 1 580 ? -0.857  -21.375 31.711  1.00 76.56  ? 580 ILE A C     1 
ATOM   4517 O  O     . ILE A 1 580 ? -0.747  -22.456 32.300  1.00 76.69  ? 580 ILE A O     1 
ATOM   4518 C  CB    . ILE A 1 580 ? 1.085   -21.794 30.151  1.00 68.69  ? 580 ILE A CB    1 
ATOM   4519 C  CG1   . ILE A 1 580 ? 2.279   -21.149 29.444  1.00 72.24  ? 580 ILE A CG1   1 
ATOM   4520 C  CG2   . ILE A 1 580 ? 0.152   -22.446 29.141  1.00 75.43  ? 580 ILE A CG2   1 
ATOM   4521 C  CD1   . ILE A 1 580 ? 3.083   -22.116 28.602  1.00 61.09  ? 580 ILE A CD1   1 
ATOM   4522 N  N     . SER A 1 581 ? -1.999  -20.693 31.671  1.00 76.27  ? 581 SER A N     1 
ATOM   4523 C  CA    . SER A 1 581 ? -3.215  -21.180 32.305  1.00 78.33  ? 581 SER A CA    1 
ATOM   4524 C  C     . SER A 1 581 ? -3.987  -22.064 31.333  1.00 75.44  ? 581 SER A C     1 
ATOM   4525 O  O     . SER A 1 581 ? -4.167  -21.704 30.166  1.00 76.42  ? 581 SER A O     1 
ATOM   4526 C  CB    . SER A 1 581 ? -4.088  -20.013 32.766  1.00 84.46  ? 581 SER A CB    1 
ATOM   4527 O  OG    . SER A 1 581 ? -5.318  -20.474 33.295  1.00 89.97  ? 581 SER A OG    1 
ATOM   4528 N  N     . LYS A 1 582 ? -4.440  -23.221 31.820  1.00 84.26  ? 582 LYS A N     1 
ATOM   4529 C  CA    . LYS A 1 582 ? -5.216  -24.119 30.972  1.00 84.79  ? 582 LYS A CA    1 
ATOM   4530 C  C     . LYS A 1 582 ? -6.591  -23.546 30.659  1.00 84.96  ? 582 LYS A C     1 
ATOM   4531 O  O     . LYS A 1 582 ? -7.121  -23.771 29.564  1.00 80.48  ? 582 LYS A O     1 
ATOM   4532 C  CB    . LYS A 1 582 ? -5.350  -25.488 31.640  1.00 78.03  ? 582 LYS A CB    1 
ATOM   4533 C  CG    . LYS A 1 582 ? -6.121  -26.506 30.817  1.00 72.64  ? 582 LYS A CG    1 
ATOM   4534 C  CD    . LYS A 1 582 ? -6.162  -27.858 31.507  1.00 78.67  ? 582 LYS A CD    1 
ATOM   4535 C  CE    . LYS A 1 582 ? -6.876  -28.892 30.652  1.00 79.03  ? 582 LYS A CE    1 
ATOM   4536 N  NZ    . LYS A 1 582 ? -6.860  -30.240 31.284  1.00 74.77  ? 582 LYS A NZ    1 
ATOM   4537 N  N     . GLU A 1 583 ? -7.182  -22.804 31.598  1.00 92.18  ? 583 GLU A N     1 
ATOM   4538 C  CA    . GLU A 1 583 ? -8.505  -22.236 31.366  1.00 89.57  ? 583 GLU A CA    1 
ATOM   4539 C  C     . GLU A 1 583 ? -8.479  -21.180 30.270  1.00 86.42  ? 583 GLU A C     1 
ATOM   4540 O  O     . GLU A 1 583 ? -9.460  -21.031 29.531  1.00 82.49  ? 583 GLU A O     1 
ATOM   4541 C  CB    . GLU A 1 583 ? -9.060  -21.636 32.660  1.00 91.65  ? 583 GLU A CB    1 
ATOM   4542 C  CG    . GLU A 1 583 ? -9.046  -22.579 33.855  1.00 105.78 ? 583 GLU A CG    1 
ATOM   4543 C  CD    . GLU A 1 583 ? -7.682  -22.670 34.513  1.00 111.55 ? 583 GLU A CD    1 
ATOM   4544 O  OE1   . GLU A 1 583 ? -6.786  -21.884 34.139  1.00 99.28  ? 583 GLU A OE1   1 
ATOM   4545 O  OE2   . GLU A 1 583 ? -7.505  -23.529 35.404  1.00 122.46 ? 583 GLU A OE2   1 
ATOM   4546 N  N     . PHE A 1 584 ? -7.374  -20.442 30.147  1.00 79.86  ? 584 PHE A N     1 
ATOM   4547 C  CA    . PHE A 1 584 ? -7.292  -19.373 29.157  1.00 71.08  ? 584 PHE A CA    1 
ATOM   4548 C  C     . PHE A 1 584 ? -7.108  -19.927 27.749  1.00 70.76  ? 584 PHE A C     1 
ATOM   4549 O  O     . PHE A 1 584 ? -7.784  -19.492 26.810  1.00 67.43  ? 584 PHE A O     1 
ATOM   4550 C  CB    . PHE A 1 584 ? -6.150  -18.418 29.512  1.00 69.96  ? 584 PHE A CB    1 
ATOM   4551 C  CG    . PHE A 1 584 ? -5.889  -17.371 28.467  1.00 56.14  ? 584 PHE A CG    1 
ATOM   4552 C  CD1   . PHE A 1 584 ? -6.647  -16.213 28.424  1.00 58.59  ? 584 PHE A CD1   1 
ATOM   4553 C  CD2   . PHE A 1 584 ? -4.885  -17.543 27.530  1.00 53.95  ? 584 PHE A CD2   1 
ATOM   4554 C  CE1   . PHE A 1 584 ? -6.409  -15.247 27.465  1.00 53.39  ? 584 PHE A CE1   1 
ATOM   4555 C  CE2   . PHE A 1 584 ? -4.642  -16.582 26.567  1.00 52.54  ? 584 PHE A CE2   1 
ATOM   4556 C  CZ    . PHE A 1 584 ? -5.405  -15.432 26.535  1.00 51.62  ? 584 PHE A CZ    1 
ATOM   4557 N  N     . TRP A 1 585 ? -6.195  -20.886 27.583  1.00 68.71  ? 585 TRP A N     1 
ATOM   4558 C  CA    . TRP A 1 585 ? -5.891  -21.402 26.254  1.00 67.98  ? 585 TRP A CA    1 
ATOM   4559 C  C     . TRP A 1 585 ? -6.960  -22.348 25.725  1.00 64.45  ? 585 TRP A C     1 
ATOM   4560 O  O     . TRP A 1 585 ? -6.985  -22.617 24.520  1.00 62.92  ? 585 TRP A O     1 
ATOM   4561 C  CB    . TRP A 1 585 ? -4.529  -22.099 26.261  1.00 62.46  ? 585 TRP A CB    1 
ATOM   4562 C  CG    . TRP A 1 585 ? -3.391  -21.139 26.416  1.00 59.58  ? 585 TRP A CG    1 
ATOM   4563 C  CD1   . TRP A 1 585 ? -2.755  -20.802 27.575  1.00 65.71  ? 585 TRP A CD1   1 
ATOM   4564 C  CD2   . TRP A 1 585 ? -2.765  -20.377 25.378  1.00 58.49  ? 585 TRP A CD2   1 
ATOM   4565 N  NE1   . TRP A 1 585 ? -1.766  -19.882 27.321  1.00 61.11  ? 585 TRP A NE1   1 
ATOM   4566 C  CE2   . TRP A 1 585 ? -1.752  -19.605 25.980  1.00 59.61  ? 585 TRP A CE2   1 
ATOM   4567 C  CE3   . TRP A 1 585 ? -2.959  -20.276 23.997  1.00 56.20  ? 585 TRP A CE3   1 
ATOM   4568 C  CZ2   . TRP A 1 585 ? -0.936  -18.743 25.249  1.00 63.41  ? 585 TRP A CZ2   1 
ATOM   4569 C  CZ3   . TRP A 1 585 ? -2.149  -19.420 23.274  1.00 57.46  ? 585 TRP A CZ3   1 
ATOM   4570 C  CH2   . TRP A 1 585 ? -1.150  -18.665 23.901  1.00 54.27  ? 585 TRP A CH2   1 
ATOM   4571 N  N     . GLU A 1 586 ? -7.839  -22.859 26.590  1.00 69.76  ? 586 GLU A N     1 
ATOM   4572 C  CA    . GLU A 1 586 ? -8.970  -23.639 26.097  1.00 70.14  ? 586 GLU A CA    1 
ATOM   4573 C  C     . GLU A 1 586 ? -10.006 -22.747 25.427  1.00 68.02  ? 586 GLU A C     1 
ATOM   4574 O  O     . GLU A 1 586 ? -10.709 -23.193 24.513  1.00 79.17  ? 586 GLU A O     1 
ATOM   4575 C  CB    . GLU A 1 586 ? -9.603  -24.436 27.237  1.00 79.23  ? 586 GLU A CB    1 
ATOM   4576 C  CG    . GLU A 1 586 ? -8.774  -25.626 27.693  1.00 88.49  ? 586 GLU A CG    1 
ATOM   4577 C  CD    . GLU A 1 586 ? -9.516  -26.513 28.673  1.00 96.46  ? 586 GLU A CD    1 
ATOM   4578 O  OE1   . GLU A 1 586 ? -10.500 -26.039 29.279  1.00 102.41 ? 586 GLU A OE1   1 
ATOM   4579 O  OE2   . GLU A 1 586 ? -9.119  -27.687 28.832  1.00 91.34  ? 586 GLU A OE2   1 
ATOM   4580 N  N     . LYS A 1 587 ? -10.115 -21.491 25.864  1.00 64.31  ? 587 LYS A N     1 
ATOM   4581 C  CA    . LYS A 1 587 ? -10.994 -20.536 25.201  1.00 54.25  ? 587 LYS A CA    1 
ATOM   4582 C  C     . LYS A 1 587 ? -10.324 -19.887 23.998  1.00 65.46  ? 587 LYS A C     1 
ATOM   4583 O  O     . LYS A 1 587 ? -10.998 -19.584 23.007  1.00 69.27  ? 587 LYS A O     1 
ATOM   4584 C  CB    . LYS A 1 587 ? -11.444 -19.462 26.193  1.00 59.81  ? 587 LYS A CB    1 
ATOM   4585 C  CG    . LYS A 1 587 ? -12.156 -18.279 25.555  1.00 66.18  ? 587 LYS A CG    1 
ATOM   4586 C  CD    . LYS A 1 587 ? -13.466 -18.697 24.910  1.00 68.84  ? 587 LYS A CD    1 
ATOM   4587 C  CE    . LYS A 1 587 ? -14.180 -17.503 24.296  1.00 65.88  ? 587 LYS A CE    1 
ATOM   4588 N  NZ    . LYS A 1 587 ? -15.495 -17.880 23.708  1.00 66.64  ? 587 LYS A NZ    1 
ATOM   4589 N  N     . GLU A 1 588 ? -9.009  -19.670 24.064  1.00 59.56  ? 588 GLU A N     1 
ATOM   4590 C  CA    . GLU A 1 588 ? -8.301  -19.045 22.952  1.00 61.09  ? 588 GLU A CA    1 
ATOM   4591 C  C     . GLU A 1 588 ? -8.435  -19.876 21.682  1.00 59.44  ? 588 GLU A C     1 
ATOM   4592 O  O     . GLU A 1 588 ? -8.732  -19.346 20.605  1.00 59.09  ? 588 GLU A O     1 
ATOM   4593 C  CB    . GLU A 1 588 ? -6.828  -18.846 23.316  1.00 57.20  ? 588 GLU A CB    1 
ATOM   4594 C  CG    . GLU A 1 588 ? -6.064  -17.940 22.363  1.00 54.17  ? 588 GLU A CG    1 
ATOM   4595 C  CD    . GLU A 1 588 ? -6.385  -16.472 22.570  1.00 52.25  ? 588 GLU A CD    1 
ATOM   4596 O  OE1   . GLU A 1 588 ? -7.023  -16.141 23.591  1.00 54.49  ? 588 GLU A OE1   1 
ATOM   4597 O  OE2   . GLU A 1 588 ? -5.997  -15.650 21.713  1.00 44.40  ? 588 GLU A OE2   1 
ATOM   4598 N  N     . VAL A 1 589 ? -8.217  -21.189 21.790  1.00 60.98  ? 589 VAL A N     1 
ATOM   4599 C  CA    . VAL A 1 589 ? -8.358  -22.057 20.625  1.00 66.77  ? 589 VAL A CA    1 
ATOM   4600 C  C     . VAL A 1 589 ? -9.802  -22.086 20.146  1.00 69.50  ? 589 VAL A C     1 
ATOM   4601 O  O     . VAL A 1 589 ? -10.062 -22.217 18.943  1.00 65.77  ? 589 VAL A O     1 
ATOM   4602 C  CB    . VAL A 1 589 ? -7.841  -23.472 20.945  1.00 59.82  ? 589 VAL A CB    1 
ATOM   4603 C  CG1   . VAL A 1 589 ? -6.346  -23.441 21.221  1.00 53.71  ? 589 VAL A CG1   1 
ATOM   4604 C  CG2   . VAL A 1 589 ? -8.595  -24.056 22.129  1.00 61.63  ? 589 VAL A CG2   1 
ATOM   4605 N  N     . GLU A 1 590 ? -10.763 -21.967 21.065  1.00 78.08  ? 590 GLU A N     1 
ATOM   4606 C  CA    . GLU A 1 590 ? -12.165 -21.925 20.662  1.00 75.74  ? 590 GLU A CA    1 
ATOM   4607 C  C     . GLU A 1 590 ? -12.429 -20.755 19.723  1.00 77.50  ? 590 GLU A C     1 
ATOM   4608 O  O     . GLU A 1 590 ? -13.133 -20.902 18.718  1.00 83.42  ? 590 GLU A O     1 
ATOM   4609 C  CB    . GLU A 1 590 ? -13.064 -21.839 21.896  1.00 77.07  ? 590 GLU A CB    1 
ATOM   4610 C  CG    . GLU A 1 590 ? -14.551 -21.867 21.584  1.00 87.09  ? 590 GLU A CG    1 
ATOM   4611 C  CD    . GLU A 1 590 ? -15.000 -23.197 21.011  1.00 101.25 ? 590 GLU A CD    1 
ATOM   4612 O  OE1   . GLU A 1 590 ? -14.286 -24.202 21.209  1.00 108.09 ? 590 GLU A OE1   1 
ATOM   4613 O  OE2   . GLU A 1 590 ? -16.066 -23.236 20.361  1.00 99.84  ? 590 GLU A OE2   1 
ATOM   4614 N  N     . GLU A 1 591 ? -11.868 -19.584 20.034  1.00 64.88  ? 591 GLU A N     1 
ATOM   4615 C  CA    . GLU A 1 591 ? -12.032 -18.431 19.156  1.00 64.72  ? 591 GLU A CA    1 
ATOM   4616 C  C     . GLU A 1 591 ? -11.206 -18.572 17.885  1.00 59.32  ? 591 GLU A C     1 
ATOM   4617 O  O     . GLU A 1 591 ? -11.604 -18.067 16.829  1.00 62.74  ? 591 GLU A O     1 
ATOM   4618 C  CB    . GLU A 1 591 ? -11.655 -17.148 19.897  1.00 59.59  ? 591 GLU A CB    1 
ATOM   4619 C  CG    . GLU A 1 591 ? -12.595 -16.802 21.039  1.00 62.91  ? 591 GLU A CG    1 
ATOM   4620 C  CD    . GLU A 1 591 ? -14.014 -16.554 20.565  1.00 67.13  ? 591 GLU A CD    1 
ATOM   4621 O  OE1   . GLU A 1 591 ? -14.185 -16.078 19.423  1.00 66.54  ? 591 GLU A OE1   1 
ATOM   4622 O  OE2   . GLU A 1 591 ? -14.958 -16.839 21.332  1.00 66.69  ? 591 GLU A OE2   1 
ATOM   4623 N  N     . ILE A 1 592 ? -10.058 -19.248 17.964  1.00 68.77  ? 592 ILE A N     1 
ATOM   4624 C  CA    . ILE A 1 592 ? -9.245  -19.464 16.771  1.00 66.55  ? 592 ILE A CA    1 
ATOM   4625 C  C     . ILE A 1 592 ? -9.925  -20.456 15.837  1.00 55.67  ? 592 ILE A C     1 
ATOM   4626 O  O     . ILE A 1 592 ? -9.937  -20.270 14.614  1.00 48.41  ? 592 ILE A O     1 
ATOM   4627 C  CB    . ILE A 1 592 ? -7.833  -19.931 17.165  1.00 53.90  ? 592 ILE A CB    1 
ATOM   4628 C  CG1   . ILE A 1 592 ? -7.103  -18.831 17.939  1.00 60.81  ? 592 ILE A CG1   1 
ATOM   4629 C  CG2   . ILE A 1 592 ? -7.043  -20.341 15.930  1.00 52.93  ? 592 ILE A CG2   1 
ATOM   4630 C  CD1   . ILE A 1 592 ? -5.701  -19.210 18.364  1.00 44.10  ? 592 ILE A CD1   1 
ATOM   4631 N  N     . ASP A 1 593 ? -10.500 -21.524 16.393  1.00 58.47  ? 593 ASP A N     1 
ATOM   4632 C  CA    . ASP A 1 593 ? -11.200 -22.500 15.565  1.00 59.91  ? 593 ASP A CA    1 
ATOM   4633 C  C     . ASP A 1 593 ? -12.378 -21.861 14.840  1.00 59.24  ? 593 ASP A C     1 
ATOM   4634 O  O     . ASP A 1 593 ? -12.619 -22.143 13.661  1.00 66.57  ? 593 ASP A O     1 
ATOM   4635 C  CB    . ASP A 1 593 ? -11.672 -23.673 16.425  1.00 53.09  ? 593 ASP A CB    1 
ATOM   4636 C  CG    . ASP A 1 593 ? -12.313 -24.776 15.605  1.00 52.27  ? 593 ASP A CG    1 
ATOM   4637 O  OD1   . ASP A 1 593 ? -12.127 -24.786 14.370  1.00 58.56  ? 593 ASP A OD1   1 
ATOM   4638 O  OD2   . ASP A 1 593 ? -13.007 -25.630 16.195  1.00 49.32  ? 593 ASP A OD2   1 
ATOM   4639 N  N     . LYS A 1 594 ? -13.121 -20.991 15.529  1.00 59.76  ? 594 LYS A N     1 
ATOM   4640 C  CA    . LYS A 1 594 ? -14.282 -20.361 14.911  1.00 51.94  ? 594 LYS A CA    1 
ATOM   4641 C  C     . LYS A 1 594 ? -13.877 -19.309 13.886  1.00 68.69  ? 594 LYS A C     1 
ATOM   4642 O  O     . LYS A 1 594 ? -14.611 -19.075 12.920  1.00 74.17  ? 594 LYS A O     1 
ATOM   4643 C  CB    . LYS A 1 594 ? -15.175 -19.741 15.986  1.00 61.77  ? 594 LYS A CB    1 
ATOM   4644 C  CG    . LYS A 1 594 ? -15.756 -20.751 16.965  1.00 63.11  ? 594 LYS A CG    1 
ATOM   4645 C  CD    . LYS A 1 594 ? -16.694 -20.091 17.965  1.00 68.10  ? 594 LYS A CD    1 
ATOM   4646 C  CE    . LYS A 1 594 ? -15.953 -19.122 18.871  1.00 66.09  ? 594 LYS A CE    1 
ATOM   4647 N  NZ    . LYS A 1 594 ? -16.856 -18.518 19.890  1.00 68.15  ? 594 LYS A NZ    1 
ATOM   4648 N  N     . TYR A 1 595 ? -12.720 -18.670 14.073  1.00 58.19  ? 595 TYR A N     1 
ATOM   4649 C  CA    . TYR A 1 595 ? -12.293 -17.636 13.136  1.00 52.36  ? 595 TYR A CA    1 
ATOM   4650 C  C     . TYR A 1 595 ? -11.813 -18.242 11.822  1.00 62.61  ? 595 TYR A C     1 
ATOM   4651 O  O     . TYR A 1 595 ? -12.141 -17.735 10.742  1.00 57.43  ? 595 TYR A O     1 
ATOM   4652 C  CB    . TYR A 1 595 ? -11.196 -16.777 13.765  1.00 56.51  ? 595 TYR A CB    1 
ATOM   4653 C  CG    . TYR A 1 595 ? -10.749 -15.621 12.898  1.00 51.76  ? 595 TYR A CG    1 
ATOM   4654 C  CD1   . TYR A 1 595 ? -11.435 -14.414 12.909  1.00 54.46  ? 595 TYR A CD1   1 
ATOM   4655 C  CD2   . TYR A 1 595 ? -9.642  -15.736 12.068  1.00 55.61  ? 595 TYR A CD2   1 
ATOM   4656 C  CE1   . TYR A 1 595 ? -11.032 -13.355 12.118  1.00 57.93  ? 595 TYR A CE1   1 
ATOM   4657 C  CE2   . TYR A 1 595 ? -9.231  -14.682 11.273  1.00 55.94  ? 595 TYR A CE2   1 
ATOM   4658 C  CZ    . TYR A 1 595 ? -9.930  -13.494 11.303  1.00 52.97  ? 595 TYR A CZ    1 
ATOM   4659 O  OH    . TYR A 1 595 ? -9.525  -12.441 10.514  1.00 54.02  ? 595 TYR A OH    1 
ATOM   4660 N  N     . LEU A 1 596 ? -11.038 -19.327 11.891  1.00 60.67  ? 596 LEU A N     1 
ATOM   4661 C  CA    . LEU A 1 596 ? -10.507 -19.932 10.673  1.00 62.76  ? 596 LEU A CA    1 
ATOM   4662 C  C     . LEU A 1 596 ? -11.610 -20.580 9.845   1.00 75.22  ? 596 LEU A C     1 
ATOM   4663 O  O     . LEU A 1 596 ? -11.636 -20.439 8.617   1.00 65.85  ? 596 LEU A O     1 
ATOM   4664 C  CB    . LEU A 1 596 ? -9.427  -20.954 11.022  1.00 61.45  ? 596 LEU A CB    1 
ATOM   4665 C  CG    . LEU A 1 596 ? -8.107  -20.390 11.551  1.00 63.38  ? 596 LEU A CG    1 
ATOM   4666 C  CD1   . LEU A 1 596 ? -7.173  -21.515 11.964  1.00 48.52  ? 596 LEU A CD1   1 
ATOM   4667 C  CD2   . LEU A 1 596 ? -7.452  -19.503 10.503  1.00 54.49  ? 596 LEU A CD2   1 
ATOM   4668 N  N     . GLU A 1 597 ? -12.529 -21.297 10.497  1.00 85.31  ? 597 GLU A N     1 
ATOM   4669 C  CA    . GLU A 1 597 ? -13.603 -21.958 9.763   1.00 85.91  ? 597 GLU A CA    1 
ATOM   4670 C  C     . GLU A 1 597 ? -14.541 -20.955 9.104   1.00 89.03  ? 597 GLU A C     1 
ATOM   4671 O  O     . GLU A 1 597 ? -15.111 -21.245 8.047   1.00 87.76  ? 597 GLU A O     1 
ATOM   4672 C  CB    . GLU A 1 597 ? -14.389 -22.879 10.697  1.00 87.81  ? 597 GLU A CB    1 
ATOM   4673 C  CG    . GLU A 1 597 ? -15.547 -23.605 10.028  1.00 101.11 ? 597 GLU A CG    1 
ATOM   4674 C  CD    . GLU A 1 597 ? -16.303 -24.503 10.989  1.00 115.71 ? 597 GLU A CD    1 
ATOM   4675 O  OE1   . GLU A 1 597 ? -15.910 -24.570 12.173  1.00 115.91 ? 597 GLU A OE1   1 
ATOM   4676 O  OE2   . GLU A 1 597 ? -17.288 -25.142 10.563  1.00 125.46 ? 597 GLU A OE2   1 
ATOM   4677 N  N     . ASP A 1 598 ? -14.716 -19.778 9.706   1.00 91.14  ? 598 ASP A N     1 
ATOM   4678 C  CA    . ASP A 1 598 ? -15.663 -18.810 9.166   1.00 91.49  ? 598 ASP A CA    1 
ATOM   4679 C  C     . ASP A 1 598 ? -15.042 -17.926 8.093   1.00 92.74  ? 598 ASP A C     1 
ATOM   4680 O  O     . ASP A 1 598 ? -15.730 -17.540 7.142   1.00 100.34 ? 598 ASP A O     1 
ATOM   4681 C  CB    . ASP A 1 598 ? -16.229 -17.949 10.297  1.00 91.30  ? 598 ASP A CB    1 
ATOM   4682 C  CG    . ASP A 1 598 ? -17.055 -16.786 9.787   1.00 98.51  ? 598 ASP A CG    1 
ATOM   4683 O  OD1   . ASP A 1 598 ? -18.175 -17.021 9.287   1.00 113.06 ? 598 ASP A OD1   1 
ATOM   4684 O  OD2   . ASP A 1 598 ? -16.579 -15.635 9.884   1.00 94.09  ? 598 ASP A OD2   1 
ATOM   4685 N  N     . GLN A 1 599 ? -13.755 -17.607 8.215   1.00 69.83  ? 599 GLN A N     1 
ATOM   4686 C  CA    . GLN A 1 599 ? -13.094 -16.671 7.313   1.00 62.66  ? 599 GLN A CA    1 
ATOM   4687 C  C     . GLN A 1 599 ? -12.334 -17.350 6.181   1.00 68.39  ? 599 GLN A C     1 
ATOM   4688 O  O     . GLN A 1 599 ? -12.414 -16.898 5.034   1.00 77.27  ? 599 GLN A O     1 
ATOM   4689 C  CB    . GLN A 1 599 ? -12.138 -15.771 8.103   1.00 74.93  ? 599 GLN A CB    1 
ATOM   4690 C  CG    . GLN A 1 599 ? -12.843 -14.817 9.056   1.00 69.07  ? 599 GLN A CG    1 
ATOM   4691 C  CD    . GLN A 1 599 ? -13.717 -13.814 8.328   1.00 67.30  ? 599 GLN A CD    1 
ATOM   4692 O  OE1   . GLN A 1 599 ? -13.493 -13.517 7.154   1.00 68.52  ? 599 GLN A OE1   1 
ATOM   4693 N  NE2   . GLN A 1 599 ? -14.721 -13.290 9.020   1.00 70.05  ? 599 GLN A NE2   1 
ATOM   4694 N  N     . VAL A 1 600 ? -11.593 -18.417 6.468   1.00 64.18  ? 600 VAL A N     1 
ATOM   4695 C  CA    . VAL A 1 600 ? -10.829 -19.102 5.429   1.00 61.71  ? 600 VAL A CA    1 
ATOM   4696 C  C     . VAL A 1 600 ? -11.661 -20.187 4.757   1.00 65.02  ? 600 VAL A C     1 
ATOM   4697 O  O     . VAL A 1 600 ? -11.623 -20.337 3.533   1.00 70.38  ? 600 VAL A O     1 
ATOM   4698 C  CB    . VAL A 1 600 ? -9.527  -19.671 6.027   1.00 73.50  ? 600 VAL A CB    1 
ATOM   4699 C  CG1   . VAL A 1 600 ? -8.550  -20.043 4.921   1.00 65.22  ? 600 VAL A CG1   1 
ATOM   4700 C  CG2   . VAL A 1 600 ? -8.901  -18.666 6.983   1.00 54.74  ? 600 VAL A CG2   1 
ATOM   4701 N  N     . ASN A 1 601 ? -12.414 -20.956 5.543   1.00 71.57  ? 601 ASN A N     1 
ATOM   4702 C  CA    . ASN A 1 601 ? -13.398 -21.915 5.034   1.00 72.29  ? 601 ASN A CA    1 
ATOM   4703 C  C     . ASN A 1 601 ? -12.694 -22.931 4.142   1.00 73.21  ? 601 ASN A C     1 
ATOM   4704 O  O     . ASN A 1 601 ? -11.836 -23.678 4.644   1.00 72.41  ? 601 ASN A O     1 
ATOM   4705 C  CB    . ASN A 1 601 ? -14.531 -21.130 4.371   1.00 78.50  ? 601 ASN A CB    1 
ATOM   4706 C  CG    . ASN A 1 601 ? -15.676 -22.018 3.930   1.00 85.77  ? 601 ASN A CG    1 
ATOM   4707 O  OD1   . ASN A 1 601 ? -15.859 -23.121 4.447   1.00 91.89  ? 601 ASN A OD1   1 
ATOM   4708 N  ND2   . ASN A 1 601 ? -16.458 -21.539 2.971   1.00 93.07  ? 601 ASN A ND2   1 
ATOM   4709 N  N     . ALA A 1 602 ? -13.008 -23.006 2.848   1.00 71.37  ? 602 ALA A N     1 
ATOM   4710 C  CA    . ALA A 1 602 ? -12.494 -24.071 1.997   1.00 73.99  ? 602 ALA A CA    1 
ATOM   4711 C  C     . ALA A 1 602 ? -11.061 -23.841 1.540   1.00 69.63  ? 602 ALA A C     1 
ATOM   4712 O  O     . ALA A 1 602 ? -10.398 -24.802 1.137   1.00 73.49  ? 602 ALA A O     1 
ATOM   4713 C  CB    . ALA A 1 602 ? -13.392 -24.242 0.770   1.00 74.84  ? 602 ALA A CB    1 
ATOM   4714 N  N     . ASP A 1 603 ? -10.575 -22.602 1.575   1.00 69.96  ? 603 ASP A N     1 
ATOM   4715 C  CA    . ASP A 1 603 ? -9.220  -22.287 1.143   1.00 71.19  ? 603 ASP A CA    1 
ATOM   4716 C  C     . ASP A 1 603 ? -8.193  -22.440 2.258   1.00 64.93  ? 603 ASP A C     1 
ATOM   4717 O  O     . ASP A 1 603 ? -7.064  -21.958 2.115   1.00 62.51  ? 603 ASP A O     1 
ATOM   4718 C  CB    . ASP A 1 603 ? -9.165  -20.866 0.573   1.00 74.63  ? 603 ASP A CB    1 
ATOM   4719 C  CG    . ASP A 1 603 ? -9.992  -20.712 -0.690  1.00 83.21  ? 603 ASP A CG    1 
ATOM   4720 O  OD1   . ASP A 1 603 ? -9.904  -21.597 -1.567  1.00 89.15  ? 603 ASP A OD1   1 
ATOM   4721 O  OD2   . ASP A 1 603 ? -10.737 -19.715 -0.803  1.00 87.61  ? 603 ASP A OD2   1 
ATOM   4722 N  N     . LEU A 1 604 ? -8.552  -23.103 3.355   1.00 53.90  ? 604 LEU A N     1 
ATOM   4723 C  CA    . LEU A 1 604 ? -7.632  -23.294 4.468   1.00 65.23  ? 604 LEU A CA    1 
ATOM   4724 C  C     . LEU A 1 604 ? -6.770  -24.525 4.220   1.00 61.37  ? 604 LEU A C     1 
ATOM   4725 O  O     . LEU A 1 604 ? -7.317  -25.618 4.023   1.00 66.35  ? 604 LEU A O     1 
ATOM   4726 C  CB    . LEU A 1 604 ? -8.394  -23.452 5.773   1.00 61.41  ? 604 LEU A CB    1 
ATOM   4727 C  CG    . LEU A 1 604 ? -7.547  -23.673 7.027   1.00 56.93  ? 604 LEU A CG    1 
ATOM   4728 C  CD1   . LEU A 1 604 ? -6.739  -22.428 7.358   1.00 48.81  ? 604 LEU A CD1   1 
ATOM   4729 C  CD2   . LEU A 1 604 ? -8.419  -24.084 8.204   1.00 46.14  ? 604 LEU A CD2   1 
ATOM   4730 N  N     . PRO A 1 605 ? -5.444  -24.403 4.217   1.00 65.01  ? 605 PRO A N     1 
ATOM   4731 C  CA    . PRO A 1 605 ? -4.595  -25.581 4.017   1.00 62.42  ? 605 PRO A CA    1 
ATOM   4732 C  C     . PRO A 1 605 ? -4.758  -26.585 5.149   1.00 68.00  ? 605 PRO A C     1 
ATOM   4733 O  O     . PRO A 1 605 ? -5.146  -26.248 6.270   1.00 60.06  ? 605 PRO A O     1 
ATOM   4734 C  CB    . PRO A 1 605 ? -3.176  -24.999 3.987   1.00 55.01  ? 605 PRO A CB    1 
ATOM   4735 C  CG    . PRO A 1 605 ? -3.361  -23.553 3.652   1.00 54.16  ? 605 PRO A CG    1 
ATOM   4736 C  CD    . PRO A 1 605 ? -4.660  -23.160 4.284   1.00 51.79  ? 605 PRO A CD    1 
ATOM   4737 N  N     . TYR A 1 606 ? -4.450  -27.846 4.835   1.00 70.64  ? 606 TYR A N     1 
ATOM   4738 C  CA    . TYR A 1 606 ? -4.579  -28.909 5.828   1.00 75.49  ? 606 TYR A CA    1 
ATOM   4739 C  C     . TYR A 1 606 ? -3.564  -28.761 6.954   1.00 71.08  ? 606 TYR A C     1 
ATOM   4740 O  O     . TYR A 1 606 ? -3.868  -29.092 8.106   1.00 69.57  ? 606 TYR A O     1 
ATOM   4741 C  CB    . TYR A 1 606 ? -4.429  -30.275 5.158   1.00 82.57  ? 606 TYR A CB    1 
ATOM   4742 C  CG    . TYR A 1 606 ? -4.224  -31.416 6.132   1.00 84.69  ? 606 TYR A CG    1 
ATOM   4743 C  CD1   . TYR A 1 606 ? -5.296  -31.974 6.816   1.00 80.94  ? 606 TYR A CD1   1 
ATOM   4744 C  CD2   . TYR A 1 606 ? -2.957  -31.937 6.363   1.00 82.27  ? 606 TYR A CD2   1 
ATOM   4745 C  CE1   . TYR A 1 606 ? -5.111  -33.016 7.706   1.00 80.92  ? 606 TYR A CE1   1 
ATOM   4746 C  CE2   . TYR A 1 606 ? -2.763  -32.979 7.250   1.00 79.85  ? 606 TYR A CE2   1 
ATOM   4747 C  CZ    . TYR A 1 606 ? -3.843  -33.515 7.919   1.00 82.78  ? 606 TYR A CZ    1 
ATOM   4748 O  OH    . TYR A 1 606 ? -3.654  -34.553 8.802   1.00 83.81  ? 606 TYR A OH    1 
ATOM   4749 N  N     . GLU A 1 607 ? -2.360  -28.272 6.648   1.00 63.09  ? 607 GLU A N     1 
ATOM   4750 C  CA    . GLU A 1 607 ? -1.333  -28.148 7.678   1.00 63.54  ? 607 GLU A CA    1 
ATOM   4751 C  C     . GLU A 1 607 ? -1.731  -27.129 8.739   1.00 52.91  ? 607 GLU A C     1 
ATOM   4752 O  O     . GLU A 1 607 ? -1.442  -27.319 9.927   1.00 52.79  ? 607 GLU A O     1 
ATOM   4753 C  CB    . GLU A 1 607 ? 0.005   -27.778 7.041   1.00 65.93  ? 607 GLU A CB    1 
ATOM   4754 C  CG    . GLU A 1 607 ? 0.563   -28.860 6.130   1.00 71.03  ? 607 GLU A CG    1 
ATOM   4755 C  CD    . GLU A 1 607 ? 1.881   -28.471 5.491   1.00 73.26  ? 607 GLU A CD    1 
ATOM   4756 O  OE1   . GLU A 1 607 ? 2.239   -27.275 5.542   1.00 83.69  ? 607 GLU A OE1   1 
ATOM   4757 O  OE2   . GLU A 1 607 ? 2.559   -29.362 4.939   1.00 79.89  ? 607 GLU A OE2   1 
ATOM   4758 N  N     . ILE A 1 608 ? -2.394  -26.043 8.336   1.00 50.22  ? 608 ILE A N     1 
ATOM   4759 C  CA    . ILE A 1 608 ? -2.888  -25.078 9.315   1.00 47.17  ? 608 ILE A CA    1 
ATOM   4760 C  C     . ILE A 1 608 ? -3.937  -25.725 10.210  1.00 52.34  ? 608 ILE A C     1 
ATOM   4761 O  O     . ILE A 1 608 ? -4.028  -25.425 11.406  1.00 49.10  ? 608 ILE A O     1 
ATOM   4762 C  CB    . ILE A 1 608 ? -3.439  -23.827 8.606   1.00 57.67  ? 608 ILE A CB    1 
ATOM   4763 C  CG1   . ILE A 1 608 ? -2.341  -23.155 7.778   1.00 56.94  ? 608 ILE A CG1   1 
ATOM   4764 C  CG2   . ILE A 1 608 ? -4.015  -22.851 9.621   1.00 44.11  ? 608 ILE A CG2   1 
ATOM   4765 C  CD1   . ILE A 1 608 ? -1.157  -22.689 8.597   1.00 56.27  ? 608 ILE A CD1   1 
ATOM   4766 N  N     . GLU A 1 609 ? -4.744  -26.626 9.645   1.00 57.27  ? 609 GLU A N     1 
ATOM   4767 C  CA    . GLU A 1 609 ? -5.731  -27.348 10.439  1.00 53.46  ? 609 GLU A CA    1 
ATOM   4768 C  C     . GLU A 1 609 ? -5.075  -28.418 11.304  1.00 51.17  ? 609 GLU A C     1 
ATOM   4769 O  O     . GLU A 1 609 ? -5.491  -28.638 12.447  1.00 42.32  ? 609 GLU A O     1 
ATOM   4770 C  CB    . GLU A 1 609 ? -6.783  -27.976 9.524   1.00 57.49  ? 609 GLU A CB    1 
ATOM   4771 C  CG    . GLU A 1 609 ? -7.860  -28.756 10.259  1.00 48.55  ? 609 GLU A CG    1 
ATOM   4772 C  CD    . GLU A 1 609 ? -8.870  -29.382 9.317   1.00 62.48  ? 609 GLU A CD    1 
ATOM   4773 O  OE1   . GLU A 1 609 ? -8.766  -29.155 8.092   1.00 64.96  ? 609 GLU A OE1   1 
ATOM   4774 O  OE2   . GLU A 1 609 ? -9.767  -30.104 9.800   1.00 70.65  ? 609 GLU A OE2   1 
ATOM   4775 N  N     . ARG A 1 610 ? -4.052  -29.093 10.775  1.00 52.18  ? 610 ARG A N     1 
ATOM   4776 C  CA    . ARG A 1 610 ? -3.366  -30.120 11.553  1.00 51.33  ? 610 ARG A CA    1 
ATOM   4777 C  C     . ARG A 1 610 ? -2.703  -29.524 12.787  1.00 53.96  ? 610 ARG A C     1 
ATOM   4778 O  O     . ARG A 1 610 ? -2.651  -30.165 13.843  1.00 40.41  ? 610 ARG A O     1 
ATOM   4779 C  CB    . ARG A 1 610 ? -2.339  -30.841 10.681  1.00 55.16  ? 610 ARG A CB    1 
ATOM   4780 C  CG    . ARG A 1 610 ? -1.655  -32.017 11.360  1.00 58.28  ? 610 ARG A CG    1 
ATOM   4781 C  CD    . ARG A 1 610 ? -0.875  -32.848 10.354  1.00 56.10  ? 610 ARG A CD    1 
ATOM   4782 N  NE    . ARG A 1 610 ? 0.181   -32.079 9.705   1.00 60.14  ? 610 ARG A NE    1 
ATOM   4783 C  CZ    . ARG A 1 610 ? 0.912   -32.520 8.690   1.00 67.88  ? 610 ARG A CZ    1 
ATOM   4784 N  NH1   . ARG A 1 610 ? 0.720   -33.722 8.171   1.00 72.25  ? 610 ARG A NH1   1 
ATOM   4785 N  NH2   . ARG A 1 610 ? 1.858   -31.735 8.183   1.00 62.52  ? 610 ARG A NH2   1 
ATOM   4786 N  N     . GLU A 1 611 ? -2.190  -28.295 12.675  1.00 45.24  ? 611 GLU A N     1 
ATOM   4787 C  CA    . GLU A 1 611 ? -1.614  -27.628 13.838  1.00 45.83  ? 611 GLU A CA    1 
ATOM   4788 C  C     . GLU A 1 611 ? -2.696  -27.207 14.825  1.00 50.64  ? 611 GLU A C     1 
ATOM   4789 O  O     . GLU A 1 611 ? -2.489  -27.267 16.043  1.00 46.95  ? 611 GLU A O     1 
ATOM   4790 C  CB    . GLU A 1 611 ? -0.786  -26.421 13.395  1.00 42.95  ? 611 GLU A CB    1 
ATOM   4791 C  CG    . GLU A 1 611 ? 0.508   -26.790 12.691  1.00 38.62  ? 611 GLU A CG    1 
ATOM   4792 C  CD    . GLU A 1 611 ? 1.450   -27.571 13.587  1.00 46.67  ? 611 GLU A CD    1 
ATOM   4793 O  OE1   . GLU A 1 611 ? 1.274   -27.522 14.823  1.00 43.07  ? 611 GLU A OE1   1 
ATOM   4794 O  OE2   . GLU A 1 611 ? 2.362   -28.238 13.055  1.00 58.85  ? 611 GLU A OE2   1 
ATOM   4795 N  N     . LEU A 1 612 ? -3.855  -26.777 14.320  1.00 46.86  ? 612 LEU A N     1 
ATOM   4796 C  CA    . LEU A 1 612 ? -4.959  -26.427 15.209  1.00 44.39  ? 612 LEU A CA    1 
ATOM   4797 C  C     . LEU A 1 612 ? -5.386  -27.625 16.049  1.00 52.39  ? 612 LEU A C     1 
ATOM   4798 O  O     . LEU A 1 612 ? -5.648  -27.490 17.250  1.00 54.10  ? 612 LEU A O     1 
ATOM   4799 C  CB    . LEU A 1 612 ? -6.136  -25.889 14.396  1.00 48.92  ? 612 LEU A CB    1 
ATOM   4800 C  CG    . LEU A 1 612 ? -7.363  -25.431 15.186  1.00 46.03  ? 612 LEU A CG    1 
ATOM   4801 C  CD1   . LEU A 1 612 ? -6.986  -24.346 16.182  1.00 53.28  ? 612 LEU A CD1   1 
ATOM   4802 C  CD2   . LEU A 1 612 ? -8.450  -24.941 14.243  1.00 48.30  ? 612 LEU A CD2   1 
ATOM   4803 N  N     . ARG A 1 613 ? -5.460  -28.808 15.434  1.00 46.61  ? 613 ARG A N     1 
ATOM   4804 C  CA    . ARG A 1 613 ? -5.781  -30.012 16.193  1.00 47.54  ? 613 ARG A CA    1 
ATOM   4805 C  C     . ARG A 1 613 ? -4.641  -30.392 17.129  1.00 46.59  ? 613 ARG A C     1 
ATOM   4806 O  O     . ARG A 1 613 ? -4.879  -30.830 18.261  1.00 48.67  ? 613 ARG A O     1 
ATOM   4807 C  CB    . ARG A 1 613 ? -6.097  -31.168 15.245  1.00 57.80  ? 613 ARG A CB    1 
ATOM   4808 C  CG    . ARG A 1 613 ? -7.326  -30.956 14.378  1.00 57.11  ? 613 ARG A CG    1 
ATOM   4809 C  CD    . ARG A 1 613 ? -7.680  -32.227 13.625  1.00 61.69  ? 613 ARG A CD    1 
ATOM   4810 N  NE    . ARG A 1 613 ? -8.877  -32.071 12.808  1.00 76.57  ? 613 ARG A NE    1 
ATOM   4811 C  CZ    . ARG A 1 613 ? -9.481  -33.064 12.169  1.00 73.54  ? 613 ARG A CZ    1 
ATOM   4812 N  NH1   . ARG A 1 613 ? -9.029  -34.305 12.237  1.00 73.20  ? 613 ARG A NH1   1 
ATOM   4813 N  NH2   . ARG A 1 613 ? -10.566 -32.805 11.445  1.00 79.93  ? 613 ARG A NH2   1 
ATOM   4814 N  N     . ALA A 1 614 ? -3.395  -30.236 16.674  1.00 45.56  ? 614 ALA A N     1 
ATOM   4815 C  CA    . ALA A 1 614 ? -2.254  -30.579 17.516  1.00 49.52  ? 614 ALA A CA    1 
ATOM   4816 C  C     . ALA A 1 614 ? -2.203  -29.702 18.760  1.00 50.24  ? 614 ALA A C     1 
ATOM   4817 O  O     . ALA A 1 614 ? -1.974  -30.198 19.870  1.00 49.27  ? 614 ALA A O     1 
ATOM   4818 C  CB    . ALA A 1 614 ? -0.957  -30.458 16.716  1.00 46.37  ? 614 ALA A CB    1 
ATOM   4819 N  N     . LEU A 1 615 ? -2.413  -28.394 18.597  1.00 51.05  ? 615 LEU A N     1 
ATOM   4820 C  CA    . LEU A 1 615 ? -2.420  -27.501 19.751  1.00 48.79  ? 615 LEU A CA    1 
ATOM   4821 C  C     . LEU A 1 615 ? -3.585  -27.814 20.682  1.00 53.79  ? 615 LEU A C     1 
ATOM   4822 O  O     . LEU A 1 615 ? -3.417  -27.844 21.907  1.00 52.43  ? 615 LEU A O     1 
ATOM   4823 C  CB    . LEU A 1 615 ? -2.476  -26.045 19.290  1.00 46.37  ? 615 LEU A CB    1 
ATOM   4824 C  CG    . LEU A 1 615 ? -2.534  -24.986 20.392  1.00 42.76  ? 615 LEU A CG    1 
ATOM   4825 C  CD1   . LEU A 1 615 ? -1.287  -25.042 21.260  1.00 52.38  ? 615 LEU A CD1   1 
ATOM   4826 C  CD2   . LEU A 1 615 ? -2.716  -23.599 19.794  1.00 39.76  ? 615 LEU A CD2   1 
ATOM   4827 N  N     . LYS A 1 616 ? -4.773  -28.049 20.119  1.00 59.36  ? 616 LYS A N     1 
ATOM   4828 C  CA    . LYS A 1 616 ? -5.929  -28.383 20.946  1.00 50.92  ? 616 LYS A CA    1 
ATOM   4829 C  C     . LYS A 1 616 ? -5.675  -29.642 21.765  1.00 46.06  ? 616 LYS A C     1 
ATOM   4830 O  O     . LYS A 1 616 ? -6.037  -29.707 22.946  1.00 44.56  ? 616 LYS A O     1 
ATOM   4831 C  CB    . LYS A 1 616 ? -7.168  -28.554 20.067  1.00 47.19  ? 616 LYS A CB    1 
ATOM   4832 C  CG    . LYS A 1 616 ? -8.426  -28.932 20.833  1.00 52.52  ? 616 LYS A CG    1 
ATOM   4833 C  CD    . LYS A 1 616 ? -9.611  -29.103 19.896  1.00 80.49  ? 616 LYS A CD    1 
ATOM   4834 C  CE    . LYS A 1 616 ? -10.871 -29.482 20.659  1.00 92.28  ? 616 LYS A CE    1 
ATOM   4835 N  NZ    . LYS A 1 616 ? -12.035 -29.674 19.750  1.00 93.79  ? 616 LYS A NZ    1 
ATOM   4836 N  N     . GLN A 1 617 ? -5.054  -30.653 21.155  1.00 63.77  ? 617 GLN A N     1 
ATOM   4837 C  CA    . GLN A 1 617 ? -4.772  -31.894 21.869  1.00 51.68  ? 617 GLN A CA    1 
ATOM   4838 C  C     . GLN A 1 617 ? -3.811  -31.653 23.028  1.00 52.77  ? 617 GLN A C     1 
ATOM   4839 O  O     . GLN A 1 617 ? -4.070  -32.071 24.163  1.00 49.54  ? 617 GLN A O     1 
ATOM   4840 C  CB    . GLN A 1 617 ? -4.202  -32.933 20.903  1.00 50.10  ? 617 GLN A CB    1 
ATOM   4841 C  CG    . GLN A 1 617 ? -3.945  -34.299 21.523  1.00 57.05  ? 617 GLN A CG    1 
ATOM   4842 C  CD    . GLN A 1 617 ? -5.217  -35.099 21.731  1.00 59.08  ? 617 GLN A CD    1 
ATOM   4843 O  OE1   . GLN A 1 617 ? -6.316  -34.626 21.442  1.00 60.55  ? 617 GLN A OE1   1 
ATOM   4844 N  NE2   . GLN A 1 617 ? -5.071  -36.321 22.229  1.00 61.16  ? 617 GLN A NE2   1 
ATOM   4845 N  N     . ARG A 1 618 ? -2.692  -30.975 22.759  1.00 50.24  ? 618 ARG A N     1 
ATOM   4846 C  CA    . ARG A 1 618 ? -1.700  -30.738 23.803  1.00 52.13  ? 618 ARG A CA    1 
ATOM   4847 C  C     . ARG A 1 618 ? -2.276  -29.929 24.958  1.00 55.55  ? 618 ARG A C     1 
ATOM   4848 O  O     . ARG A 1 618 ? -1.909  -30.155 26.117  1.00 56.55  ? 618 ARG A O     1 
ATOM   4849 C  CB    . ARG A 1 618 ? -0.479  -30.026 23.219  1.00 44.19  ? 618 ARG A CB    1 
ATOM   4850 C  CG    . ARG A 1 618 ? 0.232   -30.800 22.121  1.00 48.59  ? 618 ARG A CG    1 
ATOM   4851 C  CD    . ARG A 1 618 ? 1.517   -30.100 21.708  1.00 42.88  ? 618 ARG A CD    1 
ATOM   4852 N  NE    . ARG A 1 618 ? 1.277   -28.733 21.263  1.00 44.60  ? 618 ARG A NE    1 
ATOM   4853 C  CZ    . ARG A 1 618 ? 1.171   -28.364 19.994  1.00 54.99  ? 618 ARG A CZ    1 
ATOM   4854 N  NH1   . ARG A 1 618 ? 1.291   -29.238 19.008  1.00 58.54  ? 618 ARG A NH1   1 
ATOM   4855 N  NH2   . ARG A 1 618 ? 0.941   -27.086 19.706  1.00 52.22  ? 618 ARG A NH2   1 
ATOM   4856 N  N     . ILE A 1 619 ? -3.173  -28.984 24.667  1.00 57.19  ? 619 ILE A N     1 
ATOM   4857 C  CA    . ILE A 1 619 ? -3.747  -28.166 25.730  1.00 55.21  ? 619 ILE A CA    1 
ATOM   4858 C  C     . ILE A 1 619 ? -4.718  -28.977 26.576  1.00 56.28  ? 619 ILE A C     1 
ATOM   4859 O  O     . ILE A 1 619 ? -4.853  -28.736 27.782  1.00 54.76  ? 619 ILE A O     1 
ATOM   4860 C  CB    . ILE A 1 619 ? -4.424  -26.916 25.138  1.00 64.55  ? 619 ILE A CB    1 
ATOM   4861 C  CG1   . ILE A 1 619 ? -3.380  -25.999 24.499  1.00 54.77  ? 619 ILE A CG1   1 
ATOM   4862 C  CG2   . ILE A 1 619 ? -5.214  -26.178 26.210  1.00 60.96  ? 619 ILE A CG2   1 
ATOM   4863 C  CD1   . ILE A 1 619 ? -3.961  -24.741 23.894  1.00 50.38  ? 619 ILE A CD1   1 
ATOM   4864 N  N     . SER A 1 620 ? -5.408  -29.946 25.971  1.00 56.32  ? 620 SER A N     1 
ATOM   4865 C  CA    . SER A 1 620 ? -6.339  -30.777 26.724  1.00 59.26  ? 620 SER A CA    1 
ATOM   4866 C  C     . SER A 1 620 ? -5.627  -31.742 27.661  1.00 66.20  ? 620 SER A C     1 
ATOM   4867 O  O     . SER A 1 620 ? -6.260  -32.277 28.578  1.00 66.84  ? 620 SER A O     1 
ATOM   4868 C  CB    . SER A 1 620 ? -7.241  -31.556 25.765  1.00 59.65  ? 620 SER A CB    1 
ATOM   4869 O  OG    . SER A 1 620 ? -6.476  -32.377 24.901  1.00 61.94  ? 620 SER A OG    1 
ATOM   4870 N  N     . GLN A 1 621 ? -4.332  -31.973 27.458  1.00 67.85  ? 621 GLN A N     1 
ATOM   4871 C  CA    . GLN A 1 621 ? -3.560  -32.900 28.273  1.00 66.59  ? 621 GLN A CA    1 
ATOM   4872 C  C     . GLN A 1 621 ? -2.939  -32.238 29.498  1.00 76.86  ? 621 GLN A C     1 
ATOM   4873 O  O     . GLN A 1 621 ? -2.095  -32.853 30.156  1.00 79.52  ? 621 GLN A O     1 
ATOM   4874 C  CB    . GLN A 1 621 ? -2.465  -33.555 27.427  1.00 67.33  ? 621 GLN A CB    1 
ATOM   4875 C  CG    . GLN A 1 621 ? -2.973  -34.226 26.159  1.00 69.97  ? 621 GLN A CG    1 
ATOM   4876 C  CD    . GLN A 1 621 ? -3.865  -35.419 26.444  1.00 77.37  ? 621 GLN A CD    1 
ATOM   4877 O  OE1   . GLN A 1 621 ? -3.826  -35.993 27.532  1.00 87.69  ? 621 GLN A OE1   1 
ATOM   4878 N  NE2   . GLN A 1 621 ? -4.678  -35.797 25.463  1.00 75.83  ? 621 GLN A NE2   1 
ATOM   4879 N  N     . MET A 1 622 ? -3.332  -31.009 29.816  1.00 74.50  ? 622 MET A N     1 
ATOM   4880 C  CA    . MET A 1 622 ? -2.787  -30.309 30.974  1.00 73.13  ? 622 MET A CA    1 
ATOM   4881 C  C     . MET A 1 622 ? -3.484  -30.743 32.259  1.00 80.27  ? 622 MET A C     1 
ATOM   4882 O  O     . MET A 1 622 ? -4.593  -31.276 32.231  1.00 82.04  ? 622 MET A O     1 
ATOM   4883 C  CB    . MET A 1 622 ? -2.910  -28.794 30.797  1.00 76.00  ? 622 MET A CB    1 
ATOM   4884 C  CG    . MET A 1 622 ? -2.100  -28.233 29.640  1.00 75.73  ? 622 MET A CG    1 
ATOM   4885 S  SD    . MET A 1 622 ? -2.096  -26.431 29.610  1.00 72.79  ? 622 MET A SD    1 
ATOM   4886 C  CE    . MET A 1 622 ? -1.308  -26.069 31.177  1.00 71.47  ? 622 MET A CE    1 
ATOM   4887 O  OXT   . MET A 1 622 ? -2.952  -30.569 33.356  1.00 77.43  ? 622 MET A OXT   1 
HETATM 4888 MN MN    . MN  B 2 .   ? 2.480   0.183   9.549   1.00 60.85  ? 701 MN  A MN    1 
HETATM 4889 MN MN    . MN  C 2 .   ? 5.690   2.861   12.546  1.00 55.73  ? 702 MN  A MN    1 
HETATM 4890 MN MN    . MN  D 2 .   ? 4.835   -28.964 3.189   1.00 140.04 ? 703 MN  A MN    1 
HETATM 4891 P  P     A PGA E 3 .   ? 2.913   1.684   11.527  0.29 55.89  ? 704 PGA A P     1 
HETATM 4892 P  P     B PGA E 3 .   ? 0.745   2.829   9.979   0.37 66.56  ? 704 PGA A P     1 
HETATM 4893 P  P     C PGA E 3 .   ? -0.469  2.979   10.107  0.34 73.20  ? 704 PGA A P     1 
HETATM 4894 O  O1P   A PGA E 3 .   ? 1.970   2.074   10.284  0.29 63.06  ? 704 PGA A O1P   1 
HETATM 4895 O  O1P   B PGA E 3 .   ? -0.262  3.799   9.181   0.37 70.12  ? 704 PGA A O1P   1 
HETATM 4896 O  O1P   C PGA E 3 .   ? -0.970  4.470   9.762   0.34 70.42  ? 704 PGA A O1P   1 
HETATM 4897 O  O2P   A PGA E 3 .   ? 2.201   0.617   12.324  0.29 60.15  ? 704 PGA A O2P   1 
HETATM 4898 O  O2P   B PGA E 3 .   ? 0.805   3.269   11.422  0.37 66.80  ? 704 PGA A O2P   1 
HETATM 4899 O  O2P   C PGA E 3 .   ? 1.032   2.916   9.956   0.34 66.14  ? 704 PGA A O2P   1 
HETATM 4900 O  O3P   A PGA E 3 .   ? 3.143   2.904   12.387  0.29 60.29  ? 704 PGA A O3P   1 
HETATM 4901 O  O3P   B PGA E 3 .   ? 2.120   2.910   9.360   0.37 64.70  ? 704 PGA A O3P   1 
HETATM 4902 O  O3P   C PGA E 3 .   ? -1.129  1.994   9.172   0.34 67.66  ? 704 PGA A O3P   1 
HETATM 4903 O  O4P   A PGA E 3 .   ? 4.236   1.150   11.034  0.29 56.78  ? 704 PGA A O4P   1 
HETATM 4904 O  O4P   B PGA E 3 .   ? 0.238   1.409   9.902   0.37 62.81  ? 704 PGA A O4P   1 
HETATM 4905 O  O4P   C PGA E 3 .   ? -0.851  2.651   11.531  0.34 69.23  ? 704 PGA A O4P   1 
HETATM 4906 C  C2    A PGA E 3 .   ? 0.930   3.009   10.460  0.29 65.85  ? 704 PGA A C2    1 
HETATM 4907 C  C2    B PGA E 3 .   ? 0.216   4.946   8.513   0.37 67.25  ? 704 PGA A C2    1 
HETATM 4908 C  C2    C PGA E 3 .   ? -1.790  4.710   8.640   0.34 72.13  ? 704 PGA A C2    1 
HETATM 4909 C  C1    A PGA E 3 .   ? -0.266  2.589   9.641   0.29 68.70  ? 704 PGA A C1    1 
HETATM 4910 C  C1    B PGA E 3 .   ? -0.915  5.586   7.743   0.37 72.92  ? 704 PGA A C1    1 
HETATM 4911 C  C1    C PGA E 3 .   ? -2.023  6.194   8.492   0.34 77.94  ? 704 PGA A C1    1 
HETATM 4912 O  O1    A PGA E 3 .   ? -0.319  1.444   9.142   0.29 64.40  ? 704 PGA A O1    1 
HETATM 4913 O  O1    B PGA E 3 .   ? -1.095  6.822   7.788   0.37 81.85  ? 704 PGA A O1    1 
HETATM 4914 O  O1    C PGA E 3 .   ? -2.975  6.750   9.083   0.34 78.74  ? 704 PGA A O1    1 
HETATM 4915 O  O2    A PGA E 3 .   ? -1.221  3.375   9.458   0.29 71.61  ? 704 PGA A O2    1 
HETATM 4916 O  O2    B PGA E 3 .   ? -1.684  4.886   7.051   0.37 72.76  ? 704 PGA A O2    1 
HETATM 4917 O  O2    C PGA E 3 .   ? -1.269  6.886   7.773   0.34 81.83  ? 704 PGA A O2    1 
HETATM 4918 H  H21   A PGA E 3 .   ? 1.264   3.998   10.148  0.29 79.23  ? 704 PGA A H21   1 
HETATM 4919 H  H21   B PGA E 3 .   ? 1.020   4.669   7.830   0.37 80.91  ? 704 PGA A H21   1 
HETATM 4920 H  H21   C PGA E 3 .   ? -2.744  4.196   8.762   0.34 86.76  ? 704 PGA A H21   1 
HETATM 4921 H  H22   A PGA E 3 .   ? 0.657   3.065   11.514  0.29 79.23  ? 704 PGA A H22   1 
HETATM 4922 H  H22   B PGA E 3 .   ? 0.621   5.654   9.236   0.37 80.91  ? 704 PGA A H22   1 
HETATM 4923 H  H22   C PGA E 3 .   ? -1.312  4.319   7.742   0.34 86.76  ? 704 PGA A H22   1 
HETATM 4924 P  PB    . GDP F 4 .   ? 4.294   1.157   15.316  1.00 57.61  ? 705 GDP A PB    1 
HETATM 4925 O  O1B   . GDP F 4 .   ? 4.659   -0.295  15.115  1.00 55.09  ? 705 GDP A O1B   1 
HETATM 4926 O  O2B   . GDP F 4 .   ? 3.024   1.453   14.557  1.00 67.41  ? 705 GDP A O2B   1 
HETATM 4927 O  O3B   . GDP F 4 .   ? 5.415   2.038   14.820  1.00 45.05  ? 705 GDP A O3B   1 
HETATM 4928 O  O3A   . GDP F 4 .   ? 4.026   1.426   16.879  1.00 53.11  ? 705 GDP A O3A   1 
HETATM 4929 P  PA    . GDP F 4 .   ? 5.017   2.336   17.759  1.00 53.28  ? 705 GDP A PA    1 
HETATM 4930 O  O1A   . GDP F 4 .   ? 6.395   1.722   17.832  1.00 51.05  ? 705 GDP A O1A   1 
HETATM 4931 O  O2A   . GDP F 4 .   ? 5.085   3.745   17.219  1.00 58.36  ? 705 GDP A O2A   1 
HETATM 4932 O  "O5'" . GDP F 4 .   ? 4.299   2.312   19.198  1.00 47.86  ? 705 GDP A "O5'" 1 
HETATM 4933 C  "C5'" . GDP F 4 .   ? 3.574   3.454   19.643  1.00 59.10  ? 705 GDP A "C5'" 1 
HETATM 4934 C  "C4'" . GDP F 4 .   ? 3.323   3.350   21.139  1.00 62.89  ? 705 GDP A "C4'" 1 
HETATM 4935 O  "O4'" . GDP F 4 .   ? 3.639   2.036   21.603  1.00 57.44  ? 705 GDP A "O4'" 1 
HETATM 4936 C  "C3'" . GDP F 4 .   ? 4.210   4.317   21.903  1.00 70.78  ? 705 GDP A "C3'" 1 
HETATM 4937 O  "O3'" . GDP F 4 .   ? 3.431   5.413   22.391  1.00 75.74  ? 705 GDP A "O3'" 1 
HETATM 4938 C  "C2'" . GDP F 4 .   ? 4.787   3.521   23.056  1.00 66.46  ? 705 GDP A "C2'" 1 
HETATM 4939 O  "O2'" . GDP F 4 .   ? 4.347   4.075   24.299  1.00 64.71  ? 705 GDP A "O2'" 1 
HETATM 4940 C  "C1'" . GDP F 4 .   ? 4.257   2.104   22.890  1.00 54.00  ? 705 GDP A "C1'" 1 
HETATM 4941 N  N9    . GDP F 4 .   ? 5.378   1.135   22.981  1.00 56.83  ? 705 GDP A N9    1 
HETATM 4942 C  C8    . GDP F 4 .   ? 6.313   0.923   22.036  1.00 55.64  ? 705 GDP A C8    1 
HETATM 4943 N  N7    . GDP F 4 .   ? 7.197   -0.030  22.428  1.00 62.97  ? 705 GDP A N7    1 
HETATM 4944 C  C5    . GDP F 4 .   ? 6.825   -0.449  23.652  1.00 56.18  ? 705 GDP A C5    1 
HETATM 4945 C  C6    . GDP F 4 .   ? 7.319   -1.438  24.640  1.00 50.73  ? 705 GDP A C6    1 
HETATM 4946 O  O6    . GDP F 4 .   ? 8.334   -2.131  24.406  1.00 46.49  ? 705 GDP A O6    1 
HETATM 4947 N  N1    . GDP F 4 .   ? 6.645   -1.566  25.790  1.00 53.36  ? 705 GDP A N1    1 
HETATM 4948 C  C2    . GDP F 4 .   ? 5.549   -0.834  26.070  1.00 54.25  ? 705 GDP A C2    1 
HETATM 4949 N  N2    . GDP F 4 .   ? 4.926   -1.026  27.258  1.00 55.92  ? 705 GDP A N2    1 
HETATM 4950 N  N3    . GDP F 4 .   ? 5.041   0.089   25.212  1.00 45.65  ? 705 GDP A N3    1 
HETATM 4951 C  C4    . GDP F 4 .   ? 5.625   0.321   24.011  1.00 51.37  ? 705 GDP A C4    1 
HETATM 4952 O  O     . HOH G 5 .   ? 2.815   3.030   9.366   0.37 64.60  ? 801 HOH A O     1 
HETATM 4953 O  O     . HOH G 5 .   ? 2.477   0.283   11.709  0.37 59.21  ? 802 HOH A O     1 
HETATM 4954 O  O     . HOH G 5 .   ? 0.297   0.193   9.844   0.37 61.44  ? 803 HOH A O     1 
HETATM 4955 O  O     . HOH G 5 .   ? -7.764  9.370   -0.729  1.00 59.26  ? 804 HOH A O     1 
HETATM 4956 O  O     . HOH G 5 .   ? -0.032  -15.899 17.341  1.00 39.76  ? 805 HOH A O     1 
HETATM 4957 O  O     . HOH G 5 .   ? -0.157  -17.008 -8.059  1.00 62.82  ? 806 HOH A O     1 
HETATM 4958 O  O     . HOH G 5 .   ? 4.857   4.452   14.273  1.00 36.94  ? 807 HOH A O     1 
HETATM 4959 O  O     . HOH G 5 .   ? -5.589  -11.116 25.728  1.00 42.14  ? 808 HOH A O     1 
HETATM 4960 O  O     . HOH G 5 .   ? -16.745 -15.272 19.736  1.00 43.02  ? 809 HOH A O     1 
HETATM 4961 O  O     . HOH G 5 .   ? 4.615   -29.004 14.340  1.00 48.46  ? 810 HOH A O     1 
HETATM 4962 O  O     . HOH G 5 .   ? -5.954  -14.258 13.922  1.00 46.73  ? 811 HOH A O     1 
HETATM 4963 O  O     . HOH G 5 .   ? 5.198   3.838   9.501   1.00 55.68  ? 812 HOH A O     1 
HETATM 4964 O  O     . HOH G 5 .   ? -2.254  -13.323 20.602  1.00 41.77  ? 813 HOH A O     1 
HETATM 4965 O  O     . HOH G 5 .   ? 19.591  -18.497 23.833  1.00 42.83  ? 814 HOH A O     1 
HETATM 4966 O  O     . HOH G 5 .   ? 8.829   -2.292  21.162  1.00 58.85  ? 815 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . PRO A 3   ? 1.9772 1.2982 1.1272 -0.1293 -0.2322 0.1727  3   PRO A N   
2    C CA  . PRO A 3   ? 1.9720 1.3156 1.1408 -0.1420 -0.2511 0.1700  3   PRO A CA  
3    C C   . PRO A 3   ? 1.9239 1.3235 1.1540 -0.1447 -0.2761 0.1755  3   PRO A C   
4    O O   . PRO A 3   ? 1.7926 1.2294 1.0633 -0.1527 -0.2827 0.1726  3   PRO A O   
5    C CB  . PRO A 3   ? 1.8972 1.2586 1.0917 -0.1415 -0.2206 0.1611  3   PRO A CB  
6    C CG  . PRO A 3   ? 1.9711 1.2914 1.1252 -0.1323 -0.1903 0.1596  3   PRO A CG  
7    C CD  . PRO A 3   ? 2.0312 1.3407 1.1756 -0.1235 -0.1946 0.1679  3   PRO A CD  
8    N N   . GLN A 4   ? 1.7191 1.1240 0.9557 -0.1375 -0.2888 0.1840  4   GLN A N   
9    C CA  . GLN A 4   ? 1.6699 1.1269 0.9640 -0.1378 -0.3117 0.1907  4   GLN A CA  
10   C C   . GLN A 4   ? 1.7061 1.1474 0.9813 -0.1307 -0.3306 0.2006  4   GLN A C   
11   O O   . GLN A 4   ? 1.6672 1.0668 0.8983 -0.1228 -0.3179 0.2010  4   GLN A O   
12   C CB  . GLN A 4   ? 1.7216 1.2334 1.0847 -0.1306 -0.2909 0.1882  4   GLN A CB  
13   C CG  . GLN A 4   ? 1.7174 1.2210 1.0805 -0.1168 -0.2640 0.1880  4   GLN A CG  
14   C CD  . GLN A 4   ? 1.7910 1.3470 1.2207 -0.1098 -0.2473 0.1856  4   GLN A CD  
15   O OE1 . GLN A 4   ? 1.7775 1.3774 1.2540 -0.1141 -0.2555 0.1847  4   GLN A OE1 
16   N NE2 . GLN A 4   ? 1.8508 1.4010 1.2839 -0.0991 -0.2238 0.1847  4   GLN A NE2 
17   N N   . LEU A 5   ? 1.5911 1.0687 0.9041 -0.1329 -0.3596 0.2084  5   LEU A N   
18   C CA  . LEU A 5   ? 1.6378 1.1109 0.9465 -0.1250 -0.3775 0.2166  5   LEU A CA  
19   C C   . LEU A 5   ? 1.7974 1.3024 1.1479 -0.1107 -0.3666 0.2229  5   LEU A C   
20   O O   . LEU A 5   ? 1.6997 1.1813 1.0264 -0.1003 -0.3665 0.2287  5   LEU A O   
21   C CB  . LEU A 5   ? 1.5706 1.0685 0.9048 -0.1338 -0.4120 0.2202  5   LEU A CB  
22   C CG  . LEU A 5   ? 1.3994 0.8623 0.6939 -0.1470 -0.4249 0.2127  5   LEU A CG  
23   C CD1 . LEU A 5   ? 1.3584 0.8518 0.6877 -0.1563 -0.4587 0.2178  5   LEU A CD1 
24   C CD2 . LEU A 5   ? 1.4174 0.8202 0.6466 -0.1414 -0.4183 0.2088  5   LEU A CD2 
25   N N   . HIS A 6   ? 2.1138 1.6727 1.5290 -0.1091 -0.3548 0.2201  6   HIS A N   
26   C CA  . HIS A 6   ? 2.1303 1.7227 1.5915 -0.0950 -0.3403 0.2228  6   HIS A CA  
27   C C   . HIS A 6   ? 2.1851 1.7982 1.6762 -0.0933 -0.3077 0.2128  6   HIS A C   
28   O O   . HIS A 6   ? 2.1167 1.7373 1.6132 -0.1032 -0.3021 0.2057  6   HIS A O   
29   C CB  . HIS A 6   ? 2.0317 1.6762 1.5498 -0.0922 -0.3638 0.2319  6   HIS A CB  
30   C CG  . HIS A 6   ? 1.9669 1.5967 1.4628 -0.0930 -0.3979 0.2427  6   HIS A CG  
31   N ND1 . HIS A 6   ? 1.9441 1.5482 1.4030 -0.1069 -0.4231 0.2438  6   HIS A ND1 
32   C CD2 . HIS A 6   ? 1.9025 1.5383 1.4071 -0.0815 -0.4121 0.2530  6   HIS A CD2 
33   C CE1 . HIS A 6   ? 1.8931 1.4942 1.3487 -0.1034 -0.4452 0.2499  6   HIS A CE1 
34   N NE2 . HIS A 6   ? 1.8384 1.4567 1.3175 -0.0881 -0.4420 0.2579  6   HIS A NE2 
35   N N   . ASN A 7   ? 2.5461 2.1671 2.0560 -0.0805 -0.2870 0.2125  7   ASN A N   
36   C CA  . ASN A 7   ? 2.4809 2.1205 2.0197 -0.0778 -0.2569 0.2034  7   ASN A CA  
37   C C   . ASN A 7   ? 2.3988 2.0971 2.0023 -0.0775 -0.2608 0.2029  7   ASN A C   
38   O O   . ASN A 7   ? 2.3629 2.0912 2.0071 -0.0668 -0.2521 0.2039  7   ASN A O   
39   C CB  . ASN A 7   ? 2.5655 2.1906 2.1004 -0.0653 -0.2357 0.2036  7   ASN A CB  
40   C CG  . ASN A 7   ? 2.6606 2.2279 2.1332 -0.0661 -0.2241 0.2029  7   ASN A CG  
41   O OD1 . ASN A 7   ? 2.6052 2.1558 2.0642 -0.0687 -0.1997 0.1954  7   ASN A OD1 
42   N ND2 . ASN A 7   ? 2.7788 2.3151 2.2133 -0.0633 -0.2411 0.2113  7   ASN A ND2 
43   N N   . GLY A 8   ? 1.9571 1.6694 1.5679 -0.0896 -0.2739 0.2014  8   GLY A N   
44   C CA  . GLY A 8   ? 1.7176 1.4831 1.3863 -0.0909 -0.2768 0.2013  8   GLY A CA  
45   C C   . GLY A 8   ? 1.6479 1.4186 1.3206 -0.1007 -0.2633 0.1916  8   GLY A C   
46   O O   . GLY A 8   ? 1.5837 1.3960 1.3021 -0.1018 -0.2611 0.1903  8   GLY A O   
47   N N   . LEU A 9   ? 1.6384 1.3659 1.2621 -0.1071 -0.2533 0.1852  9   LEU A N   
48   C CA  . LEU A 9   ? 1.5189 1.2453 1.1400 -0.1159 -0.2401 0.1760  9   LEU A CA  
49   C C   . LEU A 9   ? 1.5323 1.2397 1.1400 -0.1106 -0.2088 0.1673  9   LEU A C   
50   O O   . LEU A 9   ? 1.5697 1.2823 1.1834 -0.1153 -0.1950 0.1595  9   LEU A O   
51   C CB  . LEU A 9   ? 1.5772 1.2696 1.1523 -0.1297 -0.2569 0.1758  9   LEU A CB  
52   C CG  . LEU A 9   ? 1.5492 1.2547 1.1322 -0.1378 -0.2913 0.1848  9   LEU A CG  
53   C CD1 . LEU A 9   ? 1.5351 1.2015 1.0681 -0.1522 -0.3066 0.1830  9   LEU A CD1 
54   C CD2 . LEU A 9   ? 1.4679 1.2318 1.1159 -0.1392 -0.2970 0.1875  9   LEU A CD2 
55   N N   . ASP A 10  ? 1.5197 1.2058 1.1109 -0.1010 -0.1974 0.1688  10  ASP A N   
56   C CA  . ASP A 10  ? 1.4859 1.1541 1.0667 -0.0964 -0.1680 0.1618  10  ASP A CA  
57   C C   . ASP A 10  ? 1.2971 1.0016 0.9281 -0.0863 -0.1548 0.1601  10  ASP A C   
58   O O   . ASP A 10  ? 1.2566 0.9626 0.8954 -0.0772 -0.1563 0.1652  10  ASP A O   
59   C CB  . ASP A 10  ? 1.5067 1.1253 1.0358 -0.0932 -0.1623 0.1650  10  ASP A CB  
60   C CG  . ASP A 10  ? 1.3734 0.9722 0.8911 -0.0898 -0.1315 0.1589  10  ASP A CG  
61   O OD1 . ASP A 10  ? 1.3550 0.9774 0.9031 -0.0906 -0.1162 0.1516  10  ASP A OD1 
62   O OD2 . ASP A 10  ? 1.4321 0.9918 0.9110 -0.0864 -0.1225 0.1618  10  ASP A OD2 
63   N N   . PHE A 11  ? 1.3022 1.0337 0.9650 -0.0877 -0.1422 0.1526  11  PHE A N   
64   C CA  . PHE A 11  ? 1.2514 1.0154 0.9593 -0.0787 -0.1296 0.1496  11  PHE A CA  
65   C C   . PHE A 11  ? 1.1010 0.8466 0.8020 -0.0742 -0.1043 0.1439  11  PHE A C   
66   O O   . PHE A 11  ? 1.0422 0.8106 0.7758 -0.0703 -0.0907 0.1378  11  PHE A O   
67   C CB  . PHE A 11  ? 1.2003 1.0027 0.9460 -0.0818 -0.1301 0.1450  11  PHE A CB  
68   C CG  . PHE A 11  ? 1.2105 1.0436 0.9814 -0.0830 -0.1523 0.1520  11  PHE A CG  
69   C CD1 . PHE A 11  ? 1.2131 1.0371 0.9637 -0.0935 -0.1723 0.1567  11  PHE A CD1 
70   C CD2 . PHE A 11  ? 1.1346 1.0053 0.9499 -0.0736 -0.1532 0.1544  11  PHE A CD2 
71   C CE1 . PHE A 11  ? 1.2306 1.0855 1.0089 -0.0953 -0.1932 0.1641  11  PHE A CE1 
72   C CE2 . PHE A 11  ? 1.0180 0.9193 0.8599 -0.0740 -0.1721 0.1620  11  PHE A CE2 
73   C CZ  . PHE A 11  ? 1.1636 1.0585 0.9891 -0.0853 -0.1923 0.1672  11  PHE A CZ  
74   N N   . SER A 12  ? 1.1259 0.8305 0.7854 -0.0746 -0.0977 0.1461  12  SER A N   
75   C CA  . SER A 12  ? 1.1081 0.7958 0.7633 -0.0710 -0.0731 0.1420  12  SER A CA  
76   C C   . SER A 12  ? 1.1556 0.8569 0.8392 -0.0613 -0.0681 0.1436  12  SER A C   
77   O O   . SER A 12  ? 1.0627 0.7671 0.7633 -0.0586 -0.0495 0.1384  12  SER A O   
78   C CB  . SER A 12  ? 1.1615 0.8005 0.7636 -0.0735 -0.0662 0.1453  12  SER A CB  
79   O OG  . SER A 12  ? 1.3557 0.9781 0.9283 -0.0819 -0.0688 0.1428  12  SER A OG  
80   N N   . ALA A 13  ? 1.1555 0.8641 0.8446 -0.0558 -0.0850 0.1507  13  ALA A N   
81   C CA  . ALA A 13  ? 0.9135 0.6315 0.6258 -0.0456 -0.0817 0.1527  13  ALA A CA  
82   C C   . ALA A 13  ? 0.9184 0.6791 0.6796 -0.0405 -0.0818 0.1481  13  ALA A C   
83   O O   . ALA A 13  ? 1.0004 0.7717 0.7819 -0.0310 -0.0829 0.1503  13  ALA A O   
84   C CB  . ALA A 13  ? 0.9273 0.6339 0.6236 -0.0402 -0.0994 0.1629  13  ALA A CB  
85   N N   . LYS A 14  ? 0.9912 0.7741 0.7694 -0.0460 -0.0803 0.1420  14  LYS A N   
86   C CA  . LYS A 14  ? 0.9446 0.7658 0.7658 -0.0410 -0.0793 0.1375  14  LYS A CA  
87   C C   . LYS A 14  ? 0.8579 0.6857 0.6918 -0.0444 -0.0621 0.1274  14  LYS A C   
88   O O   . LYS A 14  ? 0.8442 0.7019 0.7095 -0.0414 -0.0612 0.1229  14  LYS A O   
89   C CB  . LYS A 14  ? 0.9214 0.7711 0.7585 -0.0430 -0.0974 0.1414  14  LYS A CB  
90   C CG  . LYS A 14  ? 0.9674 0.8221 0.8061 -0.0370 -0.1157 0.1518  14  LYS A CG  
91   C CD  . LYS A 14  ? 1.0264 0.9145 0.8886 -0.0393 -0.1323 0.1561  14  LYS A CD  
92   C CE  . LYS A 14  ? 1.1538 1.0517 1.0241 -0.0321 -0.1506 0.1672  14  LYS A CE  
93   N NZ  . LYS A 14  ? 1.2250 1.0879 1.0548 -0.0359 -0.1617 0.1734  14  LYS A NZ  
94   N N   . VAL A 15  ? 0.8058 0.6066 0.6163 -0.0498 -0.0483 0.1242  15  VAL A N   
95   C CA  . VAL A 15  ? 0.8858 0.6922 0.7083 -0.0529 -0.0323 0.1154  15  VAL A CA  
96   C C   . VAL A 15  ? 0.8385 0.6441 0.6796 -0.0468 -0.0194 0.1120  15  VAL A C   
97   O O   . VAL A 15  ? 0.8219 0.6012 0.6462 -0.0467 -0.0106 0.1146  15  VAL A O   
98   C CB  . VAL A 15  ? 0.9460 0.7249 0.7357 -0.0613 -0.0231 0.1144  15  VAL A CB  
99   C CG1 . VAL A 15  ? 0.8035 0.5900 0.6087 -0.0633 -0.0065 0.1059  15  VAL A CG1 
100  C CG2 . VAL A 15  ? 0.8386 0.6146 0.6070 -0.0679 -0.0378 0.1174  15  VAL A CG2 
101  N N   . ILE A 16  ? 0.7531 0.5863 0.6279 -0.0420 -0.0183 0.1062  16  ILE A N   
102  C CA  . ILE A 16  ? 0.8322 0.6644 0.7252 -0.0369 -0.0080 0.1020  16  ILE A CA  
103  C C   . ILE A 16  ? 0.7798 0.6060 0.6766 -0.0424 0.0081  0.0952  16  ILE A C   
104  O O   . ILE A 16  ? 0.7913 0.6098 0.6986 -0.0409 0.0177  0.0928  16  ILE A O   
105  C CB  . ILE A 16  ? 0.7692 0.6295 0.6932 -0.0282 -0.0140 0.0985  16  ILE A CB  
106  C CG1 . ILE A 16  ? 0.6134 0.4989 0.5540 -0.0304 -0.0139 0.0922  16  ILE A CG1 
107  C CG2 . ILE A 16  ? 0.7683 0.6360 0.6920 -0.0214 -0.0286 0.1063  16  ILE A CG2 
108  C CD1 . ILE A 16  ? 0.6134 0.5249 0.5817 -0.0211 -0.0181 0.0889  16  ILE A CD1 
109  N N   . GLN A 17  ? 0.7591 0.5886 0.6486 -0.0487 0.0109  0.0925  17  GLN A N   
110  C CA  . GLN A 17  ? 0.7687 0.5930 0.6617 -0.0531 0.0263  0.0871  17  GLN A CA  
111  C C   . GLN A 17  ? 0.7535 0.5677 0.6217 -0.0599 0.0282  0.0880  17  GLN A C   
112  O O   . GLN A 17  ? 0.7633 0.5895 0.6278 -0.0615 0.0170  0.0882  17  GLN A O   
113  C CB  . GLN A 17  ? 0.7432 0.5935 0.6692 -0.0502 0.0282  0.0786  17  GLN A CB  
114  C CG  . GLN A 17  ? 0.7354 0.5844 0.6677 -0.0545 0.0421  0.0731  17  GLN A CG  
115  C CD  . GLN A 17  ? 0.7348 0.6085 0.6972 -0.0513 0.0418  0.0648  17  GLN A CD  
116  O OE1 . GLN A 17  ? 0.8624 0.7503 0.8416 -0.0453 0.0338  0.0626  17  GLN A OE1 
117  N NE2 . GLN A 17  ? 0.6653 0.5428 0.6330 -0.0546 0.0505  0.0602  17  GLN A NE2 
118  N N   . GLY A 18  ? 0.7297 0.5212 0.5811 -0.0637 0.0428  0.0888  18  GLY A N   
119  C CA  . GLY A 18  ? 0.8000 0.5765 0.6238 -0.0691 0.0469  0.0894  18  GLY A CA  
120  C C   . GLY A 18  ? 0.9505 0.6952 0.7331 -0.0712 0.0437  0.0971  18  GLY A C   
121  O O   . GLY A 18  ? 1.0141 0.7453 0.7887 -0.0686 0.0419  0.1026  18  GLY A O   
122  N N   . SER A 19  ? 0.9858 0.7163 0.7395 -0.0760 0.0425  0.0975  19  SER A N   
123  C CA  . SER A 19  ? 1.0356 0.7318 0.7439 -0.0784 0.0385  0.1042  19  SER A CA  
124  C C   . SER A 19  ? 1.1628 0.8548 0.8485 -0.0840 0.0271  0.1032  19  SER A C   
125  O O   . SER A 19  ? 1.2448 0.9383 0.9299 -0.0865 0.0356  0.0982  19  SER A O   
126  C CB  . SER A 19  ? 1.1202 0.7841 0.8046 -0.0781 0.0598  0.1068  19  SER A CB  
127  O OG  . SER A 19  ? 1.2988 0.9259 0.9339 -0.0799 0.0564  0.1129  19  SER A OG  
128  N N   . LEU A 20  ? 1.1730 0.8594 0.8405 -0.0861 0.0073  0.1082  20  LEU A N   
129  C CA  . LEU A 20  ? 1.2671 0.9454 0.9099 -0.0929 -0.0058 0.1081  20  LEU A CA  
130  C C   . LEU A 20  ? 1.3757 1.0118 0.9701 -0.0959 0.0053  0.1084  20  LEU A C   
131  O O   . LEU A 20  ? 1.3649 0.9919 0.9391 -0.1016 -0.0001 0.1061  20  LEU A O   
132  C CB  . LEU A 20  ? 1.1448 0.8252 0.7795 -0.0948 -0.0306 0.1145  20  LEU A CB  
133  C CG  . LEU A 20  ? 1.1579 0.8800 0.8383 -0.0912 -0.0430 0.1152  20  LEU A CG  
134  C CD1 . LEU A 20  ? 1.1665 0.8891 0.8376 -0.0928 -0.0673 0.1229  20  LEU A CD1 
135  C CD2 . LEU A 20  ? 1.0478 0.8023 0.7600 -0.0934 -0.0426 0.1090  20  LEU A CD2 
136  N N   . ASP A 21  ? 1.3534 0.9624 0.9280 -0.0920 0.0214  0.1116  21  ASP A N   
137  C CA  . ASP A 21  ? 1.5426 1.1097 1.0698 -0.0931 0.0350  0.1125  21  ASP A CA  
138  C C   . ASP A 21  ? 1.6006 1.1741 1.1398 -0.0928 0.0541  0.1061  21  ASP A C   
139  O O   . ASP A 21  ? 1.6606 1.2085 1.1648 -0.0951 0.0588  0.1046  21  ASP A O   
140  C CB  . ASP A 21  ? 1.6963 1.2337 1.2014 -0.0882 0.0488  0.1187  21  ASP A CB  
141  C CG  . ASP A 21  ? 1.7308 1.2649 1.2296 -0.0869 0.0309  0.1252  21  ASP A CG  
142  O OD1 . ASP A 21  ? 1.6073 1.1462 1.0979 -0.0907 0.0067  0.1264  21  ASP A OD1 
143  O OD2 . ASP A 21  ? 1.7781 1.3049 1.2813 -0.0822 0.0407  0.1296  21  ASP A OD2 
144  N N   . SER A 22  ? 1.4602 1.0665 1.0474 -0.0895 0.0646  0.1023  22  SER A N   
145  C CA  . SER A 22  ? 1.4357 1.0515 1.0391 -0.0884 0.0818  0.0966  22  SER A CA  
146  C C   . SER A 22  ? 1.4784 1.1109 1.0878 -0.0926 0.0703  0.0910  22  SER A C   
147  O O   . SER A 22  ? 1.5403 1.1754 1.1551 -0.0917 0.0832  0.0864  22  SER A O   
148  C CB  . SER A 22  ? 1.4195 1.0653 1.0729 -0.0842 0.0932  0.0942  22  SER A CB  
149  O OG  . SER A 22  ? 1.3845 1.0641 1.0731 -0.0841 0.0764  0.0922  22  SER A OG  
150  N N   . LEU A 23  ? 1.3571 1.0011 0.9669 -0.0970 0.0470  0.0918  23  LEU A N   
151  C CA  . LEU A 23  ? 1.3809 1.0404 0.9971 -0.1020 0.0359  0.0874  23  LEU A CA  
152  C C   . LEU A 23  ? 1.4522 1.0741 1.0173 -0.1073 0.0334  0.0878  23  LEU A C   
153  O O   . LEU A 23  ? 1.5322 1.1193 1.0557 -0.1084 0.0300  0.0925  23  LEU A O   
154  C CB  . LEU A 23  ? 1.2632 0.9511 0.9028 -0.1049 0.0127  0.0892  23  LEU A CB  
155  C CG  . LEU A 23  ? 1.1413 0.8689 0.8320 -0.0994 0.0128  0.0877  23  LEU A CG  
156  C CD1 . LEU A 23  ? 1.1263 0.8785 0.8350 -0.1015 -0.0094 0.0908  23  LEU A CD1 
157  C CD2 . LEU A 23  ? 1.0429 0.7927 0.7632 -0.0970 0.0253  0.0805  23  LEU A CD2 
158  N N   . PRO A 24  ? 1.4071 1.0328 0.9720 -0.1102 0.0348  0.0828  24  PRO A N   
159  C CA  . PRO A 24  ? 1.5142 1.1032 1.0295 -0.1160 0.0299  0.0825  24  PRO A CA  
160  C C   . PRO A 24  ? 1.5180 1.0980 1.0124 -0.1239 0.0031  0.0869  24  PRO A C   
161  O O   . PRO A 24  ? 1.4377 1.0457 0.9613 -0.1250 -0.0120 0.0900  24  PRO A O   
162  C CB  . PRO A 24  ? 1.5322 1.1376 1.0638 -0.1179 0.0327  0.0764  24  PRO A CB  
163  C CG  . PRO A 24  ? 1.4615 1.1010 1.0414 -0.1103 0.0484  0.0732  24  PRO A CG  
164  C CD  . PRO A 24  ? 1.3259 0.9864 0.9331 -0.1079 0.0419  0.0769  24  PRO A CD  
165  N N   . GLN A 25  ? 1.6757 1.2150 1.1181 -0.1294 -0.0032 0.0874  25  GLN A N   
166  C CA  . GLN A 25  ? 1.7358 1.2610 1.1531 -0.1378 -0.0301 0.0918  25  GLN A CA  
167  C C   . GLN A 25  ? 1.6268 1.1915 1.0823 -0.1454 -0.0511 0.0918  25  GLN A C   
168  O O   . GLN A 25  ? 1.5768 1.1681 1.0601 -0.1461 -0.0663 0.0964  25  GLN A O   
169  C CB  . GLN A 25  ? 1.9712 1.4425 1.3233 -0.1426 -0.0329 0.0911  25  GLN A CB  
170  C CG  . GLN A 25  ? 2.0522 1.5054 1.3749 -0.1525 -0.0632 0.0955  25  GLN A CG  
171  C CD  . GLN A 25  ? 2.2505 1.6436 1.5021 -0.1564 -0.0657 0.0945  25  GLN A CD  
172  O OE1 . GLN A 25  ? 2.4320 1.7929 1.6516 -0.1493 -0.0421 0.0919  25  GLN A OE1 
173  N NE2 . GLN A 25  ? 2.2860 1.6632 1.5124 -0.1674 -0.0945 0.0969  25  GLN A NE2 
174  N N   . GLU A 26  ? 1.7554 1.3239 1.2129 -0.1507 -0.0513 0.0872  26  GLU A N   
175  C CA  . GLU A 26  ? 1.7488 1.3530 1.2412 -0.1586 -0.0698 0.0879  26  GLU A CA  
176  C C   . GLU A 26  ? 1.5661 1.2221 1.1196 -0.1521 -0.0654 0.0881  26  GLU A C   
177  O O   . GLU A 26  ? 1.5010 1.1892 1.0862 -0.1567 -0.0819 0.0913  26  GLU A O   
178  C CB  . GLU A 26  ? 1.8599 1.4555 1.3413 -0.1646 -0.0674 0.0828  26  GLU A CB  
179  C CG  . GLU A 26  ? 1.9917 1.5370 1.4132 -0.1734 -0.0783 0.0827  26  GLU A CG  
180  C CD  . GLU A 26  ? 2.0158 1.5605 1.4305 -0.1851 -0.1094 0.0887  26  GLU A CD  
181  O OE1 . GLU A 26  ? 1.9095 1.4980 1.3715 -0.1873 -0.1220 0.0928  26  GLU A OE1 
182  O OE2 . GLU A 26  ? 2.0781 1.5780 1.4399 -0.1918 -0.1214 0.0896  26  GLU A OE2 
183  N N   . VAL A 27  ? 1.4675 1.1317 1.0380 -0.1416 -0.0435 0.0851  27  VAL A N   
184  C CA  . VAL A 27  ? 1.2916 1.0005 0.9159 -0.1350 -0.0398 0.0847  27  VAL A CA  
185  C C   . VAL A 27  ? 1.2892 1.0089 0.9253 -0.1327 -0.0519 0.0911  27  VAL A C   
186  O O   . VAL A 27  ? 1.2117 0.9680 0.8870 -0.1313 -0.0613 0.0933  27  VAL A O   
187  C CB  . VAL A 27  ? 1.3053 1.0182 0.9441 -0.1255 -0.0146 0.0794  27  VAL A CB  
188  C CG1 . VAL A 27  ? 1.0914 0.8461 0.7816 -0.1187 -0.0123 0.0786  27  VAL A CG1 
189  C CG2 . VAL A 27  ? 1.1743 0.8790 0.8040 -0.1267 -0.0034 0.0736  27  VAL A CG2 
190  N N   . ARG A 28  ? 1.2236 0.9106 0.8251 -0.1312 -0.0512 0.0945  28  ARG A N   
191  C CA  . ARG A 28  ? 1.1436 0.8375 0.7531 -0.1283 -0.0627 0.1010  28  ARG A CA  
192  C C   . ARG A 28  ? 1.2034 0.9070 0.8141 -0.1363 -0.0902 0.1067  28  ARG A C   
193  O O   . ARG A 28  ? 1.2363 0.9697 0.8796 -0.1335 -0.1012 0.1113  28  ARG A O   
194  C CB  . ARG A 28  ? 1.2533 0.9064 0.8216 -0.1248 -0.0546 0.1038  28  ARG A CB  
195  C CG  . ARG A 28  ? 1.2969 0.9524 0.8684 -0.1213 -0.0668 0.1109  28  ARG A CG  
196  C CD  . ARG A 28  ? 1.4364 1.0518 0.9690 -0.1167 -0.0552 0.1137  28  ARG A CD  
197  N NE  . ARG A 28  ? 1.4033 1.0199 0.9383 -0.1128 -0.0669 0.1208  28  ARG A NE  
198  C CZ  . ARG A 28  ? 1.3400 0.9264 0.8473 -0.1078 -0.0585 0.1248  28  ARG A CZ  
199  N NH1 . ARG A 28  ? 1.4054 0.9586 0.8813 -0.1059 -0.0372 0.1229  28  ARG A NH1 
200  N NH2 . ARG A 28  ? 1.3861 0.9755 0.8973 -0.1040 -0.0709 0.1314  28  ARG A NH2 
201  N N   . LYS A 29  ? 1.3167 0.9950 0.8926 -0.1463 -0.1019 0.1068  29  LYS A N   
202  C CA  . LYS A 29  ? 1.2854 0.9735 0.8646 -0.1557 -0.1296 0.1127  29  LYS A CA  
203  C C   . LYS A 29  ? 1.1335 0.8727 0.7683 -0.1565 -0.1351 0.1136  29  LYS A C   
204  O O   . LYS A 29  ? 1.0541 0.8180 0.7132 -0.1585 -0.1538 0.1205  29  LYS A O   
205  C CB  . LYS A 29  ? 1.3770 1.0280 0.9098 -0.1673 -0.1402 0.1114  29  LYS A CB  
206  C CG  . LYS A 29  ? 1.4365 1.0335 0.9083 -0.1670 -0.1401 0.1123  29  LYS A CG  
207  C CD  . LYS A 29  ? 1.6439 1.2035 1.0688 -0.1791 -0.1551 0.1113  29  LYS A CD  
208  C CE  . LYS A 29  ? 1.8460 1.3493 1.2064 -0.1781 -0.1573 0.1129  29  LYS A CE  
209  N NZ  . LYS A 29  ? 1.8098 1.2729 1.1206 -0.1902 -0.1747 0.1118  29  LYS A NZ  
210  N N   . PHE A 30  ? 1.1959 0.9514 0.8514 -0.1543 -0.1186 0.1071  30  PHE A N   
211  C CA  . PHE A 30  ? 1.0794 0.8809 0.7847 -0.1540 -0.1214 0.1077  30  PHE A CA  
212  C C   . PHE A 30  ? 1.0285 0.8626 0.7733 -0.1429 -0.1187 0.1107  30  PHE A C   
213  O O   . PHE A 30  ? 0.9811 0.8515 0.7636 -0.1425 -0.1281 0.1151  30  PHE A O   
214  C CB  . PHE A 30  ? 1.0512 0.8583 0.7648 -0.1530 -0.1037 0.0998  30  PHE A CB  
215  C CG  . PHE A 30  ? 0.9925 0.8445 0.7549 -0.1504 -0.1028 0.1000  30  PHE A CG  
216  C CD1 . PHE A 30  ? 0.9950 0.8689 0.7765 -0.1588 -0.1202 0.1058  30  PHE A CD1 
217  C CD2 . PHE A 30  ? 0.9943 0.8655 0.7830 -0.1397 -0.0845 0.0945  30  PHE A CD2 
218  C CE1 . PHE A 30  ? 0.9093 0.8231 0.7341 -0.1556 -0.1174 0.1067  30  PHE A CE1 
219  C CE2 . PHE A 30  ? 0.9241 0.8331 0.7532 -0.1365 -0.0832 0.0945  30  PHE A CE2 
220  C CZ  . PHE A 30  ? 0.9231 0.8531 0.7696 -0.1440 -0.0986 0.1008  30  PHE A CZ  
221  N N   . VAL A 31  ? 1.0380 0.8585 0.7743 -0.1337 -0.1054 0.1088  31  VAL A N   
222  C CA  . VAL A 31  ? 1.0215 0.8682 0.7917 -0.1229 -0.1022 0.1110  31  VAL A CA  
223  C C   . VAL A 31  ? 1.0580 0.9070 0.8278 -0.1229 -0.1218 0.1202  31  VAL A C   
224  O O   . VAL A 31  ? 0.9865 0.8695 0.7920 -0.1198 -0.1315 0.1253  31  VAL A O   
225  C CB  . VAL A 31  ? 1.0573 0.8883 0.8203 -0.1141 -0.0812 0.1059  31  VAL A CB  
226  C CG1 . VAL A 31  ? 0.9574 0.8111 0.7520 -0.1035 -0.0791 0.1080  31  VAL A CG1 
227  C CG2 . VAL A 31  ? 0.9606 0.7936 0.7293 -0.1134 -0.0631 0.0974  31  VAL A CG2 
228  N N   . GLU A 32  ? 1.1089 0.9210 0.8374 -0.1256 -0.1275 0.1230  32  GLU A N   
229  C CA  . GLU A 32  ? 1.1443 0.9555 0.8690 -0.1251 -0.1472 0.1320  32  GLU A CA  
230  C C   . GLU A 32  ? 1.1488 0.9802 0.8878 -0.1343 -0.1711 0.1384  32  GLU A C   
231  O O   . GLU A 32  ? 1.1401 0.9879 0.8958 -0.1320 -0.1877 0.1467  32  GLU A O   
232  C CB  . GLU A 32  ? 1.1919 0.9548 0.8633 -0.1267 -0.1488 0.1336  32  GLU A CB  
233  C CG  . GLU A 32  ? 1.3024 1.0495 0.9659 -0.1162 -0.1296 0.1318  32  GLU A CG  
234  C CD  . GLU A 32  ? 1.3776 1.0782 0.9892 -0.1168 -0.1327 0.1355  32  GLU A CD  
235  O OE1 . GLU A 32  ? 1.4443 1.1184 1.0188 -0.1257 -0.1460 0.1369  32  GLU A OE1 
236  O OE2 . GLU A 32  ? 1.3270 1.0158 0.9335 -0.1084 -0.1220 0.1371  32  GLU A OE2 
237  N N   . GLY A 33  ? 1.0932 0.9240 0.8275 -0.1448 -0.1735 0.1351  33  GLY A N   
238  C CA  . GLY A 33  ? 0.9949 0.8467 0.7470 -0.1549 -0.1959 0.1416  33  GLY A CA  
239  C C   . GLY A 33  ? 0.9346 0.8383 0.7447 -0.1485 -0.1972 0.1464  33  GLY A C   
240  O O   . GLY A 33  ? 0.9734 0.8978 0.8045 -0.1491 -0.2158 0.1558  33  GLY A O   
241  N N   . ASN A 34  ? 0.8858 0.8106 0.7221 -0.1417 -0.1773 0.1402  34  ASN A N   
242  C CA  . ASN A 34  ? 0.7607 0.7318 0.6486 -0.1338 -0.1754 0.1441  34  ASN A CA  
243  C C   . ASN A 34  ? 0.8953 0.8763 0.7986 -0.1194 -0.1722 0.1472  34  ASN A C   
244  O O   . ASN A 34  ? 0.9601 0.9765 0.9022 -0.1127 -0.1769 0.1536  34  ASN A O   
245  C CB  . ASN A 34  ? 0.9176 0.9038 0.8236 -0.1307 -0.1558 0.1361  34  ASN A CB  
246  C CG  . ASN A 34  ? 0.8224 0.7991 0.7143 -0.1442 -0.1581 0.1331  34  ASN A CG  
247  O OD1 . ASN A 34  ? 0.6991 0.7010 0.6159 -0.1506 -0.1666 0.1380  34  ASN A OD1 
248  N ND2 . ASN A 34  ? 0.9203 0.8596 0.7721 -0.1482 -0.1498 0.1257  34  ASN A ND2 
249  N N   . ALA A 35  ? 0.8731 0.8232 0.7470 -0.1141 -0.1634 0.1432  35  ALA A N   
250  C CA  . ALA A 35  ? 0.9471 0.9019 0.8316 -0.1013 -0.1616 0.1467  35  ALA A CA  
251  C C   . ALA A 35  ? 0.9722 0.9352 0.8621 -0.1020 -0.1848 0.1582  35  ALA A C   
252  O O   . ALA A 35  ? 1.0051 0.9934 0.9254 -0.0913 -0.1875 0.1640  35  ALA A O   
253  C CB  . ALA A 35  ? 1.0206 0.9373 0.8698 -0.0977 -0.1484 0.1413  35  ALA A CB  
254  N N   . GLN A 36  ? 1.0653 1.0059 0.9252 -0.1141 -0.2023 0.1619  36  GLN A N   
255  C CA  . GLN A 36  ? 1.0865 1.0357 0.9525 -0.1162 -0.2274 0.1733  36  GLN A CA  
256  C C   . GLN A 36  ? 1.0286 1.0256 0.9447 -0.1178 -0.2375 0.1804  36  GLN A C   
257  O O   . GLN A 36  ? 1.0096 1.0288 0.9500 -0.1131 -0.2527 0.1908  36  GLN A O   
258  C CB  . GLN A 36  ? 1.2054 1.1167 1.0247 -0.1298 -0.2450 0.1747  36  GLN A CB  
259  C CG  . GLN A 36  ? 1.3241 1.1854 1.0903 -0.1283 -0.2338 0.1686  36  GLN A CG  
260  C CD  . GLN A 36  ? 1.4818 1.3023 1.1975 -0.1413 -0.2502 0.1693  36  GLN A CD  
261  O OE1 . GLN A 36  ? 1.5629 1.3920 1.2835 -0.1525 -0.2724 0.1744  36  GLN A OE1 
262  N NE2 . GLN A 36  ? 1.5518 1.3263 1.2181 -0.1399 -0.2392 0.1646  36  GLN A NE2 
263  N N   . LEU A 37  ? 0.9676 0.9810 0.9003 -0.1237 -0.2288 0.1758  37  LEU A N   
264  C CA  . LEU A 37  ? 0.9046 0.9629 0.8849 -0.1257 -0.2361 0.1831  37  LEU A CA  
265  C C   . LEU A 37  ? 0.9415 1.0345 0.9632 -0.1090 -0.2199 0.1836  37  LEU A C   
266  O O   . LEU A 37  ? 0.7400 0.8681 0.8003 -0.1033 -0.2283 0.1936  37  LEU A O   
267  C CB  . LEU A 37  ? 0.9688 1.0274 0.9468 -0.1396 -0.2338 0.1787  37  LEU A CB  
268  C CG  . LEU A 37  ? 0.9766 1.0805 1.0033 -0.1428 -0.2378 0.1859  37  LEU A CG  
269  C CD1 . LEU A 37  ? 0.8035 0.9274 0.8517 -0.1487 -0.2643 0.1998  37  LEU A CD1 
270  C CD2 . LEU A 37  ? 0.9510 1.0484 0.9692 -0.1561 -0.2332 0.1803  37  LEU A CD2 
271  N N   . CYS A 38  ? 0.9198 1.0031 0.9342 -0.1008 -0.1970 0.1730  38  CYS A N   
272  C CA  . CYS A 38  ? 0.8335 0.9442 0.8815 -0.0850 -0.1814 0.1719  38  CYS A CA  
273  C C   . CYS A 38  ? 0.7889 0.8930 0.8354 -0.0706 -0.1797 0.1740  38  CYS A C   
274  O O   . CYS A 38  ? 0.7329 0.8628 0.8105 -0.0566 -0.1730 0.1767  38  CYS A O   
275  C CB  . CYS A 38  ? 0.8643 0.9678 0.9063 -0.0830 -0.1593 0.1596  38  CYS A CB  
276  S SG  . CYS A 38  ? 0.7802 0.8918 0.8254 -0.0976 -0.1582 0.1567  38  CYS A SG  
277  N N   . GLN A 39  ? 0.7808 0.8493 0.7902 -0.0731 -0.1851 0.1730  39  GLN A N   
278  C CA  . GLN A 39  ? 0.9681 1.0256 0.9717 -0.0604 -0.1841 0.1754  39  GLN A CA  
279  C C   . GLN A 39  ? 0.9039 0.9663 0.9207 -0.0468 -0.1625 0.1678  39  GLN A C   
280  O O   . GLN A 39  ? 0.8642 0.9511 0.9107 -0.0335 -0.1605 0.1720  39  GLN A O   
281  C CB  . GLN A 39  ? 0.8537 0.9366 0.8835 -0.0544 -0.2020 0.1887  39  GLN A CB  
282  C CG  . GLN A 39  ? 0.9088 0.9779 0.9184 -0.0660 -0.2265 0.1967  39  GLN A CG  
283  C CD  . GLN A 39  ? 0.9919 1.0832 1.0260 -0.0578 -0.2441 0.2101  39  GLN A CD  
284  O OE1 . GLN A 39  ? 0.9407 1.0655 1.0142 -0.0447 -0.2384 0.2146  39  GLN A OE1 
285  N NE2 . GLN A 39  ? 1.0543 1.1259 1.0641 -0.0645 -0.2655 0.2167  39  GLN A NE2 
286  N N   . PRO A 40  ? 0.8971 0.9363 0.8926 -0.0493 -0.1466 0.1568  40  PRO A N   
287  C CA  . PRO A 40  ? 0.8903 0.9305 0.8962 -0.0373 -0.1283 0.1494  40  PRO A CA  
288  C C   . PRO A 40  ? 0.8799 0.8970 0.8702 -0.0288 -0.1265 0.1506  40  PRO A C   
289  O O   . PRO A 40  ? 0.9109 0.9011 0.8718 -0.0339 -0.1342 0.1539  40  PRO A O   
290  C CB  . PRO A 40  ? 0.7882 0.8121 0.7774 -0.0453 -0.1143 0.1383  40  PRO A CB  
291  C CG  . PRO A 40  ? 0.7879 0.7848 0.7425 -0.0586 -0.1232 0.1398  40  PRO A CG  
292  C CD  . PRO A 40  ? 0.9101 0.9221 0.8728 -0.0631 -0.1445 0.1508  40  PRO A CD  
293  N N   . GLU A 41  ? 0.8884 0.9141 0.8968 -0.0154 -0.1161 0.1478  41  GLU A N   
294  C CA  . GLU A 41  ? 0.8635 0.8662 0.8582 -0.0070 -0.1129 0.1484  41  GLU A CA  
295  C C   . GLU A 41  ? 0.8635 0.8313 0.8283 -0.0139 -0.1012 0.1405  41  GLU A C   
296  O O   . GLU A 41  ? 0.9179 0.8577 0.8580 -0.0141 -0.1026 0.1435  41  GLU A O   
297  C CB  . GLU A 41  ? 0.8409 0.8590 0.8609 0.0088  -0.1047 0.1467  41  GLU A CB  
298  C CG  . GLU A 41  ? 0.8043 0.8021 0.8142 0.0190  -0.1046 0.1497  41  GLU A CG  
299  C CD  . GLU A 41  ? 0.9775 0.9823 0.9901 0.0240  -0.1213 0.1624  41  GLU A CD  
300  O OE1 . GLU A 41  ? 1.1113 1.1457 1.1454 0.0236  -0.1316 0.1691  41  GLU A OE1 
301  O OE2 . GLU A 41  ? 1.0064 0.9872 1.0005 0.0283  -0.1243 0.1663  41  GLU A OE2 
302  N N   . TYR A 42  ? 0.7770 0.7464 0.7441 -0.0191 -0.0891 0.1312  42  TYR A N   
303  C CA  . TYR A 42  ? 0.8574 0.7978 0.8012 -0.0254 -0.0765 0.1242  42  TYR A CA  
304  C C   . TYR A 42  ? 0.7851 0.7282 0.7238 -0.0362 -0.0724 0.1187  42  TYR A C   
305  O O   . TYR A 42  ? 0.7789 0.7474 0.7356 -0.0378 -0.0769 0.1187  42  TYR A O   
306  C CB  . TYR A 42  ? 0.7381 0.6745 0.6933 -0.0173 -0.0624 0.1171  42  TYR A CB  
307  C CG  . TYR A 42  ? 0.7834 0.7225 0.7497 -0.0045 -0.0658 0.1214  42  TYR A CG  
308  C CD1 . TYR A 42  ? 0.7631 0.6775 0.7099 -0.0025 -0.0690 0.1273  42  TYR A CD1 
309  C CD2 . TYR A 42  ? 0.7289 0.6931 0.7231 0.0063  -0.0652 0.1198  42  TYR A CD2 
310  C CE1 . TYR A 42  ? 0.7738 0.6889 0.7294 0.0099  -0.0721 0.1314  42  TYR A CE1 
311  C CE2 . TYR A 42  ? 0.6789 0.6434 0.6814 0.0192  -0.0676 0.1237  42  TYR A CE2 
312  C CZ  . TYR A 42  ? 0.7943 0.7344 0.7779 0.0209  -0.0713 0.1295  42  TYR A CZ  
313  O OH  . TYR A 42  ? 0.7514 0.6901 0.7421 0.0344  -0.0736 0.1335  42  TYR A OH  
314  N N   . ILE A 43  ? 0.6988 0.6146 0.6125 -0.0432 -0.0628 0.1145  43  ILE A N   
315  C CA  . ILE A 43  ? 0.7986 0.7119 0.7043 -0.0522 -0.0564 0.1087  43  ILE A CA  
316  C C   . ILE A 43  ? 0.7826 0.6853 0.6901 -0.0509 -0.0384 0.1004  43  ILE A C   
317  O O   . ILE A 43  ? 0.7608 0.6406 0.6549 -0.0497 -0.0311 0.1010  43  ILE A O   
318  C CB  . ILE A 43  ? 0.7578 0.6459 0.6277 -0.0625 -0.0629 0.1126  43  ILE A CB  
319  C CG1 . ILE A 43  ? 0.6172 0.5175 0.4881 -0.0652 -0.0834 0.1209  43  ILE A CG1 
320  C CG2 . ILE A 43  ? 0.6577 0.5395 0.5172 -0.0706 -0.0541 0.1061  43  ILE A CG2 
321  C CD1 . ILE A 43  ? 0.7839 0.6571 0.6170 -0.0756 -0.0929 0.1246  43  ILE A CD1 
322  N N   . HIS A 44  ? 0.5796 0.4991 0.5044 -0.0514 -0.0315 0.0933  44  HIS A N   
323  C CA  . HIS A 44  ? 0.7284 0.6433 0.6612 -0.0498 -0.0163 0.0853  44  HIS A CA  
324  C C   . HIS A 44  ? 0.5717 0.4830 0.4955 -0.0572 -0.0093 0.0805  44  HIS A C   
325  O O   . HIS A 44  ? 0.6325 0.5636 0.5696 -0.0578 -0.0112 0.0773  44  HIS A O   
326  C CB  . HIS A 44  ? 0.6676 0.6055 0.6311 -0.0406 -0.0150 0.0806  44  HIS A CB  
327  C CG  . HIS A 44  ? 0.7301 0.6627 0.7034 -0.0390 -0.0024 0.0728  44  HIS A CG  
328  N ND1 . HIS A 44  ? 0.7096 0.6497 0.6906 -0.0415 0.0048  0.0658  44  HIS A ND1 
329  C CD2 . HIS A 44  ? 0.7801 0.7005 0.7577 -0.0354 0.0034  0.0714  44  HIS A CD2 
330  C CE1 . HIS A 44  ? 0.5956 0.5299 0.5868 -0.0396 0.0136  0.0605  44  HIS A CE1 
331  N NE2 . HIS A 44  ? 0.7818 0.7040 0.7715 -0.0364 0.0130  0.0636  44  HIS A NE2 
332  N N   . ILE A 45  ? 0.5631 0.4482 0.4636 -0.0623 -0.0001 0.0805  45  ILE A N   
333  C CA  . ILE A 45  ? 0.6845 0.5627 0.5746 -0.0680 0.0087  0.0762  45  ILE A CA  
334  C C   . ILE A 45  ? 0.5926 0.4805 0.5059 -0.0643 0.0213  0.0687  45  ILE A C   
335  O O   . ILE A 45  ? 0.7050 0.5833 0.6235 -0.0620 0.0301  0.0680  45  ILE A O   
336  C CB  . ILE A 45  ? 0.7528 0.5972 0.6066 -0.0735 0.0146  0.0798  45  ILE A CB  
337  C CG1 . ILE A 45  ? 0.7315 0.5637 0.5610 -0.0765 -0.0004 0.0875  45  ILE A CG1 
338  C CG2 . ILE A 45  ? 0.6759 0.5123 0.5163 -0.0785 0.0228  0.0759  45  ILE A CG2 
339  C CD1 . ILE A 45  ? 0.8467 0.6415 0.6348 -0.0810 0.0044  0.0913  45  ILE A CD1 
340  N N   . CYS A 46  ? 0.5909 0.4973 0.5184 -0.0642 0.0215  0.0634  46  CYS A N   
341  C CA  . CYS A 46  ? 0.6502 0.5687 0.6017 -0.0600 0.0301  0.0561  46  CYS A CA  
342  C C   . CYS A 46  ? 0.6124 0.5152 0.5563 -0.0631 0.0446  0.0537  46  CYS A C   
343  O O   . CYS A 46  ? 0.6696 0.5561 0.5892 -0.0682 0.0486  0.0558  46  CYS A O   
344  C CB  . CYS A 46  ? 0.4583 0.4006 0.4253 -0.0579 0.0254  0.0518  46  CYS A CB  
345  S SG  . CYS A 46  ? 0.5942 0.5600 0.5783 -0.0515 0.0119  0.0545  46  CYS A SG  
346  N N   . ASP A 47  ? 0.6811 0.5883 0.6462 -0.0599 0.0524  0.0495  47  ASP A N   
347  C CA  . ASP A 47  ? 0.5565 0.4553 0.5237 -0.0617 0.0666  0.0472  47  ASP A CA  
348  C C   . ASP A 47  ? 0.6317 0.5499 0.6254 -0.0583 0.0686  0.0397  47  ASP A C   
349  O O   . ASP A 47  ? 0.6812 0.5962 0.6803 -0.0592 0.0796  0.0379  47  ASP A O   
350  C CB  . ASP A 47  ? 0.5744 0.4570 0.5429 -0.0624 0.0759  0.0507  47  ASP A CB  
351  C CG  . ASP A 47  ? 0.5158 0.4092 0.5109 -0.0585 0.0716  0.0480  47  ASP A CG  
352  O OD1 . ASP A 47  ? 0.5066 0.4188 0.5165 -0.0542 0.0616  0.0435  47  ASP A OD1 
353  O OD2 . ASP A 47  ? 0.5597 0.4411 0.5595 -0.0596 0.0787  0.0506  47  ASP A OD2 
354  N N   . GLY A 48  ? 0.5053 0.4429 0.5151 -0.0538 0.0584  0.0358  48  GLY A N   
355  C CA  . GLY A 48  ? 0.6598 0.6141 0.6906 -0.0500 0.0584  0.0286  48  GLY A CA  
356  C C   . GLY A 48  ? 0.6173 0.5732 0.6714 -0.0483 0.0629  0.0247  48  GLY A C   
357  O O   . GLY A 48  ? 0.6510 0.6188 0.7219 -0.0454 0.0626  0.0187  48  GLY A O   
358  N N   . SER A 49  ? 0.5725 0.5160 0.6281 -0.0501 0.0663  0.0282  49  SER A N   
359  C CA  . SER A 49  ? 0.7717 0.7158 0.8511 -0.0502 0.0703  0.0253  49  SER A CA  
360  C C   . SER A 49  ? 0.8308 0.7866 0.9277 -0.0446 0.0590  0.0191  49  SER A C   
361  O O   . SER A 49  ? 0.8357 0.7961 0.9253 -0.0402 0.0499  0.0189  49  SER A O   
362  C CB  . SER A 49  ? 0.6269 0.5526 0.7017 -0.0542 0.0777  0.0317  49  SER A CB  
363  O OG  . SER A 49  ? 0.6259 0.5453 0.6901 -0.0523 0.0696  0.0347  49  SER A OG  
364  N N   . GLU A 50  ? 0.8439 0.8040 0.9644 -0.0447 0.0595  0.0143  50  GLU A N   
365  C CA  . GLU A 50  ? 0.8538 0.8201 0.9882 -0.0395 0.0485  0.0079  50  GLU A CA  
366  C C   . GLU A 50  ? 0.9132 0.8681 1.0416 -0.0380 0.0440  0.0107  50  GLU A C   
367  O O   . GLU A 50  ? 0.9063 0.8647 1.0333 -0.0312 0.0345  0.0073  50  GLU A O   
368  C CB  . GLU A 50  ? 0.9760 0.9458 1.1364 -0.0415 0.0488  0.0029  50  GLU A CB  
369  C CG  . GLU A 50  ? 1.1023 1.0854 1.2711 -0.0405 0.0505  -0.0010 50  GLU A CG  
370  C CD  . GLU A 50  ? 1.1703 1.1642 1.3377 -0.0329 0.0393  -0.0084 50  GLU A CD  
371  O OE1 . GLU A 50  ? 1.1496 1.1409 1.3136 -0.0281 0.0303  -0.0112 50  GLU A OE1 
372  O OE2 . GLU A 50  ? 1.0670 1.0707 1.2352 -0.0309 0.0401  -0.0111 50  GLU A OE2 
373  N N   . GLU A 51  ? 0.9079 0.8480 1.0317 -0.0435 0.0515  0.0173  51  GLU A N   
374  C CA  . GLU A 51  ? 0.9221 0.8493 1.0381 -0.0418 0.0476  0.0209  51  GLU A CA  
375  C C   . GLU A 51  ? 0.8744 0.8051 0.9710 -0.0362 0.0411  0.0237  51  GLU A C   
376  O O   . GLU A 51  ? 0.8329 0.7620 0.9280 -0.0300 0.0332  0.0232  51  GLU A O   
377  C CB  . GLU A 51  ? 1.0499 0.9593 1.1609 -0.0488 0.0583  0.0286  51  GLU A CB  
378  C CG  . GLU A 51  ? 1.4222 1.3301 1.5560 -0.0551 0.0667  0.0277  51  GLU A CG  
379  C CD  . GLU A 51  ? 1.8072 1.6977 1.9338 -0.0615 0.0805  0.0366  51  GLU A CD  
380  O OE1 . GLU A 51  ? 1.8417 1.7205 1.9419 -0.0611 0.0832  0.0428  51  GLU A OE1 
381  O OE2 . GLU A 51  ? 1.9187 1.8071 2.0662 -0.0670 0.0885  0.0377  51  GLU A OE2 
382  N N   . GLU A 52  ? 0.9167 0.8519 0.9987 -0.0382 0.0440  0.0271  52  GLU A N   
383  C CA  . GLU A 52  ? 0.8104 0.7514 0.8774 -0.0342 0.0368  0.0306  52  GLU A CA  
384  C C   . GLU A 52  ? 0.8001 0.7590 0.8763 -0.0264 0.0287  0.0248  52  GLU A C   
385  O O   . GLU A 52  ? 0.6287 0.5923 0.7017 -0.0200 0.0217  0.0268  52  GLU A O   
386  C CB  . GLU A 52  ? 0.6384 0.5776 0.6873 -0.0397 0.0410  0.0352  52  GLU A CB  
387  C CG  . GLU A 52  ? 0.6713 0.6232 0.7112 -0.0370 0.0327  0.0372  52  GLU A CG  
388  C CD  . GLU A 52  ? 0.6707 0.6167 0.6904 -0.0436 0.0354  0.0416  52  GLU A CD  
389  O OE1 . GLU A 52  ? 0.6374 0.5665 0.6389 -0.0475 0.0369  0.0479  52  GLU A OE1 
390  O OE2 . GLU A 52  ? 0.6949 0.6510 0.7148 -0.0448 0.0359  0.0386  52  GLU A OE2 
391  N N   . TYR A 53  ? 0.7700 0.7387 0.8573 -0.0262 0.0301  0.0181  53  TYR A N   
392  C CA  . TYR A 53  ? 0.6758 0.6592 0.7690 -0.0182 0.0234  0.0126  53  TYR A CA  
393  C C   . TYR A 53  ? 0.8182 0.7975 0.9191 -0.0107 0.0173  0.0087  53  TYR A C   
394  O O   . TYR A 53  ? 0.7792 0.7656 0.8774 -0.0021 0.0119  0.0083  53  TYR A O   
395  C CB  . TYR A 53  ? 0.7414 0.7333 0.8429 -0.0193 0.0258  0.0065  53  TYR A CB  
396  C CG  . TYR A 53  ? 0.7253 0.7304 0.8292 -0.0110 0.0200  0.0012  53  TYR A CG  
397  C CD1 . TYR A 53  ? 0.6519 0.6680 0.7464 -0.0086 0.0187  0.0047  53  TYR A CD1 
398  C CD2 . TYR A 53  ? 0.6621 0.6676 0.7770 -0.0058 0.0157  -0.0068 53  TYR A CD2 
399  C CE1 . TYR A 53  ? 0.5785 0.6059 0.6745 -0.0006 0.0153  0.0008  53  TYR A CE1 
400  C CE2 . TYR A 53  ? 0.6488 0.6634 0.7620 0.0027  0.0111  -0.0114 53  TYR A CE2 
401  C CZ  . TYR A 53  ? 0.6674 0.6931 0.7711 0.0056  0.0119  -0.0073 53  TYR A CZ  
402  O OH  . TYR A 53  ? 0.6234 0.6576 0.7249 0.0145  0.0092  -0.0110 53  TYR A OH  
403  N N   . GLY A 54  ? 0.8438 0.8109 0.9542 -0.0137 0.0184  0.0060  54  GLY A N   
404  C CA  . GLY A 54  ? 0.9070 0.8656 1.0219 -0.0073 0.0119  0.0021  54  GLY A CA  
405  C C   . GLY A 54  ? 1.0055 0.9570 1.1093 -0.0025 0.0097  0.0084  54  GLY A C   
406  O O   . GLY A 54  ? 0.9982 0.9495 1.0999 0.0074  0.0039  0.0062  54  GLY A O   
407  N N   . ARG A 55  ? 1.1582 1.1028 1.2535 -0.0086 0.0143  0.0165  55  ARG A N   
408  C CA  . ARG A 55  ? 1.2019 1.1403 1.2862 -0.0039 0.0112  0.0233  55  ARG A CA  
409  C C   . ARG A 55  ? 1.0963 1.0520 1.1751 0.0028  0.0070  0.0265  55  ARG A C   
410  O O   . ARG A 55  ? 1.0919 1.0478 1.1669 0.0108  0.0025  0.0306  55  ARG A O   
411  C CB  . ARG A 55  ? 1.2038 1.1281 1.2777 -0.0123 0.0167  0.0313  55  ARG A CB  
412  C CG  . ARG A 55  ? 1.3797 1.2964 1.4409 -0.0078 0.0127  0.0392  55  ARG A CG  
413  C CD  . ARG A 55  ? 1.4174 1.3152 1.4658 -0.0158 0.0185  0.0464  55  ARG A CD  
414  N NE  . ARG A 55  ? 1.4440 1.3443 1.4856 -0.0244 0.0249  0.0480  55  ARG A NE  
415  C CZ  . ARG A 55  ? 1.4747 1.3796 1.5014 -0.0262 0.0225  0.0533  55  ARG A CZ  
416  N NH1 . ARG A 55  ? 1.4011 1.3117 1.4213 -0.0205 0.0136  0.0582  55  ARG A NH1 
417  N NH2 . ARG A 55  ? 1.3387 1.2419 1.3571 -0.0337 0.0289  0.0539  55  ARG A NH2 
418  N N   . LEU A 56  ? 0.9854 0.9560 1.0649 -0.0002 0.0086  0.0253  56  LEU A N   
419  C CA  . LEU A 56  ? 0.9249 0.9133 1.0021 0.0050  0.0049  0.0287  56  LEU A CA  
420  C C   . LEU A 56  ? 0.9453 0.9428 1.0298 0.0170  0.0017  0.0236  56  LEU A C   
421  O O   . LEU A 56  ? 0.9110 0.9202 0.9956 0.0249  -0.0011 0.0281  56  LEU A O   
422  C CB  . LEU A 56  ? 0.8411 0.8398 0.9154 -0.0025 0.0079  0.0290  56  LEU A CB  
423  C CG  . LEU A 56  ? 0.6687 0.6858 0.7416 -0.0001 0.0044  0.0337  56  LEU A CG  
424  C CD1 . LEU A 56  ? 0.9044 0.9203 0.9692 -0.0023 -0.0001 0.0435  56  LEU A CD1 
425  C CD2 . LEU A 56  ? 0.7574 0.7816 0.8277 -0.0070 0.0077  0.0316  56  LEU A CD2 
426  N N   . LEU A 57  ? 1.0296 1.0212 1.1200 0.0190  0.0021  0.0146  57  LEU A N   
427  C CA  . LEU A 57  ? 0.9959 0.9914 1.0884 0.0312  -0.0010 0.0090  57  LEU A CA  
428  C C   . LEU A 57  ? 1.0389 1.0231 1.1284 0.0408  -0.0041 0.0105  57  LEU A C   
429  O O   . LEU A 57  ? 1.0611 1.0519 1.1489 0.0531  -0.0054 0.0111  57  LEU A O   
430  C CB  . LEU A 57  ? 0.8840 0.8738 0.9816 0.0300  -0.0018 -0.0013 57  LEU A CB  
431  C CG  . LEU A 57  ? 0.7889 0.7911 0.8892 0.0249  0.0009  -0.0040 57  LEU A CG  
432  C CD1 . LEU A 57  ? 0.7515 0.7469 0.8586 0.0239  -0.0016 -0.0136 57  LEU A CD1 
433  C CD2 . LEU A 57  ? 0.7286 0.7473 0.8248 0.0327  0.0013  -0.0021 57  LEU A CD2 
434  N N   . ALA A 58  ? 1.2135 1.1798 1.3019 0.0359  -0.0045 0.0116  58  ALA A N   
435  C CA  . ALA A 58  ? 1.2005 1.1527 1.2845 0.0450  -0.0075 0.0129  58  ALA A CA  
436  C C   . ALA A 58  ? 1.1481 1.1114 1.2285 0.0530  -0.0082 0.0224  58  ALA A C   
437  O O   . ALA A 58  ? 1.1716 1.1325 1.2496 0.0663  -0.0100 0.0229  58  ALA A O   
438  C CB  . ALA A 58  ? 1.1828 1.1133 1.2659 0.0367  -0.0069 0.0139  58  ALA A CB  
439  N N   . HIS A 59  ? 1.0468 1.0217 1.1268 0.0453  -0.0073 0.0302  59  HIS A N   
440  C CA  . HIS A 59  ? 0.9702 0.9577 1.0498 0.0514  -0.0098 0.0401  59  HIS A CA  
441  C C   . HIS A 59  ? 1.0066 1.0144 1.0928 0.0628  -0.0094 0.0401  59  HIS A C   
442  O O   . HIS A 59  ? 1.0202 1.0322 1.1083 0.0756  -0.0106 0.0445  59  HIS A O   
443  C CB  . HIS A 59  ? 1.0385 1.0327 1.1146 0.0395  -0.0105 0.0475  59  HIS A CB  
444  C CG  . HIS A 59  ? 1.0763 1.0818 1.1528 0.0438  -0.0155 0.0584  59  HIS A CG  
445  N ND1 . HIS A 59  ? 1.0318 1.0531 1.1088 0.0367  -0.0184 0.0650  59  HIS A ND1 
446  C CD2 . HIS A 59  ? 1.0240 1.0271 1.1010 0.0545  -0.0190 0.0642  59  HIS A CD2 
447  C CE1 . HIS A 59  ? 1.0847 1.1144 1.1645 0.0423  -0.0243 0.0746  59  HIS A CE1 
448  N NE2 . HIS A 59  ? 1.1359 1.1555 1.2161 0.0537  -0.0243 0.0745  59  HIS A NE2 
449  N N   . MET A 60  ? 1.0474 1.0676 1.1370 0.0590  -0.0069 0.0357  60  MET A N   
450  C CA  . MET A 60  ? 0.9201 0.9590 1.0151 0.0695  -0.0050 0.0362  60  MET A CA  
451  C C   . MET A 60  ? 0.9303 0.9585 1.0218 0.0849  -0.0040 0.0301  60  MET A C   
452  O O   . MET A 60  ? 0.8530 0.8919 0.9473 0.0983  -0.0020 0.0342  60  MET A O   
453  C CB  . MET A 60  ? 0.8595 0.9091 0.9560 0.0622  -0.0023 0.0319  60  MET A CB  
454  C CG  . MET A 60  ? 0.8304 0.8914 0.9282 0.0489  -0.0031 0.0386  60  MET A CG  
455  S SD  . MET A 60  ? 0.7726 0.8448 0.8707 0.0421  0.0006  0.0339  60  MET A SD  
456  C CE  . MET A 60  ? 0.8435 0.8950 0.9369 0.0370  0.0020  0.0222  60  MET A CE  
457  N N   . GLN A 61  ? 0.9153 0.9217 1.0006 0.0833  -0.0053 0.0205  61  GLN A N   
458  C CA  . GLN A 61  ? 0.9950 0.9864 1.0732 0.0972  -0.0058 0.0137  61  GLN A CA  
459  C C   . GLN A 61  ? 1.0899 1.0719 1.1648 0.1079  -0.0068 0.0195  61  GLN A C   
460  O O   . GLN A 61  ? 1.1151 1.0959 1.1856 0.1242  -0.0047 0.0194  61  GLN A O   
461  C CB  . GLN A 61  ? 1.0076 0.9771 1.0814 0.0909  -0.0092 0.0026  61  GLN A CB  
462  C CG  . GLN A 61  ? 0.9647 0.9150 1.0277 0.1042  -0.0116 -0.0060 61  GLN A CG  
463  C CD  . GLN A 61  ? 1.0480 0.9769 1.1093 0.0962  -0.0173 -0.0165 61  GLN A CD  
464  O OE1 . GLN A 61  ? 1.1332 1.0600 1.2029 0.0815  -0.0182 -0.0159 61  GLN A OE1 
465  N NE2 . GLN A 61  ? 1.1032 1.0156 1.1534 0.1059  -0.0212 -0.0257 61  GLN A NE2 
466  N N   . GLU A 62  ? 1.1314 1.1057 1.2071 0.0999  -0.0092 0.0248  62  GLU A N   
467  C CA  . GLU A 62  ? 1.1592 1.1241 1.2314 0.1098  -0.0106 0.0312  62  GLU A CA  
468  C C   . GLU A 62  ? 1.0704 1.0601 1.1511 0.1180  -0.0094 0.0428  62  GLU A C   
469  O O   . GLU A 62  ? 1.1567 1.1421 1.2363 0.1292  -0.0103 0.0490  62  GLU A O   
470  C CB  . GLU A 62  ? 1.1632 1.1104 1.2320 0.0984  -0.0134 0.0337  62  GLU A CB  
471  C CG  . GLU A 62  ? 1.0766 0.9990 1.1407 0.0907  -0.0144 0.0237  62  GLU A CG  
472  C CD  . GLU A 62  ? 0.9849 0.8918 1.0471 0.0781  -0.0149 0.0275  62  GLU A CD  
473  O OE1 . GLU A 62  ? 0.9496 0.8645 1.0113 0.0744  -0.0148 0.0371  62  GLU A OE1 
474  O OE2 . GLU A 62  ? 0.9738 0.8597 1.0345 0.0717  -0.0155 0.0211  62  GLU A OE2 
475  N N   . GLU A 63  ? 1.0419 1.0571 1.1319 0.1128  -0.0077 0.0464  63  GLU A N   
476  C CA  . GLU A 63  ? 0.9834 1.0253 1.0854 0.1193  -0.0071 0.0577  63  GLU A CA  
477  C C   . GLU A 63  ? 0.9848 1.0420 1.0917 0.1327  -0.0007 0.0567  63  GLU A C   
478  O O   . GLU A 63  ? 0.9823 1.0647 1.1026 0.1380  0.0012  0.0666  63  GLU A O   
479  C CB  . GLU A 63  ? 1.0069 1.0662 1.1160 0.1031  -0.0103 0.0641  63  GLU A CB  
480  C CG  . GLU A 63  ? 1.0751 1.1222 1.1785 0.0928  -0.0162 0.0690  63  GLU A CG  
481  C CD  . GLU A 63  ? 1.1505 1.2045 1.2595 0.1017  -0.0207 0.0806  63  GLU A CD  
482  O OE1 . GLU A 63  ? 1.2439 1.3137 1.3635 0.1163  -0.0183 0.0851  63  GLU A OE1 
483  O OE2 . GLU A 63  ? 1.1580 1.2015 1.2605 0.0947  -0.0262 0.0856  63  GLU A OE2 
484  N N   . GLY A 64  ? 1.0202 1.0621 1.1163 0.1380  0.0025  0.0454  64  GLY A N   
485  C CA  . GLY A 64  ? 1.0106 1.0626 1.1066 0.1519  0.0094  0.0441  64  GLY A CA  
486  C C   . GLY A 64  ? 1.0245 1.0998 1.1289 0.1441  0.0126  0.0457  64  GLY A C   
487  O O   . GLY A 64  ? 1.0468 1.1377 1.1558 0.1552  0.0195  0.0494  64  GLY A O   
488  N N   . VAL A 65  ? 1.0503 1.1272 1.1561 0.1258  0.0086  0.0435  65  VAL A N   
489  C CA  . VAL A 65  ? 1.0241 1.1206 1.1363 0.1175  0.0112  0.0450  65  VAL A CA  
490  C C   . VAL A 65  ? 1.0051 1.0907 1.1060 0.1187  0.0139  0.0333  65  VAL A C   
491  O O   . VAL A 65  ? 0.9569 1.0544 1.0583 0.1251  0.0198  0.0339  65  VAL A O   
492  C CB  . VAL A 65  ? 0.9966 1.0987 1.1135 0.0981  0.0059  0.0489  65  VAL A CB  
493  C CG1 . VAL A 65  ? 0.8499 0.9684 0.9708 0.0892  0.0083  0.0497  65  VAL A CG1 
494  C CG2 . VAL A 65  ? 1.0793 1.1920 1.2058 0.0973  0.0016  0.0609  65  VAL A CG2 
495  N N   . ILE A 66  ? 0.9839 1.0470 1.0751 0.1127  0.0096  0.0232  66  ILE A N   
496  C CA  . ILE A 66  ? 0.8645 0.9166 0.9461 0.1126  0.0097  0.0120  66  ILE A CA  
497  C C   . ILE A 66  ? 0.9488 0.9740 1.0179 0.1218  0.0063  0.0026  66  ILE A C   
498  O O   . ILE A 66  ? 0.9748 0.9871 1.0430 0.1235  0.0033  0.0038  66  ILE A O   
499  C CB  . ILE A 66  ? 0.7687 0.8205 0.8530 0.0949  0.0067  0.0083  66  ILE A CB  
500  C CG1 . ILE A 66  ? 0.7594 0.7945 0.8443 0.0856  0.0017  0.0063  66  ILE A CG1 
501  C CG2 . ILE A 66  ? 0.8317 0.9060 0.9249 0.0853  0.0092  0.0172  66  ILE A CG2 
502  C CD1 . ILE A 66  ? 0.9125 0.9454 1.0000 0.0698  0.0005  0.0029  66  ILE A CD1 
503  N N   . ARG A 67  ? 0.9835 0.9986 1.0414 0.1277  0.0060  -0.0068 67  ARG A N   
504  C CA  . ARG A 67  ? 0.9500 0.9368 0.9937 0.1349  0.0006  -0.0173 67  ARG A CA  
505  C C   . ARG A 67  ? 0.9270 0.9040 0.9702 0.1231  -0.0061 -0.0272 67  ARG A C   
506  O O   . ARG A 67  ? 0.9182 0.9099 0.9682 0.1138  -0.0046 -0.0265 67  ARG A O   
507  C CB  . ARG A 67  ? 1.0618 1.0410 1.0891 0.1548  0.0049  -0.0202 67  ARG A CB  
508  C CG  . ARG A 67  ? 1.1942 1.1876 1.2253 0.1681  0.0136  -0.0091 67  ARG A CG  
509  C CD  . ARG A 67  ? 1.4120 1.3962 1.4250 0.1889  0.0200  -0.0117 67  ARG A CD  
510  N NE  . ARG A 67  ? 1.5566 1.5060 1.5484 0.1984  0.0143  -0.0221 67  ARG A NE  
511  C CZ  . ARG A 67  ? 1.6221 1.5540 1.5919 0.2180  0.0186  -0.0260 67  ARG A CZ  
512  N NH1 . ARG A 67  ? 1.6799 1.6270 1.6470 0.2310  0.0303  -0.0198 67  ARG A NH1 
513  N NH2 . ARG A 67  ? 1.6293 1.5263 1.5784 0.2246  0.0113  -0.0361 67  ARG A NH2 
514  N N   . LYS A 68  ? 0.9942 0.9458 1.0301 0.1235  -0.0137 -0.0360 68  LYS A N   
515  C CA  . LYS A 68  ? 0.8702 0.8122 0.9092 0.1123  -0.0215 -0.0449 68  LYS A CA  
516  C C   . LYS A 68  ? 0.9446 0.8734 0.9669 0.1225  -0.0260 -0.0549 68  LYS A C   
517  O O   . LYS A 68  ? 0.8553 0.7648 0.8599 0.1365  -0.0279 -0.0591 68  LYS A O   
518  C CB  . LYS A 68  ? 0.8851 0.8075 0.9291 0.1041  -0.0283 -0.0480 68  LYS A CB  
519  C CG  . LYS A 68  ? 0.8332 0.7527 0.8892 0.0893  -0.0348 -0.0539 68  LYS A CG  
520  C CD  . LYS A 68  ? 0.8289 0.7305 0.8926 0.0802  -0.0399 -0.0551 68  LYS A CD  
521  C CE  . LYS A 68  ? 0.8612 0.7657 0.9428 0.0644  -0.0437 -0.0581 68  LYS A CE  
522  N NZ  . LYS A 68  ? 1.0139 0.9140 1.0929 0.0663  -0.0522 -0.0680 68  LYS A NZ  
523  N N   . LEU A 69  ? 0.9001 0.8376 0.9261 0.1161  -0.0279 -0.0585 69  LEU A N   
524  C CA  . LEU A 69  ? 0.9380 0.8625 0.9474 0.1246  -0.0337 -0.0681 69  LEU A CA  
525  C C   . LEU A 69  ? 1.0586 0.9631 1.0711 0.1166  -0.0473 -0.0779 69  LEU A C   
526  O O   . LEU A 69  ? 0.9322 0.8451 0.9608 0.1035  -0.0512 -0.0794 69  LEU A O   
527  C CB  . LEU A 69  ? 0.8746 0.8186 0.8860 0.1227  -0.0289 -0.0662 69  LEU A CB  
528  C CG  . LEU A 69  ? 0.8596 0.8246 0.8704 0.1290  -0.0159 -0.0558 69  LEU A CG  
529  C CD1 . LEU A 69  ? 0.7464 0.7297 0.7618 0.1231  -0.0118 -0.0534 69  LEU A CD1 
530  C CD2 . LEU A 69  ? 0.8832 0.8374 0.8727 0.1487  -0.0115 -0.0564 69  LEU A CD2 
531  N N   . LYS A 70  ? 1.0732 0.9505 1.0707 0.1245  -0.0547 -0.0844 70  LYS A N   
532  C CA  . LYS A 70  ? 1.0931 0.9501 1.0959 0.1154  -0.0686 -0.0927 70  LYS A CA  
533  C C   . LYS A 70  ? 1.1341 0.9863 1.1344 0.1133  -0.0797 -0.1018 70  LYS A C   
534  O O   . LYS A 70  ? 1.2284 1.0742 1.2438 0.1011  -0.0907 -0.1066 70  LYS A O   
535  C CB  . LYS A 70  ? 1.1076 0.9334 1.0913 0.1252  -0.0743 -0.0976 70  LYS A CB  
536  C CG  . LYS A 70  ? 1.3266 1.1542 1.3146 0.1267  -0.0655 -0.0889 70  LYS A CG  
537  C CD  . LYS A 70  ? 1.5102 1.3034 1.4780 0.1363  -0.0718 -0.0943 70  LYS A CD  
538  C CE  . LYS A 70  ? 1.5001 1.2945 1.4728 0.1379  -0.0636 -0.0852 70  LYS A CE  
539  N NZ  . LYS A 70  ? 1.5023 1.2609 1.4544 0.1477  -0.0694 -0.0903 70  LYS A NZ  
540  N N   . LYS A 71  ? 1.0418 0.8970 1.0241 0.1247  -0.0771 -0.1038 71  LYS A N   
541  C CA  . LYS A 71  ? 0.9185 0.7663 0.8950 0.1243  -0.0890 -0.1127 71  LYS A CA  
542  C C   . LYS A 71  ? 0.8584 0.7306 0.8624 0.1094  -0.0890 -0.1098 71  LYS A C   
543  O O   . LYS A 71  ? 0.9364 0.8036 0.9443 0.1053  -0.1014 -0.1168 71  LYS A O   
544  C CB  . LYS A 71  ? 0.9899 0.8318 0.9364 0.1418  -0.0852 -0.1149 71  LYS A CB  
545  C CG  . LYS A 71  ? 0.9376 0.7672 0.8724 0.1435  -0.0991 -0.1246 71  LYS A CG  
546  C CD  . LYS A 71  ? 1.0564 0.8703 0.9539 0.1632  -0.0962 -0.1280 71  LYS A CD  
547  C CE  . LYS A 71  ? 1.1116 0.9066 0.9928 0.1657  -0.1133 -0.1388 71  LYS A CE  
548  N NZ  . LYS A 71  ? 1.3494 1.1227 1.1886 0.1861  -0.1110 -0.1428 71  LYS A NZ  
549  N N   . TYR A 72  ? 0.8384 0.7355 0.8606 0.1016  -0.0759 -0.0997 72  TYR A N   
550  C CA  . TYR A 72  ? 0.7729 0.6916 0.8181 0.0889  -0.0736 -0.0963 72  TYR A CA  
551  C C   . TYR A 72  ? 0.8101 0.7372 0.8805 0.0743  -0.0695 -0.0903 72  TYR A C   
552  O O   . TYR A 72  ? 0.9738 0.8943 1.0428 0.0747  -0.0660 -0.0867 72  TYR A O   
553  C CB  . TYR A 72  ? 0.8212 0.7603 0.8612 0.0929  -0.0611 -0.0898 72  TYR A CB  
554  C CG  . TYR A 72  ? 0.8690 0.7993 0.8811 0.1091  -0.0610 -0.0934 72  TYR A CG  
555  C CD1 . TYR A 72  ? 0.8308 0.7498 0.8315 0.1138  -0.0718 -0.1020 72  TYR A CD1 
556  C CD2 . TYR A 72  ? 0.8482 0.7815 0.8456 0.1201  -0.0497 -0.0876 72  TYR A CD2 
557  C CE1 . TYR A 72  ? 0.8785 0.7868 0.8503 0.1293  -0.0708 -0.1050 72  TYR A CE1 
558  C CE2 . TYR A 72  ? 0.9116 0.8364 0.8833 0.1356  -0.0474 -0.0899 72  TYR A CE2 
559  C CZ  . TYR A 72  ? 0.8542 0.7652 0.8113 0.1403  -0.0576 -0.0988 72  TYR A CZ  
560  O OH  . TYR A 72  ? 0.9255 0.8254 0.8536 0.1565  -0.0545 -0.1008 72  TYR A OH  
561  N N   . ASP A 73  ? 0.8113 0.7520 0.9037 0.0623  -0.0695 -0.0887 73  ASP A N   
562  C CA  . ASP A 73  ? 0.8144 0.7615 0.9306 0.0483  -0.0652 -0.0831 73  ASP A CA  
563  C C   . ASP A 73  ? 0.7732 0.7369 0.8898 0.0458  -0.0501 -0.0728 73  ASP A C   
564  O O   . ASP A 73  ? 0.7753 0.7549 0.8953 0.0431  -0.0435 -0.0693 73  ASP A O   
565  C CB  . ASP A 73  ? 0.8814 0.8359 1.0215 0.0378  -0.0704 -0.0852 73  ASP A CB  
566  C CG  . ASP A 73  ? 0.9596 0.9209 1.1238 0.0240  -0.0632 -0.0783 73  ASP A CG  
567  O OD1 . ASP A 73  ? 1.0763 1.0246 1.2475 0.0191  -0.0671 -0.0787 73  ASP A OD1 
568  O OD2 . ASP A 73  ? 0.9056 0.8835 1.0801 0.0183  -0.0532 -0.0724 73  ASP A OD2 
569  N N   . ASN A 74  ? 0.8427 0.8013 0.9548 0.0466  -0.0453 -0.0678 74  ASN A N   
570  C CA  . ASN A 74  ? 0.7838 0.7558 0.8968 0.0431  -0.0334 -0.0577 74  ASN A CA  
571  C C   . ASN A 74  ? 0.7120 0.6978 0.8122 0.0507  -0.0274 -0.0548 74  ASN A C   
572  O O   . ASN A 74  ? 0.6288 0.6290 0.7333 0.0451  -0.0212 -0.0506 74  ASN A O   
573  C CB  . ASN A 74  ? 0.6923 0.6727 0.8239 0.0289  -0.0280 -0.0530 74  ASN A CB  
574  C CG  . ASN A 74  ? 0.8540 0.8417 0.9834 0.0244  -0.0177 -0.0430 74  ASN A CG  
575  O OD1 . ASN A 74  ? 0.8926 0.8763 1.0127 0.0295  -0.0166 -0.0393 74  ASN A OD1 
576  N ND2 . ASN A 74  ? 0.8459 0.8433 0.9830 0.0154  -0.0106 -0.0385 74  ASN A ND2 
577  N N   . CYS A 75  ? 0.7382 0.7180 0.8221 0.0638  -0.0288 -0.0567 75  CYS A N   
578  C CA  . CYS A 75  ? 0.6051 0.5973 0.6775 0.0722  -0.0221 -0.0527 75  CYS A CA  
579  C C   . CYS A 75  ? 0.6737 0.6647 0.7380 0.0814  -0.0180 -0.0473 75  CYS A C   
580  O O   . CYS A 75  ? 0.7661 0.7404 0.8244 0.0877  -0.0226 -0.0509 75  CYS A O   
581  C CB  . CYS A 75  ? 0.7386 0.7256 0.7979 0.0819  -0.0266 -0.0603 75  CYS A CB  
582  S SG  . CYS A 75  ? 0.6727 0.6650 0.7418 0.0731  -0.0310 -0.0651 75  CYS A SG  
583  N N   . TRP A 76  ? 0.7293 0.7379 0.7940 0.0822  -0.0096 -0.0385 76  TRP A N   
584  C CA  . TRP A 76  ? 0.7458 0.7581 0.8081 0.0897  -0.0052 -0.0311 76  TRP A CA  
585  C C   . TRP A 76  ? 0.5220 0.5498 0.5788 0.0986  0.0020  -0.0258 76  TRP A C   
586  O O   . TRP A 76  ? 0.6893 0.7296 0.7479 0.0935  0.0052  -0.0241 76  TRP A O   
587  C CB  . TRP A 76  ? 0.7567 0.7763 0.8307 0.0786  -0.0032 -0.0228 76  TRP A CB  
588  C CG  . TRP A 76  ? 0.7092 0.7153 0.7901 0.0681  -0.0080 -0.0265 76  TRP A CG  
589  C CD1 . TRP A 76  ? 0.6065 0.6134 0.6954 0.0562  -0.0088 -0.0292 76  TRP A CD1 
590  C CD2 . TRP A 76  ? 0.7975 0.7872 0.8786 0.0688  -0.0116 -0.0273 76  TRP A CD2 
591  N NE1 . TRP A 76  ? 0.7151 0.7085 0.8111 0.0491  -0.0120 -0.0311 76  TRP A NE1 
592  C CE2 . TRP A 76  ? 0.7186 0.7005 0.8093 0.0562  -0.0141 -0.0301 76  TRP A CE2 
593  C CE3 . TRP A 76  ? 0.8884 0.8687 0.9628 0.0794  -0.0122 -0.0253 76  TRP A CE3 
594  C CZ2 . TRP A 76  ? 0.7618 0.7266 0.8556 0.0528  -0.0174 -0.0309 76  TRP A CZ2 
595  C CZ3 . TRP A 76  ? 0.8266 0.7884 0.9021 0.0764  -0.0162 -0.0267 76  TRP A CZ3 
596  C CH2 . TRP A 76  ? 0.7450 0.6992 0.8303 0.0627  -0.0188 -0.0293 76  TRP A CH2 
597  N N   . LEU A 77  ? 0.6903 0.7168 0.7408 0.1122  0.0053  -0.0226 77  LEU A N   
598  C CA  . LEU A 77  ? 0.6811 0.7235 0.7292 0.1219  0.0139  -0.0156 77  LEU A CA  
599  C C   . LEU A 77  ? 0.7476 0.8072 0.8089 0.1207  0.0182  -0.0034 77  LEU A C   
600  O O   . LEU A 77  ? 0.7716 0.8241 0.8362 0.1211  0.0152  -0.0017 77  LEU A O   
601  C CB  . LEU A 77  ? 0.6224 0.6504 0.6524 0.1409  0.0160  -0.0206 77  LEU A CB  
602  C CG  . LEU A 77  ? 0.6246 0.6680 0.6525 0.1535  0.0272  -0.0122 77  LEU A CG  
603  C CD1 . LEU A 77  ? 0.8597 0.9189 0.8902 0.1469  0.0315  -0.0097 77  LEU A CD1 
604  C CD2 . LEU A 77  ? 0.7306 0.7546 0.7368 0.1737  0.0300  -0.0176 77  LEU A CD2 
605  N N   . ALA A 78  ? 0.7058 0.7878 0.7749 0.1190  0.0245  0.0055  78  ALA A N   
606  C CA  . ALA A 78  ? 0.6464 0.7479 0.7304 0.1171  0.0273  0.0181  78  ALA A CA  
607  C C   . ALA A 78  ? 0.7660 0.8856 0.8537 0.1280  0.0366  0.0260  78  ALA A C   
608  O O   . ALA A 78  ? 0.8420 0.9682 0.9267 0.1263  0.0408  0.0256  78  ALA A O   
609  C CB  . ALA A 78  ? 0.5177 0.6299 0.6120 0.0982  0.0237  0.0228  78  ALA A CB  
610  N N   . LEU A 79  ? 0.8621 0.9895 0.9569 0.1396  0.0404  0.0338  79  LEU A N   
611  C CA  . LEU A 79  ? 0.8497 0.9968 0.9524 0.1510  0.0507  0.0435  79  LEU A CA  
612  C C   . LEU A 79  ? 0.9455 1.1198 1.0726 0.1425  0.0499  0.0577  79  LEU A C   
613  O O   . LEU A 79  ? 0.9329 1.1076 1.0680 0.1416  0.0445  0.0617  79  LEU A O   
614  C CB  . LEU A 79  ? 0.9243 1.0601 1.0169 0.1731  0.0570  0.0424  79  LEU A CB  
615  C CG  . LEU A 79  ? 0.9423 1.0478 1.0075 0.1826  0.0561  0.0281  79  LEU A CG  
616  C CD1 . LEU A 79  ? 1.0846 1.1772 1.1369 0.2057  0.0633  0.0278  79  LEU A CD1 
617  C CD2 . LEU A 79  ? 0.9330 1.0397 0.9889 0.1797  0.0596  0.0241  79  LEU A CD2 
618  N N   . THR A 80  ? 1.0515 1.2471 1.1899 0.1361  0.0544  0.0654  80  THR A N   
619  C CA  . THR A 80  ? 1.0512 1.2725 1.2131 0.1251  0.0514  0.0786  80  THR A CA  
620  C C   . THR A 80  ? 1.0571 1.3028 1.2379 0.1384  0.0609  0.0918  80  THR A C   
621  O O   . THR A 80  ? 1.0773 1.3186 1.2508 0.1569  0.0713  0.0906  80  THR A O   
622  C CB  . THR A 80  ? 1.0439 1.2721 1.2072 0.1069  0.0489  0.0792  80  THR A CB  
623  O OG1 . THR A 80  ? 1.0538 1.2895 1.2152 0.1128  0.0594  0.0806  80  THR A OG1 
624  C CG2 . THR A 80  ? 1.0459 1.2502 1.1909 0.0961  0.0418  0.0664  80  THR A CG2 
625  N N   . ASP A 81  ? 0.9263 1.1974 1.1317 0.1291  0.0571  0.1049  81  ASP A N   
626  C CA  . ASP A 81  ? 0.8515 1.1510 1.0813 0.1395  0.0659  0.1194  81  ASP A CA  
627  C C   . ASP A 81  ? 0.8294 1.1392 1.0602 0.1404  0.0776  0.1221  81  ASP A C   
628  O O   . ASP A 81  ? 0.8879 1.1949 1.1126 0.1248  0.0742  0.1187  81  ASP A O   
629  C CB  . ASP A 81  ? 0.7745 1.0988 1.0320 0.1270  0.0560  0.1328  81  ASP A CB  
630  C CG  . ASP A 81  ? 0.8172 1.1738 1.1055 0.1383  0.0641  0.1493  81  ASP A CG  
631  O OD1 . ASP A 81  ? 0.8467 1.2185 1.1440 0.1422  0.0761  0.1550  81  ASP A OD1 
632  O OD2 . ASP A 81  ? 0.7235 1.0904 1.0277 0.1438  0.0589  0.1571  81  ASP A OD2 
633  N N   . PRO A 82  ? 0.7654 1.0856 1.0023 0.1591  0.0923  0.1285  82  PRO A N   
634  C CA  . PRO A 82  ? 0.7814 1.1085 1.0161 0.1613  0.1051  0.1311  82  PRO A CA  
635  C C   . PRO A 82  ? 0.8878 1.2411 1.1467 0.1425  0.1027  0.1425  82  PRO A C   
636  O O   . PRO A 82  ? 0.8887 1.2420 1.1411 0.1386  0.1101  0.1423  82  PRO A O   
637  C CB  . PRO A 82  ? 0.7575 1.0934 0.9981 0.1861  0.1218  0.1388  82  PRO A CB  
638  C CG  . PRO A 82  ? 0.7964 1.1437 1.0565 0.1921  0.1164  0.1460  82  PRO A CG  
639  C CD  . PRO A 82  ? 0.8263 1.1516 1.0714 0.1800  0.0991  0.1343  82  PRO A CD  
640  N N   . ARG A 83  ? 0.9764 1.3502 1.2615 0.1307  0.0920  0.1526  83  ARG A N   
641  C CA  . ARG A 83  ? 0.8960 1.2932 1.2041 0.1114  0.0871  0.1636  83  ARG A CA  
642  C C   . ARG A 83  ? 0.9213 1.3014 1.2131 0.0890  0.0730  0.1547  83  ARG A C   
643  O O   . ARG A 83  ? 0.9643 1.3564 1.2672 0.0722  0.0693  0.1612  83  ARG A O   
644  C CB  . ARG A 83  ? 0.8166 1.2447 1.1618 0.1093  0.0808  0.1797  83  ARG A CB  
645  C CG  . ARG A 83  ? 0.9000 1.3515 1.2684 0.1306  0.0966  0.1921  83  ARG A CG  
646  C CD  . ARG A 83  ? 0.9348 1.4124 1.3369 0.1316  0.0881  0.2057  83  ARG A CD  
647  N NE  . ARG A 83  ? 0.8458 1.3026 1.2316 0.1351  0.0764  0.1969  83  ARG A NE  
648  C CZ  . ARG A 83  ? 0.9693 1.4407 1.3762 0.1386  0.0677  0.2058  83  ARG A CZ  
649  N NH1 . ARG A 83  ? 1.0481 1.5570 1.4959 0.1391  0.0682  0.2240  83  ARG A NH1 
650  N NH2 . ARG A 83  ? 1.0303 1.4782 1.4178 0.1416  0.0581  0.1967  83  ARG A NH2 
651  N N   . ASP A 84  ? 0.8605 1.2124 1.1265 0.0885  0.0655  0.1405  84  ASP A N   
652  C CA  . ASP A 84  ? 0.8540 1.1872 1.1024 0.0696  0.0539  0.1315  84  ASP A CA  
653  C C   . ASP A 84  ? 0.9147 1.2204 1.1327 0.0754  0.0595  0.1161  84  ASP A C   
654  O O   . ASP A 84  ? 0.8602 1.1443 1.0609 0.0801  0.0555  0.1050  84  ASP A O   
655  C CB  . ASP A 84  ? 0.6720 0.9976 0.9198 0.0627  0.0395  0.1300  84  ASP A CB  
656  C CG  . ASP A 84  ? 0.7752 1.0821 1.0054 0.0435  0.0288  0.1225  84  ASP A CG  
657  O OD1 . ASP A 84  ? 0.9041 1.2064 1.1254 0.0346  0.0316  0.1196  84  ASP A OD1 
658  O OD2 . ASP A 84  ? 0.7997 1.0952 1.0237 0.0380  0.0184  0.1199  84  ASP A OD2 
659  N N   . VAL A 85  ? 0.7609 1.0674 0.9731 0.0746  0.0682  0.1158  85  VAL A N   
660  C CA  . VAL A 85  ? 0.8775 1.1601 1.0622 0.0823  0.0738  0.1025  85  VAL A CA  
661  C C   . VAL A 85  ? 0.9114 1.1882 1.0860 0.0684  0.0736  0.1001  85  VAL A C   
662  O O   . VAL A 85  ? 0.9843 1.2399 1.1359 0.0706  0.0746  0.0884  85  VAL A O   
663  C CB  . VAL A 85  ? 0.8586 1.1428 1.0396 0.1042  0.0883  0.1037  85  VAL A CB  
664  C CG1 . VAL A 85  ? 0.8442 1.1270 1.0287 0.1195  0.0884  0.1035  85  VAL A CG1 
665  C CG2 . VAL A 85  ? 0.7756 1.0857 0.9770 0.1047  0.0994  0.1184  85  VAL A CG2 
666  N N   . ALA A 86  ? 0.8915 1.1862 1.0833 0.0541  0.0716  0.1111  86  ALA A N   
667  C CA  . ALA A 86  ? 0.9330 1.2221 1.1157 0.0409  0.0720  0.1103  86  ALA A CA  
668  C C   . ALA A 86  ? 0.9299 1.2218 1.1199 0.0194  0.0591  0.1146  86  ALA A C   
669  O O   . ALA A 86  ? 0.9432 1.2413 1.1445 0.0151  0.0496  0.1180  86  ALA A O   
670  C CB  . ALA A 86  ? 1.0131 1.3182 1.2059 0.0455  0.0853  0.1204  86  ALA A CB  
671  N N   . ARG A 87  ? 0.9427 1.2274 1.1234 0.0063  0.0585  0.1142  87  ARG A N   
672  C CA  . ARG A 87  ? 0.8627 1.1449 1.0443 -0.0145 0.0465  0.1174  87  ARG A CA  
673  C C   . ARG A 87  ? 0.9248 1.2309 1.1308 -0.0241 0.0470  0.1328  87  ARG A C   
674  O O   . ARG A 87  ? 1.0505 1.3590 1.2556 -0.0257 0.0557  0.1362  87  ARG A O   
675  C CB  . ARG A 87  ? 0.8949 1.1510 1.0490 -0.0227 0.0452  0.1070  87  ARG A CB  
676  C CG  . ARG A 87  ? 0.9323 1.1811 1.0818 -0.0436 0.0345  0.1101  87  ARG A CG  
677  C CD  . ARG A 87  ? 0.7829 1.0041 0.9038 -0.0486 0.0349  0.0991  87  ARG A CD  
678  N NE  . ARG A 87  ? 0.7664 0.9833 0.8780 -0.0384 0.0468  0.0949  87  ARG A NE  
679  C CZ  . ARG A 87  ? 0.8012 1.0223 0.9139 -0.0427 0.0528  0.1011  87  ARG A CZ  
680  N NH1 . ARG A 87  ? 0.7575 0.9884 0.8824 -0.0581 0.0479  0.1118  87  ARG A NH1 
681  N NH2 . ARG A 87  ? 0.7699 0.9843 0.8709 -0.0317 0.0634  0.0966  87  ARG A NH2 
682  N N   . ILE A 88  ? 0.9769 1.3007 1.2054 -0.0309 0.0373  0.1425  88  ILE A N   
683  C CA  . ILE A 88  ? 0.9255 1.2765 1.1839 -0.0399 0.0362  0.1586  88  ILE A CA  
684  C C   . ILE A 88  ? 0.9512 1.2913 1.2005 -0.0620 0.0276  0.1600  88  ILE A C   
685  O O   . ILE A 88  ? 0.9105 1.2389 1.1513 -0.0759 0.0125  0.1582  88  ILE A O   
686  C CB  . ILE A 88  ? 0.8574 1.2304 1.1431 -0.0399 0.0265  0.1684  88  ILE A CB  
687  C CG1 . ILE A 88  ? 0.8536 1.2322 1.1436 -0.0171 0.0350  0.1657  88  ILE A CG1 
688  C CG2 . ILE A 88  ? 0.8674 1.2721 1.1892 -0.0487 0.0256  0.1862  88  ILE A CG2 
689  C CD1 . ILE A 88  ? 0.7051 1.1031 1.0199 -0.0147 0.0257  0.1748  88  ILE A CD1 
690  N N   . GLU A 89  ? 0.9628 1.3044 1.2115 -0.0649 0.0374  0.1634  89  GLU A N   
691  C CA  . GLU A 89  ? 0.9383 1.2681 1.1779 -0.0856 0.0301  0.1654  89  GLU A CA  
692  C C   . GLU A 89  ? 0.9679 1.3220 1.2393 -0.1018 0.0198  0.1814  89  GLU A C   
693  O O   . GLU A 89  ? 0.9209 1.2628 1.1842 -0.1216 0.0063  0.1825  89  GLU A O   
694  C CB  . GLU A 89  ? 1.0706 1.3909 1.2964 -0.0827 0.0444  0.1633  89  GLU A CB  
695  C CG  . GLU A 89  ? 1.0145 1.3226 1.2317 -0.1036 0.0385  0.1666  89  GLU A CG  
696  C CD  . GLU A 89  ? 0.9843 1.2827 1.1877 -0.0996 0.0533  0.1654  89  GLU A CD  
697  O OE1 . GLU A 89  ? 0.9866 1.2836 1.1819 -0.0804 0.0669  0.1599  89  GLU A OE1 
698  O OE2 . GLU A 89  ? 0.9609 1.2511 1.1599 -0.1156 0.0507  0.1700  89  GLU A OE2 
699  N N   . SER A 90  ? 1.0052 1.3929 1.3128 -0.0935 0.0256  0.1941  90  SER A N   
700  C CA  . SER A 90  ? 0.9307 1.3456 1.2742 -0.1086 0.0156  0.2107  90  SER A CA  
701  C C   . SER A 90  ? 0.9114 1.3248 1.2579 -0.1194 -0.0064 0.2113  90  SER A C   
702  O O   . SER A 90  ? 0.8595 1.2808 1.2214 -0.1390 -0.0215 0.2208  90  SER A O   
703  C CB  . SER A 90  ? 0.8775 1.3302 1.2608 -0.0947 0.0292  0.2248  90  SER A CB  
704  O OG  . SER A 90  ? 0.9048 1.3640 1.2913 -0.0748 0.0326  0.2211  90  SER A OG  
705  N N   . LYS A 91  ? 0.8893 1.2910 1.2203 -0.1075 -0.0091 0.2014  91  LYS A N   
706  C CA  . LYS A 91  ? 0.7713 1.1693 1.1018 -0.1152 -0.0287 0.2017  91  LYS A CA  
707  C C   . LYS A 91  ? 0.7663 1.1242 1.0539 -0.1253 -0.0385 0.1878  91  LYS A C   
708  O O   . LYS A 91  ? 0.7244 1.0694 0.9983 -0.1228 -0.0476 0.1819  91  LYS A O   
709  C CB  . LYS A 91  ? 0.7237 1.1350 1.0665 -0.0955 -0.0253 0.2016  91  LYS A CB  
710  C CG  . LYS A 91  ? 0.7597 1.2118 1.1472 -0.0853 -0.0174 0.2172  91  LYS A CG  
711  C CD  . LYS A 91  ? 0.8038 1.2644 1.1985 -0.0642 -0.0130 0.2159  91  LYS A CD  
712  C CE  . LYS A 91  ? 0.9642 1.4661 1.4050 -0.0539 -0.0060 0.2329  91  LYS A CE  
713  N NZ  . LYS A 91  ? 1.0106 1.5269 1.4641 -0.0482 0.0139  0.2387  91  LYS A NZ  
714  N N   . THR A 92  ? 0.7673 1.1045 1.0330 -0.1362 -0.0361 0.1829  92  THR A N   
715  C CA  . THR A 92  ? 0.8148 1.1135 1.0396 -0.1457 -0.0437 0.1707  92  THR A CA  
716  C C   . THR A 92  ? 0.7476 1.0368 0.9679 -0.1692 -0.0573 0.1766  92  THR A C   
717  O O   . THR A 92  ? 0.8104 1.1094 1.0433 -0.1761 -0.0518 0.1835  92  THR A O   
718  C CB  . THR A 92  ? 0.8373 1.1140 1.0343 -0.1351 -0.0276 0.1576  92  THR A CB  
719  O OG1 . THR A 92  ? 0.8034 1.0884 1.0052 -0.1138 -0.0163 0.1523  92  THR A OG1 
720  C CG2 . THR A 92  ? 0.7293 0.9675 0.8861 -0.1431 -0.0342 0.1457  92  THR A CG2 
721  N N   . VAL A 93  ? 0.7393 1.0075 0.9398 -0.1816 -0.0750 0.1741  93  VAL A N   
722  C CA  . VAL A 93  ? 0.7836 1.0395 0.9771 -0.2047 -0.0915 0.1795  93  VAL A CA  
723  C C   . VAL A 93  ? 0.7464 0.9565 0.8906 -0.2120 -0.0981 0.1671  93  VAL A C   
724  O O   . VAL A 93  ? 0.8262 1.0195 0.9488 -0.2012 -0.0949 0.1572  93  VAL A O   
725  C CB  . VAL A 93  ? 0.7272 1.0069 0.9511 -0.2150 -0.1112 0.1931  93  VAL A CB  
726  C CG1 . VAL A 93  ? 0.7237 1.0502 0.9990 -0.2074 -0.1030 0.2068  93  VAL A CG1 
727  C CG2 . VAL A 93  ? 0.6541 0.9244 0.8656 -0.2086 -0.1214 0.1886  93  VAL A CG2 
728  N N   . ILE A 94  ? 0.7227 0.9118 0.8493 -0.2304 -0.1068 0.1682  94  ILE A N   
729  C CA  . ILE A 94  ? 0.7894 0.9327 0.8678 -0.2391 -0.1139 0.1580  94  ILE A CA  
730  C C   . ILE A 94  ? 0.9016 1.0351 0.9756 -0.2601 -0.1390 0.1654  94  ILE A C   
731  O O   . ILE A 94  ? 0.9187 1.0688 1.0169 -0.2744 -0.1478 0.1763  94  ILE A O   
732  C CB  . ILE A 94  ? 0.7617 0.8807 0.8147 -0.2411 -0.1015 0.1511  94  ILE A CB  
733  C CG1 . ILE A 94  ? 0.8882 1.0156 0.9440 -0.2199 -0.0787 0.1434  94  ILE A CG1 
734  C CG2 . ILE A 94  ? 0.8233 0.8940 0.8262 -0.2501 -0.1089 0.1417  94  ILE A CG2 
735  C CD1 . ILE A 94  ? 0.8813 0.9861 0.9131 -0.2197 -0.0662 0.1367  94  ILE A CD1 
736  N N   . ILE A 95  ? 0.9064 1.0122 0.9493 -0.2621 -0.1506 0.1596  95  ILE A N   
737  C CA  . ILE A 95  ? 0.8827 0.9768 0.9179 -0.2801 -0.1765 0.1659  95  ILE A CA  
738  C C   . ILE A 95  ? 1.0096 1.0531 0.9934 -0.2936 -0.1828 0.1582  95  ILE A C   
739  O O   . ILE A 95  ? 0.9783 0.9860 0.9199 -0.2876 -0.1787 0.1473  95  ILE A O   
740  C CB  . ILE A 95  ? 0.9145 1.0104 0.9479 -0.2728 -0.1863 0.1660  95  ILE A CB  
741  C CG1 . ILE A 95  ? 0.8788 1.0205 0.9583 -0.2557 -0.1759 0.1717  95  ILE A CG1 
742  C CG2 . ILE A 95  ? 1.0622 1.1510 1.0930 -0.2913 -0.2152 0.1743  95  ILE A CG2 
743  C CD1 . ILE A 95  ? 0.9382 1.1240 1.0698 -0.2617 -0.1805 0.1865  95  ILE A CD1 
744  N N   . THR A 96  ? 1.0994 1.1388 1.0865 -0.3119 -0.1922 0.1641  96  THR A N   
745  C CA  . THR A 96  ? 1.2611 1.2513 1.2000 -0.3272 -0.2020 0.1585  96  THR A CA  
746  C C   . THR A 96  ? 1.3746 1.3660 1.3243 -0.3511 -0.2296 0.1695  96  THR A C   
747  O O   . THR A 96  ? 1.3143 1.3492 1.3147 -0.3559 -0.2373 0.1823  96  THR A O   
748  C CB  . THR A 96  ? 1.2157 1.1903 1.1395 -0.3260 -0.1838 0.1527  96  THR A CB  
749  O OG1 . THR A 96  ? 1.2985 1.3078 1.2654 -0.3331 -0.1816 0.1636  96  THR A OG1 
750  C CG2 . THR A 96  ? 1.1735 1.1488 1.0895 -0.3026 -0.1582 0.1423  96  THR A CG2 
751  N N   . GLN A 97  ? 1.4081 1.3507 1.3096 -0.3659 -0.2447 0.1646  97  GLN A N   
752  C CA  . GLN A 97  ? 1.5593 1.4969 1.4656 -0.3902 -0.2742 0.1741  97  GLN A CA  
753  C C   . GLN A 97  ? 1.5968 1.5558 1.5369 -0.4046 -0.2741 0.1835  97  GLN A C   
754  O O   . GLN A 97  ? 1.4733 1.4666 1.4582 -0.4175 -0.2904 0.1973  97  GLN A O   
755  C CB  . GLN A 97  ? 1.6169 1.4910 1.4568 -0.4016 -0.2897 0.1655  97  GLN A CB  
756  C CG  . GLN A 97  ? 1.6920 1.5546 1.5306 -0.4277 -0.3232 0.1742  97  GLN A CG  
757  C CD  . GLN A 97  ? 1.7174 1.5140 1.4850 -0.4347 -0.3377 0.1650  97  GLN A CD  
758  O OE1 . GLN A 97  ? 1.7974 1.5587 1.5188 -0.4225 -0.3251 0.1531  97  GLN A OE1 
759  N NE2 . GLN A 97  ? 1.6475 1.4277 1.4060 -0.4472 -0.3588 0.1710  97  GLN A NE2 
760  N N   . GLU A 98  ? 1.7527 1.6921 1.6730 -0.4023 -0.2557 0.1771  98  GLU A N   
761  C CA  . GLU A 98  ? 1.7488 1.7029 1.6953 -0.4153 -0.2528 0.1853  98  GLU A CA  
762  C C   . GLU A 98  ? 1.6774 1.6718 1.6614 -0.3966 -0.2243 0.1871  98  GLU A C   
763  O O   . GLU A 98  ? 1.6161 1.6015 1.5802 -0.3763 -0.2032 0.1762  98  GLU A O   
764  C CB  . GLU A 98  ? 1.7954 1.6942 1.6892 -0.4273 -0.2539 0.1775  98  GLU A CB  
765  C CG  . GLU A 98  ? 1.9569 1.8129 1.8110 -0.4441 -0.2817 0.1760  98  GLU A CG  
766  C CD  . GLU A 98  ? 2.0760 1.9587 1.9680 -0.4559 -0.3012 0.1895  98  GLU A CD  
767  O OE1 . GLU A 98  ? 2.0858 2.0115 2.0291 -0.4562 -0.2923 0.1996  98  GLU A OE1 
768  O OE2 . GLU A 98  ? 2.1461 2.0058 2.0161 -0.4643 -0.3248 0.1904  98  GLU A OE2 
769  N N   . GLN A 99  ? 1.7246 1.7629 1.7627 -0.4035 -0.2239 0.2013  99  GLN A N   
770  C CA  . GLN A 99  ? 1.6654 1.7402 1.7373 -0.3861 -0.1969 0.2040  99  GLN A CA  
771  C C   . GLN A 99  ? 1.5854 1.6308 1.6252 -0.3817 -0.1774 0.1953  99  GLN A C   
772  O O   . GLN A 99  ? 1.5513 1.6101 1.5967 -0.3614 -0.1534 0.1907  99  GLN A O   
773  C CB  . GLN A 99  ? 1.6356 1.7609 1.7705 -0.3954 -0.2001 0.2222  99  GLN A CB  
774  C CG  . GLN A 99  ? 1.6239 1.7860 1.7928 -0.3772 -0.1719 0.2263  99  GLN A CG  
775  C CD  . GLN A 99  ? 1.7189 1.9286 1.9485 -0.3856 -0.1728 0.2450  99  GLN A CD  
776  O OE1 . GLN A 99  ? 1.8345 2.0454 2.0758 -0.3985 -0.1923 0.2515  99  GLN A OE1 
777  N NE2 . GLN A 99  ? 1.7142 1.9585 1.9758 -0.3697 -0.1486 0.2504  99  GLN A NE2 
778  N N   . ARG A 100 ? 1.5109 1.5145 1.5154 -0.4000 -0.1880 0.1928  100 ARG A N   
779  C CA  . ARG A 100 ? 1.4429 1.4162 1.4154 -0.3962 -0.1705 0.1851  100 ARG A CA  
780  C C   . ARG A 100 ? 1.3398 1.2857 1.2706 -0.3747 -0.1548 0.1689  100 ARG A C   
781  O O   . ARG A 100 ? 1.2746 1.2097 1.1906 -0.3633 -0.1347 0.1629  100 ARG A O   
782  C CB  . ARG A 100 ? 1.4981 1.4282 1.4383 -0.4209 -0.1871 0.1858  100 ARG A CB  
783  C CG  . ARG A 100 ? 1.5259 1.4310 1.4434 -0.4205 -0.1702 0.1822  100 ARG A CG  
784  C CD  . ARG A 100 ? 1.6185 1.4869 1.5109 -0.4420 -0.1870 0.1838  100 ARG A CD  
785  N NE  . ARG A 100 ? 1.6087 1.4582 1.4862 -0.4418 -0.1710 0.1825  100 ARG A NE  
786  C CZ  . ARG A 100 ? 1.7651 1.5858 1.6230 -0.4547 -0.1798 0.1830  100 ARG A CZ  
787  N NH1 . ARG A 100 ? 1.8270 1.6337 1.6768 -0.4692 -0.2048 0.1848  100 ARG A NH1 
788  N NH2 . ARG A 100 ? 1.7698 1.5745 1.6149 -0.4527 -0.1634 0.1819  100 ARG A NH2 
789  N N   . ASP A 101 ? 1.3698 1.3047 1.2821 -0.3688 -0.1636 0.1623  101 ASP A N   
790  C CA  . ASP A 101 ? 1.3507 1.2636 1.2289 -0.3483 -0.1480 0.1482  101 ASP A CA  
791  C C   . ASP A 101 ? 1.1952 1.1478 1.1063 -0.3255 -0.1266 0.1475  101 ASP A C   
792  O O   . ASP A 101 ? 1.1035 1.0439 0.9957 -0.3093 -0.1079 0.1379  101 ASP A O   
793  C CB  . ASP A 101 ? 1.3275 1.2182 1.1782 -0.3487 -0.1626 0.1427  101 ASP A CB  
794  C CG  . ASP A 101 ? 1.5086 1.3503 1.3151 -0.3688 -0.1827 0.1408  101 ASP A CG  
795  O OD1 . ASP A 101 ? 1.5476 1.3586 1.3277 -0.3763 -0.1790 0.1381  101 ASP A OD1 
796  O OD2 . ASP A 101 ? 1.6110 1.4427 1.4069 -0.3766 -0.2025 0.1421  101 ASP A OD2 
797  N N   . THR A 102 ? 1.1789 1.1784 1.1390 -0.3235 -0.1296 0.1577  102 THR A N   
798  C CA  . THR A 102 ? 1.1032 1.1384 1.0926 -0.3016 -0.1105 0.1571  102 THR A CA  
799  C C   . THR A 102 ? 1.1023 1.1548 1.1113 -0.2975 -0.0932 0.1616  102 THR A C   
800  O O   . THR A 102 ? 1.0342 1.0814 1.0311 -0.2807 -0.0743 0.1535  102 THR A O   
801  C CB  . THR A 102 ? 1.0643 1.1405 1.0959 -0.2993 -0.1194 0.1663  102 THR A CB  
802  O OG1 . THR A 102 ? 1.1089 1.1670 1.1186 -0.2997 -0.1333 0.1610  102 THR A OG1 
803  C CG2 . THR A 102 ? 0.9221 1.0337 0.9834 -0.2767 -0.0996 0.1662  102 THR A CG2 
804  N N   . VAL A 103 ? 1.0685 1.1414 1.1080 -0.3128 -0.0996 0.1751  103 VAL A N   
805  C CA  . VAL A 103 ? 1.0059 1.0976 1.0669 -0.3093 -0.0825 0.1816  103 VAL A CA  
806  C C   . VAL A 103 ? 1.1408 1.2131 1.1941 -0.3323 -0.0909 0.1883  103 VAL A C   
807  O O   . VAL A 103 ? 1.1756 1.2402 1.2300 -0.3530 -0.1128 0.1939  103 VAL A O   
808  C CB  . VAL A 103 ? 0.9358 1.0810 1.0520 -0.3015 -0.0764 0.1940  103 VAL A CB  
809  C CG1 . VAL A 103 ? 1.0148 1.1753 1.1350 -0.2775 -0.0663 0.1865  103 VAL A CG1 
810  C CG2 . VAL A 103 ? 1.0312 1.1982 1.1801 -0.3205 -0.0980 0.2074  103 VAL A CG2 
811  N N   . PRO A 104 ? 1.1014 1.1636 1.1454 -0.3300 -0.0751 0.1880  104 PRO A N   
812  C CA  . PRO A 104 ? 1.0809 1.1269 1.1216 -0.3524 -0.0821 0.1961  104 PRO A CA  
813  C C   . PRO A 104 ? 1.0842 1.1733 1.1802 -0.3659 -0.0886 0.2146  104 PRO A C   
814  O O   . PRO A 104 ? 0.9881 1.1187 1.1233 -0.3528 -0.0742 0.2222  104 PRO A O   
815  C CB  . PRO A 104 ? 1.0094 1.0398 1.0306 -0.3412 -0.0599 0.1916  104 PRO A CB  
816  C CG  . PRO A 104 ? 1.0176 1.0421 1.0177 -0.3156 -0.0466 0.1775  104 PRO A CG  
817  C CD  . PRO A 104 ? 1.0171 1.0766 1.0478 -0.3070 -0.0516 0.1794  104 PRO A CD  
818  N N   . ILE A 105 ? 1.0539 1.1323 1.1528 -0.3920 -0.1104 0.2220  105 ILE A N   
819  C CA  . ILE A 105 ? 0.9803 1.0982 1.1321 -0.4036 -0.1187 0.2385  105 ILE A CA  
820  C C   . ILE A 105 ? 0.9539 1.0913 1.1298 -0.3986 -0.0965 0.2472  105 ILE A C   
821  O O   . ILE A 105 ? 0.9786 1.0852 1.1288 -0.4060 -0.0918 0.2450  105 ILE A O   
822  C CB  . ILE A 105 ? 1.0640 1.1581 1.2039 -0.4241 -0.1453 0.2391  105 ILE A CB  
823  C CG1 . ILE A 105 ? 1.0657 1.1442 1.1844 -0.4272 -0.1671 0.2320  105 ILE A CG1 
824  C CG2 . ILE A 105 ? 1.0678 1.2008 1.2609 -0.4313 -0.1507 0.2544  105 ILE A CG2 
825  C CD1 . ILE A 105 ? 1.1559 1.2808 1.3171 -0.4169 -0.1697 0.2385  105 ILE A CD1 
826  N N   . PRO A 106 ? 0.9396 1.1251 1.1621 -0.3851 -0.0819 0.2571  106 PRO A N   
827  C CA  . PRO A 106 ? 0.9421 1.1435 1.1827 -0.3774 -0.0578 0.2649  106 PRO A CA  
828  C C   . PRO A 106 ? 1.0199 1.2271 1.2844 -0.3928 -0.0636 0.2754  106 PRO A C   
829  O O   . PRO A 106 ? 1.1373 1.3437 1.4118 -0.4083 -0.0866 0.2783  106 PRO A O   
830  C CB  . PRO A 106 ? 0.9018 1.1517 1.1832 -0.3570 -0.0424 0.2717  106 PRO A CB  
831  C CG  . PRO A 106 ? 0.9783 1.2326 1.2560 -0.3532 -0.0569 0.2653  106 PRO A CG  
832  C CD  . PRO A 106 ? 0.8957 1.1205 1.1523 -0.3739 -0.0850 0.2610  106 PRO A CD  
833  N N   . LYS A 107 ? 1.1410 1.3532 1.4135 -0.3880 -0.0421 0.2814  107 LYS A N   
834  C CA  . LYS A 107 ? 1.2346 1.4583 1.5361 -0.4000 -0.0418 0.2932  107 LYS A CA  
835  C C   . LYS A 107 ? 1.3818 1.6587 1.7381 -0.3866 -0.0265 0.3063  107 LYS A C   
836  O O   . LYS A 107 ? 1.3767 1.6659 1.7371 -0.3693 -0.0007 0.3087  107 LYS A O   
837  C CB  . LYS A 107 ? 1.2195 1.4105 1.4917 -0.4039 -0.0274 0.2916  107 LYS A CB  
838  C CG  . LYS A 107 ? 1.2600 1.4663 1.5653 -0.4139 -0.0216 0.3049  107 LYS A CG  
839  C CD  . LYS A 107 ? 1.2321 1.4084 1.5094 -0.4139 -0.0029 0.3042  107 LYS A CD  
840  C CE  . LYS A 107 ? 1.2282 1.3514 1.4588 -0.4314 -0.0192 0.2950  107 LYS A CE  
841  N NZ  . LYS A 107 ? 1.2834 1.3742 1.4666 -0.4264 -0.0280 0.2796  107 LYS A NZ  
842  N N   . SER A 108 ? 1.9930 2.2996 2.3892 -0.3935 -0.0425 0.3148  108 SER A N   
843  C CA  . SER A 108 ? 1.9980 2.3547 2.4474 -0.3809 -0.0295 0.3279  108 SER A CA  
844  C C   . SER A 108 ? 1.9255 2.3044 2.3803 -0.3573 -0.0183 0.3245  108 SER A C   
845  O O   . SER A 108 ? 1.9242 2.3325 2.4088 -0.3523 -0.0281 0.3287  108 SER A O   
846  C CB  . SER A 108 ? 2.0256 2.3899 2.4889 -0.3774 -0.0045 0.3368  108 SER A CB  
847  O OG  . SER A 108 ? 2.0978 2.4436 2.5599 -0.3997 -0.0146 0.3410  108 SER A OG  
848  N N   . GLY A 109 ? 1.4028 1.7670 1.8283 -0.3423 0.0019  0.3171  109 GLY A N   
849  C CA  . GLY A 109 ? 1.3087 1.6927 1.7380 -0.3187 0.0150  0.3140  109 GLY A CA  
850  C C   . GLY A 109 ? 1.1833 1.5611 1.5987 -0.3195 -0.0047 0.3047  109 GLY A C   
851  O O   . GLY A 109 ? 1.1981 1.5538 1.5972 -0.3377 -0.0290 0.2999  109 GLY A O   
852  N N   . GLN A 110 ? 1.0757 1.4718 1.4959 -0.2983 0.0065  0.3019  110 GLN A N   
853  C CA  . GLN A 110 ? 0.9750 1.3675 1.3829 -0.2956 -0.0081 0.2933  110 GLN A CA  
854  C C   . GLN A 110 ? 0.9396 1.2921 1.2929 -0.2874 -0.0024 0.2758  110 GLN A C   
855  O O   . GLN A 110 ? 0.9532 1.2909 1.2851 -0.2766 0.0172  0.2714  110 GLN A O   
856  C CB  . GLN A 110 ? 0.9097 1.3419 1.3517 -0.2743 0.0003  0.2982  110 GLN A CB  
857  C CG  . GLN A 110 ? 0.9274 1.3608 1.3649 -0.2729 -0.0173 0.2917  110 GLN A CG  
858  C CD  . GLN A 110 ? 0.9988 1.4345 1.4511 -0.2914 -0.0457 0.2959  110 GLN A CD  
859  O OE1 . GLN A 110 ? 1.0145 1.4237 1.4485 -0.3123 -0.0610 0.2942  110 GLN A OE1 
860  N NE2 . GLN A 110 ? 1.0024 1.4680 1.4861 -0.2829 -0.0530 0.3015  110 GLN A NE2 
861  N N   . SER A 111 ? 0.7921 1.1230 1.1187 -0.2887 -0.0197 0.2630  111 SER A N   
862  C CA  . SER A 111 ? 0.7981 1.0858 1.0695 -0.2795 -0.0173 0.2434  111 SER A CA  
863  C C   . SER A 111 ? 0.7338 1.0304 0.9998 -0.2508 -0.0017 0.2341  111 SER A C   
864  O O   . SER A 111 ? 0.6764 0.9900 0.9565 -0.2427 -0.0085 0.2330  111 SER A O   
865  C CB  . SER A 111 ? 0.7615 1.0197 1.0052 -0.2944 -0.0418 0.2347  111 SER A CB  
866  O OG  . SER A 111 ? 0.8365 1.0543 1.0292 -0.2849 -0.0379 0.2168  111 SER A OG  
867  N N   . GLN A 112 ? 0.6924 0.9757 0.9367 -0.2354 0.0183  0.2274  112 GLN A N   
868  C CA  . GLN A 112 ? 0.6677 0.9512 0.8987 -0.2092 0.0312  0.2161  112 GLN A CA  
869  C C   . GLN A 112 ? 0.6885 0.9362 0.8766 -0.2054 0.0233  0.1979  112 GLN A C   
870  O O   . GLN A 112 ? 0.6372 0.8848 0.8160 -0.1860 0.0297  0.1880  112 GLN A O   
871  C CB  . GLN A 112 ? 0.7587 1.0417 0.9829 -0.1937 0.0547  0.2165  112 GLN A CB  
872  C CG  . GLN A 112 ? 0.6907 1.0085 0.9557 -0.1939 0.0675  0.2348  112 GLN A CG  
873  C CD  . GLN A 112 ? 0.5340 0.8483 0.7870 -0.1755 0.0917  0.2343  112 GLN A CD  
874  O OE1 . GLN A 112 ? 0.6695 0.9600 0.8875 -0.1597 0.0981  0.2198  112 GLN A OE1 
875  N NE2 . GLN A 112 ? 0.5045 0.8423 0.7868 -0.1774 0.1052  0.2507  112 GLN A NE2 
876  N N   . LEU A 113 ? 0.8002 1.0169 0.9620 -0.2233 0.0099  0.1935  113 LEU A N   
877  C CA  . LEU A 113 ? 0.7278 0.9080 0.8469 -0.2194 0.0052  0.1770  113 LEU A CA  
878  C C   . LEU A 113 ? 0.7171 0.8975 0.8366 -0.2229 -0.0116 0.1735  113 LEU A C   
879  O O   . LEU A 113 ? 0.7642 0.9123 0.8510 -0.2301 -0.0220 0.1644  113 LEU A O   
880  C CB  . LEU A 113 ? 0.7263 0.8690 0.8122 -0.2348 0.0010  0.1738  113 LEU A CB  
881  C CG  . LEU A 113 ? 0.6640 0.8042 0.7494 -0.2352 0.0157  0.1795  113 LEU A CG  
882  C CD1 . LEU A 113 ? 0.6934 0.7940 0.7451 -0.2520 0.0091  0.1766  113 LEU A CD1 
883  C CD2 . LEU A 113 ? 0.7299 0.8706 0.8046 -0.2105 0.0353  0.1718  113 LEU A CD2 
884  N N   . GLY A 114 ? 0.8924 1.1076 1.0473 -0.2171 -0.0137 0.1809  114 GLY A N   
885  C CA  . GLY A 114 ? 1.0003 1.2170 1.1566 -0.2187 -0.0290 0.1783  114 GLY A CA  
886  C C   . GLY A 114 ? 0.9417 1.1888 1.1372 -0.2313 -0.0432 0.1933  114 GLY A C   
887  O O   . GLY A 114 ? 0.9520 1.2125 1.1695 -0.2456 -0.0456 0.2056  114 GLY A O   
888  N N   . ARG A 115 ? 0.8603 1.1187 1.0657 -0.2264 -0.0530 0.1929  115 ARG A N   
889  C CA  . ARG A 115 ? 0.9332 1.2210 1.1759 -0.2366 -0.0685 0.2066  115 ARG A CA  
890  C C   . ARG A 115 ? 0.8826 1.1454 1.1020 -0.2508 -0.0918 0.2024  115 ARG A C   
891  O O   . ARG A 115 ? 0.9121 1.1573 1.1069 -0.2411 -0.0935 0.1916  115 ARG A O   
892  C CB  . ARG A 115 ? 0.9521 1.2759 1.2280 -0.2171 -0.0602 0.2113  115 ARG A CB  
893  C CG  . ARG A 115 ? 1.0054 1.3642 1.3251 -0.2253 -0.0748 0.2270  115 ARG A CG  
894  C CD  . ARG A 115 ? 1.1106 1.5012 1.4589 -0.2036 -0.0654 0.2307  115 ARG A CD  
895  N NE  . ARG A 115 ? 1.1594 1.5653 1.5189 -0.1860 -0.0402 0.2318  115 ARG A NE  
896  C CZ  . ARG A 115 ? 1.1555 1.5946 1.5540 -0.1855 -0.0302 0.2466  115 ARG A CZ  
897  N NH1 . ARG A 115 ? 0.9628 1.4268 1.3979 -0.2023 -0.0433 0.2624  115 ARG A NH1 
898  N NH2 . ARG A 115 ? 1.1324 1.5795 1.5332 -0.1675 -0.0064 0.2461  115 ARG A NH2 
899  N N   . TRP A 116 ? 0.9950 1.2553 1.2214 -0.2738 -0.1099 0.2113  116 TRP A N   
900  C CA  . TRP A 116 ? 1.0333 1.2657 1.2336 -0.2891 -0.1338 0.2079  116 TRP A CA  
901  C C   . TRP A 116 ? 1.0353 1.2982 1.2719 -0.2942 -0.1523 0.2199  116 TRP A C   
902  O O   . TRP A 116 ? 0.9806 1.2843 1.2660 -0.2966 -0.1518 0.2346  116 TRP A O   
903  C CB  . TRP A 116 ? 1.1100 1.3127 1.2879 -0.3123 -0.1449 0.2088  116 TRP A CB  
904  C CG  . TRP A 116 ? 1.1827 1.3525 1.3293 -0.3284 -0.1701 0.2053  116 TRP A CG  
905  C CD1 . TRP A 116 ? 1.2066 1.3318 1.3005 -0.3256 -0.1725 0.1910  116 TRP A CD1 
906  C CD2 . TRP A 116 ? 1.2418 1.4198 1.4070 -0.3494 -0.1968 0.2167  116 TRP A CD2 
907  N NE1 . TRP A 116 ? 1.1578 1.2601 1.2325 -0.3429 -0.1983 0.1924  116 TRP A NE1 
908  C CE2 . TRP A 116 ? 1.2741 1.4079 1.3916 -0.3581 -0.2148 0.2078  116 TRP A CE2 
909  C CE3 . TRP A 116 ? 1.2555 1.4739 1.4736 -0.3616 -0.2072 0.2340  116 TRP A CE3 
910  C CZ2 . TRP A 116 ? 1.3574 1.4840 1.4755 -0.3787 -0.2444 0.2149  116 TRP A CZ2 
911  C CZ3 . TRP A 116 ? 1.3084 1.5227 1.5315 -0.3825 -0.2370 0.2416  116 TRP A CZ3 
912  C CH2 . TRP A 116 ? 1.3344 1.5021 1.5064 -0.3911 -0.2562 0.2317  116 TRP A CH2 
913  N N   . MET A 117 ? 1.0618 1.3045 1.2743 -0.2952 -0.1680 0.2140  117 MET A N   
914  C CA  . MET A 117 ? 1.1036 1.3694 1.3438 -0.2995 -0.1880 0.2241  117 MET A CA  
915  C C   . MET A 117 ? 1.1972 1.4234 1.3972 -0.3150 -0.2128 0.2190  117 MET A C   
916  O O   . MET A 117 ? 1.1400 1.3242 1.2898 -0.3112 -0.2090 0.2048  117 MET A O   
917  C CB  . MET A 117 ? 1.0364 1.3258 1.2936 -0.2759 -0.1775 0.2228  117 MET A CB  
918  C CG  . MET A 117 ? 1.0809 1.3959 1.3683 -0.2778 -0.1971 0.2338  117 MET A CG  
919  S SD  . MET A 117 ? 0.7790 1.1189 1.0846 -0.2490 -0.1831 0.2323  117 MET A SD  
920  C CE  . MET A 117 ? 0.8523 1.2329 1.2008 -0.2348 -0.1556 0.2395  117 MET A CE  
921  N N   . SER A 118 ? 1.4210 1.6601 1.6430 -0.3320 -0.2381 0.2308  118 SER A N   
922  C CA  . SER A 118 ? 1.5052 1.7051 1.6882 -0.3484 -0.2644 0.2272  118 SER A CA  
923  C C   . SER A 118 ? 1.5251 1.7139 1.6879 -0.3355 -0.2702 0.2213  118 SER A C   
924  O O   . SER A 118 ? 1.4725 1.6913 1.6619 -0.3167 -0.2590 0.2233  118 SER A O   
925  C CB  . SER A 118 ? 1.4799 1.6977 1.6948 -0.3719 -0.2917 0.2424  118 SER A CB  
926  O OG  . SER A 118 ? 1.4536 1.7198 1.7216 -0.3612 -0.2932 0.2549  118 SER A OG  
927  N N   . GLU A 119 ? 1.3914 1.5337 1.5039 -0.3457 -0.2878 0.2140  119 GLU A N   
928  C CA  . GLU A 119 ? 1.3984 1.5245 1.4861 -0.3348 -0.2940 0.2086  119 GLU A CA  
929  C C   . GLU A 119 ? 1.3737 1.5365 1.5033 -0.3353 -0.3135 0.2222  119 GLU A C   
930  O O   . GLU A 119 ? 1.3074 1.4803 1.4415 -0.3187 -0.3094 0.2213  119 GLU A O   
931  C CB  . GLU A 119 ? 1.4926 1.5583 1.5146 -0.3458 -0.3082 0.1987  119 GLU A CB  
932  C CG  . GLU A 119 ? 1.5159 1.5418 1.4922 -0.3422 -0.2880 0.1846  119 GLU A CG  
933  C CD  . GLU A 119 ? 1.5370 1.5542 1.5124 -0.3595 -0.2898 0.1865  119 GLU A CD  
934  O OE1 . GLU A 119 ? 1.4946 1.5422 1.5112 -0.3736 -0.3037 0.1992  119 GLU A OE1 
935  O OE2 . GLU A 119 ? 1.5512 1.5309 1.4852 -0.3590 -0.2772 0.1756  119 GLU A OE2 
936  N N   . GLU A 120 ? 1.3496 1.5327 1.5110 -0.3544 -0.3351 0.2353  120 GLU A N   
937  C CA  . GLU A 120 ? 1.2687 1.4867 1.4715 -0.3527 -0.3523 0.2487  120 GLU A CA  
938  C C   . GLU A 120 ? 1.2134 1.4876 1.4736 -0.3342 -0.3335 0.2568  120 GLU A C   
939  O O   . GLU A 120 ? 1.1045 1.3979 1.3815 -0.3213 -0.3376 0.2610  120 GLU A O   
940  C CB  . GLU A 120 ? 1.2716 1.4915 1.4905 -0.3679 -0.3686 0.2583  120 GLU A CB  
941  C CG  . GLU A 120 ? 1.3807 1.5437 1.5425 -0.3850 -0.3897 0.2516  120 GLU A CG  
942  C CD  . GLU A 120 ? 1.4248 1.5518 1.5475 -0.3945 -0.3792 0.2410  120 GLU A CD  
943  O OE1 . GLU A 120 ? 1.3687 1.5196 1.5176 -0.3917 -0.3584 0.2420  120 GLU A OE1 
944  O OE2 . GLU A 120 ? 1.4882 1.5611 1.5523 -0.4039 -0.3909 0.2319  120 GLU A OE2 
945  N N   . ASP A 121 ? 1.3130 1.6115 1.6012 -0.3314 -0.3118 0.2591  121 ASP A N   
946  C CA  . ASP A 121 ? 1.2561 1.6019 1.5920 -0.3106 -0.2898 0.2654  121 ASP A CA  
947  C C   . ASP A 121 ? 1.2160 1.5472 1.5247 -0.2862 -0.2695 0.2524  121 ASP A C   
948  O O   . ASP A 121 ? 1.1564 1.5194 1.4962 -0.2676 -0.2594 0.2571  121 ASP A O   
949  C CB  . ASP A 121 ? 1.3280 1.6962 1.6921 -0.3126 -0.2700 0.2699  121 ASP A CB  
950  C CG  . ASP A 121 ? 1.2953 1.6689 1.6788 -0.3282 -0.2817 0.2799  121 ASP A CG  
951  O OD1 . ASP A 121 ? 1.2782 1.6614 1.6787 -0.3316 -0.3008 0.2884  121 ASP A OD1 
952  O OD2 . ASP A 121 ? 1.2709 1.6381 1.6519 -0.3368 -0.2716 0.2792  121 ASP A OD2 
953  N N   . PHE A 122 ? 1.1685 1.4516 1.4202 -0.2859 -0.2632 0.2364  122 PHE A N   
954  C CA  . PHE A 122 ? 1.1174 1.3855 1.3439 -0.2644 -0.2446 0.2242  122 PHE A CA  
955  C C   . PHE A 122 ? 1.1267 1.3862 1.3413 -0.2586 -0.2597 0.2245  122 PHE A C   
956  O O   . PHE A 122 ? 1.0203 1.2918 1.2433 -0.2389 -0.2476 0.2224  122 PHE A O   
957  C CB  . PHE A 122 ? 1.0684 1.2901 1.2414 -0.2659 -0.2326 0.2082  122 PHE A CB  
958  C CG  . PHE A 122 ? 1.1232 1.3235 1.2659 -0.2475 -0.2179 0.1957  122 PHE A CG  
959  C CD1 . PHE A 122 ? 1.0194 1.2425 1.1828 -0.2269 -0.1954 0.1930  122 PHE A CD1 
960  C CD2 . PHE A 122 ? 1.1028 1.2587 1.1955 -0.2510 -0.2266 0.1868  122 PHE A CD2 
961  C CE1 . PHE A 122 ? 0.8850 1.0884 1.0225 -0.2115 -0.1831 0.1818  122 PHE A CE1 
962  C CE2 . PHE A 122 ? 1.0133 1.1506 1.0809 -0.2350 -0.2124 0.1763  122 PHE A CE2 
963  C CZ  . PHE A 122 ? 0.9188 1.0806 1.0102 -0.2158 -0.1912 0.1738  122 PHE A CZ  
964  N N   . GLU A 123 ? 1.1525 1.3889 1.3453 -0.2755 -0.2867 0.2271  123 GLU A N   
965  C CA  . GLU A 123 ? 1.0505 1.2765 1.2294 -0.2705 -0.3026 0.2282  123 GLU A CA  
966  C C   . GLU A 123 ? 0.9216 1.1976 1.1565 -0.2607 -0.3079 0.2424  123 GLU A C   
967  O O   . GLU A 123 ? 0.8695 1.1455 1.1007 -0.2465 -0.3087 0.2420  123 GLU A O   
968  C CB  . GLU A 123 ? 1.0827 1.2727 1.2258 -0.2914 -0.3321 0.2287  123 GLU A CB  
969  C CG  . GLU A 123 ? 1.1034 1.2766 1.2251 -0.2871 -0.3500 0.2298  123 GLU A CG  
970  C CD  . GLU A 123 ? 1.4303 1.5624 1.5099 -0.3074 -0.3793 0.2294  123 GLU A CD  
971  O OE1 . GLU A 123 ? 1.6052 1.7181 1.6685 -0.3245 -0.3844 0.2268  123 GLU A OE1 
972  O OE2 . GLU A 123 ? 1.3561 1.4729 1.4169 -0.3059 -0.3976 0.2315  123 GLU A OE2 
973  N N   . LYS A 124 ? 1.0286 1.3470 1.3158 -0.2675 -0.3107 0.2555  124 LYS A N   
974  C CA  . LYS A 124 ? 0.9188 1.2875 1.2629 -0.2569 -0.3138 0.2703  124 LYS A CA  
975  C C   . LYS A 124 ? 0.8403 1.2279 1.1991 -0.2305 -0.2846 0.2664  124 LYS A C   
976  O O   . LYS A 124 ? 0.8375 1.2434 1.2147 -0.2152 -0.2857 0.2715  124 LYS A O   
977  C CB  . LYS A 124 ? 0.9318 1.3380 1.3264 -0.2693 -0.3193 0.2848  124 LYS A CB  
978  C CG  . LYS A 124 ? 0.9772 1.3550 1.3503 -0.2919 -0.3428 0.2858  124 LYS A CG  
979  C CD  . LYS A 124 ? 1.1275 1.5293 1.5378 -0.3011 -0.3382 0.2953  124 LYS A CD  
980  C CE  . LYS A 124 ? 1.0786 1.4483 1.4638 -0.3241 -0.3614 0.2953  124 LYS A CE  
981  N NZ  . LYS A 124 ? 1.0507 1.4395 1.4677 -0.3344 -0.3562 0.3035  124 LYS A NZ  
982  N N   . ALA A 125 ? 0.9911 1.3726 1.3403 -0.2246 -0.2592 0.2573  125 ALA A N   
983  C CA  . ALA A 125 ? 0.9012 1.2961 1.2597 -0.2001 -0.2324 0.2523  125 ALA A CA  
984  C C   . ALA A 125 ? 0.8155 1.1730 1.1279 -0.1883 -0.2266 0.2380  125 ALA A C   
985  O O   . ALA A 125 ? 0.8058 1.1742 1.1274 -0.1681 -0.2134 0.2364  125 ALA A O   
986  C CB  . ALA A 125 ? 0.9190 1.3198 1.2828 -0.1981 -0.2087 0.2481  125 ALA A CB  
987  N N   . PHE A 126 ? 0.8551 1.1678 1.1177 -0.2005 -0.2355 0.2278  126 PHE A N   
988  C CA  . PHE A 126 ? 0.8536 1.1303 1.0729 -0.1902 -0.2290 0.2151  126 PHE A CA  
989  C C   . PHE A 126 ? 0.8805 1.1618 1.1049 -0.1819 -0.2423 0.2209  126 PHE A C   
990  O O   . PHE A 126 ? 0.8633 1.1407 1.0816 -0.1643 -0.2298 0.2158  126 PHE A O   
991  C CB  . PHE A 126 ? 0.9405 1.1685 1.1063 -0.2052 -0.2359 0.2048  126 PHE A CB  
992  C CG  . PHE A 126 ? 0.9495 1.1396 1.0708 -0.1959 -0.2287 0.1928  126 PHE A CG  
993  C CD1 . PHE A 126 ? 0.9076 1.0866 1.0149 -0.1837 -0.2042 0.1811  126 PHE A CD1 
994  C CD2 . PHE A 126 ? 0.9794 1.1444 1.0731 -0.1997 -0.2467 0.1938  126 PHE A CD2 
995  C CE1 . PHE A 126 ? 0.9238 1.0697 0.9939 -0.1760 -0.1971 0.1711  126 PHE A CE1 
996  C CE2 . PHE A 126 ? 1.1114 1.2414 1.1649 -0.1913 -0.2385 0.1838  126 PHE A CE2 
997  C CZ  . PHE A 126 ? 0.8872 1.0087 0.9306 -0.1797 -0.2133 0.1727  126 PHE A CZ  
998  N N   . ASN A 127 ? 0.8691 1.1575 1.1042 -0.1946 -0.2687 0.2320  127 ASN A N   
999  C CA  . ASN A 127 ? 0.8233 1.1155 1.0628 -0.1874 -0.2841 0.2387  127 ASN A CA  
1000 C C   . ASN A 127 ? 0.7799 1.1202 1.0733 -0.1702 -0.2770 0.2498  127 ASN A C   
1001 O O   . ASN A 127 ? 0.8211 1.1680 1.1223 -0.1620 -0.2886 0.2563  127 ASN A O   
1002 C CB  . ASN A 127 ? 0.7744 1.0579 1.0073 -0.2069 -0.3167 0.2471  127 ASN A CB  
1003 C CG  . ASN A 127 ? 0.8395 1.0688 1.0115 -0.2218 -0.3250 0.2360  127 ASN A CG  
1004 O OD1 . ASN A 127 ? 0.8072 1.0009 0.9365 -0.2141 -0.3113 0.2235  127 ASN A OD1 
1005 N ND2 . ASN A 127 ? 0.9837 1.2058 1.1516 -0.2433 -0.3472 0.2409  127 ASN A ND2 
1006 N N   . ALA A 128 ? 0.7646 1.1366 1.0931 -0.1637 -0.2579 0.2522  128 ALA A N   
1007 C CA  . ALA A 128 ? 0.7316 1.1479 1.1096 -0.1458 -0.2481 0.2627  128 ALA A CA  
1008 C C   . ALA A 128 ? 0.7030 1.1151 1.0732 -0.1238 -0.2200 0.2525  128 ALA A C   
1009 O O   . ALA A 128 ? 0.5907 1.0363 0.9980 -0.1074 -0.2069 0.2594  128 ALA A O   
1010 C CB  . ALA A 128 ? 0.6200 1.0785 1.0480 -0.1534 -0.2473 0.2756  128 ALA A CB  
1011 N N   . ARG A 129 ? 0.8032 1.1744 1.1260 -0.1229 -0.2106 0.2367  129 ARG A N   
1012 C CA  . ARG A 129 ? 0.7973 1.1623 1.1115 -0.1041 -0.1855 0.2262  129 ARG A CA  
1013 C C   . ARG A 129 ? 0.8253 1.1518 1.0975 -0.0980 -0.1849 0.2152  129 ARG A C   
1014 O O   . ARG A 129 ? 0.8368 1.1665 1.1141 -0.0809 -0.1787 0.2152  129 ARG A O   
1015 C CB  . ARG A 129 ? 0.7281 1.0867 1.0331 -0.1083 -0.1682 0.2174  129 ARG A CB  
1016 C CG  . ARG A 129 ? 0.6171 1.0076 0.9575 -0.1177 -0.1685 0.2277  129 ARG A CG  
1017 C CD  . ARG A 129 ? 0.7228 1.0989 1.0453 -0.1234 -0.1533 0.2179  129 ARG A CD  
1018 N NE  . ARG A 129 ? 0.8176 1.2174 1.1678 -0.1363 -0.1557 0.2277  129 ARG A NE  
1019 C CZ  . ARG A 129 ? 0.7839 1.2145 1.1671 -0.1278 -0.1395 0.2338  129 ARG A CZ  
1020 N NH1 . ARG A 129 ? 0.7068 1.1474 1.0979 -0.1059 -0.1201 0.2307  129 ARG A NH1 
1021 N NH2 . ARG A 129 ? 0.8214 1.2712 1.2286 -0.1418 -0.1426 0.2434  129 ARG A NH2 
1022 N N   . PHE A 130 ? 0.8176 1.1065 1.0478 -0.1117 -0.1906 0.2062  130 PHE A N   
1023 C CA  . PHE A 130 ? 0.9304 1.1803 1.1186 -0.1070 -0.1857 0.1948  130 PHE A CA  
1024 C C   . PHE A 130 ? 0.9763 1.2170 1.1563 -0.1026 -0.2006 0.2003  130 PHE A C   
1025 O O   . PHE A 130 ? 1.0380 1.2640 1.2043 -0.0894 -0.1913 0.1948  130 PHE A O   
1026 C CB  . PHE A 130 ? 0.9503 1.1633 1.0967 -0.1228 -0.1874 0.1854  130 PHE A CB  
1027 C CG  . PHE A 130 ? 0.9951 1.2053 1.1374 -0.1221 -0.1676 0.1757  130 PHE A CG  
1028 C CD1 . PHE A 130 ? 0.9390 1.1685 1.1009 -0.1312 -0.1670 0.1794  130 PHE A CD1 
1029 C CD2 . PHE A 130 ? 0.9435 1.1319 1.0633 -0.1126 -0.1501 0.1634  130 PHE A CD2 
1030 C CE1 . PHE A 130 ? 0.8791 1.1046 1.0356 -0.1298 -0.1493 0.1708  130 PHE A CE1 
1031 C CE2 . PHE A 130 ? 0.9139 1.1001 1.0304 -0.1115 -0.1335 0.1548  130 PHE A CE2 
1032 C CZ  . PHE A 130 ? 0.9015 1.1055 1.0351 -0.1196 -0.1330 0.1583  130 PHE A CZ  
1033 N N   . PRO A 131 ? 0.9650 1.2123 1.1518 -0.1135 -0.2244 0.2111  131 PRO A N   
1034 C CA  . PRO A 131 ? 0.9242 1.1602 1.1000 -0.1089 -0.2397 0.2165  131 PRO A CA  
1035 C C   . PRO A 131 ? 0.8656 1.1186 1.0629 -0.0870 -0.2290 0.2191  131 PRO A C   
1036 O O   . PRO A 131 ? 0.7769 1.0684 1.0174 -0.0788 -0.2318 0.2303  131 PRO A O   
1037 C CB  . PRO A 131 ? 0.9096 1.1666 1.1082 -0.1217 -0.2660 0.2304  131 PRO A CB  
1038 C CG  . PRO A 131 ? 0.9072 1.1609 1.1009 -0.1398 -0.2675 0.2275  131 PRO A CG  
1039 C CD  . PRO A 131 ? 0.8882 1.1500 1.0901 -0.1315 -0.2397 0.2187  131 PRO A CD  
1040 N N   . GLY A 132 ? 0.9331 1.1568 1.1006 -0.0774 -0.2163 0.2091  132 GLY A N   
1041 C CA  . GLY A 132 ? 0.8360 1.0682 1.0170 -0.0572 -0.2065 0.2103  132 GLY A CA  
1042 C C   . GLY A 132 ? 0.7932 1.0394 0.9914 -0.0440 -0.1824 0.2034  132 GLY A C   
1043 O O   . GLY A 132 ? 0.8174 1.0772 1.0341 -0.0265 -0.1749 0.2062  132 GLY A O   
1044 N N   . CYS A 133 ? 0.7448 0.9861 0.9353 -0.0513 -0.1704 0.1944  133 CYS A N   
1045 C CA  . CYS A 133 ? 0.7794 1.0336 0.9850 -0.0391 -0.1489 0.1880  133 CYS A CA  
1046 C C   . CYS A 133 ? 0.8092 1.0359 0.9906 -0.0283 -0.1349 0.1765  133 CYS A C   
1047 O O   . CYS A 133 ? 0.8594 1.0961 1.0546 -0.0135 -0.1203 0.1731  133 CYS A O   
1048 C CB  . CYS A 133 ? 0.7385 0.9963 0.9438 -0.0505 -0.1418 0.1829  133 CYS A CB  
1049 S SG  . CYS A 133 ? 0.8016 1.0158 0.9585 -0.0675 -0.1428 0.1709  133 CYS A SG  
1050 N N   . MET A 134 ? 0.8744 1.0654 1.0194 -0.0354 -0.1388 0.1706  134 MET A N   
1051 C CA  . MET A 134 ? 0.8590 1.0232 0.9823 -0.0272 -0.1261 0.1606  134 MET A CA  
1052 C C   . MET A 134 ? 0.9045 1.0587 1.0229 -0.0171 -0.1321 0.1655  134 MET A C   
1053 O O   . MET A 134 ? 0.8931 1.0178 0.9864 -0.0148 -0.1260 0.1590  134 MET A O   
1054 C CB  . MET A 134 ? 0.8508 0.9812 0.9376 -0.0400 -0.1227 0.1511  134 MET A CB  
1055 C CG  . MET A 134 ? 0.7704 0.9060 0.8584 -0.0481 -0.1143 0.1445  134 MET A CG  
1056 S SD  . MET A 134 ? 0.6196 0.7150 0.6662 -0.0590 -0.1067 0.1330  134 MET A SD  
1057 C CE  . MET A 134 ? 0.6950 0.8039 0.7503 -0.0665 -0.0993 0.1281  134 MET A CE  
1058 N N   . LYS A 135 ? 1.0180 1.1966 1.1611 -0.0109 -0.1435 0.1777  135 LYS A N   
1059 C CA  . LYS A 135 ? 1.0529 1.2232 1.1926 -0.0001 -0.1500 0.1835  135 LYS A CA  
1060 C C   . LYS A 135 ? 1.0393 1.2012 1.1792 0.0164  -0.1335 0.1766  135 LYS A C   
1061 O O   . LYS A 135 ? 1.0518 1.2374 1.2182 0.0289  -0.1244 0.1773  135 LYS A O   
1062 C CB  . LYS A 135 ? 1.1764 1.3799 1.3489 0.0051  -0.1644 0.1984  135 LYS A CB  
1063 C CG  . LYS A 135 ? 1.4330 1.6303 1.6045 0.0180  -0.1719 0.2057  135 LYS A CG  
1064 C CD  . LYS A 135 ? 1.4616 1.6963 1.6708 0.0239  -0.1857 0.2212  135 LYS A CD  
1065 C CE  . LYS A 135 ? 1.5665 1.7958 1.7759 0.0389  -0.1925 0.2288  135 LYS A CE  
1066 N NZ  . LYS A 135 ? 1.6644 1.8573 1.8352 0.0304  -0.2062 0.2288  135 LYS A NZ  
1067 N N   . GLY A 136 ? 0.9443 1.0713 1.0540 0.0163  -0.1295 0.1701  136 GLY A N   
1068 C CA  . GLY A 136 ? 0.8825 0.9971 0.9900 0.0300  -0.1158 0.1634  136 GLY A CA  
1069 C C   . GLY A 136 ? 0.8995 1.0041 1.0000 0.0279  -0.0995 0.1501  136 GLY A C   
1070 O O   . GLY A 136 ? 0.8202 0.9157 0.9209 0.0388  -0.0888 0.1440  136 GLY A O   
1071 N N   . ARG A 137 ? 0.8322 0.9372 0.9264 0.0142  -0.0979 0.1454  137 ARG A N   
1072 C CA  . ARG A 137 ? 0.6705 0.7672 0.7589 0.0117  -0.0836 0.1332  137 ARG A CA  
1073 C C   . ARG A 137 ? 0.7874 0.8535 0.8453 -0.0015 -0.0819 0.1273  137 ARG A C   
1074 O O   . ARG A 137 ? 0.8497 0.9002 0.8887 -0.0091 -0.0916 0.1326  137 ARG A O   
1075 C CB  . ARG A 137 ? 0.6361 0.7598 0.7439 0.0089  -0.0806 0.1323  137 ARG A CB  
1076 C CG  . ARG A 137 ? 0.7213 0.8756 0.8597 0.0231  -0.0788 0.1381  137 ARG A CG  
1077 C CD  . ARG A 137 ? 0.7603 0.9379 0.9152 0.0201  -0.0733 0.1369  137 ARG A CD  
1078 N NE  . ARG A 137 ? 0.8240 1.0300 1.0073 0.0348  -0.0691 0.1430  137 ARG A NE  
1079 C CZ  . ARG A 137 ? 0.7861 0.9920 0.9737 0.0494  -0.0567 0.1370  137 ARG A CZ  
1080 N NH1 . ARG A 137 ? 0.8878 1.0685 1.0560 0.0506  -0.0488 0.1247  137 ARG A NH1 
1081 N NH2 . ARG A 137 ? 0.7858 1.0170 0.9977 0.0633  -0.0522 0.1437  137 ARG A NH2 
1082 N N   . THR A 138 ? 0.7078 0.7648 0.7607 -0.0036 -0.0693 0.1167  138 THR A N   
1083 C CA  . THR A 138 ? 0.7203 0.7502 0.7475 -0.0146 -0.0642 0.1108  138 THR A CA  
1084 C C   . THR A 138 ? 0.6494 0.6861 0.6738 -0.0257 -0.0636 0.1080  138 THR A C   
1085 O O   . THR A 138 ? 0.5930 0.6505 0.6356 -0.0232 -0.0594 0.1049  138 THR A O   
1086 C CB  . THR A 138 ? 0.6838 0.6983 0.7086 -0.0099 -0.0509 0.1014  138 THR A CB  
1087 O OG1 . THR A 138 ? 0.9022 0.9073 0.9277 -0.0001 -0.0517 0.1040  138 THR A OG1 
1088 C CG2 . THR A 138 ? 0.5578 0.5464 0.5592 -0.0207 -0.0443 0.0967  138 THR A CG2 
1089 N N   . MET A 139 ? 0.6130 0.6296 0.6123 -0.0374 -0.0675 0.1092  139 MET A N   
1090 C CA  . MET A 139 ? 0.6593 0.6757 0.6500 -0.0486 -0.0671 0.1065  139 MET A CA  
1091 C C   . MET A 139 ? 0.6159 0.6111 0.5910 -0.0517 -0.0529 0.0972  139 MET A C   
1092 O O   . MET A 139 ? 0.6880 0.6561 0.6396 -0.0550 -0.0498 0.0969  139 MET A O   
1093 C CB  . MET A 139 ? 0.5740 0.5795 0.5444 -0.0594 -0.0813 0.1138  139 MET A CB  
1094 C CG  . MET A 139 ? 0.6672 0.6621 0.6197 -0.0717 -0.0801 0.1102  139 MET A CG  
1095 S SD  . MET A 139 ? 0.7246 0.6965 0.6442 -0.0846 -0.0973 0.1175  139 MET A SD  
1096 C CE  . MET A 139 ? 0.7341 0.7415 0.6847 -0.0847 -0.1164 0.1283  139 MET A CE  
1097 N N   . TYR A 140 ? 0.5840 0.5917 0.5727 -0.0502 -0.0440 0.0901  140 TYR A N   
1098 C CA  . TYR A 140 ? 0.5561 0.5481 0.5350 -0.0527 -0.0310 0.0816  140 TYR A CA  
1099 C C   . TYR A 140 ? 0.5718 0.5534 0.5313 -0.0637 -0.0310 0.0809  140 TYR A C   
1100 O O   . TYR A 140 ? 0.6711 0.6679 0.6369 -0.0677 -0.0371 0.0827  140 TYR A O   
1101 C CB  . TYR A 140 ? 0.6232 0.6319 0.6247 -0.0449 -0.0226 0.0742  140 TYR A CB  
1102 C CG  . TYR A 140 ? 0.6128 0.6293 0.6312 -0.0333 -0.0224 0.0740  140 TYR A CG  
1103 C CD1 . TYR A 140 ? 0.5753 0.5743 0.5898 -0.0302 -0.0164 0.0708  140 TYR A CD1 
1104 C CD2 . TYR A 140 ? 0.5697 0.6099 0.6078 -0.0252 -0.0275 0.0772  140 TYR A CD2 
1105 C CE1 . TYR A 140 ? 0.6393 0.6421 0.6669 -0.0197 -0.0168 0.0702  140 TYR A CE1 
1106 C CE2 . TYR A 140 ? 0.6110 0.6554 0.6615 -0.0134 -0.0267 0.0768  140 TYR A CE2 
1107 C CZ  . TYR A 140 ? 0.6830 0.7075 0.7271 -0.0109 -0.0219 0.0729  140 TYR A CZ  
1108 O OH  . TYR A 140 ? 0.7302 0.7556 0.7843 0.0006  -0.0217 0.0722  140 TYR A OH  
1109 N N   . VAL A 141 ? 0.6209 0.5757 0.5567 -0.0685 -0.0236 0.0785  141 VAL A N   
1110 C CA  . VAL A 141 ? 0.6667 0.6062 0.5801 -0.0775 -0.0211 0.0768  141 VAL A CA  
1111 C C   . VAL A 141 ? 0.6456 0.5878 0.5679 -0.0751 -0.0070 0.0684  141 VAL A C   
1112 O O   . VAL A 141 ? 0.5974 0.5288 0.5201 -0.0718 0.0040  0.0648  141 VAL A O   
1113 C CB  . VAL A 141 ? 0.6430 0.5490 0.5215 -0.0830 -0.0207 0.0801  141 VAL A CB  
1114 C CG1 . VAL A 141 ? 0.6649 0.5529 0.5171 -0.0916 -0.0189 0.0785  141 VAL A CG1 
1115 C CG2 . VAL A 141 ? 0.7308 0.6341 0.6016 -0.0839 -0.0359 0.0885  141 VAL A CG2 
1116 N N   . ILE A 142 ? 0.6778 0.6343 0.6082 -0.0770 -0.0076 0.0657  142 ILE A N   
1117 C CA  . ILE A 142 ? 0.6501 0.6128 0.5919 -0.0734 0.0037  0.0580  142 ILE A CA  
1118 C C   . ILE A 142 ? 0.6027 0.5479 0.5221 -0.0803 0.0094  0.0558  142 ILE A C   
1119 O O   . ILE A 142 ? 0.7372 0.6860 0.6503 -0.0858 0.0035  0.0572  142 ILE A O   
1120 C CB  . ILE A 142 ? 0.5817 0.5731 0.5494 -0.0681 0.0006  0.0562  142 ILE A CB  
1121 C CG1 . ILE A 142 ? 0.5711 0.5775 0.5585 -0.0599 -0.0042 0.0585  142 ILE A CG1 
1122 C CG2 . ILE A 142 ? 0.6374 0.6331 0.6146 -0.0640 0.0109  0.0481  142 ILE A CG2 
1123 C CD1 . ILE A 142 ? 0.5567 0.5897 0.5667 -0.0535 -0.0067 0.0581  142 ILE A CD1 
1124 N N   . PRO A 143 ? 0.6648 0.5903 0.5719 -0.0800 0.0213  0.0528  143 PRO A N   
1125 C CA  . PRO A 143 ? 0.7650 0.6736 0.6514 -0.0843 0.0287  0.0504  143 PRO A CA  
1126 C C   . PRO A 143 ? 0.8578 0.7792 0.7626 -0.0793 0.0380  0.0436  143 PRO A C   
1127 O O   . PRO A 143 ? 0.8650 0.7879 0.7837 -0.0739 0.0475  0.0402  143 PRO A O   
1128 C CB  . PRO A 143 ? 0.6572 0.5371 0.5203 -0.0855 0.0377  0.0523  143 PRO A CB  
1129 C CG  . PRO A 143 ? 0.7337 0.6208 0.6158 -0.0800 0.0393  0.0532  143 PRO A CG  
1130 C CD  . PRO A 143 ? 0.6514 0.5677 0.5622 -0.0758 0.0291  0.0525  143 PRO A CD  
1131 N N   . PHE A 144 ? 0.7843 0.7145 0.6896 -0.0812 0.0348  0.0420  144 PHE A N   
1132 C CA  . PHE A 144 ? 0.7984 0.7408 0.7196 -0.0760 0.0418  0.0360  144 PHE A CA  
1133 C C   . PHE A 144 ? 0.8199 0.7447 0.7187 -0.0797 0.0481  0.0345  144 PHE A C   
1134 O O   . PHE A 144 ? 0.8866 0.7892 0.7568 -0.0865 0.0464  0.0379  144 PHE A O   
1135 C CB  . PHE A 144 ? 0.7291 0.6977 0.6714 -0.0729 0.0339  0.0354  144 PHE A CB  
1136 C CG  . PHE A 144 ? 0.7626 0.7333 0.6945 -0.0802 0.0244  0.0401  144 PHE A CG  
1137 C CD1 . PHE A 144 ? 0.7958 0.7706 0.7270 -0.0844 0.0134  0.0466  144 PHE A CD1 
1138 C CD2 . PHE A 144 ? 0.7870 0.7558 0.7109 -0.0831 0.0261  0.0385  144 PHE A CD2 
1139 C CE1 . PHE A 144 ? 0.7388 0.7174 0.6641 -0.0922 0.0036  0.0516  144 PHE A CE1 
1140 C CE2 . PHE A 144 ? 0.7526 0.7230 0.6686 -0.0911 0.0171  0.0433  144 PHE A CE2 
1141 C CZ  . PHE A 144 ? 0.8626 0.8388 0.7806 -0.0961 0.0055  0.0500  144 PHE A CZ  
1142 N N   . SER A 145 ? 0.9931 0.9262 0.9036 -0.0745 0.0549  0.0294  145 SER A N   
1143 C CA  . SER A 145 ? 0.7665 0.6836 0.6577 -0.0761 0.0620  0.0276  145 SER A CA  
1144 C C   . SER A 145 ? 0.8419 0.7762 0.7480 -0.0719 0.0614  0.0237  145 SER A C   
1145 O O   . SER A 145 ? 0.8890 0.8388 0.8186 -0.0641 0.0648  0.0195  145 SER A O   
1146 C CB  . SER A 145 ? 0.8535 0.7547 0.7392 -0.0722 0.0763  0.0259  145 SER A CB  
1147 O OG  . SER A 145 ? 0.8404 0.7267 0.7087 -0.0717 0.0842  0.0241  145 SER A OG  
1148 N N   . MET A 146 ? 0.8310 0.7611 0.7226 -0.0773 0.0565  0.0252  146 MET A N   
1149 C CA  . MET A 146 ? 0.8029 0.7457 0.7040 -0.0737 0.0567  0.0223  146 MET A CA  
1150 C C   . MET A 146 ? 0.8857 0.8135 0.7755 -0.0698 0.0678  0.0185  146 MET A C   
1151 O O   . MET A 146 ? 0.8348 0.7398 0.6974 -0.0749 0.0704  0.0199  146 MET A O   
1152 C CB  . MET A 146 ? 0.7217 0.6663 0.6137 -0.0818 0.0473  0.0265  146 MET A CB  
1153 C CG  . MET A 146 ? 0.7106 0.6726 0.6166 -0.0849 0.0366  0.0314  146 MET A CG  
1154 S SD  . MET A 146 ? 0.7797 0.7720 0.7208 -0.0732 0.0366  0.0286  146 MET A SD  
1155 C CE  . MET A 146 ? 0.7598 0.7612 0.7054 -0.0687 0.0400  0.0256  146 MET A CE  
1156 N N   . GLY A 147 ? 0.9499 0.8894 0.8603 -0.0604 0.0738  0.0140  147 GLY A N   
1157 C CA  . GLY A 147 ? 0.9662 0.8951 0.8715 -0.0550 0.0845  0.0109  147 GLY A CA  
1158 C C   . GLY A 147 ? 1.0793 1.0020 0.9910 -0.0516 0.0940  0.0106  147 GLY A C   
1159 O O   . GLY A 147 ? 1.0625 0.9837 0.9759 -0.0548 0.0926  0.0131  147 GLY A O   
1160 N N   . PRO A 148 ? 1.2119 1.1312 1.1283 -0.0447 0.1042  0.0082  148 PRO A N   
1161 C CA  . PRO A 148 ? 1.2819 1.1968 1.2076 -0.0414 0.1151  0.0090  148 PRO A CA  
1162 C C   . PRO A 148 ? 1.4384 1.3266 1.3344 -0.0472 0.1214  0.0136  148 PRO A C   
1163 O O   . PRO A 148 ? 1.5098 1.3767 1.3740 -0.0513 0.1218  0.0151  148 PRO A O   
1164 C CB  . PRO A 148 ? 1.1775 1.0929 1.1108 -0.0329 0.1245  0.0066  148 PRO A CB  
1165 C CG  . PRO A 148 ? 1.0980 1.0259 1.0359 -0.0304 0.1157  0.0031  148 PRO A CG  
1166 C CD  . PRO A 148 ? 1.1532 1.0745 1.0695 -0.0390 0.1064  0.0052  148 PRO A CD  
1167 N N   . LEU A 149 ? 1.5057 1.3932 1.4106 -0.0475 0.1260  0.0160  149 LEU A N   
1168 C CA  . LEU A 149 ? 1.6075 1.4679 1.4828 -0.0519 0.1329  0.0206  149 LEU A CA  
1169 C C   . LEU A 149 ? 1.7504 1.5880 1.6046 -0.0476 0.1485  0.0215  149 LEU A C   
1170 O O   . LEU A 149 ? 1.7809 1.6275 1.6559 -0.0398 0.1592  0.0204  149 LEU A O   
1171 C CB  . LEU A 149 ? 1.5368 1.4012 1.4281 -0.0520 0.1365  0.0233  149 LEU A CB  
1172 C CG  . LEU A 149 ? 1.5095 1.3854 1.4087 -0.0571 0.1222  0.0242  149 LEU A CG  
1173 C CD1 . LEU A 149 ? 1.4188 1.2962 1.3334 -0.0565 0.1275  0.0269  149 LEU A CD1 
1174 C CD2 . LEU A 149 ? 1.4626 1.3201 1.3273 -0.0648 0.1133  0.0272  149 LEU A CD2 
1175 N N   . GLY A 150 ? 1.7164 1.5237 1.5289 -0.0523 0.1495  0.0237  150 GLY A N   
1176 C CA  . GLY A 150 ? 1.7043 1.4843 1.4894 -0.0478 0.1644  0.0247  150 GLY A CA  
1177 C C   . GLY A 150 ? 1.8042 1.5841 1.5851 -0.0440 0.1647  0.0212  150 GLY A C   
1178 O O   . GLY A 150 ? 1.8799 1.6329 1.6321 -0.0404 0.1760  0.0219  150 GLY A O   
1179 N N   . SER A 151 ? 1.9946 1.8012 1.8009 -0.0440 0.1532  0.0178  151 SER A N   
1180 C CA  . SER A 151 ? 1.9800 1.7865 1.7823 -0.0402 0.1531  0.0148  151 SER A CA  
1181 C C   . SER A 151 ? 2.0446 1.8270 1.8082 -0.0488 0.1448  0.0153  151 SER A C   
1182 O O   . SER A 151 ? 2.0430 1.8172 1.7908 -0.0585 0.1350  0.0175  151 SER A O   
1183 C CB  . SER A 151 ? 1.9068 1.7478 1.7464 -0.0370 0.1435  0.0113  151 SER A CB  
1184 O OG  . SER A 151 ? 1.8881 1.7424 1.7335 -0.0449 0.1284  0.0114  151 SER A OG  
1185 N N   . PRO A 152 ? 1.9952 1.7655 1.7433 -0.0458 0.1479  0.0135  152 PRO A N   
1186 C CA  . PRO A 152 ? 1.9954 1.7419 1.7076 -0.0551 0.1393  0.0140  152 PRO A CA  
1187 C C   . PRO A 152 ? 1.8825 1.6517 1.6104 -0.0636 0.1218  0.0140  152 PRO A C   
1188 O O   . PRO A 152 ? 1.8142 1.6152 1.5771 -0.0593 0.1181  0.0123  152 PRO A O   
1189 C CB  . PRO A 152 ? 2.0351 1.7666 1.7332 -0.0476 0.1483  0.0120  152 PRO A CB  
1190 C CG  . PRO A 152 ? 2.0188 1.7803 1.7572 -0.0356 0.1548  0.0099  152 PRO A CG  
1191 C CD  . PRO A 152 ? 2.0097 1.7866 1.7725 -0.0337 0.1589  0.0114  152 PRO A CD  
1192 N N   . LEU A 153 ? 1.7104 1.4620 1.4114 -0.0756 0.1110  0.0164  153 LEU A N   
1193 C CA  . LEU A 153 ? 1.5604 1.3324 1.2755 -0.0846 0.0949  0.0180  153 LEU A CA  
1194 C C   . LEU A 153 ? 1.3856 1.1884 1.1343 -0.0838 0.0894  0.0190  153 LEU A C   
1195 O O   . LEU A 153 ? 1.2834 1.1130 1.0566 -0.0853 0.0804  0.0195  153 LEU A O   
1196 C CB  . LEU A 153 ? 1.5378 1.3234 1.2649 -0.0819 0.0934  0.0163  153 LEU A CB  
1197 C CG  . LEU A 153 ? 1.3979 1.1532 1.0912 -0.0848 0.0959  0.0159  153 LEU A CG  
1198 C CD1 . LEU A 153 ? 1.1236 0.8948 0.8309 -0.0829 0.0931  0.0151  153 LEU A CD1 
1199 C CD2 . LEU A 153 ? 1.2937 1.0219 0.9535 -0.0994 0.0857  0.0192  153 LEU A CD2 
1200 N N   . ALA A 154 ? 1.4308 1.2285 1.1798 -0.0809 0.0956  0.0196  154 ALA A N   
1201 C CA  . ALA A 154 ? 1.3531 1.1749 1.1301 -0.0802 0.0909  0.0207  154 ALA A CA  
1202 C C   . ALA A 154 ? 1.2389 1.0499 0.9984 -0.0908 0.0796  0.0252  154 ALA A C   
1203 O O   . ALA A 154 ? 1.2104 0.9905 0.9366 -0.0946 0.0823  0.0269  154 ALA A O   
1204 C CB  . ALA A 154 ? 1.3376 1.1611 1.1279 -0.0711 0.1043  0.0195  154 ALA A CB  
1205 N N   . LYS A 155 ? 1.0756 0.9110 0.8564 -0.0948 0.0670  0.0273  155 LYS A N   
1206 C CA  . LYS A 155 ? 1.0747 0.9048 0.8441 -0.1047 0.0538  0.0322  155 LYS A CA  
1207 C C   . LYS A 155 ? 1.0094 0.8581 0.8022 -0.1013 0.0515  0.0338  155 LYS A C   
1208 O O   . LYS A 155 ? 0.9724 0.8469 0.7971 -0.0936 0.0545  0.0314  155 LYS A O   
1209 C CB  . LYS A 155 ? 1.0603 0.9027 0.8347 -0.1131 0.0402  0.0351  155 LYS A CB  
1210 C CG  . LYS A 155 ? 1.1462 0.9708 0.8991 -0.1171 0.0418  0.0337  155 LYS A CG  
1211 C CD  . LYS A 155 ? 1.1940 0.9766 0.9028 -0.1217 0.0448  0.0336  155 LYS A CD  
1212 C CE  . LYS A 155 ? 1.3163 1.0780 1.0017 -0.1250 0.0469  0.0319  155 LYS A CE  
1213 N NZ  . LYS A 155 ? 1.4909 1.2078 1.1293 -0.1285 0.0503  0.0314  155 LYS A NZ  
1214 N N   . ILE A 156 ? 1.1187 0.9518 0.8933 -0.1070 0.0454  0.0378  156 ILE A N   
1215 C CA  . ILE A 156 ? 1.0305 0.8757 0.8217 -0.1044 0.0428  0.0401  156 ILE A CA  
1216 C C   . ILE A 156 ? 0.9754 0.8293 0.7682 -0.1124 0.0251  0.0456  156 ILE A C   
1217 O O   . ILE A 156 ? 0.9407 0.7772 0.7084 -0.1220 0.0156  0.0486  156 ILE A O   
1218 C CB  . ILE A 156 ? 0.9968 0.8151 0.7655 -0.1024 0.0527  0.0409  156 ILE A CB  
1219 C CG1 . ILE A 156 ? 1.0254 0.8402 0.8000 -0.0936 0.0711  0.0365  156 ILE A CG1 
1220 C CG2 . ILE A 156 ? 1.0079 0.8357 0.7904 -0.1009 0.0485  0.0441  156 ILE A CG2 
1221 C CD1 . ILE A 156 ? 1.0578 0.8478 0.8135 -0.0907 0.0839  0.0382  156 ILE A CD1 
1222 N N   . GLY A 157 ? 0.9571 0.8376 0.7797 -0.1084 0.0203  0.0472  157 GLY A N   
1223 C CA  . GLY A 157 ? 0.9358 0.8292 0.7660 -0.1141 0.0044  0.0533  157 GLY A CA  
1224 C C   . GLY A 157 ? 0.8075 0.7075 0.6491 -0.1096 0.0022  0.0559  157 GLY A C   
1225 O O   . GLY A 157 ? 0.8271 0.7282 0.6786 -0.1017 0.0129  0.0526  157 GLY A O   
1226 N N   . ILE A 158 ? 0.8713 0.7757 0.7123 -0.1150 -0.0126 0.0624  158 ILE A N   
1227 C CA  . ILE A 158 ? 0.7613 0.6716 0.6118 -0.1110 -0.0171 0.0661  158 ILE A CA  
1228 C C   . ILE A 158 ? 0.7175 0.6592 0.5969 -0.1105 -0.0293 0.0712  158 ILE A C   
1229 O O   . ILE A 158 ? 0.8364 0.7805 0.7114 -0.1191 -0.0429 0.0768  158 ILE A O   
1230 C CB  . ILE A 158 ? 0.8279 0.7074 0.6441 -0.1168 -0.0234 0.0704  158 ILE A CB  
1231 C CG1 . ILE A 158 ? 0.8725 0.7198 0.6591 -0.1159 -0.0086 0.0661  158 ILE A CG1 
1232 C CG2 . ILE A 158 ? 0.7514 0.6377 0.5781 -0.1122 -0.0288 0.0749  158 ILE A CG2 
1233 C CD1 . ILE A 158 ? 0.9126 0.7642 0.7152 -0.1061 0.0071  0.0624  158 ILE A CD1 
1234 N N   . GLU A 159 ? 0.6397 0.6050 0.5489 -0.1005 -0.0246 0.0695  159 GLU A N   
1235 C CA  . GLU A 159 ? 0.6312 0.6268 0.5690 -0.0972 -0.0332 0.0744  159 GLU A CA  
1236 C C   . GLU A 159 ? 0.6952 0.6942 0.6409 -0.0914 -0.0378 0.0784  159 GLU A C   
1237 O O   . GLU A 159 ? 0.6692 0.6620 0.6169 -0.0840 -0.0291 0.0743  159 GLU A O   
1238 C CB  . GLU A 159 ? 0.6456 0.6641 0.6089 -0.0888 -0.0245 0.0695  159 GLU A CB  
1239 C CG  . GLU A 159 ? 0.4963 0.5450 0.4887 -0.0828 -0.0303 0.0747  159 GLU A CG  
1240 C CD  . GLU A 159 ? 0.6550 0.7227 0.6672 -0.0744 -0.0218 0.0702  159 GLU A CD  
1241 O OE1 . GLU A 159 ? 0.6862 0.7450 0.6900 -0.0747 -0.0134 0.0635  159 GLU A OE1 
1242 O OE2 . GLU A 159 ? 0.4927 0.5831 0.5276 -0.0667 -0.0233 0.0735  159 GLU A OE2 
1243 N N   . LEU A 160 ? 0.7382 0.7471 0.6893 -0.0949 -0.0520 0.0868  160 LEU A N   
1244 C CA  . LEU A 160 ? 0.6094 0.6247 0.5705 -0.0884 -0.0580 0.0919  160 LEU A CA  
1245 C C   . LEU A 160 ? 0.5456 0.5954 0.5422 -0.0798 -0.0595 0.0950  160 LEU A C   
1246 O O   . LEU A 160 ? 0.6179 0.6870 0.6284 -0.0839 -0.0654 0.0996  160 LEU A O   
1247 C CB  . LEU A 160 ? 0.5956 0.5979 0.5385 -0.0968 -0.0738 0.0999  160 LEU A CB  
1248 C CG  . LEU A 160 ? 0.5812 0.5462 0.4834 -0.1059 -0.0738 0.0978  160 LEU A CG  
1249 C CD1 . LEU A 160 ? 0.8033 0.7552 0.6870 -0.1129 -0.0916 0.1060  160 LEU A CD1 
1250 C CD2 . LEU A 160 ? 0.7949 0.7387 0.6833 -0.0997 -0.0585 0.0916  160 LEU A CD2 
1251 N N   . THR A 161 ? 0.5019 0.5580 0.5121 -0.0678 -0.0535 0.0930  161 THR A N   
1252 C CA  . THR A 161 ? 0.5876 0.6728 0.6282 -0.0573 -0.0527 0.0954  161 THR A CA  
1253 C C   . THR A 161 ? 0.6116 0.6960 0.6588 -0.0466 -0.0533 0.0972  161 THR A C   
1254 O O   . THR A 161 ? 0.5846 0.6460 0.6143 -0.0470 -0.0519 0.0950  161 THR A O   
1255 C CB  . THR A 161 ? 0.5164 0.6104 0.5672 -0.0516 -0.0404 0.0873  161 THR A CB  
1256 O OG1 . THR A 161 ? 0.5857 0.7056 0.6624 -0.0405 -0.0391 0.0902  161 THR A OG1 
1257 C CG2 . THR A 161 ? 0.5072 0.5822 0.5480 -0.0469 -0.0301 0.0779  161 THR A CG2 
1258 N N   . ASP A 162 ? 0.6012 0.7103 0.6735 -0.0363 -0.0546 0.1016  162 ASP A N   
1259 C CA  . ASP A 162 ? 0.6604 0.7700 0.7406 -0.0242 -0.0547 0.1035  162 ASP A CA  
1260 C C   . ASP A 162 ? 0.6380 0.7570 0.7330 -0.0106 -0.0438 0.0972  162 ASP A C   
1261 O O   . ASP A 162 ? 0.6170 0.7397 0.7213 0.0013  -0.0436 0.0992  162 ASP A O   
1262 C CB  . ASP A 162 ? 0.7162 0.8440 0.8113 -0.0219 -0.0669 0.1157  162 ASP A CB  
1263 C CG  . ASP A 162 ? 0.7194 0.8789 0.8399 -0.0210 -0.0682 0.1215  162 ASP A CG  
1264 O OD1 . ASP A 162 ? 0.6199 0.7851 0.7436 -0.0217 -0.0593 0.1158  162 ASP A OD1 
1265 O OD2 . ASP A 162 ? 0.7229 0.9017 0.8607 -0.0194 -0.0780 0.1324  162 ASP A OD2 
1266 N N   . SER A 163 ? 0.5424 0.6633 0.6376 -0.0117 -0.0354 0.0897  163 SER A N   
1267 C CA  . SER A 163 ? 0.5512 0.6788 0.6571 0.0008  -0.0263 0.0832  163 SER A CA  
1268 C C   . SER A 163 ? 0.6606 0.7668 0.7534 -0.0002 -0.0190 0.0719  163 SER A C   
1269 O O   . SER A 163 ? 0.6709 0.7703 0.7543 -0.0091 -0.0160 0.0674  163 SER A O   
1270 C CB  . SER A 163 ? 0.5082 0.6575 0.6270 0.0021  -0.0228 0.0845  163 SER A CB  
1271 O OG  . SER A 163 ? 0.5539 0.7055 0.6777 0.0144  -0.0139 0.0774  163 SER A OG  
1272 N N   . PRO A 164 ? 0.6295 0.7243 0.7220 0.0085  -0.0163 0.0675  164 PRO A N   
1273 C CA  . PRO A 164 ? 0.6261 0.7033 0.7109 0.0072  -0.0100 0.0571  164 PRO A CA  
1274 C C   . PRO A 164 ? 0.6645 0.7496 0.7542 0.0109  -0.0044 0.0498  164 PRO A C   
1275 O O   . PRO A 164 ? 0.6483 0.7223 0.7325 0.0066  -0.0002 0.0422  164 PRO A O   
1276 C CB  . PRO A 164 ? 0.5863 0.6517 0.6723 0.0164  -0.0100 0.0553  164 PRO A CB  
1277 C CG  . PRO A 164 ? 0.6156 0.6971 0.7126 0.0274  -0.0135 0.0624  164 PRO A CG  
1278 C CD  . PRO A 164 ? 0.5949 0.6922 0.6949 0.0200  -0.0191 0.0719  164 PRO A CD  
1279 N N   . TYR A 165 ? 0.5588 0.6625 0.6590 0.0192  -0.0037 0.0523  165 TYR A N   
1280 C CA  . TYR A 165 ? 0.5873 0.6976 0.6893 0.0227  0.0016  0.0463  165 TYR A CA  
1281 C C   . TYR A 165 ? 0.6074 0.7185 0.7031 0.0104  0.0026  0.0459  165 TYR A C   
1282 O O   . TYR A 165 ? 0.7099 0.8184 0.8024 0.0107  0.0069  0.0389  165 TYR A O   
1283 C CB  . TYR A 165 ? 0.5372 0.6669 0.6505 0.0343  0.0035  0.0510  165 TYR A CB  
1284 C CG  . TYR A 165 ? 0.6593 0.7957 0.7722 0.0381  0.0093  0.0464  165 TYR A CG  
1285 C CD1 . TYR A 165 ? 0.6110 0.7372 0.7186 0.0481  0.0128  0.0368  165 TYR A CD1 
1286 C CD2 . TYR A 165 ? 0.6710 0.8220 0.7874 0.0317  0.0107  0.0517  165 TYR A CD2 
1287 C CE1 . TYR A 165 ? 0.6024 0.7327 0.7070 0.0523  0.0176  0.0328  165 TYR A CE1 
1288 C CE2 . TYR A 165 ? 0.6505 0.8059 0.7649 0.0355  0.0165  0.0480  165 TYR A CE2 
1289 C CZ  . TYR A 165 ? 0.6128 0.7578 0.7206 0.0463  0.0201  0.0386  165 TYR A CZ  
1290 O OH  . TYR A 165 ? 0.5167 0.6641 0.6198 0.0509  0.0254  0.0350  165 TYR A OH  
1291 N N   . VAL A 166 ? 0.6394 0.7524 0.7317 -0.0001 -0.0021 0.0534  166 VAL A N   
1292 C CA  . VAL A 166 ? 0.5746 0.6836 0.6570 -0.0122 -0.0014 0.0530  166 VAL A CA  
1293 C C   . VAL A 166 ? 0.5423 0.6293 0.6112 -0.0185 0.0014  0.0467  166 VAL A C   
1294 O O   . VAL A 166 ? 0.7109 0.7920 0.7730 -0.0229 0.0058  0.0417  166 VAL A O   
1295 C CB  . VAL A 166 ? 0.6017 0.7184 0.6835 -0.0215 -0.0088 0.0631  166 VAL A CB  
1296 C CG1 . VAL A 166 ? 0.5809 0.6883 0.6482 -0.0342 -0.0087 0.0622  166 VAL A CG1 
1297 C CG2 . VAL A 166 ? 0.5776 0.7194 0.6775 -0.0155 -0.0103 0.0704  166 VAL A CG2 
1298 N N   . VAL A 167 ? 0.6039 0.6784 0.6691 -0.0185 -0.0004 0.0476  167 VAL A N   
1299 C CA  . VAL A 167 ? 0.6331 0.6871 0.6871 -0.0243 0.0038  0.0431  167 VAL A CA  
1300 C C   . VAL A 167 ? 0.5979 0.6494 0.6585 -0.0192 0.0100  0.0336  167 VAL A C   
1301 O O   . VAL A 167 ? 0.5396 0.5821 0.5948 -0.0243 0.0151  0.0294  167 VAL A O   
1302 C CB  . VAL A 167 ? 0.6456 0.6866 0.6950 -0.0245 0.0013  0.0469  167 VAL A CB  
1303 C CG1 . VAL A 167 ? 0.5591 0.5788 0.5965 -0.0312 0.0074  0.0440  167 VAL A CG1 
1304 C CG2 . VAL A 167 ? 0.6783 0.7232 0.7222 -0.0283 -0.0071 0.0566  167 VAL A CG2 
1305 N N   . ALA A 168 ? 0.6664 0.7252 0.7385 -0.0086 0.0091  0.0303  168 ALA A N   
1306 C CA  . ALA A 168 ? 0.5489 0.6041 0.6265 -0.0037 0.0124  0.0210  168 ALA A CA  
1307 C C   . ALA A 168 ? 0.6085 0.6712 0.6850 -0.0045 0.0152  0.0175  168 ALA A C   
1308 O O   . ALA A 168 ? 0.5182 0.5747 0.5952 -0.0061 0.0184  0.0112  168 ALA A O   
1309 C CB  . ALA A 168 ? 0.5455 0.6035 0.6309 0.0084  0.0098  0.0182  168 ALA A CB  
1310 N N   . SER A 169 ? 0.6051 0.6815 0.6811 -0.0034 0.0142  0.0220  169 SER A N   
1311 C CA  . SER A 169 ? 0.5297 0.6119 0.6031 -0.0040 0.0172  0.0194  169 SER A CA  
1312 C C   . SER A 169 ? 0.5733 0.6469 0.6363 -0.0153 0.0198  0.0202  169 SER A C   
1313 O O   . SER A 169 ? 0.4930 0.5629 0.5533 -0.0158 0.0236  0.0149  169 SER A O   
1314 C CB  . SER A 169 ? 0.4441 0.5432 0.5211 -0.0002 0.0163  0.0252  169 SER A CB  
1315 O OG  . SER A 169 ? 0.5423 0.6479 0.6269 0.0124  0.0160  0.0240  169 SER A OG  
1316 N N   . MET A 170 ? 0.5447 0.6134 0.5999 -0.0238 0.0175  0.0268  170 MET A N   
1317 C CA  . MET A 170 ? 0.5158 0.5721 0.5565 -0.0339 0.0203  0.0276  170 MET A CA  
1318 C C   . MET A 170 ? 0.4809 0.5235 0.5202 -0.0342 0.0265  0.0216  170 MET A C   
1319 O O   . MET A 170 ? 0.5112 0.5455 0.5413 -0.0387 0.0314  0.0198  170 MET A O   
1320 C CB  . MET A 170 ? 0.4548 0.5044 0.4847 -0.0421 0.0154  0.0355  170 MET A CB  
1321 C CG  . MET A 170 ? 0.6593 0.7233 0.6917 -0.0447 0.0086  0.0427  170 MET A CG  
1322 S SD  . MET A 170 ? 0.5638 0.6291 0.5871 -0.0517 0.0103  0.0429  170 MET A SD  
1323 C CE  . MET A 170 ? 0.4675 0.5058 0.4644 -0.0632 0.0112  0.0433  170 MET A CE  
1324 N N   . ARG A 171 ? 0.6162 0.6560 0.6653 -0.0296 0.0265  0.0188  171 ARG A N   
1325 C CA  . ARG A 171 ? 0.5320 0.5618 0.5853 -0.0300 0.0323  0.0137  171 ARG A CA  
1326 C C   . ARG A 171 ? 0.4895 0.5261 0.5512 -0.0248 0.0340  0.0066  171 ARG A C   
1327 O O   . ARG A 171 ? 0.5746 0.6051 0.6385 -0.0266 0.0394  0.0034  171 ARG A O   
1328 C CB  . ARG A 171 ? 0.5736 0.5984 0.6364 -0.0272 0.0310  0.0129  171 ARG A CB  
1329 C CG  . ARG A 171 ? 0.6893 0.7047 0.7600 -0.0291 0.0370  0.0091  171 ARG A CG  
1330 C CD  . ARG A 171 ? 0.6730 0.6818 0.7527 -0.0275 0.0352  0.0091  171 ARG A CD  
1331 N NE  . ARG A 171 ? 0.6842 0.6846 0.7739 -0.0309 0.0415  0.0070  171 ARG A NE  
1332 C CZ  . ARG A 171 ? 0.7762 0.7807 0.8836 -0.0279 0.0402  0.0006  171 ARG A CZ  
1333 N NH1 . ARG A 171 ? 0.7339 0.7479 0.8472 -0.0208 0.0328  -0.0052 171 ARG A NH1 
1334 N NH2 . ARG A 171 ? 0.7794 0.7778 0.8988 -0.0321 0.0463  0.0004  171 ARG A NH2 
1335 N N   . ILE A 172 ? 0.4977 0.5463 0.5638 -0.0179 0.0298  0.0047  172 ILE A N   
1336 C CA  . ILE A 172 ? 0.5068 0.5600 0.5780 -0.0120 0.0302  -0.0020 172 ILE A CA  
1337 C C   . ILE A 172 ? 0.5168 0.5713 0.5775 -0.0153 0.0337  -0.0007 172 ILE A C   
1338 O O   . ILE A 172 ? 0.5064 0.5584 0.5680 -0.0141 0.0366  -0.0051 172 ILE A O   
1339 C CB  . ILE A 172 ? 0.4673 0.5292 0.5440 -0.0017 0.0251  -0.0048 172 ILE A CB  
1340 C CG1 . ILE A 172 ? 0.3760 0.4329 0.4614 0.0019  0.0214  -0.0070 172 ILE A CG1 
1341 C CG2 . ILE A 172 ? 0.4512 0.5158 0.5290 0.0048  0.0246  -0.0114 172 ILE A CG2 
1342 C CD1 . ILE A 172 ? 0.3336 0.3949 0.4210 0.0132  0.0169  -0.0102 172 ILE A CD1 
1343 N N   . MET A 173 ? 0.4625 0.5203 0.5135 -0.0197 0.0328  0.0056  173 MET A N   
1344 C CA  . MET A 173 ? 0.4799 0.5383 0.5204 -0.0228 0.0352  0.0071  173 MET A CA  
1345 C C   . MET A 173 ? 0.4349 0.4791 0.4615 -0.0319 0.0396  0.0091  173 MET A C   
1346 O O   . MET A 173 ? 0.4317 0.4721 0.4487 -0.0337 0.0427  0.0085  173 MET A O   
1347 C CB  . MET A 173 ? 0.4467 0.5161 0.4854 -0.0239 0.0317  0.0135  173 MET A CB  
1348 C CG  . MET A 173 ? 0.4817 0.5644 0.5307 -0.0132 0.0299  0.0120  173 MET A CG  
1349 S SD  . MET A 173 ? 0.4823 0.5651 0.5298 -0.0046 0.0328  0.0044  173 MET A SD  
1350 C CE  . MET A 173 ? 0.6138 0.6947 0.6479 -0.0126 0.0363  0.0089  173 MET A CE  
1351 N N   . THR A 174 ? 0.4410 0.4751 0.4638 -0.0371 0.0406  0.0116  174 THR A N   
1352 C CA  . THR A 174 ? 0.4469 0.4639 0.4521 -0.0449 0.0456  0.0140  174 THR A CA  
1353 C C   . THR A 174 ? 0.5523 0.5589 0.5615 -0.0445 0.0518  0.0121  174 THR A C   
1354 O O   . THR A 174 ? 0.5755 0.5886 0.6024 -0.0393 0.0512  0.0088  174 THR A O   
1355 C CB  . THR A 174 ? 0.6629 0.6741 0.6531 -0.0533 0.0404  0.0212  174 THR A CB  
1356 O OG1 . THR A 174 ? 0.5671 0.5786 0.5630 -0.0530 0.0369  0.0239  174 THR A OG1 
1357 C CG2 . THR A 174 ? 0.4980 0.5230 0.4901 -0.0542 0.0341  0.0243  174 THR A CG2 
1358 N N   . ARG A 175 ? 0.6304 0.6192 0.6220 -0.0502 0.0582  0.0145  175 ARG A N   
1359 C CA  . ARG A 175 ? 0.6494 0.6262 0.6419 -0.0508 0.0663  0.0149  175 ARG A CA  
1360 C C   . ARG A 175 ? 0.7467 0.7112 0.7240 -0.0566 0.0637  0.0208  175 ARG A C   
1361 O O   . ARG A 175 ? 0.7292 0.6775 0.6815 -0.0626 0.0645  0.0246  175 ARG A O   
1362 C CB  . ARG A 175 ? 0.6472 0.6105 0.6285 -0.0512 0.0772  0.0140  175 ARG A CB  
1363 C CG  . ARG A 175 ? 0.6728 0.6474 0.6718 -0.0444 0.0804  0.0085  175 ARG A CG  
1364 C CD  . ARG A 175 ? 0.7247 0.7036 0.7149 -0.0434 0.0765  0.0068  175 ARG A CD  
1365 N NE  . ARG A 175 ? 0.8050 0.7881 0.8049 -0.0370 0.0815  0.0025  175 ARG A NE  
1366 C CZ  . ARG A 175 ? 0.7875 0.7729 0.7808 -0.0346 0.0800  0.0006  175 ARG A CZ  
1367 N NH1 . ARG A 175 ? 0.8427 0.8275 0.8213 -0.0387 0.0742  0.0028  175 ARG A NH1 
1368 N NH2 . ARG A 175 ? 0.7543 0.7428 0.7569 -0.0280 0.0842  -0.0031 175 ARG A NH2 
1369 N N   . MET A 176 ? 0.7461 0.7166 0.7368 -0.0547 0.0598  0.0216  176 MET A N   
1370 C CA  . MET A 176 ? 0.7515 0.7120 0.7297 -0.0589 0.0558  0.0275  176 MET A CA  
1371 C C   . MET A 176 ? 0.6944 0.6451 0.6786 -0.0581 0.0627  0.0283  176 MET A C   
1372 O O   . MET A 176 ? 0.8114 0.7714 0.8185 -0.0535 0.0650  0.0243  176 MET A O   
1373 C CB  . MET A 176 ? 0.7356 0.7118 0.7230 -0.0569 0.0438  0.0293  176 MET A CB  
1374 C CG  . MET A 176 ? 0.7391 0.7074 0.7179 -0.0595 0.0384  0.0355  176 MET A CG  
1375 S SD  . MET A 176 ? 0.6291 0.6014 0.6284 -0.0531 0.0386  0.0341  176 MET A SD  
1376 C CE  . MET A 176 ? 0.5403 0.5381 0.5620 -0.0448 0.0313  0.0299  176 MET A CE  
1377 N N   . GLY A 177 ? 0.7450 0.6758 0.7078 -0.0627 0.0655  0.0337  177 GLY A N   
1378 C CA  . GLY A 177 ? 0.6654 0.5844 0.6311 -0.0625 0.0733  0.0359  177 GLY A CA  
1379 C C   . GLY A 177 ? 0.7676 0.6595 0.7014 -0.0674 0.0797  0.0417  177 GLY A C   
1380 O O   . GLY A 177 ? 0.8222 0.7040 0.7309 -0.0714 0.0751  0.0439  177 GLY A O   
1381 N N   . THR A 178 ? 0.8122 0.6912 0.7469 -0.0672 0.0904  0.0443  178 THR A N   
1382 C CA  . THR A 178 ? 0.8554 0.7052 0.7574 -0.0705 0.0986  0.0501  178 THR A CA  
1383 C C   . THR A 178 ? 0.9611 0.7982 0.8468 -0.0708 0.1107  0.0492  178 THR A C   
1384 O O   . THR A 178 ? 0.9412 0.7545 0.7909 -0.0739 0.1119  0.0523  178 THR A O   
1385 C CB  . THR A 178 ? 0.6904 0.5298 0.5989 -0.0698 0.1083  0.0540  178 THR A CB  
1386 O OG1 . THR A 178 ? 0.7544 0.6009 0.6723 -0.0692 0.0966  0.0554  178 THR A OG1 
1387 C CG2 . THR A 178 ? 0.7631 0.5698 0.6350 -0.0721 0.1190  0.0603  178 THR A CG2 
1388 N N   . SER A 179 ? 0.9243 0.7758 0.8349 -0.0672 0.1190  0.0449  179 SER A N   
1389 C CA  . SER A 179 ? 0.9536 0.7939 0.8511 -0.0658 0.1317  0.0442  179 SER A CA  
1390 C C   . SER A 179 ? 1.0059 0.8391 0.8769 -0.0683 0.1236  0.0427  179 SER A C   
1391 O O   . SER A 179 ? 1.0969 0.9111 0.9441 -0.0679 0.1334  0.0432  179 SER A O   
1392 C CB  . SER A 179 ? 0.8940 0.7556 0.8276 -0.0609 0.1387  0.0398  179 SER A CB  
1393 O OG  . SER A 179 ? 0.8677 0.7547 0.8243 -0.0595 0.1248  0.0342  179 SER A OG  
1394 N N   . VAL A 180 ? 1.0464 0.8937 0.9210 -0.0709 0.1066  0.0411  180 VAL A N   
1395 C CA  . VAL A 180 ? 0.9924 0.8333 0.8436 -0.0749 0.0981  0.0405  180 VAL A CA  
1396 C C   . VAL A 180 ? 1.0053 0.8156 0.8153 -0.0805 0.0955  0.0457  180 VAL A C   
1397 O O   . VAL A 180 ? 1.1098 0.9017 0.8906 -0.0840 0.0946  0.0457  180 VAL A O   
1398 C CB  . VAL A 180 ? 0.8470 0.7142 0.7179 -0.0757 0.0819  0.0384  180 VAL A CB  
1399 C CG1 . VAL A 180 ? 0.9753 0.8375 0.8260 -0.0808 0.0738  0.0384  180 VAL A CG1 
1400 C CG2 . VAL A 180 ? 0.8601 0.7537 0.7678 -0.0693 0.0840  0.0331  180 VAL A CG2 
1401 N N   . LEU A 181 ? 0.9881 0.7901 0.7928 -0.0815 0.0935  0.0501  181 LEU A N   
1402 C CA  . LEU A 181 ? 1.0788 0.8492 0.8417 -0.0863 0.0903  0.0552  181 LEU A CA  
1403 C C   . LEU A 181 ? 1.2077 0.9463 0.9403 -0.0845 0.1082  0.0564  181 LEU A C   
1404 O O   . LEU A 181 ? 1.2527 0.9625 0.9444 -0.0883 0.1060  0.0579  181 LEU A O   
1405 C CB  . LEU A 181 ? 0.9933 0.7619 0.7580 -0.0865 0.0846  0.0600  181 LEU A CB  
1406 C CG  . LEU A 181 ? 0.9730 0.7665 0.7584 -0.0881 0.0657  0.0607  181 LEU A CG  
1407 C CD1 . LEU A 181 ? 0.9196 0.7089 0.7068 -0.0866 0.0627  0.0655  181 LEU A CD1 
1408 C CD2 . LEU A 181 ? 1.0710 0.8598 0.8352 -0.0948 0.0496  0.0622  181 LEU A CD2 
1409 N N   . GLU A 182 ? 1.3974 1.1400 1.1492 -0.0786 0.1261  0.0560  182 GLU A N   
1410 C CA  . GLU A 182 ? 1.4399 1.1543 1.1662 -0.0752 0.1458  0.0580  182 GLU A CA  
1411 C C   . GLU A 182 ? 1.4200 1.1274 1.1314 -0.0745 0.1486  0.0541  182 GLU A C   
1412 O O   . GLU A 182 ? 1.5136 1.1877 1.1858 -0.0735 0.1588  0.0558  182 GLU A O   
1413 C CB  . GLU A 182 ? 1.5600 1.2862 1.3186 -0.0693 0.1640  0.0591  182 GLU A CB  
1414 C CG  . GLU A 182 ? 1.6062 1.3363 1.3789 -0.0702 0.1629  0.0633  182 GLU A CG  
1415 C CD  . GLU A 182 ? 1.7868 1.5290 1.5941 -0.0659 0.1801  0.0647  182 GLU A CD  
1416 O OE1 . GLU A 182 ? 1.8939 1.6426 1.7151 -0.0617 0.1929  0.0629  182 GLU A OE1 
1417 O OE2 . GLU A 182 ? 1.8295 1.5747 1.6510 -0.0668 0.1804  0.0681  182 GLU A OE2 
1418 N N   . ALA A 183 ? 1.2573 0.9932 0.9968 -0.0744 0.1402  0.0489  183 ALA A N   
1419 C CA  . ALA A 183 ? 1.1787 0.9079 0.9045 -0.0736 0.1423  0.0454  183 ALA A CA  
1420 C C   . ALA A 183 ? 1.2036 0.9104 0.8895 -0.0815 0.1279  0.0459  183 ALA A C   
1421 O O   . ALA A 183 ? 1.3385 1.0190 0.9913 -0.0817 0.1331  0.0451  183 ALA A O   
1422 C CB  . ALA A 183 ? 1.1767 0.9418 0.9433 -0.0709 0.1376  0.0402  183 ALA A CB  
1423 N N   . LEU A 184 ? 1.2233 0.9398 0.9122 -0.0880 0.1093  0.0476  184 LEU A N   
1424 C CA  . LEU A 184 ? 1.2981 0.9964 0.9538 -0.0968 0.0930  0.0489  184 LEU A CA  
1425 C C   . LEU A 184 ? 1.3646 1.0172 0.9681 -0.0986 0.0978  0.0523  184 LEU A C   
1426 O O   . LEU A 184 ? 1.3763 1.0008 0.9430 -0.1019 0.0967  0.0512  184 LEU A O   
1427 C CB  . LEU A 184 ? 1.2327 0.9540 0.9075 -0.1023 0.0729  0.0512  184 LEU A CB  
1428 C CG  . LEU A 184 ? 1.2393 0.9460 0.8859 -0.1126 0.0533  0.0539  184 LEU A CG  
1429 C CD1 . LEU A 184 ? 1.2887 0.9958 0.9301 -0.1168 0.0493  0.0505  184 LEU A CD1 
1430 C CD2 . LEU A 184 ? 1.0510 0.7833 0.7216 -0.1160 0.0356  0.0574  184 LEU A CD2 
1431 N N   . GLY A 185 ? 1.3850 1.0271 0.9822 -0.0963 0.1031  0.0564  185 GLY A N   
1432 C CA  . GLY A 185 ? 1.4996 1.0963 1.0446 -0.0972 0.1078  0.0601  185 GLY A CA  
1433 C C   . GLY A 185 ? 1.6568 1.2330 1.1662 -0.1071 0.0854  0.0616  185 GLY A C   
1434 O O   . GLY A 185 ? 1.6311 1.2201 1.1503 -0.1120 0.0681  0.0647  185 GLY A O   
1435 N N   . ASP A 186 ? 1.9019 1.4457 1.3702 -0.1102 0.0850  0.0597  186 ASP A N   
1436 C CA  . ASP A 186 ? 1.9554 1.4768 1.3880 -0.1210 0.0625  0.0608  186 ASP A CA  
1437 C C   . ASP A 186 ? 1.8833 1.4152 1.3228 -0.1273 0.0525  0.0567  186 ASP A C   
1438 O O   . ASP A 186 ? 2.0027 1.5049 1.4033 -0.1356 0.0398  0.0564  186 ASP A O   
1439 C CB  . ASP A 186 ? 2.1338 1.5980 1.5011 -0.1207 0.0675  0.0626  186 ASP A CB  
1440 C CG  . ASP A 186 ? 2.2519 1.7023 1.6067 -0.1164 0.0729  0.0679  186 ASP A CG  
1441 O OD1 . ASP A 186 ? 2.1775 1.6573 1.5648 -0.1182 0.0618  0.0708  186 ASP A OD1 
1442 O OD2 . ASP A 186 ? 2.3983 1.8073 1.7097 -0.1107 0.0890  0.0695  186 ASP A OD2 
1443 N N   . GLY A 187 ? 1.7014 1.2736 1.1890 -0.1237 0.0579  0.0537  187 GLY A N   
1444 C CA  . GLY A 187 ? 1.6581 1.2428 1.1556 -0.1291 0.0495  0.0505  187 GLY A CA  
1445 C C   . GLY A 187 ? 1.6201 1.2366 1.1463 -0.1383 0.0263  0.0529  187 GLY A C   
1446 O O   . GLY A 187 ? 1.5587 1.1942 1.1050 -0.1386 0.0179  0.0565  187 GLY A O   
1447 N N   . GLU A 188 ? 1.7298 1.3513 1.2577 -0.1455 0.0167  0.0513  188 GLU A N   
1448 C CA  . GLU A 188 ? 1.6719 1.3244 1.2286 -0.1544 -0.0038 0.0545  188 GLU A CA  
1449 C C   . GLU A 188 ? 1.5070 1.2082 1.1194 -0.1469 0.0010  0.0541  188 GLU A C   
1450 O O   . GLU A 188 ? 1.4422 1.1546 1.0726 -0.1366 0.0185  0.0502  188 GLU A O   
1451 C CB  . GLU A 188 ? 1.7319 1.3774 1.2780 -0.1639 -0.0130 0.0534  188 GLU A CB  
1452 C CG  . GLU A 188 ? 1.9156 1.5108 1.4046 -0.1730 -0.0212 0.0535  188 GLU A CG  
1453 C CD  . GLU A 188 ? 2.1097 1.6990 1.5909 -0.1843 -0.0328 0.0530  188 GLU A CD  
1454 O OE1 . GLU A 188 ? 2.0801 1.7062 1.6017 -0.1852 -0.0342 0.0534  188 GLU A OE1 
1455 O OE2 . GLU A 188 ? 2.2255 1.7714 1.6587 -0.1924 -0.0404 0.0524  188 GLU A OE2 
1456 N N   . PHE A 189 ? 1.2696 0.9994 0.9093 -0.1519 -0.0154 0.0586  189 PHE A N   
1457 C CA  . PHE A 189 ? 1.1705 0.9443 0.8599 -0.1448 -0.0127 0.0586  189 PHE A CA  
1458 C C   . PHE A 189 ? 1.1199 0.9211 0.8336 -0.1527 -0.0310 0.0636  189 PHE A C   
1459 O O   . PHE A 189 ? 1.1796 0.9709 0.8785 -0.1622 -0.0480 0.0689  189 PHE A O   
1460 C CB  . PHE A 189 ? 1.2152 0.9950 0.9158 -0.1367 -0.0071 0.0597  189 PHE A CB  
1461 C CG  . PHE A 189 ? 1.0844 0.8554 0.7719 -0.1423 -0.0228 0.0660  189 PHE A CG  
1462 C CD1 . PHE A 189 ? 1.1499 0.8801 0.7921 -0.1457 -0.0240 0.0673  189 PHE A CD1 
1463 C CD2 . PHE A 189 ? 0.9803 0.7828 0.6994 -0.1431 -0.0362 0.0707  189 PHE A CD2 
1464 C CE1 . PHE A 189 ? 1.1695 0.8902 0.7977 -0.1504 -0.0397 0.0732  189 PHE A CE1 
1465 C CE2 . PHE A 189 ? 1.0652 0.8604 0.7734 -0.1475 -0.0515 0.0770  189 PHE A CE2 
1466 C CZ  . PHE A 189 ? 1.0802 0.8344 0.7427 -0.1514 -0.0540 0.0781  189 PHE A CZ  
1467 N N   . ILE A 190 ? 1.0207 0.8563 0.7717 -0.1483 -0.0275 0.0625  190 ILE A N   
1468 C CA  . ILE A 190 ? 0.9944 0.8598 0.7733 -0.1539 -0.0417 0.0681  190 ILE A CA  
1469 C C   . ILE A 190 ? 1.0025 0.8881 0.8031 -0.1502 -0.0494 0.0731  190 ILE A C   
1470 O O   . ILE A 190 ? 1.0204 0.9158 0.8358 -0.1393 -0.0394 0.0704  190 ILE A O   
1471 C CB  . ILE A 190 ? 1.0574 0.9502 0.8658 -0.1488 -0.0336 0.0655  190 ILE A CB  
1472 C CG1 . ILE A 190 ? 1.1099 0.9803 0.8950 -0.1509 -0.0248 0.0604  190 ILE A CG1 
1473 C CG2 . ILE A 190 ? 1.0317 0.9541 0.8679 -0.1548 -0.0464 0.0725  190 ILE A CG2 
1474 C CD1 . ILE A 190 ? 1.1880 1.0332 0.9434 -0.1654 -0.0370 0.0635  190 ILE A CD1 
1475 N N   . LYS A 191 ? 0.9574 0.8490 0.7606 -0.1593 -0.0677 0.0805  191 LYS A N   
1476 C CA  . LYS A 191 ? 0.8992 0.8080 0.7207 -0.1560 -0.0770 0.0864  191 LYS A CA  
1477 C C   . LYS A 191 ? 0.8310 0.7834 0.6987 -0.1508 -0.0778 0.0899  191 LYS A C   
1478 O O   . LYS A 191 ? 0.8676 0.8367 0.7502 -0.1585 -0.0871 0.0950  191 LYS A O   
1479 C CB  . LYS A 191 ? 0.9481 0.8401 0.7482 -0.1678 -0.0974 0.0932  191 LYS A CB  
1480 C CG  . LYS A 191 ? 1.0023 0.8465 0.7508 -0.1730 -0.0969 0.0898  191 LYS A CG  
1481 C CD  . LYS A 191 ? 1.0704 0.8958 0.7949 -0.1863 -0.1199 0.0961  191 LYS A CD  
1482 C CE  . LYS A 191 ? 1.1841 0.9573 0.8517 -0.1907 -0.1185 0.0921  191 LYS A CE  
1483 N NZ  . LYS A 191 ? 1.2976 1.0484 0.9375 -0.2044 -0.1429 0.0976  191 LYS A NZ  
1484 N N   . CYS A 192 ? 0.7462 0.7158 0.6357 -0.1377 -0.0676 0.0874  192 CYS A N   
1485 C CA  . CYS A 192 ? 0.7284 0.7359 0.6581 -0.1300 -0.0660 0.0900  192 CYS A CA  
1486 C C   . CYS A 192 ? 0.7295 0.7515 0.6758 -0.1246 -0.0742 0.0962  192 CYS A C   
1487 O O   . CYS A 192 ? 0.7139 0.7186 0.6452 -0.1209 -0.0731 0.0948  192 CYS A O   
1488 C CB  . CYS A 192 ? 0.7663 0.7811 0.7075 -0.1182 -0.0485 0.0818  192 CYS A CB  
1489 S SG  . CYS A 192 ? 0.6500 0.6488 0.5734 -0.1219 -0.0377 0.0745  192 CYS A SG  
1490 N N   . LEU A 193 ? 0.7062 0.7597 0.6836 -0.1235 -0.0815 0.1036  193 LEU A N   
1491 C CA  . LEU A 193 ? 0.6773 0.7479 0.6741 -0.1172 -0.0895 0.1106  193 LEU A CA  
1492 C C   . LEU A 193 ? 0.5862 0.6934 0.6216 -0.1071 -0.0840 0.1136  193 LEU A C   
1493 O O   . LEU A 193 ? 0.6158 0.7422 0.6682 -0.1120 -0.0863 0.1182  193 LEU A O   
1494 C CB  . LEU A 193 ? 0.6738 0.7420 0.6650 -0.1288 -0.1099 0.1201  193 LEU A CB  
1495 C CG  . LEU A 193 ? 0.7082 0.7953 0.7206 -0.1223 -0.1202 0.1289  193 LEU A CG  
1496 C CD1 . LEU A 193 ? 0.6863 0.7551 0.6837 -0.1124 -0.1143 0.1247  193 LEU A CD1 
1497 C CD2 . LEU A 193 ? 0.8454 0.9317 0.8542 -0.1352 -0.1424 0.1386  193 LEU A CD2 
1498 N N   . HIS A 194 ? 0.5900 0.7050 0.6377 -0.0929 -0.0763 0.1112  194 HIS A N   
1499 C CA  . HIS A 194 ? 0.5979 0.7433 0.6778 -0.0808 -0.0697 0.1134  194 HIS A CA  
1500 C C   . HIS A 194 ? 0.5005 0.6566 0.5950 -0.0704 -0.0743 0.1189  194 HIS A C   
1501 O O   . HIS A 194 ? 0.5295 0.6657 0.6075 -0.0680 -0.0754 0.1161  194 HIS A O   
1502 C CB  . HIS A 194 ? 0.4077 0.5498 0.4865 -0.0713 -0.0532 0.1029  194 HIS A CB  
1503 C CG  . HIS A 194 ? 0.4130 0.5806 0.5187 -0.0570 -0.0459 0.1041  194 HIS A CG  
1504 N ND1 . HIS A 194 ? 0.4449 0.6126 0.5563 -0.0433 -0.0412 0.1012  194 HIS A ND1 
1505 C CD2 . HIS A 194 ? 0.5743 0.7659 0.7007 -0.0539 -0.0419 0.1083  194 HIS A CD2 
1506 C CE1 . HIS A 194 ? 0.5587 0.7480 0.6912 -0.0318 -0.0347 0.1029  194 HIS A CE1 
1507 N NE2 . HIS A 194 ? 0.6403 0.8450 0.7826 -0.0376 -0.0344 0.1075  194 HIS A NE2 
1508 N N   . SER A 195 ? 0.4013 0.5883 0.5266 -0.0638 -0.0760 0.1271  195 SER A N   
1509 C CA  . SER A 195 ? 0.5589 0.7586 0.7010 -0.0519 -0.0792 0.1331  195 SER A CA  
1510 C C   . SER A 195 ? 0.5829 0.8141 0.7568 -0.0393 -0.0710 0.1375  195 SER A C   
1511 O O   . SER A 195 ? 0.6348 0.8858 0.8251 -0.0443 -0.0705 0.1427  195 SER A O   
1512 C CB  . SER A 195 ? 0.5820 0.7847 0.7262 -0.0600 -0.0977 0.1440  195 SER A CB  
1513 O OG  . SER A 195 ? 0.6300 0.8439 0.7896 -0.0473 -0.1006 0.1499  195 SER A OG  
1514 N N   . VAL A 196 ? 0.5846 0.8184 0.7657 -0.0229 -0.0639 0.1355  196 VAL A N   
1515 C CA  . VAL A 196 ? 0.5282 0.7880 0.7355 -0.0083 -0.0544 0.1393  196 VAL A CA  
1516 C C   . VAL A 196 ? 0.6425 0.9326 0.8801 -0.0062 -0.0629 0.1545  196 VAL A C   
1517 O O   . VAL A 196 ? 0.7016 1.0178 0.9643 0.0025  -0.0550 0.1606  196 VAL A O   
1518 C CB  . VAL A 196 ? 0.6980 0.9471 0.9001 0.0091  -0.0445 0.1318  196 VAL A CB  
1519 C CG1 . VAL A 196 ? 0.4219 0.6447 0.5992 0.0070  -0.0364 0.1174  196 VAL A CG1 
1520 C CG2 . VAL A 196 ? 0.5866 0.8273 0.7859 0.0136  -0.0531 0.1357  196 VAL A CG2 
1521 N N   . GLY A 197 ? 0.5609 0.8482 0.7971 -0.0135 -0.0785 0.1615  197 GLY A N   
1522 C CA  . GLY A 197 ? 0.6792 0.9966 0.9466 -0.0123 -0.0887 0.1767  197 GLY A CA  
1523 C C   . GLY A 197 ? 0.7053 1.0368 0.9915 0.0079  -0.0843 0.1820  197 GLY A C   
1524 O O   . GLY A 197 ? 0.6386 1.0026 0.9585 0.0146  -0.0845 0.1942  197 GLY A O   
1525 N N   . CYS A 198 ? 0.6721 0.9794 0.9379 0.0181  -0.0798 0.1737  198 CYS A N   
1526 C CA  . CYS A 198 ? 0.6913 1.0058 0.9697 0.0379  -0.0758 0.1777  198 CYS A CA  
1527 C C   . CYS A 198 ? 0.7410 1.0291 0.9975 0.0379  -0.0853 0.1757  198 CYS A C   
1528 O O   . CYS A 198 ? 0.7790 1.0420 1.0150 0.0455  -0.0776 0.1658  198 CYS A O   
1529 C CB  . CYS A 198 ? 0.6505 0.9604 0.9258 0.0540  -0.0570 0.1687  198 CYS A CB  
1530 S SG  . CYS A 198 ? 0.7613 1.1040 1.0642 0.0600  -0.0436 0.1738  198 CYS A SG  
1531 N N   . PRO A 199 ? 0.7904 1.0825 1.0501 0.0290  -0.1027 0.1853  199 PRO A N   
1532 C CA  . PRO A 199 ? 0.8911 1.1572 1.1285 0.0297  -0.1118 0.1847  199 PRO A CA  
1533 C C   . PRO A 199 ? 0.9586 1.2288 1.2070 0.0506  -0.1075 0.1885  199 PRO A C   
1534 O O   . PRO A 199 ? 0.9280 1.2256 1.2052 0.0644  -0.1007 0.1949  199 PRO A O   
1535 C CB  . PRO A 199 ? 0.9268 1.2005 1.1682 0.0157  -0.1327 0.1956  199 PRO A CB  
1536 C CG  . PRO A 199 ? 0.8021 1.1166 1.0824 0.0152  -0.1344 0.2062  199 PRO A CG  
1537 C CD  . PRO A 199 ? 0.7635 1.0831 1.0470 0.0175  -0.1156 0.1976  199 PRO A CD  
1538 N N   . LEU A 200 ? 0.9588 1.1994 1.1825 0.0533  -0.1106 0.1848  200 LEU A N   
1539 C CA  . LEU A 200 ? 0.9936 1.2331 1.2238 0.0730  -0.1072 0.1882  200 LEU A CA  
1540 C C   . LEU A 200 ? 1.0912 1.3405 1.3318 0.0749  -0.1245 0.2023  200 LEU A C   
1541 O O   . LEU A 200 ? 1.1760 1.4128 1.4005 0.0606  -0.1392 0.2048  200 LEU A O   
1542 C CB  . LEU A 200 ? 0.9815 1.1823 1.1803 0.0765  -0.0994 0.1765  200 LEU A CB  
1543 C CG  . LEU A 200 ? 0.9101 1.0965 1.0951 0.0721  -0.0851 0.1618  200 LEU A CG  
1544 C CD1 . LEU A 200 ? 0.9466 1.0972 1.1059 0.0762  -0.0786 0.1520  200 LEU A CD1 
1545 C CD2 . LEU A 200 ? 0.9047 1.1151 1.1120 0.0833  -0.0730 0.1606  200 LEU A CD2 
1546 N N   . PRO A 201 ? 1.0559 1.3265 1.3221 0.0933  -0.1234 0.2118  201 PRO A N   
1547 C CA  . PRO A 201 ? 1.1006 1.3836 1.3834 0.1130  -0.1062 0.2100  201 PRO A CA  
1548 C C   . PRO A 201 ? 1.1393 1.4547 1.4488 0.1115  -0.0976 0.2120  201 PRO A C   
1549 O O   . PRO A 201 ? 1.1727 1.5120 1.5010 0.0988  -0.1075 0.2204  201 PRO A O   
1550 C CB  . PRO A 201 ? 1.0846 1.3810 1.3863 0.1309  -0.1120 0.2229  201 PRO A CB  
1551 C CG  . PRO A 201 ? 1.0738 1.3872 1.3884 0.1183  -0.1331 0.2355  201 PRO A CG  
1552 C CD  . PRO A 201 ? 1.0198 1.3037 1.3002 0.0962  -0.1410 0.2265  201 PRO A CD  
1553 N N   . LEU A 202 ? 1.2809 1.5957 1.5912 0.1242  -0.0794 0.2047  202 LEU A N   
1554 C CA  . LEU A 202 ? 1.3780 1.7197 1.7096 0.1240  -0.0689 0.2060  202 LEU A CA  
1555 C C   . LEU A 202 ? 1.4862 1.8685 1.8591 0.1368  -0.0685 0.2227  202 LEU A C   
1556 O O   . LEU A 202 ? 1.5152 1.9006 1.8967 0.1576  -0.0630 0.2276  202 LEU A O   
1557 C CB  . LEU A 202 ? 1.3753 1.6997 1.6905 0.1346  -0.0502 0.1926  202 LEU A CB  
1558 C CG  . LEU A 202 ? 1.2786 1.5671 1.5583 0.1221  -0.0487 0.1761  202 LEU A CG  
1559 C CD1 . LEU A 202 ? 1.2392 1.5114 1.5052 0.1352  -0.0325 0.1640  202 LEU A CD1 
1560 C CD2 . LEU A 202 ? 1.1133 1.4077 1.3913 0.1003  -0.0538 0.1743  202 LEU A CD2 
1561 N N   . LYS A 203 ? 1.5751 1.9884 1.9744 0.1245  -0.0740 0.2320  203 LYS A N   
1562 C CA  . LYS A 203 ? 1.6407 2.0971 2.0847 0.1350  -0.0723 0.2490  203 LYS A CA  
1563 C C   . LYS A 203 ? 1.6796 2.1528 2.1380 0.1476  -0.0502 0.2485  203 LYS A C   
1564 O O   . LYS A 203 ? 1.6729 2.1777 2.1655 0.1634  -0.0427 0.2617  203 LYS A O   
1565 C CB  . LYS A 203 ? 1.6732 2.1560 2.1417 0.1146  -0.0904 0.2609  203 LYS A CB  
1566 C CG  . LYS A 203 ? 1.6897 2.1561 2.1430 0.1022  -0.1138 0.2627  203 LYS A CG  
1567 C CD  . LYS A 203 ? 1.7609 2.2495 2.2345 0.0806  -0.1330 0.2731  203 LYS A CD  
1568 C CE  . LYS A 203 ? 1.7130 2.1813 2.1664 0.0690  -0.1570 0.2746  203 LYS A CE  
1569 N NZ  . LYS A 203 ? 1.5506 1.9708 1.9523 0.0610  -0.1556 0.2577  203 LYS A NZ  
1570 N N   . LYS A 204 ? 1.6890 2.1413 2.1218 0.1418  -0.0395 0.2342  204 LYS A N   
1571 C CA  . LYS A 204 ? 1.5665 2.0285 2.0056 0.1538  -0.0185 0.2320  204 LYS A CA  
1572 C C   . LYS A 204 ? 1.4901 1.9137 1.8910 0.1649  -0.0067 0.2147  204 LYS A C   
1573 O O   . LYS A 204 ? 1.3916 1.7850 1.7615 0.1514  -0.0122 0.2012  204 LYS A O   
1574 C CB  . LYS A 204 ? 1.5860 2.0617 2.0325 0.1351  -0.0175 0.2322  204 LYS A CB  
1575 C CG  . LYS A 204 ? 1.6301 2.1414 2.1134 0.1205  -0.0312 0.2486  204 LYS A CG  
1576 C CD  . LYS A 204 ? 1.5864 2.1048 2.0716 0.1012  -0.0300 0.2471  204 LYS A CD  
1577 C CE  . LYS A 204 ? 1.5075 2.0586 2.0281 0.0843  -0.0457 0.2629  204 LYS A CE  
1578 N NZ  . LYS A 204 ? 1.3873 1.9419 1.9074 0.0648  -0.0448 0.2612  204 LYS A NZ  
1579 N N   . PRO A 205 ? 1.3857 1.8081 1.7871 0.1890  0.0093  0.2146  205 PRO A N   
1580 C CA  . PRO A 205 ? 1.2728 1.6571 1.6370 0.1985  0.0191  0.1976  205 PRO A CA  
1581 C C   . PRO A 205 ? 1.1600 1.5329 1.5061 0.1857  0.0245  0.1858  205 PRO A C   
1582 O O   . PRO A 205 ? 1.0883 1.4844 1.4513 0.1821  0.0316  0.1914  205 PRO A O   
1583 C CB  . PRO A 205 ? 1.1993 1.5904 1.5719 0.2269  0.0362  0.2025  205 PRO A CB  
1584 C CG  . PRO A 205 ? 1.2111 1.6377 1.6225 0.2337  0.0315  0.2218  205 PRO A CG  
1585 C CD  . PRO A 205 ? 1.3182 1.7719 1.7532 0.2095  0.0184  0.2302  205 PRO A CD  
1586 N N   . LEU A 206 ? 1.1351 1.4719 1.4473 0.1789  0.0211  0.1699  206 LEU A N   
1587 C CA  . LEU A 206 ? 1.0195 1.3427 1.3128 0.1662  0.0242  0.1579  206 LEU A CA  
1588 C C   . LEU A 206 ? 0.9665 1.2758 1.2436 0.1833  0.0402  0.1490  206 LEU A C   
1589 O O   . LEU A 206 ? 1.0255 1.3170 1.2902 0.2012  0.0454  0.1450  206 LEU A O   
1590 C CB  . LEU A 206 ? 0.8930 1.1859 1.1603 0.1504  0.0129  0.1460  206 LEU A CB  
1591 C CG  . LEU A 206 ? 0.8075 1.1061 1.0820 0.1331  -0.0035 0.1529  206 LEU A CG  
1592 C CD1 . LEU A 206 ? 0.9147 1.1802 1.1606 0.1199  -0.0109 0.1407  206 LEU A CD1 
1593 C CD2 . LEU A 206 ? 0.7908 1.1174 1.0858 0.1179  -0.0076 0.1619  206 LEU A CD2 
1594 N N   . VAL A 207 ? 0.9611 1.2762 1.2362 0.1776  0.0475  0.1460  207 VAL A N   
1595 C CA  . VAL A 207 ? 0.9773 1.2778 1.2339 0.1924  0.0618  0.1374  207 VAL A CA  
1596 C C   . VAL A 207 ? 1.0048 1.2707 1.2291 0.1836  0.0570  0.1195  207 VAL A C   
1597 O O   . VAL A 207 ? 0.9925 1.2568 1.2134 0.1639  0.0495  0.1156  207 VAL A O   
1598 C CB  . VAL A 207 ? 0.9009 1.2264 1.1727 0.1925  0.0732  0.1449  207 VAL A CB  
1599 C CG1 . VAL A 207 ? 0.9077 1.2150 1.1561 0.2091  0.0880  0.1360  207 VAL A CG1 
1600 C CG2 . VAL A 207 ? 0.9158 1.2790 1.2250 0.1996  0.0775  0.1641  207 VAL A CG2 
1601 N N   . ASN A 208 ? 1.0515 1.2892 1.2523 0.1985  0.0611  0.1091  208 ASN A N   
1602 C CA  . ASN A 208 ? 1.0031 1.2078 1.1759 0.1913  0.0557  0.0925  208 ASN A CA  
1603 C C   . ASN A 208 ? 0.9809 1.1775 1.1533 0.1724  0.0416  0.0899  208 ASN A C   
1604 O O   . ASN A 208 ? 1.0986 1.2789 1.2570 0.1591  0.0366  0.0796  208 ASN A O   
1605 C CB  . ASN A 208 ? 1.0299 1.2328 1.1922 0.1854  0.0606  0.0856  208 ASN A CB  
1606 C CG  . ASN A 208 ? 1.0598 1.2481 1.2034 0.2054  0.0723  0.0796  208 ASN A CG  
1607 O OD1 . ASN A 208 ? 1.1280 1.2936 1.2556 0.2200  0.0732  0.0736  208 ASN A OD1 
1608 N ND2 . ASN A 208 ? 1.0378 1.2368 1.1811 0.2062  0.0811  0.0811  208 ASN A ND2 
1609 N N   . ASN A 209 ? 1.0543 1.2615 1.2417 0.1717  0.0356  0.0998  209 ASN A N   
1610 C CA  . ASN A 209 ? 1.0052 1.2045 1.1910 0.1549  0.0229  0.0994  209 ASN A CA  
1611 C C   . ASN A 209 ? 0.9699 1.1789 1.1591 0.1335  0.0178  0.0994  209 ASN A C   
1612 O O   . ASN A 209 ? 1.0240 1.2184 1.2032 0.1188  0.0096  0.0948  209 ASN A O   
1613 C CB  . ASN A 209 ? 1.0152 1.1788 1.1774 0.1551  0.0193  0.0866  209 ASN A CB  
1614 C CG  . ASN A 209 ? 1.0673 1.2169 1.2237 0.1750  0.0224  0.0867  209 ASN A CG  
1615 O OD1 . ASN A 209 ? 1.1132 1.2792 1.2848 0.1858  0.0238  0.0982  209 ASN A OD1 
1616 N ND2 . ASN A 209 ? 1.1527 1.2714 1.2872 0.1800  0.0231  0.0740  209 ASN A ND2 
1617 N N   . TRP A 210 ? 0.9180 1.1499 1.1199 0.1319  0.0235  0.1049  210 TRP A N   
1618 C CA  . TRP A 210 ? 0.8444 1.0841 1.0480 0.1125  0.0196  0.1050  210 TRP A CA  
1619 C C   . TRP A 210 ? 0.7307 0.9959 0.9570 0.1031  0.0117  0.1195  210 TRP A C   
1620 O O   . TRP A 210 ? 0.7441 1.0365 0.9929 0.1090  0.0163  0.1307  210 TRP A O   
1621 C CB  . TRP A 210 ? 0.8064 1.0525 1.0080 0.1155  0.0300  0.1020  210 TRP A CB  
1622 C CG  . TRP A 210 ? 0.8076 1.0547 1.0052 0.0967  0.0266  0.0995  210 TRP A CG  
1623 C CD1 . TRP A 210 ? 0.8006 1.0702 1.0139 0.0862  0.0260  0.1089  210 TRP A CD1 
1624 C CD2 . TRP A 210 ? 0.8766 1.1003 1.0534 0.0862  0.0234  0.0870  210 TRP A CD2 
1625 N NE1 . TRP A 210 ? 0.7165 0.9758 0.9170 0.0704  0.0228  0.1025  210 TRP A NE1 
1626 C CE2 . TRP A 210 ? 0.8618 1.0940 1.0407 0.0707  0.0216  0.0893  210 TRP A CE2 
1627 C CE3 . TRP A 210 ? 0.6910 0.8878 0.8491 0.0884  0.0218  0.0746  210 TRP A CE3 
1628 C CZ2 . TRP A 210 ? 0.7262 0.9408 0.8884 0.0589  0.0194  0.0798  210 TRP A CZ2 
1629 C CZ3 . TRP A 210 ? 0.6636 0.8455 0.8083 0.0759  0.0193  0.0657  210 TRP A CZ3 
1630 C CH2 . TRP A 210 ? 0.7433 0.9342 0.8897 0.0621  0.0186  0.0683  210 TRP A CH2 
1631 N N   . ALA A 211 ? 0.6998 0.9557 0.9202 0.0884  -0.0002 0.1195  211 ALA A N   
1632 C CA  . ALA A 211 ? 0.6490 0.9247 0.8871 0.0779  -0.0108 0.1324  211 ALA A CA  
1633 C C   . ALA A 211 ? 0.7539 1.0453 0.9998 0.0636  -0.0112 0.1358  211 ALA A C   
1634 O O   . ALA A 211 ? 0.7597 1.0354 0.9878 0.0519  -0.0111 0.1269  211 ALA A O   
1635 C CB  . ALA A 211 ? 0.5494 0.8051 0.7726 0.0670  -0.0231 0.1305  211 ALA A CB  
1636 N N   . CYS A 212 ? 0.6664 0.9888 0.9401 0.0647  -0.0114 0.1493  212 CYS A N   
1637 C CA  . CYS A 212 ? 0.6770 1.0154 0.9609 0.0507  -0.0121 0.1542  212 CYS A CA  
1638 C C   . CYS A 212 ? 0.6485 1.0216 0.9674 0.0499  -0.0175 0.1716  212 CYS A C   
1639 O O   . CYS A 212 ? 0.6387 1.0249 0.9746 0.0633  -0.0178 0.1794  212 CYS A O   
1640 C CB  . CYS A 212 ? 0.6503 0.9882 0.9287 0.0571  0.0033  0.1480  212 CYS A CB  
1641 S SG  . CYS A 212 ? 0.7259 1.0826 1.0222 0.0830  0.0199  0.1538  212 CYS A SG  
1642 N N   . ASN A 213 ? 0.6402 1.0278 0.9705 0.0340  -0.0220 0.1779  213 ASN A N   
1643 C CA  . ASN A 213 ? 0.7480 1.1707 1.1152 0.0300  -0.0283 0.1952  213 ASN A CA  
1644 C C   . ASN A 213 ? 0.7105 1.1487 1.0897 0.0205  -0.0216 0.1994  213 ASN A C   
1645 O O   . ASN A 213 ? 0.7276 1.1631 1.1033 0.0002  -0.0323 0.2006  213 ASN A O   
1646 C CB  . ASN A 213 ? 0.7649 1.1860 1.1334 0.0144  -0.0501 0.2009  213 ASN A CB  
1647 C CG  . ASN A 213 ? 0.7357 1.1941 1.1457 0.0143  -0.0587 0.2194  213 ASN A CG  
1648 O OD1 . ASN A 213 ? 0.7349 1.2226 1.1747 0.0168  -0.0501 0.2293  213 ASN A OD1 
1649 N ND2 . ASN A 213 ? 0.8323 1.2899 1.2451 0.0116  -0.0755 0.2248  213 ASN A ND2 
1650 N N   . PRO A 214 ? 0.7730 1.2254 1.1643 0.0353  -0.0034 0.2017  214 PRO A N   
1651 C CA  . PRO A 214 ? 0.7594 1.2237 1.1591 0.0271  0.0050  0.2054  214 PRO A CA  
1652 C C   . PRO A 214 ? 0.8159 1.3107 1.2504 0.0115  -0.0053 0.2220  214 PRO A C   
1653 O O   . PRO A 214 ? 0.6683 1.1632 1.1017 -0.0047 -0.0066 0.2230  214 PRO A O   
1654 C CB  . PRO A 214 ? 0.7071 1.1808 1.1135 0.0499  0.0268  0.2065  214 PRO A CB  
1655 C CG  . PRO A 214 ? 0.8231 1.2767 1.2101 0.0677  0.0293  0.1968  214 PRO A CG  
1656 C CD  . PRO A 214 ? 0.8187 1.2725 1.2116 0.0606  0.0109  0.2004  214 PRO A CD  
1657 N N   . GLU A 215 ? 0.9431 1.4637 1.4093 0.0158  -0.0132 0.2352  215 GLU A N   
1658 C CA  . GLU A 215 ? 0.8811 1.4342 1.3855 0.0011  -0.0240 0.2523  215 GLU A CA  
1659 C C   . GLU A 215 ? 0.8108 1.3475 1.2998 -0.0253 -0.0458 0.2495  215 GLU A C   
1660 O O   . GLU A 215 ? 0.7828 1.3363 1.2923 -0.0425 -0.0532 0.2592  215 GLU A O   
1661 C CB  . GLU A 215 ? 0.8904 1.4741 1.4320 0.0124  -0.0294 0.2670  215 GLU A CB  
1662 C CG  . GLU A 215 ? 1.0289 1.6304 1.5881 0.0396  -0.0072 0.2720  215 GLU A CG  
1663 C CD  . GLU A 215 ? 1.0609 1.6323 1.5862 0.0588  0.0001  0.2576  215 GLU A CD  
1664 O OE1 . GLU A 215 ? 1.0164 1.5557 1.5079 0.0505  -0.0118 0.2445  215 GLU A OE1 
1665 O OE2 . GLU A 215 ? 1.0769 1.6559 1.6092 0.0821  0.0178  0.2596  215 GLU A OE2 
1666 N N   . LEU A 216 ? 0.7505 1.2533 1.2029 -0.0288 -0.0559 0.2365  216 LEU A N   
1667 C CA  . LEU A 216 ? 0.6727 1.1558 1.1057 -0.0516 -0.0766 0.2336  216 LEU A CA  
1668 C C   . LEU A 216 ? 0.7300 1.1747 1.1186 -0.0594 -0.0722 0.2168  216 LEU A C   
1669 O O   . LEU A 216 ? 0.6680 1.0866 1.0295 -0.0737 -0.0866 0.2108  216 LEU A O   
1670 C CB  . LEU A 216 ? 0.5157 0.9911 0.9432 -0.0507 -0.0939 0.2349  216 LEU A CB  
1671 C CG  . LEU A 216 ? 0.6779 1.1895 1.1479 -0.0403 -0.0993 0.2511  216 LEU A CG  
1672 C CD1 . LEU A 216 ? 0.5042 1.0020 0.9620 -0.0403 -0.1177 0.2511  216 LEU A CD1 
1673 C CD2 . LEU A 216 ? 0.5694 1.1168 1.0812 -0.0537 -0.1074 0.2679  216 LEU A CD2 
1674 N N   . THR A 217 ? 0.6651 1.1050 1.0449 -0.0498 -0.0525 0.2095  217 THR A N   
1675 C CA  . THR A 217 ? 0.6783 1.0839 1.0187 -0.0556 -0.0478 0.1941  217 THR A CA  
1676 C C   . THR A 217 ? 0.6961 1.0942 1.0293 -0.0787 -0.0578 0.1959  217 THR A C   
1677 O O   . THR A 217 ? 0.6463 1.0673 1.0050 -0.0861 -0.0566 0.2067  217 THR A O   
1678 C CB  . THR A 217 ? 0.7751 1.1796 1.1102 -0.0400 -0.0260 0.1873  217 THR A CB  
1679 O OG1 . THR A 217 ? 0.7099 1.1158 1.0467 -0.0187 -0.0177 0.1842  217 THR A OG1 
1680 C CG2 . THR A 217 ? 0.6730 1.0440 0.9702 -0.0459 -0.0220 0.1721  217 THR A CG2 
1681 N N   . LEU A 218 ? 0.6817 1.0465 0.9796 -0.0900 -0.0672 0.1857  218 LEU A N   
1682 C CA  . LEU A 218 ? 0.7076 1.0581 0.9914 -0.1115 -0.0773 0.1859  218 LEU A CA  
1683 C C   . LEU A 218 ? 0.7152 1.0250 0.9540 -0.1149 -0.0755 0.1702  218 LEU A C   
1684 O O   . LEU A 218 ? 0.6757 0.9668 0.8950 -0.1098 -0.0788 0.1633  218 LEU A O   
1685 C CB  . LEU A 218 ? 0.7103 1.0680 1.0059 -0.1270 -0.1003 0.1966  218 LEU A CB  
1686 C CG  . LEU A 218 ? 0.7538 1.0909 1.0296 -0.1504 -0.1140 0.1962  218 LEU A CG  
1687 C CD1 . LEU A 218 ? 0.7243 1.0785 1.0200 -0.1588 -0.1074 0.2030  218 LEU A CD1 
1688 C CD2 . LEU A 218 ? 0.7746 1.1119 1.0544 -0.1639 -0.1391 0.2045  218 LEU A CD2 
1689 N N   . ILE A 219 ? 0.7671 1.0633 0.9903 -0.1231 -0.0694 0.1655  219 ILE A N   
1690 C CA  . ILE A 219 ? 0.6670 0.9257 0.8494 -0.1273 -0.0672 0.1519  219 ILE A CA  
1691 C C   . ILE A 219 ? 0.6765 0.9198 0.8445 -0.1486 -0.0790 0.1545  219 ILE A C   
1692 O O   . ILE A 219 ? 0.7737 1.0267 0.9527 -0.1556 -0.0754 0.1595  219 ILE A O   
1693 C CB  . ILE A 219 ? 0.7204 0.9729 0.8932 -0.1148 -0.0479 0.1422  219 ILE A CB  
1694 C CG1 . ILE A 219 ? 0.6126 0.8776 0.7975 -0.0940 -0.0376 0.1393  219 ILE A CG1 
1695 C CG2 . ILE A 219 ? 0.6618 0.8777 0.7958 -0.1194 -0.0460 0.1295  219 ILE A CG2 
1696 C CD1 . ILE A 219 ? 0.6383 0.9388 0.8597 -0.0846 -0.0315 0.1505  219 ILE A CD1 
1697 N N   . ALA A 220 ? 0.6849 0.9019 0.8265 -0.1587 -0.0928 0.1514  220 ALA A N   
1698 C CA  . ALA A 220 ? 0.7175 0.9149 0.8407 -0.1791 -0.1066 0.1536  220 ALA A CA  
1699 C C   . ALA A 220 ? 0.7078 0.8624 0.7845 -0.1819 -0.1029 0.1407  220 ALA A C   
1700 O O   . ALA A 220 ? 0.7067 0.8464 0.7661 -0.1710 -0.0960 0.1320  220 ALA A O   
1701 C CB  . ALA A 220 ? 0.7356 0.9374 0.8662 -0.1903 -0.1291 0.1629  220 ALA A CB  
1702 N N   . HIS A 221 ? 0.7100 0.8448 0.7674 -0.1966 -0.1071 0.1400  221 HIS A N   
1703 C CA  . HIS A 221 ? 0.8218 0.9147 0.8344 -0.2000 -0.1036 0.1289  221 HIS A CA  
1704 C C   . HIS A 221 ? 0.7824 0.8493 0.7704 -0.2200 -0.1224 0.1321  221 HIS A C   
1705 O O   . HIS A 221 ? 0.6652 0.7439 0.6692 -0.2336 -0.1327 0.1408  221 HIS A O   
1706 C CB  . HIS A 221 ? 0.6796 0.7677 0.6863 -0.1954 -0.0865 0.1228  221 HIS A CB  
1707 C CG  . HIS A 221 ? 0.8097 0.9199 0.8369 -0.1762 -0.0692 0.1191  221 HIS A CG  
1708 N ND1 . HIS A 221 ? 0.8355 0.9832 0.9015 -0.1692 -0.0656 0.1271  221 HIS A ND1 
1709 C CD2 . HIS A 221 ? 0.6788 0.7775 0.6922 -0.1625 -0.0549 0.1084  221 HIS A CD2 
1710 C CE1 . HIS A 221 ? 0.6946 0.8502 0.7663 -0.1518 -0.0503 0.1208  221 HIS A CE1 
1711 N NE2 . HIS A 221 ? 0.6207 0.7477 0.6621 -0.1481 -0.0445 0.1094  221 HIS A NE2 
1712 N N   . LEU A 222 ? 0.8436 0.8741 0.7920 -0.2217 -0.1269 0.1252  222 LEU A N   
1713 C CA  . LEU A 222 ? 0.8891 0.8861 0.8042 -0.2392 -0.1446 0.1263  222 LEU A CA  
1714 C C   . LEU A 222 ? 0.8930 0.8461 0.7609 -0.2383 -0.1341 0.1150  222 LEU A C   
1715 O O   . LEU A 222 ? 0.9072 0.8343 0.7455 -0.2321 -0.1309 0.1086  222 LEU A O   
1716 C CB  . LEU A 222 ? 0.8968 0.8882 0.8051 -0.2421 -0.1621 0.1304  222 LEU A CB  
1717 C CG  . LEU A 222 ? 0.8700 0.9024 0.8234 -0.2442 -0.1759 0.1429  222 LEU A CG  
1718 C CD1 . LEU A 222 ? 0.8985 0.9661 0.8868 -0.2248 -0.1608 0.1433  222 LEU A CD1 
1719 C CD2 . LEU A 222 ? 0.9804 0.9970 0.9171 -0.2531 -0.1992 0.1474  222 LEU A CD2 
1720 N N   . PRO A 223 ? 0.9069 0.9551 0.7316 -0.2854 -0.0815 0.0233  223 PRO A N   
1721 C CA  . PRO A 223 ? 0.9022 0.9152 0.7032 -0.2841 -0.0688 0.0008  223 PRO A CA  
1722 C C   . PRO A 223 ? 1.1688 1.1595 0.9257 -0.2988 -0.0747 -0.0125 223 PRO A C   
1723 O O   . PRO A 223 ? 1.2635 1.2296 0.9957 -0.2939 -0.0605 -0.0281 223 PRO A O   
1724 C CB  . PRO A 223 ? 0.9987 1.0004 0.8187 -0.2866 -0.0692 -0.0039 223 PRO A CB  
1725 C CG  . PRO A 223 ? 1.0567 1.0820 0.8966 -0.2982 -0.0873 0.0126  223 PRO A CG  
1726 C CD  . PRO A 223 ? 0.9682 1.0268 0.8223 -0.2908 -0.0901 0.0319  223 PRO A CD  
1727 N N   . ASP A 224 ? 1.3003 1.2986 1.0461 -0.3171 -0.0950 -0.0064 224 ASP A N   
1728 C CA  . ASP A 224 ? 1.4087 1.3834 1.1077 -0.3330 -0.1022 -0.0194 224 ASP A CA  
1729 C C   . ASP A 224 ? 1.3914 1.3678 1.0641 -0.3266 -0.0955 -0.0187 224 ASP A C   
1730 O O   . ASP A 224 ? 1.4374 1.3852 1.0676 -0.3325 -0.0906 -0.0345 224 ASP A O   
1731 C CB  . ASP A 224 ? 1.5108 1.4971 1.2063 -0.3550 -0.1283 -0.0108 224 ASP A CB  
1732 C CG  . ASP A 224 ? 1.5188 1.5033 1.2428 -0.3593 -0.1330 -0.0097 224 ASP A CG  
1733 O OD1 . ASP A 224 ? 1.5028 1.4641 1.2309 -0.3538 -0.1194 -0.0233 224 ASP A OD1 
1734 O OD2 . ASP A 224 ? 1.5007 1.5068 1.2445 -0.3658 -0.1489 0.0059  224 ASP A OD2 
1735 N N   . ARG A 225 ? 1.2160 1.2235 0.9119 -0.3144 -0.0941 -0.0005 225 ARG A N   
1736 C CA  . ARG A 225 ? 1.1973 1.2081 0.8718 -0.3074 -0.0872 0.0026  225 ARG A CA  
1737 C C   . ARG A 225 ? 1.1439 1.1490 0.8294 -0.2869 -0.0626 -0.0026 225 ARG A C   
1738 O O   . ARG A 225 ? 1.1693 1.1734 0.8369 -0.2804 -0.0536 -0.0018 225 ARG A O   
1739 C CB  . ARG A 225 ? 1.2080 1.2559 0.8989 -0.3076 -0.1016 0.0272  225 ARG A CB  
1740 C CG  . ARG A 225 ? 1.2920 1.3502 0.9714 -0.3287 -0.1280 0.0352  225 ARG A CG  
1741 C CD  . ARG A 225 ? 1.3326 1.4289 1.0305 -0.3261 -0.1401 0.0611  225 ARG A CD  
1742 N NE  . ARG A 225 ? 1.4864 1.5969 1.1780 -0.3465 -0.1674 0.0711  225 ARG A NE  
1743 C CZ  . ARG A 225 ? 1.6705 1.8148 1.3769 -0.3479 -0.1824 0.0946  225 ARG A CZ  
1744 N NH1 . ARG A 225 ? 1.6393 1.8050 1.3662 -0.3298 -0.1719 0.1105  225 ARG A NH1 
1745 N NH2 . ARG A 225 ? 1.8541 2.0057 1.5631 -0.3607 -0.2010 0.1028  225 ARG A NH2 
1746 N N   . ARG A 226 ? 1.1082 1.1098 0.8228 -0.2770 -0.0521 -0.0073 226 ARG A N   
1747 C CA  . ARG A 226 ? 1.0246 1.0238 0.7542 -0.2584 -0.0311 -0.0108 226 ARG A CA  
1748 C C   . ARG A 226 ? 0.9538 0.9815 0.7030 -0.2471 -0.0293 0.0076  226 ARG A C   
1749 O O   . ARG A 226 ? 0.9946 1.0199 0.7382 -0.2366 -0.0152 0.0062  226 ARG A O   
1750 C CB  . ARG A 226 ? 1.1158 1.0860 0.8124 -0.2564 -0.0153 -0.0287 226 ARG A CB  
1751 C CG  . ARG A 226 ? 1.2310 1.1684 0.9048 -0.2664 -0.0139 -0.0482 226 ARG A CG  
1752 C CD  . ARG A 226 ? 1.3667 1.2982 1.0712 -0.2598 -0.0082 -0.0535 226 ARG A CD  
1753 N NE  . ARG A 226 ? 1.4622 1.3581 1.1457 -0.2640 0.0006  -0.0736 226 ARG A NE  
1754 C CZ  . ARG A 226 ? 1.4220 1.2997 1.0887 -0.2794 -0.0103 -0.0814 226 ARG A CZ  
1755 N NH1 . ARG A 226 ? 1.4855 1.3790 1.1556 -0.2931 -0.0316 -0.0706 226 ARG A NH1 
1756 N NH2 . ARG A 226 ? 1.5614 1.4037 1.2086 -0.2811 0.0009  -0.1002 226 ARG A NH2 
1757 N N   . GLU A 227 ? 0.8882 0.9424 0.6615 -0.2492 -0.0428 0.0255  227 GLU A N   
1758 C CA  . GLU A 227 ? 0.8238 0.9044 0.6149 -0.2393 -0.0421 0.0446  227 GLU A CA  
1759 C C   . GLU A 227 ? 0.7803 0.8789 0.6122 -0.2303 -0.0412 0.0561  227 GLU A C   
1760 O O   . GLU A 227 ? 0.7444 0.8425 0.5906 -0.2360 -0.0481 0.0549  227 GLU A O   
1761 C CB  . GLU A 227 ? 0.9207 1.0190 0.6992 -0.2500 -0.0596 0.0592  227 GLU A CB  
1762 C CG  . GLU A 227 ? 1.0087 1.0891 0.7420 -0.2596 -0.0618 0.0495  227 GLU A CG  
1763 C CD  . GLU A 227 ? 1.0454 1.1444 0.7663 -0.2712 -0.0820 0.0651  227 GLU A CD  
1764 O OE1 . GLU A 227 ? 0.9351 1.0618 0.6858 -0.2725 -0.0947 0.0833  227 GLU A OE1 
1765 O OE2 . GLU A 227 ? 1.1021 1.1884 0.7836 -0.2789 -0.0851 0.0600  227 GLU A OE2 
1766 N N   . ILE A 228 ? 0.8153 0.9279 0.6639 -0.2162 -0.0317 0.0672  228 ILE A N   
1767 C CA  . ILE A 228 ? 0.7953 0.9242 0.6788 -0.2063 -0.0290 0.0796  228 ILE A CA  
1768 C C   . ILE A 228 ? 0.7840 0.9360 0.6777 -0.1993 -0.0295 0.0998  228 ILE A C   
1769 O O   . ILE A 228 ? 0.6492 0.7986 0.5304 -0.1928 -0.0208 0.1002  228 ILE A O   
1770 C CB  . ILE A 228 ? 0.6717 0.7870 0.5660 -0.1936 -0.0127 0.0692  228 ILE A CB  
1771 C CG1 . ILE A 228 ? 0.7935 0.8857 0.6787 -0.1992 -0.0113 0.0501  228 ILE A CG1 
1772 C CG2 . ILE A 228 ? 0.6474 0.7770 0.5725 -0.1841 -0.0102 0.0818  228 ILE A CG2 
1773 C CD1 . ILE A 228 ? 0.8090 0.8892 0.7062 -0.1874 0.0027  0.0406  228 ILE A CD1 
1774 N N   . ILE A 229 ? 0.7709 0.9454 0.6886 -0.2003 -0.0387 0.1172  229 ILE A N   
1775 C CA  . ILE A 229 ? 0.7346 0.9327 0.6651 -0.1938 -0.0400 0.1387  229 ILE A CA  
1776 C C   . ILE A 229 ? 0.7735 0.9845 0.7376 -0.1826 -0.0332 0.1512  229 ILE A C   
1777 O O   . ILE A 229 ? 0.7850 1.0037 0.7672 -0.1878 -0.0403 0.1554  229 ILE A O   
1778 C CB  . ILE A 229 ? 0.8440 1.0606 0.7703 -0.2072 -0.0597 0.1514  229 ILE A CB  
1779 C CG1 . ILE A 229 ? 0.7976 0.9986 0.6846 -0.2180 -0.0655 0.1391  229 ILE A CG1 
1780 C CG2 . ILE A 229 ? 0.8341 1.0776 0.7802 -0.1986 -0.0605 0.1763  229 ILE A CG2 
1781 C CD1 . ILE A 229 ? 0.9305 1.1474 0.8080 -0.2330 -0.0872 0.1503  229 ILE A CD1 
1782 N N   . SER A 230 ? 0.8960 1.1075 0.8668 -0.1677 -0.0188 0.1570  230 SER A N   
1783 C CA  . SER A 230 ? 0.8293 1.0501 0.8272 -0.1557 -0.0100 0.1693  230 SER A CA  
1784 C C   . SER A 230 ? 0.5739 0.8118 0.5812 -0.1461 -0.0058 0.1893  230 SER A C   
1785 O O   . SER A 230 ? 0.5873 0.8227 0.5778 -0.1447 -0.0039 0.1897  230 SER A O   
1786 C CB  . SER A 230 ? 0.7225 0.9226 0.7191 -0.1457 0.0054  0.1556  230 SER A CB  
1787 O OG  . SER A 230 ? 0.7469 0.9496 0.7644 -0.1314 0.0134  0.1637  230 SER A OG  
1788 N N   . PHE A 231 ? 0.6530 0.9030 0.6875 -0.1352 -0.0048 0.2014  231 PHE A N   
1789 C CA  . PHE A 231 ? 0.7084 0.9713 0.7563 -0.1220 -0.0019 0.2170  231 PHE A CA  
1790 C C   . PHE A 231 ? 0.7039 0.9655 0.7756 -0.1054 0.0079  0.2213  231 PHE A C   
1791 O O   . PHE A 231 ? 0.6782 0.9420 0.7625 -0.1079 0.0055  0.2211  231 PHE A O   
1792 C CB  . PHE A 231 ? 0.6765 0.9687 0.7318 -0.1338 -0.0188 0.2368  231 PHE A CB  
1793 C CG  . PHE A 231 ? 0.7253 1.0339 0.7983 -0.1200 -0.0165 0.2550  231 PHE A CG  
1794 C CD1 . PHE A 231 ? 0.7371 1.0622 0.8424 -0.1099 -0.0151 0.2696  231 PHE A CD1 
1795 C CD2 . PHE A 231 ? 0.8282 1.1349 0.8858 -0.1166 -0.0148 0.2576  231 PHE A CD2 
1796 C CE1 . PHE A 231 ? 0.6978 1.0383 0.8212 -0.0969 -0.0118 0.2869  231 PHE A CE1 
1797 C CE2 . PHE A 231 ? 0.7253 1.0465 0.8006 -0.1037 -0.0122 0.2746  231 PHE A CE2 
1798 C CZ  . PHE A 231 ? 0.6478 0.9866 0.7569 -0.0939 -0.0106 0.2895  231 PHE A CZ  
1799 N N   . GLY A 232 ? 0.6664 0.9219 0.7417 -0.0889 0.0195  0.2247  232 GLY A N   
1800 C CA  . GLY A 232 ? 0.7542 1.0071 0.8483 -0.0734 0.0296  0.2298  232 GLY A CA  
1801 C C   . GLY A 232 ? 0.8227 1.0451 0.9049 -0.0643 0.0441  0.2124  232 GLY A C   
1802 O O   . GLY A 232 ? 0.8667 1.0768 0.9491 -0.0508 0.0561  0.2122  232 GLY A O   
1803 N N   . SER A 233 ? 0.9020 1.1122 0.9735 -0.0726 0.0425  0.1984  233 SER A N   
1804 C CA  . SER A 233 ? 0.8162 1.0003 0.8776 -0.0660 0.0538  0.1836  233 SER A CA  
1805 C C   . SER A 233 ? 0.8137 0.9793 0.8548 -0.0658 0.0602  0.1707  233 SER A C   
1806 O O   . SER A 233 ? 0.7994 0.9706 0.8339 -0.0686 0.0577  0.1735  233 SER A O   
1807 C CB  . SER A 233 ? 0.7949 0.9760 0.8570 -0.0743 0.0492  0.1765  233 SER A CB  
1808 O OG  . SER A 233 ? 0.8765 1.0342 0.9285 -0.0689 0.0588  0.1638  233 SER A OG  
1809 N N   . GLY A 234 ? 0.9483 1.0921 0.9795 -0.0629 0.0682  0.1574  234 GLY A N   
1810 C CA  . GLY A 234 ? 0.9860 1.1127 1.0010 -0.0632 0.0746  0.1454  234 GLY A CA  
1811 C C   . GLY A 234 ? 1.0117 1.1186 1.0197 -0.0614 0.0813  0.1335  234 GLY A C   
1812 O O   . GLY A 234 ? 1.0361 1.1270 1.0340 -0.0581 0.0892  0.1263  234 GLY A O   
1813 N N   A TYR A 235 ? 1.1519 1.2604 1.1649 -0.0648 0.0773  0.1320  235 TYR A N   
1814 N N   B TYR A 235 ? 1.1248 1.2334 1.1382 -0.0644 0.0775  0.1324  235 TYR A N   
1815 C CA  A TYR A 235 ? 1.1858 1.2778 1.1926 -0.0634 0.0822  0.1233  235 TYR A CA  
1816 C CA  B TYR A 235 ? 1.1600 1.2523 1.1669 -0.0636 0.0820  0.1233  235 TYR A CA  
1817 C C   A TYR A 235 ? 1.1210 1.2158 1.1284 -0.0733 0.0755  0.1168  235 TYR A C   
1818 C C   B TYR A 235 ? 1.1199 1.2156 1.1272 -0.0738 0.0751  0.1166  235 TYR A C   
1819 O O   A TYR A 235 ? 1.0954 1.2024 1.1113 -0.0790 0.0676  0.1213  235 TYR A O   
1820 O O   B TYR A 235 ? 1.0904 1.1993 1.1056 -0.0805 0.0667  0.1210  235 TYR A O   
1821 C CB  A TYR A 235 ? 1.1355 1.2241 1.1471 -0.0560 0.0858  0.1293  235 TYR A CB  
1822 C CB  B TYR A 235 ? 1.1363 1.2249 1.1479 -0.0569 0.0852  0.1287  235 TYR A CB  
1823 C CG  A TYR A 235 ? 1.1284 1.1979 1.1289 -0.0536 0.0918  0.1220  235 TYR A CG  
1824 C CG  B TYR A 235 ? 1.1405 1.2196 1.1482 -0.0597 0.0848  0.1227  235 TYR A CG  
1825 C CD1 A TYR A 235 ? 1.1305 1.1971 1.1306 -0.0584 0.0884  0.1182  235 TYR A CD1 
1826 C CD1 B TYR A 235 ? 1.1262 1.1876 1.1211 -0.0581 0.0907  0.1148  235 TYR A CD1 
1827 C CD2 A TYR A 235 ? 1.1022 1.1574 1.0925 -0.0472 0.1001  0.1199  235 TYR A CD2 
1828 C CD2 B TYR A 235 ? 1.1104 1.1988 1.1275 -0.0648 0.0779  0.1259  235 TYR A CD2 
1829 C CE1 A TYR A 235 ? 1.1348 1.1851 1.1238 -0.0565 0.0930  0.1135  235 TYR A CE1 
1830 C CE1 B TYR A 235 ? 1.1282 1.1822 1.1197 -0.0607 0.0896  0.1115  235 TYR A CE1 
1831 C CE2 A TYR A 235 ? 1.1260 1.1649 1.1043 -0.0463 0.1041  0.1145  235 TYR A CE2 
1832 C CE2 B TYR A 235 ? 1.0822 1.1616 1.0959 -0.0672 0.0774  0.1217  235 TYR A CE2 
1833 C CZ  A TYR A 235 ? 1.1091 1.1458 1.0864 -0.0508 0.1005  0.1117  235 TYR A CZ  
1834 C CZ  B TYR A 235 ? 1.0931 1.1558 1.0940 -0.0647 0.0831  0.1150  235 TYR A CZ  
1835 O OH  A TYR A 235 ? 1.0668 1.0876 1.0313 -0.0498 0.1039  0.1081  235 TYR A OH  
1836 O OH  B TYR A 235 ? 1.1076 1.1626 1.1051 -0.0672 0.0816  0.1129  235 TYR A OH  
1837 N N   . GLY A 236 ? 1.2201 1.3044 1.2197 -0.0762 0.0783  0.1064  236 GLY A N   
1838 C CA  . GLY A 236 ? 1.0830 1.1687 1.0834 -0.0857 0.0725  0.0992  236 GLY A CA  
1839 C C   . GLY A 236 ? 1.0142 1.1128 1.0175 -0.0963 0.0636  0.0993  236 GLY A C   
1840 O O   . GLY A 236 ? 0.9415 1.0454 0.9397 -0.1003 0.0626  0.0980  236 GLY A O   
1841 N N   . GLY A 237 ? 1.0263 1.1278 1.0359 -0.1015 0.0569  0.1003  237 GLY A N   
1842 C CA  . GLY A 237 ? 1.0235 1.1309 1.0337 -0.1115 0.0472  0.0967  237 GLY A CA  
1843 C C   . GLY A 237 ? 1.0893 1.2137 1.1011 -0.1162 0.0428  0.1081  237 GLY A C   
1844 O O   . GLY A 237 ? 1.1323 1.2596 1.1393 -0.1258 0.0344  0.1034  237 GLY A O   
1845 N N   . ASN A 238 ? 1.0056 1.1361 1.0228 -0.1063 0.0468  0.1191  238 ASN A N   
1846 C CA  . ASN A 238 ? 0.9681 1.1152 0.9889 -0.1087 0.0410  0.1302  238 ASN A CA  
1847 C C   . ASN A 238 ? 0.9522 1.0993 0.9598 -0.1103 0.0429  0.1274  238 ASN A C   
1848 O O   . ASN A 238 ? 0.8694 1.0282 0.8717 -0.1203 0.0350  0.1317  238 ASN A O   
1849 C CB  . ASN A 238 ? 0.9660 1.1189 0.9996 -0.0963 0.0448  0.1426  238 ASN A CB  
1850 C CG  . ASN A 238 ? 0.9479 1.1011 0.9937 -0.0944 0.0439  0.1464  238 ASN A CG  
1851 O OD1 . ASN A 238 ? 0.9334 1.0805 0.9837 -0.0829 0.0519  0.1500  238 ASN A OD1 
1852 N ND2 . ASN A 238 ? 0.9069 1.0651 0.9563 -0.1064 0.0349  0.1449  238 ASN A ND2 
1853 N N   . SER A 239 ? 0.9269 1.0602 0.9278 -0.1017 0.0532  0.1206  239 SER A N   
1854 C CA  . SER A 239 ? 0.8230 0.9539 0.8119 -0.1016 0.0570  0.1179  239 SER A CA  
1855 C C   . SER A 239 ? 0.8398 0.9611 0.8165 -0.1098 0.0594  0.1034  239 SER A C   
1856 O O   . SER A 239 ? 0.7769 0.8998 0.7408 -0.1160 0.0590  0.1008  239 SER A O   
1857 C CB  . SER A 239 ? 0.8668 0.9873 0.8566 -0.0878 0.0676  0.1199  239 SER A CB  
1858 O OG  . SER A 239 ? 1.0077 1.1135 0.9990 -0.0827 0.0743  0.1125  239 SER A OG  
1859 N N   . LEU A 240 ? 0.8539 0.9647 0.8338 -0.1095 0.0622  0.0935  240 LEU A N   
1860 C CA  . LEU A 240 ? 0.7693 0.8676 0.7425 -0.1130 0.0632  0.0765  240 LEU A CA  
1861 C C   . LEU A 240 ? 0.8025 0.9011 0.7725 -0.1222 0.0535  0.0702  240 LEU A C   
1862 O O   . LEU A 240 ? 0.8870 0.9799 0.8633 -0.1236 0.0498  0.0643  240 LEU A O   
1863 C CB  . LEU A 240 ? 0.8144 0.9012 0.7944 -0.1075 0.0678  0.0688  240 LEU A CB  
1864 C CG  . LEU A 240 ? 0.7773 0.8602 0.7587 -0.0994 0.0767  0.0743  240 LEU A CG  
1865 C CD1 . LEU A 240 ? 0.7255 0.7961 0.7111 -0.0963 0.0785  0.0651  240 LEU A CD1 
1866 C CD2 . LEU A 240 ? 0.6285 0.7113 0.6024 -0.0987 0.0840  0.0750  240 LEU A CD2 
1867 N N   . LEU A 241 ? 0.8460 0.9498 0.8041 -0.1290 0.0494  0.0716  241 LEU A N   
1868 C CA  . LEU A 241 ? 0.8447 0.9474 0.7962 -0.1394 0.0394  0.0664  241 LEU A CA  
1869 C C   . LEU A 241 ? 0.6928 0.7786 0.6399 -0.1417 0.0419  0.0487  241 LEU A C   
1870 O O   . LEU A 241 ? 0.8555 0.9362 0.8008 -0.1488 0.0348  0.0432  241 LEU A O   
1871 C CB  . LEU A 241 ? 0.6608 0.7702 0.5958 -0.1467 0.0341  0.0708  241 LEU A CB  
1872 C CG  . LEU A 241 ? 0.6444 0.7730 0.5855 -0.1450 0.0300  0.0903  241 LEU A CG  
1873 C CD1 . LEU A 241 ? 0.6380 0.7729 0.5612 -0.1540 0.0217  0.0943  241 LEU A CD1 
1874 C CD2 . LEU A 241 ? 0.7077 0.8480 0.6685 -0.1450 0.0232  0.1011  241 LEU A CD2 
1875 N N   . GLY A 242 ? 0.7077 0.7846 0.6544 -0.1359 0.0521  0.0401  242 GLY A N   
1876 C CA  . GLY A 242 ? 0.9086 0.9711 0.8544 -0.1368 0.0557  0.0247  242 GLY A CA  
1877 C C   . GLY A 242 ? 0.8382 0.8959 0.7998 -0.1335 0.0533  0.0215  242 GLY A C   
1878 O O   . GLY A 242 ? 0.8838 0.9300 0.8465 -0.1347 0.0544  0.0102  242 GLY A O   
1879 N N   . LYS A 243 ? 0.8094 0.8744 0.7824 -0.1289 0.0507  0.0317  243 LYS A N   
1880 C CA  . LYS A 243 ? 0.7843 0.8440 0.7701 -0.1250 0.0487  0.0300  243 LYS A CA  
1881 C C   . LYS A 243 ? 0.8549 0.9144 0.8429 -0.1310 0.0399  0.0325  243 LYS A C   
1882 O O   . LYS A 243 ? 0.8648 0.9136 0.8535 -0.1338 0.0379  0.0233  243 LYS A O   
1883 C CB  . LYS A 243 ? 0.7803 0.8444 0.7735 -0.1172 0.0515  0.0389  243 LYS A CB  
1884 C CG  . LYS A 243 ? 0.7205 0.7779 0.7233 -0.1129 0.0494  0.0376  243 LYS A CG  
1885 C CD  . LYS A 243 ? 0.6951 0.7530 0.6995 -0.1058 0.0531  0.0449  243 LYS A CD  
1886 C CE  . LYS A 243 ? 0.6204 0.6702 0.6303 -0.1020 0.0501  0.0438  243 LYS A CE  
1887 N NZ  . LYS A 243 ? 0.7033 0.7455 0.7191 -0.1018 0.0488  0.0319  243 LYS A NZ  
1888 N N   . LYS A 244 ? 0.8641 0.9353 0.8545 -0.1328 0.0352  0.0455  244 LYS A N   
1889 C CA  . LYS A 244 ? 0.7286 0.8014 0.7243 -0.1389 0.0269  0.0500  244 LYS A CA  
1890 C C   . LYS A 244 ? 0.7697 0.8441 0.7551 -0.1506 0.0197  0.0478  244 LYS A C   
1891 O O   . LYS A 244 ? 0.7460 0.8100 0.7291 -0.1575 0.0151  0.0401  244 LYS A O   
1892 C CB  . LYS A 244 ? 0.7563 0.8418 0.7626 -0.1351 0.0262  0.0662  244 LYS A CB  
1893 C CG  . LYS A 244 ? 0.7708 0.8511 0.7833 -0.1247 0.0324  0.0682  244 LYS A CG  
1894 C CD  . LYS A 244 ? 0.6659 0.7334 0.6827 -0.1245 0.0299  0.0612  244 LYS A CD  
1895 C CE  . LYS A 244 ? 0.7875 0.8493 0.8073 -0.1151 0.0343  0.0640  244 LYS A CE  
1896 N NZ  . LYS A 244 ? 0.7261 0.7759 0.7500 -0.1143 0.0311  0.0587  244 LYS A NZ  
1897 N N   . CYS A 245 ? 0.7688 0.8549 0.7467 -0.1534 0.0182  0.0546  245 CYS A N   
1898 C CA  . CYS A 245 ? 0.7395 0.8284 0.7058 -0.1658 0.0089  0.0543  245 CYS A CA  
1899 C C   . CYS A 245 ? 0.8397 0.9097 0.7878 -0.1713 0.0107  0.0368  245 CYS A C   
1900 O O   . CYS A 245 ? 0.7519 0.8142 0.6906 -0.1824 0.0031  0.0312  245 CYS A O   
1901 C CB  . CYS A 245 ? 0.6033 0.7089 0.5648 -0.1664 0.0070  0.0664  245 CYS A CB  
1902 S SG  . CYS A 245 ? 0.4823 0.6101 0.4661 -0.1591 0.0068  0.0886  245 CYS A SG  
1903 N N   . PHE A 246 ? 0.8624 0.9238 0.8052 -0.1640 0.0215  0.0279  246 PHE A N   
1904 C CA  . PHE A 246 ? 0.9169 0.9606 0.8426 -0.1676 0.0263  0.0121  246 PHE A CA  
1905 C C   . PHE A 246 ? 0.9205 0.9480 0.8549 -0.1645 0.0303  0.0007  246 PHE A C   
1906 O O   . PHE A 246 ? 0.9023 0.9150 0.8271 -0.1718 0.0279  -0.0088 246 PHE A O   
1907 C CB  . PHE A 246 ? 0.9706 1.0146 0.8883 -0.1616 0.0370  0.0096  246 PHE A CB  
1908 C CG  . PHE A 246 ? 1.0123 1.0390 0.9103 -0.1651 0.0440  -0.0051 246 PHE A CG  
1909 C CD1 . PHE A 246 ? 1.0094 1.0212 0.8926 -0.1747 0.0394  -0.0146 246 PHE A CD1 
1910 C CD2 . PHE A 246 ? 1.0356 1.0594 0.9294 -0.1590 0.0563  -0.0094 246 PHE A CD2 
1911 C CE1 . PHE A 246 ? 1.1112 1.1044 0.9740 -0.1772 0.0480  -0.0284 246 PHE A CE1 
1912 C CE2 . PHE A 246 ? 1.0690 1.0764 0.9448 -0.1615 0.0650  -0.0223 246 PHE A CE2 
1913 C CZ  . PHE A 246 ? 1.1553 1.1467 1.0146 -0.1701 0.0614  -0.0320 246 PHE A CZ  
1914 N N   . ALA A 247 ? 0.9467 0.9759 0.8985 -0.1539 0.0362  0.0018  247 ALA A N   
1915 C CA  . ALA A 247 ? 0.8945 0.9097 0.8558 -0.1493 0.0406  -0.0081 247 ALA A CA  
1916 C C   . ALA A 247 ? 0.8955 0.9048 0.8646 -0.1527 0.0331  -0.0067 247 ALA A C   
1917 O O   . ALA A 247 ? 0.9421 0.9377 0.9174 -0.1498 0.0360  -0.0148 247 ALA A O   
1918 C CB  . ALA A 247 ? 0.9505 0.9706 0.9277 -0.1380 0.0467  -0.0062 247 ALA A CB  
1919 N N   . LEU A 248 ? 0.8234 0.8431 0.7941 -0.1585 0.0240  0.0043  248 LEU A N   
1920 C CA  . LEU A 248 ? 0.7252 0.7398 0.7046 -0.1623 0.0174  0.0070  248 LEU A CA  
1921 C C   . LEU A 248 ? 0.8670 0.8812 0.8362 -0.1764 0.0080  0.0083  248 LEU A C   
1922 O O   . LEU A 248 ? 0.8538 0.8505 0.8162 -0.1833 0.0062  -0.0013 248 LEU A O   
1923 C CB  . LEU A 248 ? 0.6244 0.6514 0.6203 -0.1554 0.0159  0.0205  248 LEU A CB  
1924 C CG  . LEU A 248 ? 0.6579 0.6791 0.6645 -0.1438 0.0216  0.0183  248 LEU A CG  
1925 C CD1 . LEU A 248 ? 0.4654 0.4948 0.4828 -0.1387 0.0196  0.0314  248 LEU A CD1 
1926 C CD2 . LEU A 248 ? 0.6649 0.6677 0.6739 -0.1437 0.0227  0.0074  248 LEU A CD2 
1927 N N   . ARG A 249 ? 0.7183 0.7508 0.6869 -0.1812 0.0016  0.0202  249 ARG A N   
1928 C CA  . ARG A 249 ? 0.7743 0.8095 0.7365 -0.1958 -0.0098 0.0234  249 ARG A CA  
1929 C C   . ARG A 249 ? 0.8534 0.8725 0.7899 -0.2055 -0.0110 0.0093  249 ARG A C   
1930 O O   . ARG A 249 ? 0.8516 0.8535 0.7797 -0.2152 -0.0151 0.0004  249 ARG A O   
1931 C CB  . ARG A 249 ? 0.6956 0.7566 0.6652 -0.1975 -0.0161 0.0407  249 ARG A CB  
1932 C CG  . ARG A 249 ? 0.6905 0.7654 0.6834 -0.1884 -0.0137 0.0552  249 ARG A CG  
1933 C CD  . ARG A 249 ? 0.6688 0.7688 0.6717 -0.1910 -0.0196 0.0733  249 ARG A CD  
1934 N NE  . ARG A 249 ? 0.6971 0.8081 0.7201 -0.1811 -0.0144 0.0869  249 ARG A NE  
1935 C CZ  . ARG A 249 ? 0.6236 0.7415 0.6501 -0.1686 -0.0054 0.0932  249 ARG A CZ  
1936 N NH1 . ARG A 249 ? 0.6785 0.7952 0.6924 -0.1643 -0.0008 0.0881  249 ARG A NH1 
1937 N NH2 . ARG A 249 ? 0.6751 0.7994 0.7167 -0.1603 -0.0001 0.1048  249 ARG A NH2 
1938 N N   . ILE A 250 ? 0.8611 0.8838 0.7831 -0.2030 -0.0065 0.0070  250 ILE A N   
1939 C CA  . ILE A 250 ? 0.8011 0.8073 0.6946 -0.2118 -0.0062 -0.0060 250 ILE A CA  
1940 C C   . ILE A 250 ? 0.8877 0.8674 0.7752 -0.2077 0.0048  -0.0232 250 ILE A C   
1941 O O   . ILE A 250 ? 0.8559 0.8144 0.7234 -0.2172 0.0039  -0.0354 250 ILE A O   
1942 C CB  . ILE A 250 ? 0.8382 0.8545 0.7177 -0.2091 -0.0027 -0.0028 250 ILE A CB  
1943 C CG1 . ILE A 250 ? 0.8302 0.8731 0.7177 -0.2124 -0.0136 0.0158  250 ILE A CG1 
1944 C CG2 . ILE A 250 ? 0.8772 0.8742 0.7232 -0.2181 -0.0013 -0.0163 250 ILE A CG2 
1945 C CD1 . ILE A 250 ? 0.8945 0.9404 0.7725 -0.2292 -0.0300 0.0193  250 ILE A CD1 
1946 N N   . ALA A 251 ? 0.9227 0.9029 0.8277 -0.1936 0.0153  -0.0241 251 ALA A N   
1947 C CA  . ALA A 251 ? 0.8954 0.8535 0.8000 -0.1880 0.0262  -0.0384 251 ALA A CA  
1948 C C   . ALA A 251 ? 0.8258 0.7668 0.7335 -0.1938 0.0219  -0.0434 251 ALA A C   
1949 O O   . ALA A 251 ? 0.8814 0.7983 0.7781 -0.1951 0.0288  -0.0572 251 ALA A O   
1950 C CB  . ALA A 251 ? 0.8488 0.8145 0.7755 -0.1728 0.0353  -0.0359 251 ALA A CB  
1951 N N   . SER A 252 ? 0.8024 0.7542 0.7253 -0.1971 0.0118  -0.0321 252 SER A N   
1952 C CA  . SER A 252 ? 0.8950 0.8303 0.8214 -0.2036 0.0075  -0.0356 252 SER A CA  
1953 C C   . SER A 252 ? 0.9092 0.8272 0.8097 -0.2200 0.0016  -0.0451 252 SER A C   
1954 O O   . SER A 252 ? 0.8415 0.7332 0.7341 -0.2238 0.0049  -0.0568 252 SER A O   
1955 C CB  . SER A 252 ? 0.8807 0.8328 0.8283 -0.2044 -0.0014 -0.0199 252 SER A CB  
1956 O OG  . SER A 252 ? 0.8634 0.8361 0.8084 -0.2131 -0.0114 -0.0088 252 SER A OG  
1957 N N   . ARG A 253 ? 0.9269 0.8582 0.8131 -0.2300 -0.0074 -0.0400 253 ARG A N   
1958 C CA  . ARG A 253 ? 0.8519 0.7666 0.7093 -0.2470 -0.0148 -0.0492 253 ARG A CA  
1959 C C   . ARG A 253 ? 0.9529 0.8389 0.7844 -0.2449 -0.0017 -0.0679 253 ARG A C   
1960 O O   . ARG A 253 ? 1.1354 0.9928 0.9485 -0.2541 -0.0011 -0.0809 253 ARG A O   
1961 C CB  . ARG A 253 ? 1.0022 0.9394 0.8497 -0.2562 -0.0270 -0.0387 253 ARG A CB  
1962 C CG  . ARG A 253 ? 1.0827 1.0049 0.8980 -0.2757 -0.0379 -0.0467 253 ARG A CG  
1963 C CD  . ARG A 253 ? 1.0993 1.0112 0.9200 -0.2898 -0.0491 -0.0473 253 ARG A CD  
1964 N NE  . ARG A 253 ? 1.3312 1.2328 1.1223 -0.3108 -0.0633 -0.0526 253 ARG A NE  
1965 C CZ  . ARG A 253 ? 1.3585 1.2842 1.1534 -0.3235 -0.0815 -0.0389 253 ARG A CZ  
1966 N NH1 . ARG A 253 ? 1.3249 1.2859 1.1527 -0.3167 -0.0860 -0.0188 253 ARG A NH1 
1967 N NH2 . ARG A 253 ? 1.3545 1.2689 1.1206 -0.3410 -0.0944 -0.0445 253 ARG A NH2 
1968 N N   . LEU A 254 ? 1.0192 0.9112 0.8489 -0.2329 0.0099  -0.0695 254 LEU A N   
1969 C CA  . LEU A 254 ? 1.0822 0.9485 0.8909 -0.2291 0.0252  -0.0860 254 LEU A CA  
1970 C C   . LEU A 254 ? 1.0422 0.8873 0.8652 -0.2206 0.0361  -0.0949 254 LEU A C   
1971 O O   . LEU A 254 ? 1.1609 0.9756 0.9639 -0.2234 0.0451  -0.1101 254 LEU A O   
1972 C CB  . LEU A 254 ? 1.0225 0.9027 0.8322 -0.2175 0.0358  -0.0835 254 LEU A CB  
1973 C CG  . LEU A 254 ? 1.1272 1.0252 0.9195 -0.2242 0.0279  -0.0753 254 LEU A CG  
1974 C CD1 . LEU A 254 ? 1.0037 0.9135 0.8007 -0.2115 0.0404  -0.0726 254 LEU A CD1 
1975 C CD2 . LEU A 254 ? 1.1382 1.0154 0.8895 -0.2398 0.0232  -0.0855 254 LEU A CD2 
1976 N N   . ALA A 255 ? 1.0191 0.8786 0.8757 -0.2099 0.0358  -0.0854 255 ALA A N   
1977 C CA  . ALA A 255 ? 1.1153 0.9568 0.9880 -0.2012 0.0446  -0.0915 255 ALA A CA  
1978 C C   . ALA A 255 ? 1.0439 0.8593 0.9046 -0.2133 0.0397  -0.0989 255 ALA A C   
1979 O O   . ALA A 255 ? 1.0994 0.8868 0.9557 -0.2099 0.0506  -0.1108 255 ALA A O   
1980 C CB  . ALA A 255 ? 0.9391 0.8017 0.8465 -0.1895 0.0420  -0.0782 255 ALA A CB  
1981 N N   . LYS A 256 ? 1.0699 0.8936 0.9266 -0.2275 0.0237  -0.0914 256 LYS A N   
1982 C CA  . LYS A 256 ? 1.0713 0.8699 0.9158 -0.2416 0.0177  -0.0983 256 LYS A CA  
1983 C C   . LYS A 256 ? 1.1511 0.9192 0.9563 -0.2520 0.0225  -0.1159 256 LYS A C   
1984 O O   . LYS A 256 ? 1.1147 0.8494 0.9080 -0.2565 0.0279  -0.1283 256 LYS A O   
1985 C CB  . LYS A 256 ? 0.9946 0.8126 0.8461 -0.2554 -0.0011 -0.0850 256 LYS A CB  
1986 C CG  . LYS A 256 ? 1.0624 0.8563 0.9019 -0.2730 -0.0095 -0.0912 256 LYS A CG  
1987 C CD  . LYS A 256 ? 0.9873 0.7581 0.8422 -0.2658 -0.0009 -0.0954 256 LYS A CD  
1988 C CE  . LYS A 256 ? 1.0428 0.7892 0.8874 -0.2841 -0.0095 -0.1004 256 LYS A CE  
1989 N NZ  . LYS A 256 ? 1.0242 0.7451 0.8301 -0.2961 -0.0101 -0.1163 256 LYS A NZ  
1990 N N   . GLU A 257 ? 1.3218 1.0990 1.1047 -0.2557 0.0215  -0.1173 257 GLU A N   
1991 C CA  . GLU A 257 ? 1.3965 1.1438 1.1370 -0.2660 0.0263  -0.1338 257 GLU A CA  
1992 C C   . GLU A 257 ? 1.3742 1.0961 1.1089 -0.2520 0.0495  -0.1478 257 GLU A C   
1993 O O   . GLU A 257 ? 1.4486 1.1331 1.1567 -0.2576 0.0578  -0.1638 257 GLU A O   
1994 C CB  . GLU A 257 ? 1.5063 1.2717 1.2244 -0.2733 0.0182  -0.1293 257 GLU A CB  
1995 C CG  . GLU A 257 ? 1.5233 1.3179 1.2509 -0.2857 -0.0042 -0.1132 257 GLU A CG  
1996 C CD  . GLU A 257 ? 1.5320 1.3496 1.2451 -0.2883 -0.0106 -0.1053 257 GLU A CD  
1997 O OE1 . GLU A 257 ? 1.4810 1.2925 1.1776 -0.2798 0.0030  -0.1118 257 GLU A OE1 
1998 O OE2 . GLU A 257 ? 1.3865 1.2287 1.1061 -0.2984 -0.0287 -0.0915 257 GLU A OE2 
1999 N N   . GLU A 258 ? 1.2855 1.0268 1.0453 -0.2338 0.0605  -0.1418 258 GLU A N   
2000 C CA  . GLU A 258 ? 1.2763 0.9994 1.0349 -0.2199 0.0828  -0.1528 258 GLU A CA  
2001 C C   . GLU A 258 ? 1.2760 0.9869 1.0636 -0.2076 0.0922  -0.1544 258 GLU A C   
2002 O O   . GLU A 258 ? 1.3548 1.0394 1.1366 -0.1998 0.1104  -0.1665 258 GLU A O   
2003 C CB  . GLU A 258 ? 1.2932 1.0435 1.0643 -0.2077 0.0899  -0.1455 258 GLU A CB  
2004 C CG  . GLU A 258 ? 1.3006 1.0632 1.0437 -0.2180 0.0819  -0.1425 258 GLU A CG  
2005 C CD  . GLU A 258 ? 1.3833 1.1723 1.1405 -0.2063 0.0888  -0.1342 258 GLU A CD  
2006 O OE1 . GLU A 258 ? 1.3702 1.1621 1.1524 -0.1910 0.1030  -0.1348 258 GLU A OE1 
2007 O OE2 . GLU A 258 ? 1.3904 1.1974 1.1347 -0.2126 0.0796  -0.1264 258 GLU A OE2 
2008 N N   . GLY A 259 ? 1.1946 0.9233 1.0130 -0.2052 0.0811  -0.1419 259 GLY A N   
2009 C CA  . GLY A 259 ? 1.1455 0.8623 0.9899 -0.1949 0.0873  -0.1417 259 GLY A CA  
2010 C C   . GLY A 259 ? 1.1037 0.8458 0.9874 -0.1767 0.0910  -0.1303 259 GLY A C   
2011 O O   . GLY A 259 ? 1.1724 0.9026 1.0761 -0.1652 0.1002  -0.1318 259 GLY A O   
2012 N N   . TRP A 260 ? 0.9995 0.7748 0.8942 -0.1740 0.0840  -0.1190 260 TRP A N   
2013 C CA  . TRP A 260 ? 0.9573 0.7564 0.8864 -0.1591 0.0848  -0.1080 260 TRP A CA  
2014 C C   . TRP A 260 ? 0.8833 0.7053 0.8261 -0.1628 0.0681  -0.0928 260 TRP A C   
2015 O O   . TRP A 260 ? 0.8108 0.6281 0.7427 -0.1756 0.0573  -0.0907 260 TRP A O   
2016 C CB  . TRP A 260 ? 0.9998 0.8146 0.9304 -0.1513 0.0940  -0.1086 260 TRP A CB  
2017 C CG  . TRP A 260 ? 1.0334 0.8591 0.9390 -0.1616 0.0888  -0.1079 260 TRP A CG  
2018 C CD1 . TRP A 260 ? 1.0498 0.8574 0.9202 -0.1728 0.0913  -0.1182 260 TRP A CD1 
2019 C CD2 . TRP A 260 ? 0.9224 0.7782 0.8351 -0.1613 0.0803  -0.0957 260 TRP A CD2 
2020 N NE1 . TRP A 260 ? 1.0212 0.8478 0.8778 -0.1794 0.0838  -0.1121 260 TRP A NE1 
2021 C CE2 . TRP A 260 ? 0.9983 0.8543 0.8814 -0.1720 0.0778  -0.0982 260 TRP A CE2 
2022 C CE3 . TRP A 260 ? 0.8543 0.7350 0.7938 -0.1530 0.0749  -0.0830 260 TRP A CE3 
2023 C CZ2 . TRP A 260 ? 0.9812 0.8625 0.8636 -0.1737 0.0706  -0.0875 260 TRP A CZ2 
2024 C CZ3 . TRP A 260 ? 0.8926 0.7961 0.8294 -0.1551 0.0687  -0.0737 260 TRP A CZ3 
2025 C CH2 . TRP A 260 ? 0.9137 0.8179 0.8237 -0.1648 0.0670  -0.0756 260 TRP A CH2 
2026 N N   . LEU A 261 ? 0.9341 0.7803 0.9008 -0.1520 0.0664  -0.0821 261 LEU A N   
2027 C CA  . LEU A 261 ? 0.6595 0.5252 0.6399 -0.1529 0.0536  -0.0676 261 LEU A CA  
2028 C C   . LEU A 261 ? 0.8448 0.7380 0.8309 -0.1486 0.0513  -0.0590 261 LEU A C   
2029 O O   . LEU A 261 ? 1.0363 0.9353 1.0291 -0.1397 0.0597  -0.0618 261 LEU A O   
2030 C CB  . LEU A 261 ? 0.6404 0.5019 0.6446 -0.1433 0.0531  -0.0620 261 LEU A CB  
2031 C CG  . LEU A 261 ? 0.6025 0.4360 0.6044 -0.1467 0.0551  -0.0681 261 LEU A CG  
2032 C CD1 . LEU A 261 ? 0.5936 0.4255 0.6201 -0.1354 0.0544  -0.0604 261 LEU A CD1 
2033 C CD2 . LEU A 261 ? 0.9134 0.7411 0.8993 -0.1630 0.0450  -0.0667 261 LEU A CD2 
2034 N N   . ALA A 262 ? 0.7782 0.6877 0.7627 -0.1549 0.0406  -0.0481 262 ALA A N   
2035 C CA  . ALA A 262 ? 0.7330 0.6669 0.7234 -0.1506 0.0381  -0.0382 262 ALA A CA  
2036 C C   . ALA A 262 ? 0.7087 0.6536 0.7128 -0.1492 0.0296  -0.0246 262 ALA A C   
2037 O O   . ALA A 262 ? 0.7569 0.7043 0.7567 -0.1585 0.0218  -0.0187 262 ALA A O   
2038 C CB  . ALA A 262 ? 0.7248 0.6679 0.6961 -0.1594 0.0358  -0.0377 262 ALA A CB  
2039 N N   . GLU A 263 ? 0.6231 0.5744 0.6432 -0.1381 0.0310  -0.0195 263 GLU A N   
2040 C CA  . GLU A 263 ? 0.6090 0.5659 0.6399 -0.1353 0.0248  -0.0076 263 GLU A CA  
2041 C C   . GLU A 263 ? 0.5377 0.5120 0.5734 -0.1283 0.0245  0.0011  263 GLU A C   
2042 O O   . GLU A 263 ? 0.5964 0.5770 0.6310 -0.1243 0.0292  -0.0027 263 GLU A O   
2043 C CB  . GLU A 263 ? 0.5566 0.4991 0.5997 -0.1288 0.0255  -0.0091 263 GLU A CB  
2044 C CG  . GLU A 263 ? 0.6656 0.5870 0.7040 -0.1353 0.0267  -0.0171 263 GLU A CG  
2045 C CD  . GLU A 263 ? 0.6806 0.6009 0.7125 -0.1473 0.0196  -0.0113 263 GLU A CD  
2046 O OE1 . GLU A 263 ? 0.6675 0.6003 0.7055 -0.1469 0.0144  0.0014  263 GLU A OE1 
2047 O OE2 . GLU A 263 ? 0.7700 0.6766 0.7904 -0.1575 0.0194  -0.0194 263 GLU A OE2 
2048 N N   . HIS A 264 ? 0.6355 0.6157 0.6756 -0.1272 0.0198  0.0128  264 HIS A N   
2049 C CA  . HIS A 264 ? 0.6704 0.6629 0.7122 -0.1206 0.0200  0.0215  264 HIS A CA  
2050 C C   . HIS A 264 ? 0.5896 0.5759 0.6399 -0.1114 0.0191  0.0228  264 HIS A C   
2051 O O   . HIS A 264 ? 0.5089 0.4944 0.5604 -0.1086 0.0161  0.0322  264 HIS A O   
2052 C CB  . HIS A 264 ? 0.6200 0.6224 0.6598 -0.1245 0.0171  0.0342  264 HIS A CB  
2053 C CG  . HIS A 264 ? 0.5122 0.5244 0.5509 -0.1177 0.0193  0.0429  264 HIS A CG  
2054 N ND1 . HIS A 264 ? 0.4269 0.4443 0.4664 -0.1169 0.0188  0.0558  264 HIS A ND1 
2055 C CD2 . HIS A 264 ? 0.5307 0.5466 0.5668 -0.1117 0.0228  0.0405  264 HIS A CD2 
2056 C CE1 . HIS A 264 ? 0.5746 0.5967 0.6100 -0.1102 0.0226  0.0603  264 HIS A CE1 
2057 N NE2 . HIS A 264 ? 0.7139 0.7351 0.7471 -0.1074 0.0244  0.0511  264 HIS A NE2 
2058 N N   . MET A 265 ? 0.5849 0.5671 0.6412 -0.1066 0.0218  0.0139  265 MET A N   
2059 C CA  . MET A 265 ? 0.5538 0.5309 0.6206 -0.0984 0.0194  0.0147  265 MET A CA  
2060 C C   . MET A 265 ? 0.6023 0.5870 0.6742 -0.0932 0.0214  0.0108  265 MET A C   
2061 O O   . MET A 265 ? 0.6154 0.6059 0.6846 -0.0955 0.0268  0.0050  265 MET A O   
2062 C CB  . MET A 265 ? 0.5339 0.4970 0.6098 -0.0973 0.0201  0.0088  265 MET A CB  
2063 C CG  . MET A 265 ? 0.5722 0.5249 0.6436 -0.1038 0.0184  0.0112  265 MET A CG  
2064 S SD  . MET A 265 ? 0.4657 0.3980 0.5457 -0.1025 0.0219  0.0022  265 MET A SD  
2065 C CE  . MET A 265 ? 0.6202 0.5412 0.6921 -0.1132 0.0188  0.0060  265 MET A CE  
2066 N N   . LEU A 266 ? 0.6231 0.6072 0.7022 -0.0867 0.0166  0.0146  266 LEU A N   
2067 C CA  . LEU A 266 ? 0.5224 0.5130 0.6103 -0.0824 0.0166  0.0111  266 LEU A CA  
2068 C C   . LEU A 266 ? 0.5419 0.5287 0.6487 -0.0780 0.0177  0.0051  266 LEU A C   
2069 O O   . LEU A 266 ? 0.5369 0.5137 0.6484 -0.0771 0.0178  0.0046  266 LEU A O   
2070 C CB  . LEU A 266 ? 0.4790 0.4711 0.5625 -0.0789 0.0093  0.0187  266 LEU A CB  
2071 C CG  . LEU A 266 ? 0.5010 0.4848 0.5868 -0.0747 0.0014  0.0255  266 LEU A CG  
2072 C CD1 . LEU A 266 ? 0.4298 0.4137 0.5356 -0.0693 -0.0028 0.0227  266 LEU A CD1 
2073 C CD2 . LEU A 266 ? 0.4627 0.4447 0.5327 -0.0735 -0.0037 0.0339  266 LEU A CD2 
2074 N N   . ILE A 267 ? 0.5108 0.5056 0.6301 -0.0752 0.0193  0.0011  267 ILE A N   
2075 C CA  . ILE A 267 ? 0.5017 0.4960 0.6435 -0.0698 0.0215  -0.0034 267 ILE A CA  
2076 C C   . ILE A 267 ? 0.5567 0.5609 0.7131 -0.0658 0.0140  0.0001  267 ILE A C   
2077 O O   . ILE A 267 ? 0.5173 0.5306 0.6721 -0.0684 0.0150  -0.0014 267 ILE A O   
2078 C CB  . ILE A 267 ? 0.5086 0.5033 0.6542 -0.0715 0.0341  -0.0133 267 ILE A CB  
2079 C CG1 . ILE A 267 ? 0.5841 0.5694 0.7095 -0.0781 0.0393  -0.0168 267 ILE A CG1 
2080 C CG2 . ILE A 267 ? 0.5370 0.5287 0.7066 -0.0648 0.0388  -0.0171 267 ILE A CG2 
2081 C CD1 . ILE A 267 ? 0.5829 0.5660 0.7051 -0.0807 0.0515  -0.0267 267 ILE A CD1 
2082 N N   . LEU A 268 ? 0.5017 0.5039 0.6722 -0.0601 0.0060  0.0053  268 LEU A N   
2083 C CA  . LEU A 268 ? 0.5896 0.6015 0.7744 -0.0571 -0.0040 0.0096  268 LEU A CA  
2084 C C   . LEU A 268 ? 0.6094 0.6231 0.8232 -0.0495 -0.0061 0.0113  268 LEU A C   
2085 O O   . LEU A 268 ? 0.5578 0.5608 0.7737 -0.0454 -0.0055 0.0137  268 LEU A O   
2086 C CB  . LEU A 268 ? 0.4589 0.4669 0.6249 -0.0582 -0.0164 0.0180  268 LEU A CB  
2087 C CG  . LEU A 268 ? 0.4149 0.4113 0.5745 -0.0545 -0.0228 0.0258  268 LEU A CG  
2088 C CD1 . LEU A 268 ? 0.4854 0.4844 0.6679 -0.0476 -0.0322 0.0311  268 LEU A CD1 
2089 C CD2 . LEU A 268 ? 0.4898 0.4798 0.6216 -0.0574 -0.0287 0.0324  268 LEU A CD2 
2090 N N   . GLY A 269 ? 0.6206 0.6481 0.8585 -0.0475 -0.0082 0.0108  269 GLY A N   
2091 C CA  . GLY A 269 ? 0.5750 0.6083 0.8454 -0.0395 -0.0116 0.0148  269 GLY A CA  
2092 C C   . GLY A 269 ? 0.4271 0.4676 0.7032 -0.0383 -0.0305 0.0245  269 GLY A C   
2093 O O   . GLY A 269 ? 0.5671 0.6133 0.8312 -0.0444 -0.0386 0.0250  269 GLY A O   
2094 N N   . ILE A 270 ? 0.4513 0.4900 0.7440 -0.0307 -0.0378 0.0322  270 ILE A N   
2095 C CA  . ILE A 270 ? 0.5171 0.5609 0.8133 -0.0291 -0.0574 0.0428  270 ILE A CA  
2096 C C   . ILE A 270 ? 0.4858 0.5429 0.8246 -0.0206 -0.0616 0.0488  270 ILE A C   
2097 O O   . ILE A 270 ? 0.4487 0.5014 0.8066 -0.0128 -0.0505 0.0481  270 ILE A O   
2098 C CB  . ILE A 270 ? 0.4743 0.5010 0.7434 -0.0279 -0.0646 0.0500  270 ILE A CB  
2099 C CG1 . ILE A 270 ? 0.6696 0.7003 0.9384 -0.0265 -0.0855 0.0612  270 ILE A CG1 
2100 C CG2 . ILE A 270 ? 0.5179 0.5324 0.7961 -0.0206 -0.0551 0.0510  270 ILE A CG2 
2101 C CD1 . ILE A 270 ? 0.6570 0.6701 0.8962 -0.0255 -0.0922 0.0692  270 ILE A CD1 
2102 N N   . THR A 271 ? 0.5689 0.6418 0.9228 -0.0223 -0.0778 0.0549  271 THR A N   
2103 C CA  . THR A 271 ? 0.4585 0.5485 0.8568 -0.0148 -0.0846 0.0627  271 THR A CA  
2104 C C   . THR A 271 ? 0.5195 0.6108 0.9151 -0.0130 -0.1081 0.0760  271 THR A C   
2105 O O   . THR A 271 ? 0.4399 0.5273 0.8058 -0.0210 -0.1220 0.0774  271 THR A O   
2106 C CB  . THR A 271 ? 0.5638 0.6759 0.9899 -0.0194 -0.0837 0.0591  271 THR A CB  
2107 O OG1 . THR A 271 ? 0.6041 0.7129 1.0258 -0.0220 -0.0619 0.0469  271 THR A OG1 
2108 C CG2 . THR A 271 ? 0.6087 0.7407 1.0872 -0.0105 -0.0876 0.0679  271 THR A CG2 
2109 N N   . ASN A 272 ? 0.5556 0.6509 0.9808 -0.0021 -0.1121 0.0861  272 ASN A N   
2110 C CA  . ASN A 272 ? 0.4793 0.5753 0.9039 0.0013  -0.1342 0.1005  272 ASN A CA  
2111 C C   . ASN A 272 ? 0.5502 0.6732 1.0145 0.0017  -0.1510 0.1091  272 ASN A C   
2112 O O   . ASN A 272 ? 0.5231 0.6646 1.0232 0.0020  -0.1425 0.1050  272 ASN A O   
2113 C CB  . ASN A 272 ? 0.5469 0.6291 0.9790 0.0135  -0.1286 0.1081  272 ASN A CB  
2114 C CG  . ASN A 272 ? 0.5905 0.6841 1.0726 0.0249  -0.1164 0.1099  272 ASN A CG  
2115 O OD1 . ASN A 272 ? 0.6867 0.7943 1.1926 0.0234  -0.1050 0.1022  272 ASN A OD1 
2116 N ND2 . ASN A 272 ? 0.6122 0.6985 1.1103 0.0368  -0.1173 0.1207  272 ASN A ND2 
2117 N N   . PRO A 273 ? 0.5677 0.6941 1.0270 0.0014  -0.1755 0.1217  273 PRO A N   
2118 C CA  . PRO A 273 ? 0.6304 0.7843 1.1289 0.0006  -0.1949 0.1313  273 PRO A CA  
2119 C C   . PRO A 273 ? 0.5743 0.7466 1.1321 0.0139  -0.1876 0.1393  273 PRO A C   
2120 O O   . PRO A 273 ? 0.5452 0.7449 1.1450 0.0131  -0.1982 0.1456  273 PRO A O   
2121 C CB  . PRO A 273 ? 0.5454 0.6929 1.0182 -0.0014 -0.2220 0.1440  273 PRO A CB  
2122 C CG  . PRO A 273 ? 0.6430 0.7607 1.0563 -0.0062 -0.2157 0.1371  273 PRO A CG  
2123 C CD  . PRO A 273 ? 0.5192 0.6244 0.9340 0.0002  -0.1874 0.1278  273 PRO A CD  
2124 N N   . GLU A 274 ? 0.5995 0.7573 1.1631 0.0260  -0.1694 0.1395  274 GLU A N   
2125 C CA  . GLU A 274 ? 0.5360 0.7073 1.1543 0.0403  -0.1598 0.1472  274 GLU A CA  
2126 C C   . GLU A 274 ? 0.5705 0.7510 1.2163 0.0412  -0.1348 0.1352  274 GLU A C   
2127 O O   . GLU A 274 ? 0.4847 0.6802 1.1807 0.0525  -0.1257 0.1413  274 GLU A O   
2128 C CB  . GLU A 274 ? 0.5337 0.6818 1.1451 0.0531  -0.1504 0.1526  274 GLU A CB  
2129 C CG  . GLU A 274 ? 0.5278 0.6668 1.1162 0.0545  -0.1736 0.1670  274 GLU A CG  
2130 C CD  . GLU A 274 ? 0.5489 0.7147 1.1751 0.0584  -0.1990 0.1851  274 GLU A CD  
2131 O OE1 . GLU A 274 ? 0.5724 0.7623 1.2532 0.0656  -0.1945 0.1897  274 GLU A OE1 
2132 O OE2 . GLU A 274 ? 0.5576 0.7207 1.1587 0.0542  -0.2236 0.1953  274 GLU A OE2 
2133 N N   . GLY A 275 ? 0.6072 0.7787 1.2218 0.0303  -0.1228 0.1193  275 GLY A N   
2134 C CA  . GLY A 275 ? 0.5613 0.7401 1.1966 0.0300  -0.0995 0.1079  275 GLY A CA  
2135 C C   . GLY A 275 ? 0.5830 0.7365 1.1962 0.0337  -0.0722 0.0952  275 GLY A C   
2136 O O   . GLY A 275 ? 0.5816 0.7391 1.2153 0.0366  -0.0507 0.0873  275 GLY A O   
2137 N N   . LYS A 276 ? 0.6938 0.8212 1.2656 0.0331  -0.0724 0.0931  276 LYS A N   
2138 C CA  . LYS A 276 ? 0.6218 0.7240 1.1694 0.0344  -0.0494 0.0811  276 LYS A CA  
2139 C C   . LYS A 276 ? 0.6372 0.7278 1.1361 0.0207  -0.0483 0.0696  276 LYS A C   
2140 O O   . LYS A 276 ? 0.6740 0.7658 1.1480 0.0127  -0.0662 0.0731  276 LYS A O   
2141 C CB  . LYS A 276 ? 0.6834 0.7638 1.2230 0.0437  -0.0487 0.0876  276 LYS A CB  
2142 C CG  . LYS A 276 ? 0.6635 0.7553 1.2471 0.0575  -0.0567 0.1036  276 LYS A CG  
2143 C CD  . LYS A 276 ? 0.6580 0.7638 1.2902 0.0671  -0.0391 0.1024  276 LYS A CD  
2144 C CE  . LYS A 276 ? 0.6938 0.8082 1.3708 0.0829  -0.0444 0.1193  276 LYS A CE  
2145 N NZ  . LYS A 276 ? 0.6988 0.8358 1.3891 0.0812  -0.0750 0.1355  276 LYS A NZ  
2146 N N   . LYS A 277 ? 0.5351 0.6137 1.0200 0.0182  -0.0269 0.0563  277 LYS A N   
2147 C CA  . LYS A 277 ? 0.5802 0.6486 1.0223 0.0063  -0.0236 0.0460  277 LYS A CA  
2148 C C   . LYS A 277 ? 0.5176 0.5610 0.9351 0.0068  -0.0068 0.0373  277 LYS A C   
2149 O O   . LYS A 277 ? 0.5579 0.5945 0.9917 0.0134  0.0107  0.0322  277 LYS A O   
2150 C CB  . LYS A 277 ? 0.4717 0.5557 0.9207 -0.0008 -0.0165 0.0380  277 LYS A CB  
2151 C CG  . LYS A 277 ? 0.4873 0.5623 0.8942 -0.0124 -0.0139 0.0290  277 LYS A CG  
2152 C CD  . LYS A 277 ? 0.4584 0.5473 0.8733 -0.0186 -0.0058 0.0219  277 LYS A CD  
2153 C CE  . LYS A 277 ? 0.5810 0.6610 0.9551 -0.0292 -0.0034 0.0145  277 LYS A CE  
2154 N NZ  . LYS A 277 ? 0.6488 0.7406 1.0296 -0.0351 0.0055  0.0083  277 LYS A NZ  
2155 N N   . LYS A 278 ? 0.5650 0.5942 0.9432 -0.0006 -0.0118 0.0357  278 LYS A N   
2156 C CA  . LYS A 278 ? 0.6117 0.6181 0.9641 -0.0028 0.0011  0.0281  278 LYS A CA  
2157 C C   . LYS A 278 ? 0.6308 0.6345 0.9471 -0.0147 0.0014  0.0214  278 LYS A C   
2158 O O   . LYS A 278 ? 0.4736 0.4876 0.7791 -0.0201 -0.0105 0.0249  278 LYS A O   
2159 C CB  . LYS A 278 ? 0.5689 0.5583 0.9141 0.0019  -0.0053 0.0363  278 LYS A CB  
2160 C CG  . LYS A 278 ? 0.6212 0.6121 1.0022 0.0149  -0.0064 0.0451  278 LYS A CG  
2161 C CD  . LYS A 278 ? 0.6592 0.6314 1.0304 0.0192  -0.0124 0.0540  278 LYS A CD  
2162 C CE  . LYS A 278 ? 0.7266 0.7003 1.1347 0.0332  -0.0136 0.0643  278 LYS A CE  
2163 N NZ  . LYS A 278 ? 0.6123 0.5805 1.0443 0.0403  0.0073  0.0562  278 LYS A NZ  
2164 N N   . TYR A 279 ? 0.6026 0.5916 0.8999 -0.0188 0.0152  0.0120  279 TYR A N   
2165 C CA  . TYR A 279 ? 0.5811 0.5676 0.8463 -0.0294 0.0169  0.0063  279 TYR A CA  
2166 C C   . TYR A 279 ? 0.5440 0.5135 0.7837 -0.0332 0.0139  0.0089  279 TYR A C   
2167 O O   . TYR A 279 ? 0.6785 0.6320 0.9204 -0.0300 0.0193  0.0080  279 TYR A O   
2168 C CB  . TYR A 279 ? 0.5804 0.5652 0.8417 -0.0330 0.0337  -0.0058 279 TYR A CB  
2169 C CG  . TYR A 279 ? 0.5047 0.5077 0.7861 -0.0319 0.0376  -0.0082 279 TYR A CG  
2170 C CD1 . TYR A 279 ? 0.5141 0.5291 0.7836 -0.0391 0.0334  -0.0088 279 TYR A CD1 
2171 C CD2 . TYR A 279 ? 0.5507 0.5587 0.8643 -0.0236 0.0466  -0.0094 279 TYR A CD2 
2172 C CE1 . TYR A 279 ? 0.4342 0.4651 0.7228 -0.0391 0.0373  -0.0107 279 TYR A CE1 
2173 C CE2 . TYR A 279 ? 0.5340 0.5599 0.8688 -0.0232 0.0509  -0.0107 279 TYR A CE2 
2174 C CZ  . TYR A 279 ? 0.5014 0.5385 0.8232 -0.0315 0.0458  -0.0115 279 TYR A CZ  
2175 O OH  . TYR A 279 ? 0.5846 0.6387 0.9281 -0.0321 0.0503  -0.0126 279 TYR A OH  
2176 N N   . LEU A 280 ? 0.4859 0.4582 0.7022 -0.0399 0.0061  0.0122  280 LEU A N   
2177 C CA  . LEU A 280 ? 0.5270 0.4863 0.7208 -0.0441 0.0031  0.0163  280 LEU A CA  
2178 C C   . LEU A 280 ? 0.5115 0.4719 0.6812 -0.0536 0.0077  0.0114  280 LEU A C   
2179 O O   . LEU A 280 ? 0.5011 0.4727 0.6689 -0.0566 0.0109  0.0067  280 LEU A O   
2180 C CB  . LEU A 280 ? 0.5122 0.4724 0.7007 -0.0415 -0.0111 0.0284  280 LEU A CB  
2181 C CG  . LEU A 280 ? 0.6220 0.5833 0.8333 -0.0320 -0.0193 0.0361  280 LEU A CG  
2182 C CD1 . LEU A 280 ? 0.5693 0.5292 0.7676 -0.0311 -0.0336 0.0480  280 LEU A CD1 
2183 C CD2 . LEU A 280 ? 0.6455 0.5918 0.8698 -0.0267 -0.0118 0.0353  280 LEU A CD2 
2184 N N   . ALA A 281 ? 0.5744 0.5235 0.7273 -0.0585 0.0080  0.0137  281 ALA A N   
2185 C CA  . ALA A 281 ? 0.4851 0.4364 0.6171 -0.0674 0.0109  0.0118  281 ALA A CA  
2186 C C   . ALA A 281 ? 0.4404 0.3873 0.5583 -0.0698 0.0044  0.0220  281 ALA A C   
2187 O O   . ALA A 281 ? 0.4348 0.3706 0.5561 -0.0670 0.0013  0.0276  281 ALA A O   
2188 C CB  . ALA A 281 ? 0.4661 0.4083 0.5927 -0.0733 0.0204  0.0023  281 ALA A CB  
2189 N N   . ALA A 282 ? 0.4979 0.4530 0.6007 -0.0743 0.0036  0.0251  282 ALA A N   
2190 C CA  . ALA A 282 ? 0.5192 0.4715 0.6087 -0.0760 -0.0003 0.0356  282 ALA A CA  
2191 C C   . ALA A 282 ? 0.4328 0.3901 0.5101 -0.0840 0.0043  0.0356  282 ALA A C   
2192 O O   . ALA A 282 ? 0.4863 0.4538 0.5594 -0.0862 0.0075  0.0316  282 ALA A O   
2193 C CB  . ALA A 282 ? 0.5139 0.4708 0.5970 -0.0713 -0.0067 0.0423  282 ALA A CB  
2194 N N   . ALA A 283 ? 0.6058 0.5567 0.6788 -0.0886 0.0044  0.0412  283 ALA A N   
2195 C CA  . ALA A 283 ? 0.5228 0.4802 0.5876 -0.0967 0.0072  0.0438  283 ALA A CA  
2196 C C   . ALA A 283 ? 0.4225 0.3826 0.4793 -0.0953 0.0062  0.0568  283 ALA A C   
2197 O O   . ALA A 283 ? 0.3773 0.3294 0.4346 -0.0960 0.0049  0.0645  283 ALA A O   
2198 C CB  . ALA A 283 ? 0.5276 0.4764 0.5951 -0.1047 0.0082  0.0402  283 ALA A CB  
2199 N N   . PHE A 284 ? 0.5928 0.5625 0.6416 -0.0931 0.0080  0.0594  284 PHE A N   
2200 C CA  . PHE A 284 ? 0.6210 0.5921 0.6600 -0.0909 0.0096  0.0711  284 PHE A CA  
2201 C C   . PHE A 284 ? 0.8023 0.7861 0.8384 -0.0954 0.0147  0.0749  284 PHE A C   
2202 O O   . PHE A 284 ? 0.6238 0.6158 0.6606 -0.0976 0.0163  0.0680  284 PHE A O   
2203 C CB  . PHE A 284 ? 0.5932 0.5614 0.6226 -0.0834 0.0078  0.0721  284 PHE A CB  
2204 C CG  . PHE A 284 ? 0.5362 0.4945 0.5696 -0.0784 0.0009  0.0703  284 PHE A CG  
2205 C CD1 . PHE A 284 ? 0.4306 0.3797 0.4713 -0.0787 -0.0015 0.0731  284 PHE A CD1 
2206 C CD2 . PHE A 284 ? 0.5321 0.4903 0.5628 -0.0738 -0.0036 0.0665  284 PHE A CD2 
2207 C CE1 . PHE A 284 ? 0.5769 0.5174 0.6228 -0.0732 -0.0079 0.0730  284 PHE A CE1 
2208 C CE2 . PHE A 284 ? 0.4273 0.3788 0.4641 -0.0692 -0.0113 0.0663  284 PHE A CE2 
2209 C CZ  . PHE A 284 ? 0.4343 0.3772 0.4789 -0.0682 -0.0132 0.0700  284 PHE A CZ  
2210 N N   . PRO A 285 ? 1.0007 0.9869 1.0347 -0.0966 0.0179  0.0868  285 PRO A N   
2211 C CA  . PRO A 285 ? 0.9899 0.9901 1.0239 -0.0994 0.0229  0.0927  285 PRO A CA  
2212 C C   . PRO A 285 ? 1.0552 1.0588 1.0792 -0.0934 0.0271  0.0914  285 PRO A C   
2213 O O   . PRO A 285 ? 1.0931 1.0881 1.1092 -0.0879 0.0256  0.0865  285 PRO A O   
2214 C CB  . PRO A 285 ? 0.9248 0.9252 0.9603 -0.0996 0.0266  0.1072  285 PRO A CB  
2215 C CG  . PRO A 285 ? 1.0023 0.9895 1.0411 -0.1007 0.0222  0.1070  285 PRO A CG  
2216 C CD  . PRO A 285 ? 0.9572 0.9340 0.9908 -0.0954 0.0176  0.0964  285 PRO A CD  
2217 N N   . SER A 286 ? 0.8760 0.8921 0.9009 -0.0949 0.0321  0.0965  286 SER A N   
2218 C CA  . SER A 286 ? 0.7892 0.8072 0.8047 -0.0894 0.0376  0.0961  286 SER A CA  
2219 C C   . SER A 286 ? 0.7827 0.7894 0.7847 -0.0817 0.0425  0.1029  286 SER A C   
2220 O O   . SER A 286 ? 0.7586 0.7632 0.7601 -0.0804 0.0461  0.1137  286 SER A O   
2221 C CB  . SER A 286 ? 0.9088 0.9424 0.9295 -0.0917 0.0425  0.1028  286 SER A CB  
2222 O OG  . SER A 286 ? 0.9160 0.9582 0.9443 -0.0992 0.0374  0.0959  286 SER A OG  
2223 N N   . ALA A 287 ? 0.7711 0.7694 0.7608 -0.0773 0.0428  0.0964  287 ALA A N   
2224 C CA  . ALA A 287 ? 0.8020 0.7860 0.7733 -0.0708 0.0466  0.1007  287 ALA A CA  
2225 C C   . ALA A 287 ? 0.8004 0.7731 0.7678 -0.0698 0.0413  0.1036  287 ALA A C   
2226 O O   . ALA A 287 ? 0.8496 0.8141 0.8060 -0.0660 0.0469  0.1134  287 ALA A O   
2227 C CB  . ALA A 287 ? 0.9129 0.8991 0.8782 -0.0668 0.0589  0.1125  287 ALA A CB  
2228 N N   . CYS A 288 ? 0.7896 0.7612 0.7661 -0.0725 0.0315  0.0957  288 CYS A N   
2229 C CA  . CYS A 288 ? 0.7595 0.7203 0.7341 -0.0712 0.0256  0.0985  288 CYS A CA  
2230 C C   . CYS A 288 ? 0.7331 0.6863 0.7056 -0.0693 0.0156  0.0902  288 CYS A C   
2231 O O   . CYS A 288 ? 0.7242 0.6676 0.6934 -0.0670 0.0100  0.0937  288 CYS A O   
2232 C CB  . CYS A 288 ? 0.7738 0.7402 0.7662 -0.0763 0.0238  0.1006  288 CYS A CB  
2233 S SG  . CYS A 288 ? 0.7895 0.7644 0.7871 -0.0793 0.0330  0.1144  288 CYS A SG  
2234 N N   . GLY A 289 ? 0.6796 0.6378 0.6555 -0.0701 0.0132  0.0804  289 GLY A N   
2235 C CA  . GLY A 289 ? 0.7145 0.6675 0.6902 -0.0684 0.0035  0.0741  289 GLY A CA  
2236 C C   . GLY A 289 ? 0.7058 0.6680 0.7028 -0.0706 -0.0008 0.0640  289 GLY A C   
2237 O O   . GLY A 289 ? 0.6980 0.6579 0.7027 -0.0688 -0.0094 0.0610  289 GLY A O   
2238 N N   . LYS A 290 ? 0.5207 0.4934 0.5273 -0.0743 0.0053  0.0594  290 LYS A N   
2239 C CA  . LYS A 290 ? 0.5166 0.4963 0.5410 -0.0761 0.0036  0.0496  290 LYS A CA  
2240 C C   . LYS A 290 ? 0.7660 0.7490 0.7914 -0.0756 0.0019  0.0431  290 LYS A C   
2241 O O   . LYS A 290 ? 0.7491 0.7343 0.7887 -0.0746 -0.0034 0.0376  290 LYS A O   
2242 C CB  . LYS A 290 ? 0.6544 0.6423 0.6851 -0.0809 0.0104  0.0469  290 LYS A CB  
2243 C CG  . LYS A 290 ? 0.5971 0.5822 0.6314 -0.0835 0.0105  0.0513  290 LYS A CG  
2244 C CD  . LYS A 290 ? 0.6076 0.5993 0.6483 -0.0896 0.0144  0.0458  290 LYS A CD  
2245 C CE  . LYS A 290 ? 0.6418 0.6436 0.6753 -0.0920 0.0199  0.0479  290 LYS A CE  
2246 N NZ  . LYS A 290 ? 0.6712 0.6747 0.6972 -0.0917 0.0222  0.0599  290 LYS A NZ  
2247 N N   . THR A 291 ? 0.5951 0.5782 0.6069 -0.0763 0.0068  0.0442  291 THR A N   
2248 C CA  . THR A 291 ? 0.7336 0.7190 0.7464 -0.0772 0.0060  0.0379  291 THR A CA  
2249 C C   . THR A 291 ? 0.7076 0.6855 0.7162 -0.0756 -0.0045 0.0379  291 THR A C   
2250 O O   . THR A 291 ? 0.6725 0.6554 0.6949 -0.0768 -0.0101 0.0320  291 THR A O   
2251 C CB  . THR A 291 ? 0.7662 0.7508 0.7644 -0.0781 0.0147  0.0397  291 THR A CB  
2252 O OG1 . THR A 291 ? 0.5757 0.5696 0.5798 -0.0800 0.0226  0.0401  291 THR A OG1 
2253 C CG2 . THR A 291 ? 0.7170 0.7015 0.7154 -0.0799 0.0140  0.0332  291 THR A CG2 
2254 N N   . ASN A 292 ? 0.8201 0.7862 0.8095 -0.0733 -0.0076 0.0449  292 ASN A N   
2255 C CA  . ASN A 292 ? 0.8292 0.7867 0.8103 -0.0725 -0.0192 0.0456  292 ASN A CA  
2256 C C   . ASN A 292 ? 0.8252 0.7880 0.8275 -0.0708 -0.0296 0.0451  292 ASN A C   
2257 O O   . ASN A 292 ? 0.8281 0.7899 0.8328 -0.0711 -0.0412 0.0442  292 ASN A O   
2258 C CB  . ASN A 292 ? 0.7679 0.7095 0.7207 -0.0700 -0.0188 0.0539  292 ASN A CB  
2259 C CG  . ASN A 292 ? 0.8379 0.7715 0.7684 -0.0704 -0.0084 0.0546  292 ASN A CG  
2260 O OD1 . ASN A 292 ? 0.9631 0.8870 0.8774 -0.0723 -0.0114 0.0512  292 ASN A OD1 
2261 N ND2 . ASN A 292 ? 0.9190 0.8561 0.8492 -0.0690 0.0037  0.0593  292 ASN A ND2 
2262 N N   . LEU A 293 ? 0.8084 0.7763 0.8265 -0.0693 -0.0260 0.0459  293 LEU A N   
2263 C CA  . LEU A 293 ? 0.6453 0.6161 0.6841 -0.0664 -0.0339 0.0461  293 LEU A CA  
2264 C C   . LEU A 293 ? 0.6741 0.6577 0.7391 -0.0674 -0.0335 0.0377  293 LEU A C   
2265 O O   . LEU A 293 ? 0.5743 0.5622 0.6565 -0.0652 -0.0426 0.0377  293 LEU A O   
2266 C CB  . LEU A 293 ? 0.5305 0.4977 0.5736 -0.0647 -0.0292 0.0501  293 LEU A CB  
2267 C CG  . LEU A 293 ? 0.6222 0.5888 0.6855 -0.0607 -0.0352 0.0512  293 LEU A CG  
2268 C CD1 . LEU A 293 ? 0.6909 0.6504 0.7474 -0.0569 -0.0479 0.0590  293 LEU A CD1 
2269 C CD2 . LEU A 293 ? 0.5051 0.4664 0.5716 -0.0610 -0.0284 0.0533  293 LEU A CD2 
2270 N N   . ALA A 294 ? 0.6404 0.6306 0.7093 -0.0704 -0.0228 0.0316  294 ALA A N   
2271 C CA  . ALA A 294 ? 0.5839 0.5853 0.6762 -0.0712 -0.0197 0.0238  294 ALA A CA  
2272 C C   . ALA A 294 ? 0.5935 0.6004 0.6902 -0.0735 -0.0254 0.0212  294 ALA A C   
2273 O O   . ALA A 294 ? 0.6656 0.6827 0.7868 -0.0733 -0.0258 0.0170  294 ALA A O   
2274 C CB  . ALA A 294 ? 0.5713 0.5764 0.6620 -0.0743 -0.0066 0.0187  294 ALA A CB  
2275 N N   . MET A 295 ? 0.6340 0.6336 0.7081 -0.0760 -0.0290 0.0237  295 MET A N   
2276 C CA  . MET A 295 ? 0.6839 0.6853 0.7582 -0.0798 -0.0359 0.0211  295 MET A CA  
2277 C C   . MET A 295 ? 0.6804 0.6726 0.7407 -0.0794 -0.0508 0.0266  295 MET A C   
2278 O O   . MET A 295 ? 0.7217 0.7055 0.7622 -0.0834 -0.0554 0.0261  295 MET A O   
2279 C CB  . MET A 295 ? 0.6405 0.6378 0.6969 -0.0839 -0.0267 0.0180  295 MET A CB  
2280 C CG  . MET A 295 ? 0.6952 0.7007 0.7611 -0.0846 -0.0126 0.0138  295 MET A CG  
2281 S SD  . MET A 295 ? 0.5240 0.5237 0.5685 -0.0881 -0.0019 0.0126  295 MET A SD  
2282 C CE  . MET A 295 ? 0.5614 0.5722 0.6186 -0.0882 0.0119  0.0092  295 MET A CE  
2283 N N   . MET A 296 ? 0.6474 0.6394 0.7162 -0.0747 -0.0584 0.0320  296 MET A N   
2284 C CA  . MET A 296 ? 0.7031 0.6851 0.7556 -0.0738 -0.0726 0.0387  296 MET A CA  
2285 C C   . MET A 296 ? 0.6469 0.6365 0.7134 -0.0771 -0.0880 0.0378  296 MET A C   
2286 O O   . MET A 296 ? 0.5533 0.5591 0.6537 -0.0768 -0.0893 0.0350  296 MET A O   
2287 C CB  . MET A 296 ? 0.6898 0.6688 0.7479 -0.0673 -0.0752 0.0459  296 MET A CB  
2288 C CG  . MET A 296 ? 0.6345 0.6030 0.6757 -0.0656 -0.0903 0.0543  296 MET A CG  
2289 S SD  . MET A 296 ? 0.6110 0.5753 0.6613 -0.0577 -0.0926 0.0637  296 MET A SD  
2290 C CE  . MET A 296 ? 0.6095 0.5929 0.7082 -0.0542 -0.0937 0.0603  296 MET A CE  
2291 N N   . ASN A 297 ? 0.6362 0.6135 0.6758 -0.0807 -0.0996 0.0403  297 ASN A N   
2292 C CA  . ASN A 297 ? 0.6509 0.6334 0.6991 -0.0848 -0.1187 0.0415  297 ASN A CA  
2293 C C   . ASN A 297 ? 0.6372 0.6134 0.6776 -0.0800 -0.1327 0.0514  297 ASN A C   
2294 O O   . ASN A 297 ? 0.6195 0.5771 0.6224 -0.0814 -0.1387 0.0551  297 ASN A O   
2295 C CB  . ASN A 297 ? 0.7012 0.6716 0.7213 -0.0936 -0.1233 0.0367  297 ASN A CB  
2296 C CG  . ASN A 297 ? 0.6298 0.6088 0.6641 -0.1005 -0.1435 0.0365  297 ASN A CG  
2297 O OD1 . ASN A 297 ? 0.6328 0.6333 0.7084 -0.0996 -0.1488 0.0374  297 ASN A OD1 
2298 N ND2 . ASN A 297 ? 0.7585 0.7204 0.7585 -0.1076 -0.1548 0.0357  297 ASN A ND2 
2299 N N   . PRO A 298 ? 0.5690 0.5586 0.6424 -0.0739 -0.1373 0.0565  298 PRO A N   
2300 C CA  . PRO A 298 ? 0.6394 0.6218 0.7054 -0.0681 -0.1487 0.0672  298 PRO A CA  
2301 C C   . PRO A 298 ? 0.5714 0.5488 0.6202 -0.0728 -0.1710 0.0721  298 PRO A C   
2302 O O   . PRO A 298 ? 0.7370 0.7223 0.7929 -0.0805 -0.1809 0.0677  298 PRO A O   
2303 C CB  . PRO A 298 ? 0.6037 0.6034 0.7150 -0.0608 -0.1480 0.0704  298 PRO A CB  
2304 C CG  . PRO A 298 ? 0.5913 0.6097 0.7345 -0.0647 -0.1438 0.0622  298 PRO A CG  
2305 C CD  . PRO A 298 ? 0.5280 0.5385 0.6465 -0.0714 -0.1311 0.0529  298 PRO A CD  
2306 N N   . THR A 299 ? 0.6631 0.6261 0.6875 -0.0689 -0.1793 0.0817  299 THR A N   
2307 C CA  . THR A 299 ? 0.5463 0.5014 0.5482 -0.0729 -0.2017 0.0878  299 THR A CA  
2308 C C   . THR A 299 ? 0.6855 0.6553 0.7189 -0.0676 -0.2197 0.0987  299 THR A C   
2309 O O   . THR A 299 ? 0.7530 0.7167 0.7682 -0.0699 -0.2404 0.1064  299 THR A O   
2310 C CB  . THR A 299 ? 0.6341 0.5611 0.5828 -0.0721 -0.1992 0.0923  299 THR A CB  
2311 O OG1 . THR A 299 ? 0.7175 0.6404 0.6703 -0.0625 -0.1906 0.1007  299 THR A OG1 
2312 C CG2 . THR A 299 ? 0.7826 0.6952 0.7014 -0.0767 -0.1816 0.0826  299 THR A CG2 
2313 N N   . LEU A 300 ? 0.6272 0.6153 0.7065 -0.0603 -0.2121 0.1000  300 LEU A N   
2314 C CA  . LEU A 300 ? 0.5920 0.5955 0.7069 -0.0537 -0.2270 0.1110  300 LEU A CA  
2315 C C   . LEU A 300 ? 0.6453 0.6755 0.8059 -0.0571 -0.2339 0.1076  300 LEU A C   
2316 O O   . LEU A 300 ? 0.5206 0.5607 0.7030 -0.0581 -0.2171 0.0978  300 LEU A O   
2317 C CB  . LEU A 300 ? 0.5416 0.5443 0.6770 -0.0420 -0.2130 0.1159  300 LEU A CB  
2318 C CG  . LEU A 300 ? 0.6781 0.6567 0.7765 -0.0376 -0.2072 0.1224  300 LEU A CG  
2319 C CD1 . LEU A 300 ? 0.7474 0.7264 0.8721 -0.0270 -0.1954 0.1272  300 LEU A CD1 
2320 C CD2 . LEU A 300 ? 0.6407 0.6079 0.7089 -0.0385 -0.2289 0.1338  300 LEU A CD2 
2321 N N   . PRO A 301 ? 0.4943 0.5375 0.6710 -0.0592 -0.2580 0.1162  301 PRO A N   
2322 C CA  . PRO A 301 ? 0.4809 0.5523 0.7062 -0.0627 -0.2646 0.1145  301 PRO A CA  
2323 C C   . PRO A 301 ? 0.4575 0.5474 0.7362 -0.0507 -0.2520 0.1180  301 PRO A C   
2324 O O   . PRO A 301 ? 0.6601 0.7452 0.9453 -0.0396 -0.2503 0.1272  301 PRO A O   
2325 C CB  . PRO A 301 ? 0.7259 0.8046 0.9506 -0.0679 -0.2961 0.1252  301 PRO A CB  
2326 C CG  . PRO A 301 ? 0.6777 0.7378 0.8721 -0.0604 -0.3035 0.1367  301 PRO A CG  
2327 C CD  . PRO A 301 ? 0.6665 0.6997 0.8178 -0.0589 -0.2810 0.1287  301 PRO A CD  
2328 N N   . GLY A 302 ? 0.5991 0.7083 0.9150 -0.0530 -0.2419 0.1105  302 GLY A N   
2329 C CA  . GLY A 302 ? 0.6367 0.7623 1.0026 -0.0421 -0.2274 0.1123  302 GLY A CA  
2330 C C   . GLY A 302 ? 0.6429 0.7553 1.0004 -0.0368 -0.1988 0.1025  302 GLY A C   
2331 O O   . GLY A 302 ? 0.6565 0.7785 1.0511 -0.0279 -0.1844 0.1023  302 GLY A O   
2332 N N   . TRP A 303 ? 0.5186 0.6091 0.8289 -0.0420 -0.1901 0.0946  303 TRP A N   
2333 C CA  . TRP A 303 ? 0.5410 0.6195 0.8406 -0.0390 -0.1652 0.0856  303 TRP A CA  
2334 C C   . TRP A 303 ? 0.5368 0.6169 0.8263 -0.0483 -0.1535 0.0727  303 TRP A C   
2335 O O   . TRP A 303 ? 0.5140 0.5907 0.7797 -0.0579 -0.1631 0.0700  303 TRP A O   
2336 C CB  . TRP A 303 ? 0.6103 0.6640 0.8674 -0.0369 -0.1627 0.0884  303 TRP A CB  
2337 C CG  . TRP A 303 ? 0.5617 0.6108 0.8282 -0.0267 -0.1695 0.1008  303 TRP A CG  
2338 C CD1 . TRP A 303 ? 0.6076 0.6550 0.8664 -0.0252 -0.1909 0.1133  303 TRP A CD1 
2339 C CD2 . TRP A 303 ? 0.5769 0.6204 0.8606 -0.0169 -0.1549 0.1022  303 TRP A CD2 
2340 N NE1 . TRP A 303 ? 0.5621 0.6042 0.8340 -0.0142 -0.1900 0.1233  303 TRP A NE1 
2341 C CE2 . TRP A 303 ? 0.6503 0.6892 0.9379 -0.0091 -0.1677 0.1163  303 TRP A CE2 
2342 C CE3 . TRP A 303 ? 0.5709 0.6114 0.8652 -0.0145 -0.1326 0.0928  303 TRP A CE3 
2343 C CZ2 . TRP A 303 ? 0.6320 0.6625 0.9351 0.0013  -0.1579 0.1211  303 TRP A CZ2 
2344 C CZ3 . TRP A 303 ? 0.5713 0.6026 0.8790 -0.0051 -0.1235 0.0967  303 TRP A CZ3 
2345 C CH2 . TRP A 303 ? 0.4920 0.5182 0.8048 0.0028  -0.1356 0.1106  303 TRP A CH2 
2346 N N   . LYS A 304 ? 0.5459 0.6293 0.8518 -0.0455 -0.1325 0.0648  304 LYS A N   
2347 C CA  . LYS A 304 ? 0.5848 0.6703 0.8842 -0.0530 -0.1194 0.0535  304 LYS A CA  
2348 C C   . LYS A 304 ? 0.5310 0.6031 0.8131 -0.0505 -0.0983 0.0464  304 LYS A C   
2349 O O   . LYS A 304 ? 0.4749 0.5471 0.7759 -0.0428 -0.0874 0.0464  304 LYS A O   
2350 C CB  . LYS A 304 ? 0.4502 0.5585 0.7942 -0.0536 -0.1161 0.0512  304 LYS A CB  
2351 C CG  . LYS A 304 ? 0.5327 0.6436 0.8710 -0.0619 -0.1036 0.0407  304 LYS A CG  
2352 C CD  . LYS A 304 ? 0.7720 0.9060 1.1568 -0.0623 -0.0997 0.0399  304 LYS A CD  
2353 C CE  . LYS A 304 ? 0.8540 0.9893 1.2323 -0.0706 -0.0868 0.0303  304 LYS A CE  
2354 N NZ  . LYS A 304 ? 0.7849 0.9427 1.2097 -0.0710 -0.0810 0.0301  304 LYS A NZ  
2355 N N   . VAL A 305 ? 0.6417 0.7019 0.8882 -0.0571 -0.0927 0.0408  305 VAL A N   
2356 C CA  . VAL A 305 ? 0.5852 0.6340 0.8131 -0.0564 -0.0750 0.0351  305 VAL A CA  
2357 C C   . VAL A 305 ? 0.6138 0.6681 0.8409 -0.0625 -0.0627 0.0259  305 VAL A C   
2358 O O   . VAL A 305 ? 0.6725 0.7265 0.8851 -0.0695 -0.0675 0.0241  305 VAL A O   
2359 C CB  . VAL A 305 ? 0.6427 0.6732 0.8305 -0.0577 -0.0776 0.0387  305 VAL A CB  
2360 C CG1 . VAL A 305 ? 0.6395 0.6615 0.8119 -0.0582 -0.0606 0.0336  305 VAL A CG1 
2361 C CG2 . VAL A 305 ? 0.6138 0.6378 0.8015 -0.0515 -0.0889 0.0487  305 VAL A CG2 
2362 N N   . GLU A 306 ? 0.6800 0.7371 0.9207 -0.0599 -0.0464 0.0201  306 GLU A N   
2363 C CA  . GLU A 306 ? 0.7142 0.7754 0.9532 -0.0649 -0.0330 0.0121  306 GLU A CA  
2364 C C   . GLU A 306 ? 0.6827 0.7319 0.8968 -0.0655 -0.0200 0.0082  306 GLU A C   
2365 O O   . GLU A 306 ? 0.7488 0.7889 0.9567 -0.0615 -0.0185 0.0102  306 GLU A O   
2366 C CB  . GLU A 306 ? 0.7050 0.7808 0.9814 -0.0622 -0.0245 0.0087  306 GLU A CB  
2367 C CG  . GLU A 306 ? 0.6986 0.7903 1.0046 -0.0630 -0.0376 0.0133  306 GLU A CG  
2368 C CD  . GLU A 306 ? 0.8154 0.9227 1.1632 -0.0586 -0.0278 0.0118  306 GLU A CD  
2369 O OE1 . GLU A 306 ? 0.8684 0.9709 1.2218 -0.0527 -0.0125 0.0082  306 GLU A OE1 
2370 O OE2 . GLU A 306 ? 0.8122 0.9359 1.1871 -0.0615 -0.0350 0.0144  306 GLU A OE2 
2371 N N   . CYS A 307 ? 0.5717 0.6211 0.7720 -0.0709 -0.0110 0.0032  307 CYS A N   
2372 C CA  . CYS A 307 ? 0.5872 0.6273 0.7623 -0.0728 -0.0011 0.0009  307 CYS A CA  
2373 C C   . CYS A 307 ? 0.6310 0.6743 0.8145 -0.0730 0.0143  -0.0061 307 CYS A C   
2374 O O   . CYS A 307 ? 0.5612 0.6137 0.7607 -0.0743 0.0199  -0.0098 307 CYS A O   
2375 C CB  . CYS A 307 ? 0.6578 0.6938 0.8073 -0.0780 -0.0021 0.0021  307 CYS A CB  
2376 S SG  . CYS A 307 ? 0.6818 0.7098 0.8038 -0.0801 0.0087  0.0020  307 CYS A SG  
2377 N N   . VAL A 308 ? 0.5469 0.5818 0.7183 -0.0724 0.0210  -0.0078 308 VAL A N   
2378 C CA  . VAL A 308 ? 0.5905 0.6244 0.7605 -0.0739 0.0352  -0.0147 308 VAL A CA  
2379 C C   . VAL A 308 ? 0.6309 0.6594 0.7729 -0.0790 0.0392  -0.0147 308 VAL A C   
2380 O O   . VAL A 308 ? 0.6010 0.6315 0.7360 -0.0822 0.0488  -0.0188 308 VAL A O   
2381 C CB  . VAL A 308 ? 0.6301 0.6576 0.8129 -0.0692 0.0404  -0.0181 308 VAL A CB  
2382 C CG1 . VAL A 308 ? 0.5122 0.5365 0.6906 -0.0711 0.0557  -0.0264 308 VAL A CG1 
2383 C CG2 . VAL A 308 ? 0.5030 0.5376 0.7171 -0.0628 0.0359  -0.0159 308 VAL A CG2 
2384 N N   . GLY A 309 ? 0.6053 0.6275 0.7318 -0.0796 0.0320  -0.0090 309 GLY A N   
2385 C CA  . GLY A 309 ? 0.4532 0.4728 0.5569 -0.0841 0.0346  -0.0066 309 GLY A CA  
2386 C C   . GLY A 309 ? 0.4839 0.4990 0.5759 -0.0835 0.0262  0.0017  309 GLY A C   
2387 O O   . GLY A 309 ? 0.6059 0.6170 0.7047 -0.0800 0.0186  0.0049  309 GLY A O   
2388 N N   . ASP A 310 ? 0.4118 0.4273 0.4862 -0.0866 0.0282  0.0061  310 ASP A N   
2389 C CA  . ASP A 310 ? 0.4563 0.4675 0.5186 -0.0858 0.0229  0.0148  310 ASP A CA  
2390 C C   . ASP A 310 ? 0.5886 0.5997 0.6401 -0.0893 0.0257  0.0194  310 ASP A C   
2391 O O   . ASP A 310 ? 0.6332 0.6421 0.6753 -0.0886 0.0237  0.0278  310 ASP A O   
2392 C CB  . ASP A 310 ? 0.5682 0.5798 0.6208 -0.0848 0.0221  0.0183  310 ASP A CB  
2393 C CG  . ASP A 310 ? 0.5754 0.5917 0.6181 -0.0874 0.0301  0.0192  310 ASP A CG  
2394 O OD1 . ASP A 310 ? 0.4714 0.4929 0.5186 -0.0900 0.0358  0.0141  310 ASP A OD1 
2395 O OD2 . ASP A 310 ? 0.5819 0.5955 0.6112 -0.0864 0.0314  0.0254  310 ASP A OD2 
2396 N N   . ASP A 311 ? 0.5710 0.5842 0.6233 -0.0934 0.0302  0.0146  311 ASP A N   
2397 C CA  . ASP A 311 ? 0.6066 0.6218 0.6497 -0.0983 0.0310  0.0195  311 ASP A CA  
2398 C C   . ASP A 311 ? 0.5489 0.5603 0.5932 -0.1034 0.0322  0.0127  311 ASP A C   
2399 O O   . ASP A 311 ? 0.5822 0.5872 0.6275 -0.1058 0.0286  0.0144  311 ASP A O   
2400 C CB  . ASP A 311 ? 0.5828 0.6067 0.6167 -0.0997 0.0356  0.0235  311 ASP A CB  
2401 C CG  . ASP A 311 ? 0.6718 0.7008 0.6992 -0.1035 0.0348  0.0327  311 ASP A CG  
2402 O OD1 . ASP A 311 ? 0.6958 0.7229 0.7229 -0.1017 0.0321  0.0408  311 ASP A OD1 
2403 O OD2 . ASP A 311 ? 0.7294 0.7647 0.7523 -0.1083 0.0367  0.0325  311 ASP A OD2 
2404 N N   . ILE A 312 ? 0.5829 0.5961 0.6253 -0.1056 0.0378  0.0050  312 ILE A N   
2405 C CA  . ILE A 312 ? 0.6294 0.6362 0.6673 -0.1112 0.0401  -0.0024 312 ILE A CA  
2406 C C   . ILE A 312 ? 0.7929 0.7897 0.8422 -0.1072 0.0430  -0.0114 312 ILE A C   
2407 O O   . ILE A 312 ? 0.6256 0.6250 0.6873 -0.1010 0.0448  -0.0131 312 ILE A O   
2408 C CB  . ILE A 312 ? 0.7389 0.7512 0.7652 -0.1155 0.0456  -0.0054 312 ILE A CB  
2409 C CG1 . ILE A 312 ? 0.6640 0.6879 0.6828 -0.1171 0.0433  0.0054  312 ILE A CG1 
2410 C CG2 . ILE A 312 ? 0.6432 0.6466 0.6585 -0.1229 0.0466  -0.0126 312 ILE A CG2 
2411 C CD1 . ILE A 312 ? 0.5646 0.5907 0.5806 -0.1220 0.0365  0.0136  312 ILE A CD1 
2412 N N   . ALA A 313 ? 0.6808 0.6659 0.7269 -0.1112 0.0436  -0.0169 313 ALA A N   
2413 C CA  . ALA A 313 ? 0.6937 0.6670 0.7508 -0.1068 0.0482  -0.0252 313 ALA A CA  
2414 C C   . ALA A 313 ? 0.6754 0.6343 0.7194 -0.1136 0.0528  -0.0341 313 ALA A C   
2415 O O   . ALA A 313 ? 0.6197 0.5721 0.6545 -0.1207 0.0473  -0.0321 313 ALA A O   
2416 C CB  . ALA A 313 ? 0.6215 0.5899 0.6921 -0.1014 0.0420  -0.0199 313 ALA A CB  
2417 N N   . TRP A 314 ? 0.6485 0.6016 0.6912 -0.1120 0.0631  -0.0440 314 TRP A N   
2418 C CA  . TRP A 314 ? 0.7315 0.6666 0.7584 -0.1179 0.0694  -0.0544 314 TRP A CA  
2419 C C   . TRP A 314 ? 0.8054 0.7253 0.8469 -0.1104 0.0772  -0.0613 314 TRP A C   
2420 O O   . TRP A 314 ? 0.8856 0.8107 0.9441 -0.1017 0.0848  -0.0631 314 TRP A O   
2421 C CB  . TRP A 314 ? 0.8119 0.7490 0.8219 -0.1217 0.0774  -0.0603 314 TRP A CB  
2422 C CG  . TRP A 314 ? 0.6971 0.6473 0.6914 -0.1293 0.0700  -0.0532 314 TRP A CG  
2423 C CD1 . TRP A 314 ? 0.6344 0.5957 0.6311 -0.1320 0.0586  -0.0421 314 TRP A CD1 
2424 C CD2 . TRP A 314 ? 0.6072 0.5606 0.5819 -0.1344 0.0743  -0.0555 314 TRP A CD2 
2425 N NE1 . TRP A 314 ? 0.7427 0.7152 0.7251 -0.1380 0.0556  -0.0370 314 TRP A NE1 
2426 C CE2 . TRP A 314 ? 0.6852 0.6531 0.6533 -0.1397 0.0643  -0.0448 314 TRP A CE2 
2427 C CE3 . TRP A 314 ? 0.7005 0.6457 0.6625 -0.1344 0.0864  -0.0647 314 TRP A CE3 
2428 C CZ2 . TRP A 314 ? 0.6296 0.6045 0.5795 -0.1450 0.0647  -0.0426 314 TRP A CZ2 
2429 C CZ3 . TRP A 314 ? 0.7709 0.7219 0.7121 -0.1402 0.0869  -0.0630 314 TRP A CZ3 
2430 C CH2 . TRP A 314 ? 0.6887 0.6547 0.6244 -0.1454 0.0755  -0.0517 314 TRP A CH2 
2431 N N   . MET A 315 ? 0.8147 0.7163 0.8514 -0.1137 0.0756  -0.0645 315 MET A N   
2432 C CA  . MET A 315 ? 0.8002 0.6853 0.8515 -0.1059 0.0829  -0.0695 315 MET A CA  
2433 C C   . MET A 315 ? 0.8186 0.6771 0.8495 -0.1120 0.0920  -0.0823 315 MET A C   
2434 O O   . MET A 315 ? 0.8685 0.7202 0.8737 -0.1242 0.0879  -0.0856 315 MET A O   
2435 C CB  . MET A 315 ? 0.7659 0.6496 0.8322 -0.1025 0.0732  -0.0605 315 MET A CB  
2436 C CG  . MET A 315 ? 0.5934 0.4996 0.6743 -0.0976 0.0634  -0.0481 315 MET A CG  
2437 S SD  . MET A 315 ? 0.6643 0.5661 0.7580 -0.0938 0.0530  -0.0371 315 MET A SD  
2438 C CE  . MET A 315 ? 0.7507 0.6387 0.8225 -0.1077 0.0486  -0.0378 315 MET A CE  
2439 N N   . LYS A 316 ? 0.9174 0.7602 0.9598 -0.1033 0.1043  -0.0891 316 LYS A N   
2440 C CA  . LYS A 316 ? 1.0091 0.8219 1.0316 -0.1073 0.1159  -0.1024 316 LYS A CA  
2441 C C   . LYS A 316 ? 1.0105 0.8102 1.0561 -0.0936 0.1294  -0.1059 316 LYS A C   
2442 O O   . LYS A 316 ? 1.0104 0.8275 1.0834 -0.0820 0.1336  -0.1008 316 LYS A O   
2443 C CB  . LYS A 316 ? 1.0688 0.8785 1.0641 -0.1140 0.1243  -0.1117 316 LYS A CB  
2444 C CG  . LYS A 316 ? 1.1106 0.8859 1.0787 -0.1193 0.1366  -0.1267 316 LYS A CG  
2445 C CD  . LYS A 316 ? 1.1476 0.9201 1.0862 -0.1256 0.1448  -0.1349 316 LYS A CD  
2446 C CE  . LYS A 316 ? 1.2923 1.0804 1.2501 -0.1134 0.1582  -0.1336 316 LYS A CE  
2447 N NZ  . LYS A 316 ? 1.2485 1.0225 1.2287 -0.0998 0.1753  -0.1385 316 LYS A NZ  
2448 N N   . PHE A 317 ? 1.0747 0.8435 1.1099 -0.0952 0.1362  -0.1141 317 PHE A N   
2449 C CA  . PHE A 317 ? 1.1400 0.8933 1.1968 -0.0815 0.1507  -0.1171 317 PHE A CA  
2450 C C   . PHE A 317 ? 1.1808 0.9299 1.2362 -0.0750 0.1707  -0.1263 317 PHE A C   
2451 O O   . PHE A 317 ? 1.2572 1.0050 1.2851 -0.0834 0.1748  -0.1337 317 PHE A O   
2452 C CB  . PHE A 317 ? 1.1924 0.9097 1.2354 -0.0855 0.1542  -0.1242 317 PHE A CB  
2453 C CG  . PHE A 317 ? 1.1745 0.8941 1.2271 -0.0884 0.1380  -0.1135 317 PHE A CG  
2454 C CD1 . PHE A 317 ? 1.2116 0.9344 1.2430 -0.1040 0.1228  -0.1111 317 PHE A CD1 
2455 C CD2 . PHE A 317 ? 1.0853 0.8044 1.1690 -0.0753 0.1382  -0.1048 317 PHE A CD2 
2456 C CE1 . PHE A 317 ? 1.0888 0.8134 1.1296 -0.1065 0.1097  -0.1006 317 PHE A CE1 
2457 C CE2 . PHE A 317 ? 1.0001 0.7199 1.0907 -0.0778 0.1242  -0.0943 317 PHE A CE2 
2458 C CZ  . PHE A 317 ? 1.0122 0.7344 1.0812 -0.0934 0.1108  -0.0925 317 PHE A CZ  
2459 N N   . ASP A 318 ? 1.1635 0.9112 1.2500 -0.0596 0.1834  -0.1248 318 ASP A N   
2460 C CA  . ASP A 318 ? 1.2732 1.0172 1.3652 -0.0511 0.2050  -0.1320 318 ASP A CA  
2461 C C   . ASP A 318 ? 1.3208 1.0277 1.4096 -0.0441 0.2244  -0.1420 318 ASP A C   
2462 O O   . ASP A 318 ? 1.2555 0.9386 1.3344 -0.0476 0.2202  -0.1442 318 ASP A O   
2463 C CB  . ASP A 318 ? 1.2752 1.0527 1.4108 -0.0384 0.2048  -0.1206 318 ASP A CB  
2464 C CG  . ASP A 318 ? 1.2098 0.9895 1.3852 -0.0244 0.2038  -0.1115 318 ASP A CG  
2465 O OD1 . ASP A 318 ? 1.2417 1.0061 1.4127 -0.0262 0.1950  -0.1093 318 ASP A OD1 
2466 O OD2 . ASP A 318 ? 1.1764 0.9737 1.3887 -0.0118 0.2114  -0.1056 318 ASP A OD2 
2467 N N   . ALA A 319 ? 1.3767 1.0779 1.4746 -0.0340 0.2471  -0.1478 319 ALA A N   
2468 C CA  . ALA A 319 ? 1.4432 1.1068 1.5365 -0.0261 0.2694  -0.1580 319 ALA A CA  
2469 C C   . ALA A 319 ? 1.3926 1.0550 1.5263 -0.0119 0.2687  -0.1484 319 ALA A C   
2470 O O   . ALA A 319 ? 1.3446 0.9715 1.4705 -0.0083 0.2805  -0.1553 319 ALA A O   
2471 C CB  . ALA A 319 ? 1.4911 1.1508 1.5867 -0.0174 0.2957  -0.1651 319 ALA A CB  
2472 N N   . GLN A 320 ? 1.3871 1.0861 1.5623 -0.0040 0.2549  -0.1323 320 GLN A N   
2473 C CA  . GLN A 320 ? 1.2541 0.9561 1.4700 0.0103  0.2526  -0.1209 320 GLN A CA  
2474 C C   . GLN A 320 ? 1.2327 0.9305 1.4419 0.0034  0.2308  -0.1139 320 GLN A C   
2475 O O   . GLN A 320 ? 1.1894 0.8864 1.4279 0.0143  0.2275  -0.1038 320 GLN A O   
2476 C CB  . GLN A 320 ? 1.2483 0.9916 1.5130 0.0221  0.2480  -0.1065 320 GLN A CB  
2477 C CG  . GLN A 320 ? 1.2974 1.0520 1.5704 0.0266  0.2668  -0.1113 320 GLN A CG  
2478 C CD  . GLN A 320 ? 1.3256 1.0475 1.5956 0.0364  0.2974  -0.1223 320 GLN A CD  
2479 O OE1 . GLN A 320 ? 1.2659 0.9653 1.5483 0.0462  0.3053  -0.1215 320 GLN A OE1 
2480 N NE2 . GLN A 320 ? 1.3359 1.0532 1.5881 0.0341  0.3158  -0.1324 320 GLN A NE2 
2481 N N   . GLY A 321 ? 1.2655 0.9613 1.4385 -0.0141 0.2164  -0.1179 321 GLY A N   
2482 C CA  . GLY A 321 ? 1.2403 0.9326 1.4066 -0.0215 0.1971  -0.1110 321 GLY A CA  
2483 C C   . GLY A 321 ? 1.1780 0.9076 1.3611 -0.0230 0.1745  -0.0958 321 GLY A C   
2484 O O   . GLY A 321 ? 1.1819 0.9110 1.3691 -0.0245 0.1603  -0.0867 321 GLY A O   
2485 N N   . ASN A 322 ? 1.2021 0.9620 1.3935 -0.0228 0.1716  -0.0930 322 ASN A N   
2486 C CA  . ASN A 322 ? 1.0988 0.8918 1.3030 -0.0245 0.1514  -0.0799 322 ASN A CA  
2487 C C   . ASN A 322 ? 1.0187 0.8191 1.1895 -0.0407 0.1411  -0.0832 322 ASN A C   
2488 O O   . ASN A 322 ? 1.0919 0.8818 1.2360 -0.0488 0.1502  -0.0947 322 ASN A O   
2489 C CB  . ASN A 322 ? 1.0265 0.8490 1.2648 -0.0139 0.1537  -0.0733 322 ASN A CB  
2490 C CG  . ASN A 322 ? 1.1407 0.9587 1.4159 0.0028  0.1656  -0.0695 322 ASN A CG  
2491 O OD1 . ASN A 322 ? 1.2456 1.0686 1.5449 0.0108  0.1557  -0.0578 322 ASN A OD1 
2492 N ND2 . ASN A 322 ? 1.1484 0.9566 1.4281 0.0086  0.1875  -0.0786 322 ASN A ND2 
2493 N N   . LEU A 323 ? 0.9093 0.7275 1.0814 -0.0449 0.1223  -0.0722 323 LEU A N   
2494 C CA  . LEU A 323 ? 0.8137 0.6422 0.9594 -0.0586 0.1116  -0.0722 323 LEU A CA  
2495 C C   . LEU A 323 ? 0.9464 0.8053 1.1035 -0.0565 0.1076  -0.0672 323 LEU A C   
2496 O O   . LEU A 323 ? 0.8519 0.7300 1.0242 -0.0532 0.0950  -0.0560 323 LEU A O   
2497 C CB  . LEU A 323 ? 0.7832 0.6104 0.9225 -0.0645 0.0959  -0.0632 323 LEU A CB  
2498 C CG  . LEU A 323 ? 0.8157 0.6516 0.9294 -0.0785 0.0857  -0.0621 323 LEU A CG  
2499 C CD1 . LEU A 323 ? 0.8379 0.6552 0.9222 -0.0900 0.0932  -0.0750 323 LEU A CD1 
2500 C CD2 . LEU A 323 ? 0.6577 0.4934 0.7706 -0.0823 0.0722  -0.0514 323 LEU A CD2 
2501 N N   . ARG A 324 ? 0.8170 0.6780 0.9645 -0.0587 0.1189  -0.0758 324 ARG A N   
2502 C CA  . ARG A 324 ? 0.8404 0.7274 0.9976 -0.0575 0.1174  -0.0721 324 ARG A CA  
2503 C C   . ARG A 324 ? 0.7950 0.6924 0.9269 -0.0693 0.1070  -0.0701 324 ARG A C   
2504 O O   . ARG A 324 ? 0.8326 0.7167 0.9362 -0.0793 0.1065  -0.0754 324 ARG A O   
2505 C CB  . ARG A 324 ? 0.9503 0.8349 1.1113 -0.0534 0.1363  -0.0810 324 ARG A CB  
2506 C CG  . ARG A 324 ? 1.0213 0.9004 1.2139 -0.0398 0.1483  -0.0812 324 ARG A CG  
2507 C CD  . ARG A 324 ? 1.2061 1.0858 1.4050 -0.0354 0.1683  -0.0885 324 ARG A CD  
2508 N NE  . ARG A 324 ? 1.2319 1.1105 1.4671 -0.0211 0.1802  -0.0865 324 ARG A NE  
2509 C CZ  . ARG A 324 ? 1.1610 1.0650 1.4363 -0.0124 0.1764  -0.0766 324 ARG A CZ  
2510 N NH1 . ARG A 324 ? 1.0736 1.0037 1.3556 -0.0168 0.1613  -0.0689 324 ARG A NH1 
2511 N NH2 . ARG A 324 ? 1.1923 1.0950 1.5020 0.0010  0.1878  -0.0740 324 ARG A NH2 
2512 N N   . ALA A 325 ? 0.7688 0.6898 0.9116 -0.0681 0.0985  -0.0620 325 ALA A N   
2513 C CA  . ALA A 325 ? 0.6783 0.6104 0.8013 -0.0771 0.0891  -0.0579 325 ALA A CA  
2514 C C   . ALA A 325 ? 0.8556 0.8066 0.9850 -0.0761 0.0920  -0.0568 325 ALA A C   
2515 O O   . ALA A 325 ? 0.6794 0.6398 0.8340 -0.0685 0.0959  -0.0556 325 ALA A O   
2516 C CB  . ALA A 325 ? 0.6070 0.5450 0.7326 -0.0776 0.0734  -0.0470 325 ALA A CB  
2517 N N   . ILE A 326 ? 0.7475 0.7041 0.8549 -0.0842 0.0898  -0.0563 326 ILE A N   
2518 C CA  . ILE A 326 ? 0.6591 0.6317 0.7688 -0.0845 0.0925  -0.0546 326 ILE A CA  
2519 C C   . ILE A 326 ? 0.6428 0.6249 0.7375 -0.0903 0.0816  -0.0469 326 ILE A C   
2520 O O   . ILE A 326 ? 0.6739 0.6504 0.7531 -0.0956 0.0746  -0.0443 326 ILE A O   
2521 C CB  . ILE A 326 ? 0.6686 0.6357 0.7649 -0.0871 0.1073  -0.0633 326 ILE A CB  
2522 C CG1 . ILE A 326 ? 0.7627 0.7202 0.8255 -0.0970 0.1057  -0.0661 326 ILE A CG1 
2523 C CG2 . ILE A 326 ? 0.8329 0.7878 0.9424 -0.0806 0.1209  -0.0713 326 ILE A CG2 
2524 C CD1 . ILE A 326 ? 0.8731 0.8251 0.9167 -0.1006 0.1185  -0.0734 326 ILE A CD1 
2525 N N   . ASN A 327 ? 0.6779 0.6742 0.7785 -0.0894 0.0809  -0.0428 327 ASN A N   
2526 C CA  . ASN A 327 ? 0.6071 0.6114 0.6934 -0.0938 0.0738  -0.0357 327 ASN A CA  
2527 C C   . ASN A 327 ? 0.6296 0.6361 0.6992 -0.0986 0.0820  -0.0383 327 ASN A C   
2528 O O   . ASN A 327 ? 0.7314 0.7443 0.8089 -0.0967 0.0893  -0.0400 327 ASN A O   
2529 C CB  . ASN A 327 ? 0.5999 0.6151 0.7004 -0.0901 0.0672  -0.0293 327 ASN A CB  
2530 C CG  . ASN A 327 ? 0.6458 0.6670 0.7310 -0.0935 0.0629  -0.0224 327 ASN A CG  
2531 O OD1 . ASN A 327 ? 0.6207 0.6397 0.6887 -0.0977 0.0609  -0.0193 327 ASN A OD1 
2532 N ND2 . ASN A 327 ? 0.6155 0.6440 0.7076 -0.0920 0.0618  -0.0197 327 ASN A ND2 
2533 N N   . PRO A 328 ? 0.6574 0.6594 0.7045 -0.1051 0.0807  -0.0381 328 PRO A N   
2534 C CA  . PRO A 328 ? 0.6221 0.6259 0.6514 -0.1096 0.0876  -0.0396 328 PRO A CA  
2535 C C   . PRO A 328 ? 0.6089 0.6252 0.6367 -0.1094 0.0861  -0.0315 328 PRO A C   
2536 O O   . PRO A 328 ? 0.7604 0.7788 0.7744 -0.1124 0.0920  -0.0312 328 PRO A O   
2537 C CB  . PRO A 328 ? 0.7088 0.7050 0.7161 -0.1174 0.0828  -0.0400 328 PRO A CB  
2538 C CG  . PRO A 328 ? 0.6610 0.6581 0.6757 -0.1172 0.0715  -0.0338 328 PRO A CG  
2539 C CD  . PRO A 328 ? 0.6185 0.6140 0.6563 -0.1093 0.0720  -0.0355 328 PRO A CD  
2540 N N   . GLU A 329 ? 0.6406 0.6634 0.6800 -0.1060 0.0790  -0.0248 329 GLU A N   
2541 C CA  . GLU A 329 ? 0.5805 0.6117 0.6170 -0.1055 0.0784  -0.0174 329 GLU A CA  
2542 C C   . GLU A 329 ? 0.5539 0.5888 0.6055 -0.1022 0.0842  -0.0200 329 GLU A C   
2543 O O   . GLU A 329 ? 0.6546 0.6882 0.7228 -0.0996 0.0873  -0.0260 329 GLU A O   
2544 C CB  . GLU A 329 ? 0.6038 0.6372 0.6405 -0.1042 0.0686  -0.0089 329 GLU A CB  
2545 C CG  . GLU A 329 ? 0.5818 0.6152 0.6050 -0.1083 0.0634  -0.0034 329 GLU A CG  
2546 C CD  . GLU A 329 ? 0.5914 0.6271 0.6155 -0.1062 0.0564  0.0061  329 GLU A CD  
2547 O OE1 . GLU A 329 ? 0.7499 0.7822 0.7836 -0.1022 0.0526  0.0059  329 GLU A OE1 
2548 O OE2 . GLU A 329 ? 0.6535 0.6946 0.6685 -0.1082 0.0549  0.0145  329 GLU A OE2 
2549 N N   . ASN A 330 ? 0.5726 0.6122 0.6198 -0.1025 0.0859  -0.0147 330 ASN A N   
2550 C CA  . ASN A 330 ? 0.5996 0.6424 0.6597 -0.1013 0.0914  -0.0165 330 ASN A CA  
2551 C C   . ASN A 330 ? 0.5573 0.6012 0.6208 -0.1000 0.0850  -0.0112 330 ASN A C   
2552 O O   . ASN A 330 ? 0.4354 0.4813 0.5112 -0.1002 0.0873  -0.0130 330 ASN A O   
2553 C CB  . ASN A 330 ? 0.5233 0.5672 0.5732 -0.1036 0.1026  -0.0166 330 ASN A CB  
2554 C CG  . ASN A 330 ? 0.6039 0.6508 0.6705 -0.1032 0.1107  -0.0200 330 ASN A CG  
2555 O OD1 . ASN A 330 ? 0.6861 0.7351 0.7739 -0.1014 0.1098  -0.0245 330 ASN A OD1 
2556 N ND2 . ASN A 330 ? 0.5603 0.6078 0.6191 -0.1050 0.1186  -0.0170 330 ASN A ND2 
2557 N N   . GLY A 331 ? 0.4711 0.5128 0.5237 -0.0993 0.0778  -0.0049 331 GLY A N   
2558 C CA  . GLY A 331 ? 0.4742 0.5131 0.5251 -0.0979 0.0730  -0.0004 331 GLY A CA  
2559 C C   . GLY A 331 ? 0.4384 0.4736 0.4841 -0.0958 0.0638  0.0042  331 GLY A C   
2560 O O   . GLY A 331 ? 0.5837 0.6189 0.6331 -0.0954 0.0597  0.0028  331 GLY A O   
2561 N N   . PHE A 332 ? 0.4224 0.4525 0.4584 -0.0944 0.0616  0.0097  332 PHE A N   
2562 C CA  . PHE A 332 ? 0.4626 0.4878 0.4912 -0.0920 0.0548  0.0151  332 PHE A CA  
2563 C C   . PHE A 332 ? 0.4973 0.5202 0.5101 -0.0904 0.0595  0.0240  332 PHE A C   
2564 O O   . PHE A 332 ? 0.6212 0.6417 0.6278 -0.0902 0.0659  0.0255  332 PHE A O   
2565 C CB  . PHE A 332 ? 0.5240 0.5426 0.5556 -0.0910 0.0469  0.0132  332 PHE A CB  
2566 C CG  . PHE A 332 ? 0.5059 0.5286 0.5569 -0.0915 0.0411  0.0069  332 PHE A CG  
2567 C CD1 . PHE A 332 ? 0.5554 0.5790 0.6129 -0.0898 0.0367  0.0068  332 PHE A CD1 
2568 C CD2 . PHE A 332 ? 0.6301 0.6556 0.6944 -0.0934 0.0405  0.0016  332 PHE A CD2 
2569 C CE1 . PHE A 332 ? 0.5992 0.6261 0.6762 -0.0888 0.0327  0.0019  332 PHE A CE1 
2570 C CE2 . PHE A 332 ? 0.6086 0.6397 0.6944 -0.0929 0.0358  -0.0027 332 PHE A CE2 
2571 C CZ  . PHE A 332 ? 0.6409 0.6725 0.7330 -0.0899 0.0323  -0.0024 332 PHE A CZ  
2572 N N   . PHE A 333 ? 0.6299 0.6535 0.6378 -0.0889 0.0569  0.0305  333 PHE A N   
2573 C CA  . PHE A 333 ? 0.5076 0.5316 0.5047 -0.0865 0.0618  0.0408  333 PHE A CA  
2574 C C   . PHE A 333 ? 0.5773 0.5956 0.5696 -0.0838 0.0575  0.0466  333 PHE A C   
2575 O O   . PHE A 333 ? 0.6986 0.7223 0.6927 -0.0841 0.0564  0.0529  333 PHE A O   
2576 C CB  . PHE A 333 ? 0.5980 0.6333 0.5967 -0.0890 0.0646  0.0449  333 PHE A CB  
2577 C CG  . PHE A 333 ? 0.5431 0.5821 0.5351 -0.0861 0.0703  0.0569  333 PHE A CG  
2578 C CD1 . PHE A 333 ? 0.5943 0.6323 0.5809 -0.0839 0.0784  0.0598  333 PHE A CD1 
2579 C CD2 . PHE A 333 ? 0.7602 0.8041 0.7531 -0.0853 0.0683  0.0662  333 PHE A CD2 
2580 C CE1 . PHE A 333 ? 0.6150 0.6568 0.5977 -0.0800 0.0845  0.0721  333 PHE A CE1 
2581 C CE2 . PHE A 333 ? 0.8333 0.8827 0.8239 -0.0819 0.0742  0.0787  333 PHE A CE2 
2582 C CZ  . PHE A 333 ? 0.7264 0.7748 0.7121 -0.0787 0.0825  0.0818  333 PHE A CZ  
2583 N N   . GLY A 334 ? 0.6357 0.6424 0.6211 -0.0816 0.0549  0.0447  334 GLY A N   
2584 C CA  . GLY A 334 ? 0.7112 0.7100 0.6895 -0.0790 0.0508  0.0494  334 GLY A CA  
2585 C C   . GLY A 334 ? 0.5666 0.5552 0.5277 -0.0744 0.0581  0.0574  334 GLY A C   
2586 O O   . GLY A 334 ? 0.6332 0.6186 0.5874 -0.0731 0.0659  0.0585  334 GLY A O   
2587 N N   . VAL A 335 ? 0.7124 0.6946 0.6661 -0.0717 0.0565  0.0635  335 VAL A N   
2588 C CA  . VAL A 335 ? 0.7751 0.7457 0.7111 -0.0665 0.0653  0.0718  335 VAL A CA  
2589 C C   . VAL A 335 ? 0.7378 0.6899 0.6553 -0.0659 0.0651  0.0657  335 VAL A C   
2590 O O   . VAL A 335 ? 0.6672 0.6148 0.5849 -0.0693 0.0548  0.0573  335 VAL A O   
2591 C CB  . VAL A 335 ? 0.7689 0.7366 0.7015 -0.0639 0.0644  0.0801  335 VAL A CB  
2592 C CG1 . VAL A 335 ? 0.7556 0.7136 0.6727 -0.0576 0.0770  0.0904  335 VAL A CG1 
2593 C CG2 . VAL A 335 ? 0.7928 0.7777 0.7454 -0.0671 0.0612  0.0837  335 VAL A CG2 
2594 N N   . ALA A 336 ? 0.7762 0.7170 0.6778 -0.0617 0.0766  0.0702  336 ALA A N   
2595 C CA  . ALA A 336 ? 0.7167 0.6368 0.5975 -0.0621 0.0777  0.0639  336 ALA A CA  
2596 C C   . ALA A 336 ? 0.7746 0.6740 0.6300 -0.0591 0.0776  0.0665  336 ALA A C   
2597 O O   . ALA A 336 ? 0.7917 0.6790 0.6353 -0.0628 0.0670  0.0592  336 ALA A O   
2598 C CB  . ALA A 336 ? 0.7201 0.6352 0.5952 -0.0592 0.0915  0.0665  336 ALA A CB  
2599 N N   . PRO A 337 ? 0.8032 0.6980 0.6496 -0.0525 0.0892  0.0773  337 PRO A N   
2600 C CA  . PRO A 337 ? 0.7582 0.6306 0.5767 -0.0491 0.0914  0.0801  337 PRO A CA  
2601 C C   . PRO A 337 ? 0.8555 0.7283 0.6743 -0.0527 0.0756  0.0771  337 PRO A C   
2602 O O   . PRO A 337 ? 0.9177 0.8096 0.7602 -0.0546 0.0683  0.0788  337 PRO A O   
2603 C CB  . PRO A 337 ? 0.7187 0.5953 0.5395 -0.0414 0.1067  0.0943  337 PRO A CB  
2604 C CG  . PRO A 337 ? 0.8425 0.7361 0.6837 -0.0401 0.1148  0.0979  337 PRO A CG  
2605 C CD  . PRO A 337 ? 0.8461 0.7562 0.7076 -0.0478 0.1012  0.0883  337 PRO A CD  
2606 N N   . GLY A 338 ? 0.8310 0.6810 0.6216 -0.0537 0.0702  0.0728  338 GLY A N   
2607 C CA  . GLY A 338 ? 0.8237 0.6718 0.6117 -0.0567 0.0542  0.0707  338 GLY A CA  
2608 C C   . GLY A 338 ? 0.8266 0.6814 0.6271 -0.0641 0.0372  0.0599  338 GLY A C   
2609 O O   . GLY A 338 ? 0.9355 0.7863 0.7313 -0.0664 0.0228  0.0583  338 GLY A O   
2610 N N   . THR A 339 ? 0.7880 0.6534 0.6053 -0.0675 0.0387  0.0536  339 THR A N   
2611 C CA  . THR A 339 ? 0.8132 0.6866 0.6459 -0.0744 0.0246  0.0440  339 THR A CA  
2612 C C   . THR A 339 ? 0.9648 0.8156 0.7704 -0.0791 0.0190  0.0373  339 THR A C   
2613 O O   . THR A 339 ? 0.9970 0.8352 0.7885 -0.0798 0.0292  0.0344  339 THR A O   
2614 C CB  . THR A 339 ? 0.7733 0.6654 0.6329 -0.0764 0.0299  0.0404  339 THR A CB  
2615 O OG1 . THR A 339 ? 0.8220 0.7329 0.7030 -0.0732 0.0339  0.0462  339 THR A OG1 
2616 C CG2 . THR A 339 ? 0.7864 0.6878 0.6648 -0.0831 0.0170  0.0314  339 THR A CG2 
2617 N N   . SER A 340 ? 1.0133 0.8581 0.8110 -0.0827 0.0025  0.0350  340 SER A N   
2618 C CA  . SER A 340 ? 1.0452 0.8685 0.8158 -0.0890 -0.0066 0.0285  340 SER A CA  
2619 C C   . SER A 340 ? 1.0780 0.9149 0.8705 -0.0963 -0.0275 0.0233  340 SER A C   
2620 O O   . SER A 340 ? 1.0435 0.9045 0.8705 -0.0950 -0.0327 0.0249  340 SER A O   
2621 C CB  . SER A 340 ? 1.2021 0.9989 0.9313 -0.0860 -0.0063 0.0331  340 SER A CB  
2622 O OG  . SER A 340 ? 1.1679 0.9723 0.9032 -0.0835 -0.0175 0.0392  340 SER A OG  
2623 N N   . VAL A 341 ? 1.2819 1.1027 1.0543 -0.1041 -0.0394 0.0171  341 VAL A N   
2624 C CA  . VAL A 341 ? 1.2247 1.0594 1.0194 -0.1116 -0.0605 0.0134  341 VAL A CA  
2625 C C   . VAL A 341 ? 1.2500 1.0892 1.0455 -0.1085 -0.0752 0.0203  341 VAL A C   
2626 O O   . VAL A 341 ? 1.2480 1.1082 1.0761 -0.1101 -0.0890 0.0210  341 VAL A O   
2627 C CB  . VAL A 341 ? 1.3693 1.1854 1.1422 -0.1226 -0.0703 0.0052  341 VAL A CB  
2628 C CG1 . VAL A 341 ? 1.4532 1.2882 1.2559 -0.1309 -0.0924 0.0024  341 VAL A CG1 
2629 C CG2 . VAL A 341 ? 1.3918 1.1999 1.1613 -0.1249 -0.0537 -0.0008 341 VAL A CG2 
2630 N N   . LYS A 342 ? 1.1702 0.9893 0.9309 -0.1034 -0.0714 0.0261  342 LYS A N   
2631 C CA  . LYS A 342 ? 1.2005 1.0208 0.9582 -0.1002 -0.0848 0.0337  342 LYS A CA  
2632 C C   . LYS A 342 ? 1.0667 0.9082 0.8564 -0.0920 -0.0782 0.0408  342 LYS A C   
2633 O O   . LYS A 342 ? 1.0758 0.9281 0.8821 -0.0901 -0.0913 0.0458  342 LYS A O   
2634 C CB  . LYS A 342 ? 1.2725 1.0614 0.9785 -0.0981 -0.0821 0.0377  342 LYS A CB  
2635 C CG  . LYS A 342 ? 1.3490 1.1274 1.0391 -0.0898 -0.0574 0.0423  342 LYS A CG  
2636 C CD  . LYS A 342 ? 1.5806 1.3266 1.2189 -0.0872 -0.0533 0.0466  342 LYS A CD  
2637 C CE  . LYS A 342 ? 1.6517 1.3900 1.2794 -0.0781 -0.0276 0.0530  342 LYS A CE  
2638 N NZ  . LYS A 342 ? 1.6437 1.4061 1.3057 -0.0714 -0.0225 0.0620  342 LYS A NZ  
2639 N N   . THR A 343 ? 1.1422 0.9893 0.9407 -0.0872 -0.0586 0.0417  343 THR A N   
2640 C CA  . THR A 343 ? 0.9235 0.7881 0.7489 -0.0809 -0.0521 0.0477  343 THR A CA  
2641 C C   . THR A 343 ? 0.9107 0.8011 0.7794 -0.0826 -0.0532 0.0428  343 THR A C   
2642 O O   . THR A 343 ? 0.8706 0.7752 0.7650 -0.0806 -0.0609 0.0452  343 THR A O   
2643 C CB  . THR A 343 ? 0.9225 0.7806 0.7350 -0.0754 -0.0316 0.0527  343 THR A CB  
2644 O OG1 . THR A 343 ? 1.0351 0.8955 0.8511 -0.0773 -0.0197 0.0471  343 THR A OG1 
2645 C CG2 . THR A 343 ? 0.9875 0.8189 0.7570 -0.0726 -0.0277 0.0582  343 THR A CG2 
2646 N N   . ASN A 344 ? 0.8722 0.7672 0.7481 -0.0859 -0.0445 0.0362  344 ASN A N   
2647 C CA  . ASN A 344 ? 0.8365 0.7539 0.7497 -0.0875 -0.0426 0.0314  344 ASN A CA  
2648 C C   . ASN A 344 ? 0.8336 0.7511 0.7503 -0.0949 -0.0467 0.0233  344 ASN A C   
2649 O O   . ASN A 344 ? 0.8869 0.8033 0.8016 -0.0966 -0.0345 0.0196  344 ASN A O   
2650 C CB  . ASN A 344 ? 0.7506 0.6757 0.6718 -0.0838 -0.0253 0.0330  344 ASN A CB  
2651 C CG  . ASN A 344 ? 0.8268 0.7732 0.7835 -0.0845 -0.0234 0.0291  344 ASN A CG  
2652 O OD1 . ASN A 344 ? 0.7082 0.6638 0.6845 -0.0881 -0.0314 0.0239  344 ASN A OD1 
2653 N ND2 . ASN A 344 ? 0.8203 0.7743 0.7851 -0.0814 -0.0127 0.0317  344 ASN A ND2 
2654 N N   . PRO A 345 ? 0.8439 0.7634 0.7672 -0.0998 -0.0641 0.0212  345 PRO A N   
2655 C CA  . PRO A 345 ? 0.7969 0.7169 0.7253 -0.1085 -0.0690 0.0138  345 PRO A CA  
2656 C C   . PRO A 345 ? 0.7640 0.7055 0.7297 -0.1098 -0.0618 0.0095  345 PRO A C   
2657 O O   . PRO A 345 ? 0.8185 0.7582 0.7851 -0.1158 -0.0573 0.0039  345 PRO A O   
2658 C CB  . PRO A 345 ? 0.7526 0.6727 0.6826 -0.1132 -0.0917 0.0148  345 PRO A CB  
2659 C CG  . PRO A 345 ? 0.7685 0.6992 0.7139 -0.1056 -0.0969 0.0223  345 PRO A CG  
2660 C CD  . PRO A 345 ? 0.9106 0.8324 0.8380 -0.0981 -0.0806 0.0265  345 PRO A CD  
2661 N N   . ASN A 346 ? 0.6760 0.6359 0.6710 -0.1045 -0.0597 0.0120  346 ASN A N   
2662 C CA  . ASN A 346 ? 0.5985 0.5768 0.6258 -0.1052 -0.0512 0.0079  346 ASN A CA  
2663 C C   . ASN A 346 ? 0.6231 0.5971 0.6393 -0.1046 -0.0328 0.0058  346 ASN A C   
2664 O O   . ASN A 346 ? 0.7581 0.7406 0.7903 -0.1079 -0.0257 0.0014  346 ASN A O   
2665 C CB  . ASN A 346 ? 0.6823 0.6764 0.7378 -0.0990 -0.0512 0.0106  346 ASN A CB  
2666 C CG  . ASN A 346 ? 0.7778 0.7811 0.8547 -0.0992 -0.0684 0.0130  346 ASN A CG  
2667 O OD1 . ASN A 346 ? 0.6735 0.6852 0.7679 -0.1050 -0.0767 0.0104  346 ASN A OD1 
2668 N ND2 . ASN A 346 ? 0.6663 0.6686 0.7436 -0.0930 -0.0740 0.0190  346 ASN A ND2 
2669 N N   . ALA A 347 ? 0.7725 0.7343 0.7629 -0.1001 -0.0248 0.0100  347 ALA A N   
2670 C CA  . ALA A 347 ? 0.7787 0.7378 0.7600 -0.0988 -0.0082 0.0100  347 ALA A CA  
2671 C C   . ALA A 347 ? 0.7959 0.7412 0.7598 -0.1039 -0.0045 0.0063  347 ALA A C   
2672 O O   . ALA A 347 ? 0.7514 0.6992 0.7189 -0.1047 0.0075  0.0047  347 ALA A O   
2673 C CB  . ALA A 347 ? 0.7326 0.6844 0.6951 -0.0925 -0.0010 0.0171  347 ALA A CB  
2674 N N   . ILE A 348 ? 0.9606 0.8896 0.9038 -0.1077 -0.0146 0.0050  348 ILE A N   
2675 C CA  . ILE A 348 ? 0.7090 0.6204 0.6322 -0.1134 -0.0112 0.0006  348 ILE A CA  
2676 C C   . ILE A 348 ? 0.7673 0.6905 0.7164 -0.1207 -0.0124 -0.0055 348 ILE A C   
2677 O O   . ILE A 348 ? 0.8883 0.8036 0.8312 -0.1238 -0.0021 -0.0083 348 ILE A O   
2678 C CB  . ILE A 348 ? 0.8438 0.7335 0.7368 -0.1172 -0.0236 -0.0005 348 ILE A CB  
2679 C CG1 . ILE A 348 ? 0.8347 0.7118 0.7014 -0.1093 -0.0197 0.0065  348 ILE A CG1 
2680 C CG2 . ILE A 348 ? 1.0139 0.8816 0.8837 -0.1241 -0.0198 -0.0063 348 ILE A CG2 
2681 C CD1 . ILE A 348 ? 0.7347 0.6017 0.5843 -0.1030 0.0005  0.0102  348 ILE A CD1 
2682 N N   . LYS A 349 ? 0.7287 0.6710 0.7085 -0.1232 -0.0241 -0.0068 349 LYS A N   
2683 C CA  . LYS A 349 ? 0.7334 0.6890 0.7417 -0.1300 -0.0246 -0.0115 349 LYS A CA  
2684 C C   . LYS A 349 ? 0.7468 0.7144 0.7715 -0.1266 -0.0072 -0.0115 349 LYS A C   
2685 O O   . LYS A 349 ? 0.7119 0.6841 0.7511 -0.1321 -0.0020 -0.0150 349 LYS A O   
2686 C CB  . LYS A 349 ? 0.7948 0.7692 0.8348 -0.1321 -0.0404 -0.0112 349 LYS A CB  
2687 C CG  . LYS A 349 ? 0.8171 0.7820 0.8428 -0.1362 -0.0606 -0.0102 349 LYS A CG  
2688 C CD  . LYS A 349 ? 0.8445 0.8313 0.9068 -0.1371 -0.0759 -0.0081 349 LYS A CD  
2689 C CE  . LYS A 349 ? 1.0996 1.0779 1.1470 -0.1415 -0.0979 -0.0058 349 LYS A CE  
2690 N NZ  . LYS A 349 ? 1.2511 1.2527 1.3375 -0.1417 -0.1136 -0.0019 349 LYS A NZ  
2691 N N   . THR A 350 ? 0.7733 0.7455 0.7952 -0.1183 0.0015  -0.0073 350 THR A N   
2692 C CA  . THR A 350 ? 0.7281 0.7124 0.7643 -0.1154 0.0158  -0.0070 350 THR A CA  
2693 C C   . THR A 350 ? 0.7024 0.6752 0.7174 -0.1139 0.0303  -0.0049 350 THR A C   
2694 O O   . THR A 350 ? 0.6111 0.5904 0.6359 -0.1148 0.0413  -0.0057 350 THR A O   
2695 C CB  . THR A 350 ? 0.7816 0.7768 0.8267 -0.1085 0.0166  -0.0038 350 THR A CB  
2696 O OG1 . THR A 350 ? 0.6419 0.6461 0.7066 -0.1085 0.0037  -0.0046 350 THR A OG1 
2697 C CG2 . THR A 350 ? 0.6256 0.6329 0.6848 -0.1069 0.0296  -0.0047 350 THR A CG2 
2698 N N   . ILE A 351 ? 0.7776 0.7332 0.7639 -0.1112 0.0315  -0.0015 351 ILE A N   
2699 C CA  . ILE A 351 ? 0.8336 0.7797 0.8018 -0.1074 0.0463  0.0027  351 ILE A CA  
2700 C C   . ILE A 351 ? 0.8225 0.7504 0.7763 -0.1125 0.0506  -0.0006 351 ILE A C   
2701 O O   . ILE A 351 ? 0.6523 0.5647 0.5842 -0.1089 0.0612  0.0031  351 ILE A O   
2702 C CB  . ILE A 351 ? 0.6973 0.6349 0.6445 -0.1004 0.0483  0.0096  351 ILE A CB  
2703 C CG1 . ILE A 351 ? 0.7170 0.6350 0.6414 -0.1021 0.0394  0.0081  351 ILE A CG1 
2704 C CG2 . ILE A 351 ? 0.5836 0.5378 0.5453 -0.0964 0.0445  0.0128  351 ILE A CG2 
2705 C CD1 . ILE A 351 ? 0.6456 0.5530 0.5477 -0.0950 0.0435  0.0153  351 ILE A CD1 
2706 N N   . GLN A 352 ? 0.8359 0.7653 0.8029 -0.1209 0.0428  -0.0071 352 GLN A N   
2707 C CA  . GLN A 352 ? 0.8238 0.7347 0.7782 -0.1279 0.0454  -0.0113 352 GLN A CA  
2708 C C   . GLN A 352 ? 0.8372 0.7549 0.8084 -0.1310 0.0568  -0.0124 352 GLN A C   
2709 O O   . GLN A 352 ? 0.7168 0.6195 0.6809 -0.1378 0.0596  -0.0160 352 GLN A O   
2710 C CB  . GLN A 352 ? 0.8281 0.7335 0.7838 -0.1372 0.0278  -0.0175 352 GLN A CB  
2711 C CG  . GLN A 352 ? 0.9313 0.8201 0.8588 -0.1355 0.0178  -0.0168 352 GLN A CG  
2712 C CD  . GLN A 352 ? 0.9760 0.8593 0.9029 -0.1458 -0.0016 -0.0223 352 GLN A CD  
2713 O OE1 . GLN A 352 ? 0.9084 0.8073 0.8644 -0.1532 -0.0097 -0.0256 352 GLN A OE1 
2714 N NE2 . GLN A 352 ? 1.1492 1.0103 1.0427 -0.1465 -0.0091 -0.0229 352 GLN A NE2 
2715 N N   . LYS A 353 ? 0.8734 0.8114 0.8646 -0.1268 0.0636  -0.0094 353 LYS A N   
2716 C CA  . LYS A 353 ? 0.9178 0.8616 0.9222 -0.1291 0.0756  -0.0093 353 LYS A CA  
2717 C C   . LYS A 353 ? 0.9785 0.9401 0.9930 -0.1223 0.0836  -0.0047 353 LYS A C   
2718 O O   . LYS A 353 ? 0.9415 0.9164 0.9662 -0.1193 0.0768  -0.0047 353 LYS A O   
2719 C CB  . LYS A 353 ? 0.9085 0.8609 0.9387 -0.1387 0.0693  -0.0154 353 LYS A CB  
2720 C CG  . LYS A 353 ? 1.0260 0.9992 1.0823 -0.1388 0.0578  -0.0174 353 LYS A CG  
2721 C CD  . LYS A 353 ? 1.0476 1.0303 1.1324 -0.1483 0.0518  -0.0219 353 LYS A CD  
2722 C CE  . LYS A 353 ? 1.0665 1.0699 1.1795 -0.1471 0.0407  -0.0226 353 LYS A CE  
2723 N NZ  . LYS A 353 ? 1.2335 1.2489 1.3787 -0.1561 0.0346  -0.0255 353 LYS A NZ  
2724 N N   . ASN A 354 ? 0.8142 0.7742 0.8242 -0.1202 0.0978  -0.0005 354 ASN A N   
2725 C CA  . ASN A 354 ? 0.7569 0.7317 0.7723 -0.1149 0.1052  0.0041  354 ASN A CA  
2726 C C   . ASN A 354 ? 0.7100 0.6881 0.7144 -0.1080 0.1013  0.0090  354 ASN A C   
2727 O O   . ASN A 354 ? 0.7135 0.7057 0.7267 -0.1059 0.0993  0.0094  354 ASN A O   
2728 C CB  . ASN A 354 ? 0.7882 0.7803 0.8290 -0.1181 0.1040  -0.0007 354 ASN A CB  
2729 C CG  . ASN A 354 ? 0.7947 0.7859 0.8506 -0.1254 0.1085  -0.0046 354 ASN A CG  
2730 O OD1 . ASN A 354 ? 0.8653 0.8438 0.9111 -0.1276 0.1164  -0.0027 354 ASN A OD1 
2731 N ND2 . ASN A 354 ? 0.7465 0.7511 0.8280 -0.1291 0.1042  -0.0096 354 ASN A ND2 
2732 N N   . THR A 355 ? 0.7012 0.6649 0.6859 -0.1046 0.1011  0.0129  355 THR A N   
2733 C CA  . THR A 355 ? 0.7185 0.6843 0.6937 -0.0984 0.0979  0.0185  355 THR A CA  
2734 C C   . THR A 355 ? 0.6904 0.6483 0.6491 -0.0922 0.1090  0.0281  355 THR A C   
2735 O O   . THR A 355 ? 0.5912 0.5324 0.5379 -0.0921 0.1163  0.0290  355 THR A O   
2736 C CB  . THR A 355 ? 0.6663 0.6228 0.6341 -0.0992 0.0866  0.0152  355 THR A CB  
2737 O OG1 . THR A 355 ? 0.6783 0.6444 0.6647 -0.1042 0.0756  0.0079  355 THR A OG1 
2738 C CG2 . THR A 355 ? 0.6634 0.6219 0.6223 -0.0928 0.0849  0.0219  355 THR A CG2 
2739 N N   . ILE A 356 ? 0.5606 0.5302 0.5198 -0.0872 0.1102  0.0357  356 ILE A N   
2740 C CA  . ILE A 356 ? 0.5640 0.5310 0.5125 -0.0803 0.1198  0.0471  356 ILE A CA  
2741 C C   . ILE A 356 ? 0.5260 0.4902 0.4666 -0.0757 0.1161  0.0519  356 ILE A C   
2742 O O   . ILE A 356 ? 0.6178 0.5945 0.5663 -0.0763 0.1080  0.0519  356 ILE A O   
2743 C CB  . ILE A 356 ? 0.6546 0.6390 0.6109 -0.0789 0.1234  0.0539  356 ILE A CB  
2744 C CG1 . ILE A 356 ? 0.5828 0.5688 0.5452 -0.0817 0.1269  0.0497  356 ILE A CG1 
2745 C CG2 . ILE A 356 ? 0.6702 0.6591 0.6226 -0.0684 0.1243  0.0659  356 ILE A CG2 
2746 C CD1 . ILE A 356 ? 0.6893 0.6924 0.6571 -0.0783 0.1255  0.0554  356 ILE A CD1 
2747 N N   . PHE A 357 ? 0.5899 0.5364 0.5145 -0.0711 0.1232  0.0560  357 PHE A N   
2748 C CA  . PHE A 357 ? 0.6311 0.5724 0.5460 -0.0658 0.1229  0.0618  357 PHE A CA  
2749 C C   . PHE A 357 ? 0.7136 0.6668 0.6337 -0.0560 0.1272  0.0740  357 PHE A C   
2750 O O   . PHE A 357 ? 0.6217 0.5808 0.5471 -0.0523 0.1299  0.0770  357 PHE A O   
2751 C CB  . PHE A 357 ? 0.6693 0.5838 0.5628 -0.0655 0.1251  0.0570  357 PHE A CB  
2752 C CG  . PHE A 357 ? 0.7840 0.6923 0.6769 -0.0738 0.1124  0.0442  357 PHE A CG  
2753 C CD1 . PHE A 357 ? 0.7057 0.6085 0.6019 -0.0804 0.1117  0.0361  357 PHE A CD1 
2754 C CD2 . PHE A 357 ? 0.7926 0.7014 0.6834 -0.0750 0.1009  0.0414  357 PHE A CD2 
2755 C CE1 . PHE A 357 ? 0.6852 0.5851 0.5848 -0.0883 0.0990  0.0257  357 PHE A CE1 
2756 C CE2 . PHE A 357 ? 0.7432 0.6483 0.6357 -0.0822 0.0881  0.0313  357 PHE A CE2 
2757 C CZ  . PHE A 357 ? 0.6781 0.5798 0.5762 -0.0890 0.0868  0.0235  357 PHE A CZ  
2758 N N   . THR A 358 ? 0.7245 0.6834 0.6451 -0.0521 0.1245  0.0801  358 THR A N   
2759 C CA  . THR A 358 ? 0.7430 0.7167 0.6725 -0.0449 0.1240  0.0897  358 THR A CA  
2760 C C   . THR A 358 ? 0.7285 0.6942 0.6506 -0.0392 0.1260  0.0939  358 THR A C   
2761 O O   . THR A 358 ? 0.8957 0.8606 0.8154 -0.0421 0.1223  0.0936  358 THR A O   
2762 C CB  . THR A 358 ? 0.6224 0.6196 0.5674 -0.0495 0.1166  0.0928  358 THR A CB  
2763 O OG1 . THR A 358 ? 0.5470 0.5505 0.4968 -0.0544 0.1158  0.0887  358 THR A OG1 
2764 C CG2 . THR A 358 ? 0.8071 0.8148 0.7593 -0.0441 0.1164  0.1013  358 THR A CG2 
2765 N N   . ASN A 359 ? 0.7943 0.7531 0.7130 -0.0307 0.1330  0.0982  359 ASN A N   
2766 C CA  . ASN A 359 ? 0.8399 0.7920 0.7536 -0.0238 0.1370  0.1030  359 ASN A CA  
2767 C C   . ASN A 359 ? 0.8997 0.8274 0.7910 -0.0243 0.1401  0.0974  359 ASN A C   
2768 O O   . ASN A 359 ? 0.9410 0.8653 0.8272 -0.0216 0.1405  0.1005  359 ASN A O   
2769 C CB  . ASN A 359 ? 0.8675 0.8398 0.7963 -0.0250 0.1306  0.1096  359 ASN A CB  
2770 C CG  . ASN A 359 ? 0.8810 0.8716 0.8277 -0.0221 0.1299  0.1167  359 ASN A CG  
2771 O OD1 . ASN A 359 ? 0.9745 0.9616 0.9223 -0.0154 0.1364  0.1197  359 ASN A OD1 
2772 N ND2 . ASN A 359 ? 0.9831 0.9916 0.9431 -0.0268 0.1224  0.1200  359 ASN A ND2 
2773 N N   . VAL A 360 ? 0.8478 0.7561 0.7234 -0.0286 0.1425  0.0890  360 VAL A N   
2774 C CA  . VAL A 360 ? 0.9329 0.8118 0.7804 -0.0310 0.1453  0.0825  360 VAL A CA  
2775 C C   . VAL A 360 ? 0.9617 0.8148 0.7909 -0.0258 0.1564  0.0793  360 VAL A C   
2776 O O   . VAL A 360 ? 1.0003 0.8572 0.8393 -0.0222 0.1613  0.0808  360 VAL A O   
2777 C CB  . VAL A 360 ? 0.7887 0.6594 0.6272 -0.0437 0.1388  0.0739  360 VAL A CB  
2778 C CG1 . VAL A 360 ? 0.7313 0.6251 0.5883 -0.0483 0.1292  0.0766  360 VAL A CG1 
2779 C CG2 . VAL A 360 ? 0.7904 0.6583 0.6324 -0.0490 0.1411  0.0680  360 VAL A CG2 
2780 N N   . ALA A 361 ? 1.0516 0.8756 0.8513 -0.0256 0.1605  0.0749  361 ALA A N   
2781 C CA  . ALA A 361 ? 1.0577 0.8510 0.8344 -0.0212 0.1723  0.0709  361 ALA A CA  
2782 C C   . ALA A 361 ? 1.0553 0.8280 0.8162 -0.0317 0.1727  0.0611  361 ALA A C   
2783 O O   . ALA A 361 ? 1.1333 0.9064 0.8903 -0.0442 0.1637  0.0557  361 ALA A O   
2784 C CB  . ALA A 361 ? 1.1320 0.8983 0.8781 -0.0184 0.1764  0.0688  361 ALA A CB  
2785 N N   . GLU A 362 ? 1.1616 0.9150 0.9137 -0.0274 0.1839  0.0590  362 GLU A N   
2786 C CA  . GLU A 362 ? 1.2031 0.9342 0.9400 -0.0377 0.1865  0.0502  362 GLU A CA  
2787 C C   . GLU A 362 ? 1.2738 0.9583 0.9681 -0.0395 0.1958  0.0424  362 GLU A C   
2788 O O   . GLU A 362 ? 1.3485 1.0199 1.0347 -0.0274 0.2067  0.0455  362 GLU A O   
2789 C CB  . GLU A 362 ? 1.1284 0.8743 0.8905 -0.0325 0.1919  0.0542  362 GLU A CB  
2790 C CG  . GLU A 362 ? 1.1763 0.8989 0.9252 -0.0430 0.1961  0.0456  362 GLU A CG  
2791 C CD  . GLU A 362 ? 1.3747 1.1096 1.1461 -0.0362 0.2023  0.0506  362 GLU A CD  
2792 O OE1 . GLU A 362 ? 1.4452 1.2065 1.2407 -0.0241 0.2021  0.0608  362 GLU A OE1 
2793 O OE2 . GLU A 362 ? 1.3904 1.1080 1.1547 -0.0440 0.2068  0.0446  362 GLU A OE2 
2794 N N   . THR A 363 ? 1.3042 0.9629 0.9707 -0.0559 0.1909  0.0322  363 THR A N   
2795 C CA  . THR A 363 ? 1.3377 0.9516 0.9620 -0.0605 0.1949  0.0219  363 THR A CA  
2796 C C   . THR A 363 ? 1.3755 0.9671 0.9941 -0.0625 0.2078  0.0183  363 THR A C   
2797 O O   . THR A 363 ? 1.3661 0.9789 1.0144 -0.0637 0.2084  0.0214  363 THR A O   
2798 C CB  . THR A 363 ? 1.2114 0.8206 0.8242 -0.0752 0.1706  0.0085  363 THR A CB  
2799 O OG1 . THR A 363 ? 1.2769 0.9086 0.9197 -0.0863 0.1560  0.0026  363 THR A OG1 
2800 C CG2 . THR A 363 ? 1.2019 0.8298 0.8181 -0.0724 0.1589  0.0128  363 THR A CG2 
2801 N N   . SER A 364 ? 1.3299 0.8758 0.9074 -0.0630 0.2188  0.0117  364 SER A N   
2802 C CA  . SER A 364 ? 1.3671 0.8856 0.9350 -0.0641 0.2337  0.0085  364 SER A CA  
2803 C C   . SER A 364 ? 1.3169 0.8434 0.9018 -0.0804 0.2176  -0.0020 364 SER A C   
2804 O O   . SER A 364 ? 1.2857 0.8133 0.8865 -0.0802 0.2273  0.0005  364 SER A O   
2805 C CB  . SER A 364 ? 1.4795 0.9431 0.9955 -0.0634 0.2470  0.0009  364 SER A CB  
2806 O OG  . SER A 364 ? 1.4063 0.8512 0.8949 -0.0789 0.2268  -0.0143 364 SER A OG  
2807 N N   . ASP A 365 ? 1.2657 0.7984 0.8489 -0.0945 0.1934  -0.0129 365 ASP A N   
2808 C CA  . ASP A 365 ? 1.2119 0.7531 0.8131 -0.1108 0.1775  -0.0226 365 ASP A CA  
2809 C C   . ASP A 365 ? 1.1674 0.7572 0.8182 -0.1103 0.1702  -0.0159 365 ASP A C   
2810 O O   . ASP A 365 ? 1.1470 0.7491 0.8180 -0.1230 0.1572  -0.0227 365 ASP A O   
2811 C CB  . ASP A 365 ? 1.2419 0.7728 0.8248 -0.1259 0.1536  -0.0355 365 ASP A CB  
2812 C CG  . ASP A 365 ? 1.3734 0.9295 0.9627 -0.1220 0.1394  -0.0314 365 ASP A CG  
2813 O OD1 . ASP A 365 ? 1.3972 0.9757 1.0025 -0.1079 0.1491  -0.0193 365 ASP A OD1 
2814 O OD2 . ASP A 365 ? 1.3843 0.9379 0.9633 -0.1332 0.1181  -0.0397 365 ASP A OD2 
2815 N N   . GLY A 366 ? 1.1809 0.7976 0.8510 -0.0965 0.1784  -0.0027 366 GLY A N   
2816 C CA  . GLY A 366 ? 1.1175 0.7767 0.8295 -0.0956 0.1728  0.0035  366 GLY A CA  
2817 C C   . GLY A 366 ? 1.1457 0.8369 0.8768 -0.0978 0.1538  0.0033  366 GLY A C   
2818 O O   . GLY A 366 ? 1.1320 0.8555 0.8960 -0.1000 0.1469  0.0053  366 GLY A O   
2819 N N   . GLY A 367 ? 1.1222 0.8038 0.8324 -0.0971 0.1459  0.0011  367 GLY A N   
2820 C CA  . GLY A 367 ? 1.1102 0.8190 0.8366 -0.0984 0.1286  0.0016  367 GLY A CA  
2821 C C   . GLY A 367 ? 1.0627 0.7900 0.7975 -0.0852 0.1364  0.0142  367 GLY A C   
2822 O O   . GLY A 367 ? 1.0917 0.8167 0.8256 -0.0747 0.1545  0.0238  367 GLY A O   
2823 N N   . VAL A 368 ? 1.0333 0.7798 0.7780 -0.0859 0.1219  0.0148  368 VAL A N   
2824 C CA  . VAL A 368 ? 1.0872 0.8519 0.8410 -0.0756 0.1262  0.0259  368 VAL A CA  
2825 C C   . VAL A 368 ? 1.0349 0.7820 0.7609 -0.0735 0.1223  0.0259  368 VAL A C   
2826 O O   . VAL A 368 ? 1.1246 0.8532 0.8300 -0.0815 0.1104  0.0166  368 VAL A O   
2827 C CB  . VAL A 368 ? 0.9692 0.7715 0.7594 -0.0775 0.1146  0.0279  368 VAL A CB  
2828 C CG1 . VAL A 368 ? 0.8834 0.7013 0.6973 -0.0794 0.1196  0.0282  368 VAL A CG1 
2829 C CG2 . VAL A 368 ? 0.9814 0.7889 0.7760 -0.0866 0.0938  0.0191  368 VAL A CG2 
2830 N N   . TYR A 369 ? 0.9353 0.6886 0.6610 -0.0629 0.1322  0.0372  369 TYR A N   
2831 C CA  . TYR A 369 ? 1.0379 0.7744 0.7369 -0.0595 0.1316  0.0392  369 TYR A CA  
2832 C C   . TYR A 369 ? 1.0582 0.8176 0.7752 -0.0504 0.1367  0.0523  369 TYR A C   
2833 O O   . TYR A 369 ? 1.0710 0.8473 0.8086 -0.0439 0.1484  0.0617  369 TYR A O   
2834 C CB  . TYR A 369 ? 1.0138 0.7102 0.6726 -0.0553 0.1479  0.0380  369 TYR A CB  
2835 C CG  . TYR A 369 ? 1.0934 0.7640 0.7150 -0.0563 0.1430  0.0348  369 TYR A CG  
2836 C CD1 . TYR A 369 ? 1.1373 0.7907 0.7381 -0.0681 0.1252  0.0222  369 TYR A CD1 
2837 C CD2 . TYR A 369 ? 1.0802 0.7439 0.6877 -0.0456 0.1560  0.0451  369 TYR A CD2 
2838 C CE1 . TYR A 369 ? 1.1353 0.7642 0.6990 -0.0695 0.1196  0.0198  369 TYR A CE1 
2839 C CE2 . TYR A 369 ? 1.1780 0.8165 0.7488 -0.0464 0.1523  0.0426  369 TYR A CE2 
2840 C CZ  . TYR A 369 ? 1.2193 0.8397 0.7664 -0.0583 0.1337  0.0299  369 TYR A CZ  
2841 O OH  . TYR A 369 ? 1.2764 0.8708 0.7837 -0.0594 0.1289  0.0278  369 TYR A OH  
2842 N N   . TRP A 370 ? 0.9433 0.7032 0.6525 -0.0507 0.1273  0.0535  370 TRP A N   
2843 C CA  . TRP A 370 ? 0.9767 0.7558 0.7013 -0.0435 0.1313  0.0658  370 TRP A CA  
2844 C C   . TRP A 370 ? 1.0170 0.7805 0.7168 -0.0430 0.1257  0.0664  370 TRP A C   
2845 O O   . TRP A 370 ? 1.0131 0.7571 0.6889 -0.0496 0.1141  0.0569  370 TRP A O   
2846 C CB  . TRP A 370 ? 0.9737 0.7893 0.7383 -0.0470 0.1198  0.0671  370 TRP A CB  
2847 C CG  . TRP A 370 ? 0.9305 0.7528 0.7032 -0.0569 0.0991  0.0561  370 TRP A CG  
2848 C CD1 . TRP A 370 ? 0.8686 0.6864 0.6324 -0.0602 0.0848  0.0531  370 TRP A CD1 
2849 C CD2 . TRP A 370 ? 0.8648 0.7005 0.6583 -0.0639 0.0910  0.0480  370 TRP A CD2 
2850 N NE1 . TRP A 370 ? 0.8091 0.6379 0.5890 -0.0685 0.0682  0.0441  370 TRP A NE1 
2851 C CE2 . TRP A 370 ? 0.7592 0.5990 0.5577 -0.0710 0.0723  0.0406  370 TRP A CE2 
2852 C CE3 . TRP A 370 ? 0.7887 0.6333 0.5974 -0.0646 0.0985  0.0473  370 TRP A CE3 
2853 C CZ2 . TRP A 370 ? 0.7740 0.6273 0.5941 -0.0785 0.0619  0.0324  370 TRP A CZ2 
2854 C CZ3 . TRP A 370 ? 0.8088 0.6652 0.6361 -0.0724 0.0883  0.0387  370 TRP A CZ3 
2855 C CH2 . TRP A 370 ? 0.6989 0.5600 0.5327 -0.0792 0.0707  0.0314  370 TRP A CH2 
2856 N N   . GLU A 371 ? 1.0342 0.8093 0.7435 -0.0352 0.1322  0.0776  371 GLU A N   
2857 C CA  . GLU A 371 ? 0.9574 0.7195 0.6452 -0.0338 0.1283  0.0800  371 GLU A CA  
2858 C C   . GLU A 371 ? 0.9798 0.7497 0.6725 -0.0428 0.1060  0.0744  371 GLU A C   
2859 O O   . GLU A 371 ? 0.8748 0.6716 0.6012 -0.0471 0.0954  0.0722  371 GLU A O   
2860 C CB  . GLU A 371 ? 0.8315 0.6169 0.5461 -0.0240 0.1343  0.0908  371 GLU A CB  
2861 C CG  . GLU A 371 ? 1.0247 0.8068 0.7415 -0.0132 0.1495  0.0933  371 GLU A CG  
2862 C CD  . GLU A 371 ? 1.1435 0.9398 0.8838 -0.0104 0.1557  0.0933  371 GLU A CD  
2863 O OE1 . GLU A 371 ? 1.1186 0.9338 0.8793 -0.0164 0.1484  0.0926  371 GLU A OE1 
2864 O OE2 . GLU A 371 ? 1.3383 1.1255 1.0759 -0.0021 0.1681  0.0941  371 GLU A OE2 
2865 N N   . GLY A 372 ? 0.9986 0.7464 0.6601 -0.0448 0.0980  0.0715  372 GLY A N   
2866 C CA  . GLY A 372 ? 0.9022 0.6585 0.5708 -0.0519 0.0752  0.0664  372 GLY A CA  
2867 C C   . GLY A 372 ? 0.9518 0.7115 0.6286 -0.0615 0.0594  0.0539  372 GLY A C   
2868 O O   . GLY A 372 ? 0.9483 0.7201 0.6392 -0.0669 0.0404  0.0506  372 GLY A O   
2869 N N   . ILE A 373 ? 1.0196 0.7691 0.6897 -0.0635 0.0672  0.0476  373 ILE A N   
2870 C CA  . ILE A 373 ? 0.9816 0.7338 0.6603 -0.0736 0.0529  0.0361  373 ILE A CA  
2871 C C   . ILE A 373 ? 1.0749 0.8049 0.7228 -0.0809 0.0362  0.0292  373 ILE A C   
2872 O O   . ILE A 373 ? 1.1132 0.8530 0.7755 -0.0898 0.0175  0.0222  373 ILE A O   
2873 C CB  . ILE A 373 ? 0.9065 0.6503 0.5836 -0.0741 0.0668  0.0318  373 ILE A CB  
2874 C CG1 . ILE A 373 ? 0.9388 0.6915 0.6340 -0.0847 0.0530  0.0213  373 ILE A CG1 
2875 C CG2 . ILE A 373 ? 0.9842 0.6889 0.6152 -0.0717 0.0797  0.0302  373 ILE A CG2 
2876 C CD1 . ILE A 373 ? 1.0459 0.7924 0.7436 -0.0856 0.0664  0.0177  373 ILE A CD1 
2877 N N   . ASP A 374 ? 1.1353 0.8354 0.7407 -0.0776 0.0426  0.0317  374 ASP A N   
2878 C CA  . ASP A 374 ? 1.1653 0.8413 0.7346 -0.0845 0.0264  0.0262  374 ASP A CA  
2879 C C   . ASP A 374 ? 1.1542 0.8224 0.7202 -0.0969 0.0129  0.0136  374 ASP A C   
2880 O O   . ASP A 374 ? 1.1905 0.8728 0.7732 -0.1054 -0.0095 0.0095  374 ASP A O   
2881 C CB  . ASP A 374 ? 1.1986 0.8917 0.7813 -0.0847 0.0081  0.0317  374 ASP A CB  
2882 C CG  . ASP A 374 ? 1.3119 0.9788 0.8527 -0.0901 -0.0075 0.0293  374 ASP A CG  
2883 O OD1 . ASP A 374 ? 1.2990 0.9312 0.7949 -0.0927 -0.0015 0.0238  374 ASP A OD1 
2884 O OD2 . ASP A 374 ? 1.2510 0.9307 0.8024 -0.0917 -0.0258 0.0330  374 ASP A OD2 
2885 N N   . GLU A 375 ? 1.2102 0.8557 0.7560 -0.0976 0.0280  0.0082  375 GLU A N   
2886 C CA  . GLU A 375 ? 1.2238 0.8598 0.7670 -0.1098 0.0184  -0.0037 375 GLU A CA  
2887 C C   . GLU A 375 ? 1.2176 0.8129 0.7180 -0.1097 0.0362  -0.0092 375 GLU A C   
2888 O O   . GLU A 375 ? 1.2420 0.8354 0.7475 -0.1005 0.0597  -0.0048 375 GLU A O   
2889 C CB  . GLU A 375 ? 1.2608 0.9312 0.8560 -0.1118 0.0176  -0.0047 375 GLU A CB  
2890 C CG  . GLU A 375 ? 1.3117 0.9831 0.9169 -0.1261 0.0014  -0.0154 375 GLU A CG  
2891 C CD  . GLU A 375 ? 1.3809 1.0899 1.0400 -0.1274 -0.0009 -0.0149 375 GLU A CD  
2892 O OE1 . GLU A 375 ? 1.3327 1.0638 1.0171 -0.1176 0.0108  -0.0071 375 GLU A OE1 
2893 O OE2 . GLU A 375 ? 1.5190 1.2350 1.1946 -0.1388 -0.0143 -0.0221 375 GLU A OE2 
2894 N N   . PRO A 376 ? 1.3472 0.9087 0.8047 -0.1196 0.0257  -0.0184 376 PRO A N   
2895 C CA  . PRO A 376 ? 1.3220 0.8393 0.7338 -0.1195 0.0439  -0.0246 376 PRO A CA  
2896 C C   . PRO A 376 ? 1.3180 0.8362 0.7494 -0.1239 0.0526  -0.0309 376 PRO A C   
2897 O O   . PRO A 376 ? 1.3712 0.9138 0.8379 -0.1336 0.0371  -0.0352 376 PRO A O   
2898 C CB  . PRO A 376 ? 1.4458 0.9297 0.8089 -0.1322 0.0246  -0.0341 376 PRO A CB  
2899 C CG  . PRO A 376 ? 1.3687 0.8790 0.7483 -0.1342 0.0003  -0.0286 376 PRO A CG  
2900 C CD  . PRO A 376 ? 1.3162 0.8763 0.7618 -0.1310 -0.0031 -0.0228 376 PRO A CD  
2901 N N   . LEU A 377 ? 1.4018 0.8923 0.8102 -0.1161 0.0789  -0.0304 377 LEU A N   
2902 C CA  . LEU A 377 ? 1.4724 0.9559 0.8918 -0.1190 0.0906  -0.0356 377 LEU A CA  
2903 C C   . LEU A 377 ? 1.6297 1.0650 1.0006 -0.1314 0.0881  -0.0496 377 LEU A C   
2904 O O   . LEU A 377 ? 1.6490 1.0493 0.9694 -0.1335 0.0859  -0.0538 377 LEU A O   
2905 C CB  . LEU A 377 ? 1.4974 0.9807 0.9248 -0.1022 0.1217  -0.0253 377 LEU A CB  
2906 C CG  . LEU A 377 ? 1.3810 0.9108 0.8569 -0.0908 0.1260  -0.0114 377 LEU A CG  
2907 C CD1 . LEU A 377 ? 1.2915 0.8178 0.7717 -0.0752 0.1559  -0.0008 377 LEU A CD1 
2908 C CD2 . LEU A 377 ? 1.4658 1.0347 0.9912 -0.0987 0.1100  -0.0133 377 LEU A CD2 
2909 N N   . ALA A 378 ? 1.6944 1.1269 1.0797 -0.1403 0.0885  -0.0568 378 ALA A N   
2910 C CA  . ALA A 378 ? 1.7375 1.1234 1.0795 -0.1534 0.0870  -0.0707 378 ALA A CA  
2911 C C   . ALA A 378 ? 1.7853 1.1247 1.0813 -0.1420 0.1176  -0.0704 378 ALA A C   
2912 O O   . ALA A 378 ? 1.7035 1.0533 1.0146 -0.1245 0.1416  -0.0587 378 ALA A O   
2913 C CB  . ALA A 378 ? 1.6705 1.0666 1.0438 -0.1654 0.0816  -0.0772 378 ALA A CB  
2914 N N   . PRO A 379 ? 1.7068 0.9967 0.9497 -0.1515 0.1170  -0.0819 379 PRO A N   
2915 C CA  . PRO A 379 ? 1.5709 0.8248 0.7841 -0.1387 0.1458  -0.0770 379 PRO A CA  
2916 C C   . PRO A 379 ? 1.5018 0.7515 0.7346 -0.1323 0.1700  -0.0751 379 PRO A C   
2917 O O   . PRO A 379 ? 1.5034 0.7558 0.7525 -0.1447 0.1621  -0.0828 379 PRO A O   
2918 C CB  . PRO A 379 ? 1.4136 0.6318 0.5854 -0.1524 0.1327  -0.0861 379 PRO A CB  
2919 N N   . GLY A 380 ? 1.4447 0.6907 0.6813 -0.1123 0.1988  -0.0629 380 GLY A N   
2920 C CA  . GLY A 380 ? 1.5322 0.7748 0.7883 -0.1033 0.2232  -0.0580 380 GLY A CA  
2921 C C   . GLY A 380 ? 1.5716 0.8587 0.8752 -0.0952 0.2286  -0.0495 380 GLY A C   
2922 O O   . GLY A 380 ? 1.5836 0.8738 0.9100 -0.0912 0.2430  -0.0458 380 GLY A O   
2923 N N   . VAL A 381 ? 1.5338 0.8652 0.8675 -0.0923 0.2134  -0.0413 381 VAL A N   
2924 C CA  . VAL A 381 ? 1.5786 0.9644 0.9721 -0.0849 0.2122  -0.0286 381 VAL A CA  
2925 C C   . VAL A 381 ? 1.6146 1.0163 1.0213 -0.0643 0.2305  -0.0124 381 VAL A C   
2926 O O   . VAL A 381 ? 1.5282 0.9251 0.9204 -0.0588 0.2272  -0.0107 381 VAL A O   
2927 C CB  . VAL A 381 ? 1.5211 0.9482 0.9464 -0.0966 0.1809  -0.0312 381 VAL A CB  
2928 C CG1 . VAL A 381 ? 1.4818 0.9613 0.9643 -0.0889 0.1812  -0.0188 381 VAL A CG1 
2929 C CG2 . VAL A 381 ? 1.4890 0.9055 0.9107 -0.1169 0.1609  -0.0461 381 VAL A CG2 
2930 N N   . THR A 382 ? 1.7045 1.1354 1.1576 -0.0516 0.2416  -0.0017 382 THR A N   
2931 C CA  . THR A 382 ? 1.7433 1.2045 1.2331 -0.0308 0.2494  0.0115  382 THR A CA  
2932 C C   . THR A 382 ? 1.7255 1.2435 1.2637 -0.0293 0.2361  0.0209  382 THR A C   
2933 O O   . THR A 382 ? 1.7184 1.2525 1.2678 -0.0419 0.2247  0.0184  382 THR A O   
2934 C CB  . THR A 382 ? 1.8296 1.2835 1.3356 -0.0163 0.2692  0.0168  382 THR A CB  
2935 O OG1 . THR A 382 ? 1.7875 1.2633 1.3233 -0.0198 0.2677  0.0185  382 THR A OG1 
2936 C CG2 . THR A 382 ? 1.8512 1.2438 1.3075 -0.0185 0.2839  0.0074  382 THR A CG2 
2937 N N   . ILE A 383 ? 1.6247 1.1715 1.1911 -0.0147 0.2381  0.0318  383 ILE A N   
2938 C CA  . ILE A 383 ? 1.4889 1.0872 1.0989 -0.0128 0.2260  0.0410  383 ILE A CA  
2939 C C   . ILE A 383 ? 1.4907 1.1185 1.1414 0.0032  0.2346  0.0532  383 ILE A C   
2940 O O   . ILE A 383 ? 1.5783 1.1928 1.2245 0.0157  0.2480  0.0574  383 ILE A O   
2941 C CB  . ILE A 383 ? 1.5020 1.1086 1.1041 -0.0143 0.2156  0.0428  383 ILE A CB  
2942 C CG1 . ILE A 383 ? 1.4956 1.0717 1.0537 -0.0308 0.2046  0.0313  383 ILE A CG1 
2943 C CG2 . ILE A 383 ? 1.4542 1.1106 1.0999 -0.0133 0.2041  0.0520  383 ILE A CG2 
2944 C CD1 . ILE A 383 ? 1.4891 1.0703 1.0360 -0.0322 0.1935  0.0332  383 ILE A CD1 
2945 N N   . THR A 384 ? 1.3820 1.0486 1.0708 0.0021  0.2264  0.0590  384 THR A N   
2946 C CA  . THR A 384 ? 1.3642 1.0627 1.0914 0.0145  0.2301  0.0711  384 THR A CA  
2947 C C   . THR A 384 ? 1.2724 1.0132 1.0292 0.0130  0.2162  0.0785  384 THR A C   
2948 O O   . THR A 384 ? 1.2026 0.9614 0.9693 0.0028  0.2035  0.0761  384 THR A O   
2949 C CB  . THR A 384 ? 1.2771 0.9818 1.0203 0.0142  0.2326  0.0718  384 THR A CB  
2950 O OG1 . THR A 384 ? 1.3700 1.0323 1.0850 0.0158  0.2473  0.0651  384 THR A OG1 
2951 C CG2 . THR A 384 ? 1.1890 0.9272 0.9694 0.0257  0.2338  0.0849  384 THR A CG2 
2952 N N   . SER A 385 ? 1.3031 1.0576 1.0733 0.0228  0.2195  0.0875  385 SER A N   
2953 C CA  . SER A 385 ? 1.2832 1.0736 1.0785 0.0206  0.2074  0.0945  385 SER A CA  
2954 C C   . SER A 385 ? 1.2112 1.0359 1.0394 0.0183  0.1989  0.0999  385 SER A C   
2955 O O   . SER A 385 ? 1.2147 1.0377 1.0486 0.0202  0.2031  0.0999  385 SER A O   
2956 C CB  . SER A 385 ? 1.3517 1.1472 1.1545 0.0313  0.2146  0.1033  385 SER A CB  
2957 O OG  . SER A 385 ? 1.4109 1.2108 1.2306 0.0429  0.2255  0.1114  385 SER A OG  
2958 N N   . TRP A 386 ? 1.1305 0.9848 0.9785 0.0137  0.1871  0.1045  386 TRP A N   
2959 C CA  . TRP A 386 ? 1.1204 1.0056 0.9957 0.0103  0.1783  0.1093  386 TRP A CA  
2960 C C   . TRP A 386 ? 1.1487 1.0476 1.0444 0.0205  0.1843  0.1199  386 TRP A C   
2961 O O   . TRP A 386 ? 1.1250 1.0449 1.0394 0.0185  0.1785  0.1239  386 TRP A O   
2962 C CB  . TRP A 386 ? 1.0025 0.9104 0.8895 0.0022  0.1652  0.1106  386 TRP A CB  
2963 C CG  . TRP A 386 ? 1.0361 0.9554 0.9335 0.0069  0.1657  0.1187  386 TRP A CG  
2964 C CD1 . TRP A 386 ? 1.1034 1.0089 0.9870 0.0100  0.1701  0.1188  386 TRP A CD1 
2965 C CD2 . TRP A 386 ? 1.0179 0.9637 0.9413 0.0088  0.1621  0.1282  386 TRP A CD2 
2966 N NE1 . TRP A 386 ? 1.1344 1.0572 1.0358 0.0138  0.1700  0.1280  386 TRP A NE1 
2967 C CE2 . TRP A 386 ? 1.0543 1.0016 0.9804 0.0129  0.1650  0.1338  386 TRP A CE2 
2968 C CE3 . TRP A 386 ? 1.0320 0.9988 0.9750 0.0071  0.1569  0.1326  386 TRP A CE3 
2969 C CZ2 . TRP A 386 ? 1.0029 0.9729 0.9529 0.0153  0.1630  0.1439  386 TRP A CZ2 
2970 C CZ3 . TRP A 386 ? 1.0086 0.9969 0.9732 0.0095  0.1543  0.1426  386 TRP A CZ3 
2971 C CH2 . TRP A 386 ? 1.0063 0.9964 0.9753 0.0135  0.1573  0.1483  386 TRP A CH2 
2972 N N   . LYS A 387 ? 1.1638 1.0504 1.0559 0.0315  0.1964  0.1249  387 LYS A N   
2973 C CA  . LYS A 387 ? 1.2088 1.1053 1.1204 0.0431  0.2045  0.1361  387 LYS A CA  
2974 C C   . LYS A 387 ? 1.3367 1.2131 1.2407 0.0503  0.2163  0.1352  387 LYS A C   
2975 O O   . LYS A 387 ? 1.3114 1.1888 1.2278 0.0626  0.2268  0.1448  387 LYS A O   
2976 C CB  . LYS A 387 ? 1.2510 1.1442 1.1649 0.0528  0.2138  0.1433  387 LYS A CB  
2977 C CG  . LYS A 387 ? 1.1366 1.0517 1.0626 0.0469  0.2034  0.1469  387 LYS A CG  
2978 C CD  . LYS A 387 ? 1.1886 1.0992 1.1170 0.0571  0.2143  0.1545  387 LYS A CD  
2979 C CE  . LYS A 387 ? 1.2751 1.2074 1.2172 0.0511  0.2045  0.1588  387 LYS A CE  
2980 N NZ  . LYS A 387 ? 1.2216 1.1865 1.1936 0.0478  0.1946  0.1671  387 LYS A NZ  
2981 N N   . ASN A 388 ? 1.4140 1.2715 1.2988 0.0432  0.2155  0.1244  388 ASN A N   
2982 C CA  . ASN A 388 ? 1.4098 1.2451 1.2855 0.0486  0.2269  0.1224  388 ASN A CA  
2983 C C   . ASN A 388 ? 1.4849 1.2891 1.3447 0.0613  0.2455  0.1238  388 ASN A C   
2984 O O   . ASN A 388 ? 1.5821 1.3786 1.4485 0.0726  0.2578  0.1303  388 ASN A O   
2985 C CB  . ASN A 388 ? 1.4144 1.2725 1.3151 0.0521  0.2247  0.1315  388 ASN A CB  
2986 C CG  . ASN A 388 ? 1.4883 1.3264 1.3795 0.0530  0.2323  0.1275  388 ASN A CG  
2987 O OD1 . ASN A 388 ? 1.5013 1.3139 1.3693 0.0462  0.2345  0.1161  388 ASN A OD1 
2988 N ND2 . ASN A 388 ? 1.5986 1.4474 1.5074 0.0613  0.2366  0.1374  388 ASN A ND2 
2989 N N   . LYS A 389 ? 1.4213 1.2061 1.2589 0.0599  0.2483  0.1180  389 LYS A N   
2990 C CA  . LYS A 389 ? 1.5178 1.2690 1.3352 0.0711  0.2665  0.1180  389 LYS A CA  
2991 C C   . LYS A 389 ? 1.5929 1.3070 1.3697 0.0630  0.2682  0.1042  389 LYS A C   
2992 O O   . LYS A 389 ? 1.5111 1.2316 1.2801 0.0500  0.2543  0.0970  389 LYS A O   
2993 C CB  . LYS A 389 ? 1.5348 1.3011 1.3680 0.0808  0.2706  0.1288  389 LYS A CB  
2994 C CG  . LYS A 389 ? 1.5092 1.3101 1.3812 0.0890  0.2694  0.1437  389 LYS A CG  
2995 C CD  . LYS A 389 ? 1.4904 1.3041 1.3773 0.0978  0.2743  0.1543  389 LYS A CD  
2996 C CE  . LYS A 389 ? 1.4040 1.2517 1.3295 0.1056  0.2730  0.1702  389 LYS A CE  
2997 N NZ  . LYS A 389 ? 1.4003 1.2609 1.3425 0.1140  0.2783  0.1816  389 LYS A NZ  
2998 N N   . GLU A 390 ? 1.6902 1.3632 1.4395 0.0708  0.2858  0.1007  390 GLU A N   
2999 C CA  . GLU A 390 ? 1.7768 1.4088 1.4816 0.0632  0.2885  0.0878  390 GLU A CA  
3000 C C   . GLU A 390 ? 1.9085 1.5463 1.6065 0.0626  0.2836  0.0891  390 GLU A C   
3001 O O   . GLU A 390 ? 1.9244 1.5671 1.6331 0.0745  0.2929  0.0982  390 GLU A O   
3002 C CB  . GLU A 390 ? 1.8104 1.3929 1.4851 0.0715  0.3097  0.0839  390 GLU A CB  
3003 C CG  . GLU A 390 ? 1.7998 1.3725 1.4793 0.0727  0.3165  0.0828  390 GLU A CG  
3004 C CD  . GLU A 390 ? 1.8182 1.3841 1.4828 0.0553  0.3050  0.0710  390 GLU A CD  
3005 O OE1 . GLU A 390 ? 1.7873 1.3409 1.4258 0.0427  0.2955  0.0616  390 GLU A OE1 
3006 O OE2 . GLU A 390 ? 1.8673 1.4400 1.5463 0.0542  0.3055  0.0718  390 GLU A OE2 
3007 N N   . TRP A 391 ? 2.2036 1.8403 1.8843 0.0489  0.2696  0.0808  391 TRP A N   
3008 C CA  . TRP A 391 ? 2.2215 1.8676 1.8980 0.0469  0.2623  0.0825  391 TRP A CA  
3009 C C   . TRP A 391 ? 2.3848 1.9866 2.0105 0.0402  0.2639  0.0711  391 TRP A C   
3010 O O   . TRP A 391 ? 2.3415 1.9174 1.9395 0.0295  0.2606  0.0601  391 TRP A O   
3011 C CB  . TRP A 391 ? 2.1414 1.8282 1.8439 0.0369  0.2425  0.0848  391 TRP A CB  
3012 C CG  . TRP A 391 ? 2.1547 1.8493 1.8516 0.0337  0.2344  0.0862  391 TRP A CG  
3013 C CD1 . TRP A 391 ? 2.1668 1.8849 1.8860 0.0405  0.2352  0.0965  391 TRP A CD1 
3014 C CD2 . TRP A 391 ? 2.1952 1.8730 1.8616 0.0224  0.2240  0.0776  391 TRP A CD2 
3015 N NE1 . TRP A 391 ? 2.1817 1.8986 1.8867 0.0347  0.2268  0.0949  391 TRP A NE1 
3016 C CE2 . TRP A 391 ? 2.1708 1.8633 1.8432 0.0240  0.2194  0.0836  391 TRP A CE2 
3017 C CE3 . TRP A 391 ? 2.1764 1.8272 1.8102 0.0105  0.2177  0.0658  391 TRP A CE3 
3018 C CZ2 . TRP A 391 ? 2.2135 1.8948 1.8607 0.0154  0.2087  0.0788  391 TRP A CZ2 
3019 C CZ3 . TRP A 391 ? 2.1548 1.7948 1.7628 0.0011  0.2060  0.0609  391 TRP A CZ3 
3020 C CH2 . TRP A 391 ? 2.1903 1.8456 1.8052 0.0043  0.2016  0.0676  391 TRP A CH2 
3021 N N   . ARG A 392 ? 2.3679 1.9605 1.9804 0.0456  0.2686  0.0738  392 ARG A N   
3022 C CA  . ARG A 392 ? 2.4788 2.0318 2.0422 0.0392  0.2680  0.0643  392 ARG A CA  
3023 C C   . ARG A 392 ? 2.5397 2.1130 2.1074 0.0368  0.2570  0.0686  392 ARG A C   
3024 O O   . ARG A 392 ? 2.4961 2.1036 2.0996 0.0445  0.2579  0.0799  392 ARG A O   
3025 C CB  . ARG A 392 ? 2.5368 2.0454 2.0691 0.0493  0.2888  0.0627  392 ARG A CB  
3026 C CG  . ARG A 392 ? 2.5204 1.9994 2.0410 0.0514  0.3015  0.0578  392 ARG A CG  
3027 C CD  . ARG A 392 ? 2.5480 1.9726 2.0261 0.0579  0.3206  0.0539  392 ARG A CD  
3028 N NE  . ARG A 392 ? 2.5217 1.9536 2.0151 0.0742  0.3346  0.0652  392 ARG A NE  
3029 C CZ  . ARG A 392 ? 2.5213 1.9103 1.9828 0.0826  0.3530  0.0647  392 ARG A CZ  
3030 N NH1 . ARG A 392 ? 2.5153 1.8493 1.9257 0.0757  0.3591  0.0533  392 ARG A NH1 
3031 N NH2 . ARG A 392 ? 2.4824 1.8827 1.9628 0.0974  0.3656  0.0762  392 ARG A NH2 
3032 N N   . PRO A 393 ? 2.6305 2.1825 2.1614 0.0257  0.2460  0.0601  393 PRO A N   
3033 C CA  . PRO A 393 ? 2.6660 2.2350 2.1991 0.0235  0.2353  0.0646  393 PRO A CA  
3034 C C   . PRO A 393 ? 2.7593 2.3224 2.2896 0.0354  0.2486  0.0719  393 PRO A C   
3035 O O   . PRO A 393 ? 2.7829 2.3608 2.3173 0.0345  0.2415  0.0769  393 PRO A O   
3036 C CB  . PRO A 393 ? 2.7297 2.2679 2.2160 0.0094  0.2216  0.0530  393 PRO A CB  
3037 C CG  . PRO A 393 ? 2.7131 2.2323 2.1858 0.0011  0.2205  0.0433  393 PRO A CG  
3038 C CD  . PRO A 393 ? 2.6841 2.1966 2.1706 0.0132  0.2408  0.0464  393 PRO A CD  
3039 N N   . GLN A 394 ? 2.8131 2.3542 2.3370 0.0468  0.2684  0.0733  394 GLN A N   
3040 C CA  . GLN A 394 ? 2.7965 2.3302 2.3178 0.0588  0.2830  0.0808  394 GLN A CA  
3041 C C   . GLN A 394 ? 2.6975 2.2746 2.2719 0.0691  0.2882  0.0952  394 GLN A C   
3042 O O   . GLN A 394 ? 2.6862 2.2684 2.2662 0.0765  0.2957  0.1031  394 GLN A O   
3043 C CB  . GLN A 394 ? 2.8723 2.3566 2.3582 0.0667  0.3035  0.0761  394 GLN A CB  
3044 C CG  . GLN A 394 ? 3.0646 2.4981 2.4891 0.0569  0.3003  0.0629  394 GLN A CG  
3045 C CD  . GLN A 394 ? 3.0524 2.4765 2.4611 0.0419  0.2856  0.0515  394 GLN A CD  
3046 O OE1 . GLN A 394 ? 2.9323 2.3806 2.3729 0.0409  0.2828  0.0529  394 GLN A OE1 
3047 N NE2 . GLN A 394 ? 3.1674 2.5562 2.5265 0.0296  0.2755  0.0406  394 GLN A NE2 
3048 N N   . ASP A 395 ? 2.5489 2.1564 2.1609 0.0691  0.2839  0.0989  395 ASP A N   
3049 C CA  . ASP A 395 ? 2.4506 2.0989 2.1116 0.0772  0.2863  0.1124  395 ASP A CA  
3050 C C   . ASP A 395 ? 2.5123 2.1984 2.1974 0.0688  0.2690  0.1173  395 ASP A C   
3051 O O   . ASP A 395 ? 2.5361 2.2178 2.2021 0.0579  0.2556  0.1108  395 ASP A O   
3052 C CB  . ASP A 395 ? 2.3274 1.9915 2.0159 0.0798  0.2873  0.1146  395 ASP A CB  
3053 C CG  . ASP A 395 ? 2.2795 1.9035 1.9434 0.0873  0.3044  0.1095  395 ASP A CG  
3054 O OD1 . ASP A 395 ? 2.3169 1.9073 1.9546 0.0958  0.3206  0.1093  395 ASP A OD1 
3055 O OD2 . ASP A 395 ? 2.1564 1.7804 1.8258 0.0847  0.3024  0.1059  395 ASP A OD2 
3056 N N   . GLU A 396 ? 2.7885 2.5104 2.5153 0.0738  0.2693  0.1293  396 GLU A N   
3057 C CA  . GLU A 396 ? 2.7245 2.4809 2.4759 0.0657  0.2539  0.1345  396 GLU A CA  
3058 C C   . GLU A 396 ? 2.6318 2.4185 2.4106 0.0570  0.2385  0.1341  396 GLU A C   
3059 O O   . GLU A 396 ? 2.5399 2.3459 2.3279 0.0470  0.2234  0.1339  396 GLU A O   
3060 C CB  . GLU A 396 ? 2.6998 2.4763 2.4790 0.0741  0.2620  0.1478  396 GLU A CB  
3061 C CG  . GLU A 396 ? 2.6006 2.4076 2.4017 0.0654  0.2477  0.1532  396 GLU A CG  
3062 C CD  . GLU A 396 ? 2.5065 2.3358 2.3397 0.0728  0.2552  0.1669  396 GLU A CD  
3063 O OE1 . GLU A 396 ? 2.5163 2.3472 2.3649 0.0843  0.2682  0.1736  396 GLU A OE1 
3064 O OE2 . GLU A 396 ? 2.4108 2.2552 2.2541 0.0675  0.2483  0.1716  396 GLU A OE2 
3065 N N   . GLU A 397 ? 2.1890 1.9785 1.9799 0.0610  0.2427  0.1341  397 GLU A N   
3066 C CA  . GLU A 397 ? 1.9894 1.8058 1.8043 0.0532  0.2292  0.1337  397 GLU A CA  
3067 C C   . GLU A 397 ? 1.9492 1.7558 1.7427 0.0407  0.2164  0.1225  397 GLU A C   
3068 O O   . GLU A 397 ? 2.0217 1.7960 1.7826 0.0400  0.2212  0.1133  397 GLU A O   
3069 C CB  . GLU A 397 ? 1.9208 1.7368 1.7477 0.0607  0.2376  0.1358  397 GLU A CB  
3070 C CG  . GLU A 397 ? 1.7925 1.6204 1.6445 0.0740  0.2499  0.1487  397 GLU A CG  
3071 C CD  . GLU A 397 ? 1.7193 1.5881 1.6098 0.0709  0.2391  0.1588  397 GLU A CD  
3072 O OE1 . GLU A 397 ? 1.7377 1.6242 1.6348 0.0585  0.2227  0.1549  397 GLU A OE1 
3073 O OE2 . GLU A 397 ? 1.6750 1.5570 1.5888 0.0809  0.2475  0.1710  397 GLU A OE2 
3074 N N   . PRO A 398 ? 1.8031 1.6344 1.6125 0.0306  0.2007  0.1230  398 PRO A N   
3075 C CA  . PRO A 398 ? 1.6861 1.5088 1.4780 0.0198  0.1894  0.1136  398 PRO A CA  
3076 C C   . PRO A 398 ? 1.5783 1.4001 1.3736 0.0175  0.1888  0.1084  398 PRO A C   
3077 O O   . PRO A 398 ? 1.5684 1.4112 1.3905 0.0204  0.1895  0.1137  398 PRO A O   
3078 C CB  . PRO A 398 ? 1.5540 1.4045 1.3668 0.0117  0.1753  0.1177  398 PRO A CB  
3079 C CG  . PRO A 398 ? 1.5605 1.4389 1.4074 0.0162  0.1772  0.1276  398 PRO A CG  
3080 C CD  . PRO A 398 ? 1.7174 1.5825 1.5597 0.0286  0.1934  0.1322  398 PRO A CD  
3081 N N   . CYS A 399 ? 1.6573 1.4532 1.4236 0.0115  0.1872  0.0981  399 CYS A N   
3082 C CA  . CYS A 399 ? 1.6165 1.4078 1.3834 0.0085  0.1877  0.0926  399 CYS A CA  
3083 C C   . CYS A 399 ? 1.3880 1.2113 1.1838 0.0013  0.1756  0.0945  399 CYS A C   
3084 O O   . CYS A 399 ? 1.3713 1.2021 1.1801 0.0014  0.1768  0.0942  399 CYS A O   
3085 C CB  . CYS A 399 ? 1.6797 1.4337 1.4067 0.0013  0.1878  0.0807  399 CYS A CB  
3086 S SG  . CYS A 399 ? 1.5724 1.3259 1.2853 -0.0130 0.1707  0.0752  399 CYS A SG  
3087 N N   . ALA A 400 ? 1.2164 1.0567 1.0212 -0.0048 0.1645  0.0966  400 ALA A N   
3088 C CA  . ALA A 400 ? 1.1328 1.0006 0.9625 -0.0119 0.1538  0.0981  400 ALA A CA  
3089 C C   . ALA A 400 ? 1.1503 1.0446 1.0038 -0.0110 0.1488  0.1070  400 ALA A C   
3090 O O   . ALA A 400 ? 1.1673 1.0569 1.0138 -0.0088 0.1497  0.1102  400 ALA A O   
3091 C CB  . ALA A 400 ? 1.1159 0.9738 0.9311 -0.0227 0.1452  0.0903  400 ALA A CB  
3092 N N   . HIS A 401 ? 0.9962 0.9164 0.8756 -0.0135 0.1435  0.1107  401 HIS A N   
3093 C CA  . HIS A 401 ? 0.8910 0.8337 0.7914 -0.0145 0.1385  0.1182  401 HIS A CA  
3094 C C   . HIS A 401 ? 0.9379 0.8826 0.8358 -0.0223 0.1296  0.1168  401 HIS A C   
3095 O O   . HIS A 401 ? 0.9257 0.8644 0.8158 -0.0286 0.1248  0.1106  401 HIS A O   
3096 C CB  . HIS A 401 ? 0.8669 0.8323 0.7904 -0.0163 0.1345  0.1213  401 HIS A CB  
3097 C CG  . HIS A 401 ? 0.8578 0.8436 0.8017 -0.0171 0.1303  0.1290  401 HIS A CG  
3098 N ND1 . HIS A 401 ? 0.8570 0.8561 0.8109 -0.0258 0.1206  0.1283  401 HIS A ND1 
3099 C CD2 . HIS A 401 ? 0.8576 0.8518 0.8146 -0.0102 0.1351  0.1379  401 HIS A CD2 
3100 C CE1 . HIS A 401 ? 0.8375 0.8518 0.8088 -0.0248 0.1190  0.1361  401 HIS A CE1 
3101 N NE2 . HIS A 401 ? 0.8139 0.8266 0.7883 -0.0154 0.1275  0.1425  401 HIS A NE2 
3102 N N   . PRO A 402 ? 0.9264 0.8781 0.8314 -0.0218 0.1281  0.1228  402 PRO A N   
3103 C CA  . PRO A 402 ? 0.8115 0.7635 0.7146 -0.0286 0.1201  0.1225  402 PRO A CA  
3104 C C   . PRO A 402 ? 0.8563 0.8224 0.7735 -0.0369 0.1118  0.1197  402 PRO A C   
3105 O O   . PRO A 402 ? 0.9191 0.8774 0.8287 -0.0420 0.1073  0.1160  402 PRO A O   
3106 C CB  . PRO A 402 ? 0.7936 0.7547 0.7084 -0.0263 0.1210  0.1306  402 PRO A CB  
3107 C CG  . PRO A 402 ? 0.8612 0.8171 0.7734 -0.0167 0.1319  0.1341  402 PRO A CG  
3108 C CD  . PRO A 402 ? 0.8938 0.8514 0.8087 -0.0144 0.1347  0.1307  402 PRO A CD  
3109 N N   . ASN A 403 ? 0.8814 0.8663 0.8180 -0.0381 0.1101  0.1214  403 ASN A N   
3110 C CA  . ASN A 403 ? 0.8974 0.8959 0.8471 -0.0457 0.1030  0.1185  403 ASN A CA  
3111 C C   . ASN A 403 ? 0.8410 0.8363 0.7858 -0.0471 0.1044  0.1120  403 ASN A C   
3112 O O   . ASN A 403 ? 0.8262 0.8338 0.7822 -0.0526 0.1001  0.1095  403 ASN A O   
3113 C CB  . ASN A 403 ? 0.9012 0.9202 0.8721 -0.0466 0.0996  0.1237  403 ASN A CB  
3114 C CG  . ASN A 403 ? 0.9565 0.9890 0.9403 -0.0555 0.0907  0.1215  403 ASN A CG  
3115 O OD1 . ASN A 403 ? 0.9484 0.9770 0.9294 -0.0610 0.0865  0.1179  403 ASN A OD1 
3116 N ND2 . ASN A 403 ? 1.1271 1.1763 1.1254 -0.0574 0.0871  0.1244  403 ASN A ND2 
3117 N N   . SER A 404 ? 0.8763 0.8546 0.8044 -0.0424 0.1108  0.1090  404 SER A N   
3118 C CA  . SER A 404 ? 0.7840 0.7566 0.7072 -0.0442 0.1129  0.1025  404 SER A CA  
3119 C C   . SER A 404 ? 0.8044 0.7753 0.7283 -0.0527 0.1065  0.0944  404 SER A C   
3120 O O   . SER A 404 ? 0.7886 0.7543 0.7089 -0.0550 0.0979  0.0898  404 SER A O   
3121 C CB  . SER A 404 ? 0.8472 0.7964 0.7494 -0.0386 0.1207  0.0993  404 SER A CB  
3122 O OG  . SER A 404 ? 0.8440 0.7732 0.7263 -0.0394 0.1209  0.0971  404 SER A OG  
3123 N N   . ARG A 405 ? 0.7251 0.7034 0.6570 -0.0565 0.1046  0.0886  405 ARG A N   
3124 C CA  . ARG A 405 ? 0.6970 0.6812 0.6379 -0.0637 0.0929  0.0769  405 ARG A CA  
3125 C C   . ARG A 405 ? 0.7378 0.7123 0.6734 -0.0663 0.0941  0.0675  405 ARG A C   
3126 O O   . ARG A 405 ? 0.6411 0.6049 0.5664 -0.0631 0.1040  0.0700  405 ARG A O   
3127 C CB  . ARG A 405 ? 0.6908 0.6962 0.6494 -0.0675 0.0890  0.0788  405 ARG A CB  
3128 C CG  . ARG A 405 ? 0.7881 0.8048 0.7545 -0.0668 0.0872  0.0886  405 ARG A CG  
3129 C CD  . ARG A 405 ? 0.7029 0.7191 0.6737 -0.0707 0.0766  0.0828  405 ARG A CD  
3130 N NE  . ARG A 405 ? 0.7750 0.8006 0.7537 -0.0710 0.0752  0.0923  405 ARG A NE  
3131 C CZ  . ARG A 405 ? 0.8159 0.8431 0.8010 -0.0749 0.0668  0.0897  405 ARG A CZ  
3132 N NH1 . ARG A 405 ? 0.8009 0.8219 0.7866 -0.0776 0.0593  0.0783  405 ARG A NH1 
3133 N NH2 . ARG A 405 ? 0.8254 0.8608 0.8182 -0.0759 0.0663  0.0993  405 ARG A NH2 
3134 N N   . PHE A 406 ? 0.8031 0.7810 0.7473 -0.0721 0.0845  0.0570  406 PHE A N   
3135 C CA  . PHE A 406 ? 0.5877 0.5619 0.5340 -0.0761 0.0847  0.0482  406 PHE A CA  
3136 C C   . PHE A 406 ? 0.5952 0.5859 0.5598 -0.0805 0.0805  0.0432  406 PHE A C   
3137 O O   . PHE A 406 ? 0.7566 0.7558 0.7303 -0.0818 0.0733  0.0419  406 PHE A O   
3138 C CB  . PHE A 406 ? 0.7490 0.7083 0.6872 -0.0790 0.0773  0.0400  406 PHE A CB  
3139 C CG  . PHE A 406 ? 0.5457 0.5094 0.4914 -0.0808 0.0647  0.0365  406 PHE A CG  
3140 C CD1 . PHE A 406 ? 0.5268 0.5026 0.4920 -0.0849 0.0576  0.0296  406 PHE A CD1 
3141 C CD2 . PHE A 406 ? 0.5908 0.5454 0.5238 -0.0777 0.0612  0.0407  406 PHE A CD2 
3142 C CE1 . PHE A 406 ? 0.3971 0.3760 0.3704 -0.0854 0.0468  0.0273  406 PHE A CE1 
3143 C CE2 . PHE A 406 ? 0.5160 0.4737 0.4558 -0.0788 0.0498  0.0385  406 PHE A CE2 
3144 C CZ  . PHE A 406 ? 0.3617 0.3317 0.3223 -0.0825 0.0424  0.0320  406 PHE A CZ  
3145 N N   . CYS A 407 ? 0.4393 0.4324 0.4078 -0.0827 0.0862  0.0405  407 CYS A N   
3146 C CA  . CYS A 407 ? 0.4757 0.4822 0.4581 -0.0864 0.0853  0.0360  407 CYS A CA  
3147 C C   . CYS A 407 ? 0.5457 0.5488 0.5360 -0.0907 0.0844  0.0266  407 CYS A C   
3148 O O   . CYS A 407 ? 0.6889 0.6855 0.6752 -0.0917 0.0914  0.0264  407 CYS A O   
3149 C CB  . CYS A 407 ? 0.5153 0.5296 0.4955 -0.0851 0.0937  0.0433  407 CYS A CB  
3150 S SG  . CYS A 407 ? 0.5671 0.5963 0.5570 -0.0895 0.0923  0.0395  407 CYS A SG  
3151 N N   . THR A 408 ? 0.5566 0.5643 0.5598 -0.0933 0.0761  0.0195  408 THR A N   
3152 C CA  . THR A 408 ? 0.5459 0.5529 0.5615 -0.0975 0.0738  0.0116  408 THR A CA  
3153 C C   . THR A 408 ? 0.4483 0.4677 0.4829 -0.0991 0.0729  0.0061  408 THR A C   
3154 O O   . THR A 408 ? 0.5841 0.6086 0.6214 -0.0974 0.0693  0.0064  408 THR A O   
3155 C CB  . THR A 408 ? 0.5181 0.5163 0.5318 -0.0986 0.0633  0.0089  408 THR A CB  
3156 O OG1 . THR A 408 ? 0.5134 0.5146 0.5439 -0.1035 0.0592  0.0020  408 THR A OG1 
3157 C CG2 . THR A 408 ? 0.5596 0.5607 0.5751 -0.0958 0.0543  0.0104  408 THR A CG2 
3158 N N   . PRO A 409 ? 0.4993 0.5223 0.5471 -0.1025 0.0773  0.0011  409 PRO A N   
3159 C CA  . PRO A 409 ? 0.5138 0.5472 0.5797 -0.1032 0.0791  -0.0041 409 PRO A CA  
3160 C C   . PRO A 409 ? 0.7180 0.7546 0.7998 -0.1024 0.0684  -0.0075 409 PRO A C   
3161 O O   . PRO A 409 ? 0.6109 0.6434 0.6945 -0.1034 0.0591  -0.0075 409 PRO A O   
3162 C CB  . PRO A 409 ? 0.4884 0.5239 0.5652 -0.1070 0.0874  -0.0071 409 PRO A CB  
3163 C CG  . PRO A 409 ? 0.4361 0.4617 0.4962 -0.1081 0.0917  -0.0026 409 PRO A CG  
3164 C CD  . PRO A 409 ? 0.5978 0.6146 0.6441 -0.1059 0.0826  0.0005  409 PRO A CD  
3165 N N   . ALA A 410 ? 0.5948 0.6376 0.6870 -0.1006 0.0699  -0.0105 410 ALA A N   
3166 C CA  . ALA A 410 ? 0.6519 0.6975 0.7604 -0.0985 0.0609  -0.0126 410 ALA A CA  
3167 C C   . ALA A 410 ? 0.6811 0.7340 0.8159 -0.1001 0.0592  -0.0163 410 ALA A C   
3168 O O   . ALA A 410 ? 0.5645 0.6199 0.7133 -0.0988 0.0485  -0.0160 410 ALA A O   
3169 C CB  . ALA A 410 ? 0.5171 0.5640 0.6272 -0.0958 0.0644  -0.0148 410 ALA A CB  
3170 N N   . SER A 411 ? 0.6535 0.7108 0.7967 -0.1029 0.0695  -0.0187 411 SER A N   
3171 C CA  . SER A 411 ? 0.6635 0.7302 0.8360 -0.1050 0.0689  -0.0212 411 SER A CA  
3172 C C   . SER A 411 ? 0.6261 0.6911 0.8016 -0.1096 0.0565  -0.0196 411 SER A C   
3173 O O   . SER A 411 ? 0.6289 0.7031 0.8309 -0.1115 0.0500  -0.0204 411 SER A O   
3174 C CB  . SER A 411 ? 0.7240 0.7948 0.9035 -0.1074 0.0844  -0.0234 411 SER A CB  
3175 O OG  . SER A 411 ? 0.8277 0.8914 0.9891 -0.1115 0.0882  -0.0212 411 SER A OG  
3176 N N   . GLN A 412 ? 0.7060 0.7589 0.8547 -0.1114 0.0532  -0.0171 412 GLN A N   
3177 C CA  . GLN A 412 ? 0.5630 0.6095 0.7078 -0.1165 0.0422  -0.0167 412 GLN A CA  
3178 C C   . GLN A 412 ? 0.7155 0.7592 0.8573 -0.1147 0.0259  -0.0148 412 GLN A C   
3179 O O   . GLN A 412 ? 0.5955 0.6332 0.7328 -0.1196 0.0146  -0.0148 412 GLN A O   
3180 C CB  . GLN A 412 ? 0.6094 0.6411 0.7251 -0.1185 0.0480  -0.0150 412 GLN A CB  
3181 C CG  . GLN A 412 ? 0.6306 0.6633 0.7474 -0.1206 0.0634  -0.0155 412 GLN A CG  
3182 C CD  . GLN A 412 ? 0.7627 0.7799 0.8522 -0.1214 0.0694  -0.0126 412 GLN A CD  
3183 O OE1 . GLN A 412 ? 0.8840 0.8990 0.9725 -0.1238 0.0807  -0.0122 412 GLN A OE1 
3184 N NE2 . GLN A 412 ? 0.7209 0.7264 0.7884 -0.1189 0.0629  -0.0100 412 GLN A NE2 
3185 N N   . CYS A 413 ? 0.7127 0.7590 0.8551 -0.1085 0.0242  -0.0131 413 CYS A N   
3186 C CA  . CYS A 413 ? 0.6755 0.7185 0.8147 -0.1062 0.0094  -0.0102 413 CYS A CA  
3187 C C   . CYS A 413 ? 0.6650 0.7197 0.8344 -0.1082 -0.0020 -0.0106 413 CYS A C   
3188 O O   . CYS A 413 ? 0.6080 0.6765 0.8068 -0.1068 0.0037  -0.0124 413 CYS A O   
3189 C CB  . CYS A 413 ? 0.5729 0.6155 0.7078 -0.0994 0.0116  -0.0080 413 CYS A CB  
3190 S SG  . CYS A 413 ? 0.5770 0.6138 0.7058 -0.0958 -0.0050 -0.0029 413 CYS A SG  
3191 N N   . PRO A 414 ? 0.6313 0.6812 0.7948 -0.1114 -0.0182 -0.0085 414 PRO A N   
3192 C CA  . PRO A 414 ? 0.6451 0.7086 0.8399 -0.1141 -0.0313 -0.0075 414 PRO A CA  
3193 C C   . PRO A 414 ? 0.5877 0.6624 0.8067 -0.1063 -0.0350 -0.0041 414 PRO A C   
3194 O O   . PRO A 414 ? 0.4801 0.5713 0.7354 -0.1062 -0.0388 -0.0031 414 PRO A O   
3195 C CB  . PRO A 414 ? 0.6678 0.7191 0.8408 -0.1200 -0.0485 -0.0060 414 PRO A CB  
3196 C CG  . PRO A 414 ? 0.6554 0.6878 0.7891 -0.1159 -0.0448 -0.0044 414 PRO A CG  
3197 C CD  . PRO A 414 ? 0.6816 0.7130 0.8091 -0.1129 -0.0250 -0.0066 414 PRO A CD  
3198 N N   . ILE A 415 ? 0.7081 0.7741 0.9099 -0.0996 -0.0333 -0.0018 415 ILE A N   
3199 C CA  . ILE A 415 ? 0.5489 0.6218 0.7710 -0.0920 -0.0369 0.0018  415 ILE A CA  
3200 C C   . ILE A 415 ? 0.6393 0.7125 0.8653 -0.0865 -0.0195 -0.0014 415 ILE A C   
3201 O O   . ILE A 415 ? 0.5167 0.5870 0.7451 -0.0801 -0.0193 0.0008  415 ILE A O   
3202 C CB  . ILE A 415 ? 0.5454 0.6068 0.7461 -0.0891 -0.0502 0.0077  415 ILE A CB  
3203 C CG1 . ILE A 415 ? 0.5099 0.5549 0.6737 -0.0883 -0.0419 0.0073  415 ILE A CG1 
3204 C CG2 . ILE A 415 ? 0.4720 0.5316 0.6666 -0.0950 -0.0688 0.0105  415 ILE A CG2 
3205 C CD1 . ILE A 415 ? 0.5777 0.6103 0.7193 -0.0852 -0.0521 0.0136  415 ILE A CD1 
3206 N N   . ILE A 416 ? 0.6079 0.6832 0.8332 -0.0894 -0.0050 -0.0065 416 ILE A N   
3207 C CA  . ILE A 416 ? 0.5446 0.6191 0.7709 -0.0855 0.0110  -0.0102 416 ILE A CA  
3208 C C   . ILE A 416 ? 0.5229 0.6075 0.7834 -0.0795 0.0138  -0.0104 416 ILE A C   
3209 O O   . ILE A 416 ? 0.7051 0.8032 0.9959 -0.0801 0.0111  -0.0095 416 ILE A O   
3210 C CB  . ILE A 416 ? 0.5201 0.5953 0.7392 -0.0900 0.0252  -0.0147 416 ILE A CB  
3211 C CG1 . ILE A 416 ? 0.5750 0.6475 0.7898 -0.0867 0.0408  -0.0186 416 ILE A CG1 
3212 C CG2 . ILE A 416 ? 0.5957 0.6838 0.8428 -0.0937 0.0262  -0.0159 416 ILE A CG2 
3213 C CD1 . ILE A 416 ? 0.6429 0.7036 0.8303 -0.0851 0.0401  -0.0173 416 ILE A CD1 
3214 N N   . ASP A 417 ? 0.6017 0.6794 0.8585 -0.0738 0.0196  -0.0112 417 ASP A N   
3215 C CA  . ASP A 417 ? 0.6772 0.7608 0.9646 -0.0668 0.0237  -0.0112 417 ASP A CA  
3216 C C   . ASP A 417 ? 0.6734 0.7643 0.9787 -0.0666 0.0412  -0.0168 417 ASP A C   
3217 O O   . ASP A 417 ? 0.6735 0.7584 0.9584 -0.0701 0.0533  -0.0219 417 ASP A O   
3218 C CB  . ASP A 417 ? 0.5504 0.6207 0.8257 -0.0616 0.0264  -0.0115 417 ASP A CB  
3219 C CG  . ASP A 417 ? 0.5535 0.6265 0.8594 -0.0531 0.0312  -0.0110 417 ASP A CG  
3220 O OD1 . ASP A 417 ? 0.5925 0.6691 0.9143 -0.0509 0.0466  -0.0161 417 ASP A OD1 
3221 O OD2 . ASP A 417 ? 0.4780 0.5489 0.7920 -0.0481 0.0205  -0.0050 417 ASP A OD2 
3222 N N   . PRO A 418 ? 0.6528 0.7571 0.9966 -0.0622 0.0433  -0.0151 418 PRO A N   
3223 C CA  . PRO A 418 ? 0.6241 0.7357 0.9866 -0.0617 0.0615  -0.0196 418 PRO A CA  
3224 C C   . PRO A 418 ? 0.6887 0.7876 1.0414 -0.0566 0.0802  -0.0260 418 PRO A C   
3225 O O   . PRO A 418 ? 0.6689 0.7721 1.0415 -0.0531 0.0966  -0.0291 418 PRO A O   
3226 C CB  . PRO A 418 ? 0.6634 0.7943 1.0734 -0.0578 0.0565  -0.0138 418 PRO A CB  
3227 C CG  . PRO A 418 ? 0.5877 0.7163 1.0027 -0.0521 0.0410  -0.0077 418 PRO A CG  
3228 C CD  . PRO A 418 ? 0.6025 0.7168 0.9757 -0.0573 0.0290  -0.0076 418 PRO A CD  
3229 N N   . ALA A 419 ? 0.7274 0.8097 1.0488 -0.0566 0.0781  -0.0281 419 ALA A N   
3230 C CA  . ALA A 419 ? 0.7650 0.8320 1.0711 -0.0539 0.0939  -0.0351 419 ALA A CA  
3231 C C   . ALA A 419 ? 0.7952 0.8485 1.0587 -0.0604 0.0930  -0.0383 419 ALA A C   
3232 O O   . ALA A 419 ? 0.7745 0.8126 1.0202 -0.0597 0.0998  -0.0431 419 ALA A O   
3233 C CB  . ALA A 419 ? 0.5269 0.5863 0.8474 -0.0453 0.0935  -0.0340 419 ALA A CB  
3234 N N   . TRP A 420 ? 0.7729 0.8308 1.0203 -0.0670 0.0849  -0.0354 420 TRP A N   
3235 C CA  . TRP A 420 ? 0.7726 0.8203 0.9837 -0.0725 0.0834  -0.0362 420 TRP A CA  
3236 C C   . TRP A 420 ? 0.7767 0.8191 0.9698 -0.0759 0.0987  -0.0423 420 TRP A C   
3237 O O   . TRP A 420 ? 0.8953 0.9294 1.0595 -0.0803 0.0981  -0.0429 420 TRP A O   
3238 C CB  . TRP A 420 ? 0.7229 0.7761 0.9235 -0.0771 0.0714  -0.0305 420 TRP A CB  
3239 C CG  . TRP A 420 ? 0.7921 0.8528 0.9936 -0.0814 0.0776  -0.0312 420 TRP A CG  
3240 C CD1 . TRP A 420 ? 0.7134 0.7859 0.9415 -0.0814 0.0790  -0.0308 420 TRP A CD1 
3241 C CD2 . TRP A 420 ? 0.8011 0.8585 0.9770 -0.0864 0.0831  -0.0314 420 TRP A CD2 
3242 N NE1 . TRP A 420 ? 0.7704 0.8452 0.9898 -0.0865 0.0858  -0.0314 420 TRP A NE1 
3243 C CE2 . TRP A 420 ? 0.8285 0.8939 1.0156 -0.0891 0.0886  -0.0315 420 TRP A CE2 
3244 C CE3 . TRP A 420 ? 0.7172 0.7663 0.8637 -0.0890 0.0837  -0.0306 420 TRP A CE3 
3245 C CZ2 . TRP A 420 ? 0.7217 0.7853 0.8900 -0.0935 0.0953  -0.0308 420 TRP A CZ2 
3246 C CZ3 . TRP A 420 ? 0.6648 0.7142 0.7941 -0.0931 0.0895  -0.0293 420 TRP A CZ3 
3247 C CH2 . TRP A 420 ? 0.6578 0.7134 0.7972 -0.0949 0.0956  -0.0295 420 TRP A CH2 
3248 N N   . GLU A 421 ? 0.7118 0.7591 0.9212 -0.0742 0.1123  -0.0460 421 GLU A N   
3249 C CA  . GLU A 421 ? 0.8296 0.8699 1.0203 -0.0768 0.1283  -0.0518 421 GLU A CA  
3250 C C   . GLU A 421 ? 0.8741 0.9066 1.0756 -0.0713 0.1440  -0.0585 421 GLU A C   
3251 O O   . GLU A 421 ? 0.9170 0.9436 1.1062 -0.0726 0.1598  -0.0636 421 GLU A O   
3252 C CB  . GLU A 421 ? 0.7222 0.7726 0.9158 -0.0805 0.1340  -0.0499 421 GLU A CB  
3253 C CG  . GLU A 421 ? 0.8360 0.8880 1.0082 -0.0863 0.1238  -0.0448 421 GLU A CG  
3254 C CD  . GLU A 421 ? 0.8067 0.8654 0.9798 -0.0900 0.1313  -0.0432 421 GLU A CD  
3255 O OE1 . GLU A 421 ? 0.8040 0.8705 1.0026 -0.0885 0.1401  -0.0444 421 GLU A OE1 
3256 O OE2 . GLU A 421 ? 0.9007 0.9570 1.0506 -0.0942 0.1291  -0.0400 421 GLU A OE2 
3257 N N   . SER A 422 ? 0.8643 0.8952 1.0873 -0.0647 0.1411  -0.0582 422 SER A N   
3258 C CA  . SER A 422 ? 1.0807 1.1012 1.3133 -0.0583 0.1575  -0.0644 422 SER A CA  
3259 C C   . SER A 422 ? 1.1882 1.1861 1.3826 -0.0621 0.1640  -0.0724 422 SER A C   
3260 O O   . SER A 422 ? 1.1885 1.1793 1.3609 -0.0668 0.1513  -0.0712 422 SER A O   
3261 C CB  . SER A 422 ? 1.1243 1.1475 1.3888 -0.0498 0.1517  -0.0608 422 SER A CB  
3262 O OG  . SER A 422 ? 1.0560 1.1010 1.3565 -0.0472 0.1442  -0.0532 422 SER A OG  
3263 N N   . PRO A 423 ? 1.3155 1.3009 1.5005 -0.0605 0.1837  -0.0803 423 PRO A N   
3264 C CA  . PRO A 423 ? 1.4072 1.3693 1.5514 -0.0660 0.1888  -0.0886 423 PRO A CA  
3265 C C   . PRO A 423 ? 1.5824 1.5262 1.7237 -0.0632 0.1863  -0.0926 423 PRO A C   
3266 O O   . PRO A 423 ? 1.5750 1.5023 1.6831 -0.0704 0.1818  -0.0971 423 PRO A O   
3267 C CB  . PRO A 423 ? 1.4162 1.3698 1.5521 -0.0645 0.2121  -0.0958 423 PRO A CB  
3268 C CG  . PRO A 423 ? 1.2999 1.2673 1.4815 -0.0545 0.2219  -0.0924 423 PRO A CG  
3269 C CD  . PRO A 423 ? 1.2608 1.2526 1.4704 -0.0546 0.2025  -0.0818 423 PRO A CD  
3270 N N   . GLU A 424 ? 1.9681 1.9144 2.1439 -0.0533 0.1886  -0.0903 424 GLU A N   
3271 C CA  . GLU A 424 ? 1.8950 1.8215 2.0694 -0.0496 0.1885  -0.0938 424 GLU A CA  
3272 C C   . GLU A 424 ? 1.8611 1.7915 2.0359 -0.0523 0.1665  -0.0866 424 GLU A C   
3273 O O   . GLU A 424 ? 1.9140 1.8248 2.0736 -0.0541 0.1638  -0.0899 424 GLU A O   
3274 C CB  . GLU A 424 ? 1.9393 1.8661 2.1521 -0.0364 0.2017  -0.0932 424 GLU A CB  
3275 C CG  . GLU A 424 ? 1.9410 1.8923 2.1969 -0.0295 0.1882  -0.0811 424 GLU A CG  
3276 C CD  . GLU A 424 ? 1.9180 1.8964 2.1918 -0.0316 0.1847  -0.0751 424 GLU A CD  
3277 O OE1 . GLU A 424 ? 1.9192 1.8972 2.1763 -0.0363 0.1962  -0.0799 424 GLU A OE1 
3278 O OE2 . GLU A 424 ? 1.8907 1.8893 2.1939 -0.0289 0.1704  -0.0654 424 GLU A OE2 
3279 N N   . GLY A 425 ? 1.3635 1.3167 1.5538 -0.0530 0.1516  -0.0768 425 GLY A N   
3280 C CA  . GLY A 425 ? 1.0781 1.0348 1.2677 -0.0550 0.1322  -0.0692 425 GLY A CA  
3281 C C   . GLY A 425 ? 1.0813 1.0439 1.3058 -0.0452 0.1261  -0.0621 425 GLY A C   
3282 O O   . GLY A 425 ? 1.2014 1.1652 1.4533 -0.0361 0.1371  -0.0629 425 GLY A O   
3283 N N   . VAL A 426 ? 0.7471 0.7138 0.9707 -0.0466 0.1085  -0.0541 426 VAL A N   
3284 C CA  . VAL A 426 ? 0.6160 0.5886 0.8688 -0.0381 0.0993  -0.0455 426 VAL A CA  
3285 C C   . VAL A 426 ? 0.9220 0.8739 1.1650 -0.0368 0.0965  -0.0453 426 VAL A C   
3286 O O   . VAL A 426 ? 0.8103 0.7512 1.0239 -0.0452 0.0920  -0.0474 426 VAL A O   
3287 C CB  . VAL A 426 ? 0.6203 0.6123 0.8795 -0.0401 0.0814  -0.0356 426 VAL A CB  
3288 C CG1 . VAL A 426 ? 0.6394 0.6502 0.9111 -0.0416 0.0846  -0.0359 426 VAL A CG1 
3289 C CG2 . VAL A 426 ? 0.7769 0.7636 1.0037 -0.0488 0.0710  -0.0337 426 VAL A CG2 
3290 N N   . PRO A 427 ? 0.8191 0.7654 1.0874 -0.0266 0.0991  -0.0422 427 PRO A N   
3291 C CA  . PRO A 427 ? 0.7920 0.7164 1.0520 -0.0252 0.0973  -0.0416 427 PRO A CA  
3292 C C   . PRO A 427 ? 0.7489 0.6788 1.0041 -0.0275 0.0777  -0.0306 427 PRO A C   
3293 O O   . PRO A 427 ? 0.7645 0.7110 1.0409 -0.0221 0.0665  -0.0207 427 PRO A O   
3294 C CB  . PRO A 427 ? 0.8868 0.8066 1.1802 -0.0116 0.1071  -0.0399 427 PRO A CB  
3295 C CG  . PRO A 427 ? 0.9643 0.9121 1.2899 -0.0060 0.1034  -0.0331 427 PRO A CG  
3296 C CD  . PRO A 427 ? 0.8344 0.7944 1.1425 -0.0157 0.1047  -0.0384 427 PRO A CD  
3297 N N   . ILE A 428 ? 0.7442 0.7349 0.9990 -0.0736 0.0282  -0.1136 428 ILE A N   
3298 C CA  . ILE A 428 ? 0.7026 0.6982 0.9481 -0.0637 0.0131  -0.1063 428 ILE A CA  
3299 C C   . ILE A 428 ? 0.7217 0.7142 0.9748 -0.0592 0.0110  -0.1074 428 ILE A C   
3300 O O   . ILE A 428 ? 0.7033 0.6910 0.9518 -0.0665 0.0213  -0.1099 428 ILE A O   
3301 C CB  . ILE A 428 ? 0.6515 0.6507 0.8674 -0.0684 0.0109  -0.0972 428 ILE A CB  
3302 C CG1 . ILE A 428 ? 0.6383 0.6413 0.8511 -0.0708 0.0104  -0.0937 428 ILE A CG1 
3303 C CG2 . ILE A 428 ? 0.5239 0.5258 0.7303 -0.0595 -0.0009 -0.0908 428 ILE A CG2 
3304 C CD1 . ILE A 428 ? 0.5166 0.5229 0.7442 -0.0598 0.0006  -0.0943 428 ILE A CD1 
3305 N N   . GLU A 429 ? 0.6349 0.6293 0.8988 -0.0480 -0.0025 -0.1053 429 GLU A N   
3306 C CA  . GLU A 429 ? 0.6639 0.6554 0.9369 -0.0428 -0.0068 -0.1042 429 GLU A CA  
3307 C C   . GLU A 429 ? 0.6216 0.6145 0.8728 -0.0368 -0.0185 -0.0960 429 GLU A C   
3308 O O   . GLU A 429 ? 0.5902 0.5806 0.8470 -0.0315 -0.0246 -0.0933 429 GLU A O   
3309 C CB  . GLU A 429 ? 0.7354 0.7267 1.0426 -0.0360 -0.0134 -0.1078 429 GLU A CB  
3310 C CG  . GLU A 429 ? 0.9107 0.8998 1.2454 -0.0414 -0.0002 -0.1165 429 GLU A CG  
3311 C CD  . GLU A 429 ? 1.0005 0.9900 1.3750 -0.0345 -0.0072 -0.1188 429 GLU A CD  
3312 O OE1 . GLU A 429 ? 0.8809 0.8715 1.2607 -0.0269 -0.0218 -0.1129 429 GLU A OE1 
3313 O OE2 . GLU A 429 ? 1.1182 1.1070 1.5194 -0.0373 0.0015  -0.1258 429 GLU A OE2 
3314 N N   . GLY A 430 ? 0.6258 0.6221 0.8541 -0.0376 -0.0211 -0.0914 430 GLY A N   
3315 C CA  . GLY A 430 ? 0.5313 0.5278 0.7399 -0.0325 -0.0296 -0.0843 430 GLY A CA  
3316 C C   . GLY A 430 ? 0.4993 0.4995 0.6874 -0.0355 -0.0280 -0.0793 430 GLY A C   
3317 O O   . GLY A 430 ? 0.5145 0.5179 0.7051 -0.0383 -0.0255 -0.0803 430 GLY A O   
3318 N N   . ILE A 431 ? 0.4575 0.4574 0.6280 -0.0348 -0.0291 -0.0730 431 ILE A N   
3319 C CA  . ILE A 431 ? 0.4213 0.4251 0.5768 -0.0373 -0.0278 -0.0666 431 ILE A CA  
3320 C C   . ILE A 431 ? 0.3720 0.3735 0.5162 -0.0299 -0.0341 -0.0622 431 ILE A C   
3321 O O   . ILE A 431 ? 0.4177 0.4147 0.5570 -0.0265 -0.0370 -0.0612 431 ILE A O   
3322 C CB  . ILE A 431 ? 0.4352 0.4409 0.5808 -0.0467 -0.0205 -0.0629 431 ILE A CB  
3323 C CG1 . ILE A 431 ? 0.3344 0.3399 0.4870 -0.0560 -0.0125 -0.0685 431 ILE A CG1 
3324 C CG2 . ILE A 431 ? 0.5779 0.5890 0.7130 -0.0492 -0.0211 -0.0543 431 ILE A CG2 
3325 C CD1 . ILE A 431 ? 0.5598 0.5658 0.6990 -0.0680 -0.0056 -0.0660 431 ILE A CD1 
3326 N N   . ILE A 432 ? 0.3485 0.3521 0.4888 -0.0280 -0.0351 -0.0595 432 ILE A N   
3327 C CA  . ILE A 432 ? 0.3795 0.3789 0.5088 -0.0220 -0.0386 -0.0572 432 ILE A CA  
3328 C C   . ILE A 432 ? 0.5237 0.5267 0.6470 -0.0241 -0.0333 -0.0496 432 ILE A C   
3329 O O   . ILE A 432 ? 0.5151 0.5238 0.6461 -0.0277 -0.0303 -0.0468 432 ILE A O   
3330 C CB  . ILE A 432 ? 0.4497 0.4463 0.5830 -0.0175 -0.0436 -0.0627 432 ILE A CB  
3331 C CG1 . ILE A 432 ? 0.4045 0.3990 0.5484 -0.0158 -0.0504 -0.0691 432 ILE A CG1 
3332 C CG2 . ILE A 432 ? 0.3686 0.3585 0.4863 -0.0133 -0.0452 -0.0616 432 ILE A CG2 
3333 C CD1 . ILE A 432 ? 0.3500 0.3425 0.4994 -0.0130 -0.0566 -0.0750 432 ILE A CD1 
3334 N N   . PHE A 433 ? 0.3993 0.3988 0.5110 -0.0221 -0.0324 -0.0454 433 PHE A N   
3335 C CA  . PHE A 433 ? 0.3726 0.3746 0.4820 -0.0230 -0.0274 -0.0380 433 PHE A CA  
3336 C C   . PHE A 433 ? 0.3521 0.3462 0.4531 -0.0171 -0.0261 -0.0394 433 PHE A C   
3337 O O   . PHE A 433 ? 0.5092 0.4952 0.6003 -0.0133 -0.0306 -0.0449 433 PHE A O   
3338 C CB  . PHE A 433 ? 0.4999 0.5037 0.6037 -0.0267 -0.0250 -0.0321 433 PHE A CB  
3339 C CG  . PHE A 433 ? 0.4025 0.4129 0.5110 -0.0352 -0.0244 -0.0310 433 PHE A CG  
3340 C CD1 . PHE A 433 ? 0.4222 0.4406 0.5384 -0.0413 -0.0235 -0.0262 433 PHE A CD1 
3341 C CD2 . PHE A 433 ? 0.3706 0.3783 0.4756 -0.0378 -0.0242 -0.0345 433 PHE A CD2 
3342 C CE1 . PHE A 433 ? 0.3761 0.3988 0.4915 -0.0512 -0.0227 -0.0254 433 PHE A CE1 
3343 C CE2 . PHE A 433 ? 0.3437 0.3553 0.4503 -0.0473 -0.0216 -0.0351 433 PHE A CE2 
3344 C CZ  . PHE A 433 ? 0.4004 0.4191 0.5098 -0.0546 -0.0210 -0.0308 433 PHE A CZ  
3345 N N   . GLY A 434 ? 0.4637 0.4596 0.5691 -0.0171 -0.0199 -0.0340 434 GLY A N   
3346 C CA  . GLY A 434 ? 0.3643 0.3509 0.4614 -0.0129 -0.0151 -0.0360 434 GLY A CA  
3347 C C   . GLY A 434 ? 0.3615 0.3515 0.4742 -0.0130 -0.0072 -0.0317 434 GLY A C   
3348 O O   . GLY A 434 ? 0.3878 0.3876 0.5179 -0.0159 -0.0077 -0.0270 434 GLY A O   
3349 N N   . GLY A 435 ? 0.3741 0.3551 0.4807 -0.0103 0.0008  -0.0331 435 GLY A N   
3350 C CA  . GLY A 435 ? 0.5198 0.5017 0.6444 -0.0097 0.0107  -0.0297 435 GLY A CA  
3351 C C   . GLY A 435 ? 0.4984 0.4652 0.6100 -0.0072 0.0205  -0.0367 435 GLY A C   
3352 O O   . GLY A 435 ? 0.6436 0.5994 0.7295 -0.0067 0.0174  -0.0441 435 GLY A O   
3353 N N   . ARG A 436 ? 0.5549 0.5207 0.6851 -0.0066 0.0328  -0.0340 436 ARG A N   
3354 C CA  . ARG A 436 ? 0.6477 0.5975 0.7674 -0.0056 0.0462  -0.0416 436 ARG A CA  
3355 C C   . ARG A 436 ? 0.7350 0.6779 0.8412 -0.0056 0.0528  -0.0382 436 ARG A C   
3356 O O   . ARG A 436 ? 0.8256 0.7721 0.9523 -0.0052 0.0626  -0.0300 436 ARG A O   
3357 C CB  . ARG A 436 ? 0.6688 0.6194 0.8185 -0.0049 0.0591  -0.0402 436 ARG A CB  
3358 C CG  . ARG A 436 ? 0.6659 0.6189 0.8260 -0.0050 0.0554  -0.0458 436 ARG A CG  
3359 C CD  . ARG A 436 ? 0.7759 0.7287 0.9689 -0.0041 0.0699  -0.0436 436 ARG A CD  
3360 N NE  . ARG A 436 ? 0.7140 0.6671 0.9165 -0.0043 0.0681  -0.0501 436 ARG A NE  
3361 C CZ  . ARG A 436 ? 0.6589 0.5976 0.8488 -0.0053 0.0752  -0.0646 436 ARG A CZ  
3362 N NH1 . ARG A 436 ? 0.6872 0.6088 0.8512 -0.0069 0.0849  -0.0743 436 ARG A NH1 
3363 N NH2 . ARG A 436 ? 0.5446 0.4852 0.7466 -0.0056 0.0729  -0.0696 436 ARG A NH2 
3364 N N   . ARG A 437 ? 0.6886 0.6217 0.7619 -0.0061 0.0470  -0.0435 437 ARG A N   
3365 C CA  . ARG A 437 ? 0.7095 0.6333 0.7656 -0.0063 0.0538  -0.0412 437 ARG A CA  
3366 C C   . ARG A 437 ? 0.7459 0.6485 0.7718 -0.0081 0.0627  -0.0518 437 ARG A C   
3367 O O   . ARG A 437 ? 0.8396 0.7347 0.8385 -0.0096 0.0521  -0.0587 437 ARG A O   
3368 C CB  . ARG A 437 ? 0.6842 0.6128 0.7262 -0.0063 0.0404  -0.0368 437 ARG A CB  
3369 C CG  . ARG A 437 ? 0.6383 0.5851 0.7052 -0.0066 0.0345  -0.0267 437 ARG A CG  
3370 C CD  . ARG A 437 ? 0.7652 0.7168 0.8559 -0.0069 0.0464  -0.0181 437 ARG A CD  
3371 N NE  . ARG A 437 ? 0.6984 0.6387 0.7754 -0.0066 0.0565  -0.0172 437 ARG A NE  
3372 C CZ  . ARG A 437 ? 0.5978 0.5416 0.6724 -0.0074 0.0542  -0.0107 437 ARG A CZ  
3373 N NH1 . ARG A 437 ? 0.5782 0.5360 0.6619 -0.0093 0.0425  -0.0053 437 ARG A NH1 
3374 N NH2 . ARG A 437 ? 0.5939 0.5258 0.6559 -0.0071 0.0650  -0.0103 437 ARG A NH2 
3375 N N   . PRO A 438 ? 0.8347 0.7264 0.8639 -0.0090 0.0819  -0.0535 438 PRO A N   
3376 C CA  . PRO A 438 ? 0.9259 0.7952 0.9236 -0.0129 0.0924  -0.0655 438 PRO A CA  
3377 C C   . PRO A 438 ? 0.9109 0.7662 0.8668 -0.0155 0.0885  -0.0666 438 PRO A C   
3378 O O   . PRO A 438 ? 1.0290 0.8675 0.9501 -0.0203 0.0878  -0.0762 438 PRO A O   
3379 C CB  . PRO A 438 ? 0.9230 0.7857 0.9431 -0.0131 0.1169  -0.0660 438 PRO A CB  
3380 C CG  . PRO A 438 ? 0.8148 0.6935 0.8667 -0.0095 0.1173  -0.0518 438 PRO A CG  
3381 C CD  . PRO A 438 ? 0.8017 0.7007 0.8655 -0.0074 0.0955  -0.0447 438 PRO A CD  
3382 N N   . ALA A 439 ? 0.8808 0.7418 0.8382 -0.0134 0.0855  -0.0568 439 ALA A N   
3383 C CA  . ALA A 439 ? 0.9246 0.7718 0.8445 -0.0158 0.0828  -0.0561 439 ALA A CA  
3384 C C   . ALA A 439 ? 0.8546 0.7150 0.7838 -0.0125 0.0715  -0.0450 439 ALA A C   
3385 O O   . ALA A 439 ? 0.7306 0.6061 0.6925 -0.0098 0.0742  -0.0376 439 ALA A O   
3386 C CB  . ALA A 439 ? 0.9087 0.7365 0.8133 -0.0192 0.1057  -0.0591 439 ALA A CB  
3387 N N   . GLY A 440 ? 1.0400 0.8943 0.9407 -0.0134 0.0587  -0.0436 440 GLY A N   
3388 C CA  . GLY A 440 ? 0.7924 0.6561 0.6998 -0.0109 0.0497  -0.0341 440 GLY A CA  
3389 C C   . GLY A 440 ? 0.8493 0.7255 0.7640 -0.0091 0.0293  -0.0330 440 GLY A C   
3390 O O   . GLY A 440 ? 0.8227 0.6952 0.7212 -0.0090 0.0180  -0.0297 440 GLY A O   
3391 N N   . VAL A 441 ? 0.7975 0.6880 0.7382 -0.0078 0.0253  -0.0351 441 VAL A N   
3392 C CA  . VAL A 441 ? 0.8156 0.7183 0.7676 -0.0065 0.0089  -0.0347 441 VAL A CA  
3393 C C   . VAL A 441 ? 0.8339 0.7279 0.7647 -0.0077 -0.0032 -0.0409 441 VAL A C   
3394 O O   . VAL A 441 ? 0.7724 0.6595 0.6950 -0.0097 -0.0001 -0.0485 441 VAL A O   
3395 C CB  . VAL A 441 ? 0.7375 0.6565 0.7213 -0.0060 0.0093  -0.0350 441 VAL A CB  
3396 C CG1 . VAL A 441 ? 0.7178 0.6473 0.7119 -0.0056 -0.0052 -0.0357 441 VAL A CG1 
3397 C CG2 . VAL A 441 ? 0.6923 0.6205 0.6971 -0.0062 0.0186  -0.0273 441 VAL A CG2 
3398 N N   . PRO A 442 ? 0.8646 0.7585 0.7880 -0.0070 -0.0172 -0.0377 442 PRO A N   
3399 C CA  . PRO A 442 ? 0.8575 0.7449 0.7648 -0.0086 -0.0315 -0.0419 442 PRO A CA  
3400 C C   . PRO A 442 ? 0.7374 0.6353 0.6654 -0.0082 -0.0374 -0.0485 442 PRO A C   
3401 O O   . PRO A 442 ? 0.6694 0.5801 0.6239 -0.0066 -0.0321 -0.0486 442 PRO A O   
3402 C CB  . PRO A 442 ? 0.8287 0.7172 0.7353 -0.0070 -0.0443 -0.0344 442 PRO A CB  
3403 C CG  . PRO A 442 ? 0.7015 0.6022 0.6330 -0.0044 -0.0377 -0.0295 442 PRO A CG  
3404 C CD  . PRO A 442 ? 0.7818 0.6816 0.7141 -0.0052 -0.0205 -0.0298 442 PRO A CD  
3405 N N   . LEU A 443 ? 0.8454 0.7371 0.7600 -0.0105 -0.0493 -0.0536 443 LEU A N   
3406 C CA  . LEU A 443 ? 0.7506 0.6503 0.6834 -0.0106 -0.0545 -0.0607 443 LEU A CA  
3407 C C   . LEU A 443 ? 0.6406 0.5569 0.6063 -0.0072 -0.0599 -0.0578 443 LEU A C   
3408 O O   . LEU A 443 ? 0.5466 0.4727 0.5342 -0.0066 -0.0552 -0.0613 443 LEU A O   
3409 C CB  . LEU A 443 ? 0.7938 0.6846 0.7073 -0.0144 -0.0692 -0.0656 443 LEU A CB  
3410 C CG  . LEU A 443 ? 0.7185 0.6158 0.6491 -0.0152 -0.0747 -0.0741 443 LEU A CG  
3411 C CD1 . LEU A 443 ? 0.6474 0.5419 0.5796 -0.0167 -0.0584 -0.0818 443 LEU A CD1 
3412 C CD2 . LEU A 443 ? 0.8367 0.7265 0.7499 -0.0196 -0.0928 -0.0772 443 LEU A CD2 
3413 N N   . VAL A 444 ? 0.6132 0.5319 0.5828 -0.0055 -0.0686 -0.0515 444 VAL A N   
3414 C CA  . VAL A 444 ? 0.5804 0.5124 0.5798 -0.0036 -0.0720 -0.0501 444 VAL A CA  
3415 C C   . VAL A 444 ? 0.5773 0.5084 0.5776 -0.0020 -0.0757 -0.0424 444 VAL A C   
3416 O O   . VAL A 444 ? 0.7609 0.6828 0.7445 -0.0020 -0.0847 -0.0382 444 VAL A O   
3417 C CB  . VAL A 444 ? 0.6070 0.5435 0.6215 -0.0037 -0.0837 -0.0557 444 VAL A CB  
3418 C CG1 . VAL A 444 ? 0.6115 0.5396 0.6120 -0.0044 -0.0998 -0.0538 444 VAL A CG1 
3419 C CG2 . VAL A 444 ? 0.4859 0.4346 0.5314 -0.0026 -0.0835 -0.0554 444 VAL A CG2 
3420 N N   . TYR A 445 ? 0.4566 0.3967 0.4762 -0.0016 -0.0688 -0.0402 445 TYR A N   
3421 C CA  . TYR A 445 ? 0.5954 0.5355 0.6224 -0.0006 -0.0709 -0.0344 445 TYR A CA  
3422 C C   . TYR A 445 ? 0.6460 0.5972 0.7007 -0.0019 -0.0668 -0.0370 445 TYR A C   
3423 O O   . TYR A 445 ? 0.5385 0.4970 0.6029 -0.0039 -0.0620 -0.0417 445 TYR A O   
3424 C CB  . TYR A 445 ? 0.5528 0.4870 0.5636 -0.0007 -0.0624 -0.0282 445 TYR A CB  
3425 C CG  . TYR A 445 ? 0.5662 0.5066 0.5812 -0.0027 -0.0488 -0.0285 445 TYR A CG  
3426 C CD1 . TYR A 445 ? 0.5740 0.5120 0.5779 -0.0033 -0.0416 -0.0302 445 TYR A CD1 
3427 C CD2 . TYR A 445 ? 0.6551 0.6034 0.6862 -0.0048 -0.0432 -0.0269 445 TYR A CD2 
3428 C CE1 . TYR A 445 ? 0.6241 0.5687 0.6365 -0.0052 -0.0307 -0.0285 445 TYR A CE1 
3429 C CE2 . TYR A 445 ? 0.5697 0.5243 0.6048 -0.0079 -0.0333 -0.0257 445 TYR A CE2 
3430 C CZ  . TYR A 445 ? 0.6290 0.5825 0.6565 -0.0076 -0.0279 -0.0256 445 TYR A CZ  
3431 O OH  . TYR A 445 ? 0.5197 0.4805 0.5557 -0.0106 -0.0196 -0.0226 445 TYR A OH  
3432 N N   . GLU A 446 ? 0.6963 0.6475 0.7633 -0.0014 -0.0680 -0.0338 446 GLU A N   
3433 C CA  . GLU A 446 ? 0.6537 0.6125 0.7460 -0.0038 -0.0632 -0.0374 446 GLU A CA  
3434 C C   . GLU A 446 ? 0.5819 0.5410 0.6751 -0.0065 -0.0531 -0.0344 446 GLU A C   
3435 O O   . GLU A 446 ? 0.4514 0.4039 0.5347 -0.0046 -0.0535 -0.0284 446 GLU A O   
3436 C CB  . GLU A 446 ? 0.5665 0.5247 0.6802 -0.0014 -0.0726 -0.0380 446 GLU A CB  
3437 C CG  . GLU A 446 ? 0.5474 0.5113 0.6888 -0.0045 -0.0651 -0.0433 446 GLU A CG  
3438 C CD  . GLU A 446 ? 0.5775 0.5402 0.7457 -0.0016 -0.0731 -0.0428 446 GLU A CD  
3439 O OE1 . GLU A 446 ? 0.5629 0.5209 0.7270 0.0026  -0.0864 -0.0364 446 GLU A OE1 
3440 O OE2 . GLU A 446 ? 0.6394 0.6054 0.8331 -0.0042 -0.0660 -0.0483 446 GLU A OE2 
3441 N N   . ALA A 447 ? 0.6211 0.5870 0.7249 -0.0120 -0.0442 -0.0387 447 ALA A N   
3442 C CA  . ALA A 447 ? 0.6046 0.5710 0.7085 -0.0168 -0.0346 -0.0372 447 ALA A CA  
3443 C C   . ALA A 447 ? 0.6496 0.6111 0.7687 -0.0157 -0.0341 -0.0367 447 ALA A C   
3444 O O   . ALA A 447 ? 0.7538 0.7132 0.8879 -0.0119 -0.0409 -0.0374 447 ALA A O   
3445 C CB  . ALA A 447 ? 0.5382 0.5123 0.6474 -0.0250 -0.0266 -0.0420 447 ALA A CB  
3446 N N   . LEU A 448 ? 0.5873 0.5470 0.7048 -0.0195 -0.0257 -0.0350 448 LEU A N   
3447 C CA  . LEU A 448 ? 0.5484 0.5027 0.6821 -0.0190 -0.0226 -0.0344 448 LEU A CA  
3448 C C   . LEU A 448 ? 0.4907 0.4469 0.6422 -0.0270 -0.0114 -0.0429 448 LEU A C   
3449 O O   . LEU A 448 ? 0.5101 0.4616 0.6829 -0.0264 -0.0080 -0.0445 448 LEU A O   
3450 C CB  . LEU A 448 ? 0.4424 0.3915 0.5643 -0.0184 -0.0192 -0.0276 448 LEU A CB  
3451 C CG  . LEU A 448 ? 0.5521 0.4961 0.6538 -0.0117 -0.0275 -0.0192 448 LEU A CG  
3452 C CD1 . LEU A 448 ? 0.4547 0.3940 0.5452 -0.0124 -0.0212 -0.0134 448 LEU A CD1 
3453 C CD2 . LEU A 448 ? 0.6529 0.5914 0.7614 -0.0049 -0.0395 -0.0147 448 LEU A CD2 
3454 N N   . SER A 449 ? 0.4785 0.4404 0.6219 -0.0353 -0.0053 -0.0481 449 SER A N   
3455 C CA  . SER A 449 ? 0.5003 0.4625 0.6542 -0.0455 0.0064  -0.0570 449 SER A CA  
3456 C C   . SER A 449 ? 0.4965 0.4659 0.6368 -0.0533 0.0076  -0.0598 449 SER A C   
3457 O O   . SER A 449 ? 0.4964 0.4708 0.6238 -0.0497 0.0001  -0.0545 449 SER A O   
3458 C CB  . SER A 449 ? 0.5669 0.5243 0.7209 -0.0519 0.0167  -0.0582 449 SER A CB  
3459 O OG  . SER A 449 ? 0.6030 0.5639 0.7362 -0.0557 0.0163  -0.0533 449 SER A OG  
3460 N N   . TRP A 450 ? 0.5368 0.5058 0.6803 -0.0646 0.0180  -0.0679 450 TRP A N   
3461 C CA  . TRP A 450 ? 0.5667 0.5419 0.6962 -0.0738 0.0188  -0.0691 450 TRP A CA  
3462 C C   . TRP A 450 ? 0.5906 0.5708 0.7008 -0.0790 0.0165  -0.0621 450 TRP A C   
3463 O O   . TRP A 450 ? 0.5925 0.5799 0.6929 -0.0803 0.0108  -0.0570 450 TRP A O   
3464 C CB  . TRP A 450 ? 0.5982 0.5696 0.7319 -0.0867 0.0314  -0.0795 450 TRP A CB  
3465 C CG  . TRP A 450 ? 0.6925 0.6692 0.8095 -0.0979 0.0318  -0.0796 450 TRP A CG  
3466 C CD1 . TRP A 450 ? 0.7817 0.7596 0.8796 -0.1127 0.0359  -0.0794 450 TRP A CD1 
3467 C CD2 . TRP A 450 ? 0.7181 0.6996 0.8361 -0.0959 0.0270  -0.0788 450 TRP A CD2 
3468 N NE1 . TRP A 450 ? 0.8318 0.8150 0.9185 -0.1201 0.0332  -0.0773 450 TRP A NE1 
3469 C CE2 . TRP A 450 ? 0.7832 0.7685 0.8827 -0.1096 0.0286  -0.0771 450 TRP A CE2 
3470 C CE3 . TRP A 450 ? 0.7148 0.6977 0.8479 -0.0846 0.0211  -0.0791 450 TRP A CE3 
3471 C CZ2 . TRP A 450 ? 0.7337 0.7237 0.8303 -0.1116 0.0252  -0.0750 450 TRP A CZ2 
3472 C CZ3 . TRP A 450 ? 0.6726 0.6602 0.8032 -0.0866 0.0186  -0.0785 450 TRP A CZ3 
3473 C CH2 . TRP A 450 ? 0.7438 0.7347 0.8568 -0.0996 0.0210  -0.0762 450 TRP A CH2 
3474 N N   . GLN A 451 ? 0.6735 0.6501 0.7808 -0.0820 0.0210  -0.0613 451 GLN A N   
3475 C CA  . GLN A 451 ? 0.5092 0.4909 0.6019 -0.0870 0.0186  -0.0543 451 GLN A CA  
3476 C C   . GLN A 451 ? 0.5297 0.5150 0.6197 -0.0748 0.0094  -0.0446 451 GLN A C   
3477 O O   . GLN A 451 ? 0.5409 0.5336 0.6237 -0.0766 0.0047  -0.0384 451 GLN A O   
3478 C CB  . GLN A 451 ? 0.5610 0.5371 0.6535 -0.0930 0.0264  -0.0565 451 GLN A CB  
3479 C CG  . GLN A 451 ? 0.6614 0.6338 0.7502 -0.1095 0.0372  -0.0664 451 GLN A CG  
3480 C CD  . GLN A 451 ? 0.7833 0.7483 0.8869 -0.1091 0.0455  -0.0767 451 GLN A CD  
3481 O OE1 . GLN A 451 ? 0.5943 0.5557 0.7156 -0.0963 0.0438  -0.0762 451 GLN A OE1 
3482 N NE2 . GLN A 451 ? 0.7952 0.7577 0.8921 -0.1239 0.0544  -0.0856 451 GLN A NE2 
3483 N N   . HIS A 452 ? 0.5593 0.5386 0.6553 -0.0631 0.0070  -0.0429 452 HIS A N   
3484 C CA  . HIS A 452 ? 0.4271 0.4071 0.5170 -0.0528 -0.0001 -0.0353 452 HIS A CA  
3485 C C   . HIS A 452 ? 0.5704 0.5554 0.6595 -0.0498 -0.0059 -0.0351 452 HIS A C   
3486 O O   . HIS A 452 ? 0.4999 0.4877 0.5827 -0.0457 -0.0092 -0.0294 452 HIS A O   
3487 C CB  . HIS A 452 ? 0.4910 0.4622 0.5844 -0.0426 -0.0026 -0.0335 452 HIS A CB  
3488 C CG  . HIS A 452 ? 0.5789 0.5481 0.6620 -0.0335 -0.0090 -0.0272 452 HIS A CG  
3489 N ND1 . HIS A 452 ? 0.4509 0.4177 0.5341 -0.0263 -0.0166 -0.0279 452 HIS A ND1 
3490 C CD2 . HIS A 452 ? 0.6100 0.5783 0.6819 -0.0315 -0.0079 -0.0208 452 HIS A CD2 
3491 C CE1 . HIS A 452 ? 0.4667 0.4302 0.5362 -0.0211 -0.0195 -0.0229 452 HIS A CE1 
3492 N NE2 . HIS A 452 ? 0.5850 0.5490 0.6482 -0.0237 -0.0134 -0.0185 452 HIS A NE2 
3493 N N   . GLY A 453 ? 0.6380 0.6237 0.7353 -0.0517 -0.0059 -0.0416 453 GLY A N   
3494 C CA  . GLY A 453 ? 0.6108 0.6014 0.7088 -0.0498 -0.0105 -0.0418 453 GLY A CA  
3495 C C   . GLY A 453 ? 0.6285 0.6274 0.7202 -0.0575 -0.0100 -0.0373 453 GLY A C   
3496 O O   . GLY A 453 ? 0.6239 0.6265 0.7142 -0.0534 -0.0139 -0.0324 453 GLY A O   
3497 N N   . VAL A 454 ? 0.6165 0.6176 0.7048 -0.0696 -0.0052 -0.0385 454 VAL A N   
3498 C CA  . VAL A 454 ? 0.5106 0.5202 0.5930 -0.0785 -0.0070 -0.0319 454 VAL A CA  
3499 C C   . VAL A 454 ? 0.5118 0.5247 0.5931 -0.0740 -0.0099 -0.0226 454 VAL A C   
3500 O O   . VAL A 454 ? 0.5585 0.5786 0.6423 -0.0748 -0.0135 -0.0149 454 VAL A O   
3501 C CB  . VAL A 454 ? 0.6160 0.6258 0.6909 -0.0944 -0.0020 -0.0352 454 VAL A CB  
3502 C CG1 . VAL A 454 ? 0.5776 0.5967 0.6458 -0.1048 -0.0068 -0.0260 454 VAL A CG1 
3503 C CG2 . VAL A 454 ? 0.5081 0.5130 0.5849 -0.0995 0.0036  -0.0453 454 VAL A CG2 
3504 N N   . PHE A 455 ? 0.4832 0.4903 0.5629 -0.0693 -0.0074 -0.0226 455 PHE A N   
3505 C CA  . PHE A 455 ? 0.4682 0.4767 0.5475 -0.0646 -0.0080 -0.0145 455 PHE A CA  
3506 C C   . PHE A 455 ? 0.5309 0.5385 0.6124 -0.0540 -0.0105 -0.0119 455 PHE A C   
3507 O O   . PHE A 455 ? 0.4962 0.5082 0.5817 -0.0528 -0.0105 -0.0047 455 PHE A O   
3508 C CB  . PHE A 455 ? 0.3941 0.3947 0.4704 -0.0614 -0.0040 -0.0154 455 PHE A CB  
3509 C CG  . PHE A 455 ? 0.5537 0.5532 0.6291 -0.0555 -0.0027 -0.0081 455 PHE A CG  
3510 C CD1 . PHE A 455 ? 0.4910 0.4972 0.5701 -0.0620 -0.0016 -0.0012 455 PHE A CD1 
3511 C CD2 . PHE A 455 ? 0.5339 0.5249 0.6045 -0.0445 -0.0024 -0.0078 455 PHE A CD2 
3512 C CE1 . PHE A 455 ? 0.5426 0.5471 0.6238 -0.0567 0.0015  0.0052  455 PHE A CE1 
3513 C CE2 . PHE A 455 ? 0.5330 0.5210 0.6010 -0.0401 0.0011  -0.0019 455 PHE A CE2 
3514 C CZ  . PHE A 455 ? 0.4798 0.4745 0.5548 -0.0458 0.0040  0.0043  455 PHE A CZ  
3515 N N   . VAL A 456 ? 0.5164 0.5180 0.5970 -0.0468 -0.0123 -0.0179 456 VAL A N   
3516 C CA  . VAL A 456 ? 0.4478 0.4470 0.5279 -0.0382 -0.0144 -0.0173 456 VAL A CA  
3517 C C   . VAL A 456 ? 0.4339 0.4418 0.5221 -0.0413 -0.0155 -0.0138 456 VAL A C   
3518 O O   . VAL A 456 ? 0.4582 0.4668 0.5497 -0.0376 -0.0139 -0.0092 456 VAL A O   
3519 C CB  . VAL A 456 ? 0.5667 0.5591 0.6453 -0.0321 -0.0183 -0.0244 456 VAL A CB  
3520 C CG1 . VAL A 456 ? 0.5078 0.4977 0.5842 -0.0256 -0.0207 -0.0251 456 VAL A CG1 
3521 C CG2 . VAL A 456 ? 0.5464 0.5302 0.6192 -0.0284 -0.0184 -0.0249 456 VAL A CG2 
3522 N N   . GLY A 457 ? 0.5101 0.5236 0.6024 -0.0486 -0.0172 -0.0158 457 GLY A N   
3523 C CA  . GLY A 457 ? 0.4715 0.4931 0.5719 -0.0522 -0.0189 -0.0110 457 GLY A CA  
3524 C C   . GLY A 457 ? 0.5167 0.5459 0.6227 -0.0570 -0.0190 0.0000  457 GLY A C   
3525 O O   . GLY A 457 ? 0.4378 0.4719 0.5550 -0.0553 -0.0195 0.0066  457 GLY A O   
3526 N N   . ALA A 458 ? 0.4604 0.4908 0.5616 -0.0635 -0.0183 0.0024  458 ALA A N   
3527 C CA  . ALA A 458 ? 0.4399 0.4784 0.5488 -0.0691 -0.0197 0.0134  458 ALA A CA  
3528 C C   . ALA A 458 ? 0.4486 0.4844 0.5653 -0.0598 -0.0154 0.0178  458 ALA A C   
3529 O O   . ALA A 458 ? 0.4483 0.4914 0.5789 -0.0622 -0.0159 0.0280  458 ALA A O   
3530 C CB  . ALA A 458 ? 0.5314 0.5713 0.6324 -0.0799 -0.0201 0.0135  458 ALA A CB  
3531 N N   . ALA A 459 ? 0.4641 0.4890 0.5724 -0.0502 -0.0111 0.0108  459 ALA A N   
3532 C CA  . ALA A 459 ? 0.4413 0.4604 0.5518 -0.0425 -0.0049 0.0134  459 ALA A CA  
3533 C C   . ALA A 459 ? 0.4332 0.4478 0.5468 -0.0348 -0.0021 0.0108  459 ALA A C   
3534 O O   . ALA A 459 ? 0.4251 0.4297 0.5323 -0.0282 0.0041  0.0084  459 ALA A O   
3535 C CB  . ALA A 459 ? 0.4356 0.4439 0.5310 -0.0386 -0.0016 0.0085  459 ALA A CB  
3536 N N   . MET A 460 ? 0.4673 0.4878 0.5894 -0.0365 -0.0059 0.0108  460 MET A N   
3537 C CA  . MET A 460 ? 0.4714 0.4874 0.5979 -0.0302 -0.0028 0.0074  460 MET A CA  
3538 C C   . MET A 460 ? 0.5581 0.5761 0.7029 -0.0282 0.0045  0.0152  460 MET A C   
3539 O O   . MET A 460 ? 0.5206 0.5493 0.6835 -0.0333 0.0029  0.0258  460 MET A O   
3540 C CB  . MET A 460 ? 0.3905 0.4125 0.5233 -0.0329 -0.0083 0.0056  460 MET A CB  
3541 C CG  . MET A 460 ? 0.4156 0.4344 0.5348 -0.0340 -0.0133 -0.0034 460 MET A CG  
3542 S SD  . MET A 460 ? 0.4280 0.4527 0.5558 -0.0377 -0.0176 -0.0055 460 MET A SD  
3543 C CE  . MET A 460 ? 0.4105 0.4311 0.5482 -0.0297 -0.0134 -0.0075 460 MET A CE  
3544 N N   . ARG A 461 ? 0.6372 0.6442 0.7781 -0.0216 0.0127  0.0098  461 ARG A N   
3545 C CA  . ARG A 461 ? 0.5148 0.5209 0.6752 -0.0191 0.0231  0.0150  461 ARG A CA  
3546 C C   . ARG A 461 ? 0.5635 0.5600 0.7219 -0.0144 0.0293  0.0064  461 ARG A C   
3547 O O   . ARG A 461 ? 0.7264 0.7141 0.8625 -0.0124 0.0263  -0.0039 461 ARG A O   
3548 C CB  . ARG A 461 ? 0.4745 0.4731 0.6301 -0.0175 0.0323  0.0167  461 ARG A CB  
3549 C CG  . ARG A 461 ? 0.5678 0.5756 0.7281 -0.0226 0.0273  0.0250  461 ARG A CG  
3550 C CD  . ARG A 461 ? 0.4496 0.4487 0.6051 -0.0205 0.0375  0.0259  461 ARG A CD  
3551 N NE  . ARG A 461 ? 0.4810 0.4777 0.6591 -0.0179 0.0505  0.0302  461 ARG A NE  
3552 C CZ  . ARG A 461 ? 0.5875 0.5740 0.7639 -0.0156 0.0635  0.0299  461 ARG A CZ  
3553 N NH1 . ARG A 461 ? 0.6465 0.6241 0.7983 -0.0154 0.0645  0.0265  461 ARG A NH1 
3554 N NH2 . ARG A 461 ? 0.5921 0.5766 0.7939 -0.0137 0.0771  0.0334  461 ARG A NH2 
3555 N N   . SER A 462 ? 0.8585 0.8570 1.0425 -0.0132 0.0379  0.0111  462 SER A N   
3556 C CA  . SER A 462 ? 0.6893 0.6786 0.8748 -0.0097 0.0457  0.0026  462 SER A CA  
3557 C C   . SER A 462 ? 0.8208 0.8095 1.0372 -0.0082 0.0600  0.0085  462 SER A C   
3558 O O   . SER A 462 ? 0.7773 0.7775 1.0209 -0.0100 0.0598  0.0217  462 SER A O   
3559 C CB  . SER A 462 ? 0.6416 0.6378 0.8317 -0.0109 0.0362  0.0006  462 SER A CB  
3560 O OG  . SER A 462 ? 0.5810 0.5686 0.7759 -0.0081 0.0443  -0.0075 462 SER A OG  
3561 N N   . GLU A 463 ? 0.8561 0.8309 1.0694 -0.0054 0.0727  -0.0015 463 GLU A N   
3562 C CA  . GLU A 463 ? 0.9765 0.9482 1.2217 -0.0038 0.0896  0.0018  463 GLU A CA  
3563 C C   . GLU A 463 ? 1.0413 1.0256 1.3226 -0.0038 0.0862  0.0100  463 GLU A C   
3564 O O   . GLU A 463 ? 0.9989 0.9872 1.2729 -0.0046 0.0757  0.0067  463 GLU A O   
3565 C CB  . GLU A 463 ? 0.9882 0.9382 1.2141 -0.0025 0.1062  -0.0136 463 GLU A CB  
3566 C CG  . GLU A 463 ? 0.9913 0.9343 1.1949 -0.0029 0.1005  -0.0266 463 GLU A CG  
3567 C CD  . GLU A 463 ? 1.1117 1.0320 1.2901 -0.0040 0.1156  -0.0423 463 GLU A CD  
3568 O OE1 . GLU A 463 ? 1.1606 1.0694 1.3378 -0.0044 0.1323  -0.0435 463 GLU A OE1 
3569 O OE2 . GLU A 463 ? 1.1536 1.0668 1.3127 -0.0053 0.1111  -0.0538 463 GLU A OE2 
3570 N N   . ALA A 464 ? 1.2275 1.2178 1.5503 -0.0031 0.0955  0.0217  464 ALA A N   
3571 C CA  . ALA A 464 ? 1.4111 1.4138 1.7727 -0.0033 0.0921  0.0327  464 ALA A CA  
3572 C C   . ALA A 464 ? 1.5577 1.5495 1.9198 -0.0010 0.1014  0.0203  464 ALA A C   
3573 O O   . ALA A 464 ? 1.5990 1.5737 1.9562 0.0009  0.1196  0.0081  464 ALA A O   
3574 C CB  . ALA A 464 ? 1.4914 1.5019 1.9018 -0.0027 0.1009  0.0484  464 ALA A CB  
3575 N N   . THR A 465 ? 1.7857 1.7862 2.1526 -0.0022 0.0897  0.0229  465 THR A N   
3576 C CA  . THR A 465 ? 1.8954 1.8869 2.2645 -0.0005 0.0969  0.0116  465 THR A CA  
3577 C C   . THR A 465 ? 1.9782 1.9776 2.3987 0.0007  0.1032  0.0240  465 THR A C   
3578 O O   . THR A 465 ? 2.0422 2.0474 2.4987 0.0015  0.1100  0.0375  465 THR A O   
3579 C CB  . THR A 465 ? 1.7745 1.7686 2.1145 -0.0024 0.0811  0.0043  465 THR A CB  
3580 O OG1 . THR A 465 ? 1.6922 1.7043 2.0464 -0.0054 0.0655  0.0199  465 THR A OG1 
3581 C CG2 . THR A 465 ? 1.7084 1.6950 2.0025 -0.0032 0.0746  -0.0068 465 THR A CG2 
3582 N N   . ALA A 466 ? 1.7753 1.7749 2.2022 0.0008  0.1011  0.0204  466 ALA A N   
3583 C CA  . ALA A 466 ? 1.5864 1.5929 2.0628 0.0021  0.1065  0.0328  466 ALA A CA  
3584 C C   . ALA A 466 ? 1.4428 1.4644 1.9238 -0.0010 0.0879  0.0446  466 ALA A C   
3585 O O   . ALA A 466 ? 1.2840 1.3045 1.7797 -0.0003 0.0902  0.0427  466 ALA A O   
3586 C CB  . ALA A 466 ? 1.5123 1.5023 1.9988 0.0047  0.1264  0.0172  466 ALA A CB  
3587 N N   . ALA A 467 ? 1.4061 1.4408 1.8735 -0.0052 0.0705  0.0563  467 ALA A N   
3588 C CA  . ALA A 467 ? 1.2042 1.2519 1.6703 -0.0103 0.0532  0.0675  467 ALA A CA  
3589 C C   . ALA A 467 ? 1.2393 1.3038 1.7393 -0.0145 0.0437  0.0935  467 ALA A C   
3590 O O   . ALA A 467 ? 1.1567 1.2294 1.6797 -0.0170 0.0376  0.1068  467 ALA A O   
3591 C CB  . ALA A 467 ? 1.0728 1.1208 1.4913 -0.0141 0.0401  0.0586  467 ALA A CB  
3592 N N   . ALA A 468 ? 1.3402 1.4098 1.8439 -0.0159 0.0416  0.1019  468 ALA A N   
3593 C CA  . ALA A 468 ? 1.3397 1.4257 1.8769 -0.0208 0.0309  0.1275  468 ALA A CA  
3594 C C   . ALA A 468 ? 1.4789 1.5644 2.0675 -0.0154 0.0457  0.1364  468 ALA A C   
3595 O O   . ALA A 468 ? 1.5569 1.6314 2.1650 -0.0090 0.0633  0.1271  468 ALA A O   
3596 C CB  . ALA A 468 ? 1.3702 1.4640 1.8810 -0.0275 0.0170  0.1325  468 ALA A CB  
3597 N N   . GLU A 469 ? 1.4552 1.5520 2.0675 -0.0184 0.0395  0.1539  469 GLU A N   
3598 C CA  . GLU A 469 ? 1.5282 1.6255 2.1944 -0.0135 0.0537  0.1638  469 GLU A CA  
3599 C C   . GLU A 469 ? 1.5941 1.6819 2.2494 -0.0102 0.0671  0.1520  469 GLU A C   
3600 O O   . GLU A 469 ? 1.5546 1.6470 2.2514 -0.0088 0.0739  0.1640  469 GLU A O   
3601 C CB  . GLU A 469 ? 1.4595 1.5771 2.1708 -0.0192 0.0376  0.1946  469 GLU A CB  
3602 C CG  . GLU A 469 ? 1.3361 1.4663 2.0264 -0.0282 0.0175  0.2054  469 GLU A CG  
3603 C CD  . GLU A 469 ? 1.2093 1.3467 1.8586 -0.0379 -0.0043 0.2086  469 GLU A CD  
3604 O OE1 . GLU A 469 ? 1.2347 1.3651 1.8639 -0.0365 -0.0023 0.1981  469 GLU A OE1 
3605 O OE2 . GLU A 469 ? 1.0350 1.1843 1.6726 -0.0477 -0.0226 0.2212  469 GLU A OE2 
3606 N N   . HIS A 470 ? 1.6304 1.7050 2.2324 -0.0091 0.0711  0.1297  470 HIS A N   
3607 C CA  . HIS A 470 ? 1.6701 1.7335 2.2549 -0.0065 0.0839  0.1177  470 HIS A CA  
3608 C C   . HIS A 470 ? 1.6905 1.7327 2.2721 -0.0001 0.1092  0.0974  470 HIS A C   
3609 O O   . HIS A 470 ? 1.7300 1.7633 2.2920 0.0012  0.1118  0.0840  470 HIS A O   
3610 C CB  . HIS A 470 ? 1.6364 1.6985 2.1643 -0.0103 0.0712  0.1076  470 HIS A CB  
3611 C CG  . HIS A 470 ? 1.5780 1.6583 2.1015 -0.0184 0.0477  0.1241  470 HIS A CG  
3612 N ND1 . HIS A 470 ? 1.5279 1.6166 2.0402 -0.0236 0.0316  0.1294  470 HIS A ND1 
3613 C CD2 . HIS A 470 ? 1.5431 1.6336 2.0704 -0.0235 0.0381  0.1357  470 HIS A CD2 
3614 C CE1 . HIS A 470 ? 1.4275 1.5301 1.9343 -0.0323 0.0135  0.1432  470 HIS A CE1 
3615 N NE2 . HIS A 470 ? 1.3968 1.5012 1.9129 -0.0325 0.0164  0.1473  470 HIS A NE2 
3616 N N   . LYS A 471 ? 1.6798 1.7131 2.2800 0.0028  0.1282  0.0948  471 LYS A N   
3617 C CA  . LYS A 471 ? 1.7427 1.7536 2.3385 0.0069  0.1548  0.0753  471 LYS A CA  
3618 C C   . LYS A 471 ? 1.8756 1.8730 2.4404 0.0068  0.1661  0.0635  471 LYS A C   
3619 O O   . LYS A 471 ? 1.8173 1.8241 2.3803 0.0049  0.1568  0.0734  471 LYS A O   
3620 C CB  . LYS A 471 ? 1.6841 1.6938 2.3447 0.0103  0.1744  0.0836  471 LYS A CB  
3621 C CG  . LYS A 471 ? 1.5858 1.6072 2.2813 0.0106  0.1654  0.0962  471 LYS A CG  
3622 C CD  . LYS A 471 ? 1.4091 1.4281 2.1728 0.0145  0.1867  0.1043  471 LYS A CD  
3623 C CE  . LYS A 471 ? 1.1901 1.2203 1.9897 0.0149  0.1778  0.1180  471 LYS A CE  
3624 N NZ  . LYS A 471 ? 1.0663 1.0938 1.9373 0.0191  0.1994  0.1266  471 LYS A NZ  
3625 N N   . GLY A 472 ? 2.1907 2.1651 2.7295 0.0080  0.1864  0.0423  472 GLY A N   
3626 C CA  . GLY A 472 ? 2.2178 2.1761 2.7226 0.0072  0.1989  0.0300  472 GLY A CA  
3627 C C   . GLY A 472 ? 2.1831 2.1361 2.6224 0.0049  0.1837  0.0180  472 GLY A C   
3628 O O   . GLY A 472 ? 2.1605 2.1229 2.5806 0.0039  0.1633  0.0187  472 GLY A O   
3629 N N   . LYS A 473 ? 1.9864 1.9232 2.3922 0.0038  0.1949  0.0072  473 LYS A N   
3630 C CA  . LYS A 473 ? 1.8637 1.7932 2.2090 0.0017  0.1826  -0.0034 473 LYS A CA  
3631 C C   . LYS A 473 ? 1.7336 1.6739 2.0732 0.0010  0.1711  0.0077  473 LYS A C   
3632 O O   . LYS A 473 ? 1.7533 1.6813 2.0718 0.0002  0.1812  0.0030  473 LYS A O   
3633 C CB  . LYS A 473 ? 1.9525 1.8543 2.2590 -0.0005 0.2022  -0.0234 473 LYS A CB  
3634 C CG  . LYS A 473 ? 2.0770 1.9655 2.3945 -0.0011 0.2193  -0.0355 473 LYS A CG  
3635 C CD  . LYS A 473 ? 2.0814 1.9794 2.3954 -0.0007 0.2013  -0.0372 473 LYS A CD  
3636 C CE  . LYS A 473 ? 1.9222 1.8144 2.1780 -0.0033 0.1844  -0.0481 473 LYS A CE  
3637 N NZ  . LYS A 473 ? 1.8403 1.7401 2.0946 -0.0032 0.1694  -0.0514 473 LYS A NZ  
3638 N N   . VAL A 474 ? 1.3789 1.3414 1.7363 0.0005  0.1501  0.0224  474 VAL A N   
3639 C CA  . VAL A 474 ? 1.1260 1.1007 1.4812 -0.0015 0.1374  0.0336  474 VAL A CA  
3640 C C   . VAL A 474 ? 1.0195 1.0005 1.3364 -0.0037 0.1152  0.0307  474 VAL A C   
3641 O O   . VAL A 474 ? 1.0578 1.0471 1.3762 -0.0044 0.1030  0.0317  474 VAL A O   
3642 C CB  . VAL A 474 ? 0.9860 0.9813 1.3954 -0.0025 0.1317  0.0542  474 VAL A CB  
3643 C CG1 . VAL A 474 ? 0.9081 0.9165 1.3111 -0.0063 0.1161  0.0646  474 VAL A CG1 
3644 C CG2 . VAL A 474 ? 1.0523 1.0413 1.5056 0.0002  0.1552  0.0577  474 VAL A CG2 
3645 N N   . ILE A 475 ? 0.8615 0.8376 1.1459 -0.0049 0.1113  0.0273  475 ILE A N   
3646 C CA  . ILE A 475 ? 0.8262 0.8067 1.0766 -0.0069 0.0926  0.0241  475 ILE A CA  
3647 C C   . ILE A 475 ? 0.7800 0.7804 1.0488 -0.0111 0.0776  0.0388  475 ILE A C   
3648 O O   . ILE A 475 ? 0.8035 0.8061 1.0722 -0.0129 0.0777  0.0440  475 ILE A O   
3649 C CB  . ILE A 475 ? 0.6806 0.6452 0.8884 -0.0064 0.0956  0.0138  475 ILE A CB  
3650 C CG1 . ILE A 475 ? 0.7202 0.6634 0.9105 -0.0045 0.1130  0.0007  475 ILE A CG1 
3651 C CG2 . ILE A 475 ? 0.5701 0.5377 0.7472 -0.0077 0.0777  0.0091  475 ILE A CG2 
3652 C CD1 . ILE A 475 ? 0.7944 0.7205 0.9426 -0.0050 0.1168  -0.0073 475 ILE A CD1 
3653 N N   . MET A 476 ? 0.7329 0.7470 1.0160 -0.0137 0.0648  0.0453  476 MET A N   
3654 C CA  . MET A 476 ? 0.7188 0.7511 1.0157 -0.0200 0.0496  0.0591  476 MET A CA  
3655 C C   . MET A 476 ? 0.6321 0.6667 0.8958 -0.0239 0.0348  0.0535  476 MET A C   
3656 O O   . MET A 476 ? 0.6171 0.6417 0.8539 -0.0210 0.0349  0.0407  476 MET A O   
3657 C CB  . MET A 476 ? 0.8063 0.8523 1.1428 -0.0220 0.0452  0.0728  476 MET A CB  
3658 C CG  . MET A 476 ? 0.8769 0.9220 1.2089 -0.0208 0.0416  0.0674  476 MET A CG  
3659 S SD  . MET A 476 ? 1.2299 1.2896 1.6121 -0.0227 0.0382  0.0855  476 MET A SD  
3660 C CE  . MET A 476 ? 0.9492 1.0286 1.3400 -0.0332 0.0187  0.1044  476 MET A CE  
3661 N N   . HIS A 477 ? 0.5945 0.6422 0.8616 -0.0314 0.0224  0.0632  477 HIS A N   
3662 C CA  . HIS A 477 ? 0.4450 0.4948 0.6840 -0.0366 0.0106  0.0581  477 HIS A CA  
3663 C C   . HIS A 477 ? 0.5803 0.6378 0.8229 -0.0405 0.0013  0.0605  477 HIS A C   
3664 O O   . HIS A 477 ? 0.6009 0.6683 0.8710 -0.0430 -0.0017 0.0726  477 HIS A O   
3665 C CB  . HIS A 477 ? 0.6009 0.6590 0.8381 -0.0446 0.0032  0.0654  477 HIS A CB  
3666 C CG  . HIS A 477 ? 0.5393 0.5891 0.7696 -0.0413 0.0121  0.0622  477 HIS A CG  
3667 N ND1 . HIS A 477 ? 0.5939 0.6432 0.8487 -0.0380 0.0221  0.0688  477 HIS A ND1 
3668 C CD2 . HIS A 477 ? 0.5669 0.6080 0.7702 -0.0407 0.0132  0.0535  477 HIS A CD2 
3669 C CE1 . HIS A 477 ? 0.6144 0.6546 0.8549 -0.0359 0.0293  0.0640  477 HIS A CE1 
3670 N NE2 . HIS A 477 ? 0.5294 0.5647 0.7387 -0.0374 0.0235  0.0552  477 HIS A NE2 
3671 N N   . ASP A 478 ? 0.5883 0.6408 0.8047 -0.0411 -0.0030 0.0496  478 ASP A N   
3672 C CA  . ASP A 478 ? 0.5748 0.6326 0.7910 -0.0450 -0.0104 0.0499  478 ASP A CA  
3673 C C   . ASP A 478 ? 0.5794 0.6340 0.7677 -0.0492 -0.0159 0.0402  478 ASP A C   
3674 O O   . ASP A 478 ? 0.5007 0.5469 0.6759 -0.0442 -0.0140 0.0283  478 ASP A O   
3675 C CB  . ASP A 478 ? 0.5476 0.5991 0.7723 -0.0374 -0.0039 0.0440  478 ASP A CB  
3676 C CG  . ASP A 478 ? 0.4818 0.5405 0.7159 -0.0416 -0.0103 0.0485  478 ASP A CG  
3677 O OD1 . ASP A 478 ? 0.5097 0.5745 0.7329 -0.0502 -0.0193 0.0511  478 ASP A OD1 
3678 O OD2 . ASP A 478 ? 0.4883 0.5456 0.7405 -0.0369 -0.0051 0.0490  478 ASP A OD2 
3679 N N   . PRO A 479 ? 0.5757 0.6364 0.7560 -0.0589 -0.0224 0.0446  479 PRO A N   
3680 C CA  . PRO A 479 ? 0.4770 0.5330 0.6335 -0.0631 -0.0247 0.0342  479 PRO A CA  
3681 C C   . PRO A 479 ? 0.5027 0.5594 0.6554 -0.0662 -0.0278 0.0301  479 PRO A C   
3682 O O   . PRO A 479 ? 0.4571 0.5219 0.6192 -0.0729 -0.0326 0.0394  479 PRO A O   
3683 C CB  . PRO A 479 ? 0.5063 0.5690 0.6581 -0.0747 -0.0297 0.0409  479 PRO A CB  
3684 C CG  . PRO A 479 ? 0.5078 0.5821 0.6814 -0.0795 -0.0349 0.0570  479 PRO A CG  
3685 C CD  . PRO A 479 ? 0.4659 0.5376 0.6598 -0.0673 -0.0278 0.0589  479 PRO A CD  
3686 N N   . PHE A 480 ? 0.5033 0.5513 0.6435 -0.0614 -0.0253 0.0170  480 PHE A N   
3687 C CA  . PHE A 480 ? 0.3263 0.3734 0.4637 -0.0638 -0.0266 0.0111  480 PHE A CA  
3688 C C   . PHE A 480 ? 0.3997 0.4501 0.5535 -0.0604 -0.0267 0.0158  480 PHE A C   
3689 O O   . PHE A 480 ? 0.4362 0.4879 0.5909 -0.0642 -0.0281 0.0142  480 PHE A O   
3690 C CB  . PHE A 480 ? 0.4267 0.4780 0.5541 -0.0778 -0.0298 0.0131  480 PHE A CB  
3691 C CG  . PHE A 480 ? 0.5207 0.5665 0.6328 -0.0816 -0.0274 0.0050  480 PHE A CG  
3692 C CD1 . PHE A 480 ? 0.5383 0.5860 0.6463 -0.0857 -0.0281 0.0098  480 PHE A CD1 
3693 C CD2 . PHE A 480 ? 0.4485 0.4871 0.5536 -0.0813 -0.0239 -0.0071 480 PHE A CD2 
3694 C CE1 . PHE A 480 ? 0.6391 0.6811 0.7350 -0.0894 -0.0248 0.0021  480 PHE A CE1 
3695 C CE2 . PHE A 480 ? 0.6612 0.6943 0.7566 -0.0847 -0.0205 -0.0143 480 PHE A CE2 
3696 C CZ  . PHE A 480 ? 0.6252 0.6596 0.7153 -0.0888 -0.0206 -0.0099 480 PHE A CZ  
3697 N N   . ALA A 481 ? 0.5452 0.5963 0.7134 -0.0536 -0.0238 0.0212  481 ALA A N   
3698 C CA  . ALA A 481 ? 0.5806 0.6347 0.7687 -0.0507 -0.0224 0.0266  481 ALA A CA  
3699 C C   . ALA A 481 ? 0.5602 0.6248 0.7575 -0.0609 -0.0288 0.0396  481 ALA A C   
3700 O O   . ALA A 481 ? 0.5320 0.5989 0.7422 -0.0608 -0.0290 0.0431  481 ALA A O   
3701 C CB  . ALA A 481 ? 0.5283 0.5749 0.7140 -0.0443 -0.0196 0.0142  481 ALA A CB  
3702 N N   . MET A 482 ? 0.5332 0.6039 0.7230 -0.0708 -0.0344 0.0474  482 MET A N   
3703 C CA  . MET A 482 ? 0.5547 0.6345 0.7461 -0.0836 -0.0424 0.0602  482 MET A CA  
3704 C C   . MET A 482 ? 0.5489 0.6392 0.7579 -0.0883 -0.0484 0.0779  482 MET A C   
3705 O O   . MET A 482 ? 0.5288 0.6273 0.7371 -0.1010 -0.0577 0.0907  482 MET A O   
3706 C CB  . MET A 482 ? 0.4343 0.5117 0.5985 -0.0951 -0.0449 0.0535  482 MET A CB  
3707 C CG  . MET A 482 ? 0.3468 0.4171 0.5003 -0.0949 -0.0409 0.0412  482 MET A CG  
3708 S SD  . MET A 482 ? 0.4811 0.5567 0.6380 -0.1055 -0.0455 0.0518  482 MET A SD  
3709 C CE  . MET A 482 ? 0.4115 0.4911 0.5450 -0.1261 -0.0527 0.0598  482 MET A CE  
3710 N N   . ARG A 483 ? 0.5557 0.6454 0.7805 -0.0795 -0.0435 0.0795  483 ARG A N   
3711 C CA  . ARG A 483 ? 0.5779 0.6778 0.8245 -0.0835 -0.0486 0.0964  483 ARG A CA  
3712 C C   . ARG A 483 ? 0.6198 0.7304 0.8910 -0.0890 -0.0565 0.1148  483 ARG A C   
3713 O O   . ARG A 483 ? 0.6723 0.7933 0.9469 -0.1011 -0.0681 0.1299  483 ARG A O   
3714 C CB  . ARG A 483 ? 0.5313 0.6268 0.7956 -0.0714 -0.0383 0.0941  483 ARG A CB  
3715 C CG  . ARG A 483 ? 0.5935 0.6982 0.8788 -0.0753 -0.0419 0.1087  483 ARG A CG  
3716 C CD  . ARG A 483 ? 0.6068 0.7071 0.9177 -0.0636 -0.0293 0.1085  483 ARG A CD  
3717 N NE  . ARG A 483 ? 0.6180 0.7201 0.9600 -0.0581 -0.0249 0.1154  483 ARG A NE  
3718 C CZ  . ARG A 483 ? 0.6951 0.7865 1.0354 -0.0489 -0.0140 0.1033  483 ARG A CZ  
3719 N NH1 . ARG A 483 ? 0.6752 0.7539 0.9843 -0.0440 -0.0080 0.0848  483 ARG A NH1 
3720 N NH2 . ARG A 483 ? 0.8638 0.9572 1.2357 -0.0450 -0.0096 0.1104  483 ARG A NH2 
3721 N N   . PRO A 484 ? 0.5825 0.6913 0.8719 -0.0816 -0.0516 0.1152  484 PRO A N   
3722 C CA  . PRO A 484 ? 0.6186 0.7376 0.9344 -0.0868 -0.0593 0.1344  484 PRO A CA  
3723 C C   . PRO A 484 ? 0.5624 0.6840 0.8571 -0.0997 -0.0692 0.1386  484 PRO A C   
3724 O O   . PRO A 484 ? 0.5553 0.6851 0.8687 -0.1055 -0.0771 0.1562  484 PRO A O   
3725 C CB  . PRO A 484 ? 0.6346 0.7477 0.9754 -0.0735 -0.0474 0.1298  484 PRO A CB  
3726 C CG  . PRO A 484 ? 0.5241 0.6251 0.8528 -0.0625 -0.0344 0.1103  484 PRO A CG  
3727 C CD  . PRO A 484 ? 0.5259 0.6231 0.8161 -0.0681 -0.0385 0.0992  484 PRO A CD  
3728 N N   . PHE A 485 ? 0.4561 0.5704 0.7138 -0.1048 -0.0682 0.1236  485 PHE A N   
3729 C CA  . PHE A 485 ? 0.4979 0.6116 0.7341 -0.1169 -0.0736 0.1244  485 PHE A CA  
3730 C C   . PHE A 485 ? 0.4498 0.5625 0.6516 -0.1319 -0.0792 0.1209  485 PHE A C   
3731 O O   . PHE A 485 ? 0.4850 0.5922 0.6613 -0.1410 -0.0784 0.1138  485 PHE A O   
3732 C CB  . PHE A 485 ? 0.6212 0.7245 0.8494 -0.1087 -0.0634 0.1073  485 PHE A CB  
3733 C CG  . PHE A 485 ? 0.5087 0.6097 0.7660 -0.0934 -0.0553 0.1050  485 PHE A CG  
3734 C CD1 . PHE A 485 ? 0.4635 0.5706 0.7501 -0.0926 -0.0575 0.1203  485 PHE A CD1 
3735 C CD2 . PHE A 485 ? 0.5912 0.6832 0.8461 -0.0807 -0.0451 0.0878  485 PHE A CD2 
3736 C CE1 . PHE A 485 ? 0.6733 0.7769 0.9872 -0.0793 -0.0479 0.1168  485 PHE A CE1 
3737 C CE2 . PHE A 485 ? 0.6458 0.7340 0.9238 -0.0686 -0.0367 0.0843  485 PHE A CE2 
3738 C CZ  . PHE A 485 ? 0.6136 0.7072 0.9215 -0.0679 -0.0372 0.0979  485 PHE A CZ  
3739 N N   . PHE A 486 ? 0.5995 0.7167 0.8006 -0.1355 -0.0836 0.1251  486 PHE A N   
3740 C CA  . PHE A 486 ? 0.6074 0.7232 0.7766 -0.1510 -0.0882 0.1213  486 PHE A CA  
3741 C C   . PHE A 486 ? 0.6669 0.7902 0.8268 -0.1706 -0.1022 0.1389  486 PHE A C   
3742 O O   . PHE A 486 ? 0.7752 0.9101 0.9600 -0.1732 -0.1133 0.1598  486 PHE A O   
3743 C CB  . PHE A 486 ? 0.5930 0.7112 0.7658 -0.1492 -0.0885 0.1206  486 PHE A CB  
3744 C CG  . PHE A 486 ? 0.5310 0.6384 0.6965 -0.1358 -0.0754 0.1006  486 PHE A CG  
3745 C CD1 . PHE A 486 ? 0.5201 0.6170 0.6575 -0.1386 -0.0687 0.0832  486 PHE A CD1 
3746 C CD2 . PHE A 486 ? 0.4579 0.5651 0.6454 -0.1212 -0.0695 0.1000  486 PHE A CD2 
3747 C CE1 . PHE A 486 ? 0.4904 0.5780 0.6233 -0.1266 -0.0586 0.0671  486 PHE A CE1 
3748 C CE2 . PHE A 486 ? 0.4713 0.5680 0.6493 -0.1102 -0.0589 0.0833  486 PHE A CE2 
3749 C CZ  . PHE A 486 ? 0.5489 0.6364 0.7004 -0.1128 -0.0546 0.0677  486 PHE A CZ  
3750 N N   . GLY A 487 ? 0.7156 0.8319 0.8400 -0.1850 -0.1015 0.1307  487 GLY A N   
3751 C CA  . GLY A 487 ? 0.6933 0.8138 0.8008 -0.2058 -0.1139 0.1458  487 GLY A CA  
3752 C C   . GLY A 487 ? 0.8216 0.9455 0.9064 -0.2251 -0.1242 0.1510  487 GLY A C   
3753 O O   . GLY A 487 ? 0.9157 1.0468 0.9932 -0.2426 -0.1395 0.1696  487 GLY A O   
3754 N N   . TYR A 488 ? 0.8389 0.9573 0.9121 -0.2231 -0.1167 0.1354  488 TYR A N   
3755 C CA  . TYR A 488 ? 0.8621 0.9825 0.9136 -0.2416 -0.1249 0.1378  488 TYR A CA  
3756 C C   . TYR A 488 ? 0.8867 1.0075 0.9522 -0.2296 -0.1191 0.1293  488 TYR A C   
3757 O O   . TYR A 488 ? 0.8062 0.9285 0.9010 -0.2088 -0.1126 0.1275  488 TYR A O   
3758 C CB  . TYR A 488 ? 0.8677 0.9753 0.8734 -0.2608 -0.1188 0.1236  488 TYR A CB  
3759 C CG  . TYR A 488 ? 0.9240 1.0170 0.9193 -0.2502 -0.0986 0.0976  488 TYR A CG  
3760 C CD1 . TYR A 488 ? 0.8802 0.9662 0.8792 -0.2399 -0.0883 0.0891  488 TYR A CD1 
3761 C CD2 . TYR A 488 ? 0.9370 1.0235 0.9213 -0.2509 -0.0904 0.0823  488 TYR A CD2 
3762 C CE1 . TYR A 488 ? 0.8876 0.9614 0.8811 -0.2306 -0.0715 0.0669  488 TYR A CE1 
3763 C CE2 . TYR A 488 ? 0.9423 1.0160 0.9212 -0.2412 -0.0730 0.0606  488 TYR A CE2 
3764 C CZ  . TYR A 488 ? 0.8550 0.9228 0.8392 -0.2312 -0.0643 0.0533  488 TYR A CZ  
3765 O OH  . TYR A 488 ? 0.8943 0.9504 0.8771 -0.2218 -0.0486 0.0331  488 TYR A OH  
3766 N N   . ASN A 489 ? 0.8917 1.0102 0.9350 -0.2437 -0.1208 0.1237  489 ASN A N   
3767 C CA  . ASN A 489 ? 0.8906 1.0100 0.9467 -0.2347 -0.1165 0.1178  489 ASN A CA  
3768 C C   . ASN A 489 ? 0.8227 0.9308 0.8828 -0.2145 -0.0984 0.0978  489 ASN A C   
3769 O O   . ASN A 489 ? 0.8170 0.9132 0.8548 -0.2164 -0.0875 0.0812  489 ASN A O   
3770 C CB  . ASN A 489 ? 0.9435 1.0604 0.9714 -0.2555 -0.1200 0.1129  489 ASN A CB  
3771 C CG  . ASN A 489 ? 0.9338 1.0540 0.9783 -0.2487 -0.1186 0.1114  489 ASN A CG  
3772 O OD1 . ASN A 489 ? 0.8951 1.0058 0.9387 -0.2366 -0.1041 0.0948  489 ASN A OD1 
3773 N ND2 . ASN A 489 ? 0.9410 1.0747 1.0021 -0.2568 -0.1341 0.1297  489 ASN A ND2 
3774 N N   . PHE A 490 ? 0.6806 0.7923 0.7701 -0.1959 -0.0950 0.1000  490 PHE A N   
3775 C CA  . PHE A 490 ? 0.6767 0.7778 0.7688 -0.1776 -0.0800 0.0830  490 PHE A CA  
3776 C C   . PHE A 490 ? 0.7378 0.8293 0.8091 -0.1820 -0.0718 0.0673  490 PHE A C   
3777 O O   . PHE A 490 ? 0.7293 0.8097 0.7921 -0.1738 -0.0602 0.0514  490 PHE A O   
3778 C CB  . PHE A 490 ? 0.5663 0.6718 0.6906 -0.1593 -0.0777 0.0892  490 PHE A CB  
3779 C CG  . PHE A 490 ? 0.6571 0.7515 0.7811 -0.1423 -0.0641 0.0734  490 PHE A CG  
3780 C CD1 . PHE A 490 ? 0.6619 0.7484 0.7813 -0.1331 -0.0572 0.0629  490 PHE A CD1 
3781 C CD2 . PHE A 490 ? 0.5838 0.6755 0.7122 -0.1363 -0.0591 0.0699  490 PHE A CD2 
3782 C CE1 . PHE A 490 ? 0.4661 0.5427 0.5844 -0.1188 -0.0472 0.0499  490 PHE A CE1 
3783 C CE2 . PHE A 490 ? 0.6492 0.7302 0.7750 -0.1218 -0.0481 0.0571  490 PHE A CE2 
3784 C CZ  . PHE A 490 ? 0.5523 0.6259 0.6728 -0.1133 -0.0431 0.0475  490 PHE A CZ  
3785 N N   . GLY A 491 ? 0.7694 0.8652 0.8349 -0.1951 -0.0777 0.0720  491 GLY A N   
3786 C CA  . GLY A 491 ? 0.7204 0.8066 0.7668 -0.2010 -0.0692 0.0570  491 GLY A CA  
3787 C C   . GLY A 491 ? 0.7598 0.8347 0.7778 -0.2121 -0.0616 0.0427  491 GLY A C   
3788 O O   . GLY A 491 ? 0.7225 0.7858 0.7343 -0.2059 -0.0486 0.0264  491 GLY A O   
3789 N N   . LYS A 492 ? 0.7345 0.8121 0.7362 -0.2291 -0.0693 0.0492  492 LYS A N   
3790 C CA  . LYS A 492 ? 0.7813 0.8471 0.7566 -0.2400 -0.0601 0.0356  492 LYS A CA  
3791 C C   . LYS A 492 ? 0.8298 0.8897 0.8161 -0.2224 -0.0505 0.0274  492 LYS A C   
3792 O O   . LYS A 492 ? 0.7468 0.7947 0.7202 -0.2246 -0.0379 0.0116  492 LYS A O   
3793 C CB  . LYS A 492 ? 0.7719 0.8414 0.7253 -0.2628 -0.0711 0.0461  492 LYS A CB  
3794 C CG  . LYS A 492 ? 0.9510 1.0298 0.8977 -0.2804 -0.0860 0.0593  492 LYS A CG  
3795 C CD  . LYS A 492 ? 0.9663 1.0370 0.8974 -0.2900 -0.0780 0.0451  492 LYS A CD  
3796 C CE  . LYS A 492 ? 1.0408 1.1216 0.9674 -0.3076 -0.0940 0.0583  492 LYS A CE  
3797 N NZ  . LYS A 492 ? 1.0604 1.1331 0.9737 -0.3168 -0.0855 0.0440  492 LYS A NZ  
3798 N N   . TYR A 493 ? 0.7816 0.8495 0.7932 -0.2056 -0.0558 0.0375  493 TYR A N   
3799 C CA  . TYR A 493 ? 0.6686 0.7313 0.6918 -0.1888 -0.0478 0.0297  493 TYR A CA  
3800 C C   . TYR A 493 ? 0.6858 0.7387 0.7124 -0.1762 -0.0358 0.0137  493 TYR A C   
3801 O O   . TYR A 493 ? 0.7143 0.7578 0.7366 -0.1733 -0.0262 0.0006  493 TYR A O   
3802 C CB  . TYR A 493 ? 0.6167 0.6891 0.6665 -0.1744 -0.0549 0.0432  493 TYR A CB  
3803 C CG  . TYR A 493 ? 0.6547 0.7220 0.7173 -0.1569 -0.0477 0.0352  493 TYR A CG  
3804 C CD1 . TYR A 493 ? 0.6844 0.7488 0.7427 -0.1594 -0.0455 0.0324  493 TYR A CD1 
3805 C CD2 . TYR A 493 ? 0.6325 0.6977 0.7107 -0.1389 -0.0433 0.0307  493 TYR A CD2 
3806 C CE1 . TYR A 493 ? 0.6329 0.6931 0.7041 -0.1442 -0.0398 0.0249  493 TYR A CE1 
3807 C CE2 . TYR A 493 ? 0.6808 0.7412 0.7686 -0.1246 -0.0382 0.0235  493 TYR A CE2 
3808 C CZ  . TYR A 493 ? 0.5556 0.6141 0.6411 -0.1273 -0.0368 0.0205  493 TYR A CZ  
3809 O OH  . TYR A 493 ? 0.6122 0.6663 0.7084 -0.1139 -0.0326 0.0130  493 TYR A OH  
3810 N N   . LEU A 494 ? 0.5717 0.6267 0.6078 -0.1689 -0.0365 0.0156  494 LEU A N   
3811 C CA  . LEU A 494 ? 0.6414 0.6869 0.6799 -0.1581 -0.0264 0.0026  494 LEU A CA  
3812 C C   . LEU A 494 ? 0.7712 0.8063 0.7920 -0.1707 -0.0169 -0.0113 494 LEU A C   
3813 O O   . LEU A 494 ? 0.8646 0.8903 0.8892 -0.1626 -0.0072 -0.0235 494 LEU A O   
3814 C CB  . LEU A 494 ? 0.6388 0.6877 0.6877 -0.1513 -0.0284 0.0083  494 LEU A CB  
3815 C CG  . LEU A 494 ? 0.6005 0.6566 0.6698 -0.1369 -0.0335 0.0194  494 LEU A CG  
3816 C CD1 . LEU A 494 ? 0.5714 0.6295 0.6493 -0.1328 -0.0334 0.0243  494 LEU A CD1 
3817 C CD2 . LEU A 494 ? 0.5708 0.6207 0.6474 -0.1202 -0.0284 0.0124  494 LEU A CD2 
3818 N N   . ALA A 495 ? 0.8433 0.8795 0.8454 -0.1914 -0.0193 -0.0096 495 ALA A N   
3819 C CA  . ALA A 495 ? 0.8001 0.8245 0.7838 -0.2057 -0.0078 -0.0243 495 ALA A CA  
3820 C C   . ALA A 495 ? 0.8022 0.8190 0.7799 -0.2082 0.0004  -0.0333 495 ALA A C   
3821 O O   . ALA A 495 ? 0.8299 0.8348 0.8052 -0.2101 0.0144  -0.0485 495 ALA A O   
3822 C CB  . ALA A 495 ? 0.8184 0.8450 0.7799 -0.2293 -0.0129 -0.0203 495 ALA A CB  
3823 N N   . HIS A 496 ? 0.7829 0.8061 0.7610 -0.2081 -0.0072 -0.0241 496 HIS A N   
3824 C CA  . HIS A 496 ? 0.8697 0.8857 0.8433 -0.2106 0.0009  -0.0321 496 HIS A CA  
3825 C C   . HIS A 496 ? 0.7938 0.8040 0.7890 -0.1913 0.0097  -0.0428 496 HIS A C   
3826 O O   . HIS A 496 ? 0.6456 0.6458 0.6398 -0.1942 0.0219  -0.0554 496 HIS A O   
3827 C CB  . HIS A 496 ? 0.8702 0.8950 0.8435 -0.2125 -0.0099 -0.0181 496 HIS A CB  
3828 C CG  . HIS A 496 ? 0.8744 0.8915 0.8330 -0.2242 -0.0024 -0.0241 496 HIS A CG  
3829 N ND1 . HIS A 496 ? 0.9122 0.9183 0.8437 -0.2455 0.0075  -0.0341 496 HIS A ND1 
3830 C CD2 . HIS A 496 ? 0.8256 0.8433 0.7923 -0.2185 -0.0021 -0.0220 496 HIS A CD2 
3831 C CE1 . HIS A 496 ? 0.9147 0.9147 0.8378 -0.2522 0.0142  -0.0377 496 HIS A CE1 
3832 N NE2 . HIS A 496 ? 0.7819 0.7893 0.7269 -0.2358 0.0081  -0.0301 496 HIS A NE2 
3833 N N   . TRP A 497 ? 0.7073 0.7230 0.7222 -0.1723 0.0038  -0.0377 497 TRP A N   
3834 C CA  . TRP A 497 ? 0.7382 0.7486 0.7718 -0.1550 0.0095  -0.0463 497 TRP A CA  
3835 C C   . TRP A 497 ? 0.7789 0.7796 0.8144 -0.1554 0.0199  -0.0579 497 TRP A C   
3836 O O   . TRP A 497 ? 0.7450 0.7376 0.7909 -0.1514 0.0294  -0.0689 497 TRP A O   
3837 C CB  . TRP A 497 ? 0.6964 0.7140 0.7458 -0.1369 0.0002  -0.0373 497 TRP A CB  
3838 C CG  . TRP A 497 ? 0.7323 0.7558 0.7891 -0.1312 -0.0058 -0.0308 497 TRP A CG  
3839 C CD1 . TRP A 497 ? 0.7172 0.7495 0.7708 -0.1376 -0.0136 -0.0184 497 TRP A CD1 
3840 C CD2 . TRP A 497 ? 0.6568 0.6780 0.7279 -0.1184 -0.0046 -0.0359 497 TRP A CD2 
3841 N NE1 . TRP A 497 ? 0.6330 0.6677 0.6984 -0.1291 -0.0160 -0.0160 497 TRP A NE1 
3842 C CE2 . TRP A 497 ? 0.7406 0.7687 0.8158 -0.1176 -0.0105 -0.0272 497 TRP A CE2 
3843 C CE3 . TRP A 497 ? 0.6653 0.6796 0.7478 -0.1080 0.0001  -0.0462 497 TRP A CE3 
3844 C CZ2 . TRP A 497 ? 0.7257 0.7531 0.8143 -0.1071 -0.0108 -0.0301 497 TRP A CZ2 
3845 C CZ3 . TRP A 497 ? 0.7048 0.7192 0.8003 -0.0980 -0.0020 -0.0483 497 TRP A CZ3 
3846 C CH2 . TRP A 497 ? 0.6978 0.7185 0.7954 -0.0978 -0.0068 -0.0411 497 TRP A CH2 
3847 N N   . LEU A 498 ? 0.8248 0.8265 0.8537 -0.1600 0.0187  -0.0552 498 LEU A N   
3848 C CA  . LEU A 498 ? 0.7487 0.7408 0.7806 -0.1612 0.0294  -0.0656 498 LEU A CA  
3849 C C   . LEU A 498 ? 0.9121 0.8936 0.9333 -0.1780 0.0435  -0.0788 498 LEU A C   
3850 O O   . LEU A 498 ? 0.9955 0.9670 1.0271 -0.1766 0.0557  -0.0900 498 LEU A O   
3851 C CB  . LEU A 498 ? 0.8469 0.8423 0.8731 -0.1647 0.0254  -0.0597 498 LEU A CB  
3852 C CG  . LEU A 498 ? 0.8120 0.8153 0.8498 -0.1483 0.0151  -0.0481 498 LEU A CG  
3853 C CD1 . LEU A 498 ? 0.6643 0.6711 0.6971 -0.1543 0.0123  -0.0423 498 LEU A CD1 
3854 C CD2 . LEU A 498 ? 0.7126 0.7101 0.7674 -0.1301 0.0181  -0.0522 498 LEU A CD2 
3855 N N   . SER A 499 ? 0.9731 0.9556 0.9742 -0.1945 0.0427  -0.0775 499 SER A N   
3856 C CA  . SER A 499 ? 1.0711 1.0416 1.0582 -0.2124 0.0580  -0.0909 499 SER A CA  
3857 C C   . SER A 499 ? 1.0203 0.9834 1.0257 -0.2041 0.0690  -0.1010 499 SER A C   
3858 O O   . SER A 499 ? 1.1050 1.0553 1.1085 -0.2148 0.0862  -0.1151 499 SER A O   
3859 C CB  . SER A 499 ? 1.1169 1.0900 1.0744 -0.2330 0.0529  -0.0851 499 SER A CB  
3860 O OG  . SER A 499 ? 1.0536 1.0351 1.0154 -0.2259 0.0427  -0.0748 499 SER A OG  
3861 N N   A MET A 500 ? 1.0324 1.0026 1.0567 -0.1860 0.0602  -0.0946 500 MET A N   
3862 N N   B MET A 500 ? 1.1166 1.0869 1.1408 -0.1861 0.0601  -0.0945 500 MET A N   
3863 C CA  A MET A 500 ? 1.1115 1.0761 1.1563 -0.1779 0.0687  -0.1033 500 MET A CA  
3864 C CA  B MET A 500 ? 0.9706 0.9353 1.0155 -0.1777 0.0685  -0.1031 500 MET A CA  
3865 C C   A MET A 500 ? 1.0794 1.0356 1.1484 -0.1693 0.0791  -0.1133 500 MET A C   
3866 C C   B MET A 500 ? 0.9794 0.9352 1.0476 -0.1701 0.0796  -0.1136 500 MET A C   
3867 O O   A MET A 500 ? 1.0995 1.0489 1.1878 -0.1664 0.0896  -0.1226 500 MET A O   
3868 O O   B MET A 500 ? 1.0876 1.0359 1.1737 -0.1687 0.0912  -0.1235 500 MET A O   
3869 C CB  A MET A 500 ? 0.8932 0.8676 0.9520 -0.1613 0.0554  -0.0940 500 MET A CB  
3870 C CB  B MET A 500 ? 0.9135 0.8882 0.9735 -0.1601 0.0550  -0.0938 500 MET A CB  
3871 C CG  A MET A 500 ? 0.8099 0.7927 0.8512 -0.1684 0.0457  -0.0830 500 MET A CG  
3872 C CG  B MET A 500 ? 0.8814 0.8646 0.9252 -0.1661 0.0449  -0.0827 500 MET A CG  
3873 S SD  A MET A 500 ? 0.9797 0.9541 0.9983 -0.1917 0.0577  -0.0896 500 MET A SD  
3874 S SD  B MET A 500 ? 0.7857 0.7797 0.8484 -0.1453 0.0304  -0.0723 500 MET A SD  
3875 C CE  A MET A 500 ? 0.7467 0.7336 0.7501 -0.1960 0.0410  -0.0713 500 MET A CE  
3876 C CE  B MET A 500 ? 0.7649 0.7519 0.8525 -0.1360 0.0391  -0.0845 500 MET A CE  
3877 N N   . ALA A 501 ? 1.0567 1.0132 1.1277 -0.1652 0.0766  -0.1109 501 ALA A N   
3878 C CA  . ALA A 501 ? 1.0343 0.9826 1.1290 -0.1580 0.0863  -0.1187 501 ALA A CA  
3879 C C   . ALA A 501 ? 1.2552 1.1901 1.3448 -0.1755 0.1066  -0.1328 501 ALA A C   
3880 O O   . ALA A 501 ? 1.2574 1.1841 1.3705 -0.1709 0.1175  -0.1401 501 ALA A O   
3881 C CB  . ALA A 501 ? 0.9566 0.9097 1.0554 -0.1464 0.0761  -0.1097 501 ALA A CB  
3882 N N   . HIS A 502 ? 1.3848 1.3166 1.4446 -0.1961 0.1122  -0.1365 502 HIS A N   
3883 C CA  . HIS A 502 ? 1.4972 1.4144 1.5462 -0.2159 0.1330  -0.1515 502 HIS A CA  
3884 C C   . HIS A 502 ? 1.6292 1.5363 1.6783 -0.2262 0.1492  -0.1632 502 HIS A C   
3885 O O   . HIS A 502 ? 1.8458 1.7379 1.8916 -0.2415 0.1707  -0.1782 502 HIS A O   
3886 C CB  . HIS A 502 ? 1.5919 1.5102 1.6028 -0.2359 0.1291  -0.1488 502 HIS A CB  
3887 C CG  . HIS A 502 ? 1.6678 1.5938 1.6796 -0.2289 0.1172  -0.1396 502 HIS A CG  
3888 N ND1 . HIS A 502 ? 1.6168 1.5479 1.6003 -0.2432 0.1085  -0.1334 502 HIS A ND1 
3889 C CD2 . HIS A 502 ? 1.6500 1.5792 1.6878 -0.2098 0.1127  -0.1351 502 HIS A CD2 
3890 C CE1 . HIS A 502 ? 1.5820 1.5190 1.5759 -0.2326 0.1003  -0.1262 502 HIS A CE1 
3891 N NE2 . HIS A 502 ? 1.6170 1.5524 1.6420 -0.2125 0.1030  -0.1271 502 HIS A NE2 
3892 N N   . ARG A 503 ? 1.5904 1.5043 1.6438 -0.2187 0.1410  -0.1573 503 ARG A N   
3893 C CA  . ARG A 503 ? 1.6992 1.6035 1.7523 -0.2287 0.1567  -0.1677 503 ARG A CA  
3894 C C   . ARG A 503 ? 1.7364 1.6303 1.8300 -0.2206 0.1747  -0.1805 503 ARG A C   
3895 O O   . ARG A 503 ? 1.6199 1.5197 1.7471 -0.2003 0.1666  -0.1756 503 ARG A O   
3896 C CB  . ARG A 503 ? 1.6468 1.5615 1.6987 -0.2211 0.1430  -0.1575 503 ARG A CB  
3897 C CG  . ARG A 503 ? 1.6039 1.5291 1.6213 -0.2290 0.1254  -0.1434 503 ARG A CG  
3898 C CD  . ARG A 503 ? 1.6087 1.5435 1.6300 -0.2203 0.1133  -0.1334 503 ARG A CD  
3899 N NE  . ARG A 503 ? 1.7682 1.6933 1.7842 -0.2319 0.1279  -0.1419 503 ARG A NE  
3900 C CZ  . ARG A 503 ? 1.8740 1.7960 1.8560 -0.2514 0.1294  -0.1392 503 ARG A CZ  
3901 N NH1 . ARG A 503 ? 1.8263 1.7551 1.7782 -0.2620 0.1156  -0.1275 503 ARG A NH1 
3902 N NH2 . ARG A 503 ? 1.9236 1.8352 1.9024 -0.2611 0.1446  -0.1477 503 ARG A NH2 
3903 N N   . PRO A 504 ? 1.6925 1.5704 1.7847 -0.2366 0.1994  -0.1963 504 PRO A N   
3904 C CA  . PRO A 504 ? 1.7127 1.5829 1.8474 -0.2260 0.2168  -0.2062 504 PRO A CA  
3905 C C   . PRO A 504 ? 1.6801 1.5558 1.8526 -0.2102 0.2103  -0.2032 504 PRO A C   
3906 O O   . PRO A 504 ? 1.6262 1.5077 1.7854 -0.2110 0.2023  -0.1982 504 PRO A O   
3907 C CB  . PRO A 504 ? 1.7110 1.5691 1.8238 -0.2410 0.2418  -0.2187 504 PRO A CB  
3908 C CG  . PRO A 504 ? 1.7042 1.5610 1.7615 -0.2619 0.2369  -0.2164 504 PRO A CG  
3909 C CD  . PRO A 504 ? 1.7055 1.5751 1.7534 -0.2598 0.2105  -0.2019 504 PRO A CD  
3910 N N   . ALA A 505 ? 1.7376 1.6137 1.9568 -0.1935 0.2121  -0.2041 505 ALA A N   
3911 C CA  . ALA A 505 ? 1.6651 1.5473 1.9246 -0.1770 0.2049  -0.2007 505 ALA A CA  
3912 C C   . ALA A 505 ? 1.5915 1.4905 1.8356 -0.1649 0.1771  -0.1851 505 ALA A C   
3913 O O   . ALA A 505 ? 1.5339 1.4377 1.7887 -0.1594 0.1722  -0.1833 505 ALA A O   
3914 C CB  . ALA A 505 ? 1.6368 1.5135 1.9046 -0.1810 0.2242  -0.2098 505 ALA A CB  
3915 N N   . ALA A 506 ? 1.4572 1.3647 1.6779 -0.1611 0.1601  -0.1743 506 ALA A N   
3916 C CA  . ALA A 506 ? 1.2119 1.1340 1.4177 -0.1506 0.1358  -0.1600 506 ALA A CA  
3917 C C   . ALA A 506 ? 1.0852 1.0154 1.3251 -0.1288 0.1203  -0.1525 506 ALA A C   
3918 O O   . ALA A 506 ? 1.0553 0.9838 1.3151 -0.1207 0.1190  -0.1511 506 ALA A O   
3919 C CB  . ALA A 506 ? 1.1887 1.1162 1.3586 -0.1558 0.1252  -0.1514 506 ALA A CB  
3920 N N   . LYS A 507 ? 1.0707 1.0089 1.3165 -0.1203 0.1084  -0.1474 507 LYS A N   
3921 C CA  . LYS A 507 ? 0.9301 0.8761 1.2023 -0.1016 0.0913  -0.1399 507 LYS A CA  
3922 C C   . LYS A 507 ? 0.9109 0.8674 1.1565 -0.0950 0.0713  -0.1277 507 LYS A C   
3923 O O   . LYS A 507 ? 0.9368 0.8996 1.1764 -0.0923 0.0629  -0.1242 507 LYS A O   
3924 C CB  . LYS A 507 ? 0.9173 0.8636 1.2195 -0.0974 0.0937  -0.1448 507 LYS A CB  
3925 C CG  . LYS A 507 ? 1.0887 1.0236 1.4197 -0.1050 0.1166  -0.1577 507 LYS A CG  
3926 C CD  . LYS A 507 ? 1.2065 1.1424 1.5681 -0.1012 0.1189  -0.1620 507 LYS A CD  
3927 C CE  . LYS A 507 ? 1.1335 1.0570 1.5255 -0.1098 0.1448  -0.1757 507 LYS A CE  
3928 N NZ  . LYS A 507 ? 1.3502 1.2747 1.7746 -0.1065 0.1482  -0.1800 507 LYS A NZ  
3929 N N   . LEU A 508 ? 0.8587 0.8165 1.0903 -0.0926 0.0650  -0.1214 508 LEU A N   
3930 C CA  . LEU A 508 ? 0.7928 0.7592 0.9997 -0.0878 0.0493  -0.1105 508 LEU A CA  
3931 C C   . LEU A 508 ? 0.7144 0.6865 0.9352 -0.0719 0.0329  -0.1041 508 LEU A C   
3932 O O   . LEU A 508 ? 0.7462 0.7160 0.9911 -0.0631 0.0292  -0.1041 508 LEU A O   
3933 C CB  . LEU A 508 ? 0.8149 0.7801 1.0055 -0.0899 0.0487  -0.1061 508 LEU A CB  
3934 C CG  . LEU A 508 ? 0.7361 0.6951 0.9102 -0.1070 0.0639  -0.1127 508 LEU A CG  
3935 C CD1 . LEU A 508 ? 0.8450 0.8037 1.0059 -0.1079 0.0616  -0.1078 508 LEU A CD1 
3936 C CD2 . LEU A 508 ? 0.7984 0.7602 0.9476 -0.1198 0.0655  -0.1123 508 LEU A CD2 
3937 N N   . PRO A 509 ? 0.6613 0.6403 0.8679 -0.0688 0.0226  -0.0984 509 PRO A N   
3938 C CA  . PRO A 509 ? 0.7084 0.6915 0.9241 -0.0557 0.0077  -0.0937 509 PRO A CA  
3939 C C   . PRO A 509 ? 0.5787 0.5626 0.7811 -0.0484 -0.0025 -0.0853 509 PRO A C   
3940 O O   . PRO A 509 ? 0.7018 0.6856 0.8857 -0.0529 0.0005  -0.0816 509 PRO A O   
3941 C CB  . PRO A 509 ? 0.5863 0.5750 0.7916 -0.0575 0.0046  -0.0921 509 PRO A CB  
3942 C CG  . PRO A 509 ? 0.5458 0.5356 0.7273 -0.0689 0.0115  -0.0896 509 PRO A CG  
3943 C CD  . PRO A 509 ? 0.6618 0.6447 0.8453 -0.0783 0.0248  -0.0962 509 PRO A CD  
3944 N N   . LYS A 510 ? 0.5470 0.5312 0.7586 -0.0378 -0.0148 -0.0822 510 LYS A N   
3945 C CA  . LYS A 510 ? 0.4512 0.4345 0.6476 -0.0311 -0.0244 -0.0744 510 LYS A CA  
3946 C C   . LYS A 510 ? 0.5097 0.4971 0.6822 -0.0317 -0.0271 -0.0699 510 LYS A C   
3947 O O   . LYS A 510 ? 0.5163 0.5080 0.6872 -0.0352 -0.0250 -0.0719 510 LYS A O   
3948 C CB  . LYS A 510 ? 0.4729 0.4545 0.6819 -0.0217 -0.0378 -0.0720 510 LYS A CB  
3949 C CG  . LYS A 510 ? 0.4442 0.4216 0.6791 -0.0194 -0.0375 -0.0724 510 LYS A CG  
3950 C CD  . LYS A 510 ? 0.4949 0.4708 0.7381 -0.0109 -0.0544 -0.0668 510 LYS A CD  
3951 C CE  . LYS A 510 ? 0.4011 0.3732 0.6721 -0.0082 -0.0553 -0.0639 510 LYS A CE  
3952 N NZ  . LYS A 510 ? 0.5570 0.5245 0.8179 -0.0099 -0.0473 -0.0602 510 LYS A NZ  
3953 N N   . ILE A 511 ? 0.4551 0.4408 0.6111 -0.0282 -0.0311 -0.0634 511 ILE A N   
3954 C CA  . ILE A 511 ? 0.4049 0.3937 0.5420 -0.0284 -0.0320 -0.0585 511 ILE A CA  
3955 C C   . ILE A 511 ? 0.4478 0.4322 0.5739 -0.0204 -0.0406 -0.0542 511 ILE A C   
3956 O O   . ILE A 511 ? 0.5444 0.5234 0.6678 -0.0171 -0.0434 -0.0513 511 ILE A O   
3957 C CB  . ILE A 511 ? 0.5533 0.5441 0.6794 -0.0354 -0.0244 -0.0547 511 ILE A CB  
3958 C CG1 . ILE A 511 ? 0.5416 0.5351 0.6733 -0.0459 -0.0159 -0.0594 511 ILE A CG1 
3959 C CG2 . ILE A 511 ? 0.4303 0.4247 0.5430 -0.0349 -0.0256 -0.0484 511 ILE A CG2 
3960 C CD1 . ILE A 511 ? 0.5230 0.5182 0.6427 -0.0551 -0.0099 -0.0562 511 ILE A CD1 
3961 N N   . PHE A 512 ? 0.4010 0.3866 0.5200 -0.0180 -0.0439 -0.0540 512 PHE A N   
3962 C CA  . PHE A 512 ? 0.4618 0.4414 0.5662 -0.0124 -0.0502 -0.0516 512 PHE A CA  
3963 C C   . PHE A 512 ? 0.3893 0.3701 0.4815 -0.0131 -0.0448 -0.0485 512 PHE A C   
3964 O O   . PHE A 512 ? 0.3742 0.3618 0.4728 -0.0170 -0.0394 -0.0480 512 PHE A O   
3965 C CB  . PHE A 512 ? 0.4146 0.3919 0.5243 -0.0089 -0.0597 -0.0563 512 PHE A CB  
3966 C CG  . PHE A 512 ? 0.5121 0.4895 0.6410 -0.0080 -0.0656 -0.0587 512 PHE A CG  
3967 C CD1 . PHE A 512 ? 0.4821 0.4650 0.6324 -0.0110 -0.0615 -0.0639 512 PHE A CD1 
3968 C CD2 . PHE A 512 ? 0.4944 0.4658 0.6215 -0.0044 -0.0749 -0.0551 512 PHE A CD2 
3969 C CE1 . PHE A 512 ? 0.4793 0.4619 0.6522 -0.0101 -0.0651 -0.0664 512 PHE A CE1 
3970 C CE2 . PHE A 512 ? 0.4658 0.4379 0.6166 -0.0032 -0.0806 -0.0560 512 PHE A CE2 
3971 C CZ  . PHE A 512 ? 0.4474 0.4251 0.6228 -0.0058 -0.0749 -0.0621 512 PHE A CZ  
3972 N N   . HIS A 513 ? 0.4044 0.3778 0.4798 -0.0097 -0.0460 -0.0459 513 HIS A N   
3973 C CA  . HIS A 513 ? 0.4869 0.4593 0.5534 -0.0096 -0.0396 -0.0436 513 HIS A CA  
3974 C C   . HIS A 513 ? 0.4851 0.4481 0.5373 -0.0066 -0.0433 -0.0473 513 HIS A C   
3975 O O   . HIS A 513 ? 0.4124 0.3667 0.4499 -0.0048 -0.0492 -0.0468 513 HIS A O   
3976 C CB  . HIS A 513 ? 0.4317 0.4026 0.4901 -0.0105 -0.0329 -0.0369 513 HIS A CB  
3977 C CG  . HIS A 513 ? 0.4905 0.4630 0.5489 -0.0111 -0.0245 -0.0336 513 HIS A CG  
3978 N ND1 . HIS A 513 ? 0.5837 0.5468 0.6288 -0.0085 -0.0203 -0.0343 513 HIS A ND1 
3979 C CD2 . HIS A 513 ? 0.4715 0.4534 0.5431 -0.0147 -0.0193 -0.0290 513 HIS A CD2 
3980 C CE1 . HIS A 513 ? 0.4790 0.4458 0.5331 -0.0095 -0.0115 -0.0306 513 HIS A CE1 
3981 N NE2 . HIS A 513 ? 0.4752 0.4541 0.5462 -0.0131 -0.0121 -0.0265 513 HIS A NE2 
3982 N N   . VAL A 514 ? 0.5010 0.4650 0.5569 -0.0069 -0.0398 -0.0508 514 VAL A N   
3983 C CA  . VAL A 514 ? 0.5009 0.4553 0.5431 -0.0058 -0.0419 -0.0565 514 VAL A CA  
3984 C C   . VAL A 514 ? 0.4842 0.4341 0.5201 -0.0061 -0.0295 -0.0554 514 VAL A C   
3985 O O   . VAL A 514 ? 0.6171 0.5731 0.6636 -0.0066 -0.0212 -0.0495 514 VAL A O   
3986 C CB  . VAL A 514 ? 0.4544 0.4123 0.5092 -0.0062 -0.0477 -0.0635 514 VAL A CB  
3987 C CG1 . VAL A 514 ? 0.4042 0.3660 0.4690 -0.0058 -0.0589 -0.0646 514 VAL A CG1 
3988 C CG2 . VAL A 514 ? 0.4469 0.4145 0.5221 -0.0074 -0.0398 -0.0628 514 VAL A CG2 
3989 N N   . ASN A 515 ? 0.5628 0.5011 0.5821 -0.0066 -0.0282 -0.0615 515 ASN A N   
3990 C CA  . ASN A 515 ? 0.5577 0.4890 0.5722 -0.0072 -0.0138 -0.0623 515 ASN A CA  
3991 C C   . ASN A 515 ? 0.7368 0.6553 0.7342 -0.0095 -0.0139 -0.0725 515 ASN A C   
3992 O O   . ASN A 515 ? 0.7718 0.6767 0.7403 -0.0116 -0.0164 -0.0751 515 ASN A O   
3993 C CB  . ASN A 515 ? 0.5266 0.4513 0.5267 -0.0070 -0.0066 -0.0564 515 ASN A CB  
3994 C CG  . ASN A 515 ? 0.5997 0.5156 0.5974 -0.0079 0.0102  -0.0579 515 ASN A CG  
3995 O OD1 . ASN A 515 ? 0.6679 0.5877 0.6849 -0.0078 0.0181  -0.0599 515 ASN A OD1 
3996 N ND2 . ASN A 515 ? 0.7304 0.6340 0.7061 -0.0088 0.0170  -0.0565 515 ASN A ND2 
3997 N N   . TRP A 516 ? 0.6993 0.6217 0.7137 -0.0098 -0.0111 -0.0778 516 TRP A N   
3998 C CA  . TRP A 516 ? 0.7359 0.6464 0.7366 -0.0130 -0.0097 -0.0888 516 TRP A CA  
3999 C C   . TRP A 516 ? 0.8435 0.7402 0.8321 -0.0153 0.0082  -0.0926 516 TRP A C   
4000 O O   . TRP A 516 ? 0.9244 0.8068 0.8924 -0.0198 0.0108  -0.1028 516 TRP A O   
4001 C CB  . TRP A 516 ? 0.6937 0.6126 0.7194 -0.0127 -0.0111 -0.0936 516 TRP A CB  
4002 C CG  . TRP A 516 ? 0.5973 0.5307 0.6423 -0.0107 -0.0237 -0.0898 516 TRP A CG  
4003 C CD1 . TRP A 516 ? 0.5713 0.5174 0.6452 -0.0094 -0.0216 -0.0870 516 TRP A CD1 
4004 C CD2 . TRP A 516 ? 0.5811 0.5168 0.6189 -0.0103 -0.0391 -0.0884 516 TRP A CD2 
4005 N NE1 . TRP A 516 ? 0.5721 0.5271 0.6551 -0.0089 -0.0331 -0.0853 516 TRP A NE1 
4006 C CE2 . TRP A 516 ? 0.5134 0.4626 0.5771 -0.0090 -0.0436 -0.0862 516 TRP A CE2 
4007 C CE3 . TRP A 516 ? 0.6479 0.5750 0.6609 -0.0114 -0.0491 -0.0881 516 TRP A CE3 
4008 C CZ2 . TRP A 516 ? 0.6176 0.5717 0.6861 -0.0083 -0.0560 -0.0848 516 TRP A CZ2 
4009 C CZ3 . TRP A 516 ? 0.6890 0.6223 0.7089 -0.0102 -0.0633 -0.0851 516 TRP A CZ3 
4010 C CH2 . TRP A 516 ? 0.6468 0.5933 0.6956 -0.0085 -0.0657 -0.0841 516 TRP A CH2 
4011 N N   . PHE A 517 ? 0.7806 0.6806 0.7824 -0.0130 0.0210  -0.0850 517 PHE A N   
4012 C CA  . PHE A 517 ? 0.9095 0.7981 0.9111 -0.0146 0.0412  -0.0883 517 PHE A CA  
4013 C C   . PHE A 517 ? 0.8992 0.7742 0.8736 -0.0164 0.0491  -0.0867 517 PHE A C   
4014 O O   . PHE A 517 ? 0.9145 0.7825 0.8955 -0.0168 0.0679  -0.0864 517 PHE A O   
4015 C CB  . PHE A 517 ? 0.8033 0.7051 0.8456 -0.0112 0.0516  -0.0802 517 PHE A CB  
4016 C CG  . PHE A 517 ? 0.7327 0.6478 0.8018 -0.0098 0.0445  -0.0799 517 PHE A CG  
4017 C CD1 . PHE A 517 ? 0.7706 0.6800 0.8483 -0.0113 0.0515  -0.0891 517 PHE A CD1 
4018 C CD2 . PHE A 517 ? 0.6552 0.5872 0.7400 -0.0078 0.0322  -0.0710 517 PHE A CD2 
4019 C CE1 . PHE A 517 ? 0.7286 0.6497 0.8313 -0.0101 0.0456  -0.0883 517 PHE A CE1 
4020 C CE2 . PHE A 517 ? 0.6684 0.6112 0.7757 -0.0074 0.0269  -0.0705 517 PHE A CE2 
4021 C CZ  . PHE A 517 ? 0.7312 0.6689 0.8481 -0.0081 0.0333  -0.0787 517 PHE A CZ  
4022 N N   . ARG A 518 ? 0.9444 0.8150 0.8905 -0.0176 0.0358  -0.0851 518 ARG A N   
4023 C CA  . ARG A 518 ? 1.0810 0.9370 0.9981 -0.0199 0.0431  -0.0832 518 ARG A CA  
4024 C C   . ARG A 518 ? 1.3359 1.1693 1.2204 -0.0271 0.0535  -0.0952 518 ARG A C   
4025 O O   . ARG A 518 ? 1.3729 1.1994 1.2355 -0.0316 0.0418  -0.1029 518 ARG A O   
4026 C CB  . ARG A 518 ? 0.9805 0.8383 0.8789 -0.0193 0.0253  -0.0767 518 ARG A CB  
4027 C CG  . ARG A 518 ? 1.0741 0.9169 0.9427 -0.0217 0.0323  -0.0731 518 ARG A CG  
4028 C CD  . ARG A 518 ? 1.0106 0.8567 0.8675 -0.0201 0.0153  -0.0646 518 ARG A CD  
4029 N NE  . ARG A 518 ? 1.0734 0.9059 0.9049 -0.0221 0.0232  -0.0598 518 ARG A NE  
4030 C CZ  . ARG A 518 ? 1.1209 0.9532 0.9412 -0.0210 0.0124  -0.0512 518 ARG A CZ  
4031 N NH1 . ARG A 518 ? 1.0506 0.8953 0.8842 -0.0179 -0.0063 -0.0468 518 ARG A NH1 
4032 N NH2 . ARG A 518 ? 1.1568 0.9753 0.9540 -0.0231 0.0218  -0.0469 518 ARG A NH2 
4033 N N   . LYS A 519 ? 1.4086 1.2298 1.2903 -0.0289 0.0759  -0.0972 519 LYS A N   
4034 C CA  . LYS A 519 ? 1.6409 1.4380 1.4913 -0.0371 0.0907  -0.1099 519 LYS A CA  
4035 C C   . LYS A 519 ? 1.8966 1.6754 1.7017 -0.0426 0.0922  -0.1086 519 LYS A C   
4036 O O   . LYS A 519 ? 1.7540 1.5392 1.5563 -0.0389 0.0829  -0.0974 519 LYS A O   
4037 C CB  . LYS A 519 ? 1.6914 1.4846 1.5702 -0.0366 0.1177  -0.1140 519 LYS A CB  
4038 C CG  . LYS A 519 ? 1.4580 1.2689 1.3832 -0.0314 0.1170  -0.1132 519 LYS A CG  
4039 C CD  . LYS A 519 ? 1.4934 1.3004 1.4513 -0.0305 0.1438  -0.1149 519 LYS A CD  
4040 C CE  . LYS A 519 ? 1.4163 1.2413 1.4220 -0.0254 0.1419  -0.1116 519 LYS A CE  
4041 N NZ  . LYS A 519 ? 1.4482 1.2704 1.4918 -0.0240 0.1673  -0.1112 519 LYS A NZ  
4042 N N   . ASP A 520 ? 2.5375 2.2918 2.3055 -0.0522 0.1047  -0.1204 520 ASP A N   
4043 C CA  . ASP A 520 ? 2.6707 2.4035 2.3906 -0.0596 0.1091  -0.1203 520 ASP A CA  
4044 C C   . ASP A 520 ? 2.7133 2.4326 2.4385 -0.0609 0.1410  -0.1227 520 ASP A C   
4045 O O   . ASP A 520 ? 2.6317 2.3635 2.4041 -0.0539 0.1550  -0.1199 520 ASP A O   
4046 C CB  . ASP A 520 ? 2.7525 2.4656 2.4222 -0.0718 0.1002  -0.1317 520 ASP A CB  
4047 C CG  . ASP A 520 ? 2.7392 2.4416 2.4120 -0.0779 0.1168  -0.1484 520 ASP A CG  
4048 O OD1 . ASP A 520 ? 2.6652 2.3753 2.3811 -0.0720 0.1359  -0.1501 520 ASP A OD1 
4049 O OD2 . ASP A 520 ? 2.8016 2.4878 2.4346 -0.0892 0.1104  -0.1593 520 ASP A OD2 
4050 N N   . LYS A 521 ? 2.4329 2.1265 2.1108 -0.0703 0.1527  -0.1272 521 LYS A N   
4051 C CA  . LYS A 521 ? 2.3627 2.0405 2.0432 -0.0727 0.1852  -0.1304 521 LYS A CA  
4052 C C   . LYS A 521 ? 2.3470 2.0086 2.0309 -0.0794 0.2110  -0.1473 521 LYS A C   
4053 O O   . LYS A 521 ? 2.3261 1.9712 2.0120 -0.0827 0.2412  -0.1522 521 LYS A O   
4054 C CB  . LYS A 521 ? 2.2656 1.9204 1.8921 -0.0809 0.1894  -0.1283 521 LYS A CB  
4055 C CG  . LYS A 521 ? 2.1974 1.8660 1.8229 -0.0743 0.1675  -0.1113 521 LYS A CG  
4056 C CD  . LYS A 521 ? 2.0819 1.7263 1.6523 -0.0832 0.1714  -0.1085 521 LYS A CD  
4057 C CE  . LYS A 521 ? 2.0189 1.6768 1.5915 -0.0763 0.1500  -0.0913 521 LYS A CE  
4058 N NZ  . LYS A 521 ? 1.9570 1.5911 1.4757 -0.0851 0.1524  -0.0868 521 LYS A NZ  
4059 N N   . ASN A 522 ? 2.3283 1.9935 2.0153 -0.0817 0.2011  -0.1565 522 ASN A N   
4060 C CA  . ASN A 522 ? 2.2806 1.9302 1.9725 -0.0884 0.2253  -0.1734 522 ASN A CA  
4061 C C   . ASN A 522 ? 2.1462 1.8177 1.8994 -0.0791 0.2257  -0.1729 522 ASN A C   
4062 O O   . ASN A 522 ? 2.1088 1.7698 1.8801 -0.0824 0.2499  -0.1848 522 ASN A O   
4063 C CB  . ASN A 522 ? 2.3700 1.9979 2.0036 -0.1032 0.2174  -0.1884 522 ASN A CB  
4064 C CG  . ASN A 522 ? 2.4549 2.0585 2.0223 -0.1147 0.2164  -0.1886 522 ASN A CG  
4065 O OD1 . ASN A 522 ? 2.4576 2.0511 2.0195 -0.1146 0.2351  -0.1841 522 ASN A OD1 
4066 N ND2 . ASN A 522 ? 2.4652 2.0594 1.9827 -0.1253 0.1939  -0.1930 522 ASN A ND2 
4067 N N   . GLY A 523 ? 2.1078 1.8081 1.8932 -0.0683 0.2008  -0.1596 523 GLY A N   
4068 C CA  . GLY A 523 ? 1.8998 1.6209 1.7394 -0.0604 0.1986  -0.1576 523 GLY A CA  
4069 C C   . GLY A 523 ? 1.9264 1.6553 1.7599 -0.0619 0.1761  -0.1632 523 GLY A C   
4070 O O   . GLY A 523 ? 1.7298 1.4715 1.6041 -0.0572 0.1774  -0.1641 523 GLY A O   
4071 N N   . LYS A 524 ? 2.2470 1.9685 2.0330 -0.0684 0.1554  -0.1660 524 LYS A N   
4072 C CA  . LYS A 524 ? 2.1101 1.8387 1.8901 -0.0705 0.1326  -0.1711 524 LYS A CA  
4073 C C   . LYS A 524 ? 2.0028 1.7555 1.7964 -0.0618 0.1035  -0.1562 524 LYS A C   
4074 O O   . LYS A 524 ? 2.0643 1.8175 1.8388 -0.0605 0.0942  -0.1464 524 LYS A O   
4075 C CB  . LYS A 524 ? 2.2244 1.9284 1.9441 -0.0851 0.1276  -0.1843 524 LYS A CB  
4076 C CG  . LYS A 524 ? 2.2629 1.9747 1.9747 -0.0880 0.1003  -0.1881 524 LYS A CG  
4077 C CD  . LYS A 524 ? 2.2796 1.9678 1.9283 -0.1036 0.0913  -0.1982 524 LYS A CD  
4078 C CE  . LYS A 524 ? 2.2855 1.9833 1.9301 -0.1064 0.0613  -0.2001 524 LYS A CE  
4079 N NZ  . LYS A 524 ? 2.2460 1.9222 1.8284 -0.1228 0.0483  -0.2075 524 LYS A NZ  
4080 N N   . PHE A 525 ? 1.6285 1.4001 1.4559 -0.0563 0.0908  -0.1550 525 PHE A N   
4081 C CA  . PHE A 525 ? 1.4693 1.2627 1.3119 -0.0490 0.0655  -0.1427 525 PHE A CA  
4082 C C   . PHE A 525 ? 1.4385 1.2251 1.2398 -0.0548 0.0425  -0.1430 525 PHE A C   
4083 O O   . PHE A 525 ? 1.5005 1.2747 1.2750 -0.0638 0.0365  -0.1542 525 PHE A O   
4084 C CB  . PHE A 525 ? 1.2616 1.0733 1.1453 -0.0438 0.0587  -0.1432 525 PHE A CB  
4085 C CG  . PHE A 525 ? 1.2485 1.0706 1.1776 -0.0373 0.0767  -0.1386 525 PHE A CG  
4086 C CD1 . PHE A 525 ? 1.2015 1.0125 1.1422 -0.0404 0.0989  -0.1484 525 PHE A CD1 
4087 C CD2 . PHE A 525 ? 1.1788 1.0213 1.1396 -0.0290 0.0711  -0.1240 525 PHE A CD2 
4088 C CE1 . PHE A 525 ? 1.1823 1.0035 1.1690 -0.0344 0.1141  -0.1419 525 PHE A CE1 
4089 C CE2 . PHE A 525 ? 1.0953 0.9479 1.0978 -0.0242 0.0850  -0.1177 525 PHE A CE2 
4090 C CZ  . PHE A 525 ? 1.1057 0.9482 1.1229 -0.0264 0.1059  -0.1258 525 PHE A CZ  
4091 N N   . LEU A 526 ? 1.4089 1.2037 1.2063 -0.0503 0.0292  -0.1301 526 LEU A N   
4092 C CA  . LEU A 526 ? 1.3488 1.1389 1.1130 -0.0548 0.0061  -0.1269 526 LEU A CA  
4093 C C   . LEU A 526 ? 1.2295 1.0358 1.0138 -0.0521 -0.0178 -0.1258 526 LEU A C   
4094 O O   . LEU A 526 ? 1.2686 1.0719 1.0306 -0.0563 -0.0389 -0.1233 526 LEU A O   
4095 C CB  . LEU A 526 ? 1.2435 1.0356 0.9999 -0.0507 0.0023  -0.1131 526 LEU A CB  
4096 C CG  . LEU A 526 ? 1.4398 1.2135 1.1697 -0.0546 0.0233  -0.1131 526 LEU A CG  
4097 C CD1 . LEU A 526 ? 1.4931 1.2721 1.2229 -0.0494 0.0186  -0.0987 526 LEU A CD1 
4098 C CD2 . LEU A 526 ? 1.5435 1.2910 1.2196 -0.0679 0.0248  -0.1228 526 LEU A CD2 
4099 N N   . TRP A 527 ? 1.1527 0.9756 0.9793 -0.0457 -0.0149 -0.1268 527 TRP A N   
4100 C CA  . TRP A 527 ? 1.0589 0.8971 0.9084 -0.0430 -0.0345 -0.1262 527 TRP A CA  
4101 C C   . TRP A 527 ? 1.0312 0.8722 0.9034 -0.0438 -0.0262 -0.1369 527 TRP A C   
4102 O O   . TRP A 527 ? 1.0726 0.9173 0.9687 -0.0400 -0.0073 -0.1372 527 TRP A O   
4103 C CB  . TRP A 527 ? 0.9294 0.7876 0.8115 -0.0335 -0.0410 -0.1136 527 TRP A CB  
4104 C CG  . TRP A 527 ? 0.7898 0.6624 0.6958 -0.0310 -0.0595 -0.1127 527 TRP A CG  
4105 C CD1 . TRP A 527 ? 0.7511 0.6386 0.6942 -0.0266 -0.0575 -0.1136 527 TRP A CD1 
4106 C CD2 . TRP A 527 ? 0.8116 0.6847 0.7079 -0.0331 -0.0822 -0.1100 527 TRP A CD2 
4107 N NE1 . TRP A 527 ? 0.6763 0.5728 0.6334 -0.0258 -0.0758 -0.1129 527 TRP A NE1 
4108 C CE2 . TRP A 527 ? 0.8217 0.7102 0.7529 -0.0294 -0.0916 -0.1104 527 TRP A CE2 
4109 C CE3 . TRP A 527 ? 0.9106 0.7722 0.7732 -0.0381 -0.0958 -0.1062 527 TRP A CE3 
4110 C CZ2 . TRP A 527 ? 0.7884 0.6819 0.7260 -0.0300 -0.1132 -0.1078 527 TRP A CZ2 
4111 C CZ3 . TRP A 527 ? 0.8619 0.7291 0.7305 -0.0388 -0.1193 -0.1022 527 TRP A CZ3 
4112 C CH2 . TRP A 527 ? 0.7793 0.6626 0.6871 -0.0345 -0.1274 -0.1032 527 TRP A CH2 
4113 N N   . PRO A 528 ? 1.0825 0.9224 0.9505 -0.0488 -0.0401 -0.1450 528 PRO A N   
4114 C CA  . PRO A 528 ? 1.0345 0.8763 0.9249 -0.0498 -0.0314 -0.1557 528 PRO A CA  
4115 C C   . PRO A 528 ? 1.0196 0.8818 0.9580 -0.0404 -0.0279 -0.1492 528 PRO A C   
4116 O O   . PRO A 528 ? 0.9925 0.8560 0.9532 -0.0388 -0.0111 -0.1529 528 PRO A O   
4117 C CB  . PRO A 528 ? 1.0519 0.8899 0.9277 -0.0572 -0.0516 -0.1637 528 PRO A CB  
4118 C CG  . PRO A 528 ? 0.9842 0.8285 0.8510 -0.0556 -0.0742 -0.1525 528 PRO A CG  
4119 C CD  . PRO A 528 ? 1.0153 0.8528 0.8617 -0.0537 -0.0652 -0.1438 528 PRO A CD  
4120 N N   . GLY A 529 ? 0.8828 0.7603 0.8379 -0.0348 -0.0430 -0.1394 529 GLY A N   
4121 C CA  . GLY A 529 ? 0.7676 0.6630 0.7629 -0.0277 -0.0399 -0.1330 529 GLY A CA  
4122 C C   . GLY A 529 ? 0.7677 0.6699 0.7872 -0.0283 -0.0445 -0.1401 529 GLY A C   
4123 O O   . GLY A 529 ? 0.8018 0.6974 0.8098 -0.0338 -0.0544 -0.1494 529 GLY A O   
4124 N N   . PHE A 530 ? 0.7567 0.6722 0.8101 -0.0233 -0.0376 -0.1351 530 PHE A N   
4125 C CA  . PHE A 530 ? 0.6606 0.5834 0.7408 -0.0232 -0.0397 -0.1402 530 PHE A CA  
4126 C C   . PHE A 530 ? 0.6302 0.5582 0.7130 -0.0242 -0.0596 -0.1421 530 PHE A C   
4127 O O   . PHE A 530 ? 0.4779 0.4157 0.5705 -0.0207 -0.0675 -0.1339 530 PHE A O   
4128 C CB  . PHE A 530 ? 0.6229 0.5342 0.7000 -0.0279 -0.0292 -0.1525 530 PHE A CB  
4129 C CG  . PHE A 530 ? 0.7183 0.6241 0.7997 -0.0268 -0.0079 -0.1509 530 PHE A CG  
4130 C CD1 . PHE A 530 ? 0.6618 0.5782 0.7775 -0.0223 0.0030  -0.1437 530 PHE A CD1 
4131 C CD2 . PHE A 530 ? 0.7338 0.6234 0.7862 -0.0309 0.0016  -0.1558 530 PHE A CD2 
4132 C CE1 . PHE A 530 ? 0.5895 0.5018 0.7149 -0.0211 0.0217  -0.1406 530 PHE A CE1 
4133 C CE2 . PHE A 530 ? 0.6170 0.5013 0.6784 -0.0297 0.0227  -0.1544 530 PHE A CE2 
4134 C CZ  . PHE A 530 ? 0.5785 0.4749 0.6788 -0.0244 0.0323  -0.1463 530 PHE A CZ  
4135 N N   . GLY A 531 ? 0.6744 0.5956 0.7505 -0.0295 -0.0674 -0.1530 531 GLY A N   
4136 C CA  . GLY A 531 ? 0.5528 0.4795 0.6365 -0.0307 -0.0872 -0.1543 531 GLY A CA  
4137 C C   . GLY A 531 ? 0.6243 0.5488 0.6867 -0.0311 -0.1024 -0.1477 531 GLY A C   
4138 O O   . GLY A 531 ? 0.6169 0.5507 0.6961 -0.0287 -0.1157 -0.1425 531 GLY A O   
4139 N N   . GLU A 532 ? 0.7305 0.6420 0.7572 -0.0345 -0.0997 -0.1475 532 GLU A N   
4140 C CA  . GLU A 532 ? 0.7448 0.6525 0.7487 -0.0355 -0.1140 -0.1401 532 GLU A CA  
4141 C C   . GLU A 532 ? 0.7442 0.6623 0.7628 -0.0281 -0.1120 -0.1277 532 GLU A C   
4142 O O   . GLU A 532 ? 0.7291 0.6472 0.7394 -0.0276 -0.1252 -0.1202 532 GLU A O   
4143 C CB  . GLU A 532 ? 0.7719 0.6613 0.7316 -0.0419 -0.1087 -0.1431 532 GLU A CB  
4144 C CG  . GLU A 532 ? 0.8680 0.7441 0.8060 -0.0518 -0.1111 -0.1566 532 GLU A CG  
4145 C CD  . GLU A 532 ? 0.8718 0.7494 0.8074 -0.0572 -0.1372 -0.1578 532 GLU A CD  
4146 O OE1 . GLU A 532 ? 0.9347 0.8190 0.8747 -0.0543 -0.1537 -0.1469 532 GLU A OE1 
4147 O OE2 . GLU A 532 ? 0.8722 0.7444 0.8040 -0.0646 -0.1412 -0.1694 532 GLU A OE2 
4148 N N   . ASN A 533 ? 0.6253 0.5518 0.6656 -0.0231 -0.0964 -0.1248 533 ASN A N   
4149 C CA  . ASN A 533 ? 0.6374 0.5733 0.6905 -0.0178 -0.0943 -0.1143 533 ASN A CA  
4150 C C   . ASN A 533 ? 0.6321 0.5778 0.7083 -0.0158 -0.1084 -0.1112 533 ASN A C   
4151 O O   . ASN A 533 ? 0.6139 0.5645 0.6964 -0.0127 -0.1092 -0.1032 533 ASN A O   
4152 C CB  . ASN A 533 ? 0.6409 0.5846 0.7135 -0.0148 -0.0772 -0.1118 533 ASN A CB  
4153 C CG  . ASN A 533 ? 0.5717 0.5073 0.6275 -0.0154 -0.0621 -0.1112 533 ASN A CG  
4154 O OD1 . ASN A 533 ? 0.6195 0.5446 0.6477 -0.0170 -0.0622 -0.1101 533 ASN A OD1 
4155 N ND2 . ASN A 533 ? 0.5692 0.5092 0.6431 -0.0143 -0.0485 -0.1112 533 ASN A ND2 
4156 N N   . SER A 534 ? 0.6221 0.5701 0.7130 -0.0179 -0.1184 -0.1177 534 SER A N   
4157 C CA  . SER A 534 ? 0.5640 0.5206 0.6809 -0.0161 -0.1314 -0.1150 534 SER A CA  
4158 C C   . SER A 534 ? 0.5370 0.4896 0.6404 -0.0163 -0.1464 -0.1075 534 SER A C   
4159 O O   . SER A 534 ? 0.5612 0.5208 0.6873 -0.0133 -0.1525 -0.1017 534 SER A O   
4160 C CB  . SER A 534 ? 0.5728 0.5318 0.7079 -0.0190 -0.1401 -0.1236 534 SER A CB  
4161 O OG  . SER A 534 ? 0.6879 0.6361 0.7962 -0.0249 -0.1493 -0.1294 534 SER A OG  
4162 N N   . ARG A 535 ? 0.5594 0.4999 0.6265 -0.0203 -0.1517 -0.1073 535 ARG A N   
4163 C CA  . ARG A 535 ? 0.6593 0.5949 0.7104 -0.0209 -0.1659 -0.0983 535 ARG A CA  
4164 C C   . ARG A 535 ? 0.6879 0.6272 0.7442 -0.0155 -0.1568 -0.0890 535 ARG A C   
4165 O O   . ARG A 535 ? 0.6724 0.6139 0.7382 -0.0134 -0.1673 -0.0805 535 ARG A O   
4166 C CB  . ARG A 535 ? 0.7305 0.6504 0.7360 -0.0276 -0.1699 -0.1002 535 ARG A CB  
4167 C CG  . ARG A 535 ? 0.7421 0.6562 0.7376 -0.0351 -0.1787 -0.1107 535 ARG A CG  
4168 C CD  . ARG A 535 ? 0.9183 0.8142 0.8637 -0.0437 -0.1798 -0.1138 535 ARG A CD  
4169 N NE  . ARG A 535 ? 1.0132 0.9022 0.9467 -0.0524 -0.1858 -0.1258 535 ARG A NE  
4170 C CZ  . ARG A 535 ? 1.0183 0.9051 0.9445 -0.0596 -0.2095 -0.1258 535 ARG A CZ  
4171 N NH1 . ARG A 535 ? 1.0823 0.9734 1.0144 -0.0586 -0.2302 -0.1133 535 ARG A NH1 
4172 N NH2 . ARG A 535 ? 1.0119 0.8920 0.9267 -0.0684 -0.2128 -0.1383 535 ARG A NH2 
4173 N N   . VAL A 536 ? 0.5188 0.4588 0.5710 -0.0135 -0.1375 -0.0901 536 VAL A N   
4174 C CA  . VAL A 536 ? 0.5631 0.5072 0.6213 -0.0095 -0.1284 -0.0822 536 VAL A CA  
4175 C C   . VAL A 536 ? 0.5278 0.4843 0.6239 -0.0065 -0.1266 -0.0817 536 VAL A C   
4176 O O   . VAL A 536 ? 0.5341 0.4936 0.6418 -0.0042 -0.1279 -0.0753 536 VAL A O   
4177 C CB  . VAL A 536 ? 0.6655 0.6068 0.7088 -0.0093 -0.1099 -0.0827 536 VAL A CB  
4178 C CG1 . VAL A 536 ? 0.5327 0.4793 0.5840 -0.0063 -0.1013 -0.0751 536 VAL A CG1 
4179 C CG2 . VAL A 536 ? 0.6336 0.5605 0.6396 -0.0128 -0.1089 -0.0839 536 VAL A CG2 
4180 N N   . LEU A 537 ? 0.5086 0.4713 0.6244 -0.0071 -0.1222 -0.0887 537 LEU A N   
4181 C CA  . LEU A 537 ? 0.5228 0.4956 0.6725 -0.0057 -0.1181 -0.0892 537 LEU A CA  
4182 C C   . LEU A 537 ? 0.5671 0.5423 0.7390 -0.0046 -0.1324 -0.0871 537 LEU A C   
4183 O O   . LEU A 537 ? 0.4899 0.4707 0.6873 -0.0032 -0.1278 -0.0855 537 LEU A O   
4184 C CB  . LEU A 537 ? 0.4109 0.3886 0.5757 -0.0071 -0.1110 -0.0968 537 LEU A CB  
4185 C CG  . LEU A 537 ? 0.5060 0.4832 0.6581 -0.0079 -0.0961 -0.0972 537 LEU A CG  
4186 C CD1 . LEU A 537 ? 0.6116 0.5942 0.7835 -0.0092 -0.0895 -0.1029 537 LEU A CD1 
4187 C CD2 . LEU A 537 ? 0.4126 0.3927 0.5613 -0.0074 -0.0858 -0.0901 537 LEU A CD2 
4188 N N   . GLU A 538 ? 0.5389 0.5093 0.7025 -0.0059 -0.1494 -0.0869 538 GLU A N   
4189 C CA  . GLU A 538 ? 0.4615 0.4347 0.6492 -0.0048 -0.1654 -0.0824 538 GLU A CA  
4190 C C   . GLU A 538 ? 0.4435 0.4153 0.6318 -0.0021 -0.1652 -0.0725 538 GLU A C   
4191 O O   . GLU A 538 ? 0.4309 0.4078 0.6526 0.0002  -0.1665 -0.0695 538 GLU A O   
4192 C CB  . GLU A 538 ? 0.6285 0.5963 0.8018 -0.0085 -0.1860 -0.0824 538 GLU A CB  
4193 C CG  . GLU A 538 ? 0.6518 0.6231 0.8524 -0.0078 -0.2058 -0.0755 538 GLU A CG  
4194 C CD  . GLU A 538 ? 0.7455 0.7111 0.9271 -0.0134 -0.2286 -0.0742 538 GLU A CD  
4195 O OE1 . GLU A 538 ? 0.8096 0.7667 0.9527 -0.0181 -0.2269 -0.0798 538 GLU A OE1 
4196 O OE2 . GLU A 538 ? 0.6478 0.6171 0.8534 -0.0137 -0.2481 -0.0676 538 GLU A OE2 
4197 N N   . TRP A 539 ? 0.4989 0.4629 0.6525 -0.0024 -0.1623 -0.0678 539 TRP A N   
4198 C CA  . TRP A 539 ? 0.5006 0.4625 0.6538 0.0001  -0.1610 -0.0584 539 TRP A CA  
4199 C C   . TRP A 539 ? 0.4736 0.4420 0.6493 0.0019  -0.1434 -0.0601 539 TRP A C   
4200 O O   . TRP A 539 ? 0.4317 0.4013 0.6274 0.0039  -0.1428 -0.0549 539 TRP A O   
4201 C CB  . TRP A 539 ? 0.5398 0.4915 0.6505 -0.0011 -0.1589 -0.0540 539 TRP A CB  
4202 C CG  . TRP A 539 ? 0.6508 0.5994 0.7593 0.0013  -0.1576 -0.0441 539 TRP A CG  
4203 C CD1 . TRP A 539 ? 0.6330 0.5785 0.7476 0.0023  -0.1727 -0.0342 539 TRP A CD1 
4204 C CD2 . TRP A 539 ? 0.6781 0.6264 0.7793 0.0025  -0.1407 -0.0425 539 TRP A CD2 
4205 N NE1 . TRP A 539 ? 0.7446 0.6874 0.8565 0.0045  -0.1649 -0.0270 539 TRP A NE1 
4206 C CE2 . TRP A 539 ? 0.7355 0.6799 0.8386 0.0044  -0.1453 -0.0325 539 TRP A CE2 
4207 C CE3 . TRP A 539 ? 0.5559 0.5071 0.6508 0.0016  -0.1231 -0.0476 539 TRP A CE3 
4208 C CZ2 . TRP A 539 ? 0.7738 0.7167 0.8718 0.0054  -0.1320 -0.0290 539 TRP A CZ2 
4209 C CZ3 . TRP A 539 ? 0.6043 0.5548 0.6941 0.0022  -0.1115 -0.0434 539 TRP A CZ3 
4210 C CH2 . TRP A 539 ? 0.7046 0.6508 0.7956 0.0040  -0.1155 -0.0349 539 TRP A CH2 
4211 N N   . MET A 540 ? 0.4340 0.4058 0.6063 0.0004  -0.1288 -0.0670 540 MET A N   
4212 C CA  . MET A 540 ? 0.4707 0.4479 0.6602 -0.0003 -0.1129 -0.0689 540 MET A CA  
4213 C C   . MET A 540 ? 0.4421 0.4248 0.6709 -0.0003 -0.1130 -0.0725 540 MET A C   
4214 O O   . MET A 540 ? 0.3756 0.3597 0.6219 -0.0010 -0.1031 -0.0723 540 MET A O   
4215 C CB  . MET A 540 ? 0.3830 0.3628 0.5600 -0.0029 -0.0997 -0.0735 540 MET A CB  
4216 C CG  . MET A 540 ? 0.3913 0.3657 0.5351 -0.0029 -0.0967 -0.0703 540 MET A CG  
4217 S SD  . MET A 540 ? 0.4182 0.3972 0.5564 -0.0058 -0.0814 -0.0732 540 MET A SD  
4218 C CE  . MET A 540 ? 0.5111 0.4823 0.6163 -0.0050 -0.0790 -0.0691 540 MET A CE  
4219 N N   . PHE A 541 ? 0.4653 0.4504 0.7091 -0.0001 -0.1230 -0.0766 541 PHE A N   
4220 C CA  . PHE A 541 ? 0.4341 0.4243 0.7190 0.0000  -0.1224 -0.0803 541 PHE A CA  
4221 C C   . PHE A 541 ? 0.4239 0.4131 0.7330 0.0027  -0.1303 -0.0734 541 PHE A C   
4222 O O   . PHE A 541 ? 0.4395 0.4307 0.7800 0.0025  -0.1202 -0.0754 541 PHE A O   
4223 C CB  . PHE A 541 ? 0.5433 0.5363 0.8396 -0.0005 -0.1328 -0.0857 541 PHE A CB  
4224 C CG  . PHE A 541 ? 0.6081 0.6067 0.9456 -0.0013 -0.1268 -0.0918 541 PHE A CG  
4225 C CD1 . PHE A 541 ? 0.6053 0.6060 0.9809 0.0007  -0.1340 -0.0891 541 PHE A CD1 
4226 C CD2 . PHE A 541 ? 0.4749 0.4761 0.8149 -0.0042 -0.1134 -0.0996 541 PHE A CD2 
4227 C CE1 . PHE A 541 ? 0.6483 0.6531 1.0643 -0.0003 -0.1263 -0.0953 541 PHE A CE1 
4228 C CE2 . PHE A 541 ? 0.4991 0.5040 0.8757 -0.0056 -0.1061 -0.1055 541 PHE A CE2 
4229 C CZ  . PHE A 541 ? 0.7191 0.7256 1.1340 -0.0037 -0.1118 -0.1040 541 PHE A CZ  
4230 N N   . GLY A 542 ? 0.4510 0.4363 0.7461 0.0047  -0.1477 -0.0651 542 GLY A N   
4231 C CA  . GLY A 542 ? 0.6147 0.5991 0.9346 0.0075  -0.1570 -0.0562 542 GLY A CA  
4232 C C   . GLY A 542 ? 0.5509 0.5324 0.8710 0.0083  -0.1422 -0.0530 542 GLY A C   
4233 O O   . GLY A 542 ? 0.5161 0.4985 0.8719 0.0099  -0.1388 -0.0505 542 GLY A O   
4234 N N   . ARG A 543 ? 0.5309 0.5087 0.8135 0.0069  -0.1326 -0.0532 543 ARG A N   
4235 C CA  . ARG A 543 ? 0.5243 0.4994 0.8053 0.0065  -0.1182 -0.0510 543 ARG A CA  
4236 C C   . ARG A 543 ? 0.5301 0.5085 0.8390 0.0034  -0.0998 -0.0594 543 ARG A C   
4237 O O   . ARG A 543 ? 0.4427 0.4187 0.7692 0.0030  -0.0903 -0.0582 543 ARG A O   
4238 C CB  . ARG A 543 ? 0.5321 0.5038 0.7702 0.0048  -0.1113 -0.0504 543 ARG A CB  
4239 C CG  . ARG A 543 ? 0.5564 0.5215 0.7643 0.0068  -0.1249 -0.0417 543 ARG A CG  
4240 C CD  . ARG A 543 ? 0.6832 0.6437 0.9009 0.0095  -0.1303 -0.0315 543 ARG A CD  
4241 N NE  . ARG A 543 ? 0.6819 0.6416 0.9025 0.0085  -0.1131 -0.0320 543 ARG A NE  
4242 C CZ  . ARG A 543 ? 0.6773 0.6333 0.9123 0.0103  -0.1120 -0.0250 543 ARG A CZ  
4243 N NH1 . ARG A 543 ? 0.8770 0.8304 1.1270 0.0138  -0.1279 -0.0151 543 ARG A NH1 
4244 N NH2 . ARG A 543 ? 0.6906 0.6456 0.9261 0.0080  -0.0952 -0.0274 543 ARG A NH2 
4245 N N   . ILE A 544 ? 0.6078 0.5905 0.9204 0.0004  -0.0935 -0.0683 544 ILE A N   
4246 C CA  . ILE A 544 ? 0.6357 0.6199 0.9708 -0.0042 -0.0752 -0.0767 544 ILE A CA  
4247 C C   . ILE A 544 ? 0.6123 0.5966 0.9949 -0.0023 -0.0757 -0.0772 544 ILE A C   
4248 O O   . ILE A 544 ? 0.5414 0.5229 0.9442 -0.0054 -0.0596 -0.0811 544 ILE A O   
4249 C CB  . ILE A 544 ? 0.6624 0.6505 0.9899 -0.0079 -0.0695 -0.0845 544 ILE A CB  
4250 C CG1 . ILE A 544 ? 0.6028 0.5909 0.8895 -0.0103 -0.0657 -0.0832 544 ILE A CG1 
4251 C CG2 . ILE A 544 ? 0.7146 0.7029 1.0666 -0.0136 -0.0515 -0.0931 544 ILE A CG2 
4252 C CD1 . ILE A 544 ? 0.6070 0.5989 0.8871 -0.0140 -0.0600 -0.0889 544 ILE A CD1 
4253 N N   . GLU A 545 ? 0.6189 0.6062 1.0216 0.0022  -0.0936 -0.0735 545 GLU A N   
4254 C CA  . GLU A 545 ? 0.4951 0.4835 0.9487 0.0047  -0.0963 -0.0718 545 GLU A CA  
4255 C C   . GLU A 545 ? 0.5789 0.5629 1.0445 0.0078  -0.0986 -0.0623 545 GLU A C   
4256 O O   . GLU A 545 ? 0.6582 0.6419 1.1701 0.0092  -0.0945 -0.0614 545 GLU A O   
4257 C CB  . GLU A 545 ? 0.6053 0.5987 1.0768 0.0079  -0.1182 -0.0686 545 GLU A CB  
4258 C CG  . GLU A 545 ? 0.5053 0.5030 0.9797 0.0050  -0.1142 -0.0788 545 GLU A CG  
4259 C CD  . GLU A 545 ? 0.6950 0.6977 1.1890 0.0073  -0.1364 -0.0761 545 GLU A CD  
4260 O OE1 . GLU A 545 ? 0.7647 0.7669 1.2516 0.0100  -0.1579 -0.0657 545 GLU A OE1 
4261 O OE2 . GLU A 545 ? 0.6324 0.6391 1.1481 0.0056  -0.1327 -0.0841 545 GLU A OE2 
4262 N N   . GLY A 546 ? 0.6882 0.6686 1.1159 0.0088  -0.1040 -0.0551 546 GLY A N   
4263 C CA  . GLY A 546 ? 0.5054 0.4809 0.9418 0.0115  -0.1049 -0.0457 546 GLY A CA  
4264 C C   . GLY A 546 ? 0.6317 0.6067 1.0681 0.0166  -0.1306 -0.0312 546 GLY A C   
4265 O O   . GLY A 546 ? 0.7042 0.6775 1.1718 0.0199  -0.1357 -0.0218 546 GLY A O   
4266 N N   . GLU A 547 ? 0.6674 0.6432 1.0690 0.0164  -0.1468 -0.0290 547 GLU A N   
4267 C CA  . GLU A 547 ? 0.7281 0.7018 1.1206 0.0188  -0.1719 -0.0153 547 GLU A CA  
4268 C C   . GLU A 547 ? 0.8279 0.7938 1.1835 0.0193  -0.1714 -0.0067 547 GLU A C   
4269 O O   . GLU A 547 ? 0.7609 0.7239 1.0885 0.0175  -0.1544 -0.0126 547 GLU A O   
4270 C CB  . GLU A 547 ? 0.7173 0.6931 1.0855 0.0166  -0.1884 -0.0177 547 GLU A CB  
4271 C CG  . GLU A 547 ? 0.8814 0.8650 1.2895 0.0164  -0.1934 -0.0238 547 GLU A CG  
4272 C CD  . GLU A 547 ? 0.9626 0.9474 1.3486 0.0136  -0.2127 -0.0250 547 GLU A CD  
4273 O OE1 . GLU A 547 ? 0.9880 0.9666 1.3251 0.0114  -0.2196 -0.0225 547 GLU A OE1 
4274 O OE2 . GLU A 547 ? 1.0355 1.0267 1.4535 0.0131  -0.2199 -0.0291 547 GLU A OE2 
4275 N N   . ASP A 548 ? 0.9249 0.8872 1.2814 0.0214  -0.1911 0.0083  548 ASP A N   
4276 C CA  . ASP A 548 ? 1.0039 0.9577 1.3290 0.0220  -0.1919 0.0184  548 ASP A CA  
4277 C C   . ASP A 548 ? 1.0394 0.9876 1.3124 0.0189  -0.2078 0.0224  548 ASP A C   
4278 O O   . ASP A 548 ? 1.0304 0.9745 1.2953 0.0183  -0.2297 0.0355  548 ASP A O   
4279 C CB  . ASP A 548 ? 1.0068 0.9587 1.3682 0.0257  -0.2010 0.0336  548 ASP A CB  
4280 C CG  . ASP A 548 ? 1.1253 1.0678 1.4578 0.0264  -0.1991 0.0440  548 ASP A CG  
4281 O OD1 . ASP A 548 ? 1.1666 1.1048 1.4560 0.0241  -0.1868 0.0377  548 ASP A OD1 
4282 O OD2 . ASP A 548 ? 1.2340 1.1736 1.5894 0.0292  -0.2098 0.0592  548 ASP A OD2 
4283 N N   . SER A 549 ? 0.9394 0.8867 1.1764 0.0161  -0.1961 0.0108  549 SER A N   
4284 C CA  . SER A 549 ? 0.9055 0.8460 1.0926 0.0123  -0.2057 0.0113  549 SER A CA  
4285 C C   . SER A 549 ? 0.8192 0.7535 0.9662 0.0111  -0.1882 0.0075  549 SER A C   
4286 O O   . SER A 549 ? 0.8121 0.7404 0.9189 0.0076  -0.1901 0.0045  549 SER A O   
4287 C CB  . SER A 549 ? 0.8154 0.7610 1.0013 0.0094  -0.2115 0.0008  549 SER A CB  
4288 O OG  . SER A 549 ? 0.8738 0.8259 1.0710 0.0098  -0.1914 -0.0126 549 SER A OG  
4289 N N   . ALA A 550 ? 0.8491 0.7842 1.0076 0.0133  -0.1708 0.0071  550 ALA A N   
4290 C CA  . ALA A 550 ? 0.7837 0.7143 0.9105 0.0120  -0.1542 0.0039  550 ALA A CA  
4291 C C   . ALA A 550 ? 0.8002 0.7212 0.9089 0.0129  -0.1564 0.0163  550 ALA A C   
4292 O O   . ALA A 550 ? 0.8394 0.7584 0.9675 0.0151  -0.1673 0.0274  550 ALA A O   
4293 C CB  . ALA A 550 ? 0.6211 0.5588 0.7688 0.0120  -0.1336 -0.0051 550 ALA A CB  
4294 N N   . LYS A 551 ? 0.7838 0.6986 0.8571 0.0111  -0.1454 0.0150  551 LYS A N   
4295 C CA  . LYS A 551 ? 0.6949 0.5994 0.7469 0.0114  -0.1442 0.0257  551 LYS A CA  
4296 C C   . LYS A 551 ? 0.7519 0.6570 0.7971 0.0111  -0.1227 0.0208  551 LYS A C   
4297 O O   . LYS A 551 ? 0.6809 0.5908 0.7191 0.0093  -0.1119 0.0107  551 LYS A O   
4298 C CB  . LYS A 551 ? 0.6821 0.5747 0.6898 0.0079  -0.1555 0.0308  551 LYS A CB  
4299 C CG  . LYS A 551 ? 0.8538 0.7342 0.8403 0.0076  -0.1583 0.0445  551 LYS A CG  
4300 C CD  . LYS A 551 ? 0.8786 0.7459 0.8205 0.0022  -0.1720 0.0498  551 LYS A CD  
4301 C CE  . LYS A 551 ? 0.7666 0.6296 0.6746 -0.0019 -0.1599 0.0375  551 LYS A CE  
4302 N NZ  . LYS A 551 ? 1.1169 0.9649 0.9783 -0.0090 -0.1710 0.0406  551 LYS A NZ  
4303 N N   . LEU A 552 ? 0.7246 0.6250 0.7738 0.0125  -0.1172 0.0288  552 LEU A N   
4304 C CA  . LEU A 552 ? 0.6967 0.5986 0.7455 0.0116  -0.0979 0.0248  552 LEU A CA  
4305 C C   . LEU A 552 ? 0.7011 0.5937 0.7108 0.0099  -0.0916 0.0274  552 LEU A C   
4306 O O   . LEU A 552 ? 0.6279 0.5091 0.6157 0.0100  -0.0988 0.0374  552 LEU A O   
4307 C CB  . LEU A 552 ? 0.6783 0.5794 0.7543 0.0135  -0.0931 0.0308  552 LEU A CB  
4308 C CG  . LEU A 552 ? 0.6663 0.5688 0.7446 0.0114  -0.0741 0.0268  552 LEU A CG  
4309 C CD1 . LEU A 552 ? 0.7252 0.6384 0.8115 0.0078  -0.0637 0.0136  552 LEU A CD1 
4310 C CD2 . LEU A 552 ? 0.7355 0.6359 0.8428 0.0128  -0.0697 0.0318  552 LEU A CD2 
4311 N N   . THR A 553 ? 0.7087 0.6057 0.7109 0.0077  -0.0779 0.0191  553 THR A N   
4312 C CA  . THR A 553 ? 0.6351 0.5247 0.6073 0.0060  -0.0681 0.0201  553 THR A CA  
4313 C C   . THR A 553 ? 0.6645 0.5604 0.6484 0.0046  -0.0518 0.0169  553 THR A C   
4314 O O   . THR A 553 ? 0.6456 0.5517 0.6556 0.0037  -0.0481 0.0119  553 THR A O   
4315 C CB  . THR A 553 ? 0.7712 0.6596 0.7225 0.0041  -0.0690 0.0133  553 THR A CB  
4316 O OG1 . THR A 553 ? 0.7348 0.6361 0.7064 0.0035  -0.0646 0.0038  553 THR A OG1 
4317 C CG2 . THR A 553 ? 0.7486 0.6302 0.6856 0.0036  -0.0864 0.0159  553 THR A CG2 
4318 N N   . PRO A 554 ? 0.7418 0.6312 0.7065 0.0034  -0.0413 0.0195  554 PRO A N   
4319 C CA  . PRO A 554 ? 0.6718 0.5678 0.6488 0.0012  -0.0273 0.0175  554 PRO A CA  
4320 C C   . PRO A 554 ? 0.7121 0.6211 0.7019 -0.0014 -0.0228 0.0089  554 PRO A C   
4321 O O   . PRO A 554 ? 0.6314 0.5482 0.6356 -0.0047 -0.0145 0.0072  554 PRO A O   
4322 C CB  . PRO A 554 ? 0.6430 0.5283 0.5961 0.0008  -0.0180 0.0223  554 PRO A CB  
4323 C CG  . PRO A 554 ? 0.7206 0.5916 0.6494 0.0024  -0.0274 0.0290  554 PRO A CG  
4324 C CD  . PRO A 554 ? 0.7635 0.6382 0.6948 0.0031  -0.0417 0.0251  554 PRO A CD  
4325 N N   . ILE A 555 ? 0.6541 0.5653 0.6389 -0.0009 -0.0284 0.0040  555 ILE A N   
4326 C CA  . ILE A 555 ? 0.6639 0.5868 0.6610 -0.0034 -0.0247 -0.0026 555 ILE A CA  
4327 C C   . ILE A 555 ? 0.7048 0.6359 0.7206 -0.0038 -0.0323 -0.0080 555 ILE A C   
4328 O O   . ILE A 555 ? 0.6352 0.5765 0.6639 -0.0070 -0.0287 -0.0127 555 ILE A O   
4329 C CB  . ILE A 555 ? 0.6674 0.5872 0.6489 -0.0032 -0.0217 -0.0050 555 ILE A CB  
4330 C CG1 . ILE A 555 ? 0.6693 0.5820 0.6370 -0.0013 -0.0327 -0.0074 555 ILE A CG1 
4331 C CG2 . ILE A 555 ? 0.6849 0.5957 0.6504 -0.0034 -0.0111 -0.0004 555 ILE A CG2 
4332 C CD1 . ILE A 555 ? 0.7049 0.6131 0.6576 -0.0021 -0.0285 -0.0118 555 ILE A CD1 
4333 N N   . GLY A 556 ? 0.8034 0.7302 0.8223 -0.0010 -0.0427 -0.0069 556 GLY A N   
4334 C CA  . GLY A 556 ? 0.7595 0.6935 0.7996 -0.0012 -0.0488 -0.0121 556 GLY A CA  
4335 C C   . GLY A 556 ? 0.7053 0.6335 0.7450 0.0024  -0.0630 -0.0093 556 GLY A C   
4336 O O   . GLY A 556 ? 0.7806 0.6990 0.8042 0.0043  -0.0684 -0.0020 556 GLY A O   
4337 N N   . TYR A 557 ? 0.7008 0.6352 0.7588 0.0025  -0.0693 -0.0146 557 TYR A N   
4338 C CA  . TYR A 557 ? 0.6468 0.5779 0.7102 0.0052  -0.0847 -0.0120 557 TYR A CA  
4339 C C   . TYR A 557 ? 0.6494 0.5782 0.6926 0.0048  -0.0920 -0.0153 557 TYR A C   
4340 O O   . TYR A 557 ? 0.6591 0.5943 0.7062 0.0032  -0.0875 -0.0231 557 TYR A O   
4341 C CB  . TYR A 557 ? 0.6052 0.5438 0.7042 0.0055  -0.0866 -0.0161 557 TYR A CB  
4342 C CG  . TYR A 557 ? 0.6026 0.5403 0.7238 0.0060  -0.0815 -0.0124 557 TYR A CG  
4343 C CD1 . TYR A 557 ? 0.6605 0.5907 0.7822 0.0092  -0.0896 -0.0020 557 TYR A CD1 
4344 C CD2 . TYR A 557 ? 0.5819 0.5252 0.7234 0.0025  -0.0682 -0.0193 557 TYR A CD2 
4345 C CE1 . TYR A 557 ? 0.6130 0.5418 0.7586 0.0099  -0.0837 0.0014  557 TYR A CE1 
4346 C CE2 . TYR A 557 ? 0.7081 0.6492 0.8706 0.0020  -0.0615 -0.0175 557 TYR A CE2 
4347 C CZ  . TYR A 557 ? 0.5061 0.4401 0.6726 0.0063  -0.0689 -0.0072 557 TYR A CZ  
4348 O OH  . TYR A 557 ? 0.5587 0.4899 0.7493 0.0060  -0.0610 -0.0054 557 TYR A OH  
4349 N N   . VAL A 558 ? 0.6759 0.5947 0.6970 0.0052  -0.1030 -0.0093 558 VAL A N   
4350 C CA  . VAL A 558 ? 0.7106 0.6247 0.7095 0.0032  -0.1105 -0.0132 558 VAL A CA  
4351 C C   . VAL A 558 ? 0.7180 0.6311 0.7251 0.0034  -0.1306 -0.0097 558 VAL A C   
4352 O O   . VAL A 558 ? 0.6659 0.5780 0.6872 0.0054  -0.1389 -0.0008 558 VAL A O   
4353 C CB  . VAL A 558 ? 0.7206 0.6218 0.6803 0.0009  -0.1056 -0.0103 558 VAL A CB  
4354 C CG1 . VAL A 558 ? 0.6807 0.5843 0.6386 0.0008  -0.0863 -0.0129 558 VAL A CG1 
4355 C CG2 . VAL A 558 ? 0.7388 0.6297 0.6845 0.0012  -0.1143 0.0014  558 VAL A CG2 
4356 N N   . PRO A 559 ? 0.7600 0.6734 0.7615 0.0011  -0.1391 -0.0158 559 PRO A N   
4357 C CA  . PRO A 559 ? 0.8220 0.7352 0.8329 0.0004  -0.1602 -0.0118 559 PRO A CA  
4358 C C   . PRO A 559 ? 0.8188 0.7195 0.8016 -0.0019 -0.1736 -0.0001 559 PRO A C   
4359 O O   . PRO A 559 ? 0.8148 0.7038 0.7578 -0.0055 -0.1687 0.0002  559 PRO A O   
4360 C CB  . PRO A 559 ? 0.6692 0.5835 0.6720 -0.0030 -0.1638 -0.0223 559 PRO A CB  
4361 C CG  . PRO A 559 ? 0.8688 0.7885 0.8750 -0.0022 -0.1434 -0.0316 559 PRO A CG  
4362 C CD  . PRO A 559 ? 0.6987 0.6137 0.6899 -0.0011 -0.1299 -0.0266 559 PRO A CD  
4363 N N   . LYS A 560 ? 0.8972 0.7998 0.9021 -0.0002 -0.1900 0.0100  560 LYS A N   
4364 C CA  . LYS A 560 ? 1.0094 0.9006 0.9896 -0.0031 -0.2060 0.0235  560 LYS A CA  
4365 C C   . LYS A 560 ? 1.1548 1.0375 1.0989 -0.0107 -0.2208 0.0211  560 LYS A C   
4366 O O   . LYS A 560 ? 1.1501 1.0366 1.0937 -0.0130 -0.2191 0.0089  560 LYS A O   
4367 C CB  . LYS A 560 ? 0.9727 0.8692 0.9918 0.0006  -0.2215 0.0362  560 LYS A CB  
4368 C CG  . LYS A 560 ? 0.9403 0.8421 0.9923 0.0068  -0.2063 0.0389  560 LYS A CG  
4369 C CD  . LYS A 560 ? 0.9872 0.8911 1.0758 0.0100  -0.2210 0.0533  560 LYS A CD  
4370 C CE  . LYS A 560 ? 0.9197 0.8342 1.0493 0.0109  -0.2352 0.0515  560 LYS A CE  
4371 N NZ  . LYS A 560 ? 0.9442 0.8613 1.1171 0.0146  -0.2485 0.0664  560 LYS A NZ  
4372 N N   . GLU A 561 ? 1.4308 1.3007 1.3429 -0.0157 -0.2354 0.0331  561 GLU A N   
4373 C CA  . GLU A 561 ? 1.5142 1.3737 1.3864 -0.0254 -0.2507 0.0315  561 GLU A CA  
4374 C C   . GLU A 561 ? 1.4642 1.3336 1.3657 -0.0268 -0.2736 0.0318  561 GLU A C   
4375 O O   . GLU A 561 ? 1.4708 1.3501 1.4154 -0.0218 -0.2860 0.0419  561 GLU A O   
4376 C CB  . GLU A 561 ? 1.6715 1.5142 1.5012 -0.0316 -0.2619 0.0460  561 GLU A CB  
4377 C CG  . GLU A 561 ? 1.8485 1.6802 1.6497 -0.0307 -0.2392 0.0463  561 GLU A CG  
4378 C CD  . GLU A 561 ? 2.1764 1.9903 1.9343 -0.0375 -0.2496 0.0612  561 GLU A CD  
4379 O OE1 . GLU A 561 ? 2.2737 2.0822 2.0152 -0.0450 -0.2752 0.0701  561 GLU A OE1 
4380 O OE2 . GLU A 561 ? 2.2467 2.0519 1.9869 -0.0361 -0.2328 0.0646  561 GLU A OE2 
4381 N N   . ASP A 562 ? 1.3632 1.2297 1.2437 -0.0339 -0.2781 0.0204  562 ASP A N   
4382 C CA  . ASP A 562 ? 1.3490 1.2248 1.2561 -0.0362 -0.2990 0.0187  562 ASP A CA  
4383 C C   . ASP A 562 ? 1.2180 1.1122 1.1857 -0.0267 -0.2902 0.0126  562 ASP A C   
4384 O O   . ASP A 562 ? 1.1420 1.0466 1.1499 -0.0252 -0.3072 0.0170  562 ASP A O   
4385 C CB  . ASP A 562 ? 1.4468 1.3204 1.3557 -0.0406 -0.3302 0.0371  562 ASP A CB  
4386 C CG  . ASP A 562 ? 1.5766 1.4306 1.4204 -0.0529 -0.3418 0.0429  562 ASP A CG  
4387 O OD1 . ASP A 562 ? 1.6597 1.5029 1.4606 -0.0604 -0.3308 0.0289  562 ASP A OD1 
4388 O OD2 . ASP A 562 ? 1.6407 1.4893 1.4764 -0.0557 -0.3612 0.0615  562 ASP A OD2 
4389 N N   . ALA A 563 ? 1.1640 1.0620 1.1389 -0.0210 -0.2634 0.0028  563 ALA A N   
4390 C CA  . ALA A 563 ? 1.0113 0.9246 1.0368 -0.0137 -0.2521 -0.0040 563 ALA A CA  
4391 C C   . ALA A 563 ? 0.8524 0.7700 0.8788 -0.0152 -0.2413 -0.0206 563 ALA A C   
4392 O O   . ALA A 563 ? 0.5756 0.5051 0.6427 -0.0120 -0.2404 -0.0259 563 ALA A O   
4393 C CB  . ALA A 563 ? 0.9613 0.8769 0.9986 -0.0071 -0.2309 -0.0021 563 ALA A CB  
4394 N N   . LEU A 564 ? 0.8903 0.7979 0.8746 -0.0202 -0.2318 -0.0286 564 LEU A N   
4395 C CA  . LEU A 564 ? 0.8926 0.8030 0.8775 -0.0219 -0.2212 -0.0436 564 LEU A CA  
4396 C C   . LEU A 564 ? 0.9554 0.8618 0.9280 -0.0299 -0.2403 -0.0481 564 LEU A C   
4397 O O   . LEU A 564 ? 0.9709 0.8652 0.9067 -0.0374 -0.2546 -0.0432 564 LEU A O   
4398 C CB  . LEU A 564 ? 0.8970 0.7984 0.8486 -0.0232 -0.1992 -0.0503 564 LEU A CB  
4399 C CG  . LEU A 564 ? 0.7763 0.6846 0.7450 -0.0163 -0.1775 -0.0499 564 LEU A CG  
4400 C CD1 . LEU A 564 ? 0.8465 0.7460 0.7852 -0.0183 -0.1580 -0.0558 564 LEU A CD1 
4401 C CD2 . LEU A 564 ? 0.6888 0.6121 0.7009 -0.0119 -0.1718 -0.0557 564 LEU A CD2 
4402 N N   . ASN A 565 ? 1.0525 0.9688 1.0550 -0.0291 -0.2405 -0.0574 565 ASN A N   
4403 C CA  . ASN A 565 ? 0.8440 0.7577 0.8386 -0.0371 -0.2575 -0.0636 565 ASN A CA  
4404 C C   . ASN A 565 ? 0.9834 0.8826 0.9305 -0.0450 -0.2474 -0.0745 565 ASN A C   
4405 O O   . ASN A 565 ? 1.0366 0.9377 0.9898 -0.0443 -0.2311 -0.0869 565 ASN A O   
4406 C CB  . ASN A 565 ? 0.9352 0.8631 0.9771 -0.0338 -0.2575 -0.0712 565 ASN A CB  
4407 C CG  . ASN A 565 ? 0.9059 0.8333 0.9487 -0.0418 -0.2794 -0.0754 565 ASN A CG  
4408 O OD1 . ASN A 565 ? 0.9528 0.8676 0.9533 -0.0515 -0.2906 -0.0766 565 ASN A OD1 
4409 N ND2 . ASN A 565 ? 0.7963 0.7368 0.8868 -0.0388 -0.2851 -0.0780 565 ASN A ND2 
4410 N N   . LEU A 566 ? 1.1200 1.0038 1.0201 -0.0528 -0.2558 -0.0698 566 LEU A N   
4411 C CA  . LEU A 566 ? 1.2009 1.0678 1.0526 -0.0619 -0.2447 -0.0806 566 LEU A CA  
4412 C C   . LEU A 566 ? 1.3032 1.1616 1.1307 -0.0748 -0.2643 -0.0869 566 LEU A C   
4413 O O   . LEU A 566 ? 1.3643 1.2051 1.1442 -0.0852 -0.2581 -0.0952 566 LEU A O   
4414 C CB  . LEU A 566 ? 1.1561 1.0083 0.9660 -0.0639 -0.2367 -0.0731 566 LEU A CB  
4415 C CG  . LEU A 566 ? 1.1021 0.9608 0.9306 -0.0528 -0.2164 -0.0676 566 LEU A CG  
4416 C CD1 . LEU A 566 ? 1.1346 0.9778 0.9215 -0.0558 -0.2103 -0.0599 566 LEU A CD1 
4417 C CD2 . LEU A 566 ? 1.0325 0.8965 0.8782 -0.0481 -0.1911 -0.0798 566 LEU A CD2 
4418 N N   . LYS A 567 ? 1.4301 1.3002 1.2899 -0.0751 -0.2871 -0.0836 567 LYS A N   
4419 C CA  . LYS A 567 ? 1.5626 1.4262 1.4023 -0.0883 -0.3081 -0.0893 567 LYS A CA  
4420 C C   . LYS A 567 ? 1.5467 1.4047 1.3769 -0.0931 -0.2905 -0.1095 567 LYS A C   
4421 O O   . LYS A 567 ? 1.5407 1.4087 1.4048 -0.0841 -0.2707 -0.1170 567 LYS A O   
4422 C CB  . LYS A 567 ? 1.6255 1.5054 1.5127 -0.0862 -0.3345 -0.0815 567 LYS A CB  
4423 C CG  . LYS A 567 ? 1.6333 1.5194 1.5383 -0.0807 -0.3514 -0.0609 567 LYS A CG  
4424 C CD  . LYS A 567 ? 1.6421 1.5456 1.6046 -0.0771 -0.3735 -0.0537 567 LYS A CD  
4425 C CE  . LYS A 567 ? 1.7060 1.6156 1.6924 -0.0708 -0.3875 -0.0330 567 LYS A CE  
4426 N NZ  . LYS A 567 ? 1.8423 1.7689 1.8916 -0.0666 -0.4068 -0.0258 567 LYS A NZ  
4427 N N   . GLY A 568 ? 1.6361 1.4772 1.4191 -0.1084 -0.2977 -0.1179 568 GLY A N   
4428 C CA  . GLY A 568 ? 1.5833 1.4148 1.3504 -0.1149 -0.2792 -0.1376 568 GLY A CA  
4429 C C   . GLY A 568 ? 1.5064 1.3206 1.2342 -0.1166 -0.2502 -0.1445 568 GLY A C   
4430 O O   . GLY A 568 ? 1.5500 1.3484 1.2463 -0.1273 -0.2379 -0.1600 568 GLY A O   
4431 N N   . LEU A 569 ? 1.4537 1.2703 1.1850 -0.1066 -0.2380 -0.1337 569 LEU A N   
4432 C CA  . LEU A 569 ? 1.5047 1.3050 1.2010 -0.1081 -0.2115 -0.1379 569 LEU A CA  
4433 C C   . LEU A 569 ? 1.5527 1.3349 1.1942 -0.1184 -0.2225 -0.1293 569 LEU A C   
4434 O O   . LEU A 569 ? 1.6303 1.3922 1.2221 -0.1341 -0.2242 -0.1383 569 LEU A O   
4435 C CB  . LEU A 569 ? 1.3446 1.1576 1.0763 -0.0921 -0.1910 -0.1315 569 LEU A CB  
4436 C CG  . LEU A 569 ? 1.2024 1.0337 0.9878 -0.0818 -0.1801 -0.1372 569 LEU A CG  
4437 C CD1 . LEU A 569 ? 1.1167 0.9591 0.9299 -0.0686 -0.1626 -0.1291 569 LEU A CD1 
4438 C CD2 . LEU A 569 ? 1.2754 1.0980 1.0546 -0.0878 -0.1628 -0.1550 569 LEU A CD2 
4439 N N   . GLY A 570 ? 1.5122 1.3005 1.1611 -0.1106 -0.2293 -0.1121 570 GLY A N   
4440 C CA  . GLY A 570 ? 1.6140 1.3867 1.2152 -0.1195 -0.2424 -0.1007 570 GLY A CA  
4441 C C   . GLY A 570 ? 1.6827 1.4327 1.2344 -0.1259 -0.2171 -0.1064 570 GLY A C   
4442 O O   . GLY A 570 ? 1.6908 1.4301 1.2113 -0.1287 -0.2202 -0.0946 570 GLY A O   
4443 N N   . ASP A 571 ? 1.6870 1.4289 1.2332 -0.1284 -0.1911 -0.1243 571 ASP A N   
4444 C CA  . ASP A 571 ? 1.7515 1.4709 1.2554 -0.1350 -0.1634 -0.1321 571 ASP A CA  
4445 C C   . ASP A 571 ? 1.8064 1.5337 1.3408 -0.1203 -0.1363 -0.1289 571 ASP A C   
4446 O O   . ASP A 571 ? 1.8885 1.5987 1.3952 -0.1240 -0.1116 -0.1338 571 ASP A O   
4447 C CB  . ASP A 571 ? 1.7913 1.4951 1.2730 -0.1472 -0.1482 -0.1539 571 ASP A CB  
4448 C CG  . ASP A 571 ? 1.7832 1.5048 1.3193 -0.1376 -0.1389 -0.1640 571 ASP A CG  
4449 O OD1 . ASP A 571 ? 1.6802 1.4255 1.2637 -0.1263 -0.1552 -0.1552 571 ASP A OD1 
4450 O OD2 . ASP A 571 ? 1.9141 1.6253 1.4466 -0.1417 -0.1143 -0.1805 571 ASP A OD2 
4451 N N   . VAL A 572 ? 1.7599 1.5121 1.3503 -0.1048 -0.1400 -0.1208 572 VAL A N   
4452 C CA  . VAL A 572 ? 1.6480 1.4089 1.2680 -0.0921 -0.1167 -0.1173 572 VAL A CA  
4453 C C   . VAL A 572 ? 1.6531 1.4063 1.2502 -0.0909 -0.1153 -0.1037 572 VAL A C   
4454 O O   . VAL A 572 ? 1.6460 1.4007 1.2337 -0.0920 -0.1384 -0.0906 572 VAL A O   
4455 C CB  . VAL A 572 ? 1.5287 1.3167 1.2096 -0.0782 -0.1225 -0.1124 572 VAL A CB  
4456 C CG1 . VAL A 572 ? 1.4922 1.2889 1.2019 -0.0673 -0.0987 -0.1098 572 VAL A CG1 
4457 C CG2 . VAL A 572 ? 1.4856 1.2806 1.1878 -0.0802 -0.1268 -0.1246 572 VAL A CG2 
4458 N N   . ASN A 573 ? 1.6313 1.3762 1.2222 -0.0887 -0.0879 -0.1061 573 ASN A N   
4459 C CA  . ASN A 573 ? 1.6465 1.3834 1.2177 -0.0873 -0.0825 -0.0942 573 ASN A CA  
4460 C C   . ASN A 573 ? 1.5567 1.3163 1.1740 -0.0730 -0.0892 -0.0806 573 ASN A C   
4461 O O   . ASN A 573 ? 1.4968 1.2681 1.1490 -0.0637 -0.0720 -0.0814 573 ASN A O   
4462 C CB  . ASN A 573 ? 1.6709 1.3919 1.2255 -0.0898 -0.0497 -0.1021 573 ASN A CB  
4463 C CG  . ASN A 573 ? 1.6926 1.4035 1.2252 -0.0894 -0.0425 -0.0906 573 ASN A CG  
4464 O OD1 . ASN A 573 ? 1.6946 1.4045 1.2107 -0.0906 -0.0628 -0.0777 573 ASN A OD1 
4465 N ND2 . ASN A 573 ? 1.7422 1.4455 1.2770 -0.0876 -0.0133 -0.0947 573 ASN A ND2 
4466 N N   . VAL A 574 ? 1.5667 1.3321 1.1849 -0.0720 -0.1146 -0.0678 574 VAL A N   
4467 C CA  . VAL A 574 ? 1.4761 1.2617 1.1383 -0.0597 -0.1211 -0.0561 574 VAL A CA  
4468 C C   . VAL A 574 ? 1.4807 1.2622 1.1379 -0.0553 -0.1073 -0.0465 574 VAL A C   
4469 O O   . VAL A 574 ? 1.3626 1.1599 1.0580 -0.0452 -0.1025 -0.0410 574 VAL A O   
4470 C CB  . VAL A 574 ? 1.2981 1.0914 0.9697 -0.0598 -0.1519 -0.0455 574 VAL A CB  
4471 C CG1 . VAL A 574 ? 1.2453 1.0462 0.9316 -0.0628 -0.1654 -0.0548 574 VAL A CG1 
4472 C CG2 . VAL A 574 ? 1.4165 1.1914 1.0403 -0.0694 -0.1658 -0.0356 574 VAL A CG2 
4473 N N   . GLU A 575 ? 1.5638 1.3236 1.1740 -0.0635 -0.1001 -0.0448 575 GLU A N   
4474 C CA  . GLU A 575 ? 1.5664 1.3213 1.1716 -0.0598 -0.0866 -0.0356 575 GLU A CA  
4475 C C   . GLU A 575 ? 1.4611 1.2229 1.0936 -0.0531 -0.0594 -0.0422 575 GLU A C   
4476 O O   . GLU A 575 ? 1.4097 1.1828 1.0703 -0.0447 -0.0535 -0.0345 575 GLU A O   
4477 C CB  . GLU A 575 ? 1.7045 1.4326 1.2505 -0.0715 -0.0833 -0.0332 575 GLU A CB  
4478 C CG  . GLU A 575 ? 1.7977 1.5183 1.3144 -0.0792 -0.1126 -0.0230 575 GLU A CG  
4479 C CD  . GLU A 575 ? 1.8509 1.5844 1.3948 -0.0707 -0.1297 -0.0050 575 GLU A CD  
4480 O OE1 . GLU A 575 ? 1.8493 1.5920 1.4225 -0.0609 -0.1159 -0.0007 575 GLU A OE1 
4481 O OE2 . GLU A 575 ? 1.9035 1.6376 1.4412 -0.0743 -0.1570 0.0050  575 GLU A OE2 
4482 N N   . GLU A 576 ? 1.4732 1.2283 1.0993 -0.0572 -0.0428 -0.0561 576 GLU A N   
4483 C CA  . GLU A 576 ? 1.4739 1.2355 1.1285 -0.0514 -0.0177 -0.0612 576 GLU A CA  
4484 C C   . GLU A 576 ? 1.3327 1.1188 1.0388 -0.0425 -0.0214 -0.0628 576 GLU A C   
4485 O O   . GLU A 576 ? 1.3046 1.1007 1.0410 -0.0366 -0.0058 -0.0623 576 GLU A O   
4486 C CB  . GLU A 576 ? 1.5460 1.2889 1.1761 -0.0596 0.0040  -0.0749 576 GLU A CB  
4487 C CG  . GLU A 576 ? 1.6112 1.3582 1.2708 -0.0544 0.0313  -0.0783 576 GLU A CG  
4488 C CD  . GLU A 576 ? 1.8590 1.5856 1.4970 -0.0628 0.0550  -0.0920 576 GLU A CD  
4489 O OE1 . GLU A 576 ? 1.8236 1.5343 1.4245 -0.0731 0.0497  -0.1010 576 GLU A OE1 
4490 O OE2 . GLU A 576 ? 2.0685 1.7947 1.7281 -0.0597 0.0793  -0.0940 576 GLU A OE2 
4491 N N   . LEU A 577 ? 1.2667 1.0625 0.9835 -0.0422 -0.0420 -0.0641 577 LEU A N   
4492 C CA  . LEU A 577 ? 1.1541 0.9717 0.9171 -0.0348 -0.0454 -0.0657 577 LEU A CA  
4493 C C   . LEU A 577 ? 1.1510 0.9849 0.9433 -0.0270 -0.0539 -0.0543 577 LEU A C   
4494 O O   . LEU A 577 ? 1.0456 0.8967 0.8751 -0.0214 -0.0526 -0.0549 577 LEU A O   
4495 C CB  . LEU A 577 ? 1.0925 0.9131 0.8572 -0.0382 -0.0619 -0.0728 577 LEU A CB  
4496 C CG  . LEU A 577 ? 1.0973 0.9372 0.9057 -0.0324 -0.0625 -0.0771 577 LEU A CG  
4497 C CD1 . LEU A 577 ? 1.1002 0.9417 0.9245 -0.0305 -0.0392 -0.0831 577 LEU A CD1 
4498 C CD2 . LEU A 577 ? 1.0106 0.8509 0.8176 -0.0367 -0.0784 -0.0846 577 LEU A CD2 
4499 N N   . PHE A 578 ? 1.2626 1.0904 1.0384 -0.0272 -0.0618 -0.0442 578 PHE A N   
4500 C CA  . PHE A 578 ? 1.0944 0.9350 0.8969 -0.0206 -0.0674 -0.0340 578 PHE A CA  
4501 C C   . PHE A 578 ? 1.0271 0.8588 0.8142 -0.0202 -0.0574 -0.0256 578 PHE A C   
4502 O O   . PHE A 578 ? 1.0133 0.8497 0.8117 -0.0167 -0.0646 -0.0159 578 PHE A O   
4503 C CB  . PHE A 578 ? 0.9861 0.8316 0.7958 -0.0200 -0.0915 -0.0283 578 PHE A CB  
4504 C CG  . PHE A 578 ? 0.8827 0.7441 0.7266 -0.0171 -0.0995 -0.0340 578 PHE A CG  
4505 C CD1 . PHE A 578 ? 0.9955 0.8547 0.8323 -0.0214 -0.1065 -0.0428 578 PHE A CD1 
4506 C CD2 . PHE A 578 ? 0.7449 0.6224 0.6272 -0.0111 -0.0991 -0.0310 578 PHE A CD2 
4507 C CE1 . PHE A 578 ? 0.8934 0.7668 0.7627 -0.0188 -0.1130 -0.0479 578 PHE A CE1 
4508 C CE2 . PHE A 578 ? 0.6796 0.5702 0.5919 -0.0092 -0.1048 -0.0364 578 PHE A CE2 
4509 C CZ  . PHE A 578 ? 0.9159 0.8047 0.8227 -0.0126 -0.1118 -0.0445 578 PHE A CZ  
4510 N N   . GLY A 579 ? 1.1242 0.9423 0.8880 -0.0239 -0.0395 -0.0293 579 GLY A N   
4511 C CA  . GLY A 579 ? 1.2022 1.0103 0.9506 -0.0242 -0.0283 -0.0219 579 GLY A CA  
4512 C C   . GLY A 579 ? 1.1544 0.9760 0.9367 -0.0180 -0.0156 -0.0184 579 GLY A C   
4513 O O   . GLY A 579 ? 1.1430 0.9726 0.9463 -0.0165 -0.0028 -0.0242 579 GLY A O   
4514 N N   . ILE A 580 ? 1.1478 0.9720 0.9366 -0.0151 -0.0196 -0.0084 580 ILE A N   
4515 C CA  . ILE A 580 ? 1.1016 0.9377 0.9199 -0.0109 -0.0091 -0.0046 580 ILE A CA  
4516 C C   . ILE A 580 ? 1.0961 0.9180 0.8947 -0.0127 0.0061  0.0002  580 ILE A C   
4517 O O   . ILE A 580 ? 1.1063 0.9191 0.8886 -0.0132 0.0013  0.0086  580 ILE A O   
4518 C CB  . ILE A 580 ? 0.9727 0.8214 0.8158 -0.0069 -0.0221 0.0017  580 ILE A CB  
4519 C CG1 . ILE A 580 ? 1.0066 0.8681 0.8701 -0.0055 -0.0353 -0.0037 580 ILE A CG1 
4520 C CG2 . ILE A 580 ? 1.0459 0.9051 0.9150 -0.0046 -0.0108 0.0046  580 ILE A CG2 
4521 C CD1 . ILE A 580 ? 0.8527 0.7255 0.7430 -0.0023 -0.0456 0.0009  580 ILE A CD1 
4522 N N   . SER A 581 ? 1.0917 0.9116 0.8944 -0.0137 0.0251  -0.0045 581 SER A N   
4523 C CA  . SER A 581 ? 1.1268 0.9337 0.9156 -0.0155 0.0427  -0.0009 581 SER A CA  
4524 C C   . SER A 581 ? 1.0753 0.8953 0.8957 -0.0117 0.0483  0.0055  581 SER A C   
4525 O O   . SER A 581 ? 1.0705 0.9084 0.9247 -0.0094 0.0484  0.0037  581 SER A O   
4526 C CB  . SER A 581 ? 1.2099 1.0073 0.9920 -0.0188 0.0622  -0.0093 581 SER A CB  
4527 O OG  . SER A 581 ? 1.2863 1.0717 1.0604 -0.0205 0.0815  -0.0062 581 SER A OG  
4528 N N   . LYS A 582 ? 1.1942 1.0047 1.0025 -0.0121 0.0525  0.0132  582 LYS A N   
4529 C CA  . LYS A 582 ? 1.1879 1.0093 1.0245 -0.0096 0.0585  0.0188  582 LYS A CA  
4530 C C   . LYS A 582 ? 1.1823 1.0074 1.0384 -0.0102 0.0776  0.0164  582 LYS A C   
4531 O O   . LYS A 582 ? 1.1091 0.9505 0.9983 -0.0089 0.0791  0.0185  582 LYS A O   
4532 C CB  . LYS A 582 ? 1.1121 0.9212 0.9314 -0.0100 0.0590  0.0279  582 LYS A CB  
4533 C CG  . LYS A 582 ? 1.0311 0.8502 0.8786 -0.0082 0.0652  0.0332  582 LYS A CG  
4534 C CD  . LYS A 582 ? 1.1174 0.9234 0.9485 -0.0083 0.0656  0.0424  582 LYS A CD  
4535 C CE  . LYS A 582 ? 1.1088 0.9248 0.9692 -0.0072 0.0716  0.0466  582 LYS A CE  
4536 N NZ  . LYS A 582 ? 1.0633 0.8668 0.9110 -0.0069 0.0719  0.0560  582 LYS A NZ  
4537 N N   . GLU A 583 ? 1.2854 1.0950 1.1222 -0.0131 0.0926  0.0121  583 GLU A N   
4538 C CA  . GLU A 583 ? 1.2437 1.0560 1.1037 -0.0134 0.1121  0.0105  583 GLU A CA  
4539 C C   . GLU A 583 ? 1.1857 1.0175 1.0804 -0.0116 0.1086  0.0067  583 GLU A C   
4540 O O   . GLU A 583 ? 1.1207 0.9644 1.0493 -0.0109 0.1169  0.0095  583 GLU A O   
4541 C CB  . GLU A 583 ? 1.2871 1.0763 1.1187 -0.0175 0.1311  0.0053  583 GLU A CB  
4542 C CG  . GLU A 583 ? 1.4873 1.2543 1.2776 -0.0209 0.1348  0.0094  583 GLU A CG  
4543 C CD  . GLU A 583 ? 1.5762 1.3339 1.3284 -0.0233 0.1161  0.0088  583 GLU A CD  
4544 O OE1 . GLU A 583 ? 1.4161 1.1828 1.1731 -0.0225 0.1028  0.0034  583 GLU A OE1 
4545 O OE2 . GLU A 583 ? 1.7310 1.4723 1.4497 -0.0262 0.1140  0.0147  583 GLU A OE2 
4546 N N   . PHE A 584 ? 1.1038 0.9390 0.9915 -0.0113 0.0956  0.0011  584 PHE A N   
4547 C CA  . PHE A 584 ? 0.9768 0.8288 0.8950 -0.0100 0.0925  -0.0022 584 PHE A CA  
4548 C C   . PHE A 584 ? 0.9558 0.8294 0.9033 -0.0084 0.0798  0.0032  584 PHE A C   
4549 O O   . PHE A 584 ? 0.8981 0.7863 0.8778 -0.0085 0.0830  0.0057  584 PHE A O   
4550 C CB  . PHE A 584 ? 0.9698 0.8175 0.8707 -0.0107 0.0834  -0.0103 584 PHE A CB  
4551 C CG  . PHE A 584 ? 0.7790 0.6438 0.7101 -0.0092 0.0784  -0.0131 584 PHE A CG  
4552 C CD1 . PHE A 584 ? 0.8036 0.6689 0.7535 -0.0096 0.0925  -0.0162 584 PHE A CD1 
4553 C CD2 . PHE A 584 ? 0.7429 0.6223 0.6847 -0.0078 0.0605  -0.0122 584 PHE A CD2 
4554 C CE1 . PHE A 584 ? 0.7233 0.6040 0.7014 -0.0084 0.0874  -0.0172 584 PHE A CE1 
4555 C CE2 . PHE A 584 ? 0.7116 0.6057 0.6791 -0.0072 0.0563  -0.0142 584 PHE A CE2 
4556 C CZ  . PHE A 584 ? 0.6938 0.5887 0.6789 -0.0074 0.0691  -0.0161 584 PHE A CZ  
4557 N N   . TRP A 585 ? 0.9328 0.8080 0.8698 -0.0077 0.0656  0.0053  585 TRP A N   
4558 C CA  . TRP A 585 ? 0.9093 0.8027 0.8707 -0.0077 0.0548  0.0082  585 TRP A CA  
4559 C C   . TRP A 585 ? 0.8568 0.7562 0.8356 -0.0092 0.0615  0.0148  585 TRP A C   
4560 O O   . TRP A 585 ? 0.8250 0.7399 0.8259 -0.0112 0.0554  0.0167  585 TRP A O   
4561 C CB  . TRP A 585 ? 0.8441 0.7364 0.7927 -0.0066 0.0394  0.0075  585 TRP A CB  
4562 C CG  . TRP A 585 ? 0.8104 0.7024 0.7511 -0.0058 0.0296  0.0012  585 TRP A CG  
4563 C CD1 . TRP A 585 ? 0.9021 0.7797 0.8147 -0.0058 0.0262  -0.0020 585 TRP A CD1 
4564 C CD2 . TRP A 585 ? 0.7851 0.6916 0.7457 -0.0060 0.0219  -0.0027 585 TRP A CD2 
4565 N NE1 . TRP A 585 ? 0.8410 0.7239 0.7571 -0.0055 0.0166  -0.0080 585 TRP A NE1 
4566 C CE2 . TRP A 585 ? 0.8062 0.7066 0.7520 -0.0052 0.0145  -0.0085 585 TRP A CE2 
4567 C CE3 . TRP A 585 ? 0.7415 0.6647 0.7292 -0.0077 0.0204  -0.0016 585 TRP A CE3 
4568 C CZ2 . TRP A 585 ? 0.8461 0.7570 0.8062 -0.0051 0.0068  -0.0134 585 TRP A CZ2 
4569 C CZ3 . TRP A 585 ? 0.7505 0.6832 0.7494 -0.0081 0.0128  -0.0060 585 TRP A CZ3 
4570 C CH2 . TRP A 585 ? 0.7163 0.6429 0.7027 -0.0063 0.0066  -0.0119 585 TRP A CH2 
4571 N N   . GLU A 586 ? 0.9318 0.8186 0.9002 -0.0092 0.0742  0.0180  586 GLU A N   
4572 C CA  . GLU A 586 ? 0.9278 0.8208 0.9166 -0.0110 0.0818  0.0240  586 GLU A CA  
4573 C C   . GLU A 586 ? 0.8864 0.7918 0.9064 -0.0126 0.0890  0.0256  586 GLU A C   
4574 O O   . GLU A 586 ? 1.0148 0.9333 1.0598 -0.0155 0.0882  0.0307  586 GLU A O   
4575 C CB  . GLU A 586 ? 1.0551 0.9304 1.0249 -0.0106 0.0943  0.0272  586 GLU A CB  
4576 C CG  . GLU A 586 ? 1.1831 1.0490 1.1300 -0.0097 0.0861  0.0296  586 GLU A CG  
4577 C CD  . GLU A 586 ? 1.2949 1.1443 1.2259 -0.0101 0.0988  0.0346  586 GLU A CD  
4578 O OE1 . GLU A 586 ? 1.3738 1.2146 1.3029 -0.0110 0.1151  0.0342  586 GLU A OE1 
4579 O OE2 . GLU A 586 ? 1.2346 1.0792 1.1566 -0.0095 0.0936  0.0391  586 GLU A OE2 
4580 N N   . LYS A 587 ? 0.8407 0.7419 0.8610 -0.0113 0.0957  0.0218  587 LYS A N   
4581 C CA  . LYS A 587 ? 0.6976 0.6114 0.7522 -0.0124 0.1013  0.0246  587 LYS A CA  
4582 C C   . LYS A 587 ? 0.8284 0.7597 0.8991 -0.0136 0.0863  0.0243  587 LYS A C   
4583 O O   . LYS A 587 ? 0.8609 0.8081 0.9627 -0.0163 0.0841  0.0304  587 LYS A O   
4584 C CB  . LYS A 587 ? 0.7736 0.6741 0.8250 -0.0108 0.1177  0.0203  587 LYS A CB  
4585 C CG  . LYS A 587 ? 0.8373 0.7502 0.9271 -0.0110 0.1227  0.0231  587 LYS A CG  
4586 C CD  . LYS A 587 ? 0.8547 0.7798 0.9809 -0.0130 0.1274  0.0330  587 LYS A CD  
4587 C CE  . LYS A 587 ? 0.7990 0.7369 0.9673 -0.0132 0.1310  0.0381  587 LYS A CE  
4588 N NZ  . LYS A 587 ? 0.7917 0.7420 0.9985 -0.0157 0.1344  0.0491  587 LYS A NZ  
4589 N N   . GLU A 588 ? 0.7613 0.6900 0.8118 -0.0122 0.0756  0.0182  588 GLU A N   
4590 C CA  . GLU A 588 ? 0.7712 0.7148 0.8352 -0.0137 0.0627  0.0173  588 GLU A CA  
4591 C C   . GLU A 588 ? 0.7402 0.6989 0.8192 -0.0184 0.0535  0.0226  588 GLU A C   
4592 O O   . GLU A 588 ? 0.7233 0.6969 0.8251 -0.0221 0.0485  0.0268  588 GLU A O   
4593 C CB  . GLU A 588 ? 0.7321 0.6692 0.7722 -0.0115 0.0533  0.0097  588 GLU A CB  
4594 C CG  . GLU A 588 ? 0.6853 0.6348 0.7383 -0.0125 0.0432  0.0074  588 GLU A CG  
4595 C CD  . GLU A 588 ? 0.6569 0.6062 0.7220 -0.0112 0.0503  0.0057  588 GLU A CD  
4596 O OE1 . GLU A 588 ? 0.6913 0.6283 0.7506 -0.0094 0.0635  0.0041  588 GLU A OE1 
4597 O OE2 . GLU A 588 ? 0.5486 0.5091 0.6294 -0.0123 0.0438  0.0058  588 GLU A OE2 
4598 N N   . VAL A 589 ? 0.7656 0.7197 0.8314 -0.0191 0.0513  0.0226  589 VAL A N   
4599 C CA  . VAL A 589 ? 0.8310 0.7970 0.9088 -0.0250 0.0445  0.0259  589 VAL A CA  
4600 C C   . VAL A 589 ? 0.8541 0.8295 0.9568 -0.0293 0.0499  0.0338  589 VAL A C   
4601 O O   . VAL A 589 ? 0.7970 0.7866 0.9154 -0.0363 0.0425  0.0375  589 VAL A O   
4602 C CB  . VAL A 589 ? 0.7515 0.7088 0.8124 -0.0246 0.0432  0.0239  589 VAL A CB  
4603 C CG1 . VAL A 589 ? 0.6820 0.6333 0.7253 -0.0212 0.0350  0.0177  589 VAL A CG1 
4604 C CG2 . VAL A 589 ? 0.7824 0.7260 0.8334 -0.0212 0.0548  0.0268  589 VAL A CG2 
4605 N N   . GLU A 590 ? 0.9641 0.9315 1.0711 -0.0260 0.0628  0.0366  590 GLU A N   
4606 C CA  . GLU A 590 ? 0.9216 0.8983 1.0579 -0.0296 0.0683  0.0450  590 GLU A CA  
4607 C C   . GLU A 590 ? 0.9298 0.9223 1.0925 -0.0327 0.0618  0.0500  590 GLU A C   
4608 O O   . GLU A 590 ? 0.9922 0.9995 1.1778 -0.0395 0.0554  0.0577  590 GLU A O   
4609 C CB  . GLU A 590 ? 0.9425 0.9058 1.0800 -0.0251 0.0860  0.0460  590 GLU A CB  
4610 C CG  . GLU A 590 ? 1.0548 1.0270 1.2272 -0.0283 0.0931  0.0550  590 GLU A CG  
4611 C CD  . GLU A 590 ? 1.2304 1.2087 1.4078 -0.0339 0.0888  0.0589  590 GLU A CD  
4612 O OE1 . GLU A 590 ? 1.3283 1.2985 1.4800 -0.0336 0.0860  0.0541  590 GLU A OE1 
4613 O OE2 . GLU A 590 ? 1.1979 1.1890 1.4067 -0.0389 0.0879  0.0672  590 GLU A OE2 
4614 N N   . GLU A 591 ? 0.7720 0.7615 0.9318 -0.0285 0.0626  0.0462  591 GLU A N   
4615 C CA  . GLU A 591 ? 0.7567 0.7604 0.9418 -0.0310 0.0563  0.0517  591 GLU A CA  
4616 C C   . GLU A 591 ? 0.6862 0.7018 0.8659 -0.0374 0.0397  0.0517  591 GLU A C   
4617 O O   . GLU A 591 ? 0.7173 0.7478 0.9188 -0.0434 0.0315  0.0599  591 GLU A O   
4618 C CB  . GLU A 591 ? 0.6950 0.6904 0.8788 -0.0248 0.0637  0.0467  591 GLU A CB  
4619 C CG  . GLU A 591 ? 0.7378 0.7214 0.9310 -0.0204 0.0827  0.0467  591 GLU A CG  
4620 C CD  . GLU A 591 ? 0.7731 0.7685 1.0089 -0.0229 0.0873  0.0587  591 GLU A CD  
4621 O OE1 . GLU A 591 ? 0.7515 0.7645 1.0124 -0.0273 0.0754  0.0673  591 GLU A OE1 
4622 O OE2 . GLU A 591 ? 0.7672 0.7544 1.0123 -0.0211 0.1026  0.0600  591 GLU A OE2 
4623 N N   . ILE A 592 ? 0.8175 0.8261 0.9692 -0.0367 0.0350  0.0430  592 ILE A N   
4624 C CA  . ILE A 592 ? 0.7883 0.8059 0.9343 -0.0435 0.0223  0.0414  592 ILE A CA  
4625 C C   . ILE A 592 ? 0.6449 0.6717 0.7984 -0.0532 0.0175  0.0468  592 ILE A C   
4626 O O   . ILE A 592 ? 0.5466 0.5856 0.7073 -0.0624 0.0077  0.0509  592 ILE A O   
4627 C CB  . ILE A 592 ? 0.6405 0.6476 0.7600 -0.0399 0.0201  0.0308  592 ILE A CB  
4628 C CG1 . ILE A 592 ? 0.7327 0.7325 0.8452 -0.0325 0.0221  0.0255  592 ILE A CG1 
4629 C CG2 . ILE A 592 ? 0.6273 0.6418 0.7421 -0.0477 0.0103  0.0280  592 ILE A CG2 
4630 C CD1 . ILE A 592 ? 0.5316 0.5221 0.6217 -0.0290 0.0180  0.0163  592 ILE A CD1 
4631 N N   . ASP A 593 ? 0.6836 0.7040 0.8339 -0.0523 0.0243  0.0469  593 ASP A N   
4632 C CA  . ASP A 593 ? 0.6967 0.7250 0.8546 -0.0621 0.0205  0.0512  593 ASP A CA  
4633 C C   . ASP A 593 ? 0.6734 0.7169 0.8604 -0.0687 0.0157  0.0632  593 ASP A C   
4634 O O   . ASP A 593 ? 0.7609 0.8159 0.9528 -0.0804 0.0055  0.0674  593 ASP A O   
4635 C CB  . ASP A 593 ? 0.6157 0.6335 0.7680 -0.0589 0.0303  0.0497  593 ASP A CB  
4636 C CG  . ASP A 593 ? 0.6009 0.6255 0.7598 -0.0694 0.0270  0.0525  593 ASP A CG  
4637 O OD1 . ASP A 593 ? 0.6767 0.7118 0.8365 -0.0800 0.0166  0.0530  593 ASP A OD1 
4638 O OD2 . ASP A 593 ? 0.5644 0.5831 0.7265 -0.0679 0.0353  0.0539  593 ASP A OD2 
4639 N N   . LYS A 594 ? 0.6733 0.7166 0.8805 -0.0620 0.0231  0.0690  594 LYS A N   
4640 C CA  . LYS A 594 ? 0.5578 0.6160 0.7995 -0.0673 0.0186  0.0822  594 LYS A CA  
4641 C C   . LYS A 594 ? 0.7637 0.8338 1.0124 -0.0725 0.0059  0.0874  594 LYS A C   
4642 O O   . LYS A 594 ? 0.8209 0.9060 1.0914 -0.0819 -0.0047 0.0993  594 LYS A O   
4643 C CB  . LYS A 594 ? 0.6764 0.7293 0.9413 -0.0584 0.0331  0.0863  594 LYS A CB  
4644 C CG  . LYS A 594 ? 0.6989 0.7401 0.9591 -0.0546 0.0467  0.0832  594 LYS A CG  
4645 C CD  . LYS A 594 ? 0.7559 0.7910 1.0404 -0.0473 0.0633  0.0869  594 LYS A CD  
4646 C CE  . LYS A 594 ? 0.7399 0.7618 1.0094 -0.0384 0.0725  0.0787  594 LYS A CE  
4647 N NZ  . LYS A 594 ? 0.7620 0.7748 1.0526 -0.0325 0.0919  0.0802  594 LYS A NZ  
4648 N N   . TYR A 595 ? 0.6388 0.7025 0.8698 -0.0673 0.0061  0.0794  595 TYR A N   
4649 C CA  . TYR A 595 ? 0.5594 0.6332 0.7968 -0.0719 -0.0047 0.0842  595 TYR A CA  
4650 C C   . TYR A 595 ? 0.6925 0.7735 0.9131 -0.0852 -0.0179 0.0837  595 TYR A C   
4651 O O   . TYR A 595 ? 0.6185 0.7124 0.8511 -0.0951 -0.0297 0.0942  595 TYR A O   
4652 C CB  . TYR A 595 ? 0.6195 0.6837 0.8441 -0.0624 0.0004  0.0750  595 TYR A CB  
4653 C CG  . TYR A 595 ? 0.5534 0.6267 0.7864 -0.0660 -0.0088 0.0800  595 TYR A CG  
4654 C CD1 . TYR A 595 ? 0.5747 0.6549 0.8395 -0.0634 -0.0076 0.0907  595 TYR A CD1 
4655 C CD2 . TYR A 595 ? 0.6092 0.6834 0.8203 -0.0720 -0.0173 0.0743  595 TYR A CD2 
4656 C CE1 . TYR A 595 ? 0.6132 0.7013 0.8867 -0.0667 -0.0159 0.0964  595 TYR A CE1 
4657 C CE2 . TYR A 595 ? 0.6087 0.6902 0.8264 -0.0758 -0.0249 0.0792  595 TYR A CE2 
4658 C CZ  . TYR A 595 ? 0.5586 0.6472 0.8070 -0.0730 -0.0247 0.0908  595 TYR A CZ  
4659 O OH  . TYR A 595 ? 0.5670 0.6626 0.8229 -0.0766 -0.0323 0.0968  595 TYR A OH  
4660 N N   . LEU A 596 ? 0.6801 0.7520 0.8732 -0.0864 -0.0157 0.0720  596 LEU A N   
4661 C CA  . LEU A 596 ? 0.7111 0.7869 0.8866 -0.0997 -0.0250 0.0689  596 LEU A CA  
4662 C C   . LEU A 596 ? 0.8621 0.9484 1.0474 -0.1133 -0.0324 0.0780  596 LEU A C   
4663 O O   . LEU A 596 ? 0.7417 0.8372 0.9232 -0.1274 -0.0441 0.0832  596 LEU A O   
4664 C CB  . LEU A 596 ? 0.7076 0.7702 0.8568 -0.0970 -0.0187 0.0541  596 LEU A CB  
4665 C CG  . LEU A 596 ? 0.7392 0.7929 0.8759 -0.0873 -0.0152 0.0447  596 LEU A CG  
4666 C CD1 . LEU A 596 ? 0.5616 0.6030 0.6789 -0.0843 -0.0097 0.0325  596 LEU A CD1 
4667 C CD2 . LEU A 596 ? 0.6253 0.6857 0.7595 -0.0942 -0.0233 0.0457  596 LEU A CD2 
4668 N N   . GLU A 597 ? 0.9866 1.0712 1.1835 -0.1102 -0.0262 0.0802  597 GLU A N   
4669 C CA  . GLU A 597 ? 0.9871 1.0818 1.1953 -0.1234 -0.0336 0.0885  597 GLU A CA  
4670 C C   . GLU A 597 ? 1.0115 1.1226 1.2486 -0.1298 -0.0454 0.1058  597 GLU A C   
4671 O O   . GLU A 597 ? 0.9907 1.1127 1.2309 -0.1456 -0.0583 0.1138  597 GLU A O   
4672 C CB  . GLU A 597 ? 1.0100 1.0988 1.2277 -0.1174 -0.0228 0.0874  597 GLU A CB  
4673 C CG  . GLU A 597 ? 1.1701 1.2692 1.4026 -0.1307 -0.0299 0.0956  597 GLU A CG  
4674 C CD  . GLU A 597 ? 1.3537 1.4460 1.5968 -0.1242 -0.0176 0.0942  597 GLU A CD  
4675 O OE1 . GLU A 597 ? 1.3631 1.4419 1.5990 -0.1101 -0.0038 0.0872  597 GLU A OE1 
4676 O OE2 . GLU A 597 ? 1.4696 1.5698 1.7276 -0.1341 -0.0221 0.1004  597 GLU A OE2 
4677 N N   . ASP A 598 ? 1.0304 1.1430 1.2895 -0.1186 -0.0416 0.1122  598 ASP A N   
4678 C CA  . ASP A 598 ? 1.0181 1.1463 1.3119 -0.1232 -0.0520 0.1304  598 ASP A CA  
4679 C C   . ASP A 598 ? 1.0341 1.1697 1.3200 -0.1316 -0.0655 0.1359  598 ASP A C   
4680 O O   . ASP A 598 ? 1.1196 1.2698 1.4230 -0.1435 -0.0808 0.1518  598 ASP A O   
4681 C CB  . ASP A 598 ? 1.0058 1.1315 1.3317 -0.1080 -0.0394 0.1350  598 ASP A CB  
4682 C CG  . ASP A 598 ? 1.0784 1.2194 1.4451 -0.1108 -0.0488 0.1541  598 ASP A CG  
4683 O OD1 . ASP A 598 ? 1.2493 1.4032 1.6432 -0.1195 -0.0580 0.1681  598 ASP A OD1 
4684 O OD2 . ASP A 598 ? 1.0203 1.1607 1.3939 -0.1044 -0.0473 0.1556  598 ASP A OD2 
4685 N N   . GLN A 599 ? 0.7557 0.8816 1.0160 -0.1262 -0.0609 0.1239  599 GLN A N   
4686 C CA  . GLN A 599 ? 0.6654 0.7964 0.9189 -0.1325 -0.0709 0.1283  599 GLN A CA  
4687 C C   . GLN A 599 ? 0.7504 0.8799 0.9680 -0.1482 -0.0790 0.1214  599 GLN A C   
4688 O O   . GLN A 599 ? 0.8606 0.9994 1.0757 -0.1622 -0.0929 0.1318  599 GLN A O   
4689 C CB  . GLN A 599 ? 0.8249 0.9463 1.0756 -0.1176 -0.0605 0.1197  599 GLN A CB  
4690 C CG  . GLN A 599 ? 0.7384 0.8610 1.0250 -0.1044 -0.0522 0.1271  599 GLN A CG  
4691 C CD  . GLN A 599 ? 0.6989 0.8372 1.0211 -0.1103 -0.0638 0.1478  599 GLN A CD  
4692 O OE1 . GLN A 599 ? 0.7139 0.8608 1.0289 -0.1226 -0.0784 0.1560  599 GLN A OE1 
4693 N NE2 . GLN A 599 ? 0.7195 0.8611 1.0810 -0.1021 -0.0569 0.1570  599 GLN A NE2 
4694 N N   . VAL A 600 ? 0.7103 0.8276 0.9005 -0.1471 -0.0700 0.1044  600 VAL A N   
4695 C CA  . VAL A 600 ? 0.6913 0.8048 0.8487 -0.1622 -0.0740 0.0957  600 VAL A CA  
4696 C C   . VAL A 600 ? 0.7334 0.8517 0.8855 -0.1783 -0.0806 0.0985  600 VAL A C   
4697 O O   . VAL A 600 ? 0.8059 0.9282 0.9403 -0.1973 -0.0910 0.1011  600 VAL A O   
4698 C CB  . VAL A 600 ? 0.8534 0.9512 0.9882 -0.1531 -0.0606 0.0762  600 VAL A CB  
4699 C CG1 . VAL A 600 ? 0.7599 0.8530 0.8651 -0.1675 -0.0623 0.0668  600 VAL A CG1 
4700 C CG2 . VAL A 600 ? 0.6140 0.7072 0.7585 -0.1354 -0.0538 0.0736  600 VAL A CG2 
4701 N N   . ASN A 601 ? 0.8123 0.9292 0.9779 -0.1721 -0.0742 0.0977  601 ASN A N   
4702 C CA  . ASN A 601 ? 0.8187 0.9415 0.9867 -0.1862 -0.0806 0.1022  601 ASN A CA  
4703 C C   . ASN A 601 ? 0.8447 0.9598 0.9771 -0.2023 -0.0802 0.0888  601 ASN A C   
4704 O O   . ASN A 601 ? 0.8446 0.9460 0.9608 -0.1953 -0.0666 0.0727  601 ASN A O   
4705 C CB  . ASN A 601 ? 0.8828 1.0232 1.0768 -0.1957 -0.0976 0.1235  601 ASN A CB  
4706 C CG  . ASN A 601 ? 0.9691 1.1177 1.1719 -0.2098 -0.1060 0.1302  601 ASN A CG  
4707 O OD1 . ASN A 601 ? 1.0502 1.1916 1.2495 -0.2073 -0.0961 0.1205  601 ASN A OD1 
4708 N ND2 . ASN A 601 ? 1.0525 1.2162 1.2677 -0.2251 -0.1251 0.1477  601 ASN A ND2 
4709 N N   . ALA A 602 ? 0.8233 0.9457 0.9428 -0.2243 -0.0939 0.0948  602 ALA A N   
4710 C CA  . ALA A 602 ? 0.8706 0.9843 0.9564 -0.2420 -0.0915 0.0811  602 ALA A CA  
4711 C C   . ALA A 602 ? 0.8286 0.9312 0.8857 -0.2443 -0.0847 0.0683  602 ALA A C   
4712 O O   . ALA A 602 ? 0.8898 0.9807 0.9219 -0.2537 -0.0756 0.0524  602 ALA A O   
4713 C CB  . ALA A 602 ? 0.8800 1.0046 0.9590 -0.2673 -0.1091 0.0920  602 ALA A CB  
4714 N N   . ASP A 603 ? 0.8300 0.9357 0.8923 -0.2364 -0.0879 0.0745  603 ASP A N   
4715 C CA  . ASP A 603 ? 0.8568 0.9527 0.8954 -0.2382 -0.0814 0.0633  603 ASP A CA  
4716 C C   . ASP A 603 ? 0.7802 0.8642 0.8226 -0.2171 -0.0650 0.0492  603 ASP A C   
4717 O O   . ASP A 603 ? 0.7553 0.8328 0.7871 -0.2141 -0.0598 0.0417  603 ASP A O   
4718 C CB  . ASP A 603 ? 0.8963 1.0010 0.9384 -0.2412 -0.0933 0.0773  603 ASP A CB  
4719 C CG  . ASP A 603 ? 1.0047 1.1198 1.0372 -0.2652 -0.1115 0.0918  603 ASP A CG  
4720 O OD1 . ASP A 603 ? 1.0916 1.2009 1.0948 -0.2856 -0.1116 0.0835  603 ASP A OD1 
4721 O OD2 . ASP A 603 ? 1.0484 1.1772 1.1032 -0.2645 -0.1256 0.1117  603 ASP A OD2 
4722 N N   . LEU A 604 ? 0.6365 0.7175 0.6940 -0.2034 -0.0574 0.0460  604 LEU A N   
4723 C CA  . LEU A 604 ? 0.7827 0.8525 0.8432 -0.1844 -0.0440 0.0345  604 LEU A CA  
4724 C C   . LEU A 604 ? 0.7447 0.8012 0.7861 -0.1904 -0.0326 0.0173  604 LEU A C   
4725 O O   . LEU A 604 ? 0.8096 0.8641 0.8472 -0.1994 -0.0302 0.0141  604 LEU A O   
4726 C CB  . LEU A 604 ? 0.7266 0.7975 0.8092 -0.1680 -0.0404 0.0395  604 LEU A CB  
4727 C CG  . LEU A 604 ? 0.6734 0.7325 0.7573 -0.1492 -0.0285 0.0296  604 LEU A CG  
4728 C CD1 . LEU A 604 ? 0.5696 0.6284 0.6564 -0.1385 -0.0292 0.0299  604 LEU A CD1 
4729 C CD2 . LEU A 604 ? 0.5318 0.5898 0.6315 -0.1374 -0.0238 0.0339  604 LEU A CD2 
4730 N N   . PRO A 605 ? 0.7969 0.8441 0.8292 -0.1860 -0.0248 0.0061  605 PRO A N   
4731 C CA  . PRO A 605 ? 0.7725 0.8064 0.7927 -0.1909 -0.0122 -0.0102 605 PRO A CA  
4732 C C   . PRO A 605 ? 0.8412 0.8689 0.8735 -0.1778 -0.0042 -0.0139 605 PRO A C   
4733 O O   . PRO A 605 ? 0.7348 0.7653 0.7821 -0.1616 -0.0060 -0.0066 605 PRO A O   
4734 C CB  . PRO A 605 ? 0.6820 0.7093 0.6987 -0.1848 -0.0065 -0.0184 605 PRO A CB  
4735 C CG  . PRO A 605 ? 0.6675 0.7050 0.6855 -0.1853 -0.0176 -0.0070 605 PRO A CG  
4736 C CD  . PRO A 605 ? 0.6282 0.6768 0.6628 -0.1781 -0.0269 0.0078  605 PRO A CD  
4737 N N   . TYR A 606 ? 0.8804 0.8983 0.9053 -0.1860 0.0059  -0.0255 606 TYR A N   
4738 C CA  . TYR A 606 ? 0.9404 0.9512 0.9766 -0.1752 0.0140  -0.0286 606 TYR A CA  
4739 C C   . TYR A 606 ? 0.8835 0.8872 0.9300 -0.1552 0.0191  -0.0316 606 TYR A C   
4740 O O   . TYR A 606 ? 0.8617 0.8631 0.9187 -0.1415 0.0205  -0.0274 606 TYR A O   
4741 C CB  . TYR A 606 ? 1.0359 1.0372 1.0640 -0.1895 0.0246  -0.0408 606 TYR A CB  
4742 C CG  . TYR A 606 ? 1.0618 1.0531 1.1028 -0.1778 0.0352  -0.0455 606 TYR A CG  
4743 C CD1 . TYR A 606 ? 1.0105 1.0042 1.0607 -0.1732 0.0340  -0.0384 606 TYR A CD1 
4744 C CD2 . TYR A 606 ? 1.0334 1.0128 1.0796 -0.1716 0.0463  -0.0561 606 TYR A CD2 
4745 C CE1 . TYR A 606 ? 1.0099 0.9938 1.0710 -0.1629 0.0435  -0.0414 606 TYR A CE1 
4746 C CE2 . TYR A 606 ? 1.0012 0.9716 1.0610 -0.1611 0.0548  -0.0583 606 TYR A CE2 
4747 C CZ  . TYR A 606 ? 1.0357 1.0082 1.1014 -0.1570 0.0532  -0.0508 606 TYR A CZ  
4748 O OH  . TYR A 606 ? 1.0478 1.0106 1.1261 -0.1469 0.0615  -0.0518 606 TYR A OH  
4749 N N   . GLU A 607 ? 0.7846 0.7845 0.8279 -0.1543 0.0216  -0.0385 607 GLU A N   
4750 C CA  . GLU A 607 ? 0.7888 0.7824 0.8429 -0.1367 0.0247  -0.0412 607 GLU A CA  
4751 C C   . GLU A 607 ? 0.6500 0.6499 0.7105 -0.1216 0.0160  -0.0303 607 GLU A C   
4752 O O   . GLU A 607 ? 0.6478 0.6424 0.7156 -0.1070 0.0172  -0.0291 607 GLU A O   
4753 C CB  . GLU A 607 ? 0.8214 0.8104 0.8734 -0.1401 0.0291  -0.0506 607 GLU A CB  
4754 C CG  . GLU A 607 ? 0.8906 0.8697 0.9386 -0.1540 0.0419  -0.0637 607 GLU A CG  
4755 C CD  . GLU A 607 ? 0.9206 0.8943 0.9686 -0.1577 0.0484  -0.0735 607 GLU A CD  
4756 O OE1 . GLU A 607 ? 1.0509 1.0303 1.0986 -0.1525 0.0413  -0.0693 607 GLU A OE1 
4757 O OE2 . GLU A 607 ? 1.0074 0.9705 1.0575 -0.1661 0.0619  -0.0857 607 GLU A OE2 
4758 N N   . ILE A 608 ? 0.6132 0.6236 0.6711 -0.1255 0.0075  -0.0221 608 ILE A N   
4759 C CA  . ILE A 608 ? 0.5703 0.5858 0.6362 -0.1124 0.0016  -0.0124 608 ILE A CA  
4760 C C   . ILE A 608 ? 0.6341 0.6486 0.7059 -0.1064 0.0034  -0.0065 608 ILE A C   
4761 O O   . ILE A 608 ? 0.5925 0.6041 0.6691 -0.0927 0.0040  -0.0029 608 ILE A O   
4762 C CB  . ILE A 608 ? 0.6992 0.7264 0.7658 -0.1188 -0.0071 -0.0038 608 ILE A CB  
4763 C CG1 . ILE A 608 ? 0.6924 0.7192 0.7521 -0.1243 -0.0079 -0.0095 608 ILE A CG1 
4764 C CG2 . ILE A 608 ? 0.5221 0.5535 0.6004 -0.1057 -0.0106 0.0054  608 ILE A CG2 
4765 C CD1 . ILE A 608 ? 0.6843 0.7049 0.7488 -0.1102 -0.0054 -0.0153 608 ILE A CD1 
4766 N N   . GLU A 609 ? 0.6964 0.7126 0.7670 -0.1175 0.0050  -0.0058 609 GLU A N   
4767 C CA  . GLU A 609 ? 0.6464 0.6609 0.7238 -0.1128 0.0082  -0.0008 609 GLU A CA  
4768 C C   . GLU A 609 ? 0.6220 0.6236 0.6988 -0.1038 0.0167  -0.0072 609 GLU A C   
4769 O O   . GLU A 609 ? 0.5100 0.5071 0.5907 -0.0930 0.0193  -0.0025 609 GLU A O   
4770 C CB  . GLU A 609 ? 0.6953 0.7161 0.7731 -0.1285 0.0064  0.0018  609 GLU A CB  
4771 C CG  . GLU A 609 ? 0.5793 0.5988 0.6665 -0.1248 0.0104  0.0069  609 GLU A CG  
4772 C CD  . GLU A 609 ? 0.7529 0.7792 0.8417 -0.1416 0.0076  0.0090  609 GLU A CD  
4773 O OE1 . GLU A 609 ? 0.7854 0.8174 0.8652 -0.1569 0.0014  0.0073  609 GLU A OE1 
4774 O OE2 . GLU A 609 ? 0.8537 0.8792 0.9517 -0.1403 0.0113  0.0126  609 GLU A OE2 
4775 N N   . ARG A 610 ? 0.6382 0.6331 0.7112 -0.1087 0.0215  -0.0174 610 ARG A N   
4776 C CA  . ARG A 610 ? 0.6302 0.6131 0.7071 -0.1003 0.0288  -0.0219 610 ARG A CA  
4777 C C   . ARG A 610 ? 0.6644 0.6430 0.7427 -0.0839 0.0256  -0.0187 610 ARG A C   
4778 O O   . ARG A 610 ? 0.4948 0.4652 0.5752 -0.0744 0.0284  -0.0161 610 ARG A O   
4779 C CB  . ARG A 610 ? 0.6806 0.6572 0.7579 -0.1090 0.0357  -0.0337 610 ARG A CB  
4780 C CG  . ARG A 610 ? 0.7209 0.6855 0.8080 -0.1017 0.0437  -0.0375 610 ARG A CG  
4781 C CD  . ARG A 610 ? 0.6941 0.6521 0.7853 -0.1130 0.0538  -0.0498 610 ARG A CD  
4782 N NE  . ARG A 610 ? 0.7454 0.7045 0.8353 -0.1159 0.0532  -0.0564 610 ARG A NE  
4783 C CZ  . ARG A 610 ? 0.8448 0.7982 0.9361 -0.1275 0.0630  -0.0682 610 ARG A CZ  
4784 N NH1 . ARG A 610 ? 0.9018 0.8479 0.9954 -0.1380 0.0744  -0.0756 610 ARG A NH1 
4785 N NH2 . ARG A 610 ? 0.7769 0.7311 0.8675 -0.1291 0.0627  -0.0733 610 ARG A NH2 
4786 N N   . GLU A 611 ? 0.5531 0.5366 0.6292 -0.0812 0.0196  -0.0187 611 GLU A N   
4787 C CA  . GLU A 611 ? 0.5621 0.5418 0.6376 -0.0673 0.0157  -0.0161 611 GLU A CA  
4788 C C   . GLU A 611 ? 0.6237 0.6040 0.6963 -0.0603 0.0146  -0.0072 611 GLU A C   
4789 O O   . GLU A 611 ? 0.5810 0.5533 0.6494 -0.0500 0.0147  -0.0047 611 GLU A O   
4790 C CB  . GLU A 611 ? 0.5240 0.5085 0.5993 -0.0673 0.0105  -0.0193 611 GLU A CB  
4791 C CG  . GLU A 611 ? 0.4689 0.4499 0.5488 -0.0714 0.0132  -0.0287 611 GLU A CG  
4792 C CD  . GLU A 611 ? 0.5717 0.5428 0.6588 -0.0620 0.0146  -0.0308 611 GLU A CD  
4793 O OE1 . GLU A 611 ? 0.5285 0.4955 0.6123 -0.0516 0.0109  -0.0247 611 GLU A OE1 
4794 O OE2 . GLU A 611 ? 0.7244 0.6910 0.8207 -0.0656 0.0197  -0.0381 611 GLU A OE2 
4795 N N   . LEU A 612 ? 0.5720 0.5613 0.6472 -0.0667 0.0139  -0.0021 612 LEU A N   
4796 C CA  . LEU A 612 ? 0.5401 0.5295 0.6171 -0.0608 0.0156  0.0060  612 LEU A CA  
4797 C C   . LEU A 612 ? 0.6453 0.6251 0.7202 -0.0569 0.0223  0.0078  612 LEU A C   
4798 O O   . LEU A 612 ? 0.6711 0.6435 0.7408 -0.0480 0.0252  0.0117  612 LEU A O   
4799 C CB  . LEU A 612 ? 0.5901 0.5920 0.6765 -0.0694 0.0132  0.0122  612 LEU A CB  
4800 C CG  . LEU A 612 ? 0.5502 0.5535 0.6451 -0.0642 0.0165  0.0208  612 LEU A CG  
4801 C CD1 . LEU A 612 ? 0.6450 0.6432 0.7361 -0.0533 0.0174  0.0209  612 LEU A CD1 
4802 C CD2 . LEU A 612 ? 0.5694 0.5867 0.6792 -0.0738 0.0121  0.0284  612 LEU A CD2 
4803 N N   . ARG A 613 ? 0.5715 0.5503 0.6492 -0.0644 0.0256  0.0049  613 ARG A N   
4804 C CA  . ARG A 613 ? 0.5866 0.5556 0.6639 -0.0608 0.0324  0.0068  613 ARG A CA  
4805 C C   . ARG A 613 ? 0.5808 0.5378 0.6517 -0.0510 0.0323  0.0050  613 ARG A C   
4806 O O   . ARG A 613 ? 0.6121 0.5596 0.6774 -0.0437 0.0356  0.0100  613 ARG A O   
4807 C CB  . ARG A 613 ? 0.7140 0.6845 0.7976 -0.0721 0.0366  0.0030  613 ARG A CB  
4808 C CG  . ARG A 613 ? 0.6993 0.6814 0.7891 -0.0833 0.0350  0.0064  613 ARG A CG  
4809 C CD  . ARG A 613 ? 0.7564 0.7376 0.8501 -0.0950 0.0399  0.0021  613 ARG A CD  
4810 N NE  . ARG A 613 ? 0.9390 0.9317 1.0387 -0.1070 0.0362  0.0062  613 ARG A NE  
4811 C CZ  . ARG A 613 ? 0.8991 0.8926 1.0024 -0.1189 0.0393  0.0038  613 ARG A CZ  
4812 N NH1 . ARG A 613 ? 0.8986 0.8815 1.0012 -0.1201 0.0480  -0.0033 613 ARG A NH1 
4813 N NH2 . ARG A 613 ? 0.9741 0.9794 1.0837 -0.1303 0.0332  0.0090  613 ARG A NH2 
4814 N N   . ALA A 614 ? 0.5673 0.5244 0.6395 -0.0514 0.0283  -0.0013 614 ALA A N   
4815 C CA  . ALA A 614 ? 0.6212 0.5685 0.6918 -0.0426 0.0261  -0.0017 614 ALA A CA  
4816 C C   . ALA A 614 ? 0.6360 0.5789 0.6942 -0.0329 0.0212  0.0034  614 ALA A C   
4817 O O   . ALA A 614 ? 0.6296 0.5619 0.6806 -0.0260 0.0207  0.0081  614 ALA A O   
4818 C CB  . ALA A 614 ? 0.5780 0.5274 0.6566 -0.0454 0.0234  -0.0097 614 ALA A CB  
4819 N N   . LEU A 615 ? 0.6450 0.5950 0.6997 -0.0331 0.0178  0.0029  615 LEU A N   
4820 C CA  . LEU A 615 ? 0.6223 0.5672 0.6644 -0.0255 0.0151  0.0060  615 LEU A CA  
4821 C C   . LEU A 615 ? 0.6908 0.6285 0.7244 -0.0230 0.0223  0.0125  615 LEU A C   
4822 O O   . LEU A 615 ? 0.6826 0.6087 0.7010 -0.0170 0.0221  0.0156  615 LEU A O   
4823 C CB  . LEU A 615 ? 0.5878 0.5419 0.6321 -0.0268 0.0119  0.0037  615 LEU A CB  
4824 C CG  . LEU A 615 ? 0.5481 0.4965 0.5801 -0.0205 0.0111  0.0051  615 LEU A CG  
4825 C CD1 . LEU A 615 ? 0.6767 0.6158 0.6976 -0.0148 0.0039  0.0032  615 LEU A CD1 
4826 C CD2 . LEU A 615 ? 0.5042 0.4626 0.5438 -0.0225 0.0097  0.0034  615 LEU A CD2 
4827 N N   . LYS A 616 ? 0.7563 0.7002 0.7990 -0.0284 0.0287  0.0149  616 LYS A N   
4828 C CA  . LYS A 616 ? 0.6530 0.5902 0.6914 -0.0265 0.0373  0.0208  616 LYS A CA  
4829 C C   . LYS A 616 ? 0.5989 0.5228 0.6284 -0.0230 0.0402  0.0238  616 LYS A C   
4830 O O   . LYS A 616 ? 0.5886 0.5008 0.6036 -0.0185 0.0449  0.0284  616 LYS A O   
4831 C CB  . LYS A 616 ? 0.5969 0.5445 0.6518 -0.0339 0.0421  0.0232  616 LYS A CB  
4832 C CG  . LYS A 616 ? 0.6661 0.6077 0.7217 -0.0325 0.0525  0.0292  616 LYS A CG  
4833 C CD  . LYS A 616 ? 1.0095 0.9632 1.0855 -0.0406 0.0550  0.0321  616 LYS A CD  
4834 C CE  . LYS A 616 ? 1.1592 1.1070 1.2400 -0.0391 0.0664  0.0381  616 LYS A CE  
4835 N NZ  . LYS A 616 ? 1.1663 1.1270 1.2703 -0.0475 0.0673  0.0418  616 LYS A NZ  
4836 N N   . GLN A 617 ? 0.8200 0.7447 0.8581 -0.0257 0.0382  0.0215  617 GLN A N   
4837 C CA  . GLN A 617 ? 0.6724 0.5848 0.7065 -0.0224 0.0406  0.0256  617 GLN A CA  
4838 C C   . GLN A 617 ? 0.6953 0.5969 0.7129 -0.0149 0.0335  0.0287  617 GLN A C   
4839 O O   . GLN A 617 ? 0.6636 0.5525 0.6662 -0.0111 0.0361  0.0355  617 GLN A O   
4840 C CB  . GLN A 617 ? 0.6458 0.5612 0.6966 -0.0271 0.0409  0.0213  617 GLN A CB  
4841 C CG  . GLN A 617 ? 0.7371 0.6406 0.7901 -0.0240 0.0443  0.0262  617 GLN A CG  
4842 C CD  . GLN A 617 ? 0.7636 0.6632 0.8178 -0.0264 0.0548  0.0306  617 GLN A CD  
4843 O OE1 . GLN A 617 ? 0.7798 0.6861 0.8346 -0.0304 0.0591  0.0303  617 GLN A OE1 
4844 N NE2 . GLN A 617 ? 0.7923 0.6814 0.8500 -0.0241 0.0588  0.0355  617 GLN A NE2 
4845 N N   . ARG A 618 ? 0.6613 0.5672 0.6805 -0.0135 0.0240  0.0241  618 ARG A N   
4846 C CA  . ARG A 618 ? 0.6929 0.5897 0.6980 -0.0077 0.0147  0.0272  618 ARG A CA  
4847 C C   . ARG A 618 ? 0.7474 0.6357 0.7274 -0.0053 0.0163  0.0303  618 ARG A C   
4848 O O   . ARG A 618 ? 0.7708 0.6463 0.7317 -0.0021 0.0120  0.0361  618 ARG A O   
4849 C CB  . ARG A 618 ? 0.5867 0.4912 0.6012 -0.0074 0.0049  0.0208  618 ARG A CB  
4850 C CG  . ARG A 618 ? 0.6322 0.5428 0.6710 -0.0104 0.0051  0.0164  618 ARG A CG  
4851 C CD  . ARG A 618 ? 0.5550 0.4711 0.6031 -0.0095 -0.0037 0.0107  618 ARG A CD  
4852 N NE  . ARG A 618 ? 0.5757 0.5004 0.6186 -0.0116 -0.0046 0.0054  618 ARG A NE  
4853 C CZ  . ARG A 618 ? 0.7000 0.6352 0.7543 -0.0178 -0.0011 -0.0012 618 ARG A CZ  
4854 N NH1 . ARG A 618 ? 0.7391 0.6769 0.8082 -0.0234 0.0045  -0.0049 618 ARG A NH1 
4855 N NH2 . ARG A 618 ? 0.6640 0.6063 0.7138 -0.0191 -0.0027 -0.0039 618 ARG A NH2 
4856 N N   . ILE A 619 ? 0.7661 0.6606 0.7460 -0.0075 0.0228  0.0270  619 ILE A N   
4857 C CA  . ILE A 619 ? 0.7513 0.6365 0.7097 -0.0060 0.0276  0.0283  619 ILE A CA  
4858 C C   . ILE A 619 ? 0.7731 0.6458 0.7194 -0.0058 0.0384  0.0350  619 ILE A C   
4859 O O   . ILE A 619 ? 0.7673 0.6256 0.6879 -0.0047 0.0412  0.0377  619 ILE A O   
4860 C CB  . ILE A 619 ? 0.8630 0.7586 0.8311 -0.0081 0.0326  0.0234  619 ILE A CB  
4861 C CG1 . ILE A 619 ? 0.7335 0.6386 0.7089 -0.0079 0.0220  0.0173  619 ILE A CG1 
4862 C CG2 . ILE A 619 ? 0.8272 0.7118 0.7773 -0.0072 0.0423  0.0241  619 ILE A CG2 
4863 C CD1 . ILE A 619 ? 0.6707 0.5861 0.6575 -0.0099 0.0258  0.0138  619 ILE A CD1 
4864 N N   . SER A 620 ? 0.7667 0.6437 0.7297 -0.0080 0.0451  0.0375  620 SER A N   
4865 C CA  . SER A 620 ? 0.8106 0.6759 0.7650 -0.0080 0.0562  0.0440  620 SER A CA  
4866 C C   . SER A 620 ? 0.9092 0.7598 0.8464 -0.0052 0.0512  0.0509  620 SER A C   
4867 O O   . SER A 620 ? 0.9272 0.7640 0.8485 -0.0050 0.0597  0.0573  620 SER A O   
4868 C CB  . SER A 620 ? 0.8042 0.6789 0.7834 -0.0118 0.0638  0.0443  620 SER A CB  
4869 O OG  . SER A 620 ? 0.8258 0.7071 0.8206 -0.0133 0.0569  0.0425  620 SER A OG  
4870 N N   . GLN A 621 ? 0.9278 0.7807 0.8693 -0.0033 0.0377  0.0508  621 GLN A N   
4871 C CA  . GLN A 621 ? 0.9194 0.7602 0.8504 -0.0007 0.0304  0.0593  621 GLN A CA  
4872 C C   . GLN A 621 ? 1.0641 0.8928 0.9636 0.0006  0.0212  0.0626  621 GLN A C   
4873 O O   . GLN A 621 ? 1.1034 0.9235 0.9945 0.0023  0.0104  0.0708  621 GLN A O   
4874 C CB  . GLN A 621 ? 0.9172 0.7665 0.8746 0.0005  0.0211  0.0582  621 GLN A CB  
4875 C CG  . GLN A 621 ? 0.9375 0.7975 0.9233 -0.0029 0.0300  0.0533  621 GLN A CG  
4876 C CD  . GLN A 621 ? 1.0333 0.8852 1.0212 -0.0037 0.0411  0.0597  621 GLN A CD  
4877 O OE1 . GLN A 621 ? 1.1740 1.0117 1.1461 -0.0009 0.0406  0.0694  621 GLN A OE1 
4878 N NE2 . GLN A 621 ? 1.0047 0.8652 1.0114 -0.0084 0.0508  0.0548  621 GLN A NE2 
4879 N N   . MET A 622 ? 1.0402 0.8677 0.9228 -0.0010 0.0249  0.0568  622 MET A N   
4880 C CA  . MET A 622 ? 1.0382 0.8531 0.8875 -0.0018 0.0172  0.0581  622 MET A CA  
4881 C C   . MET A 622 ? 1.1464 0.9408 0.9626 -0.0041 0.0259  0.0657  622 MET A C   
4882 O O   . MET A 622 ? 1.1685 0.9596 0.9889 -0.0047 0.0414  0.0678  622 MET A O   
4883 C CB  . MET A 622 ? 1.0740 0.8944 0.9194 -0.0032 0.0196  0.0476  622 MET A CB  
4884 C CG  . MET A 622 ? 1.0553 0.8940 0.9282 -0.0017 0.0099  0.0405  622 MET A CG  
4885 S SD  . MET A 622 ? 1.0188 0.8616 0.8851 -0.0032 0.0112  0.0298  622 MET A SD  
4886 C CE  . MET A 622 ? 1.0226 0.8463 0.8468 -0.0055 0.0010  0.0319  622 MET A CE  
4887 O OXT . MET A 622 ? 1.1261 0.9062 0.9097 -0.0063 0.0178  0.0700  622 MET A OXT 
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