data_9EIV
# 
_entry.id   9EIV 
# 
_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   9EIV         pdb_00009eiv 10.2210/pdb9eiv/pdb 
WWPDB D_1000290520 ?            ?                   
# 
_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                        9EIV 
_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    145 ?        ? ? ? 
# 
_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 K-12' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     83333 
_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               'BL21(DE3)' 
_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                       'pESUMOstar (KAN)' 
_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   802 801 HOH HOH A . 
G 5 HOH 3   803 802 HOH HOH A . 
G 5 HOH 4   804 118 HOH HOH A . 
G 5 HOH 5   805 39  HOH HOH A . 
G 5 HOH 6   806 113 HOH HOH A . 
G 5 HOH 7   807 93  HOH HOH A . 
G 5 HOH 8   808 122 HOH HOH A . 
G 5 HOH 9   809 9   HOH HOH A . 
G 5 HOH 10  810 68  HOH HOH A . 
G 5 HOH 11  811 72  HOH HOH A . 
G 5 HOH 12  812 17  HOH HOH A . 
G 5 HOH 13  813 85  HOH HOH A . 
G 5 HOH 14  814 136 HOH HOH A . 
G 5 HOH 15  815 29  HOH HOH A . 
G 5 HOH 16  816 132 HOH HOH A . 
G 5 HOH 17  817 126 HOH HOH A . 
G 5 HOH 18  818 94  HOH HOH A . 
G 5 HOH 19  819 20  HOH HOH A . 
G 5 HOH 20  820 69  HOH HOH A . 
G 5 HOH 21  821 44  HOH HOH A . 
G 5 HOH 22  822 23  HOH HOH A . 
G 5 HOH 23  823 41  HOH HOH A . 
G 5 HOH 24  824 3   HOH HOH A . 
G 5 HOH 25  825 40  HOH HOH A . 
G 5 HOH 26  826 52  HOH HOH A . 
G 5 HOH 27  827 33  HOH HOH A . 
G 5 HOH 28  828 7   HOH HOH A . 
G 5 HOH 29  829 31  HOH HOH A . 
G 5 HOH 30  830 6   HOH HOH A . 
G 5 HOH 31  831 35  HOH HOH A . 
G 5 HOH 32  832 12  HOH HOH A . 
G 5 HOH 33  833 47  HOH HOH A . 
G 5 HOH 34  834 13  HOH HOH A . 
G 5 HOH 35  835 4   HOH HOH A . 
G 5 HOH 36  836 77  HOH HOH A . 
G 5 HOH 37  837 25  HOH HOH A . 
G 5 HOH 38  838 87  HOH HOH A . 
G 5 HOH 39  839 21  HOH HOH A . 
G 5 HOH 40  840 8   HOH HOH A . 
G 5 HOH 41  841 117 HOH HOH A . 
G 5 HOH 42  842 127 HOH HOH A . 
G 5 HOH 43  843 56  HOH HOH A . 
G 5 HOH 44  844 58  HOH HOH A . 
G 5 HOH 45  845 108 HOH HOH A . 
G 5 HOH 46  846 14  HOH HOH A . 
G 5 HOH 47  847 70  HOH HOH A . 
G 5 HOH 48  848 2   HOH HOH A . 
G 5 HOH 49  849 71  HOH HOH A . 
G 5 HOH 50  850 75  HOH HOH A . 
G 5 HOH 51  851 83  HOH HOH A . 
G 5 HOH 52  852 30  HOH HOH A . 
G 5 HOH 53  853 36  HOH HOH A . 
G 5 HOH 54  854 15  HOH HOH A . 
G 5 HOH 55  855 121 HOH HOH A . 
G 5 HOH 56  856 37  HOH HOH A . 
G 5 HOH 57  857 76  HOH HOH A . 
G 5 HOH 58  858 16  HOH HOH A . 
G 5 HOH 59  859 64  HOH HOH A . 
G 5 HOH 60  860 27  HOH HOH A . 
G 5 HOH 61  861 10  HOH HOH A . 
G 5 HOH 62  862 45  HOH HOH A . 
G 5 HOH 63  863 24  HOH HOH A . 
G 5 HOH 64  864 32  HOH HOH A . 
G 5 HOH 65  865 67  HOH HOH A . 
G 5 HOH 66  866 131 HOH HOH A . 
G 5 HOH 67  867 51  HOH HOH A . 
G 5 HOH 68  868 98  HOH HOH A . 
G 5 HOH 69  869 38  HOH HOH A . 
G 5 HOH 70  870 73  HOH HOH A . 
G 5 HOH 71  871 19  HOH HOH A . 
G 5 HOH 72  872 84  HOH HOH A . 
G 5 HOH 73  873 34  HOH HOH A . 
G 5 HOH 74  874 5   HOH HOH A . 
G 5 HOH 75  875 43  HOH HOH A . 
G 5 HOH 76  876 46  HOH HOH A . 
G 5 HOH 77  877 101 HOH HOH A . 
G 5 HOH 78  878 112 HOH HOH A . 
G 5 HOH 79  879 57  HOH HOH A . 
G 5 HOH 80  880 1   HOH HOH A . 
G 5 HOH 81  881 28  HOH HOH A . 
G 5 HOH 82  882 137 HOH HOH A . 
G 5 HOH 83  883 61  HOH HOH A . 
G 5 HOH 84  884 11  HOH HOH A . 
G 5 HOH 85  885 55  HOH HOH A . 
G 5 HOH 86  886 22  HOH HOH A . 
G 5 HOH 87  887 114 HOH HOH A . 
G 5 HOH 88  888 65  HOH HOH A . 
G 5 HOH 89  889 115 HOH HOH A . 
G 5 HOH 90  890 78  HOH HOH A . 
G 5 HOH 91  891 18  HOH HOH A . 
G 5 HOH 92  892 124 HOH HOH A . 
G 5 HOH 93  893 50  HOH HOH A . 
G 5 HOH 94  894 54  HOH HOH A . 
G 5 HOH 95  895 97  HOH HOH A . 
G 5 HOH 96  896 74  HOH HOH A . 
G 5 HOH 97  897 86  HOH HOH A . 
G 5 HOH 98  898 42  HOH HOH A . 
G 5 HOH 99  899 95  HOH HOH A . 
G 5 HOH 100 900 48  HOH HOH A . 
G 5 HOH 101 901 49  HOH HOH A . 
G 5 HOH 102 902 79  HOH HOH A . 
G 5 HOH 103 903 80  HOH HOH A . 
G 5 HOH 104 904 63  HOH HOH A . 
G 5 HOH 105 905 92  HOH HOH A . 
G 5 HOH 106 906 139 HOH HOH A . 
G 5 HOH 107 907 96  HOH HOH A . 
G 5 HOH 108 908 90  HOH HOH A . 
G 5 HOH 109 909 105 HOH HOH A . 
G 5 HOH 110 910 109 HOH HOH A . 
G 5 HOH 111 911 88  HOH HOH A . 
G 5 HOH 112 912 133 HOH HOH A . 
G 5 HOH 113 913 103 HOH HOH A . 
G 5 HOH 114 914 62  HOH HOH A . 
G 5 HOH 115 915 53  HOH HOH A . 
G 5 HOH 116 916 81  HOH HOH A . 
G 5 HOH 117 917 141 HOH HOH A . 
G 5 HOH 118 918 66  HOH HOH A . 
G 5 HOH 119 919 60  HOH HOH A . 
G 5 HOH 120 920 59  HOH HOH A . 
G 5 HOH 121 921 104 HOH HOH A . 
G 5 HOH 122 922 134 HOH HOH A . 
G 5 HOH 123 923 125 HOH HOH A . 
G 5 HOH 124 924 26  HOH HOH A . 
G 5 HOH 125 925 119 HOH HOH A . 
G 5 HOH 126 926 102 HOH HOH A . 
G 5 HOH 127 927 123 HOH HOH A . 
G 5 HOH 128 928 129 HOH HOH A . 
G 5 HOH 129 929 82  HOH HOH A . 
G 5 HOH 130 930 100 HOH HOH A . 
G 5 HOH 131 931 116 HOH HOH A . 
G 5 HOH 132 932 138 HOH HOH A . 
G 5 HOH 133 933 99  HOH HOH A . 
G 5 HOH 134 934 110 HOH HOH A . 
G 5 HOH 135 935 120 HOH HOH A . 
G 5 HOH 136 936 107 HOH HOH A . 
G 5 HOH 137 937 142 HOH HOH A . 
G 5 HOH 138 938 91  HOH HOH A . 
G 5 HOH 139 939 130 HOH HOH A . 
G 5 HOH 140 940 135 HOH HOH A . 
G 5 HOH 141 941 89  HOH HOH A . 
G 5 HOH 142 942 106 HOH HOH A . 
G 5 HOH 143 943 111 HOH HOH A . 
G 5 HOH 144 944 128 HOH HOH A . 
G 5 HOH 145 945 140 HOH HOH A . 
# 
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                   111.48 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.711 
_cell.length_a_esd                 ? 
_cell.length_b                     119.789 
_cell.length_b_esd                 ? 
_cell.length_c                     60.074 
_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                         9EIV 
_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                   9EIV 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.89 
_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                     253 
_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                                       9EIV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.92 
_reflns.d_resolution_low                               60.08 
_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                                     44474 
_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                           98.20 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.69 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.0 
_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                                0.0820 
_reflns.pdbx_Rpim_I_all                                0.0320 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9980 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.0760 
_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                                    1.92 
_reflns_shell.d_res_low                                     1.96 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2244 
_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                               6.92 
_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                               1.5760 
_reflns_shell.pdbx_Rpim_I_all                               0.5950 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.6270 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.18 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.4570 
_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                                 9EIV 
_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                            1.92 
_refine.ls_d_res_low                             55.90 
_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                     42946 
_refine.ls_number_reflns_R_free                  2176 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.53 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1904 
_refine.ls_R_factor_R_free                       0.2290 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1882 
_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                 30.06 
_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                            0.35 
_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.details                          ? 
_refine_hist.d_res_high                       1.92 
_refine_hist.d_res_low                        55.90 
_refine_hist.number_atoms_solvent             145 
_refine_hist.number_atoms_total               5054 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4869 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.521  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.508 ? 1914 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 720  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 902  ? 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' 1.92 1.95  . . 92  1806 66.00 . . . . 0.4456 . . . . . . . . . . . 0.4838 
'X-RAY DIFFRACTION' 1.95 2.00  . . 135 2421 90.00 . . . . 0.3864 . . . . . . . . . . . 0.3887 
'X-RAY DIFFRACTION' 2.00 2.05  . . 122 2560 95.00 . . . . 0.3581 . . . . . . . . . . . 0.3458 
'X-RAY DIFFRACTION' 2.05 2.10  . . 143 2538 96.00 . . . . 0.3309 . . . . . . . . . . . 0.3542 
'X-RAY DIFFRACTION' 2.10 2.17  . . 136 2611 96.00 . . . . 0.3002 . . . . . . . . . . . 0.3819 
'X-RAY DIFFRACTION' 2.17 2.24  . . 138 2625 96.00 . . . . 0.2674 . . . . . . . . . . . 0.3026 
'X-RAY DIFFRACTION' 2.24 2.32  . . 155 2544 96.00 . . . . 0.2285 . . . . . . . . . . . 0.2821 
'X-RAY DIFFRACTION' 2.32 2.41  . . 119 2613 97.00 . . . . 0.2091 . . . . . . . . . . . 0.2625 
'X-RAY DIFFRACTION' 2.41 2.52  . . 156 2580 97.00 . . . . 0.2142 . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 2.52 2.65  . . 118 2633 97.00 . . . . 0.2084 . . . . . . . . . . . 0.2488 
'X-RAY DIFFRACTION' 2.65 2.82  . . 127 2624 97.00 . . . . 0.1911 . . . . . . . . . . . 0.2530 
'X-RAY DIFFRACTION' 2.82 3.03  . . 148 2628 97.00 . . . . 0.1852 . . . . . . . . . . . 0.2477 
'X-RAY DIFFRACTION' 3.03 3.34  . . 128 2642 97.00 . . . . 0.1792 . . . . . . . . . . . 0.2212 
'X-RAY DIFFRACTION' 3.34 3.82  . . 144 2614 98.00 . . . . 0.1628 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 3.82 4.82  . . 155 2649 98.00 . . . . 0.1426 . . . . . . . . . . . 0.1777 
'X-RAY DIFFRACTION' 4.82 55.90 . . 160 2682 98.00 . . . . 0.1540 . . . . . . . . . . . 0.1917 
# 
_struct.entry_id                     9EIV 
_struct.title                        'Rat cytosolic PEPCK in complex with GDP and phosphoglycolic acid (253K)' 
_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        9EIV 
_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              9EIV 
_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   'gel filtration' 
_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 ? ALA A 128 ? SER A 118 ALA A 128 1 ? 11 
HELX_P HELX_P6  AA6 SER A 163 ? THR A 174 ? SER A 163 THR A 174 1 ? 12 
HELX_P HELX_P7  AA7 GLY A 177 ? GLY A 185 ? GLY A 177 GLY A 185 1 ? 9  
HELX_P HELX_P8  AA8 TYR A 235 ? LEU A 240 ? TYR A 235 LEU A 240 1 ? 6  
HELX_P HELX_P9  AA9 LEU A 248 ? GLY A 259 ? LEU A 248 GLY A 259 1 ? 12 
HELX_P HELX_P10 AB1 GLY A 289 ? MET A 295 ? GLY A 289 MET A 295 1 ? 7  
HELX_P HELX_P11 AB2 ASN A 344 ? ILE A 351 ? ASN A 344 ILE A 351 1 ? 8  
HELX_P HELX_P12 AB3 SER A 411 ? CYS A 413 ? SER A 411 CYS A 413 5 ? 3  
HELX_P HELX_P13 AB4 SER A 449 ? ALA A 459 ? SER A 449 ALA A 459 1 ? 11 
HELX_P HELX_P14 AB5 PRO A 479 ? MET A 482 ? PRO A 479 MET A 482 5 ? 4  
HELX_P HELX_P15 AB6 ASN A 489 ? MET A 500 ? ASN A 489 MET A 500 1 ? 12 
HELX_P HELX_P16 AB7 ALA A 501 ? ARG A 503 ? ALA A 501 ARG A 503 5 ? 3  
HELX_P HELX_P17 AB8 GLY A 529 ? GLU A 532 ? GLY A 529 GLU A 532 5 ? 4  
HELX_P HELX_P18 AB9 ASN A 533 ? GLY A 546 ? ASN A 533 GLY A 546 1 ? 14 
HELX_P HELX_P19 AC1 ASN A 573 ? GLY A 579 ? ASN A 573 GLY A 579 1 ? 7  
HELX_P HELX_P20 AC2 SER A 581 ? VAL A 600 ? SER A 581 VAL A 600 1 ? 20 
HELX_P HELX_P21 AC3 ASN A 601 ? LEU A 604 ? ASN A 601 LEU A 604 5 ? 4  
HELX_P HELX_P22 AC4 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 GLU 63  OE1 ? ? ? 1_555 D MN  . MN  ? ? A GLU 63  A MN  703 2_545 ? ? ? ? ? ? ? 2.729 ? ? 
metalc2  metalc ? ? A LYS 244 NZ  ? ? ? 1_555 B MN  . MN  ? ? A LYS 244 A MN  701 1_555 ? ? ? ? ? ? ? 2.185 ? ? 
metalc3  metalc ? ? A HIS 264 NE2 ? ? ? 1_555 B MN  . MN  ? ? A HIS 264 A MN  701 1_555 ? ? ? ? ? ? ? 2.239 ? ? 
metalc4  metalc ? ? A THR 291 OG1 ? ? ? 1_555 C MN  . MN  ? ? A THR 291 A MN  702 1_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc5  metalc ? ? A ASP 311 OD1 ? ? ? 1_555 B MN  . MN  ? ? A ASP 311 A MN  701 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc6  metalc ? ? A HIS 502 NE2 ? ? ? 1_555 D MN  . MN  ? ? A HIS 502 A MN  703 1_555 ? ? ? ? ? ? ? 2.781 ? ? 
metalc7  metalc ? ? A GLU 607 OE1 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.708 ? ? 
metalc8  metalc ? ? A GLU 607 OE2 ? ? ? 1_555 D MN  . MN  ? ? A GLU 607 A MN  703 1_555 ? ? ? ? ? ? ? 2.094 ? ? 
metalc9  metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O3P B ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.545 ? ? 
metalc10 metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O1P A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc11 metalc ? ? B MN  .   MN  ? ? ? 1_555 E PGA . O4P A ? A MN  701 A PGA 704 1_555 ? ? ? ? ? ? ? 2.538 ? ? 
metalc12 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 801 1_555 ? ? ? ? ? ? ? 2.580 ? ? 
metalc13 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 802 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc14 metalc ? ? B MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  701 A HOH 803 1_555 ? ? ? ? ? ? ? 2.225 ? ? 
metalc15 metalc ? ? C MN  .   MN  ? ? ? 1_555 E PGA . O3P A ? A MN  702 A PGA 704 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc16 metalc ? ? C MN  .   MN  ? ? ? 1_555 F GDP . O3B ? ? A MN  702 A GDP 705 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc17 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 809 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
metalc18 metalc ? ? C MN  .   MN  ? ? ? 1_555 G HOH . O   ? ? A MN  702 A HOH 826 1_555 ? ? ? ? ? ? ? 2.150 ? ? 
# 
_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  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 2_545 NE2 ? A HIS 502 ? A HIS 502 ? 1_555 58.1  ? 
2  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 2_545 OE1 ? A GLU 607 ? A GLU 607 ? 1_555 55.9  ? 
3  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 2_545 OE1 ? A GLU 607 ? A GLU 607 ? 1_555 4.8   ? 
4  OE1 ? A GLU 63  ? A GLU 63  ? 1_555 MN ? D MN . ? A MN 703 ? 2_545 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 56.2  ? 
5  NE2 ? A HIS 502 ? A HIS 502 ? 1_555 MN ? D MN . ? A MN 703 ? 2_545 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 4.3   ? 
6  OE1 ? A GLU 607 ? A GLU 607 ? 1_555 MN ? D MN . ? A MN 703 ? 2_545 OE2 ? A GLU 607 ? A GLU 607 ? 1_555 0.5   ? 
7  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 92.7  ? 
8  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 92.1  ? 
9  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 88.3  ? 
10 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 85.4  ? 
11 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_555 168.7 ? 
12 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_555 103.0 ? 
13 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_555 114.4 ? 
14 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_555 147.0 ? 
15 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_555 108.0 ? 
16 O3P 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 30.0  ? 
17 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_555 155.4 ? 
18 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 96.4  ? 
19 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 65.5  ? 
20 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 89.8  ? 
21 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 66.9  ? 
22 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 801 ? 1_555 94.7  ? 
23 NE2 ? A HIS 264 ? A HIS 264 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 801 ? 1_555 172.6 ? 
24 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 801 ? 1_555 91.0  ? 
25 O3P B E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 801 ? 1_555 14.9  ? 
26 O1P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 801 ? 1_555 27.4  ? 
27 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 801 ? 1_555 76.6  ? 
28 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 86.9  ? 
29 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 92.9  ? 
30 OD1 ? A ASP 311 ? A ASP 311 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 178.5 ? 
31 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 75.9  ? 
32 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 71.4  ? 
33 O4P A E PGA .   ? A PGA 704 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 115.2 ? 
34 O   ? G HOH .   ? A HOH 801 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 802 ? 1_555 87.9  ? 
35 NZ  ? A LYS 244 ? A LYS 244 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 169.5 ? 
36 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 85.1  ? 
37 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 98.1  ? 
38 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 94.7  ? 
39 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 64.8  ? 
40 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 34.9  ? 
41 O   ? G HOH .   ? A HOH 801 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 87.7  ? 
42 O   ? G HOH .   ? A HOH 802 ? 1_555 MN ? B MN . ? A MN 701 ? 1_555 O   ? G HOH .   ? A HOH 803 ? 1_555 83.0  ? 
43 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_555 167.4 ? 
44 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 78.3  ? 
45 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O3B ? F GDP .   ? A GDP 705 ? 1_555 105.8 ? 
46 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 809 ? 1_555 87.7  ? 
47 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 809 ? 1_555 80.7  ? 
48 O3B ? F GDP .   ? A GDP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 809 ? 1_555 86.7  ? 
49 OG1 ? A THR 291 ? A THR 291 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 826 ? 1_555 91.2  ? 
50 O3P A E PGA .   ? A PGA 704 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 826 ? 1_555 100.5 ? 
51 O3B ? F GDP .   ? A GDP 705 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 826 ? 1_555 91.0  ? 
52 O   ? G HOH .   ? A HOH 809 ? 1_555 MN ? C MN . ? A MN 702 ? 1_555 O   ? G HOH .   ? A HOH 826 ? 1_555 177.6 ? 
# 
_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       2.30 
# 
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 TRP A 76  ? ALA A 78  ? TRP A 76  ALA A 78  
AA3 3 ILE A 356 ? THR A 358 ? ILE A 356 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 ? THR A 553 ? ALA A 550 THR A 553 
AA8 2 GLY A 556 ? PRO A 559 ? GLY A 556 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 ILE A 158 ? N ILE A 158 O CYS A 192 ? O CYS A 192 
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 THR A 358 ? N THR A 358 O ARG A 405 ? O ARG A 405 
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 LYS A 278 ? O LYS A 278 N ILE A 270 ? N ILE A 270 
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 ILE A 431 ? N ILE A 431 O LYS A 510 ? O LYS A 510 
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                   9EIV 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE2 A GLU 421 ? ? O A HOH 804 ? ? 2.18 
2 1 O   A GLU 463 ? ? O A HOH 805 ? ? 2.18 
3 1 OG  A SER 286 ? ? O A HOH 806 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 6   ? ? -136.15 -130.57 
2  1 ASN A 7   ? ? -141.45 48.59   
3  1 ARG A 129 ? ? -126.75 -50.51  
4  1 LYS A 243 ? ? -73.43  -83.35  
5  1 TRP A 260 ? ? -122.98 -162.34 
6  1 ASP A 311 ? ? -152.74 -42.72  
7  1 PHE A 333 ? ? -119.26 73.30   
8  1 THR A 465 ? ? -109.46 -146.77 
9  1 ALA A 467 ? ? -106.12 -65.64  
10 1 ALA A 468 ? ? -89.42  -142.34 
11 1 ASP A 478 ? ? -150.82 67.12   
12 1 PHE A 480 ? ? 57.42   15.94   
13 1 PHE A 530 ? ? 59.23   -130.21 
14 1 LEU A 569 ? ? -104.00 -82.47  
15 1 ASN A 601 ? ? 49.73   -119.44 
# 
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 -0.8909 -18.6450 -7.2082 0.3420 ? 0.0647  ? 0.0236  ? 0.2721 ? -0.0172 ? 0.3512 ? 2.1545 ? 1.0765  
? -0.7808 ? 3.3407 ? -0.0684 ? 4.3894 ? -0.1338 ? 0.2311  ? -0.2880 ? -0.3686 ? -0.0865 ? -0.0490 ? 0.4132  ? 0.0881  ? 0.2453  ? 
2 'X-RAY DIFFRACTION' ? refined 4.7578  -5.9875  -5.3152 0.3242 ? 0.0234  ? 0.0564  ? 0.3813 ? 0.0072  ? 0.2589 ? 2.5646 ? 1.5761  
? 0.3254  ? 5.2905 ? 0.6447  ? 1.8414 ? 0.1619  ? 0.0411  ? 0.0672  ? -0.2727 ? -0.1351 ? -0.2441 ? -0.1086 ? 0.1694  ? -0.0145 ? 
3 'X-RAY DIFFRACTION' ? refined -9.5263 -0.5143  9.1723  0.4610 ? -0.0836 ? 0.0960  ? 0.3795 ? -0.0408 ? 0.3953 ? 0.4962 ? -0.4931 
? -0.0238 ? 1.2070 ? 0.5130  ? 0.3329 ? 0.0013  ? 0.0292  ? -0.0518 ? 0.2456  ? -0.0705 ? 0.1913  ? 0.0936  ? -0.1038 ? 0.0651  ? 
4 'X-RAY DIFFRACTION' ? refined -0.9772 -18.1358 21.4234 0.7815 ? -0.2276 ? -0.0401 ? 0.4883 ? 0.0297  ? 0.3541 ? 2.8178 ? -1.0381 
? -1.4205 ? 5.1271 ? -1.2393 ? 2.4774 ? 0.0564  ? -0.2754 ? -0.3801 ? 0.9868  ? -0.2478 ? -0.2979 ? 0.0424  ? 0.8625  ? 0.2375  ? 
5 'X-RAY DIFFRACTION' ? refined -5.4457 9.2780   14.4734 0.2974 ? 0.0131  ? 0.0424  ? 0.2030 ? 0.0309  ? 0.3057 ? 3.9133 ? 0.6979  
? -0.0496 ? 2.3590 ? 0.7149  ? 3.0103 ? -0.0838 ? 0.0245  ? -0.5544 ? 0.2759  ? 0.0144  ? -0.2023 ? 0.0917  ? 0.1457  ? 0.0566  ? 
6 'X-RAY DIFFRACTION' ? refined -3.0560 17.2792  18.9492 0.4729 ? -0.0322 ? -0.0183 ? 0.2453 ? 0.0251  ? 0.3168 ? 3.5662 ? 0.1649  
? -0.8885 ? 2.0567 ? -0.1839 ? 2.0409 ? -0.0513 ? -0.3175 ? 0.0493  ? 0.3724  ? -0.0600 ? -0.0803 ? -0.1385 ? 0.0881  ? 0.1032  ? 
# 
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 91 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 92 through 225 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 226 through 368 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 369 through 412 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 413 through 474 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 475 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                    9EIV 
_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]   0.022366 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.008803 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008348 
_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]   0.017889 
_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   ? 2.965   -13.086 -31.893 1.00 128.29 ? 3   PRO A N     1 
ATOM   2    C  CA    . PRO A 1 3   ? 3.564   -14.162 -32.688 1.00 122.27 ? 3   PRO A CA    1 
ATOM   3    C  C     . PRO A 1 3   ? 4.775   -14.788 -32.003 1.00 120.92 ? 3   PRO A C     1 
ATOM   4    O  O     . PRO A 1 3   ? 5.061   -14.472 -30.848 1.00 119.27 ? 3   PRO A O     1 
ATOM   5    C  CB    . PRO A 1 3   ? 3.978   -13.449 -33.975 1.00 123.74 ? 3   PRO A CB    1 
ATOM   6    C  CG    . PRO A 1 3   ? 4.272   -12.057 -33.535 1.00 122.33 ? 3   PRO A CG    1 
ATOM   7    C  CD    . PRO A 1 3   ? 3.282   -11.755 -32.440 1.00 123.08 ? 3   PRO A CD    1 
ATOM   8    N  N     . GLN A 1 4   ? 5.476   -15.665 -32.718 1.00 97.36  ? 4   GLN A N     1 
ATOM   9    C  CA    . GLN A 1 4   ? 6.686   -16.294 -32.205 1.00 87.06  ? 4   GLN A CA    1 
ATOM   10   C  C     . GLN A 1 4   ? 7.254   -17.199 -33.288 1.00 81.79  ? 4   GLN A C     1 
ATOM   11   O  O     . GLN A 1 4   ? 6.537   -17.644 -34.189 1.00 84.79  ? 4   GLN A O     1 
ATOM   12   C  CB    . GLN A 1 4   ? 6.420   -17.093 -30.923 1.00 90.09  ? 4   GLN A CB    1 
ATOM   13   C  CG    . GLN A 1 4   ? 5.406   -18.216 -31.077 1.00 87.97  ? 4   GLN A CG    1 
ATOM   14   C  CD    . GLN A 1 4   ? 5.133   -18.927 -29.767 1.00 91.41  ? 4   GLN A CD    1 
ATOM   15   O  OE1   . GLN A 1 4   ? 5.727   -18.605 -28.738 1.00 88.88  ? 4   GLN A OE1   1 
ATOM   16   N  NE2   . GLN A 1 4   ? 4.228   -19.899 -29.797 1.00 92.02  ? 4   GLN A NE2   1 
ATOM   17   N  N     . LEU A 1 5   ? 8.557   -17.460 -33.189 1.00 82.48  ? 5   LEU A N     1 
ATOM   18   C  CA    . LEU A 1 5   ? 9.236   -18.385 -34.084 1.00 79.89  ? 5   LEU A CA    1 
ATOM   19   C  C     . LEU A 1 5   ? 9.372   -19.785 -33.502 1.00 77.39  ? 5   LEU A C     1 
ATOM   20   O  O     . LEU A 1 5   ? 9.738   -20.711 -34.235 1.00 79.22  ? 5   LEU A O     1 
ATOM   21   C  CB    . LEU A 1 5   ? 10.626  -17.849 -34.449 1.00 78.19  ? 5   LEU A CB    1 
ATOM   22   C  CG    . LEU A 1 5   ? 10.644  -16.614 -35.353 1.00 79.89  ? 5   LEU A CG    1 
ATOM   23   C  CD1   . LEU A 1 5   ? 12.061  -16.090 -35.530 1.00 81.83  ? 5   LEU A CD1   1 
ATOM   24   C  CD2   . LEU A 1 5   ? 10.013  -16.934 -36.699 1.00 83.36  ? 5   LEU A CD2   1 
ATOM   25   N  N     . HIS A 1 6   ? 9.093   -19.962 -32.212 1.00 77.81  ? 6   HIS A N     1 
ATOM   26   C  CA    . HIS A 1 6   ? 9.125   -21.282 -31.594 1.00 86.69  ? 6   HIS A CA    1 
ATOM   27   C  C     . HIS A 1 6   ? 7.910   -21.465 -30.692 1.00 89.67  ? 6   HIS A C     1 
ATOM   28   O  O     . HIS A 1 6   ? 6.778   -21.202 -31.110 1.00 88.32  ? 6   HIS A O     1 
ATOM   29   C  CB    . HIS A 1 6   ? 10.424  -21.480 -30.807 1.00 80.21  ? 6   HIS A CB    1 
ATOM   30   C  CG    . HIS A 1 6   ? 11.659  -21.428 -31.654 1.00 81.31  ? 6   HIS A CG    1 
ATOM   31   N  ND1   . HIS A 1 6   ? 12.346  -20.258 -31.897 1.00 75.89  ? 6   HIS A ND1   1 
ATOM   32   C  CD2   . HIS A 1 6   ? 12.330  -22.402 -32.314 1.00 79.47  ? 6   HIS A CD2   1 
ATOM   33   C  CE1   . HIS A 1 6   ? 13.387  -20.513 -32.670 1.00 79.78  ? 6   HIS A CE1   1 
ATOM   34   N  NE2   . HIS A 1 6   ? 13.400  -21.806 -32.937 1.00 82.03  ? 6   HIS A NE2   1 
ATOM   35   N  N     . ASN A 1 7   ? 8.129   -21.910 -29.458 1.00 109.47 ? 7   ASN A N     1 
ATOM   36   C  CA    . ASN A 1 7   ? 7.046   -22.109 -28.498 1.00 108.96 ? 7   ASN A CA    1 
ATOM   37   C  C     . ASN A 1 7   ? 7.499   -21.687 -27.105 1.00 111.13 ? 7   ASN A C     1 
ATOM   38   O  O     . ASN A 1 7   ? 7.317   -22.403 -26.120 1.00 113.58 ? 7   ASN A O     1 
ATOM   39   C  CB    . ASN A 1 7   ? 6.569   -23.560 -28.507 1.00 107.89 ? 7   ASN A CB    1 
ATOM   40   C  CG    . ASN A 1 7   ? 5.762   -23.903 -29.744 1.00 123.64 ? 7   ASN A CG    1 
ATOM   41   O  OD1   . ASN A 1 7   ? 6.320   -24.232 -30.791 1.00 125.00 ? 7   ASN A OD1   1 
ATOM   42   N  ND2   . ASN A 1 7   ? 4.442   -23.832 -29.628 1.00 119.70 ? 7   ASN A ND2   1 
ATOM   43   N  N     . GLY A 1 8   ? 8.091   -20.499 -27.008 1.00 112.81 ? 8   GLY A N     1 
ATOM   44   C  CA    . GLY A 1 8   ? 8.622   -20.035 -25.741 1.00 111.53 ? 8   GLY A CA    1 
ATOM   45   C  C     . GLY A 1 8   ? 7.952   -18.791 -25.195 1.00 112.04 ? 8   GLY A C     1 
ATOM   46   O  O     . GLY A 1 8   ? 8.386   -18.247 -24.175 1.00 111.82 ? 8   GLY A O     1 
ATOM   47   N  N     . LEU A 1 9   ? 6.890   -18.328 -25.857 1.00 93.92  ? 9   LEU A N     1 
ATOM   48   C  CA    . LEU A 1 9   ? 6.192   -17.122 -25.437 1.00 86.04  ? 9   LEU A CA    1 
ATOM   49   C  C     . LEU A 1 9   ? 4.706   -17.319 -25.172 1.00 78.29  ? 9   LEU A C     1 
ATOM   50   O  O     . LEU A 1 9   ? 4.111   -16.485 -24.480 1.00 74.82  ? 9   LEU A O     1 
ATOM   51   C  CB    . LEU A 1 9   ? 6.360   -16.010 -26.486 1.00 83.15  ? 9   LEU A CB    1 
ATOM   52   C  CG    . LEU A 1 9   ? 7.801   -15.584 -26.783 1.00 81.29  ? 9   LEU A CG    1 
ATOM   53   C  CD1   . LEU A 1 9   ? 7.833   -14.452 -27.799 1.00 79.65  ? 9   LEU A CD1   1 
ATOM   54   C  CD2   . LEU A 1 9   ? 8.522   -15.184 -25.502 1.00 76.58  ? 9   LEU A CD2   1 
ATOM   55   N  N     . ASP A 1 10  ? 4.095   -18.381 -25.693 1.00 81.44  ? 10  ASP A N     1 
ATOM   56   C  CA    . ASP A 1 10  ? 2.673   -18.647 -25.481 1.00 77.96  ? 10  ASP A CA    1 
ATOM   57   C  C     . ASP A 1 10  ? 2.540   -19.621 -24.317 1.00 66.17  ? 10  ASP A C     1 
ATOM   58   O  O     . ASP A 1 10  ? 2.730   -20.830 -24.475 1.00 63.24  ? 10  ASP A O     1 
ATOM   59   C  CB    . ASP A 1 10  ? 2.031   -19.196 -26.750 1.00 78.93  ? 10  ASP A CB    1 
ATOM   60   C  CG    . ASP A 1 10  ? 0.542   -19.434 -26.596 1.00 72.76  ? 10  ASP A CG    1 
ATOM   61   O  OD1   . ASP A 1 10  ? -0.032  -18.996 -25.576 1.00 72.36  ? 10  ASP A OD1   1 
ATOM   62   O  OD2   . ASP A 1 10  ? -0.054  -20.063 -27.495 1.00 80.13  ? 10  ASP A OD2   1 
ATOM   63   N  N     . PHE A 1 11  ? 2.215   -19.089 -23.141 1.00 61.07  ? 11  PHE A N     1 
ATOM   64   C  CA    . PHE A 1 11  ? 2.071   -19.885 -21.931 1.00 59.66  ? 11  PHE A CA    1 
ATOM   65   C  C     . PHE A 1 11  ? 0.697   -20.524 -21.797 1.00 52.03  ? 11  PHE A C     1 
ATOM   66   O  O     . PHE A 1 11  ? 0.328   -20.926 -20.689 1.00 51.60  ? 11  PHE A O     1 
ATOM   67   C  CB    . PHE A 1 11  ? 2.365   -19.023 -20.699 1.00 55.26  ? 11  PHE A CB    1 
ATOM   68   C  CG    . PHE A 1 11  ? 3.820   -18.978 -20.320 1.00 59.84  ? 11  PHE A CG    1 
ATOM   69   C  CD1   . PHE A 1 11  ? 4.720   -18.216 -21.046 1.00 61.82  ? 11  PHE A CD1   1 
ATOM   70   C  CD2   . PHE A 1 11  ? 4.284   -19.690 -19.225 1.00 62.24  ? 11  PHE A CD2   1 
ATOM   71   C  CE1   . PHE A 1 11  ? 6.059   -18.174 -20.693 1.00 60.29  ? 11  PHE A CE1   1 
ATOM   72   C  CE2   . PHE A 1 11  ? 5.621   -19.651 -18.867 1.00 56.29  ? 11  PHE A CE2   1 
ATOM   73   C  CZ    . PHE A 1 11  ? 6.509   -18.892 -19.603 1.00 52.70  ? 11  PHE A CZ    1 
ATOM   74   N  N     . SER A 1 12  ? -0.066  -20.633 -22.886 1.00 47.50  ? 12  SER A N     1 
ATOM   75   C  CA    . SER A 1 12  ? -1.408  -21.195 -22.786 1.00 53.23  ? 12  SER A CA    1 
ATOM   76   C  C     . SER A 1 12  ? -1.375  -22.636 -22.290 1.00 57.38  ? 12  SER A C     1 
ATOM   77   O  O     . SER A 1 12  ? -2.272  -23.065 -21.554 1.00 53.53  ? 12  SER A O     1 
ATOM   78   C  CB    . SER A 1 12  ? -2.118  -21.107 -24.137 1.00 54.68  ? 12  SER A CB    1 
ATOM   79   O  OG    . SER A 1 12  ? -2.447  -19.763 -24.445 1.00 65.01  ? 12  SER A OG    1 
ATOM   80   N  N     . ALA A 1 13  ? -0.347  -23.398 -22.672 1.00 56.32  ? 13  ALA A N     1 
ATOM   81   C  CA    . ALA A 1 13  ? -0.257  -24.797 -22.268 1.00 50.44  ? 13  ALA A CA    1 
ATOM   82   C  C     . ALA A 1 13  ? 0.002   -24.973 -20.777 1.00 54.39  ? 13  ALA A C     1 
ATOM   83   O  O     . ALA A 1 13  ? -0.180  -26.083 -20.265 1.00 54.30  ? 13  ALA A O     1 
ATOM   84   C  CB    . ALA A 1 13  ? 0.838   -25.506 -23.070 1.00 56.86  ? 13  ALA A CB    1 
ATOM   85   N  N     . LYS A 1 14  ? 0.410   -23.920 -20.070 1.00 48.64  ? 14  LYS A N     1 
ATOM   86   C  CA    . LYS A 1 14  ? 0.677   -24.000 -18.640 1.00 50.53  ? 14  LYS A CA    1 
ATOM   87   C  C     . LYS A 1 14  ? -0.445  -23.416 -17.790 1.00 45.08  ? 14  LYS A C     1 
ATOM   88   O  O     . LYS A 1 14  ? -0.322  -23.390 -16.562 1.00 45.84  ? 14  LYS A O     1 
ATOM   89   C  CB    . LYS A 1 14  ? 1.996   -23.294 -18.306 1.00 51.05  ? 14  LYS A CB    1 
ATOM   90   C  CG    . LYS A 1 14  ? 3.233   -23.981 -18.864 1.00 56.27  ? 14  LYS A CG    1 
ATOM   91   C  CD    . LYS A 1 14  ? 4.504   -23.316 -18.357 1.00 55.48  ? 14  LYS A CD    1 
ATOM   92   C  CE    . LYS A 1 14  ? 5.742   -23.973 -18.945 1.00 63.28  ? 14  LYS A CE    1 
ATOM   93   N  NZ    . LYS A 1 14  ? 5.775   -25.436 -18.669 1.00 59.96  ? 14  LYS A NZ    1 
ATOM   94   N  N     . VAL A 1 15  ? -1.526  -22.949 -18.408 1.00 49.31  ? 15  VAL A N     1 
ATOM   95   C  CA    . VAL A 1 15  ? -2.660  -22.402 -17.670 1.00 46.31  ? 15  VAL A CA    1 
ATOM   96   C  C     . VAL A 1 15  ? -3.512  -23.555 -17.152 1.00 47.99  ? 15  VAL A C     1 
ATOM   97   O  O     . VAL A 1 15  ? -4.079  -24.326 -17.934 1.00 50.54  ? 15  VAL A O     1 
ATOM   98   C  CB    . VAL A 1 15  ? -3.486  -21.454 -18.550 1.00 50.75  ? 15  VAL A CB    1 
ATOM   99   C  CG1   . VAL A 1 15  ? -4.693  -20.932 -17.783 1.00 43.13  ? 15  VAL A CG1   1 
ATOM   100  C  CG2   . VAL A 1 15  ? -2.621  -20.297 -19.048 1.00 42.64  ? 15  VAL A CG2   1 
ATOM   101  N  N     . ILE A 1 16  ? -3.601  -23.678 -15.824 1.00 40.16  ? 16  ILE A N     1 
ATOM   102  C  CA    . ILE A 1 16  ? -4.383  -24.744 -15.204 1.00 47.21  ? 16  ILE A CA    1 
ATOM   103  C  C     . ILE A 1 16  ? -5.752  -24.276 -14.723 1.00 44.62  ? 16  ILE A C     1 
ATOM   104  O  O     . ILE A 1 16  ? -6.575  -25.119 -14.332 1.00 44.48  ? 16  ILE A O     1 
ATOM   105  C  CB    . ILE A 1 16  ? -3.615  -25.402 -14.036 1.00 44.08  ? 16  ILE A CB    1 
ATOM   106  C  CG1   . ILE A 1 16  ? -3.194  -24.355 -13.005 1.00 46.80  ? 16  ILE A CG1   1 
ATOM   107  C  CG2   . ILE A 1 16  ? -2.409  -26.171 -14.556 1.00 41.03  ? 16  ILE A CG2   1 
ATOM   108  C  CD1   . ILE A 1 16  ? -2.531  -24.944 -11.775 1.00 48.53  ? 16  ILE A CD1   1 
ATOM   109  N  N     . GLN A 1 17  ? -6.021  -22.971 -14.725 1.00 43.26  ? 17  GLN A N     1 
ATOM   110  C  CA    . GLN A 1 17  ? -7.375  -22.471 -14.515 1.00 44.52  ? 17  GLN A CA    1 
ATOM   111  C  C     . GLN A 1 17  ? -7.532  -21.144 -15.238 1.00 46.60  ? 17  GLN A C     1 
ATOM   112  O  O     . GLN A 1 17  ? -6.711  -20.239 -15.065 1.00 45.78  ? 17  GLN A O     1 
ATOM   113  C  CB    . GLN A 1 17  ? -7.707  -22.295 -13.028 1.00 44.88  ? 17  GLN A CB    1 
ATOM   114  C  CG    . GLN A 1 17  ? -9.035  -21.573 -12.806 1.00 45.09  ? 17  GLN A CG    1 
ATOM   115  C  CD    . GLN A 1 17  ? -9.514  -21.625 -11.368 1.00 49.71  ? 17  GLN A CD    1 
ATOM   116  O  OE1   . GLN A 1 17  ? -9.395  -22.650 -10.698 1.00 52.83  ? 17  GLN A OE1   1 
ATOM   117  N  NE2   . GLN A 1 17  ? -10.065 -20.515 -10.888 1.00 47.92  ? 17  GLN A NE2   1 
ATOM   118  N  N     . GLY A 1 18  ? -8.586  -21.035 -16.034 1.00 48.77  ? 18  GLY A N     1 
ATOM   119  C  CA    . GLY A 1 18  ? -8.852  -19.837 -16.794 1.00 45.07  ? 18  GLY A CA    1 
ATOM   120  C  C     . GLY A 1 18  ? -8.330  -19.924 -18.213 1.00 52.39  ? 18  GLY A C     1 
ATOM   121  O  O     . GLY A 1 18  ? -8.028  -20.997 -18.742 1.00 55.85  ? 18  GLY A O     1 
ATOM   122  N  N     . SER A 1 19  ? -8.222  -18.755 -18.837 1.00 54.96  ? 19  SER A N     1 
ATOM   123  C  CA    . SER A 1 19  ? -7.750  -18.669 -20.211 1.00 53.40  ? 19  SER A CA    1 
ATOM   124  C  C     . SER A 1 19  ? -7.063  -17.329 -20.414 1.00 59.65  ? 19  SER A C     1 
ATOM   125  O  O     . SER A 1 19  ? -7.622  -16.285 -20.064 1.00 58.03  ? 19  SER A O     1 
ATOM   126  C  CB    . SER A 1 19  ? -8.907  -18.830 -21.204 1.00 54.86  ? 19  SER A CB    1 
ATOM   127  O  OG    . SER A 1 19  ? -8.474  -18.602 -22.534 1.00 70.27  ? 19  SER A OG    1 
ATOM   128  N  N     . LEU A 1 20  ? -5.848  -17.362 -20.968 1.00 59.10  ? 20  LEU A N     1 
ATOM   129  C  CA    . LEU A 1 20  ? -5.178  -16.116 -21.326 1.00 62.58  ? 20  LEU A CA    1 
ATOM   130  C  C     . LEU A 1 20  ? -5.964  -15.349 -22.380 1.00 63.78  ? 20  LEU A C     1 
ATOM   131  O  O     . LEU A 1 20  ? -5.827  -14.125 -22.487 1.00 64.33  ? 20  LEU A O     1 
ATOM   132  C  CB    . LEU A 1 20  ? -3.761  -16.402 -21.825 1.00 54.91  ? 20  LEU A CB    1 
ATOM   133  C  CG    . LEU A 1 20  ? -2.800  -17.070 -20.840 1.00 53.01  ? 20  LEU A CG    1 
ATOM   134  C  CD1   . LEU A 1 20  ? -1.489  -17.417 -21.519 1.00 59.92  ? 20  LEU A CD1   1 
ATOM   135  C  CD2   . LEU A 1 20  ? -2.558  -16.182 -19.627 1.00 48.63  ? 20  LEU A CD2   1 
ATOM   136  N  N     . ASP A 1 21  ? -6.787  -16.048 -23.164 1.00 66.49  ? 21  ASP A N     1 
ATOM   137  C  CA    . ASP A 1 21  ? -7.582  -15.382 -24.190 1.00 76.02  ? 21  ASP A CA    1 
ATOM   138  C  C     . ASP A 1 21  ? -8.650  -14.488 -23.571 1.00 77.87  ? 21  ASP A C     1 
ATOM   139  O  O     . ASP A 1 21  ? -8.925  -13.397 -24.083 1.00 89.73  ? 21  ASP A O     1 
ATOM   140  C  CB    . ASP A 1 21  ? -8.220  -16.421 -25.114 1.00 83.98  ? 21  ASP A CB    1 
ATOM   141  C  CG    . ASP A 1 21  ? -7.192  -17.302 -25.803 1.00 87.88  ? 21  ASP A CG    1 
ATOM   142  O  OD1   . ASP A 1 21  ? -6.076  -16.813 -26.076 1.00 84.18  ? 21  ASP A OD1   1 
ATOM   143  O  OD2   . ASP A 1 21  ? -7.502  -18.483 -26.069 1.00 95.94  ? 21  ASP A OD2   1 
ATOM   144  N  N     . SER A 1 22  ? -9.262  -14.930 -22.472 1.00 73.98  ? 22  SER A N     1 
ATOM   145  C  CA    . SER A 1 22  ? -10.337 -14.179 -21.834 1.00 71.64  ? 22  SER A CA    1 
ATOM   146  C  C     . SER A 1 22  ? -9.848  -12.945 -21.087 1.00 71.21  ? 22  SER A C     1 
ATOM   147  O  O     . SER A 1 22  ? -10.676 -12.159 -20.613 1.00 73.00  ? 22  SER A O     1 
ATOM   148  C  CB    . SER A 1 22  ? -11.111 -15.087 -20.873 1.00 68.19  ? 22  SER A CB    1 
ATOM   149  O  OG    . SER A 1 22  ? -10.268 -15.588 -19.850 1.00 71.06  ? 22  SER A OG    1 
ATOM   150  N  N     . LEU A 1 23  ? -8.540  -12.752 -20.975 1.00 66.37  ? 23  LEU A N     1 
ATOM   151  C  CA    . LEU A 1 23  ? -8.016  -11.607 -20.252 1.00 62.25  ? 23  LEU A CA    1 
ATOM   152  C  C     . LEU A 1 23  ? -7.982  -10.369 -21.146 1.00 65.22  ? 23  LEU A C     1 
ATOM   153  O  O     . LEU A 1 23  ? -7.777  -10.473 -22.359 1.00 65.90  ? 23  LEU A O     1 
ATOM   154  C  CB    . LEU A 1 23  ? -6.612  -11.900 -19.738 1.00 56.25  ? 23  LEU A CB    1 
ATOM   155  C  CG    . LEU A 1 23  ? -6.475  -13.043 -18.732 1.00 56.48  ? 23  LEU A CG    1 
ATOM   156  C  CD1   . LEU A 1 23  ? -5.014  -13.280 -18.390 1.00 58.48  ? 23  LEU A CD1   1 
ATOM   157  C  CD2   . LEU A 1 23  ? -7.281  -12.744 -17.477 1.00 56.67  ? 23  LEU A CD2   1 
ATOM   158  N  N     . PRO A 1 24  ? -8.191  -9.185  -20.572 1.00 63.94  ? 24  PRO A N     1 
ATOM   159  C  CA    . PRO A 1 24  ? -7.991  -7.957  -21.345 1.00 56.89  ? 24  PRO A CA    1 
ATOM   160  C  C     . PRO A 1 24  ? -6.562  -7.887  -21.860 1.00 58.18  ? 24  PRO A C     1 
ATOM   161  O  O     . PRO A 1 24  ? -5.633  -8.417  -21.248 1.00 58.46  ? 24  PRO A O     1 
ATOM   162  C  CB    . PRO A 1 24  ? -8.285  -6.845  -20.332 1.00 59.49  ? 24  PRO A CB    1 
ATOM   163  C  CG    . PRO A 1 24  ? -9.156  -7.497  -19.300 1.00 63.65  ? 24  PRO A CG    1 
ATOM   164  C  CD    . PRO A 1 24  ? -8.666  -8.911  -19.205 1.00 59.76  ? 24  PRO A CD    1 
ATOM   165  N  N     . GLN A 1 25  ? -6.398  -7.226  -23.007 1.00 59.36  ? 25  GLN A N     1 
ATOM   166  C  CA    . GLN A 1 25  ? -5.110  -7.211  -23.694 1.00 63.02  ? 25  GLN A CA    1 
ATOM   167  C  C     . GLN A 1 25  ? -3.962  -6.921  -22.732 1.00 59.26  ? 25  GLN A C     1 
ATOM   168  O  O     . GLN A 1 25  ? -3.039  -7.728  -22.581 1.00 59.10  ? 25  GLN A O     1 
ATOM   169  C  CB    . GLN A 1 25  ? -5.135  -6.183  -24.825 1.00 73.04  ? 25  GLN A CB    1 
ATOM   170  C  CG    . GLN A 1 25  ? -3.851  -6.132  -25.635 1.00 79.47  ? 25  GLN A CG    1 
ATOM   171  C  CD    . GLN A 1 25  ? -3.902  -5.096  -26.737 1.00 86.82  ? 25  GLN A CD    1 
ATOM   172  O  OE1   . GLN A 1 25  ? -3.899  -3.894  -26.474 1.00 88.74  ? 25  GLN A OE1   1 
ATOM   173  N  NE2   . GLN A 1 25  ? -3.956  -5.558  -27.980 1.00 96.19  ? 25  GLN A NE2   1 
ATOM   174  N  N     . GLU A 1 26  ? -4.009  -5.765  -22.066 1.00 60.46  ? 26  GLU A N     1 
ATOM   175  C  CA    . GLU A 1 26  ? -2.909  -5.368  -21.195 1.00 55.92  ? 26  GLU A CA    1 
ATOM   176  C  C     . GLU A 1 26  ? -2.747  -6.291  -19.994 1.00 54.00  ? 26  GLU A C     1 
ATOM   177  O  O     . GLU A 1 26  ? -1.648  -6.370  -19.437 1.00 53.82  ? 26  GLU A O     1 
ATOM   178  C  CB    . GLU A 1 26  ? -3.105  -3.924  -20.733 1.00 59.18  ? 26  GLU A CB    1 
ATOM   179  C  CG    . GLU A 1 26  ? -2.967  -2.914  -21.857 1.00 61.76  ? 26  GLU A CG    1 
ATOM   180  C  CD    . GLU A 1 26  ? -1.624  -3.009  -22.557 1.00 63.39  ? 26  GLU A CD    1 
ATOM   181  O  OE1   . GLU A 1 26  ? -0.598  -3.149  -21.860 1.00 61.56  ? 26  GLU A OE1   1 
ATOM   182  O  OE2   . GLU A 1 26  ? -1.593  -2.949  -23.804 1.00 73.36  ? 26  GLU A OE2   1 
ATOM   183  N  N     . VAL A 1 27  ? -3.806  -6.991  -19.584 1.00 53.82  ? 27  VAL A N     1 
ATOM   184  C  CA    . VAL A 1 27  ? -3.655  -7.984  -18.525 1.00 53.99  ? 27  VAL A CA    1 
ATOM   185  C  C     . VAL A 1 27  ? -2.857  -9.179  -19.030 1.00 48.15  ? 27  VAL A C     1 
ATOM   186  O  O     . VAL A 1 27  ? -1.980  -9.698  -18.329 1.00 43.36  ? 27  VAL A O     1 
ATOM   187  C  CB    . VAL A 1 27  ? -5.029  -8.415  -17.983 1.00 54.25  ? 27  VAL A CB    1 
ATOM   188  C  CG1   . VAL A 1 27  ? -4.858  -9.495  -16.927 1.00 48.99  ? 27  VAL A CG1   1 
ATOM   189  C  CG2   . VAL A 1 27  ? -5.779  -7.219  -17.413 1.00 48.43  ? 27  VAL A CG2   1 
ATOM   190  N  N     . ARG A 1 28  ? -3.146  -9.636  -20.250 1.00 50.29  ? 28  ARG A N     1 
ATOM   191  C  CA    . ARG A 1 28  ? -2.417  -10.776 -20.797 1.00 53.71  ? 28  ARG A CA    1 
ATOM   192  C  C     . ARG A 1 28  ? -0.934  -10.459 -20.938 1.00 43.88  ? 28  ARG A C     1 
ATOM   193  O  O     . ARG A 1 28  ? -0.078  -11.242 -20.510 1.00 49.39  ? 28  ARG A O     1 
ATOM   194  C  CB    . ARG A 1 28  ? -3.008  -11.194 -22.144 1.00 47.53  ? 28  ARG A CB    1 
ATOM   195  C  CG    . ARG A 1 28  ? -2.389  -12.473 -22.692 1.00 60.00  ? 28  ARG A CG    1 
ATOM   196  C  CD    . ARG A 1 28  ? -2.656  -12.658 -24.177 1.00 63.46  ? 28  ARG A CD    1 
ATOM   197  N  NE    . ARG A 1 28  ? -1.980  -13.845 -24.690 1.00 66.16  ? 28  ARG A NE    1 
ATOM   198  C  CZ    . ARG A 1 28  ? -2.572  -15.009 -24.921 1.00 66.57  ? 28  ARG A CZ    1 
ATOM   199  N  NH1   . ARG A 1 28  ? -3.871  -15.172 -24.736 1.00 69.33  ? 28  ARG A NH1   1 
ATOM   200  N  NH2   . ARG A 1 28  ? -1.841  -16.035 -25.349 1.00 65.30  ? 28  ARG A NH2   1 
ATOM   201  N  N     . LYS A 1 29  ? -0.609  -9.314  -21.540 1.00 46.70  ? 29  LYS A N     1 
ATOM   202  C  CA    . LYS A 1 29  ? 0.790   -8.915  -21.657 1.00 49.61  ? 29  LYS A CA    1 
ATOM   203  C  C     . LYS A 1 29  ? 1.470   -8.917  -20.293 1.00 48.88  ? 29  LYS A C     1 
ATOM   204  O  O     . LYS A 1 29  ? 2.587   -9.426  -20.141 1.00 49.31  ? 29  LYS A O     1 
ATOM   205  C  CB    . LYS A 1 29  ? 0.899   -7.531  -22.301 1.00 54.08  ? 29  LYS A CB    1 
ATOM   206  C  CG    . LYS A 1 29  ? 0.300   -7.418  -23.694 1.00 58.92  ? 29  LYS A CG    1 
ATOM   207  C  CD    . LYS A 1 29  ? 0.582   -6.042  -24.288 1.00 62.90  ? 29  LYS A CD    1 
ATOM   208  C  CE    . LYS A 1 29  ? -0.372  -5.705  -25.425 1.00 72.96  ? 29  LYS A CE    1 
ATOM   209  N  NZ    . LYS A 1 29  ? -0.242  -6.637  -26.575 1.00 88.78  ? 29  LYS A NZ    1 
ATOM   210  N  N     . PHE A 1 30  ? 0.803   -8.351  -19.283 1.00 48.79  ? 30  PHE A N     1 
ATOM   211  C  CA    . PHE A 1 30  ? 1.384   -8.303  -17.945 1.00 43.32  ? 30  PHE A CA    1 
ATOM   212  C  C     . PHE A 1 30  ? 1.607   -9.704  -17.393 1.00 43.86  ? 30  PHE A C     1 
ATOM   213  O  O     . PHE A 1 30  ? 2.648   -9.984  -16.786 1.00 42.04  ? 30  PHE A O     1 
ATOM   214  C  CB    . PHE A 1 30  ? 0.482   -7.485  -17.020 1.00 45.74  ? 30  PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 30  ? 0.954   -7.434  -15.595 1.00 41.94  ? 30  PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 30  ? 2.203   -6.926  -15.284 1.00 41.29  ? 30  PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 30  ? 0.139   -7.873  -14.562 1.00 39.36  ? 30  PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 30  ? 2.637   -6.868  -13.974 1.00 44.69  ? 30  PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 30  ? 0.569   -7.820  -13.250 1.00 39.30  ? 30  PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 30  ? 1.820   -7.317  -12.956 1.00 40.17  ? 30  PHE A CZ    1 
ATOM   221  N  N     . VAL A 1 31  ? 0.643   -10.600 -17.599 1.00 42.24  ? 31  VAL A N     1 
ATOM   222  C  CA    . VAL A 1 31  ? 0.775   -11.964 -17.098 1.00 48.16  ? 31  VAL A CA    1 
ATOM   223  C  C     . VAL A 1 31  ? 1.853   -12.716 -17.871 1.00 46.39  ? 31  VAL A C     1 
ATOM   224  O  O     . VAL A 1 31  ? 2.771   -13.297 -17.281 1.00 40.57  ? 31  VAL A O     1 
ATOM   225  C  CB    . VAL A 1 31  ? -0.579  -12.694 -17.161 1.00 47.34  ? 31  VAL A CB    1 
ATOM   226  C  CG1   . VAL A 1 31  ? -0.408  -14.169 -16.818 1.00 44.00  ? 31  VAL A CG1   1 
ATOM   227  C  CG2   . VAL A 1 31  ? -1.580  -12.035 -16.222 1.00 43.07  ? 31  VAL A CG2   1 
ATOM   228  N  N     . GLU A 1 32  ? 1.762   -12.713 -19.204 1.00 47.32  ? 32  GLU A N     1 
ATOM   229  C  CA    . GLU A 1 32  ? 2.697   -13.500 -20.003 1.00 50.02  ? 32  GLU A CA    1 
ATOM   230  C  C     . GLU A 1 32  ? 4.116   -12.952 -19.910 1.00 49.11  ? 32  GLU A C     1 
ATOM   231  O  O     . GLU A 1 32  ? 5.080   -13.724 -19.849 1.00 52.68  ? 32  GLU A O     1 
ATOM   232  C  CB    . GLU A 1 32  ? 2.235   -13.554 -21.459 1.00 50.51  ? 32  GLU A CB    1 
ATOM   233  C  CG    . GLU A 1 32  ? 1.179   -14.616 -21.740 1.00 59.98  ? 32  GLU A CG    1 
ATOM   234  C  CD    . GLU A 1 32  ? 0.982   -14.856 -23.223 1.00 61.47  ? 32  GLU A CD    1 
ATOM   235  O  OE1   . GLU A 1 32  ? 1.126   -13.892 -24.002 1.00 54.63  ? 32  GLU A OE1   1 
ATOM   236  O  OE2   . GLU A 1 32  ? 0.695   -16.009 -23.611 1.00 66.12  ? 32  GLU A OE2   1 
ATOM   237  N  N     . GLY A 1 33  ? 4.267   -11.626 -19.901 1.00 49.73  ? 33  GLY A N     1 
ATOM   238  C  CA    . GLY A 1 33  ? 5.598   -11.049 -19.811 1.00 45.65  ? 33  GLY A CA    1 
ATOM   239  C  C     . GLY A 1 33  ? 6.345   -11.491 -18.567 1.00 45.68  ? 33  GLY A C     1 
ATOM   240  O  O     . GLY A 1 33  ? 7.530   -11.833 -18.630 1.00 47.42  ? 33  GLY A O     1 
ATOM   241  N  N     . ASN A 1 34  ? 5.665   -11.489 -17.418 1.00 44.72  ? 34  ASN A N     1 
ATOM   242  C  CA    . ASN A 1 34  ? 6.300   -11.920 -16.178 1.00 44.35  ? 34  ASN A CA    1 
ATOM   243  C  C     . ASN A 1 34  ? 6.389   -13.438 -16.080 1.00 46.52  ? 34  ASN A C     1 
ATOM   244  O  O     . ASN A 1 34  ? 7.318   -13.959 -15.454 1.00 50.64  ? 34  ASN A O     1 
ATOM   245  C  CB    . ASN A 1 34  ? 5.546   -11.354 -14.971 1.00 41.92  ? 34  ASN A CB    1 
ATOM   246  C  CG    . ASN A 1 34  ? 5.754   -9.855  -14.798 1.00 40.41  ? 34  ASN A CG    1 
ATOM   247  O  OD1   . ASN A 1 34  ? 6.797   -9.412  -14.315 1.00 45.86  ? 34  ASN A OD1   1 
ATOM   248  N  ND2   . ASN A 1 34  ? 4.752   -9.069  -15.179 1.00 42.62  ? 34  ASN A ND2   1 
ATOM   249  N  N     . ALA A 1 35  ? 5.438   -14.161 -16.676 1.00 48.21  ? 35  ALA A N     1 
ATOM   250  C  CA    . ALA A 1 35  ? 5.583   -15.608 -16.806 1.00 47.01  ? 35  ALA A CA    1 
ATOM   251  C  C     . ALA A 1 35  ? 6.884   -15.953 -17.516 1.00 50.65  ? 35  ALA A C     1 
ATOM   252  O  O     . ALA A 1 35  ? 7.651   -16.810 -17.062 1.00 49.92  ? 35  ALA A O     1 
ATOM   253  C  CB    . ALA A 1 35  ? 4.387   -16.193 -17.560 1.00 44.97  ? 35  ALA A CB    1 
ATOM   254  N  N     . GLN A 1 36  ? 7.149   -15.280 -18.638 1.00 49.46  ? 36  GLN A N     1 
ATOM   255  C  CA    . GLN A 1 36  ? 8.392   -15.500 -19.367 1.00 51.77  ? 36  GLN A CA    1 
ATOM   256  C  C     . GLN A 1 36  ? 9.606   -15.104 -18.536 1.00 45.92  ? 36  GLN A C     1 
ATOM   257  O  O     . GLN A 1 36  ? 10.674  -15.714 -18.669 1.00 49.18  ? 36  GLN A O     1 
ATOM   258  C  CB    . GLN A 1 36  ? 8.360   -14.721 -20.682 1.00 53.11  ? 36  GLN A CB    1 
ATOM   259  C  CG    . GLN A 1 36  ? 7.130   -15.013 -21.533 1.00 58.73  ? 36  GLN A CG    1 
ATOM   260  C  CD    . GLN A 1 36  ? 6.956   -14.026 -22.672 1.00 68.61  ? 36  GLN A CD    1 
ATOM   261  O  OE1   . GLN A 1 36  ? 7.594   -12.973 -22.699 1.00 70.93  ? 36  GLN A OE1   1 
ATOM   262  N  NE2   . GLN A 1 36  ? 6.086   -14.361 -23.618 1.00 70.45  ? 36  GLN A NE2   1 
ATOM   263  N  N     . LEU A 1 37  ? 9.465   -14.094 -17.675 1.00 48.37  ? 37  LEU A N     1 
ATOM   264  C  CA    . LEU A 1 37  ? 10.584  -13.664 -16.842 1.00 48.74  ? 37  LEU A CA    1 
ATOM   265  C  C     . LEU A 1 37  ? 10.777  -14.587 -15.644 1.00 50.54  ? 37  LEU A C     1 
ATOM   266  O  O     . LEU A 1 37  ? 11.901  -15.008 -15.350 1.00 47.58  ? 37  LEU A O     1 
ATOM   267  C  CB    . LEU A 1 37  ? 10.367  -12.224 -16.370 1.00 53.64  ? 37  LEU A CB    1 
ATOM   268  C  CG    . LEU A 1 37  ? 11.360  -11.707 -15.324 1.00 51.19  ? 37  LEU A CG    1 
ATOM   269  C  CD1   . LEU A 1 37  ? 12.727  -11.454 -15.944 1.00 49.11  ? 37  LEU A CD1   1 
ATOM   270  C  CD2   . LEU A 1 37  ? 10.834  -10.455 -14.634 1.00 55.32  ? 37  LEU A CD2   1 
ATOM   271  N  N     . CYS A 1 38  ? 9.690   -14.904 -14.938 1.00 48.10  ? 38  CYS A N     1 
ATOM   272  C  CA    . CYS A 1 38  ? 9.756   -15.706 -13.723 1.00 50.79  ? 38  CYS A CA    1 
ATOM   273  C  C     . CYS A 1 38  ? 9.765   -17.204 -13.994 1.00 50.30  ? 38  CYS A C     1 
ATOM   274  O  O     . CYS A 1 38  ? 10.248  -17.971 -13.152 1.00 50.61  ? 38  CYS A O     1 
ATOM   275  C  CB    . CYS A 1 38  ? 8.582   -15.355 -12.803 1.00 45.52  ? 38  CYS A CB    1 
ATOM   276  S  SG    . CYS A 1 38  ? 8.509   -13.611 -12.338 1.00 47.47  ? 38  CYS A SG    1 
ATOM   277  N  N     A GLN A 1 39  ? 9.246   -17.637 -15.142 0.44 48.56  ? 39  GLN A N     1 
ATOM   278  N  N     B GLN A 1 39  ? 9.236   -17.636 -15.135 0.56 49.79  ? 39  GLN A N     1 
ATOM   279  C  CA    A GLN A 1 39  ? 9.261   -19.044 -15.524 0.44 52.00  ? 39  GLN A CA    1 
ATOM   280  C  CA    B GLN A 1 39  ? 9.264   -19.041 -15.518 0.56 51.94  ? 39  GLN A CA    1 
ATOM   281  C  C     A GLN A 1 39  ? 8.522   -19.906 -14.504 0.44 50.85  ? 39  GLN A C     1 
ATOM   282  C  C     B GLN A 1 39  ? 8.522   -19.909 -14.506 0.56 50.88  ? 39  GLN A C     1 
ATOM   283  O  O     A GLN A 1 39  ? 9.120   -20.812 -13.913 0.44 50.99  ? 39  GLN A O     1 
ATOM   284  O  O     B GLN A 1 39  ? 9.115   -20.824 -13.921 0.56 50.92  ? 39  GLN A O     1 
ATOM   285  C  CB    A GLN A 1 39  ? 10.700  -19.541 -15.682 0.44 52.99  ? 39  GLN A CB    1 
ATOM   286  C  CB    B GLN A 1 39  ? 10.709  -19.519 -15.667 0.56 53.18  ? 39  GLN A CB    1 
ATOM   287  C  CG    A GLN A 1 39  ? 11.425  -18.972 -16.891 0.44 53.65  ? 39  GLN A CG    1 
ATOM   288  C  CG    B GLN A 1 39  ? 11.508  -18.741 -16.697 0.56 53.44  ? 39  GLN A CG    1 
ATOM   289  C  CD    A GLN A 1 39  ? 10.902  -19.529 -18.202 0.44 56.25  ? 39  GLN A CD    1 
ATOM   290  C  CD    B GLN A 1 39  ? 12.898  -19.306 -16.905 0.56 55.52  ? 39  GLN A CD    1 
ATOM   291  O  OE1   A GLN A 1 39  ? 10.541  -20.703 -18.293 0.44 59.67  ? 39  GLN A OE1   1 
ATOM   292  O  OE1   B GLN A 1 39  ? 13.804  -19.075 -16.103 0.56 56.03  ? 39  GLN A OE1   1 
ATOM   293  N  NE2   A GLN A 1 39  ? 10.855  -18.685 -19.226 0.44 54.24  ? 39  GLN A NE2   1 
ATOM   294  N  NE2   B GLN A 1 39  ? 13.073  -20.058 -17.985 0.56 56.74  ? 39  GLN A NE2   1 
ATOM   295  N  N     . PRO A 1 40  ? 7.236   -19.659 -14.269 1.00 49.04  ? 40  PRO A N     1 
ATOM   296  C  CA    . PRO A 1 40  ? 6.473   -20.553 -13.394 1.00 50.48  ? 40  PRO A CA    1 
ATOM   297  C  C     . PRO A 1 40  ? 6.123   -21.836 -14.126 1.00 50.90  ? 40  PRO A C     1 
ATOM   298  O  O     . PRO A 1 40  ? 6.019   -21.872 -15.354 1.00 46.61  ? 40  PRO A O     1 
ATOM   299  C  CB    . PRO A 1 40  ? 5.218   -19.737 -13.068 1.00 44.62  ? 40  PRO A CB    1 
ATOM   300  C  CG    . PRO A 1 40  ? 5.035   -18.868 -14.268 1.00 48.93  ? 40  PRO A CG    1 
ATOM   301  C  CD    . PRO A 1 40  ? 6.421   -18.538 -14.767 1.00 47.61  ? 40  PRO A CD    1 
ATOM   302  N  N     A GLU A 1 41  ? 5.952   -22.906 -13.347 0.51 47.91  ? 41  GLU A N     1 
ATOM   303  N  N     B GLU A 1 41  ? 5.944   -22.909 -13.355 0.49 47.91  ? 41  GLU A N     1 
ATOM   304  C  CA    A GLU A 1 41  ? 5.559   -24.183 -13.929 0.51 50.89  ? 41  GLU A CA    1 
ATOM   305  C  CA    B GLU A 1 41  ? 5.563   -24.172 -13.976 0.49 50.92  ? 41  GLU A CA    1 
ATOM   306  C  C     A GLU A 1 41  ? 4.103   -24.172 -14.371 0.51 50.90  ? 41  GLU A C     1 
ATOM   307  C  C     B GLU A 1 41  ? 4.093   -24.178 -14.378 0.49 50.89  ? 41  GLU A C     1 
ATOM   308  O  O     A GLU A 1 41  ? 3.748   -24.833 -15.353 0.51 52.40  ? 41  GLU A O     1 
ATOM   309  O  O     B GLU A 1 41  ? 3.719   -24.856 -15.341 0.49 52.42  ? 41  GLU A O     1 
ATOM   310  C  CB    A GLU A 1 41  ? 5.800   -25.312 -12.927 0.51 50.16  ? 41  GLU A CB    1 
ATOM   311  C  CB    B GLU A 1 41  ? 5.866   -25.342 -13.041 0.49 49.93  ? 41  GLU A CB    1 
ATOM   312  C  CG    A GLU A 1 41  ? 5.482   -26.694 -13.465 0.51 54.40  ? 41  GLU A CG    1 
ATOM   313  C  CG    B GLU A 1 41  ? 5.588   -26.700 -13.669 0.49 54.23  ? 41  GLU A CG    1 
ATOM   314  C  CD    A GLU A 1 41  ? 6.445   -27.129 -14.551 0.51 55.31  ? 41  GLU A CD    1 
ATOM   315  C  CD    B GLU A 1 41  ? 5.837   -27.854 -12.720 0.49 52.88  ? 41  GLU A CD    1 
ATOM   316  O  OE1   A GLU A 1 41  ? 7.451   -26.420 -14.770 0.51 57.35  ? 41  GLU A OE1   1 
ATOM   317  O  OE1   B GLU A 1 41  ? 6.342   -27.611 -11.604 0.49 54.23  ? 41  GLU A OE1   1 
ATOM   318  O  OE2   A GLU A 1 41  ? 6.199   -28.177 -15.183 0.51 61.89  ? 41  GLU A OE2   1 
ATOM   319  O  OE2   B GLU A 1 41  ? 5.526   -29.006 -13.091 0.49 59.23  ? 41  GLU A OE2   1 
ATOM   320  N  N     . TYR A 1 42  ? 3.251   -23.436 -13.663 1.00 45.62  ? 42  TYR A N     1 
ATOM   321  C  CA    . TYR A 1 42  ? 1.831   -23.364 -13.974 1.00 44.77  ? 42  TYR A CA    1 
ATOM   322  C  C     . TYR A 1 42  ? 1.351   -21.929 -13.810 1.00 47.48  ? 42  TYR A C     1 
ATOM   323  O  O     . TYR A 1 42  ? 1.960   -21.128 -13.098 1.00 44.35  ? 42  TYR A O     1 
ATOM   324  C  CB    . TYR A 1 42  ? 0.996   -24.295 -13.076 1.00 44.58  ? 42  TYR A CB    1 
ATOM   325  C  CG    . TYR A 1 42  ? 1.364   -25.757 -13.187 1.00 51.41  ? 42  TYR A CG    1 
ATOM   326  C  CD1   . TYR A 1 42  ? 1.144   -26.459 -14.363 1.00 49.32  ? 42  TYR A CD1   1 
ATOM   327  C  CD2   . TYR A 1 42  ? 1.912   -26.439 -12.109 1.00 50.17  ? 42  TYR A CD2   1 
ATOM   328  C  CE1   . TYR A 1 42  ? 1.476   -27.798 -14.469 1.00 58.33  ? 42  TYR A CE1   1 
ATOM   329  C  CE2   . TYR A 1 42  ? 2.247   -27.778 -12.204 1.00 48.91  ? 42  TYR A CE2   1 
ATOM   330  C  CZ    . TYR A 1 42  ? 2.026   -28.453 -13.388 1.00 53.15  ? 42  TYR A CZ    1 
ATOM   331  O  OH    . TYR A 1 42  ? 2.357   -29.786 -13.489 1.00 61.02  ? 42  TYR A OH    1 
ATOM   332  N  N     . ILE A 1 43  ? 0.246   -21.613 -14.483 1.00 43.94  ? 43  ILE A N     1 
ATOM   333  C  CA    . ILE A 1 43  ? -0.417  -20.321 -14.356 1.00 42.46  ? 43  ILE A CA    1 
ATOM   334  C  C     . ILE A 1 43  ? -1.866  -20.570 -13.962 1.00 44.16  ? 43  ILE A C     1 
ATOM   335  O  O     . ILE A 1 43  ? -2.585  -21.301 -14.652 1.00 42.60  ? 43  ILE A O     1 
ATOM   336  C  CB    . ILE A 1 43  ? -0.340  -19.497 -15.655 1.00 39.98  ? 43  ILE A CB    1 
ATOM   337  C  CG1   . ILE A 1 43  ? 1.120   -19.209 -16.011 1.00 48.27  ? 43  ILE A CG1   1 
ATOM   338  C  CG2   . ILE A 1 43  ? -1.103  -18.191 -15.501 1.00 41.13  ? 43  ILE A CG2   1 
ATOM   339  C  CD1   . ILE A 1 43  ? 1.293   -18.335 -17.235 1.00 46.14  ? 43  ILE A CD1   1 
ATOM   340  N  N     . HIS A 1 44  ? -2.289  -19.968 -12.852 1.00 37.33  ? 44  HIS A N     1 
ATOM   341  C  CA    . HIS A 1 44  ? -3.632  -20.137 -12.301 1.00 38.85  ? 44  HIS A CA    1 
ATOM   342  C  C     . HIS A 1 44  ? -4.289  -18.765 -12.239 1.00 39.29  ? 44  HIS A C     1 
ATOM   343  O  O     . HIS A 1 44  ? -3.888  -17.917 -11.437 1.00 35.80  ? 44  HIS A O     1 
ATOM   344  C  CB    . HIS A 1 44  ? -3.572  -20.791 -10.917 1.00 35.29  ? 44  HIS A CB    1 
ATOM   345  C  CG    . HIS A 1 44  ? -4.902  -20.927 -10.239 1.00 41.99  ? 44  HIS A CG    1 
ATOM   346  N  ND1   . HIS A 1 44  ? -5.427  -22.148 -9.871  1.00 41.06  ? 44  HIS A ND1   1 
ATOM   347  C  CD2   . HIS A 1 44  ? -5.801  -19.997 -9.836  1.00 40.30  ? 44  HIS A CD2   1 
ATOM   348  C  CE1   . HIS A 1 44  ? -6.595  -21.966 -9.283  1.00 44.24  ? 44  HIS A CE1   1 
ATOM   349  N  NE2   . HIS A 1 44  ? -6.847  -20.670 -9.251  1.00 40.91  ? 44  HIS A NE2   1 
ATOM   350  N  N     . ILE A 1 45  ? -5.291  -18.547 -13.086 1.00 41.83  ? 45  ILE A N     1 
ATOM   351  C  CA    . ILE A 1 45  ? -6.039  -17.295 -13.107 1.00 38.03  ? 45  ILE A CA    1 
ATOM   352  C  C     . ILE A 1 45  ? -7.191  -17.430 -12.116 1.00 39.00  ? 45  ILE A C     1 
ATOM   353  O  O     . ILE A 1 45  ? -8.167  -18.140 -12.374 1.00 40.18  ? 45  ILE A O     1 
ATOM   354  C  CB    . ILE A 1 45  ? -6.544  -16.963 -14.516 1.00 39.11  ? 45  ILE A CB    1 
ATOM   355  C  CG1   . ILE A 1 45  ? -5.388  -16.987 -15.517 1.00 39.80  ? 45  ILE A CG1   1 
ATOM   356  C  CG2   . ILE A 1 45  ? -7.218  -15.602 -14.535 1.00 38.35  ? 45  ILE A CG2   1 
ATOM   357  C  CD1   . ILE A 1 45  ? -5.805  -16.644 -16.934 1.00 44.32  ? 45  ILE A CD1   1 
ATOM   358  N  N     . CYS A 1 46  ? -7.077  -16.746 -10.979 1.00 43.17  ? 46  CYS A N     1 
ATOM   359  C  CA    . CYS A 1 46  ? -8.077  -16.857 -9.925  1.00 38.82  ? 46  CYS A CA    1 
ATOM   360  C  C     . CYS A 1 46  ? -9.425  -16.326 -10.393 1.00 38.03  ? 46  CYS A C     1 
ATOM   361  O  O     . CYS A 1 46  ? -9.510  -15.276 -11.033 1.00 41.08  ? 46  CYS A O     1 
ATOM   362  C  CB    . CYS A 1 46  ? -7.626  -16.093 -8.678  1.00 32.99  ? 46  CYS A CB    1 
ATOM   363  S  SG    . CYS A 1 46  ? -6.048  -16.636 -7.974  1.00 39.81  ? 46  CYS A SG    1 
ATOM   364  N  N     . ASP A 1 47  ? -10.486 -17.064 -10.066 1.00 40.42  ? 47  ASP A N     1 
ATOM   365  C  CA    . ASP A 1 47  ? -11.848 -16.599 -10.279 1.00 42.83  ? 47  ASP A CA    1 
ATOM   366  C  C     . ASP A 1 47  ? -12.541 -16.183 -8.990  1.00 38.48  ? 47  ASP A C     1 
ATOM   367  O  O     . ASP A 1 47  ? -13.682 -15.712 -9.044  1.00 45.52  ? 47  ASP A O     1 
ATOM   368  C  CB    . ASP A 1 47  ? -12.685 -17.679 -10.984 1.00 43.90  ? 47  ASP A CB    1 
ATOM   369  C  CG    . ASP A 1 47  ? -12.774 -18.969 -10.189 1.00 41.92  ? 47  ASP A CG    1 
ATOM   370  O  OD1   . ASP A 1 47  ? -12.449 -18.962 -8.981  1.00 44.47  ? 47  ASP A OD1   1 
ATOM   371  O  OD2   . ASP A 1 47  ? -13.168 -19.998 -10.778 1.00 48.08  ? 47  ASP A OD2   1 
ATOM   372  N  N     . GLY A 1 48  ? -11.890 -16.356 -7.840  1.00 39.19  ? 48  GLY A N     1 
ATOM   373  C  CA    . GLY A 1 48  ? -12.437 -15.924 -6.569  1.00 45.61  ? 48  GLY A CA    1 
ATOM   374  C  C     . GLY A 1 48  ? -13.591 -16.742 -6.044  1.00 44.37  ? 48  GLY A C     1 
ATOM   375  O  O     . GLY A 1 48  ? -14.228 -16.330 -5.070  1.00 41.59  ? 48  GLY A O     1 
ATOM   376  N  N     . SER A 1 49  ? -13.873 -17.894 -6.644  1.00 41.98  ? 49  SER A N     1 
ATOM   377  C  CA    . SER A 1 49  ? -15.016 -18.699 -6.250  1.00 45.68  ? 49  SER A CA    1 
ATOM   378  C  C     . SER A 1 49  ? -14.731 -19.452 -4.954  1.00 47.16  ? 49  SER A C     1 
ATOM   379  O  O     . SER A 1 49  ? -13.580 -19.629 -4.544  1.00 42.99  ? 49  SER A O     1 
ATOM   380  C  CB    . SER A 1 49  ? -15.380 -19.687 -7.361  1.00 48.87  ? 49  SER A CB    1 
ATOM   381  O  OG    . SER A 1 49  ? -14.320 -20.598 -7.605  1.00 43.50  ? 49  SER A OG    1 
ATOM   382  N  N     . GLU A 1 50  ? -15.811 -19.891 -4.303  1.00 50.58  ? 50  GLU A N     1 
ATOM   383  C  CA    . GLU A 1 50  ? -15.671 -20.737 -3.123  1.00 49.72  ? 50  GLU A CA    1 
ATOM   384  C  C     . GLU A 1 50  ? -14.974 -22.045 -3.472  1.00 53.51  ? 50  GLU A C     1 
ATOM   385  O  O     . GLU A 1 50  ? -14.129 -22.532 -2.710  1.00 48.25  ? 50  GLU A O     1 
ATOM   386  C  CB    . GLU A 1 50  ? -17.043 -21.015 -2.508  1.00 54.74  ? 50  GLU A CB    1 
ATOM   387  C  CG    . GLU A 1 50  ? -17.732 -19.791 -1.930  1.00 63.27  ? 50  GLU A CG    1 
ATOM   388  C  CD    . GLU A 1 50  ? -17.116 -19.341 -0.623  1.00 71.37  ? 50  GLU A CD    1 
ATOM   389  O  OE1   . GLU A 1 50  ? -16.170 -20.002 -0.151  1.00 70.19  ? 50  GLU A OE1   1 
ATOM   390  O  OE2   . GLU A 1 50  ? -17.580 -18.326 -0.064  1.00 71.65  ? 50  GLU A OE2   1 
ATOM   391  N  N     . GLU A 1 51  ? -15.322 -22.633 -4.619  1.00 53.14  ? 51  GLU A N     1 
ATOM   392  C  CA    . GLU A 1 51  ? -14.686 -23.872 -5.053  1.00 51.53  ? 51  GLU A CA    1 
ATOM   393  C  C     . GLU A 1 51  ? -13.172 -23.713 -5.114  1.00 51.96  ? 51  GLU A C     1 
ATOM   394  O  O     . GLU A 1 51  ? -12.425 -24.514 -4.540  1.00 52.48  ? 51  GLU A O     1 
ATOM   395  C  CB    . GLU A 1 51  ? -15.236 -24.291 -6.417  1.00 51.80  ? 51  GLU A CB    1 
ATOM   396  C  CG    . GLU A 1 51  ? -16.703 -24.701 -6.411  1.00 64.75  ? 51  GLU A CG    1 
ATOM   397  C  CD    . GLU A 1 51  ? -17.636 -23.541 -6.129  1.00 71.29  ? 51  GLU A CD    1 
ATOM   398  O  OE1   . GLU A 1 51  ? -17.210 -22.381 -6.291  1.00 60.95  ? 51  GLU A OE1   1 
ATOM   399  O  OE2   . GLU A 1 51  ? -18.796 -23.787 -5.741  1.00 75.72  ? 51  GLU A OE2   1 
ATOM   400  N  N     . GLU A 1 52  ? -12.703 -22.677 -5.813  1.00 49.40  ? 52  GLU A N     1 
ATOM   401  C  CA    . GLU A 1 52  ? -11.269 -22.428 -5.901  1.00 42.66  ? 52  GLU A CA    1 
ATOM   402  C  C     . GLU A 1 52  ? -10.665 -22.227 -4.517  1.00 46.83  ? 52  GLU A C     1 
ATOM   403  O  O     . GLU A 1 52  ? -9.607  -22.783 -4.201  1.00 45.90  ? 52  GLU A O     1 
ATOM   404  C  CB    . GLU A 1 52  ? -11.008 -21.214 -6.792  1.00 43.60  ? 52  GLU A CB    1 
ATOM   405  C  CG    . GLU A 1 52  ? -9.775  -20.404 -6.420  1.00 42.91  ? 52  GLU A CG    1 
ATOM   406  C  CD    . GLU A 1 52  ? -9.584  -19.184 -7.303  1.00 41.60  ? 52  GLU A CD    1 
ATOM   407  O  OE1   . GLU A 1 52  ? -9.249  -19.351 -8.497  1.00 37.47  ? 52  GLU A OE1   1 
ATOM   408  O  OE2   . GLU A 1 52  ? -9.777  -18.057 -6.808  1.00 41.67  ? 52  GLU A OE2   1 
ATOM   409  N  N     . TYR A 1 53  ? -11.331 -21.436 -3.673  1.00 47.01  ? 53  TYR A N     1 
ATOM   410  C  CA    . TYR A 1 53  ? -10.814 -21.181 -2.332  1.00 47.10  ? 53  TYR A CA    1 
ATOM   411  C  C     . TYR A 1 53  ? -10.681 -22.476 -1.540  1.00 48.39  ? 53  TYR A C     1 
ATOM   412  O  O     . TYR A 1 53  ? -9.680  -22.690 -0.846  1.00 47.48  ? 53  TYR A O     1 
ATOM   413  C  CB    . TYR A 1 53  ? -11.724 -20.185 -1.609  1.00 46.88  ? 53  TYR A CB    1 
ATOM   414  C  CG    . TYR A 1 53  ? -11.195 -19.686 -0.281  1.00 43.94  ? 53  TYR A CG    1 
ATOM   415  C  CD1   . TYR A 1 53  ? -9.932  -19.117 -0.181  1.00 45.83  ? 53  TYR A CD1   1 
ATOM   416  C  CD2   . TYR A 1 53  ? -11.970 -19.760 0.870   1.00 48.20  ? 53  TYR A CD2   1 
ATOM   417  C  CE1   . TYR A 1 53  ? -9.448  -18.653 1.032   1.00 50.10  ? 53  TYR A CE1   1 
ATOM   418  C  CE2   . TYR A 1 53  ? -11.495 -19.297 2.085   1.00 47.38  ? 53  TYR A CE2   1 
ATOM   419  C  CZ    . TYR A 1 53  ? -10.234 -18.744 2.160   1.00 52.78  ? 53  TYR A CZ    1 
ATOM   420  O  OH    . TYR A 1 53  ? -9.757  -18.282 3.365   1.00 56.76  ? 53  TYR A OH    1 
ATOM   421  N  N     . GLY A 1 54  ? -11.677 -23.359 -1.641  1.00 49.20  ? 54  GLY A N     1 
ATOM   422  C  CA    . GLY A 1 54  ? -11.623 -24.609 -0.900  1.00 51.56  ? 54  GLY A CA    1 
ATOM   423  C  C     . GLY A 1 54  ? -10.492 -25.514 -1.348  1.00 55.39  ? 54  GLY A C     1 
ATOM   424  O  O     . GLY A 1 54  ? -9.804  -26.115 -0.518  1.00 50.02  ? 54  GLY A O     1 
ATOM   425  N  N     . ARG A 1 55  ? -10.291 -25.637 -2.663  1.00 53.33  ? 55  ARG A N     1 
ATOM   426  C  CA    . ARG A 1 55  ? -9.182  -26.442 -3.165  1.00 50.28  ? 55  ARG A CA    1 
ATOM   427  C  C     . ARG A 1 55  ? -7.841  -25.829 -2.782  1.00 51.64  ? 55  ARG A C     1 
ATOM   428  O  O     . ARG A 1 55  ? -6.905  -26.547 -2.407  1.00 48.77  ? 55  ARG A O     1 
ATOM   429  C  CB    . ARG A 1 55  ? -9.286  -26.597 -4.683  1.00 50.24  ? 55  ARG A CB    1 
ATOM   430  C  CG    . ARG A 1 55  ? -10.463 -27.430 -5.154  1.00 63.33  ? 55  ARG A CG    1 
ATOM   431  C  CD    . ARG A 1 55  ? -10.492 -28.795 -4.482  1.00 68.26  ? 55  ARG A CD    1 
ATOM   432  N  NE    . ARG A 1 55  ? -10.989 -28.716 -3.113  1.00 72.05  ? 55  ARG A NE    1 
ATOM   433  C  CZ    . ARG A 1 55  ? -11.102 -29.752 -2.292  1.00 73.44  ? 55  ARG A CZ    1 
ATOM   434  N  NH1   . ARG A 1 55  ? -10.755 -30.972 -2.667  1.00 68.85  ? 55  ARG A NH1   1 
ATOM   435  N  NH2   . ARG A 1 55  ? -11.579 -29.558 -1.066  1.00 70.19  ? 55  ARG A NH2   1 
ATOM   436  N  N     . LEU A 1 56  ? -7.727  -24.501 -2.875  1.00 48.01  ? 56  LEU A N     1 
ATOM   437  C  CA    . LEU A 1 56  ? -6.507  -23.823 -2.452  1.00 42.67  ? 56  LEU A CA    1 
ATOM   438  C  C     . LEU A 1 56  ? -6.175  -24.157 -1.003  1.00 49.27  ? 56  LEU A C     1 
ATOM   439  O  O     . LEU A 1 56  ? -5.036  -24.515 -0.681  1.00 49.93  ? 56  LEU A O     1 
ATOM   440  C  CB    . LEU A 1 56  ? -6.665  -22.315 -2.646  1.00 45.57  ? 56  LEU A CB    1 
ATOM   441  C  CG    . LEU A 1 56  ? -5.474  -21.396 -2.347  1.00 50.31  ? 56  LEU A CG    1 
ATOM   442  C  CD1   . LEU A 1 56  ? -4.378  -21.570 -3.386  1.00 52.35  ? 56  LEU A CD1   1 
ATOM   443  C  CD2   . LEU A 1 56  ? -5.929  -19.944 -2.269  1.00 49.51  ? 56  LEU A CD2   1 
ATOM   444  N  N     . LEU A 1 57  ? -7.165  -24.047 -0.111  1.00 50.06  ? 57  LEU A N     1 
ATOM   445  C  CA    . LEU A 1 57  ? -6.940  -24.383 1.291   1.00 48.70  ? 57  LEU A CA    1 
ATOM   446  C  C     . LEU A 1 57  ? -6.540  -25.847 1.444   1.00 52.34  ? 57  LEU A C     1 
ATOM   447  O  O     . LEU A 1 57  ? -5.603  -26.174 2.180   1.00 53.45  ? 57  LEU A O     1 
ATOM   448  C  CB    . LEU A 1 57  ? -8.194  -24.077 2.111   1.00 47.47  ? 57  LEU A CB    1 
ATOM   449  C  CG    . LEU A 1 57  ? -8.549  -22.598 2.270   1.00 44.18  ? 57  LEU A CG    1 
ATOM   450  C  CD1   . LEU A 1 57  ? -9.918  -22.440 2.916   1.00 48.24  ? 57  LEU A CD1   1 
ATOM   451  C  CD2   . LEU A 1 57  ? -7.487  -21.875 3.080   1.00 39.27  ? 57  LEU A CD2   1 
ATOM   452  N  N     . ALA A 1 58  ? -7.246  -26.746 0.753   1.00 46.86  ? 58  ALA A N     1 
ATOM   453  C  CA    . ALA A 1 58  ? -6.894  -28.162 0.808   1.00 52.72  ? 58  ALA A CA    1 
ATOM   454  C  C     . ALA A 1 58  ? -5.470  -28.391 0.316   1.00 51.29  ? 58  ALA A C     1 
ATOM   455  O  O     . ALA A 1 58  ? -4.700  -29.139 0.927   1.00 56.06  ? 58  ALA A O     1 
ATOM   456  C  CB    . ALA A 1 58  ? -7.891  -28.978 -0.014  1.00 52.73  ? 58  ALA A CB    1 
ATOM   457  N  N     . HIS A 1 59  ? -5.103  -27.750 -0.794  1.00 49.04  ? 59  HIS A N     1 
ATOM   458  C  CA    . HIS A 1 59  ? -3.742  -27.872 -1.305  1.00 51.70  ? 59  HIS A CA    1 
ATOM   459  C  C     . HIS A 1 59  ? -2.721  -27.429 -0.262  1.00 54.43  ? 59  HIS A C     1 
ATOM   460  O  O     . HIS A 1 59  ? -1.735  -28.130 -0.005  1.00 55.31  ? 59  HIS A O     1 
ATOM   461  C  CB    . HIS A 1 59  ? -3.591  -27.049 -2.583  1.00 53.41  ? 59  HIS A CB    1 
ATOM   462  C  CG    . HIS A 1 59  ? -2.173  -26.899 -3.032  1.00 54.93  ? 59  HIS A CG    1 
ATOM   463  N  ND1   . HIS A 1 59  ? -1.375  -27.979 -3.343  1.00 58.38  ? 59  HIS A ND1   1 
ATOM   464  C  CD2   . HIS A 1 59  ? -1.407  -25.798 -3.214  1.00 60.37  ? 59  HIS A CD2   1 
ATOM   465  C  CE1   . HIS A 1 59  ? -0.179  -27.549 -3.704  1.00 58.83  ? 59  HIS A CE1   1 
ATOM   466  N  NE2   . HIS A 1 59  ? -0.172  -26.230 -3.632  1.00 64.16  ? 59  HIS A NE2   1 
ATOM   467  N  N     . MET A 1 60  ? -2.934  -26.257 0.342   1.00 52.09  ? 60  MET A N     1 
ATOM   468  C  CA    . MET A 1 60  ? -2.008  -25.776 1.363   1.00 51.41  ? 60  MET A CA    1 
ATOM   469  C  C     . MET A 1 60  ? -1.984  -26.708 2.567   1.00 52.06  ? 60  MET A C     1 
ATOM   470  O  O     . MET A 1 60  ? -0.932  -26.903 3.189   1.00 54.41  ? 60  MET A O     1 
ATOM   471  C  CB    . MET A 1 60  ? -2.380  -24.354 1.783   1.00 52.54  ? 60  MET A CB    1 
ATOM   472  C  CG    . MET A 1 60  ? -1.884  -23.269 0.834   1.00 48.00  ? 60  MET A CG    1 
ATOM   473  S  SD    . MET A 1 60  ? -2.233  -21.588 1.398   1.00 48.10  ? 60  MET A SD    1 
ATOM   474  C  CE    . MET A 1 60  ? -3.976  -21.442 1.013   1.00 43.59  ? 60  MET A CE    1 
ATOM   475  N  N     . GLN A 1 61  ? -3.133  -27.292 2.911   1.00 47.54  ? 61  GLN A N     1 
ATOM   476  C  CA    . GLN A 1 61  ? -3.172  -28.263 3.997   1.00 57.27  ? 61  GLN A CA    1 
ATOM   477  C  C     . GLN A 1 61  ? -2.398  -29.526 3.645   1.00 61.21  ? 61  GLN A C     1 
ATOM   478  O  O     . GLN A 1 61  ? -1.786  -30.143 4.525   1.00 54.42  ? 61  GLN A O     1 
ATOM   479  C  CB    . GLN A 1 61  ? -4.623  -28.607 4.343   1.00 55.33  ? 61  GLN A CB    1 
ATOM   480  C  CG    . GLN A 1 61  ? -4.803  -29.390 5.635   1.00 56.71  ? 61  GLN A CG    1 
ATOM   481  C  CD    . GLN A 1 61  ? -6.248  -29.774 5.881   1.00 67.53  ? 61  GLN A CD    1 
ATOM   482  O  OE1   . GLN A 1 61  ? -7.089  -29.660 4.992   1.00 66.96  ? 61  GLN A OE1   1 
ATOM   483  N  NE2   . GLN A 1 61  ? -6.544  -30.230 7.091   1.00 64.40  ? 61  GLN A NE2   1 
ATOM   484  N  N     . GLU A 1 62  ? -2.418  -29.931 2.373   1.00 62.01  ? 62  GLU A N     1 
ATOM   485  C  CA    . GLU A 1 62  ? -1.683  -31.124 1.968   1.00 59.63  ? 62  GLU A CA    1 
ATOM   486  C  C     . GLU A 1 62  ? -0.185  -30.864 1.898   1.00 60.69  ? 62  GLU A C     1 
ATOM   487  O  O     . GLU A 1 62  ? 0.614   -31.787 2.094   1.00 63.44  ? 62  GLU A O     1 
ATOM   488  C  CB    . GLU A 1 62  ? -2.198  -31.620 0.619   1.00 58.00  ? 62  GLU A CB    1 
ATOM   489  C  CG    . GLU A 1 62  ? -3.672  -31.972 0.618   1.00 57.42  ? 62  GLU A CG    1 
ATOM   490  C  CD    . GLU A 1 62  ? -4.205  -32.204 -0.776  1.00 55.17  ? 62  GLU A CD    1 
ATOM   491  O  OE1   . GLU A 1 62  ? -3.500  -31.852 -1.745  1.00 56.37  ? 62  GLU A OE1   1 
ATOM   492  O  OE2   . GLU A 1 62  ? -5.325  -32.740 -0.905  1.00 56.14  ? 62  GLU A OE2   1 
ATOM   493  N  N     . GLU A 1 63  ? 0.211   -29.625 1.612   1.00 61.82  ? 63  GLU A N     1 
ATOM   494  C  CA    . GLU A 1 63  ? 1.614   -29.237 1.555   1.00 64.04  ? 63  GLU A CA    1 
ATOM   495  C  C     . GLU A 1 63  ? 2.197   -28.924 2.928   1.00 63.19  ? 63  GLU A C     1 
ATOM   496  O  O     . GLU A 1 63  ? 3.405   -28.685 3.030   1.00 68.25  ? 63  GLU A O     1 
ATOM   497  C  CB    . GLU A 1 63  ? 1.783   -28.022 0.636   1.00 63.16  ? 63  GLU A CB    1 
ATOM   498  C  CG    . GLU A 1 63  ? 1.370   -28.251 -0.816  1.00 68.56  ? 63  GLU A CG    1 
ATOM   499  C  CD    . GLU A 1 63  ? 2.382   -29.068 -1.596  1.00 71.30  ? 63  GLU A CD    1 
ATOM   500  O  OE1   . GLU A 1 63  ? 2.757   -30.163 -1.125  1.00 74.90  ? 63  GLU A OE1   1 
ATOM   501  O  OE2   . GLU A 1 63  ? 2.811   -28.608 -2.676  1.00 77.65  ? 63  GLU A OE2   1 
ATOM   502  N  N     . GLY A 1 64  ? 1.380   -28.925 3.979   1.00 62.36  ? 64  GLY A N     1 
ATOM   503  C  CA    . GLY A 1 64  ? 1.862   -28.528 5.285   1.00 64.35  ? 64  GLY A CA    1 
ATOM   504  C  C     . GLY A 1 64  ? 2.044   -27.039 5.451   1.00 57.52  ? 64  GLY A C     1 
ATOM   505  O  O     . GLY A 1 64  ? 2.734   -26.605 6.378   1.00 62.87  ? 64  GLY A O     1 
ATOM   506  N  N     . VAL A 1 65  ? 1.442   -26.238 4.572   1.00 56.09  ? 65  VAL A N     1 
ATOM   507  C  CA    . VAL A 1 65  ? 1.581   -24.790 4.668   1.00 56.93  ? 65  VAL A CA    1 
ATOM   508  C  C     . VAL A 1 65  ? 0.652   -24.227 5.738   1.00 57.77  ? 65  VAL A C     1 
ATOM   509  O  O     . VAL A 1 65  ? 1.027   -23.311 6.479   1.00 56.43  ? 65  VAL A O     1 
ATOM   510  C  CB    . VAL A 1 65  ? 1.331   -24.143 3.294   1.00 51.97  ? 65  VAL A CB    1 
ATOM   511  C  CG1   . VAL A 1 65  ? 1.365   -22.631 3.406   1.00 50.01  ? 65  VAL A CG1   1 
ATOM   512  C  CG2   . VAL A 1 65  ? 2.367   -24.624 2.291   1.00 59.58  ? 65  VAL A CG2   1 
ATOM   513  N  N     . ILE A 1 66  ? -0.564  -24.762 5.847   1.00 53.83  ? 66  ILE A N     1 
ATOM   514  C  CA    . ILE A 1 66  ? -1.519  -24.315 6.850   1.00 48.79  ? 66  ILE A CA    1 
ATOM   515  C  C     . ILE A 1 66  ? -2.096  -25.528 7.565   1.00 55.78  ? 66  ILE A C     1 
ATOM   516  O  O     . ILE A 1 66  ? -2.081  -26.651 7.055   1.00 50.37  ? 66  ILE A O     1 
ATOM   517  C  CB    . ILE A 1 66  ? -2.655  -23.460 6.249   1.00 48.13  ? 66  ILE A CB    1 
ATOM   518  C  CG1   . ILE A 1 66  ? -3.488  -24.286 5.264   1.00 48.92  ? 66  ILE A CG1   1 
ATOM   519  C  CG2   . ILE A 1 66  ? -2.088  -22.216 5.580   1.00 56.24  ? 66  ILE A CG2   1 
ATOM   520  C  CD1   . ILE A 1 66  ? -4.737  -23.581 4.774   1.00 48.94  ? 66  ILE A CD1   1 
ATOM   521  N  N     . ARG A 1 67  ? -2.607  -25.283 8.767   1.00 50.21  ? 67  ARG A N     1 
ATOM   522  C  CA    . ARG A 1 67  ? -3.299  -26.291 9.553   1.00 47.46  ? 67  ARG A CA    1 
ATOM   523  C  C     . ARG A 1 67  ? -4.747  -25.871 9.748   1.00 47.22  ? 67  ARG A C     1 
ATOM   524  O  O     . ARG A 1 67  ? -5.060  -24.680 9.830   1.00 48.50  ? 67  ARG A O     1 
ATOM   525  C  CB    . ARG A 1 67  ? -2.638  -26.494 10.921  1.00 54.77  ? 67  ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 67  ? -1.302  -27.205 10.877  1.00 60.93  ? 67  ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 67  ? -0.763  -27.405 12.281  1.00 63.85  ? 67  ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 67  ? -1.795  -27.903 13.184  1.00 63.78  ? 67  ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 67  ? -2.175  -29.171 13.263  1.00 71.62  ? 67  ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 67  ? -1.620  -30.106 12.510  1.00 75.76  ? 67  ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 67  ? -3.140  -29.508 14.114  1.00 73.13  ? 67  ARG A NH2   1 
ATOM   532  N  N     . LYS A 1 68  ? -5.629  -26.862 9.815   1.00 46.48  ? 68  LYS A N     1 
ATOM   533  C  CA    . LYS A 1 68  ? -7.032  -26.599 10.092  1.00 50.29  ? 68  LYS A CA    1 
ATOM   534  C  C     . LYS A 1 68  ? -7.232  -26.475 11.595  1.00 52.76  ? 68  LYS A C     1 
ATOM   535  O  O     . LYS A 1 68  ? -6.784  -27.332 12.363  1.00 55.05  ? 68  LYS A O     1 
ATOM   536  C  CB    . LYS A 1 68  ? -7.913  -27.710 9.524   1.00 53.41  ? 68  LYS A CB    1 
ATOM   537  C  CG    . LYS A 1 68  ? -9.392  -27.352 9.466   1.00 52.50  ? 68  LYS A CG    1 
ATOM   538  C  CD    . LYS A 1 68  ? -10.165 -28.324 8.589   1.00 57.83  ? 68  LYS A CD    1 
ATOM   539  C  CE    . LYS A 1 68  ? -11.507 -27.744 8.166   1.00 59.45  ? 68  LYS A CE    1 
ATOM   540  N  NZ    . LYS A 1 68  ? -12.388 -27.451 9.329   1.00 66.47  ? 68  LYS A NZ    1 
ATOM   541  N  N     . LEU A 1 69  ? -7.887  -25.398 12.015  1.00 48.28  ? 69  LEU A N     1 
ATOM   542  C  CA    . LEU A 1 69  ? -8.231  -25.194 13.419  1.00 55.56  ? 69  LEU A CA    1 
ATOM   543  C  C     . LEU A 1 69  ? -9.590  -25.844 13.647  1.00 54.36  ? 69  LEU A C     1 
ATOM   544  O  O     . LEU A 1 69  ? -10.635 -25.245 13.381  1.00 55.99  ? 69  LEU A O     1 
ATOM   545  C  CB    . LEU A 1 69  ? -8.227  -23.710 13.763  1.00 46.64  ? 69  LEU A CB    1 
ATOM   546  C  CG    . LEU A 1 69  ? -6.855  -23.046 13.628  1.00 50.11  ? 69  LEU A CG    1 
ATOM   547  C  CD1   . LEU A 1 69  ? -6.984  -21.531 13.577  1.00 43.07  ? 69  LEU A CD1   1 
ATOM   548  C  CD2   . LEU A 1 69  ? -5.937  -23.471 14.765  1.00 49.28  ? 69  LEU A CD2   1 
ATOM   549  N  N     . LYS A 1 70  ? -9.570  -27.088 14.133  1.00 54.48  ? 70  LYS A N     1 
ATOM   550  C  CA    . LYS A 1 70  ? -10.781 -27.899 14.194  1.00 55.67  ? 70  LYS A CA    1 
ATOM   551  C  C     . LYS A 1 70  ? -11.843 -27.304 15.106  1.00 56.22  ? 70  LYS A C     1 
ATOM   552  O  O     . LYS A 1 70  ? -13.029 -27.610 14.939  1.00 59.55  ? 70  LYS A O     1 
ATOM   553  C  CB    . LYS A 1 70  ? -10.441 -29.312 14.662  1.00 61.25  ? 70  LYS A CB    1 
ATOM   554  C  CG    . LYS A 1 70  ? -9.470  -30.058 13.764  1.00 72.79  ? 70  LYS A CG    1 
ATOM   555  C  CD    . LYS A 1 70  ? -10.118 -30.443 12.445  1.00 75.93  ? 70  LYS A CD    1 
ATOM   556  C  CE    . LYS A 1 70  ? -9.287  -31.483 11.711  1.00 82.70  ? 70  LYS A CE    1 
ATOM   557  N  NZ    . LYS A 1 70  ? -10.029 -32.060 10.558  1.00 86.18  ? 70  LYS A NZ    1 
ATOM   558  N  N     . LYS A 1 71  ? -11.449 -26.471 16.069  1.00 54.67  ? 71  LYS A N     1 
ATOM   559  C  CA    . LYS A 1 71  ? -12.415 -25.951 17.029  1.00 52.97  ? 71  LYS A CA    1 
ATOM   560  C  C     . LYS A 1 71  ? -13.381 -24.964 16.387  1.00 58.71  ? 71  LYS A C     1 
ATOM   561  O  O     . LYS A 1 71  ? -14.501 -24.790 16.879  1.00 58.73  ? 71  LYS A O     1 
ATOM   562  C  CB    . LYS A 1 71  ? -11.682 -25.288 18.195  1.00 57.49  ? 71  LYS A CB    1 
ATOM   563  C  CG    . LYS A 1 71  ? -12.574 -24.905 19.365  1.00 57.88  ? 71  LYS A CG    1 
ATOM   564  C  CD    . LYS A 1 71  ? -11.783 -24.226 20.470  1.00 56.07  ? 71  LYS A CD    1 
ATOM   565  C  CE    . LYS A 1 71  ? -12.645 -23.964 21.695  1.00 60.90  ? 71  LYS A CE    1 
ATOM   566  N  NZ    . LYS A 1 71  ? -13.134 -25.229 22.306  1.00 74.70  ? 71  LYS A NZ    1 
ATOM   567  N  N     . TYR A 1 72  ? -12.979 -24.321 15.296  1.00 60.25  ? 72  TYR A N     1 
ATOM   568  C  CA    . TYR A 1 72  ? -13.746 -23.239 14.697  1.00 58.85  ? 72  TYR A CA    1 
ATOM   569  C  C     . TYR A 1 72  ? -14.266 -23.648 13.322  1.00 58.80  ? 72  TYR A C     1 
ATOM   570  O  O     . TYR A 1 72  ? -13.993 -24.744 12.821  1.00 59.43  ? 72  TYR A O     1 
ATOM   571  C  CB    . TYR A 1 72  ? -12.898 -21.968 14.619  1.00 51.72  ? 72  TYR A CB    1 
ATOM   572  C  CG    . TYR A 1 72  ? -12.243 -21.616 15.931  1.00 52.50  ? 72  TYR A CG    1 
ATOM   573  C  CD1   . TYR A 1 72  ? -13.007 -21.339 17.056  1.00 50.17  ? 72  TYR A CD1   1 
ATOM   574  C  CD2   . TYR A 1 72  ? -10.861 -21.568 16.049  1.00 51.03  ? 72  TYR A CD2   1 
ATOM   575  C  CE1   . TYR A 1 72  ? -12.415 -21.023 18.262  1.00 51.18  ? 72  TYR A CE1   1 
ATOM   576  C  CE2   . TYR A 1 72  ? -10.258 -21.251 17.253  1.00 54.00  ? 72  TYR A CE2   1 
ATOM   577  C  CZ    . TYR A 1 72  ? -11.040 -20.979 18.356  1.00 52.37  ? 72  TYR A CZ    1 
ATOM   578  O  OH    . TYR A 1 72  ? -10.445 -20.664 19.555  1.00 61.14  ? 72  TYR A OH    1 
ATOM   579  N  N     . ASP A 1 73  ? -15.026 -22.738 12.712  1.00 55.65  ? 73  ASP A N     1 
ATOM   580  C  CA    . ASP A 1 73  ? -15.710 -22.976 11.443  1.00 52.19  ? 73  ASP A CA    1 
ATOM   581  C  C     . ASP A 1 73  ? -14.860 -22.399 10.315  1.00 51.76  ? 73  ASP A C     1 
ATOM   582  O  O     . ASP A 1 73  ? -14.846 -21.185 10.090  1.00 52.81  ? 73  ASP A O     1 
ATOM   583  C  CB    . ASP A 1 73  ? -17.104 -22.354 11.467  1.00 58.54  ? 73  ASP A CB    1 
ATOM   584  C  CG    . ASP A 1 73  ? -17.836 -22.493 10.145  1.00 61.39  ? 73  ASP A CG    1 
ATOM   585  O  OD1   . ASP A 1 73  ? -17.291 -23.120 9.214   1.00 64.14  ? 73  ASP A OD1   1 
ATOM   586  O  OD2   . ASP A 1 73  ? -18.964 -21.968 10.040  1.00 66.50  ? 73  ASP A OD2   1 
ATOM   587  N  N     . ASN A 1 74  ? -14.152 -23.276 9.604   1.00 47.57  ? 74  ASN A N     1 
ATOM   588  C  CA    . ASN A 1 74  ? -13.363 -22.885 8.437   1.00 45.50  ? 74  ASN A CA    1 
ATOM   589  C  C     . ASN A 1 74  ? -12.300 -21.848 8.804   1.00 44.43  ? 74  ASN A C     1 
ATOM   590  O  O     . ASN A 1 74  ? -12.165 -20.805 8.162   1.00 43.07  ? 74  ASN A O     1 
ATOM   591  C  CB    . ASN A 1 74  ? -14.268 -22.368 7.317   1.00 47.40  ? 74  ASN A CB    1 
ATOM   592  C  CG    . ASN A 1 74  ? -13.508 -22.086 6.038   1.00 51.74  ? 74  ASN A CG    1 
ATOM   593  O  OD1   . ASN A 1 74  ? -12.514 -22.744 5.736   1.00 53.66  ? 74  ASN A OD1   1 
ATOM   594  N  ND2   . ASN A 1 74  ? -13.970 -21.100 5.280   1.00 53.52  ? 74  ASN A ND2   1 
ATOM   595  N  N     . CYS A 1 75  ? -11.543 -22.141 9.855   1.00 46.15  ? 75  CYS A N     1 
ATOM   596  C  CA    . CYS A 1 75  ? -10.426 -21.305 10.267  1.00 46.69  ? 75  CYS A CA    1 
ATOM   597  C  C     . CYS A 1 75  ? -9.131  -22.084 10.097  1.00 46.04  ? 75  CYS A C     1 
ATOM   598  O  O     . CYS A 1 75  ? -9.109  -23.312 10.215  1.00 43.43  ? 75  CYS A O     1 
ATOM   599  C  CB    . CYS A 1 75  ? -10.578 -20.836 11.717  1.00 43.27  ? 75  CYS A CB    1 
ATOM   600  S  SG    . CYS A 1 75  ? -11.932 -19.667 11.964  1.00 43.59  ? 75  CYS A SG    1 
ATOM   601  N  N     . TRP A 1 76  ? -8.050  -21.361 9.816   1.00 40.93  ? 76  TRP A N     1 
ATOM   602  C  CA    . TRP A 1 76  ? -6.785  -21.983 9.459   1.00 45.21  ? 76  TRP A CA    1 
ATOM   603  C  C     . TRP A 1 76  ? -5.636  -21.238 10.116  1.00 42.82  ? 76  TRP A C     1 
ATOM   604  O  O     . TRP A 1 76  ? -5.721  -20.035 10.376  1.00 43.26  ? 76  TRP A O     1 
ATOM   605  C  CB    . TRP A 1 76  ? -6.598  -22.013 7.935   1.00 41.38  ? 76  TRP A CB    1 
ATOM   606  C  CG    . TRP A 1 76  ? -7.741  -22.665 7.228   1.00 40.72  ? 76  TRP A CG    1 
ATOM   607  C  CD1   . TRP A 1 76  ? -8.925  -22.084 6.874   1.00 40.47  ? 76  TRP A CD1   1 
ATOM   608  C  CD2   . TRP A 1 76  ? -7.819  -24.028 6.798   1.00 46.96  ? 76  TRP A CD2   1 
ATOM   609  N  NE1   . TRP A 1 76  ? -9.734  -23.000 6.247   1.00 45.39  ? 76  TRP A NE1   1 
ATOM   610  C  CE2   . TRP A 1 76  ? -9.078  -24.201 6.187   1.00 43.03  ? 76  TRP A CE2   1 
ATOM   611  C  CE3   . TRP A 1 76  ? -6.947  -25.119 6.867   1.00 45.68  ? 76  TRP A CE3   1 
ATOM   612  C  CZ2   . TRP A 1 76  ? -9.487  -25.420 5.651   1.00 48.91  ? 76  TRP A CZ2   1 
ATOM   613  C  CZ3   . TRP A 1 76  ? -7.357  -26.329 6.334   1.00 49.68  ? 76  TRP A CZ3   1 
ATOM   614  C  CH2   . TRP A 1 76  ? -8.615  -26.470 5.734   1.00 53.23  ? 76  TRP A CH2   1 
ATOM   615  N  N     . LEU A 1 77  ? -4.559  -21.971 10.383  1.00 46.20  ? 77  LEU A N     1 
ATOM   616  C  CA    . LEU A 1 77  ? -3.371  -21.428 11.026  1.00 43.83  ? 77  LEU A CA    1 
ATOM   617  C  C     . LEU A 1 77  ? -2.169  -21.607 10.112  1.00 46.64  ? 77  LEU A C     1 
ATOM   618  O  O     . LEU A 1 77  ? -1.907  -22.715 9.632   1.00 51.26  ? 77  LEU A O     1 
ATOM   619  C  CB    . LEU A 1 77  ? -3.104  -22.101 12.375  1.00 46.95  ? 77  LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 77  ? -1.837  -21.627 13.093  1.00 47.65  ? 77  LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 77  ? -1.983  -20.184 13.557  1.00 49.50  ? 77  LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 77  ? -1.477  -22.537 14.258  1.00 47.16  ? 77  LEU A CD2   1 
ATOM   623  N  N     . ALA A 1 78  ? -1.448  -20.516 9.876   1.00 44.13  ? 78  ALA A N     1 
ATOM   624  C  CA    . ALA A 1 78  ? -0.184  -20.536 9.158   1.00 46.84  ? 78  ALA A CA    1 
ATOM   625  C  C     . ALA A 1 78  ? 0.938   -20.168 10.116  1.00 45.45  ? 78  ALA A C     1 
ATOM   626  O  O     . ALA A 1 78  ? 0.778   -19.284 10.962  1.00 51.44  ? 78  ALA A O     1 
ATOM   627  C  CB    . ALA A 1 78  ? -0.204  -19.566 7.972   1.00 42.91  ? 78  ALA A CB    1 
ATOM   628  N  N     . LEU A 1 79  ? 2.065   -20.863 9.996   1.00 47.56  ? 79  LEU A N     1 
ATOM   629  C  CA    . LEU A 1 79  ? 3.253   -20.577 10.790  1.00 48.66  ? 79  LEU A CA    1 
ATOM   630  C  C     . LEU A 1 79  ? 4.374   -20.204 9.835   1.00 56.30  ? 79  LEU A C     1 
ATOM   631  O  O     . LEU A 1 79  ? 4.747   -21.003 8.969   1.00 56.71  ? 79  LEU A O     1 
ATOM   632  C  CB    . LEU A 1 79  ? 3.645   -21.775 11.657  1.00 47.39  ? 79  LEU A CB    1 
ATOM   633  C  CG    . LEU A 1 79  ? 2.598   -22.220 12.682  1.00 53.01  ? 79  LEU A CG    1 
ATOM   634  C  CD1   . LEU A 1 79  ? 3.174   -23.275 13.612  1.00 54.32  ? 79  LEU A CD1   1 
ATOM   635  C  CD2   . LEU A 1 79  ? 2.064   -21.030 13.469  1.00 49.68  ? 79  LEU A CD2   1 
ATOM   636  N  N     . THR A 1 80  ? 4.899   -18.994 9.986   1.00 49.64  ? 80  THR A N     1 
ATOM   637  C  CA    . THR A 1 80  ? 5.878   -18.461 9.053   1.00 50.05  ? 80  THR A CA    1 
ATOM   638  C  C     . THR A 1 80  ? 7.300   -18.761 9.513   1.00 54.10  ? 80  THR A C     1 
ATOM   639  O  O     . THR A 1 80  ? 7.554   -19.147 10.657  1.00 55.70  ? 80  THR A O     1 
ATOM   640  C  CB    . THR A 1 80  ? 5.704   -16.950 8.893   1.00 53.31  ? 80  THR A CB    1 
ATOM   641  O  OG1   . THR A 1 80  ? 6.094   -16.294 10.107  1.00 55.09  ? 80  THR A OG1   1 
ATOM   642  C  CG2   . THR A 1 80  ? 4.257   -16.609 8.585   1.00 47.24  ? 80  THR A CG2   1 
ATOM   643  N  N     . ASP A 1 81  ? 8.234   -18.579 8.592   1.00 57.13  ? 81  ASP A N     1 
ATOM   644  C  CA    . ASP A 1 81  ? 9.638   -18.552 8.956   1.00 56.16  ? 81  ASP A CA    1 
ATOM   645  C  C     . ASP A 1 81  ? 9.859   -17.425 9.959   1.00 52.06  ? 81  ASP A C     1 
ATOM   646  O  O     . ASP A 1 81  ? 9.369   -16.309 9.744   1.00 55.22  ? 81  ASP A O     1 
ATOM   647  C  CB    . ASP A 1 81  ? 10.499  -18.347 7.710   1.00 58.27  ? 81  ASP A CB    1 
ATOM   648  C  CG    . ASP A 1 81  ? 11.980  -18.488 7.987   1.00 60.40  ? 81  ASP A CG    1 
ATOM   649  O  OD1   . ASP A 1 81  ? 12.459  -17.923 8.993   1.00 63.79  ? 81  ASP A OD1   1 
ATOM   650  O  OD2   . ASP A 1 81  ? 12.667  -19.166 7.196   1.00 61.02  ? 81  ASP A OD2   1 
ATOM   651  N  N     . PRO A 1 82  ? 10.563  -17.671 11.066  1.00 53.59  ? 82  PRO A N     1 
ATOM   652  C  CA    . PRO A 1 82  ? 10.756  -16.599 12.057  1.00 56.99  ? 82  PRO A CA    1 
ATOM   653  C  C     . PRO A 1 82  ? 11.468  -15.381 11.499  1.00 61.87  ? 82  PRO A C     1 
ATOM   654  O  O     . PRO A 1 82  ? 11.393  -14.306 12.107  1.00 57.30  ? 82  PRO A O     1 
ATOM   655  C  CB    . PRO A 1 82  ? 11.581  -17.280 13.159  1.00 57.99  ? 82  PRO A CB    1 
ATOM   656  C  CG    . PRO A 1 82  ? 12.222  -18.457 12.489  1.00 64.12  ? 82  PRO A CG    1 
ATOM   657  C  CD    . PRO A 1 82  ? 11.240  -18.919 11.457  1.00 61.52  ? 82  PRO A CD    1 
ATOM   658  N  N     . ARG A 1 83  ? 12.157  -15.512 10.364  1.00 57.91  ? 83  ARG A N     1 
ATOM   659  C  CA    . ARG A 1 83  ? 12.824  -14.375 9.742   1.00 58.36  ? 83  ARG A CA    1 
ATOM   660  C  C     . ARG A 1 83  ? 11.871  -13.500 8.940   1.00 53.57  ? 83  ARG A C     1 
ATOM   661  O  O     . ARG A 1 83  ? 12.204  -12.344 8.659   1.00 61.41  ? 83  ARG A O     1 
ATOM   662  C  CB    . ARG A 1 83  ? 13.953  -14.862 8.830   1.00 55.00  ? 83  ARG A CB    1 
ATOM   663  C  CG    . ARG A 1 83  ? 15.009  -15.689 9.535   1.00 59.18  ? 83  ARG A CG    1 
ATOM   664  C  CD    . ARG A 1 83  ? 15.995  -16.278 8.538   1.00 65.71  ? 83  ARG A CD    1 
ATOM   665  N  NE    . ARG A 1 83  ? 15.338  -17.166 7.586   1.00 68.81  ? 83  ARG A NE    1 
ATOM   666  C  CZ    . ARG A 1 83  ? 15.968  -17.852 6.642   1.00 70.17  ? 83  ARG A CZ    1 
ATOM   667  N  NH1   . ARG A 1 83  ? 17.280  -17.776 6.491   1.00 77.41  ? 83  ARG A NH1   1 
ATOM   668  N  NH2   . ARG A 1 83  ? 15.263  -18.635 5.831   1.00 64.34  ? 83  ARG A NH2   1 
ATOM   669  N  N     . ASP A 1 84  ? 10.704  -14.017 8.572   1.00 54.48  ? 84  ASP A N     1 
ATOM   670  C  CA    . ASP A 1 84  ? 9.731   -13.307 7.745   1.00 55.22  ? 84  ASP A CA    1 
ATOM   671  C  C     . ASP A 1 84  ? 8.429   -13.173 8.535   1.00 54.43  ? 84  ASP A C     1 
ATOM   672  O  O     . ASP A 1 84  ? 7.429   -13.830 8.221   1.00 55.39  ? 84  ASP A O     1 
ATOM   673  C  CB    . ASP A 1 84  ? 9.523   -14.048 6.416   1.00 51.91  ? 84  ASP A CB    1 
ATOM   674  C  CG    . ASP A 1 84  ? 8.520   -13.363 5.516   1.00 51.87  ? 84  ASP A CG    1 
ATOM   675  O  OD1   . ASP A 1 84  ? 8.331   -12.139 5.660   1.00 52.71  ? 84  ASP A OD1   1 
ATOM   676  O  OD2   . ASP A 1 84  ? 7.912   -14.052 4.670   1.00 50.89  ? 84  ASP A OD2   1 
ATOM   677  N  N     . VAL A 1 85  ? 8.438   -12.310 9.551   1.00 50.34  ? 85  VAL A N     1 
ATOM   678  C  CA    . VAL A 1 85  ? 7.341   -12.219 10.503  1.00 54.80  ? 85  VAL A CA    1 
ATOM   679  C  C     . VAL A 1 85  ? 6.747   -10.817 10.563  1.00 58.92  ? 85  VAL A C     1 
ATOM   680  O  O     . VAL A 1 85  ? 5.949   -10.522 11.460  1.00 54.01  ? 85  VAL A O     1 
ATOM   681  C  CB    . VAL A 1 85  ? 7.784   -12.668 11.910  1.00 51.68  ? 85  VAL A CB    1 
ATOM   682  C  CG1   . VAL A 1 85  ? 8.219   -14.129 11.891  1.00 57.21  ? 85  VAL A CG1   1 
ATOM   683  C  CG2   . VAL A 1 85  ? 8.900   -11.775 12.428  1.00 55.17  ? 85  VAL A CG2   1 
ATOM   684  N  N     . ALA A 1 86  ? 7.103   -9.937  9.629   1.00 57.60  ? 86  ALA A N     1 
ATOM   685  C  CA    . ALA A 1 86  ? 6.586   -8.573  9.710   1.00 54.54  ? 86  ALA A CA    1 
ATOM   686  C  C     . ALA A 1 86  ? 6.891   -7.811  8.427   1.00 60.79  ? 86  ALA A C     1 
ATOM   687  O  O     . ALA A 1 86  ? 7.711   -8.228  7.603   1.00 52.92  ? 86  ALA A O     1 
ATOM   688  C  CB    . ALA A 1 86  ? 7.165   -7.832  10.916  1.00 58.97  ? 86  ALA A CB    1 
ATOM   689  N  N     . ARG A 1 87  ? 6.204   -6.682  8.280   1.00 60.64  ? 87  ARG A N     1 
ATOM   690  C  CA    . ARG A 1 87  ? 6.483   -5.745  7.202   1.00 57.63  ? 87  ARG A CA    1 
ATOM   691  C  C     . ARG A 1 87  ? 7.804   -5.032  7.469   1.00 62.06  ? 87  ARG A C     1 
ATOM   692  O  O     . ARG A 1 87  ? 8.002   -4.452  8.541   1.00 70.90  ? 87  ARG A O     1 
ATOM   693  C  CB    . ARG A 1 87  ? 5.333   -4.742  7.085   1.00 55.55  ? 87  ARG A CB    1 
ATOM   694  C  CG    . ARG A 1 87  ? 5.588   -3.549  6.186   1.00 54.27  ? 87  ARG A CG    1 
ATOM   695  C  CD    . ARG A 1 87  ? 4.349   -2.665  6.100   1.00 49.45  ? 87  ARG A CD    1 
ATOM   696  N  NE    . ARG A 1 87  ? 3.863   -2.264  7.416   1.00 48.89  ? 87  ARG A NE    1 
ATOM   697  C  CZ    . ARG A 1 87  ? 4.419   -1.322  8.165   1.00 54.78  ? 87  ARG A CZ    1 
ATOM   698  N  NH1   . ARG A 1 87  ? 5.515   -0.691  7.778   1.00 56.86  ? 87  ARG A NH1   1 
ATOM   699  N  NH2   . ARG A 1 87  ? 3.863   -1.007  9.331   1.00 56.43  ? 87  ARG A NH2   1 
ATOM   700  N  N     . ILE A 1 88  ? 8.715   -5.086  6.501   1.00 70.69  ? 88  ILE A N     1 
ATOM   701  C  CA    . ILE A 1 88  ? 10.070  -4.567  6.660   1.00 72.61  ? 88  ILE A CA    1 
ATOM   702  C  C     . ILE A 1 88  ? 10.123  -3.172  6.048   1.00 70.88  ? 88  ILE A C     1 
ATOM   703  O  O     . ILE A 1 88  ? 10.000  -3.011  4.829   1.00 66.99  ? 88  ILE A O     1 
ATOM   704  C  CB    . ILE A 1 88  ? 11.110  -5.498  6.023   1.00 70.96  ? 88  ILE A CB    1 
ATOM   705  C  CG1   . ILE A 1 88  ? 10.959  -6.917  6.574   1.00 67.72  ? 88  ILE A CG1   1 
ATOM   706  C  CG2   . ILE A 1 88  ? 12.517  -4.982  6.290   1.00 72.75  ? 88  ILE A CG2   1 
ATOM   707  C  CD1   . ILE A 1 88  ? 11.938  -7.912  5.985   1.00 69.87  ? 88  ILE A CD1   1 
ATOM   708  N  N     . GLU A 1 89  ? 10.324  -2.160  6.894   1.00 68.24  ? 89  GLU A N     1 
ATOM   709  C  CA    . GLU A 1 89  ? 10.364  -0.784  6.412   1.00 64.75  ? 89  GLU A CA    1 
ATOM   710  C  C     . GLU A 1 89  ? 11.693  -0.440  5.753   1.00 68.97  ? 89  GLU A C     1 
ATOM   711  O  O     . GLU A 1 89  ? 11.724  0.370   4.820   1.00 63.61  ? 89  GLU A O     1 
ATOM   712  C  CB    . GLU A 1 89  ? 10.092  0.186   7.564   1.00 70.58  ? 89  GLU A CB    1 
ATOM   713  C  CG    . GLU A 1 89  ? 9.980   1.639   7.134   1.00 68.67  ? 89  GLU A CG    1 
ATOM   714  C  CD    . GLU A 1 89  ? 9.675   2.562   8.294   1.00 78.82  ? 89  GLU A CD    1 
ATOM   715  O  OE1   . GLU A 1 89  ? 9.206   2.070   9.340   1.00 78.54  ? 89  GLU A OE1   1 
ATOM   716  O  OE2   . GLU A 1 89  ? 9.908   3.781   8.164   1.00 71.49  ? 89  GLU A OE2   1 
ATOM   717  N  N     . SER A 1 90  ? 12.794  -1.031  6.222   1.00 71.24  ? 90  SER A N     1 
ATOM   718  C  CA    . SER A 1 90  ? 14.103  -0.708  5.669   1.00 68.78  ? 90  SER A CA    1 
ATOM   719  C  C     . SER A 1 90  ? 14.306  -1.293  4.278   1.00 65.25  ? 90  SER A C     1 
ATOM   720  O  O     . SER A 1 90  ? 15.208  -0.849  3.560   1.00 66.30  ? 90  SER A O     1 
ATOM   721  C  CB    . SER A 1 90  ? 15.206  -1.197  6.608   1.00 70.52  ? 90  SER A CB    1 
ATOM   722  O  OG    . SER A 1 90  ? 15.070  -2.581  6.882   1.00 74.02  ? 90  SER A OG    1 
ATOM   723  N  N     . LYS A 1 91  ? 13.498  -2.275  3.882   1.00 61.25  ? 91  LYS A N     1 
ATOM   724  C  CA    . LYS A 1 91  ? 13.570  -2.857  2.549   1.00 55.83  ? 91  LYS A CA    1 
ATOM   725  C  C     . LYS A 1 91  ? 12.485  -2.326  1.622   1.00 52.61  ? 91  LYS A C     1 
ATOM   726  O  O     . LYS A 1 91  ? 12.286  -2.877  0.535   1.00 51.10  ? 91  LYS A O     1 
ATOM   727  C  CB    . LYS A 1 91  ? 13.481  -4.382  2.632   1.00 59.58  ? 91  LYS A CB    1 
ATOM   728  C  CG    . LYS A 1 91  ? 14.472  -5.020  3.592   1.00 60.36  ? 91  LYS A CG    1 
ATOM   729  C  CD    . LYS A 1 91  ? 15.896  -4.954  3.067   1.00 64.42  ? 91  LYS A CD    1 
ATOM   730  C  CE    . LYS A 1 91  ? 16.855  -5.644  4.020   1.00 71.52  ? 91  LYS A CE    1 
ATOM   731  N  NZ    . LYS A 1 91  ? 16.411  -7.030  4.326   1.00 68.08  ? 91  LYS A NZ    1 
ATOM   732  N  N     . THR A 1 92  ? 11.783  -1.271  2.025   1.00 51.91  ? 92  THR A N     1 
ATOM   733  C  CA    . THR A 1 92  ? 10.683  -0.704  1.257   1.00 49.63  ? 92  THR A CA    1 
ATOM   734  C  C     . THR A 1 92  ? 11.160  0.584   0.603   1.00 48.95  ? 92  THR A C     1 
ATOM   735  O  O     . THR A 1 92  ? 11.609  1.506   1.294   1.00 54.17  ? 92  THR A O     1 
ATOM   736  C  CB    . THR A 1 92  ? 9.474   -0.439  2.153   1.00 52.44  ? 92  THR A CB    1 
ATOM   737  O  OG1   . THR A 1 92  ? 9.124   -1.643  2.845   1.00 53.37  ? 92  THR A OG1   1 
ATOM   738  C  CG2   . THR A 1 92  ? 8.285   0.030   1.327   1.00 45.79  ? 92  THR A CG2   1 
ATOM   739  N  N     . VAL A 1 93  ? 11.057  0.648   -0.725  1.00 48.61  ? 93  VAL A N     1 
ATOM   740  C  CA    . VAL A 1 93  ? 11.604  1.752   -1.500  1.00 45.48  ? 93  VAL A CA    1 
ATOM   741  C  C     . VAL A 1 93  ? 10.557  2.253   -2.484  1.00 45.82  ? 93  VAL A C     1 
ATOM   742  O  O     . VAL A 1 93  ? 9.623   1.540   -2.857  1.00 44.48  ? 93  VAL A O     1 
ATOM   743  C  CB    . VAL A 1 93  ? 12.888  1.349   -2.253  1.00 50.47  ? 93  VAL A CB    1 
ATOM   744  C  CG1   . VAL A 1 93  ? 13.978  0.976   -1.269  1.00 57.14  ? 93  VAL A CG1   1 
ATOM   745  C  CG2   . VAL A 1 93  ? 12.604  0.195   -3.206  1.00 44.17  ? 93  VAL A CG2   1 
ATOM   746  N  N     . ILE A 1 94  ? 10.733  3.502   -2.908  1.00 46.73  ? 94  ILE A N     1 
ATOM   747  C  CA    . ILE A 1 94  ? 9.905   4.125   -3.933  1.00 48.12  ? 94  ILE A CA    1 
ATOM   748  C  C     . ILE A 1 94  ? 10.827  4.650   -5.023  1.00 47.49  ? 94  ILE A C     1 
ATOM   749  O  O     . ILE A 1 94  ? 11.806  5.347   -4.730  1.00 49.53  ? 94  ILE A O     1 
ATOM   750  C  CB    . ILE A 1 94  ? 9.034   5.257   -3.360  1.00 45.50  ? 94  ILE A CB    1 
ATOM   751  C  CG1   . ILE A 1 94  ? 8.003   4.695   -2.381  1.00 41.19  ? 94  ILE A CG1   1 
ATOM   752  C  CG2   . ILE A 1 94  ? 8.343   6.023   -4.480  1.00 43.99  ? 94  ILE A CG2   1 
ATOM   753  C  CD1   . ILE A 1 94  ? 7.082   5.745   -1.801  1.00 48.44  ? 94  ILE A CD1   1 
ATOM   754  N  N     . ILE A 1 95  ? 10.519  4.314   -6.272  1.00 46.34  ? 95  ILE A N     1 
ATOM   755  C  CA    . ILE A 1 95  ? 11.379  4.636   -7.405  1.00 45.09  ? 95  ILE A CA    1 
ATOM   756  C  C     . ILE A 1 95  ? 10.780  5.813   -8.163  1.00 48.24  ? 95  ILE A C     1 
ATOM   757  O  O     . ILE A 1 95  ? 9.660   5.728   -8.682  1.00 45.28  ? 95  ILE A O     1 
ATOM   758  C  CB    . ILE A 1 95  ? 11.568  3.424   -8.331  1.00 49.98  ? 95  ILE A CB    1 
ATOM   759  C  CG1   . ILE A 1 95  ? 12.472  2.374   -7.675  1.00 50.75  ? 95  ILE A CG1   1 
ATOM   760  C  CG2   . ILE A 1 95  ? 12.142  3.863   -9.673  1.00 50.41  ? 95  ILE A CG2   1 
ATOM   761  C  CD1   . ILE A 1 95  ? 11.845  1.660   -6.496  1.00 47.69  ? 95  ILE A CD1   1 
ATOM   762  N  N     . THR A 1 96  ? 11.530  6.911   -8.224  1.00 47.55  ? 96  THR A N     1 
ATOM   763  C  CA    . THR A 1 96  ? 11.193  8.054   -9.058  1.00 50.02  ? 96  THR A CA    1 
ATOM   764  C  C     . THR A 1 96  ? 12.474  8.584   -9.684  1.00 57.14  ? 96  THR A C     1 
ATOM   765  O  O     . THR A 1 96  ? 13.560  8.459   -9.109  1.00 49.76  ? 96  THR A O     1 
ATOM   766  C  CB    . THR A 1 96  ? 10.502  9.172   -8.262  1.00 50.47  ? 96  THR A CB    1 
ATOM   767  O  OG1   . THR A 1 96  ? 11.329  9.551   -7.155  1.00 47.44  ? 96  THR A OG1   1 
ATOM   768  C  CG2   . THR A 1 96  ? 9.145   8.712   -7.745  1.00 50.75  ? 96  THR A CG2   1 
ATOM   769  N  N     . GLN A 1 97  ? 12.346  9.173   -10.876 1.00 56.34  ? 97  GLN A N     1 
ATOM   770  C  CA    . GLN A 1 97  ? 13.520  9.737   -11.532 1.00 60.29  ? 97  GLN A CA    1 
ATOM   771  C  C     . GLN A 1 97  ? 14.197  10.769  -10.640 1.00 55.08  ? 97  GLN A C     1 
ATOM   772  O  O     . GLN A 1 97  ? 15.430  10.839  -10.579 1.00 59.37  ? 97  GLN A O     1 
ATOM   773  C  CB    . GLN A 1 97  ? 13.135  10.358  -12.875 1.00 65.23  ? 97  GLN A CB    1 
ATOM   774  C  CG    . GLN A 1 97  ? 12.396  11.686  -12.769 1.00 72.94  ? 97  GLN A CG    1 
ATOM   775  C  CD    . GLN A 1 97  ? 10.928  11.516  -12.440 1.00 79.72  ? 97  GLN A CD    1 
ATOM   776  O  OE1   . GLN A 1 97  ? 10.532  11.555  -11.276 1.00 69.42  ? 97  GLN A OE1   1 
ATOM   777  N  NE2   . GLN A 1 97  ? 10.111  11.331  -13.468 1.00 87.35  ? 97  GLN A NE2   1 
ATOM   778  N  N     . GLU A 1 98  ? 13.406  11.565  -9.928  1.00 59.39  ? 98  GLU A N     1 
ATOM   779  C  CA    . GLU A 1 98  ? 13.909  12.589  -9.023  1.00 58.47  ? 98  GLU A CA    1 
ATOM   780  C  C     . GLU A 1 98  ? 13.616  12.181  -7.587  1.00 51.08  ? 98  GLU A C     1 
ATOM   781  O  O     . GLU A 1 98  ? 12.475  11.843  -7.254  1.00 49.36  ? 98  GLU A O     1 
ATOM   782  C  CB    . GLU A 1 98  ? 13.273  13.947  -9.330  1.00 62.23  ? 98  GLU A CB    1 
ATOM   783  C  CG    . GLU A 1 98  ? 13.547  14.462  -10.733 1.00 68.90  ? 98  GLU A CG    1 
ATOM   784  C  CD    . GLU A 1 98  ? 14.962  14.978  -10.891 1.00 72.32  ? 98  GLU A CD    1 
ATOM   785  O  OE1   . GLU A 1 98  ? 15.578  15.334  -9.867  1.00 76.87  ? 98  GLU A OE1   1 
ATOM   786  O  OE2   . GLU A 1 98  ? 15.456  15.024  -12.037 1.00 80.51  ? 98  GLU A OE2   1 
ATOM   787  N  N     . GLN A 1 99  ? 14.648  12.207  -6.741  1.00 48.86  ? 99  GLN A N     1 
ATOM   788  C  CA    . GLN A 1 99  ? 14.450  11.862  -5.338  1.00 53.74  ? 99  GLN A CA    1 
ATOM   789  C  C     . GLN A 1 99  ? 13.493  12.828  -4.654  1.00 52.62  ? 99  GLN A C     1 
ATOM   790  O  O     . GLN A 1 99  ? 12.761  12.432  -3.739  1.00 46.45  ? 99  GLN A O     1 
ATOM   791  C  CB    . GLN A 1 99  ? 15.791  11.839  -4.605  1.00 52.51  ? 99  GLN A CB    1 
ATOM   792  C  CG    . GLN A 1 99  ? 15.675  11.540  -3.115  1.00 52.61  ? 99  GLN A CG    1 
ATOM   793  C  CD    . GLN A 1 99  ? 17.001  11.661  -2.387  1.00 56.57  ? 99  GLN A CD    1 
ATOM   794  O  OE1   . GLN A 1 99  ? 17.981  12.168  -2.934  1.00 56.06  ? 99  GLN A OE1   1 
ATOM   795  N  NE2   . GLN A 1 99  ? 17.036  11.192  -1.146  1.00 56.30  ? 99  GLN A NE2   1 
ATOM   796  N  N     . ARG A 1 100 ? 13.479  14.093  -5.081  1.00 47.04  ? 100 ARG A N     1 
ATOM   797  C  CA    . ARG A 1 100 ? 12.640  15.084  -4.421  1.00 47.09  ? 100 ARG A CA    1 
ATOM   798  C  C     . ARG A 1 100 ? 11.155  14.810  -4.614  1.00 47.22  ? 100 ARG A C     1 
ATOM   799  O  O     . ARG A 1 100 ? 10.338  15.339  -3.852  1.00 46.53  ? 100 ARG A O     1 
ATOM   800  C  CB    . ARG A 1 100 ? 12.978  16.486  -4.926  1.00 48.96  ? 100 ARG A CB    1 
ATOM   801  C  CG    . ARG A 1 100 ? 12.336  17.602  -4.117  1.00 55.34  ? 100 ARG A CG    1 
ATOM   802  C  CD    . ARG A 1 100 ? 12.719  18.963  -4.666  1.00 60.60  ? 100 ARG A CD    1 
ATOM   803  N  NE    . ARG A 1 100 ? 12.311  20.046  -3.780  1.00 68.00  ? 100 ARG A NE    1 
ATOM   804  C  CZ    . ARG A 1 100 ? 12.472  21.335  -4.048  1.00 71.19  ? 100 ARG A CZ    1 
ATOM   805  N  NH1   . ARG A 1 100 ? 13.023  21.741  -5.181  1.00 72.56  ? 100 ARG A NH1   1 
ATOM   806  N  NH2   . ARG A 1 100 ? 12.070  22.238  -3.159  1.00 71.97  ? 100 ARG A NH2   1 
ATOM   807  N  N     . ASP A 1 101 ? 10.789  14.010  -5.619  1.00 46.69  ? 101 ASP A N     1 
ATOM   808  C  CA    . ASP A 1 101 ? 9.390   13.636  -5.791  1.00 50.42  ? 101 ASP A CA    1 
ATOM   809  C  C     . ASP A 1 101 ? 8.930   12.676  -4.703  1.00 47.82  ? 101 ASP A C     1 
ATOM   810  O  O     . ASP A 1 101 ? 7.750   12.680  -4.334  1.00 42.97  ? 101 ASP A O     1 
ATOM   811  C  CB    . ASP A 1 101 ? 9.173   13.005  -7.167  1.00 53.80  ? 101 ASP A CB    1 
ATOM   812  C  CG    . ASP A 1 101 ? 9.423   13.975  -8.303  1.00 60.07  ? 101 ASP A CG    1 
ATOM   813  O  OD1   . ASP A 1 101 ? 9.133   15.177  -8.135  1.00 63.73  ? 101 ASP A OD1   1 
ATOM   814  O  OD2   . ASP A 1 101 ? 9.905   13.533  -9.366  1.00 68.45  ? 101 ASP A OD2   1 
ATOM   815  N  N     . THR A 1 102 ? 9.840   11.856  -4.177  1.00 48.53  ? 102 THR A N     1 
ATOM   816  C  CA    . THR A 1 102 ? 9.507   10.849  -3.176  1.00 47.12  ? 102 THR A CA    1 
ATOM   817  C  C     . THR A 1 102 ? 9.666   11.362  -1.751  1.00 43.10  ? 102 THR A C     1 
ATOM   818  O  O     . THR A 1 102 ? 8.804   11.108  -0.901  1.00 46.57  ? 102 THR A O     1 
ATOM   819  C  CB    . THR A 1 102 ? 10.381  9.608   -3.373  1.00 48.30  ? 102 THR A CB    1 
ATOM   820  O  OG1   . THR A 1 102 ? 10.130  9.050   -4.669  1.00 50.29  ? 102 THR A OG1   1 
ATOM   821  C  CG2   . THR A 1 102 ? 10.083  8.563   -2.305  1.00 44.04  ? 102 THR A CG2   1 
ATOM   822  N  N     . VAL A 1 103 ? 10.755  12.072  -1.469  1.00 46.12  ? 103 VAL A N     1 
ATOM   823  C  CA    . VAL A 1 103 ? 11.014  12.577  -0.121  1.00 41.27  ? 103 VAL A CA    1 
ATOM   824  C  C     . VAL A 1 103 ? 11.577  13.974  -0.205  1.00 47.94  ? 103 VAL A C     1 
ATOM   825  O  O     . VAL A 1 103 ? 12.307  14.327  -1.152  1.00 55.12  ? 103 VAL A O     1 
ATOM   826  C  CB    . VAL A 1 103 ? 11.996  11.675  0.653   1.00 43.99  ? 103 VAL A CB    1 
ATOM   827  C  CG1   . VAL A 1 103 ? 11.407  10.285  0.838   1.00 43.07  ? 103 VAL A CG1   1 
ATOM   828  C  CG2   . VAL A 1 103 ? 13.336  11.613  -0.072  1.00 41.85  ? 103 VAL A CG2   1 
ATOM   829  N  N     . PRO A 1 104 ? 11.255  14.818  0.770   1.00 45.08  ? 104 PRO A N     1 
ATOM   830  C  CA    . PRO A 1 104 ? 11.933  16.110  0.876   1.00 50.17  ? 104 PRO A CA    1 
ATOM   831  C  C     . PRO A 1 104 ? 13.422  15.896  1.091   1.00 49.78  ? 104 PRO A C     1 
ATOM   832  O  O     . PRO A 1 104 ? 13.845  14.952  1.759   1.00 47.28  ? 104 PRO A O     1 
ATOM   833  C  CB    . PRO A 1 104 ? 11.274  16.765  2.096   1.00 48.09  ? 104 PRO A CB    1 
ATOM   834  C  CG    . PRO A 1 104 ? 9.995   16.005  2.310   1.00 47.65  ? 104 PRO A CG    1 
ATOM   835  C  CD    . PRO A 1 104 ? 10.269  14.613  1.847   1.00 44.39  ? 104 PRO A CD    1 
ATOM   836  N  N     . ILE A 1 105 ? 14.223  16.783  0.513   1.00 49.65  ? 105 ILE A N     1 
ATOM   837  C  CA    . ILE A 1 105 ? 15.670  16.701  0.682   1.00 54.27  ? 105 ILE A CA    1 
ATOM   838  C  C     . ILE A 1 105 ? 16.013  17.187  2.084   1.00 52.13  ? 105 ILE A C     1 
ATOM   839  O  O     . ILE A 1 105 ? 15.938  18.393  2.356   1.00 54.87  ? 105 ILE A O     1 
ATOM   840  C  CB    . ILE A 1 105 ? 16.412  17.502  -0.399  1.00 57.18  ? 105 ILE A CB    1 
ATOM   841  C  CG1   . ILE A 1 105 ? 16.034  16.982  -1.786  1.00 54.62  ? 105 ILE A CG1   1 
ATOM   842  C  CG2   . ILE A 1 105 ? 17.915  17.417  -0.188  1.00 54.21  ? 105 ILE A CG2   1 
ATOM   843  C  CD1   . ILE A 1 105 ? 16.128  15.482  -1.914  1.00 52.47  ? 105 ILE A CD1   1 
ATOM   844  N  N     . PRO A 1 106 ? 16.382  16.292  2.998   1.00 53.49  ? 106 PRO A N     1 
ATOM   845  C  CA    . PRO A 1 106 ? 16.675  16.713  4.371   1.00 53.31  ? 106 PRO A CA    1 
ATOM   846  C  C     . PRO A 1 106 ? 17.762  17.775  4.402   1.00 60.62  ? 106 PRO A C     1 
ATOM   847  O  O     . PRO A 1 106 ? 18.589  17.888  3.495   1.00 59.14  ? 106 PRO A O     1 
ATOM   848  C  CB    . PRO A 1 106 ? 17.137  15.418  5.052   1.00 55.78  ? 106 PRO A CB    1 
ATOM   849  C  CG    . PRO A 1 106 ? 16.575  14.318  4.205   1.00 52.74  ? 106 PRO A CG    1 
ATOM   850  C  CD    . PRO A 1 106 ? 16.579  14.845  2.806   1.00 51.22  ? 106 PRO A CD    1 
ATOM   851  N  N     . LYS A 1 107 ? 17.750  18.567  5.474   1.00 59.45  ? 107 LYS A N     1 
ATOM   852  C  CA    . LYS A 1 107 ? 18.734  19.635  5.603   1.00 64.89  ? 107 LYS A CA    1 
ATOM   853  C  C     . LYS A 1 107 ? 20.081  19.101  6.075   1.00 66.76  ? 107 LYS A C     1 
ATOM   854  O  O     . LYS A 1 107 ? 21.127  19.498  5.549   1.00 67.29  ? 107 LYS A O     1 
ATOM   855  C  CB    . LYS A 1 107 ? 18.218  20.712  6.560   1.00 66.72  ? 107 LYS A CB    1 
ATOM   856  C  CG    . LYS A 1 107 ? 18.999  22.013  6.505   1.00 67.15  ? 107 LYS A CG    1 
ATOM   857  C  CD    . LYS A 1 107 ? 18.367  23.075  7.389   1.00 71.93  ? 107 LYS A CD    1 
ATOM   858  C  CE    . LYS A 1 107 ? 19.023  24.430  7.186   1.00 77.94  ? 107 LYS A CE    1 
ATOM   859  N  NZ    . LYS A 1 107 ? 18.399  25.475  8.042   1.00 89.31  ? 107 LYS A NZ    1 
ATOM   860  N  N     . SER A 1 108 ? 20.078  18.198  7.056   1.00 70.22  ? 108 SER A N     1 
ATOM   861  C  CA    . SER A 1 108 ? 21.311  17.709  7.663   1.00 72.06  ? 108 SER A CA    1 
ATOM   862  C  C     . SER A 1 108 ? 21.495  16.209  7.479   1.00 71.86  ? 108 SER A C     1 
ATOM   863  O  O     . SER A 1 108 ? 22.516  15.785  6.927   1.00 76.94  ? 108 SER A O     1 
ATOM   864  C  CB    . SER A 1 108 ? 21.339  18.072  9.155   1.00 74.22  ? 108 SER A CB    1 
ATOM   865  O  OG    . SER A 1 108 ? 20.367  17.333  9.872   1.00 73.22  ? 108 SER A OG    1 
ATOM   866  N  N     . GLY A 1 109 ? 20.542  15.386  7.922   1.00 62.51  ? 109 GLY A N     1 
ATOM   867  C  CA    . GLY A 1 109 ? 20.723  13.960  7.989   1.00 58.77  ? 109 GLY A CA    1 
ATOM   868  C  C     . GLY A 1 109 ? 19.929  13.195  6.949   1.00 56.71  ? 109 GLY A C     1 
ATOM   869  O  O     . GLY A 1 109 ? 19.581  13.710  5.877   1.00 54.60  ? 109 GLY A O     1 
ATOM   870  N  N     . GLN A 1 110 ? 19.650  11.936  7.268   1.00 54.25  ? 110 GLN A N     1 
ATOM   871  C  CA    . GLN A 1 110 ? 18.937  11.016  6.397   1.00 51.47  ? 110 GLN A CA    1 
ATOM   872  C  C     . GLN A 1 110 ? 17.432  11.185  6.572   1.00 49.65  ? 110 GLN A C     1 
ATOM   873  O  O     . GLN A 1 110 ? 16.945  11.491  7.663   1.00 56.48  ? 110 GLN A O     1 
ATOM   874  C  CB    . GLN A 1 110 ? 19.356  9.577   6.715   1.00 51.24  ? 110 GLN A CB    1 
ATOM   875  C  CG    . GLN A 1 110 ? 18.907  8.519   5.726   1.00 56.38  ? 110 GLN A CG    1 
ATOM   876  C  CD    . GLN A 1 110 ? 19.507  7.157   6.040   1.00 61.72  ? 110 GLN A CD    1 
ATOM   877  O  OE1   . GLN A 1 110 ? 19.109  6.493   6.997   1.00 61.20  ? 110 GLN A OE1   1 
ATOM   878  N  NE2   . GLN A 1 110 ? 20.478  6.740   5.236   1.00 67.45  ? 110 GLN A NE2   1 
ATOM   879  N  N     . SER A 1 111 ? 16.696  10.973  5.485   1.00 47.52  ? 111 SER A N     1 
ATOM   880  C  CA    . SER A 1 111 ? 15.254  11.177  5.499   1.00 48.14  ? 111 SER A CA    1 
ATOM   881  C  C     . SER A 1 111 ? 14.545  10.007  6.179   1.00 53.43  ? 111 SER A C     1 
ATOM   882  O  O     . SER A 1 111 ? 14.825  8.840   5.886   1.00 50.48  ? 111 SER A O     1 
ATOM   883  C  CB    . SER A 1 111 ? 14.736  11.358  4.072   1.00 49.67  ? 111 SER A CB    1 
ATOM   884  O  OG    . SER A 1 111 ? 13.322  11.414  4.043   1.00 44.60  ? 111 SER A OG    1 
ATOM   885  N  N     . GLN A 1 112 ? 13.628  10.325  7.093   1.00 46.03  ? 112 GLN A N     1 
ATOM   886  C  CA    . GLN A 1 112 ? 12.761  9.334   7.715   1.00 49.04  ? 112 GLN A CA    1 
ATOM   887  C  C     . GLN A 1 112 ? 11.399  9.247   7.042   1.00 49.66  ? 112 GLN A C     1 
ATOM   888  O  O     . GLN A 1 112 ? 10.571  8.425   7.448   1.00 50.23  ? 112 GLN A O     1 
ATOM   889  C  CB    . GLN A 1 112 ? 12.557  9.652   9.202   1.00 47.74  ? 112 GLN A CB    1 
ATOM   890  C  CG    . GLN A 1 112 ? 13.810  9.949   10.009  1.00 48.53  ? 112 GLN A CG    1 
ATOM   891  C  CD    . GLN A 1 112 ? 13.489  10.142  11.484  1.00 50.66  ? 112 GLN A CD    1 
ATOM   892  O  OE1   . GLN A 1 112 ? 12.350  9.940   11.908  1.00 58.38  ? 112 GLN A OE1   1 
ATOM   893  N  NE2   . GLN A 1 112 ? 14.485  10.532  12.268  1.00 53.24  ? 112 GLN A NE2   1 
ATOM   894  N  N     . LEU A 1 113 ? 11.140  10.084  6.042   1.00 48.56  ? 113 LEU A N     1 
ATOM   895  C  CA    . LEU A 1 113 ? 9.827   10.185  5.426   1.00 43.59  ? 113 LEU A CA    1 
ATOM   896  C  C     . LEU A 1 113 ? 9.667   9.268   4.224   1.00 43.56  ? 113 LEU A C     1 
ATOM   897  O  O     . LEU A 1 113 ? 8.646   9.344   3.534   1.00 46.62  ? 113 LEU A O     1 
ATOM   898  C  CB    . LEU A 1 113 ? 9.559   11.637  5.025   1.00 50.61  ? 113 LEU A CB    1 
ATOM   899  C  CG    . LEU A 1 113 ? 9.686   12.585  6.217   1.00 48.83  ? 113 LEU A CG    1 
ATOM   900  C  CD1   . LEU A 1 113 ? 9.413   14.029  5.826   1.00 50.86  ? 113 LEU A CD1   1 
ATOM   901  C  CD2   . LEU A 1 113 ? 8.755   12.133  7.329   1.00 46.62  ? 113 LEU A CD2   1 
ATOM   902  N  N     . GLY A 1 114 ? 10.639  8.407   3.967   1.00 46.94  ? 114 GLY A N     1 
ATOM   903  C  CA    . GLY A 1 114 ? 10.593  7.520   2.822   1.00 44.12  ? 114 GLY A CA    1 
ATOM   904  C  C     . GLY A 1 114 ? 11.972  7.011   2.472   1.00 45.49  ? 114 GLY A C     1 
ATOM   905  O  O     . GLY A 1 114 ? 12.993  7.512   2.943   1.00 47.68  ? 114 GLY A O     1 
ATOM   906  N  N     . ARG A 1 115 ? 11.986  5.987   1.621   1.00 48.32  ? 115 ARG A N     1 
ATOM   907  C  CA    . ARG A 1 115 ? 13.216  5.362   1.144   1.00 44.32  ? 115 ARG A CA    1 
ATOM   908  C  C     . ARG A 1 115 ? 13.216  5.421   -0.376  1.00 45.95  ? 115 ARG A C     1 
ATOM   909  O  O     . ARG A 1 115 ? 12.480  4.673   -1.027  1.00 51.49  ? 115 ARG A O     1 
ATOM   910  C  CB    . ARG A 1 115 ? 13.326  3.918   1.636   1.00 52.72  ? 115 ARG A CB    1 
ATOM   911  C  CG    . ARG A 1 115 ? 14.477  3.130   1.024   1.00 67.20  ? 115 ARG A CG    1 
ATOM   912  C  CD    . ARG A 1 115 ? 15.746  3.226   1.859   1.00 72.83  ? 115 ARG A CD    1 
ATOM   913  N  NE    . ARG A 1 115 ? 16.485  1.968   1.852   1.00 81.10  ? 115 ARG A NE    1 
ATOM   914  C  CZ    . ARG A 1 115 ? 17.340  1.601   0.908   1.00 77.89  ? 115 ARG A CZ    1 
ATOM   915  N  NH1   . ARG A 1 115 ? 17.607  2.383   -0.125  1.00 74.36  ? 115 ARG A NH1   1 
ATOM   916  N  NH2   . ARG A 1 115 ? 17.941  0.418   1.001   1.00 80.62  ? 115 ARG A NH2   1 
ATOM   917  N  N     . TRP A 1 116 ? 14.036  6.301   -0.942  1.00 49.11  ? 116 TRP A N     1 
ATOM   918  C  CA    . TRP A 1 116 ? 14.085  6.495   -2.384  1.00 49.84  ? 116 TRP A CA    1 
ATOM   919  C  C     . TRP A 1 116 ? 15.190  5.651   -3.005  1.00 53.12  ? 116 TRP A C     1 
ATOM   920  O  O     . TRP A 1 116 ? 16.276  5.508   -2.435  1.00 55.01  ? 116 TRP A O     1 
ATOM   921  C  CB    . TRP A 1 116 ? 14.301  7.968   -2.736  1.00 55.96  ? 116 TRP A CB    1 
ATOM   922  C  CG    . TRP A 1 116 ? 14.438  8.224   -4.215  1.00 53.01  ? 116 TRP A CG    1 
ATOM   923  C  CD1   . TRP A 1 116 ? 13.430  8.291   -5.132  1.00 52.67  ? 116 TRP A CD1   1 
ATOM   924  C  CD2   . TRP A 1 116 ? 15.653  8.451   -4.941  1.00 52.49  ? 116 TRP A CD2   1 
ATOM   925  N  NE1   . TRP A 1 116 ? 13.941  8.542   -6.383  1.00 50.27  ? 116 TRP A NE1   1 
ATOM   926  C  CE2   . TRP A 1 116 ? 15.304  8.646   -6.292  1.00 49.84  ? 116 TRP A CE2   1 
ATOM   927  C  CE3   . TRP A 1 116 ? 17.002  8.507   -4.578  1.00 54.70  ? 116 TRP A CE3   1 
ATOM   928  C  CZ2   . TRP A 1 116 ? 16.255  8.895   -7.281  1.00 53.19  ? 116 TRP A CZ2   1 
ATOM   929  C  CZ3   . TRP A 1 116 ? 17.945  8.754   -5.561  1.00 52.89  ? 116 TRP A CZ3   1 
ATOM   930  C  CH2   . TRP A 1 116 ? 17.567  8.942   -6.896  1.00 52.44  ? 116 TRP A CH2   1 
ATOM   931  N  N     . MET A 1 117 ? 14.900  5.095   -4.178  1.00 53.73  ? 117 MET A N     1 
ATOM   932  C  CA    . MET A 1 117 ? 15.864  4.352   -4.974  1.00 53.61  ? 117 MET A CA    1 
ATOM   933  C  C     . MET A 1 117 ? 15.721  4.771   -6.429  1.00 49.22  ? 117 MET A C     1 
ATOM   934  O  O     . MET A 1 117 ? 14.603  4.920   -6.931  1.00 53.01  ? 117 MET A O     1 
ATOM   935  C  CB    . MET A 1 117 ? 15.659  2.834   -4.836  1.00 56.46  ? 117 MET A CB    1 
ATOM   936  C  CG    . MET A 1 117 ? 16.672  1.999   -5.604  1.00 55.56  ? 117 MET A CG    1 
ATOM   937  S  SD    . MET A 1 117 ? 16.390  0.223   -5.446  1.00 62.08  ? 117 MET A SD    1 
ATOM   938  C  CE    . MET A 1 117 ? 16.703  -0.026  -3.701  1.00 62.59  ? 117 MET A CE    1 
ATOM   939  N  N     . SER A 1 118 ? 16.852  4.976   -7.099  1.00 57.04  ? 118 SER A N     1 
ATOM   940  C  CA    . SER A 1 118 ? 16.814  5.388   -8.492  1.00 62.80  ? 118 SER A CA    1 
ATOM   941  C  C     . SER A 1 118 ? 16.363  4.229   -9.378  1.00 59.75  ? 118 SER A C     1 
ATOM   942  O  O     . SER A 1 118 ? 16.366  3.064   -8.973  1.00 57.94  ? 118 SER A O     1 
ATOM   943  C  CB    . SER A 1 118 ? 18.185  5.898   -8.942  1.00 57.97  ? 118 SER A CB    1 
ATOM   944  O  OG    . SER A 1 118 ? 19.146  4.855   -8.958  1.00 60.97  ? 118 SER A OG    1 
ATOM   945  N  N     . GLU A 1 119 ? 15.954  4.568   -10.603 1.00 56.50  ? 119 GLU A N     1 
ATOM   946  C  CA    . GLU A 1 119 ? 15.582  3.530   -11.560 1.00 68.36  ? 119 GLU A CA    1 
ATOM   947  C  C     . GLU A 1 119 ? 16.764  2.619   -11.863 1.00 63.25  ? 119 GLU A C     1 
ATOM   948  O  O     . GLU A 1 119 ? 16.621  1.391   -11.892 1.00 61.97  ? 119 GLU A O     1 
ATOM   949  C  CB    . GLU A 1 119 ? 15.047  4.157   -12.850 1.00 66.64  ? 119 GLU A CB    1 
ATOM   950  C  CG    . GLU A 1 119 ? 13.585  4.576   -12.797 1.00 68.93  ? 119 GLU A CG    1 
ATOM   951  C  CD    . GLU A 1 119 ? 13.397  6.000   -12.321 1.00 73.83  ? 119 GLU A CD    1 
ATOM   952  O  OE1   . GLU A 1 119 ? 14.409  6.694   -12.100 1.00 70.55  ? 119 GLU A OE1   1 
ATOM   953  O  OE2   . GLU A 1 119 ? 12.232  6.425   -12.175 1.00 74.90  ? 119 GLU A OE2   1 
ATOM   954  N  N     . GLU A 1 120 ? 17.942  3.204   -12.088 1.00 64.81  ? 120 GLU A N     1 
ATOM   955  C  CA    . GLU A 1 120 ? 19.116  2.404   -12.423 1.00 69.03  ? 120 GLU A CA    1 
ATOM   956  C  C     . GLU A 1 120 ? 19.412  1.384   -11.331 1.00 64.20  ? 120 GLU A C     1 
ATOM   957  O  O     . GLU A 1 120 ? 19.649  0.204   -11.614 1.00 62.26  ? 120 GLU A O     1 
ATOM   958  C  CB    . GLU A 1 120 ? 20.326  3.312   -12.658 1.00 70.31  ? 120 GLU A CB    1 
ATOM   959  C  CG    . GLU A 1 120 ? 20.179  4.272   -13.831 1.00 76.13  ? 120 GLU A CG    1 
ATOM   960  C  CD    . GLU A 1 120 ? 19.217  5.406   -13.541 1.00 80.22  ? 120 GLU A CD    1 
ATOM   961  O  OE1   . GLU A 1 120 ? 18.819  5.559   -12.366 1.00 72.80  ? 120 GLU A OE1   1 
ATOM   962  O  OE2   . GLU A 1 120 ? 18.857  6.139   -14.482 1.00 86.18  ? 120 GLU A OE2   1 
ATOM   963  N  N     . ASP A 1 121 ? 19.398  1.821   -10.070 1.00 62.68  ? 121 ASP A N     1 
ATOM   964  C  CA    . ASP A 1 121 ? 19.695  0.902   -8.976  1.00 59.93  ? 121 ASP A CA    1 
ATOM   965  C  C     . ASP A 1 121 ? 18.624  -0.175  -8.852  1.00 61.54  ? 121 ASP A C     1 
ATOM   966  O  O     . ASP A 1 121 ? 18.938  -1.338  -8.572  1.00 59.93  ? 121 ASP A O     1 
ATOM   967  C  CB    . ASP A 1 121 ? 19.840  1.672   -7.663  1.00 63.43  ? 121 ASP A CB    1 
ATOM   968  C  CG    . ASP A 1 121 ? 20.994  2.658   -7.690  1.00 68.53  ? 121 ASP A CG    1 
ATOM   969  O  OD1   . ASP A 1 121 ? 21.903  2.493   -8.531  1.00 69.55  ? 121 ASP A OD1   1 
ATOM   970  O  OD2   . ASP A 1 121 ? 20.995  3.596   -6.865  1.00 67.40  ? 121 ASP A OD2   1 
ATOM   971  N  N     . PHE A 1 122 ? 17.354  0.185   -9.057  1.00 56.56  ? 122 PHE A N     1 
ATOM   972  C  CA    . PHE A 1 122 ? 16.298  -0.816  -8.939  1.00 56.78  ? 122 PHE A CA    1 
ATOM   973  C  C     . PHE A 1 122 ? 16.395  -1.858  -10.045 1.00 56.71  ? 122 PHE A C     1 
ATOM   974  O  O     . PHE A 1 122 ? 16.163  -3.047  -9.802  1.00 56.06  ? 122 PHE A O     1 
ATOM   975  C  CB    . PHE A 1 122 ? 14.918  -0.164  -8.954  1.00 53.76  ? 122 PHE A CB    1 
ATOM   976  C  CG    . PHE A 1 122 ? 13.794  -1.161  -8.961  1.00 50.93  ? 122 PHE A CG    1 
ATOM   977  C  CD1   . PHE A 1 122 ? 13.546  -1.947  -7.848  1.00 48.42  ? 122 PHE A CD1   1 
ATOM   978  C  CD2   . PHE A 1 122 ? 13.001  -1.330  -10.084 1.00 47.46  ? 122 PHE A CD2   1 
ATOM   979  C  CE1   . PHE A 1 122 ? 12.522  -2.878  -7.848  1.00 46.37  ? 122 PHE A CE1   1 
ATOM   980  C  CE2   . PHE A 1 122 ? 11.972  -2.259  -10.091 1.00 49.94  ? 122 PHE A CE2   1 
ATOM   981  C  CZ    . PHE A 1 122 ? 11.733  -3.033  -8.972  1.00 46.60  ? 122 PHE A CZ    1 
ATOM   982  N  N     . GLU A 1 123 ? 16.727  -1.437  -11.269 1.00 57.52  ? 123 GLU A N     1 
ATOM   983  C  CA    . GLU A 1 123 ? 16.859  -2.407  -12.350 1.00 53.08  ? 123 GLU A CA    1 
ATOM   984  C  C     . GLU A 1 123 ? 17.902  -3.460  -12.006 1.00 55.61  ? 123 GLU A C     1 
ATOM   985  O  O     . GLU A 1 123 ? 17.716  -4.649  -12.290 1.00 57.12  ? 123 GLU A O     1 
ATOM   986  C  CB    . GLU A 1 123 ? 17.217  -1.709  -13.660 1.00 64.61  ? 123 GLU A CB    1 
ATOM   987  C  CG    . GLU A 1 123 ? 17.052  -2.611  -14.875 1.00 73.96  ? 123 GLU A CG    1 
ATOM   988  C  CD    . GLU A 1 123 ? 17.613  -2.010  -16.148 1.00 85.46  ? 123 GLU A CD    1 
ATOM   989  O  OE1   . GLU A 1 123 ? 18.827  -1.721  -16.192 1.00 82.61  ? 123 GLU A OE1   1 
ATOM   990  O  OE2   . GLU A 1 123 ? 16.838  -1.831  -17.108 1.00 89.86  ? 123 GLU A OE2   1 
ATOM   991  N  N     . LYS A 1 124 ? 19.008  -3.040  -11.390 1.00 54.29  ? 124 LYS A N     1 
ATOM   992  C  CA    . LYS A 1 124 ? 20.025  -3.995  -10.967 1.00 58.51  ? 124 LYS A CA    1 
ATOM   993  C  C     . LYS A 1 124 ? 19.488  -4.917  -9.880  1.00 56.47  ? 124 LYS A C     1 
ATOM   994  O  O     . LYS A 1 124 ? 19.698  -6.135  -9.928  1.00 60.47  ? 124 LYS A O     1 
ATOM   995  C  CB    . LYS A 1 124 ? 21.268  -3.248  -10.483 1.00 55.01  ? 124 LYS A CB    1 
ATOM   996  C  CG    . LYS A 1 124 ? 21.831  -2.289  -11.521 1.00 67.87  ? 124 LYS A CG    1 
ATOM   997  C  CD    . LYS A 1 124 ? 22.894  -1.371  -10.940 1.00 68.81  ? 124 LYS A CD    1 
ATOM   998  C  CE    . LYS A 1 124 ? 23.287  -0.304  -11.951 1.00 75.99  ? 124 LYS A CE    1 
ATOM   999  N  NZ    . LYS A 1 124 ? 24.278  0.661   -11.403 1.00 83.56  ? 124 LYS A NZ    1 
ATOM   1000 N  N     . ALA A 1 125 ? 18.784  -4.355  -8.895  1.00 55.54  ? 125 ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 125 ? 18.190  -5.179  -7.848  1.00 57.57  ? 125 ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 125 ? 17.112  -6.097  -8.412  1.00 54.86  ? 125 ALA A C     1 
ATOM   1003 O  O     . ALA A 1 125 ? 17.015  -7.264  -8.018  1.00 57.76  ? 125 ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 125 ? 17.619  -4.291  -6.743  1.00 49.04  ? 125 ALA A CB    1 
ATOM   1005 N  N     . PHE A 1 126 ? 16.292  -5.588  -9.332  1.00 54.31  ? 126 PHE A N     1 
ATOM   1006 C  CA    . PHE A 1 126 ? 15.228  -6.399  -9.916  1.00 53.68  ? 126 PHE A CA    1 
ATOM   1007 C  C     . PHE A 1 126 ? 15.803  -7.580  -10.690 1.00 54.94  ? 126 PHE A C     1 
ATOM   1008 O  O     . PHE A 1 126 ? 15.464  -8.740  -10.426 1.00 56.79  ? 126 PHE A O     1 
ATOM   1009 C  CB    . PHE A 1 126 ? 14.350  -5.527  -10.818 1.00 53.54  ? 126 PHE A CB    1 
ATOM   1010 C  CG    . PHE A 1 126 ? 13.295  -6.292  -11.567 1.00 50.30  ? 126 PHE A CG    1 
ATOM   1011 C  CD1   . PHE A 1 126 ? 12.060  -6.540  -10.994 1.00 44.49  ? 126 PHE A CD1   1 
ATOM   1012 C  CD2   . PHE A 1 126 ? 13.537  -6.753  -12.852 1.00 51.94  ? 126 PHE A CD2   1 
ATOM   1013 C  CE1   . PHE A 1 126 ? 11.087  -7.238  -11.683 1.00 49.16  ? 126 PHE A CE1   1 
ATOM   1014 C  CE2   . PHE A 1 126 ? 12.567  -7.452  -13.547 1.00 49.64  ? 126 PHE A CE2   1 
ATOM   1015 C  CZ    . PHE A 1 126 ? 11.341  -7.694  -12.962 1.00 44.52  ? 126 PHE A CZ    1 
ATOM   1016 N  N     . ASN A 1 127 ? 16.688  -7.301  -11.651 1.00 52.28  ? 127 ASN A N     1 
ATOM   1017 C  CA    . ASN A 1 127 ? 17.276  -8.363  -12.459 1.00 56.76  ? 127 ASN A CA    1 
ATOM   1018 C  C     . ASN A 1 127 ? 18.096  -9.339  -11.627 1.00 58.10  ? 127 ASN A C     1 
ATOM   1019 O  O     . ASN A 1 127 ? 18.405  -10.436 -12.105 1.00 54.71  ? 127 ASN A O     1 
ATOM   1020 C  CB    . ASN A 1 127 ? 18.145  -7.759  -13.563 1.00 63.42  ? 127 ASN A CB    1 
ATOM   1021 C  CG    . ASN A 1 127 ? 17.330  -7.039  -14.618 1.00 64.27  ? 127 ASN A CG    1 
ATOM   1022 O  OD1   . ASN A 1 127 ? 16.188  -7.405  -14.891 1.00 64.00  ? 127 ASN A OD1   1 
ATOM   1023 N  ND2   . ASN A 1 127 ? 17.915  -6.009  -15.218 1.00 72.26  ? 127 ASN A ND2   1 
ATOM   1024 N  N     . ALA A 1 128 ? 18.455  -8.969  -10.400 1.00 59.89  ? 128 ALA A N     1 
ATOM   1025 C  CA    . ALA A 1 128 ? 19.192  -9.844  -9.498  1.00 59.26  ? 128 ALA A CA    1 
ATOM   1026 C  C     . ALA A 1 128 ? 18.282  -10.758 -8.686  1.00 60.68  ? 128 ALA A C     1 
ATOM   1027 O  O     . ALA A 1 128 ? 18.784  -11.582 -7.913  1.00 63.87  ? 128 ALA A O     1 
ATOM   1028 C  CB    . ALA A 1 128 ? 20.062  -9.008  -8.552  1.00 56.77  ? 128 ALA A CB    1 
ATOM   1029 N  N     . ARG A 1 129 ? 16.965  -10.652 -8.860  1.00 56.14  ? 129 ARG A N     1 
ATOM   1030 C  CA    . ARG A 1 129 ? 16.003  -11.362 -8.025  1.00 52.67  ? 129 ARG A CA    1 
ATOM   1031 C  C     . ARG A 1 129 ? 15.002  -12.182 -8.822  1.00 51.78  ? 129 ARG A C     1 
ATOM   1032 O  O     . ARG A 1 129 ? 14.818  -13.375 -8.539  1.00 50.38  ? 129 ARG A O     1 
ATOM   1033 C  CB    . ARG A 1 129 ? 15.253  -10.364 -7.133  1.00 51.61  ? 129 ARG A CB    1 
ATOM   1034 C  CG    . ARG A 1 129 ? 16.101  -9.762  -6.023  1.00 48.54  ? 129 ARG A CG    1 
ATOM   1035 C  CD    . ARG A 1 129 ? 15.408  -8.589  -5.354  1.00 46.37  ? 129 ARG A CD    1 
ATOM   1036 N  NE    . ARG A 1 129 ? 16.050  -8.233  -4.094  1.00 52.81  ? 129 ARG A NE    1 
ATOM   1037 C  CZ    . ARG A 1 129 ? 17.212  -7.601  -3.995  1.00 56.15  ? 129 ARG A CZ    1 
ATOM   1038 N  NH1   . ARG A 1 129 ? 17.895  -7.239  -5.069  1.00 55.95  ? 129 ARG A NH1   1 
ATOM   1039 N  NH2   . ARG A 1 129 ? 17.707  -7.337  -2.789  1.00 56.49  ? 129 ARG A NH2   1 
ATOM   1040 N  N     . PHE A 1 130 ? 14.354  -11.587 -9.822  1.00 49.70  ? 130 PHE A N     1 
ATOM   1041 C  CA    . PHE A 1 130 ? 13.128  -12.159 -10.372 1.00 50.21  ? 130 PHE A CA    1 
ATOM   1042 C  C     . PHE A 1 130 ? 13.330  -13.182 -11.488 1.00 52.41  ? 130 PHE A C     1 
ATOM   1043 O  O     . PHE A 1 130 ? 12.528  -14.120 -11.594 1.00 51.91  ? 130 PHE A O     1 
ATOM   1044 C  CB    . PHE A 1 130 ? 12.212  -11.032 -10.855 1.00 49.31  ? 130 PHE A CB    1 
ATOM   1045 C  CG    . PHE A 1 130 ? 11.360  -10.448 -9.764  1.00 53.07  ? 130 PHE A CG    1 
ATOM   1046 C  CD1   . PHE A 1 130 ? 10.120  -10.988 -9.476  1.00 47.04  ? 130 PHE A CD1   1 
ATOM   1047 C  CD2   . PHE A 1 130 ? 11.809  -9.375  -9.013  1.00 49.27  ? 130 PHE A CD2   1 
ATOM   1048 C  CE1   . PHE A 1 130 ? 9.333   -10.463 -8.463  1.00 42.16  ? 130 PHE A CE1   1 
ATOM   1049 C  CE2   . PHE A 1 130 ? 11.028  -8.843  -8.004  1.00 48.48  ? 130 PHE A CE2   1 
ATOM   1050 C  CZ    . PHE A 1 130 ? 9.789   -9.388  -7.727  1.00 45.71  ? 130 PHE A CZ    1 
ATOM   1051 N  N     . PRO A 1 131 ? 14.356  -13.052 -12.348 1.00 55.49  ? 131 PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 131 ? 14.540  -14.054 -13.410 1.00 52.98  ? 131 PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 131 ? 14.536  -15.487 -12.891 1.00 54.86  ? 131 PRO A C     1 
ATOM   1054 O  O     . PRO A 1 131 ? 15.418  -15.885 -12.123 1.00 53.01  ? 131 PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 131 ? 15.897  -13.675 -14.015 1.00 50.10  ? 131 PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 131 ? 15.981  -12.201 -13.801 1.00 55.91  ? 131 PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 131 ? 15.329  -11.950 -12.465 1.00 50.01  ? 131 PRO A CD    1 
ATOM   1058 N  N     . GLY A 1 132 ? 13.537  -16.266 -13.308 1.00 54.89  ? 132 GLY A N     1 
ATOM   1059 C  CA    . GLY A 1 132 ? 13.418  -17.654 -12.904 1.00 50.22  ? 132 GLY A CA    1 
ATOM   1060 C  C     . GLY A 1 132 ? 12.983  -17.883 -11.475 1.00 49.15  ? 132 GLY A C     1 
ATOM   1061 O  O     . GLY A 1 132 ? 13.004  -19.029 -11.015 1.00 50.94  ? 132 GLY A O     1 
ATOM   1062 N  N     . CYS A 1 133 ? 12.569  -16.834 -10.761 1.00 47.10  ? 133 CYS A N     1 
ATOM   1063 C  CA    . CYS A 1 133 ? 12.292  -16.957 -9.334  1.00 50.78  ? 133 CYS A CA    1 
ATOM   1064 C  C     . CYS A 1 133 ? 11.103  -17.860 -9.028  1.00 45.60  ? 133 CYS A C     1 
ATOM   1065 O  O     . CYS A 1 133 ? 10.974  -18.319 -7.888  1.00 53.35  ? 133 CYS A O     1 
ATOM   1066 C  CB    . CYS A 1 133 ? 12.054  -15.575 -8.725  1.00 44.07  ? 133 CYS A CB    1 
ATOM   1067 S  SG    . CYS A 1 133 ? 10.548  -14.757 -9.300  1.00 48.89  ? 133 CYS A SG    1 
ATOM   1068 N  N     . MET A 1 134 ? 10.229  -18.119 -10.002 1.00 43.47  ? 134 MET A N     1 
ATOM   1069 C  CA    . MET A 1 134 ? 9.052   -18.950 -9.787  1.00 43.12  ? 134 MET A CA    1 
ATOM   1070 C  C     . MET A 1 134 ? 9.214   -20.356 -10.354 1.00 48.41  ? 134 MET A C     1 
ATOM   1071 O  O     . MET A 1 134 ? 8.217   -21.063 -10.531 1.00 49.84  ? 134 MET A O     1 
ATOM   1072 C  CB    . MET A 1 134 ? 7.812   -18.285 -10.385 1.00 41.15  ? 134 MET A CB    1 
ATOM   1073 C  CG    . MET A 1 134 ? 7.370   -17.017 -9.671  1.00 34.28  ? 134 MET A CG    1 
ATOM   1074 S  SD    . MET A 1 134 ? 5.800   -16.399 -10.308 1.00 42.81  ? 134 MET A SD    1 
ATOM   1075 C  CE    . MET A 1 134 ? 5.602   -14.897 -9.347  1.00 40.09  ? 134 MET A CE    1 
ATOM   1076 N  N     . LYS A 1 135 ? 10.444  -20.775 -10.640 1.00 48.66  ? 135 LYS A N     1 
ATOM   1077 C  CA    . LYS A 1 135 ? 10.671  -22.091 -11.222 1.00 49.35  ? 135 LYS A CA    1 
ATOM   1078 C  C     . LYS A 1 135 ? 9.992   -23.171 -10.389 1.00 53.12  ? 135 LYS A C     1 
ATOM   1079 O  O     . LYS A 1 135 ? 10.112  -23.193 -9.161  1.00 53.43  ? 135 LYS A O     1 
ATOM   1080 C  CB    . LYS A 1 135 ? 12.171  -22.369 -11.320 1.00 48.80  ? 135 LYS A CB    1 
ATOM   1081 C  CG    . LYS A 1 135 ? 12.566  -23.228 -12.510 1.00 56.80  ? 135 LYS A CG    1 
ATOM   1082 C  CD    . LYS A 1 135 ? 12.334  -22.482 -13.814 1.00 60.44  ? 135 LYS A CD    1 
ATOM   1083 C  CE    . LYS A 1 135 ? 12.726  -23.332 -15.014 1.00 69.30  ? 135 LYS A CE    1 
ATOM   1084 N  NZ    . LYS A 1 135 ? 12.505  -22.620 -16.305 1.00 70.66  ? 135 LYS A NZ    1 
ATOM   1085 N  N     . GLY A 1 136 ? 9.268   -24.061 -11.066 1.00 54.54  ? 136 GLY A N     1 
ATOM   1086 C  CA    . GLY A 1 136 ? 8.589   -25.159 -10.412 1.00 49.56  ? 136 GLY A CA    1 
ATOM   1087 C  C     . GLY A 1 136 ? 7.373   -24.782 -9.598  1.00 52.00  ? 136 GLY A C     1 
ATOM   1088 O  O     . GLY A 1 136 ? 6.761   -25.668 -8.988  1.00 48.05  ? 136 GLY A O     1 
ATOM   1089 N  N     . ARG A 1 137 ? 6.996   -23.509 -9.569  1.00 51.49  ? 137 ARG A N     1 
ATOM   1090 C  CA    . ARG A 1 137 ? 5.865   -23.043 -8.785  1.00 44.69  ? 137 ARG A CA    1 
ATOM   1091 C  C     . ARG A 1 137 ? 4.741   -22.567 -9.694  1.00 47.38  ? 137 ARG A C     1 
ATOM   1092 O  O     . ARG A 1 137 ? 4.928   -22.329 -10.891 1.00 44.24  ? 137 ARG A O     1 
ATOM   1093 C  CB    . ARG A 1 137 ? 6.275   -21.906 -7.843  1.00 42.24  ? 137 ARG A CB    1 
ATOM   1094 C  CG    . ARG A 1 137 ? 7.388   -22.265 -6.878  1.00 50.68  ? 137 ARG A CG    1 
ATOM   1095 C  CD    . ARG A 1 137 ? 7.548   -21.195 -5.810  1.00 48.21  ? 137 ARG A CD    1 
ATOM   1096 N  NE    . ARG A 1 137 ? 8.601   -21.532 -4.859  1.00 49.99  ? 137 ARG A NE    1 
ATOM   1097 C  CZ    . ARG A 1 137 ? 8.439   -22.339 -3.819  1.00 51.29  ? 137 ARG A CZ    1 
ATOM   1098 N  NH1   . ARG A 1 137 ? 7.276   -22.919 -3.570  1.00 50.00  ? 137 ARG A NH1   1 
ATOM   1099 N  NH2   . ARG A 1 137 ? 9.470   -22.574 -3.013  1.00 51.14  ? 137 ARG A NH2   1 
ATOM   1100 N  N     . THR A 1 138 ? 3.560   -22.430 -9.099  1.00 40.03  ? 138 THR A N     1 
ATOM   1101 C  CA    . THR A 1 138 ? 2.408   -21.872 -9.786  1.00 45.24  ? 138 THR A CA    1 
ATOM   1102 C  C     . THR A 1 138 ? 2.411   -20.357 -9.645  1.00 43.42  ? 138 THR A C     1 
ATOM   1103 O  O     . THR A 1 138 ? 2.667   -19.822 -8.563  1.00 40.59  ? 138 THR A O     1 
ATOM   1104 C  CB    . THR A 1 138 ? 1.102   -22.436 -9.220  1.00 44.74  ? 138 THR A CB    1 
ATOM   1105 O  OG1   . THR A 1 138 ? 1.031   -23.843 -9.470  1.00 43.22  ? 138 THR A OG1   1 
ATOM   1106 C  CG2   . THR A 1 138 ? -0.092  -21.757 -9.864  1.00 41.50  ? 138 THR A CG2   1 
ATOM   1107 N  N     . MET A 1 139 ? 2.134   -19.670 -10.749 1.00 43.68  ? 139 MET A N     1 
ATOM   1108 C  CA    . MET A 1 139 ? 1.915   -18.229 -10.738 1.00 42.11  ? 139 MET A CA    1 
ATOM   1109 C  C     . MET A 1 139 ? 0.413   -17.985 -10.680 1.00 39.28  ? 139 MET A C     1 
ATOM   1110 O  O     . MET A 1 139 ? -0.310  -18.279 -11.639 1.00 40.73  ? 139 MET A O     1 
ATOM   1111 C  CB    . MET A 1 139 ? 2.520   -17.549 -11.964 1.00 43.34  ? 139 MET A CB    1 
ATOM   1112 C  CG    . MET A 1 139 ? 2.121   -16.079 -12.063 1.00 39.70  ? 139 MET A CG    1 
ATOM   1113 S  SD    . MET A 1 139 ? 2.623   -15.255 -13.590 1.00 44.98  ? 139 MET A SD    1 
ATOM   1114 C  CE    . MET A 1 139 ? 4.375   -15.036 -13.301 1.00 45.26  ? 139 MET A CE    1 
ATOM   1115 N  N     . TYR A 1 140 ? -0.057  -17.453 -9.558  1.00 39.20  ? 140 TYR A N     1 
ATOM   1116 C  CA    . TYR A 1 140 ? -1.461  -17.111 -9.409  1.00 35.98  ? 140 TYR A CA    1 
ATOM   1117 C  C     . TYR A 1 140 ? -1.692  -15.690 -9.903  1.00 40.20  ? 140 TYR A C     1 
ATOM   1118 O  O     . TYR A 1 140 ? -0.886  -14.791 -9.646  1.00 35.49  ? 140 TYR A O     1 
ATOM   1119 C  CB    . TYR A 1 140 ? -1.904  -17.242 -7.951  1.00 39.05  ? 140 TYR A CB    1 
ATOM   1120 C  CG    . TYR A 1 140 ? -1.747  -18.638 -7.387  1.00 35.42  ? 140 TYR A CG    1 
ATOM   1121 C  CD1   . TYR A 1 140 ? -2.757  -19.583 -7.525  1.00 39.40  ? 140 TYR A CD1   1 
ATOM   1122 C  CD2   . TYR A 1 140 ? -0.588  -19.013 -6.720  1.00 34.15  ? 140 TYR A CD2   1 
ATOM   1123 C  CE1   . TYR A 1 140 ? -2.616  -20.865 -7.007  1.00 43.91  ? 140 TYR A CE1   1 
ATOM   1124 C  CE2   . TYR A 1 140 ? -0.437  -20.290 -6.203  1.00 37.77  ? 140 TYR A CE2   1 
ATOM   1125 C  CZ    . TYR A 1 140 ? -1.453  -21.211 -6.349  1.00 41.22  ? 140 TYR A CZ    1 
ATOM   1126 O  OH    . TYR A 1 140 ? -1.309  -22.481 -5.833  1.00 47.28  ? 140 TYR A OH    1 
ATOM   1127 N  N     . VAL A 1 141 ? -2.790  -15.495 -10.623 1.00 40.11  ? 141 VAL A N     1 
ATOM   1128 C  CA    . VAL A 1 141 ? -3.165  -14.191 -11.158 1.00 38.55  ? 141 VAL A CA    1 
ATOM   1129 C  C     . VAL A 1 141 ? -4.389  -13.717 -10.386 1.00 41.18  ? 141 VAL A C     1 
ATOM   1130 O  O     . VAL A 1 141 ? -5.503  -14.217 -10.593 1.00 40.10  ? 141 VAL A O     1 
ATOM   1131 C  CB    . VAL A 1 141 ? -3.437  -14.249 -12.666 1.00 36.85  ? 141 VAL A CB    1 
ATOM   1132 C  CG1   . VAL A 1 141 ? -3.839  -12.880 -13.187 1.00 37.53  ? 141 VAL A CG1   1 
ATOM   1133 C  CG2   . VAL A 1 141 ? -2.206  -14.757 -13.399 1.00 33.20  ? 141 VAL A CG2   1 
ATOM   1134 N  N     . ILE A 1 142 ? -4.185  -12.748 -9.499  1.00 37.65  ? 142 ILE A N     1 
ATOM   1135 C  CA    . ILE A 1 142 ? -5.249  -12.253 -8.630  1.00 33.52  ? 142 ILE A CA    1 
ATOM   1136 C  C     . ILE A 1 142 ? -5.814  -10.954 -9.192  1.00 39.23  ? 142 ILE A C     1 
ATOM   1137 O  O     . ILE A 1 142 ? -5.170  -9.900  -9.083  1.00 35.02  ? 142 ILE A O     1 
ATOM   1138 C  CB    . ILE A 1 142 ? -4.740  -12.040 -7.195  1.00 36.15  ? 142 ILE A CB    1 
ATOM   1139 C  CG1   . ILE A 1 142 ? -3.954  -13.263 -6.707  1.00 35.43  ? 142 ILE A CG1   1 
ATOM   1140 C  CG2   . ILE A 1 142 ? -5.900  -11.741 -6.261  1.00 36.05  ? 142 ILE A CG2   1 
ATOM   1141 C  CD1   . ILE A 1 142 ? -3.255  -13.044 -5.380  1.00 33.03  ? 142 ILE A CD1   1 
ATOM   1142 N  N     . PRO A 1 143 ? -6.999  -10.973 -9.797  1.00 34.31  ? 143 PRO A N     1 
ATOM   1143 C  CA    . PRO A 1 143 ? -7.665  -9.713  -10.141 1.00 38.73  ? 143 PRO A CA    1 
ATOM   1144 C  C     . PRO A 1 143 ? -8.472  -9.213  -8.958  1.00 42.01  ? 143 PRO A C     1 
ATOM   1145 O  O     . PRO A 1 143 ? -9.402  -9.895  -8.519  1.00 43.40  ? 143 PRO A O     1 
ATOM   1146 C  CB    . PRO A 1 143 ? -8.567  -10.095 -11.321 1.00 41.76  ? 143 PRO A CB    1 
ATOM   1147 C  CG    . PRO A 1 143 ? -8.599  -11.623 -11.345 1.00 41.71  ? 143 PRO A CG    1 
ATOM   1148 C  CD    . PRO A 1 143 ? -7.826  -12.133 -10.159 1.00 36.45  ? 143 PRO A CD    1 
ATOM   1149 N  N     . PHE A 1 144 ? -8.132  -8.045  -8.421  1.00 39.70  ? 144 PHE A N     1 
ATOM   1150 C  CA    . PHE A 1 144 ? -8.789  -7.568  -7.215  1.00 41.76  ? 144 PHE A CA    1 
ATOM   1151 C  C     . PHE A 1 144 ? -9.156  -6.098  -7.354  1.00 43.69  ? 144 PHE A C     1 
ATOM   1152 O  O     . PHE A 1 144 ? -8.522  -5.344  -8.097  1.00 41.31  ? 144 PHE A O     1 
ATOM   1153 C  CB    . PHE A 1 144 ? -7.909  -7.787  -5.975  1.00 37.81  ? 144 PHE A CB    1 
ATOM   1154 C  CG    . PHE A 1 144 ? -6.635  -6.995  -5.981  1.00 41.19  ? 144 PHE A CG    1 
ATOM   1155 C  CD1   . PHE A 1 144 ? -5.507  -7.466  -6.635  1.00 43.77  ? 144 PHE A CD1   1 
ATOM   1156 C  CD2   . PHE A 1 144 ? -6.556  -5.788  -5.307  1.00 42.21  ? 144 PHE A CD2   1 
ATOM   1157 C  CE1   . PHE A 1 144 ? -4.330  -6.741  -6.629  1.00 39.56  ? 144 PHE A CE1   1 
ATOM   1158 C  CE2   . PHE A 1 144 ? -5.383  -5.058  -5.297  1.00 42.79  ? 144 PHE A CE2   1 
ATOM   1159 C  CZ    . PHE A 1 144 ? -4.269  -5.534  -5.957  1.00 36.59  ? 144 PHE A CZ    1 
ATOM   1160 N  N     . SER A 1 145 ? -10.198 -5.710  -6.629  1.00 41.43  ? 145 SER A N     1 
ATOM   1161 C  CA    . SER A 1 145 ? -10.688 -4.341  -6.594  1.00 47.13  ? 145 SER A CA    1 
ATOM   1162 C  C     . SER A 1 145 ? -10.490 -3.782  -5.194  1.00 45.21  ? 145 SER A C     1 
ATOM   1163 O  O     . SER A 1 145 ? -10.834 -4.437  -4.204  1.00 42.38  ? 145 SER A O     1 
ATOM   1164 C  CB    . SER A 1 145 ? -12.166 -4.273  -6.983  1.00 47.32  ? 145 SER A CB    1 
ATOM   1165 O  OG    . SER A 1 145 ? -12.663 -2.953  -6.864  1.00 51.48  ? 145 SER A OG    1 
ATOM   1166 N  N     . MET A 1 146 ? -9.919  -2.587  -5.113  1.00 49.44  ? 146 MET A N     1 
ATOM   1167 C  CA    . MET A 1 146 ? -9.829  -1.858  -3.856  1.00 45.95  ? 146 MET A CA    1 
ATOM   1168 C  C     . MET A 1 146 ? -11.025 -0.921  -3.771  1.00 46.85  ? 146 MET A C     1 
ATOM   1169 O  O     . MET A 1 146 ? -11.151 0.006   -4.577  1.00 50.85  ? 146 MET A O     1 
ATOM   1170 C  CB    . MET A 1 146 ? -8.513  -1.089  -3.758  1.00 46.23  ? 146 MET A CB    1 
ATOM   1171 C  CG    . MET A 1 146 ? -7.279  -1.968  -3.815  1.00 45.47  ? 146 MET A CG    1 
ATOM   1172 S  SD    . MET A 1 146 ? -7.262  -3.253  -2.550  1.00 44.80  ? 146 MET A SD    1 
ATOM   1173 C  CE    . MET A 1 146 ? -7.012  -2.284  -1.065  1.00 46.23  ? 146 MET A CE    1 
ATOM   1174 N  N     . GLY A 1 147 ? -11.906 -1.176  -2.810  1.00 53.17  ? 147 GLY A N     1 
ATOM   1175 C  CA    . GLY A 1 147 ? -13.161 -0.471  -2.719  1.00 51.23  ? 147 GLY A CA    1 
ATOM   1176 C  C     . GLY A 1 147 ? -14.267 -1.224  -3.430  1.00 63.62  ? 147 GLY A C     1 
ATOM   1177 O  O     . GLY A 1 147 ? -14.014 -2.095  -4.268  1.00 58.45  ? 147 GLY A O     1 
ATOM   1178 N  N     . PRO A 1 148 ? -15.519 -0.906  -3.107  1.00 72.77  ? 148 PRO A N     1 
ATOM   1179 C  CA    . PRO A 1 148 ? -16.640 -1.618  -3.734  1.00 77.30  ? 148 PRO A CA    1 
ATOM   1180 C  C     . PRO A 1 148 ? -16.586 -1.514  -5.251  1.00 81.66  ? 148 PRO A C     1 
ATOM   1181 O  O     . PRO A 1 148 ? -16.223 -0.477  -5.810  1.00 84.82  ? 148 PRO A O     1 
ATOM   1182 C  CB    . PRO A 1 148 ? -17.873 -0.907  -3.165  1.00 75.30  ? 148 PRO A CB    1 
ATOM   1183 C  CG    . PRO A 1 148 ? -17.401 -0.301  -1.882  1.00 72.89  ? 148 PRO A CG    1 
ATOM   1184 C  CD    . PRO A 1 148 ? -15.974 0.092   -2.124  1.00 69.80  ? 148 PRO A CD    1 
ATOM   1185 N  N     . LEU A 1 149 ? -16.949 -2.609  -5.918  1.00 73.01  ? 149 LEU A N     1 
ATOM   1186 C  CA    . LEU A 1 149 ? -16.999 -2.610  -7.373  1.00 71.53  ? 149 LEU A CA    1 
ATOM   1187 C  C     . LEU A 1 149 ? -17.874 -1.468  -7.873  1.00 85.91  ? 149 LEU A C     1 
ATOM   1188 O  O     . LEU A 1 149 ? -18.929 -1.175  -7.303  1.00 87.40  ? 149 LEU A O     1 
ATOM   1189 C  CB    . LEU A 1 149 ? -17.532 -3.949  -7.890  1.00 74.61  ? 149 LEU A CB    1 
ATOM   1190 C  CG    . LEU A 1 149 ? -16.597 -5.158  -7.808  1.00 72.18  ? 149 LEU A CG    1 
ATOM   1191 C  CD1   . LEU A 1 149 ? -17.267 -6.395  -8.389  1.00 61.39  ? 149 LEU A CD1   1 
ATOM   1192 C  CD2   . LEU A 1 149 ? -15.282 -4.869  -8.521  1.00 68.62  ? 149 LEU A CD2   1 
ATOM   1193 N  N     . GLY A 1 150 ? -17.425 -0.818  -8.943  1.00 86.76  ? 150 GLY A N     1 
ATOM   1194 C  CA    . GLY A 1 150 ? -18.140 0.311   -9.497  1.00 83.29  ? 150 GLY A CA    1 
ATOM   1195 C  C     . GLY A 1 150 ? -18.104 1.573   -8.666  1.00 88.86  ? 150 GLY A C     1 
ATOM   1196 O  O     . GLY A 1 150 ? -18.690 2.581   -9.079  1.00 92.55  ? 150 GLY A O     1 
ATOM   1197 N  N     . SER A 1 151 ? -17.444 1.556   -7.513  1.00 89.47  ? 151 SER A N     1 
ATOM   1198 C  CA    . SER A 1 151 ? -17.342 2.759   -6.704  1.00 89.33  ? 151 SER A CA    1 
ATOM   1199 C  C     . SER A 1 151 ? -16.477 3.796   -7.418  1.00 97.03  ? 151 SER A C     1 
ATOM   1200 O  O     . SER A 1 151 ? -15.453 3.448   -8.016  1.00 94.17  ? 151 SER A O     1 
ATOM   1201 C  CB    . SER A 1 151 ? -16.746 2.440   -5.333  1.00 87.19  ? 151 SER A CB    1 
ATOM   1202 O  OG    . SER A 1 151 ? -16.580 3.619   -4.564  1.00 86.76  ? 151 SER A OG    1 
ATOM   1203 N  N     . PRO A 1 152 ? -16.855 5.075   -7.371  1.00 91.10  ? 152 PRO A N     1 
ATOM   1204 C  CA    . PRO A 1 152 ? -16.052 6.096   -8.062  1.00 91.98  ? 152 PRO A CA    1 
ATOM   1205 C  C     . PRO A 1 152 ? -14.621 6.174   -7.563  1.00 84.04  ? 152 PRO A C     1 
ATOM   1206 O  O     . PRO A 1 152 ? -13.720 6.514   -8.341  1.00 92.69  ? 152 PRO A O     1 
ATOM   1207 C  CB    . PRO A 1 152 ? -16.823 7.395   -7.787  1.00 90.92  ? 152 PRO A CB    1 
ATOM   1208 C  CG    . PRO A 1 152 ? -17.641 7.108   -6.567  1.00 90.07  ? 152 PRO A CG    1 
ATOM   1209 C  CD    . PRO A 1 152 ? -18.000 5.656   -6.651  1.00 89.21  ? 152 PRO A CD    1 
ATOM   1210 N  N     . LEU A 1 153 ? -14.383 5.869   -6.290  1.00 76.45  ? 153 LEU A N     1 
ATOM   1211 C  CA    . LEU A 1 153 ? -13.046 5.864   -5.713  1.00 72.77  ? 153 LEU A CA    1 
ATOM   1212 C  C     . LEU A 1 153 ? -12.406 4.484   -5.724  1.00 67.56  ? 153 LEU A C     1 
ATOM   1213 O  O     . LEU A 1 153 ? -11.349 4.300   -5.114  1.00 64.75  ? 153 LEU A O     1 
ATOM   1214 C  CB    . LEU A 1 153 ? -13.088 6.400   -4.282  1.00 71.56  ? 153 LEU A CB    1 
ATOM   1215 C  CG    . LEU A 1 153 ? -13.240 7.911   -4.133  1.00 71.42  ? 153 LEU A CG    1 
ATOM   1216 C  CD1   . LEU A 1 153 ? -13.586 8.270   -2.699  1.00 60.98  ? 153 LEU A CD1   1 
ATOM   1217 C  CD2   . LEU A 1 153 ? -11.963 8.609   -4.572  1.00 56.32  ? 153 LEU A CD2   1 
ATOM   1218 N  N     . ALA A 1 154 ? -13.021 3.514   -6.392  1.00 62.73  ? 154 ALA A N     1 
ATOM   1219 C  CA    . ALA A 1 154 ? -12.475 2.168   -6.450  1.00 70.31  ? 154 ALA A CA    1 
ATOM   1220 C  C     . ALA A 1 154 ? -11.429 2.065   -7.551  1.00 59.92  ? 154 ALA A C     1 
ATOM   1221 O  O     . ALA A 1 154 ? -11.572 2.664   -8.621  1.00 67.28  ? 154 ALA A O     1 
ATOM   1222 C  CB    . ALA A 1 154 ? -13.591 1.150   -6.688  1.00 66.81  ? 154 ALA A CB    1 
ATOM   1223 N  N     . LYS A 1 155 ? -10.370 1.302   -7.280  1.00 54.88  ? 155 LYS A N     1 
ATOM   1224 C  CA    . LYS A 1 155 ? -9.308  1.065   -8.246  1.00 49.18  ? 155 LYS A CA    1 
ATOM   1225 C  C     . LYS A 1 155 ? -8.966  -0.418  -8.281  1.00 53.42  ? 155 LYS A C     1 
ATOM   1226 O  O     . LYS A 1 155 ? -8.992  -1.100  -7.251  1.00 48.16  ? 155 LYS A O     1 
ATOM   1227 C  CB    . LYS A 1 155 ? -8.062  1.899   -7.922  1.00 49.78  ? 155 LYS A CB    1 
ATOM   1228 C  CG    . LYS A 1 155 ? -8.213  3.364   -8.308  1.00 54.86  ? 155 LYS A CG    1 
ATOM   1229 C  CD    . LYS A 1 155 ? -6.937  4.152   -8.082  1.00 58.45  ? 155 LYS A CD    1 
ATOM   1230 C  CE    . LYS A 1 155 ? -6.981  5.467   -8.842  1.00 68.52  ? 155 LYS A CE    1 
ATOM   1231 N  NZ    . LYS A 1 155 ? -8.224  6.235   -8.550  1.00 57.71  ? 155 LYS A NZ    1 
ATOM   1232 N  N     . ILE A 1 156 ? -8.644  -0.908  -9.475  1.00 46.44  ? 156 ILE A N     1 
ATOM   1233 C  CA    . ILE A 1 156 ? -8.466  -2.331  -9.733  1.00 48.14  ? 156 ILE A CA    1 
ATOM   1234 C  C     . ILE A 1 156 ? -6.983  -2.635  -9.883  1.00 45.75  ? 156 ILE A C     1 
ATOM   1235 O  O     . ILE A 1 156 ? -6.235  -1.862  -10.496 1.00 41.75  ? 156 ILE A O     1 
ATOM   1236 C  CB    . ILE A 1 156 ? -9.235  -2.765  -10.994 1.00 41.27  ? 156 ILE A CB    1 
ATOM   1237 C  CG1   . ILE A 1 156 ? -10.742 -2.655  -10.758 1.00 41.21  ? 156 ILE A CG1   1 
ATOM   1238 C  CG2   . ILE A 1 156 ? -8.826  -4.170  -11.411 1.00 42.43  ? 156 ILE A CG2   1 
ATOM   1239 C  CD1   . ILE A 1 156 ? -11.571 -2.908  -11.995 1.00 50.02  ? 156 ILE A CD1   1 
ATOM   1240 N  N     . GLY A 1 157 ? -6.561  -3.770  -9.327  1.00 40.84  ? 157 GLY A N     1 
ATOM   1241 C  CA    . GLY A 1 157 ? -5.193  -4.210  -9.457  1.00 39.30  ? 157 GLY A CA    1 
ATOM   1242 C  C     . GLY A 1 157 ? -5.132  -5.666  -9.876  1.00 40.95  ? 157 GLY A C     1 
ATOM   1243 O  O     . GLY A 1 157 ? -6.111  -6.409  -9.787  1.00 35.50  ? 157 GLY A O     1 
ATOM   1244 N  N     . ILE A 1 158 ? -3.956  -6.057  -10.355 1.00 41.73  ? 158 ILE A N     1 
ATOM   1245 C  CA    . ILE A 1 158 ? -3.650  -7.442  -10.686 1.00 36.01  ? 158 ILE A CA    1 
ATOM   1246 C  C     . ILE A 1 158 ? -2.370  -7.801  -9.950  1.00 39.99  ? 158 ILE A C     1 
ATOM   1247 O  O     . ILE A 1 158 ? -1.322  -7.191  -10.195 1.00 38.52  ? 158 ILE A O     1 
ATOM   1248 C  CB    . ILE A 1 158 ? -3.475  -7.655  -12.199 1.00 35.49  ? 158 ILE A CB    1 
ATOM   1249 C  CG1   . ILE A 1 158 ? -4.724  -7.207  -12.963 1.00 42.16  ? 158 ILE A CG1   1 
ATOM   1250 C  CG2   . ILE A 1 158 ? -3.160  -9.115  -12.500 1.00 35.88  ? 158 ILE A CG2   1 
ATOM   1251 C  CD1   . ILE A 1 158 ? -5.863  -8.200  -12.897 1.00 45.43  ? 158 ILE A CD1   1 
ATOM   1252 N  N     . GLU A 1 159 ? -2.450  -8.768  -9.043  1.00 35.52  ? 159 GLU A N     1 
ATOM   1253 C  CA    . GLU A 1 159 ? -1.265  -9.270  -8.364  1.00 36.18  ? 159 GLU A CA    1 
ATOM   1254 C  C     . GLU A 1 159 ? -0.884  -10.632 -8.929  1.00 37.12  ? 159 GLU A C     1 
ATOM   1255 O  O     . GLU A 1 159 ? -1.720  -11.540 -9.010  1.00 37.75  ? 159 GLU A O     1 
ATOM   1256 C  CB    . GLU A 1 159 ? -1.470  -9.380  -6.853  1.00 33.05  ? 159 GLU A CB    1 
ATOM   1257 C  CG    . GLU A 1 159 ? -0.303  -10.094 -6.179  1.00 36.30  ? 159 GLU A CG    1 
ATOM   1258 C  CD    . GLU A 1 159 ? -0.171  -9.780  -4.703  1.00 38.72  ? 159 GLU A CD    1 
ATOM   1259 O  OE1   . GLU A 1 159 ? -0.959  -8.953  -4.201  1.00 41.05  ? 159 GLU A OE1   1 
ATOM   1260 O  OE2   . GLU A 1 159 ? 0.723   -10.364 -4.049  1.00 38.24  ? 159 GLU A OE2   1 
ATOM   1261 N  N     . LEU A 1 160 ? 0.375   -10.761 -9.330  1.00 37.38  ? 160 LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 160 ? 0.961   -12.043 -9.684  1.00 39.83  ? 160 LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 160 ? 1.785   -12.517 -8.499  1.00 41.66  ? 160 LEU A C     1 
ATOM   1264 O  O     . LEU A 1 160 ? 2.596   -11.756 -7.961  1.00 41.39  ? 160 LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 160 ? 1.831   -11.925 -10.937 1.00 36.53  ? 160 LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 160 ? 1.180   -11.232 -12.133 1.00 38.45  ? 160 LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 160 ? 2.156   -11.165 -13.294 1.00 37.79  ? 160 LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 160 ? -0.111  -11.938 -12.542 1.00 38.30  ? 160 LEU A CD2   1 
ATOM   1269 N  N     . THR A 1 161 ? 1.558   -13.758 -8.080  1.00 35.98  ? 161 THR A N     1 
ATOM   1270 C  CA    . THR A 1 161 ? 2.237   -14.293 -6.912  1.00 36.26  ? 161 THR A CA    1 
ATOM   1271 C  C     . THR A 1 161 ? 2.373   -15.801 -7.052  1.00 36.18  ? 161 THR A C     1 
ATOM   1272 O  O     . THR A 1 161 ? 1.563   -16.456 -7.715  1.00 36.32  ? 161 THR A O     1 
ATOM   1273 C  CB    . THR A 1 161 ? 1.485   -13.957 -5.617  1.00 36.78  ? 161 THR A CB    1 
ATOM   1274 O  OG1   . THR A 1 161 ? 2.217   -14.457 -4.489  1.00 31.75  ? 161 THR A OG1   1 
ATOM   1275 C  CG2   . THR A 1 161 ? 0.100   -14.584 -5.630  1.00 35.57  ? 161 THR A CG2   1 
ATOM   1276 N  N     . ASP A 1 162 ? 3.413   -16.344 -6.419  1.00 32.32  ? 162 ASP A N     1 
ATOM   1277 C  CA    . ASP A 1 162 ? 3.645   -17.780 -6.367  1.00 35.41  ? 162 ASP A CA    1 
ATOM   1278 C  C     . ASP A 1 162 ? 3.301   -18.365 -5.004  1.00 36.44  ? 162 ASP A C     1 
ATOM   1279 O  O     . ASP A 1 162 ? 3.729   -19.480 -4.687  1.00 37.91  ? 162 ASP A O     1 
ATOM   1280 C  CB    . ASP A 1 162 ? 5.096   -18.097 -6.735  1.00 38.73  ? 162 ASP A CB    1 
ATOM   1281 C  CG    . ASP A 1 162 ? 6.096   -17.307 -5.911  1.00 41.70  ? 162 ASP A CG    1 
ATOM   1282 O  OD1   . ASP A 1 162 ? 5.677   -16.524 -5.034  1.00 37.17  ? 162 ASP A OD1   1 
ATOM   1283 O  OD2   . ASP A 1 162 ? 7.311   -17.464 -6.145  1.00 40.94  ? 162 ASP A OD2   1 
ATOM   1284 N  N     . SER A 1 163 ? 2.529   -17.637 -4.201  1.00 35.91  ? 163 SER A N     1 
ATOM   1285 C  CA    . SER A 1 163 ? 2.182   -18.061 -2.851  1.00 35.84  ? 163 SER A CA    1 
ATOM   1286 C  C     . SER A 1 163 ? 0.678   -18.271 -2.738  1.00 39.11  ? 163 SER A C     1 
ATOM   1287 O  O     . SER A 1 163 ? -0.088  -17.299 -2.858  1.00 37.92  ? 163 SER A O     1 
ATOM   1288 C  CB    . SER A 1 163 ? 2.651   -17.020 -1.835  1.00 39.58  ? 163 SER A CB    1 
ATOM   1289 O  OG    . SER A 1 163 ? 2.068   -17.248 -0.564  1.00 40.13  ? 163 SER A OG    1 
ATOM   1290 N  N     . PRO A 1 164 ? 0.206   -19.507 -2.533  1.00 38.43  ? 164 PRO A N     1 
ATOM   1291 C  CA    . PRO A 1 164 ? -1.230  -19.710 -2.278  1.00 37.34  ? 164 PRO A CA    1 
ATOM   1292 C  C     . PRO A 1 164 ? -1.704  -19.072 -0.984  1.00 38.25  ? 164 PRO A C     1 
ATOM   1293 O  O     . PRO A 1 164 ? -2.899  -18.776 -0.856  1.00 36.00  ? 164 PRO A O     1 
ATOM   1294 C  CB    . PRO A 1 164 ? -1.370  -21.238 -2.234  1.00 45.37  ? 164 PRO A CB    1 
ATOM   1295 C  CG    . PRO A 1 164 ? -0.000  -21.730 -1.868  1.00 44.49  ? 164 PRO A CG    1 
ATOM   1296 C  CD    . PRO A 1 164 ? 0.960   -20.772 -2.519  1.00 40.14  ? 164 PRO A CD    1 
ATOM   1297 N  N     . TYR A 1 165 ? -0.807  -18.859 -0.019  1.00 36.34  ? 165 TYR A N     1 
ATOM   1298 C  CA    . TYR A 1 165 ? -1.174  -18.117 1.183   1.00 38.98  ? 165 TYR A CA    1 
ATOM   1299 C  C     . TYR A 1 165 ? -1.578  -16.688 0.839   1.00 40.17  ? 165 TYR A C     1 
ATOM   1300 O  O     . TYR A 1 165 ? -2.507  -16.135 1.438   1.00 37.34  ? 165 TYR A O     1 
ATOM   1301 C  CB    . TYR A 1 165 ? -0.007  -18.129 2.172   1.00 38.91  ? 165 TYR A CB    1 
ATOM   1302 C  CG    . TYR A 1 165 ? -0.173  -17.215 3.373   1.00 42.24  ? 165 TYR A CG    1 
ATOM   1303 C  CD1   . TYR A 1 165 ? 0.248   -15.891 3.326   1.00 38.38  ? 165 TYR A CD1   1 
ATOM   1304 C  CD2   . TYR A 1 165 ? -0.725  -17.683 4.559   1.00 39.20  ? 165 TYR A CD2   1 
ATOM   1305 C  CE1   . TYR A 1 165 ? 0.110   -15.055 4.422   1.00 44.66  ? 165 TYR A CE1   1 
ATOM   1306 C  CE2   . TYR A 1 165 ? -0.867  -16.853 5.659   1.00 38.52  ? 165 TYR A CE2   1 
ATOM   1307 C  CZ    . TYR A 1 165 ? -0.448  -15.542 5.585   1.00 42.12  ? 165 TYR A CZ    1 
ATOM   1308 O  OH    . TYR A 1 165 ? -0.586  -14.712 6.677   1.00 40.23  ? 165 TYR A OH    1 
ATOM   1309 N  N     . VAL A 1 166 ? -0.891  -16.074 -0.129  1.00 40.38  ? 166 VAL A N     1 
ATOM   1310 C  CA    . VAL A 1 166 ? -1.245  -14.723 -0.552  1.00 36.24  ? 166 VAL A CA    1 
ATOM   1311 C  C     . VAL A 1 166 ? -2.609  -14.717 -1.231  1.00 36.55  ? 166 VAL A C     1 
ATOM   1312 O  O     . VAL A 1 166 ? -3.431  -13.823 -0.997  1.00 33.20  ? 166 VAL A O     1 
ATOM   1313 C  CB    . VAL A 1 166 ? -0.154  -14.150 -1.476  1.00 37.39  ? 166 VAL A CB    1 
ATOM   1314 C  CG1   . VAL A 1 166 ? -0.637  -12.869 -2.126  1.00 36.93  ? 166 VAL A CG1   1 
ATOM   1315 C  CG2   . VAL A 1 166 ? 1.130   -13.904 -0.693  1.00 35.20  ? 166 VAL A CG2   1 
ATOM   1316 N  N     . VAL A 1 167 ? -2.870  -15.705 -2.088  1.00 36.07  ? 167 VAL A N     1 
ATOM   1317 C  CA    . VAL A 1 167 ? -4.160  -15.779 -2.769  1.00 35.88  ? 167 VAL A CA    1 
ATOM   1318 C  C     . VAL A 1 167 ? -5.290  -15.854 -1.752  1.00 36.70  ? 167 VAL A C     1 
ATOM   1319 O  O     . VAL A 1 167 ? -6.255  -15.084 -1.808  1.00 36.86  ? 167 VAL A O     1 
ATOM   1320 C  CB    . VAL A 1 167 ? -4.187  -16.978 -3.732  1.00 37.56  ? 167 VAL A CB    1 
ATOM   1321 C  CG1   . VAL A 1 167 ? -5.576  -17.134 -4.335  1.00 38.23  ? 167 VAL A CG1   1 
ATOM   1322 C  CG2   . VAL A 1 167 ? -3.135  -16.811 -4.814  1.00 34.84  ? 167 VAL A CG2   1 
ATOM   1323 N  N     . ALA A 1 168 ? -5.185  -16.786 -0.801  1.00 37.73  ? 168 ALA A N     1 
ATOM   1324 C  CA    . ALA A 1 168 ? -6.233  -16.938 0.203   1.00 39.57  ? 168 ALA A CA    1 
ATOM   1325 C  C     . ALA A 1 168 ? -6.420  -15.656 1.004   1.00 37.25  ? 168 ALA A C     1 
ATOM   1326 O  O     . ALA A 1 168 ? -7.553  -15.227 1.248   1.00 36.90  ? 168 ALA A O     1 
ATOM   1327 C  CB    . ALA A 1 168 ? -5.907  -18.111 1.127   1.00 38.01  ? 168 ALA A CB    1 
ATOM   1328 N  N     . SER A 1 169 ? -5.319  -15.024 1.416   1.00 37.49  ? 169 SER A N     1 
ATOM   1329 C  CA    . SER A 1 169 ? -5.433  -13.796 2.195   1.00 38.83  ? 169 SER A CA    1 
ATOM   1330 C  C     . SER A 1 169 ? -6.021  -12.662 1.362   1.00 38.77  ? 169 SER A C     1 
ATOM   1331 O  O     . SER A 1 169 ? -6.820  -11.865 1.869   1.00 41.09  ? 169 SER A O     1 
ATOM   1332 C  CB    . SER A 1 169 ? -4.068  -13.401 2.755   1.00 40.69  ? 169 SER A CB    1 
ATOM   1333 O  OG    . SER A 1 169 ? -3.497  -14.456 3.507   1.00 39.15  ? 169 SER A OG    1 
ATOM   1334 N  N     . MET A 1 170 ? -5.638  -12.569 0.085   1.00 32.91  ? 170 MET A N     1 
ATOM   1335 C  CA    . MET A 1 170 ? -6.179  -11.513 -0.764  1.00 32.96  ? 170 MET A CA    1 
ATOM   1336 C  C     . MET A 1 170 ? -7.669  -11.704 -1.015  1.00 34.44  ? 170 MET A C     1 
ATOM   1337 O  O     . MET A 1 170 ? -8.400  -10.720 -1.180  1.00 36.33  ? 170 MET A O     1 
ATOM   1338 C  CB    . MET A 1 170 ? -5.410  -11.455 -2.087  1.00 33.14  ? 170 MET A CB    1 
ATOM   1339 C  CG    . MET A 1 170 ? -4.005  -10.890 -1.960  1.00 36.11  ? 170 MET A CG    1 
ATOM   1340 S  SD    . MET A 1 170 ? -3.982  -9.096  -1.742  1.00 40.67  ? 170 MET A SD    1 
ATOM   1341 C  CE    . MET A 1 170 ? -4.470  -8.553  -3.376  1.00 32.89  ? 170 MET A CE    1 
ATOM   1342 N  N     . ARG A 1 171 ? -8.140  -12.953 -1.037  1.00 35.58  ? 171 ARG A N     1 
ATOM   1343 C  CA    . ARG A 1 171 ? -9.572  -13.185 -1.187  1.00 36.60  ? 171 ARG A CA    1 
ATOM   1344 C  C     . ARG A 1 171 ? -10.350 -12.603 -0.015  1.00 37.43  ? 171 ARG A C     1 
ATOM   1345 O  O     . ARG A 1 171 ? -11.507 -12.196 -0.176  1.00 38.34  ? 171 ARG A O     1 
ATOM   1346 C  CB    . ARG A 1 171 ? -9.858  -14.681 -1.319  1.00 37.13  ? 171 ARG A CB    1 
ATOM   1347 C  CG    . ARG A 1 171 ? -11.330 -14.998 -1.529  1.00 41.00  ? 171 ARG A CG    1 
ATOM   1348 C  CD    . ARG A 1 171 ? -11.587 -16.494 -1.618  1.00 44.25  ? 171 ARG A CD    1 
ATOM   1349 N  NE    . ARG A 1 171 ? -12.893 -16.783 -2.201  1.00 44.58  ? 171 ARG A NE    1 
ATOM   1350 C  CZ    . ARG A 1 171 ? -14.038 -16.766 -1.531  1.00 50.55  ? 171 ARG A CZ    1 
ATOM   1351 N  NH1   . ARG A 1 171 ? -14.080 -16.476 -0.241  1.00 48.29  ? 171 ARG A NH1   1 
ATOM   1352 N  NH2   . ARG A 1 171 ? -15.169 -17.043 -2.173  1.00 49.66  ? 171 ARG A NH2   1 
ATOM   1353 N  N     . ILE A 1 172 ? -9.732  -12.554 1.165   1.00 34.01  ? 172 ILE A N     1 
ATOM   1354 C  CA    . ILE A 1 172 ? -10.379 -11.972 2.335   1.00 40.82  ? 172 ILE A CA    1 
ATOM   1355 C  C     . ILE A 1 172 ? -10.197 -10.460 2.354   1.00 38.75  ? 172 ILE A C     1 
ATOM   1356 O  O     . ILE A 1 172 ? -11.142 -9.710  2.621   1.00 41.60  ? 172 ILE A O     1 
ATOM   1357 C  CB    . ILE A 1 172 ? -9.828  -12.618 3.621   1.00 38.93  ? 172 ILE A CB    1 
ATOM   1358 C  CG1   . ILE A 1 172 ? -10.216 -14.097 3.701   1.00 38.46  ? 172 ILE A CG1   1 
ATOM   1359 C  CG2   . ILE A 1 172 ? -10.311 -11.860 4.850   1.00 40.38  ? 172 ILE A CG2   1 
ATOM   1360 C  CD1   . ILE A 1 172 ? -9.553  -14.838 4.850   1.00 36.69  ? 172 ILE A CD1   1 
ATOM   1361 N  N     . MET A 1 173 ? -8.984  -9.990  2.060   1.00 37.45  ? 173 MET A N     1 
ATOM   1362 C  CA    . MET A 1 173 ? -8.659  -8.582  2.250   1.00 44.42  ? 173 MET A CA    1 
ATOM   1363 C  C     . MET A 1 173 ? -9.104  -7.690  1.096   1.00 44.09  ? 173 MET A C     1 
ATOM   1364 O  O     . MET A 1 173 ? -9.135  -6.467  1.263   1.00 42.99  ? 173 MET A O     1 
ATOM   1365 C  CB    . MET A 1 173 ? -7.153  -8.418  2.467   1.00 43.00  ? 173 MET A CB    1 
ATOM   1366 C  CG    . MET A 1 173 ? -6.654  -9.017  3.768   1.00 38.86  ? 173 MET A CG    1 
ATOM   1367 S  SD    . MET A 1 173 ? -7.517  -8.328  5.190   1.00 42.47  ? 173 MET A SD    1 
ATOM   1368 C  CE    . MET A 1 173 ? -7.077  -6.596  5.048   1.00 43.13  ? 173 MET A CE    1 
ATOM   1369 N  N     . THR A 1 174 ? -9.440  -8.259  -0.061  1.00 39.94  ? 174 THR A N     1 
ATOM   1370 C  CA    . THR A 1 174 ? -9.882  -7.487  -1.215  1.00 36.92  ? 174 THR A CA    1 
ATOM   1371 C  C     . THR A 1 174 ? -11.120 -8.141  -1.813  1.00 39.64  ? 174 THR A C     1 
ATOM   1372 O  O     . THR A 1 174 ? -11.549 -9.219  -1.390  1.00 40.78  ? 174 THR A O     1 
ATOM   1373 C  CB    . THR A 1 174 ? -8.779  -7.379  -2.278  1.00 40.45  ? 174 THR A CB    1 
ATOM   1374 O  OG1   . THR A 1 174 ? -8.493  -8.681  -2.810  1.00 40.11  ? 174 THR A OG1   1 
ATOM   1375 C  CG2   . THR A 1 174 ? -7.513  -6.792  -1.680  1.00 35.15  ? 174 THR A CG2   1 
ATOM   1376 N  N     . ARG A 1 175 ? -11.707 -7.467  -2.800  1.00 37.74  ? 175 ARG A N     1 
ATOM   1377 C  CA    . ARG A 1 175 ? -12.681 -8.085  -3.691  1.00 45.20  ? 175 ARG A CA    1 
ATOM   1378 C  C     . ARG A 1 175 ? -11.903 -8.724  -4.837  1.00 42.29  ? 175 ARG A C     1 
ATOM   1379 O  O     . ARG A 1 175 ? -11.257 -8.023  -5.624  1.00 44.54  ? 175 ARG A O     1 
ATOM   1380 C  CB    . ARG A 1 175 ? -13.686 -7.060  -4.212  1.00 44.14  ? 175 ARG A CB    1 
ATOM   1381 C  CG    . ARG A 1 175 ? -14.792 -6.693  -3.232  1.00 47.41  ? 175 ARG A CG    1 
ATOM   1382 C  CD    . ARG A 1 175 ? -14.369 -5.577  -2.298  1.00 46.43  ? 175 ARG A CD    1 
ATOM   1383 N  NE    . ARG A 1 175 ? -15.504 -5.027  -1.565  1.00 51.98  ? 175 ARG A NE    1 
ATOM   1384 C  CZ    . ARG A 1 175 ? -15.434 -3.977  -0.760  1.00 51.37  ? 175 ARG A CZ    1 
ATOM   1385 N  NH1   . ARG A 1 175 ? -14.293 -3.343  -0.548  1.00 48.31  ? 175 ARG A NH1   1 
ATOM   1386 N  NH2   . ARG A 1 175 ? -16.539 -3.547  -0.156  1.00 53.31  ? 175 ARG A NH2   1 
ATOM   1387 N  N     A MET A 1 176 ? -11.974 -10.049 -4.941  0.65 43.12  ? 176 MET A N     1 
ATOM   1388 N  N     B MET A 1 176 ? -11.948 -10.049 -4.915  0.35 43.27  ? 176 MET A N     1 
ATOM   1389 C  CA    A MET A 1 176 ? -11.156 -10.799 -5.884  0.65 45.02  ? 176 MET A CA    1 
ATOM   1390 C  CA    B MET A 1 176 ? -11.180 -10.809 -5.888  0.35 42.71  ? 176 MET A CA    1 
ATOM   1391 C  C     A MET A 1 176 ? -12.015 -11.801 -6.641  0.65 44.25  ? 176 MET A C     1 
ATOM   1392 C  C     B MET A 1 176 ? -12.104 -11.715 -6.686  0.35 44.52  ? 176 MET A C     1 
ATOM   1393 O  O     A MET A 1 176 ? -12.922 -12.410 -6.067  0.65 43.39  ? 176 MET A O     1 
ATOM   1394 O  O     B MET A 1 176 ? -13.137 -12.171 -6.186  0.35 43.43  ? 176 MET A O     1 
ATOM   1395 C  CB    A MET A 1 176 ? -10.013 -11.521 -5.152  0.65 40.84  ? 176 MET A CB    1 
ATOM   1396 C  CB    B MET A 1 176 ? -10.099 -11.655 -5.203  0.35 40.96  ? 176 MET A CB    1 
ATOM   1397 C  CG    A MET A 1 176 ? -9.020  -12.227 -6.060  0.65 44.80  ? 176 MET A CG    1 
ATOM   1398 C  CG    B MET A 1 176 ? -9.341  -12.571 -6.148  0.35 44.04  ? 176 MET A CG    1 
ATOM   1399 S  SD    A MET A 1 176 ? -9.535  -13.889 -6.533  0.65 41.96  ? 176 MET A SD    1 
ATOM   1400 S  SD    B MET A 1 176 ? -8.407  -13.850 -5.287  0.35 42.57  ? 176 MET A SD    1 
ATOM   1401 C  CE    A MET A 1 176 ? -9.301  -14.774 -4.993  0.65 41.17  ? 176 MET A CE    1 
ATOM   1402 C  CE    B MET A 1 176 ? -9.735  -14.831 -4.595  0.35 42.04  ? 176 MET A CE    1 
ATOM   1403 N  N     . GLY A 1 177 ? -11.728 -11.970 -7.928  1.00 45.78  ? 177 GLY A N     1 
ATOM   1404 C  CA    . GLY A 1 177 ? -12.410 -12.955 -8.731  1.00 47.63  ? 177 GLY A CA    1 
ATOM   1405 C  C     . GLY A 1 177 ? -12.655 -12.474 -10.143 1.00 49.39  ? 177 GLY A C     1 
ATOM   1406 O  O     . GLY A 1 177 ? -12.153 -11.437 -10.576 1.00 46.46  ? 177 GLY A O     1 
ATOM   1407 N  N     . THR A 1 178 ? -13.458 -13.266 -10.857 1.00 51.40  ? 178 THR A N     1 
ATOM   1408 C  CA    . THR A 1 178 ? -13.729 -13.011 -12.267 1.00 53.47  ? 178 THR A CA    1 
ATOM   1409 C  C     . THR A 1 178 ? -14.495 -11.710 -12.467 1.00 55.79  ? 178 THR A C     1 
ATOM   1410 O  O     . THR A 1 178 ? -14.287 -11.006 -13.463 1.00 55.13  ? 178 THR A O     1 
ATOM   1411 C  CB    . THR A 1 178 ? -14.511 -14.184 -12.854 1.00 47.51  ? 178 THR A CB    1 
ATOM   1412 O  OG1   . THR A 1 178 ? -13.725 -15.374 -12.750 1.00 47.47  ? 178 THR A OG1   1 
ATOM   1413 C  CG2   . THR A 1 178 ? -14.853 -13.927 -14.313 1.00 55.52  ? 178 THR A CG2   1 
ATOM   1414 N  N     . SER A 1 179 ? -15.393 -11.376 -11.537 1.00 55.59  ? 179 SER A N     1 
ATOM   1415 C  CA    . SER A 1 179 ? -16.194 -10.166 -11.680 1.00 53.36  ? 179 SER A CA    1 
ATOM   1416 C  C     . SER A 1 179 ? -15.336 -8.910  -11.729 1.00 53.99  ? 179 SER A C     1 
ATOM   1417 O  O     . SER A 1 179 ? -15.806 -7.870  -12.204 1.00 55.52  ? 179 SER A O     1 
ATOM   1418 C  CB    . SER A 1 179 ? -17.203 -10.065 -10.534 1.00 59.43  ? 179 SER A CB    1 
ATOM   1419 O  OG    . SER A 1 179 ? -16.552 -9.852  -9.294  1.00 62.41  ? 179 SER A OG    1 
ATOM   1420 N  N     . VAL A 1 180 ? -14.094 -8.979  -11.249 1.00 52.25  ? 180 VAL A N     1 
ATOM   1421 C  CA    . VAL A 1 180 ? -13.205 -7.824  -11.318 1.00 54.53  ? 180 VAL A CA    1 
ATOM   1422 C  C     . VAL A 1 180 ? -12.655 -7.652  -12.728 1.00 54.91  ? 180 VAL A C     1 
ATOM   1423 O  O     . VAL A 1 180 ? -12.583 -6.532  -13.246 1.00 53.92  ? 180 VAL A O     1 
ATOM   1424 C  CB    . VAL A 1 180 ? -12.076 -7.962  -10.282 1.00 48.87  ? 180 VAL A CB    1 
ATOM   1425 C  CG1   . VAL A 1 180 ? -11.151 -6.755  -10.341 1.00 50.37  ? 180 VAL A CG1   1 
ATOM   1426 C  CG2   . VAL A 1 180 ? -12.658 -8.129  -8.888  1.00 45.45  ? 180 VAL A CG2   1 
ATOM   1427 N  N     . LEU A 1 181 ? -12.253 -8.753  -13.370 1.00 55.63  ? 181 LEU A N     1 
ATOM   1428 C  CA    . LEU A 1 181 ? -11.800 -8.672  -14.755 1.00 53.34  ? 181 LEU A CA    1 
ATOM   1429 C  C     . LEU A 1 181 ? -12.890 -8.103  -15.652 1.00 55.85  ? 181 LEU A C     1 
ATOM   1430 O  O     . LEU A 1 181 ? -12.621 -7.252  -16.509 1.00 56.59  ? 181 LEU A O     1 
ATOM   1431 C  CB    . LEU A 1 181 ? -11.362 -10.052 -15.247 1.00 52.45  ? 181 LEU A CB    1 
ATOM   1432 C  CG    . LEU A 1 181 ? -10.021 -10.568 -14.722 1.00 54.00  ? 181 LEU A CG    1 
ATOM   1433 C  CD1   . LEU A 1 181 ? -9.834  -12.032 -15.084 1.00 54.18  ? 181 LEU A CD1   1 
ATOM   1434 C  CD2   . LEU A 1 181 ? -8.876  -9.733  -15.275 1.00 58.04  ? 181 LEU A CD2   1 
ATOM   1435 N  N     . GLU A 1 182 ? -14.132 -8.556  -15.465 1.00 56.55  ? 182 GLU A N     1 
ATOM   1436 C  CA    . GLU A 1 182 ? -15.236 -8.027  -16.258 1.00 58.47  ? 182 GLU A CA    1 
ATOM   1437 C  C     . GLU A 1 182 ? -15.435 -6.539  -15.996 1.00 59.20  ? 182 GLU A C     1 
ATOM   1438 O  O     . GLU A 1 182 ? -15.739 -5.774  -16.918 1.00 64.54  ? 182 GLU A O     1 
ATOM   1439 C  CB    . GLU A 1 182 ? -16.518 -8.804  -15.957 1.00 60.57  ? 182 GLU A CB    1 
ATOM   1440 C  CG    . GLU A 1 182 ? -16.390 -10.304 -16.167 1.00 66.47  ? 182 GLU A CG    1 
ATOM   1441 C  CD    . GLU A 1 182 ? -17.648 -11.062 -15.790 1.00 75.23  ? 182 GLU A CD    1 
ATOM   1442 O  OE1   . GLU A 1 182 ? -18.551 -10.460 -15.173 1.00 78.12  ? 182 GLU A OE1   1 
ATOM   1443 O  OE2   . GLU A 1 182 ? -17.734 -12.266 -16.111 1.00 79.18  ? 182 GLU A OE2   1 
ATOM   1444 N  N     . ALA A 1 183 ? -15.269 -6.111  -14.743 1.00 59.87  ? 183 ALA A N     1 
ATOM   1445 C  CA    . ALA A 1 183 ? -15.407 -4.693  -14.426 1.00 56.49  ? 183 ALA A CA    1 
ATOM   1446 C  C     . ALA A 1 183 ? -14.229 -3.890  -14.961 1.00 58.15  ? 183 ALA A C     1 
ATOM   1447 O  O     . ALA A 1 183 ? -14.395 -2.739  -15.381 1.00 59.87  ? 183 ALA A O     1 
ATOM   1448 C  CB    . ALA A 1 183 ? -15.545 -4.505  -12.916 1.00 51.32  ? 183 ALA A CB    1 
ATOM   1449 N  N     . LEU A 1 184 ? -13.030 -4.477  -14.950 1.00 59.67  ? 184 LEU A N     1 
ATOM   1450 C  CA    . LEU A 1 184 ? -11.856 -3.771  -15.451 1.00 56.11  ? 184 LEU A CA    1 
ATOM   1451 C  C     . LEU A 1 184 ? -11.953 -3.526  -16.951 1.00 55.56  ? 184 LEU A C     1 
ATOM   1452 O  O     . LEU A 1 184 ? -11.658 -2.422  -17.425 1.00 58.64  ? 184 LEU A O     1 
ATOM   1453 C  CB    . LEU A 1 184 ? -10.589 -4.559  -15.117 1.00 52.91  ? 184 LEU A CB    1 
ATOM   1454 C  CG    . LEU A 1 184 ? -9.277  -4.056  -15.723 1.00 58.09  ? 184 LEU A CG    1 
ATOM   1455 C  CD1   . LEU A 1 184 ? -8.856  -2.732  -15.098 1.00 52.37  ? 184 LEU A CD1   1 
ATOM   1456 C  CD2   . LEU A 1 184 ? -8.187  -5.106  -15.571 1.00 47.69  ? 184 LEU A CD2   1 
ATOM   1457 N  N     . GLY A 1 185 ? -12.360 -4.539  -17.711 1.00 59.77  ? 185 GLY A N     1 
ATOM   1458 C  CA    . GLY A 1 185 ? -12.379 -4.395  -19.157 1.00 61.03  ? 185 GLY A CA    1 
ATOM   1459 C  C     . GLY A 1 185 ? -11.002 -4.020  -19.666 1.00 61.65  ? 185 GLY A C     1 
ATOM   1460 O  O     . GLY A 1 185 ? -9.988  -4.597  -19.261 1.00 62.57  ? 185 GLY A O     1 
ATOM   1461 N  N     . ASP A 1 186 ? -10.956 -3.039  -20.567 1.00 59.36  ? 186 ASP A N     1 
ATOM   1462 C  CA    . ASP A 1 186 ? -9.700  -2.485  -21.049 1.00 64.98  ? 186 ASP A CA    1 
ATOM   1463 C  C     . ASP A 1 186 ? -9.233  -1.293  -20.220 1.00 67.09  ? 186 ASP A C     1 
ATOM   1464 O  O     . ASP A 1 186 ? -8.425  -0.491  -20.702 1.00 64.79  ? 186 ASP A O     1 
ATOM   1465 C  CB    . ASP A 1 186 ? -9.825  -2.091  -22.522 1.00 70.28  ? 186 ASP A CB    1 
ATOM   1466 C  CG    . ASP A 1 186 ? -9.834  -3.293  -23.447 1.00 72.52  ? 186 ASP A CG    1 
ATOM   1467 O  OD1   . ASP A 1 186 ? -9.175  -4.302  -23.120 1.00 71.10  ? 186 ASP A OD1   1 
ATOM   1468 O  OD2   . ASP A 1 186 ? -10.496 -3.228  -24.505 1.00 83.01  ? 186 ASP A OD2   1 
ATOM   1469 N  N     . GLY A 1 187 ? -9.724  -1.159  -18.986 1.00 65.93  ? 187 GLY A N     1 
ATOM   1470 C  CA    . GLY A 1 187 ? -9.331  -0.051  -18.145 1.00 57.20  ? 187 GLY A CA    1 
ATOM   1471 C  C     . GLY A 1 187 ? -7.934  -0.212  -17.578 1.00 61.73  ? 187 GLY A C     1 
ATOM   1472 O  O     . GLY A 1 187 ? -7.286  -1.250  -17.711 1.00 57.35  ? 187 GLY A O     1 
ATOM   1473 N  N     . GLU A 1 188 ? -7.468  0.851   -16.930 1.00 58.73  ? 188 GLU A N     1 
ATOM   1474 C  CA    . GLU A 1 188 ? -6.159  0.839   -16.297 1.00 58.46  ? 188 GLU A CA    1 
ATOM   1475 C  C     . GLU A 1 188 ? -6.199  0.033   -15.004 1.00 57.96  ? 188 GLU A C     1 
ATOM   1476 O  O     . GLU A 1 188 ? -7.229  -0.052  -14.328 1.00 54.86  ? 188 GLU A O     1 
ATOM   1477 C  CB    . GLU A 1 188 ? -5.694  2.267   -16.010 1.00 63.72  ? 188 GLU A CB    1 
ATOM   1478 C  CG    . GLU A 1 188 ? -4.328  2.357   -15.355 1.00 70.55  ? 188 GLU A CG    1 
ATOM   1479 C  CD    . GLU A 1 188 ? -3.835  3.786   -15.238 1.00 81.82  ? 188 GLU A CD    1 
ATOM   1480 O  OE1   . GLU A 1 188 ? -4.507  4.697   -15.766 1.00 85.69  ? 188 GLU A OE1   1 
ATOM   1481 O  OE2   . GLU A 1 188 ? -2.773  3.999   -14.617 1.00 85.16  ? 188 GLU A OE2   1 
ATOM   1482 N  N     . PHE A 1 189 ? -5.060  -0.565  -14.661 1.00 52.60  ? 189 PHE A N     1 
ATOM   1483 C  CA    . PHE A 1 189 ? -4.954  -1.339  -13.434 1.00 49.42  ? 189 PHE A CA    1 
ATOM   1484 C  C     . PHE A 1 189 ? -3.553  -1.190  -12.862 1.00 49.22  ? 189 PHE A C     1 
ATOM   1485 O  O     . PHE A 1 189 ? -2.592  -0.922  -13.588 1.00 46.01  ? 189 PHE A O     1 
ATOM   1486 C  CB    . PHE A 1 189 ? -5.278  -2.822  -13.666 1.00 46.06  ? 189 PHE A CB    1 
ATOM   1487 C  CG    . PHE A 1 189 ? -4.389  -3.492  -14.679 1.00 47.92  ? 189 PHE A CG    1 
ATOM   1488 C  CD1   . PHE A 1 189 ? -4.671  -3.404  -16.031 1.00 52.24  ? 189 PHE A CD1   1 
ATOM   1489 C  CD2   . PHE A 1 189 ? -3.280  -4.221  -14.277 1.00 46.32  ? 189 PHE A CD2   1 
ATOM   1490 C  CE1   . PHE A 1 189 ? -3.859  -4.023  -16.967 1.00 51.61  ? 189 PHE A CE1   1 
ATOM   1491 C  CE2   . PHE A 1 189 ? -2.466  -4.843  -15.209 1.00 44.66  ? 189 PHE A CE2   1 
ATOM   1492 C  CZ    . PHE A 1 189 ? -2.757  -4.745  -16.556 1.00 43.75  ? 189 PHE A CZ    1 
ATOM   1493 N  N     . ILE A 1 190 ? -3.454  -1.356  -11.548 1.00 46.05  ? 190 ILE A N     1 
ATOM   1494 C  CA    . ILE A 1 190 ? -2.164  -1.340  -10.871 1.00 44.85  ? 190 ILE A CA    1 
ATOM   1495 C  C     . ILE A 1 190 ? -1.513  -2.706  -11.034 1.00 43.34  ? 190 ILE A C     1 
ATOM   1496 O  O     . ILE A 1 190 ? -2.125  -3.738  -10.739 1.00 39.74  ? 190 ILE A O     1 
ATOM   1497 C  CB    . ILE A 1 190 ? -2.331  -0.975  -9.388  1.00 44.41  ? 190 ILE A CB    1 
ATOM   1498 C  CG1   . ILE A 1 190 ? -2.994  0.398   -9.248  1.00 46.60  ? 190 ILE A CG1   1 
ATOM   1499 C  CG2   . ILE A 1 190 ? -0.988  -1.013  -8.675  1.00 44.74  ? 190 ILE A CG2   1 
ATOM   1500 C  CD1   . ILE A 1 190 ? -2.299  1.497   -10.024 1.00 53.71  ? 190 ILE A CD1   1 
ATOM   1501 N  N     . LYS A 1 191 ? -0.274  -2.717  -11.515 1.00 44.25  ? 191 LYS A N     1 
ATOM   1502 C  CA    . LYS A 1 191 ? 0.468   -3.955  -11.716 1.00 41.97  ? 191 LYS A CA    1 
ATOM   1503 C  C     . LYS A 1 191 ? 1.186   -4.319  -10.423 1.00 43.44  ? 191 LYS A C     1 
ATOM   1504 O  O     . LYS A 1 191 ? 2.010   -3.543  -9.929  1.00 41.52  ? 191 LYS A O     1 
ATOM   1505 C  CB    . LYS A 1 191 ? 1.466   -3.808  -12.864 1.00 44.15  ? 191 LYS A CB    1 
ATOM   1506 C  CG    . LYS A 1 191 ? 0.853   -3.342  -14.177 1.00 49.18  ? 191 LYS A CG    1 
ATOM   1507 C  CD    . LYS A 1 191 ? 1.925   -3.163  -15.242 1.00 47.13  ? 191 LYS A CD    1 
ATOM   1508 C  CE    . LYS A 1 191 ? 1.330   -2.786  -16.593 1.00 59.53  ? 191 LYS A CE    1 
ATOM   1509 N  NZ    . LYS A 1 191 ? 0.722   -1.429  -16.596 1.00 71.93  ? 191 LYS A NZ    1 
ATOM   1510 N  N     . CYS A 1 192 ? 0.874   -5.493  -9.879  1.00 41.53  ? 192 CYS A N     1 
ATOM   1511 C  CA    . CYS A 1 192 ? 1.473   -5.977  -8.641  1.00 36.36  ? 192 CYS A CA    1 
ATOM   1512 C  C     . CYS A 1 192 ? 2.158   -7.309  -8.913  1.00 42.45  ? 192 CYS A C     1 
ATOM   1513 O  O     . CYS A 1 192 ? 1.499   -8.282  -9.294  1.00 42.61  ? 192 CYS A O     1 
ATOM   1514 C  CB    . CYS A 1 192 ? 0.418   -6.126  -7.541  1.00 38.75  ? 192 CYS A CB    1 
ATOM   1515 S  SG    . CYS A 1 192 ? -0.557  -4.633  -7.246  1.00 38.65  ? 192 CYS A SG    1 
ATOM   1516 N  N     . LEU A 1 193 ? 3.474   -7.345  -8.721  1.00 34.95  ? 193 LEU A N     1 
ATOM   1517 C  CA    . LEU A 1 193 ? 4.279   -8.543  -8.921  1.00 43.48  ? 193 LEU A CA    1 
ATOM   1518 C  C     . LEU A 1 193 ? 4.905   -8.942  -7.594  1.00 43.70  ? 193 LEU A C     1 
ATOM   1519 O  O     . LEU A 1 193 ? 5.574   -8.126  -6.950  1.00 42.56  ? 193 LEU A O     1 
ATOM   1520 C  CB    . LEU A 1 193 ? 5.368   -8.308  -9.973  1.00 36.44  ? 193 LEU A CB    1 
ATOM   1521 C  CG    . LEU A 1 193 ? 6.363   -9.445  -10.218 1.00 43.09  ? 193 LEU A CG    1 
ATOM   1522 C  CD1   . LEU A 1 193 ? 5.631   -10.707 -10.647 1.00 35.51  ? 193 LEU A CD1   1 
ATOM   1523 C  CD2   . LEU A 1 193 ? 7.399   -9.041  -11.255 1.00 39.49  ? 193 LEU A CD2   1 
ATOM   1524 N  N     . HIS A 1 194 ? 4.688   -10.193 -7.186  1.00 36.55  ? 194 HIS A N     1 
ATOM   1525 C  CA    . HIS A 1 194 ? 5.204   -10.700 -5.923  1.00 39.13  ? 194 HIS A CA    1 
ATOM   1526 C  C     . HIS A 1 194 ? 5.762   -12.102 -6.107  1.00 41.50  ? 194 HIS A C     1 
ATOM   1527 O  O     . HIS A 1 194 ? 5.185   -12.922 -6.826  1.00 40.20  ? 194 HIS A O     1 
ATOM   1528 C  CB    . HIS A 1 194 ? 4.118   -10.727 -4.842  1.00 36.51  ? 194 HIS A CB    1 
ATOM   1529 C  CG    . HIS A 1 194 ? 4.532   -11.435 -3.588  1.00 36.01  ? 194 HIS A CG    1 
ATOM   1530 N  ND1   . HIS A 1 194 ? 4.010   -12.654 -3.214  1.00 38.49  ? 194 HIS A ND1   1 
ATOM   1531 C  CD2   . HIS A 1 194 ? 5.415   -11.091 -2.621  1.00 35.77  ? 194 HIS A CD2   1 
ATOM   1532 C  CE1   . HIS A 1 194 ? 4.552   -13.030 -2.069  1.00 39.45  ? 194 HIS A CE1   1 
ATOM   1533 N  NE2   . HIS A 1 194 ? 5.408   -12.100 -1.687  1.00 38.83  ? 194 HIS A NE2   1 
ATOM   1534 N  N     . SER A 1 195 ? 6.879   -12.371 -5.435  1.00 35.89  ? 195 SER A N     1 
ATOM   1535 C  CA    . SER A 1 195 ? 7.468   -13.700 -5.389  1.00 42.52  ? 195 SER A CA    1 
ATOM   1536 C  C     . SER A 1 195 ? 8.119   -13.899 -4.029  1.00 44.63  ? 195 SER A C     1 
ATOM   1537 O  O     . SER A 1 195 ? 8.731   -12.975 -3.483  1.00 40.33  ? 195 SER A O     1 
ATOM   1538 C  CB    . SER A 1 195 ? 8.505   -13.902 -6.502  1.00 41.13  ? 195 SER A CB    1 
ATOM   1539 O  OG    . SER A 1 195 ? 9.116   -15.178 -6.403  1.00 41.65  ? 195 SER A OG    1 
ATOM   1540 N  N     . VAL A 1 196 ? 7.969   -15.104 -3.474  1.00 40.53  ? 196 VAL A N     1 
ATOM   1541 C  CA    . VAL A 1 196 ? 8.665   -15.443 -2.240  1.00 40.16  ? 196 VAL A CA    1 
ATOM   1542 C  C     . VAL A 1 196 ? 10.152  -15.659 -2.466  1.00 44.61  ? 196 VAL A C     1 
ATOM   1543 O  O     . VAL A 1 196 ? 10.916  -15.738 -1.497  1.00 47.82  ? 196 VAL A O     1 
ATOM   1544 C  CB    . VAL A 1 196 ? 8.033   -16.693 -1.598  1.00 48.37  ? 196 VAL A CB    1 
ATOM   1545 C  CG1   . VAL A 1 196 ? 6.562   -16.440 -1.311  1.00 46.33  ? 196 VAL A CG1   1 
ATOM   1546 C  CG2   . VAL A 1 196 ? 8.206   -17.896 -2.507  1.00 43.84  ? 196 VAL A CG2   1 
ATOM   1547 N  N     . GLY A 1 197 ? 10.576  -15.756 -3.724  1.00 46.51  ? 197 GLY A N     1 
ATOM   1548 C  CA    . GLY A 1 197 ? 11.985  -15.860 -4.046  1.00 46.73  ? 197 GLY A CA    1 
ATOM   1549 C  C     . GLY A 1 197 ? 12.624  -17.200 -3.767  1.00 52.33  ? 197 GLY A C     1 
ATOM   1550 O  O     . GLY A 1 197 ? 13.806  -17.249 -3.416  1.00 52.74  ? 197 GLY A O     1 
ATOM   1551 N  N     . CYS A 1 198 ? 11.886  -18.296 -3.922  1.00 47.77  ? 198 CYS A N     1 
ATOM   1552 C  CA    . CYS A 1 198 ? 12.401  -19.638 -3.655  1.00 48.55  ? 198 CYS A CA    1 
ATOM   1553 C  C     . CYS A 1 198 ? 12.105  -20.545 -4.841  1.00 54.34  ? 198 CYS A C     1 
ATOM   1554 O  O     . CYS A 1 198 ? 11.276  -21.460 -4.754  1.00 55.51  ? 198 CYS A O     1 
ATOM   1555 C  CB    . CYS A 1 198 ? 11.806  -20.210 -2.368  1.00 55.54  ? 198 CYS A CB    1 
ATOM   1556 S  SG    . CYS A 1 198 ? 12.396  -19.405 -0.862  1.00 62.47  ? 198 CYS A SG    1 
ATOM   1557 N  N     . PRO A 1 199 ? 12.775  -20.323 -5.971  1.00 55.39  ? 199 PRO A N     1 
ATOM   1558 C  CA    . PRO A 1 199 ? 12.580  -21.215 -7.119  1.00 52.88  ? 199 PRO A CA    1 
ATOM   1559 C  C     . PRO A 1 199 ? 12.974  -22.644 -6.775  1.00 60.13  ? 199 PRO A C     1 
ATOM   1560 O  O     . PRO A 1 199 ? 13.915  -22.885 -6.016  1.00 62.11  ? 199 PRO A O     1 
ATOM   1561 C  CB    . PRO A 1 199 ? 13.497  -20.619 -8.195  1.00 51.77  ? 199 PRO A CB    1 
ATOM   1562 C  CG    . PRO A 1 199 ? 14.505  -19.817 -7.439  1.00 56.26  ? 199 PRO A CG    1 
ATOM   1563 C  CD    . PRO A 1 199 ? 13.775  -19.279 -6.246  1.00 52.60  ? 199 PRO A CD    1 
ATOM   1564 N  N     . LEU A 1 200 ? 12.234  -23.596 -7.339  1.00 60.70  ? 200 LEU A N     1 
ATOM   1565 C  CA    . LEU A 1 200 ? 12.544  -25.002 -7.132  1.00 65.62  ? 200 LEU A CA    1 
ATOM   1566 C  C     . LEU A 1 200 ? 13.468  -25.503 -8.239  1.00 66.52  ? 200 LEU A C     1 
ATOM   1567 O  O     . LEU A 1 200 ? 13.360  -25.058 -9.386  1.00 63.39  ? 200 LEU A O     1 
ATOM   1568 C  CB    . LEU A 1 200 ? 11.267  -25.836 -7.111  1.00 62.13  ? 200 LEU A CB    1 
ATOM   1569 C  CG    . LEU A 1 200 ? 10.233  -25.440 -6.052  1.00 60.23  ? 200 LEU A CG    1 
ATOM   1570 C  CD1   . LEU A 1 200 ? 8.955   -26.250 -6.206  1.00 56.49  ? 200 LEU A CD1   1 
ATOM   1571 C  CD2   . LEU A 1 200 ? 10.803  -25.602 -4.652  1.00 63.99  ? 200 LEU A CD2   1 
ATOM   1572 N  N     . PRO A 1 201 ? 14.393  -26.420 -7.932  1.00 74.63  ? 201 PRO A N     1 
ATOM   1573 C  CA    . PRO A 1 201 ? 14.625  -27.073 -6.632  1.00 76.02  ? 201 PRO A CA    1 
ATOM   1574 C  C     . PRO A 1 201 ? 15.135  -26.105 -5.568  1.00 80.32  ? 201 PRO A C     1 
ATOM   1575 O  O     . PRO A 1 201 ? 15.824  -25.136 -5.877  1.00 82.04  ? 201 PRO A O     1 
ATOM   1576 C  CB    . PRO A 1 201 ? 15.667  -28.147 -6.973  1.00 78.76  ? 201 PRO A CB    1 
ATOM   1577 C  CG    . PRO A 1 201 ? 16.426  -27.570 -8.131  1.00 78.55  ? 201 PRO A CG    1 
ATOM   1578 C  CD    . PRO A 1 201 ? 15.387  -26.839 -8.938  1.00 76.20  ? 201 PRO A CD    1 
ATOM   1579 N  N     . LEU A 1 202 ? 14.812  -26.350 -4.300  1.00 78.95  ? 202 LEU A N     1 
ATOM   1580 C  CA    . LEU A 1 202 ? 15.252  -25.464 -3.232  1.00 85.12  ? 202 LEU A CA    1 
ATOM   1581 C  C     . LEU A 1 202 ? 16.750  -25.599 -2.996  1.00 91.87  ? 202 LEU A C     1 
ATOM   1582 O  O     . LEU A 1 202 ? 17.309  -26.698 -3.044  1.00 91.58  ? 202 LEU A O     1 
ATOM   1583 C  CB    . LEU A 1 202 ? 14.495  -25.765 -1.940  1.00 84.75  ? 202 LEU A CB    1 
ATOM   1584 C  CG    . LEU A 1 202 ? 13.017  -25.386 -1.917  1.00 77.60  ? 202 LEU A CG    1 
ATOM   1585 C  CD1   . LEU A 1 202 ? 12.441  -25.578 -0.525  1.00 76.46  ? 202 LEU A CD1   1 
ATOM   1586 C  CD2   . LEU A 1 202 ? 12.832  -23.952 -2.386  1.00 66.28  ? 202 LEU A CD2   1 
ATOM   1587 N  N     . LYS A 1 203 ? 17.398  -24.464 -2.736  1.00 104.54 ? 203 LYS A N     1 
ATOM   1588 C  CA    . LYS A 1 203 ? 18.800  -24.432 -2.354  1.00 110.76 ? 203 LYS A CA    1 
ATOM   1589 C  C     . LYS A 1 203 ? 19.003  -24.112 -0.881  1.00 116.41 ? 203 LYS A C     1 
ATOM   1590 O  O     . LYS A 1 203 ? 20.119  -24.277 -0.376  1.00 116.59 ? 203 LYS A O     1 
ATOM   1591 C  CB    . LYS A 1 203 ? 19.559  -23.410 -3.214  1.00 118.12 ? 203 LYS A CB    1 
ATOM   1592 C  CG    . LYS A 1 203 ? 19.465  -23.692 -4.706  1.00 121.38 ? 203 LYS A CG    1 
ATOM   1593 C  CD    . LYS A 1 203 ? 20.080  -22.581 -5.538  1.00 128.63 ? 203 LYS A CD    1 
ATOM   1594 C  CE    . LYS A 1 203 ? 19.946  -22.879 -7.023  1.00 130.99 ? 203 LYS A CE    1 
ATOM   1595 N  NZ    . LYS A 1 203 ? 18.532  -23.138 -7.412  1.00 123.25 ? 203 LYS A NZ    1 
ATOM   1596 N  N     . LYS A 1 204 ? 17.959  -23.663 -0.186  1.00 116.40 ? 204 LYS A N     1 
ATOM   1597 C  CA    . LYS A 1 204 ? 18.002  -23.422 1.252   1.00 114.70 ? 204 LYS A CA    1 
ATOM   1598 C  C     . LYS A 1 204 ? 16.797  -24.123 1.862   1.00 109.37 ? 204 LYS A C     1 
ATOM   1599 O  O     . LYS A 1 204 ? 15.650  -23.842 1.455   1.00 105.99 ? 204 LYS A O     1 
ATOM   1600 C  CB    . LYS A 1 204 ? 17.983  -21.925 1.569   1.00 117.90 ? 204 LYS A CB    1 
ATOM   1601 C  CG    . LYS A 1 204 ? 18.993  -21.103 0.786   1.00 118.98 ? 204 LYS A CG    1 
ATOM   1602 C  CD    . LYS A 1 204 ? 18.777  -19.616 1.021   1.00 121.58 ? 204 LYS A CD    1 
ATOM   1603 C  CE    . LYS A 1 204 ? 19.718  -18.775 0.176   1.00 115.99 ? 204 LYS A CE    1 
ATOM   1604 N  NZ    . LYS A 1 204 ? 19.453  -17.320 0.345   1.00 98.45  ? 204 LYS A NZ    1 
ATOM   1605 N  N     . PRO A 1 205 ? 16.989  -25.034 2.815   1.00 109.76 ? 205 PRO A N     1 
ATOM   1606 C  CA    . PRO A 1 205 ? 15.840  -25.732 3.405   1.00 104.02 ? 205 PRO A CA    1 
ATOM   1607 C  C     . PRO A 1 205 ? 14.831  -24.750 3.985   1.00 93.40  ? 205 PRO A C     1 
ATOM   1608 O  O     . PRO A 1 205 ? 15.195  -23.744 4.599   1.00 93.57  ? 205 PRO A O     1 
ATOM   1609 C  CB    . PRO A 1 205 ? 16.475  -26.601 4.496   1.00 102.73 ? 205 PRO A CB    1 
ATOM   1610 C  CG    . PRO A 1 205 ? 17.893  -26.787 4.051   1.00 106.04 ? 205 PRO A CG    1 
ATOM   1611 C  CD    . PRO A 1 205 ? 18.270  -25.504 3.367   1.00 112.87 ? 205 PRO A CD    1 
ATOM   1612 N  N     . LEU A 1 206 ? 13.551  -25.052 3.779   1.00 85.57  ? 206 LEU A N     1 
ATOM   1613 C  CA    . LEU A 1 206 ? 12.479  -24.185 4.248   1.00 80.62  ? 206 LEU A CA    1 
ATOM   1614 C  C     . LEU A 1 206 ? 12.204  -24.411 5.728   1.00 79.55  ? 206 LEU A C     1 
ATOM   1615 O  O     . LEU A 1 206 ? 12.170  -25.550 6.205   1.00 81.28  ? 206 LEU A O     1 
ATOM   1616 C  CB    . LEU A 1 206 ? 11.200  -24.425 3.444   1.00 71.54  ? 206 LEU A CB    1 
ATOM   1617 C  CG    . LEU A 1 206 ? 11.200  -23.972 1.983   1.00 68.98  ? 206 LEU A CG    1 
ATOM   1618 C  CD1   . LEU A 1 206 ? 9.812   -24.114 1.375   1.00 68.13  ? 206 LEU A CD1   1 
ATOM   1619 C  CD2   . LEU A 1 206 ? 11.695  -22.541 1.870   1.00 70.29  ? 206 LEU A CD2   1 
ATOM   1620 N  N     . VAL A 1 207 ? 12.007  -23.313 6.452   1.00 73.44  ? 207 VAL A N     1 
ATOM   1621 C  CA    . VAL A 1 207 ? 11.655  -23.358 7.865   1.00 72.78  ? 207 VAL A CA    1 
ATOM   1622 C  C     . VAL A 1 207 ? 10.142  -23.259 7.992   1.00 73.32  ? 207 VAL A C     1 
ATOM   1623 O  O     . VAL A 1 207 ? 9.523   -22.332 7.456   1.00 69.73  ? 207 VAL A O     1 
ATOM   1624 C  CB    . VAL A 1 207 ? 12.348  -22.228 8.644   1.00 68.06  ? 207 VAL A CB    1 
ATOM   1625 C  CG1   . VAL A 1 207 ? 11.849  -22.191 10.083  1.00 67.69  ? 207 VAL A CG1   1 
ATOM   1626 C  CG2   . VAL A 1 207 ? 13.857  -22.400 8.602   1.00 71.91  ? 207 VAL A CG2   1 
ATOM   1627 N  N     . ASN A 1 208 ? 9.545   -24.218 8.701   1.00 72.58  ? 208 ASN A N     1 
ATOM   1628 C  CA    . ASN A 1 208 ? 8.097   -24.260 8.900   1.00 69.44  ? 208 ASN A CA    1 
ATOM   1629 C  C     . ASN A 1 208 ? 7.342   -24.248 7.574   1.00 66.30  ? 208 ASN A C     1 
ATOM   1630 O  O     . ASN A 1 208 ? 6.238   -23.705 7.484   1.00 66.58  ? 208 ASN A O     1 
ATOM   1631 C  CB    . ASN A 1 208 ? 7.624   -23.107 9.791   1.00 68.92  ? 208 ASN A CB    1 
ATOM   1632 C  CG    . ASN A 1 208 ? 8.075   -23.259 11.231  1.00 74.82  ? 208 ASN A CG    1 
ATOM   1633 O  OD1   . ASN A 1 208 ? 8.996   -24.016 11.532  1.00 82.06  ? 208 ASN A OD1   1 
ATOM   1634 N  ND2   . ASN A 1 208 ? 7.421   -22.533 12.132  1.00 73.45  ? 208 ASN A ND2   1 
ATOM   1635 N  N     . ASN A 1 209 ? 7.929   -24.843 6.535   1.00 68.76  ? 209 ASN A N     1 
ATOM   1636 C  CA    . ASN A 1 209 ? 7.308   -24.889 5.209   1.00 66.34  ? 209 ASN A CA    1 
ATOM   1637 C  C     . ASN A 1 209 ? 6.904   -23.496 4.734   1.00 60.44  ? 209 ASN A C     1 
ATOM   1638 O  O     . ASN A 1 209 ? 5.907   -23.330 4.026   1.00 57.46  ? 209 ASN A O     1 
ATOM   1639 C  CB    . ASN A 1 209 ? 6.098   -25.829 5.196   1.00 65.96  ? 209 ASN A CB    1 
ATOM   1640 C  CG    . ASN A 1 209 ? 6.482   -27.280 5.418   1.00 72.38  ? 209 ASN A CG    1 
ATOM   1641 O  OD1   . ASN A 1 209 ? 7.619   -27.679 5.168   1.00 78.20  ? 209 ASN A OD1   1 
ATOM   1642 N  ND2   . ASN A 1 209 ? 5.528   -28.080 5.881   1.00 74.97  ? 209 ASN A ND2   1 
ATOM   1643 N  N     . TRP A 1 210 ? 7.677   -22.484 5.121   1.00 55.54  ? 210 TRP A N     1 
ATOM   1644 C  CA    . TRP A 1 210 ? 7.382   -21.092 4.791   1.00 61.26  ? 210 TRP A CA    1 
ATOM   1645 C  C     . TRP A 1 210 ? 8.436   -20.599 3.805   1.00 55.89  ? 210 TRP A C     1 
ATOM   1646 O  O     . TRP A 1 210 ? 9.568   -20.291 4.191   1.00 56.50  ? 210 TRP A O     1 
ATOM   1647 C  CB    . TRP A 1 210 ? 7.344   -20.227 6.047   1.00 56.65  ? 210 TRP A CB    1 
ATOM   1648 C  CG    . TRP A 1 210 ? 6.929   -18.814 5.779   1.00 49.25  ? 210 TRP A CG    1 
ATOM   1649 C  CD1   . TRP A 1 210 ? 7.744   -17.726 5.671   1.00 53.04  ? 210 TRP A CD1   1 
ATOM   1650 C  CD2   . TRP A 1 210 ? 5.594   -18.338 5.575   1.00 50.49  ? 210 TRP A CD2   1 
ATOM   1651 N  NE1   . TRP A 1 210 ? 6.999   -16.599 5.416   1.00 48.00  ? 210 TRP A NE1   1 
ATOM   1652 C  CE2   . TRP A 1 210 ? 5.676   -16.949 5.350   1.00 49.73  ? 210 TRP A CE2   1 
ATOM   1653 C  CE3   . TRP A 1 210 ? 4.338   -18.951 5.559   1.00 50.43  ? 210 TRP A CE3   1 
ATOM   1654 C  CZ2   . TRP A 1 210 ? 4.550   -16.164 5.114   1.00 47.63  ? 210 TRP A CZ2   1 
ATOM   1655 C  CZ3   . TRP A 1 210 ? 3.224   -18.171 5.325   1.00 45.91  ? 210 TRP A CZ3   1 
ATOM   1656 C  CH2   . TRP A 1 210 ? 3.336   -16.791 5.107   1.00 44.11  ? 210 TRP A CH2   1 
ATOM   1657 N  N     . ALA A 1 211 ? 8.055   -20.519 2.533   1.00 51.90  ? 211 ALA A N     1 
ATOM   1658 C  CA    . ALA A 1 211 ? 8.962   -20.027 1.506   1.00 53.34  ? 211 ALA A CA    1 
ATOM   1659 C  C     . ALA A 1 211 ? 9.187   -18.528 1.675   1.00 53.58  ? 211 ALA A C     1 
ATOM   1660 O  O     . ALA A 1 211 ? 8.231   -17.750 1.774   1.00 50.33  ? 211 ALA A O     1 
ATOM   1661 C  CB    . ALA A 1 211 ? 8.398   -20.326 0.119   1.00 51.14  ? 211 ALA A CB    1 
ATOM   1662 N  N     . CYS A 1 212 ? 10.454  -18.125 1.709   1.00 54.21  ? 212 CYS A N     1 
ATOM   1663 C  CA    . CYS A 1 212 ? 10.820  -16.721 1.848   1.00 49.97  ? 212 CYS A CA    1 
ATOM   1664 C  C     . CYS A 1 212 ? 12.308  -16.584 1.565   1.00 53.96  ? 212 CYS A C     1 
ATOM   1665 O  O     . CYS A 1 212 ? 13.053  -17.567 1.579   1.00 52.11  ? 212 CYS A O     1 
ATOM   1666 C  CB    . CYS A 1 212 ? 10.480  -16.181 3.244   1.00 50.37  ? 212 CYS A CB    1 
ATOM   1667 S  SG    . CYS A 1 212 ? 11.393  -16.953 4.603   1.00 52.37  ? 212 CYS A SG    1 
ATOM   1668 N  N     . ASN A 1 213 ? 12.727  -15.349 1.300   1.00 54.79  ? 213 ASN A N     1 
ATOM   1669 C  CA    . ASN A 1 213 ? 14.125  -15.036 1.002   1.00 55.43  ? 213 ASN A CA    1 
ATOM   1670 C  C     . ASN A 1 213 ? 14.483  -13.745 1.720   1.00 57.84  ? 213 ASN A C     1 
ATOM   1671 O  O     . ASN A 1 213 ? 14.528  -12.666 1.117   1.00 57.77  ? 213 ASN A O     1 
ATOM   1672 C  CB    . ASN A 1 213 ? 14.355  -14.919 -0.508  1.00 57.11  ? 213 ASN A CB    1 
ATOM   1673 C  CG    . ASN A 1 213 ? 15.818  -15.039 -0.889  1.00 59.04  ? 213 ASN A CG    1 
ATOM   1674 O  OD1   . ASN A 1 213 ? 16.704  -14.598 -0.156  1.00 63.52  ? 213 ASN A OD1   1 
ATOM   1675 N  ND2   . ASN A 1 213 ? 16.078  -15.640 -2.043  1.00 55.78  ? 213 ASN A ND2   1 
ATOM   1676 N  N     . PRO A 1 214 ? 14.746  -13.820 3.028   1.00 60.26  ? 214 PRO A N     1 
ATOM   1677 C  CA    . PRO A 1 214 ? 15.003  -12.586 3.789   1.00 60.97  ? 214 PRO A CA    1 
ATOM   1678 C  C     . PRO A 1 214 ? 16.154  -11.763 3.240   1.00 65.40  ? 214 PRO A C     1 
ATOM   1679 O  O     . PRO A 1 214 ? 16.050  -10.532 3.171   1.00 63.62  ? 214 PRO A O     1 
ATOM   1680 C  CB    . PRO A 1 214 ? 15.305  -13.107 5.203   1.00 60.24  ? 214 PRO A CB    1 
ATOM   1681 C  CG    . PRO A 1 214 ? 14.668  -14.457 5.258   1.00 59.24  ? 214 PRO A CG    1 
ATOM   1682 C  CD    . PRO A 1 214 ? 14.795  -15.021 3.878   1.00 60.37  ? 214 PRO A CD    1 
ATOM   1683 N  N     . GLU A 1 215 ? 17.255  -12.408 2.847   1.00 66.63  ? 215 GLU A N     1 
ATOM   1684 C  CA    . GLU A 1 215 ? 18.423  -11.664 2.385   1.00 66.70  ? 215 GLU A CA    1 
ATOM   1685 C  C     . GLU A 1 215 ? 18.079  -10.766 1.203   1.00 65.20  ? 215 GLU A C     1 
ATOM   1686 O  O     . GLU A 1 215 ? 18.506  -9.607  1.151   1.00 62.71  ? 215 GLU A O     1 
ATOM   1687 C  CB    . GLU A 1 215 ? 19.550  -12.628 2.011   1.00 71.16  ? 215 GLU A CB    1 
ATOM   1688 C  CG    . GLU A 1 215 ? 20.009  -13.536 3.141   1.00 77.51  ? 215 GLU A CG    1 
ATOM   1689 C  CD    . GLU A 1 215 ? 19.099  -14.728 3.340   1.00 84.15  ? 215 GLU A CD    1 
ATOM   1690 O  OE1   . GLU A 1 215 ? 18.072  -14.816 2.637   1.00 77.74  ? 215 GLU A OE1   1 
ATOM   1691 O  OE2   . GLU A 1 215 ? 19.411  -15.581 4.195   1.00 84.52  ? 215 GLU A OE2   1 
ATOM   1692 N  N     . LEU A 1 216 ? 17.308  -11.279 0.247   1.00 62.61  ? 216 LEU A N     1 
ATOM   1693 C  CA    . LEU A 1 216 ? 16.977  -10.547 -0.968  1.00 55.45  ? 216 LEU A CA    1 
ATOM   1694 C  C     . LEU A 1 216 ? 15.639  -9.825  -0.881  1.00 52.54  ? 216 LEU A C     1 
ATOM   1695 O  O     . LEU A 1 216 ? 15.143  -9.344  -1.904  1.00 49.96  ? 216 LEU A O     1 
ATOM   1696 C  CB    . LEU A 1 216 ? 16.972  -11.496 -2.167  1.00 56.16  ? 216 LEU A CB    1 
ATOM   1697 C  CG    . LEU A 1 216 ? 18.284  -12.223 -2.456  1.00 58.19  ? 216 LEU A CG    1 
ATOM   1698 C  CD1   . LEU A 1 216 ? 18.119  -13.176 -3.627  1.00 60.12  ? 216 LEU A CD1   1 
ATOM   1699 C  CD2   . LEU A 1 216 ? 19.401  -11.228 -2.729  1.00 56.74  ? 216 LEU A CD2   1 
ATOM   1700 N  N     . THR A 1 217 ? 15.045  -9.739  0.306   1.00 54.31  ? 217 THR A N     1 
ATOM   1701 C  CA    . THR A 1 217 ? 13.743  -9.100  0.435   1.00 51.70  ? 217 THR A CA    1 
ATOM   1702 C  C     . THR A 1 217 ? 13.808  -7.651  -0.032  1.00 54.51  ? 217 THR A C     1 
ATOM   1703 O  O     . THR A 1 217 ? 14.732  -6.909  0.310   1.00 51.81  ? 217 THR A O     1 
ATOM   1704 C  CB    . THR A 1 217 ? 13.254  -9.164  1.883   1.00 50.83  ? 217 THR A CB    1 
ATOM   1705 O  OG1   . THR A 1 217 ? 12.962  -10.522 2.231   1.00 55.39  ? 217 THR A OG1   1 
ATOM   1706 C  CG2   . THR A 1 217 ? 12.000  -8.322  2.054   1.00 48.10  ? 217 THR A CG2   1 
ATOM   1707 N  N     . LEU A 1 218 ? 12.813  -7.253  -0.823  1.00 51.21  ? 218 LEU A N     1 
ATOM   1708 C  CA    . LEU A 1 218 ? 12.734  -5.891  -1.335  1.00 44.25  ? 218 LEU A CA    1 
ATOM   1709 C  C     . LEU A 1 218 ? 11.303  -5.618  -1.769  1.00 44.78  ? 218 LEU A C     1 
ATOM   1710 O  O     . LEU A 1 218 ? 10.745  -6.374  -2.570  1.00 46.42  ? 218 LEU A O     1 
ATOM   1711 C  CB    . LEU A 1 218 ? 13.699  -5.684  -2.509  1.00 48.26  ? 218 LEU A CB    1 
ATOM   1712 C  CG    . LEU A 1 218 ? 13.767  -4.284  -3.123  1.00 45.88  ? 218 LEU A CG    1 
ATOM   1713 C  CD1   . LEU A 1 218 ? 14.373  -3.290  -2.143  1.00 41.47  ? 218 LEU A CD1   1 
ATOM   1714 C  CD2   . LEU A 1 218 ? 14.552  -4.307  -4.422  1.00 48.80  ? 218 LEU A CD2   1 
ATOM   1715 N  N     . ILE A 1 219 ? 10.712  -4.551  -1.238  1.00 46.97  ? 219 ILE A N     1 
ATOM   1716 C  CA    . ILE A 1 219 ? 9.381   -4.104  -1.631  1.00 45.36  ? 219 ILE A CA    1 
ATOM   1717 C  C     . ILE A 1 219 ? 9.542   -2.767  -2.341  1.00 45.04  ? 219 ILE A C     1 
ATOM   1718 O  O     . ILE A 1 219 ? 9.941   -1.772  -1.723  1.00 43.47  ? 219 ILE A O     1 
ATOM   1719 C  CB    . ILE A 1 219 ? 8.434   -3.979  -0.428  1.00 44.94  ? 219 ILE A CB    1 
ATOM   1720 C  CG1   . ILE A 1 219 ? 8.388   -5.290  0.370   1.00 44.05  ? 219 ILE A CG1   1 
ATOM   1721 C  CG2   . ILE A 1 219 ? 7.041   -3.600  -0.895  1.00 41.04  ? 219 ILE A CG2   1 
ATOM   1722 C  CD1   . ILE A 1 219 ? 9.557   -5.478  1.312   1.00 43.95  ? 219 ILE A CD1   1 
ATOM   1723 N  N     . ALA A 1 220 ? 9.233   -2.743  -3.637  1.00 42.17  ? 220 ALA A N     1 
ATOM   1724 C  CA    . ALA A 1 220 ? 9.466   -1.580  -4.479  1.00 45.68  ? 220 ALA A CA    1 
ATOM   1725 C  C     . ALA A 1 220 ? 8.150   -1.019  -4.998  1.00 40.92  ? 220 ALA A C     1 
ATOM   1726 O  O     . ALA A 1 220 ? 7.203   -1.762  -5.274  1.00 39.82  ? 220 ALA A O     1 
ATOM   1727 C  CB    . ALA A 1 220 ? 10.373  -1.927  -5.662  1.00 43.74  ? 220 ALA A CB    1 
ATOM   1728 N  N     . HIS A 1 221 ? 8.106   0.305   -5.128  1.00 39.36  ? 221 HIS A N     1 
ATOM   1729 C  CA    . HIS A 1 221 ? 6.960   1.013   -5.680  1.00 40.31  ? 221 HIS A CA    1 
ATOM   1730 C  C     . HIS A 1 221 ? 7.437   1.907   -6.814  1.00 43.94  ? 221 HIS A C     1 
ATOM   1731 O  O     . HIS A 1 221 ? 8.409   2.653   -6.652  1.00 44.02  ? 221 HIS A O     1 
ATOM   1732 C  CB    . HIS A 1 221 ? 6.249   1.852   -4.611  1.00 38.18  ? 221 HIS A CB    1 
ATOM   1733 C  CG    . HIS A 1 221 ? 5.887   1.080   -3.381  1.00 41.83  ? 221 HIS A CG    1 
ATOM   1734 N  ND1   . HIS A 1 221 ? 6.811   0.741   -2.417  1.00 43.98  ? 221 HIS A ND1   1 
ATOM   1735 C  CD2   . HIS A 1 221 ? 4.702   0.579   -2.959  1.00 36.83  ? 221 HIS A CD2   1 
ATOM   1736 C  CE1   . HIS A 1 221 ? 6.212   0.064   -1.454  1.00 44.20  ? 221 HIS A CE1   1 
ATOM   1737 N  NE2   . HIS A 1 221 ? 4.931   -0.047  -1.759  1.00 42.62  ? 221 HIS A NE2   1 
ATOM   1738 N  N     . LEU A 1 222 ? 6.759   1.824   -7.960  1.00 45.79  ? 222 LEU A N     1 
ATOM   1739 C  CA    . LEU A 1 222 ? 7.048   2.666   -9.121  1.00 46.03  ? 222 LEU A CA    1 
ATOM   1740 C  C     . LEU A 1 222 ? 5.760   3.384   -9.505  1.00 50.54  ? 222 LEU A C     1 
ATOM   1741 O  O     . LEU A 1 222 ? 5.026   2.940   -10.400 1.00 47.79  ? 222 LEU A O     1 
ATOM   1742 C  CB    . LEU A 1 222 ? 7.603   1.848   -10.289 1.00 47.91  ? 222 LEU A CB    1 
ATOM   1743 C  CG    . LEU A 1 222 ? 8.933   1.127   -10.049 1.00 48.00  ? 222 LEU A CG    1 
ATOM   1744 C  CD1   . LEU A 1 222 ? 8.738   -0.088  -9.157  1.00 46.13  ? 222 LEU A CD1   1 
ATOM   1745 C  CD2   . LEU A 1 222 ? 9.592   0.733   -11.366 1.00 49.98  ? 222 LEU A CD2   1 
ATOM   1746 N  N     . PRO A 1 223 ? 5.450   4.502   -8.840  1.00 44.80  ? 223 PRO A N     1 
ATOM   1747 C  CA    . PRO A 1 223 ? 4.185   5.198   -9.136  1.00 48.01  ? 223 PRO A CA    1 
ATOM   1748 C  C     . PRO A 1 223 ? 4.048   5.622   -10.588 1.00 50.77  ? 223 PRO A C     1 
ATOM   1749 O  O     . PRO A 1 223 ? 2.961   5.489   -11.163 1.00 54.47  ? 223 PRO A O     1 
ATOM   1750 C  CB    . PRO A 1 223 ? 4.221   6.406   -8.187  1.00 48.85  ? 223 PRO A CB    1 
ATOM   1751 C  CG    . PRO A 1 223 ? 5.660   6.555   -7.791  1.00 50.48  ? 223 PRO A CG    1 
ATOM   1752 C  CD    . PRO A 1 223 ? 6.213   5.168   -7.772  1.00 46.30  ? 223 PRO A CD    1 
ATOM   1753 N  N     . ASP A 1 224 ? 5.120   6.132   -11.201 1.00 50.66  ? 224 ASP A N     1 
ATOM   1754 C  CA    . ASP A 1 224 ? 5.030   6.573   -12.590 1.00 59.72  ? 224 ASP A CA    1 
ATOM   1755 C  C     . ASP A 1 224 ? 4.566   5.442   -13.500 1.00 59.88  ? 224 ASP A C     1 
ATOM   1756 O  O     . ASP A 1 224 ? 3.800   5.671   -14.444 1.00 63.57  ? 224 ASP A O     1 
ATOM   1757 C  CB    . ASP A 1 224 ? 6.379   7.119   -13.059 1.00 66.93  ? 224 ASP A CB    1 
ATOM   1758 C  CG    . ASP A 1 224 ? 6.866   8.276   -12.211 1.00 69.21  ? 224 ASP A CG    1 
ATOM   1759 O  OD1   . ASP A 1 224 ? 6.021   9.052   -11.717 1.00 64.84  ? 224 ASP A OD1   1 
ATOM   1760 O  OD2   . ASP A 1 224 ? 8.096   8.408   -12.036 1.00 79.21  ? 224 ASP A OD2   1 
ATOM   1761 N  N     . ARG A 1 225 ? 5.014   4.218   -13.232 1.00 55.23  ? 225 ARG A N     1 
ATOM   1762 C  CA    . ARG A 1 225 ? 4.644   3.054   -14.026 1.00 58.81  ? 225 ARG A CA    1 
ATOM   1763 C  C     . ARG A 1 225 ? 3.478   2.277   -13.433 1.00 59.26  ? 225 ARG A C     1 
ATOM   1764 O  O     . ARG A 1 225 ? 3.073   1.260   -14.007 1.00 54.43  ? 225 ARG A O     1 
ATOM   1765 C  CB    . ARG A 1 225 ? 5.854   2.127   -14.196 1.00 59.99  ? 225 ARG A CB    1 
ATOM   1766 C  CG    . ARG A 1 225 ? 6.955   2.701   -15.073 1.00 68.74  ? 225 ARG A CG    1 
ATOM   1767 C  CD    . ARG A 1 225 ? 8.280   1.994   -14.845 1.00 74.77  ? 225 ARG A CD    1 
ATOM   1768 N  NE    . ARG A 1 225 ? 8.205   0.564   -15.119 1.00 79.59  ? 225 ARG A NE    1 
ATOM   1769 C  CZ    . ARG A 1 225 ? 8.558   0.001   -16.267 1.00 83.03  ? 225 ARG A CZ    1 
ATOM   1770 N  NH1   . ARG A 1 225 ? 9.012   0.721   -17.279 1.00 85.93  ? 225 ARG A NH1   1 
ATOM   1771 N  NH2   . ARG A 1 225 ? 8.453   -1.318  -16.401 1.00 81.29  ? 225 ARG A NH2   1 
ATOM   1772 N  N     . ARG A 1 226 ? 2.930   2.725   -12.302 1.00 52.48  ? 226 ARG A N     1 
ATOM   1773 C  CA    . ARG A 1 226 ? 1.776   2.078   -11.680 1.00 53.14  ? 226 ARG A CA    1 
ATOM   1774 C  C     . ARG A 1 226 ? 2.081   0.632   -11.296 1.00 52.11  ? 226 ARG A C     1 
ATOM   1775 O  O     . ARG A 1 226 ? 1.207   -0.237  -11.351 1.00 43.37  ? 226 ARG A O     1 
ATOM   1776 C  CB    . ARG A 1 226 ? 0.550   2.143   -12.598 1.00 58.85  ? 226 ARG A CB    1 
ATOM   1777 C  CG    . ARG A 1 226 ? 0.174   3.548   -13.061 1.00 64.61  ? 226 ARG A CG    1 
ATOM   1778 C  CD    . ARG A 1 226 ? -0.451  4.370   -11.941 1.00 63.23  ? 226 ARG A CD    1 
ATOM   1779 N  NE    . ARG A 1 226 ? -1.114  5.566   -12.450 1.00 73.31  ? 226 ARG A NE    1 
ATOM   1780 C  CZ    . ARG A 1 226 ? -0.606  6.790   -12.404 1.00 71.70  ? 226 ARG A CZ    1 
ATOM   1781 N  NH1   . ARG A 1 226 ? 0.573   7.029   -11.856 1.00 62.71  ? 226 ARG A NH1   1 
ATOM   1782 N  NH2   . ARG A 1 226 ? -1.303  7.802   -12.915 1.00 72.53  ? 226 ARG A NH2   1 
ATOM   1783 N  N     . GLU A 1 227 ? 3.322   0.360   -10.901 1.00 50.31  ? 227 GLU A N     1 
ATOM   1784 C  CA    . GLU A 1 227 ? 3.779   -0.993  -10.626 1.00 44.37  ? 227 GLU A CA    1 
ATOM   1785 C  C     . GLU A 1 227 ? 4.223   -1.122  -9.178  1.00 41.00  ? 227 GLU A C     1 
ATOM   1786 O  O     . GLU A 1 227 ? 4.886   -0.231  -8.639  1.00 42.83  ? 227 GLU A O     1 
ATOM   1787 C  CB    . GLU A 1 227 ? 4.939   -1.388  -11.550 1.00 48.69  ? 227 GLU A CB    1 
ATOM   1788 C  CG    . GLU A 1 227 ? 4.548   -1.602  -13.000 1.00 59.01  ? 227 GLU A CG    1 
ATOM   1789 C  CD    . GLU A 1 227 ? 5.709   -2.095  -13.843 1.00 58.10  ? 227 GLU A CD    1 
ATOM   1790 O  OE1   . GLU A 1 227 ? 6.853   -2.096  -13.336 1.00 54.07  ? 227 GLU A OE1   1 
ATOM   1791 O  OE2   . GLU A 1 227 ? 5.479   -2.484  -15.008 1.00 73.33  ? 227 GLU A OE2   1 
ATOM   1792 N  N     . ILE A 1 228 ? 3.846   -2.233  -8.552  1.00 39.53  ? 228 ILE A N     1 
ATOM   1793 C  CA    . ILE A 1 228 ? 4.364   -2.636  -7.250  1.00 39.79  ? 228 ILE A CA    1 
ATOM   1794 C  C     . ILE A 1 228 ? 5.099   -3.954  -7.442  1.00 35.83  ? 228 ILE A C     1 
ATOM   1795 O  O     . ILE A 1 228 ? 4.540   -4.902  -8.006  1.00 33.90  ? 228 ILE A O     1 
ATOM   1796 C  CB    . ILE A 1 228 ? 3.246   -2.776  -6.200  1.00 39.76  ? 228 ILE A CB    1 
ATOM   1797 C  CG1   . ILE A 1 228 ? 2.511   -1.447  -6.026  1.00 42.99  ? 228 ILE A CG1   1 
ATOM   1798 C  CG2   . ILE A 1 228 ? 3.819   -3.244  -4.870  1.00 40.22  ? 228 ILE A CG2   1 
ATOM   1799 C  CD1   . ILE A 1 228 ? 1.299   -1.530  -5.125  1.00 36.41  ? 228 ILE A CD1   1 
ATOM   1800 N  N     . ILE A 1 229 ? 6.348   -4.011  -6.989  1.00 35.75  ? 229 ILE A N     1 
ATOM   1801 C  CA    . ILE A 1 229 ? 7.199   -5.180  -7.180  1.00 37.65  ? 229 ILE A CA    1 
ATOM   1802 C  C     . ILE A 1 229 ? 7.773   -5.571  -5.826  1.00 38.23  ? 229 ILE A C     1 
ATOM   1803 O  O     . ILE A 1 229 ? 8.551   -4.811  -5.235  1.00 40.98  ? 229 ILE A O     1 
ATOM   1804 C  CB    . ILE A 1 229 ? 8.320   -4.911  -8.200  1.00 39.18  ? 229 ILE A CB    1 
ATOM   1805 C  CG1   . ILE A 1 229 ? 7.717   -4.419  -9.520  1.00 37.88  ? 229 ILE A CG1   1 
ATOM   1806 C  CG2   . ILE A 1 229 ? 9.155   -6.163  -8.430  1.00 34.53  ? 229 ILE A CG2   1 
ATOM   1807 C  CD1   . ILE A 1 229 ? 8.734   -4.049  -10.574 1.00 40.64  ? 229 ILE A CD1   1 
ATOM   1808 N  N     . SER A 1 230 ? 7.399   -6.755  -5.342  1.00 38.82  ? 230 SER A N     1 
ATOM   1809 C  CA    . SER A 1 230 ? 7.758   -7.221  -4.009  1.00 38.51  ? 230 SER A CA    1 
ATOM   1810 C  C     . SER A 1 230 ? 8.391   -8.603  -4.105  1.00 38.71  ? 230 SER A C     1 
ATOM   1811 O  O     . SER A 1 230 ? 7.859   -9.486  -4.787  1.00 38.31  ? 230 SER A O     1 
ATOM   1812 C  CB    . SER A 1 230 ? 6.526   -7.261  -3.098  1.00 40.85  ? 230 SER A CB    1 
ATOM   1813 O  OG    . SER A 1 230 ? 6.880   -7.622  -1.776  1.00 42.35  ? 230 SER A OG    1 
ATOM   1814 N  N     . PHE A 1 231 ? 9.512   -8.792  -3.408  1.00 38.50  ? 231 PHE A N     1 
ATOM   1815 C  CA    . PHE A 1 231 ? 10.296  -10.015 -3.517  1.00 40.98  ? 231 PHE A CA    1 
ATOM   1816 C  C     . PHE A 1 231 ? 10.800  -10.450 -2.149  1.00 44.14  ? 231 PHE A C     1 
ATOM   1817 O  O     . PHE A 1 231 ? 11.238  -9.619  -1.350  1.00 44.81  ? 231 PHE A O     1 
ATOM   1818 C  CB    . PHE A 1 231 ? 11.489  -9.816  -4.464  1.00 44.47  ? 231 PHE A CB    1 
ATOM   1819 C  CG    . PHE A 1 231 ? 12.298  -11.062 -4.702  1.00 44.08  ? 231 PHE A CG    1 
ATOM   1820 C  CD1   . PHE A 1 231 ? 13.364  -11.384 -3.876  1.00 45.86  ? 231 PHE A CD1   1 
ATOM   1821 C  CD2   . PHE A 1 231 ? 12.004  -11.899 -5.761  1.00 43.96  ? 231 PHE A CD2   1 
ATOM   1822 C  CE1   . PHE A 1 231 ? 14.107  -12.522 -4.098  1.00 46.49  ? 231 PHE A CE1   1 
ATOM   1823 C  CE2   . PHE A 1 231 ? 12.747  -13.039 -5.989  1.00 48.02  ? 231 PHE A CE2   1 
ATOM   1824 C  CZ    . PHE A 1 231 ? 13.800  -13.352 -5.154  1.00 48.39  ? 231 PHE A CZ    1 
ATOM   1825 N  N     . GLY A 1 232 ? 10.737  -11.757 -1.887  1.00 42.92  ? 232 GLY A N     1 
ATOM   1826 C  CA    . GLY A 1 232 ? 11.423  -12.369 -0.771  1.00 46.56  ? 232 GLY A CA    1 
ATOM   1827 C  C     . GLY A 1 232 ? 10.577  -12.623 0.462   1.00 50.72  ? 232 GLY A C     1 
ATOM   1828 O  O     . GLY A 1 232 ? 10.931  -13.496 1.265   1.00 55.10  ? 232 GLY A O     1 
ATOM   1829 N  N     . SER A 1 233 ? 9.487   -11.888 0.646   1.00 46.49  ? 233 SER A N     1 
ATOM   1830 C  CA    . SER A 1 233 ? 8.665   -12.005 1.841   1.00 50.80  ? 233 SER A CA    1 
ATOM   1831 C  C     . SER A 1 233 ? 7.263   -12.468 1.475   1.00 51.03  ? 233 SER A C     1 
ATOM   1832 O  O     . SER A 1 233 ? 6.697   -12.034 0.468   1.00 43.69  ? 233 SER A O     1 
ATOM   1833 C  CB    . SER A 1 233 ? 8.592   -10.674 2.594   1.00 50.76  ? 233 SER A CB    1 
ATOM   1834 O  OG    . SER A 1 233 ? 7.724   -10.773 3.708   1.00 49.96  ? 233 SER A OG    1 
ATOM   1835 N  N     . GLY A 1 234 ? 6.707   -13.352 2.296   1.00 51.38  ? 234 GLY A N     1 
ATOM   1836 C  CA    . GLY A 1 234 ? 5.331   -13.769 2.156   1.00 44.44  ? 234 GLY A CA    1 
ATOM   1837 C  C     . GLY A 1 234 ? 4.401   -13.198 3.197   1.00 47.26  ? 234 GLY A C     1 
ATOM   1838 O  O     . GLY A 1 234 ? 3.232   -13.596 3.254   1.00 46.50  ? 234 GLY A O     1 
ATOM   1839 N  N     . TYR A 1 235 ? 4.874   -12.260 4.011   1.00 45.54  ? 235 TYR A N     1 
ATOM   1840 C  CA    . TYR A 1 235 ? 4.145   -11.813 5.187   1.00 49.16  ? 235 TYR A CA    1 
ATOM   1841 C  C     . TYR A 1 235 ? 3.386   -10.520 4.904   1.00 47.97  ? 235 TYR A C     1 
ATOM   1842 O  O     . TYR A 1 235 ? 3.927   -9.589  4.293   1.00 49.11  ? 235 TYR A O     1 
ATOM   1843 C  CB    . TYR A 1 235 ? 5.100   -11.607 6.361   1.00 51.62  ? 235 TYR A CB    1 
ATOM   1844 C  CG    . TYR A 1 235 ? 4.398   -11.633 7.694   1.00 53.27  ? 235 TYR A CG    1 
ATOM   1845 C  CD1   . TYR A 1 235 ? 3.888   -10.473 8.253   1.00 49.25  ? 235 TYR A CD1   1 
ATOM   1846 C  CD2   . TYR A 1 235 ? 4.223   -12.825 8.385   1.00 47.27  ? 235 TYR A CD2   1 
ATOM   1847 C  CE1   . TYR A 1 235 ? 3.234   -10.494 9.471   1.00 50.81  ? 235 TYR A CE1   1 
ATOM   1848 C  CE2   . TYR A 1 235 ? 3.571   -12.857 9.602   1.00 49.71  ? 235 TYR A CE2   1 
ATOM   1849 C  CZ    . TYR A 1 235 ? 3.079   -11.689 10.140  1.00 54.20  ? 235 TYR A CZ    1 
ATOM   1850 O  OH    . TYR A 1 235 ? 2.429   -11.718 11.353  1.00 51.07  ? 235 TYR A OH    1 
ATOM   1851 N  N     . GLY A 1 236 ? 2.131   -10.477 5.349   1.00 42.22  ? 236 GLY A N     1 
ATOM   1852 C  CA    . GLY A 1 236 ? 1.286   -9.296  5.365   1.00 47.29  ? 236 GLY A CA    1 
ATOM   1853 C  C     . GLY A 1 236 ? 1.596   -8.182  4.387   1.00 46.70  ? 236 GLY A C     1 
ATOM   1854 O  O     . GLY A 1 236 ? 1.443   -8.346  3.174   1.00 49.17  ? 236 GLY A O     1 
ATOM   1855 N  N     . GLY A 1 237 ? 2.025   -7.032  4.918   1.00 44.23  ? 237 GLY A N     1 
ATOM   1856 C  CA    . GLY A 1 237 ? 2.196   -5.852  4.088   1.00 45.02  ? 237 GLY A CA    1 
ATOM   1857 C  C     . GLY A 1 237 ? 3.158   -6.053  2.937   1.00 46.64  ? 237 GLY A C     1 
ATOM   1858 O  O     . GLY A 1 237 ? 3.073   -5.354  1.923   1.00 48.12  ? 237 GLY A O     1 
ATOM   1859 N  N     . ASN A 1 238 ? 4.080   -7.008  3.071   1.00 46.07  ? 238 ASN A N     1 
ATOM   1860 C  CA    . ASN A 1 238 ? 5.050   -7.265  2.015   1.00 46.69  ? 238 ASN A CA    1 
ATOM   1861 C  C     . ASN A 1 238 ? 4.438   -8.013  0.836   1.00 48.44  ? 238 ASN A C     1 
ATOM   1862 O  O     . ASN A 1 238 ? 4.894   -7.843  -0.300  1.00 47.48  ? 238 ASN A O     1 
ATOM   1863 C  CB    . ASN A 1 238 ? 6.232   -8.062  2.572   1.00 44.21  ? 238 ASN A CB    1 
ATOM   1864 C  CG    . ASN A 1 238 ? 6.899   -7.377  3.749   1.00 48.07  ? 238 ASN A CG    1 
ATOM   1865 O  OD1   . ASN A 1 238 ? 6.903   -6.151  3.852   1.00 52.44  ? 238 ASN A OD1   1 
ATOM   1866 N  ND2   . ASN A 1 238 ? 7.478   -8.173  4.642   1.00 52.61  ? 238 ASN A ND2   1 
ATOM   1867 N  N     . SER A 1 239 ? 3.417   -8.837  1.081   1.00 46.18  ? 239 SER A N     1 
ATOM   1868 C  CA    . SER A 1 239 ? 2.871   -9.731  0.067   1.00 39.45  ? 239 SER A CA    1 
ATOM   1869 C  C     . SER A 1 239 ? 1.432   -9.426  -0.324  1.00 43.52  ? 239 SER A C     1 
ATOM   1870 O  O     . SER A 1 239 ? 1.068   -9.645  -1.482  1.00 40.22  ? 239 SER A O     1 
ATOM   1871 C  CB    . SER A 1 239 ? 2.959   -11.188 0.541   1.00 41.01  ? 239 SER A CB    1 
ATOM   1872 O  OG    . SER A 1 239 ? 2.168   -11.398 1.697   1.00 44.39  ? 239 SER A OG    1 
ATOM   1873 N  N     . LEU A 1 240 ? 0.600   -8.948  0.600   1.00 45.20  ? 240 LEU A N     1 
ATOM   1874 C  CA    . LEU A 1 240 ? -0.745  -8.486  0.257   1.00 44.36  ? 240 LEU A CA    1 
ATOM   1875 C  C     . LEU A 1 240 ? -0.595  -7.076  -0.301  1.00 40.14  ? 240 LEU A C     1 
ATOM   1876 O  O     . LEU A 1 240 ? -0.721  -6.077  0.409   1.00 43.09  ? 240 LEU A O     1 
ATOM   1877 C  CB    . LEU A 1 240 ? -1.664  -8.532  1.471   1.00 45.16  ? 240 LEU A CB    1 
ATOM   1878 C  CG    . LEU A 1 240 ? -1.639  -9.818  2.304   1.00 41.26  ? 240 LEU A CG    1 
ATOM   1879 C  CD1   . LEU A 1 240 ? -2.665  -9.761  3.427   1.00 46.38  ? 240 LEU A CD1   1 
ATOM   1880 C  CD2   . LEU A 1 240 ? -1.866  -11.050 1.435   1.00 36.00  ? 240 LEU A CD2   1 
ATOM   1881 N  N     . LEU A 1 241 ? -0.316  -7.000  -1.603  1.00 39.69  ? 241 LEU A N     1 
ATOM   1882 C  CA    . LEU A 1 241 ? 0.143   -5.749  -2.195  1.00 45.95  ? 241 LEU A CA    1 
ATOM   1883 C  C     . LEU A 1 241 ? -0.953  -4.697  -2.298  1.00 39.02  ? 241 LEU A C     1 
ATOM   1884 O  O     . LEU A 1 241 ? -0.642  -3.522  -2.520  1.00 42.81  ? 241 LEU A O     1 
ATOM   1885 C  CB    . LEU A 1 241 ? 0.747   -6.015  -3.571  1.00 36.28  ? 241 LEU A CB    1 
ATOM   1886 C  CG    . LEU A 1 241 ? 1.982   -6.913  -3.526  1.00 40.83  ? 241 LEU A CG    1 
ATOM   1887 C  CD1   . LEU A 1 241 ? 2.681   -6.943  -4.873  1.00 33.23  ? 241 LEU A CD1   1 
ATOM   1888 C  CD2   . LEU A 1 241 ? 2.926   -6.448  -2.427  1.00 40.18  ? 241 LEU A CD2   1 
ATOM   1889 N  N     . GLY A 1 242 ? -2.220  -5.081  -2.147  1.00 45.59  ? 242 GLY A N     1 
ATOM   1890 C  CA    . GLY A 1 242 ? -3.282  -4.091  -2.185  1.00 43.55  ? 242 GLY A CA    1 
ATOM   1891 C  C     . GLY A 1 242 ? -3.390  -3.251  -0.930  1.00 41.26  ? 242 GLY A C     1 
ATOM   1892 O  O     . GLY A 1 242 ? -3.929  -2.140  -0.986  1.00 49.94  ? 242 GLY A O     1 
ATOM   1893 N  N     . LYS A 1 243 ? -2.875  -3.746  0.194   1.00 41.50  ? 243 LYS A N     1 
ATOM   1894 C  CA    . LYS A 1 243 ? -3.052  -3.088  1.483   1.00 46.75  ? 243 LYS A CA    1 
ATOM   1895 C  C     . LYS A 1 243 ? -2.206  -1.826  1.616   1.00 43.32  ? 243 LYS A C     1 
ATOM   1896 O  O     . LYS A 1 243 ? -2.698  -0.714  1.397   1.00 49.25  ? 243 LYS A O     1 
ATOM   1897 C  CB    . LYS A 1 243 ? -2.725  -4.066  2.612   1.00 45.81  ? 243 LYS A CB    1 
ATOM   1898 C  CG    . LYS A 1 243 ? -3.082  -3.559  3.994   1.00 50.04  ? 243 LYS A CG    1 
ATOM   1899 C  CD    . LYS A 1 243 ? -3.096  -4.695  5.000   1.00 42.78  ? 243 LYS A CD    1 
ATOM   1900 C  CE    . LYS A 1 243 ? -3.488  -4.193  6.377   1.00 43.50  ? 243 LYS A CE    1 
ATOM   1901 N  NZ    . LYS A 1 243 ? -4.767  -3.433  6.340   1.00 40.42  ? 243 LYS A NZ    1 
ATOM   1902 N  N     . LYS A 1 244 ? -0.936  -1.983  1.990   1.00 44.09  ? 244 LYS A N     1 
ATOM   1903 C  CA    . LYS A 1 244 ? -0.071  -0.824  2.185   1.00 34.77  ? 244 LYS A CA    1 
ATOM   1904 C  C     . LYS A 1 244 ? 0.498   -0.321  0.864   1.00 40.24  ? 244 LYS A C     1 
ATOM   1905 O  O     . LYS A 1 244 ? 0.379   0.866   0.541   1.00 36.89  ? 244 LYS A O     1 
ATOM   1906 C  CB    . LYS A 1 244 ? 1.063   -1.169  3.152   1.00 39.70  ? 244 LYS A CB    1 
ATOM   1907 C  CG    . LYS A 1 244 ? 0.600   -1.661  4.513   1.00 42.65  ? 244 LYS A CG    1 
ATOM   1908 C  CD    . LYS A 1 244 ? -0.330  -0.663  5.185   1.00 39.18  ? 244 LYS A CD    1 
ATOM   1909 C  CE    . LYS A 1 244 ? -0.612  -1.063  6.625   1.00 40.38  ? 244 LYS A CE    1 
ATOM   1910 N  NZ    . LYS A 1 244 ? -1.493  -0.071  7.301   1.00 42.82  ? 244 LYS A NZ    1 
ATOM   1911 N  N     . CYS A 1 245 ? 1.124   -1.211  0.092   1.00 36.01  ? 245 CYS A N     1 
ATOM   1912 C  CA    . CYS A 1 245 ? 1.769   -0.798  -1.152  1.00 38.00  ? 245 CYS A CA    1 
ATOM   1913 C  C     . CYS A 1 245 ? 0.785   -0.085  -2.074  1.00 38.23  ? 245 CYS A C     1 
ATOM   1914 O  O     . CYS A 1 245 ? 1.068   1.008   -2.579  1.00 41.78  ? 245 CYS A O     1 
ATOM   1915 C  CB    . CYS A 1 245 ? 2.381   -2.015  -1.849  1.00 35.60  ? 245 CYS A CB    1 
ATOM   1916 S  SG    . CYS A 1 245 ? 3.546   -2.960  -0.836  1.00 42.78  ? 245 CYS A SG    1 
ATOM   1917 N  N     . PHE A 1 246 ? -0.385  -0.689  -2.297  1.00 37.09  ? 246 PHE A N     1 
ATOM   1918 C  CA    . PHE A 1 246 ? -1.387  -0.122  -3.197  1.00 40.93  ? 246 PHE A CA    1 
ATOM   1919 C  C     . PHE A 1 246 ? -2.214  0.953   -2.497  1.00 43.28  ? 246 PHE A C     1 
ATOM   1920 O  O     . PHE A 1 246 ? -2.202  2.122   -2.899  1.00 42.90  ? 246 PHE A O     1 
ATOM   1921 C  CB    . PHE A 1 246 ? -2.287  -1.249  -3.725  1.00 39.37  ? 246 PHE A CB    1 
ATOM   1922 C  CG    . PHE A 1 246 ? -3.292  -0.825  -4.785  1.00 42.76  ? 246 PHE A CG    1 
ATOM   1923 C  CD1   . PHE A 1 246 ? -3.615  0.508   -5.007  1.00 41.12  ? 246 PHE A CD1   1 
ATOM   1924 C  CD2   . PHE A 1 246 ? -3.925  -1.789  -5.557  1.00 45.89  ? 246 PHE A CD2   1 
ATOM   1925 C  CE1   . PHE A 1 246 ? -4.542  0.865   -5.977  1.00 52.05  ? 246 PHE A CE1   1 
ATOM   1926 C  CE2   . PHE A 1 246 ? -4.849  -1.438  -6.527  1.00 48.27  ? 246 PHE A CE2   1 
ATOM   1927 C  CZ    . PHE A 1 246 ? -5.158  -0.109  -6.736  1.00 54.04  ? 246 PHE A CZ    1 
ATOM   1928 N  N     . ALA A 1 247 ? -2.953  0.569   -1.453  1.00 43.66  ? 247 ALA A N     1 
ATOM   1929 C  CA    . ALA A 1 247 ? -3.974  1.446   -0.890  1.00 45.31  ? 247 ALA A CA    1 
ATOM   1930 C  C     . ALA A 1 247 ? -3.400  2.695   -0.233  1.00 39.56  ? 247 ALA A C     1 
ATOM   1931 O  O     . ALA A 1 247 ? -4.143  3.661   -0.027  1.00 42.78  ? 247 ALA A O     1 
ATOM   1932 C  CB    . ALA A 1 247 ? -4.823  0.679   0.123   1.00 42.76  ? 247 ALA A CB    1 
ATOM   1933 N  N     . LEU A 1 248 ? -2.112  2.712   0.107   1.00 43.69  ? 248 LEU A N     1 
ATOM   1934 C  CA    . LEU A 1 248 ? -1.526  3.859   0.790   1.00 43.01  ? 248 LEU A CA    1 
ATOM   1935 C  C     . LEU A 1 248 ? -0.422  4.520   -0.026  1.00 42.39  ? 248 LEU A C     1 
ATOM   1936 O  O     . LEU A 1 248 ? -0.530  5.702   -0.365  1.00 43.28  ? 248 LEU A O     1 
ATOM   1937 C  CB    . LEU A 1 248 ? -1.007  3.437   2.174   1.00 39.81  ? 248 LEU A CB    1 
ATOM   1938 C  CG    . LEU A 1 248 ? -2.082  3.274   3.255   1.00 45.00  ? 248 LEU A CG    1 
ATOM   1939 C  CD1   . LEU A 1 248 ? -1.461  2.960   4.611   1.00 41.53  ? 248 LEU A CD1   1 
ATOM   1940 C  CD2   . LEU A 1 248 ? -2.960  4.517   3.339   1.00 36.81  ? 248 LEU A CD2   1 
ATOM   1941 N  N     . ARG A 1 249 ? 0.638   3.786   -0.371  1.00 39.72  ? 249 ARG A N     1 
ATOM   1942 C  CA    . ARG A 1 249 ? 1.775   4.408   -1.044  1.00 43.00  ? 249 ARG A CA    1 
ATOM   1943 C  C     . ARG A 1 249 ? 1.423   4.814   -2.472  1.00 37.53  ? 249 ARG A C     1 
ATOM   1944 O  O     . ARG A 1 249 ? 1.476   5.998   -2.823  1.00 44.06  ? 249 ARG A O     1 
ATOM   1945 C  CB    . ARG A 1 249 ? 2.975   3.463   -1.014  1.00 44.40  ? 249 ARG A CB    1 
ATOM   1946 C  CG    . ARG A 1 249 ? 3.421   3.148   0.404   1.00 45.00  ? 249 ARG A CG    1 
ATOM   1947 C  CD    . ARG A 1 249 ? 4.834   2.609   0.458   1.00 44.51  ? 249 ARG A CD    1 
ATOM   1948 N  NE    . ARG A 1 249 ? 5.128   2.075   1.781   1.00 47.76  ? 249 ARG A NE    1 
ATOM   1949 C  CZ    . ARG A 1 249 ? 4.937   0.811   2.133   1.00 44.52  ? 249 ARG A CZ    1 
ATOM   1950 N  NH1   . ARG A 1 249 ? 4.487   -0.085  1.269   1.00 43.07  ? 249 ARG A NH1   1 
ATOM   1951 N  NH2   . ARG A 1 249 ? 5.198   0.438   3.382   1.00 48.58  ? 249 ARG A NH2   1 
ATOM   1952 N  N     . ILE A 1 250 ? 1.066   3.846   -3.317  1.00 44.89  ? 250 ILE A N     1 
ATOM   1953 C  CA    . ILE A 1 250 ? 0.639   4.178   -4.674  1.00 45.65  ? 250 ILE A CA    1 
ATOM   1954 C  C     . ILE A 1 250 ? -0.566  5.109   -4.632  1.00 46.49  ? 250 ILE A C     1 
ATOM   1955 O  O     . ILE A 1 250 ? -0.632  6.105   -5.362  1.00 45.42  ? 250 ILE A O     1 
ATOM   1956 C  CB    . ILE A 1 250 ? 0.337   2.898   -5.475  1.00 45.84  ? 250 ILE A CB    1 
ATOM   1957 C  CG1   . ILE A 1 250 ? 1.625   2.125   -5.761  1.00 39.83  ? 250 ILE A CG1   1 
ATOM   1958 C  CG2   . ILE A 1 250 ? -0.389  3.239   -6.767  1.00 46.45  ? 250 ILE A CG2   1 
ATOM   1959 C  CD1   . ILE A 1 250 ? 2.679   2.931   -6.492  1.00 40.82  ? 250 ILE A CD1   1 
ATOM   1960 N  N     . ALA A 1 251 ? -1.531  4.805   -3.760  1.00 48.06  ? 251 ALA A N     1 
ATOM   1961 C  CA    . ALA A 1 251 ? -2.786  5.551   -3.743  1.00 47.43  ? 251 ALA A CA    1 
ATOM   1962 C  C     . ALA A 1 251 ? -2.578  6.995   -3.302  1.00 39.94  ? 251 ALA A C     1 
ATOM   1963 O  O     . ALA A 1 251 ? -3.198  7.911   -3.853  1.00 41.81  ? 251 ALA A O     1 
ATOM   1964 C  CB    . ALA A 1 251 ? -3.796  4.851   -2.834  1.00 43.92  ? 251 ALA A CB    1 
ATOM   1965 N  N     . SER A 1 252 ? -1.716  7.221   -2.308  1.00 42.31  ? 252 SER A N     1 
ATOM   1966 C  CA    . SER A 1 252 ? -1.474  8.586   -1.850  1.00 42.74  ? 252 SER A CA    1 
ATOM   1967 C  C     . SER A 1 252 ? -0.944  9.459   -2.981  1.00 45.29  ? 252 SER A C     1 
ATOM   1968 O  O     . SER A 1 252 ? -1.278  10.647  -3.068  1.00 40.93  ? 252 SER A O     1 
ATOM   1969 C  CB    . SER A 1 252 ? -0.501  8.583   -0.672  1.00 42.59  ? 252 SER A CB    1 
ATOM   1970 O  OG    . SER A 1 252 ? 0.784   8.145   -1.073  1.00 39.37  ? 252 SER A OG    1 
ATOM   1971 N  N     . ARG A 1 253 ? -0.112  8.887   -3.854  1.00 42.86  ? 253 ARG A N     1 
ATOM   1972 C  CA    . ARG A 1 253 ? 0.392   9.630   -5.006  1.00 44.77  ? 253 ARG A CA    1 
ATOM   1973 C  C     . ARG A 1 253 ? -0.728  9.922   -5.995  1.00 45.07  ? 253 ARG A C     1 
ATOM   1974 O  O     . ARG A 1 253 ? -0.857  11.048  -6.492  1.00 47.28  ? 253 ARG A O     1 
ATOM   1975 C  CB    . ARG A 1 253 ? 1.521   8.842   -5.676  1.00 45.60  ? 253 ARG A CB    1 
ATOM   1976 C  CG    . ARG A 1 253 ? 1.813   9.226   -7.121  1.00 56.79  ? 253 ARG A CG    1 
ATOM   1977 C  CD    . ARG A 1 253 ? 2.590   10.527  -7.238  1.00 49.66  ? 253 ARG A CD    1 
ATOM   1978 N  NE    . ARG A 1 253 ? 3.087   10.720  -8.597  1.00 65.37  ? 253 ARG A NE    1 
ATOM   1979 C  CZ    . ARG A 1 253 ? 4.327   10.461  -8.991  1.00 62.18  ? 253 ARG A CZ    1 
ATOM   1980 N  NH1   . ARG A 1 253 ? 5.246   10.026  -8.145  1.00 59.85  ? 253 ARG A NH1   1 
ATOM   1981 N  NH2   . ARG A 1 253 ? 4.655   10.649  -10.267 1.00 69.02  ? 253 ARG A NH2   1 
ATOM   1982 N  N     . LEU A 1 254 ? -1.549  8.913   -6.295  1.00 47.87  ? 254 LEU A N     1 
ATOM   1983 C  CA    . LEU A 1 254 ? -2.689  9.125   -7.180  1.00 47.74  ? 254 LEU A CA    1 
ATOM   1984 C  C     . LEU A 1 254 ? -3.648  10.157  -6.600  1.00 48.12  ? 254 LEU A C     1 
ATOM   1985 O  O     . LEU A 1 254 ? -4.133  11.038  -7.320  1.00 51.48  ? 254 LEU A O     1 
ATOM   1986 C  CB    . LEU A 1 254 ? -3.413  7.800   -7.430  1.00 50.93  ? 254 LEU A CB    1 
ATOM   1987 C  CG    . LEU A 1 254 ? -2.616  6.669   -8.084  1.00 55.35  ? 254 LEU A CG    1 
ATOM   1988 C  CD1   . LEU A 1 254 ? -3.458  5.406   -8.205  1.00 56.47  ? 254 LEU A CD1   1 
ATOM   1989 C  CD2   . LEU A 1 254 ? -2.097  7.095   -9.447  1.00 54.35  ? 254 LEU A CD2   1 
ATOM   1990 N  N     . ALA A 1 255 ? -3.939  10.061  -5.299  1.00 47.25  ? 255 ALA A N     1 
ATOM   1991 C  CA    . ALA A 1 255 ? -4.834  11.030  -4.673  1.00 46.02  ? 255 ALA A CA    1 
ATOM   1992 C  C     . ALA A 1 255 ? -4.288  12.445  -4.808  1.00 46.60  ? 255 ALA A C     1 
ATOM   1993 O  O     . ALA A 1 255 ? -5.040  13.384  -5.096  1.00 48.50  ? 255 ALA A O     1 
ATOM   1994 C  CB    . ALA A 1 255 ? -5.055  10.672  -3.203  1.00 45.91  ? 255 ALA A CB    1 
ATOM   1995 N  N     . LYS A 1 256 ? -2.981  12.618  -4.603  1.00 46.15  ? 256 LYS A N     1 
ATOM   1996 C  CA    . LYS A 1 256 ? -2.369  13.924  -4.820  1.00 44.26  ? 256 LYS A CA    1 
ATOM   1997 C  C     . LYS A 1 256 ? -2.602  14.407  -6.246  1.00 49.34  ? 256 LYS A C     1 
ATOM   1998 O  O     . LYS A 1 256 ? -2.903  15.586  -6.470  1.00 53.46  ? 256 LYS A O     1 
ATOM   1999 C  CB    . LYS A 1 256 ? -0.873  13.857  -4.510  1.00 46.66  ? 256 LYS A CB    1 
ATOM   2000 C  CG    . LYS A 1 256 ? -0.101  15.112  -4.884  1.00 45.70  ? 256 LYS A CG    1 
ATOM   2001 C  CD    . LYS A 1 256 ? -0.605  16.330  -4.128  1.00 48.26  ? 256 LYS A CD    1 
ATOM   2002 C  CE    . LYS A 1 256 ? 0.169   17.573  -4.525  1.00 57.59  ? 256 LYS A CE    1 
ATOM   2003 N  NZ    . LYS A 1 256 ? 0.061   17.834  -5.983  1.00 64.67  ? 256 LYS A NZ    1 
ATOM   2004 N  N     . GLU A 1 257 ? -2.478  13.508  -7.224  1.00 48.66  ? 257 GLU A N     1 
ATOM   2005 C  CA    . GLU A 1 257 ? -2.681  13.900  -8.615  1.00 54.52  ? 257 GLU A CA    1 
ATOM   2006 C  C     . GLU A 1 257 ? -4.145  14.209  -8.899  1.00 54.30  ? 257 GLU A C     1 
ATOM   2007 O  O     . GLU A 1 257 ? -4.454  15.131  -9.662  1.00 52.63  ? 257 GLU A O     1 
ATOM   2008 C  CB    . GLU A 1 257 ? -2.185  12.796  -9.548  1.00 55.86  ? 257 GLU A CB    1 
ATOM   2009 C  CG    . GLU A 1 257 ? -0.705  12.486  -9.426  1.00 56.11  ? 257 GLU A CG    1 
ATOM   2010 C  CD    . GLU A 1 257 ? -0.316  11.229  -10.180 1.00 63.01  ? 257 GLU A CD    1 
ATOM   2011 O  OE1   . GLU A 1 257 ? -1.185  10.652  -10.867 1.00 62.01  ? 257 GLU A OE1   1 
ATOM   2012 O  OE2   . GLU A 1 257 ? 0.858   10.816  -10.083 1.00 64.94  ? 257 GLU A OE2   1 
ATOM   2013 N  N     . GLU A 1 258 ? -5.059  13.454  -8.292  1.00 48.47  ? 258 GLU A N     1 
ATOM   2014 C  CA    . GLU A 1 258 ? -6.469  13.488  -8.656  1.00 50.25  ? 258 GLU A CA    1 
ATOM   2015 C  C     . GLU A 1 258 ? -7.335  14.257  -7.666  1.00 50.23  ? 258 GLU A C     1 
ATOM   2016 O  O     . GLU A 1 258 ? -8.540  14.394  -7.898  1.00 50.42  ? 258 GLU A O     1 
ATOM   2017 C  CB    . GLU A 1 258 ? -6.995  12.058  -8.811  1.00 49.39  ? 258 GLU A CB    1 
ATOM   2018 C  CG    . GLU A 1 258 ? -6.209  11.242  -9.828  1.00 52.71  ? 258 GLU A CG    1 
ATOM   2019 C  CD    . GLU A 1 258 ? -6.529  9.764   -9.764  1.00 60.32  ? 258 GLU A CD    1 
ATOM   2020 O  OE1   . GLU A 1 258 ? -7.439  9.385   -9.001  1.00 57.90  ? 258 GLU A OE1   1 
ATOM   2021 O  OE2   . GLU A 1 258 ? -5.863  8.980   -10.475 1.00 65.29  ? 258 GLU A OE2   1 
ATOM   2022 N  N     . GLY A 1 259 ? -6.764  14.753  -6.573  1.00 47.81  ? 259 GLY A N     1 
ATOM   2023 C  CA    . GLY A 1 259 ? -7.491  15.629  -5.675  1.00 47.69  ? 259 GLY A CA    1 
ATOM   2024 C  C     . GLY A 1 259 ? -8.235  14.961  -4.541  1.00 47.69  ? 259 GLY A C     1 
ATOM   2025 O  O     . GLY A 1 259 ? -9.169  15.563  -4.000  1.00 51.33  ? 259 GLY A O     1 
ATOM   2026 N  N     . TRP A 1 260 ? -7.859  13.743  -4.158  1.00 48.75  ? 260 TRP A N     1 
ATOM   2027 C  CA    . TRP A 1 260 ? -8.465  13.108  -2.994  1.00 41.61  ? 260 TRP A CA    1 
ATOM   2028 C  C     . TRP A 1 260 ? -7.392  12.733  -1.980  1.00 40.90  ? 260 TRP A C     1 
ATOM   2029 O  O     . TRP A 1 260 ? -6.272  13.250  -2.041  1.00 43.22  ? 260 TRP A O     1 
ATOM   2030 C  CB    . TRP A 1 260 ? -9.288  11.882  -3.404  1.00 48.58  ? 260 TRP A CB    1 
ATOM   2031 C  CG    . TRP A 1 260 ? -8.613  10.951  -4.377  1.00 48.33  ? 260 TRP A CG    1 
ATOM   2032 C  CD1   . TRP A 1 260 ? -8.374  11.181  -5.703  1.00 48.41  ? 260 TRP A CD1   1 
ATOM   2033 C  CD2   . TRP A 1 260 ? -8.128  9.628   -4.107  1.00 43.57  ? 260 TRP A CD2   1 
ATOM   2034 N  NE1   . TRP A 1 260 ? -7.757  10.092  -6.268  1.00 46.01  ? 260 TRP A NE1   1 
ATOM   2035 C  CE2   . TRP A 1 260 ? -7.595  9.125   -5.311  1.00 50.05  ? 260 TRP A CE2   1 
ATOM   2036 C  CE3   . TRP A 1 260 ? -8.087  8.824   -2.963  1.00 44.77  ? 260 TRP A CE3   1 
ATOM   2037 C  CZ2   . TRP A 1 260 ? -7.028  7.856   -5.403  1.00 48.30  ? 260 TRP A CZ2   1 
ATOM   2038 C  CZ3   . TRP A 1 260 ? -7.525  7.562   -3.058  1.00 45.44  ? 260 TRP A CZ3   1 
ATOM   2039 C  CH2   . TRP A 1 260 ? -7.002  7.091   -4.269  1.00 43.44  ? 260 TRP A CH2   1 
ATOM   2040 N  N     . LEU A 1 261 ? -7.717  11.841  -1.047  1.00 45.82  ? 261 LEU A N     1 
ATOM   2041 C  CA    . LEU A 1 261 ? -6.806  11.491  0.033   1.00 40.71  ? 261 LEU A CA    1 
ATOM   2042 C  C     . LEU A 1 261 ? -6.809  9.988   0.259   1.00 42.08  ? 261 LEU A C     1 
ATOM   2043 O  O     . LEU A 1 261 ? -7.871  9.364   0.319   1.00 45.22  ? 261 LEU A O     1 
ATOM   2044 C  CB    . LEU A 1 261 ? -7.193  12.206  1.336   1.00 37.27  ? 261 LEU A CB    1 
ATOM   2045 C  CG    . LEU A 1 261 ? -7.332  13.728  1.296   1.00 39.42  ? 261 LEU A CG    1 
ATOM   2046 C  CD1   . LEU A 1 261 ? -7.943  14.240  2.590   1.00 36.79  ? 261 LEU A CD1   1 
ATOM   2047 C  CD2   . LEU A 1 261 ? -5.992  14.394  1.030   1.00 36.51  ? 261 LEU A CD2   1 
ATOM   2048 N  N     . ALA A 1 262 ? -5.614  9.414   0.389   1.00 41.68  ? 262 ALA A N     1 
ATOM   2049 C  CA    . ALA A 1 262 ? -5.432  8.019   0.782   1.00 39.24  ? 262 ALA A CA    1 
ATOM   2050 C  C     . ALA A 1 262 ? -4.690  8.022   2.111   1.00 37.57  ? 262 ALA A C     1 
ATOM   2051 O  O     . ALA A 1 262 ? -3.508  8.380   2.160   1.00 37.19  ? 262 ALA A O     1 
ATOM   2052 C  CB    . ALA A 1 262 ? -4.664  7.233   -0.282  1.00 35.96  ? 262 ALA A CB    1 
ATOM   2053 N  N     . GLU A 1 263 ? -5.372  7.621   3.182   1.00 36.72  ? 263 GLU A N     1 
ATOM   2054 C  CA    . GLU A 1 263 ? -4.892  7.872   4.533   1.00 38.99  ? 263 GLU A CA    1 
ATOM   2055 C  C     . GLU A 1 263 ? -4.914  6.605   5.380   1.00 38.93  ? 263 GLU A C     1 
ATOM   2056 O  O     . GLU A 1 263 ? -5.686  5.675   5.129   1.00 38.51  ? 263 GLU A O     1 
ATOM   2057 C  CB    . GLU A 1 263 ? -5.726  8.967   5.207   1.00 37.63  ? 263 GLU A CB    1 
ATOM   2058 C  CG    . GLU A 1 263 ? -5.662  10.311  4.492   1.00 35.90  ? 263 GLU A CG    1 
ATOM   2059 C  CD    . GLU A 1 263 ? -4.258  10.891  4.467   1.00 34.59  ? 263 GLU A CD    1 
ATOM   2060 O  OE1   . GLU A 1 263 ? -3.429  10.475  5.304   1.00 34.68  ? 263 GLU A OE1   1 
ATOM   2061 O  OE2   . GLU A 1 263 ? -3.980  11.758  3.614   1.00 39.00  ? 263 GLU A OE2   1 
ATOM   2062 N  N     . HIS A 1 264 ? -4.041  6.592   6.392   1.00 34.37  ? 264 HIS A N     1 
ATOM   2063 C  CA    . HIS A 1 264 ? -3.914  5.486   7.345   1.00 39.43  ? 264 HIS A CA    1 
ATOM   2064 C  C     . HIS A 1 264 ? -4.897  5.709   8.495   1.00 39.09  ? 264 HIS A C     1 
ATOM   2065 O  O     . HIS A 1 264 ? -4.531  6.010   9.633   1.00 31.22  ? 264 HIS A O     1 
ATOM   2066 C  CB    . HIS A 1 264 ? -2.474  5.388   7.839   1.00 36.39  ? 264 HIS A CB    1 
ATOM   2067 C  CG    . HIS A 1 264 ? -2.175  4.152   8.632   1.00 39.06  ? 264 HIS A CG    1 
ATOM   2068 N  ND1   . HIS A 1 264 ? -1.180  4.109   9.585   1.00 35.98  ? 264 HIS A ND1   1 
ATOM   2069 C  CD2   . HIS A 1 264 ? -2.718  2.912   8.598   1.00 37.68  ? 264 HIS A CD2   1 
ATOM   2070 C  CE1   . HIS A 1 264 ? -1.133  2.900   10.115  1.00 36.96  ? 264 HIS A CE1   1 
ATOM   2071 N  NE2   . HIS A 1 264 ? -2.056  2.154   9.534   1.00 40.35  ? 264 HIS A NE2   1 
ATOM   2072 N  N     . MET A 1 265 ? -6.179  5.562   8.169   1.00 36.08  ? 265 MET A N     1 
ATOM   2073 C  CA    . MET A 1 265 ? -7.240  5.940   9.088   1.00 35.45  ? 265 MET A CA    1 
ATOM   2074 C  C     . MET A 1 265 ? -8.313  4.866   9.152   1.00 37.89  ? 265 MET A C     1 
ATOM   2075 O  O     . MET A 1 265 ? -8.715  4.306   8.127   1.00 40.38  ? 265 MET A O     1 
ATOM   2076 C  CB    . MET A 1 265 ? -7.890  7.267   8.676   1.00 35.03  ? 265 MET A CB    1 
ATOM   2077 C  CG    . MET A 1 265 ? -6.980  8.474   8.779   1.00 35.79  ? 265 MET A CG    1 
ATOM   2078 S  SD    . MET A 1 265 ? -7.825  9.969   8.223   1.00 39.28  ? 265 MET A SD    1 
ATOM   2079 C  CE    . MET A 1 265 ? -6.548  11.193  8.496   1.00 33.90  ? 265 MET A CE    1 
ATOM   2080 N  N     . LEU A 1 266 ? -8.772  4.590   10.368  1.00 36.74  ? 266 LEU A N     1 
ATOM   2081 C  CA    . LEU A 1 266 ? -10.020 3.876   10.559  1.00 35.52  ? 266 LEU A CA    1 
ATOM   2082 C  C     . LEU A 1 266 ? -11.193 4.799   10.242  1.00 38.52  ? 266 LEU A C     1 
ATOM   2083 O  O     . LEU A 1 266 ? -11.080 6.028   10.280  1.00 36.83  ? 266 LEU A O     1 
ATOM   2084 C  CB    . LEU A 1 266 ? -10.135 3.368   11.997  1.00 37.30  ? 266 LEU A CB    1 
ATOM   2085 C  CG    . LEU A 1 266 ? -10.310 4.444   13.078  1.00 36.41  ? 266 LEU A CG    1 
ATOM   2086 C  CD1   . LEU A 1 266 ? -11.778 4.816   13.265  1.00 41.97  ? 266 LEU A CD1   1 
ATOM   2087 C  CD2   . LEU A 1 266 ? -9.694  4.003   14.397  1.00 33.82  ? 266 LEU A CD2   1 
ATOM   2088 N  N     . ILE A 1 267 ? -12.332 4.193   9.931   1.00 38.28  ? 267 ILE A N     1 
ATOM   2089 C  CA    . ILE A 1 267 ? -13.582 4.921   9.766   1.00 39.67  ? 267 ILE A CA    1 
ATOM   2090 C  C     . ILE A 1 267 ? -14.628 4.255   10.644  1.00 41.84  ? 267 ILE A C     1 
ATOM   2091 O  O     . ILE A 1 267 ? -14.808 3.033   10.582  1.00 43.08  ? 267 ILE A O     1 
ATOM   2092 C  CB    . ILE A 1 267 ? -14.051 4.952   8.300   1.00 40.21  ? 267 ILE A CB    1 
ATOM   2093 C  CG1   . ILE A 1 267 ? -12.938 5.483   7.395   1.00 42.45  ? 267 ILE A CG1   1 
ATOM   2094 C  CG2   . ILE A 1 267 ? -15.306 5.801   8.168   1.00 39.42  ? 267 ILE A CG2   1 
ATOM   2095 C  CD1   . ILE A 1 267 ? -13.208 5.271   5.922   1.00 40.02  ? 267 ILE A CD1   1 
ATOM   2096 N  N     . LEU A 1 268 ? -15.305 5.049   11.468  1.00 39.23  ? 268 LEU A N     1 
ATOM   2097 C  CA    . LEU A 1 268 ? -16.372 4.532   12.306  1.00 42.70  ? 268 LEU A CA    1 
ATOM   2098 C  C     . LEU A 1 268 ? -17.553 5.486   12.265  1.00 44.99  ? 268 LEU A C     1 
ATOM   2099 O  O     . LEU A 1 268 ? -17.388 6.704   12.144  1.00 42.06  ? 268 LEU A O     1 
ATOM   2100 C  CB    . LEU A 1 268 ? -15.912 4.323   13.759  1.00 42.33  ? 268 LEU A CB    1 
ATOM   2101 C  CG    . LEU A 1 268 ? -15.420 5.520   14.579  1.00 43.09  ? 268 LEU A CG    1 
ATOM   2102 C  CD1   . LEU A 1 268 ? -16.567 6.432   14.999  1.00 41.39  ? 268 LEU A CD1   1 
ATOM   2103 C  CD2   . LEU A 1 268 ? -14.663 5.024   15.798  1.00 43.39  ? 268 LEU A CD2   1 
ATOM   2104 N  N     . GLY A 1 269 ? -18.749 4.916   12.355  1.00 44.43  ? 269 GLY A N     1 
ATOM   2105 C  CA    . GLY A 1 269 ? -19.962 5.687   12.556  1.00 41.96  ? 269 GLY A CA    1 
ATOM   2106 C  C     . GLY A 1 269 ? -20.399 5.561   14.004  1.00 43.21  ? 269 GLY A C     1 
ATOM   2107 O  O     . GLY A 1 269 ? -20.341 4.478   14.588  1.00 48.73  ? 269 GLY A O     1 
ATOM   2108 N  N     . ILE A 1 270 ? -20.823 6.682   14.580  1.00 42.28  ? 270 ILE A N     1 
ATOM   2109 C  CA    . ILE A 1 270 ? -21.248 6.732   15.972  1.00 42.77  ? 270 ILE A CA    1 
ATOM   2110 C  C     . ILE A 1 270 ? -22.615 7.395   16.041  1.00 44.03  ? 270 ILE A C     1 
ATOM   2111 O  O     . ILE A 1 270 ? -22.807 8.492   15.504  1.00 43.25  ? 270 ILE A O     1 
ATOM   2112 C  CB    . ILE A 1 270 ? -20.233 7.479   16.858  1.00 48.26  ? 270 ILE A CB    1 
ATOM   2113 C  CG1   . ILE A 1 270 ? -20.729 7.531   18.305  1.00 40.41  ? 270 ILE A CG1   1 
ATOM   2114 C  CG2   . ILE A 1 270 ? -19.969 8.876   16.308  1.00 47.96  ? 270 ILE A CG2   1 
ATOM   2115 C  CD1   . ILE A 1 270 ? -19.659 7.885   19.313  1.00 44.76  ? 270 ILE A CD1   1 
ATOM   2116 N  N     . THR A 1 271 ? -23.559 6.730   16.701  1.00 45.99  ? 271 THR A N     1 
ATOM   2117 C  CA    . THR A 1 271 ? -24.919 7.221   16.871  1.00 46.36  ? 271 THR A CA    1 
ATOM   2118 C  C     . THR A 1 271 ? -25.150 7.544   18.340  1.00 46.64  ? 271 THR A C     1 
ATOM   2119 O  O     . THR A 1 271 ? -24.795 6.752   19.216  1.00 44.04  ? 271 THR A O     1 
ATOM   2120 C  CB    . THR A 1 271 ? -25.937 6.179   16.397  1.00 45.75  ? 271 THR A CB    1 
ATOM   2121 O  OG1   . THR A 1 271 ? -25.643 5.801   15.048  1.00 51.88  ? 271 THR A OG1   1 
ATOM   2122 C  CG2   . THR A 1 271 ? -27.349 6.732   16.461  1.00 45.55  ? 271 THR A CG2   1 
ATOM   2123 N  N     . ASN A 1 272 ? -25.743 8.705   18.611  1.00 43.73  ? 272 ASN A N     1 
ATOM   2124 C  CA    . ASN A 1 272 ? -25.923 9.113   19.997  1.00 45.65  ? 272 ASN A CA    1 
ATOM   2125 C  C     . ASN A 1 272 ? -27.321 8.752   20.485  1.00 48.05  ? 272 ASN A C     1 
ATOM   2126 O  O     . ASN A 1 272 ? -28.142 8.247   19.709  1.00 49.30  ? 272 ASN A O     1 
ATOM   2127 C  CB    . ASN A 1 272 ? -25.662 10.615  20.155  1.00 46.70  ? 272 ASN A CB    1 
ATOM   2128 C  CG    . ASN A 1 272 ? -26.775 11.473  19.587  1.00 41.56  ? 272 ASN A CG    1 
ATOM   2129 O  OD1   . ASN A 1 272 ? -27.698 10.978  18.937  1.00 48.62  ? 272 ASN A OD1   1 
ATOM   2130 N  ND2   . ASN A 1 272 ? -26.683 12.778  19.820  1.00 48.09  ? 272 ASN A ND2   1 
ATOM   2131 N  N     . PRO A 1 273 ? -27.628 8.991   21.763  1.00 51.26  ? 273 PRO A N     1 
ATOM   2132 C  CA    . PRO A 1 273 ? -28.960 8.630   22.278  1.00 50.73  ? 273 PRO A CA    1 
ATOM   2133 C  C     . PRO A 1 273 ? -30.098 9.394   21.626  1.00 56.15  ? 273 PRO A C     1 
ATOM   2134 O  O     . PRO A 1 273 ? -31.251 8.961   21.740  1.00 56.04  ? 273 PRO A O     1 
ATOM   2135 C  CB    . PRO A 1 273 ? -28.858 8.958   23.776  1.00 53.10  ? 273 PRO A CB    1 
ATOM   2136 C  CG    . PRO A 1 273 ? -27.387 8.959   24.067  1.00 48.64  ? 273 PRO A CG    1 
ATOM   2137 C  CD    . PRO A 1 273 ? -26.745 9.496   22.829  1.00 44.98  ? 273 PRO A CD    1 
ATOM   2138 N  N     . GLU A 1 274 ? -29.820 10.512  20.958  1.00 51.77  ? 274 GLU A N     1 
ATOM   2139 C  CA    . GLU A 1 274 ? -30.848 11.296  20.288  1.00 53.56  ? 274 GLU A CA    1 
ATOM   2140 C  C     . GLU A 1 274 ? -31.064 10.861  18.841  1.00 54.74  ? 274 GLU A C     1 
ATOM   2141 O  O     . GLU A 1 274 ? -31.765 11.553  18.095  1.00 52.48  ? 274 GLU A O     1 
ATOM   2142 C  CB    . GLU A 1 274 ? -30.494 12.786  20.341  1.00 51.05  ? 274 GLU A CB    1 
ATOM   2143 C  CG    . GLU A 1 274 ? -30.069 13.287  21.718  1.00 51.69  ? 274 GLU A CG    1 
ATOM   2144 C  CD    . GLU A 1 274 ? -31.228 13.437  22.688  1.00 54.79  ? 274 GLU A CD    1 
ATOM   2145 O  OE1   . GLU A 1 274 ? -32.391 13.265  22.262  1.00 63.98  ? 274 GLU A OE1   1 
ATOM   2146 O  OE2   . GLU A 1 274 ? -30.970 13.730  23.873  1.00 65.69  ? 274 GLU A OE2   1 
ATOM   2147 N  N     . GLY A 1 275 ? -30.483 9.736   18.430  1.00 50.90  ? 275 GLY A N     1 
ATOM   2148 C  CA    . GLY A 1 275 ? -30.664 9.245   17.080  1.00 52.43  ? 275 GLY A CA    1 
ATOM   2149 C  C     . GLY A 1 275 ? -29.832 9.932   16.022  1.00 54.79  ? 275 GLY A C     1 
ATOM   2150 O  O     . GLY A 1 275 ? -30.032 9.663   14.831  1.00 59.57  ? 275 GLY A O     1 
ATOM   2151 N  N     . LYS A 1 276 ? -28.909 10.808  16.410  1.00 46.06  ? 276 LYS A N     1 
ATOM   2152 C  CA    . LYS A 1 276 ? -28.015 11.459  15.464  1.00 50.00  ? 276 LYS A CA    1 
ATOM   2153 C  C     . LYS A 1 276 ? -26.763 10.611  15.278  1.00 47.11  ? 276 LYS A C     1 
ATOM   2154 O  O     . LYS A 1 276 ? -26.212 10.074  16.244  1.00 50.09  ? 276 LYS A O     1 
ATOM   2155 C  CB    . LYS A 1 276 ? -27.640 12.859  15.954  1.00 50.38  ? 276 LYS A CB    1 
ATOM   2156 C  CG    . LYS A 1 276 ? -28.787 13.637  16.595  1.00 56.84  ? 276 LYS A CG    1 
ATOM   2157 C  CD    . LYS A 1 276 ? -29.872 13.987  15.591  1.00 55.84  ? 276 LYS A CD    1 
ATOM   2158 C  CE    . LYS A 1 276 ? -30.740 15.139  16.085  1.00 47.55  ? 276 LYS A CE    1 
ATOM   2159 N  NZ    . LYS A 1 276 ? -31.530 14.790  17.296  1.00 48.69  ? 276 LYS A NZ    1 
ATOM   2160 N  N     . LYS A 1 277 ? -26.319 10.489  14.029  1.00 43.33  ? 277 LYS A N     1 
ATOM   2161 C  CA    . LYS A 1 277 ? -25.179 9.649   13.685  1.00 41.56  ? 277 LYS A CA    1 
ATOM   2162 C  C     . LYS A 1 277 ? -24.156 10.462  12.907  1.00 44.73  ? 277 LYS A C     1 
ATOM   2163 O  O     . LYS A 1 277 ? -24.512 11.168  11.956  1.00 43.51  ? 277 LYS A O     1 
ATOM   2164 C  CB    . LYS A 1 277 ? -25.617 8.429   12.870  1.00 44.47  ? 277 LYS A CB    1 
ATOM   2165 C  CG    . LYS A 1 277 ? -24.464 7.543   12.424  1.00 41.43  ? 277 LYS A CG    1 
ATOM   2166 C  CD    . LYS A 1 277 ? -24.969 6.280   11.739  1.00 42.68  ? 277 LYS A CD    1 
ATOM   2167 C  CE    . LYS A 1 277 ? -23.825 5.352   11.351  1.00 46.98  ? 277 LYS A CE    1 
ATOM   2168 N  NZ    . LYS A 1 277 ? -24.320 4.014   10.924  1.00 43.11  ? 277 LYS A NZ    1 
ATOM   2169 N  N     . LYS A 1 278 ? -22.891 10.354  13.312  1.00 41.13  ? 278 LYS A N     1 
ATOM   2170 C  CA    . LYS A 1 278 ? -21.779 11.012  12.643  1.00 43.10  ? 278 LYS A CA    1 
ATOM   2171 C  C     . LYS A 1 278 ? -20.687 9.994   12.353  1.00 47.04  ? 278 LYS A C     1 
ATOM   2172 O  O     . LYS A 1 278 ? -20.539 8.994   13.064  1.00 42.32  ? 278 LYS A O     1 
ATOM   2173 C  CB    . LYS A 1 278 ? -21.206 12.159  13.491  1.00 43.81  ? 278 LYS A CB    1 
ATOM   2174 C  CG    . LYS A 1 278 ? -22.217 13.247  13.816  1.00 42.46  ? 278 LYS A CG    1 
ATOM   2175 C  CD    . LYS A 1 278 ? -21.584 14.360  14.633  1.00 46.87  ? 278 LYS A CD    1 
ATOM   2176 C  CE    . LYS A 1 278 ? -22.582 15.468  14.920  1.00 45.89  ? 278 LYS A CE    1 
ATOM   2177 N  NZ    . LYS A 1 278 ? -23.127 16.056  13.664  1.00 40.01  ? 278 LYS A NZ    1 
ATOM   2178 N  N     . TYR A 1 279 ? -19.925 10.252  11.295  1.00 40.56  ? 279 TYR A N     1 
ATOM   2179 C  CA    . TYR A 1 279 ? -18.816 9.397   10.901  1.00 37.11  ? 279 TYR A CA    1 
ATOM   2180 C  C     . TYR A 1 279 ? -17.501 10.086  11.231  1.00 38.57  ? 279 TYR A C     1 
ATOM   2181 O  O     . TYR A 1 279 ? -17.318 11.269  10.922  1.00 39.54  ? 279 TYR A O     1 
ATOM   2182 C  CB    . TYR A 1 279 ? -18.884 9.059   9.412   1.00 39.46  ? 279 TYR A CB    1 
ATOM   2183 C  CG    . TYR A 1 279 ? -19.919 8.007   9.090   1.00 41.91  ? 279 TYR A CG    1 
ATOM   2184 C  CD1   . TYR A 1 279 ? -19.599 6.658   9.148   1.00 39.05  ? 279 TYR A CD1   1 
ATOM   2185 C  CD2   . TYR A 1 279 ? -21.214 8.359   8.739   1.00 38.64  ? 279 TYR A CD2   1 
ATOM   2186 C  CE1   . TYR A 1 279 ? -20.537 5.688   8.857   1.00 41.22  ? 279 TYR A CE1   1 
ATOM   2187 C  CE2   . TYR A 1 279 ? -22.162 7.395   8.448   1.00 44.40  ? 279 TYR A CE2   1 
ATOM   2188 C  CZ    . TYR A 1 279 ? -21.819 6.062   8.511   1.00 46.66  ? 279 TYR A CZ    1 
ATOM   2189 O  OH    . TYR A 1 279 ? -22.755 5.094   8.220   1.00 47.50  ? 279 TYR A OH    1 
ATOM   2190 N  N     . LEU A 1 280 ? -16.593 9.346   11.860  1.00 38.87  ? 280 LEU A N     1 
ATOM   2191 C  CA    . LEU A 1 280 ? -15.288 9.857   12.244  1.00 39.15  ? 280 LEU A CA    1 
ATOM   2192 C  C     . LEU A 1 280 ? -14.190 9.015   11.607  1.00 39.92  ? 280 LEU A C     1 
ATOM   2193 O  O     . LEU A 1 280 ? -14.365 7.817   11.361  1.00 41.10  ? 280 LEU A O     1 
ATOM   2194 C  CB    . LEU A 1 280 ? -15.117 9.851   13.769  1.00 41.41  ? 280 LEU A CB    1 
ATOM   2195 C  CG    . LEU A 1 280 ? -16.174 10.578  14.600  1.00 46.00  ? 280 LEU A CG    1 
ATOM   2196 C  CD1   . LEU A 1 280 ? -16.063 10.191  16.065  1.00 42.77  ? 280 LEU A CD1   1 
ATOM   2197 C  CD2   . LEU A 1 280 ? -16.047 12.083  14.438  1.00 39.99  ? 280 LEU A CD2   1 
ATOM   2198 N  N     . ALA A 1 281 ? -13.054 9.654   11.341  1.00 38.07  ? 281 ALA A N     1 
ATOM   2199 C  CA    . ALA A 1 281 ? -11.844 8.972   10.910  1.00 38.19  ? 281 ALA A CA    1 
ATOM   2200 C  C     . ALA A 1 281 ? -10.735 9.248   11.915  1.00 35.02  ? 281 ALA A C     1 
ATOM   2201 O  O     . ALA A 1 281 ? -10.666 10.332  12.502  1.00 37.37  ? 281 ALA A O     1 
ATOM   2202 C  CB    . ALA A 1 281 ? -11.412 9.421   9.509   1.00 32.59  ? 281 ALA A CB    1 
ATOM   2203 N  N     . ALA A 1 282 ? -9.867  8.258   12.119  1.00 35.75  ? 282 ALA A N     1 
ATOM   2204 C  CA    . ALA A 1 282 ? -8.812  8.356   13.120  1.00 36.48  ? 282 ALA A CA    1 
ATOM   2205 C  C     . ALA A 1 282 ? -7.527  7.763   12.570  1.00 38.63  ? 282 ALA A C     1 
ATOM   2206 O  O     . ALA A 1 282 ? -7.521  6.627   12.091  1.00 36.38  ? 282 ALA A O     1 
ATOM   2207 C  CB    . ALA A 1 282 ? -9.207  7.639   14.417  1.00 36.84  ? 282 ALA A CB    1 
ATOM   2208 N  N     . ALA A 1 283 ? -6.443  8.529   12.646  1.00 35.50  ? 283 ALA A N     1 
ATOM   2209 C  CA    . ALA A 1 283 ? -5.126  8.087   12.203  1.00 33.95  ? 283 ALA A CA    1 
ATOM   2210 C  C     . ALA A 1 283 ? -4.262  7.845   13.432  1.00 33.20  ? 283 ALA A C     1 
ATOM   2211 O  O     . ALA A 1 283 ? -3.789  8.796   14.060  1.00 37.40  ? 283 ALA A O     1 
ATOM   2212 C  CB    . ALA A 1 283 ? -4.479  9.114   11.274  1.00 34.07  ? 283 ALA A CB    1 
ATOM   2213 N  N     . PHE A 1 284 ? -4.067  6.575   13.774  1.00 33.43  ? 284 PHE A N     1 
ATOM   2214 C  CA    . PHE A 1 284 ? -3.119  6.154   14.788  1.00 35.96  ? 284 PHE A CA    1 
ATOM   2215 C  C     . PHE A 1 284 ? -2.032  5.306   14.137  1.00 38.15  ? 284 PHE A C     1 
ATOM   2216 O  O     . PHE A 1 284 ? -2.305  4.588   13.170  1.00 38.63  ? 284 PHE A O     1 
ATOM   2217 C  CB    . PHE A 1 284 ? -3.785  5.324   15.897  1.00 34.61  ? 284 PHE A CB    1 
ATOM   2218 C  CG    . PHE A 1 284 ? -4.988  5.970   16.522  1.00 41.54  ? 284 PHE A CG    1 
ATOM   2219 C  CD1   . PHE A 1 284 ? -5.097  7.348   16.606  1.00 39.02  ? 284 PHE A CD1   1 
ATOM   2220 C  CD2   . PHE A 1 284 ? -6.012  5.189   17.037  1.00 43.45  ? 284 PHE A CD2   1 
ATOM   2221 C  CE1   . PHE A 1 284 ? -6.208  7.934   17.189  1.00 37.50  ? 284 PHE A CE1   1 
ATOM   2222 C  CE2   . PHE A 1 284 ? -7.126  5.768   17.619  1.00 41.40  ? 284 PHE A CE2   1 
ATOM   2223 C  CZ    . PHE A 1 284 ? -7.223  7.142   17.694  1.00 41.44  ? 284 PHE A CZ    1 
ATOM   2224 N  N     . PRO A 1 285 ? -0.796  5.368   14.632  1.00 37.24  ? 285 PRO A N     1 
ATOM   2225 C  CA    . PRO A 1 285 ? 0.228   4.431   14.157  1.00 40.59  ? 285 PRO A CA    1 
ATOM   2226 C  C     . PRO A 1 285 ? -0.127  2.998   14.526  1.00 46.12  ? 285 PRO A C     1 
ATOM   2227 O  O     . PRO A 1 285 ? -1.009  2.736   15.347  1.00 47.19  ? 285 PRO A O     1 
ATOM   2228 C  CB    . PRO A 1 285 ? 1.502   4.894   14.876  1.00 42.01  ? 285 PRO A CB    1 
ATOM   2229 C  CG    . PRO A 1 285 ? 1.235   6.318   15.243  1.00 40.97  ? 285 PRO A CG    1 
ATOM   2230 C  CD    . PRO A 1 285 ? -0.236  6.395   15.526  1.00 42.76  ? 285 PRO A CD    1 
ATOM   2231 N  N     . SER A 1 286 ? 0.588   2.058   13.911  1.00 45.62  ? 286 SER A N     1 
ATOM   2232 C  CA    . SER A 1 286 ? 0.346   0.647   14.179  1.00 44.74  ? 286 SER A CA    1 
ATOM   2233 C  C     . SER A 1 286 ? 0.478   0.352   15.667  1.00 46.88  ? 286 SER A C     1 
ATOM   2234 O  O     . SER A 1 286 ? 1.326   0.921   16.359  1.00 44.91  ? 286 SER A O     1 
ATOM   2235 C  CB    . SER A 1 286 ? 1.320   -0.220  13.382  1.00 47.52  ? 286 SER A CB    1 
ATOM   2236 O  OG    . SER A 1 286 ? 1.069   -0.104  11.994  1.00 54.75  ? 286 SER A OG    1 
ATOM   2237 N  N     . ALA A 1 287 ? -0.376  -0.545  16.158  1.00 47.71  ? 287 ALA A N     1 
ATOM   2238 C  CA    . ALA A 1 287 ? -0.359  -0.964  17.556  1.00 48.64  ? 287 ALA A CA    1 
ATOM   2239 C  C     . ALA A 1 287 ? -0.733  0.174   18.503  1.00 46.05  ? 287 ALA A C     1 
ATOM   2240 O  O     . ALA A 1 287 ? -0.308  0.187   19.660  1.00 53.92  ? 287 ALA A O     1 
ATOM   2241 C  CB    . ALA A 1 287 ? 1.003   -1.545  17.943  1.00 51.36  ? 287 ALA A CB    1 
ATOM   2242 N  N     . CYS A 1 288 ? -1.531  1.133   18.026  1.00 48.68  ? 288 CYS A N     1 
ATOM   2243 C  CA    . CYS A 1 288 ? -1.961  2.259   18.845  1.00 44.05  ? 288 CYS A CA    1 
ATOM   2244 C  C     . CYS A 1 288 ? -3.472  2.347   19.021  1.00 44.08  ? 288 CYS A C     1 
ATOM   2245 O  O     . CYS A 1 288 ? -3.950  3.318   19.618  1.00 40.72  ? 288 CYS A O     1 
ATOM   2246 C  CB    . CYS A 1 288 ? -1.438  3.580   18.264  1.00 50.40  ? 288 CYS A CB    1 
ATOM   2247 S  SG    . CYS A 1 288 ? 0.365   3.778   18.367  1.00 52.90  ? 288 CYS A SG    1 
ATOM   2248 N  N     . GLY A 1 289 ? -4.235  1.384   18.518  1.00 46.04  ? 289 GLY A N     1 
ATOM   2249 C  CA    . GLY A 1 289 ? -5.631  1.238   18.869  1.00 39.78  ? 289 GLY A CA    1 
ATOM   2250 C  C     . GLY A 1 289 ? -6.674  1.505   17.790  1.00 41.24  ? 289 GLY A C     1 
ATOM   2251 O  O     . GLY A 1 289 ? -7.853  1.666   18.134  1.00 40.49  ? 289 GLY A O     1 
ATOM   2252 N  N     . LYS A 1 290 ? -6.291  1.543   16.511  1.00 42.60  ? 290 LYS A N     1 
ATOM   2253 C  CA    . LYS A 1 290 ? -7.278  1.789   15.464  1.00 40.83  ? 290 LYS A CA    1 
ATOM   2254 C  C     . LYS A 1 290 ? -8.352  0.706   15.454  1.00 41.89  ? 290 LYS A C     1 
ATOM   2255 O  O     . LYS A 1 290 ? -9.551  1.005   15.439  1.00 41.03  ? 290 LYS A O     1 
ATOM   2256 C  CB    . LYS A 1 290 ? -6.590  1.884   14.105  1.00 38.30  ? 290 LYS A CB    1 
ATOM   2257 C  CG    . LYS A 1 290 ? -5.768  3.149   13.924  1.00 37.37  ? 290 LYS A CG    1 
ATOM   2258 C  CD    . LYS A 1 290 ? -5.441  3.400   12.462  1.00 37.77  ? 290 LYS A CD    1 
ATOM   2259 C  CE    . LYS A 1 290 ? -4.699  2.225   11.858  1.00 39.46  ? 290 LYS A CE    1 
ATOM   2260 N  NZ    . LYS A 1 290 ? -3.485  1.871   12.636  1.00 40.43  ? 290 LYS A NZ    1 
ATOM   2261 N  N     . THR A 1 291 ? -7.939  -0.563  15.472  1.00 44.64  ? 291 THR A N     1 
ATOM   2262 C  CA    . THR A 1 291 ? -8.910  -1.652  15.402  1.00 45.83  ? 291 THR A CA    1 
ATOM   2263 C  C     . THR A 1 291 ? -9.792  -1.694  16.646  1.00 41.59  ? 291 THR A C     1 
ATOM   2264 O  O     . THR A 1 291 ? -10.990 -1.984  16.551  1.00 47.74  ? 291 THR A O     1 
ATOM   2265 C  CB    . THR A 1 291 ? -8.193  -2.986  15.204  1.00 42.69  ? 291 THR A CB    1 
ATOM   2266 O  OG1   . THR A 1 291 ? -7.628  -3.036  13.889  1.00 44.71  ? 291 THR A OG1   1 
ATOM   2267 C  CG2   . THR A 1 291 ? -9.170  -4.144  15.377  1.00 44.58  ? 291 THR A CG2   1 
ATOM   2268 N  N     . ASN A 1 292 ? -9.221  -1.410  17.818  1.00 46.19  ? 292 ASN A N     1 
ATOM   2269 C  CA    . ASN A 1 292 ? -10.023 -1.385  19.039  1.00 44.07  ? 292 ASN A CA    1 
ATOM   2270 C  C     . ASN A 1 292 ? -11.043 -0.252  19.008  1.00 43.16  ? 292 ASN A C     1 
ATOM   2271 O  O     . ASN A 1 292 ? -12.188 -0.423  19.444  1.00 45.51  ? 292 ASN A O     1 
ATOM   2272 C  CB    . ASN A 1 292 ? -9.115  -1.254  20.261  1.00 49.47  ? 292 ASN A CB    1 
ATOM   2273 C  CG    . ASN A 1 292 ? -8.691  -2.596  20.821  1.00 55.08  ? 292 ASN A CG    1 
ATOM   2274 O  OD1   . ASN A 1 292 ? -9.118  -2.993  21.902  1.00 52.66  ? 292 ASN A OD1   1 
ATOM   2275 N  ND2   . ASN A 1 292 ? -7.842  -3.303  20.085  1.00 53.41  ? 292 ASN A ND2   1 
ATOM   2276 N  N     . LEU A 1 293 ? -10.648 0.914   18.493  1.00 43.37  ? 293 LEU A N     1 
ATOM   2277 C  CA    . LEU A 1 293 ? -11.576 2.037   18.416  1.00 43.21  ? 293 LEU A CA    1 
ATOM   2278 C  C     . LEU A 1 293 ? -12.657 1.794   17.368  1.00 40.93  ? 293 LEU A C     1 
ATOM   2279 O  O     . LEU A 1 293 ? -13.836 2.075   17.610  1.00 41.68  ? 293 LEU A O     1 
ATOM   2280 C  CB    . LEU A 1 293 ? -10.811 3.325   18.112  1.00 37.48  ? 293 LEU A CB    1 
ATOM   2281 C  CG    . LEU A 1 293 ? -11.628 4.616   18.149  1.00 39.67  ? 293 LEU A CG    1 
ATOM   2282 C  CD1   . LEU A 1 293 ? -12.206 4.828   19.532  1.00 44.84  ? 293 LEU A CD1   1 
ATOM   2283 C  CD2   . LEU A 1 293 ? -10.772 5.802   17.738  1.00 39.87  ? 293 LEU A CD2   1 
ATOM   2284 N  N     . ALA A 1 294 ? -12.278 1.271   16.200  1.00 43.22  ? 294 ALA A N     1 
ATOM   2285 C  CA    . ALA A 1 294 ? -13.243 1.089   15.121  1.00 35.67  ? 294 ALA A CA    1 
ATOM   2286 C  C     . ALA A 1 294 ? -14.283 0.025   15.448  1.00 45.12  ? 294 ALA A C     1 
ATOM   2287 O  O     . ALA A 1 294 ? -15.397 0.076   14.915  1.00 45.03  ? 294 ALA A O     1 
ATOM   2288 C  CB    . ALA A 1 294 ? -12.519 0.742   13.820  1.00 41.00  ? 294 ALA A CB    1 
ATOM   2289 N  N     . MET A 1 295 ? -13.949 -0.931  16.315  1.00 43.38  ? 295 MET A N     1 
ATOM   2290 C  CA    . MET A 1 295 ? -14.877 -1.969  16.745  1.00 48.35  ? 295 MET A CA    1 
ATOM   2291 C  C     . MET A 1 295 ? -15.278 -1.812  18.206  1.00 47.38  ? 295 MET A C     1 
ATOM   2292 O  O     . MET A 1 295 ? -15.743 -2.775  18.822  1.00 46.19  ? 295 MET A O     1 
ATOM   2293 C  CB    . MET A 1 295 ? -14.268 -3.355  16.535  1.00 43.59  ? 295 MET A CB    1 
ATOM   2294 C  CG    . MET A 1 295 ? -13.919 -3.723  15.104  1.00 48.32  ? 295 MET A CG    1 
ATOM   2295 S  SD    . MET A 1 295 ? -13.289 -5.418  15.034  1.00 53.41  ? 295 MET A SD    1 
ATOM   2296 C  CE    . MET A 1 295 ? -12.910 -5.587  13.290  1.00 51.74  ? 295 MET A CE    1 
ATOM   2297 N  N     A MET A 1 296 ? -15.115 -0.620  18.771  0.12 48.85  ? 296 MET A N     1 
ATOM   2298 N  N     B MET A 1 296 ? -15.104 -0.619  18.770  0.88 47.65  ? 296 MET A N     1 
ATOM   2299 C  CA    A MET A 1 296 ? -15.288 -0.447  20.206  0.12 48.31  ? 296 MET A CA    1 
ATOM   2300 C  CA    B MET A 1 296 ? -15.344 -0.404  20.190  0.88 48.32  ? 296 MET A CA    1 
ATOM   2301 C  C     A MET A 1 296 ? -16.711 -0.776  20.641  0.12 49.30  ? 296 MET A C     1 
ATOM   2302 C  C     B MET A 1 296 ? -16.735 -0.875  20.595  0.88 49.30  ? 296 MET A C     1 
ATOM   2303 O  O     A MET A 1 296 ? -17.681 -0.482  19.936  0.12 49.90  ? 296 MET A O     1 
ATOM   2304 O  O     B MET A 1 296 ? -17.698 -0.783  19.829  0.88 50.95  ? 296 MET A O     1 
ATOM   2305 C  CB    A MET A 1 296 ? -14.943 0.986   20.607  0.12 48.15  ? 296 MET A CB    1 
ATOM   2306 C  CB    B MET A 1 296 ? -15.190 1.078   20.533  0.88 48.28  ? 296 MET A CB    1 
ATOM   2307 C  CG    A MET A 1 296 ? -15.007 1.239   22.103  0.12 49.29  ? 296 MET A CG    1 
ATOM   2308 C  CG    B MET A 1 296 ? -15.706 1.452   21.913  0.88 49.14  ? 296 MET A CG    1 
ATOM   2309 S  SD    A MET A 1 296 ? -14.877 2.988   22.514  0.12 47.07  ? 296 MET A SD    1 
ATOM   2310 S  SD    B MET A 1 296 ? -15.959 3.228   22.105  0.88 51.36  ? 296 MET A SD    1 
ATOM   2311 C  CE    A MET A 1 296 ? -16.368 3.616   21.745  0.12 49.76  ? 296 MET A CE    1 
ATOM   2312 C  CE    B MET A 1 296 ? -14.347 3.849   21.653  0.88 44.19  ? 296 MET A CE    1 
ATOM   2313 N  N     . ASN A 1 297 ? -16.829 -1.390  21.822  1.00 48.06  ? 297 ASN A N     1 
ATOM   2314 C  CA    . ASN A 1 297 ? -18.109 -1.640  22.465  1.00 52.05  ? 297 ASN A CA    1 
ATOM   2315 C  C     . ASN A 1 297 ? -18.307 -0.522  23.477  1.00 47.13  ? 297 ASN A C     1 
ATOM   2316 O  O     . ASN A 1 297 ? -17.741 -0.582  24.579  1.00 51.97  ? 297 ASN A O     1 
ATOM   2317 C  CB    . ASN A 1 297 ? -18.139 -3.009  23.151  1.00 51.09  ? 297 ASN A CB    1 
ATOM   2318 C  CG    . ASN A 1 297 ? -19.508 -3.346  23.721  1.00 60.31  ? 297 ASN A CG    1 
ATOM   2319 O  OD1   . ASN A 1 297 ? -20.518 -2.762  23.325  1.00 67.08  ? 297 ASN A OD1   1 
ATOM   2320 N  ND2   . ASN A 1 297 ? -19.548 -4.290  24.655  1.00 63.71  ? 297 ASN A ND2   1 
ATOM   2321 N  N     . PRO A 1 298 ? -19.074 0.517   23.158  1.00 48.10  ? 298 PRO A N     1 
ATOM   2322 C  CA    . PRO A 1 298 ? -19.132 1.688   24.041  1.00 52.13  ? 298 PRO A CA    1 
ATOM   2323 C  C     . PRO A 1 298 ? -19.775 1.356   25.378  1.00 52.42  ? 298 PRO A C     1 
ATOM   2324 O  O     . PRO A 1 298 ? -20.728 0.578   25.457  1.00 52.30  ? 298 PRO A O     1 
ATOM   2325 C  CB    . PRO A 1 298 ? -19.977 2.689   23.246  1.00 53.00  ? 298 PRO A CB    1 
ATOM   2326 C  CG    . PRO A 1 298 ? -20.814 1.834   22.347  1.00 58.01  ? 298 PRO A CG    1 
ATOM   2327 C  CD    . PRO A 1 298 ? -19.960 0.654   21.990  1.00 49.24  ? 298 PRO A CD    1 
ATOM   2328 N  N     . THR A 1 299 ? -19.238 1.960   26.437  1.00 53.46  ? 299 THR A N     1 
ATOM   2329 C  CA    . THR A 1 299 ? -19.755 1.763   27.783  1.00 47.76  ? 299 THR A CA    1 
ATOM   2330 C  C     . THR A 1 299 ? -20.877 2.731   28.135  1.00 51.00  ? 299 THR A C     1 
ATOM   2331 O  O     . THR A 1 299 ? -21.572 2.511   29.131  1.00 57.88  ? 299 THR A O     1 
ATOM   2332 C  CB    . THR A 1 299 ? -18.622 1.899   28.809  1.00 48.13  ? 299 THR A CB    1 
ATOM   2333 O  OG1   . THR A 1 299 ? -18.071 3.219   28.742  1.00 47.80  ? 299 THR A OG1   1 
ATOM   2334 C  CG2   . THR A 1 299 ? -17.521 0.887   28.526  1.00 48.35  ? 299 THR A CG2   1 
ATOM   2335 N  N     . LEU A 1 300 ? -21.069 3.784   27.351  1.00 51.80  ? 300 LEU A N     1 
ATOM   2336 C  CA    . LEU A 1 300 ? -22.152 4.725   27.614  1.00 53.95  ? 300 LEU A CA    1 
ATOM   2337 C  C     . LEU A 1 300 ? -23.463 4.175   27.060  1.00 53.53  ? 300 LEU A C     1 
ATOM   2338 O  O     . LEU A 1 300 ? -23.520 3.786   25.887  1.00 54.12  ? 300 LEU A O     1 
ATOM   2339 C  CB    . LEU A 1 300 ? -21.852 6.086   26.989  1.00 48.87  ? 300 LEU A CB    1 
ATOM   2340 C  CG    . LEU A 1 300 ? -20.675 6.873   27.570  1.00 49.69  ? 300 LEU A CG    1 
ATOM   2341 C  CD1   . LEU A 1 300 ? -20.464 8.167   26.797  1.00 49.23  ? 300 LEU A CD1   1 
ATOM   2342 C  CD2   . LEU A 1 300 ? -20.900 7.162   29.048  1.00 50.25  ? 300 LEU A CD2   1 
ATOM   2343 N  N     . PRO A 1 301 ? -24.523 4.123   27.861  1.00 50.95  ? 301 PRO A N     1 
ATOM   2344 C  CA    . PRO A 1 301 ? -25.806 3.630   27.349  1.00 54.42  ? 301 PRO A CA    1 
ATOM   2345 C  C     . PRO A 1 301 ? -26.390 4.579   26.316  1.00 51.73  ? 301 PRO A C     1 
ATOM   2346 O  O     . PRO A 1 301 ? -26.244 5.800   26.411  1.00 52.10  ? 301 PRO A O     1 
ATOM   2347 C  CB    . PRO A 1 301 ? -26.681 3.556   28.604  1.00 51.53  ? 301 PRO A CB    1 
ATOM   2348 C  CG    . PRO A 1 301 ? -26.086 4.570   29.528  1.00 55.60  ? 301 PRO A CG    1 
ATOM   2349 C  CD    . PRO A 1 301 ? -24.604 4.513   29.277  1.00 58.47  ? 301 PRO A CD    1 
ATOM   2350 N  N     . GLY A 1 302 ? -27.060 4.002   25.322  1.00 48.22  ? 302 GLY A N     1 
ATOM   2351 C  CA    . GLY A 1 302 ? -27.633 4.780   24.248  1.00 51.79  ? 302 GLY A CA    1 
ATOM   2352 C  C     . GLY A 1 302 ? -26.668 5.181   23.155  1.00 56.14  ? 302 GLY A C     1 
ATOM   2353 O  O     . GLY A 1 302 ? -27.082 5.865   22.210  1.00 56.21  ? 302 GLY A O     1 
ATOM   2354 N  N     . TRP A 1 303 ? -25.403 4.782   23.246  1.00 55.37  ? 303 TRP A N     1 
ATOM   2355 C  CA    . TRP A 1 303 ? -24.409 5.068   22.223  1.00 48.91  ? 303 TRP A CA    1 
ATOM   2356 C  C     . TRP A 1 303 ? -24.096 3.803   21.436  1.00 55.66  ? 303 TRP A C     1 
ATOM   2357 O  O     . TRP A 1 303 ? -24.005 2.709   22.005  1.00 49.95  ? 303 TRP A O     1 
ATOM   2358 C  CB    . TRP A 1 303 ? -23.129 5.635   22.844  1.00 46.68  ? 303 TRP A CB    1 
ATOM   2359 C  CG    . TRP A 1 303 ? -23.281 7.052   23.305  1.00 48.95  ? 303 TRP A CG    1 
ATOM   2360 C  CD1   . TRP A 1 303 ? -23.766 7.475   24.506  1.00 50.05  ? 303 TRP A CD1   1 
ATOM   2361 C  CD2   . TRP A 1 303 ? -22.950 8.234   22.566  1.00 46.55  ? 303 TRP A CD2   1 
ATOM   2362 N  NE1   . TRP A 1 303 ? -23.757 8.848   24.563  1.00 46.94  ? 303 TRP A NE1   1 
ATOM   2363 C  CE2   . TRP A 1 303 ? -23.261 9.338   23.383  1.00 45.62  ? 303 TRP A CE2   1 
ATOM   2364 C  CE3   . TRP A 1 303 ? -22.418 8.465   21.295  1.00 42.17  ? 303 TRP A CE3   1 
ATOM   2365 C  CZ2   . TRP A 1 303 ? -23.060 10.653  22.969  1.00 45.83  ? 303 TRP A CZ2   1 
ATOM   2366 C  CZ3   . TRP A 1 303 ? -22.220 9.771   20.886  1.00 44.76  ? 303 TRP A CZ3   1 
ATOM   2367 C  CH2   . TRP A 1 303 ? -22.540 10.848  21.720  1.00 44.39  ? 303 TRP A CH2   1 
ATOM   2368 N  N     . LYS A 1 304 ? -23.929 3.958   20.126  1.00 47.78  ? 304 LYS A N     1 
ATOM   2369 C  CA    . LYS A 1 304 ? -23.669 2.843   19.227  1.00 48.14  ? 304 LYS A CA    1 
ATOM   2370 C  C     . LYS A 1 304 ? -22.496 3.188   18.324  1.00 53.13  ? 304 LYS A C     1 
ATOM   2371 O  O     . LYS A 1 304 ? -22.505 4.230   17.661  1.00 51.06  ? 304 LYS A O     1 
ATOM   2372 C  CB    . LYS A 1 304 ? -24.907 2.517   18.383  1.00 47.37  ? 304 LYS A CB    1 
ATOM   2373 C  CG    . LYS A 1 304 ? -24.790 1.238   17.568  1.00 58.58  ? 304 LYS A CG    1 
ATOM   2374 C  CD    . LYS A 1 304 ? -26.039 1.024   16.725  1.00 63.97  ? 304 LYS A CD    1 
ATOM   2375 C  CE    . LYS A 1 304 ? -25.978 -0.275  15.935  1.00 67.31  ? 304 LYS A CE    1 
ATOM   2376 N  NZ    . LYS A 1 304 ? -26.181 -1.465  16.800  1.00 69.86  ? 304 LYS A NZ    1 
ATOM   2377 N  N     . VAL A 1 305 ? -21.495 2.314   18.299  1.00 52.08  ? 305 VAL A N     1 
ATOM   2378 C  CA    . VAL A 1 305 ? -20.350 2.436   17.404  1.00 50.14  ? 305 VAL A CA    1 
ATOM   2379 C  C     . VAL A 1 305 ? -20.469 1.376   16.318  1.00 48.13  ? 305 VAL A C     1 
ATOM   2380 O  O     . VAL A 1 305 ? -20.784 0.213   16.598  1.00 52.11  ? 305 VAL A O     1 
ATOM   2381 C  CB    . VAL A 1 305 ? -19.013 2.296   18.157  1.00 50.51  ? 305 VAL A CB    1 
ATOM   2382 C  CG1   . VAL A 1 305 ? -17.870 2.095   17.172  1.00 51.96  ? 305 VAL A CG1   1 
ATOM   2383 C  CG2   . VAL A 1 305 ? -18.761 3.520   19.024  1.00 46.82  ? 305 VAL A CG2   1 
ATOM   2384 N  N     . GLU A 1 306 ? -20.214 1.781   15.077  1.00 45.42  ? 306 GLU A N     1 
ATOM   2385 C  CA    . GLU A 1 306 ? -20.266 0.884   13.932  1.00 48.47  ? 306 GLU A CA    1 
ATOM   2386 C  C     . GLU A 1 306 ? -18.999 1.057   13.110  1.00 44.29  ? 306 GLU A C     1 
ATOM   2387 O  O     . GLU A 1 306 ? -18.501 2.176   12.947  1.00 43.83  ? 306 GLU A O     1 
ATOM   2388 C  CB    . GLU A 1 306 ? -21.516 1.147   13.081  1.00 47.47  ? 306 GLU A CB    1 
ATOM   2389 C  CG    . GLU A 1 306 ? -22.803 0.688   13.756  1.00 49.34  ? 306 GLU A CG    1 
ATOM   2390 C  CD    . GLU A 1 306 ? -24.050 1.202   13.068  1.00 51.51  ? 306 GLU A CD    1 
ATOM   2391 O  OE1   . GLU A 1 306 ? -24.286 2.428   13.098  1.00 51.27  ? 306 GLU A OE1   1 
ATOM   2392 O  OE2   . GLU A 1 306 ? -24.792 0.379   12.492  1.00 59.73  ? 306 GLU A OE2   1 
ATOM   2393 N  N     . CYS A 1 307 ? -18.476 -0.055  12.603  1.00 46.16  ? 307 CYS A N     1 
ATOM   2394 C  CA    . CYS A 1 307 ? -17.172 -0.087  11.956  1.00 46.10  ? 307 CYS A CA    1 
ATOM   2395 C  C     . CYS A 1 307 ? -17.338 -0.046  10.442  1.00 46.86  ? 307 CYS A C     1 
ATOM   2396 O  O     . CYS A 1 307 ? -17.981 -0.926  9.859   1.00 44.59  ? 307 CYS A O     1 
ATOM   2397 C  CB    . CYS A 1 307 ? -16.396 -1.337  12.373  1.00 47.03  ? 307 CYS A CB    1 
ATOM   2398 S  SG    . CYS A 1 307 ? -14.792 -1.534  11.568  1.00 46.66  ? 307 CYS A SG    1 
ATOM   2399 N  N     . VAL A 1 308 ? -16.764 0.977   9.814   1.00 44.72  ? 308 VAL A N     1 
ATOM   2400 C  CA    . VAL A 1 308 ? -16.648 1.016   8.359   1.00 39.80  ? 308 VAL A CA    1 
ATOM   2401 C  C     . VAL A 1 308 ? -15.323 0.417   7.902   1.00 45.91  ? 308 VAL A C     1 
ATOM   2402 O  O     . VAL A 1 308 ? -15.262 -0.270  6.878   1.00 41.02  ? 308 VAL A O     1 
ATOM   2403 C  CB    . VAL A 1 308 ? -16.812 2.466   7.860   1.00 40.61  ? 308 VAL A CB    1 
ATOM   2404 C  CG1   . VAL A 1 308 ? -16.584 2.543   6.356   1.00 40.48  ? 308 VAL A CG1   1 
ATOM   2405 C  CG2   . VAL A 1 308 ? -18.190 3.008   8.234   1.00 39.98  ? 308 VAL A CG2   1 
ATOM   2406 N  N     . GLY A 1 309 ? -14.262 0.672   8.661   1.00 41.65  ? 309 GLY A N     1 
ATOM   2407 C  CA    . GLY A 1 309 ? -12.942 0.154   8.356   1.00 38.82  ? 309 GLY A CA    1 
ATOM   2408 C  C     . GLY A 1 309 ? -12.008 0.459   9.503   1.00 39.72  ? 309 GLY A C     1 
ATOM   2409 O  O     . GLY A 1 309 ? -12.291 1.318   10.345  1.00 41.82  ? 309 GLY A O     1 
ATOM   2410 N  N     . ASP A 1 310 ? -10.880 -0.250  9.526   1.00 36.34  ? 310 ASP A N     1 
ATOM   2411 C  CA    . ASP A 1 310 ? -9.965  -0.168  10.659  1.00 35.23  ? 310 ASP A CA    1 
ATOM   2412 C  C     . ASP A 1 310 ? -8.532  0.178   10.276  1.00 38.01  ? 310 ASP A C     1 
ATOM   2413 O  O     . ASP A 1 310 ? -7.642  0.076   11.129  1.00 39.69  ? 310 ASP A O     1 
ATOM   2414 C  CB    . ASP A 1 310 ? -9.969  -1.487  11.435  1.00 39.32  ? 310 ASP A CB    1 
ATOM   2415 C  CG    . ASP A 1 310 ? -9.093  -2.544  10.791  1.00 44.05  ? 310 ASP A CG    1 
ATOM   2416 O  OD1   . ASP A 1 310 ? -8.952  -2.545  9.547   1.00 38.05  ? 310 ASP A OD1   1 
ATOM   2417 O  OD2   . ASP A 1 310 ? -8.549  -3.386  11.529  1.00 44.22  ? 310 ASP A OD2   1 
ATOM   2418 N  N     . ASP A 1 311 ? -8.269  0.581   9.036   1.00 39.02  ? 311 ASP A N     1 
ATOM   2419 C  CA    . ASP A 1 311 ? -6.874  0.775   8.661   1.00 36.90  ? 311 ASP A CA    1 
ATOM   2420 C  C     . ASP A 1 311 ? -6.660  1.801   7.555   1.00 38.36  ? 311 ASP A C     1 
ATOM   2421 O  O     . ASP A 1 311 ? -5.725  2.604   7.634   1.00 36.58  ? 311 ASP A O     1 
ATOM   2422 C  CB    . ASP A 1 311 ? -6.259  -0.566  8.246   1.00 37.67  ? 311 ASP A CB    1 
ATOM   2423 C  CG    . ASP A 1 311 ? -4.763  -0.478  8.033   1.00 38.65  ? 311 ASP A CG    1 
ATOM   2424 O  OD1   . ASP A 1 311 ? -4.066  0.018   8.942   1.00 35.10  ? 311 ASP A OD1   1 
ATOM   2425 O  OD2   . ASP A 1 311 ? -4.288  -0.909  6.962   1.00 46.93  ? 311 ASP A OD2   1 
ATOM   2426 N  N     . ILE A 1 312 ? -7.491  1.782   6.515   1.00 38.25  ? 312 ILE A N     1 
ATOM   2427 C  CA    . ILE A 1 312 ? -7.246  2.586   5.323   1.00 37.56  ? 312 ILE A CA    1 
ATOM   2428 C  C     . ILE A 1 312 ? -8.519  3.317   4.930   1.00 36.03  ? 312 ILE A C     1 
ATOM   2429 O  O     . ILE A 1 312 ? -9.592  2.709   4.849   1.00 36.75  ? 312 ILE A O     1 
ATOM   2430 C  CB    . ILE A 1 312 ? -6.740  1.729   4.148   1.00 40.85  ? 312 ILE A CB    1 
ATOM   2431 C  CG1   . ILE A 1 312 ? -5.416  1.059   4.517   1.00 40.97  ? 312 ILE A CG1   1 
ATOM   2432 C  CG2   . ILE A 1 312 ? -6.596  2.585   2.895   1.00 41.30  ? 312 ILE A CG2   1 
ATOM   2433 C  CD1   . ILE A 1 312 ? -4.799  0.264   3.392   1.00 53.08  ? 312 ILE A CD1   1 
ATOM   2434 N  N     . ALA A 1 313 ? -8.390  4.615   4.667   1.00 38.83  ? 313 ALA A N     1 
ATOM   2435 C  CA    . ALA A 1 313 ? -9.496  5.450   4.228   1.00 38.94  ? 313 ALA A CA    1 
ATOM   2436 C  C     . ALA A 1 313 ? -9.115  6.160   2.940   1.00 38.09  ? 313 ALA A C     1 
ATOM   2437 O  O     . ALA A 1 313 ? -8.032  6.746   2.846   1.00 37.19  ? 313 ALA A O     1 
ATOM   2438 C  CB    . ALA A 1 313 ? -9.869  6.479   5.302   1.00 36.59  ? 313 ALA A CB    1 
ATOM   2439 N  N     . TRP A 1 314 ? -10.002 6.098   1.953   1.00 37.12  ? 314 TRP A N     1 
ATOM   2440 C  CA    . TRP A 1 314 ? -9.896  6.895   0.739   1.00 45.32  ? 314 TRP A CA    1 
ATOM   2441 C  C     . TRP A 1 314 ? -10.973 7.967   0.798   1.00 41.82  ? 314 TRP A C     1 
ATOM   2442 O  O     . TRP A 1 314 ? -12.163 7.648   0.880   1.00 39.44  ? 314 TRP A O     1 
ATOM   2443 C  CB    . TRP A 1 314 ? -10.048 6.030   -0.514  1.00 39.62  ? 314 TRP A CB    1 
ATOM   2444 C  CG    . TRP A 1 314 ? -8.864  5.159   -0.794  1.00 35.01  ? 314 TRP A CG    1 
ATOM   2445 C  CD1   . TRP A 1 314 ? -7.738  5.040   -0.031  1.00 38.97  ? 314 TRP A CD1   1 
ATOM   2446 C  CD2   . TRP A 1 314 ? -8.681  4.285   -1.916  1.00 42.01  ? 314 TRP A CD2   1 
ATOM   2447 N  NE1   . TRP A 1 314 ? -6.866  4.148   -0.608  1.00 38.49  ? 314 TRP A NE1   1 
ATOM   2448 C  CE2   . TRP A 1 314 ? -7.421  3.670   -1.767  1.00 36.55  ? 314 TRP A CE2   1 
ATOM   2449 C  CE3   . TRP A 1 314 ? -9.458  3.964   -3.033  1.00 41.88  ? 314 TRP A CE3   1 
ATOM   2450 C  CZ2   . TRP A 1 314 ? -6.922  2.754   -2.692  1.00 43.55  ? 314 TRP A CZ2   1 
ATOM   2451 C  CZ3   . TRP A 1 314 ? -8.958  3.053   -3.951  1.00 45.20  ? 314 TRP A CZ3   1 
ATOM   2452 C  CH2   . TRP A 1 314 ? -7.706  2.458   -3.772  1.00 43.43  ? 314 TRP A CH2   1 
ATOM   2453 N  N     . MET A 1 315 ? -10.557 9.230   0.768   1.00 40.09  ? 315 MET A N     1 
ATOM   2454 C  CA    . MET A 1 315 ? -11.461 10.339  1.025   1.00 42.35  ? 315 MET A CA    1 
ATOM   2455 C  C     . MET A 1 315 ? -11.395 11.356  -0.103  1.00 43.38  ? 315 MET A C     1 
ATOM   2456 O  O     . MET A 1 315 ? -10.357 11.537  -0.745  1.00 46.37  ? 315 MET A O     1 
ATOM   2457 C  CB    . MET A 1 315 ? -11.136 11.011  2.363   1.00 41.31  ? 315 MET A CB    1 
ATOM   2458 C  CG    . MET A 1 315 ? -11.104 10.036  3.528   1.00 44.44  ? 315 MET A CG    1 
ATOM   2459 S  SD    . MET A 1 315 ? -10.962 10.849  5.133   1.00 47.62  ? 315 MET A SD    1 
ATOM   2460 C  CE    . MET A 1 315 ? -9.391  11.684  4.953   1.00 49.44  ? 315 MET A CE    1 
ATOM   2461 N  N     . LYS A 1 316 ? -12.524 12.022  -0.333  1.00 47.68  ? 316 LYS A N     1 
ATOM   2462 C  CA    . LYS A 1 316 ? -12.640 13.019  -1.386  1.00 46.60  ? 316 LYS A CA    1 
ATOM   2463 C  C     . LYS A 1 316 ? -13.863 13.877  -1.104  1.00 48.29  ? 316 LYS A C     1 
ATOM   2464 O  O     . LYS A 1 316 ? -14.904 13.362  -0.690  1.00 47.28  ? 316 LYS A O     1 
ATOM   2465 C  CB    . LYS A 1 316 ? -12.749 12.359  -2.768  1.00 53.63  ? 316 LYS A CB    1 
ATOM   2466 C  CG    . LYS A 1 316 ? -12.940 13.332  -3.922  1.00 53.63  ? 316 LYS A CG    1 
ATOM   2467 C  CD    . LYS A 1 316 ? -12.822 12.625  -5.267  1.00 60.12  ? 316 LYS A CD    1 
ATOM   2468 C  CE    . LYS A 1 316 ? -13.882 11.548  -5.432  1.00 64.20  ? 316 LYS A CE    1 
ATOM   2469 N  NZ    . LYS A 1 316 ? -15.258 12.116  -5.395  1.00 65.85  ? 316 LYS A NZ    1 
ATOM   2470 N  N     . PHE A 1 317 ? -13.723 15.184  -1.311  1.00 50.45  ? 317 PHE A N     1 
ATOM   2471 C  CA    . PHE A 1 317 ? -14.867 16.078  -1.201  1.00 53.56  ? 317 PHE A CA    1 
ATOM   2472 C  C     . PHE A 1 317 ? -15.816 15.848  -2.370  1.00 54.90  ? 317 PHE A C     1 
ATOM   2473 O  O     . PHE A 1 317 ? -15.387 15.772  -3.525  1.00 52.72  ? 317 PHE A O     1 
ATOM   2474 C  CB    . PHE A 1 317 ? -14.410 17.535  -1.172  1.00 54.10  ? 317 PHE A CB    1 
ATOM   2475 C  CG    . PHE A 1 317 ? -13.740 17.940  0.111   1.00 55.25  ? 317 PHE A CG    1 
ATOM   2476 C  CD1   . PHE A 1 317 ? -14.489 18.195  1.248   1.00 54.40  ? 317 PHE A CD1   1 
ATOM   2477 C  CD2   . PHE A 1 317 ? -12.364 18.076  0.177   1.00 55.22  ? 317 PHE A CD2   1 
ATOM   2478 C  CE1   . PHE A 1 317 ? -13.878 18.570  2.431   1.00 51.62  ? 317 PHE A CE1   1 
ATOM   2479 C  CE2   . PHE A 1 317 ? -11.747 18.454  1.354   1.00 53.44  ? 317 PHE A CE2   1 
ATOM   2480 C  CZ    . PHE A 1 317 ? -12.506 18.702  2.484   1.00 53.74  ? 317 PHE A CZ    1 
ATOM   2481 N  N     . ASP A 1 318 ? -17.106 15.733  -2.073  1.00 54.38  ? 318 ASP A N     1 
ATOM   2482 C  CA    . ASP A 1 318 ? -18.100 15.511  -3.111  1.00 55.56  ? 318 ASP A CA    1 
ATOM   2483 C  C     . ASP A 1 318 ? -18.597 16.862  -3.627  1.00 60.20  ? 318 ASP A C     1 
ATOM   2484 O  O     . ASP A 1 318 ? -18.079 17.921  -3.264  1.00 53.93  ? 318 ASP A O     1 
ATOM   2485 C  CB    . ASP A 1 318 ? -19.228 14.624  -2.585  1.00 60.12  ? 318 ASP A CB    1 
ATOM   2486 C  CG    . ASP A 1 318 ? -20.052 15.293  -1.499  1.00 56.19  ? 318 ASP A CG    1 
ATOM   2487 O  OD1   . ASP A 1 318 ? -19.852 16.497  -1.236  1.00 57.73  ? 318 ASP A OD1   1 
ATOM   2488 O  OD2   . ASP A 1 318 ? -20.909 14.604  -0.904  1.00 55.45  ? 318 ASP A OD2   1 
ATOM   2489 N  N     . ALA A 1 319 ? -19.618 16.839  -4.486  1.00 61.72  ? 319 ALA A N     1 
ATOM   2490 C  CA    . ALA A 1 319 ? -20.115 18.081  -5.068  1.00 62.92  ? 319 ALA A CA    1 
ATOM   2491 C  C     . ALA A 1 319 ? -20.639 19.035  -4.002  1.00 62.09  ? 319 ALA A C     1 
ATOM   2492 O  O     . ALA A 1 319 ? -20.496 20.255  -4.138  1.00 61.17  ? 319 ALA A O     1 
ATOM   2493 C  CB    . ALA A 1 319 ? -21.205 17.781  -6.098  1.00 63.16  ? 319 ALA A CB    1 
ATOM   2494 N  N     . GLN A 1 320 ? -21.233 18.505  -2.935  1.00 60.14  ? 320 GLN A N     1 
ATOM   2495 C  CA    . GLN A 1 320 ? -21.842 19.336  -1.904  1.00 59.65  ? 320 GLN A CA    1 
ATOM   2496 C  C     . GLN A 1 320 ? -20.837 19.872  -0.892  1.00 57.64  ? 320 GLN A C     1 
ATOM   2497 O  O     . GLN A 1 320 ? -21.230 20.627  0.004   1.00 57.79  ? 320 GLN A O     1 
ATOM   2498 C  CB    . GLN A 1 320 ? -22.931 18.547  -1.175  1.00 60.69  ? 320 GLN A CB    1 
ATOM   2499 C  CG    . GLN A 1 320 ? -23.857 17.772  -2.101  1.00 64.50  ? 320 GLN A CG    1 
ATOM   2500 C  CD    . GLN A 1 320 ? -24.589 18.667  -3.082  1.00 68.60  ? 320 GLN A CD    1 
ATOM   2501 O  OE1   . GLN A 1 320 ? -24.838 19.839  -2.803  1.00 69.32  ? 320 GLN A OE1   1 
ATOM   2502 N  NE2   . GLN A 1 320 ? -24.936 18.118  -4.241  1.00 71.79  ? 320 GLN A NE2   1 
ATOM   2503 N  N     . GLY A 1 321 ? -19.563 19.508  -1.008  1.00 59.05  ? 321 GLY A N     1 
ATOM   2504 C  CA    . GLY A 1 321 ? -18.550 19.978  -0.089  1.00 55.63  ? 321 GLY A CA    1 
ATOM   2505 C  C     . GLY A 1 321 ? -18.286 19.078  1.096   1.00 57.06  ? 321 GLY A C     1 
ATOM   2506 O  O     . GLY A 1 321 ? -17.485 19.448  1.965   1.00 52.71  ? 321 GLY A O     1 
ATOM   2507 N  N     . ASN A 1 322 ? -18.932 17.915  1.166   1.00 53.14  ? 322 ASN A N     1 
ATOM   2508 C  CA    . ASN A 1 322 ? -18.698 16.975  2.253   1.00 49.91  ? 322 ASN A CA    1 
ATOM   2509 C  C     . ASN A 1 322 ? -17.483 16.109  1.950   1.00 52.86  ? 322 ASN A C     1 
ATOM   2510 O  O     . ASN A 1 322 ? -17.253 15.715  0.803   1.00 49.61  ? 322 ASN A O     1 
ATOM   2511 C  CB    . ASN A 1 322 ? -19.920 16.082  2.469   1.00 53.96  ? 322 ASN A CB    1 
ATOM   2512 C  CG    . ASN A 1 322 ? -21.197 16.872  2.646   1.00 58.52  ? 322 ASN A CG    1 
ATOM   2513 O  OD1   . ASN A 1 322 ? -21.485 17.367  3.734   1.00 59.65  ? 322 ASN A OD1   1 
ATOM   2514 N  ND2   . ASN A 1 322 ? -21.978 16.984  1.578   1.00 62.58  ? 322 ASN A ND2   1 
ATOM   2515 N  N     . LEU A 1 323 ? -16.704 15.813  2.987   1.00 53.07  ? 323 LEU A N     1 
ATOM   2516 C  CA    . LEU A 1 323 ? -15.579 14.891  2.864   1.00 46.61  ? 323 LEU A CA    1 
ATOM   2517 C  C     . LEU A 1 323 ? -16.109 13.467  2.984   1.00 45.73  ? 323 LEU A C     1 
ATOM   2518 O  O     . LEU A 1 323 ? -16.518 13.039  4.069   1.00 49.79  ? 323 LEU A O     1 
ATOM   2519 C  CB    . LEU A 1 323 ? -14.527 15.185  3.929   1.00 44.51  ? 323 LEU A CB    1 
ATOM   2520 C  CG    . LEU A 1 323 ? -13.236 14.366  3.872   1.00 47.13  ? 323 LEU A CG    1 
ATOM   2521 C  CD1   . LEU A 1 323 ? -12.519 14.576  2.545   1.00 42.22  ? 323 LEU A CD1   1 
ATOM   2522 C  CD2   . LEU A 1 323 ? -12.325 14.709  5.045   1.00 41.88  ? 323 LEU A CD2   1 
ATOM   2523 N  N     . ARG A 1 324 ? -16.114 12.735  1.874   1.00 39.76  ? 324 ARG A N     1 
ATOM   2524 C  CA    . ARG A 1 324 ? -16.646 11.380  1.838   1.00 47.26  ? 324 ARG A CA    1 
ATOM   2525 C  C     . ARG A 1 324 ? -15.511 10.366  1.829   1.00 47.65  ? 324 ARG A C     1 
ATOM   2526 O  O     . ARG A 1 324 ? -14.509 10.541  1.130   1.00 47.67  ? 324 ARG A O     1 
ATOM   2527 C  CB    . ARG A 1 324 ? -17.552 11.178  0.621   1.00 51.01  ? 324 ARG A CB    1 
ATOM   2528 C  CG    . ARG A 1 324 ? -18.785 12.063  0.652   1.00 51.81  ? 324 ARG A CG    1 
ATOM   2529 C  CD    . ARG A 1 324 ? -19.977 11.424  -0.034  1.00 52.04  ? 324 ARG A CD    1 
ATOM   2530 N  NE    . ARG A 1 324 ? -21.217 12.075  0.371   1.00 60.23  ? 324 ARG A NE    1 
ATOM   2531 C  CZ    . ARG A 1 324 ? -22.100 11.554  1.212   1.00 58.72  ? 324 ARG A CZ    1 
ATOM   2532 N  NH1   . ARG A 1 324 ? -21.941 10.343  1.720   1.00 59.00  ? 324 ARG A NH1   1 
ATOM   2533 N  NH2   . ARG A 1 324 ? -23.174 12.265  1.546   1.00 68.94  ? 324 ARG A NH2   1 
ATOM   2534 N  N     . ALA A 1 325 ? -15.674 9.311   2.621   1.00 45.30  ? 325 ALA A N     1 
ATOM   2535 C  CA    . ALA A 1 325 ? -14.647 8.301   2.808   1.00 43.73  ? 325 ALA A CA    1 
ATOM   2536 C  C     . ALA A 1 325 ? -15.229 6.923   2.544   1.00 46.91  ? 325 ALA A C     1 
ATOM   2537 O  O     . ALA A 1 325 ? -16.404 6.665   2.817   1.00 43.33  ? 325 ALA A O     1 
ATOM   2538 C  CB    . ALA A 1 325 ? -14.061 8.353   4.227   1.00 37.84  ? 325 ALA A CB    1 
ATOM   2539 N  N     . ILE A 1 326 ? -14.392 6.043   2.004   1.00 41.45  ? 326 ILE A N     1 
ATOM   2540 C  CA    . ILE A 1 326 ? -14.708 4.628   1.876   1.00 42.63  ? 326 ILE A CA    1 
ATOM   2541 C  C     . ILE A 1 326 ? -13.548 3.827   2.443   1.00 38.28  ? 326 ILE A C     1 
ATOM   2542 O  O     . ILE A 1 326 ? -12.397 4.276   2.447   1.00 38.82  ? 326 ILE A O     1 
ATOM   2543 C  CB    . ILE A 1 326 ? -14.985 4.202   0.415   1.00 45.23  ? 326 ILE A CB    1 
ATOM   2544 C  CG1   . ILE A 1 326 ? -13.731 4.366   -0.449  1.00 45.98  ? 326 ILE A CG1   1 
ATOM   2545 C  CG2   . ILE A 1 326 ? -16.159 4.986   -0.158  1.00 49.14  ? 326 ILE A CG2   1 
ATOM   2546 C  CD1   . ILE A 1 326 ? -13.820 3.658   -1.779  1.00 56.00  ? 326 ILE A CD1   1 
ATOM   2547 N  N     . ASN A 1 327 ? -13.861 2.634   2.939   1.00 41.67  ? 327 ASN A N     1 
ATOM   2548 C  CA    . ASN A 1 327 ? -12.836 1.664   3.287   1.00 42.81  ? 327 ASN A CA    1 
ATOM   2549 C  C     . ASN A 1 327 ? -12.530 0.849   2.038   1.00 39.31  ? 327 ASN A C     1 
ATOM   2550 O  O     . ASN A 1 327 ? -13.400 0.090   1.585   1.00 46.24  ? 327 ASN A O     1 
ATOM   2551 C  CB    . ASN A 1 327 ? -13.307 0.764   4.417   1.00 42.98  ? 327 ASN A CB    1 
ATOM   2552 C  CG    . ASN A 1 327 ? -12.412 -0.441  4.617   1.00 40.26  ? 327 ASN A CG    1 
ATOM   2553 O  OD1   . ASN A 1 327 ? -11.249 -0.444  4.213   1.00 41.17  ? 327 ASN A OD1   1 
ATOM   2554 N  ND2   . ASN A 1 327 ? -12.956 -1.477  5.244   1.00 43.41  ? 327 ASN A ND2   1 
ATOM   2555 N  N     . PRO A 1 328 ? -11.345 0.982   1.439   1.00 38.22  ? 328 PRO A N     1 
ATOM   2556 C  CA    . PRO A 1 328 ? -11.056 0.233   0.209   1.00 43.04  ? 328 PRO A CA    1 
ATOM   2557 C  C     . PRO A 1 328 ? -10.836 -1.251  0.431   1.00 43.41  ? 328 PRO A C     1 
ATOM   2558 O  O     . PRO A 1 328 ? -10.777 -2.003  -0.551  1.00 44.09  ? 328 PRO A O     1 
ATOM   2559 C  CB    . PRO A 1 328 ? -9.781  0.907   -0.311  1.00 41.09  ? 328 PRO A CB    1 
ATOM   2560 C  CG    . PRO A 1 328 ? -9.094  1.383   0.929   1.00 38.71  ? 328 PRO A CG    1 
ATOM   2561 C  CD    . PRO A 1 328 ? -10.197 1.797   1.878   1.00 39.68  ? 328 PRO A CD    1 
ATOM   2562 N  N     . GLU A 1 329 ? -10.723 -1.696  1.676   1.00 40.93  ? 329 GLU A N     1 
ATOM   2563 C  CA    . GLU A 1 329 ? -10.425 -3.086  1.971   1.00 41.96  ? 329 GLU A CA    1 
ATOM   2564 C  C     . GLU A 1 329 ? -11.706 -3.903  2.113   1.00 40.67  ? 329 GLU A C     1 
ATOM   2565 O  O     . GLU A 1 329 ? -12.815 -3.371  2.208   1.00 46.75  ? 329 GLU A O     1 
ATOM   2566 C  CB    . GLU A 1 329 ? -9.582  -3.190  3.239   1.00 43.91  ? 329 GLU A CB    1 
ATOM   2567 C  CG    . GLU A 1 329 ? -8.225  -2.518  3.124   1.00 40.42  ? 329 GLU A CG    1 
ATOM   2568 C  CD    . GLU A 1 329 ? -7.295  -2.884  4.265   1.00 43.34  ? 329 GLU A CD    1 
ATOM   2569 O  OE1   . GLU A 1 329 ? -7.596  -2.514  5.417   1.00 44.16  ? 329 GLU A OE1   1 
ATOM   2570 O  OE2   . GLU A 1 329 ? -6.262  -3.546  4.010   1.00 45.95  ? 329 GLU A OE2   1 
ATOM   2571 N  N     . ASN A 1 330 ? -11.534 -5.225  2.126   1.00 39.64  ? 330 ASN A N     1 
ATOM   2572 C  CA    . ASN A 1 330 ? -12.645 -6.152  2.235   1.00 39.83  ? 330 ASN A CA    1 
ATOM   2573 C  C     . ASN A 1 330 ? -12.618 -6.962  3.527   1.00 42.10  ? 330 ASN A C     1 
ATOM   2574 O  O     . ASN A 1 330 ? -13.545 -7.746  3.769   1.00 36.55  ? 330 ASN A O     1 
ATOM   2575 C  CB    . ASN A 1 330 ? -12.655 -7.103  1.032   1.00 43.93  ? 330 ASN A CB    1 
ATOM   2576 C  CG    . ASN A 1 330 ? -13.988 -7.794  0.847   1.00 43.24  ? 330 ASN A CG    1 
ATOM   2577 O  OD1   . ASN A 1 330 ? -15.030 -7.279  1.254   1.00 43.07  ? 330 ASN A OD1   1 
ATOM   2578 N  ND2   . ASN A 1 330 ? -13.964 -8.968  0.231   1.00 42.49  ? 330 ASN A ND2   1 
ATOM   2579 N  N     . GLY A 1 331 ? -11.596 -6.797  4.361   1.00 38.56  ? 331 GLY A N     1 
ATOM   2580 C  CA    . GLY A 1 331 ? -11.526 -7.518  5.612   1.00 38.65  ? 331 GLY A CA    1 
ATOM   2581 C  C     . GLY A 1 331 ? -10.615 -6.801  6.587   1.00 40.39  ? 331 GLY A C     1 
ATOM   2582 O  O     . GLY A 1 331 ? -10.166 -5.679  6.338   1.00 40.34  ? 331 GLY A O     1 
ATOM   2583 N  N     . PHE A 1 332 ? -10.343 -7.468  7.708   1.00 38.64  ? 332 PHE A N     1 
ATOM   2584 C  CA    . PHE A 1 332 ? -9.492  -6.923  8.758   1.00 41.71  ? 332 PHE A CA    1 
ATOM   2585 C  C     . PHE A 1 332 ? -8.258  -7.794  8.919   1.00 38.86  ? 332 PHE A C     1 
ATOM   2586 O  O     . PHE A 1 332 ? -8.366  -9.020  9.012   1.00 42.06  ? 332 PHE A O     1 
ATOM   2587 C  CB    . PHE A 1 332 ? -10.246 -6.816  10.093  1.00 45.64  ? 332 PHE A CB    1 
ATOM   2588 C  CG    . PHE A 1 332 ? -11.563 -6.100  9.990   1.00 46.18  ? 332 PHE A CG    1 
ATOM   2589 C  CD1   . PHE A 1 332 ? -11.616 -4.762  9.645   1.00 39.80  ? 332 PHE A CD1   1 
ATOM   2590 C  CD2   . PHE A 1 332 ? -12.752 -6.771  10.242  1.00 43.05  ? 332 PHE A CD2   1 
ATOM   2591 C  CE1   . PHE A 1 332 ? -12.831 -4.102  9.545   1.00 45.49  ? 332 PHE A CE1   1 
ATOM   2592 C  CE2   . PHE A 1 332 ? -13.967 -6.118  10.144  1.00 46.27  ? 332 PHE A CE2   1 
ATOM   2593 C  CZ    . PHE A 1 332 ? -14.007 -4.782  9.794   1.00 51.80  ? 332 PHE A CZ    1 
ATOM   2594 N  N     . PHE A 1 333 ? -7.095  -7.152  8.951   1.00 36.66  ? 333 PHE A N     1 
ATOM   2595 C  CA    . PHE A 1 333 ? -5.798  -7.802  9.135   1.00 40.91  ? 333 PHE A CA    1 
ATOM   2596 C  C     . PHE A 1 333 ? -5.189  -7.230  10.410  1.00 43.56  ? 333 PHE A C     1 
ATOM   2597 O  O     . PHE A 1 333 ? -4.257  -6.425  10.367  1.00 39.77  ? 333 PHE A O     1 
ATOM   2598 C  CB    . PHE A 1 333 ? -4.902  -7.571  7.904   1.00 43.13  ? 333 PHE A CB    1 
ATOM   2599 C  CG    . PHE A 1 333 ? -3.619  -8.356  7.918   1.00 40.42  ? 333 PHE A CG    1 
ATOM   2600 C  CD1   . PHE A 1 333 ? -3.627  -9.728  7.748   1.00 42.25  ? 333 PHE A CD1   1 
ATOM   2601 C  CD2   . PHE A 1 333 ? -2.400  -7.712  8.073   1.00 44.93  ? 333 PHE A CD2   1 
ATOM   2602 C  CE1   . PHE A 1 333 ? -2.447  -10.453 7.751   1.00 43.74  ? 333 PHE A CE1   1 
ATOM   2603 C  CE2   . PHE A 1 333 ? -1.213  -8.432  8.076   1.00 43.46  ? 333 PHE A CE2   1 
ATOM   2604 C  CZ    . PHE A 1 333 ? -1.237  -9.803  7.914   1.00 39.46  ? 333 PHE A CZ    1 
ATOM   2605 N  N     . GLY A 1 334 ? -5.739  -7.644  11.553  1.00 45.12  ? 334 GLY A N     1 
ATOM   2606 C  CA    . GLY A 1 334 ? -5.403  -7.054  12.828  1.00 48.43  ? 334 GLY A CA    1 
ATOM   2607 C  C     . GLY A 1 334 ? -4.442  -7.888  13.654  1.00 47.24  ? 334 GLY A C     1 
ATOM   2608 O  O     . GLY A 1 334 ? -4.311  -9.097  13.472  1.00 44.80  ? 334 GLY A O     1 
ATOM   2609 N  N     . VAL A 1 335 ? -3.754  -7.207  14.571  1.00 45.52  ? 335 VAL A N     1 
ATOM   2610 C  CA    . VAL A 1 335 ? -2.843  -7.877  15.490  1.00 47.41  ? 335 VAL A CA    1 
ATOM   2611 C  C     . VAL A 1 335 ? -3.651  -8.723  16.464  1.00 47.98  ? 335 VAL A C     1 
ATOM   2612 O  O     . VAL A 1 335 ? -4.652  -8.263  17.028  1.00 45.55  ? 335 VAL A O     1 
ATOM   2613 C  CB    . VAL A 1 335 ? -1.977  -6.847  16.230  1.00 49.69  ? 335 VAL A CB    1 
ATOM   2614 C  CG1   . VAL A 1 335 ? -1.005  -7.538  17.170  1.00 48.21  ? 335 VAL A CG1   1 
ATOM   2615 C  CG2   . VAL A 1 335 ? -1.243  -5.962  15.234  1.00 55.67  ? 335 VAL A CG2   1 
ATOM   2616 N  N     . ALA A 1 336 ? -3.216  -9.965  16.669  1.00 48.72  ? 336 ALA A N     1 
ATOM   2617 C  CA    . ALA A 1 336 ? -3.959  -10.914 17.489  1.00 48.08  ? 336 ALA A CA    1 
ATOM   2618 C  C     . ALA A 1 336 ? -3.720  -10.661 18.974  1.00 48.97  ? 336 ALA A C     1 
ATOM   2619 O  O     . ALA A 1 336 ? -4.676  -10.402 19.717  1.00 48.95  ? 336 ALA A O     1 
ATOM   2620 C  CB    . ALA A 1 336 ? -3.577  -12.350 17.124  1.00 48.47  ? 336 ALA A CB    1 
ATOM   2621 N  N     . PRO A 1 337 ? -2.473  -10.727 19.443  1.00 51.42  ? 337 PRO A N     1 
ATOM   2622 C  CA    . PRO A 1 337 ? -2.210  -10.549 20.877  1.00 49.63  ? 337 PRO A CA    1 
ATOM   2623 C  C     . PRO A 1 337 ? -2.834  -9.266  21.408  1.00 51.98  ? 337 PRO A C     1 
ATOM   2624 O  O     . PRO A 1 337 ? -2.864  -8.236  20.730  1.00 53.88  ? 337 PRO A O     1 
ATOM   2625 C  CB    . PRO A 1 337 ? -0.681  -10.511 20.951  1.00 48.90  ? 337 PRO A CB    1 
ATOM   2626 C  CG    . PRO A 1 337 ? -0.237  -11.306 19.766  1.00 50.72  ? 337 PRO A CG    1 
ATOM   2627 C  CD    . PRO A 1 337 ? -1.242  -11.021 18.686  1.00 52.22  ? 337 PRO A CD    1 
ATOM   2628 N  N     . GLY A 1 338 ? -3.335  -9.338  22.639  1.00 47.50  ? 338 GLY A N     1 
ATOM   2629 C  CA    . GLY A 1 338 ? -4.078  -8.252  23.229  1.00 50.47  ? 338 GLY A CA    1 
ATOM   2630 C  C     . GLY A 1 338 ? -5.554  -8.243  22.895  1.00 50.90  ? 338 GLY A C     1 
ATOM   2631 O  O     . GLY A 1 338 ? -6.316  -7.520  23.549  1.00 53.18  ? 338 GLY A O     1 
ATOM   2632 N  N     . THR A 1 339 ? -5.981  -9.019  21.902  1.00 49.64  ? 339 THR A N     1 
ATOM   2633 C  CA    . THR A 1 339 ? -7.394  -9.131  21.555  1.00 53.66  ? 339 THR A CA    1 
ATOM   2634 C  C     . THR A 1 339 ? -8.060  -10.119 22.507  1.00 52.99  ? 339 THR A C     1 
ATOM   2635 O  O     . THR A 1 339 ? -7.766  -11.319 22.476  1.00 51.29  ? 339 THR A O     1 
ATOM   2636 C  CB    . THR A 1 339 ? -7.557  -9.578  20.105  1.00 49.83  ? 339 THR A CB    1 
ATOM   2637 O  OG1   . THR A 1 339 ? -6.786  -8.724  19.251  1.00 50.40  ? 339 THR A OG1   1 
ATOM   2638 C  CG2   . THR A 1 339 ? -9.018  -9.509  19.689  1.00 50.53  ? 339 THR A CG2   1 
ATOM   2639 N  N     . SER A 1 340 ? -8.957  -9.619  23.355  1.00 54.04  ? 340 SER A N     1 
ATOM   2640 C  CA    . SER A 1 340 ? -9.675  -10.447 24.313  1.00 59.22  ? 340 SER A CA    1 
ATOM   2641 C  C     . SER A 1 340 ? -11.150 -10.069 24.284  1.00 56.92  ? 340 SER A C     1 
ATOM   2642 O  O     . SER A 1 340 ? -11.565 -9.155  23.564  1.00 58.07  ? 340 SER A O     1 
ATOM   2643 C  CB    . SER A 1 340 ? -9.088  -10.299 25.722  1.00 59.34  ? 340 SER A CB    1 
ATOM   2644 O  OG    . SER A 1 340 ? -9.123  -8.948  26.151  1.00 63.93  ? 340 SER A OG    1 
ATOM   2645 N  N     . VAL A 1 341 ? -11.950 -10.784 25.078  1.00 58.43  ? 341 VAL A N     1 
ATOM   2646 C  CA    . VAL A 1 341 ? -13.378 -10.490 25.142  1.00 65.65  ? 341 VAL A CA    1 
ATOM   2647 C  C     . VAL A 1 341 ? -13.629 -9.165  25.849  1.00 63.60  ? 341 VAL A C     1 
ATOM   2648 O  O     . VAL A 1 341 ? -14.619 -8.480  25.564  1.00 63.90  ? 341 VAL A O     1 
ATOM   2649 C  CB    . VAL A 1 341 ? -14.135 -11.643 25.827  1.00 70.70  ? 341 VAL A CB    1 
ATOM   2650 C  CG1   . VAL A 1 341 ? -15.582 -11.248 26.089  1.00 66.35  ? 341 VAL A CG1   1 
ATOM   2651 C  CG2   . VAL A 1 341 ? -14.070 -12.901 24.975  1.00 68.47  ? 341 VAL A CG2   1 
ATOM   2652 N  N     . LYS A 1 342 ? -12.747 -8.776  26.773  1.00 61.99  ? 342 LYS A N     1 
ATOM   2653 C  CA    . LYS A 1 342 ? -12.944 -7.526  27.495  1.00 65.05  ? 342 LYS A CA    1 
ATOM   2654 C  C     . LYS A 1 342 ? -12.410 -6.327  26.720  1.00 68.19  ? 342 LYS A C     1 
ATOM   2655 O  O     . LYS A 1 342 ? -12.946 -5.221  26.855  1.00 73.44  ? 342 LYS A O     1 
ATOM   2656 C  CB    . LYS A 1 342 ? -12.286 -7.598  28.875  1.00 72.93  ? 342 LYS A CB    1 
ATOM   2657 C  CG    . LYS A 1 342 ? -10.772 -7.476  28.867  1.00 80.54  ? 342 LYS A CG    1 
ATOM   2658 C  CD    . LYS A 1 342 ? -10.224 -7.479  30.287  1.00 86.47  ? 342 LYS A CD    1 
ATOM   2659 C  CE    . LYS A 1 342 ? -8.753  -7.105  30.319  1.00 95.02  ? 342 LYS A CE    1 
ATOM   2660 N  NZ    . LYS A 1 342 ? -8.539  -5.701  29.880  1.00 91.28  ? 342 LYS A NZ    1 
ATOM   2661 N  N     . THR A 1 343 ? -11.372 -6.521  25.903  1.00 60.24  ? 343 THR A N     1 
ATOM   2662 C  CA    . THR A 1 343 ? -10.823 -5.413  25.128  1.00 61.61  ? 343 THR A CA    1 
ATOM   2663 C  C     . THR A 1 343 ? -11.586 -5.215  23.820  1.00 62.34  ? 343 THR A C     1 
ATOM   2664 O  O     . THR A 1 343 ? -12.092 -4.121  23.547  1.00 56.29  ? 343 THR A O     1 
ATOM   2665 C  CB    . THR A 1 343 ? -9.333  -5.642  24.851  1.00 60.50  ? 343 THR A CB    1 
ATOM   2666 O  OG1   . THR A 1 343 ? -9.155  -6.869  24.129  1.00 52.60  ? 343 THR A OG1   1 
ATOM   2667 C  CG2   . THR A 1 343 ? -8.543  -5.693  26.156  1.00 62.14  ? 343 THR A CG2   1 
ATOM   2668 N  N     . ASN A 1 344 ? -11.683 -6.263  23.002  1.00 55.66  ? 344 ASN A N     1 
ATOM   2669 C  CA    . ASN A 1 344 ? -12.315 -6.186  21.683  1.00 48.85  ? 344 ASN A CA    1 
ATOM   2670 C  C     . ASN A 1 344 ? -13.237 -7.384  21.487  1.00 54.59  ? 344 ASN A C     1 
ATOM   2671 O  O     . ASN A 1 344 ? -12.957 -8.278  20.679  1.00 55.70  ? 344 ASN A O     1 
ATOM   2672 C  CB    . ASN A 1 344 ? -11.256 -6.121  20.581  1.00 49.33  ? 344 ASN A CB    1 
ATOM   2673 C  CG    . ASN A 1 344 ? -11.782 -5.516  19.293  1.00 49.69  ? 344 ASN A CG    1 
ATOM   2674 O  OD1   . ASN A 1 344 ? -12.991 -5.462  19.067  1.00 48.58  ? 344 ASN A OD1   1 
ATOM   2675 N  ND2   . ASN A 1 344 ? -10.873 -5.063  18.437  1.00 52.55  ? 344 ASN A ND2   1 
ATOM   2676 N  N     . PRO A 1 345 ? -14.358 -7.430  22.212  1.00 55.58  ? 345 PRO A N     1 
ATOM   2677 C  CA    . PRO A 1 345 ? -15.297 -8.549  22.024  1.00 57.36  ? 345 PRO A CA    1 
ATOM   2678 C  C     . PRO A 1 345 ? -15.856 -8.636  20.615  1.00 58.00  ? 345 PRO A C     1 
ATOM   2679 O  O     . PRO A 1 345 ? -16.155 -9.741  20.143  1.00 55.28  ? 345 PRO A O     1 
ATOM   2680 C  CB    . PRO A 1 345 ? -16.399 -8.261  23.056  1.00 58.87  ? 345 PRO A CB    1 
ATOM   2681 C  CG    . PRO A 1 345 ? -16.294 -6.789  23.327  1.00 55.40  ? 345 PRO A CG    1 
ATOM   2682 C  CD    . PRO A 1 345 ? -14.834 -6.468  23.220  1.00 57.48  ? 345 PRO A CD    1 
ATOM   2683 N  N     . ASN A 1 346 ? -16.007 -7.502  19.925  1.00 54.29  ? 346 ASN A N     1 
ATOM   2684 C  CA    . ASN A 1 346 ? -16.507 -7.537  18.554  1.00 52.47  ? 346 ASN A CA    1 
ATOM   2685 C  C     . ASN A 1 346 ? -15.513 -8.203  17.611  1.00 54.97  ? 346 ASN A C     1 
ATOM   2686 O  O     . ASN A 1 346 ? -15.922 -8.849  16.640  1.00 54.68  ? 346 ASN A O     1 
ATOM   2687 C  CB    . ASN A 1 346 ? -16.838 -6.121  18.077  1.00 51.98  ? 346 ASN A CB    1 
ATOM   2688 C  CG    . ASN A 1 346 ? -18.156 -5.614  18.635  1.00 56.63  ? 346 ASN A CG    1 
ATOM   2689 O  OD1   . ASN A 1 346 ? -19.149 -6.341  18.667  1.00 53.07  ? 346 ASN A OD1   1 
ATOM   2690 N  ND2   . ASN A 1 346 ? -18.170 -4.365  19.082  1.00 51.11  ? 346 ASN A ND2   1 
ATOM   2691 N  N     . ALA A 1 347 ? -14.213 -8.063  17.875  1.00 51.92  ? 347 ALA A N     1 
ATOM   2692 C  CA    . ALA A 1 347 ? -13.228 -8.791  17.083  1.00 46.58  ? 347 ALA A CA    1 
ATOM   2693 C  C     . ALA A 1 347 ? -13.321 -10.289 17.341  1.00 51.75  ? 347 ALA A C     1 
ATOM   2694 O  O     . ALA A 1 347 ? -13.231 -11.093 16.407  1.00 51.53  ? 347 ALA A O     1 
ATOM   2695 C  CB    . ALA A 1 347 ? -11.821 -8.281  17.391  1.00 44.49  ? 347 ALA A CB    1 
ATOM   2696 N  N     . ILE A 1 348 ? -13.505 -10.680 18.604  1.00 55.61  ? 348 ILE A N     1 
ATOM   2697 C  CA    . ILE A 1 348 ? -13.625 -12.095 18.943  1.00 54.10  ? 348 ILE A CA    1 
ATOM   2698 C  C     . ILE A 1 348 ? -14.776 -12.727 18.169  1.00 54.47  ? 348 ILE A C     1 
ATOM   2699 O  O     . ILE A 1 348 ? -14.643 -13.816 17.599  1.00 53.43  ? 348 ILE A O     1 
ATOM   2700 C  CB    . ILE A 1 348 ? -13.805 -12.267 20.463  1.00 51.97  ? 348 ILE A CB    1 
ATOM   2701 C  CG1   . ILE A 1 348 ? -12.589 -11.718 21.212  1.00 54.95  ? 348 ILE A CG1   1 
ATOM   2702 C  CG2   . ILE A 1 348 ? -14.051 -13.726 20.815  1.00 65.28  ? 348 ILE A CG2   1 
ATOM   2703 C  CD1   . ILE A 1 348 ? -11.284 -12.385 20.829  1.00 56.27  ? 348 ILE A CD1   1 
ATOM   2704 N  N     . LYS A 1 349 ? -15.925 -12.048 18.138  1.00 55.56  ? 349 LYS A N     1 
ATOM   2705 C  CA    . LYS A 1 349 ? -17.074 -12.577 17.413  1.00 52.71  ? 349 LYS A CA    1 
ATOM   2706 C  C     . LYS A 1 349 ? -16.793 -12.696 15.921  1.00 54.40  ? 349 LYS A C     1 
ATOM   2707 O  O     . LYS A 1 349 ? -17.383 -13.546 15.245  1.00 51.23  ? 349 LYS A O     1 
ATOM   2708 C  CB    . LYS A 1 349 ? -18.298 -11.691 17.647  1.00 53.08  ? 349 LYS A CB    1 
ATOM   2709 C  CG    . LYS A 1 349 ? -18.725 -11.587 19.102  1.00 73.26  ? 349 LYS A CG    1 
ATOM   2710 C  CD    . LYS A 1 349 ? -19.993 -10.755 19.253  1.00 75.01  ? 349 LYS A CD    1 
ATOM   2711 C  CE    . LYS A 1 349 ? -20.471 -10.721 20.703  1.00 78.73  ? 349 LYS A CE    1 
ATOM   2712 N  NZ    . LYS A 1 349 ? -21.761 -9.983  20.843  1.00 83.22  ? 349 LYS A NZ    1 
ATOM   2713 N  N     . THR A 1 350 ? -15.896 -11.863 15.391  1.00 53.37  ? 350 THR A N     1 
ATOM   2714 C  CA    . THR A 1 350 ? -15.656 -11.839 13.952  1.00 47.42  ? 350 THR A CA    1 
ATOM   2715 C  C     . THR A 1 350 ? -14.728 -12.964 13.507  1.00 47.41  ? 350 THR A C     1 
ATOM   2716 O  O     . THR A 1 350 ? -14.906 -13.521 12.418  1.00 47.53  ? 350 THR A O     1 
ATOM   2717 C  CB    . THR A 1 350 ? -15.072 -10.485 13.542  1.00 49.83  ? 350 THR A CB    1 
ATOM   2718 O  OG1   . THR A 1 350 ? -16.002 -9.444  13.864  1.00 54.69  ? 350 THR A OG1   1 
ATOM   2719 C  CG2   . THR A 1 350 ? -14.788 -10.454 12.047  1.00 46.85  ? 350 THR A CG2   1 
ATOM   2720 N  N     . ILE A 1 351 ? -13.746 -13.320 14.334  1.00 47.90  ? 351 ILE A N     1 
ATOM   2721 C  CA    . ILE A 1 351 ? -12.640 -14.168 13.901  1.00 45.11  ? 351 ILE A CA    1 
ATOM   2722 C  C     . ILE A 1 351 ? -12.915 -15.640 14.180  1.00 50.44  ? 351 ILE A C     1 
ATOM   2723 O  O     . ILE A 1 351 ? -12.016 -16.480 14.063  1.00 51.35  ? 351 ILE A O     1 
ATOM   2724 C  CB    . ILE A 1 351 ? -11.332 -13.728 14.580  1.00 46.22  ? 351 ILE A CB    1 
ATOM   2725 C  CG1   . ILE A 1 351 ? -11.452 -13.879 16.096  1.00 47.94  ? 351 ILE A CG1   1 
ATOM   2726 C  CG2   . ILE A 1 351 ? -11.000 -12.291 14.208  1.00 41.74  ? 351 ILE A CG2   1 
ATOM   2727 C  CD1   . ILE A 1 351 ? -10.183 -13.542 16.844  1.00 50.28  ? 351 ILE A CD1   1 
ATOM   2728 N  N     . GLN A 1 352 ? -14.153 -15.972 14.542  1.00 48.47  ? 352 GLN A N     1 
ATOM   2729 C  CA    . GLN A 1 352 ? -14.485 -17.347 14.896  1.00 55.76  ? 352 GLN A CA    1 
ATOM   2730 C  C     . GLN A 1 352 ? -14.812 -18.220 13.689  1.00 52.68  ? 352 GLN A C     1 
ATOM   2731 O  O     . GLN A 1 352 ? -15.092 -19.411 13.870  1.00 52.73  ? 352 GLN A O     1 
ATOM   2732 C  CB    . GLN A 1 352 ? -15.654 -17.368 15.884  1.00 54.52  ? 352 GLN A CB    1 
ATOM   2733 C  CG    . GLN A 1 352 ? -15.307 -16.822 17.265  1.00 63.71  ? 352 GLN A CG    1 
ATOM   2734 C  CD    . GLN A 1 352 ? -16.464 -16.919 18.243  1.00 72.84  ? 352 GLN A CD    1 
ATOM   2735 O  OE1   . GLN A 1 352 ? -17.587 -17.250 17.862  1.00 80.95  ? 352 GLN A OE1   1 
ATOM   2736 N  NE2   . GLN A 1 352 ? -16.195 -16.630 19.511  1.00 81.74  ? 352 GLN A NE2   1 
ATOM   2737 N  N     . LYS A 1 353 ? -14.777 -17.676 12.472  1.00 47.41  ? 353 LYS A N     1 
ATOM   2738 C  CA    . LYS A 1 353 ? -15.044 -18.477 11.283  1.00 50.29  ? 353 LYS A CA    1 
ATOM   2739 C  C     . LYS A 1 353 ? -14.446 -17.791 10.063  1.00 50.05  ? 353 LYS A C     1 
ATOM   2740 O  O     . LYS A 1 353 ? -14.272 -16.569 10.034  1.00 51.01  ? 353 LYS A O     1 
ATOM   2741 C  CB    . LYS A 1 353 ? -16.548 -18.701 11.079  1.00 54.78  ? 353 LYS A CB    1 
ATOM   2742 C  CG    . LYS A 1 353 ? -17.316 -17.461 10.639  1.00 57.43  ? 353 LYS A CG    1 
ATOM   2743 C  CD    . LYS A 1 353 ? -18.772 -17.797 10.363  1.00 63.03  ? 353 LYS A CD    1 
ATOM   2744 C  CE    . LYS A 1 353 ? -19.544 -16.593 9.848   1.00 63.90  ? 353 LYS A CE    1 
ATOM   2745 N  NZ    . LYS A 1 353 ? -20.953 -16.946 9.510   1.00 73.30  ? 353 LYS A NZ    1 
ATOM   2746 N  N     . ASN A 1 354 ? -14.133 -18.604 9.052   1.00 45.67  ? 354 ASN A N     1 
ATOM   2747 C  CA    . ASN A 1 354 ? -13.642 -18.109 7.767   1.00 43.32  ? 354 ASN A CA    1 
ATOM   2748 C  C     . ASN A 1 354 ? -12.453 -17.170 7.950   1.00 40.79  ? 354 ASN A C     1 
ATOM   2749 O  O     . ASN A 1 354 ? -12.287 -16.192 7.218   1.00 43.69  ? 354 ASN A O     1 
ATOM   2750 C  CB    . ASN A 1 354 ? -14.764 -17.421 6.987   1.00 42.23  ? 354 ASN A CB    1 
ATOM   2751 C  CG    . ASN A 1 354 ? -15.954 -18.332 6.747   1.00 48.58  ? 354 ASN A CG    1 
ATOM   2752 O  OD1   . ASN A 1 354 ? -15.797 -19.512 6.434   1.00 52.97  ? 354 ASN A OD1   1 
ATOM   2753 N  ND2   . ASN A 1 354 ? -17.157 -17.786 6.905   1.00 51.14  ? 354 ASN A ND2   1 
ATOM   2754 N  N     . THR A 1 355 ? -11.611 -17.475 8.933   1.00 40.99  ? 355 THR A N     1 
ATOM   2755 C  CA    . THR A 1 355 ? -10.514 -16.601 9.322   1.00 41.69  ? 355 THR A CA    1 
ATOM   2756 C  C     . THR A 1 355 ? -9.198  -17.359 9.266   1.00 42.65  ? 355 THR A C     1 
ATOM   2757 O  O     . THR A 1 355 ? -9.122  -18.518 9.683   1.00 44.40  ? 355 THR A O     1 
ATOM   2758 C  CB    . THR A 1 355 ? -10.723 -16.041 10.733  1.00 43.64  ? 355 THR A CB    1 
ATOM   2759 O  OG1   . THR A 1 355 ? -11.936 -15.282 10.769  1.00 40.29  ? 355 THR A OG1   1 
ATOM   2760 C  CG2   . THR A 1 355 ? -9.556  -15.148 11.135  1.00 40.45  ? 355 THR A CG2   1 
ATOM   2761 N  N     . ILE A 1 356 ? -8.164  -16.695 8.758   1.00 40.49  ? 356 ILE A N     1 
ATOM   2762 C  CA    . ILE A 1 356 ? -6.822  -17.257 8.665   1.00 41.94  ? 356 ILE A CA    1 
ATOM   2763 C  C     . ILE A 1 356 ? -5.952  -16.586 9.718   1.00 41.04  ? 356 ILE A C     1 
ATOM   2764 O  O     . ILE A 1 356 ? -5.854  -15.354 9.758   1.00 42.75  ? 356 ILE A O     1 
ATOM   2765 C  CB    . ILE A 1 356 ? -6.225  -17.067 7.259   1.00 44.03  ? 356 ILE A CB    1 
ATOM   2766 C  CG1   . ILE A 1 356 ? -7.087  -17.765 6.204   1.00 43.77  ? 356 ILE A CG1   1 
ATOM   2767 C  CG2   . ILE A 1 356 ? -4.791  -17.585 7.211   1.00 39.87  ? 356 ILE A CG2   1 
ATOM   2768 C  CD1   . ILE A 1 356 ? -6.492  -17.725 4.811   1.00 44.64  ? 356 ILE A CD1   1 
ATOM   2769 N  N     . PHE A 1 357 ? -5.325  -17.392 10.568  1.00 39.89  ? 357 PHE A N     1 
ATOM   2770 C  CA    . PHE A 1 357 ? -4.426  -16.903 11.603  1.00 40.20  ? 357 PHE A CA    1 
ATOM   2771 C  C     . PHE A 1 357 ? -2.987  -17.188 11.201  1.00 43.00  ? 357 PHE A C     1 
ATOM   2772 O  O     . PHE A 1 357 ? -2.698  -18.216 10.581  1.00 44.66  ? 357 PHE A O     1 
ATOM   2773 C  CB    . PHE A 1 357 ? -4.730  -17.555 12.956  1.00 40.52  ? 357 PHE A CB    1 
ATOM   2774 C  CG    . PHE A 1 357 ? -6.119  -17.288 13.458  1.00 45.42  ? 357 PHE A CG    1 
ATOM   2775 C  CD1   . PHE A 1 357 ? -7.175  -18.093 13.071  1.00 40.47  ? 357 PHE A CD1   1 
ATOM   2776 C  CD2   . PHE A 1 357 ? -6.368  -16.231 14.319  1.00 47.30  ? 357 PHE A CD2   1 
ATOM   2777 C  CE1   . PHE A 1 357 ? -8.455  -17.852 13.533  1.00 46.19  ? 357 PHE A CE1   1 
ATOM   2778 C  CE2   . PHE A 1 357 ? -7.647  -15.983 14.784  1.00 46.22  ? 357 PHE A CE2   1 
ATOM   2779 C  CZ    . PHE A 1 357 ? -8.692  -16.796 14.389  1.00 46.31  ? 357 PHE A CZ    1 
ATOM   2780 N  N     . THR A 1 358 ? -2.085  -16.274 11.551  1.00 43.16  ? 358 THR A N     1 
ATOM   2781 C  CA    . THR A 1 358 ? -0.671  -16.410 11.223  1.00 46.98  ? 358 THR A CA    1 
ATOM   2782 C  C     . THR A 1 358 ? 0.153   -16.219 12.487  1.00 43.16  ? 358 THR A C     1 
ATOM   2783 O  O     . THR A 1 358 ? 0.134   -15.139 13.086  1.00 44.47  ? 358 THR A O     1 
ATOM   2784 C  CB    . THR A 1 358 ? -0.245  -15.399 10.150  1.00 45.60  ? 358 THR A CB    1 
ATOM   2785 O  OG1   . THR A 1 358 ? -1.064  -15.560 8.986   1.00 41.52  ? 358 THR A OG1   1 
ATOM   2786 C  CG2   . THR A 1 358 ? 1.214   -15.610 9.766   1.00 46.26  ? 358 THR A CG2   1 
ATOM   2787 N  N     . ASN A 1 359 ? 0.864   -17.270 12.892  1.00 48.54  ? 359 ASN A N     1 
ATOM   2788 C  CA    . ASN A 1 359 ? 1.852   -17.218 13.965  1.00 50.05  ? 359 ASN A CA    1 
ATOM   2789 C  C     . ASN A 1 359 ? 1.238   -17.059 15.351  1.00 49.33  ? 359 ASN A C     1 
ATOM   2790 O  O     . ASN A 1 359 ? 1.921   -16.614 16.278  1.00 54.20  ? 359 ASN A O     1 
ATOM   2791 C  CB    . ASN A 1 359 ? 2.873   -16.100 13.724  1.00 49.37  ? 359 ASN A CB    1 
ATOM   2792 C  CG    . ASN A 1 359 ? 3.786   -16.388 12.552  1.00 47.97  ? 359 ASN A CG    1 
ATOM   2793 O  OD1   . ASN A 1 359 ? 4.005   -17.545 12.190  1.00 47.85  ? 359 ASN A OD1   1 
ATOM   2794 N  ND2   . ASN A 1 359 ? 4.333   -15.335 11.959  1.00 50.59  ? 359 ASN A ND2   1 
ATOM   2795 N  N     . VAL A 1 360 ? -0.032  -17.414 15.525  1.00 47.81  ? 360 VAL A N     1 
ATOM   2796 C  CA    . VAL A 1 360 ? -0.610  -17.480 16.862  1.00 50.05  ? 360 VAL A CA    1 
ATOM   2797 C  C     . VAL A 1 360 ? -0.432  -18.901 17.377  1.00 49.81  ? 360 VAL A C     1 
ATOM   2798 O  O     . VAL A 1 360 ? -0.132  -19.821 16.606  1.00 53.96  ? 360 VAL A O     1 
ATOM   2799 C  CB    . VAL A 1 360 ? -2.093  -17.062 16.873  1.00 48.65  ? 360 VAL A CB    1 
ATOM   2800 C  CG1   . VAL A 1 360 ? -2.259  -15.661 16.309  1.00 44.93  ? 360 VAL A CG1   1 
ATOM   2801 C  CG2   . VAL A 1 360 ? -2.932  -18.069 16.103  1.00 43.68  ? 360 VAL A CG2   1 
ATOM   2802 N  N     . ALA A 1 361 ? -0.613  -19.092 18.678  1.00 53.58  ? 361 ALA A N     1 
ATOM   2803 C  CA    . ALA A 1 361 ? -0.500  -20.422 19.253  1.00 53.54  ? 361 ALA A CA    1 
ATOM   2804 C  C     . ALA A 1 361 ? -1.754  -21.236 18.963  1.00 49.15  ? 361 ALA A C     1 
ATOM   2805 O  O     . ALA A 1 361 ? -2.846  -20.693 18.777  1.00 46.54  ? 361 ALA A O     1 
ATOM   2806 C  CB    . ALA A 1 361 ? -0.267  -20.345 20.760  1.00 53.74  ? 361 ALA A CB    1 
ATOM   2807 N  N     . GLU A 1 362 ? -1.587  -22.553 18.928  1.00 48.74  ? 362 GLU A N     1 
ATOM   2808 C  CA    . GLU A 1 362 ? -2.690  -23.482 18.737  1.00 53.41  ? 362 GLU A CA    1 
ATOM   2809 C  C     . GLU A 1 362 ? -2.913  -24.278 20.014  1.00 52.01  ? 362 GLU A C     1 
ATOM   2810 O  O     . GLU A 1 362 ? -1.959  -24.759 20.632  1.00 54.33  ? 362 GLU A O     1 
ATOM   2811 C  CB    . GLU A 1 362 ? -2.416  -24.434 17.568  1.00 47.62  ? 362 GLU A CB    1 
ATOM   2812 C  CG    . GLU A 1 362 ? -3.544  -25.427 17.303  1.00 56.03  ? 362 GLU A CG    1 
ATOM   2813 C  CD    . GLU A 1 362 ? -3.213  -26.407 16.193  1.00 61.02  ? 362 GLU A CD    1 
ATOM   2814 O  OE1   . GLU A 1 362 ? -2.179  -26.215 15.523  1.00 58.02  ? 362 GLU A OE1   1 
ATOM   2815 O  OE2   . GLU A 1 362 ? -3.983  -27.371 15.991  1.00 59.52  ? 362 GLU A OE2   1 
ATOM   2816 N  N     . THR A 1 363 ? -4.173  -24.410 20.408  1.00 54.69  ? 363 THR A N     1 
ATOM   2817 C  CA    . THR A 1 363 ? -4.521  -25.236 21.551  1.00 51.50  ? 363 THR A CA    1 
ATOM   2818 C  C     . THR A 1 363 ? -4.765  -26.674 21.102  1.00 54.51  ? 363 THR A C     1 
ATOM   2819 O  O     . THR A 1 363 ? -5.110  -26.944 19.949  1.00 52.66  ? 363 THR A O     1 
ATOM   2820 C  CB    . THR A 1 363 ? -5.757  -24.691 22.263  1.00 53.04  ? 363 THR A CB    1 
ATOM   2821 O  OG1   . THR A 1 363 ? -6.874  -24.705 21.368  1.00 56.33  ? 363 THR A OG1   1 
ATOM   2822 C  CG2   . THR A 1 363 ? -5.509  -23.268 22.736  1.00 55.16  ? 363 THR A CG2   1 
ATOM   2823 N  N     . SER A 1 364 ? -4.581  -27.604 22.041  1.00 53.85  ? 364 SER A N     1 
ATOM   2824 C  CA    . SER A 1 364 ? -4.691  -29.022 21.715  1.00 55.13  ? 364 SER A CA    1 
ATOM   2825 C  C     . SER A 1 364 ? -6.066  -29.398 21.176  1.00 54.83  ? 364 SER A C     1 
ATOM   2826 O  O     . SER A 1 364 ? -6.182  -30.393 20.453  1.00 59.03  ? 364 SER A O     1 
ATOM   2827 C  CB    . SER A 1 364 ? -4.361  -29.868 22.946  1.00 53.34  ? 364 SER A CB    1 
ATOM   2828 O  OG    . SER A 1 364 ? -5.142  -29.473 24.060  1.00 58.97  ? 364 SER A OG    1 
ATOM   2829 N  N     . ASP A 1 365 ? -7.109  -28.634 21.501  1.00 55.57  ? 365 ASP A N     1 
ATOM   2830 C  CA    . ASP A 1 365 ? -8.453  -28.921 21.021  1.00 52.19  ? 365 ASP A CA    1 
ATOM   2831 C  C     . ASP A 1 365 ? -8.793  -28.178 19.731  1.00 55.57  ? 365 ASP A C     1 
ATOM   2832 O  O     . ASP A 1 365 ? -9.976  -28.061 19.390  1.00 58.91  ? 365 ASP A O     1 
ATOM   2833 C  CB    . ASP A 1 365 ? -9.482  -28.592 22.105  1.00 55.20  ? 365 ASP A CB    1 
ATOM   2834 C  CG    . ASP A 1 365 ? -9.421  -27.146 22.543  1.00 59.16  ? 365 ASP A CG    1 
ATOM   2835 O  OD1   . ASP A 1 365 ? -8.548  -26.410 22.039  1.00 56.85  ? 365 ASP A OD1   1 
ATOM   2836 O  OD2   . ASP A 1 365 ? -10.244 -26.746 23.390  1.00 62.98  ? 365 ASP A OD2   1 
ATOM   2837 N  N     . GLY A 1 366 ? -7.791  -27.676 19.014  1.00 54.64  ? 366 GLY A N     1 
ATOM   2838 C  CA    . GLY A 1 366 ? -8.022  -27.029 17.738  1.00 53.68  ? 366 GLY A CA    1 
ATOM   2839 C  C     . GLY A 1 366 ? -8.365  -25.560 17.799  1.00 57.06  ? 366 GLY A C     1 
ATOM   2840 O  O     . GLY A 1 366 ? -8.985  -25.046 16.861  1.00 53.17  ? 366 GLY A O     1 
ATOM   2841 N  N     . GLY A 1 367 ? -7.981  -24.861 18.867  1.00 57.43  ? 367 GLY A N     1 
ATOM   2842 C  CA    . GLY A 1 367 ? -8.248  -23.454 19.012  1.00 56.53  ? 367 GLY A CA    1 
ATOM   2843 C  C     . GLY A 1 367 ? -7.005  -22.601 18.844  1.00 51.75  ? 367 GLY A C     1 
ATOM   2844 O  O     . GLY A 1 367 ? -5.912  -23.081 18.528  1.00 49.15  ? 367 GLY A O     1 
ATOM   2845 N  N     . VAL A 1 368 ? -7.188  -21.303 19.064  1.00 50.03  ? 368 VAL A N     1 
ATOM   2846 C  CA    . VAL A 1 368 ? -6.111  -20.329 18.963  1.00 52.57  ? 368 VAL A CA    1 
ATOM   2847 C  C     . VAL A 1 368 ? -5.810  -19.796 20.354  1.00 52.15  ? 368 VAL A C     1 
ATOM   2848 O  O     . VAL A 1 368 ? -6.668  -19.802 21.242  1.00 54.52  ? 368 VAL A O     1 
ATOM   2849 C  CB    . VAL A 1 368 ? -6.468  -19.179 17.998  1.00 46.38  ? 368 VAL A CB    1 
ATOM   2850 C  CG1   . VAL A 1 368 ? -6.686  -19.713 16.595  1.00 44.66  ? 368 VAL A CG1   1 
ATOM   2851 C  CG2   . VAL A 1 368 ? -7.706  -18.444 18.485  1.00 48.74  ? 368 VAL A CG2   1 
ATOM   2852 N  N     . TYR A 1 369 ? -4.577  -19.335 20.541  1.00 50.57  ? 369 TYR A N     1 
ATOM   2853 C  CA    . TYR A 1 369 ? -4.180  -18.725 21.800  1.00 52.81  ? 369 TYR A CA    1 
ATOM   2854 C  C     . TYR A 1 369 ? -3.095  -17.692 21.534  1.00 50.74  ? 369 TYR A C     1 
ATOM   2855 O  O     . TYR A 1 369 ? -2.301  -17.831 20.600  1.00 54.29  ? 369 TYR A O     1 
ATOM   2856 C  CB    . TYR A 1 369 ? -3.686  -19.769 22.809  1.00 54.23  ? 369 TYR A CB    1 
ATOM   2857 C  CG    . TYR A 1 369 ? -4.043  -19.426 24.235  1.00 58.49  ? 369 TYR A CG    1 
ATOM   2858 C  CD1   . TYR A 1 369 ? -5.355  -19.509 24.675  1.00 60.14  ? 369 TYR A CD1   1 
ATOM   2859 C  CD2   . TYR A 1 369 ? -3.072  -19.019 25.140  1.00 57.35  ? 369 TYR A CD2   1 
ATOM   2860 C  CE1   . TYR A 1 369 ? -5.695  -19.194 25.976  1.00 63.51  ? 369 TYR A CE1   1 
ATOM   2861 C  CE2   . TYR A 1 369 ? -3.403  -18.699 26.446  1.00 60.28  ? 369 TYR A CE2   1 
ATOM   2862 C  CZ    . TYR A 1 369 ? -4.717  -18.791 26.859  1.00 61.71  ? 369 TYR A CZ    1 
ATOM   2863 O  OH    . TYR A 1 369 ? -5.058  -18.480 28.156  1.00 70.87  ? 369 TYR A OH    1 
ATOM   2864 N  N     . TRP A 1 370 ? -3.073  -16.652 22.363  1.00 51.53  ? 370 TRP A N     1 
ATOM   2865 C  CA    . TRP A 1 370 ? -2.066  -15.606 22.260  1.00 62.43  ? 370 TRP A CA    1 
ATOM   2866 C  C     . TRP A 1 370 ? -2.024  -14.847 23.577  1.00 65.34  ? 370 TRP A C     1 
ATOM   2867 O  O     . TRP A 1 370 ? -2.908  -14.982 24.426  1.00 60.19  ? 370 TRP A O     1 
ATOM   2868 C  CB    . TRP A 1 370 ? -2.347  -14.654 21.089  1.00 50.02  ? 370 TRP A CB    1 
ATOM   2869 C  CG    . TRP A 1 370 ? -3.739  -14.091 21.069  1.00 48.56  ? 370 TRP A CG    1 
ATOM   2870 C  CD1   . TRP A 1 370 ? -4.270  -13.169 21.926  1.00 49.61  ? 370 TRP A CD1   1 
ATOM   2871 C  CD2   . TRP A 1 370 ? -4.773  -14.404 20.129  1.00 48.69  ? 370 TRP A CD2   1 
ATOM   2872 N  NE1   . TRP A 1 370 ? -5.574  -12.899 21.584  1.00 45.34  ? 370 TRP A NE1   1 
ATOM   2873 C  CE2   . TRP A 1 370 ? -5.906  -13.643 20.483  1.00 48.42  ? 370 TRP A CE2   1 
ATOM   2874 C  CE3   . TRP A 1 370 ? -4.852  -15.258 19.024  1.00 45.98  ? 370 TRP A CE3   1 
ATOM   2875 C  CZ2   . TRP A 1 370 ? -7.104  -13.712 19.771  1.00 43.58  ? 370 TRP A CZ2   1 
ATOM   2876 C  CZ3   . TRP A 1 370 ? -6.042  -15.325 18.319  1.00 41.17  ? 370 TRP A CZ3   1 
ATOM   2877 C  CH2   . TRP A 1 370 ? -7.151  -14.559 18.697  1.00 43.23  ? 370 TRP A CH2   1 
ATOM   2878 N  N     . GLU A 1 371 ? -0.977  -14.042 23.733  1.00 59.12  ? 371 GLU A N     1 
ATOM   2879 C  CA    . GLU A 1 371 ? -0.845  -13.216 24.924  1.00 59.91  ? 371 GLU A CA    1 
ATOM   2880 C  C     . GLU A 1 371 ? -1.978  -12.201 24.987  1.00 60.06  ? 371 GLU A C     1 
ATOM   2881 O  O     . GLU A 1 371 ? -2.307  -11.552 23.989  1.00 58.08  ? 371 GLU A O     1 
ATOM   2882 C  CB    . GLU A 1 371 ? 0.508   -12.502 24.929  1.00 60.10  ? 371 GLU A CB    1 
ATOM   2883 C  CG    . GLU A 1 371 ? 1.677   -13.382 25.342  1.00 63.70  ? 371 GLU A CG    1 
ATOM   2884 C  CD    . GLU A 1 371 ? 1.871   -14.572 24.425  1.00 69.23  ? 371 GLU A CD    1 
ATOM   2885 O  OE1   . GLU A 1 371 ? 1.498   -14.477 23.237  1.00 59.34  ? 371 GLU A OE1   1 
ATOM   2886 O  OE2   . GLU A 1 371 ? 2.393   -15.605 24.890  1.00 66.20  ? 371 GLU A OE2   1 
ATOM   2887 N  N     . GLY A 1 372 ? -2.585  -12.078 26.164  1.00 61.75  ? 372 GLY A N     1 
ATOM   2888 C  CA    . GLY A 1 372 ? -3.653  -11.129 26.384  1.00 57.99  ? 372 GLY A CA    1 
ATOM   2889 C  C     . GLY A 1 372 ? -5.041  -11.607 26.016  1.00 58.21  ? 372 GLY A C     1 
ATOM   2890 O  O     . GLY A 1 372 ? -5.999  -10.836 26.164  1.00 65.73  ? 372 GLY A O     1 
ATOM   2891 N  N     . ILE A 1 373 ? -5.189  -12.849 25.547  1.00 54.99  ? 373 ILE A N     1 
ATOM   2892 C  CA    . ILE A 1 373 ? -6.509  -13.357 25.186  1.00 57.43  ? 373 ILE A CA    1 
ATOM   2893 C  C     . ILE A 1 373 ? -7.428  -13.413 26.398  1.00 58.37  ? 373 ILE A C     1 
ATOM   2894 O  O     . ILE A 1 373 ? -8.652  -13.480 26.244  1.00 54.43  ? 373 ILE A O     1 
ATOM   2895 C  CB    . ILE A 1 373 ? -6.390  -14.740 24.510  1.00 55.11  ? 373 ILE A CB    1 
ATOM   2896 C  CG1   . ILE A 1 373 ? -7.647  -15.054 23.696  1.00 56.68  ? 373 ILE A CG1   1 
ATOM   2897 C  CG2   . ILE A 1 373 ? -6.145  -15.825 25.544  1.00 54.19  ? 373 ILE A CG2   1 
ATOM   2898 C  CD1   . ILE A 1 373 ? -7.556  -16.351 22.906  1.00 59.01  ? 373 ILE A CD1   1 
ATOM   2899 N  N     . ASP A 1 374 ? -6.862  -13.397 27.607  1.00 61.42  ? 374 ASP A N     1 
ATOM   2900 C  CA    . ASP A 1 374 ? -7.629  -13.235 28.843  1.00 62.42  ? 374 ASP A CA    1 
ATOM   2901 C  C     . ASP A 1 374 ? -8.711  -14.302 28.993  1.00 65.05  ? 374 ASP A C     1 
ATOM   2902 O  O     . ASP A 1 374 ? -9.768  -14.052 29.579  1.00 69.82  ? 374 ASP A O     1 
ATOM   2903 C  CB    . ASP A 1 374 ? -8.244  -11.833 28.920  1.00 62.54  ? 374 ASP A CB    1 
ATOM   2904 C  CG    . ASP A 1 374 ? -8.713  -11.477 30.315  1.00 76.93  ? 374 ASP A CG    1 
ATOM   2905 O  OD1   . ASP A 1 374 ? -8.484  -12.282 31.240  1.00 82.32  ? 374 ASP A OD1   1 
ATOM   2906 O  OD2   . ASP A 1 374 ? -9.312  -10.394 30.486  1.00 85.98  ? 374 ASP A OD2   1 
ATOM   2907 N  N     . GLU A 1 375 ? -8.459  -15.504 28.479  1.00 65.18  ? 375 GLU A N     1 
ATOM   2908 C  CA    . GLU A 1 375 ? -9.448  -16.578 28.491  1.00 64.06  ? 375 GLU A CA    1 
ATOM   2909 C  C     . GLU A 1 375 ? -8.801  -17.837 29.050  1.00 66.55  ? 375 GLU A C     1 
ATOM   2910 O  O     . GLU A 1 375 ? -7.817  -18.337 28.466  1.00 65.93  ? 375 GLU A O     1 
ATOM   2911 C  CB    . GLU A 1 375 ? -10.006 -16.819 27.087  1.00 61.51  ? 375 GLU A CB    1 
ATOM   2912 C  CG    . GLU A 1 375 ? -11.283 -17.644 27.050  1.00 76.65  ? 375 GLU A CG    1 
ATOM   2913 C  CD    . GLU A 1 375 ? -11.960 -17.600 25.693  1.00 78.71  ? 375 GLU A CD    1 
ATOM   2914 O  OE1   . GLU A 1 375 ? -11.573 -16.751 24.864  1.00 71.88  ? 375 GLU A OE1   1 
ATOM   2915 O  OE2   . GLU A 1 375 ? -12.878 -18.414 25.454  1.00 80.21  ? 375 GLU A OE2   1 
ATOM   2916 N  N     . PRO A 1 376 ? -9.295  -18.379 30.161  1.00 70.58  ? 376 PRO A N     1 
ATOM   2917 C  CA    . PRO A 1 376 ? -8.715  -19.616 30.693  1.00 69.43  ? 376 PRO A CA    1 
ATOM   2918 C  C     . PRO A 1 376 ? -8.968  -20.795 29.767  1.00 68.14  ? 376 PRO A C     1 
ATOM   2919 O  O     . PRO A 1 376 ? -9.973  -20.855 29.055  1.00 70.79  ? 376 PRO A O     1 
ATOM   2920 C  CB    . PRO A 1 376 ? -9.438  -19.802 32.035  1.00 61.06  ? 376 PRO A CB    1 
ATOM   2921 C  CG    . PRO A 1 376 ? -10.027 -18.459 32.356  1.00 72.16  ? 376 PRO A CG    1 
ATOM   2922 C  CD    . PRO A 1 376 ? -10.360 -17.853 31.029  1.00 71.57  ? 376 PRO A CD    1 
ATOM   2923 N  N     . LEU A 1 377 ? -8.039  -21.744 29.792  1.00 68.80  ? 377 LEU A N     1 
ATOM   2924 C  CA    . LEU A 1 377 ? -8.156  -22.974 29.024  1.00 67.14  ? 377 LEU A CA    1 
ATOM   2925 C  C     . LEU A 1 377 ? -8.708  -24.090 29.902  1.00 72.85  ? 377 LEU A C     1 
ATOM   2926 O  O     . LEU A 1 377 ? -8.523  -24.096 31.121  1.00 70.94  ? 377 LEU A O     1 
ATOM   2927 C  CB    . LEU A 1 377 ? -6.802  -23.387 28.443  1.00 68.12  ? 377 LEU A CB    1 
ATOM   2928 C  CG    . LEU A 1 377 ? -6.246  -22.452 27.367  1.00 62.13  ? 377 LEU A CG    1 
ATOM   2929 C  CD1   . LEU A 1 377 ? -4.849  -22.878 26.937  1.00 64.33  ? 377 LEU A CD1   1 
ATOM   2930 C  CD2   . LEU A 1 377 ? -7.188  -22.409 26.176  1.00 65.54  ? 377 LEU A CD2   1 
ATOM   2931 N  N     . ALA A 1 378 ? -9.399  -25.034 29.267  1.00 70.12  ? 378 ALA A N     1 
ATOM   2932 C  CA    . ALA A 1 378 ? -9.966  -26.157 29.989  1.00 73.32  ? 378 ALA A CA    1 
ATOM   2933 C  C     . ALA A 1 378 ? -8.856  -27.062 30.516  1.00 67.96  ? 378 ALA A C     1 
ATOM   2934 O  O     . ALA A 1 378 ? -7.742  -27.068 29.988  1.00 70.68  ? 378 ALA A O     1 
ATOM   2935 C  CB    . ALA A 1 378 ? -10.904 -26.953 29.087  1.00 67.96  ? 378 ALA A CB    1 
ATOM   2936 N  N     . PRO A 1 379 ? -9.134  -27.829 31.567  1.00 72.40  ? 379 PRO A N     1 
ATOM   2937 C  CA    . PRO A 1 379 ? -8.148  -28.806 32.040  1.00 73.41  ? 379 PRO A CA    1 
ATOM   2938 C  C     . PRO A 1 379 ? -7.722  -29.741 30.917  1.00 66.66  ? 379 PRO A C     1 
ATOM   2939 O  O     . PRO A 1 379 ? -8.540  -30.193 30.113  1.00 68.18  ? 379 PRO A O     1 
ATOM   2940 C  CB    . PRO A 1 379 ? -8.898  -29.555 33.147  1.00 74.30  ? 379 PRO A CB    1 
ATOM   2941 C  CG    . PRO A 1 379 ? -9.903  -28.570 33.642  1.00 69.73  ? 379 PRO A CG    1 
ATOM   2942 C  CD    . PRO A 1 379 ? -10.324 -27.778 32.434  1.00 73.14  ? 379 PRO A CD    1 
ATOM   2943 N  N     . GLY A 1 380 ? -6.422  -30.026 30.861  1.00 63.90  ? 380 GLY A N     1 
ATOM   2944 C  CA    . GLY A 1 380 ? -5.871  -30.908 29.859  1.00 63.14  ? 380 GLY A CA    1 
ATOM   2945 C  C     . GLY A 1 380 ? -5.525  -30.256 28.539  1.00 67.06  ? 380 GLY A C     1 
ATOM   2946 O  O     . GLY A 1 380 ? -4.782  -30.849 27.749  1.00 66.03  ? 380 GLY A O     1 
ATOM   2947 N  N     . VAL A 1 381 ? -6.039  -29.057 28.266  1.00 66.79  ? 381 VAL A N     1 
ATOM   2948 C  CA    . VAL A 1 381 ? -5.725  -28.380 27.014  1.00 64.30  ? 381 VAL A CA    1 
ATOM   2949 C  C     . VAL A 1 381 ? -4.270  -27.932 27.035  1.00 62.56  ? 381 VAL A C     1 
ATOM   2950 O  O     . VAL A 1 381 ? -3.822  -27.261 27.974  1.00 63.06  ? 381 VAL A O     1 
ATOM   2951 C  CB    . VAL A 1 381 ? -6.672  -27.192 26.788  1.00 60.62  ? 381 VAL A CB    1 
ATOM   2952 C  CG1   . VAL A 1 381 ? -6.392  -26.540 25.442  1.00 56.10  ? 381 VAL A CG1   1 
ATOM   2953 C  CG2   . VAL A 1 381 ? -8.120  -27.647 26.869  1.00 66.42  ? 381 VAL A CG2   1 
ATOM   2954 N  N     . THR A 1 382 ? -3.523  -28.310 26.003  1.00 61.01  ? 382 THR A N     1 
ATOM   2955 C  CA    . THR A 1 382 ? -2.132  -27.917 25.850  1.00 63.07  ? 382 THR A CA    1 
ATOM   2956 C  C     . THR A 1 382 ? -2.011  -26.874 24.746  1.00 57.77  ? 382 THR A C     1 
ATOM   2957 O  O     . THR A 1 382 ? -2.930  -26.669 23.949  1.00 53.96  ? 382 THR A O     1 
ATOM   2958 C  CB    . THR A 1 382 ? -1.247  -29.130 25.539  1.00 59.52  ? 382 THR A CB    1 
ATOM   2959 O  OG1   . THR A 1 382 ? -1.696  -29.758 24.333  1.00 63.87  ? 382 THR A OG1   1 
ATOM   2960 C  CG2   . THR A 1 382 ? -1.304  -30.132 26.680  1.00 65.08  ? 382 THR A CG2   1 
ATOM   2961 N  N     . ILE A 1 383 ? -0.857  -26.213 24.705  1.00 59.93  ? 383 ILE A N     1 
ATOM   2962 C  CA    . ILE A 1 383 ? -0.626  -25.096 23.798  1.00 61.83  ? 383 ILE A CA    1 
ATOM   2963 C  C     . ILE A 1 383 ? 0.631   -25.362 22.985  1.00 63.38  ? 383 ILE A C     1 
ATOM   2964 O  O     . ILE A 1 383 ? 1.668   -25.744 23.539  1.00 69.63  ? 383 ILE A O     1 
ATOM   2965 C  CB    . ILE A 1 383 ? -0.499  -23.763 24.558  1.00 62.50  ? 383 ILE A CB    1 
ATOM   2966 C  CG1   . ILE A 1 383 ? -1.787  -23.458 25.325  1.00 62.04  ? 383 ILE A CG1   1 
ATOM   2967 C  CG2   . ILE A 1 383 ? -0.167  -22.634 23.598  1.00 63.20  ? 383 ILE A CG2   1 
ATOM   2968 C  CD1   . ILE A 1 383 ? -1.741  -22.157 26.092  1.00 67.73  ? 383 ILE A CD1   1 
ATOM   2969 N  N     . THR A 1 384 ? 0.538   -25.157 21.675  1.00 62.06  ? 384 THR A N     1 
ATOM   2970 C  CA    . THR A 1 384 ? 1.683   -25.209 20.776  1.00 62.81  ? 384 THR A CA    1 
ATOM   2971 C  C     . THR A 1 384 ? 1.997   -23.788 20.330  1.00 60.53  ? 384 THR A C     1 
ATOM   2972 O  O     . THR A 1 384 ? 1.121   -23.092 19.805  1.00 56.92  ? 384 THR A O     1 
ATOM   2973 C  CB    . THR A 1 384 ? 1.402   -26.103 19.568  1.00 62.26  ? 384 THR A CB    1 
ATOM   2974 O  OG1   . THR A 1 384 ? 1.171   -27.447 20.006  1.00 65.57  ? 384 THR A OG1   1 
ATOM   2975 C  CG2   . THR A 1 384 ? 2.581   -26.082 18.603  1.00 63.45  ? 384 THR A CG2   1 
ATOM   2976 N  N     . SER A 1 385 ? 3.238   -23.361 20.541  1.00 62.51  ? 385 SER A N     1 
ATOM   2977 C  CA    . SER A 1 385 ? 3.623   -22.002 20.200  1.00 64.67  ? 385 SER A CA    1 
ATOM   2978 C  C     . SER A 1 385 ? 3.632   -21.810 18.683  1.00 61.25  ? 385 SER A C     1 
ATOM   2979 O  O     . SER A 1 385 ? 3.502   -22.758 17.902  1.00 61.23  ? 385 SER A O     1 
ATOM   2980 C  CB    . SER A 1 385 ? 4.997   -21.672 20.781  1.00 69.59  ? 385 SER A CB    1 
ATOM   2981 O  OG    . SER A 1 385 ? 6.017   -22.406 20.127  1.00 71.31  ? 385 SER A OG    1 
ATOM   2982 N  N     . TRP A 1 386 ? 3.786   -20.549 18.269  1.00 61.26  ? 386 TRP A N     1 
ATOM   2983 C  CA    . TRP A 1 386 ? 3.919   -20.247 16.849  1.00 61.00  ? 386 TRP A CA    1 
ATOM   2984 C  C     . TRP A 1 386 ? 5.192   -20.839 16.264  1.00 64.24  ? 386 TRP A C     1 
ATOM   2985 O  O     . TRP A 1 386 ? 5.289   -20.991 15.041  1.00 61.72  ? 386 TRP A O     1 
ATOM   2986 C  CB    . TRP A 1 386 ? 3.896   -18.735 16.624  1.00 60.07  ? 386 TRP A CB    1 
ATOM   2987 C  CG    . TRP A 1 386 ? 5.153   -18.046 17.056  1.00 59.45  ? 386 TRP A CG    1 
ATOM   2988 C  CD1   . TRP A 1 386 ? 5.497   -17.692 18.326  1.00 61.57  ? 386 TRP A CD1   1 
ATOM   2989 C  CD2   . TRP A 1 386 ? 6.234   -17.626 16.215  1.00 62.00  ? 386 TRP A CD2   1 
ATOM   2990 N  NE1   . TRP A 1 386 ? 6.727   -17.079 18.330  1.00 64.56  ? 386 TRP A NE1   1 
ATOM   2991 C  CE2   . TRP A 1 386 ? 7.199   -17.026 17.045  1.00 65.11  ? 386 TRP A CE2   1 
ATOM   2992 C  CE3   . TRP A 1 386 ? 6.479   -17.701 14.840  1.00 62.09  ? 386 TRP A CE3   1 
ATOM   2993 C  CZ2   . TRP A 1 386 ? 8.390   -16.504 16.547  1.00 62.83  ? 386 TRP A CZ2   1 
ATOM   2994 C  CZ3   . TRP A 1 386 ? 7.662   -17.182 14.348  1.00 58.52  ? 386 TRP A CZ3   1 
ATOM   2995 C  CH2   . TRP A 1 386 ? 8.603   -16.592 15.199  1.00 64.40  ? 386 TRP A CH2   1 
ATOM   2996 N  N     . LYS A 1 387 ? 6.170   -21.166 17.108  1.00 70.00  ? 387 LYS A N     1 
ATOM   2997 C  CA    . LYS A 1 387 ? 7.377   -21.863 16.687  1.00 74.79  ? 387 LYS A CA    1 
ATOM   2998 C  C     . LYS A 1 387 ? 7.163   -23.363 16.531  1.00 79.67  ? 387 LYS A C     1 
ATOM   2999 O  O     . LYS A 1 387 ? 8.140   -24.101 16.364  1.00 83.02  ? 387 LYS A O     1 
ATOM   3000 C  CB    . LYS A 1 387 ? 8.512   -21.602 17.684  1.00 75.70  ? 387 LYS A CB    1 
ATOM   3001 C  CG    . LYS A 1 387 ? 9.001   -20.161 17.722  1.00 73.03  ? 387 LYS A CG    1 
ATOM   3002 C  CD    . LYS A 1 387 ? 10.102  -19.976 18.758  1.00 80.75  ? 387 LYS A CD    1 
ATOM   3003 C  CE    . LYS A 1 387 ? 10.647  -18.555 18.750  1.00 84.24  ? 387 LYS A CE    1 
ATOM   3004 N  NZ    . LYS A 1 387 ? 11.308  -18.214 17.458  1.00 85.00  ? 387 LYS A NZ    1 
ATOM   3005 N  N     . ASN A 1 388 ? 5.914   -23.828 16.591  1.00 73.90  ? 388 ASN A N     1 
ATOM   3006 C  CA    . ASN A 1 388 ? 5.593   -25.244 16.414  1.00 74.36  ? 388 ASN A CA    1 
ATOM   3007 C  C     . ASN A 1 388 ? 6.278   -26.098 17.481  1.00 77.69  ? 388 ASN A C     1 
ATOM   3008 O  O     . ASN A 1 388 ? 6.901   -27.120 17.188  1.00 79.43  ? 388 ASN A O     1 
ATOM   3009 C  CB    . ASN A 1 388 ? 5.966   -25.715 15.006  1.00 70.11  ? 388 ASN A CB    1 
ATOM   3010 C  CG    . ASN A 1 388 ? 5.235   -26.978 14.600  1.00 74.03  ? 388 ASN A CG    1 
ATOM   3011 O  OD1   . ASN A 1 388 ? 4.076   -27.182 14.961  1.00 73.11  ? 388 ASN A OD1   1 
ATOM   3012 N  ND2   . ASN A 1 388 ? 5.912   -27.836 13.845  1.00 81.23  ? 388 ASN A ND2   1 
ATOM   3013 N  N     . LYS A 1 389 ? 6.157   -25.667 18.736  1.00 73.10  ? 389 LYS A N     1 
ATOM   3014 C  CA    . LYS A 1 389 ? 6.769   -26.364 19.857  1.00 77.56  ? 389 LYS A CA    1 
ATOM   3015 C  C     . LYS A 1 389 ? 5.826   -26.341 21.051  1.00 79.44  ? 389 LYS A C     1 
ATOM   3016 O  O     . LYS A 1 389 ? 4.986   -25.446 21.181  1.00 74.34  ? 389 LYS A O     1 
ATOM   3017 C  CB    . LYS A 1 389 ? 8.114   -25.738 20.252  1.00 82.19  ? 389 LYS A CB    1 
ATOM   3018 C  CG    . LYS A 1 389 ? 9.133   -25.689 19.130  1.00 87.45  ? 389 LYS A CG    1 
ATOM   3019 C  CD    . LYS A 1 389 ? 10.403  -24.987 19.579  1.00 91.05  ? 389 LYS A CD    1 
ATOM   3020 C  CE    . LYS A 1 389 ? 11.390  -24.846 18.432  1.00 92.09  ? 389 LYS A CE    1 
ATOM   3021 N  NZ    . LYS A 1 389 ? 12.603  -24.090 18.845  1.00 91.81  ? 389 LYS A NZ    1 
ATOM   3022 N  N     . GLU A 1 390 ? 5.975   -27.337 21.921  1.00 83.48  ? 390 GLU A N     1 
ATOM   3023 C  CA    . GLU A 1 390 ? 5.190   -27.380 23.147  1.00 87.35  ? 390 GLU A CA    1 
ATOM   3024 C  C     . GLU A 1 390 ? 5.517   -26.167 24.007  1.00 85.08  ? 390 GLU A C     1 
ATOM   3025 O  O     . GLU A 1 390 ? 6.688   -25.873 24.268  1.00 87.24  ? 390 GLU A O     1 
ATOM   3026 C  CB    . GLU A 1 390 ? 5.474   -28.674 23.913  1.00 89.24  ? 390 GLU A CB    1 
ATOM   3027 C  CG    . GLU A 1 390 ? 4.295   -29.198 24.721  1.00 97.77  ? 390 GLU A CG    1 
ATOM   3028 C  CD    . GLU A 1 390 ? 3.138   -29.644 23.846  1.00 102.31 ? 390 GLU A CD    1 
ATOM   3029 O  OE1   . GLU A 1 390 ? 3.139   -29.314 22.641  1.00 100.02 ? 390 GLU A OE1   1 
ATOM   3030 O  OE2   . GLU A 1 390 ? 2.228   -30.327 24.360  1.00 103.72 ? 390 GLU A OE2   1 
ATOM   3031 N  N     . TRP A 1 391 ? 4.479   -25.459 24.446  1.00 81.34  ? 391 TRP A N     1 
ATOM   3032 C  CA    . TRP A 1 391 ? 4.642   -24.185 25.133  1.00 86.60  ? 391 TRP A CA    1 
ATOM   3033 C  C     . TRP A 1 391 ? 3.935   -24.225 26.479  1.00 89.70  ? 391 TRP A C     1 
ATOM   3034 O  O     . TRP A 1 391 ? 2.771   -24.627 26.562  1.00 85.25  ? 391 TRP A O     1 
ATOM   3035 C  CB    . TRP A 1 391 ? 4.096   -23.034 24.281  1.00 76.39  ? 391 TRP A CB    1 
ATOM   3036 C  CG    . TRP A 1 391 ? 4.162   -21.696 24.951  1.00 82.46  ? 391 TRP A CG    1 
ATOM   3037 C  CD1   . TRP A 1 391 ? 5.157   -20.770 24.840  1.00 80.05  ? 391 TRP A CD1   1 
ATOM   3038 C  CD2   . TRP A 1 391 ? 3.186   -21.131 25.835  1.00 88.38  ? 391 TRP A CD2   1 
ATOM   3039 N  NE1   . TRP A 1 391 ? 4.863   -19.665 25.601  1.00 80.85  ? 391 TRP A NE1   1 
ATOM   3040 C  CE2   . TRP A 1 391 ? 3.658   -19.862 26.223  1.00 84.93  ? 391 TRP A CE2   1 
ATOM   3041 C  CE3   . TRP A 1 391 ? 1.959   -21.577 26.337  1.00 87.55  ? 391 TRP A CE3   1 
ATOM   3042 C  CZ2   . TRP A 1 391 ? 2.946   -19.033 27.088  1.00 87.52  ? 391 TRP A CZ2   1 
ATOM   3043 C  CZ3   . TRP A 1 391 ? 1.255   -20.754 27.197  1.00 87.43  ? 391 TRP A CZ3   1 
ATOM   3044 C  CH2   . TRP A 1 391 ? 1.750   -19.495 27.563  1.00 85.44  ? 391 TRP A CH2   1 
ATOM   3045 N  N     . ARG A 1 392 ? 4.643   -23.805 27.526  1.00 95.34  ? 392 ARG A N     1 
ATOM   3046 C  CA    . ARG A 1 392 ? 4.077   -23.638 28.852  1.00 102.08 ? 392 ARG A CA    1 
ATOM   3047 C  C     . ARG A 1 392 ? 4.178   -22.180 29.281  1.00 107.73 ? 392 ARG A C     1 
ATOM   3048 O  O     . ARG A 1 392 ? 5.122   -21.480 28.899  1.00 106.41 ? 392 ARG A O     1 
ATOM   3049 C  CB    . ARG A 1 392 ? 4.788   -24.515 29.891  1.00 109.81 ? 392 ARG A CB    1 
ATOM   3050 C  CG    . ARG A 1 392 ? 4.645   -26.010 29.669  1.00 106.68 ? 392 ARG A CG    1 
ATOM   3051 C  CD    . ARG A 1 392 ? 5.067   -26.774 30.914  1.00 109.15 ? 392 ARG A CD    1 
ATOM   3052 N  NE    . ARG A 1 392 ? 6.362   -26.325 31.413  1.00 111.71 ? 392 ARG A NE    1 
ATOM   3053 C  CZ    . ARG A 1 392 ? 6.902   -26.719 32.558  1.00 114.96 ? 392 ARG A CZ    1 
ATOM   3054 N  NH1   . ARG A 1 392 ? 6.283   -27.572 33.357  1.00 110.31 ? 392 ARG A NH1   1 
ATOM   3055 N  NH2   . ARG A 1 392 ? 8.093   -26.242 32.912  1.00 111.88 ? 392 ARG A NH2   1 
ATOM   3056 N  N     . PRO A 1 393 ? 3.222   -21.691 30.075  1.00 113.43 ? 393 PRO A N     1 
ATOM   3057 C  CA    . PRO A 1 393 ? 3.300   -20.299 30.548  1.00 116.40 ? 393 PRO A CA    1 
ATOM   3058 C  C     . PRO A 1 393 ? 4.532   -20.005 31.389  1.00 125.65 ? 393 PRO A C     1 
ATOM   3059 O  O     . PRO A 1 393 ? 4.802   -18.828 31.664  1.00 127.61 ? 393 PRO A O     1 
ATOM   3060 C  CB    . PRO A 1 393 ? 2.014   -20.132 31.370  1.00 119.22 ? 393 PRO A CB    1 
ATOM   3061 C  CG    . PRO A 1 393 ? 1.090   -21.191 30.851  1.00 116.37 ? 393 PRO A CG    1 
ATOM   3062 C  CD    . PRO A 1 393 ? 1.973   -22.349 30.492  1.00 114.99 ? 393 PRO A CD    1 
ATOM   3063 N  N     . GLN A 1 394 ? 5.286   -21.025 31.806  1.00 129.56 ? 394 GLN A N     1 
ATOM   3064 C  CA    . GLN A 1 394 ? 6.476   -20.803 32.617  1.00 135.37 ? 394 GLN A CA    1 
ATOM   3065 C  C     . GLN A 1 394 ? 7.674   -20.345 31.796  1.00 136.64 ? 394 GLN A C     1 
ATOM   3066 O  O     . GLN A 1 394 ? 8.572   -19.697 32.346  1.00 141.48 ? 394 GLN A O     1 
ATOM   3067 C  CB    . GLN A 1 394 ? 6.836   -22.076 33.389  1.00 134.01 ? 394 GLN A CB    1 
ATOM   3068 C  CG    . GLN A 1 394 ? 5.964   -22.333 34.611  1.00 139.87 ? 394 GLN A CG    1 
ATOM   3069 C  CD    . GLN A 1 394 ? 4.509   -22.569 34.257  1.00 138.69 ? 394 GLN A CD    1 
ATOM   3070 O  OE1   . GLN A 1 394 ? 4.191   -23.019 33.157  1.00 132.57 ? 394 GLN A OE1   1 
ATOM   3071 N  NE2   . GLN A 1 394 ? 3.615   -22.260 35.190  1.00 142.12 ? 394 GLN A NE2   1 
ATOM   3072 N  N     . ASP A 1 395 ? 7.712   -20.664 30.505  1.00 134.16 ? 395 ASP A N     1 
ATOM   3073 C  CA    . ASP A 1 395 ? 8.792   -20.202 29.650  1.00 137.74 ? 395 ASP A CA    1 
ATOM   3074 C  C     . ASP A 1 395 ? 8.683   -18.699 29.410  1.00 134.37 ? 395 ASP A C     1 
ATOM   3075 O  O     . ASP A 1 395 ? 7.619   -18.090 29.557  1.00 132.98 ? 395 ASP A O     1 
ATOM   3076 C  CB    . ASP A 1 395 ? 8.777   -20.942 28.311  1.00 132.12 ? 395 ASP A CB    1 
ATOM   3077 C  CG    . ASP A 1 395 ? 9.327   -22.351 28.415  1.00 138.04 ? 395 ASP A CG    1 
ATOM   3078 O  OD1   . ASP A 1 395 ? 10.409  -22.527 29.013  1.00 141.54 ? 395 ASP A OD1   1 
ATOM   3079 O  OD2   . ASP A 1 395 ? 8.676   -23.283 27.897  1.00 130.46 ? 395 ASP A OD2   1 
ATOM   3080 N  N     . GLU A 1 396 ? 9.812   -18.097 29.036  1.00 138.85 ? 396 GLU A N     1 
ATOM   3081 C  CA    . GLU A 1 396 ? 9.820   -16.690 28.659  1.00 137.01 ? 396 GLU A CA    1 
ATOM   3082 C  C     . GLU A 1 396 ? 9.362   -16.474 27.225  1.00 134.40 ? 396 GLU A C     1 
ATOM   3083 O  O     . GLU A 1 396 ? 8.931   -15.367 26.884  1.00 131.56 ? 396 GLU A O     1 
ATOM   3084 C  CB    . GLU A 1 396 ? 11.219  -16.098 28.844  1.00 138.51 ? 396 GLU A CB    1 
ATOM   3085 C  CG    . GLU A 1 396 ? 11.285  -14.598 28.610  1.00 140.02 ? 396 GLU A CG    1 
ATOM   3086 C  CD    . GLU A 1 396 ? 12.701  -14.060 28.659  1.00 141.05 ? 396 GLU A CD    1 
ATOM   3087 O  OE1   . GLU A 1 396 ? 13.644  -14.842 28.418  1.00 144.04 ? 396 GLU A OE1   1 
ATOM   3088 O  OE2   . GLU A 1 396 ? 12.871  -12.856 28.941  1.00 140.92 ? 396 GLU A OE2   1 
ATOM   3089 N  N     . GLU A 1 397 ? 9.448   -17.498 26.389  1.00 114.50 ? 397 GLU A N     1 
ATOM   3090 C  CA    . GLU A 1 397 ? 9.003   -17.403 25.007  1.00 102.48 ? 397 GLU A CA    1 
ATOM   3091 C  C     . GLU A 1 397 ? 7.499   -17.171 24.951  1.00 93.66  ? 397 GLU A C     1 
ATOM   3092 O  O     . GLU A 1 397 ? 6.735   -17.988 25.485  1.00 89.74  ? 397 GLU A O     1 
ATOM   3093 C  CB    . GLU A 1 397 ? 9.361   -18.679 24.249  1.00 99.90  ? 397 GLU A CB    1 
ATOM   3094 C  CG    . GLU A 1 397 ? 10.842  -18.859 23.979  1.00 103.90 ? 397 GLU A CG    1 
ATOM   3095 C  CD    . GLU A 1 397 ? 11.310  -18.078 22.769  1.00 106.31 ? 397 GLU A CD    1 
ATOM   3096 O  OE1   . GLU A 1 397 ? 10.476  -17.790 21.886  1.00 103.15 ? 397 GLU A OE1   1 
ATOM   3097 O  OE2   . GLU A 1 397 ? 12.512  -17.752 22.701  1.00 106.61 ? 397 GLU A OE2   1 
ATOM   3098 N  N     . PRO A 1 398 ? 7.032   -16.091 24.329  1.00 86.88  ? 398 PRO A N     1 
ATOM   3099 C  CA    . PRO A 1 398 ? 5.592   -15.954 24.094  1.00 79.57  ? 398 PRO A CA    1 
ATOM   3100 C  C     . PRO A 1 398 ? 5.108   -17.020 23.124  1.00 72.55  ? 398 PRO A C     1 
ATOM   3101 O  O     . PRO A 1 398 ? 5.798   -17.370 22.164  1.00 75.22  ? 398 PRO A O     1 
ATOM   3102 C  CB    . PRO A 1 398 ? 5.461   -14.547 23.499  1.00 73.99  ? 398 PRO A CB    1 
ATOM   3103 C  CG    . PRO A 1 398 ? 6.801   -14.274 22.886  1.00 78.95  ? 398 PRO A CG    1 
ATOM   3104 C  CD    . PRO A 1 398 ? 7.800   -14.966 23.770  1.00 85.23  ? 398 PRO A CD    1 
ATOM   3105 N  N     . CYS A 1 399 ? 3.910   -17.546 23.388  1.00 68.20  ? 399 CYS A N     1 
ATOM   3106 C  CA    . CYS A 1 399 ? 3.360   -18.599 22.543  1.00 71.75  ? 399 CYS A CA    1 
ATOM   3107 C  C     . CYS A 1 399 ? 2.896   -18.083 21.187  1.00 60.10  ? 399 CYS A C     1 
ATOM   3108 O  O     . CYS A 1 399 ? 2.829   -18.864 20.232  1.00 62.46  ? 399 CYS A O     1 
ATOM   3109 C  CB    . CYS A 1 399 ? 2.200   -19.298 23.257  1.00 63.64  ? 399 CYS A CB    1 
ATOM   3110 S  SG    . CYS A 1 399 ? 0.734   -18.274 23.483  1.00 63.42  ? 399 CYS A SG    1 
ATOM   3111 N  N     . ALA A 1 400 ? 2.577   -16.795 21.081  1.00 57.25  ? 400 ALA A N     1 
ATOM   3112 C  CA    . ALA A 1 400 ? 2.207   -16.167 19.822  1.00 55.72  ? 400 ALA A CA    1 
ATOM   3113 C  C     . ALA A 1 400 ? 3.166   -15.022 19.529  1.00 60.97  ? 400 ALA A C     1 
ATOM   3114 O  O     . ALA A 1 400 ? 3.547   -14.275 20.436  1.00 64.75  ? 400 ALA A O     1 
ATOM   3115 C  CB    . ALA A 1 400 ? 0.764   -15.650 19.865  1.00 59.07  ? 400 ALA A CB    1 
ATOM   3116 N  N     . HIS A 1 401 ? 3.561   -14.890 18.265  1.00 57.55  ? 401 HIS A N     1 
ATOM   3117 C  CA    . HIS A 1 401 ? 4.469   -13.814 17.896  1.00 54.97  ? 401 HIS A CA    1 
ATOM   3118 C  C     . HIS A 1 401 ? 3.787   -12.466 18.120  1.00 54.93  ? 401 HIS A C     1 
ATOM   3119 O  O     . HIS A 1 401 ? 2.586   -12.324 17.858  1.00 55.71  ? 401 HIS A O     1 
ATOM   3120 C  CB    . HIS A 1 401 ? 4.918   -13.944 16.438  1.00 53.14  ? 401 HIS A CB    1 
ATOM   3121 C  CG    . HIS A 1 401 ? 5.986   -12.968 16.042  1.00 56.51  ? 401 HIS A CG    1 
ATOM   3122 N  ND1   . HIS A 1 401 ? 5.705   -11.747 15.467  1.00 52.31  ? 401 HIS A ND1   1 
ATOM   3123 C  CD2   . HIS A 1 401 ? 7.336   -13.035 16.136  1.00 54.79  ? 401 HIS A CD2   1 
ATOM   3124 C  CE1   . HIS A 1 401 ? 6.834   -11.104 15.226  1.00 55.82  ? 401 HIS A CE1   1 
ATOM   3125 N  NE2   . HIS A 1 401 ? 7.839   -11.865 15.621  1.00 52.74  ? 401 HIS A NE2   1 
ATOM   3126 N  N     . PRO A 1 402 ? 4.515   -11.462 18.611  1.00 53.09  ? 402 PRO A N     1 
ATOM   3127 C  CA    . PRO A 1 402 ? 3.882   -10.159 18.872  1.00 52.61  ? 402 PRO A CA    1 
ATOM   3128 C  C     . PRO A 1 402 ? 3.200   -9.557  17.656  1.00 52.20  ? 402 PRO A C     1 
ATOM   3129 O  O     . PRO A 1 402 ? 2.229   -8.804  17.812  1.00 58.75  ? 402 PRO A O     1 
ATOM   3130 C  CB    . PRO A 1 402 ? 5.057   -9.294  19.349  1.00 51.65  ? 402 PRO A CB    1 
ATOM   3131 C  CG    . PRO A 1 402 ? 6.032   -10.277 19.921  1.00 53.43  ? 402 PRO A CG    1 
ATOM   3132 C  CD    . PRO A 1 402 ? 5.917   -11.502 19.060  1.00 56.81  ? 402 PRO A CD    1 
ATOM   3133 N  N     . ASN A 1 403 ? 3.674   -9.859  16.449  1.00 50.47  ? 403 ASN A N     1 
ATOM   3134 C  CA    . ASN A 1 403 ? 3.054   -9.374  15.225  1.00 53.83  ? 403 ASN A CA    1 
ATOM   3135 C  C     . ASN A 1 403 ? 2.102   -10.392 14.610  1.00 54.72  ? 403 ASN A C     1 
ATOM   3136 O  O     . ASN A 1 403 ? 1.681   -10.215 13.462  1.00 46.12  ? 403 ASN A O     1 
ATOM   3137 C  CB    . ASN A 1 403 ? 4.124   -8.983  14.203  1.00 52.42  ? 403 ASN A CB    1 
ATOM   3138 C  CG    . ASN A 1 403 ? 3.580   -8.084  13.103  1.00 58.91  ? 403 ASN A CG    1 
ATOM   3139 O  OD1   . ASN A 1 403 ? 2.758   -7.204  13.356  1.00 57.58  ? 403 ASN A OD1   1 
ATOM   3140 N  ND2   . ASN A 1 403 ? 4.033   -8.307  11.875  1.00 53.12  ? 403 ASN A ND2   1 
ATOM   3141 N  N     . SER A 1 404 ? 1.763   -11.455 15.338  1.00 46.90  ? 404 SER A N     1 
ATOM   3142 C  CA    . SER A 1 404 ? 0.817   -12.436 14.827  1.00 47.92  ? 404 SER A CA    1 
ATOM   3143 C  C     . SER A 1 404 ? -0.493  -11.751 14.450  1.00 49.01  ? 404 SER A C     1 
ATOM   3144 O  O     . SER A 1 404 ? -0.821  -10.664 14.935  1.00 52.11  ? 404 SER A O     1 
ATOM   3145 C  CB    . SER A 1 404 ? 0.574   -13.539 15.858  1.00 50.54  ? 404 SER A CB    1 
ATOM   3146 O  OG    . SER A 1 404 ? 0.105   -13.004 17.082  1.00 50.79  ? 404 SER A OG    1 
ATOM   3147 N  N     . ARG A 1 405 ? -1.253  -12.406 13.575  1.00 46.04  ? 405 ARG A N     1 
ATOM   3148 C  CA    . ARG A 1 405 ? -2.366  -11.753 12.905  1.00 45.04  ? 405 ARG A CA    1 
ATOM   3149 C  C     . ARG A 1 405 ? -3.550  -12.693 12.755  1.00 42.53  ? 405 ARG A C     1 
ATOM   3150 O  O     . ARG A 1 405 ? -3.394  -13.915 12.685  1.00 45.38  ? 405 ARG A O     1 
ATOM   3151 C  CB    . ARG A 1 405 ? -1.949  -11.265 11.511  1.00 47.36  ? 405 ARG A CB    1 
ATOM   3152 C  CG    . ARG A 1 405 ? -0.838  -10.244 11.513  1.00 46.35  ? 405 ARG A CG    1 
ATOM   3153 C  CD    . ARG A 1 405 ? -1.399  -8.858  11.744  1.00 46.14  ? 405 ARG A CD    1 
ATOM   3154 N  NE    . ARG A 1 405 ? -0.353  -7.857  11.918  1.00 51.77  ? 405 ARG A NE    1 
ATOM   3155 C  CZ    . ARG A 1 405 ? -0.550  -6.551  11.815  1.00 49.98  ? 405 ARG A CZ    1 
ATOM   3156 N  NH1   . ARG A 1 405 ? -1.737  -6.052  11.512  1.00 44.58  ? 405 ARG A NH1   1 
ATOM   3157 N  NH2   . ARG A 1 405 ? 0.471   -5.723  12.018  1.00 49.26  ? 405 ARG A NH2   1 
ATOM   3158 N  N     . PHE A 1 406 ? -4.739  -12.099 12.710  1.00 42.18  ? 406 PHE A N     1 
ATOM   3159 C  CA    . PHE A 1 406 ? -5.912  -12.727 12.123  1.00 40.33  ? 406 PHE A CA    1 
ATOM   3160 C  C     . PHE A 1 406 ? -6.266  -11.998 10.834  1.00 40.28  ? 406 PHE A C     1 
ATOM   3161 O  O     . PHE A 1 406 ? -6.068  -10.786 10.715  1.00 46.52  ? 406 PHE A O     1 
ATOM   3162 C  CB    . PHE A 1 406 ? -7.118  -12.723 13.087  1.00 43.43  ? 406 PHE A CB    1 
ATOM   3163 C  CG    . PHE A 1 406 ? -7.472  -11.360 13.630  1.00 44.45  ? 406 PHE A CG    1 
ATOM   3164 C  CD1   . PHE A 1 406 ? -8.174  -10.448 12.858  1.00 47.62  ? 406 PHE A CD1   1 
ATOM   3165 C  CD2   . PHE A 1 406 ? -7.134  -11.010 14.924  1.00 42.78  ? 406 PHE A CD2   1 
ATOM   3166 C  CE1   . PHE A 1 406 ? -8.508  -9.199  13.364  1.00 46.33  ? 406 PHE A CE1   1 
ATOM   3167 C  CE2   . PHE A 1 406 ? -7.464  -9.766  15.436  1.00 50.88  ? 406 PHE A CE2   1 
ATOM   3168 C  CZ    . PHE A 1 406 ? -8.153  -8.859  14.655  1.00 51.50  ? 406 PHE A CZ    1 
ATOM   3169 N  N     . CYS A 1 407 ? -6.763  -12.757 9.861   1.00 38.84  ? 407 CYS A N     1 
ATOM   3170 C  CA    . CYS A 1 407 ? -7.217  -12.224 8.578   1.00 42.49  ? 407 CYS A CA    1 
ATOM   3171 C  C     . CYS A 1 407 ? -8.677  -12.634 8.415   1.00 39.37  ? 407 CYS A C     1 
ATOM   3172 O  O     . CYS A 1 407 ? -8.968  -13.787 8.081   1.00 42.43  ? 407 CYS A O     1 
ATOM   3173 C  CB    . CYS A 1 407 ? -6.354  -12.742 7.430   1.00 40.80  ? 407 CYS A CB    1 
ATOM   3174 S  SG    . CYS A 1 407 ? -6.714  -12.018 5.820   1.00 41.81  ? 407 CYS A SG    1 
ATOM   3175 N  N     . THR A 1 408 ? -9.591  -11.698 8.647   1.00 43.10  ? 408 THR A N     1 
ATOM   3176 C  CA    . THR A 1 408 ? -11.001 -12.032 8.755   1.00 39.59  ? 408 THR A CA    1 
ATOM   3177 C  C     . THR A 1 408 ? -11.839 -11.187 7.806   1.00 38.16  ? 408 THR A C     1 
ATOM   3178 O  O     . THR A 1 408 ? -11.510 -10.027 7.538   1.00 44.17  ? 408 THR A O     1 
ATOM   3179 C  CB    . THR A 1 408 ? -11.502 -11.823 10.191  1.00 44.16  ? 408 THR A CB    1 
ATOM   3180 O  OG1   . THR A 1 408 ? -12.766 -12.479 10.359  1.00 41.69  ? 408 THR A OG1   1 
ATOM   3181 C  CG2   . THR A 1 408 ? -11.654 -10.335 10.488  1.00 38.43  ? 408 THR A CG2   1 
ATOM   3182 N  N     . PRO A 1 409 ? -12.934 -11.746 7.292   1.00 38.50  ? 409 PRO A N     1 
ATOM   3183 C  CA    . PRO A 1 409 ? -13.808 -10.977 6.393   1.00 38.60  ? 409 PRO A CA    1 
ATOM   3184 C  C     . PRO A 1 409 ? -14.546 -9.885  7.157   1.00 44.84  ? 409 PRO A C     1 
ATOM   3185 O  O     . PRO A 1 409 ? -15.130 -10.132 8.215   1.00 42.75  ? 409 PRO A O     1 
ATOM   3186 C  CB    . PRO A 1 409 ? -14.776 -12.036 5.848   1.00 44.66  ? 409 PRO A CB    1 
ATOM   3187 C  CG    . PRO A 1 409 ? -14.120 -13.362 6.140   1.00 45.60  ? 409 PRO A CG    1 
ATOM   3188 C  CD    . PRO A 1 409 ? -13.356 -13.150 7.406   1.00 42.53  ? 409 PRO A CD    1 
ATOM   3189 N  N     . ALA A 1 410 ? -14.519 -8.669  6.607   1.00 41.28  ? 410 ALA A N     1 
ATOM   3190 C  CA    . ALA A 1 410 ? -15.179 -7.548  7.268   1.00 46.53  ? 410 ALA A CA    1 
ATOM   3191 C  C     . ALA A 1 410 ? -16.676 -7.789  7.414   1.00 49.12  ? 410 ALA A C     1 
ATOM   3192 O  O     . ALA A 1 410 ? -17.286 -7.365  8.403   1.00 51.40  ? 410 ALA A O     1 
ATOM   3193 C  CB    . ALA A 1 410 ? -14.916 -6.256  6.495   1.00 42.63  ? 410 ALA A CB    1 
ATOM   3194 N  N     . SER A 1 411 ? -17.285 -8.479  6.447   1.00 48.08  ? 411 SER A N     1 
ATOM   3195 C  CA    . SER A 1 411 ? -18.728 -8.691  6.474   1.00 50.15  ? 411 SER A CA    1 
ATOM   3196 C  C     . SER A 1 411 ? -19.185 -9.431  7.723   1.00 48.53  ? 411 SER A C     1 
ATOM   3197 O  O     . SER A 1 411 ? -20.361 -9.333  8.091   1.00 56.54  ? 411 SER A O     1 
ATOM   3198 C  CB    . SER A 1 411 ? -19.172 -9.459  5.226   1.00 49.93  ? 411 SER A CB    1 
ATOM   3199 O  OG    . SER A 1 411 ? -18.645 -10.773 5.221   1.00 51.32  ? 411 SER A OG    1 
ATOM   3200 N  N     . GLN A 1 412 ? -18.288 -10.166 8.381   1.00 47.29  ? 412 GLN A N     1 
ATOM   3201 C  CA    . GLN A 1 412 ? -18.654 -10.939 9.560   1.00 51.75  ? 412 GLN A CA    1 
ATOM   3202 C  C     . GLN A 1 412 ? -18.638 -10.120 10.845  1.00 54.98  ? 412 GLN A C     1 
ATOM   3203 O  O     . GLN A 1 412 ? -19.096 -10.618 11.878  1.00 58.65  ? 412 GLN A O     1 
ATOM   3204 C  CB    . GLN A 1 412 ? -17.717 -12.141 9.706   1.00 47.81  ? 412 GLN A CB    1 
ATOM   3205 C  CG    . GLN A 1 412 ? -17.807 -13.152 8.571   1.00 46.97  ? 412 GLN A CG    1 
ATOM   3206 C  CD    . GLN A 1 412 ? -16.801 -14.279 8.723   1.00 47.40  ? 412 GLN A CD    1 
ATOM   3207 O  OE1   . GLN A 1 412 ? -16.814 -15.248 7.966   1.00 57.33  ? 412 GLN A OE1   1 
ATOM   3208 N  NE2   . GLN A 1 412 ? -15.918 -14.152 9.707   1.00 45.24  ? 412 GLN A NE2   1 
ATOM   3209 N  N     . CYS A 1 413 ? -18.126 -8.896  10.812  1.00 54.87  ? 413 CYS A N     1 
ATOM   3210 C  CA    . CYS A 1 413 ? -18.124 -8.057  12.006  1.00 54.68  ? 413 CYS A CA    1 
ATOM   3211 C  C     . CYS A 1 413 ? -19.559 -7.754  12.422  1.00 59.22  ? 413 CYS A C     1 
ATOM   3212 O  O     . CYS A 1 413 ? -20.334 -7.223  11.619  1.00 57.16  ? 413 CYS A O     1 
ATOM   3213 C  CB    . CYS A 1 413 ? -17.357 -6.763  11.756  1.00 51.24  ? 413 CYS A CB    1 
ATOM   3214 S  SG    . CYS A 1 413 ? -17.180 -5.706  13.214  1.00 53.47  ? 413 CYS A SG    1 
ATOM   3215 N  N     . PRO A 1 414 ? -19.949 -8.064  13.660  1.00 59.51  ? 414 PRO A N     1 
ATOM   3216 C  CA    . PRO A 1 414 ? -21.345 -7.832  14.067  1.00 58.07  ? 414 PRO A CA    1 
ATOM   3217 C  C     . PRO A 1 414 ? -21.752 -6.370  14.059  1.00 49.59  ? 414 PRO A C     1 
ATOM   3218 O  O     . PRO A 1 414 ? -22.953 -6.077  13.998  1.00 55.59  ? 414 PRO A O     1 
ATOM   3219 C  CB    . PRO A 1 414 ? -21.398 -8.425  15.482  1.00 56.84  ? 414 PRO A CB    1 
ATOM   3220 C  CG    . PRO A 1 414 ? -19.984 -8.334  15.973  1.00 63.97  ? 414 PRO A CG    1 
ATOM   3221 C  CD    . PRO A 1 414 ? -19.126 -8.585  14.765  1.00 57.39  ? 414 PRO A CD    1 
ATOM   3222 N  N     . ILE A 1 415 ? -20.801 -5.445  14.127  1.00 48.42  ? 415 ILE A N     1 
ATOM   3223 C  CA    . ILE A 1 415 ? -21.098 -4.021  14.130  1.00 50.51  ? 415 ILE A CA    1 
ATOM   3224 C  C     . ILE A 1 415 ? -20.616 -3.351  12.845  1.00 51.26  ? 415 ILE A C     1 
ATOM   3225 O  O     . ILE A 1 415 ? -20.400 -2.141  12.821  1.00 46.22  ? 415 ILE A O     1 
ATOM   3226 C  CB    . ILE A 1 415 ? -20.510 -3.327  15.368  1.00 52.27  ? 415 ILE A CB    1 
ATOM   3227 C  CG1   . ILE A 1 415 ? -18.998 -3.556  15.437  1.00 52.99  ? 415 ILE A CG1   1 
ATOM   3228 C  CG2   . ILE A 1 415 ? -21.201 -3.818  16.633  1.00 51.43  ? 415 ILE A CG2   1 
ATOM   3229 C  CD1   . ILE A 1 415 ? -18.291 -2.640  16.404  1.00 56.40  ? 415 ILE A CD1   1 
ATOM   3230 N  N     . ILE A 1 416 ? -20.433 -4.124  11.773  1.00 50.34  ? 416 ILE A N     1 
ATOM   3231 C  CA    . ILE A 1 416 ? -20.035 -3.533  10.503  1.00 50.48  ? 416 ILE A CA    1 
ATOM   3232 C  C     . ILE A 1 416 ? -21.095 -2.529  10.075  1.00 50.92  ? 416 ILE A C     1 
ATOM   3233 O  O     . ILE A 1 416 ? -22.299 -2.807  10.135  1.00 51.47  ? 416 ILE A O     1 
ATOM   3234 C  CB    . ILE A 1 416 ? -19.820 -4.623  9.443   1.00 47.98  ? 416 ILE A CB    1 
ATOM   3235 C  CG1   . ILE A 1 416 ? -19.030 -4.058  8.261   1.00 48.75  ? 416 ILE A CG1   1 
ATOM   3236 C  CG2   . ILE A 1 416 ? -21.153 -5.196  8.989   1.00 50.72  ? 416 ILE A CG2   1 
ATOM   3237 C  CD1   . ILE A 1 416 ? -17.603 -3.692  8.609   1.00 47.29  ? 416 ILE A CD1   1 
ATOM   3238 N  N     . ASP A 1 417 ? -20.651 -1.351  9.652   1.00 49.74  ? 417 ASP A N     1 
ATOM   3239 C  CA    . ASP A 1 417 ? -21.589 -0.286  9.334   1.00 50.26  ? 417 ASP A CA    1 
ATOM   3240 C  C     . ASP A 1 417 ? -22.452 -0.687  8.140   1.00 51.11  ? 417 ASP A C     1 
ATOM   3241 O  O     . ASP A 1 417 ? -21.946 -1.270  7.172   1.00 50.07  ? 417 ASP A O     1 
ATOM   3242 C  CB    . ASP A 1 417 ? -20.847 1.019   9.036   1.00 49.13  ? 417 ASP A CB    1 
ATOM   3243 C  CG    . ASP A 1 417 ? -21.770 2.225   9.018   1.00 49.83  ? 417 ASP A CG    1 
ATOM   3244 O  OD1   . ASP A 1 417 ? -22.140 2.717   10.104  1.00 49.37  ? 417 ASP A OD1   1 
ATOM   3245 O  OD2   . ASP A 1 417 ? -22.128 2.682   7.912   1.00 52.51  ? 417 ASP A OD2   1 
ATOM   3246 N  N     . PRO A 1 418 ? -23.755 -0.398  8.175   1.00 50.51  ? 418 PRO A N     1 
ATOM   3247 C  CA    . PRO A 1 418 ? -24.618 -0.720  7.026   1.00 55.40  ? 418 PRO A CA    1 
ATOM   3248 C  C     . PRO A 1 418 ? -24.220 -0.009  5.741   1.00 54.76  ? 418 PRO A C     1 
ATOM   3249 O  O     . PRO A 1 418 ? -24.771 -0.333  4.682   1.00 63.93  ? 418 PRO A O     1 
ATOM   3250 C  CB    . PRO A 1 418 ? -26.012 -0.282  7.497   1.00 53.02  ? 418 PRO A CB    1 
ATOM   3251 C  CG    . PRO A 1 418 ? -25.754 0.690   8.620   1.00 56.95  ? 418 PRO A CG    1 
ATOM   3252 C  CD    . PRO A 1 418 ? -24.505 0.209   9.286   1.00 56.41  ? 418 PRO A CD    1 
ATOM   3253 N  N     . ALA A 1 419 ? -23.289 0.945   5.796   1.00 54.11  ? 419 ALA A N     1 
ATOM   3254 C  CA    . ALA A 1 419 ? -22.826 1.655   4.609   1.00 58.06  ? 419 ALA A CA    1 
ATOM   3255 C  C     . ALA A 1 419 ? -21.348 1.406   4.337   1.00 57.07  ? 419 ALA A C     1 
ATOM   3256 O  O     . ALA A 1 419 ? -20.727 2.153   3.575   1.00 58.12  ? 419 ALA A O     1 
ATOM   3257 C  CB    . ALA A 1 419 ? -23.094 3.155   4.743   1.00 55.97  ? 419 ALA A CB    1 
ATOM   3258 N  N     . TRP A 1 420 ? -20.768 0.368   4.946   1.00 54.16  ? 420 TRP A N     1 
ATOM   3259 C  CA    . TRP A 1 420 ? -19.343 0.113   4.775   1.00 55.37  ? 420 TRP A CA    1 
ATOM   3260 C  C     . TRP A 1 420 ? -18.989 -0.242  3.338   1.00 50.54  ? 420 TRP A C     1 
ATOM   3261 O  O     . TRP A 1 420 ? -17.818 -0.136  2.959   1.00 47.53  ? 420 TRP A O     1 
ATOM   3262 C  CB    . TRP A 1 420 ? -18.886 -0.999  5.726   1.00 49.85  ? 420 TRP A CB    1 
ATOM   3263 C  CG    . TRP A 1 420 ? -19.157 -2.394  5.243   1.00 52.31  ? 420 TRP A CG    1 
ATOM   3264 C  CD1   . TRP A 1 420 ? -20.324 -3.088  5.351   1.00 50.94  ? 420 TRP A CD1   1 
ATOM   3265 C  CD2   . TRP A 1 420 ? -18.225 -3.276  4.602   1.00 54.12  ? 420 TRP A CD2   1 
ATOM   3266 N  NE1   . TRP A 1 420 ? -20.183 -4.341  4.807   1.00 52.08  ? 420 TRP A NE1   1 
ATOM   3267 C  CE2   . TRP A 1 420 ? -18.902 -4.483  4.343   1.00 52.43  ? 420 TRP A CE2   1 
ATOM   3268 C  CE3   . TRP A 1 420 ? -16.884 -3.160  4.218   1.00 50.91  ? 420 TRP A CE3   1 
ATOM   3269 C  CZ2   . TRP A 1 420 ? -18.288 -5.566  3.714   1.00 54.91  ? 420 TRP A CZ2   1 
ATOM   3270 C  CZ3   . TRP A 1 420 ? -16.275 -4.237  3.595   1.00 50.63  ? 420 TRP A CZ3   1 
ATOM   3271 C  CH2   . TRP A 1 420 ? -16.975 -5.423  3.350   1.00 52.25  ? 420 TRP A CH2   1 
ATOM   3272 N  N     . GLU A 1 421 ? -19.968 -0.649  2.532   1.00 52.38  ? 421 GLU A N     1 
ATOM   3273 C  CA    . GLU A 1 421 ? -19.751 -0.956  1.124   1.00 54.37  ? 421 GLU A CA    1 
ATOM   3274 C  C     . GLU A 1 421 ? -20.437 0.034   0.191   1.00 59.75  ? 421 GLU A C     1 
ATOM   3275 O  O     . GLU A 1 421 ? -20.427 -0.170  -1.028  1.00 59.86  ? 421 GLU A O     1 
ATOM   3276 C  CB    . GLU A 1 421 ? -20.221 -2.380  0.812   1.00 57.76  ? 421 GLU A CB    1 
ATOM   3277 C  CG    . GLU A 1 421 ? -19.327 -3.459  1.392   1.00 60.24  ? 421 GLU A CG    1 
ATOM   3278 C  CD    . GLU A 1 421 ? -19.675 -4.845  0.889   1.00 61.16  ? 421 GLU A CD    1 
ATOM   3279 O  OE1   . GLU A 1 421 ? -20.822 -5.286  1.102   1.00 63.08  ? 421 GLU A OE1   1 
ATOM   3280 O  OE2   . GLU A 1 421 ? -18.798 -5.492  0.274   1.00 56.18  ? 421 GLU A OE2   1 
ATOM   3281 N  N     . SER A 1 422 ? -21.025 1.095   0.726   1.00 62.52  ? 422 SER A N     1 
ATOM   3282 C  CA    . SER A 1 422 ? -21.690 2.089   -0.102  1.00 62.11  ? 422 SER A CA    1 
ATOM   3283 C  C     . SER A 1 422 ? -20.680 2.753   -1.031  1.00 60.73  ? 422 SER A C     1 
ATOM   3284 O  O     . SER A 1 422 ? -19.679 3.310   -0.552  1.00 58.83  ? 422 SER A O     1 
ATOM   3285 C  CB    . SER A 1 422 ? -22.380 3.137   0.769   1.00 62.99  ? 422 SER A CB    1 
ATOM   3286 O  OG    . SER A 1 422 ? -23.389 2.549   1.571   1.00 66.65  ? 422 SER A OG    1 
ATOM   3287 N  N     . PRO A 1 423 ? -20.893 2.721   -2.349  1.00 63.54  ? 423 PRO A N     1 
ATOM   3288 C  CA    . PRO A 1 423 ? -19.928 3.351   -3.263  1.00 67.31  ? 423 PRO A CA    1 
ATOM   3289 C  C     . PRO A 1 423 ? -19.824 4.859   -3.104  1.00 64.65  ? 423 PRO A C     1 
ATOM   3290 O  O     . PRO A 1 423 ? -18.830 5.441   -3.554  1.00 70.55  ? 423 PRO A O     1 
ATOM   3291 C  CB    . PRO A 1 423 ? -20.460 2.971   -4.652  1.00 71.74  ? 423 PRO A CB    1 
ATOM   3292 C  CG    . PRO A 1 423 ? -21.916 2.691   -4.437  1.00 67.47  ? 423 PRO A CG    1 
ATOM   3293 C  CD    . PRO A 1 423 ? -22.007 2.081   -3.069  1.00 66.93  ? 423 PRO A CD    1 
ATOM   3294 N  N     . GLU A 1 424 ? -20.811 5.512   -2.491  1.00 61.21  ? 424 GLU A N     1 
ATOM   3295 C  CA    . GLU A 1 424 ? -20.747 6.955   -2.295  1.00 60.60  ? 424 GLU A CA    1 
ATOM   3296 C  C     . GLU A 1 424 ? -19.926 7.355   -1.077  1.00 58.82  ? 424 GLU A C     1 
ATOM   3297 O  O     . GLU A 1 424 ? -19.663 8.548   -0.894  1.00 54.62  ? 424 GLU A O     1 
ATOM   3298 C  CB    . GLU A 1 424 ? -22.156 7.541   -2.172  1.00 60.94  ? 424 GLU A CB    1 
ATOM   3299 C  CG    . GLU A 1 424 ? -22.992 6.960   -1.041  1.00 65.04  ? 424 GLU A CG    1 
ATOM   3300 C  CD    . GLU A 1 424 ? -23.547 5.590   -1.374  1.00 72.54  ? 424 GLU A CD    1 
ATOM   3301 O  OE1   . GLU A 1 424 ? -22.752 4.690   -1.709  1.00 68.26  ? 424 GLU A OE1   1 
ATOM   3302 O  OE2   . GLU A 1 424 ? -24.781 5.415   -1.310  1.00 80.95  ? 424 GLU A OE2   1 
ATOM   3303 N  N     . GLY A 1 425 ? -19.517 6.401   -0.249  1.00 56.65  ? 425 GLY A N     1 
ATOM   3304 C  CA    . GLY A 1 425 ? -18.748 6.710   0.938   1.00 53.18  ? 425 GLY A CA    1 
ATOM   3305 C  C     . GLY A 1 425 ? -19.611 7.316   2.033   1.00 52.55  ? 425 GLY A C     1 
ATOM   3306 O  O     . GLY A 1 425 ? -20.805 7.563   1.873   1.00 53.03  ? 425 GLY A O     1 
ATOM   3307 N  N     . VAL A 1 426 ? -18.971 7.559   3.173   1.00 48.58  ? 426 VAL A N     1 
ATOM   3308 C  CA    . VAL A 1 426 ? -19.649 8.122   4.339   1.00 47.41  ? 426 VAL A CA    1 
ATOM   3309 C  C     . VAL A 1 426 ? -19.092 9.515   4.616   1.00 50.16  ? 426 VAL A C     1 
ATOM   3310 O  O     . VAL A 1 426 ? -17.878 9.732   4.486   1.00 44.78  ? 426 VAL A O     1 
ATOM   3311 C  CB    . VAL A 1 426 ? -19.498 7.208   5.565   1.00 43.77  ? 426 VAL A CB    1 
ATOM   3312 C  CG1   . VAL A 1 426 ? -20.193 5.880   5.319   1.00 43.16  ? 426 VAL A CG1   1 
ATOM   3313 C  CG2   . VAL A 1 426 ? -18.025 6.994   5.893   1.00 44.08  ? 426 VAL A CG2   1 
ATOM   3314 N  N     . PRO A 1 427 ? -19.930 10.481  4.997   1.00 46.94  ? 427 PRO A N     1 
ATOM   3315 C  CA    . PRO A 1 427 ? -19.429 11.838  5.257   1.00 46.69  ? 427 PRO A CA    1 
ATOM   3316 C  C     . PRO A 1 427 ? -18.648 11.896  6.562   1.00 45.94  ? 427 PRO A C     1 
ATOM   3317 O  O     . PRO A 1 427 ? -19.151 11.511  7.619   1.00 46.97  ? 427 PRO A O     1 
ATOM   3318 C  CB    . PRO A 1 427 ? -20.709 12.680  5.330   1.00 50.27  ? 427 PRO A CB    1 
ATOM   3319 C  CG    . PRO A 1 427 ? -21.747 11.712  5.804   1.00 48.50  ? 427 PRO A CG    1 
ATOM   3320 C  CD    . PRO A 1 427 ? -21.386 10.381  5.191   1.00 46.62  ? 427 PRO A CD    1 
ATOM   3321 N  N     . ILE A 1 428 ? -17.411 12.380  6.479   1.00 45.36  ? 428 ILE A N     1 
ATOM   3322 C  CA    . ILE A 1 428 ? -16.539 12.512  7.642   1.00 39.63  ? 428 ILE A CA    1 
ATOM   3323 C  C     . ILE A 1 428 ? -16.746 13.893  8.247   1.00 42.77  ? 428 ILE A C     1 
ATOM   3324 O  O     . ILE A 1 428 ? -16.559 14.909  7.571   1.00 43.81  ? 428 ILE A O     1 
ATOM   3325 C  CB    . ILE A 1 428 ? -15.067 12.298  7.263   1.00 38.80  ? 428 ILE A CB    1 
ATOM   3326 C  CG1   . ILE A 1 428 ? -14.879 10.936  6.595   1.00 40.62  ? 428 ILE A CG1   1 
ATOM   3327 C  CG2   . ILE A 1 428 ? -14.179 12.428  8.492   1.00 36.39  ? 428 ILE A CG2   1 
ATOM   3328 C  CD1   . ILE A 1 428 ? -15.269 9.767   7.479   1.00 40.08  ? 428 ILE A CD1   1 
ATOM   3329 N  N     . GLU A 1 429 ? -17.135 13.932  9.521   1.00 40.62  ? 429 GLU A N     1 
ATOM   3330 C  CA    . GLU A 1 429 ? -17.317 15.187  10.239  1.00 42.46  ? 429 GLU A CA    1 
ATOM   3331 C  C     . GLU A 1 429 ? -16.223 15.454  11.264  1.00 41.97  ? 429 GLU A C     1 
ATOM   3332 O  O     . GLU A 1 429 ? -16.191 16.545  11.841  1.00 40.16  ? 429 GLU A O     1 
ATOM   3333 C  CB    . GLU A 1 429 ? -18.687 15.212  10.937  1.00 41.27  ? 429 GLU A CB    1 
ATOM   3334 C  CG    . GLU A 1 429 ? -19.884 15.081  9.995   1.00 49.46  ? 429 GLU A CG    1 
ATOM   3335 C  CD    . GLU A 1 429 ? -21.216 15.247  10.709  1.00 48.57  ? 429 GLU A CD    1 
ATOM   3336 O  OE1   . GLU A 1 429 ? -21.340 16.168  11.545  1.00 47.88  ? 429 GLU A OE1   1 
ATOM   3337 O  OE2   . GLU A 1 429 ? -22.140 14.452  10.435  1.00 52.30  ? 429 GLU A OE2   1 
ATOM   3338 N  N     . GLY A 1 430 ? -15.333 14.494  11.499  1.00 39.78  ? 430 GLY A N     1 
ATOM   3339 C  CA    . GLY A 1 430 ? -14.243 14.685  12.433  1.00 38.85  ? 430 GLY A CA    1 
ATOM   3340 C  C     . GLY A 1 430 ? -13.072 13.779  12.103  1.00 38.60  ? 430 GLY A C     1 
ATOM   3341 O  O     . GLY A 1 430 ? -13.255 12.641  11.667  1.00 38.38  ? 430 GLY A O     1 
ATOM   3342 N  N     . ILE A 1 431 ? -11.871 14.299  12.323  1.00 35.61  ? 431 ILE A N     1 
ATOM   3343 C  CA    . ILE A 1 431 ? -10.635 13.555  12.102  1.00 36.53  ? 431 ILE A CA    1 
ATOM   3344 C  C     . ILE A 1 431 ? -9.861  13.531  13.412  1.00 35.07  ? 431 ILE A C     1 
ATOM   3345 O  O     . ILE A 1 431 ? -9.721  14.565  14.075  1.00 39.65  ? 431 ILE A O     1 
ATOM   3346 C  CB    . ILE A 1 431 ? -9.797  14.172  10.967  1.00 36.36  ? 431 ILE A CB    1 
ATOM   3347 C  CG1   . ILE A 1 431 ? -10.563 14.095  9.639   1.00 34.30  ? 431 ILE A CG1   1 
ATOM   3348 C  CG2   . ILE A 1 431 ? -8.442  13.479  10.859  1.00 34.59  ? 431 ILE A CG2   1 
ATOM   3349 C  CD1   . ILE A 1 431 ? -9.860  14.775  8.481   1.00 40.92  ? 431 ILE A CD1   1 
ATOM   3350 N  N     . ILE A 1 432 ? -9.361  12.357  13.781  1.00 36.35  ? 432 ILE A N     1 
ATOM   3351 C  CA    . ILE A 1 432 ? -8.674  12.154  15.050  1.00 36.98  ? 432 ILE A CA    1 
ATOM   3352 C  C     . ILE A 1 432 ? -7.242  11.726  14.766  1.00 32.82  ? 432 ILE A C     1 
ATOM   3353 O  O     . ILE A 1 432 ? -7.009  10.814  13.966  1.00 36.19  ? 432 ILE A O     1 
ATOM   3354 C  CB    . ILE A 1 432 ? -9.393  11.106  15.918  1.00 34.68  ? 432 ILE A CB    1 
ATOM   3355 C  CG1   . ILE A 1 432 ? -10.893 11.403  15.976  1.00 36.83  ? 432 ILE A CG1   1 
ATOM   3356 C  CG2   . ILE A 1 432 ? -8.802  11.086  17.319  1.00 39.84  ? 432 ILE A CG2   1 
ATOM   3357 C  CD1   . ILE A 1 432 ? -11.703 10.321  16.671  1.00 38.44  ? 432 ILE A CD1   1 
ATOM   3358 N  N     . PHE A 1 433 ? -6.290  12.391  15.413  1.00 32.97  ? 433 PHE A N     1 
ATOM   3359 C  CA    . PHE A 1 433 ? -4.898  11.969  15.440  1.00 33.00  ? 433 PHE A CA    1 
ATOM   3360 C  C     . PHE A 1 433 ? -4.534  11.529  16.851  1.00 35.92  ? 433 PHE A C     1 
ATOM   3361 O  O     . PHE A 1 433 ? -5.131  11.986  17.828  1.00 34.78  ? 433 PHE A O     1 
ATOM   3362 C  CB    . PHE A 1 433 ? -3.961  13.096  14.986  1.00 33.92  ? 433 PHE A CB    1 
ATOM   3363 C  CG    . PHE A 1 433 ? -4.215  13.565  13.585  1.00 38.01  ? 433 PHE A CG    1 
ATOM   3364 C  CD1   . PHE A 1 433 ? -4.045  12.704  12.516  1.00 38.94  ? 433 PHE A CD1   1 
ATOM   3365 C  CD2   . PHE A 1 433 ? -4.612  14.868  13.336  1.00 38.46  ? 433 PHE A CD2   1 
ATOM   3366 C  CE1   . PHE A 1 433 ? -4.275  13.127  11.220  1.00 39.64  ? 433 PHE A CE1   1 
ATOM   3367 C  CE2   . PHE A 1 433 ? -4.843  15.300  12.041  1.00 41.83  ? 433 PHE A CE2   1 
ATOM   3368 C  CZ    . PHE A 1 433 ? -4.674  14.427  10.982  1.00 37.44  ? 433 PHE A CZ    1 
ATOM   3369 N  N     . GLY A 1 434 ? -3.560  10.635  16.954  1.00 36.62  ? 434 GLY A N     1 
ATOM   3370 C  CA    . GLY A 1 434 ? -3.164  10.138  18.258  1.00 37.63  ? 434 GLY A CA    1 
ATOM   3371 C  C     . GLY A 1 434 ? -2.072  9.096   18.148  1.00 38.72  ? 434 GLY A C     1 
ATOM   3372 O  O     . GLY A 1 434 ? -1.828  8.526   17.081  1.00 39.15  ? 434 GLY A O     1 
ATOM   3373 N  N     . GLY A 1 435 ? -1.420  8.865   19.278  1.00 42.90  ? 435 GLY A N     1 
ATOM   3374 C  CA    . GLY A 1 435 ? -0.401  7.842   19.384  1.00 38.89  ? 435 GLY A CA    1 
ATOM   3375 C  C     . GLY A 1 435 ? -0.097  7.570   20.838  1.00 40.34  ? 435 GLY A C     1 
ATOM   3376 O  O     . GLY A 1 435 ? -0.775  8.073   21.734  1.00 37.43  ? 435 GLY A O     1 
ATOM   3377 N  N     . ARG A 1 436 ? 0.939   6.769   21.064  1.00 36.14  ? 436 ARG A N     1 
ATOM   3378 C  CA    . ARG A 1 436 ? 1.357   6.426   22.421  1.00 43.89  ? 436 ARG A CA    1 
ATOM   3379 C  C     . ARG A 1 436 ? 2.296   7.510   22.934  1.00 42.50  ? 436 ARG A C     1 
ATOM   3380 O  O     . ARG A 1 436 ? 3.473   7.555   22.573  1.00 47.04  ? 436 ARG A O     1 
ATOM   3381 C  CB    . ARG A 1 436 ? 2.016   5.052   22.447  1.00 45.21  ? 436 ARG A CB    1 
ATOM   3382 C  CG    . ARG A 1 436 ? 1.061   3.931   22.090  1.00 45.68  ? 436 ARG A CG    1 
ATOM   3383 C  CD    . ARG A 1 436 ? 1.760   2.589   21.976  1.00 51.14  ? 436 ARG A CD    1 
ATOM   3384 N  NE    . ARG A 1 436 ? 0.797   1.524   21.727  1.00 53.69  ? 436 ARG A NE    1 
ATOM   3385 C  CZ    . ARG A 1 436 ? 0.244   0.783   22.676  1.00 52.39  ? 436 ARG A CZ    1 
ATOM   3386 N  NH1   . ARG A 1 436 ? 0.557   0.947   23.951  1.00 49.44  ? 436 ARG A NH1   1 
ATOM   3387 N  NH2   . ARG A 1 436 ? -0.646  -0.146  22.338  1.00 57.70  ? 436 ARG A NH2   1 
ATOM   3388 N  N     . ARG A 1 437 ? 1.770   8.396   23.769  1.00 36.91  ? 437 ARG A N     1 
ATOM   3389 C  CA    . ARG A 1 437 ? 2.585   9.380   24.480  1.00 45.12  ? 437 ARG A CA    1 
ATOM   3390 C  C     . ARG A 1 437 ? 2.478   9.106   25.971  1.00 45.35  ? 437 ARG A C     1 
ATOM   3391 O  O     . ARG A 1 437 ? 1.413   9.355   26.569  1.00 43.85  ? 437 ARG A O     1 
ATOM   3392 C  CB    . ARG A 1 437 ? 2.142   10.809  24.166  1.00 36.56  ? 437 ARG A CB    1 
ATOM   3393 C  CG    . ARG A 1 437 ? 2.388   11.248  22.729  1.00 45.44  ? 437 ARG A CG    1 
ATOM   3394 C  CD    . ARG A 1 437 ? 3.831   11.013  22.291  1.00 45.93  ? 437 ARG A CD    1 
ATOM   3395 N  NE    . ARG A 1 437 ? 4.790   11.809  23.049  1.00 43.85  ? 437 ARG A NE    1 
ATOM   3396 C  CZ    . ARG A 1 437 ? 5.142   13.051  22.747  1.00 45.50  ? 437 ARG A CZ    1 
ATOM   3397 N  NH1   . ARG A 1 437 ? 4.623   13.683  21.707  1.00 34.03  ? 437 ARG A NH1   1 
ATOM   3398 N  NH2   . ARG A 1 437 ? 6.039   13.674  23.506  1.00 42.85  ? 437 ARG A NH2   1 
ATOM   3399 N  N     . PRO A 1 438 ? 3.528   8.592   26.618  1.00 47.72  ? 438 PRO A N     1 
ATOM   3400 C  CA    . PRO A 1 438 ? 3.426   8.279   28.051  1.00 53.18  ? 438 PRO A CA    1 
ATOM   3401 C  C     . PRO A 1 438 ? 3.384   9.506   28.948  1.00 47.41  ? 438 PRO A C     1 
ATOM   3402 O  O     . PRO A 1 438 ? 3.077   9.364   30.138  1.00 50.74  ? 438 PRO A O     1 
ATOM   3403 C  CB    . PRO A 1 438 ? 4.686   7.443   28.315  1.00 49.32  ? 438 PRO A CB    1 
ATOM   3404 C  CG    . PRO A 1 438 ? 5.666   7.934   27.295  1.00 47.23  ? 438 PRO A CG    1 
ATOM   3405 C  CD    . PRO A 1 438 ? 4.852   8.251   26.066  1.00 43.57  ? 438 PRO A CD    1 
ATOM   3406 N  N     . ALA A 1 439 ? 3.672   10.697  28.427  1.00 48.48  ? 439 ALA A N     1 
ATOM   3407 C  CA    . ALA A 1 439 ? 3.753   11.883  29.263  1.00 47.43  ? 439 ALA A CA    1 
ATOM   3408 C  C     . ALA A 1 439 ? 3.391   13.116  28.452  1.00 44.97  ? 439 ALA A C     1 
ATOM   3409 O  O     . ALA A 1 439 ? 3.521   13.133  27.226  1.00 47.73  ? 439 ALA A O     1 
ATOM   3410 C  CB    . ALA A 1 439 ? 5.151   12.052  29.867  1.00 43.31  ? 439 ALA A CB    1 
ATOM   3411 N  N     . GLY A 1 440 ? 2.927   14.146  29.158  1.00 46.35  ? 440 GLY A N     1 
ATOM   3412 C  CA    . GLY A 1 440 ? 2.797   15.475  28.592  1.00 46.14  ? 440 GLY A CA    1 
ATOM   3413 C  C     . GLY A 1 440 ? 1.540   15.761  27.793  1.00 48.33  ? 440 GLY A C     1 
ATOM   3414 O  O     . GLY A 1 440 ? 0.983   16.857  27.891  1.00 52.05  ? 440 GLY A O     1 
ATOM   3415 N  N     . VAL A 1 441 ? 1.089   14.798  26.999  1.00 45.65  ? 441 VAL A N     1 
ATOM   3416 C  CA    . VAL A 1 441 ? 0.009   15.018  26.038  1.00 46.09  ? 441 VAL A CA    1 
ATOM   3417 C  C     . VAL A 1 441 ? -1.321  14.648  26.723  1.00 43.81  ? 441 VAL A C     1 
ATOM   3418 O  O     . VAL A 1 441 ? -1.458  13.510  27.180  1.00 42.56  ? 441 VAL A O     1 
ATOM   3419 C  CB    . VAL A 1 441 ? 0.213   14.197  24.764  1.00 41.59  ? 441 VAL A CB    1 
ATOM   3420 C  CG1   . VAL A 1 441 ? -0.873  14.515  23.747  1.00 37.81  ? 441 VAL A CG1   1 
ATOM   3421 C  CG2   . VAL A 1 441 ? 1.593   14.474  24.185  1.00 41.76  ? 441 VAL A CG2   1 
ATOM   3422 N  N     . PRO A 1 442 ? -2.280  15.565  26.780  1.00 43.94  ? 442 PRO A N     1 
ATOM   3423 C  CA    . PRO A 1 442 ? -3.523  15.279  27.514  1.00 45.57  ? 442 PRO A CA    1 
ATOM   3424 C  C     . PRO A 1 442 ? -4.420  14.310  26.756  1.00 43.11  ? 442 PRO A C     1 
ATOM   3425 O  O     . PRO A 1 442 ? -4.164  13.930  25.611  1.00 41.67  ? 442 PRO A O     1 
ATOM   3426 C  CB    . PRO A 1 442 ? -4.172  16.660  27.651  1.00 50.32  ? 442 PRO A CB    1 
ATOM   3427 C  CG    . PRO A 1 442 ? -3.658  17.424  26.481  1.00 42.90  ? 442 PRO A CG    1 
ATOM   3428 C  CD    . PRO A 1 442 ? -2.258  16.928  26.233  1.00 46.21  ? 442 PRO A CD    1 
ATOM   3429 N  N     . LEU A 1 443 ? -5.502  13.913  27.434  1.00 44.15  ? 443 LEU A N     1 
ATOM   3430 C  CA    . LEU A 1 443 ? -6.385  12.873  26.909  1.00 41.43  ? 443 LEU A CA    1 
ATOM   3431 C  C     . LEU A 1 443 ? -6.946  13.246  25.544  1.00 41.08  ? 443 LEU A C     1 
ATOM   3432 O  O     . LEU A 1 443 ? -7.009  12.405  24.639  1.00 41.82  ? 443 LEU A O     1 
ATOM   3433 C  CB    . LEU A 1 443 ? -7.523  12.605  27.896  1.00 40.77  ? 443 LEU A CB    1 
ATOM   3434 C  CG    . LEU A 1 443 ? -8.595  11.604  27.459  1.00 44.26  ? 443 LEU A CG    1 
ATOM   3435 C  CD1   . LEU A 1 443 ? -7.992  10.226  27.247  1.00 44.08  ? 443 LEU A CD1   1 
ATOM   3436 C  CD2   . LEU A 1 443 ? -9.722  11.548  28.477  1.00 47.01  ? 443 LEU A CD2   1 
ATOM   3437 N  N     . VAL A 1 444 ? -7.368  14.496  25.379  1.00 36.59  ? 444 VAL A N     1 
ATOM   3438 C  CA    . VAL A 1 444 ? -7.971  14.941  24.129  1.00 34.80  ? 444 VAL A CA    1 
ATOM   3439 C  C     . VAL A 1 444 ? -7.899  16.458  24.072  1.00 39.48  ? 444 VAL A C     1 
ATOM   3440 O  O     . VAL A 1 444 ? -8.112  17.144  25.075  1.00 38.25  ? 444 VAL A O     1 
ATOM   3441 C  CB    . VAL A 1 444 ? -9.431  14.447  24.001  1.00 39.01  ? 444 VAL A CB    1 
ATOM   3442 C  CG1   . VAL A 1 444 ? -10.276 14.997  25.142  1.00 37.20  ? 444 VAL A CG1   1 
ATOM   3443 C  CG2   . VAL A 1 444 ? -10.010 14.853  22.654  1.00 33.64  ? 444 VAL A CG2   1 
ATOM   3444 N  N     . TYR A 1 445 ? -7.594  16.976  22.885  1.00 40.36  ? 445 TYR A N     1 
ATOM   3445 C  CA    . TYR A 1 445 ? -7.763  18.390  22.598  1.00 40.49  ? 445 TYR A CA    1 
ATOM   3446 C  C     . TYR A 1 445 ? -8.203  18.546  21.151  1.00 37.26  ? 445 TYR A C     1 
ATOM   3447 O  O     . TYR A 1 445 ? -8.092  17.621  20.341  1.00 36.82  ? 445 TYR A O     1 
ATOM   3448 C  CB    . TYR A 1 445 ? -6.490  19.209  22.882  1.00 38.52  ? 445 TYR A CB    1 
ATOM   3449 C  CG    . TYR A 1 445 ? -5.259  18.848  22.076  1.00 36.59  ? 445 TYR A CG    1 
ATOM   3450 C  CD1   . TYR A 1 445 ? -4.365  17.886  22.532  1.00 37.72  ? 445 TYR A CD1   1 
ATOM   3451 C  CD2   . TYR A 1 445 ? -4.966  19.497  20.882  1.00 44.55  ? 445 TYR A CD2   1 
ATOM   3452 C  CE1   . TYR A 1 445 ? -3.229  17.564  21.813  1.00 35.71  ? 445 TYR A CE1   1 
ATOM   3453 C  CE2   . TYR A 1 445 ? -3.829  19.180  20.153  1.00 42.20  ? 445 TYR A CE2   1 
ATOM   3454 C  CZ    . TYR A 1 445 ? -2.966  18.214  20.624  1.00 40.93  ? 445 TYR A CZ    1 
ATOM   3455 O  OH    . TYR A 1 445 ? -1.835  17.897  19.906  1.00 41.81  ? 445 TYR A OH    1 
ATOM   3456 N  N     . GLU A 1 446 ? -8.726  19.729  20.846  1.00 38.61  ? 446 GLU A N     1 
ATOM   3457 C  CA    . GLU A 1 446 ? -9.291  20.048  19.544  1.00 35.00  ? 446 GLU A CA    1 
ATOM   3458 C  C     . GLU A 1 446 ? -8.462  21.144  18.890  1.00 36.53  ? 446 GLU A C     1 
ATOM   3459 O  O     . GLU A 1 446 ? -8.039  22.093  19.557  1.00 39.63  ? 446 GLU A O     1 
ATOM   3460 C  CB    . GLU A 1 446 ? -10.750 20.499  19.685  1.00 37.87  ? 446 GLU A CB    1 
ATOM   3461 C  CG    . GLU A 1 446 ? -11.365 21.051  18.414  1.00 44.14  ? 446 GLU A CG    1 
ATOM   3462 C  CD    . GLU A 1 446 ? -12.738 21.652  18.652  1.00 44.30  ? 446 GLU A CD    1 
ATOM   3463 O  OE1   . GLU A 1 446 ? -13.398 21.257  19.639  1.00 42.70  ? 446 GLU A OE1   1 
ATOM   3464 O  OE2   . GLU A 1 446 ? -13.155 22.521  17.859  1.00 45.75  ? 446 GLU A OE2   1 
ATOM   3465 N  N     . ALA A 1 447 ? -8.227  21.009  17.588  1.00 39.07  ? 447 ALA A N     1 
ATOM   3466 C  CA    . ALA A 1 447 ? -7.408  21.984  16.882  1.00 36.43  ? 447 ALA A CA    1 
ATOM   3467 C  C     . ALA A 1 447 ? -8.128  23.324  16.779  1.00 41.08  ? 447 ALA A C     1 
ATOM   3468 O  O     . ALA A 1 447 ? -9.360  23.397  16.760  1.00 43.49  ? 447 ALA A O     1 
ATOM   3469 C  CB    . ALA A 1 447 ? -7.043  21.475  15.487  1.00 35.70  ? 447 ALA A CB    1 
ATOM   3470 N  N     . LEU A 1 448 ? -7.336  24.395  16.710  1.00 41.17  ? 448 LEU A N     1 
ATOM   3471 C  CA    . LEU A 1 448 ? -7.883  25.744  16.638  1.00 43.92  ? 448 LEU A CA    1 
ATOM   3472 C  C     . LEU A 1 448 ? -8.412  26.094  15.255  1.00 45.10  ? 448 LEU A C     1 
ATOM   3473 O  O     . LEU A 1 448 ? -9.252  26.992  15.135  1.00 38.33  ? 448 LEU A O     1 
ATOM   3474 C  CB    . LEU A 1 448 ? -6.816  26.761  17.045  1.00 38.43  ? 448 LEU A CB    1 
ATOM   3475 C  CG    . LEU A 1 448 ? -6.192  26.552  18.423  1.00 45.91  ? 448 LEU A CG    1 
ATOM   3476 C  CD1   . LEU A 1 448 ? -5.082  27.558  18.658  1.00 44.32  ? 448 LEU A CD1   1 
ATOM   3477 C  CD2   . LEU A 1 448 ? -7.257  26.648  19.505  1.00 43.62  ? 448 LEU A CD2   1 
ATOM   3478 N  N     . SER A 1 449 ? -7.945  25.412  14.218  1.00 37.47  ? 449 SER A N     1 
ATOM   3479 C  CA    . SER A 1 449 ? -8.326  25.717  12.845  1.00 39.23  ? 449 SER A CA    1 
ATOM   3480 C  C     . SER A 1 449 ? -7.871  24.556  11.970  1.00 37.45  ? 449 SER A C     1 
ATOM   3481 O  O     . SER A 1 449 ? -7.250  23.600  12.446  1.00 37.58  ? 449 SER A O     1 
ATOM   3482 C  CB    . SER A 1 449 ? -7.714  27.040  12.383  1.00 45.12  ? 449 SER A CB    1 
ATOM   3483 O  OG    . SER A 1 449 ? -6.298  26.970  12.368  1.00 43.40  ? 449 SER A OG    1 
ATOM   3484 N  N     . TRP A 1 450 ? -8.186  24.646  10.679  1.00 40.45  ? 450 TRP A N     1 
ATOM   3485 C  CA    . TRP A 1 450 ? -7.725  23.627  9.744   1.00 41.79  ? 450 TRP A CA    1 
ATOM   3486 C  C     . TRP A 1 450 ? -6.204  23.605  9.673   1.00 39.48  ? 450 TRP A C     1 
ATOM   3487 O  O     . TRP A 1 450 ? -5.581  22.538  9.734   1.00 38.79  ? 450 TRP A O     1 
ATOM   3488 C  CB    . TRP A 1 450 ? -8.324  23.864  8.358   1.00 41.16  ? 450 TRP A CB    1 
ATOM   3489 C  CG    . TRP A 1 450 ? -7.974  22.780  7.389   1.00 45.53  ? 450 TRP A CG    1 
ATOM   3490 C  CD1   . TRP A 1 450 ? -7.102  22.860  6.343   1.00 41.42  ? 450 TRP A CD1   1 
ATOM   3491 C  CD2   . TRP A 1 450 ? -8.471  21.438  7.395   1.00 45.00  ? 450 TRP A CD2   1 
ATOM   3492 N  NE1   . TRP A 1 450 ? -7.037  21.654  5.687   1.00 43.94  ? 450 TRP A NE1   1 
ATOM   3493 C  CE2   . TRP A 1 450 ? -7.867  20.764  6.315   1.00 41.56  ? 450 TRP A CE2   1 
ATOM   3494 C  CE3   . TRP A 1 450 ? -9.374  20.742  8.204   1.00 45.73  ? 450 TRP A CE3   1 
ATOM   3495 C  CZ2   . TRP A 1 450 ? -8.134  19.428  6.027   1.00 41.89  ? 450 TRP A CZ2   1 
ATOM   3496 C  CZ3   . TRP A 1 450 ? -9.639  19.417  7.914   1.00 38.95  ? 450 TRP A CZ3   1 
ATOM   3497 C  CH2   . TRP A 1 450 ? -9.023  18.774  6.835   1.00 43.40  ? 450 TRP A CH2   1 
ATOM   3498 N  N     . GLN A 1 451 ? -5.586  24.782  9.552   1.00 39.62  ? 451 GLN A N     1 
ATOM   3499 C  CA    . GLN A 1 451 ? -4.132  24.845  9.453   1.00 40.24  ? 451 GLN A CA    1 
ATOM   3500 C  C     . GLN A 1 451 ? -3.466  24.296  10.709  1.00 38.98  ? 451 GLN A C     1 
ATOM   3501 O  O     . GLN A 1 451 ? -2.465  23.575  10.625  1.00 41.14  ? 451 GLN A O     1 
ATOM   3502 C  CB    . GLN A 1 451 ? -3.682  26.283  9.184   1.00 43.87  ? 451 GLN A CB    1 
ATOM   3503 C  CG    . GLN A 1 451 ? -4.154  26.846  7.844   1.00 49.74  ? 451 GLN A CG    1 
ATOM   3504 C  CD    . GLN A 1 451 ? -5.623  27.225  7.854   1.00 51.39  ? 451 GLN A CD    1 
ATOM   3505 O  OE1   . GLN A 1 451 ? -6.209  27.444  8.912   1.00 47.36  ? 451 GLN A OE1   1 
ATOM   3506 N  NE2   . GLN A 1 451 ? -6.225  27.299  6.673   1.00 49.42  ? 451 GLN A NE2   1 
ATOM   3507 N  N     . HIS A 1 452 ? -4.000  24.629  11.886  1.00 36.04  ? 452 HIS A N     1 
ATOM   3508 C  CA    . HIS A 1 452 ? -3.462  24.058  13.117  1.00 37.46  ? 452 HIS A CA    1 
ATOM   3509 C  C     . HIS A 1 452 ? -3.702  22.555  13.166  1.00 39.71  ? 452 HIS A C     1 
ATOM   3510 O  O     . HIS A 1 452 ? -2.850  21.796  13.643  1.00 33.23  ? 452 HIS A O     1 
ATOM   3511 C  CB    . HIS A 1 452 ? -4.080  24.742  14.336  1.00 37.39  ? 452 HIS A CB    1 
ATOM   3512 C  CG    . HIS A 1 452 ? -3.563  24.229  15.645  1.00 38.31  ? 452 HIS A CG    1 
ATOM   3513 N  ND1   . HIS A 1 452 ? -4.394  23.785  16.650  1.00 36.40  ? 452 HIS A ND1   1 
ATOM   3514 C  CD2   . HIS A 1 452 ? -2.300  24.089  16.112  1.00 35.70  ? 452 HIS A CD2   1 
ATOM   3515 C  CE1   . HIS A 1 452 ? -3.667  23.398  17.683  1.00 38.84  ? 452 HIS A CE1   1 
ATOM   3516 N  NE2   . HIS A 1 452 ? -2.393  23.571  17.381  1.00 36.40  ? 452 HIS A NE2   1 
ATOM   3517 N  N     . GLY A 1 453 ? -4.857  22.107  12.671  1.00 40.13  ? 453 GLY A N     1 
ATOM   3518 C  CA    . GLY A 1 453 ? -5.117  20.679  12.616  1.00 35.46  ? 453 GLY A CA    1 
ATOM   3519 C  C     . GLY A 1 453 ? -4.096  19.948  11.768  1.00 37.26  ? 453 GLY A C     1 
ATOM   3520 O  O     . GLY A 1 453 ? -3.579  18.899  12.161  1.00 38.96  ? 453 GLY A O     1 
ATOM   3521 N  N     . VAL A 1 454 ? -3.789  20.497  10.591  1.00 35.65  ? 454 VAL A N     1 
ATOM   3522 C  CA    . VAL A 1 454 ? -2.758  19.904  9.745   1.00 35.44  ? 454 VAL A CA    1 
ATOM   3523 C  C     . VAL A 1 454 ? -1.430  19.858  10.490  1.00 38.69  ? 454 VAL A C     1 
ATOM   3524 O  O     . VAL A 1 454 ? -0.690  18.868  10.415  1.00 38.70  ? 454 VAL A O     1 
ATOM   3525 C  CB    . VAL A 1 454 ? -2.641  20.676  8.416   1.00 37.09  ? 454 VAL A CB    1 
ATOM   3526 C  CG1   . VAL A 1 454 ? -1.512  20.114  7.566   1.00 37.87  ? 454 VAL A CG1   1 
ATOM   3527 C  CG2   . VAL A 1 454 ? -3.953  20.618  7.653   1.00 36.30  ? 454 VAL A CG2   1 
ATOM   3528 N  N     . PHE A 1 455 ? -1.115  20.923  11.234  1.00 38.24  ? 455 PHE A N     1 
ATOM   3529 C  CA    . PHE A 1 455 ? 0.110   20.938  12.028  1.00 39.20  ? 455 PHE A CA    1 
ATOM   3530 C  C     . PHE A 1 455 ? 0.077   19.871  13.115  1.00 36.18  ? 455 PHE A C     1 
ATOM   3531 O  O     . PHE A 1 455 ? 1.103   19.249  13.415  1.00 39.33  ? 455 PHE A O     1 
ATOM   3532 C  CB    . PHE A 1 455 ? 0.323   22.320  12.647  1.00 38.42  ? 455 PHE A CB    1 
ATOM   3533 C  CG    . PHE A 1 455 ? 1.391   22.349  13.700  1.00 38.70  ? 455 PHE A CG    1 
ATOM   3534 C  CD1   . PHE A 1 455 ? 2.723   22.433  13.345  1.00 39.73  ? 455 PHE A CD1   1 
ATOM   3535 C  CD2   . PHE A 1 455 ? 1.062   22.284  15.044  1.00 37.19  ? 455 PHE A CD2   1 
ATOM   3536 C  CE1   . PHE A 1 455 ? 3.713   22.455  14.308  1.00 37.52  ? 455 PHE A CE1   1 
ATOM   3537 C  CE2   . PHE A 1 455 ? 2.047   22.305  16.013  1.00 41.94  ? 455 PHE A CE2   1 
ATOM   3538 C  CZ    . PHE A 1 455 ? 3.376   22.390  15.642  1.00 39.56  ? 455 PHE A CZ    1 
ATOM   3539 N  N     . VAL A 1 456 ? -1.091  19.651  13.722  1.00 33.74  ? 456 VAL A N     1 
ATOM   3540 C  CA    . VAL A 1 456 ? -1.203  18.621  14.752  1.00 35.48  ? 456 VAL A CA    1 
ATOM   3541 C  C     . VAL A 1 456 ? -0.873  17.253  14.168  1.00 36.44  ? 456 VAL A C     1 
ATOM   3542 O  O     . VAL A 1 456 ? -0.140  16.462  14.771  1.00 36.98  ? 456 VAL A O     1 
ATOM   3543 C  CB    . VAL A 1 456 ? -2.609  18.637  15.379  1.00 36.01  ? 456 VAL A CB    1 
ATOM   3544 C  CG1   . VAL A 1 456 ? -2.813  17.396  16.242  1.00 37.05  ? 456 VAL A CG1   1 
ATOM   3545 C  CG2   . VAL A 1 456 ? -2.811  19.910  16.196  1.00 34.38  ? 456 VAL A CG2   1 
ATOM   3546 N  N     . GLY A 1 457 ? -1.408  16.950  12.984  1.00 34.69  ? 457 GLY A N     1 
ATOM   3547 C  CA    . GLY A 1 457 ? -1.076  15.689  12.343  1.00 32.34  ? 457 GLY A CA    1 
ATOM   3548 C  C     . GLY A 1 457 ? 0.392   15.592  11.983  1.00 36.78  ? 457 GLY A C     1 
ATOM   3549 O  O     . GLY A 1 457 ? 1.008   14.535  12.131  1.00 33.59  ? 457 GLY A O     1 
ATOM   3550 N  N     . ALA A 1 458 ? 0.974   16.696  11.508  1.00 31.83  ? 458 ALA A N     1 
ATOM   3551 C  CA    . ALA A 1 458 ? 2.384   16.677  11.136  1.00 33.34  ? 458 ALA A CA    1 
ATOM   3552 C  C     . ALA A 1 458 ? 3.283   16.497  12.351  1.00 33.13  ? 458 ALA A C     1 
ATOM   3553 O  O     . ALA A 1 458 ? 4.378   15.940  12.227  1.00 38.30  ? 458 ALA A O     1 
ATOM   3554 C  CB    . ALA A 1 458 ? 2.756   17.959  10.390  1.00 35.96  ? 458 ALA A CB    1 
ATOM   3555 N  N     . ALA A 1 459 ? 2.846   16.951  13.524  1.00 33.51  ? 459 ALA A N     1 
ATOM   3556 C  CA    . ALA A 1 459 ? 3.661   16.881  14.730  1.00 35.46  ? 459 ALA A CA    1 
ATOM   3557 C  C     . ALA A 1 459 ? 3.476   15.586  15.508  1.00 34.99  ? 459 ALA A C     1 
ATOM   3558 O  O     . ALA A 1 459 ? 4.080   15.434  16.576  1.00 37.90  ? 459 ALA A O     1 
ATOM   3559 C  CB    . ALA A 1 459 ? 3.351   18.071  15.644  1.00 34.84  ? 459 ALA A CB    1 
ATOM   3560 N  N     . MET A 1 460 ? 2.669   14.655  15.002  1.00 33.52  ? 460 MET A N     1 
ATOM   3561 C  CA    . MET A 1 460 ? 2.384   13.422  15.725  1.00 35.63  ? 460 MET A CA    1 
ATOM   3562 C  C     . MET A 1 460 ? 3.667   12.693  16.096  1.00 37.40  ? 460 MET A C     1 
ATOM   3563 O  O     . MET A 1 460 ? 4.595   12.580  15.292  1.00 39.82  ? 460 MET A O     1 
ATOM   3564 C  CB    . MET A 1 460 ? 1.496   12.506  14.882  1.00 34.32  ? 460 MET A CB    1 
ATOM   3565 C  CG    . MET A 1 460 ? 0.041   12.930  14.813  1.00 32.83  ? 460 MET A CG    1 
ATOM   3566 S  SD    . MET A 1 460 ? -0.946  11.791  13.825  1.00 40.21  ? 460 MET A SD    1 
ATOM   3567 C  CE    . MET A 1 460 ? -0.604  10.240  14.646  1.00 31.72  ? 460 MET A CE    1 
ATOM   3568 N  N     . ARG A 1 461 ? 3.717   12.213  17.336  1.00 33.68  ? 461 ARG A N     1 
ATOM   3569 C  CA    . ARG A 1 461 ? 4.803   11.367  17.802  1.00 37.08  ? 461 ARG A CA    1 
ATOM   3570 C  C     . ARG A 1 461 ? 4.208   10.251  18.647  1.00 39.18  ? 461 ARG A C     1 
ATOM   3571 O  O     . ARG A 1 461 ? 3.095   10.366  19.168  1.00 36.25  ? 461 ARG A O     1 
ATOM   3572 C  CB    . ARG A 1 461 ? 5.846   12.163  18.598  1.00 36.23  ? 461 ARG A CB    1 
ATOM   3573 C  CG    . ARG A 1 461 ? 6.368   13.397  17.872  1.00 42.10  ? 461 ARG A CG    1 
ATOM   3574 C  CD    . ARG A 1 461 ? 7.290   14.216  18.759  1.00 40.32  ? 461 ARG A CD    1 
ATOM   3575 N  NE    . ARG A 1 461 ? 8.523   13.507  19.074  1.00 40.06  ? 461 ARG A NE    1 
ATOM   3576 C  CZ    . ARG A 1 461 ? 9.285   13.770  20.126  1.00 41.57  ? 461 ARG A CZ    1 
ATOM   3577 N  NH1   . ARG A 1 461 ? 8.959   14.709  20.999  1.00 42.50  ? 461 ARG A NH1   1 
ATOM   3578 N  NH2   . ARG A 1 461 ? 10.402  13.070  20.311  1.00 46.21  ? 461 ARG A NH2   1 
ATOM   3579 N  N     . SER A 1 462 ? 4.963   9.163   18.772  1.00 39.46  ? 462 SER A N     1 
ATOM   3580 C  CA    . SER A 1 462 ? 4.463   7.970   19.438  1.00 43.98  ? 462 SER A CA    1 
ATOM   3581 C  C     . SER A 1 462 ? 5.644   7.097   19.828  1.00 52.39  ? 462 SER A C     1 
ATOM   3582 O  O     . SER A 1 462 ? 6.689   7.114   19.169  1.00 48.48  ? 462 SER A O     1 
ATOM   3583 C  CB    . SER A 1 462 ? 3.490   7.200   18.537  1.00 44.14  ? 462 SER A CB    1 
ATOM   3584 O  OG    . SER A 1 462 ? 2.940   6.078   19.204  1.00 48.49  ? 462 SER A OG    1 
ATOM   3585 N  N     . GLU A 1 463 ? 5.467   6.335   20.903  1.00 48.57  ? 463 GLU A N     1 
ATOM   3586 C  CA    . GLU A 1 463 ? 6.531   5.475   21.396  1.00 61.87  ? 463 GLU A CA    1 
ATOM   3587 C  C     . GLU A 1 463 ? 6.650   4.225   20.531  1.00 61.65  ? 463 GLU A C     1 
ATOM   3588 O  O     . GLU A 1 463 ? 5.672   3.752   19.945  1.00 59.12  ? 463 GLU A O     1 
ATOM   3589 C  CB    . GLU A 1 463 ? 6.284   5.081   22.854  1.00 63.57  ? 463 GLU A CB    1 
ATOM   3590 C  CG    . GLU A 1 463 ? 5.101   4.149   23.066  1.00 69.21  ? 463 GLU A CG    1 
ATOM   3591 C  CD    . GLU A 1 463 ? 5.165   3.427   24.397  1.00 76.28  ? 463 GLU A CD    1 
ATOM   3592 O  OE1   . GLU A 1 463 ? 5.844   3.928   25.316  1.00 72.39  ? 463 GLU A OE1   1 
ATOM   3593 O  OE2   . GLU A 1 463 ? 4.547   2.351   24.523  1.00 78.15  ? 463 GLU A OE2   1 
ATOM   3594 N  N     . ALA A 1 464 ? 7.868   3.695   20.459  1.00 68.80  ? 464 ALA A N     1 
ATOM   3595 C  CA    . ALA A 1 464 ? 8.133   2.523   19.635  1.00 84.48  ? 464 ALA A CA    1 
ATOM   3596 C  C     . ALA A 1 464 ? 7.289   1.340   20.091  1.00 93.92  ? 464 ALA A C     1 
ATOM   3597 O  O     . ALA A 1 464 ? 7.297   0.969   21.268  1.00 98.33  ? 464 ALA A O     1 
ATOM   3598 C  CB    . ALA A 1 464 ? 9.618   2.166   19.693  1.00 93.47  ? 464 ALA A CB    1 
ATOM   3599 N  N     . THR A 1 465 ? 6.563   0.746   19.147  1.00 103.86 ? 465 THR A N     1 
ATOM   3600 C  CA    . THR A 1 465 ? 5.701   -0.393  19.389  1.00 110.20 ? 465 THR A CA    1 
ATOM   3601 C  C     . THR A 1 465 ? 6.321   -1.632  18.737  1.00 125.22 ? 465 THR A C     1 
ATOM   3602 O  O     . THR A 1 465 ? 7.559   -1.750  18.681  1.00 123.20 ? 465 THR A O     1 
ATOM   3603 C  CB    . THR A 1 465 ? 4.298   -0.065  18.885  1.00 102.62 ? 465 THR A CB    1 
ATOM   3604 O  OG1   . THR A 1 465 ? 4.341   0.175   17.472  1.00 104.24 ? 465 THR A OG1   1 
ATOM   3605 C  CG2   . THR A 1 465 ? 3.762   1.175   19.586  1.00 94.52  ? 465 THR A CG2   1 
ATOM   3606 N  N     . ALA A 1 466 ? 5.480   -2.543  18.250  1.00 132.99 ? 466 ALA A N     1 
ATOM   3607 C  CA    . ALA A 1 466 ? 5.931   -3.775  17.610  1.00 140.14 ? 466 ALA A CA    1 
ATOM   3608 C  C     . ALA A 1 466 ? 5.222   -3.935  16.265  1.00 140.86 ? 466 ALA A C     1 
ATOM   3609 O  O     . ALA A 1 466 ? 4.520   -4.913  16.009  1.00 134.03 ? 466 ALA A O     1 
ATOM   3610 C  CB    . ALA A 1 466 ? 5.687   -4.984  18.509  1.00 136.00 ? 466 ALA A CB    1 
ATOM   3611 N  N     . ALA A 1 467 ? 5.407   -2.944  15.393  1.00 132.28 ? 467 ALA A N     1 
ATOM   3612 C  CA    . ALA A 1 467 ? 4.817   -2.956  14.059  1.00 122.41 ? 467 ALA A CA    1 
ATOM   3613 C  C     . ALA A 1 467 ? 5.884   -3.246  13.006  1.00 124.04 ? 467 ALA A C     1 
ATOM   3614 O  O     . ALA A 1 467 ? 5.834   -4.288  12.350  1.00 109.48 ? 467 ALA A O     1 
ATOM   3615 C  CB    . ALA A 1 467 ? 4.108   -1.631  13.775  1.00 105.36 ? 467 ALA A CB    1 
ATOM   3616 N  N     . ALA A 1 468 ? 6.850   -2.347  12.827  1.00 122.22 ? 468 ALA A N     1 
ATOM   3617 C  CA    . ALA A 1 468 ? 7.953   -2.593  11.908  1.00 120.18 ? 468 ALA A CA    1 
ATOM   3618 C  C     . ALA A 1 468 ? 9.094   -3.290  12.636  1.00 124.64 ? 468 ALA A C     1 
ATOM   3619 O  O     . ALA A 1 468 ? 8.856   -4.143  13.498  1.00 124.81 ? 468 ALA A O     1 
ATOM   3620 C  CB    . ALA A 1 468 ? 8.432   -1.283  11.280  1.00 112.24 ? 468 ALA A CB    1 
ATOM   3621 N  N     . GLU A 1 469 ? 10.336  -2.936  12.302  1.00 125.35 ? 469 GLU A N     1 
ATOM   3622 C  CA    . GLU A 1 469 ? 11.511  -3.496  12.959  1.00 127.13 ? 469 GLU A CA    1 
ATOM   3623 C  C     . GLU A 1 469 ? 12.087  -2.556  14.014  1.00 130.47 ? 469 GLU A C     1 
ATOM   3624 O  O     . GLU A 1 469 ? 13.290  -2.601  14.296  1.00 130.26 ? 469 GLU A O     1 
ATOM   3625 C  CB    . GLU A 1 469 ? 12.581  -3.859  11.929  1.00 125.13 ? 469 GLU A CB    1 
ATOM   3626 C  CG    . GLU A 1 469 ? 13.087  -2.694  11.094  1.00 120.67 ? 469 GLU A CG    1 
ATOM   3627 C  CD    . GLU A 1 469 ? 12.250  -2.453  9.854   1.00 102.22 ? 469 GLU A CD    1 
ATOM   3628 O  OE1   . GLU A 1 469 ? 11.012  -2.605  9.928   1.00 104.54 ? 469 GLU A OE1   1 
ATOM   3629 O  OE2   . GLU A 1 469 ? 12.834  -2.120  8.801   1.00 92.50  ? 469 GLU A OE2   1 
ATOM   3630 N  N     . HIS A 1 470 ? 11.251  -1.707  14.608  1.00 135.53 ? 470 HIS A N     1 
ATOM   3631 C  CA    . HIS A 1 470 ? 11.693  -0.786  15.646  1.00 139.64 ? 470 HIS A CA    1 
ATOM   3632 C  C     . HIS A 1 470 ? 11.520  -1.419  17.021  1.00 140.07 ? 470 HIS A C     1 
ATOM   3633 O  O     . HIS A 1 470 ? 10.516  -2.083  17.293  1.00 138.20 ? 470 HIS A O     1 
ATOM   3634 C  CB    . HIS A 1 470 ? 10.913  0.529   15.577  1.00 136.13 ? 470 HIS A CB    1 
ATOM   3635 C  CG    . HIS A 1 470 ? 11.010  1.220   14.252  1.00 134.28 ? 470 HIS A CG    1 
ATOM   3636 N  ND1   . HIS A 1 470 ? 10.183  0.916   13.192  1.00 132.79 ? 470 HIS A ND1   1 
ATOM   3637 C  CD2   . HIS A 1 470 ? 11.837  2.198   13.815  1.00 132.80 ? 470 HIS A CD2   1 
ATOM   3638 C  CE1   . HIS A 1 470 ? 10.496  1.678   12.160  1.00 125.51 ? 470 HIS A CE1   1 
ATOM   3639 N  NE2   . HIS A 1 470 ? 11.497  2.465   12.511  1.00 126.52 ? 470 HIS A NE2   1 
ATOM   3640 N  N     . LYS A 1 471 ? 12.508  -1.205  17.888  1.00 136.01 ? 471 LYS A N     1 
ATOM   3641 C  CA    . LYS A 1 471 ? 12.485  -1.770  19.230  1.00 134.12 ? 471 LYS A CA    1 
ATOM   3642 C  C     . LYS A 1 471 ? 12.777  -0.700  20.273  1.00 136.51 ? 471 LYS A C     1 
ATOM   3643 O  O     . LYS A 1 471 ? 12.858  0.490   19.949  1.00 129.49 ? 471 LYS A O     1 
ATOM   3644 C  CB    . LYS A 1 471 ? 13.491  -2.917  19.345  1.00 130.08 ? 471 LYS A CB    1 
ATOM   3645 C  CG    . LYS A 1 471 ? 13.270  -4.044  18.345  1.00 126.93 ? 471 LYS A CG    1 
ATOM   3646 C  CD    . LYS A 1 471 ? 14.326  -5.128  18.490  1.00 124.25 ? 471 LYS A CD    1 
ATOM   3647 C  CE    . LYS A 1 471 ? 14.114  -6.243  17.477  1.00 117.02 ? 471 LYS A CE    1 
ATOM   3648 N  NZ    . LYS A 1 471 ? 15.153  -7.306  17.579  1.00 105.94 ? 471 LYS A NZ    1 
ATOM   3649 N  N     . GLY A 1 472 ? 12.935  -1.115  21.526  1.00 142.78 ? 472 GLY A N     1 
ATOM   3650 C  CA    . GLY A 1 472 ? 13.266  -0.195  22.597  1.00 136.56 ? 472 GLY A CA    1 
ATOM   3651 C  C     . GLY A 1 472 ? 12.117  0.738   22.940  1.00 132.18 ? 472 GLY A C     1 
ATOM   3652 O  O     . GLY A 1 472 ? 11.051  0.733   22.325  1.00 128.35 ? 472 GLY A O     1 
ATOM   3653 N  N     . LYS A 1 473 ? 12.358  1.557   23.960  1.00 127.12 ? 473 LYS A N     1 
ATOM   3654 C  CA    . LYS A 1 473 ? 11.394  2.546   24.440  1.00 119.72 ? 473 LYS A CA    1 
ATOM   3655 C  C     . LYS A 1 473 ? 11.862  3.915   23.950  1.00 106.04 ? 473 LYS A C     1 
ATOM   3656 O  O     . LYS A 1 473 ? 12.639  4.601   24.617  1.00 100.54 ? 473 LYS A O     1 
ATOM   3657 C  CB    . LYS A 1 473 ? 11.268  2.501   25.959  1.00 125.87 ? 473 LYS A CB    1 
ATOM   3658 C  CG    . LYS A 1 473 ? 10.979  1.115   26.514  1.00 130.44 ? 473 LYS A CG    1 
ATOM   3659 C  CD    . LYS A 1 473 ? 9.703   0.536   25.927  1.00 128.76 ? 473 LYS A CD    1 
ATOM   3660 C  CE    . LYS A 1 473 ? 8.491   1.371   26.304  1.00 118.92 ? 473 LYS A CE    1 
ATOM   3661 N  NZ    . LYS A 1 473 ? 7.233   0.792   25.758  1.00 112.62 ? 473 LYS A NZ    1 
ATOM   3662 N  N     . VAL A 1 474 ? 11.379  4.304   22.771  1.00 91.89  ? 474 VAL A N     1 
ATOM   3663 C  CA    . VAL A 1 474 ? 11.750  5.563   22.139  1.00 75.13  ? 474 VAL A CA    1 
ATOM   3664 C  C     . VAL A 1 474 ? 10.494  6.216   21.578  1.00 60.89  ? 474 VAL A C     1 
ATOM   3665 O  O     . VAL A 1 474 ? 9.556   5.536   21.152  1.00 64.29  ? 474 VAL A O     1 
ATOM   3666 C  CB    . VAL A 1 474 ? 12.801  5.352   21.025  1.00 69.11  ? 474 VAL A CB    1 
ATOM   3667 C  CG1   . VAL A 1 474 ? 12.960  6.611   20.193  1.00 65.02  ? 474 VAL A CG1   1 
ATOM   3668 C  CG2   . VAL A 1 474 ? 14.134  4.934   21.624  1.00 72.90  ? 474 VAL A CG2   1 
ATOM   3669 N  N     . ILE A 1 475 ? 10.481  7.545   21.582  1.00 58.92  ? 475 ILE A N     1 
ATOM   3670 C  CA    . ILE A 1 475 ? 9.393   8.333   21.012  1.00 51.55  ? 475 ILE A CA    1 
ATOM   3671 C  C     . ILE A 1 475 ? 9.855   8.864   19.662  1.00 51.78  ? 475 ILE A C     1 
ATOM   3672 O  O     . ILE A 1 475 ? 10.829  9.621   19.584  1.00 57.08  ? 475 ILE A O     1 
ATOM   3673 C  CB    . ILE A 1 475 ? 8.979   9.480   21.946  1.00 43.28  ? 475 ILE A CB    1 
ATOM   3674 C  CG1   . ILE A 1 475 ? 8.617   8.933   23.330  1.00 47.77  ? 475 ILE A CG1   1 
ATOM   3675 C  CG2   . ILE A 1 475 ? 7.815   10.251  21.350  1.00 44.39  ? 475 ILE A CG2   1 
ATOM   3676 C  CD1   . ILE A 1 475 ? 8.228   10.010  24.327  1.00 56.96  ? 475 ILE A CD1   1 
ATOM   3677 N  N     . MET A 1 476 ? 9.164   8.468   18.596  1.00 43.97  ? 476 MET A N     1 
ATOM   3678 C  CA    . MET A 1 476 ? 9.543   8.826   17.238  1.00 47.76  ? 476 MET A CA    1 
ATOM   3679 C  C     . MET A 1 476 ? 8.417   9.588   16.554  1.00 45.92  ? 476 MET A C     1 
ATOM   3680 O  O     . MET A 1 476 ? 7.274   9.591   17.013  1.00 43.70  ? 476 MET A O     1 
ATOM   3681 C  CB    . MET A 1 476 ? 9.906   7.581   16.417  1.00 51.31  ? 476 MET A CB    1 
ATOM   3682 C  CG    . MET A 1 476 ? 8.795   6.545   16.334  1.00 58.37  ? 476 MET A CG    1 
ATOM   3683 S  SD    . MET A 1 476 ? 9.367   5.013   15.570  1.00 89.80  ? 476 MET A SD    1 
ATOM   3684 C  CE    . MET A 1 476 ? 7.885   4.011   15.649  1.00 80.55  ? 476 MET A CE    1 
ATOM   3685 N  N     . HIS A 1 477 ? 8.759   10.233  15.442  1.00 42.26  ? 477 HIS A N     1 
ATOM   3686 C  CA    . HIS A 1 477 ? 7.780   10.988  14.674  1.00 41.51  ? 477 HIS A CA    1 
ATOM   3687 C  C     . HIS A 1 477 ? 7.059   10.076  13.691  1.00 41.93  ? 477 HIS A C     1 
ATOM   3688 O  O     . HIS A 1 477 ? 7.665   9.193   13.077  1.00 45.19  ? 477 HIS A O     1 
ATOM   3689 C  CB    . HIS A 1 477 ? 8.451   12.141  13.925  1.00 39.64  ? 477 HIS A CB    1 
ATOM   3690 C  CG    . HIS A 1 477 ? 9.040   13.186  14.823  1.00 41.48  ? 477 HIS A CG    1 
ATOM   3691 N  ND1   . HIS A 1 477 ? 8.414   14.387  15.081  1.00 34.41  ? 477 HIS A ND1   1 
ATOM   3692 C  CD2   . HIS A 1 477 ? 10.202  13.208  15.520  1.00 41.37  ? 477 HIS A CD2   1 
ATOM   3693 C  CE1   . HIS A 1 477 ? 9.165   15.101  15.902  1.00 44.83  ? 477 HIS A CE1   1 
ATOM   3694 N  NE2   . HIS A 1 477 ? 10.255  14.409  16.183  1.00 38.78  ? 477 HIS A NE2   1 
ATOM   3695 N  N     . ASP A 1 478 ? 5.750   10.291  13.553  1.00 34.54  ? 478 ASP A N     1 
ATOM   3696 C  CA    . ASP A 1 478 ? 4.924   9.533   12.611  1.00 38.93  ? 478 ASP A CA    1 
ATOM   3697 C  C     . ASP A 1 478 ? 3.774   10.427  12.170  1.00 36.66  ? 478 ASP A C     1 
ATOM   3698 O  O     . ASP A 1 478 ? 2.606   10.178  12.491  1.00 36.88  ? 478 ASP A O     1 
ATOM   3699 C  CB    . ASP A 1 478 ? 4.412   8.241   13.248  1.00 42.61  ? 478 ASP A CB    1 
ATOM   3700 C  CG    . ASP A 1 478 ? 3.918   7.236   12.223  1.00 39.14  ? 478 ASP A CG    1 
ATOM   3701 O  OD1   . ASP A 1 478 ? 3.614   7.644   11.078  1.00 39.15  ? 478 ASP A OD1   1 
ATOM   3702 O  OD2   . ASP A 1 478 ? 3.836   6.037   12.552  1.00 41.23  ? 478 ASP A OD2   1 
ATOM   3703 N  N     . PRO A 1 479 ? 4.077   11.495  11.432  1.00 36.84  ? 479 PRO A N     1 
ATOM   3704 C  CA    . PRO A 1 479 ? 3.033   12.462  11.065  1.00 37.38  ? 479 PRO A CA    1 
ATOM   3705 C  C     . PRO A 1 479 ? 1.897   11.794  10.308  1.00 34.76  ? 479 PRO A C     1 
ATOM   3706 O  O     . PRO A 1 479 ? 2.119   11.026  9.370   1.00 35.75  ? 479 PRO A O     1 
ATOM   3707 C  CB    . PRO A 1 479 ? 3.782   13.478  10.192  1.00 37.05  ? 479 PRO A CB    1 
ATOM   3708 C  CG    . PRO A 1 479 ? 5.000   12.752  9.719   1.00 37.20  ? 479 PRO A CG    1 
ATOM   3709 C  CD    . PRO A 1 479 ? 5.381   11.845  10.848  1.00 39.80  ? 479 PRO A CD    1 
ATOM   3710 N  N     . PHE A 1 480 ? 0.668   12.102  10.723  1.00 36.92  ? 480 PHE A N     1 
ATOM   3711 C  CA    . PHE A 1 480 ? -0.539  11.532  10.132  1.00 36.71  ? 480 PHE A CA    1 
ATOM   3712 C  C     . PHE A 1 480 ? -0.547  10.010  10.199  1.00 36.44  ? 480 PHE A C     1 
ATOM   3713 O  O     . PHE A 1 480 ? -1.336  9.360   9.505   1.00 32.55  ? 480 PHE A O     1 
ATOM   3714 C  CB    . PHE A 1 480 ? -0.724  11.999  8.682   1.00 35.57  ? 480 PHE A CB    1 
ATOM   3715 C  CG    . PHE A 1 480 ? -1.033  13.468  8.550   1.00 39.56  ? 480 PHE A CG    1 
ATOM   3716 C  CD1   . PHE A 1 480 ? -0.033  14.414  8.691   1.00 35.05  ? 480 PHE A CD1   1 
ATOM   3717 C  CD2   . PHE A 1 480 ? -2.318  13.898  8.268   1.00 36.71  ? 480 PHE A CD2   1 
ATOM   3718 C  CE1   . PHE A 1 480 ? -0.311  15.765  8.571   1.00 37.06  ? 480 PHE A CE1   1 
ATOM   3719 C  CE2   . PHE A 1 480 ? -2.603  15.247  8.144   1.00 38.46  ? 480 PHE A CE2   1 
ATOM   3720 C  CZ    . PHE A 1 480 ? -1.599  16.182  8.296   1.00 35.84  ? 480 PHE A CZ    1 
ATOM   3721 N  N     . ALA A 1 481 ? 0.313   9.422   11.031  1.00 32.40  ? 481 ALA A N     1 
ATOM   3722 C  CA    . ALA A 1 481 ? 0.462   7.971   11.102  1.00 38.63  ? 481 ALA A CA    1 
ATOM   3723 C  C     . ALA A 1 481 ? 0.856   7.388   9.749   1.00 37.53  ? 481 ALA A C     1 
ATOM   3724 O  O     . ALA A 1 481 ? 0.554   6.232   9.443   1.00 36.75  ? 481 ALA A O     1 
ATOM   3725 C  CB    . ALA A 1 481 ? -0.811  7.301   11.625  1.00 34.98  ? 481 ALA A CB    1 
ATOM   3726 N  N     . MET A 1 482 ? 1.544   8.185   8.933   1.00 36.76  ? 482 MET A N     1 
ATOM   3727 C  CA    . MET A 1 482 ? 1.853   7.821   7.558   1.00 34.22  ? 482 MET A CA    1 
ATOM   3728 C  C     . MET A 1 482 ? 3.344   7.685   7.289   1.00 36.28  ? 482 MET A C     1 
ATOM   3729 O  O     . MET A 1 482 ? 3.729   7.447   6.139   1.00 40.49  ? 482 MET A O     1 
ATOM   3730 C  CB    . MET A 1 482 ? 1.252   8.855   6.596   1.00 40.92  ? 482 MET A CB    1 
ATOM   3731 C  CG    . MET A 1 482 ? -0.259  8.758   6.417   1.00 40.31  ? 482 MET A CG    1 
ATOM   3732 S  SD    . MET A 1 482 ? -0.741  7.460   5.261   1.00 41.55  ? 482 MET A SD    1 
ATOM   3733 C  CE    . MET A 1 482 ? -0.145  8.139   3.712   1.00 40.75  ? 482 MET A CE    1 
ATOM   3734 N  N     . ARG A 1 483 ? 4.192   7.822   8.308   1.00 34.17  ? 483 ARG A N     1 
ATOM   3735 C  CA    . ARG A 1 483 ? 5.634   7.788   8.082   1.00 36.44  ? 483 ARG A CA    1 
ATOM   3736 C  C     . ARG A 1 483 ? 6.083   6.605   7.236   1.00 41.45  ? 483 ARG A C     1 
ATOM   3737 O  O     . ARG A 1 483 ? 6.934   6.804   6.353   1.00 42.07  ? 483 ARG A O     1 
ATOM   3738 C  CB    . ARG A 1 483 ? 6.384   7.782   9.422   1.00 40.24  ? 483 ARG A CB    1 
ATOM   3739 C  CG    . ARG A 1 483 ? 7.873   8.071   9.272   1.00 41.36  ? 483 ARG A CG    1 
ATOM   3740 C  CD    . ARG A 1 483 ? 8.685   7.571   10.457  1.00 42.45  ? 483 ARG A CD    1 
ATOM   3741 N  NE    . ARG A 1 483 ? 8.675   6.117   10.552  1.00 56.31  ? 483 ARG A NE    1 
ATOM   3742 C  CZ    . ARG A 1 483 ? 7.978   5.431   11.448  1.00 64.61  ? 483 ARG A CZ    1 
ATOM   3743 N  NH1   . ARG A 1 483 ? 7.236   6.040   12.357  1.00 59.71  ? 483 ARG A NH1   1 
ATOM   3744 N  NH2   . ARG A 1 483 ? 8.032   4.102   11.435  1.00 64.80  ? 483 ARG A NH2   1 
ATOM   3745 N  N     . PRO A 1 484 ? 5.591   5.380   7.444   1.00 47.12  ? 484 PRO A N     1 
ATOM   3746 C  CA    . PRO A 1 484 ? 6.025   4.261   6.597   1.00 41.71  ? 484 PRO A CA    1 
ATOM   3747 C  C     . PRO A 1 484 ? 5.336   4.202   5.247   1.00 39.45  ? 484 PRO A C     1 
ATOM   3748 O  O     . PRO A 1 484 ? 5.699   3.344   4.432   1.00 45.55  ? 484 PRO A O     1 
ATOM   3749 C  CB    . PRO A 1 484 ? 5.664   3.021   7.439   1.00 45.05  ? 484 PRO A CB    1 
ATOM   3750 C  CG    . PRO A 1 484 ? 5.218   3.543   8.787   1.00 43.69  ? 484 PRO A CG    1 
ATOM   3751 C  CD    . PRO A 1 484 ? 4.729   4.930   8.548   1.00 40.86  ? 484 PRO A CD    1 
ATOM   3752 N  N     . PHE A 1 485 ? 4.371   5.083   4.972   1.00 39.06  ? 485 PHE A N     1 
ATOM   3753 C  CA    . PHE A 1 485 ? 3.468   4.884   3.848   1.00 43.07  ? 485 PHE A CA    1 
ATOM   3754 C  C     . PHE A 1 485 ? 3.379   6.048   2.871   1.00 42.78  ? 485 PHE A C     1 
ATOM   3755 O  O     . PHE A 1 485 ? 2.608   5.956   1.910   1.00 43.90  ? 485 PHE A O     1 
ATOM   3756 C  CB    . PHE A 1 485 ? 2.055   4.571   4.356   1.00 40.89  ? 485 PHE A CB    1 
ATOM   3757 C  CG    . PHE A 1 485 ? 2.013   3.471   5.372   1.00 42.35  ? 485 PHE A CG    1 
ATOM   3758 C  CD1   . PHE A 1 485 ? 2.458   2.197   5.054   1.00 40.67  ? 485 PHE A CD1   1 
ATOM   3759 C  CD2   . PHE A 1 485 ? 1.528   3.708   6.646   1.00 41.15  ? 485 PHE A CD2   1 
ATOM   3760 C  CE1   . PHE A 1 485 ? 2.423   1.180   5.989   1.00 42.20  ? 485 PHE A CE1   1 
ATOM   3761 C  CE2   . PHE A 1 485 ? 1.489   2.699   7.586   1.00 39.35  ? 485 PHE A CE2   1 
ATOM   3762 C  CZ    . PHE A 1 485 ? 1.937   1.433   7.259   1.00 43.27  ? 485 PHE A CZ    1 
ATOM   3763 N  N     . PHE A 1 486 ? 4.128   7.128   3.075   1.00 38.35  ? 486 PHE A N     1 
ATOM   3764 C  CA    . PHE A 1 486 ? 4.054   8.252   2.150   1.00 42.70  ? 486 PHE A CA    1 
ATOM   3765 C  C     . PHE A 1 486 ? 4.428   7.810   0.743   1.00 41.05  ? 486 PHE A C     1 
ATOM   3766 O  O     . PHE A 1 486 ? 5.498   7.233   0.522   1.00 41.27  ? 486 PHE A O     1 
ATOM   3767 C  CB    . PHE A 1 486 ? 4.974   9.383   2.600   1.00 39.26  ? 486 PHE A CB    1 
ATOM   3768 C  CG    . PHE A 1 486 ? 4.511   10.079  3.845   1.00 36.68  ? 486 PHE A CG    1 
ATOM   3769 C  CD1   . PHE A 1 486 ? 3.265   10.683  3.894   1.00 36.61  ? 486 PHE A CD1   1 
ATOM   3770 C  CD2   . PHE A 1 486 ? 5.321   10.130  4.968   1.00 40.22  ? 486 PHE A CD2   1 
ATOM   3771 C  CE1   . PHE A 1 486 ? 2.836   11.324  5.039   1.00 37.30  ? 486 PHE A CE1   1 
ATOM   3772 C  CE2   . PHE A 1 486 ? 4.895   10.766  6.115   1.00 35.84  ? 486 PHE A CE2   1 
ATOM   3773 C  CZ    . PHE A 1 486 ? 3.653   11.363  6.151   1.00 37.37  ? 486 PHE A CZ    1 
ATOM   3774 N  N     . GLY A 1 487 ? 3.541   8.082   -0.211  1.00 39.42  ? 487 GLY A N     1 
ATOM   3775 C  CA    . GLY A 1 487 ? 3.832   7.797   -1.601  1.00 41.74  ? 487 GLY A CA    1 
ATOM   3776 C  C     . GLY A 1 487 ? 4.653   8.849   -2.312  1.00 39.96  ? 487 GLY A C     1 
ATOM   3777 O  O     . GLY A 1 487 ? 5.135   8.593   -3.418  1.00 39.13  ? 487 GLY A O     1 
ATOM   3778 N  N     . TYR A 1 488 ? 4.835   10.018  -1.706  1.00 38.81  ? 488 TYR A N     1 
ATOM   3779 C  CA    . TYR A 1 488 ? 5.534   11.116  -2.359  1.00 43.22  ? 488 TYR A CA    1 
ATOM   3780 C  C     . TYR A 1 488 ? 6.016   12.092  -1.293  1.00 43.72  ? 488 TYR A C     1 
ATOM   3781 O  O     . TYR A 1 488 ? 5.869   11.856  -0.090  1.00 40.76  ? 488 TYR A O     1 
ATOM   3782 C  CB    . TYR A 1 488 ? 4.630   11.804  -3.385  1.00 45.61  ? 488 TYR A CB    1 
ATOM   3783 C  CG    . TYR A 1 488 ? 3.399   12.432  -2.775  1.00 43.03  ? 488 TYR A CG    1 
ATOM   3784 C  CD1   . TYR A 1 488 ? 2.292   11.662  -2.446  1.00 43.23  ? 488 TYR A CD1   1 
ATOM   3785 C  CD2   . TYR A 1 488 ? 3.344   13.796  -2.528  1.00 40.77  ? 488 TYR A CD2   1 
ATOM   3786 C  CE1   . TYR A 1 488 ? 1.164   12.233  -1.887  1.00 43.30  ? 488 TYR A CE1   1 
ATOM   3787 C  CE2   . TYR A 1 488 ? 2.222   14.375  -1.968  1.00 40.94  ? 488 TYR A CE2   1 
ATOM   3788 C  CZ    . TYR A 1 488 ? 1.135   13.590  -1.649  1.00 48.56  ? 488 TYR A CZ    1 
ATOM   3789 O  OH    . TYR A 1 488 ? 0.017   14.166  -1.092  1.00 41.14  ? 488 TYR A OH    1 
ATOM   3790 N  N     . ASN A 1 489 ? 6.589   13.202  -1.756  1.00 44.11  ? 489 ASN A N     1 
ATOM   3791 C  CA    . ASN A 1 489 ? 7.168   14.214  -0.880  1.00 43.09  ? 489 ASN A CA    1 
ATOM   3792 C  C     . ASN A 1 489 ? 6.202   14.604  0.230   1.00 40.67  ? 489 ASN A C     1 
ATOM   3793 O  O     . ASN A 1 489 ? 5.075   15.036  -0.036  1.00 37.85  ? 489 ASN A O     1 
ATOM   3794 C  CB    . ASN A 1 489 ? 7.547   15.442  -1.709  1.00 42.34  ? 489 ASN A CB    1 
ATOM   3795 C  CG    . ASN A 1 489 ? 8.438   16.404  -0.954  1.00 42.21  ? 489 ASN A CG    1 
ATOM   3796 O  OD1   . ASN A 1 489 ? 8.019   17.008  0.037   1.00 46.21  ? 489 ASN A OD1   1 
ATOM   3797 N  ND2   . ASN A 1 489 ? 9.667   16.569  -1.428  1.00 44.15  ? 489 ASN A ND2   1 
ATOM   3798 N  N     . PHE A 1 490 ? 6.655   14.458  1.478   1.00 40.34  ? 490 PHE A N     1 
ATOM   3799 C  CA    . PHE A 1 490 ? 5.803   14.773  2.622   1.00 42.60  ? 490 PHE A CA    1 
ATOM   3800 C  C     . PHE A 1 490 ? 5.451   16.254  2.662   1.00 40.90  ? 490 PHE A C     1 
ATOM   3801 O  O     . PHE A 1 490 ? 4.329   16.620  3.031   1.00 39.28  ? 490 PHE A O     1 
ATOM   3802 C  CB    . PHE A 1 490 ? 6.489   14.345  3.920   1.00 40.94  ? 490 PHE A CB    1 
ATOM   3803 C  CG    . PHE A 1 490 ? 5.754   14.763  5.166   1.00 43.72  ? 490 PHE A CG    1 
ATOM   3804 C  CD1   . PHE A 1 490 ? 4.434   14.390  5.368   1.00 39.12  ? 490 PHE A CD1   1 
ATOM   3805 C  CD2   . PHE A 1 490 ? 6.390   15.508  6.144   1.00 42.66  ? 490 PHE A CD2   1 
ATOM   3806 C  CE1   . PHE A 1 490 ? 3.759   14.765  6.519   1.00 39.44  ? 490 PHE A CE1   1 
ATOM   3807 C  CE2   . PHE A 1 490 ? 5.718   15.890  7.296   1.00 44.57  ? 490 PHE A CE2   1 
ATOM   3808 C  CZ    . PHE A 1 490 ? 4.401   15.518  7.482   1.00 38.19  ? 490 PHE A CZ    1 
ATOM   3809 N  N     . GLY A 1 491 ? 6.397   17.120  2.298   1.00 43.85  ? 491 GLY A N     1 
ATOM   3810 C  CA    . GLY A 1 491 ? 6.092   18.539  2.223   1.00 35.77  ? 491 GLY A CA    1 
ATOM   3811 C  C     . GLY A 1 491 ? 4.955   18.830  1.262   1.00 40.21  ? 491 GLY A C     1 
ATOM   3812 O  O     . GLY A 1 491 ? 4.044   19.602  1.570   1.00 37.91  ? 491 GLY A O     1 
ATOM   3813 N  N     . LYS A 1 492 ? 4.996   18.212  0.079   1.00 39.73  ? 492 LYS A N     1 
ATOM   3814 C  CA    . LYS A 1 492 ? 3.882   18.335  -0.855  1.00 39.72  ? 492 LYS A CA    1 
ATOM   3815 C  C     . LYS A 1 492 ? 2.616   17.703  -0.294  1.00 41.08  ? 492 LYS A C     1 
ATOM   3816 O  O     . LYS A 1 492 ? 1.507   18.128  -0.635  1.00 40.07  ? 492 LYS A O     1 
ATOM   3817 C  CB    . LYS A 1 492 ? 4.248   17.696  -2.193  1.00 38.68  ? 492 LYS A CB    1 
ATOM   3818 C  CG    . LYS A 1 492 ? 5.577   18.167  -2.747  1.00 47.19  ? 492 LYS A CG    1 
ATOM   3819 C  CD    . LYS A 1 492 ? 5.638   19.683  -2.812  1.00 51.25  ? 492 LYS A CD    1 
ATOM   3820 C  CE    . LYS A 1 492 ? 6.975   20.144  -3.360  1.00 57.60  ? 492 LYS A CE    1 
ATOM   3821 N  NZ    . LYS A 1 492 ? 7.198   21.598  -3.139  1.00 57.49  ? 492 LYS A NZ    1 
ATOM   3822 N  N     . TYR A 1 493 ? 2.767   16.686  0.558   1.00 37.40  ? 493 TYR A N     1 
ATOM   3823 C  CA    . TYR A 1 493 ? 1.620   16.089  1.235   1.00 38.12  ? 493 TYR A CA    1 
ATOM   3824 C  C     . TYR A 1 493 ? 0.960   17.086  2.180   1.00 38.47  ? 493 TYR A C     1 
ATOM   3825 O  O     . TYR A 1 493 ? -0.273  17.164  2.249   1.00 39.25  ? 493 TYR A O     1 
ATOM   3826 C  CB    . TYR A 1 493 ? 2.076   14.837  1.985   1.00 39.48  ? 493 TYR A CB    1 
ATOM   3827 C  CG    . TYR A 1 493 ? 1.050   14.177  2.883   1.00 37.70  ? 493 TYR A CG    1 
ATOM   3828 C  CD1   . TYR A 1 493 ? 0.951   14.517  4.226   1.00 40.76  ? 493 TYR A CD1   1 
ATOM   3829 C  CD2   . TYR A 1 493 ? 0.217   13.176  2.399   1.00 38.90  ? 493 TYR A CD2   1 
ATOM   3830 C  CE1   . TYR A 1 493 ? 0.030   13.902  5.055   1.00 36.94  ? 493 TYR A CE1   1 
ATOM   3831 C  CE2   . TYR A 1 493 ? -0.708  12.552  3.221   1.00 35.48  ? 493 TYR A CE2   1 
ATOM   3832 C  CZ    . TYR A 1 493 ? -0.795  12.918  4.549   1.00 36.71  ? 493 TYR A CZ    1 
ATOM   3833 O  OH    . TYR A 1 493 ? -1.714  12.303  5.375   1.00 38.18  ? 493 TYR A OH    1 
ATOM   3834 N  N     . LEU A 1 494 ? 1.764   17.862  2.911   1.00 38.63  ? 494 LEU A N     1 
ATOM   3835 C  CA    . LEU A 1 494 ? 1.211   18.885  3.793   1.00 36.39  ? 494 LEU A CA    1 
ATOM   3836 C  C     . LEU A 1 494 ? 0.475   19.958  2.996   1.00 40.70  ? 494 LEU A C     1 
ATOM   3837 O  O     . LEU A 1 494 ? -0.658  20.328  3.328   1.00 39.20  ? 494 LEU A O     1 
ATOM   3838 C  CB    . LEU A 1 494 ? 2.326   19.506  4.637   1.00 41.72  ? 494 LEU A CB    1 
ATOM   3839 C  CG    . LEU A 1 494 ? 2.998   18.591  5.662   1.00 37.82  ? 494 LEU A CG    1 
ATOM   3840 C  CD1   . LEU A 1 494 ? 4.170   19.287  6.332   1.00 37.89  ? 494 LEU A CD1   1 
ATOM   3841 C  CD2   . LEU A 1 494 ? 1.977   18.136  6.700   1.00 34.41  ? 494 LEU A CD2   1 
ATOM   3842 N  N     . ALA A 1 495 ? 1.111   20.477  1.940   1.00 40.87  ? 495 ALA A N     1 
ATOM   3843 C  CA    . ALA A 1 495 ? 0.463   21.472  1.091   1.00 38.66  ? 495 ALA A CA    1 
ATOM   3844 C  C     . ALA A 1 495 ? -0.836  20.940  0.495   1.00 42.79  ? 495 ALA A C     1 
ATOM   3845 O  O     . ALA A 1 495 ? -1.808  21.692  0.353   1.00 42.12  ? 495 ALA A O     1 
ATOM   3846 C  CB    . ALA A 1 495 ? 1.419   21.916  -0.020  1.00 37.97  ? 495 ALA A CB    1 
ATOM   3847 N  N     . HIS A 1 496 ? -0.870  19.653  0.136   1.00 39.81  ? 496 HIS A N     1 
ATOM   3848 C  CA    . HIS A 1 496 ? -2.099  19.043  -0.361  1.00 39.36  ? 496 HIS A CA    1 
ATOM   3849 C  C     . HIS A 1 496 ? -3.196  19.097  0.697   1.00 42.15  ? 496 HIS A C     1 
ATOM   3850 O  O     . HIS A 1 496 ? -4.339  19.469  0.408   1.00 39.23  ? 496 HIS A O     1 
ATOM   3851 C  CB    . HIS A 1 496 ? -1.820  17.599  -0.785  1.00 40.70  ? 496 HIS A CB    1 
ATOM   3852 C  CG    . HIS A 1 496 ? -2.974  16.925  -1.459  1.00 43.09  ? 496 HIS A CG    1 
ATOM   3853 N  ND1   . HIS A 1 496 ? -3.583  17.438  -2.584  1.00 45.63  ? 496 HIS A ND1   1 
ATOM   3854 C  CD2   . HIS A 1 496 ? -3.620  15.770  -1.174  1.00 39.31  ? 496 HIS A CD2   1 
ATOM   3855 C  CE1   . HIS A 1 496 ? -4.561  16.632  -2.959  1.00 41.81  ? 496 HIS A CE1   1 
ATOM   3856 N  NE2   . HIS A 1 496 ? -4.603  15.611  -2.121  1.00 42.19  ? 496 HIS A NE2   1 
ATOM   3857 N  N     . TRP A 1 497 ? -2.861  18.732  1.936   1.00 36.55  ? 497 TRP A N     1 
ATOM   3858 C  CA    . TRP A 1 497 ? -3.835  18.814  3.020   1.00 37.64  ? 497 TRP A CA    1 
ATOM   3859 C  C     . TRP A 1 497 ? -4.272  20.253  3.261   1.00 44.53  ? 497 TRP A C     1 
ATOM   3860 O  O     . TRP A 1 497 ? -5.464  20.527  3.443   1.00 43.74  ? 497 TRP A O     1 
ATOM   3861 C  CB    . TRP A 1 497 ? -3.245  18.219  4.297   1.00 33.08  ? 497 TRP A CB    1 
ATOM   3862 C  CG    . TRP A 1 497 ? -3.575  16.775  4.502   1.00 38.59  ? 497 TRP A CG    1 
ATOM   3863 C  CD1   . TRP A 1 497 ? -2.941  15.701  3.948   1.00 37.74  ? 497 TRP A CD1   1 
ATOM   3864 C  CD2   . TRP A 1 497 ? -4.619  16.244  5.328   1.00 38.65  ? 497 TRP A CD2   1 
ATOM   3865 N  NE1   . TRP A 1 497 ? -3.528  14.534  4.377   1.00 37.65  ? 497 TRP A NE1   1 
ATOM   3866 C  CE2   . TRP A 1 497 ? -4.560  14.841  5.225   1.00 41.42  ? 497 TRP A CE2   1 
ATOM   3867 C  CE3   . TRP A 1 497 ? -5.596  16.820  6.147   1.00 39.24  ? 497 TRP A CE3   1 
ATOM   3868 C  CZ2   . TRP A 1 497 ? -5.444  14.005  5.906   1.00 42.09  ? 497 TRP A CZ2   1 
ATOM   3869 C  CZ3   . TRP A 1 497 ? -6.474  15.987  6.821   1.00 38.09  ? 497 TRP A CZ3   1 
ATOM   3870 C  CH2   . TRP A 1 497 ? -6.391  14.596  6.696   1.00 40.90  ? 497 TRP A CH2   1 
ATOM   3871 N  N     . LEU A 1 498 ? -3.317  21.187  3.271   1.00 39.75  ? 498 LEU A N     1 
ATOM   3872 C  CA    . LEU A 1 498 ? -3.652  22.589  3.495   1.00 43.60  ? 498 LEU A CA    1 
ATOM   3873 C  C     . LEU A 1 498 ? -4.551  23.134  2.394   1.00 45.65  ? 498 LEU A C     1 
ATOM   3874 O  O     . LEU A 1 498 ? -5.401  23.993  2.656   1.00 46.54  ? 498 LEU A O     1 
ATOM   3875 C  CB    . LEU A 1 498 ? -2.370  23.418  3.600   1.00 42.24  ? 498 LEU A CB    1 
ATOM   3876 C  CG    . LEU A 1 498 ? -1.513  23.195  4.849   1.00 40.23  ? 498 LEU A CG    1 
ATOM   3877 C  CD1   . LEU A 1 498 ? -0.104  23.722  4.636   1.00 38.60  ? 498 LEU A CD1   1 
ATOM   3878 C  CD2   . LEU A 1 498 ? -2.148  23.862  6.057   1.00 39.42  ? 498 LEU A CD2   1 
ATOM   3879 N  N     . SER A 1 499 ? -4.389  22.644  1.162   1.00 42.39  ? 499 SER A N     1 
ATOM   3880 C  CA    . SER A 1 499 ? -5.162  23.169  0.042   1.00 48.21  ? 499 SER A CA    1 
ATOM   3881 C  C     . SER A 1 499 ? -6.648  22.862  0.162   1.00 47.45  ? 499 SER A C     1 
ATOM   3882 O  O     . SER A 1 499 ? -7.459  23.546  -0.472  1.00 48.83  ? 499 SER A O     1 
ATOM   3883 C  CB    . SER A 1 499 ? -4.625  22.611  -1.278  1.00 47.63  ? 499 SER A CB    1 
ATOM   3884 O  OG    . SER A 1 499 ? -4.834  21.212  -1.365  1.00 48.87  ? 499 SER A OG    1 
ATOM   3885 N  N     A MET A 1 500 ? -7.027  21.859  0.956   0.59 48.36  ? 500 MET A N     1 
ATOM   3886 N  N     B MET A 1 500 ? -7.016  21.843  0.944   0.41 50.24  ? 500 MET A N     1 
ATOM   3887 C  CA    A MET A 1 500 ? -8.443  21.538  1.099   0.59 50.01  ? 500 MET A CA    1 
ATOM   3888 C  CA    B MET A 1 500 ? -8.426  21.519  1.139   0.41 48.46  ? 500 MET A CA    1 
ATOM   3889 C  C     A MET A 1 500 ? -9.228  22.705  1.683   0.59 52.03  ? 500 MET A C     1 
ATOM   3890 C  C     B MET A 1 500 ? -9.209  22.716  1.657   0.41 50.56  ? 500 MET A C     1 
ATOM   3891 O  O     A MET A 1 500 ? -10.433 22.828  1.432   0.59 54.46  ? 500 MET A O     1 
ATOM   3892 O  O     B MET A 1 500 ? -10.392 22.872  1.334   0.41 54.68  ? 500 MET A O     1 
ATOM   3893 C  CB    A MET A 1 500 ? -8.615  20.292  1.966   0.59 47.47  ? 500 MET A CB    1 
ATOM   3894 C  CB    B MET A 1 500 ? -8.564  20.343  2.106   0.41 47.52  ? 500 MET A CB    1 
ATOM   3895 C  CG    A MET A 1 500 ? -7.900  19.068  1.426   0.59 47.08  ? 500 MET A CG    1 
ATOM   3896 C  CG    B MET A 1 500 ? -7.941  19.048  1.607   0.41 47.03  ? 500 MET A CG    1 
ATOM   3897 S  SD    A MET A 1 500 ? -8.470  18.610  -0.223  0.59 56.19  ? 500 MET A SD    1 
ATOM   3898 S  SD    B MET A 1 500 ? -7.760  17.796  2.895   0.41 41.54  ? 500 MET A SD    1 
ATOM   3899 C  CE    A MET A 1 500 ? -7.232  17.402  -0.680  0.59 47.78  ? 500 MET A CE    1 
ATOM   3900 C  CE    B MET A 1 500 ? -9.455  17.593  3.437   0.41 43.39  ? 500 MET A CE    1 
ATOM   3901 N  N     . ALA A 1 501 ? -8.572  23.568  2.462   1.00 47.12  ? 501 ALA A N     1 
ATOM   3902 C  CA    . ALA A 1 501 ? -9.249  24.742  2.998   1.00 51.12  ? 501 ALA A CA    1 
ATOM   3903 C  C     . ALA A 1 501 ? -9.590  25.755  1.914   1.00 61.85  ? 501 ALA A C     1 
ATOM   3904 O  O     . ALA A 1 501 ? -10.411 26.646  2.151   1.00 62.81  ? 501 ALA A O     1 
ATOM   3905 C  CB    . ALA A 1 501 ? -8.388  25.400  4.077   1.00 53.79  ? 501 ALA A CB    1 
ATOM   3906 N  N     . HIS A 1 502 ? -8.978  25.641  0.736   1.00 61.63  ? 502 HIS A N     1 
ATOM   3907 C  CA    . HIS A 1 502 ? -9.270  26.532  -0.377  1.00 67.16  ? 502 HIS A CA    1 
ATOM   3908 C  C     . HIS A 1 502 ? -10.398 26.022  -1.262  1.00 69.60  ? 502 HIS A C     1 
ATOM   3909 O  O     . HIS A 1 502 ? -10.802 26.728  -2.193  1.00 78.35  ? 502 HIS A O     1 
ATOM   3910 C  CB    . HIS A 1 502 ? -8.011  26.748  -1.224  1.00 65.98  ? 502 HIS A CB    1 
ATOM   3911 C  CG    . HIS A 1 502 ? -6.804  27.133  -0.425  1.00 68.30  ? 502 HIS A CG    1 
ATOM   3912 N  ND1   . HIS A 1 502 ? -5.518  26.877  -0.849  1.00 74.53  ? 502 HIS A ND1   1 
ATOM   3913 C  CD2   . HIS A 1 502 ? -6.690  27.753  0.773   1.00 66.98  ? 502 HIS A CD2   1 
ATOM   3914 C  CE1   . HIS A 1 502 ? -4.662  27.324  0.054   1.00 73.43  ? 502 HIS A CE1   1 
ATOM   3915 N  NE2   . HIS A 1 502 ? -5.348  27.860  1.048   1.00 74.63  ? 502 HIS A NE2   1 
ATOM   3916 N  N     . ARG A 1 503 ? -10.910 24.824  -0.998  1.00 65.94  ? 503 ARG A N     1 
ATOM   3917 C  CA    . ARG A 1 503 ? -11.997 24.288  -1.801  1.00 72.18  ? 503 ARG A CA    1 
ATOM   3918 C  C     . ARG A 1 503 ? -13.277 25.083  -1.549  1.00 83.80  ? 503 ARG A C     1 
ATOM   3919 O  O     . ARG A 1 503 ? -13.597 25.400  -0.398  1.00 79.01  ? 503 ARG A O     1 
ATOM   3920 C  CB    . ARG A 1 503 ? -12.227 22.812  -1.475  1.00 72.95  ? 503 ARG A CB    1 
ATOM   3921 C  CG    . ARG A 1 503 ? -11.065 21.899  -1.839  1.00 65.45  ? 503 ARG A CG    1 
ATOM   3922 C  CD    . ARG A 1 503 ? -10.979 21.687  -3.341  1.00 81.55  ? 503 ARG A CD    1 
ATOM   3923 N  NE    . ARG A 1 503 ? -12.121 20.938  -3.852  1.00 84.80  ? 503 ARG A NE    1 
ATOM   3924 C  CZ    . ARG A 1 503 ? -12.115 19.634  -4.091  1.00 77.66  ? 503 ARG A CZ    1 
ATOM   3925 N  NH1   . ARG A 1 503 ? -11.035 18.898  -3.885  1.00 67.84  ? 503 ARG A NH1   1 
ATOM   3926 N  NH2   . ARG A 1 503 ? -13.220 19.054  -4.551  1.00 72.36  ? 503 ARG A NH2   1 
ATOM   3927 N  N     . PRO A 1 504 ? -14.021 25.430  -2.597  1.00 101.97 ? 504 PRO A N     1 
ATOM   3928 C  CA    . PRO A 1 504 ? -15.282 26.153  -2.393  1.00 103.21 ? 504 PRO A CA    1 
ATOM   3929 C  C     . PRO A 1 504 ? -16.326 25.268  -1.731  1.00 104.09 ? 504 PRO A C     1 
ATOM   3930 O  O     . PRO A 1 504 ? -16.501 24.101  -2.093  1.00 103.67 ? 504 PRO A O     1 
ATOM   3931 C  CB    . PRO A 1 504 ? -15.704 26.547  -3.816  1.00 104.06 ? 504 PRO A CB    1 
ATOM   3932 C  CG    . PRO A 1 504 ? -14.460 26.412  -4.647  1.00 104.58 ? 504 PRO A CG    1 
ATOM   3933 C  CD    . PRO A 1 504 ? -13.686 25.294  -4.024  1.00 102.51 ? 504 PRO A CD    1 
ATOM   3934 N  N     . ALA A 1 505 ? -17.021 25.837  -0.749  1.00 89.07  ? 505 ALA A N     1 
ATOM   3935 C  CA    . ALA A 1 505 ? -18.095 25.157  -0.028  1.00 76.92  ? 505 ALA A CA    1 
ATOM   3936 C  C     . ALA A 1 505 ? -17.614 23.896  0.682   1.00 71.03  ? 505 ALA A C     1 
ATOM   3937 O  O     . ALA A 1 505 ? -18.423 23.033  1.038   1.00 66.84  ? 505 ALA A O     1 
ATOM   3938 C  CB    . ALA A 1 505 ? -19.260 24.821  -0.965  1.00 79.26  ? 505 ALA A CB    1 
ATOM   3939 N  N     . ALA A 1 506 ? -16.308 23.768  0.901   1.00 70.44  ? 506 ALA A N     1 
ATOM   3940 C  CA    . ALA A 1 506 ? -15.777 22.591  1.574   1.00 65.59  ? 506 ALA A CA    1 
ATOM   3941 C  C     . ALA A 1 506 ? -16.166 22.605  3.046   1.00 58.95  ? 506 ALA A C     1 
ATOM   3942 O  O     . ALA A 1 506 ? -15.933 23.590  3.753   1.00 57.63  ? 506 ALA A O     1 
ATOM   3943 C  CB    . ALA A 1 506 ? -14.258 22.534  1.427   1.00 60.75  ? 506 ALA A CB    1 
ATOM   3944 N  N     . LYS A 1 507 ? -16.770 21.511  3.504   1.00 55.87  ? 507 LYS A N     1 
ATOM   3945 C  CA    . LYS A 1 507 ? -17.151 21.361  4.907   1.00 51.10  ? 507 LYS A CA    1 
ATOM   3946 C  C     . LYS A 1 507 ? -16.018 20.627  5.609   1.00 48.05  ? 507 LYS A C     1 
ATOM   3947 O  O     . LYS A 1 507 ? -15.998 19.399  5.693   1.00 53.70  ? 507 LYS A O     1 
ATOM   3948 C  CB    . LYS A 1 507 ? -18.476 20.622  5.035   1.00 48.90  ? 507 LYS A CB    1 
ATOM   3949 C  CG    . LYS A 1 507 ? -19.614 21.267  4.261   1.00 54.53  ? 507 LYS A CG    1 
ATOM   3950 C  CD    . LYS A 1 507 ? -20.836 20.361  4.223   1.00 58.50  ? 507 LYS A CD    1 
ATOM   3951 C  CE    . LYS A 1 507 ? -21.962 20.978  3.406   1.00 59.41  ? 507 LYS A CE    1 
ATOM   3952 N  NZ    . LYS A 1 507 ? -23.110 20.040  3.259   1.00 69.14  ? 507 LYS A NZ    1 
ATOM   3953 N  N     . LEU A 1 508 ? -15.061 21.392  6.112   1.00 48.98  ? 508 LEU A N     1 
ATOM   3954 C  CA    . LEU A 1 508 ? -13.881 20.801  6.730   1.00 45.70  ? 508 LEU A CA    1 
ATOM   3955 C  C     . LEU A 1 508 ? -14.261 20.145  8.053   1.00 47.26  ? 508 LEU A C     1 
ATOM   3956 O  O     . LEU A 1 508 ? -14.908 20.783  8.894   1.00 43.63  ? 508 LEU A O     1 
ATOM   3957 C  CB    . LEU A 1 508 ? -12.813 21.868  6.953   1.00 43.84  ? 508 LEU A CB    1 
ATOM   3958 C  CG    . LEU A 1 508 ? -12.353 22.612  5.698   1.00 45.73  ? 508 LEU A CG    1 
ATOM   3959 C  CD1   . LEU A 1 508 ? -11.411 23.752  6.051   1.00 47.72  ? 508 LEU A CD1   1 
ATOM   3960 C  CD2   . LEU A 1 508 ? -11.696 21.650  4.717   1.00 44.12  ? 508 LEU A CD2   1 
ATOM   3961 N  N     . PRO A 1 509 ? -13.882 18.891  8.280   1.00 46.30  ? 509 PRO A N     1 
ATOM   3962 C  CA    . PRO A 1 509 ? -14.173 18.258  9.568   1.00 40.45  ? 509 PRO A CA    1 
ATOM   3963 C  C     . PRO A 1 509 ? -13.324 18.855  10.679  1.00 46.30  ? 509 PRO A C     1 
ATOM   3964 O  O     . PRO A 1 509 ? -12.244 19.409  10.453  1.00 43.49  ? 509 PRO A O     1 
ATOM   3965 C  CB    . PRO A 1 509 ? -13.811 16.791  9.328   1.00 42.10  ? 509 PRO A CB    1 
ATOM   3966 C  CG    . PRO A 1 509 ? -12.742 16.854  8.288   1.00 40.91  ? 509 PRO A CG    1 
ATOM   3967 C  CD    . PRO A 1 509 ? -13.125 18.000  7.385   1.00 42.75  ? 509 PRO A CD    1 
ATOM   3968 N  N     . LYS A 1 510 ? -13.839 18.745  11.899  1.00 41.86  ? 510 LYS A N     1 
ATOM   3969 C  CA    . LYS A 1 510 ? -13.048 19.103  13.066  1.00 39.65  ? 510 LYS A CA    1 
ATOM   3970 C  C     . LYS A 1 510 ? -11.897 18.120  13.237  1.00 36.48  ? 510 LYS A C     1 
ATOM   3971 O  O     . LYS A 1 510 ? -11.985 16.951  12.851  1.00 38.10  ? 510 LYS A O     1 
ATOM   3972 C  CB    . LYS A 1 510 ? -13.916 19.128  14.325  1.00 40.43  ? 510 LYS A CB    1 
ATOM   3973 C  CG    . LYS A 1 510 ? -14.689 20.425  14.509  1.00 47.66  ? 510 LYS A CG    1 
ATOM   3974 C  CD    . LYS A 1 510 ? -15.350 20.491  15.878  1.00 46.14  ? 510 LYS A CD    1 
ATOM   3975 C  CE    . LYS A 1 510 ? -15.972 21.858  16.126  1.00 43.88  ? 510 LYS A CE    1 
ATOM   3976 N  NZ    . LYS A 1 510 ? -14.962 22.956  16.068  1.00 52.40  ? 510 LYS A NZ    1 
ATOM   3977 N  N     . ILE A 1 511 ? -10.805 18.605  13.817  1.00 38.38  ? 511 ILE A N     1 
ATOM   3978 C  CA    . ILE A 1 511 ? -9.597  17.812  14.002  1.00 34.74  ? 511 ILE A CA    1 
ATOM   3979 C  C     . ILE A 1 511 ? -9.294  17.729  15.490  1.00 36.86  ? 511 ILE A C     1 
ATOM   3980 O  O     . ILE A 1 511 ? -9.154  18.758  16.162  1.00 38.17  ? 511 ILE A O     1 
ATOM   3981 C  CB    . ILE A 1 511 ? -8.408  18.403  13.224  1.00 41.31  ? 511 ILE A CB    1 
ATOM   3982 C  CG1   . ILE A 1 511 ? -8.576  18.126  11.726  1.00 39.60  ? 511 ILE A CG1   1 
ATOM   3983 C  CG2   . ILE A 1 511 ? -7.088  17.841  13.745  1.00 32.90  ? 511 ILE A CG2   1 
ATOM   3984 C  CD1   . ILE A 1 511 ? -7.485  18.713  10.865  1.00 41.09  ? 511 ILE A CD1   1 
ATOM   3985 N  N     . PHE A 1 512 ? -9.206  16.505  16.002  1.00 33.67  ? 512 PHE A N     1 
ATOM   3986 C  CA    . PHE A 1 512 ? -8.902  16.246  17.399  1.00 34.82  ? 512 PHE A CA    1 
ATOM   3987 C  C     . PHE A 1 512 ? -7.592  15.477  17.501  1.00 35.30  ? 512 PHE A C     1 
ATOM   3988 O  O     . PHE A 1 512 ? -7.155  14.821  16.551  1.00 35.82  ? 512 PHE A O     1 
ATOM   3989 C  CB    . PHE A 1 512 ? -10.020 15.442  18.077  1.00 33.37  ? 512 PHE A CB    1 
ATOM   3990 C  CG    . PHE A 1 512 ? -11.386 16.048  17.918  1.00 35.11  ? 512 PHE A CG    1 
ATOM   3991 C  CD1   . PHE A 1 512 ? -12.178 15.724  16.832  1.00 31.18  ? 512 PHE A CD1   1 
ATOM   3992 C  CD2   . PHE A 1 512 ? -11.876 16.942  18.858  1.00 33.47  ? 512 PHE A CD2   1 
ATOM   3993 C  CE1   . PHE A 1 512 ? -13.439 16.279  16.682  1.00 34.27  ? 512 PHE A CE1   1 
ATOM   3994 C  CE2   . PHE A 1 512 ? -13.137 17.498  18.718  1.00 33.05  ? 512 PHE A CE2   1 
ATOM   3995 C  CZ    . PHE A 1 512 ? -13.917 17.169  17.626  1.00 31.04  ? 512 PHE A CZ    1 
ATOM   3996 N  N     . HIS A 1 513 ? -6.967  15.569  18.671  1.00 32.83  ? 513 HIS A N     1 
ATOM   3997 C  CA    . HIS A 1 513 ? -5.817  14.743  19.013  1.00 35.79  ? 513 HIS A CA    1 
ATOM   3998 C  C     . HIS A 1 513 ? -6.095  14.070  20.346  1.00 37.30  ? 513 HIS A C     1 
ATOM   3999 O  O     . HIS A 1 513 ? -6.426  14.742  21.328  1.00 34.47  ? 513 HIS A O     1 
ATOM   4000 C  CB    . HIS A 1 513 ? -4.528  15.561  19.099  1.00 32.15  ? 513 HIS A CB    1 
ATOM   4001 C  CG    . HIS A 1 513 ? -3.296  14.723  19.248  1.00 33.00  ? 513 HIS A CG    1 
ATOM   4002 N  ND1   . HIS A 1 513 ? -2.840  14.276  20.470  1.00 33.53  ? 513 HIS A ND1   1 
ATOM   4003 C  CD2   . HIS A 1 513 ? -2.427  14.244  18.325  1.00 35.04  ? 513 HIS A CD2   1 
ATOM   4004 C  CE1   . HIS A 1 513 ? -1.741  13.565  20.294  1.00 36.89  ? 513 HIS A CE1   1 
ATOM   4005 N  NE2   . HIS A 1 513 ? -1.470  13.529  19.001  1.00 39.76  ? 513 HIS A NE2   1 
ATOM   4006 N  N     . VAL A 1 514 ? -5.965  12.746  20.380  1.00 35.13  ? 514 VAL A N     1 
ATOM   4007 C  CA    . VAL A 1 514 ? -6.243  11.971  21.578  1.00 35.58  ? 514 VAL A CA    1 
ATOM   4008 C  C     . VAL A 1 514 ? -4.971  11.267  22.029  1.00 36.54  ? 514 VAL A C     1 
ATOM   4009 O  O     . VAL A 1 514 ? -4.029  11.066  21.259  1.00 40.74  ? 514 VAL A O     1 
ATOM   4010 C  CB    . VAL A 1 514 ? -7.370  10.946  21.359  1.00 37.90  ? 514 VAL A CB    1 
ATOM   4011 C  CG1   . VAL A 1 514 ? -8.623  11.647  20.862  1.00 33.14  ? 514 VAL A CG1   1 
ATOM   4012 C  CG2   . VAL A 1 514 ? -6.919  9.862   20.386  1.00 38.78  ? 514 VAL A CG2   1 
ATOM   4013 N  N     . ASN A 1 515 ? -4.958  10.887  23.305  1.00 34.17  ? 515 ASN A N     1 
ATOM   4014 C  CA    . ASN A 1 515 ? -3.852  10.129  23.891  1.00 37.29  ? 515 ASN A CA    1 
ATOM   4015 C  C     . ASN A 1 515 ? -4.456  9.168   24.908  1.00 43.11  ? 515 ASN A C     1 
ATOM   4016 O  O     . ASN A 1 515 ? -4.766  9.567   26.034  1.00 41.47  ? 515 ASN A O     1 
ATOM   4017 C  CB    . ASN A 1 515 ? -2.821  11.047  24.540  1.00 40.09  ? 515 ASN A CB    1 
ATOM   4018 C  CG    . ASN A 1 515 ? -1.664  10.280  25.145  1.00 41.72  ? 515 ASN A CG    1 
ATOM   4019 O  OD1   . ASN A 1 515 ? -1.415  9.127   24.790  1.00 41.09  ? 515 ASN A OD1   1 
ATOM   4020 N  ND2   . ASN A 1 515 ? -0.945  10.918  26.061  1.00 42.57  ? 515 ASN A ND2   1 
ATOM   4021 N  N     . TRP A 1 516 ? -4.637  7.909   24.506  1.00 43.21  ? 516 TRP A N     1 
ATOM   4022 C  CA    . TRP A 1 516 ? -5.126  6.897   25.432  1.00 43.58  ? 516 TRP A CA    1 
ATOM   4023 C  C     . TRP A 1 516 ? -4.057  6.419   26.407  1.00 45.72  ? 516 TRP A C     1 
ATOM   4024 O  O     . TRP A 1 516 ? -4.380  5.656   27.324  1.00 46.43  ? 516 TRP A O     1 
ATOM   4025 C  CB    . TRP A 1 516 ? -5.654  5.663   24.683  1.00 46.81  ? 516 TRP A CB    1 
ATOM   4026 C  CG    . TRP A 1 516 ? -6.635  5.902   23.570  1.00 42.86  ? 516 TRP A CG    1 
ATOM   4027 C  CD1   . TRP A 1 516 ? -6.755  5.169   22.423  1.00 44.18  ? 516 TRP A CD1   1 
ATOM   4028 C  CD2   . TRP A 1 516 ? -7.643  6.919   23.499  1.00 43.10  ? 516 TRP A CD2   1 
ATOM   4029 N  NE1   . TRP A 1 516 ? -7.767  5.667   21.642  1.00 40.35  ? 516 TRP A NE1   1 
ATOM   4030 C  CE2   . TRP A 1 516 ? -8.327  6.743   22.277  1.00 39.14  ? 516 TRP A CE2   1 
ATOM   4031 C  CE3   . TRP A 1 516 ? -8.028  7.966   24.343  1.00 42.31  ? 516 TRP A CE3   1 
ATOM   4032 C  CZ2   . TRP A 1 516 ? -9.373  7.573   21.881  1.00 37.00  ? 516 TRP A CZ2   1 
ATOM   4033 C  CZ3   . TRP A 1 516 ? -9.068  8.787   23.947  1.00 44.00  ? 516 TRP A CZ3   1 
ATOM   4034 C  CH2   . TRP A 1 516 ? -9.727  8.586   22.726  1.00 42.13  ? 516 TRP A CH2   1 
ATOM   4035 N  N     . PHE A 1 517 ? -2.801  6.839   26.236  1.00 44.30  ? 517 PHE A N     1 
ATOM   4036 C  CA    . PHE A 1 517 ? -1.668  6.125   26.816  1.00 49.16  ? 517 PHE A CA    1 
ATOM   4037 C  C     . PHE A 1 517 ? -0.832  6.976   27.769  1.00 46.20  ? 517 PHE A C     1 
ATOM   4038 O  O     . PHE A 1 517 ? 0.313   6.618   28.058  1.00 46.99  ? 517 PHE A O     1 
ATOM   4039 C  CB    . PHE A 1 517 ? -0.783  5.566   25.701  1.00 48.47  ? 517 PHE A CB    1 
ATOM   4040 C  CG    . PHE A 1 517 ? -1.510  4.652   24.760  1.00 48.11  ? 517 PHE A CG    1 
ATOM   4041 C  CD1   . PHE A 1 517 ? -1.659  3.308   25.059  1.00 51.77  ? 517 PHE A CD1   1 
ATOM   4042 C  CD2   . PHE A 1 517 ? -2.048  5.135   23.579  1.00 47.11  ? 517 PHE A CD2   1 
ATOM   4043 C  CE1   . PHE A 1 517 ? -2.332  2.461   24.195  1.00 49.98  ? 517 PHE A CE1   1 
ATOM   4044 C  CE2   . PHE A 1 517 ? -2.723  4.295   22.712  1.00 45.94  ? 517 PHE A CE2   1 
ATOM   4045 C  CZ    . PHE A 1 517 ? -2.865  2.956   23.020  1.00 46.50  ? 517 PHE A CZ    1 
ATOM   4046 N  N     . ARG A 1 518 ? -1.366  8.088   28.267  1.00 46.49  ? 518 ARG A N     1 
ATOM   4047 C  CA    . ARG A 1 518 ? -0.633  8.853   29.268  1.00 51.82  ? 518 ARG A CA    1 
ATOM   4048 C  C     . ARG A 1 518 ? -0.493  8.033   30.545  1.00 55.30  ? 518 ARG A C     1 
ATOM   4049 O  O     . ARG A 1 518 ? -1.418  7.325   30.950  1.00 53.55  ? 518 ARG A O     1 
ATOM   4050 C  CB    . ARG A 1 518 ? -1.339  10.178  29.558  1.00 51.72  ? 518 ARG A CB    1 
ATOM   4051 C  CG    . ARG A 1 518 ? -0.485  11.171  30.331  1.00 50.65  ? 518 ARG A CG    1 
ATOM   4052 C  CD    . ARG A 1 518 ? -1.163  12.526  30.435  1.00 50.94  ? 518 ARG A CD    1 
ATOM   4053 N  NE    . ARG A 1 518 ? -0.262  13.552  30.947  1.00 51.77  ? 518 ARG A NE    1 
ATOM   4054 C  CZ    . ARG A 1 518 ? -0.501  14.855  30.882  1.00 58.49  ? 518 ARG A CZ    1 
ATOM   4055 N  NH1   . ARG A 1 518 ? -1.604  15.328  30.326  1.00 52.11  ? 518 ARG A NH1   1 
ATOM   4056 N  NH2   . ARG A 1 518 ? 0.393   15.705  31.380  1.00 57.35  ? 518 ARG A NH2   1 
ATOM   4057 N  N     . LYS A 1 519 ? 0.677   8.118   31.172  1.00 58.28  ? 519 LYS A N     1 
ATOM   4058 C  CA    . LYS A 1 519 ? 0.977   7.356   32.374  1.00 61.58  ? 519 LYS A CA    1 
ATOM   4059 C  C     . LYS A 1 519 ? 1.359   8.294   33.510  1.00 66.39  ? 519 LYS A C     1 
ATOM   4060 O  O     . LYS A 1 519 ? 1.849   9.404   33.283  1.00 68.41  ? 519 LYS A O     1 
ATOM   4061 C  CB    . LYS A 1 519 ? 2.115   6.354   32.133  1.00 65.55  ? 519 LYS A CB    1 
ATOM   4062 C  CG    . LYS A 1 519 ? 1.782   5.254   31.137  1.00 59.42  ? 519 LYS A CG    1 
ATOM   4063 C  CD    . LYS A 1 519 ? 2.959   4.306   30.963  1.00 61.64  ? 519 LYS A CD    1 
ATOM   4064 C  CE    . LYS A 1 519 ? 2.608   3.142   30.050  1.00 62.91  ? 519 LYS A CE    1 
ATOM   4065 N  NZ    . LYS A 1 519 ? 3.729   2.168   29.950  1.00 67.53  ? 519 LYS A NZ    1 
ATOM   4066 N  N     . ASP A 1 520 ? 1.132   7.838   34.739  1.00 70.99  ? 520 ASP A N     1 
ATOM   4067 C  CA    . ASP A 1 520 ? 1.495   8.612   35.914  1.00 76.92  ? 520 ASP A CA    1 
ATOM   4068 C  C     . ASP A 1 520 ? 2.946   8.325   36.299  1.00 83.77  ? 520 ASP A C     1 
ATOM   4069 O  O     . ASP A 1 520 ? 3.672   7.612   35.603  1.00 82.25  ? 520 ASP A O     1 
ATOM   4070 C  CB    . ASP A 1 520 ? 0.542   8.312   37.070  1.00 81.64  ? 520 ASP A CB    1 
ATOM   4071 C  CG    . ASP A 1 520 ? 0.551   6.849   37.471  1.00 82.55  ? 520 ASP A CG    1 
ATOM   4072 O  OD1   . ASP A 1 520 ? 1.392   6.086   36.951  1.00 83.61  ? 520 ASP A OD1   1 
ATOM   4073 O  OD2   . ASP A 1 520 ? -0.290  6.459   38.308  1.00 81.82  ? 520 ASP A OD2   1 
ATOM   4074 N  N     . LYS A 1 521 ? 3.372   8.880   37.435  1.00 89.05  ? 521 LYS A N     1 
ATOM   4075 C  CA    . LYS A 1 521 ? 4.746   8.692   37.885  1.00 91.34  ? 521 LYS A CA    1 
ATOM   4076 C  C     . LYS A 1 521 ? 5.077   7.229   38.150  1.00 95.80  ? 521 LYS A C     1 
ATOM   4077 O  O     . LYS A 1 521 ? 6.259   6.866   38.159  1.00 101.54 ? 521 LYS A O     1 
ATOM   4078 C  CB    . LYS A 1 521 ? 5.003   9.520   39.146  1.00 98.40  ? 521 LYS A CB    1 
ATOM   4079 C  CG    . LYS A 1 521 ? 4.931   11.024  38.925  1.00 110.79 ? 521 LYS A CG    1 
ATOM   4080 C  CD    . LYS A 1 521 ? 5.333   11.784  40.179  1.00 124.21 ? 521 LYS A CD    1 
ATOM   4081 C  CE    . LYS A 1 521 ? 5.320   13.286  39.946  1.00 128.05 ? 521 LYS A CE    1 
ATOM   4082 N  NZ    . LYS A 1 521 ? 5.754   14.044  41.153  1.00 133.52 ? 521 LYS A NZ    1 
ATOM   4083 N  N     . ASN A 1 522 ? 4.070   6.386   38.363  1.00 91.30  ? 522 ASN A N     1 
ATOM   4084 C  CA    . ASN A 1 522 ? 4.277   4.972   38.637  1.00 91.88  ? 522 ASN A CA    1 
ATOM   4085 C  C     . ASN A 1 522 ? 4.215   4.110   37.383  1.00 87.19  ? 522 ASN A C     1 
ATOM   4086 O  O     . ASN A 1 522 ? 4.225   2.879   37.491  1.00 89.33  ? 522 ASN A O     1 
ATOM   4087 C  CB    . ASN A 1 522 ? 3.244   4.478   39.655  1.00 97.56  ? 522 ASN A CB    1 
ATOM   4088 C  CG    . ASN A 1 522 ? 3.234   5.304   40.925  1.00 99.58  ? 522 ASN A CG    1 
ATOM   4089 O  OD1   . ASN A 1 522 ? 4.221   5.961   41.259  1.00 101.98 ? 522 ASN A OD1   1 
ATOM   4090 N  ND2   . ASN A 1 522 ? 2.118   5.272   41.644  1.00 94.43  ? 522 ASN A ND2   1 
ATOM   4091 N  N     . GLY A 1 523 ? 4.152   4.722   36.202  1.00 88.85  ? 523 GLY A N     1 
ATOM   4092 C  CA    . GLY A 1 523 ? 4.040   3.955   34.978  1.00 86.44  ? 523 GLY A CA    1 
ATOM   4093 C  C     . GLY A 1 523 ? 2.694   3.305   34.764  1.00 82.81  ? 523 GLY A C     1 
ATOM   4094 O  O     . GLY A 1 523 ? 2.592   2.349   33.991  1.00 83.28  ? 523 GLY A O     1 
ATOM   4095 N  N     . LYS A 1 524 ? 1.653   3.796   35.429  1.00 78.11  ? 524 LYS A N     1 
ATOM   4096 C  CA    . LYS A 1 524 ? 0.313   3.242   35.316  1.00 73.02  ? 524 LYS A CA    1 
ATOM   4097 C  C     . LYS A 1 524 ? -0.542  4.129   34.420  1.00 67.49  ? 524 LYS A C     1 
ATOM   4098 O  O     . LYS A 1 524 ? -0.484  5.358   34.509  1.00 65.94  ? 524 LYS A O     1 
ATOM   4099 C  CB    . LYS A 1 524 ? -0.333  3.108   36.697  1.00 73.32  ? 524 LYS A CB    1 
ATOM   4100 C  CG    . LYS A 1 524 ? -1.654  2.359   36.708  1.00 76.17  ? 524 LYS A CG    1 
ATOM   4101 C  CD    . LYS A 1 524 ? -2.093  2.064   38.135  1.00 80.27  ? 524 LYS A CD    1 
ATOM   4102 C  CE    . LYS A 1 524 ? -3.382  1.257   38.173  1.00 75.95  ? 524 LYS A CE    1 
ATOM   4103 N  NZ    . LYS A 1 524 ? -3.779  0.923   39.568  1.00 80.36  ? 524 LYS A NZ    1 
ATOM   4104 N  N     . PHE A 1 525 ? -1.327  3.496   33.551  1.00 64.69  ? 525 PHE A N     1 
ATOM   4105 C  CA    . PHE A 1 525 ? -2.204  4.240   32.656  1.00 58.90  ? 525 PHE A CA    1 
ATOM   4106 C  C     . PHE A 1 525 ? -3.187  5.086   33.456  1.00 61.86  ? 525 PHE A C     1 
ATOM   4107 O  O     . PHE A 1 525 ? -3.861  4.588   34.362  1.00 62.51  ? 525 PHE A O     1 
ATOM   4108 C  CB    . PHE A 1 525 ? -2.960  3.279   31.737  1.00 60.85  ? 525 PHE A CB    1 
ATOM   4109 C  CG    . PHE A 1 525 ? -2.119  2.703   30.631  1.00 59.48  ? 525 PHE A CG    1 
ATOM   4110 C  CD1   . PHE A 1 525 ? -1.357  3.526   29.822  1.00 56.41  ? 525 PHE A CD1   1 
ATOM   4111 C  CD2   . PHE A 1 525 ? -2.092  1.336   30.403  1.00 61.49  ? 525 PHE A CD2   1 
ATOM   4112 C  CE1   . PHE A 1 525 ? -0.586  2.999   28.805  1.00 59.72  ? 525 PHE A CE1   1 
ATOM   4113 C  CE2   . PHE A 1 525 ? -1.321  0.805   29.389  1.00 57.08  ? 525 PHE A CE2   1 
ATOM   4114 C  CZ    . PHE A 1 525 ? -0.566  1.636   28.590  1.00 56.03  ? 525 PHE A CZ    1 
ATOM   4115 N  N     . LEU A 1 526 ? -3.263  6.374   33.117  1.00 59.16  ? 526 LEU A N     1 
ATOM   4116 C  CA    . LEU A 1 526 ? -4.213  7.269   33.765  1.00 62.16  ? 526 LEU A CA    1 
ATOM   4117 C  C     . LEU A 1 526 ? -5.633  7.094   33.244  1.00 61.32  ? 526 LEU A C     1 
ATOM   4118 O  O     . LEU A 1 526 ? -6.585  7.457   33.944  1.00 63.97  ? 526 LEU A O     1 
ATOM   4119 C  CB    . LEU A 1 526 ? -3.776  8.725   33.580  1.00 59.23  ? 526 LEU A CB    1 
ATOM   4120 C  CG    . LEU A 1 526 ? -2.500  9.167   34.300  1.00 62.87  ? 526 LEU A CG    1 
ATOM   4121 C  CD1   . LEU A 1 526 ? -2.119  10.589  33.913  1.00 65.53  ? 526 LEU A CD1   1 
ATOM   4122 C  CD2   . LEU A 1 526 ? -2.677  9.053   35.806  1.00 70.57  ? 526 LEU A CD2   1 
ATOM   4123 N  N     . TRP A 1 527 ? -5.795  6.545   32.043  1.00 58.43  ? 527 TRP A N     1 
ATOM   4124 C  CA    . TRP A 1 527 ? -7.085  6.403   31.395  1.00 54.85  ? 527 TRP A CA    1 
ATOM   4125 C  C     . TRP A 1 527 ? -7.366  4.930   31.128  1.00 55.35  ? 527 TRP A C     1 
ATOM   4126 O  O     . TRP A 1 527 ? -6.509  4.233   30.564  1.00 50.39  ? 527 TRP A O     1 
ATOM   4127 C  CB    . TRP A 1 527 ? -7.108  7.199   30.075  1.00 50.77  ? 527 TRP A CB    1 
ATOM   4128 C  CG    . TRP A 1 527 ? -8.431  7.222   29.365  1.00 46.94  ? 527 TRP A CG    1 
ATOM   4129 C  CD1   . TRP A 1 527 ? -8.722  6.654   28.158  1.00 45.79  ? 527 TRP A CD1   1 
ATOM   4130 C  CD2   . TRP A 1 527 ? -9.637  7.857   29.809  1.00 48.96  ? 527 TRP A CD2   1 
ATOM   4131 N  NE1   . TRP A 1 527 ? -10.034 6.892   27.826  1.00 44.67  ? 527 TRP A NE1   1 
ATOM   4132 C  CE2   . TRP A 1 527 ? -10.618 7.627   28.823  1.00 45.15  ? 527 TRP A CE2   1 
ATOM   4133 C  CE3   . TRP A 1 527 ? -9.984  8.598   30.944  1.00 48.97  ? 527 TRP A CE3   1 
ATOM   4134 C  CZ2   . TRP A 1 527 ? -11.922 8.108   28.939  1.00 46.30  ? 527 TRP A CZ2   1 
ATOM   4135 C  CZ3   . TRP A 1 527 ? -11.280 9.072   31.058  1.00 51.11  ? 527 TRP A CZ3   1 
ATOM   4136 C  CH2   . TRP A 1 527 ? -12.231 8.827   30.061  1.00 42.56  ? 527 TRP A CH2   1 
ATOM   4137 N  N     . PRO A 1 528 ? -8.535  4.414   31.521  1.00 55.49  ? 528 PRO A N     1 
ATOM   4138 C  CA    . PRO A 1 528 ? -8.813  2.987   31.288  1.00 53.77  ? 528 PRO A CA    1 
ATOM   4139 C  C     . PRO A 1 528 ? -8.923  2.629   29.817  1.00 52.45  ? 528 PRO A C     1 
ATOM   4140 O  O     . PRO A 1 528 ? -8.564  1.508   29.436  1.00 57.08  ? 528 PRO A O     1 
ATOM   4141 C  CB    . PRO A 1 528 ? -10.137 2.760   32.032  1.00 51.32  ? 528 PRO A CB    1 
ATOM   4142 C  CG    . PRO A 1 528 ? -10.768 4.116   32.109  1.00 55.05  ? 528 PRO A CG    1 
ATOM   4143 C  CD    . PRO A 1 528 ? -9.634  5.092   32.229  1.00 52.83  ? 528 PRO A CD    1 
ATOM   4144 N  N     . GLY A 1 529 ? -9.414  3.537   28.979  1.00 48.36  ? 529 GLY A N     1 
ATOM   4145 C  CA    . GLY A 1 529 ? -9.428  3.289   27.553  1.00 46.94  ? 529 GLY A CA    1 
ATOM   4146 C  C     . GLY A 1 529 ? -10.430 2.222   27.131  1.00 52.78  ? 529 GLY A C     1 
ATOM   4147 O  O     . GLY A 1 529 ? -11.371 1.875   27.852  1.00 52.52  ? 529 GLY A O     1 
ATOM   4148 N  N     . PHE A 1 530 ? -10.207 1.703   25.926  1.00 46.48  ? 530 PHE A N     1 
ATOM   4149 C  CA    . PHE A 1 530 ? -11.048 0.662   25.325  1.00 48.98  ? 530 PHE A CA    1 
ATOM   4150 C  C     . PHE A 1 530 ? -12.468 1.217   25.230  1.00 54.00  ? 530 PHE A C     1 
ATOM   4151 O  O     . PHE A 1 530 ? -12.647 2.336   24.723  1.00 47.70  ? 530 PHE A O     1 
ATOM   4152 C  CB    . PHE A 1 530 ? -10.900 -0.635  26.112  1.00 55.40  ? 530 PHE A CB    1 
ATOM   4153 C  CG    . PHE A 1 530 ? -9.508  -1.201  26.096  1.00 56.94  ? 530 PHE A CG    1 
ATOM   4154 C  CD1   . PHE A 1 530 ? -8.966  -1.708  24.926  1.00 52.89  ? 530 PHE A CD1   1 
ATOM   4155 C  CD2   . PHE A 1 530 ? -8.743  -1.230  27.250  1.00 57.91  ? 530 PHE A CD2   1 
ATOM   4156 C  CE1   . PHE A 1 530 ? -7.682  -2.226  24.905  1.00 50.95  ? 530 PHE A CE1   1 
ATOM   4157 C  CE2   . PHE A 1 530 ? -7.461  -1.750  27.237  1.00 59.10  ? 530 PHE A CE2   1 
ATOM   4158 C  CZ    . PHE A 1 530 ? -6.930  -2.248  26.062  1.00 55.10  ? 530 PHE A CZ    1 
ATOM   4159 N  N     . GLY A 1 531 ? -13.490 0.493   25.688  1.00 51.00  ? 531 GLY A N     1 
ATOM   4160 C  CA    . GLY A 1 531 ? -14.856 0.973   25.582  1.00 47.88  ? 531 GLY A CA    1 
ATOM   4161 C  C     . GLY A 1 531 ? -15.095 2.307   26.256  1.00 51.26  ? 531 GLY A C     1 
ATOM   4162 O  O     . GLY A 1 531 ? -16.022 3.026   25.872  1.00 52.45  ? 531 GLY A O     1 
ATOM   4163 N  N     . GLU A 1 532 ? -14.286 2.653   27.260  1.00 46.62  ? 532 GLU A N     1 
ATOM   4164 C  CA    . GLU A 1 532 ? -14.453 3.930   27.945  1.00 48.23  ? 532 GLU A CA    1 
ATOM   4165 C  C     . GLU A 1 532 ? -14.136 5.115   27.044  1.00 49.09  ? 532 GLU A C     1 
ATOM   4166 O  O     . GLU A 1 532 ? -14.551 6.239   27.351  1.00 47.36  ? 532 GLU A O     1 
ATOM   4167 C  CB    . GLU A 1 532 ? -13.573 3.977   29.196  1.00 49.65  ? 532 GLU A CB    1 
ATOM   4168 C  CG    . GLU A 1 532 ? -13.849 2.859   30.186  1.00 46.78  ? 532 GLU A CG    1 
ATOM   4169 C  CD    . GLU A 1 532 ? -15.268 2.888   30.722  1.00 48.65  ? 532 GLU A CD    1 
ATOM   4170 O  OE1   . GLU A 1 532 ? -16.042 3.787   30.326  1.00 53.26  ? 532 GLU A OE1   1 
ATOM   4171 O  OE2   . GLU A 1 532 ? -15.609 2.009   31.542  1.00 58.14  ? 532 GLU A OE2   1 
ATOM   4172 N  N     . ASN A 1 533 ? -13.416 4.891   25.943  1.00 44.55  ? 533 ASN A N     1 
ATOM   4173 C  CA    . ASN A 1 533 ? -13.146 5.963   24.992  1.00 44.27  ? 533 ASN A CA    1 
ATOM   4174 C  C     . ASN A 1 533 ? -14.421 6.539   24.389  1.00 45.59  ? 533 ASN A C     1 
ATOM   4175 O  O     . ASN A 1 533 ? -14.366 7.612   23.776  1.00 43.46  ? 533 ASN A O     1 
ATOM   4176 C  CB    . ASN A 1 533 ? -12.219 5.461   23.879  1.00 43.02  ? 533 ASN A CB    1 
ATOM   4177 C  CG    . ASN A 1 533 ? -10.839 5.078   24.392  1.00 46.22  ? 533 ASN A CG    1 
ATOM   4178 O  OD1   . ASN A 1 533 ? -10.366 5.611   25.395  1.00 43.78  ? 533 ASN A OD1   1 
ATOM   4179 N  ND2   . ASN A 1 533 ? -10.186 4.152   23.699  1.00 43.41  ? 533 ASN A ND2   1 
ATOM   4180 N  N     . SER A 1 534 ? -15.562 5.860   24.545  1.00 50.82  ? 534 SER A N     1 
ATOM   4181 C  CA    . SER A 1 534 ? -16.828 6.430   24.094  1.00 49.67  ? 534 SER A CA    1 
ATOM   4182 C  C     . SER A 1 534 ? -17.116 7.754   24.786  1.00 42.25  ? 534 SER A C     1 
ATOM   4183 O  O     . SER A 1 534 ? -17.819 8.605   24.231  1.00 43.91  ? 534 SER A O     1 
ATOM   4184 C  CB    . SER A 1 534 ? -17.969 5.443   24.342  1.00 45.75  ? 534 SER A CB    1 
ATOM   4185 O  OG    . SER A 1 534 ? -18.042 5.081   25.711  1.00 47.67  ? 534 SER A OG    1 
ATOM   4186 N  N     . ARG A 1 535 ? -16.591 7.939   26.000  1.00 42.68  ? 535 ARG A N     1 
ATOM   4187 C  CA    . ARG A 1 535 ? -16.754 9.209   26.697  1.00 46.80  ? 535 ARG A CA    1 
ATOM   4188 C  C     . ARG A 1 535 ? -16.007 10.332  25.991  1.00 46.33  ? 535 ARG A C     1 
ATOM   4189 O  O     . ARG A 1 535 ? -16.475 11.477  25.982  1.00 39.33  ? 535 ARG A O     1 
ATOM   4190 C  CB    . ARG A 1 535 ? -16.274 9.076   28.141  1.00 41.63  ? 535 ARG A CB    1 
ATOM   4191 C  CG    . ARG A 1 535 ? -16.882 7.904   28.889  1.00 46.18  ? 535 ARG A CG    1 
ATOM   4192 C  CD    . ARG A 1 535 ? -16.146 7.655   30.191  1.00 52.65  ? 535 ARG A CD    1 
ATOM   4193 N  NE    . ARG A 1 535 ? -16.632 6.464   30.877  1.00 53.63  ? 535 ARG A NE    1 
ATOM   4194 C  CZ    . ARG A 1 535 ? -17.523 6.473   31.860  1.00 55.89  ? 535 ARG A CZ    1 
ATOM   4195 N  NH1   . ARG A 1 535 ? -18.048 7.602   32.307  1.00 54.99  ? 535 ARG A NH1   1 
ATOM   4196 N  NH2   . ARG A 1 535 ? -17.893 5.321   32.410  1.00 50.05  ? 535 ARG A NH2   1 
ATOM   4197 N  N     . VAL A 1 536 ? -14.849 10.028  25.399  1.00 44.90  ? 536 VAL A N     1 
ATOM   4198 C  CA    . VAL A 1 536 ? -14.126 11.031  24.624  1.00 42.30  ? 536 VAL A CA    1 
ATOM   4199 C  C     . VAL A 1 536 ? -14.844 11.303  23.310  1.00 40.12  ? 536 VAL A C     1 
ATOM   4200 O  O     . VAL A 1 536 ? -14.975 12.457  22.885  1.00 41.41  ? 536 VAL A O     1 
ATOM   4201 C  CB    . VAL A 1 536 ? -12.673 10.581  24.391  1.00 43.93  ? 536 VAL A CB    1 
ATOM   4202 C  CG1   . VAL A 1 536 ? -11.954 11.561  23.471  1.00 47.96  ? 536 VAL A CG1   1 
ATOM   4203 C  CG2   . VAL A 1 536 ? -11.941 10.439  25.716  1.00 38.39  ? 536 VAL A CG2   1 
ATOM   4204 N  N     . LEU A 1 537 ? -15.317 10.247  22.643  1.00 41.31  ? 537 LEU A N     1 
ATOM   4205 C  CA    . LEU A 1 537 ? -16.076 10.433  21.411  1.00 41.45  ? 537 LEU A CA    1 
ATOM   4206 C  C     . LEU A 1 537 ? -17.322 11.276  21.657  1.00 39.59  ? 537 LEU A C     1 
ATOM   4207 O  O     . LEU A 1 537 ? -17.708 12.090  20.810  1.00 39.21  ? 537 LEU A O     1 
ATOM   4208 C  CB    . LEU A 1 537 ? -16.453 9.076   20.814  1.00 40.27  ? 537 LEU A CB    1 
ATOM   4209 C  CG    . LEU A 1 537 ? -15.314 8.115   20.454  1.00 43.00  ? 537 LEU A CG    1 
ATOM   4210 C  CD1   . LEU A 1 537 ? -15.849 6.822   19.855  1.00 46.75  ? 537 LEU A CD1   1 
ATOM   4211 C  CD2   . LEU A 1 537 ? -14.331 8.780   19.500  1.00 37.96  ? 537 LEU A CD2   1 
ATOM   4212 N  N     . GLU A 1 538 ? -17.973 11.091  22.810  1.00 38.41  ? 538 GLU A N     1 
ATOM   4213 C  CA    . GLU A 1 538 ? -19.143 11.904  23.124  1.00 39.30  ? 538 GLU A CA    1 
ATOM   4214 C  C     . GLU A 1 538 ? -18.797 13.386  23.119  1.00 40.46  ? 538 GLU A C     1 
ATOM   4215 O  O     . GLU A 1 538 ? -19.552 14.207  22.586  1.00 40.03  ? 538 GLU A O     1 
ATOM   4216 C  CB    . GLU A 1 538 ? -19.724 11.497  24.477  1.00 42.64  ? 538 GLU A CB    1 
ATOM   4217 C  CG    . GLU A 1 538 ? -20.900 12.353  24.915  1.00 46.69  ? 538 GLU A CG    1 
ATOM   4218 C  CD    . GLU A 1 538 ? -21.454 11.947  26.263  1.00 49.85  ? 538 GLU A CD    1 
ATOM   4219 O  OE1   . GLU A 1 538 ? -20.665 11.518  27.134  1.00 44.73  ? 538 GLU A OE1   1 
ATOM   4220 O  OE2   . GLU A 1 538 ? -22.683 12.057  26.452  1.00 53.00  ? 538 GLU A OE2   1 
ATOM   4221 N  N     . TRP A 1 539 ? -17.657 13.747  23.709  1.00 41.22  ? 539 TRP A N     1 
ATOM   4222 C  CA    . TRP A 1 539 ? -17.247 15.146  23.715  1.00 40.27  ? 539 TRP A CA    1 
ATOM   4223 C  C     . TRP A 1 539 ? -16.998 15.652  22.299  1.00 41.67  ? 539 TRP A C     1 
ATOM   4224 O  O     . TRP A 1 539 ? -17.440 16.749  21.938  1.00 41.18  ? 539 TRP A O     1 
ATOM   4225 C  CB    . TRP A 1 539 ? -16.005 15.325  24.586  1.00 43.46  ? 539 TRP A CB    1 
ATOM   4226 C  CG    . TRP A 1 539 ? -15.558 16.749  24.690  1.00 43.06  ? 539 TRP A CG    1 
ATOM   4227 C  CD1   . TRP A 1 539 ? -16.118 17.731  25.451  1.00 45.46  ? 539 TRP A CD1   1 
ATOM   4228 C  CD2   . TRP A 1 539 ? -14.454 17.351  24.007  1.00 42.50  ? 539 TRP A CD2   1 
ATOM   4229 N  NE1   . TRP A 1 539 ? -15.432 18.909  25.283  1.00 45.85  ? 539 TRP A NE1   1 
ATOM   4230 C  CE2   . TRP A 1 539 ? -14.405 18.701  24.400  1.00 43.50  ? 539 TRP A CE2   1 
ATOM   4231 C  CE3   . TRP A 1 539 ? -13.501 16.880  23.098  1.00 40.46  ? 539 TRP A CE3   1 
ATOM   4232 C  CZ2   . TRP A 1 539 ? -13.439 19.585  23.918  1.00 41.98  ? 539 TRP A CZ2   1 
ATOM   4233 C  CZ3   . TRP A 1 539 ? -12.543 17.758  22.622  1.00 38.62  ? 539 TRP A CZ3   1 
ATOM   4234 C  CH2   . TRP A 1 539 ? -12.520 19.095  23.030  1.00 39.12  ? 539 TRP A CH2   1 
ATOM   4235 N  N     . MET A 1 540 ? -16.294 14.867  21.481  1.00 38.59  ? 540 MET A N     1 
ATOM   4236 C  CA    . MET A 1 540 ? -16.097 15.257  20.088  1.00 40.46  ? 540 MET A CA    1 
ATOM   4237 C  C     . MET A 1 540 ? -17.434 15.422  19.379  1.00 37.62  ? 540 MET A C     1 
ATOM   4238 O  O     . MET A 1 540 ? -17.638 16.386  18.633  1.00 39.67  ? 540 MET A O     1 
ATOM   4239 C  CB    . MET A 1 540 ? -15.241 14.220  19.362  1.00 35.88  ? 540 MET A CB    1 
ATOM   4240 C  CG    . MET A 1 540 ? -13.895 13.923  20.002  1.00 36.42  ? 540 MET A CG    1 
ATOM   4241 S  SD    . MET A 1 540 ? -13.091 12.543  19.158  1.00 42.36  ? 540 MET A SD    1 
ATOM   4242 C  CE    . MET A 1 540 ? -11.450 12.611  19.873  1.00 40.54  ? 540 MET A CE    1 
ATOM   4243 N  N     . PHE A 1 541 ? -18.357 14.486  19.605  1.00 33.20  ? 541 PHE A N     1 
ATOM   4244 C  CA    . PHE A 1 541 ? -19.675 14.559  18.987  1.00 40.09  ? 541 PHE A CA    1 
ATOM   4245 C  C     . PHE A 1 541 ? -20.352 15.885  19.312  1.00 41.41  ? 541 PHE A C     1 
ATOM   4246 O  O     . PHE A 1 541 ? -20.860 16.573  18.420  1.00 44.31  ? 541 PHE A O     1 
ATOM   4247 C  CB    . PHE A 1 541 ? -20.529 13.379  19.459  1.00 37.33  ? 541 PHE A CB    1 
ATOM   4248 C  CG    . PHE A 1 541 ? -21.757 13.145  18.629  1.00 43.39  ? 541 PHE A CG    1 
ATOM   4249 C  CD1   . PHE A 1 541 ? -22.871 13.960  18.765  1.00 41.78  ? 541 PHE A CD1   1 
ATOM   4250 C  CD2   . PHE A 1 541 ? -21.806 12.100  17.723  1.00 43.26  ? 541 PHE A CD2   1 
ATOM   4251 C  CE1   . PHE A 1 541 ? -24.006 13.741  18.003  1.00 42.02  ? 541 PHE A CE1   1 
ATOM   4252 C  CE2   . PHE A 1 541 ? -22.937 11.873  16.959  1.00 43.79  ? 541 PHE A CE2   1 
ATOM   4253 C  CZ    . PHE A 1 541 ? -24.040 12.694  17.102  1.00 43.53  ? 541 PHE A CZ    1 
ATOM   4254 N  N     . GLY A 1 542 ? -20.365 16.262  20.592  1.00 38.04  ? 542 GLY A N     1 
ATOM   4255 C  CA    . GLY A 1 542 ? -20.960 17.534  20.968  1.00 42.66  ? 542 GLY A CA    1 
ATOM   4256 C  C     . GLY A 1 542 ? -20.222 18.719  20.379  1.00 44.21  ? 542 GLY A C     1 
ATOM   4257 O  O     . GLY A 1 542 ? -20.839 19.702  19.962  1.00 44.72  ? 542 GLY A O     1 
ATOM   4258 N  N     . ARG A 1 543 ? -18.889 18.644  20.333  1.00 41.52  ? 543 ARG A N     1 
ATOM   4259 C  CA    . ARG A 1 543 ? -18.112 19.741  19.769  1.00 41.87  ? 543 ARG A CA    1 
ATOM   4260 C  C     . ARG A 1 543 ? -18.399 19.925  18.284  1.00 45.08  ? 543 ARG A C     1 
ATOM   4261 O  O     . ARG A 1 543 ? -18.340 21.050  17.776  1.00 42.34  ? 543 ARG A O     1 
ATOM   4262 C  CB    . ARG A 1 543 ? -16.620 19.502  20.004  1.00 37.04  ? 543 ARG A CB    1 
ATOM   4263 C  CG    . ARG A 1 543 ? -16.167 19.821  21.416  1.00 40.87  ? 543 ARG A CG    1 
ATOM   4264 C  CD    . ARG A 1 543 ? -16.385 21.290  21.730  1.00 47.06  ? 543 ARG A CD    1 
ATOM   4265 N  NE    . ARG A 1 543 ? -15.647 22.151  20.813  1.00 42.99  ? 543 ARG A NE    1 
ATOM   4266 C  CZ    . ARG A 1 543 ? -15.928 23.428  20.592  1.00 51.32  ? 543 ARG A CZ    1 
ATOM   4267 N  NH1   . ARG A 1 543 ? -16.955 24.021  21.177  1.00 54.48  ? 543 ARG A NH1   1 
ATOM   4268 N  NH2   . ARG A 1 543 ? -15.164 24.125  19.756  1.00 51.96  ? 543 ARG A NH2   1 
ATOM   4269 N  N     . ILE A 1 544 ? -18.710 18.839  17.574  1.00 43.27  ? 544 ILE A N     1 
ATOM   4270 C  CA    . ILE A 1 544 ? -19.071 18.960  16.165  1.00 46.87  ? 544 ILE A CA    1 
ATOM   4271 C  C     . ILE A 1 544 ? -20.435 19.624  16.020  1.00 45.04  ? 544 ILE A C     1 
ATOM   4272 O  O     . ILE A 1 544 ? -20.664 20.406  15.088  1.00 43.57  ? 544 ILE A O     1 
ATOM   4273 C  CB    . ILE A 1 544 ? -19.030 17.580  15.484  1.00 44.18  ? 544 ILE A CB    1 
ATOM   4274 C  CG1   . ILE A 1 544 ? -17.586 17.075  15.401  1.00 38.59  ? 544 ILE A CG1   1 
ATOM   4275 C  CG2   . ILE A 1 544 ? -19.672 17.646  14.107  1.00 44.88  ? 544 ILE A CG2   1 
ATOM   4276 C  CD1   . ILE A 1 544 ? -17.464 15.642  14.935  1.00 41.09  ? 544 ILE A CD1   1 
ATOM   4277 N  N     . GLU A 1 545 ? -21.359 19.326  16.935  1.00 42.88  ? 545 GLU A N     1 
ATOM   4278 C  CA    . GLU A 1 545 ? -22.661 19.978  16.924  1.00 47.46  ? 545 GLU A CA    1 
ATOM   4279 C  C     . GLU A 1 545 ? -22.592 21.431  17.370  1.00 45.47  ? 545 GLU A C     1 
ATOM   4280 O  O     . GLU A 1 545 ? -23.590 22.148  17.242  1.00 48.22  ? 545 GLU A O     1 
ATOM   4281 C  CB    . GLU A 1 545 ? -23.647 19.212  17.813  1.00 48.22  ? 545 GLU A CB    1 
ATOM   4282 C  CG    . GLU A 1 545 ? -24.031 17.842  17.287  1.00 44.90  ? 545 GLU A CG    1 
ATOM   4283 C  CD    . GLU A 1 545 ? -25.243 17.260  17.997  1.00 52.79  ? 545 GLU A CD    1 
ATOM   4284 O  OE1   . GLU A 1 545 ? -25.507 17.651  19.155  1.00 59.74  ? 545 GLU A OE1   1 
ATOM   4285 O  OE2   . GLU A 1 545 ? -25.932 16.412  17.394  1.00 57.26  ? 545 GLU A OE2   1 
ATOM   4286 N  N     . GLY A 1 546 ? -21.454 21.878  17.887  1.00 45.58  ? 546 GLY A N     1 
ATOM   4287 C  CA    . GLY A 1 546 ? -21.296 23.247  18.317  1.00 51.90  ? 546 GLY A CA    1 
ATOM   4288 C  C     . GLY A 1 546 ? -21.518 23.505  19.791  1.00 48.86  ? 546 GLY A C     1 
ATOM   4289 O  O     . GLY A 1 546 ? -21.737 24.663  20.167  1.00 46.53  ? 546 GLY A O     1 
ATOM   4290 N  N     . GLU A 1 547 ? -21.462 22.478  20.634  1.00 48.26  ? 547 GLU A N     1 
ATOM   4291 C  CA    . GLU A 1 547 ? -21.697 22.671  22.059  1.00 53.18  ? 547 GLU A CA    1 
ATOM   4292 C  C     . GLU A 1 547 ? -20.554 23.454  22.696  1.00 52.78  ? 547 GLU A C     1 
ATOM   4293 O  O     . GLU A 1 547 ? -19.375 23.213  22.414  1.00 47.91  ? 547 GLU A O     1 
ATOM   4294 C  CB    . GLU A 1 547 ? -21.871 21.322  22.757  1.00 46.40  ? 547 GLU A CB    1 
ATOM   4295 C  CG    . GLU A 1 547 ? -23.161 20.599  22.385  1.00 57.17  ? 547 GLU A CG    1 
ATOM   4296 C  CD    . GLU A 1 547 ? -23.312 19.258  23.079  1.00 68.33  ? 547 GLU A CD    1 
ATOM   4297 O  OE1   . GLU A 1 547 ? -22.559 18.987  24.037  1.00 69.73  ? 547 GLU A OE1   1 
ATOM   4298 O  OE2   . GLU A 1 547 ? -24.191 18.473  22.667  1.00 71.46  ? 547 GLU A OE2   1 
ATOM   4299 N  N     . ASP A 1 548 ? -20.915 24.396  23.569  1.00 64.32  ? 548 ASP A N     1 
ATOM   4300 C  CA    . ASP A 1 548 ? -19.944 25.244  24.257  1.00 63.92  ? 548 ASP A CA    1 
ATOM   4301 C  C     . ASP A 1 548 ? -19.327 24.486  25.438  1.00 62.51  ? 548 ASP A C     1 
ATOM   4302 O  O     . ASP A 1 548 ? -19.482 24.839  26.608  1.00 62.69  ? 548 ASP A O     1 
ATOM   4303 C  CB    . ASP A 1 548 ? -20.614 26.537  24.706  1.00 68.64  ? 548 ASP A CB    1 
ATOM   4304 C  CG    . ASP A 1 548 ? -19.633 27.529  25.295  1.00 74.14  ? 548 ASP A CG    1 
ATOM   4305 O  OD1   . ASP A 1 548 ? -18.413 27.271  25.234  1.00 76.25  ? 548 ASP A OD1   1 
ATOM   4306 O  OD2   . ASP A 1 548 ? -20.086 28.567  25.825  1.00 75.93  ? 548 ASP A OD2   1 
ATOM   4307 N  N     . SER A 1 549 ? -18.605 23.418  25.099  1.00 52.19  ? 549 SER A N     1 
ATOM   4308 C  CA    . SER A 1 549 ? -18.014 22.522  26.085  1.00 52.49  ? 549 SER A CA    1 
ATOM   4309 C  C     . SER A 1 549 ? -16.491 22.550  26.075  1.00 46.87  ? 549 SER A C     1 
ATOM   4310 O  O     . SER A 1 549 ? -15.865 21.676  26.683  1.00 46.69  ? 549 SER A O     1 
ATOM   4311 C  CB    . SER A 1 549 ? -18.502 21.090  25.851  1.00 50.76  ? 549 SER A CB    1 
ATOM   4312 O  OG    . SER A 1 549 ? -18.153 20.639  24.553  1.00 48.52  ? 549 SER A OG    1 
ATOM   4313 N  N     . ALA A 1 550 ? -15.880 23.521  25.406  1.00 49.85  ? 550 ALA A N     1 
ATOM   4314 C  CA    . ALA A 1 550 ? -14.437 23.553  25.230  1.00 49.48  ? 550 ALA A CA    1 
ATOM   4315 C  C     . ALA A 1 550 ? -13.823 24.737  25.965  1.00 50.59  ? 550 ALA A C     1 
ATOM   4316 O  O     . ALA A 1 550 ? -14.423 25.811  26.057  1.00 44.45  ? 550 ALA A O     1 
ATOM   4317 C  CB    . ALA A 1 550 ? -14.066 23.619  23.744  1.00 49.40  ? 550 ALA A CB    1 
ATOM   4318 N  N     . LYS A 1 551 ? -12.620 24.521  26.490  1.00 52.73  ? 551 LYS A N     1 
ATOM   4319 C  CA    . LYS A 1 551 ? -11.808 25.568  27.092  1.00 49.47  ? 551 LYS A CA    1 
ATOM   4320 C  C     . LYS A 1 551 ? -10.554 25.770  26.253  1.00 46.26  ? 551 LYS A C     1 
ATOM   4321 O  O     . LYS A 1 551 ? -9.972  24.804  25.750  1.00 43.06  ? 551 LYS A O     1 
ATOM   4322 C  CB    . LYS A 1 551 ? -11.425 25.214  28.534  1.00 49.85  ? 551 LYS A CB    1 
ATOM   4323 C  CG    . LYS A 1 551 ? -10.429 26.175  29.169  1.00 56.61  ? 551 LYS A CG    1 
ATOM   4324 C  CD    . LYS A 1 551 ? -10.070 25.760  30.590  1.00 66.19  ? 551 LYS A CD    1 
ATOM   4325 C  CE    . LYS A 1 551 ? -9.545  24.333  30.645  1.00 64.38  ? 551 LYS A CE    1 
ATOM   4326 N  NZ    . LYS A 1 551 ? -9.098  23.944  32.014  1.00 75.06  ? 551 LYS A NZ    1 
ATOM   4327 N  N     . LEU A 1 552 ? -10.139 27.024  26.103  1.00 51.21  ? 552 LEU A N     1 
ATOM   4328 C  CA    . LEU A 1 552 ? -8.980  27.340  25.281  1.00 48.08  ? 552 LEU A CA    1 
ATOM   4329 C  C     . LEU A 1 552 ? -7.695  27.164  26.081  1.00 50.13  ? 552 LEU A C     1 
ATOM   4330 O  O     . LEU A 1 552 ? -7.574  27.667  27.202  1.00 50.19  ? 552 LEU A O     1 
ATOM   4331 C  CB    . LEU A 1 552 ? -9.081  28.768  24.745  1.00 48.28  ? 552 LEU A CB    1 
ATOM   4332 C  CG    . LEU A 1 552 ? -7.920  29.274  23.884  1.00 51.43  ? 552 LEU A CG    1 
ATOM   4333 C  CD1   . LEU A 1 552 ? -7.788  28.464  22.603  1.00 52.85  ? 552 LEU A CD1   1 
ATOM   4334 C  CD2   . LEU A 1 552 ? -8.090  30.755  23.577  1.00 47.01  ? 552 LEU A CD2   1 
ATOM   4335 N  N     . THR A 1 553 ? -6.745  26.442  25.506  1.00 44.36  ? 553 THR A N     1 
ATOM   4336 C  CA    . THR A 1 553 ? -5.410  26.263  26.058  1.00 44.04  ? 553 THR A CA    1 
ATOM   4337 C  C     . THR A 1 553 ? -4.393  26.572  24.981  1.00 46.38  ? 553 THR A C     1 
ATOM   4338 O  O     . THR A 1 553 ? -4.740  26.730  23.804  1.00 40.23  ? 553 THR A O     1 
ATOM   4339 C  CB    . THR A 1 553 ? -5.201  24.831  26.580  1.00 46.16  ? 553 THR A CB    1 
ATOM   4340 O  OG1   . THR A 1 553 ? -5.002  23.943  25.472  1.00 39.57  ? 553 THR A OG1   1 
ATOM   4341 C  CG2   . THR A 1 553 ? -6.408  24.372  27.383  1.00 42.24  ? 553 THR A CG2   1 
ATOM   4342 N  N     . PRO A 1 554 ? -3.114  26.672  25.345  1.00 43.04  ? 554 PRO A N     1 
ATOM   4343 C  CA    . PRO A 1 554 ? -2.083  26.976  24.339  1.00 45.13  ? 554 PRO A CA    1 
ATOM   4344 C  C     . PRO A 1 554 ? -1.958  25.931  23.238  1.00 47.54  ? 554 PRO A C     1 
ATOM   4345 O  O     . PRO A 1 554 ? -1.491  26.267  22.142  1.00 48.21  ? 554 PRO A O     1 
ATOM   4346 C  CB    . PRO A 1 554 ? -0.799  27.063  25.173  1.00 51.74  ? 554 PRO A CB    1 
ATOM   4347 C  CG    . PRO A 1 554 ? -1.272  27.414  26.551  1.00 49.14  ? 554 PRO A CG    1 
ATOM   4348 C  CD    . PRO A 1 554 ? -2.577  26.695  26.716  1.00 44.38  ? 554 PRO A CD    1 
ATOM   4349 N  N     . ILE A 1 555 ? -2.349  24.678  23.488  1.00 36.50  ? 555 ILE A N     1 
ATOM   4350 C  CA    . ILE A 1 555 ? -2.220  23.615  22.496  1.00 42.74  ? 555 ILE A CA    1 
ATOM   4351 C  C     . ILE A 1 555 ? -3.510  23.370  21.727  1.00 41.95  ? 555 ILE A C     1 
ATOM   4352 O  O     . ILE A 1 555 ? -3.519  22.551  20.797  1.00 38.37  ? 555 ILE A O     1 
ATOM   4353 C  CB    . ILE A 1 555 ? -1.745  22.301  23.149  1.00 42.60  ? 555 ILE A CB    1 
ATOM   4354 C  CG1   . ILE A 1 555 ? -2.806  21.775  24.118  1.00 45.77  ? 555 ILE A CG1   1 
ATOM   4355 C  CG2   . ILE A 1 555 ? -0.413  22.501  23.861  1.00 40.45  ? 555 ILE A CG2   1 
ATOM   4356 C  CD1   . ILE A 1 555 ? -2.610  20.323  24.512  1.00 43.37  ? 555 ILE A CD1   1 
ATOM   4357 N  N     . GLY A 1 556 ? -4.593  24.049  22.083  1.00 41.15  ? 556 GLY A N     1 
ATOM   4358 C  CA    . GLY A 1 556 ? -5.883  23.870  21.460  1.00 43.76  ? 556 GLY A CA    1 
ATOM   4359 C  C     . GLY A 1 556 ? -6.977  23.860  22.505  1.00 45.72  ? 556 GLY A C     1 
ATOM   4360 O  O     . GLY A 1 556 ? -6.755  24.170  23.674  1.00 45.19  ? 556 GLY A O     1 
ATOM   4361 N  N     . TYR A 1 557 ? -8.183  23.501  22.072  1.00 44.29  ? 557 TYR A N     1 
ATOM   4362 C  CA    . TYR A 1 557 ? -9.329  23.430  22.967  1.00 44.31  ? 557 TYR A CA    1 
ATOM   4363 C  C     . TYR A 1 557 ? -9.338  22.098  23.707  1.00 42.64  ? 557 TYR A C     1 
ATOM   4364 O  O     . TYR A 1 557 ? -9.145  21.036  23.105  1.00 44.55  ? 557 TYR A O     1 
ATOM   4365 C  CB    . TYR A 1 557 ? -10.640 23.593  22.196  1.00 43.94  ? 557 TYR A CB    1 
ATOM   4366 C  CG    . TYR A 1 557 ? -10.823 24.939  21.536  1.00 48.85  ? 557 TYR A CG    1 
ATOM   4367 C  CD1   . TYR A 1 557 ? -11.027 26.083  22.294  1.00 53.88  ? 557 TYR A CD1   1 
ATOM   4368 C  CD2   . TYR A 1 557 ? -10.815 25.063  20.154  1.00 48.42  ? 557 TYR A CD2   1 
ATOM   4369 C  CE1   . TYR A 1 557 ? -11.202 27.316  21.694  1.00 49.42  ? 557 TYR A CE1   1 
ATOM   4370 C  CE2   . TYR A 1 557 ? -10.992 26.290  19.544  1.00 48.62  ? 557 TYR A CE2   1 
ATOM   4371 C  CZ    . TYR A 1 557 ? -11.184 27.413  20.318  1.00 57.11  ? 557 TYR A CZ    1 
ATOM   4372 O  OH    . TYR A 1 557 ? -11.359 28.636  19.712  1.00 59.75  ? 557 TYR A OH    1 
ATOM   4373 N  N     . VAL A 1 558 ? -9.571  22.162  25.011  1.00 42.61  ? 558 VAL A N     1 
ATOM   4374 C  CA    . VAL A 1 558 ? -9.732  20.969  25.837  1.00 44.14  ? 558 VAL A CA    1 
ATOM   4375 C  C     . VAL A 1 558 ? -11.123 21.024  26.460  1.00 42.38  ? 558 VAL A C     1 
ATOM   4376 O  O     . VAL A 1 558 ? -11.760 22.089  26.499  1.00 44.53  ? 558 VAL A O     1 
ATOM   4377 C  CB    . VAL A 1 558 ? -8.633  20.863  26.917  1.00 45.13  ? 558 VAL A CB    1 
ATOM   4378 C  CG1   . VAL A 1 558 ? -7.266  20.690  26.272  1.00 40.41  ? 558 VAL A CG1   1 
ATOM   4379 C  CG2   . VAL A 1 558 ? -8.660  22.084  27.824  1.00 45.80  ? 558 VAL A CG2   1 
ATOM   4380 N  N     . PRO A 1 559 ? -11.623 19.893  26.953  1.00 47.89  ? 559 PRO A N     1 
ATOM   4381 C  CA    . PRO A 1 559 ? -12.959 19.891  27.563  1.00 43.02  ? 559 PRO A CA    1 
ATOM   4382 C  C     . PRO A 1 559 ? -13.000 20.761  28.809  1.00 45.15  ? 559 PRO A C     1 
ATOM   4383 O  O     . PRO A 1 559 ? -12.045 20.814  29.586  1.00 48.53  ? 559 PRO A O     1 
ATOM   4384 C  CB    . PRO A 1 559 ? -13.194 18.412  27.901  1.00 43.45  ? 559 PRO A CB    1 
ATOM   4385 C  CG    . PRO A 1 559 ? -12.214 17.653  27.055  1.00 43.13  ? 559 PRO A CG    1 
ATOM   4386 C  CD    . PRO A 1 559 ? -11.025 18.549  26.917  1.00 45.05  ? 559 PRO A CD    1 
ATOM   4387 N  N     . LYS A 1 560 ? -14.123 21.449  28.993  1.00 45.40  ? 560 LYS A N     1 
ATOM   4388 C  CA    . LYS A 1 560 ? -14.343 22.181  30.228  1.00 53.46  ? 560 LYS A CA    1 
ATOM   4389 C  C     . LYS A 1 560 ? -14.434 21.211  31.402  1.00 59.61  ? 560 LYS A C     1 
ATOM   4390 O  O     . LYS A 1 560 ? -14.622 20.002  31.235  1.00 52.28  ? 560 LYS A O     1 
ATOM   4391 C  CB    . LYS A 1 560 ? -15.625 23.011  30.148  1.00 53.51  ? 560 LYS A CB    1 
ATOM   4392 C  CG    . LYS A 1 560 ? -15.577 24.179  29.179  1.00 52.03  ? 560 LYS A CG    1 
ATOM   4393 C  CD    . LYS A 1 560 ? -16.882 24.961  29.245  1.00 49.68  ? 560 LYS A CD    1 
ATOM   4394 C  CE    . LYS A 1 560 ? -16.850 26.211  28.386  1.00 62.68  ? 560 LYS A CE    1 
ATOM   4395 N  NZ    . LYS A 1 560 ? -18.106 26.998  28.547  1.00 58.40  ? 560 LYS A NZ    1 
ATOM   4396 N  N     . GLU A 1 561 ? -14.293 21.755  32.606  1.00 58.85  ? 561 GLU A N     1 
ATOM   4397 C  CA    . GLU A 1 561 ? -14.543 20.960  33.797  1.00 62.87  ? 561 GLU A CA    1 
ATOM   4398 C  C     . GLU A 1 561 ? -15.956 20.392  33.746  1.00 65.93  ? 561 GLU A C     1 
ATOM   4399 O  O     . GLU A 1 561 ? -16.912 21.090  33.395  1.00 69.43  ? 561 GLU A O     1 
ATOM   4400 C  CB    . GLU A 1 561 ? -14.359 21.804  35.056  1.00 73.44  ? 561 GLU A CB    1 
ATOM   4401 C  CG    . GLU A 1 561 ? -14.777 21.092  36.328  1.00 79.72  ? 561 GLU A CG    1 
ATOM   4402 C  CD    . GLU A 1 561 ? -14.850 22.025  37.516  1.00 89.36  ? 561 GLU A CD    1 
ATOM   4403 O  OE1   . GLU A 1 561 ? -14.499 23.211  37.358  1.00 92.36  ? 561 GLU A OE1   1 
ATOM   4404 O  OE2   . GLU A 1 561 ? -15.262 21.573  38.605  1.00 94.98  ? 561 GLU A OE2   1 
ATOM   4405 N  N     . ASP A 1 562 ? -16.083 19.111  34.082  1.00 63.88  ? 562 ASP A N     1 
ATOM   4406 C  CA    . ASP A 1 562 ? -17.354 18.393  34.089  1.00 68.76  ? 562 ASP A CA    1 
ATOM   4407 C  C     . ASP A 1 562 ? -17.964 18.255  32.699  1.00 64.64  ? 562 ASP A C     1 
ATOM   4408 O  O     . ASP A 1 562 ? -19.102 17.788  32.572  1.00 66.15  ? 562 ASP A O     1 
ATOM   4409 C  CB    . ASP A 1 562 ? -18.365 19.056  35.034  1.00 79.41  ? 562 ASP A CB    1 
ATOM   4410 C  CG    . ASP A 1 562 ? -17.918 19.023  36.481  1.00 88.05  ? 562 ASP A CG    1 
ATOM   4411 O  OD1   . ASP A 1 562 ? -17.231 18.057  36.871  1.00 90.93  ? 562 ASP A OD1   1 
ATOM   4412 O  OD2   . ASP A 1 562 ? -18.257 19.962  37.230  1.00 90.67  ? 562 ASP A OD2   1 
ATOM   4413 N  N     . ALA A 1 563 ? -17.240 18.655  31.652  1.00 66.23  ? 563 ALA A N     1 
ATOM   4414 C  CA    . ALA A 1 563 ? -17.728 18.465  30.292  1.00 61.36  ? 563 ALA A CA    1 
ATOM   4415 C  C     . ALA A 1 563 ? -17.604 17.014  29.845  1.00 55.42  ? 563 ALA A C     1 
ATOM   4416 O  O     . ALA A 1 563 ? -18.392 16.556  29.010  1.00 57.47  ? 563 ALA A O     1 
ATOM   4417 C  CB    . ALA A 1 563 ? -16.975 19.383  29.327  1.00 55.66  ? 563 ALA A CB    1 
ATOM   4418 N  N     . LEU A 1 564 ? -16.627 16.285  30.382  1.00 54.16  ? 564 LEU A N     1 
ATOM   4419 C  CA    . LEU A 1 564 ? -16.488 14.864  30.098  1.00 56.55  ? 564 LEU A CA    1 
ATOM   4420 C  C     . LEU A 1 564 ? -17.385 14.060  31.027  1.00 54.50  ? 564 LEU A C     1 
ATOM   4421 O  O     . LEU A 1 564 ? -17.370 14.262  32.246  1.00 57.62  ? 564 LEU A O     1 
ATOM   4422 C  CB    . LEU A 1 564 ? -15.037 14.413  30.266  1.00 52.42  ? 564 LEU A CB    1 
ATOM   4423 C  CG    . LEU A 1 564 ? -14.081 14.509  29.077  1.00 54.73  ? 564 LEU A CG    1 
ATOM   4424 C  CD1   . LEU A 1 564 ? -12.796 13.748  29.372  1.00 54.21  ? 564 LEU A CD1   1 
ATOM   4425 C  CD2   . LEU A 1 564 ? -14.741 13.982  27.812  1.00 51.26  ? 564 LEU A CD2   1 
ATOM   4426 N  N     . ASN A 1 565 ? -18.167 13.153  30.453  1.00 53.41  ? 565 ASN A N     1 
ATOM   4427 C  CA    . ASN A 1 565 ? -18.946 12.213  31.252  1.00 54.31  ? 565 ASN A CA    1 
ATOM   4428 C  C     . ASN A 1 565 ? -17.978 11.253  31.926  1.00 55.34  ? 565 ASN A C     1 
ATOM   4429 O  O     . ASN A 1 565 ? -17.428 10.355  31.286  1.00 56.27  ? 565 ASN A O     1 
ATOM   4430 C  CB    . ASN A 1 565 ? -19.950 11.464  30.382  1.00 54.10  ? 565 ASN A CB    1 
ATOM   4431 C  CG    . ASN A 1 565 ? -20.870 10.570  31.192  1.00 63.67  ? 565 ASN A CG    1 
ATOM   4432 O  OD1   . ASN A 1 565 ? -20.574 10.225  32.338  1.00 62.05  ? 565 ASN A OD1   1 
ATOM   4433 N  ND2   . ASN A 1 565 ? -21.995 10.192  30.600  1.00 67.64  ? 565 ASN A ND2   1 
ATOM   4434 N  N     . LEU A 1 566 ? -17.758 11.446  33.225  1.00 59.44  ? 566 LEU A N     1 
ATOM   4435 C  CA    . LEU A 1 566 ? -16.851 10.609  33.997  1.00 61.40  ? 566 LEU A CA    1 
ATOM   4436 C  C     . LEU A 1 566 ? -17.578 9.755   35.027  1.00 69.53  ? 566 LEU A C     1 
ATOM   4437 O  O     . LEU A 1 566 ? -16.924 9.086   35.834  1.00 74.19  ? 566 LEU A O     1 
ATOM   4438 C  CB    . LEU A 1 566 ? -15.790 11.472  34.686  1.00 60.09  ? 566 LEU A CB    1 
ATOM   4439 C  CG    . LEU A 1 566 ? -14.834 12.260  33.785  1.00 61.64  ? 566 LEU A CG    1 
ATOM   4440 C  CD1   . LEU A 1 566 ? -13.915 13.139  34.623  1.00 62.42  ? 566 LEU A CD1   1 
ATOM   4441 C  CD2   . LEU A 1 566 ? -14.025 11.321  32.902  1.00 59.16  ? 566 LEU A CD2   1 
ATOM   4442 N  N     . LYS A 1 567 ? -18.909 9.761   35.024  1.00 70.21  ? 567 LYS A N     1 
ATOM   4443 C  CA    . LYS A 1 567 ? -19.648 8.941   35.974  1.00 70.58  ? 567 LYS A CA    1 
ATOM   4444 C  C     . LYS A 1 567 ? -19.325 7.467   35.758  1.00 71.51  ? 567 LYS A C     1 
ATOM   4445 O  O     . LYS A 1 567 ? -19.002 7.033   34.649  1.00 66.80  ? 567 LYS A O     1 
ATOM   4446 C  CB    . LYS A 1 567 ? -21.153 9.178   35.841  1.00 73.39  ? 567 LYS A CB    1 
ATOM   4447 C  CG    . LYS A 1 567 ? -21.967 8.490   36.925  1.00 86.41  ? 567 LYS A CG    1 
ATOM   4448 C  CD    . LYS A 1 567 ? -23.439 8.845   36.837  1.00 91.36  ? 567 LYS A CD    1 
ATOM   4449 C  CE    . LYS A 1 567 ? -24.226 8.175   37.951  1.00 94.98  ? 567 LYS A CE    1 
ATOM   4450 N  NZ    . LYS A 1 567 ? -23.784 8.632   39.298  1.00 87.99  ? 567 LYS A NZ    1 
ATOM   4451 N  N     . GLY A 1 568 ? -19.418 6.690   36.837  1.00 72.75  ? 568 GLY A N     1 
ATOM   4452 C  CA    . GLY A 1 568 ? -18.965 5.318   36.821  1.00 76.06  ? 568 GLY A CA    1 
ATOM   4453 C  C     . GLY A 1 568 ? -17.470 5.154   36.962  1.00 79.62  ? 568 GLY A C     1 
ATOM   4454 O  O     . GLY A 1 568 ? -17.010 4.046   37.276  1.00 85.06  ? 568 GLY A O     1 
ATOM   4455 N  N     . LEU A 1 569 ? -16.695 6.215   36.735  1.00 82.06  ? 569 LEU A N     1 
ATOM   4456 C  CA    . LEU A 1 569 ? -15.267 6.207   37.022  1.00 90.42  ? 569 LEU A CA    1 
ATOM   4457 C  C     . LEU A 1 569 ? -14.997 6.995   38.299  1.00 98.64  ? 569 LEU A C     1 
ATOM   4458 O  O     . LEU A 1 569 ? -14.872 6.411   39.381  1.00 94.73  ? 569 LEU A O     1 
ATOM   4459 C  CB    . LEU A 1 569 ? -14.477 6.803   35.856  1.00 85.39  ? 569 LEU A CB    1 
ATOM   4460 C  CG    . LEU A 1 569 ? -14.700 6.163   34.481  1.00 71.41  ? 569 LEU A CG    1 
ATOM   4461 C  CD1   . LEU A 1 569 ? -13.869 6.871   33.427  1.00 63.29  ? 569 LEU A CD1   1 
ATOM   4462 C  CD2   . LEU A 1 569 ? -14.368 4.682   34.522  1.00 71.84  ? 569 LEU A CD2   1 
ATOM   4463 N  N     . GLY A 1 570 ? -14.909 8.317   38.187  1.00 104.20 ? 570 GLY A N     1 
ATOM   4464 C  CA    . GLY A 1 570 ? -14.666 9.169   39.349  1.00 102.32 ? 570 GLY A CA    1 
ATOM   4465 C  C     . GLY A 1 570 ? -13.293 9.062   39.971  1.00 105.08 ? 570 GLY A C     1 
ATOM   4466 O  O     . GLY A 1 570 ? -12.697 10.079  40.341  1.00 102.73 ? 570 GLY A O     1 
ATOM   4467 N  N     . ASP A 1 571 ? -12.769 7.846   40.094  1.00 98.20  ? 571 ASP A N     1 
ATOM   4468 C  CA    . ASP A 1 571 ? -11.426 7.596   40.612  1.00 95.38  ? 571 ASP A CA    1 
ATOM   4469 C  C     . ASP A 1 571 ? -10.332 7.992   39.641  1.00 92.81  ? 571 ASP A C     1 
ATOM   4470 O  O     . ASP A 1 571 ? -9.157  7.699   39.910  1.00 89.17  ? 571 ASP A O     1 
ATOM   4471 C  CB    . ASP A 1 571 ? -11.281 6.118   40.969  1.00 94.81  ? 571 ASP A CB    1 
ATOM   4472 C  CG    . ASP A 1 571 ? -11.673 5.207   39.824  1.00 98.19  ? 571 ASP A CG    1 
ATOM   4473 O  OD1   . ASP A 1 571 ? -12.458 5.649   38.963  1.00 97.02  ? 571 ASP A OD1   1 
ATOM   4474 O  OD2   . ASP A 1 571 ? -11.197 4.052   39.784  1.00 107.28 ? 571 ASP A OD2   1 
ATOM   4475 N  N     . VAL A 1 572 ? -10.674 8.639   38.532  1.00 92.52  ? 572 VAL A N     1 
ATOM   4476 C  CA    . VAL A 1 572 ? -9.690  9.011   37.524  1.00 89.94  ? 572 VAL A CA    1 
ATOM   4477 C  C     . VAL A 1 572 ? -9.026  10.320  37.929  1.00 85.17  ? 572 VAL A C     1 
ATOM   4478 O  O     . VAL A 1 572 ? -9.705  11.303  38.248  1.00 82.84  ? 572 VAL A O     1 
ATOM   4479 C  CB    . VAL A 1 572 ? -10.350 9.130   36.142  1.00 80.48  ? 572 VAL A CB    1 
ATOM   4480 C  CG1   . VAL A 1 572 ? -9.346  9.637   35.120  1.00 78.49  ? 572 VAL A CG1   1 
ATOM   4481 C  CG2   . VAL A 1 572 ? -10.928 7.789   35.713  1.00 83.91  ? 572 VAL A CG2   1 
ATOM   4482 N  N     . ASN A 1 573 ? -7.693  10.335  37.915  1.00 79.43  ? 573 ASN A N     1 
ATOM   4483 C  CA    . ASN A 1 573 ? -6.946  11.555  38.189  1.00 78.07  ? 573 ASN A CA    1 
ATOM   4484 C  C     . ASN A 1 573 ? -7.087  12.525  37.023  1.00 77.40  ? 573 ASN A C     1 
ATOM   4485 O  O     . ASN A 1 573 ? -6.324  12.459  36.054  1.00 75.72  ? 573 ASN A O     1 
ATOM   4486 C  CB    . ASN A 1 573 ? -5.471  11.240  38.453  1.00 80.04  ? 573 ASN A CB    1 
ATOM   4487 C  CG    . ASN A 1 573 ? -4.657  12.479  38.775  1.00 83.91  ? 573 ASN A CG    1 
ATOM   4488 O  OD1   . ASN A 1 573 ? -5.202  13.570  38.941  1.00 84.63  ? 573 ASN A OD1   1 
ATOM   4489 N  ND2   . ASN A 1 573 ? -3.344  12.313  38.875  1.00 85.19  ? 573 ASN A ND2   1 
ATOM   4490 N  N     . VAL A 1 574 ? -8.063  13.431  37.112  1.00 76.64  ? 574 VAL A N     1 
ATOM   4491 C  CA    . VAL A 1 574 ? -8.325  14.354  36.012  1.00 76.48  ? 574 VAL A CA    1 
ATOM   4492 C  C     . VAL A 1 574 ? -7.223  15.400  35.896  1.00 73.01  ? 574 VAL A C     1 
ATOM   4493 O  O     . VAL A 1 574 ? -6.887  15.834  34.787  1.00 67.75  ? 574 VAL A O     1 
ATOM   4494 C  CB    . VAL A 1 574 ? -9.706  15.010  36.190  1.00 75.10  ? 574 VAL A CB    1 
ATOM   4495 C  CG1   . VAL A 1 574 ? -10.810 13.979  36.004  1.00 73.18  ? 574 VAL A CG1   1 
ATOM   4496 C  CG2   . VAL A 1 574 ? -9.807  15.667  37.560  1.00 78.06  ? 574 VAL A CG2   1 
ATOM   4497 N  N     . GLU A 1 575 ? -6.647  15.824  37.021  1.00 78.84  ? 575 GLU A N     1 
ATOM   4498 C  CA    . GLU A 1 575 ? -5.602  16.843  36.986  1.00 81.54  ? 575 GLU A CA    1 
ATOM   4499 C  C     . GLU A 1 575 ? -4.426  16.395  36.127  1.00 72.63  ? 575 GLU A C     1 
ATOM   4500 O  O     . GLU A 1 575 ? -4.054  17.066  35.157  1.00 70.10  ? 575 GLU A O     1 
ATOM   4501 C  CB    . GLU A 1 575 ? -5.143  17.169  38.409  1.00 87.24  ? 575 GLU A CB    1 
ATOM   4502 C  CG    . GLU A 1 575 ? -5.824  18.384  39.012  1.00 99.13  ? 575 GLU A CG    1 
ATOM   4503 C  CD    . GLU A 1 575 ? -5.411  19.674  38.330  1.00 106.92 ? 575 GLU A CD    1 
ATOM   4504 O  OE1   . GLU A 1 575 ? -4.246  19.768  37.891  1.00 105.60 ? 575 GLU A OE1   1 
ATOM   4505 O  OE2   . GLU A 1 575 ? -6.251  20.593  38.227  1.00 112.91 ? 575 GLU A OE2   1 
ATOM   4506 N  N     . GLU A 1 576 ? -3.825  15.256  36.472  1.00 75.11  ? 576 GLU A N     1 
ATOM   4507 C  CA    . GLU A 1 576 ? -2.672  14.769  35.727  1.00 71.83  ? 576 GLU A CA    1 
ATOM   4508 C  C     . GLU A 1 576 ? -3.040  14.312  34.321  1.00 69.74  ? 576 GLU A C     1 
ATOM   4509 O  O     . GLU A 1 576 ? -2.160  14.244  33.457  1.00 66.77  ? 576 GLU A O     1 
ATOM   4510 C  CB    . GLU A 1 576 ? -2.002  13.631  36.498  1.00 78.08  ? 576 GLU A CB    1 
ATOM   4511 C  CG    . GLU A 1 576 ? -0.695  13.142  35.902  1.00 83.41  ? 576 GLU A CG    1 
ATOM   4512 C  CD    . GLU A 1 576 ? -0.001  12.135  36.796  1.00 85.15  ? 576 GLU A CD    1 
ATOM   4513 O  OE1   . GLU A 1 576 ? -0.548  11.825  37.874  1.00 85.68  ? 576 GLU A OE1   1 
ATOM   4514 O  OE2   . GLU A 1 576 ? 1.090   11.656  36.425  1.00 85.46  ? 576 GLU A OE2   1 
ATOM   4515 N  N     . LEU A 1 577 ? -4.316  14.005  34.070  1.00 69.89  ? 577 LEU A N     1 
ATOM   4516 C  CA    . LEU A 1 577 ? -4.721  13.511  32.758  1.00 65.37  ? 577 LEU A CA    1 
ATOM   4517 C  C     . LEU A 1 577 ? -4.853  14.632  31.735  1.00 59.98  ? 577 LEU A C     1 
ATOM   4518 O  O     . LEU A 1 577 ? -4.644  14.399  30.539  1.00 54.90  ? 577 LEU A O     1 
ATOM   4519 C  CB    . LEU A 1 577 ? -6.041  12.744  32.868  1.00 62.75  ? 577 LEU A CB    1 
ATOM   4520 C  CG    . LEU A 1 577 ? -6.556  12.055  31.601  1.00 56.68  ? 577 LEU A CG    1 
ATOM   4521 C  CD1   . LEU A 1 577 ? -5.494  11.131  31.023  1.00 59.12  ? 577 LEU A CD1   1 
ATOM   4522 C  CD2   . LEU A 1 577 ? -7.837  11.285  31.890  1.00 56.39  ? 577 LEU A CD2   1 
ATOM   4523 N  N     . PHE A 1 578 ? -5.204  15.839  32.176  1.00 59.59  ? 578 PHE A N     1 
ATOM   4524 C  CA    . PHE A 1 578 ? -5.313  16.994  31.296  1.00 56.35  ? 578 PHE A CA    1 
ATOM   4525 C  C     . PHE A 1 578 ? -4.279  18.066  31.613  1.00 58.30  ? 578 PHE A C     1 
ATOM   4526 O  O     . PHE A 1 578 ? -4.350  19.167  31.058  1.00 59.86  ? 578 PHE A O     1 
ATOM   4527 C  CB    . PHE A 1 578 ? -6.723  17.585  31.368  1.00 58.33  ? 578 PHE A CB    1 
ATOM   4528 C  CG    . PHE A 1 578 ? -7.722  16.879  30.495  1.00 56.93  ? 578 PHE A CG    1 
ATOM   4529 C  CD1   . PHE A 1 578 ? -7.756  17.121  29.131  1.00 53.87  ? 578 PHE A CD1   1 
ATOM   4530 C  CD2   . PHE A 1 578 ? -8.630  15.981  31.034  1.00 49.05  ? 578 PHE A CD2   1 
ATOM   4531 C  CE1   . PHE A 1 578 ? -8.673  16.479  28.318  1.00 51.38  ? 578 PHE A CE1   1 
ATOM   4532 C  CE2   . PHE A 1 578 ? -9.552  15.334  30.226  1.00 52.62  ? 578 PHE A CE2   1 
ATOM   4533 C  CZ    . PHE A 1 578 ? -9.572  15.583  28.866  1.00 53.49  ? 578 PHE A CZ    1 
ATOM   4534 N  N     . GLY A 1 579 ? -3.325  17.773  32.491  1.00 61.63  ? 579 GLY A N     1 
ATOM   4535 C  CA    . GLY A 1 579 ? -2.302  18.754  32.803  1.00 57.51  ? 579 GLY A CA    1 
ATOM   4536 C  C     . GLY A 1 579 ? -1.522  19.151  31.562  1.00 60.42  ? 579 GLY A C     1 
ATOM   4537 O  O     . GLY A 1 579 ? -1.145  18.309  30.743  1.00 58.69  ? 579 GLY A O     1 
ATOM   4538 N  N     . ILE A 1 580 ? -1.292  20.453  31.420  1.00 56.12  ? 580 ILE A N     1 
ATOM   4539 C  CA    . ILE A 1 580 ? -0.493  21.009  30.335  1.00 55.13  ? 580 ILE A CA    1 
ATOM   4540 C  C     . ILE A 1 580 ? 0.685   21.733  30.970  1.00 56.30  ? 580 ILE A C     1 
ATOM   4541 O  O     . ILE A 1 580 ? 0.516   22.800  31.576  1.00 61.14  ? 580 ILE A O     1 
ATOM   4542 C  CB    . ILE A 1 580 ? -1.306  21.949  29.435  1.00 55.34  ? 580 ILE A CB    1 
ATOM   4543 C  CG1   . ILE A 1 580 ? -2.378  21.165  28.676  1.00 56.11  ? 580 ILE A CG1   1 
ATOM   4544 C  CG2   . ILE A 1 580 ? -0.390  22.674  28.461  1.00 55.33  ? 580 ILE A CG2   1 
ATOM   4545 C  CD1   . ILE A 1 580 ? -3.275  22.028  27.813  1.00 51.56  ? 580 ILE A CD1   1 
ATOM   4546 N  N     . SER A 1 581 ? 1.875   21.157  30.832  1.00 53.62  ? 581 SER A N     1 
ATOM   4547 C  CA    . SER A 1 581 ? 3.086   21.675  31.451  1.00 53.26  ? 581 SER A CA    1 
ATOM   4548 C  C     . SER A 1 581 ? 3.867   22.514  30.449  1.00 56.40  ? 581 SER A C     1 
ATOM   4549 O  O     . SER A 1 581 ? 4.206   22.036  29.361  1.00 56.30  ? 581 SER A O     1 
ATOM   4550 C  CB    . SER A 1 581 ? 3.957   20.530  31.968  1.00 55.24  ? 581 SER A CB    1 
ATOM   4551 O  OG    . SER A 1 581 ? 5.264   20.979  32.276  1.00 63.09  ? 581 SER A OG    1 
ATOM   4552 N  N     . LYS A 1 582 ? 4.155   23.763  30.820  1.00 59.08  ? 582 LYS A N     1 
ATOM   4553 C  CA    . LYS A 1 582 ? 4.992   24.607  29.975  1.00 59.31  ? 582 LYS A CA    1 
ATOM   4554 C  C     . LYS A 1 582 ? 6.342   23.949  29.715  1.00 58.07  ? 582 LYS A C     1 
ATOM   4555 O  O     . LYS A 1 582 ? 6.836   23.941  28.582  1.00 54.68  ? 582 LYS A O     1 
ATOM   4556 C  CB    . LYS A 1 582 ? 5.179   25.981  30.622  1.00 58.77  ? 582 LYS A CB    1 
ATOM   4557 C  CG    . LYS A 1 582 ? 6.069   26.918  29.819  1.00 60.45  ? 582 LYS A CG    1 
ATOM   4558 C  CD    . LYS A 1 582 ? 6.175   28.289  30.464  1.00 64.38  ? 582 LYS A CD    1 
ATOM   4559 C  CE    . LYS A 1 582 ? 6.973   29.245  29.593  1.00 62.15  ? 582 LYS A CE    1 
ATOM   4560 N  NZ    . LYS A 1 582 ? 7.012   30.621  30.160  1.00 62.27  ? 582 LYS A NZ    1 
ATOM   4561 N  N     . GLU A 1 583 ? 6.947   23.379  30.760  1.00 58.96  ? 583 GLU A N     1 
ATOM   4562 C  CA    . GLU A 1 583 ? 8.268   22.775  30.616  1.00 58.47  ? 583 GLU A CA    1 
ATOM   4563 C  C     . GLU A 1 583 ? 8.249   21.640  29.599  1.00 57.31  ? 583 GLU A C     1 
ATOM   4564 O  O     . GLU A 1 583 ? 9.171   21.511  28.785  1.00 58.05  ? 583 GLU A O     1 
ATOM   4565 C  CB    . GLU A 1 583 ? 8.770   22.273  31.971  1.00 62.19  ? 583 GLU A CB    1 
ATOM   4566 C  CG    . GLU A 1 583 ? 8.932   23.362  33.025  1.00 72.95  ? 583 GLU A CG    1 
ATOM   4567 C  CD    . GLU A 1 583 ? 7.603   23.907  33.510  1.00 77.03  ? 583 GLU A CD    1 
ATOM   4568 O  OE1   . GLU A 1 583 ? 6.582   23.206  33.357  1.00 72.29  ? 583 GLU A OE1   1 
ATOM   4569 O  OE2   . GLU A 1 583 ? 7.575   25.040  34.032  1.00 80.91  ? 583 GLU A OE2   1 
ATOM   4570 N  N     . PHE A 1 584 ? 7.209   20.801  29.629  1.00 54.99  ? 584 PHE A N     1 
ATOM   4571 C  CA    . PHE A 1 584 ? 7.127   19.707  28.666  1.00 50.46  ? 584 PHE A CA    1 
ATOM   4572 C  C     . PHE A 1 584 ? 6.929   20.230  27.251  1.00 52.17  ? 584 PHE A C     1 
ATOM   4573 O  O     . PHE A 1 584 ? 7.574   19.754  26.310  1.00 48.38  ? 584 PHE A O     1 
ATOM   4574 C  CB    . PHE A 1 584 ? 5.991   18.752  29.034  1.00 52.76  ? 584 PHE A CB    1 
ATOM   4575 C  CG    . PHE A 1 584 ? 5.703   17.715  27.975  1.00 51.12  ? 584 PHE A CG    1 
ATOM   4576 C  CD1   . PHE A 1 584 ? 6.411   16.524  27.942  1.00 48.92  ? 584 PHE A CD1   1 
ATOM   4577 C  CD2   . PHE A 1 584 ? 4.729   17.934  27.015  1.00 47.05  ? 584 PHE A CD2   1 
ATOM   4578 C  CE1   . PHE A 1 584 ? 6.149   15.574  26.973  1.00 51.49  ? 584 PHE A CE1   1 
ATOM   4579 C  CE2   . PHE A 1 584 ? 4.464   16.985  26.044  1.00 48.87  ? 584 PHE A CE2   1 
ATOM   4580 C  CZ    . PHE A 1 584 ? 5.174   15.804  26.024  1.00 47.74  ? 584 PHE A CZ    1 
ATOM   4581 N  N     . TRP A 1 585 ? 6.037   21.206  27.078  1.00 50.91  ? 585 TRP A N     1 
ATOM   4582 C  CA    . TRP A 1 585 ? 5.676   21.646  25.737  1.00 51.37  ? 585 TRP A CA    1 
ATOM   4583 C  C     . TRP A 1 585 ? 6.731   22.552  25.121  1.00 52.66  ? 585 TRP A C     1 
ATOM   4584 O  O     . TRP A 1 585 ? 6.869   22.583  23.893  1.00 48.66  ? 585 TRP A O     1 
ATOM   4585 C  CB    . TRP A 1 585 ? 4.311   22.330  25.768  1.00 46.52  ? 585 TRP A CB    1 
ATOM   4586 C  CG    . TRP A 1 585 ? 3.215   21.328  25.862  1.00 49.13  ? 585 TRP A CG    1 
ATOM   4587 C  CD1   . TRP A 1 585 ? 2.560   20.927  26.986  1.00 49.95  ? 585 TRP A CD1   1 
ATOM   4588 C  CD2   . TRP A 1 585 ? 2.673   20.560  24.784  1.00 50.31  ? 585 TRP A CD2   1 
ATOM   4589 N  NE1   . TRP A 1 585 ? 1.629   19.966  26.673  1.00 47.84  ? 585 TRP A NE1   1 
ATOM   4590 C  CE2   . TRP A 1 585 ? 1.679   19.725  25.325  1.00 43.68  ? 585 TRP A CE2   1 
ATOM   4591 C  CE3   . TRP A 1 585 ? 2.925   20.506  23.410  1.00 46.17  ? 585 TRP A CE3   1 
ATOM   4592 C  CZ2   . TRP A 1 585 ? 0.937   18.846  24.540  1.00 43.62  ? 585 TRP A CZ2   1 
ATOM   4593 C  CZ3   . TRP A 1 585 ? 2.190   19.635  22.635  1.00 51.98  ? 585 TRP A CZ3   1 
ATOM   4594 C  CH2   . TRP A 1 585 ? 1.207   18.818  23.199  1.00 45.97  ? 585 TRP A CH2   1 
ATOM   4595 N  N     . GLU A 1 586 ? 7.484   23.289  25.940  1.00 51.75  ? 586 GLU A N     1 
ATOM   4596 C  CA    . GLU A 1 586 ? 8.661   23.974  25.420  1.00 51.97  ? 586 GLU A CA    1 
ATOM   4597 C  C     . GLU A 1 586 ? 9.599   22.981  24.748  1.00 53.43  ? 586 GLU A C     1 
ATOM   4598 O  O     . GLU A 1 586 ? 10.119  23.233  23.656  1.00 51.18  ? 586 GLU A O     1 
ATOM   4599 C  CB    . GLU A 1 586 ? 9.382   24.719  26.544  1.00 55.79  ? 586 GLU A CB    1 
ATOM   4600 C  CG    . GLU A 1 586 ? 8.689   25.988  27.015  1.00 55.81  ? 586 GLU A CG    1 
ATOM   4601 C  CD    . GLU A 1 586 ? 9.493   26.720  28.072  1.00 66.90  ? 586 GLU A CD    1 
ATOM   4602 O  OE1   . GLU A 1 586 ? 10.218  26.050  28.835  1.00 64.20  ? 586 GLU A OE1   1 
ATOM   4603 O  OE2   . GLU A 1 586 ? 9.408   27.965  28.131  1.00 75.35  ? 586 GLU A OE2   1 
ATOM   4604 N  N     . LYS A 1 587 ? 9.819   21.833  25.393  1.00 51.63  ? 587 LYS A N     1 
ATOM   4605 C  CA    . LYS A 1 587 ? 10.653  20.792  24.803  1.00 48.51  ? 587 LYS A CA    1 
ATOM   4606 C  C     . LYS A 1 587 ? 9.994   20.192  23.568  1.00 48.66  ? 587 LYS A C     1 
ATOM   4607 O  O     . LYS A 1 587 ? 10.673  19.893  22.578  1.00 52.75  ? 587 LYS A O     1 
ATOM   4608 C  CB    . LYS A 1 587 ? 10.935  19.704  25.839  1.00 56.16  ? 587 LYS A CB    1 
ATOM   4609 C  CG    . LYS A 1 587 ? 11.862  18.608  25.348  1.00 63.52  ? 587 LYS A CG    1 
ATOM   4610 C  CD    . LYS A 1 587 ? 13.308  19.065  25.375  1.00 69.01  ? 587 LYS A CD    1 
ATOM   4611 C  CE    . LYS A 1 587 ? 14.174  18.196  24.484  1.00 68.49  ? 587 LYS A CE    1 
ATOM   4612 N  NZ    . LYS A 1 587 ? 13.798  18.358  23.056  1.00 64.91  ? 587 LYS A NZ    1 
ATOM   4613 N  N     . GLU A 1 588 ? 8.673   20.008  23.607  1.00 48.19  ? 588 GLU A N     1 
ATOM   4614 C  CA    . GLU A 1 588 ? 7.976   19.377  22.490  1.00 48.36  ? 588 GLU A CA    1 
ATOM   4615 C  C     . GLU A 1 588 ? 8.089   20.219  21.225  1.00 45.57  ? 588 GLU A C     1 
ATOM   4616 O  O     . GLU A 1 588 ? 8.386   19.699  20.144  1.00 45.96  ? 588 GLU A O     1 
ATOM   4617 C  CB    . GLU A 1 588 ? 6.510   19.142  22.853  1.00 46.12  ? 588 GLU A CB    1 
ATOM   4618 C  CG    . GLU A 1 588 ? 5.759   18.259  21.866  1.00 46.14  ? 588 GLU A CG    1 
ATOM   4619 C  CD    . GLU A 1 588 ? 6.175   16.802  21.952  1.00 47.10  ? 588 GLU A CD    1 
ATOM   4620 O  OE1   . GLU A 1 588 ? 6.791   16.420  22.967  1.00 43.21  ? 588 GLU A OE1   1 
ATOM   4621 O  OE2   . GLU A 1 588 ? 5.881   16.038  21.008  1.00 40.90  ? 588 GLU A OE2   1 
ATOM   4622 N  N     . VAL A 1 589 ? 7.845   21.526  21.338  1.00 47.85  ? 589 VAL A N     1 
ATOM   4623 C  CA    . VAL A 1 589 ? 7.926   22.396  20.168  1.00 50.13  ? 589 VAL A CA    1 
ATOM   4624 C  C     . VAL A 1 589 ? 9.323   22.345  19.560  1.00 47.18  ? 589 VAL A C     1 
ATOM   4625 O  O     . VAL A 1 589 ? 9.482   22.330  18.333  1.00 48.98  ? 589 VAL A O     1 
ATOM   4626 C  CB    . VAL A 1 589 ? 7.520   23.838  20.535  1.00 48.15  ? 589 VAL A CB    1 
ATOM   4627 C  CG1   . VAL A 1 589 ? 6.031   23.914  20.829  1.00 51.67  ? 589 VAL A CG1   1 
ATOM   4628 C  CG2   . VAL A 1 589 ? 8.321   24.329  21.728  1.00 53.71  ? 589 VAL A CG2   1 
ATOM   4629 N  N     . GLU A 1 590 ? 10.355  22.304  20.405  1.00 48.40  ? 590 GLU A N     1 
ATOM   4630 C  CA    . GLU A 1 590 ? 11.724  22.302  19.897  1.00 48.14  ? 590 GLU A CA    1 
ATOM   4631 C  C     . GLU A 1 590 ? 12.013  21.046  19.084  1.00 52.27  ? 590 GLU A C     1 
ATOM   4632 O  O     . GLU A 1 590 ? 12.645  21.118  18.023  1.00 53.70  ? 590 GLU A O     1 
ATOM   4633 C  CB    . GLU A 1 590 ? 12.714  22.434  21.054  1.00 55.42  ? 590 GLU A CB    1 
ATOM   4634 C  CG    . GLU A 1 590 ? 12.495  23.674  21.905  1.00 65.16  ? 590 GLU A CG    1 
ATOM   4635 C  CD    . GLU A 1 590 ? 12.438  24.945  21.079  1.00 77.53  ? 590 GLU A CD    1 
ATOM   4636 O  OE1   . GLU A 1 590 ? 13.047  24.978  19.990  1.00 75.78  ? 590 GLU A OE1   1 
ATOM   4637 O  OE2   . GLU A 1 590 ? 11.782  25.911  21.516  1.00 79.08  ? 590 GLU A OE2   1 
ATOM   4638 N  N     . GLU A 1 591 ? 11.567  19.884  19.565  1.00 49.22  ? 591 GLU A N     1 
ATOM   4639 C  CA    . GLU A 1 591 ? 11.767  18.652  18.808  1.00 50.80  ? 591 GLU A CA    1 
ATOM   4640 C  C     . GLU A 1 591 ? 10.987  18.677  17.500  1.00 46.26  ? 591 GLU A C     1 
ATOM   4641 O  O     . GLU A 1 591 ? 11.492  18.237  16.461  1.00 48.13  ? 591 GLU A O     1 
ATOM   4642 C  CB    . GLU A 1 591 ? 11.368  17.444  19.653  1.00 45.27  ? 591 GLU A CB    1 
ATOM   4643 C  CG    . GLU A 1 591 ? 12.329  17.156  20.785  1.00 51.71  ? 591 GLU A CG    1 
ATOM   4644 C  CD    . GLU A 1 591 ? 13.746  16.902  20.298  1.00 57.29  ? 591 GLU A CD    1 
ATOM   4645 O  OE1   . GLU A 1 591 ? 13.912  16.141  19.323  1.00 57.67  ? 591 GLU A OE1   1 
ATOM   4646 O  OE2   . GLU A 1 591 ? 14.693  17.460  20.887  1.00 54.48  ? 591 GLU A OE2   1 
ATOM   4647 N  N     . ILE A 1 592 ? 9.751   19.180  17.532  1.00 39.96  ? 592 ILE A N     1 
ATOM   4648 C  CA    . ILE A 1 592 ? 8.985   19.326  16.298  1.00 40.93  ? 592 ILE A CA    1 
ATOM   4649 C  C     . ILE A 1 592 ? 9.689   20.296  15.360  1.00 47.28  ? 592 ILE A C     1 
ATOM   4650 O  O     . ILE A 1 592 ? 9.792   20.054  14.150  1.00 45.71  ? 592 ILE A O     1 
ATOM   4651 C  CB    . ILE A 1 592 ? 7.551   19.788  16.610  1.00 45.95  ? 592 ILE A CB    1 
ATOM   4652 C  CG1   . ILE A 1 592 ? 6.879   18.825  17.593  1.00 48.77  ? 592 ILE A CG1   1 
ATOM   4653 C  CG2   . ILE A 1 592 ? 6.742   19.918  15.325  1.00 42.45  ? 592 ILE A CG2   1 
ATOM   4654 C  CD1   . ILE A 1 592 ? 5.548   19.329  18.117  1.00 46.00  ? 592 ILE A CD1   1 
ATOM   4655 N  N     . ASP A 1 593 ? 10.191  21.404  15.906  1.00 45.60  ? 593 ASP A N     1 
ATOM   4656 C  CA    . ASP A 1 593 ? 10.911  22.381  15.098  1.00 41.23  ? 593 ASP A CA    1 
ATOM   4657 C  C     . ASP A 1 593 ? 12.124  21.747  14.426  1.00 50.48  ? 593 ASP A C     1 
ATOM   4658 O  O     . ASP A 1 593 ? 12.278  21.812  13.201  1.00 49.57  ? 593 ASP A O     1 
ATOM   4659 C  CB    . ASP A 1 593 ? 11.331  23.560  15.974  1.00 47.93  ? 593 ASP A CB    1 
ATOM   4660 C  CG    . ASP A 1 593 ? 11.843  24.731  15.166  1.00 56.70  ? 593 ASP A CG    1 
ATOM   4661 O  OD1   . ASP A 1 593 ? 11.743  24.682  13.921  1.00 60.72  ? 593 ASP A OD1   1 
ATOM   4662 O  OD2   . ASP A 1 593 ? 12.343  25.700  15.775  1.00 57.40  ? 593 ASP A OD2   1 
ATOM   4663 N  N     . LYS A 1 594 ? 13.005  21.129  15.220  1.00 45.58  ? 594 LYS A N     1 
ATOM   4664 C  CA    . LYS A 1 594 ? 14.187  20.487  14.651  1.00 46.94  ? 594 LYS A CA    1 
ATOM   4665 C  C     . LYS A 1 594 ? 13.799  19.429  13.626  1.00 49.85  ? 594 LYS A C     1 
ATOM   4666 O  O     . LYS A 1 594 ? 14.441  19.305  12.576  1.00 44.44  ? 594 LYS A O     1 
ATOM   4667 C  CB    . LYS A 1 594 ? 15.035  19.866  15.761  1.00 46.48  ? 594 LYS A CB    1 
ATOM   4668 C  CG    . LYS A 1 594 ? 15.646  20.861  16.729  1.00 52.81  ? 594 LYS A CG    1 
ATOM   4669 C  CD    . LYS A 1 594 ? 16.549  20.162  17.736  1.00 54.80  ? 594 LYS A CD    1 
ATOM   4670 C  CE    . LYS A 1 594 ? 15.792  19.108  18.528  1.00 54.11  ? 594 LYS A CE    1 
ATOM   4671 N  NZ    . LYS A 1 594 ? 16.597  18.554  19.655  1.00 56.68  ? 594 LYS A NZ    1 
ATOM   4672 N  N     . TYR A 1 595 ? 12.750  18.657  13.914  1.00 45.38  ? 595 TYR A N     1 
ATOM   4673 C  CA    . TYR A 1 595 ? 12.321  17.600  13.003  1.00 42.77  ? 595 TYR A CA    1 
ATOM   4674 C  C     . TYR A 1 595 ? 11.813  18.178  11.689  1.00 47.19  ? 595 TYR A C     1 
ATOM   4675 O  O     . TYR A 1 595 ? 12.291  17.815  10.607  1.00 45.00  ? 595 TYR A O     1 
ATOM   4676 C  CB    . TYR A 1 595 ? 11.243  16.745  13.672  1.00 42.63  ? 595 TYR A CB    1 
ATOM   4677 C  CG    . TYR A 1 595 ? 10.662  15.667  12.784  1.00 41.61  ? 595 TYR A CG    1 
ATOM   4678 C  CD1   . TYR A 1 595 ? 11.300  14.445  12.639  1.00 43.21  ? 595 TYR A CD1   1 
ATOM   4679 C  CD2   . TYR A 1 595 ? 9.470   15.870  12.099  1.00 43.25  ? 595 TYR A CD2   1 
ATOM   4680 C  CE1   . TYR A 1 595 ? 10.771  13.453  11.833  1.00 41.34  ? 595 TYR A CE1   1 
ATOM   4681 C  CE2   . TYR A 1 595 ? 8.933   14.884  11.291  1.00 43.68  ? 595 TYR A CE2   1 
ATOM   4682 C  CZ    . TYR A 1 595 ? 9.589   13.677  11.163  1.00 41.08  ? 595 TYR A CZ    1 
ATOM   4683 O  OH    . TYR A 1 595 ? 9.064   12.689  10.360  1.00 54.82  ? 595 TYR A OH    1 
ATOM   4684 N  N     . LEU A 1 596 ? 10.830  19.078  11.763  1.00 44.87  ? 596 LEU A N     1 
ATOM   4685 C  CA    . LEU A 1 596 ? 10.274  19.665  10.548  1.00 47.56  ? 596 LEU A CA    1 
ATOM   4686 C  C     . LEU A 1 596 ? 11.344  20.396  9.746   1.00 48.99  ? 596 LEU A C     1 
ATOM   4687 O  O     . LEU A 1 596 ? 11.350  20.339  8.511   1.00 47.56  ? 596 LEU A O     1 
ATOM   4688 C  CB    . LEU A 1 596 ? 9.125   20.611  10.897  1.00 47.87  ? 596 LEU A CB    1 
ATOM   4689 C  CG    . LEU A 1 596 ? 7.856   19.965  11.459  1.00 48.80  ? 596 LEU A CG    1 
ATOM   4690 C  CD1   . LEU A 1 596 ? 6.838   21.026  11.837  1.00 50.87  ? 596 LEU A CD1   1 
ATOM   4691 C  CD2   . LEU A 1 596 ? 7.265   18.982  10.458  1.00 47.89  ? 596 LEU A CD2   1 
ATOM   4692 N  N     . GLU A 1 597 ? 12.263  21.087  10.425  1.00 46.38  ? 597 GLU A N     1 
ATOM   4693 C  CA    . GLU A 1 597 ? 13.297  21.827  9.707   1.00 48.45  ? 597 GLU A CA    1 
ATOM   4694 C  C     . GLU A 1 597 ? 14.218  20.885  8.942   1.00 51.52  ? 597 GLU A C     1 
ATOM   4695 O  O     . GLU A 1 597 ? 14.558  21.136  7.780   1.00 53.35  ? 597 GLU A O     1 
ATOM   4696 C  CB    . GLU A 1 597 ? 14.102  22.692  10.675  1.00 53.22  ? 597 GLU A CB    1 
ATOM   4697 C  CG    . GLU A 1 597 ? 15.182  23.518  9.990   1.00 58.88  ? 597 GLU A CG    1 
ATOM   4698 C  CD    . GLU A 1 597 ? 16.255  23.999  10.945  1.00 61.64  ? 597 GLU A CD    1 
ATOM   4699 O  OE1   . GLU A 1 597 ? 16.271  23.531  12.103  1.00 61.21  ? 597 GLU A OE1   1 
ATOM   4700 O  OE2   . GLU A 1 597 ? 17.080  24.844  10.539  1.00 71.55  ? 597 GLU A OE2   1 
ATOM   4701 N  N     . ASP A 1 598 ? 14.637  19.793  9.581   1.00 50.52  ? 598 ASP A N     1 
ATOM   4702 C  CA    . ASP A 1 598 ? 15.572  18.876  8.936   1.00 52.58  ? 598 ASP A CA    1 
ATOM   4703 C  C     . ASP A 1 598 ? 14.867  17.995  7.911   1.00 49.81  ? 598 ASP A C     1 
ATOM   4704 O  O     . ASP A 1 598 ? 15.335  17.850  6.777   1.00 53.00  ? 598 ASP A O     1 
ATOM   4705 C  CB    . ASP A 1 598 ? 16.272  18.017  9.988   1.00 52.86  ? 598 ASP A CB    1 
ATOM   4706 C  CG    . ASP A 1 598 ? 17.133  16.936  9.375   1.00 60.73  ? 598 ASP A CG    1 
ATOM   4707 O  OD1   . ASP A 1 598 ? 17.983  17.266  8.522   1.00 55.89  ? 598 ASP A OD1   1 
ATOM   4708 O  OD2   . ASP A 1 598 ? 16.969  15.756  9.753   1.00 61.09  ? 598 ASP A OD2   1 
ATOM   4709 N  N     . GLN A 1 599 ? 13.727  17.414  8.288   1.00 48.07  ? 599 GLN A N     1 
ATOM   4710 C  CA    . GLN A 1 599 ? 13.102  16.379  7.477   1.00 45.98  ? 599 GLN A CA    1 
ATOM   4711 C  C     . GLN A 1 599 ? 12.277  16.947  6.329   1.00 45.91  ? 599 GLN A C     1 
ATOM   4712 O  O     . GLN A 1 599 ? 12.173  16.306  5.275   1.00 48.77  ? 599 GLN A O     1 
ATOM   4713 C  CB    . GLN A 1 599 ? 12.233  15.490  8.366   1.00 43.87  ? 599 GLN A CB    1 
ATOM   4714 C  CG    . GLN A 1 599 ? 13.031  14.596  9.308   1.00 46.63  ? 599 GLN A CG    1 
ATOM   4715 C  CD    . GLN A 1 599 ? 13.936  13.635  8.558   1.00 45.95  ? 599 GLN A CD    1 
ATOM   4716 O  OE1   . GLN A 1 599 ? 13.492  12.932  7.652   1.00 44.60  ? 599 GLN A OE1   1 
ATOM   4717 N  NE2   . GLN A 1 599 ? 15.215  13.614  8.920   1.00 47.47  ? 599 GLN A NE2   1 
ATOM   4718 N  N     . VAL A 1 600 ? 11.667  18.120  6.505   1.00 43.46  ? 600 VAL A N     1 
ATOM   4719 C  CA    . VAL A 1 600 ? 10.883  18.735  5.446   1.00 44.21  ? 600 VAL A CA    1 
ATOM   4720 C  C     . VAL A 1 600 ? 11.619  19.899  4.788   1.00 44.49  ? 600 VAL A C     1 
ATOM   4721 O  O     . VAL A 1 600 ? 11.390  20.170  3.604   1.00 42.88  ? 600 VAL A O     1 
ATOM   4722 C  CB    . VAL A 1 600 ? 9.511   19.199  5.972   1.00 44.28  ? 600 VAL A CB    1 
ATOM   4723 C  CG1   . VAL A 1 600 ? 8.505   19.336  4.827   1.00 40.46  ? 600 VAL A CG1   1 
ATOM   4724 C  CG2   . VAL A 1 600 ? 8.967   18.245  7.037   1.00 49.01  ? 600 VAL A CG2   1 
ATOM   4725 N  N     . ASN A 1 601 ? 12.494  20.599  5.515   1.00 45.31  ? 601 ASN A N     1 
ATOM   4726 C  CA    . ASN A 1 601 ? 13.424  21.565  4.924   1.00 48.27  ? 601 ASN A CA    1 
ATOM   4727 C  C     . ASN A 1 601 ? 12.736  22.553  3.987   1.00 46.30  ? 601 ASN A C     1 
ATOM   4728 O  O     . ASN A 1 601 ? 11.865  23.318  4.410   1.00 45.79  ? 601 ASN A O     1 
ATOM   4729 C  CB    . ASN A 1 601 ? 14.541  20.817  4.194   1.00 54.90  ? 601 ASN A CB    1 
ATOM   4730 C  CG    . ASN A 1 601 ? 15.759  21.669  3.943   1.00 57.55  ? 601 ASN A CG    1 
ATOM   4731 O  OD1   . ASN A 1 601 ? 15.879  22.785  4.448   1.00 58.23  ? 601 ASN A OD1   1 
ATOM   4732 N  ND2   . ASN A 1 601 ? 16.676  21.143  3.148   1.00 52.46  ? 601 ASN A ND2   1 
ATOM   4733 N  N     . ALA A 1 602 ? 13.143  22.555  2.719   1.00 43.88  ? 602 ALA A N     1 
ATOM   4734 C  CA    . ALA A 1 602 ? 12.669  23.529  1.748   1.00 44.73  ? 602 ALA A CA    1 
ATOM   4735 C  C     . ALA A 1 602 ? 11.226  23.303  1.326   1.00 46.24  ? 602 ALA A C     1 
ATOM   4736 O  O     . ALA A 1 602 ? 10.625  24.219  0.754   1.00 46.51  ? 602 ALA A O     1 
ATOM   4737 C  CB    . ALA A 1 602 ? 13.571  23.516  0.510   1.00 52.41  ? 602 ALA A CB    1 
ATOM   4738 N  N     . ASP A 1 603 ? 10.656  22.126  1.584   1.00 41.28  ? 603 ASP A N     1 
ATOM   4739 C  CA    . ASP A 1 603 ? 9.300   21.806  1.158   1.00 47.01  ? 603 ASP A CA    1 
ATOM   4740 C  C     . ASP A 1 603 ? 8.271   21.967  2.273   1.00 42.89  ? 603 ASP A C     1 
ATOM   4741 O  O     . ASP A 1 603 ? 7.129   21.518  2.123   1.00 42.11  ? 603 ASP A O     1 
ATOM   4742 C  CB    . ASP A 1 603 ? 9.249   20.383  0.601   1.00 42.49  ? 603 ASP A CB    1 
ATOM   4743 C  CG    . ASP A 1 603 ? 9.903   20.268  -0.761  1.00 54.15  ? 603 ASP A CG    1 
ATOM   4744 O  OD1   . ASP A 1 603 ? 9.551   21.060  -1.658  1.00 51.41  ? 603 ASP A OD1   1 
ATOM   4745 O  OD2   . ASP A 1 603 ? 10.775  19.390  -0.933  1.00 51.49  ? 603 ASP A OD2   1 
ATOM   4746 N  N     . LEU A 1 604 ? 8.648   22.591  3.381   1.00 41.18  ? 604 LEU A N     1 
ATOM   4747 C  CA    . LEU A 1 604 ? 7.709   22.835  4.469   1.00 43.37  ? 604 LEU A CA    1 
ATOM   4748 C  C     . LEU A 1 604 ? 6.825   24.030  4.125   1.00 44.21  ? 604 LEU A C     1 
ATOM   4749 O  O     . LEU A 1 604 ? 7.348   25.131  3.915   1.00 43.27  ? 604 LEU A O     1 
ATOM   4750 C  CB    . LEU A 1 604 ? 8.460   23.092  5.770   1.00 43.80  ? 604 LEU A CB    1 
ATOM   4751 C  CG    . LEU A 1 604 ? 7.648   23.322  7.047   1.00 46.55  ? 604 LEU A CG    1 
ATOM   4752 C  CD1   . LEU A 1 604 ? 6.863   22.076  7.414   1.00 42.35  ? 604 LEU A CD1   1 
ATOM   4753 C  CD2   . LEU A 1 604 ? 8.568   23.732  8.185   1.00 45.17  ? 604 LEU A CD2   1 
ATOM   4754 N  N     . PRO A 1 605 ? 5.505   23.864  4.044   1.00 42.06  ? 605 PRO A N     1 
ATOM   4755 C  CA    . PRO A 1 605 ? 4.641   25.014  3.752   1.00 44.32  ? 605 PRO A CA    1 
ATOM   4756 C  C     . PRO A 1 605 ? 4.753   26.067  4.843   1.00 42.55  ? 605 PRO A C     1 
ATOM   4757 O  O     . PRO A 1 605 ? 4.919   25.755  6.024   1.00 41.37  ? 605 PRO A O     1 
ATOM   4758 C  CB    . PRO A 1 605 ? 3.235   24.404  3.703   1.00 38.96  ? 605 PRO A CB    1 
ATOM   4759 C  CG    . PRO A 1 605 ? 3.458   22.941  3.466   1.00 39.86  ? 605 PRO A CG    1 
ATOM   4760 C  CD    . PRO A 1 605 ? 4.741   22.612  4.164   1.00 37.26  ? 605 PRO A CD    1 
ATOM   4761 N  N     . TYR A 1 606 ? 4.660   27.333  4.432   1.00 42.83  ? 606 TYR A N     1 
ATOM   4762 C  CA    . TYR A 1 606 ? 4.787   28.424  5.394   1.00 49.71  ? 606 TYR A CA    1 
ATOM   4763 C  C     . TYR A 1 606 ? 3.713   28.352  6.473   1.00 46.89  ? 606 TYR A C     1 
ATOM   4764 O  O     . TYR A 1 606 ? 3.990   28.611  7.650   1.00 47.69  ? 606 TYR A O     1 
ATOM   4765 C  CB    . TYR A 1 606 ? 4.722   29.772  4.682   1.00 44.67  ? 606 TYR A CB    1 
ATOM   4766 C  CG    . TYR A 1 606 ? 4.541   30.926  5.642   1.00 52.88  ? 606 TYR A CG    1 
ATOM   4767 C  CD1   . TYR A 1 606 ? 5.589   31.356  6.442   1.00 55.82  ? 606 TYR A CD1   1 
ATOM   4768 C  CD2   . TYR A 1 606 ? 3.321   31.579  5.755   1.00 51.60  ? 606 TYR A CD2   1 
ATOM   4769 C  CE1   . TYR A 1 606 ? 5.432   32.411  7.327   1.00 64.76  ? 606 TYR A CE1   1 
ATOM   4770 C  CE2   . TYR A 1 606 ? 3.154   32.638  6.635   1.00 55.66  ? 606 TYR A CE2   1 
ATOM   4771 C  CZ    . TYR A 1 606 ? 4.213   33.048  7.420   1.00 61.01  ? 606 TYR A CZ    1 
ATOM   4772 O  OH    . TYR A 1 606 ? 4.054   34.100  8.301   1.00 70.83  ? 606 TYR A OH    1 
ATOM   4773 N  N     . GLU A 1 607 ? 2.476   28.017  6.092   1.00 42.75  ? 607 GLU A N     1 
ATOM   4774 C  CA    . GLU A 1 607 ? 1.402   27.941  7.077   1.00 46.86  ? 607 GLU A CA    1 
ATOM   4775 C  C     . GLU A 1 607 ? 1.716   26.933  8.176   1.00 45.43  ? 607 GLU A C     1 
ATOM   4776 O  O     . GLU A 1 607 ? 1.325   27.135  9.331   1.00 46.97  ? 607 GLU A O     1 
ATOM   4777 C  CB    . GLU A 1 607 ? 0.080   27.594  6.390   1.00 46.90  ? 607 GLU A CB    1 
ATOM   4778 C  CG    . GLU A 1 607 ? -0.511  28.738  5.568   1.00 52.79  ? 607 GLU A CG    1 
ATOM   4779 C  CD    . GLU A 1 607 ? -1.913  28.437  5.068   1.00 56.65  ? 607 GLU A CD    1 
ATOM   4780 O  OE1   . GLU A 1 607 ? -2.255  27.243  4.946   1.00 58.87  ? 607 GLU A OE1   1 
ATOM   4781 O  OE2   . GLU A 1 607 ? -2.675  29.394  4.802   1.00 72.74  ? 607 GLU A OE2   1 
ATOM   4782 N  N     . ILE A 1 608 ? 2.416   25.848  7.842   1.00 41.77  ? 608 ILE A N     1 
ATOM   4783 C  CA    . ILE A 1 608 ? 2.844   24.910  8.874   1.00 41.83  ? 608 ILE A CA    1 
ATOM   4784 C  C     . ILE A 1 608 ? 3.911   25.546  9.758   1.00 43.04  ? 608 ILE A C     1 
ATOM   4785 O  O     . ILE A 1 608 ? 3.881   25.410  10.987  1.00 42.29  ? 608 ILE A O     1 
ATOM   4786 C  CB    . ILE A 1 608 ? 3.336   23.596  8.238   1.00 39.96  ? 608 ILE A CB    1 
ATOM   4787 C  CG1   . ILE A 1 608 ? 2.179   22.867  7.551   1.00 39.71  ? 608 ILE A CG1   1 
ATOM   4788 C  CG2   . ILE A 1 608 ? 3.984   22.706  9.288   1.00 40.36  ? 608 ILE A CG2   1 
ATOM   4789 C  CD1   . ILE A 1 608 ? 1.094   22.415  8.501   1.00 40.95  ? 608 ILE A CD1   1 
ATOM   4790 N  N     . GLU A 1 609 ? 4.868   26.253  9.150   1.00 38.09  ? 609 GLU A N     1 
ATOM   4791 C  CA    . GLU A 1 609 ? 5.872   26.967  9.933   1.00 44.04  ? 609 GLU A CA    1 
ATOM   4792 C  C     . GLU A 1 609 ? 5.233   28.045  10.800  1.00 45.94  ? 609 GLU A C     1 
ATOM   4793 O  O     . GLU A 1 609 ? 5.698   28.313  11.914  1.00 46.25  ? 609 GLU A O     1 
ATOM   4794 C  CB    . GLU A 1 609 ? 6.923   27.579  9.005   1.00 44.26  ? 609 GLU A CB    1 
ATOM   4795 C  CG    . GLU A 1 609 ? 7.945   28.469  9.702   1.00 53.46  ? 609 GLU A CG    1 
ATOM   4796 C  CD    . GLU A 1 609 ? 8.921   29.107  8.731   1.00 65.52  ? 609 GLU A CD    1 
ATOM   4797 O  OE1   . GLU A 1 609 ? 9.010   28.629  7.582   1.00 68.35  ? 609 GLU A OE1   1 
ATOM   4798 O  OE2   . GLU A 1 609 ? 9.595   30.085  9.114   1.00 77.84  ? 609 GLU A OE2   1 
ATOM   4799 N  N     . ARG A 1 610 ? 4.165   28.678  10.305  1.00 39.76  ? 610 ARG A N     1 
ATOM   4800 C  CA    . ARG A 1 610 ? 3.471   29.693  11.090  1.00 39.41  ? 610 ARG A CA    1 
ATOM   4801 C  C     . ARG A 1 610 ? 2.793   29.083  12.311  1.00 40.68  ? 610 ARG A C     1 
ATOM   4802 O  O     . ARG A 1 610 ? 2.844   29.656  13.404  1.00 43.03  ? 610 ARG A O     1 
ATOM   4803 C  CB    . ARG A 1 610 ? 2.452   30.420  10.216  1.00 47.78  ? 610 ARG A CB    1 
ATOM   4804 C  CG    . ARG A 1 610 ? 1.685   31.517  10.935  1.00 43.54  ? 610 ARG A CG    1 
ATOM   4805 C  CD    . ARG A 1 610 ? 0.848   32.316  9.959   1.00 48.18  ? 610 ARG A CD    1 
ATOM   4806 N  NE    . ARG A 1 610 ? -0.226  31.523  9.372   1.00 50.04  ? 610 ARG A NE    1 
ATOM   4807 C  CZ    . ARG A 1 610 ? -0.905  31.876  8.289   1.00 52.08  ? 610 ARG A CZ    1 
ATOM   4808 N  NH1   . ARG A 1 610 ? -0.630  32.992  7.636   1.00 58.94  ? 610 ARG A NH1   1 
ATOM   4809 N  NH2   . ARG A 1 610 ? -1.881  31.088  7.848   1.00 54.35  ? 610 ARG A NH2   1 
ATOM   4810 N  N     . GLU A 1 611 ? 2.148   27.925  12.146  1.00 40.38  ? 611 GLU A N     1 
ATOM   4811 C  CA    . GLU A 1 611 ? 1.541   27.255  13.292  1.00 40.88  ? 611 GLU A CA    1 
ATOM   4812 C  C     . GLU A 1 611 ? 2.590   26.892  14.336  1.00 43.92  ? 611 GLU A C     1 
ATOM   4813 O  O     . GLU A 1 611 ? 2.373   27.088  15.538  1.00 42.26  ? 611 GLU A O     1 
ATOM   4814 C  CB    . GLU A 1 611 ? 0.780   26.014  12.829  1.00 38.18  ? 611 GLU A CB    1 
ATOM   4815 C  CG    . GLU A 1 611 ? -0.425  26.328  11.957  1.00 41.07  ? 611 GLU A CG    1 
ATOM   4816 C  CD    . GLU A 1 611 ? -1.440  27.200  12.668  1.00 43.25  ? 611 GLU A CD    1 
ATOM   4817 O  OE1   . GLU A 1 611 ? -1.580  27.063  13.902  1.00 41.04  ? 611 GLU A OE1   1 
ATOM   4818 O  OE2   . GLU A 1 611 ? -2.091  28.026  11.996  1.00 51.57  ? 611 GLU A OE2   1 
ATOM   4819 N  N     . LEU A 1 612 ? 3.733   26.362  13.897  1.00 42.86  ? 612 LEU A N     1 
ATOM   4820 C  CA    . LEU A 1 612 ? 4.826   26.086  14.826  1.00 44.45  ? 612 LEU A CA    1 
ATOM   4821 C  C     . LEU A 1 612 ? 5.235   27.350  15.574  1.00 44.78  ? 612 LEU A C     1 
ATOM   4822 O  O     . LEU A 1 612 ? 5.410   27.334  16.799  1.00 42.20  ? 612 LEU A O     1 
ATOM   4823 C  CB    . LEU A 1 612 ? 6.018   25.494  14.070  1.00 43.87  ? 612 LEU A CB    1 
ATOM   4824 C  CG    . LEU A 1 612 ? 7.274   25.186  14.890  1.00 49.84  ? 612 LEU A CG    1 
ATOM   4825 C  CD1   . LEU A 1 612 ? 7.021   24.030  15.843  1.00 44.62  ? 612 LEU A CD1   1 
ATOM   4826 C  CD2   . LEU A 1 612 ? 8.451   24.889  13.973  1.00 55.13  ? 612 LEU A CD2   1 
ATOM   4827 N  N     . ARG A 1 613 ? 5.397   28.458  14.849  1.00 44.49  ? 613 ARG A N     1 
ATOM   4828 C  CA    . ARG A 1 613 ? 5.726   29.724  15.496  1.00 46.83  ? 613 ARG A CA    1 
ATOM   4829 C  C     . ARG A 1 613 ? 4.621   30.161  16.450  1.00 42.42  ? 613 ARG A C     1 
ATOM   4830 O  O     . ARG A 1 613 ? 4.899   30.676  17.540  1.00 44.54  ? 613 ARG A O     1 
ATOM   4831 C  CB    . ARG A 1 613 ? 5.978   30.803  14.445  1.00 50.89  ? 613 ARG A CB    1 
ATOM   4832 C  CG    . ARG A 1 613 ? 7.235   30.615  13.620  1.00 44.18  ? 613 ARG A CG    1 
ATOM   4833 C  CD    . ARG A 1 613 ? 7.459   31.831  12.737  1.00 56.27  ? 613 ARG A CD    1 
ATOM   4834 N  NE    . ARG A 1 613 ? 8.745   31.806  12.050  1.00 63.96  ? 613 ARG A NE    1 
ATOM   4835 C  CZ    . ARG A 1 613 ? 9.337   32.881  11.547  1.00 72.76  ? 613 ARG A CZ    1 
ATOM   4836 N  NH1   . ARG A 1 613 ? 8.797   34.083  11.660  1.00 60.44  ? 613 ARG A NH1   1 
ATOM   4837 N  NH2   . ARG A 1 613 ? 10.503  32.747  10.922  1.00 79.61  ? 613 ARG A NH2   1 
ATOM   4838 N  N     . ALA A 1 614 ? 3.361   29.970  16.054  1.00 42.33  ? 614 ALA A N     1 
ATOM   4839 C  CA    . ALA A 1 614 ? 2.247   30.385  16.901  1.00 45.89  ? 614 ALA A CA    1 
ATOM   4840 C  C     . ALA A 1 614 ? 2.157   29.530  18.160  1.00 44.89  ? 614 ALA A C     1 
ATOM   4841 O  O     . ALA A 1 614 ? 1.914   30.051  19.256  1.00 48.46  ? 614 ALA A O     1 
ATOM   4842 C  CB    . ALA A 1 614 ? 0.938   30.323  16.113  1.00 40.64  ? 614 ALA A CB    1 
ATOM   4843 N  N     . LEU A 1 615 ? 2.345   28.215  18.025  1.00 42.62  ? 615 LEU A N     1 
ATOM   4844 C  CA    . LEU A 1 615 ? 2.354   27.351  19.200  1.00 45.23  ? 615 LEU A CA    1 
ATOM   4845 C  C     . LEU A 1 615 ? 3.499   27.716  20.136  1.00 49.05  ? 615 LEU A C     1 
ATOM   4846 O  O     . LEU A 1 615 ? 3.315   27.801  21.357  1.00 45.18  ? 615 LEU A O     1 
ATOM   4847 C  CB    . LEU A 1 615 ? 2.454   25.887  18.773  1.00 47.85  ? 615 LEU A CB    1 
ATOM   4848 C  CG    . LEU A 1 615 ? 2.569   24.872  19.909  1.00 45.85  ? 615 LEU A CG    1 
ATOM   4849 C  CD1   . LEU A 1 615 ? 1.377   24.987  20.843  1.00 44.70  ? 615 LEU A CD1   1 
ATOM   4850 C  CD2   . LEU A 1 615 ? 2.696   23.456  19.367  1.00 37.00  ? 615 LEU A CD2   1 
ATOM   4851 N  N     . LYS A 1 616 ? 4.690   27.945  19.579  1.00 49.67  ? 616 LYS A N     1 
ATOM   4852 C  CA    . LYS A 1 616 ? 5.823   28.364  20.396  1.00 49.29  ? 616 LYS A CA    1 
ATOM   4853 C  C     . LYS A 1 616 ? 5.502   29.636  21.169  1.00 49.41  ? 616 LYS A C     1 
ATOM   4854 O  O     . LYS A 1 616 ? 5.890   29.779  22.334  1.00 50.78  ? 616 LYS A O     1 
ATOM   4855 C  CB    . LYS A 1 616 ? 7.052   28.566  19.512  1.00 49.83  ? 616 LYS A CB    1 
ATOM   4856 C  CG    . LYS A 1 616 ? 8.311   28.942  20.265  1.00 59.42  ? 616 LYS A CG    1 
ATOM   4857 C  CD    . LYS A 1 616 ? 9.522   28.801  19.361  1.00 63.81  ? 616 LYS A CD    1 
ATOM   4858 C  CE    . LYS A 1 616 ? 9.596   27.404  18.771  1.00 67.55  ? 616 LYS A CE    1 
ATOM   4859 N  NZ    . LYS A 1 616 ? 10.762  27.241  17.866  1.00 68.01  ? 616 LYS A NZ    1 
ATOM   4860 N  N     . GLN A 1 617 ? 4.789   30.571  20.538  1.00 50.80  ? 617 GLN A N     1 
ATOM   4861 C  CA    . GLN A 1 617 ? 4.476   31.831  21.203  1.00 51.79  ? 617 GLN A CA    1 
ATOM   4862 C  C     . GLN A 1 617 ? 3.487   31.619  22.343  1.00 49.22  ? 617 GLN A C     1 
ATOM   4863 O  O     . GLN A 1 617 ? 3.690   32.115  23.457  1.00 50.72  ? 617 GLN A O     1 
ATOM   4864 C  CB    . GLN A 1 617 ? 3.929   32.839  20.190  1.00 48.13  ? 617 GLN A CB    1 
ATOM   4865 C  CG    . GLN A 1 617 ? 3.825   34.256  20.722  1.00 48.48  ? 617 GLN A CG    1 
ATOM   4866 C  CD    . GLN A 1 617 ? 5.179   34.838  21.069  1.00 52.14  ? 617 GLN A CD    1 
ATOM   4867 O  OE1   . GLN A 1 617 ? 6.213   34.290  20.688  1.00 62.34  ? 617 GLN A OE1   1 
ATOM   4868 N  NE2   . GLN A 1 617 ? 5.183   35.947  21.798  1.00 58.74  ? 617 GLN A NE2   1 
ATOM   4869 N  N     . ARG A 1 618 ? 2.407   30.877  22.083  1.00 47.28  ? 618 ARG A N     1 
ATOM   4870 C  CA    . ARG A 1 618 ? 1.399   30.658  23.116  1.00 47.54  ? 618 ARG A CA    1 
ATOM   4871 C  C     . ARG A 1 618 ? 1.994   29.957  24.329  1.00 48.96  ? 618 ARG A C     1 
ATOM   4872 O  O     . ARG A 1 618 ? 1.632   30.263  25.472  1.00 51.87  ? 618 ARG A O     1 
ATOM   4873 C  CB    . ARG A 1 618 ? 0.229   29.852  22.553  1.00 42.53  ? 618 ARG A CB    1 
ATOM   4874 C  CG    . ARG A 1 618 ? -0.568  30.564  21.470  1.00 41.10  ? 618 ARG A CG    1 
ATOM   4875 C  CD    . ARG A 1 618 ? -1.839  29.797  21.128  1.00 38.49  ? 618 ARG A CD    1 
ATOM   4876 N  NE    . ARG A 1 618 ? -1.552  28.448  20.654  1.00 43.06  ? 618 ARG A NE    1 
ATOM   4877 C  CZ    . ARG A 1 618 ? -1.359  28.126  19.382  1.00 48.47  ? 618 ARG A CZ    1 
ATOM   4878 N  NH1   . ARG A 1 618 ? -1.440  29.031  18.421  1.00 48.66  ? 618 ARG A NH1   1 
ATOM   4879 N  NH2   . ARG A 1 618 ? -1.073  26.866  19.068  1.00 43.39  ? 618 ARG A NH2   1 
ATOM   4880 N  N     . ILE A 1 619 ? 2.909   29.014  24.102  1.00 49.99  ? 619 ILE A N     1 
ATOM   4881 C  CA    . ILE A 1 619 ? 3.547   28.312  25.212  1.00 52.57  ? 619 ILE A CA    1 
ATOM   4882 C  C     . ILE A 1 619 ? 4.430   29.266  26.007  1.00 54.95  ? 619 ILE A C     1 
ATOM   4883 O  O     . ILE A 1 619 ? 4.401   29.279  27.243  1.00 55.61  ? 619 ILE A O     1 
ATOM   4884 C  CB    . ILE A 1 619 ? 4.342   27.100  24.695  1.00 54.86  ? 619 ILE A CB    1 
ATOM   4885 C  CG1   . ILE A 1 619 ? 3.394   26.023  24.167  1.00 45.68  ? 619 ILE A CG1   1 
ATOM   4886 C  CG2   . ILE A 1 619 ? 5.244   26.544  25.791  1.00 53.79  ? 619 ILE A CG2   1 
ATOM   4887 C  CD1   . ILE A 1 619 ? 4.102   24.791  23.644  1.00 55.39  ? 619 ILE A CD1   1 
ATOM   4888 N  N     . SER A 1 620 ? 5.225   30.082  25.310  1.00 54.58  ? 620 SER A N     1 
ATOM   4889 C  CA    . SER A 1 620 ? 6.104   31.028  25.988  1.00 55.61  ? 620 SER A CA    1 
ATOM   4890 C  C     . SER A 1 620 ? 5.334   32.001  26.870  1.00 56.80  ? 620 SER A C     1 
ATOM   4891 O  O     . SER A 1 620 ? 5.909   32.555  27.814  1.00 57.99  ? 620 SER A O     1 
ATOM   4892 C  CB    . SER A 1 620 ? 6.939   31.799  24.964  1.00 60.20  ? 620 SER A CB    1 
ATOM   4893 O  OG    . SER A 1 620 ? 6.122   32.644  24.172  1.00 62.23  ? 620 SER A OG    1 
ATOM   4894 N  N     . GLN A 1 621 ? 4.053   32.221  26.590  1.00 56.37  ? 621 GLN A N     1 
ATOM   4895 C  CA    . GLN A 1 621 ? 3.218   33.093  27.405  1.00 61.54  ? 621 GLN A CA    1 
ATOM   4896 C  C     . GLN A 1 621 ? 2.593   32.376  28.593  1.00 65.01  ? 621 GLN A C     1 
ATOM   4897 O  O     . GLN A 1 621 ? 1.838   33.000  29.347  1.00 68.40  ? 621 GLN A O     1 
ATOM   4898 C  CB    . GLN A 1 621 ? 2.119   33.723  26.544  1.00 63.22  ? 621 GLN A CB    1 
ATOM   4899 C  CG    . GLN A 1 621 ? 2.656   34.640  25.458  1.00 59.68  ? 621 GLN A CG    1 
ATOM   4900 C  CD    . GLN A 1 621 ? 3.563   35.719  26.013  1.00 66.70  ? 621 GLN A CD    1 
ATOM   4901 O  OE1   . GLN A 1 621 ? 3.131   36.570  26.791  1.00 70.18  ? 621 GLN A OE1   1 
ATOM   4902 N  NE2   . GLN A 1 621 ? 4.831   35.686  25.622  1.00 67.76  ? 621 GLN A NE2   1 
ATOM   4903 N  N     . MET A 1 622 ? 2.885   31.092  28.783  1.00 66.01  ? 622 MET A N     1 
ATOM   4904 C  CA    . MET A 1 622 ? 2.370   30.355  29.932  1.00 63.83  ? 622 MET A CA    1 
ATOM   4905 C  C     . MET A 1 622 ? 3.082   30.790  31.208  1.00 64.83  ? 622 MET A C     1 
ATOM   4906 O  O     . MET A 1 622 ? 4.236   31.218  31.177  1.00 73.50  ? 622 MET A O     1 
ATOM   4907 C  CB    . MET A 1 622 ? 2.529   28.844  29.729  1.00 59.88  ? 622 MET A CB    1 
ATOM   4908 C  CG    . MET A 1 622 ? 1.775   28.276  28.537  1.00 56.36  ? 622 MET A CG    1 
ATOM   4909 S  SD    . MET A 1 622 ? 1.847   26.476  28.489  1.00 59.49  ? 622 MET A SD    1 
ATOM   4910 C  CE    . MET A 1 622 ? 1.190   26.068  30.106  1.00 58.42  ? 622 MET A CE    1 
ATOM   4911 O  OXT   . MET A 1 622 ? 2.524   30.723  32.302  1.00 77.09  ? 622 MET A OXT   1 
HETATM 4912 MN MN    . MN  B 2 .   ? -2.068  -0.081  9.409   1.00 45.17  ? 701 MN  A MN    1 
HETATM 4913 MN MN    . MN  C 2 .   ? -5.226  -2.949  13.348  1.00 59.73  ? 702 MN  A MN    1 
HETATM 4914 MN MN    . MN  D 2 .   ? -3.932  28.613  3.320   1.00 101.41 ? 703 MN  A MN    1 
HETATM 4915 P  P     A PGA E 3 .   ? -2.520  -1.436  11.708  0.22 43.87  ? 704 PGA A P     1 
HETATM 4916 P  P     B PGA E 3 .   ? -0.431  -3.053  10.166  0.50 46.51  ? 704 PGA A P     1 
HETATM 4917 P  P     C PGA E 3 .   ? 0.701   -3.307  9.867   0.28 50.03  ? 704 PGA A P     1 
HETATM 4918 O  O1P   A PGA E 3 .   ? -1.727  -1.865  10.374  0.22 45.85  ? 704 PGA A O1P   1 
HETATM 4919 O  O1P   B PGA E 3 .   ? 0.413   -4.161  9.361   0.50 50.51  ? 704 PGA A O1P   1 
HETATM 4920 O  O1P   C PGA E 3 .   ? 1.130   -4.775  9.367   0.28 49.63  ? 704 PGA A O1P   1 
HETATM 4921 O  O2P   A PGA E 3 .   ? -1.527  -0.768  12.625  0.22 46.09  ? 704 PGA A O2P   1 
HETATM 4922 O  O2P   B PGA E 3 .   ? -0.939  -3.658  11.452  0.50 45.81  ? 704 PGA A O2P   1 
HETATM 4923 O  O2P   C PGA E 3 .   ? -0.803  -3.178  9.828   0.28 46.40  ? 704 PGA A O2P   1 
HETATM 4924 O  O3P   A PGA E 3 .   ? -3.090  -2.660  12.386  0.22 45.69  ? 704 PGA A O3P   1 
HETATM 4925 O  O3P   B PGA E 3 .   ? -1.584  -2.578  9.318   0.50 45.51  ? 704 PGA A O3P   1 
HETATM 4926 O  O3P   C PGA E 3 .   ? 1.337   -2.265  8.981   0.28 47.63  ? 704 PGA A O3P   1 
HETATM 4927 O  O4P   A PGA E 3 .   ? -3.627  -0.466  11.375  0.22 42.63  ? 704 PGA A O4P   1 
HETATM 4928 O  O4P   B PGA E 3 .   ? 0.477   -1.887  10.480  0.50 48.34  ? 704 PGA A O4P   1 
HETATM 4929 O  O4P   C PGA E 3 .   ? 1.187   -3.125  11.284  0.28 47.60  ? 704 PGA A O4P   1 
HETATM 4930 C  C2    A PGA E 3 .   ? -0.801  -2.926  10.428  0.22 46.58  ? 704 PGA A C2    1 
HETATM 4931 C  C2    B PGA E 3 .   ? -0.096  -4.801  8.214   0.50 46.38  ? 704 PGA A C2    1 
HETATM 4932 C  C2    C PGA E 3 .   ? 2.135   -4.946  8.392   0.28 48.82  ? 704 PGA A C2    1 
HETATM 4933 C  C1    A PGA E 3 .   ? 0.530   -2.446  9.898   0.22 47.79  ? 704 PGA A C1    1 
HETATM 4934 C  C1    B PGA E 3 .   ? 1.080   -5.321  7.419   0.50 45.29  ? 704 PGA A C1    1 
HETATM 4935 C  C1    C PGA E 3 .   ? 2.446   -6.418  8.259   0.28 48.58  ? 704 PGA A C1    1 
HETATM 4936 O  O1    A PGA E 3 .   ? 0.686   -1.248  9.579   0.22 46.15  ? 704 PGA A O1    1 
HETATM 4937 O  O1    B PGA E 3 .   ? 1.546   -6.466  7.625   0.50 46.66  ? 704 PGA A O1    1 
HETATM 4938 O  O1    C PGA E 3 .   ? 3.273   -6.965  9.023   0.28 47.13  ? 704 PGA A O1    1 
HETATM 4939 O  O2    A PGA E 3 .   ? 1.496   -3.230  9.785   0.22 49.71  ? 704 PGA A O2    1 
HETATM 4940 O  O2    B PGA E 3 .   ? 1.613   -4.596  6.551   0.50 47.74  ? 704 PGA A O2    1 
HETATM 4941 O  O2    C PGA E 3 .   ? 1.883   -7.103  7.379   0.28 48.24  ? 704 PGA A O2    1 
HETATM 4942 H  H21   A PGA E 3 .   ? -1.159  -3.764  9.830   0.22 55.95  ? 704 PGA A H21   1 
HETATM 4943 H  H21   B PGA E 3 .   ? -0.677  -4.100  7.615   0.50 55.71  ? 704 PGA A H21   1 
HETATM 4944 H  H21   C PGA E 3 .   ? 3.033   -4.400  8.683   0.28 58.64  ? 704 PGA A H21   1 
HETATM 4945 H  H22   A PGA E 3 .   ? -0.689  -3.271  11.456  0.22 55.95  ? 704 PGA A H22   1 
HETATM 4946 H  H22   B PGA E 3 .   ? -0.754  -5.623  8.499   0.50 55.71  ? 704 PGA A H22   1 
HETATM 4947 H  H22   C PGA E 3 .   ? 1.797   -4.548  7.435   0.28 58.64  ? 704 PGA A H22   1 
HETATM 4948 P  PB    . GDP F 4 .   ? -4.082  -0.893  15.579  1.00 48.74  ? 705 GDP A PB    1 
HETATM 4949 O  O1B   . GDP F 4 .   ? -3.910  0.585   15.336  1.00 48.58  ? 705 GDP A O1B   1 
HETATM 4950 O  O2B   . GDP F 4 .   ? -2.923  -1.624  14.939  1.00 45.08  ? 705 GDP A O2B   1 
HETATM 4951 O  O3B   . GDP F 4 .   ? -5.388  -1.366  14.990  1.00 50.74  ? 705 GDP A O3B   1 
HETATM 4952 O  O3A   . GDP F 4 .   ? -4.070  -1.159  17.162  1.00 52.09  ? 705 GDP A O3A   1 
HETATM 4953 P  PA    . GDP F 4 .   ? -4.915  -2.333  17.865  1.00 46.05  ? 705 GDP A PA    1 
HETATM 4954 O  O1A   . GDP F 4 .   ? -6.398  -2.040  17.892  1.00 43.99  ? 705 GDP A O1A   1 
HETATM 4955 O  O2A   . GDP F 4 .   ? -4.637  -3.658  17.205  1.00 54.23  ? 705 GDP A O2A   1 
HETATM 4956 O  "O5'" . GDP F 4 .   ? -4.293  -2.287  19.346  1.00 44.45  ? 705 GDP A "O5'" 1 
HETATM 4957 C  "C5'" . GDP F 4 .   ? -2.958  -2.740  19.561  1.00 45.49  ? 705 GDP A "C5'" 1 
HETATM 4958 C  "C4'" . GDP F 4 .   ? -2.710  -2.832  21.057  1.00 48.41  ? 705 GDP A "C4'" 1 
HETATM 4959 O  "O4'" . GDP F 4 .   ? -3.082  -1.594  21.672  1.00 48.73  ? 705 GDP A "O4'" 1 
HETATM 4960 C  "C3'" . GDP F 4 .   ? -3.574  -3.925  21.668  1.00 49.96  ? 705 GDP A "C3'" 1 
HETATM 4961 O  "O3'" . GDP F 4 .   ? -2.747  -4.895  22.316  1.00 61.35  ? 705 GDP A "O3'" 1 
HETATM 4962 C  "C2'" . GDP F 4 .   ? -4.458  -3.227  22.682  1.00 50.67  ? 705 GDP A "C2'" 1 
HETATM 4963 O  "O2'" . GDP F 4 .   ? -4.445  -3.911  23.937  1.00 59.65  ? 705 GDP A "O2'" 1 
HETATM 4964 C  "C1'" . GDP F 4 .   ? -3.868  -1.835  22.840  1.00 51.40  ? 705 GDP A "C1'" 1 
HETATM 4965 N  N9    . GDP F 4 .   ? -4.964  -0.844  22.965  1.00 46.51  ? 705 GDP A N9    1 
HETATM 4966 C  C8    . GDP F 4 .   ? -5.916  -0.600  22.043  1.00 44.54  ? 705 GDP A C8    1 
HETATM 4967 N  N7    . GDP F 4 .   ? -6.768  0.368   22.466  1.00 44.18  ? 705 GDP A N7    1 
HETATM 4968 C  C5    . GDP F 4 .   ? -6.350  0.764   23.686  1.00 40.57  ? 705 GDP A C5    1 
HETATM 4969 C  C6    . GDP F 4 .   ? -6.788  1.747   24.699  1.00 40.80  ? 705 GDP A C6    1 
HETATM 4970 O  O6    . GDP F 4 .   ? -7.788  2.474   24.511  1.00 44.51  ? 705 GDP A O6    1 
HETATM 4971 N  N1    . GDP F 4 .   ? -6.082  1.845   25.832  1.00 46.19  ? 705 GDP A N1    1 
HETATM 4972 C  C2    . GDP F 4 .   ? -4.997  1.085   26.074  1.00 46.36  ? 705 GDP A C2    1 
HETATM 4973 N  N2    . GDP F 4 .   ? -4.345  1.252   27.250  1.00 47.70  ? 705 GDP A N2    1 
HETATM 4974 N  N3    . GDP F 4 .   ? -4.537  0.162   25.193  1.00 43.17  ? 705 GDP A N3    1 
HETATM 4975 C  C4    . GDP F 4 .   ? -5.160  -0.038  24.006  1.00 44.00  ? 705 GDP A C4    1 
HETATM 4976 O  O     . HOH G 5 .   ? -2.189  -2.652  9.582   0.50 45.29  ? 801 HOH A O     1 
HETATM 4977 O  O     . HOH G 5 .   ? -0.051  -0.221  9.843   0.50 41.20  ? 802 HOH A O     1 
HETATM 4978 O  O     . HOH G 5 .   ? -2.261  -0.012  11.625  0.50 39.77  ? 803 HOH A O     1 
HETATM 4979 O  O     . HOH G 5 .   ? -17.481 -7.192  -0.055  1.00 51.16  ? 804 HOH A O     1 
HETATM 4980 O  O     . HOH G 5 .   ? 4.111   3.971   18.441  1.00 52.17  ? 805 HOH A O     1 
HETATM 4981 O  O     . HOH G 5 .   ? 1.949   1.805   11.383  1.00 44.81  ? 806 HOH A O     1 
HETATM 4982 O  O     . HOH G 5 .   ? -11.392 -22.473 28.278  1.00 73.71  ? 807 HOH A O     1 
HETATM 4983 O  O     . HOH G 5 .   ? -6.413  -6.478  19.690  1.00 54.78  ? 808 HOH A O     1 
HETATM 4984 O  O     . HOH G 5 .   ? -5.666  -1.436  12.010  1.00 38.00  ? 809 HOH A O     1 
HETATM 4985 O  O     . HOH G 5 .   ? -14.948 -2.200  23.020  1.00 48.53  ? 810 HOH A O     1 
HETATM 4986 O  O     . HOH G 5 .   ? -11.676 23.786  16.347  1.00 47.59  ? 811 HOH A O     1 
HETATM 4987 O  O     . HOH G 5 .   ? -15.381 -4.535  20.426  1.00 44.89  ? 812 HOH A O     1 
HETATM 4988 O  O     . HOH G 5 .   ? -6.993  -28.017 14.681  1.00 56.48  ? 813 HOH A O     1 
HETATM 4989 O  O     . HOH G 5 .   ? 13.208  19.177  -0.744  1.00 47.75  ? 814 HOH A O     1 
HETATM 4990 O  O     . HOH G 5 .   ? 13.189  13.963  3.908   1.00 42.54  ? 815 HOH A O     1 
HETATM 4991 O  O     . HOH G 5 .   ? -4.723  -29.212 17.448  1.00 61.07  ? 816 HOH A O     1 
HETATM 4992 O  O     . HOH G 5 .   ? 9.987   -27.459 5.805   1.00 71.20  ? 817 HOH A O     1 
HETATM 4993 O  O     . HOH G 5 .   ? 3.877   -23.002 7.427   1.00 62.97  ? 818 HOH A O     1 
HETATM 4994 O  O     . HOH G 5 .   ? -16.502 26.020  24.291  1.00 54.37  ? 819 HOH A O     1 
HETATM 4995 O  O     . HOH G 5 .   ? 8.335   16.959  24.820  1.00 49.95  ? 820 HOH A O     1 
HETATM 4996 O  O     . HOH G 5 .   ? 7.700   1.919   4.735   1.00 48.09  ? 821 HOH A O     1 
HETATM 4997 O  O     . HOH G 5 .   ? 0.348   16.150  17.179  1.00 36.02  ? 822 HOH A O     1 
HETATM 4998 O  O     . HOH G 5 .   ? -4.157  8.985   28.385  1.00 41.47  ? 823 HOH A O     1 
HETATM 4999 O  O     . HOH G 5 .   ? 6.223   14.318  13.853  1.00 35.44  ? 824 HOH A O     1 
HETATM 5000 O  O     . HOH G 5 .   ? -0.495  26.687  16.162  1.00 42.19  ? 825 HOH A O     1 
HETATM 5001 O  O     . HOH G 5 .   ? -4.796  -4.469  14.806  1.00 49.61  ? 826 HOH A O     1 
HETATM 5002 O  O     . HOH G 5 .   ? -8.347  2.513   20.475  1.00 41.00  ? 827 HOH A O     1 
HETATM 5003 O  O     . HOH G 5 .   ? -3.646  6.651   29.929  1.00 44.34  ? 828 HOH A O     1 
HETATM 5004 O  O     . HOH G 5 .   ? -10.591 15.945  -1.926  1.00 50.43  ? 829 HOH A O     1 
HETATM 5005 O  O     . HOH G 5 .   ? 0.728   -4.080  1.121   1.00 40.30  ? 830 HOH A O     1 
HETATM 5006 O  O     . HOH G 5 .   ? -5.607  3.356   28.060  1.00 44.92  ? 831 HOH A O     1 
HETATM 5007 O  O     . HOH G 5 .   ? -9.206  -0.612  6.103   1.00 35.32  ? 832 HOH A O     1 
HETATM 5008 O  O     . HOH G 5 .   ? -20.469 -0.673  19.006  1.00 52.62  ? 833 HOH A O     1 
HETATM 5009 O  O     . HOH G 5 .   ? 7.259   6.715   3.785   1.00 44.43  ? 834 HOH A O     1 
HETATM 5010 O  O     . HOH G 5 .   ? 9.723   -18.624 -5.627  1.00 43.79  ? 835 HOH A O     1 
HETATM 5011 O  O     . HOH G 5 .   ? 1.125   -23.269 -5.320  1.00 46.27  ? 836 HOH A O     1 
HETATM 5012 O  O     . HOH G 5 .   ? -1.278  10.632  21.642  1.00 36.78  ? 837 HOH A O     1 
HETATM 5013 O  O     . HOH G 5 .   ? -23.922 1.625   24.480  1.00 51.41  ? 838 HOH A O     1 
HETATM 5014 O  O     . HOH G 5 .   ? 0.096   16.355  20.752  1.00 35.93  ? 839 HOH A O     1 
HETATM 5015 O  O     . HOH G 5 .   ? 3.940   16.050  19.257  1.00 34.46  ? 840 HOH A O     1 
HETATM 5016 O  O     . HOH G 5 .   ? -17.431 18.792  11.313  1.00 47.55  ? 841 HOH A O     1 
HETATM 5017 O  O     . HOH G 5 .   ? -13.920 -13.762 -4.055  1.00 44.55  ? 842 HOH A O     1 
HETATM 5018 O  O     . HOH G 5 .   ? 2.739   -31.233 -15.641 1.00 52.19  ? 843 HOH A O     1 
HETATM 5019 O  O     . HOH G 5 .   ? -18.321 12.548  27.711  1.00 45.11  ? 844 HOH A O     1 
HETATM 5020 O  O     . HOH G 5 .   ? 8.722   -22.380 -17.414 1.00 58.42  ? 845 HOH A O     1 
HETATM 5021 O  O     . HOH G 5 .   ? -3.303  9.087   7.781   1.00 33.44  ? 846 HOH A O     1 
HETATM 5022 O  O     . HOH G 5 .   ? -11.097 -13.480 25.273  1.00 58.73  ? 847 HOH A O     1 
HETATM 5023 O  O     . HOH G 5 .   ? -11.356 -18.065 -4.703  1.00 38.66  ? 848 HOH A O     1 
HETATM 5024 O  O     . HOH G 5 .   ? 20.996  11.095  9.367   1.00 50.52  ? 849 HOH A O     1 
HETATM 5025 O  O     . HOH G 5 .   ? -10.567 -30.594 28.483  1.00 54.22  ? 850 HOH A O     1 
HETATM 5026 O  O     . HOH G 5 .   ? 8.023   5.705   -10.744 1.00 50.44  ? 851 HOH A O     1 
HETATM 5027 O  O     . HOH G 5 .   ? -16.445 2.166   2.707   1.00 43.26  ? 852 HOH A O     1 
HETATM 5028 O  O     . HOH G 5 .   ? 4.468   -12.973 13.147  1.00 49.07  ? 853 HOH A O     1 
HETATM 5029 O  O     . HOH G 5 .   ? -23.460 4.220   14.863  1.00 47.69  ? 854 HOH A O     1 
HETATM 5030 O  O     . HOH G 5 .   ? -2.488  19.213  -4.223  1.00 53.60  ? 855 HOH A O     1 
HETATM 5031 O  O     . HOH G 5 .   ? 11.953  -20.979 5.169   1.00 59.13  ? 856 HOH A O     1 
HETATM 5032 O  O     . HOH G 5 .   ? -3.428  -14.325 8.934   1.00 39.23  ? 857 HOH A O     1 
HETATM 5033 O  O     . HOH G 5 .   ? 2.341   13.931  20.346  1.00 38.93  ? 858 HOH A O     1 
HETATM 5034 O  O     . HOH G 5 .   ? -11.048 -15.004 -13.203 1.00 50.86  ? 859 HOH A O     1 
HETATM 5035 O  O     . HOH G 5 .   ? -18.954 18.270  23.607  1.00 41.41  ? 860 HOH A O     1 
HETATM 5036 O  O     . HOH G 5 .   ? -11.409 -4.423  -1.496  1.00 40.56  ? 861 HOH A O     1 
HETATM 5037 O  O     . HOH G 5 .   ? 2.251   4.358   11.191  1.00 39.79  ? 862 HOH A O     1 
HETATM 5038 O  O     . HOH G 5 .   ? -3.202  10.856  1.180   1.00 37.85  ? 863 HOH A O     1 
HETATM 5039 O  O     . HOH G 5 .   ? 1.189   -12.421 6.940   1.00 43.89  ? 864 HOH A O     1 
HETATM 5040 O  O     . HOH G 5 .   ? 2.086   18.545  29.671  1.00 52.04  ? 865 HOH A O     1 
HETATM 5041 O  O     . HOH G 5 .   ? -14.458 17.156  31.717  1.00 56.78  ? 866 HOH A O     1 
HETATM 5042 O  O     . HOH G 5 .   ? -7.173  -4.329  8.582   1.00 41.73  ? 867 HOH A O     1 
HETATM 5043 O  O     . HOH G 5 .   ? -17.113 16.677  5.513   1.00 51.84  ? 868 HOH A O     1 
HETATM 5044 O  O     . HOH G 5 .   ? 6.906   -0.744  5.462   1.00 50.97  ? 869 HOH A O     1 
HETATM 5045 O  O     . HOH G 5 .   ? -18.879 3.577   2.016   1.00 53.89  ? 870 HOH A O     1 
HETATM 5046 O  O     . HOH G 5 .   ? 5.194   11.455  25.708  1.00 40.57  ? 871 HOH A O     1 
HETATM 5047 O  O     . HOH G 5 .   ? 17.478  -7.059  -0.095  1.00 56.49  ? 872 HOH A O     1 
HETATM 5048 O  O     . HOH G 5 .   ? -15.700 -1.362  1.551   1.00 45.35  ? 873 HOH A O     1 
HETATM 5049 O  O     . HOH G 5 .   ? -2.108  12.234  -1.020  1.00 37.61  ? 874 HOH A O     1 
HETATM 5050 O  O     . HOH G 5 .   ? 6.609   9.411   -5.576  1.00 45.83  ? 875 HOH A O     1 
HETATM 5051 O  O     . HOH G 5 .   ? 0.969   12.332  18.649  1.00 42.43  ? 876 HOH A O     1 
HETATM 5052 O  O     . HOH G 5 .   ? 12.539  26.403  11.938  1.00 64.41  ? 877 HOH A O     1 
HETATM 5053 O  O     . HOH G 5 .   ? 11.412  9.428   14.437  1.00 47.96  ? 878 HOH A O     1 
HETATM 5054 O  O     . HOH G 5 .   ? -1.140  28.913  9.577   1.00 46.63  ? 879 HOH A O     1 
HETATM 5055 O  O     . HOH G 5 .   ? -4.154  14.428  22.908  1.00 35.09  ? 880 HOH A O     1 
HETATM 5056 O  O     . HOH G 5 .   ? -21.149 12.076  9.431   1.00 41.93  ? 881 HOH A O     1 
HETATM 5057 O  O     . HOH G 5 .   ? 5.485   -17.909 1.960   1.00 48.42  ? 882 HOH A O     1 
HETATM 5058 O  O     . HOH G 5 .   ? 1.984   -12.265 21.508  1.00 57.90  ? 883 HOH A O     1 
HETATM 5059 O  O     . HOH G 5 .   ? 16.539  15.286  19.273  1.00 48.01  ? 884 HOH A O     1 
HETATM 5060 O  O     . HOH G 5 .   ? -1.005  22.438  19.489  1.00 43.06  ? 885 HOH A O     1 
HETATM 5061 O  O     . HOH G 5 .   ? -11.768 -25.065 10.590  1.00 48.31  ? 886 HOH A O     1 
HETATM 5062 O  O     . HOH G 5 .   ? -4.127  6.081   19.495  1.00 41.54  ? 887 HOH A O     1 
HETATM 5063 O  O     . HOH G 5 .   ? -10.333 -17.869 -14.086 1.00 44.15  ? 888 HOH A O     1 
HETATM 5064 O  O     . HOH G 5 .   ? 8.489   -9.407  -0.382  1.00 50.37  ? 889 HOH A O     1 
HETATM 5065 O  O     . HOH G 5 .   ? -27.414 4.866   19.619  1.00 50.03  ? 890 HOH A O     1 
HETATM 5066 O  O     . HOH G 5 .   ? 7.979   11.730  1.748   1.00 35.99  ? 891 HOH A O     1 
HETATM 5067 O  O     . HOH G 5 .   ? -18.326 -19.259 -5.364  1.00 58.58  ? 892 HOH A O     1 
HETATM 5068 O  O     . HOH G 5 .   ? -3.397  -13.830 6.241   1.00 42.27  ? 893 HOH A O     1 
HETATM 5069 O  O     . HOH G 5 .   ? 4.497   -2.516  2.677   1.00 40.04  ? 894 HOH A O     1 
HETATM 5070 O  O     . HOH G 5 .   ? 3.036   -21.824 -6.076  1.00 44.60  ? 895 HOH A O     1 
HETATM 5071 O  O     . HOH G 5 .   ? -10.722 2.351   7.415   1.00 42.25  ? 896 HOH A O     1 
HETATM 5072 O  O     . HOH G 5 .   ? 1.016   -22.602 16.560  1.00 50.89  ? 897 HOH A O     1 
HETATM 5073 O  O     . HOH G 5 .   ? -16.032 -9.100  3.686   1.00 41.54  ? 898 HOH A O     1 
HETATM 5074 O  O     . HOH G 5 .   ? -13.916 -12.818 1.186   1.00 51.36  ? 899 HOH A O     1 
HETATM 5075 O  O     . HOH G 5 .   ? -4.411  -3.845  9.124   1.00 46.20  ? 900 HOH A O     1 
HETATM 5076 O  O     . HOH G 5 .   ? -11.116 2.332   21.727  1.00 48.30  ? 901 HOH A O     1 
HETATM 5077 O  O     . HOH G 5 .   ? 6.531   5.044   2.010   1.00 40.82  ? 902 HOH A O     1 
HETATM 5078 O  O     . HOH G 5 .   ? -1.606  31.867  18.586  1.00 47.04  ? 903 HOH A O     1 
HETATM 5079 O  O     . HOH G 5 .   ? -3.906  7.550   21.768  1.00 39.20  ? 904 HOH A O     1 
HETATM 5080 O  O     . HOH G 5 .   ? 7.474   11.114  -10.154 1.00 60.54  ? 905 HOH A O     1 
HETATM 5081 O  O     . HOH G 5 .   ? -7.794  1.017   -11.412 1.00 53.72  ? 906 HOH A O     1 
HETATM 5082 O  O     . HOH G 5 .   ? 1.347   35.027  8.098   1.00 49.21  ? 907 HOH A O     1 
HETATM 5083 O  O     . HOH G 5 .   ? 6.776   -3.118  3.592   1.00 51.91  ? 908 HOH A O     1 
HETATM 5084 O  O     . HOH G 5 .   ? 2.080   4.688   26.865  1.00 54.63  ? 909 HOH A O     1 
HETATM 5085 O  O     . HOH G 5 .   ? -20.315 18.782  10.896  1.00 48.69  ? 910 HOH A O     1 
HETATM 5086 O  O     . HOH G 5 .   ? -6.596  -6.249  16.341  1.00 51.93  ? 911 HOH A O     1 
HETATM 5087 O  O     . HOH G 5 .   ? 8.725   32.992  20.119  1.00 57.98  ? 912 HOH A O     1 
HETATM 5088 O  O     . HOH G 5 .   ? -13.192 -11.490 -2.748  1.00 44.90  ? 913 HOH A O     1 
HETATM 5089 O  O     . HOH G 5 .   ? 14.414  20.566  1.043   1.00 51.37  ? 914 HOH A O     1 
HETATM 5090 O  O     . HOH G 5 .   ? -6.462  -5.106  1.569   1.00 40.52  ? 915 HOH A O     1 
HETATM 5091 O  O     . HOH G 5 .   ? -10.143 26.597  9.773   1.00 47.65  ? 916 HOH A O     1 
HETATM 5092 O  O     . HOH G 5 .   ? -7.441  -21.911 -21.444 1.00 52.96  ? 917 HOH A O     1 
HETATM 5093 O  O     . HOH G 5 .   ? -15.908 -18.853 2.527   1.00 57.26  ? 918 HOH A O     1 
HETATM 5094 O  O     . HOH G 5 .   ? -6.618  -4.420  -21.690 1.00 54.70  ? 919 HOH A O     1 
HETATM 5095 O  O     . HOH G 5 .   ? -13.787 -10.913 3.100   1.00 38.60  ? 920 HOH A O     1 
HETATM 5096 O  O     . HOH G 5 .   ? 5.309   5.174   14.964  1.00 48.29  ? 921 HOH A O     1 
HETATM 5097 O  O     . HOH G 5 .   ? 13.678  24.630  -5.026  1.00 80.70  ? 922 HOH A O     1 
HETATM 5098 O  O     . HOH G 5 .   ? 2.765   -24.835 -7.272  1.00 51.08  ? 923 HOH A O     1 
HETATM 5099 O  O     . HOH G 5 .   ? -10.665 21.564  14.059  1.00 43.46  ? 924 HOH A O     1 
HETATM 5100 O  O     . HOH G 5 .   ? 3.880   24.631  33.668  1.00 59.24  ? 925 HOH A O     1 
HETATM 5101 O  O     . HOH G 5 .   ? -12.181 -19.938 -13.609 1.00 59.32  ? 926 HOH A O     1 
HETATM 5102 O  O     . HOH G 5 .   ? -23.542 19.024  13.517  1.00 55.15  ? 927 HOH A O     1 
HETATM 5103 O  O     . HOH G 5 .   ? -1.007  24.593  0.402   1.00 52.29  ? 928 HOH A O     1 
HETATM 5104 O  O     . HOH G 5 .   ? 17.436  13.122  -7.466  1.00 56.33  ? 929 HOH A O     1 
HETATM 5105 O  O     . HOH G 5 .   ? -10.698 -2.482  7.065   1.00 46.00  ? 930 HOH A O     1 
HETATM 5106 O  O     . HOH G 5 .   ? -0.027  20.200  19.101  1.00 43.41  ? 931 HOH A O     1 
HETATM 5107 O  O     . HOH G 5 .   ? -15.019 -26.161 8.437   1.00 53.06  ? 932 HOH A O     1 
HETATM 5108 O  O     . HOH G 5 .   ? 9.963   3.191   3.261   1.00 54.08  ? 933 HOH A O     1 
HETATM 5109 O  O     . HOH G 5 .   ? -14.415 26.600  18.040  1.00 58.68  ? 934 HOH A O     1 
HETATM 5110 O  O     . HOH G 5 .   ? -21.679 20.618  12.155  1.00 55.36  ? 935 HOH A O     1 
HETATM 5111 O  O     . HOH G 5 .   ? 9.660   27.347  23.370  1.00 78.05  ? 936 HOH A O     1 
HETATM 5112 O  O     . HOH G 5 .   ? 10.840  -26.301 34.600  1.00 74.61  ? 937 HOH A O     1 
HETATM 5113 O  O     . HOH G 5 .   ? -4.612  -6.566  0.407   1.00 42.13  ? 938 HOH A O     1 
HETATM 5114 O  O     . HOH G 5 .   ? 5.651   -5.905  -14.181 1.00 56.34  ? 939 HOH A O     1 
HETATM 5115 O  O     . HOH G 5 .   ? -11.153 22.636  12.036  1.00 48.67  ? 940 HOH A O     1 
HETATM 5116 O  O     . HOH G 5 .   ? 1.857   17.553  19.050  1.00 41.75  ? 941 HOH A O     1 
HETATM 5117 O  O     . HOH G 5 .   ? 15.864  24.222  17.481  1.00 64.20  ? 942 HOH A O     1 
HETATM 5118 O  O     . HOH G 5 .   ? 3.772   23.251  36.136  1.00 67.54  ? 943 HOH A O     1 
HETATM 5119 O  O     . HOH G 5 .   ? 16.247  21.538  -0.906  1.00 58.01  ? 944 HOH A O     1 
HETATM 5120 O  O     . HOH G 5 .   ? -25.985 19.939  14.320  1.00 50.12  ? 945 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   ? 2.0477 1.6764 1.1504 -0.1281 0.0924  -0.0435 3   PRO A N   
2    C CA  . PRO A 3   ? 1.9810 1.5993 1.0652 -0.1354 0.1236  -0.0672 3   PRO A CA  
3    C C   . PRO A 3   ? 1.9436 1.5773 1.0734 -0.1222 0.1670  -0.0813 3   PRO A C   
4    O O   . PRO A 3   ? 1.9001 1.5546 1.0769 -0.1084 0.1708  -0.0739 3   PRO A O   
5    C CB  . PRO A 3   ? 2.0214 1.6240 1.0560 -0.1516 0.1288  -0.0574 3   PRO A CB  
6    C CG  . PRO A 3   ? 1.9966 1.6071 1.0443 -0.1487 0.1217  -0.0315 3   PRO A CG  
7    C CD  . PRO A 3   ? 1.9922 1.6135 1.0709 -0.1356 0.0873  -0.0201 3   PRO A CD  
8    N N   . GLN A 4   ? 1.6518 1.2770 0.7704 -0.1250 0.1987  -0.1007 4   GLN A N   
9    C CA  . GLN A 4   ? 1.4992 1.1430 0.6656 -0.1094 0.2403  -0.1132 4   GLN A CA  
10   C C   . GLN A 4   ? 1.4471 1.0737 0.5870 -0.1149 0.2689  -0.1332 4   GLN A C   
11   O O   . GLN A 4   ? 1.5115 1.1090 0.6012 -0.1293 0.2554  -0.1421 4   GLN A O   
12   C CB  . GLN A 4   ? 1.5167 1.1714 0.7350 -0.0893 0.2397  -0.1222 4   GLN A CB  
13   C CG  . GLN A 4   ? 1.5046 1.1338 0.7041 -0.0921 0.2242  -0.1397 4   GLN A CG  
14   C CD  . GLN A 4   ? 1.5285 1.1656 0.7789 -0.0731 0.2230  -0.1466 4   GLN A CD  
15   O OE1 . GLN A 4   ? 1.4632 1.1342 0.7796 -0.0546 0.2291  -0.1352 4   GLN A OE1 
16   N NE2 . GLN A 4   ? 1.5476 1.1629 0.7858 -0.0775 0.2091  -0.1614 4   GLN A NE2 
17   N N   . LEU A 5   ? 1.4371 1.0840 0.6128 -0.1033 0.3080  -0.1397 5   LEU A N   
18   C CA  . LEU A 5   ? 1.4141 1.0474 0.5740 -0.1035 0.3400  -0.1595 5   LEU A CA  
19   C C   . LEU A 5   ? 1.3706 1.0007 0.5692 -0.0820 0.3567  -0.1789 5   LEU A C   
20   O O   . LEU A 5   ? 1.4065 1.0163 0.5871 -0.0815 0.3798  -0.1970 5   LEU A O   
21   C CB  . LEU A 5   ? 1.3784 1.0381 0.5544 -0.1034 0.3736  -0.1550 5   LEU A CB  
22   C CG  . LEU A 5   ? 1.4195 1.0710 0.5449 -0.1280 0.3645  -0.1389 5   LEU A CG  
23   C CD1 . LEU A 5   ? 1.4247 1.1083 0.5762 -0.1281 0.3987  -0.1344 5   LEU A CD1 
24   C CD2 . LEU A 5   ? 1.5033 1.1114 0.5527 -0.1481 0.3558  -0.1481 5   LEU A CD2 
25   N N   . HIS A 6   ? 1.3534 1.0001 0.6031 -0.0643 0.3460  -0.1748 6   HIS A N   
26   C CA  . HIS A 6   ? 1.4564 1.0953 0.7422 -0.0434 0.3578  -0.1904 6   HIS A CA  
27   C C   . HIS A 6   ? 1.4951 1.1234 0.7885 -0.0420 0.3253  -0.1881 6   HIS A C   
28   O O   . HIS A 6   ? 1.5008 1.1079 0.7471 -0.0625 0.2948  -0.1867 6   HIS A O   
29   C CB  . HIS A 6   ? 1.3365 1.0158 0.6953 -0.0158 0.3876  -0.1881 6   HIS A CB  
30   C CG  . HIS A 6   ? 1.3454 1.0402 0.7037 -0.0155 0.4215  -0.1926 6   HIS A CG  
31   N ND1 . HIS A 6   ? 1.2651 0.9919 0.6264 -0.0258 0.4283  -0.1784 6   HIS A ND1 
32   C CD2 . HIS A 6   ? 1.3278 1.0096 0.6822 -0.0069 0.4511  -0.2098 6   HIS A CD2 
33   C CE1 . HIS A 6   ? 1.3112 1.0476 0.6723 -0.0239 0.4608  -0.1872 6   HIS A CE1 
34   N NE2 . HIS A 6   ? 1.3501 1.0597 0.7070 -0.0114 0.4754  -0.2064 6   HIS A NE2 
35   N N   . ASN A 7   ? 1.7198 1.3655 1.0740 -0.0180 0.3303  -0.1869 7   ASN A N   
36   C CA  . ASN A 7   ? 1.7120 1.3494 1.0787 -0.0154 0.3026  -0.1850 7   ASN A CA  
37   C C   . ASN A 7   ? 1.7047 1.3796 1.1382 0.0068  0.3045  -0.1708 7   ASN A C   
38   O O   . ASN A 7   ? 1.7213 1.3969 1.1971 0.0243  0.3011  -0.1723 7   ASN A O   
39   C CB  . ASN A 7   ? 1.7121 1.3138 1.0735 -0.0120 0.3051  -0.2036 7   ASN A CB  
40   C CG  . ASN A 7   ? 1.9471 1.5115 1.2392 -0.0394 0.2932  -0.2164 7   ASN A CG  
41   O OD1 . ASN A 7   ? 1.9795 1.5284 1.2414 -0.0455 0.3144  -0.2263 7   ASN A OD1 
42   N ND2 . ASN A 7   ? 1.9091 1.4616 1.1773 -0.0567 0.2587  -0.2163 7   ASN A ND2 
43   N N   . GLY A 8   ? 1.7077 1.4191 1.1596 0.0046  0.3040  -0.1529 8   GLY A N   
44   C CA  . GLY A 8   ? 1.6494 1.4091 1.1792 0.0227  0.2978  -0.1347 8   GLY A CA  
45   C C   . GLY A 8   ? 1.6443 1.4250 1.1876 0.0121  0.2595  -0.1128 8   GLY A C   
46   O O   . GLY A 8   ? 1.6095 1.4286 1.2104 0.0225  0.2533  -0.0975 8   GLY A O   
47   N N   . LEU A 9   ? 1.4410 1.1964 0.9312 -0.0080 0.2333  -0.1110 9   LEU A N   
48   C CA  . LEU A 9   ? 1.3334 1.1034 0.8322 -0.0158 0.1979  -0.0904 9   LEU A CA  
49   C C   . LEU A 9   ? 1.2422 0.9985 0.7340 -0.0198 0.1615  -0.0906 9   LEU A C   
50   O O   . LEU A 9   ? 1.1837 0.9573 0.7018 -0.0185 0.1338  -0.0744 9   LEU A O   
51   C CB  . LEU A 9   ? 1.3179 1.0781 0.7632 -0.0354 0.1973  -0.0806 9   LEU A CB  
52   C CG  . LEU A 9   ? 1.2863 1.0649 0.7375 -0.0370 0.2325  -0.0779 9   LEU A CG  
53   C CD1 . LEU A 9   ? 1.2911 1.0529 0.6823 -0.0595 0.2293  -0.0664 9   LEU A CD1 
54   C CD2 . LEU A 9   ? 1.1861 1.0095 0.7139 -0.0226 0.2351  -0.0656 9   LEU A CD2 
55   N N   . ASP A 10  ? 1.3033 1.0298 0.7612 -0.0258 0.1620  -0.1092 10  ASP A N   
56   C CA  . ASP A 10  ? 1.2633 0.9820 0.7167 -0.0329 0.1284  -0.1111 10  ASP A CA  
57   C C   . ASP A 10  ? 1.0946 0.8192 0.6003 -0.0175 0.1318  -0.1180 10  ASP A C   
58   O O   . ASP A 10  ? 1.0699 0.7689 0.5639 -0.0150 0.1525  -0.1365 10  ASP A O   
59   C CB  . ASP A 10  ? 1.3119 0.9946 0.6927 -0.0540 0.1243  -0.1273 10  ASP A CB  
60   C CG  . ASP A 10  ? 1.2347 0.9170 0.6127 -0.0646 0.0877  -0.1290 10  ASP A CG  
61   O OD1 . ASP A 10  ? 1.2029 0.9135 0.6330 -0.0552 0.0652  -0.1157 10  ASP A OD1 
62   O OD2 . ASP A 10  ? 1.3553 1.0104 0.6789 -0.0837 0.0823  -0.1446 10  ASP A OD2 
63   N N   . PHE A 11  ? 1.0024 0.7562 0.5619 -0.0075 0.1127  -0.1028 11  PHE A N   
64   C CA  . PHE A 11  ? 0.9660 0.7265 0.5744 0.0062  0.1137  -0.1056 11  PHE A CA  
65   C C   . PHE A 11  ? 0.8763 0.6237 0.4767 -0.0049 0.0914  -0.1145 11  PHE A C   
66   O O   . PHE A 11  ? 0.8543 0.6108 0.4957 0.0030  0.0852  -0.1125 11  PHE A O   
67   C CB  . PHE A 11  ? 0.8790 0.6760 0.5446 0.0192  0.1048  -0.0864 11  PHE A CB  
68   C CG  . PHE A 11  ? 0.9212 0.7359 0.6167 0.0343  0.1315  -0.0815 11  PHE A CG  
69   C CD1 . PHE A 11  ? 0.9491 0.7722 0.6275 0.0300  0.1459  -0.0765 11  PHE A CD1 
70   C CD2 . PHE A 11  ? 0.9327 0.7580 0.6742 0.0518  0.1414  -0.0809 11  PHE A CD2 
71   C CE1 . PHE A 11  ? 0.9104 0.7582 0.6221 0.0424  0.1702  -0.0722 11  PHE A CE1 
72   C CE2 . PHE A 11  ? 0.8386 0.6879 0.6125 0.0665  0.1632  -0.0752 11  PHE A CE2 
73   C CZ  . PHE A 11  ? 0.7923 0.6560 0.5540 0.0614  0.1777  -0.0714 11  PHE A CZ  
74   N N   . SER A 12  ? 0.8430 0.5711 0.3909 -0.0248 0.0790  -0.1239 12  SER A N   
75   C CA  . SER A 12  ? 0.9188 0.6419 0.4619 -0.0390 0.0557  -0.1323 12  SER A CA  
76   C C   . SER A 12  ? 0.9776 0.6740 0.5286 -0.0368 0.0741  -0.1493 12  SER A C   
77   O O   . SER A 12  ? 0.9187 0.6208 0.4942 -0.0415 0.0595  -0.1511 12  SER A O   
78   C CB  . SER A 12  ? 0.9630 0.6711 0.4436 -0.0627 0.0393  -0.1400 12  SER A CB  
79   O OG  . SER A 12  ? 1.0867 0.8193 0.5639 -0.0640 0.0145  -0.1209 12  SER A OG  
80   N N   . ALA A 13  ? 0.9812 0.6470 0.5119 -0.0292 0.1078  -0.1616 13  ALA A N   
81   C CA  . ALA A 13  ? 0.9179 0.5485 0.4501 -0.0247 0.1278  -0.1773 13  ALA A CA  
82   C C   . ALA A 13  ? 0.9412 0.5893 0.5360 -0.0034 0.1302  -0.1651 13  ALA A C   
83   O O   . ALA A 13  ? 0.9485 0.5675 0.5472 -0.0013 0.1399  -0.1746 13  ALA A O   
84   C CB  . ALA A 13  ? 1.0238 0.6166 0.5200 -0.0174 0.1657  -0.1929 13  ALA A CB  
85   N N   . LYS A 14  ? 0.8394 0.5302 0.4785 0.0107  0.1216  -0.1445 14  LYS A N   
86   C CA  . LYS A 14  ? 0.8387 0.5482 0.5331 0.0289  0.1219  -0.1319 14  LYS A CA  
87   C C   . LYS A 14  ? 0.7509 0.4878 0.4739 0.0207  0.0918  -0.1214 14  LYS A C   
88   O O   . LYS A 14  ? 0.7412 0.4941 0.5062 0.0328  0.0900  -0.1106 14  LYS A O   
89   C CB  . LYS A 14  ? 0.8249 0.5639 0.5510 0.0494  0.1353  -0.1173 14  LYS A CB  
90   C CG  . LYS A 14  ? 0.9012 0.6212 0.6157 0.0641  0.1696  -0.1262 14  LYS A CG  
91   C CD  . LYS A 14  ? 0.8637 0.6235 0.6209 0.0833  0.1807  -0.1105 14  LYS A CD  
92   C CE  . LYS A 14  ? 0.9678 0.7165 0.7199 0.0998  0.2165  -0.1194 14  LYS A CE  
93   N NZ  . LYS A 14  ? 0.9400 0.6483 0.6901 0.1142  0.2334  -0.1310 14  LYS A NZ  
94   N N   . VAL A 15  ? 0.8092 0.5534 0.5108 0.0010  0.0686  -0.1242 15  VAL A N   
95   C CA  . VAL A 15  ? 0.7517 0.5249 0.4831 -0.0055 0.0416  -0.1157 15  VAL A CA  
96   C C   . VAL A 15  ? 0.7779 0.5329 0.5127 -0.0167 0.0405  -0.1275 15  VAL A C   
97   O O   . VAL A 15  ? 0.8310 0.5605 0.5288 -0.0356 0.0398  -0.1440 15  VAL A O   
98   C CB  . VAL A 15  ? 0.8084 0.6003 0.5195 -0.0192 0.0162  -0.1123 15  VAL A CB  
99   C CG1 . VAL A 15  ? 0.6889 0.5136 0.4362 -0.0229 -0.0096 -0.1044 15  VAL A CG1 
100  C CG2 . VAL A 15  ? 0.7050 0.5078 0.4075 -0.0099 0.0190  -0.0994 15  VAL A CG2 
101  N N   . ILE A 16  ? 0.6613 0.4275 0.4370 -0.0076 0.0408  -0.1192 16  ILE A N   
102  C CA  . ILE A 16  ? 0.7555 0.5032 0.5352 -0.0194 0.0416  -0.1284 16  ILE A CA  
103  C C   . ILE A 16  ? 0.7027 0.4850 0.5076 -0.0339 0.0172  -0.1256 16  ILE A C   
104  O O   . ILE A 16  ? 0.7042 0.4754 0.5104 -0.0499 0.0163  -0.1347 16  ILE A O   
105  C CB  . ILE A 16  ? 0.7140 0.4445 0.5163 -0.0015 0.0603  -0.1218 16  ILE A CB  
106  C CG1 . ILE A 16  ? 0.7214 0.4906 0.5661 0.0153  0.0538  -0.1021 16  ILE A CG1 
107  C CG2 . ILE A 16  ? 0.6961 0.3886 0.4744 0.0128  0.0866  -0.1279 16  ILE A CG2 
108  C CD1 . ILE A 16  ? 0.7399 0.4975 0.6065 0.0311  0.0669  -0.0932 16  ILE A CD1 
109  N N   . GLN A 17  ? 0.6652 0.4878 0.4906 -0.0286 -0.0008 -0.1134 17  GLN A N   
110  C CA  . GLN A 17  ? 0.6614 0.5201 0.5099 -0.0406 -0.0243 -0.1119 17  GLN A CA  
111  C C   . GLN A 17  ? 0.6789 0.5659 0.5258 -0.0352 -0.0434 -0.1019 17  GLN A C   
112  O O   . GLN A 17  ? 0.6642 0.5566 0.5188 -0.0179 -0.0393 -0.0890 17  GLN A O   
113  C CB  . GLN A 17  ? 0.6444 0.5230 0.5377 -0.0339 -0.0235 -0.1036 17  GLN A CB  
114  C CG  . GLN A 17  ? 0.6221 0.5450 0.5460 -0.0412 -0.0454 -0.1009 17  GLN A CG  
115  C CD  . GLN A 17  ? 0.6626 0.6010 0.6251 -0.0401 -0.0408 -0.0973 17  GLN A CD  
116  O OE1 . GLN A 17  ? 0.7112 0.6251 0.6709 -0.0469 -0.0259 -0.1025 17  GLN A OE1 
117  N NE2 . GLN A 17  ? 0.6163 0.5923 0.6122 -0.0314 -0.0524 -0.0882 17  GLN A NE2 
118  N N   . GLY A 18  ? 0.7042 0.6086 0.5404 -0.0510 -0.0648 -0.1071 18  GLY A N   
119  C CA  . GLY A 18  ? 0.6514 0.5793 0.4818 -0.0460 -0.0858 -0.0963 18  GLY A CA  
120  C C   . GLY A 18  ? 0.7712 0.6736 0.5457 -0.0536 -0.0855 -0.1010 18  GLY A C   
121  O O   . GLY A 18  ? 0.8379 0.7074 0.5767 -0.0670 -0.0718 -0.1166 18  GLY A O   
122  N N   . SER A 19  ? 0.8038 0.7175 0.5669 -0.0451 -0.0993 -0.0873 19  SER A N   
123  C CA  . SER A 19  ? 0.8109 0.7014 0.5167 -0.0531 -0.0999 -0.0894 19  SER A CA  
124  C C   . SER A 19  ? 0.8913 0.7831 0.5919 -0.0367 -0.1010 -0.0705 19  SER A C   
125  O O   . SER A 19  ? 0.8530 0.7705 0.5814 -0.0257 -0.1197 -0.0554 19  SER A O   
126  C CB  . SER A 19  ? 0.8336 0.7375 0.5131 -0.0736 -0.1282 -0.0952 19  SER A CB  
127  O OG  . SER A 19  ? 1.0566 0.9378 0.6756 -0.0816 -0.1308 -0.0949 19  SER A OG  
128  N N   . LEU A 20  ? 0.9058 0.7685 0.5712 -0.0352 -0.0792 -0.0718 20  LEU A N   
129  C CA  . LEU A 20  ? 0.9555 0.8154 0.6069 -0.0254 -0.0791 -0.0547 20  LEU A CA  
130  C C   . LEU A 20  ? 0.9804 0.8451 0.5978 -0.0323 -0.1082 -0.0448 20  LEU A C   
131  O O   . LEU A 20  ? 0.9878 0.8542 0.6025 -0.0224 -0.1171 -0.0264 20  LEU A O   
132  C CB  . LEU A 20  ? 0.8785 0.7103 0.4976 -0.0261 -0.0483 -0.0601 20  LEU A CB  
133  C CG  . LEU A 20  ? 0.8439 0.6731 0.4971 -0.0151 -0.0196 -0.0662 20  LEU A CG  
134  C CD1 . LEU A 20  ? 0.9495 0.7561 0.5711 -0.0155 0.0103  -0.0729 20  LEU A CD1 
135  C CD2 . LEU A 20  ? 0.7643 0.6162 0.4673 0.0004  -0.0213 -0.0507 20  LEU A CD2 
136  N N   . ASP A 21  ? 1.0243 0.8891 0.6130 -0.0501 -0.1242 -0.0561 21  ASP A N   
137  C CA  . ASP A 21  ? 1.1535 1.0263 0.7085 -0.0572 -0.1559 -0.0455 21  ASP A CA  
138  C C   . ASP A 21  ? 1.1476 1.0591 0.7521 -0.0423 -0.1848 -0.0291 21  ASP A C   
139  O O   . ASP A 21  ? 1.3016 1.2165 0.8914 -0.0340 -0.2057 -0.0100 21  ASP A O   
140  C CB  . ASP A 21  ? 1.2702 1.1373 0.7835 -0.0830 -0.1671 -0.0634 21  ASP A CB  
141  C CG  . ASP A 21  ? 1.3523 1.1756 0.8112 -0.0968 -0.1362 -0.0814 21  ASP A CG  
142  O OD1 . ASP A 21  ? 1.3206 1.1213 0.7566 -0.0890 -0.1148 -0.0749 21  ASP A OD1 
143  O OD2 . ASP A 21  ? 1.4651 1.2760 0.9043 -0.1159 -0.1317 -0.1027 21  ASP A OD2 
144  N N   . SER A 22  ? 1.0699 1.0088 0.7323 -0.0380 -0.1849 -0.0358 22  SER A N   
145  C CA  . SER A 22  ? 1.0095 0.9886 0.7238 -0.0235 -0.2087 -0.0233 22  SER A CA  
146  C C   . SER A 22  ? 0.9968 0.9716 0.7373 0.0012  -0.2010 -0.0055 22  SER A C   
147  O O   . SER A 22  ? 0.9974 0.9995 0.7769 0.0169  -0.2187 0.0063  22  SER A O   
148  C CB  . SER A 22  ? 0.9392 0.9473 0.7042 -0.0297 -0.2068 -0.0378 22  SER A CB  
149  O OG  . SER A 22  ? 0.9751 0.9651 0.7599 -0.0255 -0.1753 -0.0458 22  SER A OG  
150  N N   . LEU A 23  ? 0.9529 0.8952 0.6736 0.0043  -0.1748 -0.0039 23  LEU A N   
151  C CA  . LEU A 23  ? 0.8961 0.8314 0.6376 0.0228  -0.1665 0.0111  23  LEU A CA  
152  C C   . LEU A 23  ? 0.9520 0.8700 0.6560 0.0294  -0.1822 0.0312  23  LEU A C   
153  O O   . LEU A 23  ? 0.9848 0.8848 0.6342 0.0172  -0.1880 0.0325  23  LEU A O   
154  C CB  . LEU A 23  ? 0.8283 0.7417 0.5673 0.0214  -0.1332 0.0052  23  LEU A CB  
155  C CG  . LEU A 23  ? 0.8161 0.7395 0.5903 0.0186  -0.1157 -0.0109 23  LEU A CG  
156  C CD1 . LEU A 23  ? 0.8494 0.7540 0.6186 0.0193  -0.0858 -0.0138 23  LEU A CD1 
157  C CD2 . LEU A 23  ? 0.7912 0.7411 0.6209 0.0299  -0.1228 -0.0082 23  LEU A CD2 
158  N N   . PRO A 24  ? 0.9275 0.8462 0.6557 0.0482  -0.1884 0.0471  24  PRO A N   
159  C CA  . PRO A 24  ? 0.8608 0.7519 0.5489 0.0551  -0.1990 0.0680  24  PRO A CA  
160  C C   . PRO A 24  ? 0.9054 0.7597 0.5454 0.0421  -0.1743 0.0680  24  PRO A C   
161  O O   . PRO A 24  ? 0.9049 0.7572 0.5589 0.0361  -0.1471 0.0561  24  PRO A O   
162  C CB  . PRO A 24  ? 0.8800 0.7719 0.6085 0.0774  -0.2003 0.0801  24  PRO A CB  
163  C CG  . PRO A 24  ? 0.8984 0.8313 0.6887 0.0832  -0.2026 0.0673  24  PRO A CG  
164  C CD  . PRO A 24  ? 0.8471 0.7874 0.6362 0.0636  -0.1854 0.0466  24  PRO A CD  
165  N N   . GLN A 25  ? 0.9484 0.7753 0.5316 0.0377  -0.1843 0.0824  25  GLN A N   
166  C CA  . GLN A 25  ? 1.0227 0.8173 0.5545 0.0218  -0.1606 0.0818  25  GLN A CA  
167  C C   . GLN A 25  ? 0.9689 0.7562 0.5263 0.0231  -0.1301 0.0794  25  GLN A C   
168  O O   . GLN A 25  ? 0.9645 0.7557 0.5253 0.0128  -0.1044 0.0647  25  GLN A O   
169  C CB  . GLN A 25  ? 1.1812 0.9424 0.6515 0.0200  -0.1757 0.1033  25  GLN A CB  
170  C CG  . GLN A 25  ? 1.2930 1.0212 0.7053 0.0007  -0.1501 0.1030  25  GLN A CG  
171  C CD  . GLN A 25  ? 1.4208 1.1112 0.7667 -0.0028 -0.1649 0.1259  25  GLN A CD  
172  O OE1 . GLN A 25  ? 1.4531 1.1207 0.7980 0.0084  -0.1700 0.1456  25  GLN A OE1 
173  N NE2 . GLN A 25  ? 1.5635 1.2425 0.8489 -0.0192 -0.1716 0.1238  25  GLN A NE2 
174  N N   . GLU A 26  ? 0.9818 0.7582 0.5574 0.0360  -0.1330 0.0939  26  GLU A N   
175  C CA  . GLU A 26  ? 0.9207 0.6891 0.5148 0.0334  -0.1066 0.0928  26  GLU A CA  
176  C C   . GLU A 26  ? 0.8670 0.6675 0.5173 0.0358  -0.0929 0.0754  26  GLU A C   
177  O O   . GLU A 26  ? 0.8602 0.6622 0.5226 0.0291  -0.0693 0.0705  26  GLU A O   
178  C CB  . GLU A 26  ? 0.9694 0.7133 0.5660 0.0452  -0.1136 0.1106  26  GLU A CB  
179  C CG  . GLU A 26  ? 1.0368 0.7385 0.5713 0.0409  -0.1215 0.1305  26  GLU A CG  
180  C CD  . GLU A 26  ? 1.0780 0.7617 0.5687 0.0176  -0.0964 0.1287  26  GLU A CD  
181  O OE1 . GLU A 26  ? 1.0442 0.7372 0.5577 0.0085  -0.0709 0.1197  26  GLU A OE1 
182  O OE2 . GLU A 26  ? 1.2304 0.8932 0.6640 0.0079  -0.1022 0.1363  26  GLU A OE2 
183  N N   . VAL A 27  ? 0.8443 0.6717 0.5288 0.0443  -0.1076 0.0667  27  VAL A N   
184  C CA  . VAL A 27  ? 0.8229 0.6758 0.5528 0.0444  -0.0942 0.0507  27  VAL A CA  
185  C C   . VAL A 27  ? 0.7541 0.6085 0.4668 0.0314  -0.0761 0.0366  27  VAL A C   
186  O O   . VAL A 27  ? 0.6835 0.5457 0.4182 0.0298  -0.0549 0.0287  27  VAL A O   
187  C CB  . VAL A 27  ? 0.8042 0.6842 0.5728 0.0540  -0.1128 0.0451  27  VAL A CB  
188  C CG1 . VAL A 27  ? 0.7177 0.6180 0.5255 0.0519  -0.0979 0.0295  27  VAL A CG1 
189  C CG2 . VAL A 27  ? 0.7235 0.6028 0.5139 0.0706  -0.1265 0.0580  27  VAL A CG2 
190  N N   . ARG A 28  ? 0.7976 0.6438 0.4695 0.0225  -0.0842 0.0332  28  ARG A N   
191  C CA  . ARG A 28  ? 0.8495 0.6910 0.5002 0.0108  -0.0644 0.0179  28  ARG A CA  
192  C C   . ARG A 28  ? 0.7340 0.5634 0.3697 0.0058  -0.0371 0.0206  28  ARG A C   
193  O O   . ARG A 28  ? 0.7944 0.6325 0.4496 0.0057  -0.0139 0.0098  28  ARG A O   
194  C CB  . ARG A 28  ? 0.7917 0.6218 0.3924 -0.0006 -0.0785 0.0137  28  ARG A CB  
195  C CG  . ARG A 28  ? 0.9608 0.7814 0.5376 -0.0124 -0.0566 -0.0056 28  ARG A CG  
196  C CD  . ARG A 28  ? 1.0333 0.8335 0.5442 -0.0280 -0.0653 -0.0088 28  ARG A CD  
197  N NE  . ARG A 28  ? 1.0813 0.8663 0.5661 -0.0387 -0.0394 -0.0290 28  ARG A NE  
198  C CZ  . ARG A 28  ? 1.0906 0.8725 0.5662 -0.0477 -0.0427 -0.0470 28  ARG A CZ  
199  N NH1 . ARG A 28  ? 1.1147 0.9137 0.6060 -0.0502 -0.0721 -0.0476 28  ARG A NH1 
200  N NH2 . ARG A 28  ? 1.0899 0.8510 0.5404 -0.0549 -0.0145 -0.0656 28  ARG A NH2 
201  N N   . LYS A 29  ? 0.7876 0.5975 0.3893 0.0015  -0.0391 0.0357  29  LYS A N   
202  C CA  . LYS A 29  ? 0.8309 0.6332 0.4207 -0.0065 -0.0126 0.0389  29  LYS A CA  
203  C C   . LYS A 29  ? 0.7960 0.6205 0.4406 0.0000  0.0016  0.0369  29  LYS A C   
204  O O   . LYS A 29  ? 0.7930 0.6303 0.4502 -0.0035 0.0263  0.0297  29  LYS A O   
205  C CB  . LYS A 29  ? 0.9108 0.6852 0.4587 -0.0128 -0.0192 0.0579  29  LYS A CB  
206  C CG  . LYS A 29  ? 1.0008 0.7509 0.4870 -0.0202 -0.0351 0.0635  29  LYS A CG  
207  C CD  . LYS A 29  ? 1.0775 0.7940 0.5185 -0.0270 -0.0378 0.0843  29  LYS A CD  
208  C CE  . LYS A 29  ? 1.2311 0.9238 0.6173 -0.0281 -0.0655 0.0962  29  LYS A CE  
209  N NZ  . LYS A 29  ? 1.4488 1.1370 0.7875 -0.0430 -0.0592 0.0840  29  LYS A NZ  
210  N N   . PHE A 30  ? 0.7817 0.6124 0.4595 0.0099  -0.0139 0.0435  30  PHE A N   
211  C CA  . PHE A 30  ? 0.6906 0.5405 0.4150 0.0140  -0.0031 0.0421  30  PHE A CA  
212  C C   . PHE A 30  ? 0.6787 0.5522 0.4357 0.0188  0.0077  0.0273  30  PHE A C   
213  O O   . PHE A 30  ? 0.6418 0.5323 0.4233 0.0183  0.0255  0.0248  30  PHE A O   
214  C CB  . PHE A 30  ? 0.7142 0.5618 0.4620 0.0236  -0.0211 0.0497  30  PHE A CB  
215  C CG  . PHE A 30  ? 0.6461 0.5110 0.4362 0.0258  -0.0123 0.0475  30  PHE A CG  
216  C CD1 . PHE A 30  ? 0.6365 0.5041 0.4284 0.0154  0.0043  0.0515  30  PHE A CD1 
217  C CD2 . PHE A 30  ? 0.5964 0.4761 0.4229 0.0359  -0.0210 0.0417  30  PHE A CD2 
218  C CE1 . PHE A 30  ? 0.6619 0.5468 0.4892 0.0153  0.0096  0.0500  30  PHE A CE1 
219  C CE2 . PHE A 30  ? 0.5803 0.4736 0.4392 0.0362  -0.0137 0.0402  30  PHE A CE2 
220  C CZ  . PHE A 30  ? 0.5907 0.4865 0.4491 0.0260  0.0003  0.0446  30  PHE A CZ  
221  N N   . VAL A 31  ? 0.6578 0.5323 0.4150 0.0231  -0.0034 0.0180  31  VAL A N   
222  C CA  . VAL A 31  ? 0.7200 0.6077 0.5024 0.0273  0.0070  0.0043  31  VAL A CA  
223  C C   . VAL A 31  ? 0.7055 0.5890 0.4681 0.0231  0.0308  -0.0040 31  VAL A C   
224  O O   . VAL A 31  ? 0.6180 0.5159 0.4076 0.0286  0.0490  -0.0078 31  VAL A O   
225  C CB  . VAL A 31  ? 0.7091 0.5962 0.4932 0.0287  -0.0106 -0.0042 31  VAL A CB  
226  C CG1 . VAL A 31  ? 0.6610 0.5508 0.4600 0.0305  0.0026  -0.0187 31  VAL A CG1 
227  C CG2 . VAL A 31  ? 0.6413 0.5396 0.4557 0.0356  -0.0294 0.0027  31  VAL A CG2 
228  N N   . GLU A 32  ? 0.7396 0.6040 0.4543 0.0141  0.0313  -0.0067 32  GLU A N   
229  C CA  . GLU A 32  ? 0.7835 0.6410 0.4758 0.0103  0.0569  -0.0175 32  GLU A CA  
230  C C   . GLU A 32  ? 0.7639 0.6352 0.4667 0.0090  0.0796  -0.0109 32  GLU A C   
231  O O   . GLU A 32  ? 0.8000 0.6830 0.5188 0.0144  0.1039  -0.0191 32  GLU A O   
232  C CB  . GLU A 32  ? 0.8187 0.6503 0.4503 -0.0021 0.0518  -0.0222 32  GLU A CB  
233  C CG  . GLU A 32  ? 0.9466 0.7672 0.5653 -0.0045 0.0395  -0.0363 32  GLU A CG  
234  C CD  . GLU A 32  ? 0.9957 0.7904 0.5493 -0.0194 0.0398  -0.0440 32  GLU A CD  
235  O OE1 . GLU A 32  ? 0.9249 0.7097 0.4410 -0.0276 0.0350  -0.0326 32  GLU A OE1 
236  O OE2 . GLU A 32  ? 1.0654 0.8459 0.6009 -0.0245 0.0454  -0.0617 32  GLU A OE2 
237  N N   . GLY A 33  ? 0.7747 0.6450 0.4697 0.0019  0.0726  0.0038  33  GLY A N   
238  C CA  . GLY A 33  ? 0.7146 0.6005 0.4195 -0.0042 0.0937  0.0100  33  GLY A CA  
239  C C   . GLY A 33  ? 0.6840 0.6042 0.4472 0.0060  0.1037  0.0084  33  GLY A C   
240  O O   . GLY A 33  ? 0.6932 0.6357 0.4730 0.0065  0.1276  0.0053  33  GLY A O   
241  N N   . ASN A 34  ? 0.6589 0.5859 0.4543 0.0144  0.0856  0.0112  34  ASN A N   
242  C CA  . ASN A 34  ? 0.6271 0.5847 0.4733 0.0234  0.0916  0.0113  34  ASN A CA  
243  C C   . ASN A 34  ? 0.6475 0.6099 0.5102 0.0377  0.1021  -0.0006 34  ASN A C   
244  O O   . ASN A 34  ? 0.6789 0.6678 0.5773 0.0467  0.1151  -0.0004 34  ASN A O   
245  C CB  . ASN A 34  ? 0.5884 0.5473 0.4568 0.0254  0.0705  0.0181  34  ASN A CB  
246  C CG  . ASN A 34  ? 0.5737 0.5283 0.4332 0.0127  0.0651  0.0299  34  ASN A CG  
247  O OD1 . ASN A 34  ? 0.6293 0.6056 0.5074 0.0053  0.0749  0.0350  34  ASN A OD1 
248  N ND2 . ASN A 34  ? 0.6207 0.5468 0.4519 0.0100  0.0490  0.0347  34  ASN A ND2 
249  N N   . ALA A 35  ? 0.6862 0.6225 0.5230 0.0396  0.0959  -0.0105 35  ALA A N   
250  C CA  . ALA A 35  ? 0.6717 0.6016 0.5127 0.0505  0.1101  -0.0236 35  ALA A CA  
251  C C   . ALA A 35  ? 0.7159 0.6551 0.5535 0.0535  0.1395  -0.0283 35  ALA A C   
252  O O   . ALA A 35  ? 0.6912 0.6454 0.5599 0.0685  0.1558  -0.0316 35  ALA A O   
253  C CB  . ALA A 35  ? 0.6692 0.5668 0.4727 0.0451  0.0997  -0.0349 35  ALA A CB  
254  N N   . GLN A 36  ? 0.7164 0.6469 0.5160 0.0401  0.1473  -0.0280 36  GLN A N   
255  C CA  . GLN A 36  ? 0.7431 0.6853 0.5385 0.0407  0.1783  -0.0330 36  GLN A CA  
256  C C   . GLN A 36  ? 0.6364 0.6247 0.4835 0.0458  0.1890  -0.0229 36  GLN A C   
257  O O   . GLN A 36  ? 0.6625 0.6736 0.5326 0.0564  0.2149  -0.0278 36  GLN A O   
258  C CB  . GLN A 36  ? 0.7858 0.7074 0.5248 0.0213  0.1828  -0.0326 36  GLN A CB  
259  C CG  . GLN A 36  ? 0.8887 0.7688 0.5739 0.0136  0.1674  -0.0407 36  GLN A CG  
260  C CD  . GLN A 36  ? 1.0400 0.8992 0.6678 -0.0060 0.1631  -0.0346 36  GLN A CD  
261  O OE1 . GLN A 36  ? 1.0651 0.9364 0.6935 -0.0151 0.1680  -0.0222 36  GLN A OE1 
262  N NE2 . GLN A 36  ? 1.0918 0.9180 0.6668 -0.0143 0.1532  -0.0426 36  GLN A NE2 
263  N N   . LEU A 37  ? 0.6557 0.6596 0.5225 0.0383  0.1697  -0.0093 37  LEU A N   
264  C CA  . LEU A 37  ? 0.6295 0.6792 0.5433 0.0386  0.1763  0.0003  37  LEU A CA  
265  C C   . LEU A 37  ? 0.6279 0.7008 0.5915 0.0591  0.1726  0.0010  37  LEU A C   
266  O O   . LEU A 37  ? 0.5644 0.6760 0.5674 0.0698  0.1888  0.0027  37  LEU A O   
267  C CB  . LEU A 37  ? 0.6927 0.7434 0.6019 0.0204  0.1581  0.0131  37  LEU A CB  
268  C CG  . LEU A 37  ? 0.6310 0.7274 0.5866 0.0158  0.1589  0.0228  37  LEU A CG  
269  C CD1 . LEU A 37  ? 0.5897 0.7207 0.5555 0.0060  0.1849  0.0236  37  LEU A CD1 
270  C CD2 . LEU A 37  ? 0.6902 0.7742 0.6374 0.0003  0.1374  0.0327  37  LEU A CD2 
271  N N   . CYS A 38  ? 0.6045 0.6557 0.5676 0.0649  0.1514  0.0008  38  CYS A N   
272  C CA  . CYS A 38  ? 0.6202 0.6866 0.6232 0.0818  0.1452  0.0036  38  CYS A CA  
273  C C   . CYS A 38  ? 0.6193 0.6688 0.6233 0.1019  0.1596  -0.0070 38  CYS A C   
274  O O   . CYS A 38  ? 0.6054 0.6722 0.6454 0.1198  0.1622  -0.0030 38  CYS A O   
275  C CB  . CYS A 38  ? 0.5599 0.6095 0.5601 0.0768  0.1188  0.0078  38  CYS A CB  
276  S SG  . CYS A 38  ? 0.5822 0.6420 0.5794 0.0557  0.1030  0.0194  38  CYS A SG  
277  N N   A GLN A 39  ? 0.6232 0.6363 0.5855 0.0989  0.1686  -0.0202 39  GLN A N   
278  N N   B GLN A 39  ? 0.6389 0.6518 0.6012 0.0989  0.1684  -0.0201 39  GLN A N   
279  C CA  A GLN A 39  ? 0.6777 0.6656 0.6324 0.1153  0.1856  -0.0330 39  GLN A CA  
280  C CA  B GLN A 39  ? 0.6768 0.6649 0.6317 0.1153  0.1856  -0.0329 39  GLN A CA  
281  C C   A GLN A 39  ? 0.6646 0.6345 0.6328 0.1261  0.1717  -0.0325 39  GLN A C   
282  C C   B GLN A 39  ? 0.6651 0.6349 0.6333 0.1261  0.1718  -0.0325 39  GLN A C   
283  O O   A GLN A 39  ? 0.6545 0.6309 0.6518 0.1469  0.1818  -0.0304 39  GLN A O   
284  O O   B GLN A 39  ? 0.6540 0.6299 0.6509 0.1469  0.1819  -0.0305 39  GLN A O   
285  C CB  A GLN A 39  ? 0.6700 0.6878 0.6557 0.1332  0.2138  -0.0333 39  GLN A CB  
286  C CB  B GLN A 39  ? 0.6719 0.6905 0.6582 0.1330  0.2135  -0.0330 39  GLN A CB  
287  C CG  A GLN A 39  ? 0.6813 0.7101 0.6470 0.1223  0.2356  -0.0383 39  GLN A CG  
288  C CG  B GLN A 39  ? 0.6729 0.7112 0.6463 0.1207  0.2321  -0.0346 39  GLN A CG  
289  C CD  A GLN A 39  ? 0.7496 0.7296 0.6581 0.1167  0.2499  -0.0564 39  GLN A CD  
290  C CD  B GLN A 39  ? 0.6763 0.7485 0.6847 0.1397  0.2632  -0.0367 39  GLN A CD  
291  O OE1 A GLN A 39  ? 0.8082 0.7540 0.7049 0.1295  0.2573  -0.0682 39  GLN A OE1 
292  O OE1 B GLN A 39  ? 0.6479 0.7718 0.7090 0.1483  0.2628  -0.0243 39  GLN A OE1 
293  N NE2 A GLN A 39  ? 0.7399 0.7130 0.6081 0.0956  0.2535  -0.0585 39  GLN A NE2 
294  N NE2 B GLN A 39  ? 0.7106 0.7554 0.6900 0.1464  0.2904  -0.0529 39  GLN A NE2 
295  N N   . PRO A 40  ? 0.6556 0.6035 0.6043 0.1131  0.1493  -0.0335 40  PRO A N   
296  C CA  . PRO A 40  ? 0.6782 0.6054 0.6346 0.1200  0.1394  -0.0348 40  PRO A CA  
297  C C   . PRO A 40  ? 0.7080 0.5913 0.6345 0.1244  0.1539  -0.0513 40  PRO A C   
298  O O   . PRO A 40  ? 0.6725 0.5363 0.5622 0.1157  0.1638  -0.0636 40  PRO A O   
299  C CB  . PRO A 40  ? 0.6086 0.5322 0.5544 0.1024  0.1136  -0.0319 40  PRO A CB  
300  C CG  . PRO A 40  ? 0.6753 0.5954 0.5886 0.0878  0.1123  -0.0356 40  PRO A CG  
301  C CD  . PRO A 40  ? 0.6486 0.5910 0.5693 0.0925  0.1324  -0.0323 40  PRO A CD  
302  N N   A GLU A 41  ? 0.6727 0.5366 0.6110 0.1368  0.1554  -0.0516 41  GLU A N   
303  N N   B GLU A 41  ? 0.6730 0.5365 0.6109 0.1366  0.1555  -0.0518 41  GLU A N   
304  C CA  A GLU A 41  ? 0.7376 0.5515 0.6445 0.1391  0.1694  -0.0681 41  GLU A CA  
305  C CA  B GLU A 41  ? 0.7384 0.5521 0.6442 0.1388  0.1698  -0.0685 41  GLU A CA  
306  C C   A GLU A 41  ? 0.7590 0.5456 0.6292 0.1147  0.1532  -0.0794 41  GLU A C   
307  C C   B GLU A 41  ? 0.7592 0.5455 0.6291 0.1145  0.1532  -0.0796 41  GLU A C   
308  O O   A GLU A 41  ? 0.8037 0.5532 0.6341 0.1063  0.1633  -0.0965 41  GLU A O   
309  O O   B GLU A 41  ? 0.8043 0.5530 0.6344 0.1061  0.1631  -0.0967 41  GLU A O   
310  C CB  A GLU A 41  ? 0.7275 0.5234 0.6551 0.1591  0.1757  -0.0631 41  GLU A CB  
311  C CB  B GLU A 41  ? 0.7255 0.5203 0.6514 0.1597  0.1780  -0.0642 41  GLU A CB  
312  C CG  A GLU A 41  ? 0.8126 0.5486 0.7059 0.1624  0.1933  -0.0801 41  GLU A CG  
313  C CG  B GLU A 41  ? 0.8118 0.5468 0.7019 0.1630  0.1968  -0.0821 41  GLU A CG  
314  C CD  A GLU A 41  ? 0.8330 0.5561 0.7124 0.1764  0.2232  -0.0917 41  GLU A CD  
315  C CD  B GLU A 41  ? 0.7986 0.5065 0.7041 0.1844  0.2044  -0.0758 41  GLU A CD  
316  O OE1 A GLU A 41  ? 0.8363 0.6027 0.7401 0.1858  0.2310  -0.0843 41  GLU A OE1 
317  O OE1 B GLU A 41  ? 0.7914 0.5320 0.7370 0.1986  0.1951  -0.0565 41  GLU A OE1 
318  O OE2 A GLU A 41  ? 0.9466 0.6154 0.7894 0.1765  0.2404  -0.1091 41  GLU A OE2 
319  O OE2 B GLU A 41  ? 0.9087 0.5594 0.7825 0.1858  0.2193  -0.0899 41  GLU A OE2 
320  N N   . TYR A 42  ? 0.6813 0.4873 0.5648 0.1026  0.1286  -0.0708 42  TYR A N   
321  C CA  . TYR A 42  ? 0.6834 0.4749 0.5425 0.0809  0.1108  -0.0795 42  TYR A CA  
322  C C   . TYR A 42  ? 0.7021 0.5287 0.5732 0.0711  0.0889  -0.0689 42  TYR A C   
323  O O   . TYR A 42  ? 0.6428 0.4991 0.5431 0.0791  0.0858  -0.0548 42  TYR A O   
324  C CB  . TYR A 42  ? 0.6866 0.4559 0.5514 0.0774  0.1056  -0.0822 42  TYR A CB  
325  C CG  . TYR A 42  ? 0.7938 0.5176 0.6420 0.0868  0.1272  -0.0923 42  TYR A CG  
326  C CD1 . TYR A 42  ? 0.7944 0.4799 0.5996 0.0769  0.1391  -0.1114 42  TYR A CD1 
327  C CD2 . TYR A 42  ? 0.7731 0.4884 0.6449 0.1053  0.1354  -0.0825 42  TYR A CD2 
328  C CE1 . TYR A 42  ? 0.9313 0.5673 0.7176 0.0860  0.1613  -0.1219 42  TYR A CE1 
329  C CE2 . TYR A 42  ? 0.7787 0.4460 0.6338 0.1168  0.1559  -0.0904 42  TYR A CE2 
330  C CZ  . TYR A 42  ? 0.8604 0.4863 0.6728 0.1074  0.1700  -0.1109 42  TYR A CZ  
331  O OH  . TYR A 42  ? 0.9852 0.5557 0.7774 0.1192  0.1927  -0.1201 42  TYR A OH  
332  N N   . ILE A 43  ? 0.6668 0.4887 0.5142 0.0536  0.0731  -0.0757 43  ILE A N   
333  C CA  . ILE A 43  ? 0.6357 0.4848 0.4928 0.0463  0.0512  -0.0662 43  ILE A CA  
334  C C   . ILE A 43  ? 0.6553 0.5047 0.5178 0.0343  0.0334  -0.0710 43  ILE A C   
335  O O   . ILE A 43  ? 0.6504 0.4809 0.4873 0.0212  0.0307  -0.0843 43  ILE A O   
336  C CB  . ILE A 43  ? 0.6146 0.4648 0.4396 0.0386  0.0469  -0.0663 43  ILE A CB  
337  C CG1 . ILE A 43  ? 0.7191 0.5734 0.5416 0.0481  0.0673  -0.0617 43  ILE A CG1 
338  C CG2 . ILE A 43  ? 0.6188 0.4909 0.4530 0.0340  0.0235  -0.0551 43  ILE A CG2 
339  C CD1 . ILE A 43  ? 0.7043 0.5571 0.4917 0.0390  0.0656  -0.0599 43  ILE A CD1 
340  N N   . HIS A 44  ? 0.5504 0.4222 0.4457 0.0371  0.0224  -0.0611 44  HIS A N   
341  C CA  . HIS A 44  ? 0.5623 0.4421 0.4716 0.0269  0.0083  -0.0647 44  HIS A CA  
342  C C   . HIS A 44  ? 0.5536 0.4618 0.4775 0.0268  -0.0104 -0.0558 44  HIS A C   
343  O O   . HIS A 44  ? 0.4977 0.4198 0.4427 0.0360  -0.0103 -0.0447 44  HIS A O   
344  C CB  . HIS A 44  ? 0.5104 0.3864 0.4441 0.0313  0.0162  -0.0621 44  HIS A CB  
345  C CG  . HIS A 44  ? 0.5860 0.4730 0.5365 0.0196  0.0054  -0.0655 44  HIS A CG  
346  N ND1 . HIS A 44  ? 0.5823 0.4491 0.5288 0.0091  0.0117  -0.0745 44  HIS A ND1 
347  C CD2 . HIS A 44  ? 0.5474 0.4636 0.5203 0.0169  -0.0091 -0.0614 44  HIS A CD2 
348  C CE1 . HIS A 44  ? 0.6089 0.4962 0.5757 -0.0017 0.0016  -0.0761 44  HIS A CE1 
349  N NE2 . HIS A 44  ? 0.5502 0.4691 0.5351 0.0044  -0.0108 -0.0684 44  HIS A NE2 
350  N N   . ILE A 45  ? 0.5875 0.5030 0.4988 0.0168  -0.0268 -0.0606 45  ILE A N   
351  C CA  . ILE A 45  ? 0.5263 0.4669 0.4519 0.0197  -0.0458 -0.0516 45  ILE A CA  
352  C C   . ILE A 45  ? 0.5196 0.4817 0.4804 0.0164  -0.0532 -0.0540 45  ILE A C   
353  O O   . ILE A 45  ? 0.5321 0.5011 0.4936 0.0031  -0.0609 -0.0641 45  ILE A O   
354  C CB  . ILE A 45  ? 0.5495 0.4912 0.4454 0.0125  -0.0621 -0.0529 45  ILE A CB  
355  C CG1 . ILE A 45  ? 0.5798 0.4969 0.4356 0.0127  -0.0502 -0.0529 45  ILE A CG1 
356  C CG2 . ILE A 45  ? 0.5275 0.4916 0.4383 0.0208  -0.0815 -0.0404 45  ILE A CG2 
357  C CD1 . ILE A 45  ? 0.6511 0.5645 0.4683 0.0039  -0.0659 -0.0531 45  ILE A CD1 
358  N N   . CYS A 46  ? 0.5596 0.5326 0.5481 0.0263  -0.0497 -0.0457 46  CYS A N   
359  C CA  . CYS A 46  ? 0.4871 0.4794 0.5084 0.0234  -0.0518 -0.0484 46  CYS A CA  
360  C C   . CYS A 46  ? 0.4619 0.4837 0.4991 0.0212  -0.0713 -0.0496 46  CYS A C   
361  O O   . CYS A 46  ? 0.4997 0.5287 0.5323 0.0306  -0.0839 -0.0413 46  CYS A O   
362  C CB  . CYS A 46  ? 0.4059 0.4010 0.4467 0.0339  -0.0437 -0.0396 46  CYS A CB  
363  S SG  . CYS A 46  ? 0.5038 0.4752 0.5337 0.0377  -0.0247 -0.0353 46  CYS A SG  
364  N N   . ASP A 47  ? 0.4797 0.5195 0.5365 0.0088  -0.0740 -0.0591 47  ASP A N   
365  C CA  . ASP A 47  ? 0.4879 0.5669 0.5725 0.0076  -0.0918 -0.0601 47  ASP A CA  
366  C C   . ASP A 47  ? 0.4105 0.5141 0.5374 0.0133  -0.0856 -0.0593 47  ASP A C   
367  O O   . ASP A 47  ? 0.4764 0.6181 0.6350 0.0162  -0.0981 -0.0596 47  ASP A O   
368  C CB  . ASP A 47  ? 0.4996 0.5901 0.5783 -0.0145 -0.1011 -0.0729 47  ASP A CB  
369  C CG  . ASP A 47  ? 0.4783 0.5551 0.5594 -0.0320 -0.0841 -0.0842 47  ASP A CG  
370  O OD1 . ASP A 47  ? 0.5085 0.5771 0.6040 -0.0262 -0.0680 -0.0810 47  ASP A OD1 
371  O OD2 . ASP A 47  ? 0.5638 0.6347 0.6283 -0.0532 -0.0869 -0.0960 47  ASP A OD2 
372  N N   . GLY A 48  ? 0.4255 0.5098 0.5535 0.0150  -0.0666 -0.0583 48  GLY A N   
373  C CA  . GLY A 48  ? 0.4904 0.5919 0.6507 0.0194  -0.0576 -0.0582 48  GLY A CA  
374  C C   . GLY A 48  ? 0.4572 0.5845 0.6441 0.0028  -0.0537 -0.0689 48  GLY A C   
375  O O   . GLY A 48  ? 0.4052 0.5532 0.6220 0.0059  -0.0458 -0.0701 48  GLY A O   
376  N N   . SER A 49  ? 0.4319 0.5566 0.6066 -0.0167 -0.0571 -0.0777 49  SER A N   
377  C CA  . SER A 49  ? 0.4621 0.6126 0.6608 -0.0374 -0.0540 -0.0887 49  SER A CA  
378  C C   . SER A 49  ? 0.4911 0.6165 0.6842 -0.0476 -0.0313 -0.0910 49  SER A C   
379  O O   . SER A 49  ? 0.4610 0.5461 0.6264 -0.0408 -0.0207 -0.0847 49  SER A O   
380  C CB  . SER A 49  ? 0.5086 0.6587 0.6895 -0.0586 -0.0653 -0.0984 49  SER A CB  
381  O OG  . SER A 49  ? 0.4732 0.5704 0.6093 -0.0649 -0.0552 -0.1003 49  SER A OG  
382  N N   . GLU A 50  ? 0.5163 0.6686 0.7368 -0.0645 -0.0243 -0.0992 50  GLU A N   
383  C CA  . GLU A 50  ? 0.5178 0.6437 0.7276 -0.0789 -0.0030 -0.1013 50  GLU A CA  
384  C C   . GLU A 50  ? 0.5967 0.6725 0.7639 -0.0931 0.0019  -0.1037 50  GLU A C   
385  O O   . GLU A 50  ? 0.5524 0.5866 0.6944 -0.0911 0.0160  -0.0978 50  GLU A O   
386  C CB  . GLU A 50  ? 0.5557 0.7222 0.8019 -0.0985 0.0044  -0.1109 50  GLU A CB  
387  C CG  . GLU A 50  ? 0.6337 0.8463 0.9240 -0.0823 0.0062  -0.1094 50  GLU A CG  
388  C CD  . GLU A 50  ? 0.7485 0.9354 1.0279 -0.0718 0.0250  -0.1030 50  GLU A CD  
389  O OE1 . GLU A 50  ? 0.7628 0.9010 1.0032 -0.0771 0.0342  -0.0982 50  GLU A OE1 
390  O OE2 . GLU A 50  ? 0.7330 0.9477 1.0418 -0.0580 0.0303  -0.1029 50  GLU A OE2 
391  N N   . GLU A 51  ? 0.5946 0.6727 0.7520 -0.1070 -0.0096 -0.1124 51  GLU A N   
392  C CA  . GLU A 51  ? 0.6062 0.6315 0.7203 -0.1196 -0.0031 -0.1169 51  GLU A CA  
393  C C   . GLU A 51  ? 0.6356 0.6189 0.7198 -0.0960 0.0016  -0.1060 51  GLU A C   
394  O O   . GLU A 51  ? 0.6656 0.6037 0.7248 -0.0958 0.0163  -0.1024 51  GLU A O   
395  C CB  . GLU A 51  ? 0.6095 0.6450 0.7138 -0.1367 -0.0185 -0.1286 51  GLU A CB  
396  C CG  . GLU A 51  ? 0.7502 0.8274 0.8824 -0.1662 -0.0234 -0.1409 51  GLU A CG  
397  C CD  . GLU A 51  ? 0.7913 0.9386 0.9787 -0.1560 -0.0342 -0.1373 51  GLU A CD  
398  O OE1 . GLU A 51  ? 0.6525 0.8131 0.8501 -0.1272 -0.0429 -0.1267 51  GLU A OE1 
399  O OE2 . GLU A 51  ? 0.8226 1.0109 1.0436 -0.1768 -0.0324 -0.1454 51  GLU A OE2 
400  N N   . GLU A 52  ? 0.5970 0.5959 0.6843 -0.0758 -0.0109 -0.0999 52  GLU A N   
401  C CA  . GLU A 52  ? 0.5295 0.4975 0.5939 -0.0549 -0.0061 -0.0898 52  GLU A CA  
402  C C   . GLU A 52  ? 0.5841 0.5412 0.6541 -0.0444 0.0065  -0.0791 52  GLU A C   
403  O O   . GLU A 52  ? 0.5915 0.5130 0.6397 -0.0370 0.0164  -0.0729 52  GLU A O   
404  C CB  . GLU A 52  ? 0.5327 0.5227 0.6012 -0.0385 -0.0210 -0.0844 52  GLU A CB  
405  C CG  . GLU A 52  ? 0.5291 0.5082 0.5929 -0.0167 -0.0163 -0.0714 52  GLU A CG  
406  C CD  . GLU A 52  ? 0.5067 0.5029 0.5711 -0.0036 -0.0298 -0.0657 52  GLU A CD  
407  O OE1 . GLU A 52  ? 0.4660 0.4513 0.5064 -0.0045 -0.0354 -0.0683 52  GLU A OE1 
408  O OE2 . GLU A 52  ? 0.4938 0.5104 0.5790 0.0070  -0.0337 -0.0589 52  GLU A OE2 
409  N N   . TYR A 53  ? 0.5664 0.5548 0.6652 -0.0434 0.0062  -0.0769 53  TYR A N   
410  C CA  . TYR A 53  ? 0.5705 0.5489 0.6701 -0.0365 0.0174  -0.0678 53  TYR A CA  
411  C C   . TYR A 53  ? 0.6051 0.5486 0.6850 -0.0497 0.0315  -0.0675 53  TYR A C   
412  O O   . TYR A 53  ? 0.6084 0.5249 0.6708 -0.0408 0.0382  -0.0569 53  TYR A O   
413  C CB  . TYR A 53  ? 0.5448 0.5602 0.6762 -0.0357 0.0177  -0.0691 53  TYR A CB  
414  C CG  . TYR A 53  ? 0.5117 0.5179 0.6397 -0.0292 0.0281  -0.0608 53  TYR A CG  
415  C CD1 . TYR A 53  ? 0.5462 0.5365 0.6584 -0.0138 0.0259  -0.0502 53  TYR A CD1 
416  C CD2 . TYR A 53  ? 0.5589 0.5743 0.6981 -0.0408 0.0405  -0.0643 53  TYR A CD2 
417  C CE1 . TYR A 53  ? 0.6048 0.5879 0.7108 -0.0111 0.0333  -0.0432 53  TYR A CE1 
418  C CE2 . TYR A 53  ? 0.5552 0.5599 0.6850 -0.0372 0.0497  -0.0576 53  TYR A CE2 
419  C CZ  . TYR A 53  ? 0.6350 0.6233 0.7473 -0.0228 0.0448  -0.0471 53  TYR A CZ  
420  O OH  . TYR A 53  ? 0.6928 0.6714 0.7925 -0.0224 0.0520  -0.0409 53  TYR A OH  
421  N N   . GLY A 54  ? 0.6151 0.5580 0.6964 -0.0719 0.0353  -0.0782 54  GLY A N   
422  C CA  . GLY A 54  ? 0.6661 0.5689 0.7242 -0.0866 0.0497  -0.0774 54  GLY A CA  
423  C C   . GLY A 54  ? 0.7430 0.5953 0.7664 -0.0779 0.0532  -0.0727 54  GLY A C   
424  O O   . GLY A 54  ? 0.6937 0.5100 0.6969 -0.0732 0.0629  -0.0624 54  GLY A O   
425  N N   . ARG A 55  ? 0.7210 0.5695 0.7359 -0.0748 0.0458  -0.0799 55  ARG A N   
426  C CA  . ARG A 55  ? 0.7083 0.5100 0.6922 -0.0634 0.0519  -0.0770 55  ARG A CA  
427  C C   . ARG A 55  ? 0.7250 0.5265 0.7105 -0.0357 0.0516  -0.0613 55  ARG A C   
428  O O   . ARG A 55  ? 0.7069 0.4720 0.6743 -0.0241 0.0604  -0.0523 55  ARG A O   
429  C CB  . ARG A 55  ? 0.7124 0.5122 0.6842 -0.0677 0.0452  -0.0897 55  ARG A CB  
430  C CG  . ARG A 55  ? 0.8835 0.6765 0.8464 -0.0983 0.0452  -0.1063 55  ARG A CG  
431  C CD  . ARG A 55  ? 0.9726 0.7114 0.9095 -0.1123 0.0623  -0.1075 55  ARG A CD  
432  N NE  . ARG A 55  ? 1.0114 0.7616 0.9647 -0.1201 0.0679  -0.0999 55  ARG A NE  
433  C CZ  . ARG A 55  ? 1.0507 0.7570 0.9827 -0.1334 0.0825  -0.0974 55  ARG A CZ  
434  N NH1 . ARG A 55  ? 1.0259 0.6702 0.9200 -0.1389 0.0933  -0.1018 55  ARG A NH1 
435  N NH2 . ARG A 55  ? 1.0002 0.7210 0.9456 -0.1416 0.0878  -0.0905 55  ARG A NH2 
436  N N   . LEU A 56  ? 0.6581 0.5003 0.6657 -0.0251 0.0412  -0.0573 56  LEU A N   
437  C CA  . LEU A 56  ? 0.5876 0.4351 0.5986 -0.0038 0.0403  -0.0431 56  LEU A CA  
438  C C   . LEU A 56  ? 0.6774 0.5102 0.6843 -0.0026 0.0471  -0.0312 56  LEU A C   
439  O O   . LEU A 56  ? 0.6954 0.5097 0.6922 0.0124  0.0503  -0.0194 56  LEU A O   
440  C CB  . LEU A 56  ? 0.6035 0.4920 0.6359 0.0018  0.0293  -0.0420 56  LEU A CB  
441  C CG  . LEU A 56  ? 0.6587 0.5578 0.6951 0.0189  0.0268  -0.0295 56  LEU A CG  
442  C CD1 . LEU A 56  ? 0.6916 0.5808 0.7167 0.0317  0.0277  -0.0277 56  LEU A CD1 
443  C CD2 . LEU A 56  ? 0.6320 0.5629 0.6863 0.0197  0.0185  -0.0296 56  LEU A CD2 
444  N N   . LEU A 57  ? 0.6816 0.5244 0.6961 -0.0182 0.0495  -0.0336 57  LEU A N   
445  C CA  . LEU A 57  ? 0.6736 0.4995 0.6774 -0.0206 0.0563  -0.0224 57  LEU A CA  
446  C C   . LEU A 57  ? 0.7455 0.5215 0.7218 -0.0210 0.0652  -0.0172 57  LEU A C   
447  O O   . LEU A 57  ? 0.7706 0.5267 0.7337 -0.0086 0.0664  -0.0017 57  LEU A O   
448  C CB  . LEU A 57  ? 0.6482 0.4925 0.6630 -0.0400 0.0611  -0.0288 57  LEU A CB  
449  C CG  . LEU A 57  ? 0.5838 0.4710 0.6240 -0.0362 0.0553  -0.0317 57  LEU A CG  
450  C CD1 . LEU A 57  ? 0.6235 0.5305 0.6789 -0.0546 0.0634  -0.0412 57  LEU A CD1 
451  C CD2 . LEU A 57  ? 0.5237 0.4114 0.5568 -0.0233 0.0525  -0.0185 57  LEU A CD2 
452  N N   . ALA A 58  ? 0.6868 0.4407 0.6530 -0.0354 0.0708  -0.0296 58  ALA A N   
453  C CA  . ALA A 58  ? 0.7901 0.4871 0.7259 -0.0357 0.0812  -0.0260 58  ALA A CA  
454  C C   . ALA A 58  ? 0.7805 0.4593 0.7089 -0.0072 0.0806  -0.0166 58  ALA A C   
455  O O   . ALA A 58  ? 0.8586 0.5017 0.7699 0.0058  0.0859  -0.0024 58  ALA A O   
456  C CB  . ALA A 58  ? 0.8004 0.4777 0.7253 -0.0589 0.0870  -0.0441 58  ALA A CB  
457  N N   . HIS A 59  ? 0.7391 0.4434 0.6809 0.0033  0.0745  -0.0235 59  HIS A N   
458  C CA  . HIS A 59  ? 0.7763 0.4717 0.7162 0.0299  0.0762  -0.0159 59  HIS A CA  
459  C C   . HIS A 59  ? 0.8020 0.5135 0.7528 0.0482  0.0711  0.0046  59  HIS A C   
460  O O   . HIS A 59  ? 0.8237 0.5109 0.7670 0.0678  0.0756  0.0172  59  HIS A O   
461  C CB  . HIS A 59  ? 0.7839 0.5099 0.7356 0.0341  0.0705  -0.0262 59  HIS A CB  
462  C CG  . HIS A 59  ? 0.7998 0.5306 0.7565 0.0600  0.0729  -0.0180 59  HIS A CG  
463  N ND1 . HIS A 59  ? 0.8617 0.5533 0.8033 0.0764  0.0856  -0.0160 59  HIS A ND1 
464  C CD2 . HIS A 59  ? 0.8488 0.6197 0.8253 0.0719  0.0659  -0.0116 59  HIS A CD2 
465  C CE1 . HIS A 59  ? 0.8552 0.5687 0.8114 0.0982  0.0864  -0.0089 59  HIS A CE1 
466  N NE2 . HIS A 59  ? 0.8999 0.6615 0.8763 0.0939  0.0743  -0.0060 59  HIS A NE2 
467  N N   . MET A 60  ? 0.7525 0.5054 0.7211 0.0424  0.0613  0.0081  60  MET A N   
468  C CA  . MET A 60  ? 0.7359 0.5060 0.7116 0.0546  0.0548  0.0262  60  MET A CA  
469  C C   . MET A 60  ? 0.7624 0.4981 0.7175 0.0531  0.0583  0.0397  60  MET A C   
470  O O   . MET A 60  ? 0.7933 0.5272 0.7470 0.0702  0.0540  0.0576  60  MET A O   
471  C CB  . MET A 60  ? 0.7307 0.5430 0.7225 0.0447  0.0460  0.0243  60  MET A CB  
472  C CG  . MET A 60  ? 0.6559 0.5021 0.6659 0.0529  0.0398  0.0199  60  MET A CG  
473  S SD  . MET A 60  ? 0.6397 0.5242 0.6636 0.0433  0.0312  0.0189  60  MET A SD  
474  C CE  . MET A 60  ? 0.5805 0.4670 0.6089 0.0258  0.0339  0.0012  60  MET A CE  
475  N N   . GLN A 61  ? 0.7193 0.4290 0.6581 0.0319  0.0657  0.0322  61  GLN A N   
476  C CA  . GLN A 61  ? 0.8651 0.5335 0.7773 0.0279  0.0710  0.0453  61  GLN A CA  
477  C C   . GLN A 61  ? 0.9370 0.5569 0.8317 0.0474  0.0776  0.0537  61  GLN A C   
478  O O   . GLN A 61  ? 0.8655 0.4586 0.7435 0.0590  0.0765  0.0733  61  GLN A O   
479  C CB  . GLN A 61  ? 0.8503 0.5027 0.7495 -0.0026 0.0802  0.0335  61  GLN A CB  
480  C CG  . GLN A 61  ? 0.8912 0.5043 0.7593 -0.0129 0.0863  0.0475  61  GLN A CG  
481  C CD  . GLN A 61  ? 1.0363 0.6358 0.8936 -0.0458 0.0985  0.0340  61  GLN A CD  
482  O OE1 . GLN A 61  ? 1.0184 0.6341 0.8917 -0.0596 0.1017  0.0145  61  GLN A OE1 
483  N NE2 . GLN A 61  ? 1.0149 0.5870 0.8449 -0.0600 0.1051  0.0450  61  GLN A NE2 
484  N N   . GLU A 62  ? 0.9514 0.5572 0.8475 0.0518  0.0847  0.0394  62  GLU A N   
485  C CA  . GLU A 62  ? 0.9439 0.4992 0.8226 0.0723  0.0945  0.0448  62  GLU A CA  
486  C C   . GLU A 62  ? 0.9428 0.5214 0.8418 0.1067  0.0885  0.0602  62  GLU A C   
487  O O   . GLU A 62  ? 0.9931 0.5355 0.8819 0.1302  0.0937  0.0742  62  GLU A O   
488  C CB  . GLU A 62  ? 0.9346 0.4655 0.8035 0.0633  0.1055  0.0221  62  GLU A CB  
489  C CG  . GLU A 62  ? 0.9394 0.4511 0.7910 0.0272  0.1108  0.0061  62  GLU A CG  
490  C CD  . GLU A 62  ? 0.9162 0.4189 0.7613 0.0145  0.1165  -0.0175 62  GLU A CD  
491  O OE1 . GLU A 62  ? 0.9223 0.4415 0.7779 0.0323  0.1154  -0.0224 62  GLU A OE1 
492  O OE2 . GLU A 62  ? 0.9416 0.4218 0.7698 -0.0153 0.1221  -0.0314 62  GLU A OE2 
493  N N   . GLU A 63  ? 0.9273 0.5658 0.8559 0.1103  0.0783  0.0584  63  GLU A N   
494  C CA  . GLU A 63  ? 0.9361 0.6081 0.8892 0.1382  0.0721  0.0721  63  GLU A CA  
495  C C   . GLU A 63  ? 0.9163 0.6099 0.8747 0.1440  0.0581  0.0952  63  GLU A C   
496  O O   . GLU A 63  ? 0.9626 0.6875 0.9431 0.1664  0.0509  0.1093  63  GLU A O   
497  C CB  . GLU A 63  ? 0.8994 0.6230 0.8775 0.1353  0.0680  0.0600  63  GLU A CB  
498  C CG  . GLU A 63  ? 0.9756 0.6829 0.9466 0.1309  0.0796  0.0386  63  GLU A CG  
499  C CD  . GLU A 63  ? 1.0174 0.7030 0.9886 0.1577  0.0930  0.0392  63  GLU A CD  
500  O OE1 . GLU A 63  ? 1.0805 0.7254 1.0400 0.1739  0.0999  0.0500  63  GLU A OE1 
501  O OE2 . GLU A 63  ? 1.0869 0.7946 1.0688 0.1634  0.0976  0.0294  63  GLU A OE2 
502  N N   . GLY A 64  ? 0.9171 0.5969 0.8553 0.1231  0.0542  0.0992  64  GLY A N   
503  C CA  . GLY A 64  ? 0.9358 0.6365 0.8727 0.1239  0.0400  0.1194  64  GLY A CA  
504  C C   . GLY A 64  ? 0.8221 0.5825 0.7809 0.1141  0.0281  0.1162  64  GLY A C   
505  O O   . GLY A 64  ? 0.8806 0.6663 0.8419 0.1170  0.0146  0.1327  64  GLY A O   
506  N N   . VAL A 65  ? 0.7926 0.5738 0.7647 0.1018  0.0322  0.0959  65  VAL A N   
507  C CA  . VAL A 65  ? 0.7812 0.6111 0.7706 0.0925  0.0228  0.0922  65  VAL A CA  
508  C C   . VAL A 65  ? 0.7972 0.6272 0.7706 0.0684  0.0205  0.0897  65  VAL A C   
509  O O   . VAL A 65  ? 0.7705 0.6282 0.7455 0.0621  0.0108  0.0958  65  VAL A O   
510  C CB  . VAL A 65  ? 0.7067 0.5546 0.7134 0.0912  0.0277  0.0739  65  VAL A CB  
511  C CG1 . VAL A 65  ? 0.6640 0.5526 0.6837 0.0805  0.0194  0.0700  65  VAL A CG1 
512  C CG2 . VAL A 65  ? 0.7975 0.6479 0.8182 0.1145  0.0322  0.0761  65  VAL A CG2 
513  N N   . ILE A 66  ? 0.7630 0.5625 0.7199 0.0529  0.0308  0.0798  66  ILE A N   
514  C CA  . ILE A 66  ? 0.7040 0.5031 0.6466 0.0300  0.0330  0.0758  66  ILE A CA  
515  C C   . ILE A 66  ? 0.8175 0.5711 0.7306 0.0207  0.0416  0.0818  66  ILE A C   
516  O O   . ILE A 66  ? 0.7633 0.4821 0.6683 0.0282  0.0481  0.0830  66  ILE A O   
517  C CB  . ILE A 66  ? 0.6837 0.5027 0.6423 0.0156  0.0387  0.0543  66  ILE A CB  
518  C CG1 . ILE A 66  ? 0.6998 0.4983 0.6607 0.0117  0.0482  0.0410  66  ILE A CG1 
519  C CG2 . ILE A 66  ? 0.7662 0.6229 0.7477 0.0239  0.0306  0.0502  66  ILE A CG2 
520  C CD1 . ILE A 66  ? 0.6872 0.5076 0.6648 -0.0030 0.0520  0.0220  66  ILE A CD1 
521  N N   . ARG A 67  ? 0.7549 0.5049 0.6480 0.0026  0.0433  0.0851  67  ARG A N   
522  C CA  . ARG A 67  ? 0.7451 0.4523 0.6060 -0.0125 0.0536  0.0899  67  ARG A CA  
523  C C   . ARG A 67  ? 0.7385 0.4541 0.6016 -0.0391 0.0671  0.0709  67  ARG A C   
524  O O   . ARG A 67  ? 0.7368 0.4890 0.6170 -0.0450 0.0662  0.0603  67  ARG A O   
525  C CB  . ARG A 67  ? 0.8532 0.5456 0.6820 -0.0125 0.0453  0.1127  67  ARG A CB  
526  C CG  . ARG A 67  ? 0.9368 0.6160 0.7623 0.0148  0.0325  0.1353  67  ARG A CG  
527  C CD  . ARG A 67  ? 0.9896 0.6558 0.7807 0.0126  0.0217  0.1592  67  ARG A CD  
528  N NE  . ARG A 67  ? 1.0150 0.6421 0.7663 -0.0130 0.0346  0.1590  67  ARG A NE  
529  C CZ  . ARG A 67  ? 1.1416 0.7134 0.8660 -0.0152 0.0450  0.1660  67  ARG A CZ  
530  N NH1 . ARG A 67  ? 1.2010 0.7454 0.9320 0.0087  0.0445  0.1734  67  ARG A NH1 
531  N NH2 . ARG A 67  ? 1.1834 0.7238 0.8715 -0.0429 0.0584  0.1647  67  ARG A NH2 
532  N N   . LYS A 68  ? 0.7461 0.4273 0.5926 -0.0550 0.0808  0.0664  68  LYS A N   
533  C CA  . LYS A 68  ? 0.7891 0.4815 0.6401 -0.0816 0.0955  0.0494  68  LYS A CA  
534  C C   . LYS A 68  ? 0.8348 0.5162 0.6538 -0.0983 0.1017  0.0583  68  LYS A C   
535  O O   . LYS A 68  ? 0.8903 0.5303 0.6710 -0.0995 0.1011  0.0769  68  LYS A O   
536  C CB  . LYS A 68  ? 0.8397 0.5032 0.6865 -0.0966 0.1082  0.0396  68  LYS A CB  
537  C CG  . LYS A 68  ? 0.8117 0.5036 0.6794 -0.1221 0.1216  0.0187  68  LYS A CG  
538  C CD  . LYS A 68  ? 0.8839 0.5580 0.7555 -0.1367 0.1296  0.0062  68  LYS A CD  
539  C CE  . LYS A 68  ? 0.8755 0.5984 0.7850 -0.1552 0.1363  -0.0158 68  LYS A CE  
540  N NZ  . LYS A 68  ? 0.9605 0.6975 0.8675 -0.1775 0.1520  -0.0193 68  LYS A NZ  
541  N N   . LEU A 69  ? 0.7621 0.4780 0.5943 -0.1102 0.1080  0.0456  69  LEU A N   
542  C CA  . LEU A 69  ? 0.8681 0.5748 0.6683 -0.1297 0.1182  0.0495  69  LEU A CA  
543  C C   . LEU A 69  ? 0.8585 0.5528 0.6540 -0.1567 0.1407  0.0377  69  LEU A C   
544  O O   . LEU A 69  ? 0.8567 0.5862 0.6844 -0.1670 0.1527  0.0176  69  LEU A O   
545  C CB  . LEU A 69  ? 0.7376 0.4828 0.5518 -0.1286 0.1168  0.0400  69  LEU A CB  
546  C CG  . LEU A 69  ? 0.7768 0.5347 0.5925 -0.1074 0.0951  0.0518  69  LEU A CG  
547  C CD1 . LEU A 69  ? 0.6684 0.4626 0.5054 -0.1059 0.0953  0.0374  69  LEU A CD1 
548  C CD2 . LEU A 69  ? 0.7908 0.5214 0.5602 -0.1095 0.0853  0.0747  69  LEU A CD2 
549  N N   . LYS A 70  ? 0.8898 0.5342 0.6460 -0.1679 0.1465  0.0512  70  LYS A N   
550  C CA  . LYS A 70  ? 0.9124 0.5397 0.6630 -0.1958 0.1678  0.0409  70  LYS A CA  
551  C C   . LYS A 70  ? 0.9118 0.5625 0.6618 -0.2216 0.1888  0.0280  70  LYS A C   
552  O O   . LYS A 70  ? 0.9443 0.6069 0.7116 -0.2443 0.2073  0.0123  70  LYS A O   
553  C CB  . LYS A 70  ? 1.0229 0.5821 0.7221 -0.2030 0.1704  0.0609  70  LYS A CB  
554  C CG  . LYS A 70  ? 1.1791 0.7086 0.8780 -0.1768 0.1546  0.0726  70  LYS A CG  
555  C CD  . LYS A 70  ? 1.2052 0.7427 0.9371 -0.1808 0.1597  0.0532  70  LYS A CD  
556  C CE  . LYS A 70  ? 1.3121 0.8012 1.0291 -0.1609 0.1517  0.0643  70  LYS A CE  
557  N NZ  . LYS A 70  ? 1.3521 0.8356 1.0865 -0.1733 0.1598  0.0448  70  LYS A NZ  
558  N N   . LYS A 71  ? 0.8961 0.5547 0.6263 -0.2199 0.1873  0.0333  71  LYS A N   
559  C CA  . LYS A 71  ? 0.8719 0.5461 0.5946 -0.2445 0.2110  0.0208  71  LYS A CA  
560  C C   . LYS A 71  ? 0.9045 0.6384 0.6878 -0.2427 0.2210  -0.0053 71  LYS A C   
561  O O   . LYS A 71  ? 0.8953 0.6483 0.6880 -0.2642 0.2457  -0.0202 71  LYS A O   
562  C CB  . LYS A 71  ? 0.9469 0.6101 0.6272 -0.2436 0.2061  0.0321  71  LYS A CB  
563  C CG  . LYS A 71  ? 0.9591 0.6248 0.6155 -0.2713 0.2336  0.0214  71  LYS A CG  
564  C CD  . LYS A 71  ? 0.9564 0.6086 0.5653 -0.2719 0.2266  0.0316  71  LYS A CD  
565  C CE  . LYS A 71  ? 1.0253 0.6790 0.6096 -0.2935 0.2491  0.0182  71  LYS A CE  
566  N NZ  . LYS A 71  ? 1.2208 0.8428 0.7748 -0.3096 0.2558  0.0249  71  LYS A NZ  
567  N N   . TYR A 72  ? 0.9000 0.6644 0.7250 -0.2170 0.2028  -0.0104 72  TYR A N   
568  C CA  . TYR A 72  ? 0.8456 0.6647 0.7256 -0.2094 0.2079  -0.0314 72  TYR A CA  
569  C C   . TYR A 72  ? 0.8221 0.6646 0.7473 -0.2047 0.2012  -0.0406 72  TYR A C   
570  O O   . TYR A 72  ? 0.8444 0.6575 0.7561 -0.2078 0.1940  -0.0326 72  TYR A O   
571  C CB  . TYR A 72  ? 0.7482 0.5825 0.6344 -0.1857 0.1929  -0.0300 72  TYR A CB  
572  C CG  . TYR A 72  ? 0.7836 0.5920 0.6192 -0.1924 0.1953  -0.0200 72  TYR A CG  
573  C CD1 . TYR A 72  ? 0.7611 0.5684 0.5767 -0.2136 0.2203  -0.0292 72  TYR A CD1 
574  C CD2 . TYR A 72  ? 0.7814 0.5689 0.5887 -0.1789 0.1727  -0.0018 72  TYR A CD2 
575  C CE1 . TYR A 72  ? 0.8003 0.5815 0.5628 -0.2226 0.2220  -0.0207 72  TYR A CE1 
576  C CE2 . TYR A 72  ? 0.8420 0.6089 0.6010 -0.1876 0.1719  0.0078  72  TYR A CE2 
577  C CZ  . TYR A 72  ? 0.8316 0.5930 0.5653 -0.2102 0.1961  -0.0019 72  TYR A CZ  
578  O OH  . TYR A 72  ? 0.9685 0.7070 0.6477 -0.2215 0.1948  0.0069  72  TYR A OH  
579  N N   . ASP A 73  ? 0.7478 0.6419 0.7249 -0.1967 0.2035  -0.0577 73  ASP A N   
580  C CA  . ASP A 73  ? 0.6779 0.6043 0.7009 -0.1951 0.1970  -0.0686 73  ASP A CA  
581  C C   . ASP A 73  ? 0.6643 0.5988 0.7035 -0.1659 0.1717  -0.0646 73  ASP A C   
582  O O   . ASP A 73  ? 0.6592 0.6234 0.7239 -0.1478 0.1668  -0.0699 73  ASP A O   
583  C CB  . ASP A 73  ? 0.7232 0.7055 0.7954 -0.2031 0.2137  -0.0878 73  ASP A CB  
584  C CG  . ASP A 73  ? 0.7288 0.7528 0.8512 -0.2012 0.2030  -0.0984 73  ASP A CG  
585  O OD1 . ASP A 73  ? 0.7731 0.7774 0.8865 -0.1966 0.1849  -0.0925 73  ASP A OD1 
586  O OD2 . ASP A 73  ? 0.7592 0.8372 0.9301 -0.2040 0.2129  -0.1128 73  ASP A OD2 
587  N N   . ASN A 74  ? 0.6268 0.5316 0.6492 -0.1616 0.1577  -0.0554 74  ASN A N   
588  C CA  . ASN A 74  ? 0.5939 0.5051 0.6297 -0.1370 0.1362  -0.0523 74  ASN A CA  
589  C C   . ASN A 74  ? 0.5850 0.4936 0.6095 -0.1164 0.1271  -0.0430 74  ASN A C   
590  O O   . ASN A 74  ? 0.5506 0.4860 0.6000 -0.0991 0.1173  -0.0472 74  ASN A O   
591  C CB  . ASN A 74  ? 0.5857 0.5451 0.6703 -0.1329 0.1304  -0.0672 74  ASN A CB  
592  C CG  . ASN A 74  ? 0.6376 0.5989 0.7294 -0.1114 0.1094  -0.0640 74  ASN A CG  
593  O OD1 . ASN A 74  ? 0.6828 0.6085 0.7473 -0.1051 0.1018  -0.0540 74  ASN A OD1 
594  N ND2 . ASN A 74  ? 0.6343 0.6366 0.7626 -0.0990 0.1009  -0.0719 74  ASN A ND2 
595  N N   . CYS A 75  ? 0.6314 0.5065 0.6156 -0.1200 0.1296  -0.0295 75  CYS A N   
596  C CA  . CYS A 75  ? 0.6449 0.5157 0.6133 -0.1051 0.1192  -0.0194 75  CYS A CA  
597  C C   . CYS A 75  ? 0.6556 0.4953 0.5985 -0.0942 0.1049  -0.0013 75  CYS A C   
598  O O   . CYS A 75  ? 0.6400 0.4480 0.5622 -0.1015 0.1081  0.0062  75  CYS A O   
599  C CB  . CYS A 75  ? 0.6127 0.4765 0.5549 -0.1183 0.1323  -0.0188 75  CYS A CB  
600  S SG  . CYS A 75  ? 0.5929 0.4953 0.5682 -0.1241 0.1515  -0.0408 75  CYS A SG  
601  N N   . TRP A 76  ? 0.5870 0.4356 0.5326 -0.0762 0.0900  0.0059  76  TRP A N   
602  C CA  . TRP A 76  ? 0.6512 0.4819 0.5847 -0.0611 0.0760  0.0219  76  TRP A CA  
603  C C   . TRP A 76  ? 0.6236 0.4604 0.5430 -0.0537 0.0645  0.0341  76  TRP A C   
604  O O   . TRP A 76  ? 0.6204 0.4775 0.5459 -0.0563 0.0648  0.0268  76  TRP A O   
605  C CB  . TRP A 76  ? 0.5892 0.4324 0.5504 -0.0458 0.0683  0.0160  76  TRP A CB  
606  C CG  . TRP A 76  ? 0.5770 0.4186 0.5517 -0.0559 0.0769  0.0025  76  TRP A CG  
607  C CD1 . TRP A 76  ? 0.5553 0.4258 0.5567 -0.0645 0.0826  -0.0139 76  TRP A CD1 
608  C CD2 . TRP A 76  ? 0.6707 0.4806 0.6329 -0.0597 0.0805  0.0042  76  TRP A CD2 
609  N NE1 . TRP A 76  ? 0.6175 0.4818 0.6253 -0.0757 0.0877  -0.0226 76  TRP A NE1 
610  C CE2 . TRP A 76  ? 0.6101 0.4337 0.5913 -0.0744 0.0874  -0.0127 76  TRP A CE2 
611  C CE3 . TRP A 76  ? 0.6761 0.4465 0.6131 -0.0514 0.0786  0.0183  76  TRP A CE3 
612  C CZ2 . TRP A 76  ? 0.6969 0.4933 0.6684 -0.0854 0.0928  -0.0173 76  TRP A CZ2 
613  C CZ3 . TRP A 76  ? 0.7412 0.4790 0.6675 -0.0590 0.0859  0.0139  76  TRP A CZ3 
614  C CH2 . TRP A 76  ? 0.7771 0.5268 0.7186 -0.0779 0.0930  -0.0045 76  TRP A CH2 
615  N N   . LEU A 77  ? 0.6789 0.4973 0.5793 -0.0447 0.0544  0.0528  77  LEU A N   
616  C CA  . LEU A 77  ? 0.6498 0.4781 0.5375 -0.0391 0.0403  0.0669  77  LEU A CA  
617  C C   . LEU A 77  ? 0.6749 0.5152 0.5819 -0.0165 0.0266  0.0766  77  LEU A C   
618  O O   . LEU A 77  ? 0.7397 0.5604 0.6475 -0.0044 0.0266  0.0840  77  LEU A O   
619  C CB  . LEU A 77  ? 0.7119 0.5136 0.5586 -0.0488 0.0386  0.0839  77  LEU A CB  
620  C CG  . LEU A 77  ? 0.7211 0.5365 0.5530 -0.0449 0.0203  0.1005  77  LEU A CG  
621  C CD1 . LEU A 77  ? 0.7381 0.5756 0.5670 -0.0593 0.0214  0.0883  77  LEU A CD1 
622  C CD2 . LEU A 77  ? 0.7383 0.5248 0.5288 -0.0499 0.0145  0.1220  77  LEU A CD2 
623  N N   . ALA A 78  ? 0.6283 0.4988 0.5498 -0.0117 0.0170  0.0757  78  ALA A N   
624  C CA  . ALA A 78  ? 0.6499 0.5394 0.5903 0.0073  0.0048  0.0856  78  ALA A CA  
625  C C   . ALA A 78  ? 0.6310 0.5371 0.5590 0.0054  -0.0103 0.1020  78  ALA A C   
626  O O   . ALA A 78  ? 0.7105 0.6226 0.6214 -0.0120 -0.0118 0.0983  78  ALA A O   
627  C CB  . ALA A 78  ? 0.5829 0.4965 0.5510 0.0120  0.0057  0.0718  78  ALA A CB  
628  N N   . LEU A 79  ? 0.6523 0.5661 0.5885 0.0233  -0.0214 0.1196  79  LEU A N   
629  C CA  . LEU A 79  ? 0.6594 0.5987 0.5909 0.0236  -0.0394 0.1372  79  LEU A CA  
630  C C   . LEU A 79  ? 0.7309 0.7092 0.6990 0.0393  -0.0468 0.1398  79  LEU A C   
631  O O   . LEU A 79  ? 0.7296 0.7062 0.7189 0.0614  -0.0431 0.1436  79  LEU A O   
632  C CB  . LEU A 79  ? 0.6574 0.5759 0.5673 0.0323  -0.0478 0.1599  79  LEU A CB  
633  C CG  . LEU A 79  ? 0.7565 0.6335 0.6243 0.0142  -0.0395 0.1597  79  LEU A CG  
634  C CD1 . LEU A 79  ? 0.7886 0.6455 0.6299 0.0225  -0.0517 0.1864  79  LEU A CD1 
635  C CD2 . LEU A 79  ? 0.7187 0.6035 0.5653 -0.0136 -0.0372 0.1472  79  LEU A CD2 
636  N N   . THR A 80  ? 0.6338 0.6447 0.6074 0.0263  -0.0549 0.1366  80  THR A N   
637  C CA  . THR A 80  ? 0.6149 0.6645 0.6223 0.0352  -0.0590 0.1363  80  THR A CA  
638  C C   . THR A 80  ? 0.6485 0.7363 0.6708 0.0449  -0.0773 0.1580  80  THR A C   
639  O O   . THR A 80  ? 0.6760 0.7624 0.6781 0.0411  -0.0906 0.1736  80  THR A O   
640  C CB  . THR A 80  ? 0.6527 0.7149 0.6578 0.0142  -0.0569 0.1210  80  THR A CB  
641  O OG1 . THR A 80  ? 0.6789 0.7529 0.6615 -0.0068 -0.0696 0.1268  80  THR A OG1 
642  C CG2 . THR A 80  ? 0.5914 0.6197 0.5837 0.0065  -0.0408 0.1016  80  THR A CG2 
643  N N   . ASP A 81  ? 0.6625 0.7871 0.7211 0.0575  -0.0780 0.1595  81  ASP A N   
644  C CA  . ASP A 81  ? 0.6253 0.8014 0.7071 0.0629  -0.0958 0.1777  81  ASP A CA  
645  C C   . ASP A 81  ? 0.5736 0.7697 0.6346 0.0315  -0.1103 0.1776  81  ASP A C   
646  O O   . ASP A 81  ? 0.6206 0.8081 0.6693 0.0097  -0.1026 0.1599  81  ASP A O   
647  C CB  . ASP A 81  ? 0.6248 0.8394 0.7498 0.0765  -0.0892 0.1747  81  ASP A CB  
648  C CG  . ASP A 81  ? 0.6198 0.8957 0.7794 0.0867  -0.1059 0.1943  81  ASP A CG  
649  O OD1 . ASP A 81  ? 0.6562 0.9607 0.8070 0.0669  -0.1252 0.2033  81  ASP A OD1 
650  O OD2 . ASP A 81  ? 0.6084 0.9055 0.8046 0.1143  -0.0993 0.2002  81  ASP A OD2 
651  N N   . PRO A 82  ? 0.5879 0.8073 0.6411 0.0278  -0.1316 0.1969  82  PRO A N   
652  C CA  . PRO A 82  ? 0.6348 0.8695 0.6610 -0.0062 -0.1455 0.1951  82  PRO A CA  
653  C C   . PRO A 82  ? 0.6754 0.9514 0.7238 -0.0238 -0.1466 0.1855  82  PRO A C   
654  O O   . PRO A 82  ? 0.6275 0.9019 0.6479 -0.0560 -0.1513 0.1764  82  PRO A O   
655  C CB  . PRO A 82  ? 0.6404 0.9016 0.6615 -0.0014 -0.1713 0.2217  82  PRO A CB  
656  C CG  . PRO A 82  ? 0.6972 0.9774 0.7615 0.0384  -0.1717 0.2380  82  PRO A CG  
657  C CD  . PRO A 82  ? 0.6797 0.9115 0.7462 0.0547  -0.1446 0.2219  82  PRO A CD  
658  N N   . ARG A 83  ? 0.5987 0.9082 0.6933 -0.0053 -0.1407 0.1865  83  ARG A N   
659  C CA  . ARG A 83  ? 0.5856 0.9317 0.7002 -0.0236 -0.1388 0.1774  83  ARG A CA  
660  C C   . ARG A 83  ? 0.5448 0.8486 0.6419 -0.0353 -0.1175 0.1539  83  ARG A C   
661  O O   . ARG A 83  ? 0.6399 0.9572 0.7362 -0.0585 -0.1156 0.1445  83  ARG A O   
662  C CB  . ARG A 83  ? 0.5061 0.9067 0.6770 0.0003  -0.1382 0.1876  83  ARG A CB  
663  C CG  . ARG A 83  ? 0.5330 0.9847 0.7310 0.0165  -0.1603 0.2129  83  ARG A CG  
664  C CD  . ARG A 83  ? 0.5795 1.0804 0.8369 0.0466  -0.1537 0.2211  83  ARG A CD  
665  N NE  . ARG A 83  ? 0.6325 1.0884 0.8935 0.0776  -0.1309 0.2142  83  ARG A NE  
666  C CZ  . ARG A 83  ? 0.6273 1.1076 0.9313 0.1082  -0.1188 0.2180  83  ARG A CZ  
667  N NH1 . ARG A 83  ? 0.6853 1.2259 1.0301 0.1120  -0.1228 0.2235  83  ARG A NH1 
668  N NH2 . ARG A 83  ? 0.5724 1.0027 0.8696 0.1315  -0.0980 0.2093  83  ARG A NH2 
669  N N   . ASP A 84  ? 0.5779 0.8313 0.6608 -0.0204 -0.1022 0.1450  84  ASP A N   
670  C CA  . ASP A 84  ? 0.6040 0.8197 0.6744 -0.0260 -0.0837 0.1249  84  ASP A CA  
671  C C   . ASP A 84  ? 0.6239 0.7900 0.6543 -0.0366 -0.0787 0.1151  84  ASP A C   
672  O O   . ASP A 84  ? 0.6486 0.7813 0.6747 -0.0220 -0.0674 0.1096  84  ASP A O   
673  C CB  . ASP A 84  ? 0.5562 0.7646 0.6517 0.0012  -0.0693 0.1219  84  ASP A CB  
674  C CG  . ASP A 84  ? 0.5715 0.7446 0.6546 -0.0031 -0.0536 0.1036  84  ASP A CG  
675  O OD1 . ASP A 84  ? 0.5910 0.7554 0.6564 -0.0251 -0.0528 0.0946  84  ASP A OD1 
676  O OD2 . ASP A 84  ? 0.5639 0.7163 0.6532 0.0154  -0.0427 0.0986  84  ASP A OD2 
677  N N   . VAL A 85  ? 0.5833 0.7451 0.5841 -0.0636 -0.0859 0.1119  85  VAL A N   
678  C CA  . VAL A 85  ? 0.6670 0.7868 0.6284 -0.0749 -0.0807 0.1038  85  VAL A CA  
679  C C   . VAL A 85  ? 0.7366 0.8291 0.6730 -0.0971 -0.0700 0.0848  85  VAL A C   
680  O O   . VAL A 85  ? 0.6965 0.7573 0.5984 -0.1104 -0.0643 0.0761  85  VAL A O   
681  C CB  . VAL A 85  ? 0.6320 0.7617 0.5698 -0.0860 -0.0978 0.1181  85  VAL A CB  
682  C CG1 . VAL A 85  ? 0.6896 0.8356 0.6487 -0.0596 -0.1068 0.1382  85  VAL A CG1 
683  C CG2 . VAL A 85  ? 0.6663 0.8315 0.5983 -0.1115 -0.1143 0.1221  85  VAL A CG2 
684  N N   . ALA A 86  ? 0.7124 0.8131 0.6632 -0.1009 -0.0655 0.0780  86  ALA A N   
685  C CA  . ALA A 86  ? 0.6934 0.7618 0.6172 -0.1207 -0.0553 0.0614  86  ALA A CA  
686  C C   . ALA A 86  ? 0.7654 0.8373 0.7070 -0.1187 -0.0488 0.0567  86  ALA A C   
687  O O   . ALA A 86  ? 0.6436 0.7503 0.6166 -0.1082 -0.0532 0.0661  86  ALA A O   
688  C CB  . ALA A 86  ? 0.7598 0.8307 0.6501 -0.1528 -0.0652 0.0605  86  ALA A CB  
689  N N   . ARG A 87  ? 0.7841 0.8167 0.7033 -0.1283 -0.0368 0.0422  87  ARG A N   
690  C CA  . ARG A 87  ? 0.7464 0.7724 0.6706 -0.1318 -0.0306 0.0381  87  ARG A CA  
691  C C   . ARG A 87  ? 0.7961 0.8476 0.7141 -0.1605 -0.0399 0.0422  87  ARG A C   
692  O O   . ARG A 87  ? 0.9214 0.9632 0.8093 -0.1862 -0.0443 0.0377  87  ARG A O   
693  C CB  . ARG A 87  ? 0.7464 0.7184 0.6459 -0.1318 -0.0157 0.0230  87  ARG A CB  
694  C CG  . ARG A 87  ? 0.7399 0.6914 0.6309 -0.1403 -0.0093 0.0191  87  ARG A CG  
695  C CD  . ARG A 87  ? 0.7044 0.6006 0.5738 -0.1332 0.0049  0.0061  87  ARG A CD  
696  N NE  . ARG A 87  ? 0.7168 0.5853 0.5556 -0.1468 0.0104  -0.0047 87  ARG A NE  
697  C CZ  . ARG A 87  ? 0.8094 0.6583 0.6136 -0.1765 0.0112  -0.0109 87  ARG A CZ  
698  N NH1 . ARG A 87  ? 0.8347 0.6926 0.6333 -0.1978 0.0058  -0.0068 87  ARG A NH1 
699  N NH2 . ARG A 87  ? 0.8506 0.6698 0.6235 -0.1874 0.0189  -0.0226 87  ARG A NH2 
700  N N   . ILE A 88  ? 0.8849 0.9705 0.8305 -0.1583 -0.0422 0.0499  88  ILE A N   
701  C CA  . ILE A 88  ? 0.8950 1.0188 0.8452 -0.1855 -0.0515 0.0555  88  ILE A CA  
702  C C   . ILE A 88  ? 0.8918 0.9821 0.8194 -0.2061 -0.0405 0.0461  88  ILE A C   
703  O O   . ILE A 88  ? 0.8420 0.9228 0.7804 -0.1936 -0.0304 0.0461  88  ILE A O   
704  C CB  . ILE A 88  ? 0.8373 1.0239 0.8347 -0.1711 -0.0585 0.0700  88  ILE A CB  
705  C CG1 . ILE A 88  ? 0.7829 0.9910 0.7991 -0.1465 -0.0678 0.0802  88  ILE A CG1 
706  C CG2 . ILE A 88  ? 0.8399 1.0764 0.8480 -0.2008 -0.0693 0.0760  88  ILE A CG2 
707  C CD1 . ILE A 88  ? 0.7753 1.0407 0.8388 -0.1268 -0.0728 0.0943  88  ILE A CD1 
708  N N   . GLU A 89  ? 0.8776 0.9462 0.7692 -0.2392 -0.0421 0.0381  89  GLU A N   
709  C CA  . GLU A 89  ? 0.8570 0.8833 0.7197 -0.2611 -0.0306 0.0290  89  GLU A CA  
710  C C   . GLU A 89  ? 0.8899 0.9591 0.7715 -0.2828 -0.0336 0.0362  89  GLU A C   
711  O O   . GLU A 89  ? 0.8353 0.8759 0.7057 -0.2894 -0.0215 0.0334  89  GLU A O   
712  C CB  . GLU A 89  ? 0.9630 0.9433 0.7754 -0.2905 -0.0286 0.0158  89  GLU A CB  
713  C CG  . GLU A 89  ? 0.9711 0.8917 0.7462 -0.3110 -0.0141 0.0051  89  GLU A CG  
714  C CD  . GLU A 89  ? 1.1350 1.0032 0.8566 -0.3390 -0.0094 -0.0102 89  GLU A CD  
715  O OE1 . GLU A 89  ? 1.1349 1.0031 0.8463 -0.3352 -0.0136 -0.0142 89  GLU A OE1 
716  O OE2 . GLU A 89  ? 1.0689 0.8922 0.7550 -0.3660 0.0000  -0.0187 89  GLU A OE2 
717  N N   . SER A 90  ? 0.8859 1.0246 0.7962 -0.2942 -0.0494 0.0462  90  SER A N   
718  C CA  . SER A 90  ? 0.8300 1.0194 0.7639 -0.3171 -0.0516 0.0526  90  SER A CA  
719  C C   . SER A 90  ? 0.7634 0.9789 0.7368 -0.2898 -0.0419 0.0604  90  SER A C   
720  O O   . SER A 90  ? 0.7627 1.0063 0.7500 -0.3080 -0.0363 0.0632  90  SER A O   
721  C CB  . SER A 90  ? 0.8190 1.0828 0.7777 -0.3348 -0.0732 0.0621  90  SER A CB  
722  O OG  . SER A 90  ? 0.8402 1.1401 0.8321 -0.2998 -0.0837 0.0734  90  SER A OG  
723  N N   . LYS A 91  ? 0.7107 0.9168 0.6998 -0.2494 -0.0385 0.0631  91  LYS A N   
724  C CA  . LYS A 91  ? 0.6270 0.8488 0.6456 -0.2234 -0.0279 0.0682  91  LYS A CA  
725  C C   . LYS A 91  ? 0.6185 0.7726 0.6078 -0.2109 -0.0129 0.0606  91  LYS A C   
726  O O   . LYS A 91  ? 0.5931 0.7499 0.5985 -0.1868 -0.0047 0.0634  91  LYS A O   
727  C CB  . LYS A 91  ? 0.6501 0.9080 0.7057 -0.1877 -0.0343 0.0765  91  LYS A CB  
728  C CG  . LYS A 91  ? 0.6280 0.9518 0.7137 -0.1932 -0.0518 0.0873  91  LYS A CG  
729  C CD  . LYS A 91  ? 0.6432 1.0360 0.7684 -0.2058 -0.0514 0.0950  91  LYS A CD  
730  C CE  . LYS A 91  ? 0.6976 1.1619 0.8581 -0.2068 -0.0717 0.1079  91  LYS A CE  
731  N NZ  . LYS A 91  ? 0.6470 1.1144 0.8251 -0.1673 -0.0780 0.1162  91  LYS A NZ  
732  N N   . THR A 92  ? 0.6071 0.7210 0.6442 -0.0728 0.0119  0.0065  92  THR A N   
733  C CA  . THR A 92  ? 0.5898 0.6891 0.6067 -0.0647 0.0313  0.0022  92  THR A CA  
734  C C   . THR A 92  ? 0.5781 0.6735 0.6083 -0.0680 0.0449  0.0010  92  THR A C   
735  O O   . THR A 92  ? 0.6445 0.7362 0.6775 -0.0820 0.0409  -0.0033 92  THR A O   
736  C CB  . THR A 92  ? 0.6427 0.7252 0.6246 -0.0711 0.0305  -0.0059 92  THR A CB  
737  O OG1 . THR A 92  ? 0.6591 0.7431 0.6257 -0.0721 0.0182  -0.0035 92  THR A OG1 
738  C CG2 . THR A 92  ? 0.5661 0.6360 0.5377 -0.0600 0.0467  -0.0099 92  THR A CG2 
739  N N   . VAL A 93  ? 0.5734 0.6660 0.6075 -0.0568 0.0605  0.0049  93  VAL A N   
740  C CA  . VAL A 93  ? 0.5325 0.6186 0.5767 -0.0609 0.0748  0.0067  93  VAL A CA  
741  C C   . VAL A 93  ? 0.5531 0.6162 0.5718 -0.0517 0.0865  0.0085  93  VAL A C   
742  O O   . VAL A 93  ? 0.5433 0.6019 0.5450 -0.0401 0.0851  0.0092  93  VAL A O   
743  C CB  . VAL A 93  ? 0.5784 0.6835 0.6558 -0.0604 0.0833  0.0115  93  VAL A CB  
744  C CG1 . VAL A 93  ? 0.6434 0.7719 0.7559 -0.0694 0.0672  0.0104  93  VAL A CG1 
745  C CG2 . VAL A 93  ? 0.4994 0.6077 0.5711 -0.0455 0.0905  0.0144  93  VAL A CG2 
746  N N   . ILE A 94  ? 0.5705 0.6172 0.5879 -0.0580 0.0958  0.0101  94  ILE A N   
747  C CA  . ILE A 94  ? 0.6043 0.6247 0.5991 -0.0507 0.1037  0.0150  94  ILE A CA  
748  C C   . ILE A 94  ? 0.5981 0.6111 0.5953 -0.0567 0.1192  0.0235  94  ILE A C   
749  O O   . ILE A 94  ? 0.6155 0.6333 0.6332 -0.0700 0.1243  0.0229  94  ILE A O   
750  C CB  . ILE A 94  ? 0.5809 0.5796 0.5681 -0.0531 0.0995  0.0091  94  ILE A CB  
751  C CG1 . ILE A 94  ? 0.5261 0.5308 0.5083 -0.0481 0.0897  -0.0010 94  ILE A CG1 
752  C CG2 . ILE A 94  ? 0.5777 0.5462 0.5475 -0.0461 0.1036  0.0169  94  ILE A CG2 
753  C CD1 . ILE A 94  ? 0.6251 0.6100 0.6053 -0.0494 0.0895  -0.0108 94  ILE A CD1 
754  N N   . ILE A 95  ? 0.5955 0.5955 0.5699 -0.0488 0.1271  0.0310  95  ILE A N   
755  C CA  . ILE A 95  ? 0.5847 0.5755 0.5529 -0.0562 0.1461  0.0388  95  ILE A CA  
756  C C   . ILE A 95  ? 0.6486 0.5992 0.5851 -0.0586 0.1477  0.0483  95  ILE A C   
757  O O   . ILE A 95  ? 0.6279 0.5572 0.5355 -0.0479 0.1380  0.0527  95  ILE A O   
758  C CB  . ILE A 95  ? 0.6475 0.6465 0.6049 -0.0489 0.1560  0.0399  95  ILE A CB  
759  C CG1 . ILE A 95  ? 0.6308 0.6682 0.6294 -0.0481 0.1563  0.0319  95  ILE A CG1 
760  C CG2 . ILE A 95  ? 0.6677 0.6458 0.6016 -0.0576 0.1785  0.0479  95  ILE A CG2 
761  C CD1 . ILE A 95  ? 0.5834 0.6362 0.5923 -0.0401 0.1344  0.0260  95  ILE A CD1 
762  N N   . THR A 96  ? 0.6411 0.5803 0.5855 -0.0731 0.1579  0.0522  96  THR A N   
763  C CA  . THR A 96  ? 0.6966 0.5934 0.6105 -0.0783 0.1610  0.0641  96  THR A CA  
764  C C   . THR A 96  ? 0.7873 0.6796 0.7042 -0.0968 0.1846  0.0703  96  THR A C   
765  O O   . THR A 96  ? 0.6703 0.5935 0.6270 -0.1066 0.1938  0.0628  96  THR A O   
766  C CB  . THR A 96  ? 0.7057 0.5837 0.6281 -0.0778 0.1464  0.0613  96  THR A CB  
767  O OG1 . THR A 96  ? 0.6481 0.5474 0.6070 -0.0896 0.1486  0.0511  96  THR A OG1 
768  C CG2 . THR A 96  ? 0.7089 0.5894 0.6299 -0.0604 0.1273  0.0543  96  THR A CG2 
769  N N   . GLN A 97  ? 0.8045 0.6570 0.6791 -0.1030 0.1935  0.0846  97  GLN A N   
770  C CA  . GLN A 97  ? 0.8581 0.7018 0.7309 -0.1237 0.2198  0.0911  97  GLN A CA  
771  C C   . GLN A 97  ? 0.7764 0.6266 0.6896 -0.1375 0.2206  0.0870  97  GLN A C   
772  O O   . GLN A 97  ? 0.8128 0.6850 0.7581 -0.1531 0.2403  0.0833  97  GLN A O   
773  C CB  . GLN A 97  ? 0.9595 0.7491 0.7699 -0.1306 0.2255  0.1095  97  GLN A CB  
774  C CG  . GLN A 97  ? 1.0768 0.8227 0.8721 -0.1313 0.2068  0.1205  97  GLN A CG  
775  C CD  . GLN A 97  ? 1.1679 0.9046 0.9564 -0.1091 0.1756  0.1193  97  GLN A CD  
776  O OE1 . GLN A 97  ? 1.0170 0.7759 0.8448 -0.0995 0.1617  0.1063  97  GLN A OE1 
777  N NE2 . GLN A 97  ? 1.2925 0.9956 1.0310 -0.1022 0.1647  0.1322  97  GLN A NE2 
778  N N   . GLU A 98  ? 0.8362 0.6682 0.7520 -0.1322 0.1997  0.0860  98  GLU A N   
779  C CA  . GLU A 98  ? 0.8133 0.6458 0.7624 -0.1451 0.1977  0.0801  98  GLU A CA  
780  C C   . GLU A 98  ? 0.6979 0.5625 0.6804 -0.1361 0.1796  0.0627  98  GLU A C   
781  O O   . GLU A 98  ? 0.6813 0.5421 0.6519 -0.1192 0.1632  0.0586  98  GLU A O   
782  C CB  . GLU A 98  ? 0.8870 0.6662 0.8113 -0.1485 0.1903  0.0910  98  GLU A CB  
783  C CG  . GLU A 98  ? 0.9994 0.7375 0.8812 -0.1609 0.2061  0.1111  98  GLU A CG  
784  C CD  . GLU A 98  ? 1.0340 0.7783 0.9356 -0.1867 0.2318  0.1128  98  GLU A CD  
785  O OE1 . GLU A 98  ? 1.0678 0.8364 1.0164 -0.1952 0.2306  0.1003  98  GLU A OE1 
786  O OE2 . GLU A 98  ? 1.1553 0.8794 1.0244 -0.2001 0.2537  0.1260  98  GLU A OE2 
787  N N   . GLN A 99  ? 0.6459 0.5411 0.6694 -0.1490 0.1823  0.0527  99  GLN A N   
788  C CA  . GLN A 99  ? 0.6915 0.6120 0.7382 -0.1448 0.1640  0.0372  99  GLN A CA  
789  C C   . GLN A 99  ? 0.6911 0.5815 0.7267 -0.1423 0.1510  0.0308  99  GLN A C   
790  O O   . GLN A 99  ? 0.6099 0.5097 0.6451 -0.1329 0.1374  0.0191  99  GLN A O   
791  C CB  . GLN A 99  ? 0.6501 0.6037 0.7414 -0.1617 0.1652  0.0294  99  GLN A CB  
792  C CG  . GLN A 99  ? 0.6394 0.6133 0.7462 -0.1616 0.1437  0.0148  99  GLN A CG  
793  C CD  . GLN A 99  ? 0.6657 0.6674 0.8163 -0.1803 0.1389  0.0084  99  GLN A CD  
794  O OE1 . GLN A 99  ? 0.6499 0.6548 0.8255 -0.1946 0.1535  0.0132  99  GLN A OE1 
795  N NE2 . GLN A 99  ? 0.6528 0.6737 0.8126 -0.1818 0.1177  -0.0023 99  GLN A NE2 
796  N N   . ARG A 100 ? 0.6359 0.4883 0.6632 -0.1511 0.1565  0.0375  100 ARG A N   
797  C CA  . ARG A 100 ? 0.6475 0.4696 0.6720 -0.1488 0.1458  0.0291  100 ARG A CA  
798  C C   . ARG A 100 ? 0.6610 0.4676 0.6654 -0.1264 0.1354  0.0293  100 ARG A C   
799  O O   . ARG A 100 ? 0.6551 0.4474 0.6654 -0.1209 0.1271  0.0165  100 ARG A O   
800  C CB  . ARG A 100 ? 0.6858 0.4667 0.7078 -0.1628 0.1532  0.0381  100 ARG A CB  
801  C CG  . ARG A 100 ? 0.7745 0.5249 0.8034 -0.1633 0.1440  0.0257  100 ARG A CG  
802  C CD  . ARG A 100 ? 0.8565 0.5627 0.8835 -0.1778 0.1505  0.0364  100 ARG A CD  
803  N NE  . ARG A 100 ? 0.9549 0.6336 0.9953 -0.1810 0.1435  0.0210  100 ARG A NE  
804  C CZ  . ARG A 100 ? 1.0095 0.6438 1.0515 -0.1922 0.1460  0.0267  100 ARG A CZ  
805  N NH1 . ARG A 100 ? 1.0398 0.6500 1.0671 -0.2029 0.1553  0.0495  100 ARG A NH1 
806  N NH2 . ARG A 100 ? 1.0223 0.6331 1.0790 -0.1940 0.1404  0.0087  100 ARG A NH2 
807  N N   . ASP A 101 ? 0.6609 0.4694 0.6436 -0.1142 0.1364  0.0420  101 ASP A N   
808  C CA  . ASP A 101 ? 0.7158 0.5147 0.6852 -0.0934 0.1239  0.0416  101 ASP A CA  
809  C C   . ASP A 101 ? 0.6666 0.5006 0.6496 -0.0851 0.1173  0.0243  101 ASP A C   
810  O O   . ASP A 101 ? 0.6065 0.4338 0.5923 -0.0720 0.1084  0.0160  101 ASP A O   
811  C CB  . ASP A 101 ? 0.7720 0.5618 0.7104 -0.0853 0.1249  0.0594  101 ASP A CB  
812  C CG  . ASP A 101 ? 0.8748 0.6202 0.7876 -0.0941 0.1297  0.0787  101 ASP A CG  
813  O OD1 . ASP A 101 ? 0.9303 0.6421 0.8492 -0.0969 0.1240  0.0801  101 ASP A OD1 
814  O OD2 . ASP A 101 ? 0.9917 0.7331 0.8762 -0.0992 0.1401  0.0922  101 ASP A OD2 
815  N N   . THR A 102 ? 0.6600 0.5303 0.6537 -0.0932 0.1212  0.0191  102 THR A N   
816  C CA  . THR A 102 ? 0.6299 0.5306 0.6300 -0.0880 0.1139  0.0060  102 THR A CA  
817  C C   . THR A 102 ? 0.5736 0.4778 0.5863 -0.1000 0.1101  -0.0115 102 THR A C   
818  O O   . THR A 102 ? 0.6177 0.5248 0.6269 -0.0949 0.1052  -0.0248 102 THR A O   
819  C CB  . THR A 102 ? 0.6318 0.5666 0.6366 -0.0893 0.1163  0.0108  102 THR A CB  
820  O OG1 . THR A 102 ? 0.6650 0.5942 0.6518 -0.0785 0.1213  0.0238  102 THR A OG1 
821  C CG2 . THR A 102 ? 0.5678 0.5292 0.5761 -0.0856 0.1063  -0.0003 102 THR A CG2 
822  N N   . VAL A 103 ? 0.6080 0.5108 0.6336 -0.1177 0.1132  -0.0126 103 VAL A N   
823  C CA  . VAL A 103 ? 0.5441 0.4474 0.5766 -0.1324 0.1078  -0.0297 103 VAL A CA  
824  C C   . VAL A 103 ? 0.6339 0.5110 0.6765 -0.1470 0.1129  -0.0302 103 VAL A C   
825  O O   . VAL A 103 ? 0.7243 0.5957 0.7744 -0.1523 0.1207  -0.0158 103 VAL A O   
826  C CB  . VAL A 103 ? 0.5635 0.5024 0.6056 -0.1434 0.0988  -0.0327 103 VAL A CB  
827  C CG1 . VAL A 103 ? 0.5485 0.5090 0.5790 -0.1301 0.0926  -0.0323 103 VAL A CG1 
828  C CG2 . VAL A 103 ? 0.5228 0.4783 0.5890 -0.1520 0.1036  -0.0201 103 VAL A CG2 
829  N N   . PRO A 104 ? 0.6044 0.4623 0.6460 -0.1553 0.1106  -0.0476 104 PRO A N   
830  C CA  . PRO A 104 ? 0.6731 0.5070 0.7263 -0.1727 0.1138  -0.0506 104 PRO A CA  
831  C C   . PRO A 104 ? 0.6532 0.5138 0.7245 -0.1922 0.1101  -0.0471 104 PRO A C   
832  O O   . PRO A 104 ? 0.6099 0.5028 0.6837 -0.1959 0.0999  -0.0511 104 PRO A O   
833  C CB  . PRO A 104 ? 0.6559 0.4697 0.7017 -0.1780 0.1117  -0.0751 104 PRO A CB  
834  C CG  . PRO A 104 ? 0.6526 0.4727 0.6851 -0.1591 0.1121  -0.0819 104 PRO A CG  
835  C CD  . PRO A 104 ? 0.6005 0.4566 0.6294 -0.1510 0.1074  -0.0670 104 PRO A CD  
836  N N   . ILE A 105 ? 0.6511 0.4974 0.7382 -0.2053 0.1174  -0.0389 105 ILE A N   
837  C CA  . ILE A 105 ? 0.6914 0.5641 0.8065 -0.2253 0.1150  -0.0367 105 ILE A CA  
838  C C   . ILE A 105 ? 0.6637 0.5346 0.7825 -0.2440 0.1009  -0.0566 105 ILE A C   
839  O O   . ILE A 105 ? 0.7102 0.5473 0.8273 -0.2554 0.1034  -0.0657 105 ILE A O   
840  C CB  . ILE A 105 ? 0.7280 0.5854 0.8590 -0.2361 0.1305  -0.0220 105 ILE A CB  
841  C CG1 . ILE A 105 ? 0.7019 0.5561 0.8174 -0.2196 0.1441  -0.0027 105 ILE A CG1 
842  C CG2 . ILE A 105 ? 0.6666 0.5560 0.8372 -0.2575 0.1294  -0.0220 105 ILE A CG2 
843  C CD1 . ILE A 105 ? 0.6597 0.5555 0.7782 -0.2069 0.1417  0.0004  105 ILE A CD1 
844  N N   . PRO A 106 ? 0.6699 0.5721 0.7905 -0.2487 0.0845  -0.0638 106 PRO A N   
845  C CA  . PRO A 106 ? 0.6719 0.5679 0.7855 -0.2688 0.0682  -0.0828 106 PRO A CA  
846  C C   . PRO A 106 ? 0.7577 0.6456 0.9002 -0.2928 0.0671  -0.0849 106 PRO A C   
847  O O   . PRO A 106 ? 0.7232 0.6244 0.8995 -0.2968 0.0763  -0.0706 106 PRO A O   
848  C CB  . PRO A 106 ? 0.6899 0.6243 0.8053 -0.2701 0.0480  -0.0818 106 PRO A CB  
849  C CG  . PRO A 106 ? 0.6465 0.5989 0.7586 -0.2452 0.0567  -0.0677 106 PRO A CG  
850  C CD  . PRO A 106 ? 0.6258 0.5671 0.7531 -0.2369 0.0786  -0.0542 106 PRO A CD  
851  N N   . LYS A 107 ? 0.7556 0.6198 0.8834 -0.3108 0.0573  -0.1045 107 LYS A N   
852  C CA  . LYS A 107 ? 0.8195 0.6723 0.9736 -0.3358 0.0545  -0.1090 107 LYS A CA  
853  C C   . LYS A 107 ? 0.8183 0.7115 1.0069 -0.3542 0.0325  -0.1067 107 LYS A C   
854  O O   . LYS A 107 ? 0.8055 0.7121 1.0392 -0.3676 0.0359  -0.0985 107 LYS A O   
855  C CB  . LYS A 107 ? 0.8669 0.6759 0.9921 -0.3491 0.0524  -0.1331 107 LYS A CB  
856  C CG  . LYS A 107 ? 0.8721 0.6574 1.0218 -0.3725 0.0543  -0.1377 107 LYS A CG  
857  C CD  . LYS A 107 ? 0.9589 0.6959 1.0783 -0.3830 0.0554  -0.1638 107 LYS A CD  
858  C CE  . LYS A 107 ? 1.0369 0.7435 1.1810 -0.4041 0.0599  -0.1671 107 LYS A CE  
859  N NZ  . LYS A 107 ? 1.2070 0.8634 1.3231 -0.4137 0.0624  -0.1950 107 LYS A NZ  
860  N N   . SER A 108 ? 0.8618 0.7742 1.0321 -0.3557 0.0093  -0.1132 108 SER A N   
861  C CA  . SER A 108 ? 0.8626 0.8097 1.0657 -0.3735 -0.0192 -0.1118 108 SER A CA  
862  C C   . SER A 108 ? 0.8409 0.8303 1.0591 -0.3570 -0.0300 -0.0975 108 SER A C   
863  O O   . SER A 108 ? 0.8737 0.9004 1.1494 -0.3578 -0.0330 -0.0855 108 SER A O   
864  C CB  . SER A 108 ? 0.9095 0.8353 1.0754 -0.3968 -0.0456 -0.1324 108 SER A CB  
865  O OG  . SER A 108 ? 0.9190 0.8350 1.0280 -0.3871 -0.0516 -0.1391 108 SER A OG  
866  N N   . GLY A 109 ? 0.7398 0.7240 0.9112 -0.3426 -0.0344 -0.0994 109 GLY A N   
867  C CA  . GLY A 109 ? 0.6781 0.6965 0.8584 -0.3304 -0.0504 -0.0878 109 GLY A CA  
868  C C   . GLY A 109 ? 0.6508 0.6774 0.8265 -0.3012 -0.0267 -0.0756 109 GLY A C   
869  O O   . GLY A 109 ? 0.6252 0.6411 0.8083 -0.2904 0.0015  -0.0706 109 GLY A O   
870  N N   . GLN A 110 ? 0.6191 0.6622 0.7800 -0.2896 -0.0404 -0.0699 110 GLN A N   
871  C CA  . GLN A 110 ? 0.5822 0.6354 0.7380 -0.2632 -0.0233 -0.0590 110 GLN A CA  
872  C C   . GLN A 110 ? 0.5891 0.6098 0.6875 -0.2531 -0.0086 -0.0676 110 GLN A C   
873  O O   . GLN A 110 ? 0.6972 0.6948 0.7538 -0.2654 -0.0178 -0.0818 110 GLN A O   
874  C CB  . GLN A 110 ? 0.5643 0.6481 0.7344 -0.2565 -0.0466 -0.0495 110 GLN A CB  
875  C CG  . GLN A 110 ? 0.6214 0.7215 0.7993 -0.2306 -0.0309 -0.0377 110 GLN A CG  
876  C CD  . GLN A 110 ? 0.6708 0.8006 0.8737 -0.2252 -0.0558 -0.0285 110 GLN A CD  
877  O OE1 . GLN A 110 ? 0.6790 0.8008 0.8455 -0.2278 -0.0779 -0.0291 110 GLN A OE1 
878  N NE2 . GLN A 110 ? 0.7115 0.8738 0.9774 -0.2185 -0.0514 -0.0203 110 GLN A NE2 
879  N N   . SER A 111 ? 0.5631 0.5819 0.6605 -0.2315 0.0145  -0.0599 111 SER A N   
880  C CA  . SER A 111 ? 0.5938 0.5852 0.6500 -0.2198 0.0292  -0.0677 111 SER A CA  
881  C C   . SER A 111 ? 0.6694 0.6671 0.6936 -0.2129 0.0190  -0.0693 111 SER A C   
882  O O   . SER A 111 ? 0.6192 0.6424 0.6564 -0.2029 0.0110  -0.0570 111 SER A O   
883  C CB  . SER A 111 ? 0.6117 0.5972 0.6783 -0.2003 0.0524  -0.0572 111 SER A CB  
884  O OG  . SER A 111 ? 0.5647 0.5288 0.6011 -0.1865 0.0629  -0.0635 111 SER A OG  
885  N N   . GLN A 112 ? 0.5978 0.5705 0.5806 -0.2194 0.0213  -0.0853 112 GLN A N   
886  C CA  . GLN A 112 ? 0.6480 0.6207 0.5948 -0.2146 0.0181  -0.0883 112 GLN A CA  
887  C C   . GLN A 112 ? 0.6611 0.6250 0.6009 -0.1936 0.0405  -0.0902 112 GLN A C   
888  O O   . GLN A 112 ? 0.6764 0.6412 0.5909 -0.1888 0.0418  -0.0929 112 GLN A O   
889  C CB  . GLN A 112 ? 0.6542 0.6042 0.5554 -0.2377 0.0094  -0.1068 112 GLN A CB  
890  C CG  . GLN A 112 ? 0.6637 0.6148 0.5654 -0.2625 -0.0165 -0.1082 112 GLN A CG  
891  C CD  . GLN A 112 ? 0.7197 0.6430 0.5621 -0.2867 -0.0249 -0.1267 112 GLN A CD  
892  O OE1 . GLN A 112 ? 0.8363 0.7427 0.6391 -0.2847 -0.0088 -0.1381 112 GLN A OE1 
893  N NE2 . GLN A 112 ? 0.7567 0.6743 0.5920 -0.3112 -0.0495 -0.1307 112 GLN A NE2 
894  N N   . LEU A 113 ? 0.6431 0.5970 0.6050 -0.1822 0.0567  -0.0882 113 LEU A N   
895  C CA  . LEU A 113 ? 0.5850 0.5269 0.5444 -0.1632 0.0739  -0.0907 113 LEU A CA  
896  C C   . LEU A 113 ? 0.5734 0.5341 0.5475 -0.1425 0.0754  -0.0723 113 LEU A C   
897  O O   . LEU A 113 ? 0.6145 0.5661 0.5905 -0.1260 0.0858  -0.0714 113 LEU A O   
898  C CB  . LEU A 113 ? 0.6789 0.5928 0.6512 -0.1624 0.0866  -0.0979 113 LEU A CB  
899  C CG  . LEU A 113 ? 0.6690 0.5607 0.6258 -0.1834 0.0869  -0.1194 113 LEU A CG  
900  C CD1 . LEU A 113 ? 0.6997 0.5602 0.6725 -0.1819 0.0991  -0.1271 113 LEU A CD1 
901  C CD2 . LEU A 113 ? 0.6537 0.5400 0.5776 -0.1880 0.0915  -0.1378 113 LEU A CD2 
902  N N   . GLY A 114 ? 0.6040 0.5896 0.5901 -0.1433 0.0645  -0.0588 114 GLY A N   
903  C CA  . GLY A 114 ? 0.5588 0.5605 0.5571 -0.1256 0.0676  -0.0436 114 GLY A CA  
904  C C   . GLY A 114 ? 0.5592 0.5854 0.5839 -0.1297 0.0601  -0.0320 114 GLY A C   
905  O O   . GLY A 114 ? 0.5800 0.6109 0.6206 -0.1456 0.0526  -0.0340 114 GLY A O   
906  N N   . ARG A 115 ? 0.5870 0.6292 0.6199 -0.1152 0.0626  -0.0212 115 ARG A N   
907  C CA  . ARG A 115 ? 0.5171 0.5846 0.5821 -0.1156 0.0597  -0.0118 115 ARG A CA  
908  C C   . ARG A 115 ? 0.5367 0.6012 0.6082 -0.1040 0.0790  -0.0029 115 ARG A C   
909  O O   . ARG A 115 ? 0.6123 0.6752 0.6687 -0.0890 0.0835  0.0010  115 ARG A O   
910  C CB  . ARG A 115 ? 0.6161 0.7038 0.6834 -0.1104 0.0442  -0.0089 115 ARG A CB  
911  C CG  . ARG A 115 ? 0.7768 0.8915 0.8849 -0.1060 0.0433  -0.0007 115 ARG A CG  
912  C CD  . ARG A 115 ? 0.8306 0.9635 0.9731 -0.1213 0.0246  -0.0013 115 ARG A CD  
913  N NE  . ARG A 115 ? 0.9152 1.0742 1.0922 -0.1143 0.0118  0.0047  115 ARG A NE  
914  C CZ  . ARG A 115 ? 0.8522 1.0326 1.0747 -0.1072 0.0243  0.0082  115 ARG A CZ  
915  N NH1 . ARG A 115 ? 0.8046 0.9827 1.0381 -0.1085 0.0506  0.0077  115 ARG A NH1 
916  N NH2 . ARG A 115 ? 0.8677 1.0703 1.1253 -0.0994 0.0111  0.0119  115 ARG A NH2 
917  N N   . TRP A 116 ? 0.5713 0.6328 0.6618 -0.1130 0.0902  0.0003  116 TRP A N   
918  C CA  . TRP A 116 ? 0.5848 0.6366 0.6721 -0.1068 0.1104  0.0093  116 TRP A CA  
919  C C   . TRP A 116 ? 0.6064 0.6862 0.7259 -0.1060 0.1190  0.0138  116 TRP A C   
920  O O   . TRP A 116 ? 0.6088 0.7135 0.7679 -0.1158 0.1122  0.0109  116 TRP A O   
921  C CB  . TRP A 116 ? 0.6712 0.6983 0.7569 -0.1188 0.1213  0.0112  116 TRP A CB  
922  C CG  . TRP A 116 ? 0.6426 0.6543 0.7174 -0.1168 0.1419  0.0225  116 TRP A CG  
923  C CD1 . TRP A 116 ? 0.6597 0.6439 0.6976 -0.1051 0.1467  0.0298  116 TRP A CD1 
924  C CD2 . TRP A 116 ? 0.6251 0.6457 0.7234 -0.1289 0.1605  0.0277  116 TRP A CD2 
925  N NE1 . TRP A 116 ? 0.6368 0.6083 0.6650 -0.1103 0.1662  0.0403  116 TRP A NE1 
926  C CE2 . TRP A 116 ? 0.6115 0.6055 0.6768 -0.1253 0.1778  0.0384  116 TRP A CE2 
927  C CE3 . TRP A 116 ? 0.6279 0.6766 0.7739 -0.1435 0.1639  0.0240  116 TRP A CE3 
928  C CZ2 . TRP A 116 ? 0.6520 0.6445 0.7243 -0.1374 0.2026  0.0449  116 TRP A CZ2 
929  C CZ3 . TRP A 116 ? 0.5980 0.6500 0.7614 -0.1540 0.1889  0.0293  116 TRP A CZ3 
930  C CH2 . TRP A 116 ? 0.6151 0.6383 0.7390 -0.1516 0.2101  0.0394  116 TRP A CH2 
931  N N   . MET A 117 ? 0.6210 0.6956 0.7248 -0.0946 0.1337  0.0196  117 MET A N   
932  C CA  . MET A 117 ? 0.6033 0.6994 0.7343 -0.0934 0.1494  0.0214  117 MET A CA  
933  C C   . MET A 117 ? 0.5658 0.6371 0.6671 -0.0938 0.1744  0.0285  117 MET A C   
934  O O   . MET A 117 ? 0.6386 0.6812 0.6943 -0.0855 0.1725  0.0332  117 MET A O   
935  C CB  . MET A 117 ? 0.6309 0.7463 0.7679 -0.0784 0.1401  0.0189  117 MET A CB  
936  C CG  . MET A 117 ? 0.6000 0.7385 0.7724 -0.0756 0.1574  0.0175  117 MET A CG  
937  S SD  . MET A 117 ? 0.6743 0.8298 0.8548 -0.0572 0.1452  0.0143  117 MET A SD  
938  C CE  . MET A 117 ? 0.6633 0.8394 0.8756 -0.0617 0.1100  0.0129  117 MET A CE  
939  N N   . SER A 118 ? 0.6531 0.7343 0.7801 -0.1048 0.1972  0.0293  118 SER A N   
940  C CA  . SER A 118 ? 0.7471 0.8006 0.8385 -0.1095 0.2233  0.0367  118 SER A CA  
941  C C   . SER A 118 ? 0.7187 0.7692 0.7822 -0.0956 0.2316  0.0363  118 SER A C   
942  O O   . SER A 118 ? 0.6800 0.7558 0.7655 -0.0834 0.2221  0.0293  118 SER A O   
943  C CB  . SER A 118 ? 0.6696 0.7355 0.7974 -0.1281 0.2500  0.0360  118 SER A CB  
944  O OG  . SER A 118 ? 0.6770 0.7827 0.8569 -0.1251 0.2606  0.0269  118 SER A OG  
945  N N   . GLU A 119 ? 0.7070 0.7220 0.7177 -0.0985 0.2478  0.0444  119 GLU A N   
946  C CA  . GLU A 119 ? 0.8709 0.8780 0.8483 -0.0886 0.2575  0.0430  119 GLU A CA  
947  C C   . GLU A 119 ? 0.7810 0.8207 0.8014 -0.0904 0.2824  0.0319  119 GLU A C   
948  O O   . GLU A 119 ? 0.7571 0.8120 0.7856 -0.0768 0.2794  0.0241  119 GLU A O   
949  C CB  . GLU A 119 ? 0.8887 0.8472 0.7963 -0.0956 0.2694  0.0548  119 GLU A CB  
950  C CG  . GLU A 119 ? 0.9435 0.8690 0.8064 -0.0858 0.2408  0.0642  119 GLU A CG  
951  C CD  . GLU A 119 ? 1.0116 0.9172 0.8764 -0.0940 0.2302  0.0725  119 GLU A CD  
952  O OE1 . GLU A 119 ? 0.9574 0.8716 0.8515 -0.1094 0.2453  0.0721  119 GLU A OE1 
953  O OE2 . GLU A 119 ? 1.0412 0.9226 0.8820 -0.0851 0.2068  0.0784  119 GLU A OE2 
954  N N   . GLU A 120 ? 0.7861 0.8369 0.8395 -0.1074 0.3077  0.0303  120 GLU A N   
955  C CA  . GLU A 120 ? 0.8116 0.8953 0.9161 -0.1096 0.3352  0.0177  120 GLU A CA  
956  C C   . GLU A 120 ? 0.7139 0.8410 0.8842 -0.0947 0.3127  0.0081  120 GLU A C   
957  O O   . GLU A 120 ? 0.6770 0.8209 0.8677 -0.0835 0.3213  -0.0018 120 GLU A O   
958  C CB  . GLU A 120 ? 0.8125 0.9055 0.9534 -0.1317 0.3633  0.0171  120 GLU A CB  
959  C CG  . GLU A 120 ? 0.9250 0.9711 0.9967 -0.1459 0.3793  0.0275  120 GLU A CG  
960  C CD  . GLU A 120 ? 1.0051 1.0130 1.0298 -0.1524 0.3636  0.0437  120 GLU A CD  
961  O OE1 . GLU A 120 ? 0.8978 0.9197 0.9485 -0.1433 0.3308  0.0436  120 GLU A OE1 
962  O OE2 . GLU A 120 ? 1.1171 1.0800 1.0775 -0.1615 0.3697  0.0553  120 GLU A OE2 
963  N N   . ASP A 121 ? 0.6795 0.8216 0.8805 -0.0951 0.2828  0.0108  121 ASP A N   
964  C CA  . ASP A 121 ? 0.6140 0.7920 0.8709 -0.0837 0.2573  0.0045  121 ASP A CA  
965  C C   . ASP A 121 ? 0.6491 0.8177 0.8716 -0.0646 0.2383  0.0044  121 ASP A C   
966  O O   . ASP A 121 ? 0.6082 0.8003 0.8685 -0.0530 0.2310  -0.0022 121 ASP A O   
967  C CB  . ASP A 121 ? 0.6464 0.8348 0.9290 -0.0918 0.2287  0.0077  121 ASP A CB  
968  C CG  . ASP A 121 ? 0.6916 0.8935 1.0189 -0.1117 0.2447  0.0065  121 ASP A CG  
969  O OD1 . ASP A 121 ? 0.6885 0.9050 1.0490 -0.1176 0.2768  0.0009  121 ASP A OD1 
970  O OD2 . ASP A 121 ? 0.6775 0.8753 1.0081 -0.1225 0.2267  0.0097  121 ASP A OD2 
971  N N   . PHE A 122 ? 0.6198 0.7540 0.7751 -0.0612 0.2290  0.0118  122 PHE A N   
972  C CA  . PHE A 122 ? 0.6351 0.7613 0.7609 -0.0448 0.2113  0.0113  122 PHE A CA  
973  C C   . PHE A 122 ? 0.6389 0.7620 0.7540 -0.0368 0.2326  0.0047  122 PHE A C   
974  O O   . PHE A 122 ? 0.6233 0.7567 0.7499 -0.0235 0.2213  -0.0004 122 PHE A O   
975  C CB  . PHE A 122 ? 0.6282 0.7208 0.6938 -0.0431 0.1971  0.0192  122 PHE A CB  
976  C CG  . PHE A 122 ? 0.6048 0.6889 0.6414 -0.0282 0.1817  0.0182  122 PHE A CG  
977  C CD1 . PHE A 122 ? 0.5593 0.6618 0.6186 -0.0205 0.1586  0.0153  122 PHE A CD1 
978  C CD2 . PHE A 122 ? 0.5876 0.6433 0.5725 -0.0236 0.1894  0.0206  122 PHE A CD2 
979  C CE1 . PHE A 122 ? 0.5441 0.6387 0.5790 -0.0086 0.1461  0.0143  122 PHE A CE1 
980  C CE2 . PHE A 122 ? 0.6285 0.6778 0.5912 -0.0111 0.1743  0.0189  122 PHE A CE2 
981  C CZ  . PHE A 122 ? 0.5704 0.6401 0.5603 -0.0037 0.1540  0.0155  122 PHE A CZ  
982  N N   . GLU A 123 ? 0.6638 0.7691 0.7526 -0.0461 0.2642  0.0043  123 GLU A N   
983  C CA  . GLU A 123 ? 0.6148 0.7138 0.6881 -0.0409 0.2881  -0.0048 123 GLU A CA  
984  C C   . GLU A 123 ? 0.6088 0.7469 0.7574 -0.0334 0.2953  -0.0180 123 GLU A C   
985  O O   . GLU A 123 ? 0.6273 0.7666 0.7764 -0.0207 0.2966  -0.0265 123 GLU A O   
986  C CB  . GLU A 123 ? 0.7834 0.8560 0.8155 -0.0569 0.3244  -0.0036 123 GLU A CB  
987  C CG  . GLU A 123 ? 0.9225 0.9753 0.9124 -0.0538 0.3477  -0.0127 123 GLU A CG  
988  C CD  . GLU A 123 ? 1.0890 1.1170 1.0411 -0.0702 0.3738  -0.0127 123 GLU A CD  
989  O OE1 . GLU A 123 ? 1.0292 1.0790 1.0307 -0.0793 0.3924  -0.0189 123 GLU A OE1 
990  O OE2 . GLU A 123 ? 1.1850 1.1708 1.0586 -0.0743 0.3723  -0.0062 123 GLU A OE2 
991  N N   . LYS A 124 ? 0.5589 0.7285 0.7754 -0.0409 0.2981  -0.0199 124 LYS A N   
992  C CA  . LYS A 124 ? 0.5716 0.7804 0.8712 -0.0326 0.2989  -0.0313 124 LYS A CA  
993  C C   . LYS A 124 ? 0.5376 0.7560 0.8521 -0.0166 0.2585  -0.0284 124 LYS A C   
994  O O   . LYS A 124 ? 0.5738 0.8039 0.9200 -0.0030 0.2576  -0.0370 124 LYS A O   
995  C CB  . LYS A 124 ? 0.4929 0.7333 0.8641 -0.0456 0.3049  -0.0325 124 LYS A CB  
996  C CG  . LYS A 124 ? 0.6651 0.8937 1.0199 -0.0643 0.3450  -0.0343 124 LYS A CG  
997  C CD  . LYS A 124 ? 0.6485 0.9024 1.0637 -0.0789 0.3423  -0.0329 124 LYS A CD  
998  C CE  . LYS A 124 ? 0.7609 0.9898 1.1368 -0.0973 0.3704  -0.0306 124 LYS A CE  
999  N NZ  . LYS A 124 ? 0.8311 1.0817 1.2623 -0.1129 0.3682  -0.0292 124 LYS A NZ  
1000 N N   . ALA A 125 ? 0.5363 0.7471 0.8269 -0.0189 0.2261  -0.0169 125 ALA A N   
1001 C CA  . ALA A 125 ? 0.5599 0.7743 0.8531 -0.0074 0.1897  -0.0130 125 ALA A CA  
1002 C C   . ALA A 125 ? 0.5502 0.7411 0.7929 0.0050  0.1896  -0.0147 125 ALA A C   
1003 O O   . ALA A 125 ? 0.5782 0.7760 0.8406 0.0171  0.1739  -0.0171 125 ALA A O   
1004 C CB  . ALA A 125 ? 0.4619 0.6692 0.7322 -0.0157 0.1617  -0.0029 125 ALA A CB  
1005 N N   . PHE A 126 ? 0.5750 0.7360 0.7526 0.0016  0.2045  -0.0127 126 PHE A N   
1006 C CA  . PHE A 126 ? 0.5913 0.7288 0.7196 0.0116  0.2022  -0.0145 126 PHE A CA  
1007 C C   . PHE A 126 ? 0.5978 0.7409 0.7486 0.0202  0.2227  -0.0277 126 PHE A C   
1008 O O   . PHE A 126 ? 0.6180 0.7623 0.7775 0.0324  0.2084  -0.0313 126 PHE A O   
1009 C CB  . PHE A 126 ? 0.6244 0.7278 0.6821 0.0047  0.2117  -0.0089 126 PHE A CB  
1010 C CG  . PHE A 126 ? 0.6090 0.6869 0.6152 0.0129  0.2091  -0.0113 126 PHE A CG  
1011 C CD1 . PHE A 126 ? 0.5462 0.6151 0.5290 0.0196  0.1810  -0.0060 126 PHE A CD1 
1012 C CD2 . PHE A 126 ? 0.6436 0.7057 0.6240 0.0122  0.2358  -0.0200 126 PHE A CD2 
1013 C CE1 . PHE A 126 ? 0.6269 0.6737 0.5671 0.0260  0.1766  -0.0085 126 PHE A CE1 
1014 C CE2 . PHE A 126 ? 0.6398 0.6762 0.5701 0.0181  0.2308  -0.0228 126 PHE A CE2 
1015 C CZ  . PHE A 126 ? 0.5830 0.6129 0.4957 0.0252  0.1996  -0.0166 126 PHE A CZ  
1016 N N   . ASN A 127 ? 0.5599 0.7051 0.7213 0.0130  0.2584  -0.0361 127 ASN A N   
1017 C CA  . ASN A 127 ? 0.6080 0.7571 0.7916 0.0200  0.2845  -0.0524 127 ASN A CA  
1018 C C   . ASN A 127 ? 0.5850 0.7680 0.8544 0.0323  0.2717  -0.0589 127 ASN A C   
1019 O O   . ASN A 127 ? 0.5334 0.7185 0.8266 0.0426  0.2856  -0.0729 127 ASN A O   
1020 C CB  . ASN A 127 ? 0.6941 0.8403 0.8754 0.0064  0.3294  -0.0611 127 ASN A CB  
1021 C CG  . ASN A 127 ? 0.7506 0.8540 0.8375 -0.0052 0.3429  -0.0550 127 ASN A CG  
1022 O OD1 . ASN A 127 ? 0.7763 0.8519 0.8034 0.0005  0.3265  -0.0514 127 ASN A OD1 
1023 N ND2 . ASN A 127 ? 0.8592 0.9547 0.9316 -0.0220 0.3638  -0.0520 127 ASN A ND2 
1024 N N   . ALA A 128 ? 0.5845 0.7913 0.8996 0.0309  0.2441  -0.0493 128 ALA A N   
1025 C CA  . ALA A 128 ? 0.5406 0.7761 0.9347 0.0417  0.2229  -0.0514 128 ALA A CA  
1026 C C   . ALA A 128 ? 0.5692 0.7928 0.9437 0.0527  0.1857  -0.0435 128 ALA A C   
1027 O O   . ALA A 128 ? 0.5849 0.8253 1.0167 0.0619  0.1630  -0.0425 128 ALA A O   
1028 C CB  . ALA A 128 ? 0.4812 0.7453 0.9307 0.0322  0.2076  -0.0443 128 ALA A CB  
1029 N N   . ARG A 129 ? 0.5471 0.7414 0.8447 0.0515  0.1786  -0.0375 129 ARG A N   
1030 C CA  . ARG A 129 ? 0.5147 0.6972 0.7893 0.0579  0.1451  -0.0291 129 ARG A CA  
1031 C C   . ARG A 129 ? 0.5291 0.6846 0.7539 0.0653  0.1518  -0.0349 129 ARG A C   
1032 O O   . ARG A 129 ? 0.5077 0.6595 0.7472 0.0756  0.1374  -0.0367 129 ARG A O   
1033 C CB  . ARG A 129 ? 0.5159 0.6921 0.7527 0.0471  0.1233  -0.0155 129 ARG A CB  
1034 C CG  . ARG A 129 ? 0.4543 0.6535 0.7363 0.0392  0.1054  -0.0087 129 ARG A CG  
1035 C CD  . ARG A 129 ? 0.4442 0.6338 0.6840 0.0266  0.0933  0.0002  129 ARG A CD  
1036 N NE  . ARG A 129 ? 0.5091 0.7150 0.7824 0.0182  0.0685  0.0067  129 ARG A NE  
1037 C CZ  . ARG A 129 ? 0.5280 0.7555 0.8499 0.0112  0.0730  0.0051  129 ARG A CZ  
1038 N NH1 . ARG A 129 ? 0.5148 0.7514 0.8597 0.0107  0.1050  -0.0029 129 ARG A NH1 
1039 N NH2 . ARG A 129 ? 0.5201 0.7592 0.8670 0.0026  0.0449  0.0114  129 ARG A NH2 
1040 N N   . PHE A 130 ? 0.5294 0.6637 0.6952 0.0595  0.1710  -0.0373 130 PHE A N   
1041 C CA  . PHE A 130 ? 0.5641 0.6706 0.6729 0.0635  0.1667  -0.0391 130 PHE A CA  
1042 C C   . PHE A 130 ? 0.5977 0.6913 0.7022 0.0707  0.1892  -0.0552 130 PHE A C   
1043 O O   . PHE A 130 ? 0.6045 0.6814 0.6865 0.0773  0.1775  -0.0580 130 PHE A O   
1044 C CB  . PHE A 130 ? 0.5807 0.6668 0.6263 0.0539  0.1689  -0.0321 130 PHE A CB  
1045 C CG  . PHE A 130 ? 0.6317 0.7193 0.6656 0.0503  0.1412  -0.0194 130 PHE A CG  
1046 C CD1 . PHE A 130 ? 0.5689 0.6434 0.5748 0.0540  0.1214  -0.0167 130 PHE A CD1 
1047 C CD2 . PHE A 130 ? 0.5723 0.6742 0.6253 0.0422  0.1368  -0.0120 130 PHE A CD2 
1048 C CE1 . PHE A 130 ? 0.5094 0.5857 0.5070 0.0496  0.1008  -0.0077 130 PHE A CE1 
1049 C CE2 . PHE A 130 ? 0.5668 0.6679 0.6072 0.0379  0.1148  -0.0034 130 PHE A CE2 
1050 C CZ  . PHE A 130 ? 0.5450 0.6337 0.5582 0.0417  0.0984  -0.0018 130 PHE A CZ  
1051 N N   . PRO A 131 ? 0.6283 0.7275 0.7524 0.0685  0.2231  -0.0675 131 PRO A N   
1052 C CA  . PRO A 131 ? 0.6039 0.6881 0.7209 0.0744  0.2479  -0.0863 131 PRO A CA  
1053 C C   . PRO A 131 ? 0.6127 0.7006 0.7713 0.0894  0.2307  -0.0920 131 PRO A C   
1054 O O   . PRO A 131 ? 0.5559 0.6697 0.7887 0.0971  0.2224  -0.0920 131 PRO A O   
1055 C CB  . PRO A 131 ? 0.5484 0.6492 0.7058 0.0694  0.2868  -0.0987 131 PRO A CB  
1056 C CG  . PRO A 131 ? 0.6251 0.7323 0.7668 0.0556  0.2868  -0.0847 131 PRO A CG  
1057 C CD  . PRO A 131 ? 0.5452 0.6616 0.6933 0.0582  0.2439  -0.0665 131 PRO A CD  
1058 N N   . GLY A 132 ? 0.6378 0.6983 0.7496 0.0929  0.2227  -0.0962 132 GLY A N   
1059 C CA  . GLY A 132 ? 0.5694 0.6263 0.7124 0.1057  0.2066  -0.1014 132 GLY A CA  
1060 C C   . GLY A 132 ? 0.5451 0.6120 0.7102 0.1089  0.1662  -0.0831 132 GLY A C   
1061 O O   . GLY A 132 ? 0.5584 0.6219 0.7551 0.1187  0.1504  -0.0845 132 GLY A O   
1062 N N   . CYS A 133 ? 0.5226 0.5982 0.6687 0.0997  0.1497  -0.0664 133 CYS A N   
1063 C CA  . CYS A 133 ? 0.5597 0.6447 0.7249 0.0994  0.1150  -0.0500 133 CYS A CA  
1064 C C   . CYS A 133 ? 0.5116 0.5752 0.6456 0.1011  0.0937  -0.0461 133 CYS A C   
1065 O O   . CYS A 133 ? 0.6029 0.6692 0.7551 0.1012  0.0672  -0.0346 133 CYS A O   
1066 C CB  . CYS A 133 ? 0.4777 0.5732 0.6234 0.0876  0.1070  -0.0368 133 CYS A CB  
1067 S SG  . CYS A 133 ? 0.5727 0.6458 0.6393 0.0788  0.1084  -0.0335 133 CYS A SG  
1068 N N   . MET A 134 ? 0.5084 0.5494 0.5940 0.1005  0.1034  -0.0549 134 MET A N   
1069 C CA  . MET A 134 ? 0.5196 0.5411 0.5778 0.1004  0.0844  -0.0524 134 MET A CA  
1070 C C   . MET A 134 ? 0.5877 0.5920 0.6596 0.1100  0.0897  -0.0664 134 MET A C   
1071 O O   . MET A 134 ? 0.6224 0.6060 0.6652 0.1089  0.0795  -0.0686 134 MET A O   
1072 C CB  . MET A 134 ? 0.5195 0.5269 0.5172 0.0921  0.0845  -0.0516 134 MET A CB  
1073 C CG  . MET A 134 ? 0.4323 0.4524 0.4175 0.0832  0.0747  -0.0379 134 MET A CG  
1074 S SD  . MET A 134 ? 0.5654 0.5683 0.4928 0.0763  0.0688  -0.0368 134 MET A SD  
1075 C CE  . MET A 134 ? 0.5242 0.5446 0.4544 0.0684  0.0616  -0.0235 134 MET A CE  
1076 N N   . LYS A 135 ? 0.5721 0.5847 0.6922 0.1194  0.1059  -0.0772 135 LYS A N   
1077 C CA  . LYS A 135 ? 0.5807 0.5755 0.7189 0.1297  0.1142  -0.0937 135 LYS A CA  
1078 C C   . LYS A 135 ? 0.6314 0.6114 0.7756 0.1321  0.0841  -0.0845 135 LYS A C   
1079 O O   . LYS A 135 ? 0.6230 0.6137 0.7936 0.1311  0.0591  -0.0669 135 LYS A O   
1080 C CB  . LYS A 135 ? 0.5442 0.5565 0.7534 0.1407  0.1318  -0.1046 135 LYS A CB  
1081 C CG  . LYS A 135 ? 0.6491 0.6439 0.8651 0.1488  0.1616  -0.1312 135 LYS A CG  
1082 C CD  . LYS A 135 ? 0.7200 0.7031 0.8733 0.1385  0.1939  -0.1444 135 LYS A CD  
1083 C CE  . LYS A 135 ? 0.8401 0.8018 0.9912 0.1437  0.2269  -0.1735 135 LYS A CE  
1084 N NZ  . LYS A 135 ? 0.8874 0.8313 0.9661 0.1306  0.2575  -0.1854 135 LYS A NZ  
1085 N N   . GLY A 136 ? 0.6682 0.6207 0.7833 0.1332  0.0862  -0.0962 136 GLY A N   
1086 C CA  . GLY A 136 ? 0.6103 0.5443 0.7286 0.1338  0.0607  -0.0892 136 GLY A CA  
1087 C C   . GLY A 136 ? 0.6536 0.5870 0.7350 0.1208  0.0372  -0.0708 136 GLY A C   
1088 O O   . GLY A 136 ? 0.6089 0.5263 0.6904 0.1182  0.0172  -0.0635 136 GLY A O   
1089 N N   . ARG A 137 ? 0.6518 0.6009 0.7038 0.1118  0.0405  -0.0638 137 ARG A N   
1090 C CA  . ARG A 137 ? 0.5742 0.5260 0.5980 0.0996  0.0223  -0.0491 137 ARG A CA  
1091 C C   . ARG A 137 ? 0.6276 0.5704 0.6024 0.0930  0.0279  -0.0562 137 ARG A C   
1092 O O   . ARG A 137 ? 0.5972 0.5325 0.5511 0.0958  0.0454  -0.0696 137 ARG A O   
1093 C CB  . ARG A 137 ? 0.5313 0.5076 0.5661 0.0944  0.0176  -0.0345 137 ARG A CB  
1094 C CG  . ARG A 137 ? 0.6191 0.6049 0.7016 0.0992  0.0061  -0.0251 137 ARG A CG  
1095 C CD  . ARG A 137 ? 0.5815 0.5864 0.6641 0.0898  -0.0037 -0.0101 137 ARG A CD  
1096 N NE  . ARG A 137 ? 0.5873 0.5992 0.7129 0.0928  -0.0204 0.0003  137 ARG A NE  
1097 C CZ  . ARG A 137 ? 0.6072 0.6052 0.7364 0.0884  -0.0453 0.0138  137 ARG A CZ  
1098 N NH1 . ARG A 137 ? 0.6090 0.5870 0.7040 0.0800  -0.0529 0.0175  137 ARG A NH1 
1099 N NH2 . ARG A 137 ? 0.5905 0.5935 0.7591 0.0912  -0.0641 0.0244  137 ARG A NH2 
1100 N N   . THR A 138 ? 0.5406 0.4831 0.4972 0.0830  0.0123  -0.0472 138 THR A N   
1101 C CA  . THR A 138 ? 0.6205 0.5586 0.5399 0.0766  0.0114  -0.0512 138 THR A CA  
1102 C C   . THR A 138 ? 0.5941 0.5509 0.5046 0.0730  0.0160  -0.0439 138 THR A C   
1103 O O   . THR A 138 ? 0.5468 0.5204 0.4749 0.0696  0.0120  -0.0327 138 THR A O   
1104 C CB  . THR A 138 ? 0.6180 0.5498 0.5322 0.0673  -0.0057 -0.0469 138 THR A CB  
1105 O OG1 . THR A 138 ? 0.6043 0.5142 0.5236 0.0696  -0.0103 -0.0544 138 THR A OG1 
1106 C CG2 . THR A 138 ? 0.5860 0.5177 0.4730 0.0614  -0.0100 -0.0504 138 THR A CG2 
1107 N N   . MET A 139 ? 0.6099 0.5601 0.4898 0.0729  0.0232  -0.0502 139 MET A N   
1108 C CA  . MET A 139 ? 0.5900 0.5519 0.4579 0.0691  0.0247  -0.0432 139 MET A CA  
1109 C C   . MET A 139 ? 0.5591 0.5192 0.4140 0.0628  0.0084  -0.0410 139 MET A C   
1110 O O   . MET A 139 ? 0.5915 0.5347 0.4215 0.0620  0.0017  -0.0480 139 MET A O   
1111 C CB  . MET A 139 ? 0.6179 0.5702 0.4586 0.0711  0.0407  -0.0489 139 MET A CB  
1112 C CG  . MET A 139 ? 0.5757 0.5331 0.3997 0.0667  0.0385  -0.0405 139 MET A CG  
1113 S SD  . MET A 139 ? 0.6646 0.6015 0.4428 0.0648  0.0547  -0.0441 139 MET A SD  
1114 C CE  . MET A 139 ? 0.6523 0.6059 0.4614 0.0675  0.0811  -0.0453 139 MET A CE  
1115 N N   . TYR A 140 ? 0.5464 0.5235 0.4196 0.0576  0.0020  -0.0324 140 TYR A N   
1116 C CA  . TYR A 140 ? 0.5045 0.4851 0.3774 0.0520  -0.0102 -0.0318 140 TYR A CA  
1117 C C   . TYR A 140 ? 0.5609 0.5442 0.4223 0.0531  -0.0101 -0.0291 140 TYR A C   
1118 O O   . TYR A 140 ? 0.4980 0.4890 0.3616 0.0543  0.0000  -0.0241 140 TYR A O   
1119 C CB  . TYR A 140 ? 0.5304 0.5257 0.4274 0.0440  -0.0130 -0.0264 140 TYR A CB  
1120 C CG  . TYR A 140 ? 0.4841 0.4720 0.3898 0.0409  -0.0163 -0.0259 140 TYR A CG  
1121 C CD1 . TYR A 140 ? 0.5371 0.5159 0.4440 0.0359  -0.0253 -0.0306 140 TYR A CD1 
1122 C CD2 . TYR A 140 ? 0.4647 0.4531 0.3799 0.0426  -0.0124 -0.0200 140 TYR A CD2 
1123 C CE1 . TYR A 140 ? 0.5958 0.5634 0.5094 0.0322  -0.0289 -0.0289 140 TYR A CE1 
1124 C CE2 . TYR A 140 ? 0.5115 0.4887 0.4350 0.0402  -0.0187 -0.0175 140 TYR A CE2 
1125 C CZ  . TYR A 140 ? 0.5600 0.5254 0.4809 0.0348  -0.0261 -0.0217 140 TYR A CZ  
1126 O OH  . TYR A 140 ? 0.6394 0.5895 0.5674 0.0316  -0.0329 -0.0180 140 TYR A OH  
1127 N N   . VAL A 141 ? 0.5659 0.5412 0.4167 0.0524  -0.0234 -0.0319 141 VAL A N   
1128 C CA  . VAL A 141 ? 0.5503 0.5232 0.3911 0.0540  -0.0289 -0.0279 141 VAL A CA  
1129 C C   . VAL A 141 ? 0.5671 0.5567 0.4408 0.0509  -0.0390 -0.0275 141 VAL A C   
1130 O O   . VAL A 141 ? 0.5499 0.5391 0.4345 0.0487  -0.0536 -0.0321 141 VAL A O   
1131 C CB  . VAL A 141 ? 0.5505 0.4974 0.3523 0.0554  -0.0399 -0.0306 141 VAL A CB  
1132 C CG1 . VAL A 141 ? 0.5652 0.5052 0.3558 0.0566  -0.0498 -0.0233 141 VAL A CG1 
1133 C CG2 . VAL A 141 ? 0.5204 0.4506 0.2904 0.0569  -0.0235 -0.0346 141 VAL A CG2 
1134 N N   . ILE A 142 ? 0.5114 0.5157 0.4036 0.0499  -0.0300 -0.0235 142 ILE A N   
1135 C CA  . ILE A 142 ? 0.4416 0.4631 0.3689 0.0462  -0.0328 -0.0261 142 ILE A CA  
1136 C C   . ILE A 142 ? 0.5131 0.5310 0.4465 0.0515  -0.0427 -0.0239 142 ILE A C   
1137 O O   . ILE A 142 ? 0.4623 0.4783 0.3900 0.0535  -0.0348 -0.0190 142 ILE A O   
1138 C CB  . ILE A 142 ? 0.4651 0.5018 0.4068 0.0397  -0.0164 -0.0252 142 ILE A CB  
1139 C CG1 . ILE A 142 ? 0.4599 0.4946 0.3916 0.0355  -0.0106 -0.0236 142 ILE A CG1 
1140 C CG2 . ILE A 142 ? 0.4472 0.5000 0.4226 0.0332  -0.0141 -0.0316 142 ILE A CG2 
1141 C CD1 . ILE A 142 ? 0.4248 0.4689 0.3611 0.0282  0.0008  -0.0200 142 ILE A CD1 
1142 N N   . PRO A 143 ? 0.4470 0.4624 0.3944 0.0537  -0.0620 -0.0268 143 PRO A N   
1143 C CA  . PRO A 143 ? 0.4976 0.5110 0.4628 0.0594  -0.0747 -0.0243 143 PRO A CA  
1144 C C   . PRO A 143 ? 0.5132 0.5512 0.5317 0.0572  -0.0664 -0.0320 143 PRO A C   
1145 O O   . PRO A 143 ? 0.5149 0.5684 0.5658 0.0526  -0.0680 -0.0405 143 PRO A O   
1146 C CB  . PRO A 143 ? 0.5429 0.5422 0.5017 0.0621  -0.1030 -0.0242 143 PRO A CB  
1147 C CG  . PRO A 143 ? 0.5454 0.5455 0.4940 0.0561  -0.1019 -0.0305 143 PRO A CG  
1148 C CD  . PRO A 143 ? 0.4723 0.4869 0.4257 0.0508  -0.0756 -0.0327 143 PRO A CD  
1149 N N   . PHE A 144 ? 0.4796 0.5206 0.5081 0.0590  -0.0552 -0.0308 144 PHE A N   
1150 C CA  . PHE A 144 ? 0.4834 0.5456 0.5579 0.0552  -0.0413 -0.0412 144 PHE A CA  
1151 C C   . PHE A 144 ? 0.5003 0.5586 0.6011 0.0634  -0.0468 -0.0412 144 PHE A C   
1152 O O   . PHE A 144 ? 0.4861 0.5240 0.5596 0.0692  -0.0550 -0.0305 144 PHE A O   
1153 C CB  . PHE A 144 ? 0.4353 0.5056 0.4956 0.0449  -0.0158 -0.0434 144 PHE A CB  
1154 C CG  . PHE A 144 ? 0.4918 0.5506 0.5225 0.0463  -0.0081 -0.0355 144 PHE A CG  
1155 C CD1 . PHE A 144 ? 0.5423 0.5881 0.5328 0.0476  -0.0098 -0.0259 144 PHE A CD1 
1156 C CD2 . PHE A 144 ? 0.4987 0.5600 0.5452 0.0455  0.0029  -0.0395 144 PHE A CD2 
1157 C CE1 . PHE A 144 ? 0.4983 0.5365 0.4684 0.0474  -0.0012 -0.0196 144 PHE A CE1 
1158 C CE2 . PHE A 144 ? 0.5176 0.5686 0.5397 0.0450  0.0095  -0.0326 144 PHE A CE2 
1159 C CZ  . PHE A 144 ? 0.4546 0.4954 0.4401 0.0457  0.0074  -0.0222 144 PHE A CZ  
1160 N N   . SER A 145 ? 0.4471 0.5240 0.6030 0.0631  -0.0409 -0.0540 145 SER A N   
1161 C CA  . SER A 145 ? 0.5070 0.5824 0.7016 0.0716  -0.0444 -0.0576 145 SER A CA  
1162 C C   . SER A 145 ? 0.4731 0.5608 0.6840 0.0637  -0.0134 -0.0703 145 SER A C   
1163 O O   . SER A 145 ? 0.4266 0.5327 0.6510 0.0523  0.0063  -0.0823 145 SER A O   
1164 C CB  . SER A 145 ? 0.4847 0.5718 0.7414 0.0793  -0.0643 -0.0649 145 SER A CB  
1165 O OG  . SER A 145 ? 0.5222 0.6082 0.8256 0.0888  -0.0670 -0.0699 145 SER A OG  
1166 N N   . MET A 146 ? 0.5333 0.6075 0.7378 0.0676  -0.0090 -0.0675 146 MET A N   
1167 C CA  . MET A 146 ? 0.4808 0.5624 0.7026 0.0605  0.0180  -0.0818 146 MET A CA  
1168 C C   . MET A 146 ? 0.4670 0.5553 0.7577 0.0700  0.0162  -0.0955 146 MET A C   
1169 O O   . MET A 146 ? 0.5183 0.5899 0.8240 0.0834  -0.0040 -0.0877 146 MET A O   
1170 C CB  . MET A 146 ? 0.5045 0.5676 0.6845 0.0580  0.0246  -0.0731 146 MET A CB  
1171 C CG  . MET A 146 ? 0.5153 0.5744 0.6382 0.0497  0.0269  -0.0611 146 MET A CG  
1172 S SD  . MET A 146 ? 0.5042 0.5823 0.6156 0.0327  0.0464  -0.0703 146 MET A SD  
1173 C CE  . MET A 146 ? 0.5209 0.5999 0.6357 0.0202  0.0727  -0.0852 146 MET A CE  
1174 N N   . GLY A 147 ? 0.5250 0.6362 0.8589 0.0627  0.0373  -0.1157 147 GLY A N   
1175 C CA  . GLY A 147 ? 0.4701 0.5936 0.8827 0.0721  0.0376  -0.1321 147 GLY A CA  
1176 C C   . GLY A 147 ? 0.6069 0.7467 1.0637 0.0786  0.0156  -0.1319 147 GLY A C   
1177 O O   . GLY A 147 ? 0.5557 0.6893 0.9760 0.0790  -0.0068 -0.1158 147 GLY A O   
1178 N N   . PRO A 148 ? 0.6882 0.8493 1.2276 0.0831  0.0220  -0.1513 148 PRO A N   
1179 C CA  . PRO A 148 ? 0.7217 0.9019 1.3133 0.0881  -0.0002 -0.1528 148 PRO A CA  
1180 C C   . PRO A 148 ? 0.7887 0.9478 1.3661 0.1036  -0.0491 -0.1298 148 PRO A C   
1181 O O   . PRO A 148 ? 0.8397 0.9744 1.4086 0.1159  -0.0670 -0.1187 148 PRO A O   
1182 C CB  . PRO A 148 ? 0.6545 0.8587 1.3478 0.0939  0.0148  -0.1783 148 PRO A CB  
1183 C CG  . PRO A 148 ? 0.6295 0.8320 1.3080 0.0828  0.0590  -0.1953 148 PRO A CG  
1184 C CD  . PRO A 148 ? 0.6298 0.7997 1.2225 0.0829  0.0517  -0.1752 148 PRO A CD  
1185 N N   . LEU A 149 ? 0.6796 0.8448 1.2496 0.1010  -0.0708 -0.1226 149 LEU A N   
1186 C CA  . LEU A 149 ? 0.6746 0.8176 1.2258 0.1126  -0.1183 -0.1024 149 LEU A CA  
1187 C C   . LEU A 149 ? 0.8335 0.9733 1.4576 0.1306  -0.1465 -0.1032 149 LEU A C   
1188 O O   . LEU A 149 ? 0.8123 0.9804 1.5279 0.1347  -0.1372 -0.1232 149 LEU A O   
1189 C CB  . LEU A 149 ? 0.7103 0.8644 1.2601 0.1060  -0.1364 -0.1009 149 LEU A CB  
1190 C CG  . LEU A 149 ? 0.7091 0.8555 1.1781 0.0915  -0.1222 -0.0938 149 LEU A CG  
1191 C CD1 . LEU A 149 ? 0.5670 0.7218 1.0438 0.0861  -0.1435 -0.0940 149 LEU A CD1 
1192 C CD2 . LEU A 149 ? 0.7047 0.8150 1.0875 0.0946  -0.1314 -0.0736 149 LEU A CD2 
1193 N N   . GLY A 150 ? 0.8695 0.9733 1.4536 0.1409  -0.1806 -0.0815 150 GLY A N   
1194 C CA  . GLY A 150 ? 0.8095 0.9015 1.4538 0.1586  -0.2133 -0.0774 150 GLY A CA  
1195 C C   . GLY A 150 ? 0.8645 0.9573 1.5544 0.1658  -0.1885 -0.0899 150 GLY A C   
1196 O O   . GLY A 150 ? 0.9045 0.9812 1.6308 0.1750  -0.2101 -0.0856 150 GLY A O   
1197 N N   . SER A 151 ? 0.8762 0.9800 1.5433 0.1541  -0.1402 -0.1038 151 SER A N   
1198 C CA  . SER A 151 ? 0.8637 0.9643 1.5660 0.1589  -0.1149 -0.1175 151 SER A CA  
1199 C C   . SER A 151 ? 0.9930 1.0491 1.6447 0.1668  -0.1356 -0.0951 151 SER A C   
1200 O O   . SER A 151 ? 0.9944 1.0267 1.5568 0.1595  -0.1437 -0.0741 151 SER A O   
1201 C CB  . SER A 151 ? 0.8405 0.9577 1.5144 0.1410  -0.0615 -0.1358 151 SER A CB  
1202 O OG  . SER A 151 ? 0.8293 0.9390 1.5282 0.1438  -0.0368 -0.1502 151 SER A OG  
1203 N N   . PRO A 152 ? 0.9035 0.9463 1.6114 0.1806  -0.1427 -0.0996 152 PRO A N   
1204 C CA  . PRO A 152 ? 0.9461 0.9425 1.6062 0.1867  -0.1631 -0.0768 152 PRO A CA  
1205 C C   . PRO A 152 ? 0.8784 0.8607 1.4541 0.1714  -0.1305 -0.0729 152 PRO A C   
1206 O O   . PRO A 152 ? 1.0227 0.9690 1.5300 0.1696  -0.1466 -0.0488 152 PRO A O   
1207 C CB  . PRO A 152 ? 0.9121 0.9030 1.6396 0.1940  -0.1630 -0.0876 152 PRO A CB  
1208 C CG  . PRO A 152 ? 0.8660 0.8998 1.6563 0.1860  -0.1240 -0.1206 152 PRO A CG  
1209 C CD  . PRO A 152 ? 0.8463 0.9102 1.6331 0.1790  -0.1253 -0.1230 152 PRO A CD  
1210 N N   . LEU A 153 ? 0.7725 0.7812 1.3509 0.1590  -0.0856 -0.0958 153 LEU A N   
1211 C CA  . LEU A 153 ? 0.7538 0.7531 1.2582 0.1434  -0.0567 -0.0936 153 LEU A CA  
1212 C C   . LEU A 153 ? 0.7050 0.7181 1.1440 0.1288  -0.0486 -0.0862 153 LEU A C   
1213 O O   . LEU A 153 ? 0.6875 0.6995 1.0733 0.1150  -0.0240 -0.0866 153 LEU A O   
1214 C CB  . LEU A 153 ? 0.7229 0.7362 1.2601 0.1364  -0.0149 -0.1222 153 LEU A CB  
1215 C CG  . LEU A 153 ? 0.7139 0.7043 1.2954 0.1474  -0.0146 -0.1297 153 LEU A CG  
1216 C CD1 . LEU A 153 ? 0.5612 0.5701 1.1857 0.1401  0.0287  -0.1645 153 LEU A CD1 
1217 C CD2 . LEU A 153 ? 0.5580 0.5104 1.0714 0.1433  -0.0221 -0.1083 153 LEU A CD2 
1218 N N   . ALA A 154 ? 0.6378 0.6629 1.0827 0.1315  -0.0702 -0.0800 154 ALA A N   
1219 C CA  . ALA A 154 ? 0.7493 0.7851 1.1371 0.1190  -0.0641 -0.0738 154 ALA A CA  
1220 C C   . ALA A 154 ? 0.6538 0.6588 0.9642 0.1179  -0.0836 -0.0479 154 ALA A C   
1221 O O   . ALA A 154 ? 0.7580 0.7356 1.0626 0.1277  -0.1146 -0.0317 154 ALA A O   
1222 C CB  . ALA A 154 ? 0.6835 0.7438 1.1112 0.1207  -0.0777 -0.0801 154 ALA A CB  
1223 N N   . LYS A 155 ? 0.6087 0.6166 0.8598 0.1051  -0.0649 -0.0443 155 LYS A N   
1224 C CA  . LYS A 155 ? 0.5685 0.5517 0.7484 0.1020  -0.0756 -0.0236 155 LYS A CA  
1225 C C   . LYS A 155 ? 0.6293 0.6266 0.7739 0.0933  -0.0696 -0.0234 155 LYS A C   
1226 O O   . LYS A 155 ? 0.5503 0.5724 0.7070 0.0852  -0.0477 -0.0366 155 LYS A O   
1227 C CB  . LYS A 155 ? 0.5927 0.5600 0.7386 0.0959  -0.0573 -0.0185 155 LYS A CB  
1228 C CG  . LYS A 155 ? 0.6603 0.6003 0.8239 0.1044  -0.0703 -0.0117 155 LYS A CG  
1229 C CD  . LYS A 155 ? 0.7236 0.6460 0.8513 0.0963  -0.0532 -0.0055 155 LYS A CD  
1230 C CE  . LYS A 155 ? 0.8632 0.7482 0.9920 0.1036  -0.0722 0.0084  155 LYS A CE  
1231 N NZ  . LYS A 155 ? 0.7022 0.5882 0.9023 0.1169  -0.0840 -0.0025 155 LYS A NZ  
1232 N N   . ILE A 156 ? 0.5631 0.5406 0.6610 0.0941  -0.0889 -0.0083 156 ILE A N   
1233 C CA  . ILE A 156 ? 0.5917 0.5775 0.6598 0.0882  -0.0884 -0.0085 156 ILE A CA  
1234 C C   . ILE A 156 ? 0.5847 0.5597 0.5938 0.0805  -0.0716 -0.0005 156 ILE A C   
1235 O O   . ILE A 156 ? 0.5530 0.5039 0.5292 0.0805  -0.0729 0.0113  156 ILE A O   
1236 C CB  . ILE A 156 ? 0.5129 0.4834 0.5717 0.0934  -0.1221 -0.0007 156 ILE A CB  
1237 C CG1 . ILE A 156 ? 0.4822 0.4711 0.6126 0.1007  -0.1391 -0.0109 156 ILE A CG1 
1238 C CG2 . ILE A 156 ? 0.5419 0.5125 0.5577 0.0865  -0.1202 -0.0003 156 ILE A CG2 
1239 C CD1 . ILE A 156 ? 0.6002 0.5725 0.7278 0.1060  -0.1792 -0.0025 156 ILE A CD1 
1240 N N   . GLY A 157 ? 0.5200 0.5126 0.5191 0.0735  -0.0559 -0.0068 157 GLY A N   
1241 C CA  . GLY A 157 ? 0.5174 0.5039 0.4720 0.0675  -0.0412 -0.0011 157 GLY A CA  
1242 C C   . GLY A 157 ? 0.5447 0.5333 0.4779 0.0653  -0.0442 -0.0026 157 GLY A C   
1243 O O   . GLY A 157 ? 0.4650 0.4639 0.4197 0.0660  -0.0542 -0.0093 157 GLY A O   
1244 N N   . ILE A 158 ? 0.5713 0.5493 0.4649 0.0624  -0.0343 0.0025  158 ILE A N   
1245 C CA  . ILE A 158 ? 0.5056 0.4837 0.3789 0.0604  -0.0324 -0.0005 158 ILE A CA  
1246 C C   . ILE A 158 ? 0.5527 0.5426 0.4241 0.0561  -0.0108 -0.0015 158 ILE A C   
1247 O O   . ILE A 158 ? 0.5420 0.5248 0.3970 0.0546  0.0006  0.0037  158 ILE A O   
1248 C CB  . ILE A 158 ? 0.5242 0.4737 0.3505 0.0614  -0.0424 0.0048  158 ILE A CB  
1249 C CG1 . ILE A 158 ? 0.6137 0.5479 0.4401 0.0652  -0.0704 0.0084  158 ILE A CG1 
1250 C CG2 . ILE A 158 ? 0.5355 0.4839 0.3439 0.0596  -0.0380 -0.0017 158 ILE A CG2 
1251 C CD1 . ILE A 158 ? 0.6440 0.5888 0.4935 0.0661  -0.0867 0.0002  158 ILE A CD1 
1252 N N   . GLU A 159 ? 0.4843 0.4912 0.3740 0.0530  -0.0063 -0.0075 159 GLU A N   
1253 C CA  . GLU A 159 ? 0.4895 0.5057 0.3795 0.0494  0.0079  -0.0071 159 GLU A CA  
1254 C C   . GLU A 159 ? 0.5085 0.5180 0.3838 0.0513  0.0079  -0.0095 159 GLU A C   
1255 O O   . GLU A 159 ? 0.5159 0.5241 0.3942 0.0513  -0.0017 -0.0139 159 GLU A O   
1256 C CB  . GLU A 159 ? 0.4356 0.4697 0.3505 0.0426  0.0122  -0.0102 159 GLU A CB  
1257 C CG  . GLU A 159 ? 0.4747 0.5152 0.3892 0.0388  0.0195  -0.0079 159 GLU A CG  
1258 C CD  . GLU A 159 ? 0.4974 0.5496 0.4243 0.0293  0.0238  -0.0081 159 GLU A CD  
1259 O OE1 . GLU A 159 ? 0.5226 0.5785 0.4586 0.0255  0.0258  -0.0123 159 GLU A OE1 
1260 O OE2 . GLU A 159 ? 0.4898 0.5457 0.4172 0.0252  0.0245  -0.0046 159 GLU A OE2 
1261 N N   . LEU A 160 ? 0.5171 0.5225 0.3806 0.0525  0.0196  -0.0080 160 LEU A N   
1262 C CA  . LEU A 160 ? 0.5513 0.5523 0.4097 0.0550  0.0238  -0.0125 160 LEU A CA  
1263 C C   . LEU A 160 ? 0.5600 0.5774 0.4453 0.0530  0.0286  -0.0109 160 LEU A C   
1264 O O   . LEU A 160 ? 0.5492 0.5770 0.4463 0.0505  0.0356  -0.0068 160 LEU A O   
1265 C CB  . LEU A 160 ? 0.5235 0.5090 0.3554 0.0573  0.0363  -0.0141 160 LEU A CB  
1266 C CG  . LEU A 160 ? 0.5677 0.5307 0.3624 0.0565  0.0300  -0.0122 160 LEU A CG  
1267 C CD1 . LEU A 160 ? 0.5765 0.5213 0.3381 0.0550  0.0473  -0.0144 160 LEU A CD1 
1268 C CD2 . LEU A 160 ? 0.5730 0.5254 0.3569 0.0575  0.0105  -0.0163 160 LEU A CD2 
1269 N N   . THR A 161 ? 0.4851 0.5026 0.3795 0.0530  0.0223  -0.0133 161 THR A N   
1270 C CA  . THR A 161 ? 0.4778 0.5057 0.3943 0.0501  0.0210  -0.0093 161 THR A CA  
1271 C C   . THR A 161 ? 0.4780 0.4967 0.3998 0.0539  0.0167  -0.0124 161 THR A C   
1272 O O   . THR A 161 ? 0.4883 0.4946 0.3971 0.0553  0.0123  -0.0182 161 THR A O   
1273 C CB  . THR A 161 ? 0.4795 0.5161 0.4020 0.0405  0.0142  -0.0053 161 THR A CB  
1274 O OG1 . THR A 161 ? 0.4101 0.4514 0.3449 0.0355  0.0100  0.0007  161 THR A OG1 
1275 C CG2 . THR A 161 ? 0.4675 0.4985 0.3856 0.0373  0.0067  -0.0091 161 THR A CG2 
1276 N N   . ASP A 162 ? 0.4204 0.4439 0.3638 0.0553  0.0158  -0.0087 162 ASP A N   
1277 C CA  . ASP A 162 ? 0.4590 0.4721 0.4144 0.0594  0.0096  -0.0102 162 ASP A CA  
1278 C C   . ASP A 162 ? 0.4705 0.4822 0.4319 0.0505  -0.0054 -0.0006 162 ASP A C   
1279 O O   . ASP A 162 ? 0.4874 0.4896 0.4633 0.0530  -0.0140 0.0023  162 ASP A O   
1280 C CB  . ASP A 162 ? 0.4912 0.5077 0.4727 0.0689  0.0178  -0.0133 162 ASP A CB  
1281 C CG  . ASP A 162 ? 0.5150 0.5497 0.5195 0.0663  0.0169  -0.0052 162 ASP A CG  
1282 O OD1 . ASP A 162 ? 0.4587 0.5004 0.4530 0.0565  0.0101  0.0023  162 ASP A OD1 
1283 O OD2 . ASP A 162 ? 0.4926 0.5349 0.5281 0.0734  0.0234  -0.0079 162 ASP A OD2 
1284 N N   . SER A 163 ? 0.4657 0.4838 0.4148 0.0394  -0.0079 0.0039  163 SER A N   
1285 C CA  . SER A 163 ? 0.4675 0.4815 0.4126 0.0266  -0.0185 0.0127  163 SER A CA  
1286 C C   . SER A 163 ? 0.5153 0.5245 0.4464 0.0176  -0.0178 0.0090  163 SER A C   
1287 O O   . SER A 163 ? 0.4986 0.5176 0.4245 0.0146  -0.0105 0.0039  163 SER A O   
1288 C CB  . SER A 163 ? 0.5120 0.5371 0.4548 0.0179  -0.0189 0.0191  163 SER A CB  
1289 O OG  . SER A 163 ? 0.5268 0.5448 0.4533 0.0015  -0.0255 0.0257  163 SER A OG  
1290 N N   . PRO A 164 ? 0.5122 0.5066 0.4415 0.0131  -0.0253 0.0110  164 PRO A N   
1291 C CA  . PRO A 164 ? 0.5016 0.4939 0.4232 0.0014  -0.0235 0.0074  164 PRO A CA  
1292 C C   . PRO A 164 ? 0.5145 0.5131 0.4256 -0.0157 -0.0184 0.0115  164 PRO A C   
1293 O O   . PRO A 164 ? 0.4834 0.4887 0.3958 -0.0242 -0.0105 0.0047  164 PRO A O   
1294 C CB  . PRO A 164 ? 0.6100 0.5816 0.5322 -0.0012 -0.0330 0.0106  164 PRO A CB  
1295 C CG  . PRO A 164 ? 0.5999 0.5622 0.5283 0.0048  -0.0423 0.0204  164 PRO A CG  
1296 C CD  . PRO A 164 ? 0.5360 0.5142 0.4750 0.0184  -0.0357 0.0161  164 PRO A CD  
1297 N N   . TYR A 165 ? 0.4942 0.4903 0.3962 -0.0216 -0.0226 0.0214  165 TYR A N   
1298 C CA  . TYR A 165 ? 0.5324 0.5317 0.4169 -0.0392 -0.0157 0.0229  165 TYR A CA  
1299 C C   . TYR A 165 ? 0.5383 0.5569 0.4310 -0.0352 -0.0021 0.0119  165 TYR A C   
1300 O O   . TYR A 165 ? 0.5022 0.5261 0.3905 -0.0475 0.0100  0.0052  165 TYR A O   
1301 C CB  . TYR A 165 ? 0.5393 0.5296 0.4097 -0.0459 -0.0276 0.0359  165 TYR A CB  
1302 C CG  . TYR A 165 ? 0.5894 0.5806 0.4349 -0.0645 -0.0205 0.0360  165 TYR A CG  
1303 C CD1 . TYR A 165 ? 0.5338 0.5402 0.3843 -0.0606 -0.0138 0.0300  165 TYR A CD1 
1304 C CD2 . TYR A 165 ? 0.5676 0.5410 0.3810 -0.0877 -0.0195 0.0415  165 TYR A CD2 
1305 C CE1 . TYR A 165 ? 0.6222 0.6265 0.4481 -0.0782 -0.0064 0.0277  165 TYR A CE1 
1306 C CE2 . TYR A 165 ? 0.5696 0.5403 0.3539 -0.1067 -0.0104 0.0392  165 TYR A CE2 
1307 C CZ  . TYR A 165 ? 0.6075 0.5938 0.3990 -0.1014 -0.0041 0.0314  165 TYR A CZ  
1308 O OH  . TYR A 165 ? 0.5955 0.5765 0.3566 -0.1210 0.0058  0.0268  165 TYR A OH  
1309 N N   . VAL A 166 ? 0.5336 0.5612 0.4394 -0.0188 -0.0026 0.0094  166 VAL A N   
1310 C CA  . VAL A 166 ? 0.4743 0.5154 0.3874 -0.0141 0.0076  0.0009  166 VAL A CA  
1311 C C   . VAL A 166 ? 0.4728 0.5182 0.3978 -0.0115 0.0116  -0.0087 166 VAL A C   
1312 O O   . VAL A 166 ? 0.4243 0.4790 0.3583 -0.0155 0.0205  -0.0163 166 VAL A O   
1313 C CB  . VAL A 166 ? 0.4850 0.5304 0.4052 0.0006  0.0064  0.0022  166 VAL A CB  
1314 C CG1 . VAL A 166 ? 0.4748 0.5279 0.4005 0.0062  0.0142  -0.0048 166 VAL A CG1 
1315 C CG2 . VAL A 166 ? 0.4576 0.5041 0.3755 -0.0036 0.0022  0.0100  166 VAL A CG2 
1316 N N   . VAL A 167 ? 0.4677 0.5062 0.3965 -0.0047 0.0041  -0.0094 167 VAL A N   
1317 C CA  . VAL A 167 ? 0.4596 0.5019 0.4020 -0.0030 0.0031  -0.0181 167 VAL A CA  
1318 C C   . VAL A 167 ? 0.4647 0.5133 0.4166 -0.0191 0.0115  -0.0228 167 VAL A C   
1319 O O   . VAL A 167 ? 0.4556 0.5169 0.4281 -0.0199 0.0175  -0.0318 167 VAL A O   
1320 C CB  . VAL A 167 ? 0.4859 0.5155 0.4256 0.0038  -0.0073 -0.0186 167 VAL A CB  
1321 C CG1 . VAL A 167 ? 0.4880 0.5213 0.4431 0.0027  -0.0123 -0.0274 167 VAL A CG1 
1322 C CG2 . VAL A 167 ? 0.4570 0.4801 0.3865 0.0184  -0.0100 -0.0175 167 VAL A CG2 
1323 N N   . ALA A 168 ? 0.4855 0.5241 0.4240 -0.0329 0.0127  -0.0169 168 ALA A N   
1324 C CA  . ALA A 168 ? 0.5065 0.5482 0.4487 -0.0520 0.0250  -0.0216 168 ALA A CA  
1325 C C   . ALA A 168 ? 0.4729 0.5261 0.4163 -0.0593 0.0409  -0.0283 168 ALA A C   
1326 O O   . ALA A 168 ? 0.4566 0.5225 0.4228 -0.0663 0.0544  -0.0403 168 ALA A O   
1327 C CB  . ALA A 168 ? 0.5019 0.5238 0.4186 -0.0676 0.0223  -0.0107 168 ALA A CB  
1328 N N   . SER A 169 ? 0.4840 0.5333 0.4073 -0.0579 0.0399  -0.0222 169 SER A N   
1329 C CA  . SER A 169 ? 0.4993 0.5558 0.4204 -0.0657 0.0549  -0.0299 169 SER A CA  
1330 C C   . SER A 169 ? 0.4820 0.5545 0.4366 -0.0514 0.0590  -0.0412 169 SER A C   
1331 O O   . SER A 169 ? 0.5027 0.5845 0.4742 -0.0580 0.0750  -0.0539 169 SER A O   
1332 C CB  . SER A 169 ? 0.5350 0.5827 0.4284 -0.0677 0.0490  -0.0205 169 SER A CB  
1333 O OG  . SER A 169 ? 0.5309 0.5611 0.3953 -0.0799 0.0397  -0.0079 169 SER A OG  
1334 N N   . MET A 170 ? 0.4043 0.4778 0.3684 -0.0324 0.0448  -0.0371 170 MET A N   
1335 C CA  . MET A 170 ? 0.3929 0.4758 0.3839 -0.0192 0.0437  -0.0445 170 MET A CA  
1336 C C   . MET A 170 ? 0.3961 0.4900 0.4225 -0.0201 0.0451  -0.0552 170 MET A C   
1337 O O   . MET A 170 ? 0.4062 0.5103 0.4638 -0.0149 0.0489  -0.0646 170 MET A O   
1338 C CB  . MET A 170 ? 0.4001 0.4761 0.3829 -0.0023 0.0286  -0.0365 170 MET A CB  
1339 C CG  . MET A 170 ? 0.4464 0.5170 0.4087 0.0002  0.0298  -0.0289 170 MET A CG  
1340 S SD  . MET A 170 ? 0.4992 0.5739 0.4722 0.0020  0.0387  -0.0344 170 MET A SD  
1341 C CE  . MET A 170 ? 0.3977 0.4682 0.3839 0.0193  0.0262  -0.0334 170 MET A CE  
1342 N N   . ARG A 171 ? 0.4111 0.5030 0.4380 -0.0267 0.0413  -0.0542 171 ARG A N   
1343 C CA  . ARG A 171 ? 0.4064 0.5114 0.4728 -0.0302 0.0431  -0.0652 171 ARG A CA  
1344 C C   . ARG A 171 ? 0.4053 0.5232 0.4938 -0.0446 0.0676  -0.0783 171 ARG A C   
1345 O O   . ARG A 171 ? 0.3951 0.5300 0.5319 -0.0430 0.0720  -0.0912 171 ARG A O   
1346 C CB  . ARG A 171 ? 0.4175 0.5155 0.4778 -0.0378 0.0361  -0.0616 171 ARG A CB  
1347 C CG  . ARG A 171 ? 0.4462 0.5593 0.5522 -0.0426 0.0362  -0.0732 171 ARG A CG  
1348 C CD  . ARG A 171 ? 0.4931 0.5966 0.5916 -0.0523 0.0298  -0.0697 171 ARG A CD  
1349 N NE  . ARG A 171 ? 0.4768 0.5947 0.6224 -0.0530 0.0219  -0.0800 171 ARG A NE  
1350 C CZ  . ARG A 171 ? 0.5322 0.6687 0.7196 -0.0672 0.0386  -0.0921 171 ARG A CZ  
1351 N NH1 . ARG A 171 ? 0.5043 0.6447 0.6859 -0.0834 0.0669  -0.0963 171 ARG A NH1 
1352 N NH2 . ARG A 171 ? 0.4997 0.6510 0.7362 -0.0665 0.0271  -0.1011 171 ARG A NH2 
1353 N N   . ILE A 172 ? 0.3761 0.4854 0.4307 -0.0595 0.0835  -0.0761 172 ILE A N   
1354 C CA  . ILE A 172 ? 0.4564 0.5733 0.5214 -0.0761 0.1109  -0.0905 172 ILE A CA  
1355 C C   . ILE A 172 ? 0.4237 0.5460 0.5028 -0.0665 0.1173  -0.0988 172 ILE A C   
1356 O O   . ILE A 172 ? 0.4411 0.5776 0.5618 -0.0677 0.1341  -0.1161 172 ILE A O   
1357 C CB  . ILE A 172 ? 0.4558 0.5549 0.4686 -0.0997 0.1233  -0.0841 172 ILE A CB  
1358 C CG1 . ILE A 172 ? 0.4551 0.5467 0.4593 -0.1119 0.1198  -0.0772 172 ILE A CG1 
1359 C CG2 . ILE A 172 ? 0.4742 0.5758 0.4843 -0.1186 0.1542  -0.1001 172 ILE A CG2 
1360 C CD1 . ILE A 172 ? 0.4603 0.5271 0.4065 -0.1341 0.1242  -0.0653 172 ILE A CD1 
1361 N N   . MET A 173 ? 0.4208 0.5317 0.4702 -0.0567 0.1047  -0.0875 173 MET A N   
1362 C CA  . MET A 173 ? 0.5075 0.6184 0.5619 -0.0516 0.1121  -0.0942 173 MET A CA  
1363 C C   . MET A 173 ? 0.4864 0.6052 0.5836 -0.0300 0.0998  -0.0973 173 MET A C   
1364 O O   . MET A 173 ? 0.4670 0.5860 0.5804 -0.0257 0.1077  -0.1058 173 MET A O   
1365 C CB  . MET A 173 ? 0.5100 0.6057 0.5179 -0.0526 0.1039  -0.0809 173 MET A CB  
1366 C CG  . MET A 173 ? 0.4765 0.5602 0.4398 -0.0752 0.1131  -0.0776 173 MET A CG  
1367 S SD  . MET A 173 ? 0.5224 0.6064 0.4848 -0.0977 0.1466  -0.0995 173 MET A SD  
1368 C CE  . MET A 173 ? 0.5260 0.6102 0.5027 -0.0864 0.1499  -0.1085 173 MET A CE  
1369 N N   . THR A 174 ? 0.4277 0.5493 0.5406 -0.0174 0.0793  -0.0903 174 THR A N   
1370 C CA  . THR A 174 ? 0.3774 0.5013 0.5239 0.0015  0.0622  -0.0903 174 THR A CA  
1371 C C   . THR A 174 ? 0.3941 0.5305 0.5817 0.0050  0.0511  -0.0954 174 THR A C   
1372 O O   . THR A 174 ? 0.4062 0.5490 0.5944 -0.0073 0.0578  -0.0984 174 THR A O   
1373 C CB  . THR A 174 ? 0.4394 0.5468 0.5508 0.0139  0.0422  -0.0735 174 THR A CB  
1374 O OG1 . THR A 174 ? 0.4449 0.5473 0.5320 0.0133  0.0303  -0.0643 174 THR A OG1 
1375 C CG2 . THR A 174 ? 0.3870 0.4848 0.4638 0.0093  0.0522  -0.0686 174 THR A CG2 
1376 N N   . ARG A 175 ? 0.3577 0.4957 0.5805 0.0207  0.0320  -0.0957 175 ARG A N   
1377 C CA  . ARG A 175 ? 0.4391 0.5844 0.6941 0.0266  0.0103  -0.0962 175 ARG A CA  
1378 C C   . ARG A 175 ? 0.4253 0.5505 0.6309 0.0332  -0.0135 -0.0796 175 ARG A C   
1379 O O   . ARG A 175 ? 0.4676 0.5759 0.6489 0.0441  -0.0269 -0.0694 175 ARG A O   
1380 C CB  . ARG A 175 ? 0.4022 0.5559 0.7189 0.0400  -0.0036 -0.1034 175 ARG A CB  
1381 C CG  . ARG A 175 ? 0.4127 0.5917 0.7969 0.0338  0.0197  -0.1248 175 ARG A CG  
1382 C CD  . ARG A 175 ? 0.4017 0.5780 0.7845 0.0316  0.0459  -0.1335 175 ARG A CD  
1383 N NE  . ARG A 175 ? 0.4403 0.6388 0.8959 0.0291  0.0674  -0.1566 175 ARG A NE  
1384 C CZ  . ARG A 175 ? 0.4279 0.6258 0.8981 0.0278  0.0918  -0.1703 175 ARG A CZ  
1385 N NH1 . ARG A 175 ? 0.4140 0.5907 0.8310 0.0277  0.0959  -0.1622 175 ARG A NH1 
1386 N NH2 . ARG A 175 ? 0.4211 0.6404 0.9641 0.0258  0.1134  -0.1942 175 ARG A NH2 
1387 N N   A MET A 176 ? 0.4411 0.5660 0.6314 0.0256  -0.0171 -0.0778 176 MET A N   
1388 N N   B MET A 176 ? 0.4433 0.5681 0.6327 0.0254  -0.0165 -0.0778 176 MET A N   
1389 C CA  A MET A 176 ? 0.4884 0.5931 0.6293 0.0297  -0.0333 -0.0656 176 MET A CA  
1390 C CA  B MET A 176 ? 0.4588 0.5637 0.6005 0.0296  -0.0335 -0.0658 176 MET A CA  
1391 C C   A MET A 176 ? 0.4738 0.5790 0.6287 0.0288  -0.0533 -0.0680 176 MET A C   
1392 C C   B MET A 176 ? 0.4755 0.5816 0.6345 0.0296  -0.0546 -0.0685 176 MET A C   
1393 O O   A MET A 176 ? 0.4452 0.5670 0.6362 0.0189  -0.0466 -0.0775 176 MET A O   
1394 O O   B MET A 176 ? 0.4413 0.5655 0.6433 0.0213  -0.0500 -0.0787 176 MET A O   
1395 C CB  A MET A 176 ? 0.4522 0.5496 0.5501 0.0205  -0.0164 -0.0601 176 MET A CB  
1396 C CB  B MET A 176 ? 0.4533 0.5508 0.5523 0.0201  -0.0177 -0.0604 176 MET A CB  
1397 C CG  A MET A 176 ? 0.5243 0.6015 0.5764 0.0258  -0.0279 -0.0499 176 MET A CG  
1398 C CG  B MET A 176 ? 0.5124 0.5907 0.5703 0.0244  -0.0312 -0.0517 176 MET A CG  
1399 S SD  A MET A 176 ? 0.4914 0.5627 0.5400 0.0205  -0.0399 -0.0521 176 MET A SD  
1400 S SD  B MET A 176 ? 0.5060 0.5778 0.5336 0.0133  -0.0176 -0.0471 176 MET A SD  
1401 C CE  A MET A 176 ? 0.4803 0.5574 0.5266 0.0038  -0.0183 -0.0526 176 MET A CE  
1402 C CE  B MET A 176 ? 0.4845 0.5683 0.5447 -0.0015 -0.0136 -0.0560 176 MET A CE  
1403 N N   . GLY A 177 ? 0.5099 0.5954 0.6342 0.0373  -0.0767 -0.0603 177 GLY A N   
1404 C CA  . GLY A 177 ? 0.5340 0.6145 0.6613 0.0354  -0.0981 -0.0627 177 GLY A CA  
1405 C C   . GLY A 177 ? 0.5668 0.6292 0.6807 0.0457  -0.1297 -0.0572 177 GLY A C   
1406 O O   . GLY A 177 ? 0.5406 0.5902 0.6346 0.0542  -0.1341 -0.0492 177 GLY A O   
1407 N N   . THR A 178 ? 0.5905 0.6493 0.7131 0.0429  -0.1532 -0.0610 178 THR A N   
1408 C CA  . THR A 178 ? 0.6321 0.6679 0.7315 0.0493  -0.1882 -0.0553 178 THR A CA  
1409 C C   . THR A 178 ? 0.6445 0.6875 0.7878 0.0586  -0.2075 -0.0526 178 THR A C   
1410 O O   . THR A 178 ? 0.6560 0.6731 0.7655 0.0656  -0.2302 -0.0420 178 THR A O   
1411 C CB  . THR A 178 ? 0.5561 0.5883 0.6609 0.0420  -0.2103 -0.0620 178 THR A CB  
1412 O OG1 . THR A 178 ? 0.5741 0.5938 0.6358 0.0348  -0.1934 -0.0642 178 THR A OG1 
1413 C CG2 . THR A 178 ? 0.6765 0.6812 0.7517 0.0462  -0.2505 -0.0562 178 THR A CG2 
1414 N N   . SER A 179 ? 0.6059 0.6816 0.8248 0.0582  -0.1983 -0.0624 179 SER A N   
1415 C CA  . SER A 179 ? 0.5563 0.6407 0.8304 0.0687  -0.2166 -0.0622 179 SER A CA  
1416 C C   . SER A 179 ? 0.5803 0.6471 0.8242 0.0779  -0.2095 -0.0516 179 SER A C   
1417 O O   . SER A 179 ? 0.5932 0.6529 0.8635 0.0883  -0.2331 -0.0463 179 SER A O   
1418 C CB  . SER A 179 ? 0.5900 0.7147 0.9532 0.0654  -0.1979 -0.0785 179 SER A CB  
1419 O OG  . SER A 179 ? 0.6260 0.7620 0.9834 0.0602  -0.1554 -0.0835 179 SER A OG  
1420 N N   . VAL A 180 ? 0.5779 0.6367 0.7705 0.0739  -0.1795 -0.0480 180 VAL A N   
1421 C CA  . VAL A 180 ? 0.6227 0.6641 0.7852 0.0805  -0.1719 -0.0380 180 VAL A CA  
1422 C C   . VAL A 180 ? 0.6626 0.6652 0.7584 0.0837  -0.1970 -0.0225 180 VAL A C   
1423 O O   . VAL A 180 ? 0.6591 0.6423 0.7473 0.0909  -0.2119 -0.0121 180 VAL A O   
1424 C CB  . VAL A 180 ? 0.5573 0.6057 0.6938 0.0738  -0.1330 -0.0401 180 VAL A CB  
1425 C CG1 . VAL A 180 ? 0.5909 0.6225 0.7004 0.0790  -0.1251 -0.0306 180 VAL A CG1 
1426 C CG2 . VAL A 180 ? 0.4846 0.5656 0.6765 0.0672  -0.1081 -0.0550 180 VAL A CG2 
1427 N N   . LEU A 181 ? 0.6939 0.6815 0.7380 0.0771  -0.2010 -0.0213 181 LEU A N   
1428 C CA  . LEU A 181 ? 0.7014 0.6492 0.6761 0.0771  -0.2227 -0.0091 181 LEU A CA  
1429 C C   . LEU A 181 ? 0.7321 0.6652 0.7246 0.0824  -0.2671 -0.0025 181 LEU A C   
1430 O O   . LEU A 181 ? 0.7661 0.6662 0.7176 0.0852  -0.2853 0.0118  181 LEU A O   
1431 C CB  . LEU A 181 ? 0.7108 0.6464 0.6359 0.0688  -0.2188 -0.0137 181 LEU A CB  
1432 C CG  . LEU A 181 ? 0.7408 0.6785 0.6326 0.0648  -0.1811 -0.0161 181 LEU A CG  
1433 C CD1 . LEU A 181 ? 0.7557 0.6851 0.6178 0.0581  -0.1790 -0.0240 181 LEU A CD1 
1434 C CD2 . LEU A 181 ? 0.8187 0.7306 0.6562 0.0660  -0.1707 -0.0050 181 LEU A CD2 
1435 N N   . GLU A 182 ? 0.7125 0.6687 0.7674 0.0830  -0.2863 -0.0120 182 GLU A N   
1436 C CA  . GLU A 182 ? 0.7302 0.6762 0.8151 0.0889  -0.3331 -0.0061 182 GLU A CA  
1437 C C   . GLU A 182 ? 0.7253 0.6721 0.8520 0.1006  -0.3386 0.0011  182 GLU A C   
1438 O O   . GLU A 182 ? 0.8076 0.7245 0.9202 0.1060  -0.3764 0.0154  182 GLU A O   
1439 C CB  . GLU A 182 ? 0.7213 0.6995 0.8805 0.0867  -0.3483 -0.0202 182 GLU A CB  
1440 C CG  . GLU A 182 ? 0.8087 0.7849 0.9319 0.0745  -0.3435 -0.0283 182 GLU A CG  
1441 C CD  . GLU A 182 ? 0.8826 0.8922 1.0836 0.0701  -0.3553 -0.0427 182 GLU A CD  
1442 O OE1 . GLU A 182 ? 0.8793 0.9204 1.1686 0.0763  -0.3579 -0.0490 182 GLU A OE1 
1443 O OE2 . GLU A 182 ? 0.9427 0.9467 1.1192 0.0598  -0.3603 -0.0489 182 GLU A OE2 
1444 N N   . ALA A 183 ? 0.7074 0.6845 0.8831 0.1037  -0.3024 -0.0085 183 ALA A N   
1445 C CA  . ALA A 183 ? 0.6511 0.6275 0.8677 0.1147  -0.3035 -0.0043 183 ALA A CA  
1446 C C   . ALA A 183 ? 0.7106 0.6477 0.8510 0.1148  -0.2991 0.0131  183 ALA A C   
1447 O O   . ALA A 183 ? 0.7374 0.6521 0.8854 0.1231  -0.3208 0.0250  183 ALA A O   
1448 C CB  . ALA A 183 ? 0.5499 0.5668 0.8333 0.1152  -0.2632 -0.0222 183 ALA A CB  
1449 N N   . LEU A 184 ? 0.7565 0.6842 0.8266 0.1053  -0.2709 0.0148  184 LEU A N   
1450 C CA  . LEU A 184 ? 0.7462 0.6392 0.7465 0.1031  -0.2621 0.0298  184 LEU A CA  
1451 C C   . LEU A 184 ? 0.7753 0.6212 0.7147 0.1015  -0.3012 0.0478  184 LEU A C   
1452 O O   . LEU A 184 ? 0.8330 0.6475 0.7474 0.1039  -0.3123 0.0634  184 LEU A O   
1453 C CB  . LEU A 184 ? 0.7212 0.6187 0.6705 0.0934  -0.2238 0.0255  184 LEU A CB  
1454 C CG  . LEU A 184 ? 0.8226 0.6869 0.6977 0.0881  -0.2104 0.0387  184 LEU A CG  
1455 C CD1 . LEU A 184 ? 0.7425 0.6073 0.6402 0.0922  -0.1957 0.0433  184 LEU A CD1 
1456 C CD2 . LEU A 184 ? 0.7025 0.5732 0.5361 0.0796  -0.1792 0.0322  184 LEU A CD2 
1457 N N   . GLY A 185 ? 0.8413 0.6779 0.7518 0.0958  -0.3231 0.0463  185 GLY A N   
1458 C CA  . GLY A 185 ? 0.8985 0.6848 0.7357 0.0906  -0.3594 0.0629  185 GLY A CA  
1459 C C   . GLY A 185 ? 0.9477 0.6983 0.6966 0.0820  -0.3355 0.0745  185 GLY A C   
1460 O O   . GLY A 185 ? 0.9635 0.7264 0.6873 0.0761  -0.2947 0.0658  185 GLY A O   
1461 N N   . ASP A 186 ? 0.9491 0.6541 0.6523 0.0804  -0.3615 0.0946  186 ASP A N   
1462 C CA  . ASP A 186 ? 1.0585 0.7277 0.6828 0.0708  -0.3380 0.1070  186 ASP A CA  
1463 C C   . ASP A 186 ? 1.0681 0.7482 0.7328 0.0775  -0.3160 0.1114  186 ASP A C   
1464 O O   . ASP A 186 ? 1.0693 0.7137 0.6788 0.0703  -0.3074 0.1264  186 ASP A O   
1465 C CB  . ASP A 186 ? 1.1650 0.7840 0.7212 0.0581  -0.3615 0.1221  186 ASP A CB  
1466 C CG  . ASP A 186 ? 1.2169 0.8224 0.7159 0.0447  -0.3623 0.1137  186 ASP A CG  
1467 O OD1 . ASP A 186 ? 1.2007 0.8213 0.6794 0.0417  -0.3340 0.1002  186 ASP A OD1 
1468 O OD2 . ASP A 186 ? 1.3672 0.9451 0.8418 0.0371  -0.3917 0.1200  186 ASP A OD2 
1469 N N   . GLY A 187 ? 1.0070 0.7338 0.7643 0.0893  -0.3052 0.0978  187 GLY A N   
1470 C CA  . GLY A 187 ? 0.8800 0.6167 0.6767 0.0949  -0.2842 0.0989  187 GLY A CA  
1471 C C   . GLY A 187 ? 0.9425 0.6916 0.7112 0.0864  -0.2353 0.0929  187 GLY A C   
1472 O O   . GLY A 187 ? 0.8976 0.6538 0.6276 0.0782  -0.2147 0.0858  187 GLY A O   
1473 N N   . GLU A 188 ? 0.8958 0.6470 0.6887 0.0887  -0.2178 0.0952  188 GLU A N   
1474 C CA  . GLU A 188 ? 0.8929 0.6581 0.6703 0.0809  -0.1747 0.0897  188 GLU A CA  
1475 C C   . GLU A 188 ? 0.8516 0.6678 0.6826 0.0836  -0.1503 0.0686  188 GLU A C   
1476 O O   . GLU A 188 ? 0.7829 0.6247 0.6768 0.0921  -0.1599 0.0578  188 GLU A O   
1477 C CB  . GLU A 188 ? 0.9619 0.7106 0.7487 0.0809  -0.1668 0.0985  188 GLU A CB  
1478 C CG  . GLU A 188 ? 1.0474 0.8105 0.8229 0.0717  -0.1256 0.0933  188 GLU A CG  
1479 C CD  . GLU A 188 ? 1.1973 0.9374 0.9742 0.0692  -0.1199 0.1035  188 GLU A CD  
1480 O OE1 . GLU A 188 ? 1.2562 0.9638 1.0357 0.0746  -0.1484 0.1167  188 GLU A OE1 
1481 O OE2 . GLU A 188 ? 1.2351 0.9882 1.0123 0.0616  -0.0890 0.0986  188 GLU A OE2 
1482 N N   . PHE A 189 ? 0.7873 0.6172 0.5939 0.0753  -0.1182 0.0629  189 PHE A N   
1483 C CA  . PHE A 189 ? 0.7196 0.5916 0.5666 0.0756  -0.0961 0.0460  189 PHE A CA  
1484 C C   . PHE A 189 ? 0.7186 0.5993 0.5524 0.0678  -0.0638 0.0447  189 PHE A C   
1485 O O   . PHE A 189 ? 0.7008 0.5589 0.4886 0.0610  -0.0546 0.0543  189 PHE A O   
1486 C CB  . PHE A 189 ? 0.6762 0.5603 0.5135 0.0745  -0.1004 0.0383  189 PHE A CB  
1487 C CG  . PHE A 189 ? 0.7289 0.5912 0.5006 0.0671  -0.0934 0.0434  189 PHE A CG  
1488 C CD1 . PHE A 189 ? 0.8131 0.6379 0.5340 0.0648  -0.1159 0.0541  189 PHE A CD1 
1489 C CD2 . PHE A 189 ? 0.7071 0.5848 0.4682 0.0618  -0.0646 0.0366  189 PHE A CD2 
1490 C CE1 . PHE A 189 ? 0.8340 0.6363 0.4905 0.0561  -0.1050 0.0558  189 PHE A CE1 
1491 C CE2 . PHE A 189 ? 0.7103 0.5690 0.4177 0.0555  -0.0544 0.0381  189 PHE A CE2 
1492 C CZ  . PHE A 189 ? 0.7295 0.5502 0.3826 0.0520  -0.0722 0.0465  189 PHE A CZ  
1493 N N   . ILE A 190 ? 0.6541 0.5667 0.5288 0.0674  -0.0468 0.0324  190 ILE A N   
1494 C CA  . ILE A 190 ? 0.6367 0.5617 0.5058 0.0598  -0.0204 0.0300  190 ILE A CA  
1495 C C   . ILE A 190 ? 0.6212 0.5569 0.4687 0.0562  -0.0102 0.0265  190 ILE A C   
1496 O O   . ILE A 190 ? 0.5659 0.5170 0.4272 0.0586  -0.0154 0.0188  190 ILE A O   
1497 C CB  . ILE A 190 ? 0.6078 0.5577 0.5220 0.0587  -0.0093 0.0186  190 ILE A CB  
1498 C CG1 . ILE A 190 ? 0.6309 0.5682 0.5715 0.0634  -0.0177 0.0193  190 ILE A CG1 
1499 C CG2 . ILE A 190 ? 0.6099 0.5719 0.5179 0.0497  0.0126  0.0169  190 ILE A CG2 
1500 C CD1 . ILE A 190 ? 0.7405 0.6471 0.6532 0.0611  -0.0189 0.0332  190 ILE A CD1 
1501 N N   . LYS A 191 ? 0.6457 0.5726 0.4628 0.0503  0.0053  0.0315  191 LYS A N   
1502 C CA  . LYS A 191 ? 0.6190 0.5547 0.4211 0.0480  0.0173  0.0269  191 LYS A CA  
1503 C C   . LYS A 191 ? 0.6168 0.5821 0.4516 0.0453  0.0317  0.0200  191 LYS A C   
1504 O O   . LYS A 191 ? 0.5874 0.5579 0.4324 0.0402  0.0433  0.0219  191 LYS A O   
1505 C CB  . LYS A 191 ? 0.6685 0.5815 0.4273 0.0422  0.0302  0.0333  191 LYS A CB  
1506 C CG  . LYS A 191 ? 0.7597 0.6354 0.4733 0.0415  0.0145  0.0430  191 LYS A CG  
1507 C CD  . LYS A 191 ? 0.7584 0.6094 0.4229 0.0318  0.0334  0.0485  191 LYS A CD  
1508 C CE  . LYS A 191 ? 0.9496 0.7565 0.5557 0.0280  0.0159  0.0596  191 LYS A CE  
1509 N NZ  . LYS A 191 ? 1.1121 0.8994 0.7216 0.0291  -0.0035 0.0731  191 LYS A NZ  
1510 N N   . CYS A 192 ? 0.5822 0.5642 0.4315 0.0473  0.0289  0.0127  192 CYS A N   
1511 C CA  . CYS A 192 ? 0.5004 0.5059 0.3751 0.0437  0.0373  0.0080  192 CYS A CA  
1512 C C   . CYS A 192 ? 0.5779 0.5877 0.4472 0.0451  0.0427  0.0053  192 CYS A C   
1513 O O   . CYS A 192 ? 0.5840 0.5893 0.4456 0.0486  0.0347  0.0018  192 CYS A O   
1514 C CB  . CYS A 192 ? 0.5183 0.5369 0.4170 0.0428  0.0295  0.0023  192 CYS A CB  
1515 S SG  . CYS A 192 ? 0.5134 0.5270 0.4283 0.0435  0.0244  0.0011  192 CYS A SG  
1516 N N   . LEU A 193 ? 0.4773 0.4956 0.3551 0.0423  0.0557  0.0061  193 LEU A N   
1517 C CA  . LEU A 193 ? 0.5816 0.6054 0.4649 0.0449  0.0623  0.0024  193 LEU A CA  
1518 C C   . LEU A 193 ? 0.5669 0.6112 0.4822 0.0420  0.0599  0.0026  193 LEU A C   
1519 O O   . LEU A 193 ? 0.5443 0.5984 0.4744 0.0364  0.0632  0.0054  193 LEU A O   
1520 C CB  . LEU A 193 ? 0.4991 0.5149 0.3705 0.0441  0.0805  0.0021  193 LEU A CB  
1521 C CG  . LEU A 193 ? 0.5758 0.5989 0.4626 0.0477  0.0921  -0.0046 193 LEU A CG  
1522 C CD1 . LEU A 193 ? 0.4882 0.5004 0.3606 0.0536  0.0843  -0.0107 193 LEU A CD1 
1523 C CD2 . LEU A 193 ? 0.5361 0.5520 0.4125 0.0445  0.1157  -0.0069 193 LEU A CD2 
1524 N N   . HIS A 194 ? 0.4726 0.5203 0.3960 0.0446  0.0521  0.0002  194 HIS A N   
1525 C CA  . HIS A 194 ? 0.4927 0.5539 0.4400 0.0409  0.0448  0.0027  194 HIS A CA  
1526 C C   . HIS A 194 ? 0.5182 0.5791 0.4794 0.0471  0.0431  0.0007  194 HIS A C   
1527 O O   . HIS A 194 ? 0.5100 0.5591 0.4582 0.0524  0.0427  -0.0040 194 HIS A O   
1528 C CB  . HIS A 194 ? 0.4611 0.5228 0.4032 0.0341  0.0335  0.0039  194 HIS A CB  
1529 C CG  . HIS A 194 ? 0.4489 0.5165 0.4029 0.0278  0.0234  0.0081  194 HIS A CG  
1530 N ND1 . HIS A 194 ? 0.4832 0.5447 0.4345 0.0270  0.0143  0.0091  194 HIS A ND1 
1531 C CD2 . HIS A 194 ? 0.4391 0.5151 0.4050 0.0207  0.0185  0.0128  194 HIS A CD2 
1532 C CE1 . HIS A 194 ? 0.4925 0.5560 0.4502 0.0195  0.0038  0.0156  194 HIS A CE1 
1533 N NE2 . HIS A 194 ? 0.4788 0.5514 0.4453 0.0156  0.0050  0.0178  194 HIS A NE2 
1534 N N   . SER A 195 ? 0.4335 0.5064 0.4239 0.0465  0.0400  0.0038  195 SER A N   
1535 C CA  . SER A 195 ? 0.5097 0.5825 0.5232 0.0532  0.0348  0.0028  195 SER A CA  
1536 C C   . SER A 195 ? 0.5251 0.6075 0.5630 0.0477  0.0176  0.0115  195 SER A C   
1537 O O   . SER A 195 ? 0.4632 0.5573 0.5118 0.0412  0.0163  0.0152  195 SER A O   
1538 C CB  . SER A 195 ? 0.4846 0.5604 0.5177 0.0619  0.0529  -0.0052 195 SER A CB  
1539 O OG  . SER A 195 ? 0.4807 0.5567 0.5451 0.0699  0.0477  -0.0077 195 SER A OG  
1540 N N   . VAL A 196 ? 0.4741 0.5482 0.5178 0.0490  0.0022  0.0156  196 VAL A N   
1541 C CA  . VAL A 196 ? 0.4613 0.5390 0.5254 0.0437  -0.0187 0.0260  196 VAL A CA  
1542 C C   . VAL A 196 ? 0.4959 0.5878 0.6114 0.0527  -0.0194 0.0251  196 VAL A C   
1543 O O   . VAL A 196 ? 0.5266 0.6245 0.6659 0.0484  -0.0397 0.0343  196 VAL A O   
1544 C CB  . VAL A 196 ? 0.5755 0.6348 0.6273 0.0411  -0.0361 0.0327  196 VAL A CB  
1545 C CG1 . VAL A 196 ? 0.5675 0.6167 0.5760 0.0303  -0.0328 0.0321  196 VAL A CG1 
1546 C CG2 . VAL A 196 ? 0.5143 0.5652 0.5864 0.0554  -0.0322 0.0262  196 VAL A CG2 
1547 N N   . GLY A 197 ? 0.5123 0.6091 0.6458 0.0640  0.0021  0.0136  197 GLY A N   
1548 C CA  . GLY A 197 ? 0.4907 0.6047 0.6800 0.0721  0.0084  0.0091  197 GLY A CA  
1549 C C   . GLY A 197 ? 0.5475 0.6591 0.7816 0.0826  -0.0074 0.0107  197 GLY A C   
1550 O O   . GLY A 197 ? 0.5285 0.6571 0.8182 0.0864  -0.0163 0.0128  197 GLY A O   
1551 N N   . CYS A 198 ? 0.5029 0.5933 0.7190 0.0876  -0.0126 0.0097  198 CYS A N   
1552 C CA  . CYS A 198 ? 0.5018 0.5838 0.7592 0.0981  -0.0296 0.0119  198 CYS A CA  
1553 C C   . CYS A 198 ? 0.5804 0.6478 0.8366 0.1099  -0.0095 -0.0041 198 CYS A C   
1554 O O   . CYS A 198 ? 0.6110 0.6550 0.8431 0.1102  -0.0195 -0.0021 198 CYS A O   
1555 C CB  . CYS A 198 ? 0.6044 0.6675 0.8382 0.0888  -0.0628 0.0299  198 CYS A CB  
1556 S SG  . CYS A 198 ? 0.6870 0.7612 0.9252 0.0742  -0.0919 0.0482  198 CYS A SG  
1557 N N   . PRO A 199 ? 0.5821 0.6608 0.8618 0.1182  0.0202  -0.0211 199 PRO A N   
1558 C CA  . PRO A 199 ? 0.5572 0.6189 0.8331 0.1282  0.0407  -0.0389 199 PRO A CA  
1559 C C   . PRO A 199 ? 0.6377 0.6871 0.9600 0.1404  0.0235  -0.0391 199 PRO A C   
1560 O O   . PRO A 199 ? 0.6389 0.7010 1.0199 0.1461  0.0046  -0.0309 199 PRO A O   
1561 C CB  . PRO A 199 ? 0.5298 0.6082 0.8289 0.1320  0.0765  -0.0561 199 PRO A CB  
1562 C CG  . PRO A 199 ? 0.5611 0.6690 0.9076 0.1291  0.0683  -0.0467 199 PRO A CG  
1563 C CD  . PRO A 199 ? 0.5275 0.6331 0.8379 0.1168  0.0379  -0.0258 199 PRO A CD  
1564 N N   . LEU A 200 ? 0.6623 0.6850 0.9591 0.1442  0.0275  -0.0481 200 LEU A N   
1565 C CA  . LEU A 200 ? 0.7163 0.7216 1.0553 0.1564  0.0130  -0.0500 200 LEU A CA  
1566 C C   . LEU A 200 ? 0.7107 0.7189 1.0980 0.1716  0.0433  -0.0755 200 LEU A C   
1567 O O   . LEU A 200 ? 0.6808 0.6893 1.0383 0.1695  0.0773  -0.0937 200 LEU A O   
1568 C CB  . LEU A 200 ? 0.6995 0.6722 0.9892 0.1512  0.0012  -0.0472 200 LEU A CB  
1569 C CG  . LEU A 200 ? 0.6931 0.6609 0.9343 0.1345  -0.0235 -0.0251 200 LEU A CG  
1570 C CD1 . LEU A 200 ? 0.6701 0.6084 0.8677 0.1284  -0.0293 -0.0262 200 LEU A CD1 
1571 C CD2 . LEU A 200 ? 0.7293 0.7002 1.0018 0.1323  -0.0564 -0.0031 200 LEU A CD2 
1572 N N   . PRO A 201 ? 0.7883 0.7969 1.2503 0.1866  0.0324  -0.0778 201 PRO A N   
1573 C CA  . PRO A 201 ? 0.7957 0.7977 1.2952 0.1899  -0.0112 -0.0554 201 PRO A CA  
1574 C C   . PRO A 201 ? 0.8361 0.8647 1.3510 0.1816  -0.0339 -0.0344 201 PRO A C   
1575 O O   . PRO A 201 ? 0.8406 0.8994 1.3772 0.1805  -0.0144 -0.0414 201 PRO A O   
1576 C CB  . PRO A 201 ? 0.8025 0.8017 1.3885 0.2112  -0.0070 -0.0709 201 PRO A CB  
1577 C CG  . PRO A 201 ? 0.7823 0.8064 1.3958 0.2167  0.0393  -0.0979 201 PRO A CG  
1578 C CD  . PRO A 201 ? 0.7865 0.8021 1.3066 0.2016  0.0654  -0.1051 201 PRO A CD  
1579 N N   . LEU A 202 ? 0.8280 0.8431 1.3285 0.1736  -0.0748 -0.0087 202 LEU A N   
1580 C CA  . LEU A 202 ? 0.8976 0.9325 1.4040 0.1631  -0.0991 0.0109  202 LEU A CA  
1581 C C   . LEU A 202 ? 0.9431 1.0012 1.5462 0.1769  -0.1120 0.0104  202 LEU A C   
1582 O O   . LEU A 202 ? 0.9225 0.9701 1.5869 0.1933  -0.1239 0.0071  202 LEU A O   
1583 C CB  . LEU A 202 ? 0.9180 0.9265 1.3757 0.1483  -0.1384 0.0377  202 LEU A CB  
1584 C CG  . LEU A 202 ? 0.8625 0.8556 1.2302 0.1308  -0.1283 0.0406  202 LEU A CG  
1585 C CD1 . LEU A 202 ? 0.8702 0.8403 1.1947 0.1133  -0.1640 0.0665  202 LEU A CD1 
1586 C CD2 . LEU A 202 ? 0.7202 0.7398 1.0585 0.1227  -0.1007 0.0314  202 LEU A CD2 
1587 N N   . LYS A 203 ? 1.0869 1.1770 1.7080 0.1702  -0.1104 0.0131  203 LYS A N   
1588 C CA  . LYS A 203 ? 1.1255 1.2423 1.8406 0.1798  -0.1280 0.0152  203 LYS A CA  
1589 C C   . LYS A 203 ? 1.1998 1.3148 1.9083 0.1668  -0.1780 0.0436  203 LYS A C   
1590 O O   . LYS A 203 ? 1.1800 1.3057 1.9441 0.1678  -0.1995 0.0482  203 LYS A O   
1591 C CB  . LYS A 203 ? 1.1933 1.3493 1.9453 0.1810  -0.0879 -0.0049 203 LYS A CB  
1592 C CG  . LYS A 203 ? 1.2342 1.3895 1.9884 0.1913  -0.0364 -0.0340 203 LYS A CG  
1593 C CD  . LYS A 203 ? 1.3092 1.4973 2.0808 0.1869  0.0057  -0.0513 203 LYS A CD  
1594 C CE  . LYS A 203 ? 1.3474 1.5268 2.1027 0.1925  0.0570  -0.0795 203 LYS A CE  
1595 N NZ  . LYS A 203 ? 1.2925 1.4367 1.9538 0.1872  0.0627  -0.0793 203 LYS A NZ  
1596 N N   . LYS A 204 ? 1.2367 1.3319 1.8540 0.1466  -0.1903 0.0594  204 LYS A N   
1597 C CA  . LYS A 204 ? 1.2272 1.3116 1.8194 0.1304  -0.2366 0.0859  204 LYS A CA  
1598 C C   . LYS A 204 ? 1.2004 1.2413 1.7138 0.1188  -0.2539 0.1016  204 LYS A C   
1599 O O   . LYS A 204 ? 1.1836 1.2151 1.6282 0.1100  -0.2261 0.0943  204 LYS A O   
1600 C CB  . LYS A 204 ? 1.2721 1.3786 1.8288 0.1123  -0.2284 0.0868  204 LYS A CB  
1601 C CG  . LYS A 204 ? 1.2495 1.3985 1.8727 0.1202  -0.2008 0.0687  204 LYS A CG  
1602 C CD  . LYS A 204 ? 1.2929 1.4570 1.8696 0.1011  -0.1893 0.0690  204 LYS A CD  
1603 C CE  . LYS A 204 ? 1.1888 1.3922 1.8260 0.1064  -0.1578 0.0512  204 LYS A CE  
1604 N NZ  . LYS A 204 ? 0.9792 1.1927 1.5687 0.0877  -0.1454 0.0513  204 LYS A NZ  
1605 N N   . PRO A 205 ? 1.2123 1.2246 1.7335 0.1175  -0.2991 0.1233  205 PRO A N   
1606 C CA  . PRO A 205 ? 1.1799 1.1482 1.6244 0.1037  -0.3131 0.1388  205 PRO A CA  
1607 C C   . PRO A 205 ? 1.0781 1.0416 1.4290 0.0772  -0.3039 0.1445  205 PRO A C   
1608 O O   . PRO A 205 ? 1.0790 1.0582 1.4181 0.0644  -0.3136 0.1500  205 PRO A O   
1609 C CB  . PRO A 205 ? 1.1690 1.1096 1.6247 0.0976  -0.3577 0.1592  205 PRO A CB  
1610 C CG  . PRO A 205 ? 1.1700 1.1381 1.7208 0.1156  -0.3558 0.1458  205 PRO A CG  
1611 C CD  . PRO A 205 ? 1.2310 1.2455 1.8120 0.1209  -0.3272 0.1292  205 PRO A CD  
1612 N N   . LEU A 206 ? 1.0072 0.9490 1.2952 0.0688  -0.2844 0.1415  206 LEU A N   
1613 C CA  . LEU A 206 ? 0.9731 0.9109 1.1791 0.0452  -0.2705 0.1433  206 LEU A CA  
1614 C C   . LEU A 206 ? 0.9900 0.8934 1.1393 0.0209  -0.3067 0.1690  206 LEU A C   
1615 O O   . LEU A 206 ? 1.0247 0.8934 1.1702 0.0195  -0.3341 0.1855  206 LEU A O   
1616 C CB  . LEU A 206 ? 0.8733 0.8034 1.0416 0.0452  -0.2365 0.1292  206 LEU A CB  
1617 C CG  . LEU A 206 ? 0.8215 0.7807 1.0186 0.0622  -0.1969 0.1034  206 LEU A CG  
1618 C CD1 . LEU A 206 ? 0.8303 0.7786 0.9797 0.0573  -0.1710 0.0928  206 LEU A CD1 
1619 C CD2 . LEU A 206 ? 0.8246 0.8173 1.0290 0.0596  -0.1829 0.0960  206 LEU A CD2 
1620 N N   . VAL A 207 ? 0.9262 0.8361 1.0279 0.0004  -0.3061 0.1721  207 VAL A N   
1621 C CA  . VAL A 207 ? 0.9524 0.8279 0.9848 -0.0277 -0.3340 0.1936  207 VAL A CA  
1622 C C   . VAL A 207 ? 0.9894 0.8488 0.9477 -0.0463 -0.3052 0.1884  207 VAL A C   
1623 O O   . VAL A 207 ? 0.9399 0.8237 0.8858 -0.0469 -0.2692 0.1696  207 VAL A O   
1624 C CB  . VAL A 207 ? 0.8917 0.7806 0.9136 -0.0414 -0.3504 0.1979  207 VAL A CB  
1625 C CG1 . VAL A 207 ? 0.9293 0.7788 0.8638 -0.0746 -0.3724 0.2165  207 VAL A CG1 
1626 C CG2 . VAL A 207 ? 0.9081 0.8134 1.0109 -0.0245 -0.3835 0.2045  207 VAL A CG2 
1627 N N   . ASN A 208 ? 1.0093 0.8268 0.9216 -0.0619 -0.3215 0.2054  208 ASN A N   
1628 C CA  . ASN A 208 ? 0.9967 0.7975 0.8440 -0.0818 -0.2947 0.2012  208 ASN A CA  
1629 C C   . ASN A 208 ? 0.9395 0.7650 0.8147 -0.0644 -0.2554 0.1777  208 ASN A C   
1630 O O   . ASN A 208 ? 0.9525 0.7853 0.7921 -0.0761 -0.2251 0.1655  208 ASN A O   
1631 C CB  . ASN A 208 ? 1.0112 0.8128 0.7945 -0.1089 -0.2834 0.1989  208 ASN A CB  
1632 C CG  . ASN A 208 ? 1.1158 0.8804 0.8467 -0.1344 -0.3212 0.2230  208 ASN A CG  
1633 O OD1 . ASN A 208 ? 1.2011 0.9522 0.9647 -0.1269 -0.3522 0.2348  208 ASN A OD1 
1634 N ND2 . ASN A 208 ? 1.1239 0.8787 0.7880 -0.1627 -0.3042 0.2178  208 ASN A ND2 
1635 N N   . ASN A 209 ? 0.9451 0.7826 0.8848 -0.0369 -0.2559 0.1704  209 ASN A N   
1636 C CA  . ASN A 209 ? 0.9003 0.7571 0.8631 -0.0207 -0.2222 0.1483  209 ASN A CA  
1637 C C   . ASN A 209 ? 0.8175 0.7083 0.7706 -0.0216 -0.1909 0.1301  209 ASN A C   
1638 O O   . ASN A 209 ? 0.7808 0.6798 0.7226 -0.0206 -0.1639 0.1154  209 ASN A O   
1639 C CB  . ASN A 209 ? 0.9158 0.7447 0.8458 -0.0310 -0.2145 0.1499  209 ASN A CB  
1640 C CG  . ASN A 209 ? 1.0035 0.7965 0.9503 -0.0263 -0.2430 0.1658  209 ASN A CG  
1641 O OD1 . ASN A 209 ? 1.0586 0.8538 1.0589 -0.0068 -0.2624 0.1690  209 ASN A OD1 
1642 N ND2 . ASN A 209 ? 1.0612 0.8207 0.9666 -0.0442 -0.2448 0.1752  209 ASN A ND2 
1643 N N   . TRP A 210 ? 0.7472 0.6565 0.7067 -0.0238 -0.1967 0.1313  210 TRP A N   
1644 C CA  . TRP A 210 ? 0.8134 0.7508 0.7634 -0.0260 -0.1704 0.1162  210 TRP A CA  
1645 C C   . TRP A 210 ? 0.7160 0.6837 0.7240 -0.0041 -0.1628 0.1052  210 TRP A C   
1646 O O   . TRP A 210 ? 0.7110 0.6884 0.7473 -0.0020 -0.1811 0.1117  210 TRP A O   
1647 C CB  . TRP A 210 ? 0.7721 0.7037 0.6768 -0.0499 -0.1790 0.1241  210 TRP A CB  
1648 C CG  . TRP A 210 ? 0.6739 0.6297 0.5676 -0.0531 -0.1517 0.1081  210 TRP A CG  
1649 C CD1 . TRP A 210 ? 0.7073 0.6857 0.6222 -0.0491 -0.1502 0.1028  210 TRP A CD1 
1650 C CD2 . TRP A 210 ? 0.6986 0.6573 0.5627 -0.0608 -0.1231 0.0954  210 TRP A CD2 
1651 N NE1 . TRP A 210 ? 0.6451 0.6369 0.5418 -0.0536 -0.1229 0.0884  210 TRP A NE1 
1652 C CE2 . TRP A 210 ? 0.6800 0.6611 0.5482 -0.0598 -0.1066 0.0834  210 TRP A CE2 
1653 C CE3 . TRP A 210 ? 0.7106 0.6554 0.5501 -0.0685 -0.1106 0.0928  210 TRP A CE3 
1654 C CZ2 . TRP A 210 ? 0.6566 0.6457 0.5074 -0.0645 -0.0799 0.0693  210 TRP A CZ2 
1655 C CZ3 . TRP A 210 ? 0.6541 0.6107 0.4798 -0.0737 -0.0834 0.0779  210 TRP A CZ3 
1656 C CH2 . TRP A 210 ? 0.6218 0.5999 0.4542 -0.0708 -0.0691 0.0665  210 TRP A CH2 
1657 N N   . ALA A 211 ? 0.6553 0.6370 0.6798 0.0105  -0.1360 0.0884  211 ALA A N   
1658 C CA  . ALA A 211 ? 0.6491 0.6569 0.7209 0.0285  -0.1222 0.0763  211 ALA A CA  
1659 C C   . ALA A 211 ? 0.6477 0.6767 0.7112 0.0209  -0.1121 0.0723  211 ALA A C   
1660 O O   . ALA A 211 ? 0.6195 0.6489 0.6438 0.0102  -0.0975 0.0675  211 ALA A O   
1661 C CB  . ALA A 211 ? 0.6188 0.6288 0.6956 0.0420  -0.0966 0.0600  211 ALA A CB  
1662 N N   . CYS A 212 ? 0.6357 0.6824 0.7415 0.0266  -0.1200 0.0736  212 CYS A N   
1663 C CA  . CYS A 212 ? 0.5761 0.6422 0.6804 0.0193  -0.1117 0.0698  212 CYS A CA  
1664 C C   . CYS A 212 ? 0.5979 0.6862 0.7662 0.0299  -0.1174 0.0685  212 CYS A C   
1665 O O   . CYS A 212 ? 0.5601 0.6471 0.7726 0.0406  -0.1343 0.0733  212 CYS A O   
1666 C CB  . CYS A 212 ? 0.6003 0.6544 0.6594 -0.0031 -0.1290 0.0801  212 CYS A CB  
1667 S SG  . CYS A 212 ? 0.6281 0.6660 0.6957 -0.0124 -0.1749 0.1009  212 CYS A SG  
1668 N N   . ASN A 213 ? 0.5985 0.7070 0.7761 0.0267  -0.1027 0.0616  213 ASN A N   
1669 C CA  . ASN A 213 ? 0.5768 0.7106 0.8186 0.0340  -0.1033 0.0584  213 ASN A CA  
1670 C C   . ASN A 213 ? 0.6070 0.7511 0.8397 0.0180  -0.1101 0.0612  213 ASN A C   
1671 O O   . ASN A 213 ? 0.6021 0.7591 0.8337 0.0161  -0.0856 0.0518  213 ASN A O   
1672 C CB  . ASN A 213 ? 0.5841 0.7324 0.8535 0.0485  -0.0675 0.0424  213 ASN A CB  
1673 C CG  . ASN A 213 ? 0.5738 0.7474 0.9220 0.0587  -0.0655 0.0372  213 ASN A CG  
1674 O OD1 . ASN A 213 ? 0.6139 0.8027 0.9968 0.0521  -0.0853 0.0436  213 ASN A OD1 
1675 N ND2 . ASN A 213 ? 0.5209 0.6990 0.8995 0.0738  -0.0410 0.0243  213 ASN A ND2 
1676 N N   . PRO A 214 ? 0.6442 0.7790 0.8663 0.0047  -0.1445 0.0744  214 PRO A N   
1677 C CA  . PRO A 214 ? 0.6573 0.7971 0.8620 -0.0132 -0.1521 0.0755  214 PRO A CA  
1678 C C   . PRO A 214 ? 0.6835 0.8537 0.9476 -0.0094 -0.1419 0.0679  214 PRO A C   
1679 O O   . PRO A 214 ? 0.6650 0.8407 0.9114 -0.0193 -0.1261 0.0613  214 PRO A O   
1680 C CB  . PRO A 214 ? 0.6589 0.7811 0.8487 -0.0267 -0.1962 0.0921  214 PRO A CB  
1681 C CG  . PRO A 214 ? 0.6601 0.7594 0.8315 -0.0200 -0.2048 0.1001  214 PRO A CG  
1682 C CD  . PRO A 214 ? 0.6533 0.7679 0.8727 0.0036  -0.1792 0.0893  214 PRO A CD  
1683 N N   . GLU A 215 ? 0.6679 0.8576 1.0060 0.0043  -0.1494 0.0679  215 GLU A N   
1684 C CA  . GLU A 215 ? 0.6369 0.8580 1.0394 0.0058  -0.1391 0.0602  215 GLU A CA  
1685 C C   . GLU A 215 ? 0.6200 0.8487 1.0087 0.0078  -0.0934 0.0461  215 GLU A C   
1686 O O   . GLU A 215 ? 0.5812 0.8227 0.9786 -0.0025 -0.0832 0.0419  215 GLU A O   
1687 C CB  . GLU A 215 ? 0.6569 0.8987 1.1481 0.0228  -0.1479 0.0591  215 GLU A CB  
1688 C CG  . GLU A 215 ? 0.7328 0.9656 1.2465 0.0222  -0.1987 0.0754  215 GLU A CG  
1689 C CD  . GLU A 215 ? 0.8420 1.0430 1.3122 0.0284  -0.2096 0.0837  215 GLU A CD  
1690 O OE1 . GLU A 215 ? 0.7808 0.9691 1.2037 0.0325  -0.1784 0.0759  215 GLU A OE1 
1691 O OE2 . GLU A 215 ? 0.8468 1.0340 1.3305 0.0285  -0.2511 0.0989  215 GLU A OE2 
1692 N N   . LEU A 216 ? 0.5988 0.8167 0.9635 0.0196  -0.0674 0.0396  216 LEU A N   
1693 C CA  . LEU A 216 ? 0.5133 0.7331 0.8606 0.0218  -0.0271 0.0280  216 LEU A CA  
1694 C C   . LEU A 216 ? 0.5093 0.7067 0.7803 0.0129  -0.0189 0.0289  216 LEU A C   
1695 O O   . LEU A 216 ? 0.4865 0.6783 0.7335 0.0157  0.0097  0.0217  216 LEU A O   
1696 C CB  . LEU A 216 ? 0.5161 0.7358 0.8818 0.0390  -0.0036 0.0187  216 LEU A CB  
1697 C CG  . LEU A 216 ? 0.5058 0.7489 0.9562 0.0506  -0.0033 0.0131  216 LEU A CG  
1698 C CD1 . LEU A 216 ? 0.5302 0.7668 0.9872 0.0663  0.0230  0.0010  216 LEU A CD1 
1699 C CD2 . LEU A 216 ? 0.4614 0.7323 0.9623 0.0437  0.0125  0.0071  216 LEU A CD2 
1700 N N   . THR A 217 ? 0.5492 0.7323 0.7820 0.0016  -0.0432 0.0370  217 THR A N   
1701 C CA  . THR A 217 ? 0.5438 0.7075 0.7131 -0.0060 -0.0339 0.0353  217 THR A CA  
1702 C C   . THR A 217 ? 0.5800 0.7479 0.7432 -0.0127 -0.0130 0.0291  217 THR A C   
1703 O O   . THR A 217 ? 0.5323 0.7132 0.7232 -0.0215 -0.0179 0.0293  217 THR A O   
1704 C CB  . THR A 217 ? 0.5502 0.6985 0.6825 -0.0206 -0.0601 0.0429  217 THR A CB  
1705 O OG1 . THR A 217 ? 0.6136 0.7506 0.7402 -0.0156 -0.0772 0.0501  217 THR A OG1 
1706 C CG2 . THR A 217 ? 0.5393 0.6715 0.6169 -0.0294 -0.0463 0.0376  217 THR A CG2 
1707 N N   . LEU A 218 ? 0.5542 0.7094 0.6822 -0.0088 0.0082  0.0243  218 LEU A N   
1708 C CA  . LEU A 218 ? 0.4706 0.6231 0.5875 -0.0144 0.0269  0.0202  218 LEU A CA  
1709 C C   . LEU A 218 ? 0.4994 0.6318 0.5701 -0.0112 0.0373  0.0176  218 LEU A C   
1710 O O   . LEU A 218 ? 0.5259 0.6522 0.5858 -0.0002 0.0445  0.0165  218 LEU A O   
1711 C CB  . LEU A 218 ? 0.5058 0.6709 0.6569 -0.0093 0.0485  0.0170  218 LEU A CB  
1712 C CG  . LEU A 218 ? 0.4812 0.6403 0.6216 -0.0167 0.0682  0.0150  218 LEU A CG  
1713 C CD1 . LEU A 218 ? 0.4179 0.5840 0.5737 -0.0318 0.0568  0.0159  218 LEU A CD1 
1714 C CD2 . LEU A 218 ? 0.5083 0.6746 0.6713 -0.0125 0.0943  0.0117  218 LEU A CD2 
1715 N N   . ILE A 219 ? 0.5384 0.6606 0.5855 -0.0207 0.0373  0.0156  219 ILE A N   
1716 C CA  . ILE A 219 ? 0.5347 0.6399 0.5489 -0.0174 0.0462  0.0124  219 ILE A CA  
1717 C C   . ILE A 219 ? 0.5335 0.6313 0.5466 -0.0197 0.0608  0.0114  219 ILE A C   
1718 O O   . ILE A 219 ? 0.5120 0.6094 0.5304 -0.0308 0.0594  0.0098  219 ILE A O   
1719 C CB  . ILE A 219 ? 0.5401 0.6367 0.5308 -0.0259 0.0365  0.0089  219 ILE A CB  
1720 C CG1 . ILE A 219 ? 0.5290 0.6286 0.5162 -0.0275 0.0208  0.0123  219 ILE A CG1 
1721 C CG2 . ILE A 219 ? 0.5022 0.5851 0.4721 -0.0203 0.0456  0.0041  219 ILE A CG2 
1722 C CD1 . ILE A 219 ? 0.5193 0.6278 0.5227 -0.0374 0.0035  0.0172  219 ILE A CD1 
1723 N N   . ALA A 220 ? 0.5038 0.5923 0.5062 -0.0109 0.0736  0.0129  220 ALA A N   
1724 C CA  . ALA A 220 ? 0.5540 0.6306 0.5509 -0.0137 0.0873  0.0150  220 ALA A CA  
1725 C C   . ALA A 220 ? 0.5111 0.5649 0.4788 -0.0085 0.0874  0.0155  220 ALA A C   
1726 O O   . ALA A 220 ? 0.5034 0.5527 0.4570 0.0003  0.0820  0.0146  220 ALA A O   
1727 C CB  . ALA A 220 ? 0.5255 0.6057 0.5307 -0.0108 0.1033  0.0173  220 ALA A CB  
1728 N N   . HIS A 221 ? 0.4978 0.5368 0.4608 -0.0141 0.0920  0.0171  221 HIS A N   
1729 C CA  . HIS A 221 ? 0.5247 0.5396 0.4672 -0.0087 0.0897  0.0190  221 HIS A CA  
1730 C C   . HIS A 221 ? 0.5823 0.5765 0.5109 -0.0122 0.1003  0.0277  221 HIS A C   
1731 O O   . HIS A 221 ? 0.5787 0.5743 0.5195 -0.0228 0.1091  0.0290  221 HIS A O   
1732 C CB  . HIS A 221 ? 0.4967 0.5069 0.4468 -0.0123 0.0835  0.0117  221 HIS A CB  
1733 C CG  . HIS A 221 ? 0.5350 0.5621 0.4923 -0.0141 0.0765  0.0030  221 HIS A CG  
1734 N ND1 . HIS A 221 ? 0.5532 0.5969 0.5210 -0.0241 0.0740  0.0007  221 HIS A ND1 
1735 C CD2 . HIS A 221 ? 0.4723 0.5006 0.4265 -0.0091 0.0710  -0.0032 221 HIS A CD2 
1736 C CE1 . HIS A 221 ? 0.5553 0.6056 0.5186 -0.0259 0.0671  -0.0054 221 HIS A CE1 
1737 N NE2 . HIS A 221 ? 0.5403 0.5825 0.4965 -0.0174 0.0675  -0.0085 221 HIS A NE2 
1738 N N   . LEU A 222 ? 0.6220 0.5951 0.5228 -0.0050 0.0986  0.0340  222 LEU A N   
1739 C CA  . LEU A 222 ? 0.6430 0.5878 0.5182 -0.0098 0.1067  0.0447  222 LEU A CA  
1740 C C   . LEU A 222 ? 0.7155 0.6313 0.5736 -0.0029 0.0910  0.0501  222 LEU A C   
1741 O O   . LEU A 222 ? 0.6947 0.5947 0.5263 0.0043  0.0817  0.0551  222 LEU A O   
1742 C CB  . LEU A 222 ? 0.6763 0.6174 0.5266 -0.0104 0.1193  0.0483  222 LEU A CB  
1743 C CG  . LEU A 222 ? 0.6592 0.6292 0.5355 -0.0157 0.1364  0.0421  222 LEU A CG  
1744 C CD1 . LEU A 222 ? 0.6176 0.6160 0.5191 -0.0072 0.1261  0.0330  222 LEU A CD1 
1745 C CD2 . LEU A 222 ? 0.6969 0.6554 0.5469 -0.0198 0.1569  0.0446  222 LEU A CD2 
1746 N N   . PRO A 223 ? 0.6398 0.5469 0.5153 -0.0048 0.0860  0.0485  223 PRO A N   
1747 C CA  . PRO A 223 ? 0.6906 0.5716 0.5618 0.0040  0.0691  0.0524  223 PRO A CA  
1748 C C   . PRO A 223 ? 0.7516 0.5947 0.5829 0.0037  0.0633  0.0691  223 PRO A C   
1749 O O   . PRO A 223 ? 0.8077 0.6345 0.6275 0.0137  0.0443  0.0737  223 PRO A O   
1750 C CB  . PRO A 223 ? 0.6938 0.5704 0.5921 -0.0008 0.0708  0.0463  223 PRO A CB  
1751 C CG  . PRO A 223 ? 0.7080 0.5983 0.6118 -0.0154 0.0879  0.0449  223 PRO A CG  
1752 C CD  . PRO A 223 ? 0.6456 0.5655 0.5480 -0.0150 0.0940  0.0417  223 PRO A CD  
1753 N N   . ASP A 224 ? 0.7630 0.5900 0.5718 -0.0092 0.0786  0.0786  224 ASP A N   
1754 C CA  . ASP A 224 ? 0.9082 0.6925 0.6682 -0.0133 0.0744  0.0960  224 ASP A CA  
1755 C C   . ASP A 224 ? 0.9233 0.7038 0.6482 -0.0075 0.0672  0.0982  224 ASP A C   
1756 O O   . ASP A 224 ? 0.9938 0.7388 0.6827 -0.0045 0.0483  0.1105  224 ASP A O   
1757 C CB  . ASP A 224 ? 1.0098 0.7822 0.7509 -0.0315 0.0989  0.1036  224 ASP A CB  
1758 C CG  . ASP A 224 ? 1.0275 0.8003 0.8018 -0.0393 0.1048  0.1015  224 ASP A CG  
1759 O OD1 . ASP A 224 ? 0.9703 0.7299 0.7634 -0.0317 0.0874  0.1008  224 ASP A OD1 
1760 O OD2 . ASP A 224 ? 1.1459 0.9328 0.9310 -0.0533 0.1270  0.0991  224 ASP A OD2 
1761 N N   . ARG A 225 ? 0.8500 0.6641 0.5846 -0.0062 0.0796  0.0867  225 ARG A N   
1762 C CA  . ARG A 225 ? 0.9064 0.7182 0.6100 -0.0014 0.0750  0.0856  225 ARG A CA  
1763 C C   . ARG A 225 ? 0.8966 0.7286 0.6265 0.0132  0.0543  0.0762  225 ARG A C   
1764 O O   . ARG A 225 ? 0.8428 0.6739 0.5513 0.0174  0.0478  0.0739  225 ARG A O   
1765 C CB  . ARG A 225 ? 0.9154 0.7483 0.6158 -0.0085 0.1025  0.0778  225 ARG A CB  
1766 C CG  . ARG A 225 ? 1.0447 0.8552 0.7121 -0.0249 0.1272  0.0859  225 ARG A CG  
1767 C CD  . ARG A 225 ? 1.1015 0.9447 0.7948 -0.0310 0.1568  0.0744  225 ARG A CD  
1768 N NE  . ARG A 225 ? 1.1594 1.0171 0.8476 -0.0235 0.1600  0.0638  225 ARG A NE  
1769 C CZ  . ARG A 225 ? 1.2237 1.0628 0.8681 -0.0298 0.1774  0.0622  225 ARG A CZ  
1770 N NH1 . ARG A 225 ? 1.2878 1.0925 0.8847 -0.0452 0.1944  0.0716  225 ARG A NH1 
1771 N NH2 . ARG A 225 ? 1.1966 1.0494 0.8424 -0.0218 0.1790  0.0503  225 ARG A NH2 
1772 N N   . ARG A 226 ? 0.6989 0.6780 0.6172 -0.0065 0.0822  -0.0021 226 ARG A N   
1773 C CA  . ARG A 226 ? 0.7049 0.6887 0.6256 -0.0084 0.0742  -0.0074 226 ARG A CA  
1774 C C   . ARG A 226 ? 0.6885 0.6770 0.6146 -0.0122 0.0695  -0.0124 226 ARG A C   
1775 O O   . ARG A 226 ? 0.5765 0.5694 0.5021 -0.0112 0.0634  -0.0171 226 ARG A O   
1776 C CB  . ARG A 226 ? 0.7800 0.7651 0.6908 -0.0004 0.0705  -0.0089 226 ARG A CB  
1777 C CG  . ARG A 226 ? 0.8574 0.8368 0.7607 0.0047  0.0745  -0.0041 226 ARG A CG  
1778 C CD  . ARG A 226 ? 0.8379 0.8164 0.7483 -0.0001 0.0738  -0.0041 226 ARG A CD  
1779 N NE  . ARG A 226 ? 0.9698 0.9435 0.8723 0.0059  0.0754  -0.0010 226 ARG A NE  
1780 C CZ  . ARG A 226 ? 0.9520 0.9188 0.8534 0.0057  0.0820  0.0050  226 ARG A CZ  
1781 N NH1 . ARG A 226 ? 0.8363 0.8007 0.7455 -0.0004 0.0878  0.0080  226 ARG A NH1 
1782 N NH2 . ARG A 226 ? 0.9670 0.9289 0.8599 0.0119  0.0827  0.0075  226 ARG A NH2 
1783 N N   . GLU A 227 ? 0.6640 0.6515 0.5962 -0.0166 0.0721  -0.0117 227 GLU A N   
1784 C CA  . GLU A 227 ? 0.5862 0.5769 0.5226 -0.0196 0.0678  -0.0160 227 GLU A CA  
1785 C C   . GLU A 227 ? 0.5412 0.5299 0.4867 -0.0273 0.0663  -0.0175 227 GLU A C   
1786 O O   . GLU A 227 ? 0.5639 0.5490 0.5144 -0.0300 0.0702  -0.0148 227 GLU A O   
1787 C CB  . GLU A 227 ? 0.6413 0.6327 0.5762 -0.0167 0.0713  -0.0150 227 GLU A CB  
1788 C CG  . GLU A 227 ? 0.7751 0.7682 0.6989 -0.0083 0.0716  -0.0147 227 GLU A CG  
1789 C CD  . GLU A 227 ? 0.7638 0.7575 0.6861 -0.0057 0.0754  -0.0142 227 GLU A CD  
1790 O OE1 . GLU A 227 ? 0.7101 0.7029 0.6414 -0.0106 0.0787  -0.0138 227 GLU A OE1 
1791 O OE2 . GLU A 227 ? 0.9595 0.9546 0.8720 0.0015  0.0749  -0.0148 227 GLU A OE2 
1792 N N   . ILE A 228 ? 0.5214 0.5117 0.4688 -0.0304 0.0605  -0.0219 228 ILE A N   
1793 C CA  . ILE A 228 ? 0.5239 0.5109 0.4771 -0.0365 0.0582  -0.0238 228 ILE A CA  
1794 C C   . ILE A 228 ? 0.4728 0.4614 0.4273 -0.0369 0.0549  -0.0271 228 ILE A C   
1795 O O   . ILE A 228 ? 0.4481 0.4403 0.3995 -0.0347 0.0515  -0.0299 228 ILE A O   
1796 C CB  . ILE A 228 ? 0.5242 0.5093 0.4771 -0.0400 0.0551  -0.0258 228 ILE A CB  
1797 C CG1 . ILE A 228 ? 0.5658 0.5497 0.5180 -0.0394 0.0581  -0.0229 228 ILE A CG1 
1798 C CG2 . ILE A 228 ? 0.5308 0.5106 0.4867 -0.0453 0.0526  -0.0276 228 ILE A CG2 
1799 C CD1 . ILE A 228 ? 0.4828 0.4657 0.4351 -0.0423 0.0561  -0.0251 228 ILE A CD1 
1800 N N   . ILE A 229 ? 0.4707 0.4569 0.4306 -0.0393 0.0554  -0.0275 229 ILE A N   
1801 C CA  . ILE A 229 ? 0.4937 0.4813 0.4557 -0.0394 0.0523  -0.0308 229 ILE A CA  
1802 C C   . ILE A 229 ? 0.5016 0.4837 0.4675 -0.0441 0.0483  -0.0334 229 ILE A C   
1803 O O   . ILE A 229 ? 0.5355 0.5145 0.5070 -0.0458 0.0499  -0.0327 229 ILE A O   
1804 C CB  . ILE A 229 ? 0.5111 0.5015 0.4761 -0.0363 0.0571  -0.0294 229 ILE A CB  
1805 C CG1 . ILE A 229 ? 0.4959 0.4895 0.4537 -0.0306 0.0614  -0.0263 229 ILE A CG1 
1806 C CG2 . ILE A 229 ? 0.4506 0.4431 0.4181 -0.0361 0.0535  -0.0335 229 ILE A CG2 
1807 C CD1 . ILE A 229 ? 0.5302 0.5250 0.4889 -0.0271 0.0681  -0.0240 229 ILE A CD1 
1808 N N   . SER A 230 ? 0.5106 0.4908 0.4735 -0.0457 0.0429  -0.0366 230 SER A N   
1809 C CA  . SER A 230 ? 0.5092 0.4819 0.4722 -0.0493 0.0385  -0.0390 230 SER A CA  
1810 C C   . SER A 230 ? 0.5118 0.4841 0.4749 -0.0491 0.0336  -0.0429 230 SER A C   
1811 O O   . SER A 230 ? 0.5064 0.4824 0.4669 -0.0477 0.0321  -0.0442 230 SER A O   
1812 C CB  . SER A 230 ? 0.5423 0.5102 0.4997 -0.0520 0.0376  -0.0386 230 SER A CB  
1813 O OG  . SER A 230 ? 0.5652 0.5239 0.5200 -0.0547 0.0340  -0.0403 230 SER A OG  
1814 N N   . PHE A 231 ? 0.5095 0.4772 0.4761 -0.0501 0.0305  -0.0453 231 PHE A N   
1815 C CA  . PHE A 231 ? 0.5407 0.5079 0.5083 -0.0494 0.0255  -0.0493 231 PHE A CA  
1816 C C   . PHE A 231 ? 0.5850 0.5418 0.5502 -0.0512 0.0197  -0.0521 231 PHE A C   
1817 O O   . PHE A 231 ? 0.5941 0.5466 0.5617 -0.0520 0.0196  -0.0520 231 PHE A O   
1818 C CB  . PHE A 231 ? 0.5797 0.5537 0.5562 -0.0469 0.0278  -0.0504 231 PHE A CB  
1819 C CG  . PHE A 231 ? 0.5738 0.5485 0.5523 -0.0457 0.0228  -0.0549 231 PHE A CG  
1820 C CD1 . PHE A 231 ? 0.5967 0.5662 0.5796 -0.0464 0.0177  -0.0590 231 PHE A CD1 
1821 C CD2 . PHE A 231 ? 0.5712 0.5518 0.5475 -0.0434 0.0226  -0.0557 231 PHE A CD2 
1822 C CE1 . PHE A 231 ? 0.6039 0.5739 0.5888 -0.0450 0.0127  -0.0635 231 PHE A CE1 
1823 C CE2 . PHE A 231 ? 0.6216 0.6029 0.6000 -0.0422 0.0179  -0.0601 231 PHE A CE2 
1824 C CZ  . PHE A 231 ? 0.6265 0.6026 0.6094 -0.0431 0.0130  -0.0639 231 PHE A CZ  
1825 N N   . GLY A 232 ? 0.5728 0.5251 0.5328 -0.0514 0.0146  -0.0548 232 GLY A N   
1826 C CA  . GLY A 232 ? 0.6235 0.5654 0.5800 -0.0517 0.0081  -0.0581 232 GLY A CA  
1827 C C   . GLY A 232 ? 0.6842 0.6139 0.6290 -0.0538 0.0066  -0.0569 232 GLY A C   
1828 O O   . GLY A 232 ? 0.7455 0.6648 0.6835 -0.0534 0.0011  -0.0594 232 GLY A O   
1829 N N   . SER A 233 ? 0.6316 0.5616 0.5734 -0.0556 0.0117  -0.0532 233 SER A N   
1830 C CA  . SER A 233 ? 0.6937 0.6119 0.6245 -0.0576 0.0118  -0.0519 233 SER A CA  
1831 C C   . SER A 233 ? 0.6967 0.6173 0.6248 -0.0597 0.0159  -0.0500 233 SER A C   
1832 O O   . SER A 233 ? 0.5979 0.5296 0.5324 -0.0595 0.0197  -0.0487 233 SER A O   
1833 C CB  . SER A 233 ? 0.6944 0.6097 0.6247 -0.0581 0.0142  -0.0499 233 SER A CB  
1834 O OG  . SER A 233 ? 0.6917 0.5958 0.6107 -0.0598 0.0153  -0.0485 233 SER A OG  
1835 N N   . GLY A 234 ? 0.7080 0.6174 0.6267 -0.0615 0.0151  -0.0503 234 GLY A N   
1836 C CA  . GLY A 234 ? 0.6204 0.5304 0.5379 -0.0641 0.0194  -0.0492 234 GLY A CA  
1837 C C   . GLY A 234 ? 0.6610 0.5629 0.5717 -0.0666 0.0241  -0.0467 234 GLY A C   
1838 O O   . GLY A 234 ? 0.6518 0.5528 0.5621 -0.0692 0.0283  -0.0463 234 GLY A O   
1839 N N   . TYR A 235 ? 0.6424 0.5389 0.5490 -0.0657 0.0237  -0.0455 235 TYR A N   
1840 C CA  . TYR A 235 ? 0.6947 0.5808 0.5922 -0.0675 0.0275  -0.0436 235 TYR A CA  
1841 C C   . TYR A 235 ? 0.6744 0.5697 0.5785 -0.0683 0.0326  -0.0416 235 TYR A C   
1842 O O   . TYR A 235 ? 0.6831 0.5877 0.5951 -0.0665 0.0318  -0.0413 235 TYR A O   
1843 C CB  . TYR A 235 ? 0.7337 0.6065 0.6210 -0.0652 0.0230  -0.0442 235 TYR A CB  
1844 C CG  . TYR A 235 ? 0.7645 0.6219 0.6375 -0.0664 0.0264  -0.0424 235 TYR A CG  
1845 C CD1 . TYR A 235 ? 0.7144 0.5712 0.5859 -0.0669 0.0302  -0.0407 235 TYR A CD1 
1846 C CD2 . TYR A 235 ? 0.6978 0.5403 0.5580 -0.0669 0.0262  -0.0424 235 TYR A CD2 
1847 C CE1 . TYR A 235 ? 0.7436 0.5859 0.6011 -0.0676 0.0340  -0.0392 235 TYR A CE1 
1848 C CE2 . TYR A 235 ? 0.7388 0.5657 0.5842 -0.0677 0.0305  -0.0405 235 TYR A CE2 
1849 C CZ  . TYR A 235 ? 0.7960 0.6231 0.6401 -0.0680 0.0345  -0.0389 235 TYR A CZ  
1850 O OH  . TYR A 235 ? 0.7669 0.5780 0.5954 -0.0685 0.0394  -0.0370 235 TYR A OH  
1851 N N   . GLY A 236 ? 0.6036 0.4957 0.5048 -0.0710 0.0383  -0.0404 236 GLY A N   
1852 C CA  . GLY A 236 ? 0.6645 0.5624 0.5698 -0.0719 0.0432  -0.0388 236 GLY A CA  
1853 C C   . GLY A 236 ? 0.6491 0.5605 0.5648 -0.0698 0.0426  -0.0382 236 GLY A C   
1854 O O   . GLY A 236 ? 0.6739 0.5965 0.5978 -0.0688 0.0424  -0.0389 236 GLY A O   
1855 N N   . GLY A 237 ? 0.6189 0.5283 0.5335 -0.0687 0.0424  -0.0369 237 GLY A N   
1856 C CA  . GLY A 237 ? 0.6221 0.5425 0.5460 -0.0670 0.0434  -0.0357 237 GLY A CA  
1857 C C   . GLY A 237 ? 0.6375 0.5662 0.5685 -0.0647 0.0405  -0.0363 237 GLY A C   
1858 O O   . GLY A 237 ? 0.6505 0.5891 0.5886 -0.0631 0.0425  -0.0351 237 GLY A O   
1859 N N   . ASN A 238 ? 0.6327 0.5567 0.5612 -0.0642 0.0361  -0.0383 238 ASN A N   
1860 C CA  . ASN A 238 ? 0.6356 0.5672 0.5711 -0.0620 0.0337  -0.0393 238 ASN A CA  
1861 C C   . ASN A 238 ? 0.6539 0.5941 0.5924 -0.0615 0.0346  -0.0398 238 ASN A C   
1862 O O   . ASN A 238 ? 0.6368 0.5859 0.5813 -0.0591 0.0349  -0.0397 238 ASN A O   
1863 C CB  . ASN A 238 ? 0.6078 0.5318 0.5403 -0.0612 0.0279  -0.0421 238 ASN A CB  
1864 C CG  . ASN A 238 ? 0.6606 0.5757 0.5901 -0.0607 0.0255  -0.0428 238 ASN A CG  
1865 O OD1 . ASN A 238 ? 0.7136 0.6313 0.6475 -0.0605 0.0279  -0.0414 238 ASN A OD1 
1866 N ND2 . ASN A 238 ? 0.7245 0.6284 0.6462 -0.0600 0.0202  -0.0453 238 ASN A ND2 
1867 N N   . SER A 239 ? 0.6276 0.5649 0.5623 -0.0634 0.0354  -0.0407 239 SER A N   
1868 C CA  . SER A 239 ? 0.5387 0.4831 0.4769 -0.0628 0.0350  -0.0424 239 SER A CA  
1869 C C   . SER A 239 ? 0.5872 0.5375 0.5288 -0.0633 0.0387  -0.0425 239 SER A C   
1870 O O   . SER A 239 ? 0.5407 0.5002 0.4872 -0.0609 0.0382  -0.0439 239 SER A O   
1871 C CB  . SER A 239 ? 0.5627 0.4992 0.4963 -0.0645 0.0321  -0.0448 239 SER A CB  
1872 O OG  . SER A 239 ? 0.6111 0.5372 0.5382 -0.0678 0.0347  -0.0442 239 SER A OG  
1873 N N   . LEU A 240 ? 0.6112 0.5562 0.5501 -0.0659 0.0422  -0.0415 240 LEU A N   
1874 C CA  . LEU A 240 ? 0.5968 0.5481 0.5406 -0.0662 0.0457  -0.0421 240 LEU A CA  
1875 C C   . LEU A 240 ? 0.5402 0.4982 0.4867 -0.0632 0.0468  -0.0397 240 LEU A C   
1876 O O   . LEU A 240 ? 0.5793 0.5340 0.5241 -0.0642 0.0492  -0.0377 240 LEU A O   
1877 C CB  . LEU A 240 ? 0.6108 0.5538 0.5514 -0.0702 0.0497  -0.0421 240 LEU A CB  
1878 C CG  . LEU A 240 ? 0.5671 0.4989 0.5017 -0.0733 0.0498  -0.0433 240 LEU A CG  
1879 C CD1 . LEU A 240 ? 0.6358 0.5593 0.5670 -0.0771 0.0556  -0.0430 240 LEU A CD1 
1880 C CD2 . LEU A 240 ? 0.4969 0.4338 0.4373 -0.0731 0.0475  -0.0465 240 LEU A CD2 
1881 N N   . LEU A 241 ? 0.5304 0.4972 0.4805 -0.0593 0.0452  -0.0399 241 LEU A N   
1882 C CA  . LEU A 241 ? 0.6079 0.5790 0.5590 -0.0561 0.0465  -0.0369 241 LEU A CA  
1883 C C   . LEU A 241 ? 0.5183 0.4929 0.4713 -0.0551 0.0494  -0.0361 241 LEU A C   
1884 O O   . LEU A 241 ? 0.5660 0.5416 0.5189 -0.0531 0.0512  -0.0331 241 LEU A O   
1885 C CB  . LEU A 241 ? 0.4828 0.4607 0.4351 -0.0516 0.0449  -0.0371 241 LEU A CB  
1886 C CG  . LEU A 241 ? 0.5414 0.5167 0.4931 -0.0522 0.0422  -0.0380 241 LEU A CG  
1887 C CD1 . LEU A 241 ? 0.4426 0.4245 0.3953 -0.0475 0.0419  -0.0376 241 LEU A CD1 
1888 C CD2 . LEU A 241 ? 0.5362 0.5038 0.4866 -0.0548 0.0424  -0.0364 241 LEU A CD2 
1889 N N   . GLY A 242 ? 0.6002 0.5763 0.5557 -0.0564 0.0499  -0.0391 242 GLY A N   
1890 C CA  . GLY A 242 ? 0.5723 0.5518 0.5305 -0.0553 0.0521  -0.0391 242 GLY A CA  
1891 C C   . GLY A 242 ? 0.5462 0.5191 0.5024 -0.0587 0.0553  -0.0370 242 GLY A C   
1892 O O   . GLY A 242 ? 0.6549 0.6301 0.6126 -0.0572 0.0570  -0.0360 242 GLY A O   
1893 N N   . LYS A 243 ? 0.5536 0.5177 0.5054 -0.0625 0.0556  -0.0365 243 LYS A N   
1894 C CA  . LYS A 243 ? 0.6238 0.5804 0.5722 -0.0654 0.0584  -0.0352 243 LYS A CA  
1895 C C   . LYS A 243 ? 0.5811 0.5365 0.5284 -0.0637 0.0583  -0.0320 243 LYS A C   
1896 O O   . LYS A 243 ? 0.6541 0.6131 0.6041 -0.0621 0.0601  -0.0308 243 LYS A O   
1897 C CB  . LYS A 243 ? 0.6176 0.5635 0.5593 -0.0689 0.0584  -0.0359 243 LYS A CB  
1898 C CG  . LYS A 243 ? 0.6762 0.6129 0.6122 -0.0714 0.0616  -0.0351 243 LYS A CG  
1899 C CD  . LYS A 243 ? 0.5908 0.5160 0.5188 -0.0744 0.0626  -0.0359 243 LYS A CD  
1900 C CE  . LYS A 243 ? 0.6058 0.5208 0.5261 -0.0761 0.0664  -0.0351 243 LYS A CE  
1901 N NZ  . LYS A 243 ? 0.5627 0.4837 0.4894 -0.0771 0.0712  -0.0359 243 LYS A NZ  
1902 N N   . LYS A 244 ? 0.5937 0.5436 0.5378 -0.0639 0.0561  -0.0309 244 LYS A N   
1903 C CA  . LYS A 244 ? 0.4758 0.4242 0.4211 -0.0626 0.0560  -0.0286 244 LYS A CA  
1904 C C   . LYS A 244 ? 0.5409 0.4968 0.4913 -0.0592 0.0562  -0.0268 244 LYS A C   
1905 O O   . LYS A 244 ? 0.4967 0.4552 0.4499 -0.0575 0.0584  -0.0246 244 LYS A O   
1906 C CB  . LYS A 244 ? 0.5426 0.4821 0.4838 -0.0637 0.0530  -0.0293 244 LYS A CB  
1907 C CG  . LYS A 244 ? 0.5861 0.5154 0.5190 -0.0662 0.0531  -0.0306 244 LYS A CG  
1908 C CD  . LYS A 244 ? 0.5431 0.4708 0.4749 -0.0670 0.0566  -0.0299 244 LYS A CD  
1909 C CE  . LYS A 244 ? 0.5657 0.4812 0.4872 -0.0689 0.0573  -0.0309 244 LYS A CE  
1910 N NZ  . LYS A 244 ? 0.5974 0.5115 0.5180 -0.0695 0.0610  -0.0304 244 LYS A NZ  
1911 N N   . CYS A 245 ? 0.4861 0.4449 0.4372 -0.0581 0.0543  -0.0275 245 CYS A N   
1912 C CA  . CYS A 245 ? 0.5082 0.4729 0.4628 -0.0546 0.0554  -0.0256 245 CYS A CA  
1913 C C   . CYS A 245 ? 0.5091 0.4797 0.4640 -0.0514 0.0578  -0.0241 245 CYS A C   
1914 O O   . CYS A 245 ? 0.5532 0.5248 0.5095 -0.0490 0.0605  -0.0211 245 CYS A O   
1915 C CB  . CYS A 245 ? 0.4770 0.4443 0.4314 -0.0536 0.0529  -0.0273 245 CYS A CB  
1916 S SG  . CYS A 245 ? 0.5707 0.5305 0.5242 -0.0564 0.0489  -0.0298 245 CYS A SG  
1917 N N   . PHE A 246 ? 0.4938 0.4677 0.4476 -0.0510 0.0567  -0.0266 246 PHE A N   
1918 C CA  . PHE A 246 ? 0.5405 0.5200 0.4946 -0.0471 0.0576  -0.0265 246 PHE A CA  
1919 C C   . PHE A 246 ? 0.5705 0.5483 0.5257 -0.0482 0.0596  -0.0258 246 PHE A C   
1920 O O   . PHE A 246 ? 0.5656 0.5439 0.5206 -0.0453 0.0615  -0.0230 246 PHE A O   
1921 C CB  . PHE A 246 ? 0.5189 0.5033 0.4738 -0.0460 0.0548  -0.0308 246 PHE A CB  
1922 C CG  . PHE A 246 ? 0.5596 0.5502 0.5149 -0.0406 0.0541  -0.0320 246 PHE A CG  
1923 C CD1 . PHE A 246 ? 0.5392 0.5297 0.4933 -0.0377 0.0560  -0.0294 246 PHE A CD1 
1924 C CD2 . PHE A 246 ? 0.5970 0.5929 0.5538 -0.0380 0.0507  -0.0364 246 PHE A CD2 
1925 C CE1 . PHE A 246 ? 0.6765 0.6717 0.6297 -0.0318 0.0544  -0.0311 246 PHE A CE1 
1926 C CE2 . PHE A 246 ? 0.6252 0.6265 0.5822 -0.0320 0.0488  -0.0386 246 PHE A CE2 
1927 C CZ  . PHE A 246 ? 0.6993 0.7000 0.6539 -0.0287 0.0505  -0.0359 246 PHE A CZ  
1928 N N   . ALA A 247 ? 0.5758 0.5511 0.5318 -0.0521 0.0596  -0.0284 247 ALA A N   
1929 C CA  . ALA A 247 ? 0.5962 0.5713 0.5539 -0.0528 0.0615  -0.0289 247 ALA A CA  
1930 C C   . ALA A 247 ? 0.5253 0.4956 0.4822 -0.0534 0.0634  -0.0255 247 ALA A C   
1931 O O   . ALA A 247 ? 0.5654 0.5363 0.5238 -0.0527 0.0649  -0.0253 247 ALA A O   
1932 C CB  . ALA A 247 ? 0.5646 0.5371 0.5232 -0.0572 0.0624  -0.0324 247 ALA A CB  
1933 N N   . LEU A 248 ? 0.5796 0.5453 0.5353 -0.0546 0.0630  -0.0235 248 LEU A N   
1934 C CA  . LEU A 248 ? 0.5722 0.5332 0.5289 -0.0553 0.0643  -0.0213 248 LEU A CA  
1935 C C   . LEU A 248 ? 0.5630 0.5250 0.5226 -0.0527 0.0654  -0.0181 248 LEU A C   
1936 O O   . LEU A 248 ? 0.5734 0.5359 0.5350 -0.0506 0.0677  -0.0155 248 LEU A O   
1937 C CB  . LEU A 248 ? 0.5351 0.4884 0.4891 -0.0589 0.0629  -0.0228 248 LEU A CB  
1938 C CG  . LEU A 248 ? 0.6033 0.5529 0.5538 -0.0614 0.0639  -0.0250 248 LEU A CG  
1939 C CD1 . LEU A 248 ? 0.5644 0.5042 0.5093 -0.0637 0.0624  -0.0260 248 LEU A CD1 
1940 C CD2 . LEU A 248 ? 0.4979 0.4497 0.4510 -0.0604 0.0662  -0.0243 248 LEU A CD2 
1941 N N   . ARG A 249 ? 0.5291 0.4909 0.4893 -0.0528 0.0643  -0.0182 249 ARG A N   
1942 C CA  . ARG A 249 ? 0.5692 0.5313 0.5335 -0.0510 0.0665  -0.0154 249 ARG A CA  
1943 C C   . ARG A 249 ? 0.4990 0.4656 0.4615 -0.0464 0.0694  -0.0126 249 ARG A C   
1944 O O   . ARG A 249 ? 0.5815 0.5469 0.5455 -0.0445 0.0728  -0.0093 249 ARG A O   
1945 C CB  . ARG A 249 ? 0.5866 0.5477 0.5529 -0.0522 0.0645  -0.0171 249 ARG A CB  
1946 C CG  . ARG A 249 ? 0.5961 0.5510 0.5626 -0.0555 0.0609  -0.0200 249 ARG A CG  
1947 C CD  . ARG A 249 ? 0.5889 0.5423 0.5599 -0.0560 0.0588  -0.0217 249 ARG A CD  
1948 N NE  . ARG A 249 ? 0.6333 0.5797 0.6015 -0.0581 0.0541  -0.0251 249 ARG A NE  
1949 C CZ  . ARG A 249 ? 0.5954 0.5392 0.5569 -0.0590 0.0508  -0.0274 249 ARG A CZ  
1950 N NH1 . ARG A 249 ? 0.5763 0.5249 0.5354 -0.0585 0.0512  -0.0272 249 ARG A NH1 
1951 N NH2 . ARG A 249 ? 0.6512 0.5866 0.6080 -0.0602 0.0468  -0.0300 249 ARG A NH2 
1952 N N   . ILE A 250 ? 0.5920 0.5628 0.5506 -0.0442 0.0679  -0.0138 250 ILE A N   
1953 C CA  . ILE A 250 ? 0.6020 0.5761 0.5565 -0.0387 0.0697  -0.0117 250 ILE A CA  
1954 C C   . ILE A 250 ? 0.6131 0.5875 0.5659 -0.0367 0.0701  -0.0112 250 ILE A C   
1955 O O   . ILE A 250 ? 0.6007 0.5739 0.5511 -0.0326 0.0730  -0.0077 250 ILE A O   
1956 C CB  . ILE A 250 ? 0.6040 0.5829 0.5549 -0.0363 0.0667  -0.0145 250 ILE A CB  
1957 C CG1 . ILE A 250 ? 0.5274 0.5062 0.4797 -0.0371 0.0670  -0.0145 250 ILE A CG1 
1958 C CG2 . ILE A 250 ? 0.6128 0.5945 0.5577 -0.0295 0.0671  -0.0134 250 ILE A CG2 
1959 C CD1 . ILE A 250 ? 0.5404 0.5173 0.4934 -0.0346 0.0723  -0.0102 250 ILE A CD1 
1960 N N   . ALA A 251 ? 0.6322 0.6075 0.5864 -0.0395 0.0674  -0.0147 251 ALA A N   
1961 C CA  . ALA A 251 ? 0.6238 0.6006 0.5776 -0.0375 0.0672  -0.0155 251 ALA A CA  
1962 C C   . ALA A 251 ? 0.5299 0.5023 0.4854 -0.0377 0.0702  -0.0121 251 ALA A C   
1963 O O   . ALA A 251 ? 0.5542 0.5268 0.5077 -0.0336 0.0710  -0.0106 251 ALA A O   
1964 C CB  . ALA A 251 ? 0.5779 0.5564 0.5343 -0.0412 0.0650  -0.0203 251 ALA A CB  
1965 N N   . SER A 252 ? 0.5601 0.5282 0.5193 -0.0421 0.0712  -0.0113 252 SER A N   
1966 C CA  . SER A 252 ? 0.5659 0.5299 0.5281 -0.0424 0.0736  -0.0087 252 SER A CA  
1967 C C   . SER A 252 ? 0.5990 0.5616 0.5603 -0.0381 0.0775  -0.0039 252 SER A C   
1968 O O   . SER A 252 ? 0.5445 0.5047 0.5060 -0.0361 0.0795  -0.0016 252 SER A O   
1969 C CB  . SER A 252 ? 0.5640 0.5235 0.5308 -0.0470 0.0732  -0.0095 252 SER A CB  
1970 O OG  . SER A 252 ? 0.5226 0.4814 0.4918 -0.0473 0.0740  -0.0085 252 SER A OG  
1971 N N   . ARG A 253 ? 0.5685 0.5317 0.5282 -0.0366 0.0790  -0.0024 253 ARG A N   
1972 C CA  . ARG A 253 ? 0.5945 0.5552 0.5515 -0.0321 0.0839  0.0025  253 ARG A CA  
1973 C C   . ARG A 253 ? 0.6009 0.5626 0.5490 -0.0257 0.0832  0.0034  253 ARG A C   
1974 O O   . ARG A 253 ? 0.6314 0.5888 0.5765 -0.0220 0.0866  0.0074  253 ARG A O   
1975 C CB  . ARG A 253 ? 0.6047 0.5661 0.5619 -0.0319 0.0859  0.0033  253 ARG A CB  
1976 C CG  . ARG A 253 ? 0.7494 0.7085 0.6998 -0.0260 0.0911  0.0079  253 ARG A CG  
1977 C CD  . ARG A 253 ? 0.6598 0.6126 0.6146 -0.0261 0.0983  0.0129  253 ARG A CD  
1978 N NE  . ARG A 253 ? 0.8624 0.8116 0.8100 -0.0208 0.1047  0.0175  253 ARG A NE  
1979 C CZ  . ARG A 253 ? 0.8207 0.7689 0.7728 -0.0220 0.1100  0.0190  253 ARG A CZ  
1980 N NH1 . ARG A 253 ? 0.7863 0.7369 0.7509 -0.0280 0.1090  0.0157  253 ARG A NH1 
1981 N NH2 . ARG A 253 ? 0.9116 0.8558 0.8551 -0.0166 0.1167  0.0235  253 ARG A NH2 
1982 N N   . LEU A 254 ? 0.6358 0.6028 0.5801 -0.0240 0.0786  -0.0005 254 LEU A N   
1983 C CA  . LEU A 254 ? 0.6361 0.6047 0.5730 -0.0173 0.0764  -0.0012 254 LEU A CA  
1984 C C   . LEU A 254 ? 0.6406 0.6081 0.5795 -0.0171 0.0755  -0.0018 254 LEU A C   
1985 O O   . LEU A 254 ? 0.6861 0.6507 0.6191 -0.0111 0.0761  0.0005  254 LEU A O   
1986 C CB  . LEU A 254 ? 0.6746 0.6498 0.6105 -0.0163 0.0710  -0.0068 254 LEU A CB  
1987 C CG  . LEU A 254 ? 0.7309 0.7080 0.6643 -0.0157 0.0708  -0.0071 254 LEU A CG  
1988 C CD1 . LEU A 254 ? 0.7425 0.7261 0.6768 -0.0152 0.0650  -0.0133 254 LEU A CD1 
1989 C CD2 . LEU A 254 ? 0.7226 0.6959 0.6464 -0.0085 0.0743  -0.0025 254 LEU A CD2 
1990 N N   . ALA A 255 ? 0.6266 0.5957 0.5730 -0.0232 0.0739  -0.0049 255 ALA A N   
1991 C CA  . ALA A 255 ? 0.6104 0.5787 0.5594 -0.0233 0.0733  -0.0059 255 ALA A CA  
1992 C C   . ALA A 255 ? 0.6202 0.5819 0.5686 -0.0216 0.0775  -0.0005 255 ALA A C   
1993 O O   . ALA A 255 ? 0.6456 0.6056 0.5914 -0.0175 0.0771  0.0003  255 ALA A O   
1994 C CB  . ALA A 255 ? 0.6063 0.5759 0.5621 -0.0302 0.0721  -0.0097 255 ALA A CB  
1995 N N   . LYS A 256 ? 0.6148 0.5725 0.5664 -0.0248 0.0814  0.0029  256 LYS A N   
1996 C CA  . LYS A 256 ? 0.5927 0.5436 0.5453 -0.0234 0.0863  0.0082  256 LYS A CA  
1997 C C   . LYS A 256 ? 0.6617 0.6091 0.6041 -0.0157 0.0887  0.0123  256 LYS A C   
1998 O O   . LYS A 256 ? 0.7163 0.6584 0.6563 -0.0124 0.0907  0.0154  256 LYS A O   
1999 C CB  . LYS A 256 ? 0.6217 0.5700 0.5813 -0.0278 0.0902  0.0101  256 LYS A CB  
2000 C CG  . LYS A 256 ? 0.6109 0.5520 0.5733 -0.0266 0.0966  0.0156  256 LYS A CG  
2001 C CD  . LYS A 256 ? 0.6430 0.5810 0.6098 -0.0274 0.0962  0.0157  256 LYS A CD  
2002 C CE  . LYS A 256 ? 0.7625 0.6927 0.7329 -0.0263 0.1031  0.0211  256 LYS A CE  
2003 N NZ  . LYS A 256 ? 0.8576 0.7830 0.8165 -0.0197 0.1077  0.0264  256 LYS A NZ  
2004 N N   . GLU A 257 ? 0.6547 0.6040 0.5899 -0.0121 0.0883  0.0123  257 GLU A N   
2005 C CA  . GLU A 257 ? 0.7347 0.6793 0.6575 -0.0036 0.0904  0.0161  257 GLU A CA  
2006 C C   . GLU A 257 ? 0.7334 0.6795 0.6501 0.0023  0.0848  0.0132  257 GLU A C   
2007 O O   . GLU A 257 ? 0.7175 0.6569 0.6252 0.0091  0.0864  0.0168  257 GLU A O   
2008 C CB  . GLU A 257 ? 0.7531 0.6998 0.6695 -0.0009 0.0907  0.0161  257 GLU A CB  
2009 C CG  . GLU A 257 ? 0.7547 0.6999 0.6772 -0.0058 0.0964  0.0187  257 GLU A CG  
2010 C CD  . GLU A 257 ? 0.8425 0.7915 0.7601 -0.0039 0.0955  0.0172  257 GLU A CD  
2011 O OE1 . GLU A 257 ? 0.8318 0.7838 0.7406 0.0018  0.0906  0.0145  257 GLU A OE1 
2012 O OE2 . GLU A 257 ? 0.8650 0.8141 0.7884 -0.0078 0.0994  0.0182  257 GLU A OE2 
2013 N N   . GLU A 258 ? 0.6551 0.6094 0.5770 0.0000  0.0785  0.0064  258 GLU A N   
2014 C CA  . GLU A 258 ? 0.6778 0.6354 0.5961 0.0059  0.0724  0.0018  258 GLU A CA  
2015 C C   . GLU A 258 ? 0.6746 0.6336 0.6005 0.0032  0.0704  -0.0010 258 GLU A C   
2016 O O   . GLU A 258 ? 0.6762 0.6382 0.6011 0.0080  0.0654  -0.0055 258 GLU A O   
2017 C CB  . GLU A 258 ? 0.6635 0.6296 0.5836 0.0058  0.0670  -0.0047 258 GLU A CB  
2018 C CG  . GLU A 258 ? 0.7084 0.6737 0.6206 0.0090  0.0682  -0.0027 258 GLU A CG  
2019 C CD  . GLU A 258 ? 0.8004 0.7742 0.7172 0.0070  0.0634  -0.0091 258 GLU A CD  
2020 O OE1 . GLU A 258 ? 0.7649 0.7447 0.6905 0.0035  0.0595  -0.0151 258 GLU A OE1 
2021 O OE2 . GLU A 258 ? 0.8650 0.8390 0.7767 0.0088  0.0640  -0.0082 258 GLU A OE2 
2022 N N   . GLY A 259 ? 0.6419 0.5989 0.5757 -0.0037 0.0739  0.0008  259 GLY A N   
2023 C CA  . GLY A 259 ? 0.6383 0.5955 0.5782 -0.0056 0.0727  -0.0012 259 GLY A CA  
2024 C C   . GLY A 259 ? 0.6329 0.5974 0.5818 -0.0112 0.0696  -0.0078 259 GLY A C   
2025 O O   . GLY A 259 ? 0.6771 0.6431 0.6300 -0.0110 0.0677  -0.0110 259 GLY A O   
2026 N N   . TRP A 260 ? 0.6440 0.6123 0.5958 -0.0161 0.0693  -0.0101 260 TRP A N   
2027 C CA  . TRP A 260 ? 0.5496 0.5227 0.5087 -0.0219 0.0679  -0.0156 260 TRP A CA  
2028 C C   . TRP A 260 ? 0.5407 0.5109 0.5026 -0.0289 0.0705  -0.0140 260 TRP A C   
2029 O O   . TRP A 260 ? 0.5721 0.5371 0.5331 -0.0295 0.0733  -0.0092 260 TRP A O   
2030 C CB  . TRP A 260 ? 0.6352 0.6153 0.5955 -0.0208 0.0644  -0.0213 260 TRP A CB  
2031 C CG  . TRP A 260 ? 0.6335 0.6143 0.5885 -0.0186 0.0637  -0.0199 260 TRP A CG  
2032 C CD1 . TRP A 260 ? 0.6379 0.6168 0.5847 -0.0114 0.0630  -0.0169 260 TRP A CD1 
2033 C CD2 . TRP A 260 ? 0.5719 0.5550 0.5286 -0.0231 0.0636  -0.0215 260 TRP A CD2 
2034 N NE1 . TRP A 260 ? 0.6079 0.5884 0.5518 -0.0113 0.0627  -0.0168 260 TRP A NE1 
2035 C CE2 . TRP A 260 ? 0.6559 0.6393 0.6063 -0.0185 0.0628  -0.0197 260 TRP A CE2 
2036 C CE3 . TRP A 260 ? 0.5851 0.5691 0.5470 -0.0302 0.0644  -0.0242 260 TRP A CE3 
2037 C CZ2 . TRP A 260 ? 0.6330 0.6185 0.5836 -0.0211 0.0622  -0.0209 260 TRP A CZ2 
2038 C CZ3 . TRP A 260 ? 0.5934 0.5785 0.5547 -0.0326 0.0638  -0.0250 260 TRP A CZ3 
2039 C CH2 . TRP A 260 ? 0.5693 0.5556 0.5256 -0.0282 0.0625  -0.0235 260 TRP A CH2 
2040 N N   . LEU A 261 ? 0.6009 0.5737 0.5664 -0.0340 0.0698  -0.0182 261 LEU A N   
2041 C CA  . LEU A 261 ? 0.5371 0.5060 0.5038 -0.0398 0.0714  -0.0174 261 LEU A CA  
2042 C C   . LEU A 261 ? 0.5538 0.5250 0.5200 -0.0430 0.0704  -0.0205 261 LEU A C   
2043 O O   . LEU A 261 ? 0.5915 0.5670 0.5596 -0.0434 0.0694  -0.0249 261 LEU A O   
2044 C CB  . LEU A 261 ? 0.4934 0.4596 0.4631 -0.0428 0.0723  -0.0190 261 LEU A CB  
2045 C CG  . LEU A 261 ? 0.5208 0.4846 0.4921 -0.0400 0.0730  -0.0168 261 LEU A CG  
2046 C CD1 . LEU A 261 ? 0.4871 0.4495 0.4612 -0.0428 0.0734  -0.0197 261 LEU A CD1 
2047 C CD2 . LEU A 261 ? 0.4857 0.4442 0.4571 -0.0396 0.0746  -0.0116 261 LEU A CD2 
2048 N N   . ALA A 262 ? 0.5504 0.5185 0.5149 -0.0452 0.0706  -0.0185 262 ALA A N   
2049 C CA  . ALA A 262 ? 0.5198 0.4880 0.4831 -0.0487 0.0697  -0.0210 262 ALA A CA  
2050 C C   . ALA A 262 ? 0.5013 0.4627 0.4637 -0.0529 0.0702  -0.0208 262 ALA A C   
2051 O O   . ALA A 262 ? 0.4974 0.4553 0.4603 -0.0530 0.0701  -0.0182 262 ALA A O   
2052 C CB  . ALA A 262 ? 0.4782 0.4485 0.4396 -0.0468 0.0686  -0.0196 262 ALA A CB  
2053 N N   . GLU A 263 ? 0.4916 0.4508 0.4528 -0.0561 0.0708  -0.0238 263 GLU A N   
2054 C CA  . GLU A 263 ? 0.5239 0.4754 0.4823 -0.0588 0.0710  -0.0240 263 GLU A CA  
2055 C C   . GLU A 263 ? 0.5266 0.4732 0.4795 -0.0621 0.0711  -0.0262 263 GLU A C   
2056 O O   . GLU A 263 ? 0.5203 0.4698 0.4732 -0.0632 0.0722  -0.0283 263 GLU A O   
2057 C CB  . GLU A 263 ? 0.5065 0.4572 0.4663 -0.0586 0.0727  -0.0249 263 GLU A CB  
2058 C CG  . GLU A 263 ? 0.4821 0.4356 0.4465 -0.0552 0.0726  -0.0224 263 GLU A CG  
2059 C CD  . GLU A 263 ? 0.4663 0.4158 0.4322 -0.0546 0.0717  -0.0194 263 GLU A CD  
2060 O OE1 . GLU A 263 ? 0.4699 0.4140 0.4337 -0.0568 0.0703  -0.0202 263 GLU A OE1 
2061 O OE2 . GLU A 263 ? 0.5204 0.4716 0.4898 -0.0519 0.0724  -0.0164 263 GLU A OE2 
2062 N N   . HIS A 264 ? 0.4732 0.4115 0.4213 -0.0633 0.0698  -0.0261 264 HIS A N   
2063 C CA  . HIS A 264 ? 0.5425 0.4730 0.4826 -0.0657 0.0697  -0.0277 264 HIS A CA  
2064 C C   . HIS A 264 ? 0.5416 0.4669 0.4768 -0.0672 0.0731  -0.0294 264 HIS A C   
2065 O O   . HIS A 264 ? 0.4471 0.3635 0.3755 -0.0671 0.0725  -0.0298 264 HIS A O   
2066 C CB  . HIS A 264 ? 0.5075 0.4310 0.4441 -0.0650 0.0657  -0.0273 264 HIS A CB  
2067 C CG  . HIS A 264 ? 0.5475 0.4621 0.4745 -0.0664 0.0645  -0.0287 264 HIS A CG  
2068 N ND1 . HIS A 264 ? 0.5139 0.4187 0.4344 -0.0654 0.0607  -0.0297 264 HIS A ND1 
2069 C CD2 . HIS A 264 ? 0.5319 0.4451 0.4545 -0.0684 0.0663  -0.0295 264 HIS A CD2 
2070 C CE1 . HIS A 264 ? 0.5321 0.4291 0.4430 -0.0664 0.0603  -0.0307 264 HIS A CE1 
2071 N NE2 . HIS A 264 ? 0.5730 0.4749 0.4853 -0.0686 0.0640  -0.0303 264 HIS A NE2 
2072 N N   . MET A 265 ? 0.5002 0.4313 0.4394 -0.0682 0.0767  -0.0310 265 MET A N   
2073 C CA  . MET A 265 ? 0.4938 0.4220 0.4312 -0.0695 0.0810  -0.0329 265 MET A CA  
2074 C C   . MET A 265 ? 0.5241 0.4532 0.4622 -0.0725 0.0856  -0.0354 265 MET A C   
2075 O O   . MET A 265 ? 0.5506 0.4878 0.4960 -0.0725 0.0852  -0.0366 265 MET A O   
2076 C CB  . MET A 265 ? 0.4833 0.4189 0.4288 -0.0675 0.0814  -0.0331 265 MET A CB  
2077 C CG  . MET A 265 ? 0.4935 0.4272 0.4393 -0.0650 0.0782  -0.0309 265 MET A CG  
2078 S SD  . MET A 265 ? 0.5321 0.4736 0.4869 -0.0624 0.0788  -0.0310 265 MET A SD  
2079 C CE  . MET A 265 ? 0.4654 0.4022 0.4206 -0.0603 0.0755  -0.0284 265 MET A CE  
2080 N N   . LEU A 266 ? 0.5152 0.4351 0.4457 -0.0746 0.0902  -0.0365 266 LEU A N   
2081 C CA  . LEU A 266 ? 0.4984 0.4192 0.4320 -0.0778 0.0967  -0.0394 266 LEU A CA  
2082 C C   . LEU A 266 ? 0.5293 0.4598 0.4744 -0.0772 0.0990  -0.0422 266 LEU A C   
2083 O O   . LEU A 266 ? 0.5067 0.4394 0.4532 -0.0747 0.0969  -0.0414 266 LEU A O   
2084 C CB  . LEU A 266 ? 0.5301 0.4366 0.4506 -0.0800 0.1022  -0.0392 266 LEU A CB  
2085 C CG  . LEU A 266 ? 0.5230 0.4233 0.4370 -0.0787 0.1043  -0.0392 266 LEU A CG  
2086 C CD1 . LEU A 266 ? 0.5889 0.4944 0.5112 -0.0806 0.1114  -0.0425 266 LEU A CD1 
2087 C CD2 . LEU A 266 ? 0.5022 0.3853 0.3975 -0.0783 0.1056  -0.0377 266 LEU A CD2 
2088 N N   . ILE A 267 ? 0.5212 0.4575 0.4756 -0.0795 0.1033  -0.0459 267 ILE A N   
2089 C CA  . ILE A 267 ? 0.5322 0.4770 0.4982 -0.0792 0.1061  -0.0500 267 ILE A CA  
2090 C C   . ILE A 267 ? 0.5607 0.5010 0.5282 -0.0835 0.1152  -0.0533 267 ILE A C   
2091 O O   . ILE A 267 ? 0.5766 0.5149 0.5453 -0.0865 0.1183  -0.0545 267 ILE A O   
2092 C CB  . ILE A 267 ? 0.5298 0.4883 0.5095 -0.0767 0.1016  -0.0528 267 ILE A CB  
2093 C CG1 . ILE A 267 ? 0.5584 0.5195 0.5349 -0.0725 0.0940  -0.0487 267 ILE A CG1 
2094 C CG2 . ILE A 267 ? 0.5130 0.4800 0.5047 -0.0755 0.1033  -0.0575 267 ILE A CG2 
2095 C CD1 . ILE A 267 ? 0.5210 0.4929 0.5067 -0.0693 0.0894  -0.0507 267 ILE A CD1 
2096 N N   . LEU A 268 ? 0.5282 0.4666 0.4957 -0.0839 0.1200  -0.0549 268 LEU A N   
2097 C CA  . LEU A 268 ? 0.5726 0.5070 0.5426 -0.0880 0.1301  -0.0584 268 LEU A CA  
2098 C C   . LEU A 268 ? 0.5941 0.5379 0.5775 -0.0874 0.1327  -0.0633 268 LEU A C   
2099 O O   . LEU A 268 ? 0.5557 0.5032 0.5393 -0.0838 0.1279  -0.0626 268 LEU A O   
2100 C CB  . LEU A 268 ? 0.5802 0.4973 0.5309 -0.0894 0.1357  -0.0549 268 LEU A CB  
2101 C CG  . LEU A 268 ? 0.5956 0.5066 0.5351 -0.0862 0.1337  -0.0526 268 LEU A CG  
2102 C CD1 . LEU A 268 ? 0.5698 0.4854 0.5174 -0.0864 0.1391  -0.0565 268 LEU A CD1 
2103 C CD2 . LEU A 268 ? 0.6127 0.5054 0.5306 -0.0863 0.1363  -0.0489 268 LEU A CD2 
2104 N N   . GLY A 269 ? 0.5816 0.5291 0.5775 -0.0909 0.1403  -0.0688 269 GLY A N   
2105 C CA  . GLY A 269 ? 0.5435 0.4983 0.5524 -0.0910 0.1447  -0.0745 269 GLY A CA  
2106 C C   . GLY A 269 ? 0.5661 0.5091 0.5665 -0.0946 0.1564  -0.0744 269 GLY A C   
2107 O O   . GLY A 269 ? 0.6420 0.5746 0.6350 -0.0984 0.1637  -0.0729 269 GLY A O   
2108 N N   . ILE A 270 ? 0.5542 0.4979 0.5546 -0.0929 0.1582  -0.0759 270 ILE A N   
2109 C CA  . ILE A 270 ? 0.5673 0.4995 0.5582 -0.0953 0.1694  -0.0759 270 ILE A CA  
2110 C C   . ILE A 270 ? 0.5738 0.5162 0.5829 -0.0961 0.1748  -0.0832 270 ILE A C   
2111 O O   . ILE A 270 ? 0.5575 0.5104 0.5754 -0.0923 0.1676  -0.0856 270 ILE A O   
2112 C CB  . ILE A 270 ? 0.6483 0.5683 0.6170 -0.0919 0.1662  -0.0701 270 ILE A CB  
2113 C CG1 . ILE A 270 ? 0.5569 0.4643 0.5141 -0.0936 0.1779  -0.0705 270 ILE A CG1 
2114 C CG2 . ILE A 270 ? 0.6397 0.5692 0.6135 -0.0871 0.1561  -0.0703 270 ILE A CG2 
2115 C CD1 . ILE A 270 ? 0.6258 0.5173 0.5576 -0.0902 0.1755  -0.0650 270 ILE A CD1 
2116 N N   . THR A 271 ? 0.5980 0.5367 0.6127 -0.1009 0.1878  -0.0870 271 THR A N   
2117 C CA  . THR A 271 ? 0.5934 0.5411 0.6269 -0.1023 0.1950  -0.0948 271 THR A CA  
2118 C C   . THR A 271 ? 0.6061 0.5406 0.6253 -0.1035 0.2064  -0.0934 271 THR A C   
2119 O O   . THR A 271 ? 0.5845 0.5028 0.5860 -0.1060 0.2148  -0.0889 271 THR A O   
2120 C CB  . THR A 271 ? 0.5756 0.5310 0.6315 -0.1072 0.2020  -0.1017 271 THR A CB  
2121 O OG1 . THR A 271 ? 0.6461 0.6123 0.7127 -0.1054 0.1908  -0.1028 271 THR A OG1 
2122 C CG2 . THR A 271 ? 0.5616 0.5284 0.6406 -0.1083 0.2082  -0.1112 271 THR A CG2 
2123 N N   . ASN A 272 ? 0.5651 0.5057 0.5907 -0.1012 0.2065  -0.0973 272 ASN A N   
2124 C CA  . ASN A 272 ? 0.5986 0.5266 0.6092 -0.1013 0.2166  -0.0961 272 ASN A CA  
2125 C C   . ASN A 272 ? 0.6230 0.5533 0.6496 -0.1063 0.2322  -0.1032 272 ASN A C   
2126 O O   . ASN A 272 ? 0.6263 0.5691 0.6777 -0.1094 0.2339  -0.1097 272 ASN A O   
2127 C CB  . ASN A 272 ? 0.6124 0.5437 0.6184 -0.0958 0.2083  -0.0958 272 ASN A CB  
2128 C CG  . ASN A 272 ? 0.5330 0.4818 0.5643 -0.0948 0.2065  -0.1043 272 ASN A CG  
2129 O OD1 . ASN A 272 ? 0.6111 0.5712 0.6650 -0.0977 0.2096  -0.1109 272 ASN A OD1 
2130 N ND2 . ASN A 272 ? 0.6161 0.5670 0.6442 -0.0903 0.2009  -0.1046 272 ASN A ND2 
2131 N N   . PRO A 273 ? 0.6720 0.5902 0.6855 -0.1069 0.2439  -0.1026 273 PRO A N   
2132 C CA  . PRO A 273 ? 0.6597 0.5791 0.6887 -0.1120 0.2607  -0.1093 273 PRO A CA  
2133 C C   . PRO A 273 ? 0.7111 0.6513 0.7712 -0.1118 0.2585  -0.1195 273 PRO A C   
2134 O O   . PRO A 273 ? 0.7010 0.6465 0.7818 -0.1166 0.2708  -0.1269 273 PRO A O   
2135 C CB  . PRO A 273 ? 0.7042 0.6054 0.7080 -0.1108 0.2714  -0.1055 273 PRO A CB  
2136 C CG  . PRO A 273 ? 0.6627 0.5494 0.6359 -0.1063 0.2619  -0.0961 273 PRO A CG  
2137 C CD  . PRO A 273 ? 0.6081 0.5096 0.5913 -0.1029 0.2432  -0.0958 273 PRO A CD  
2138 N N   . GLU A 274 ? 0.6503 0.6018 0.7150 -0.1063 0.2436  -0.1205 274 GLU A N   
2139 C CA  . GLU A 274 ? 0.6572 0.6277 0.7499 -0.1048 0.2396  -0.1302 274 GLU A CA  
2140 C C   . GLU A 274 ? 0.6596 0.6456 0.7748 -0.1047 0.2298  -0.1349 274 GLU A C   
2141 O O   . GLU A 274 ? 0.6185 0.6203 0.7553 -0.1018 0.2227  -0.1426 274 GLU A O   
2142 C CB  . GLU A 274 ? 0.6270 0.6005 0.7122 -0.0984 0.2289  -0.1290 274 GLU A CB  
2143 C CG  . GLU A 274 ? 0.6488 0.6063 0.7087 -0.0970 0.2354  -0.1239 274 GLU A CG  
2144 C CD  . GLU A 274 ? 0.6861 0.6423 0.7535 -0.0997 0.2512  -0.1303 274 GLU A CD  
2145 O OE1 . GLU A 274 ? 0.7886 0.7582 0.8840 -0.1027 0.2565  -0.1395 274 GLU A OE1 
2146 O OE2 . GLU A 274 ? 0.8362 0.7780 0.8818 -0.0985 0.2583  -0.1265 274 GLU A OE2 
2147 N N   . GLY A 275 ? 0.6141 0.5954 0.7243 -0.1072 0.2289  -0.1306 275 GLY A N   
2148 C CA  . GLY A 275 ? 0.6223 0.6173 0.7524 -0.1067 0.2197  -0.1351 275 GLY A CA  
2149 C C   . GLY A 275 ? 0.6518 0.6533 0.7767 -0.1001 0.2015  -0.1316 275 GLY A C   
2150 O O   . GLY A 275 ? 0.7030 0.7163 0.8439 -0.0983 0.1929  -0.1360 275 GLY A O   
2151 N N   . LYS A 276 ? 0.5511 0.5448 0.6543 -0.0962 0.1957  -0.1242 276 LYS A N   
2152 C CA  . LYS A 276 ? 0.6018 0.5995 0.6984 -0.0903 0.1800  -0.1199 276 LYS A CA  
2153 C C   . LYS A 276 ? 0.5744 0.5624 0.6530 -0.0911 0.1765  -0.1112 276 LYS A C   
2154 O O   . LYS A 276 ? 0.6231 0.5965 0.6835 -0.0940 0.1839  -0.1056 276 LYS A O   
2155 C CB  . LYS A 276 ? 0.6116 0.6061 0.6965 -0.0858 0.1754  -0.1168 276 LYS A CB  
2156 C CG  . LYS A 276 ? 0.6877 0.6872 0.7847 -0.0859 0.1822  -0.1243 276 LYS A CG  
2157 C CD  . LYS A 276 ? 0.6602 0.6771 0.7845 -0.0835 0.1769  -0.1343 276 LYS A CD  
2158 C CE  . LYS A 276 ? 0.5502 0.5725 0.6839 -0.0814 0.1790  -0.1406 276 LYS A CE  
2159 N NZ  . LYS A 276 ? 0.5652 0.5828 0.7022 -0.0867 0.1954  -0.1445 276 LYS A NZ  
2160 N N   . LYS A 277 ? 0.5226 0.5180 0.6057 -0.0880 0.1651  -0.1103 277 LYS A N   
2161 C CA  . LYS A 277 ? 0.5071 0.4955 0.5764 -0.0885 0.1611  -0.1032 277 LYS A CA  
2162 C C   . LYS A 277 ? 0.5498 0.5398 0.6099 -0.0827 0.1479  -0.0978 277 LYS A C   
2163 O O   . LYS A 277 ? 0.5268 0.5279 0.5985 -0.0782 0.1398  -0.1014 277 LYS A O   
2164 C CB  . LYS A 277 ? 0.5367 0.5319 0.6211 -0.0912 0.1617  -0.1076 277 LYS A CB  
2165 C CG  . LYS A 277 ? 0.5046 0.4936 0.5759 -0.0914 0.1569  -0.1009 277 LYS A CG  
2166 C CD  . LYS A 277 ? 0.5133 0.5083 0.6002 -0.0944 0.1586  -0.1059 277 LYS A CD  
2167 C CE  . LYS A 277 ? 0.5743 0.5626 0.6479 -0.0948 0.1543  -0.0993 277 LYS A CE  
2168 N NZ  . LYS A 277 ? 0.5197 0.5113 0.6071 -0.0986 0.1579  -0.1040 277 LYS A NZ  
2169 N N   . LYS A 278 ? 0.5149 0.4933 0.5545 -0.0825 0.1460  -0.0895 278 LYS A N   
2170 C CA  . LYS A 278 ? 0.5428 0.5211 0.5735 -0.0778 0.1350  -0.0838 278 LYS A CA  
2171 C C   . LYS A 278 ? 0.5985 0.5704 0.6182 -0.0791 0.1325  -0.0781 278 LYS A C   
2172 O O   . LYS A 278 ? 0.5443 0.5073 0.5563 -0.0833 0.1394  -0.0767 278 LYS A O   
2173 C CB  . LYS A 278 ? 0.5587 0.5294 0.5764 -0.0755 0.1338  -0.0799 278 LYS A CB  
2174 C CG  . LYS A 278 ? 0.5364 0.5129 0.5640 -0.0739 0.1357  -0.0853 278 LYS A CG  
2175 C CD  . LYS A 278 ? 0.5991 0.5678 0.6139 -0.0714 0.1339  -0.0815 278 LYS A CD  
2176 C CE  . LYS A 278 ? 0.5814 0.5561 0.6062 -0.0694 0.1352  -0.0871 278 LYS A CE  
2177 N NZ  . LYS A 278 ? 0.4973 0.4851 0.5380 -0.0656 0.1277  -0.0908 278 LYS A NZ  
2178 N N   . TYR A 279 ? 0.5155 0.4915 0.5341 -0.0753 0.1229  -0.0750 279 TYR A N   
2179 C CA  . TYR A 279 ? 0.4766 0.4478 0.4858 -0.0758 0.1195  -0.0699 279 TYR A CA  
2180 C C   . TYR A 279 ? 0.5028 0.4658 0.4970 -0.0735 0.1148  -0.0632 279 TYR A C   
2181 O O   . TYR A 279 ? 0.5135 0.4796 0.5090 -0.0696 0.1098  -0.0621 279 TYR A O   
2182 C CB  . TYR A 279 ? 0.4995 0.4812 0.5188 -0.0731 0.1127  -0.0716 279 TYR A CB  
2183 C CG  . TYR A 279 ? 0.5237 0.5118 0.5570 -0.0759 0.1166  -0.0782 279 TYR A CG  
2184 C CD1 . TYR A 279 ? 0.4899 0.4736 0.5202 -0.0796 0.1196  -0.0771 279 TYR A CD1 
2185 C CD2 . TYR A 279 ? 0.4729 0.4716 0.5236 -0.0747 0.1172  -0.0860 279 TYR A CD2 
2186 C CE1 . TYR A 279 ? 0.5106 0.5000 0.5555 -0.0824 0.1234  -0.0835 279 TYR A CE1 
2187 C CE2 . TYR A 279 ? 0.5386 0.5437 0.6048 -0.0773 0.1207  -0.0930 279 TYR A CE2 
2188 C CZ  . TYR A 279 ? 0.5697 0.5701 0.6332 -0.0813 0.1240  -0.0916 279 TYR A CZ  
2189 O OH  . TYR A 279 ? 0.5725 0.5792 0.6531 -0.0841 0.1277  -0.0990 279 TYR A OH  
2190 N N   . LEU A 280 ? 0.5147 0.4668 0.4954 -0.0756 0.1164  -0.0591 280 LEU A N   
2191 C CA  . LEU A 280 ? 0.5253 0.4692 0.4930 -0.0735 0.1118  -0.0537 280 LEU A CA  
2192 C C   . LEU A 280 ? 0.5373 0.4793 0.5000 -0.0735 0.1072  -0.0500 280 LEU A C   
2193 O O   . LEU A 280 ? 0.5518 0.4939 0.5157 -0.0761 0.1095  -0.0509 280 LEU A O   
2194 C CB  . LEU A 280 ? 0.5629 0.4937 0.5168 -0.0750 0.1170  -0.0528 280 LEU A CB  
2195 C CG  . LEU A 280 ? 0.6202 0.5509 0.5767 -0.0753 0.1231  -0.0565 280 LEU A CG  
2196 C CD1 . LEU A 280 ? 0.5895 0.5054 0.5300 -0.0768 0.1297  -0.0556 280 LEU A CD1 
2197 C CD2 . LEU A 280 ? 0.5413 0.4765 0.5017 -0.0713 0.1176  -0.0565 280 LEU A CD2 
2198 N N   . ALA A 281 ? 0.5160 0.4562 0.4742 -0.0706 0.1009  -0.0462 281 ALA A N   
2199 C CA  . ALA A 281 ? 0.5205 0.4575 0.4731 -0.0704 0.0967  -0.0426 281 ALA A CA  
2200 C C   . ALA A 281 ? 0.4882 0.4138 0.4286 -0.0697 0.0948  -0.0400 281 ALA A C   
2201 O O   . ALA A 281 ? 0.5192 0.4423 0.4582 -0.0679 0.0940  -0.0401 281 ALA A O   
2202 C CB  . ALA A 281 ? 0.4440 0.3899 0.4041 -0.0673 0.0909  -0.0409 281 ALA A CB  
2203 N N   . ALA A 282 ? 0.5026 0.4211 0.4345 -0.0706 0.0935  -0.0383 282 ALA A N   
2204 C CA  . ALA A 282 ? 0.5199 0.4265 0.4397 -0.0694 0.0909  -0.0368 282 ALA A CA  
2205 C C   . ALA A 282 ? 0.5479 0.4535 0.4662 -0.0686 0.0853  -0.0347 282 ALA A C   
2206 O O   . ALA A 282 ? 0.5193 0.4258 0.4373 -0.0704 0.0860  -0.0344 282 ALA A O   
2207 C CB  . ALA A 282 ? 0.5330 0.4273 0.4394 -0.0710 0.0963  -0.0379 282 ALA A CB  
2208 N N   . ALA A 283 ? 0.5089 0.4125 0.4273 -0.0661 0.0800  -0.0336 283 ALA A N   
2209 C CA  . ALA A 283 ? 0.4897 0.3921 0.4081 -0.0651 0.0747  -0.0322 283 ALA A CA  
2210 C C   . ALA A 283 ? 0.4887 0.3778 0.3949 -0.0636 0.0715  -0.0333 283 ALA A C   
2211 O O   . ALA A 283 ? 0.5434 0.4286 0.4490 -0.0612 0.0685  -0.0343 283 ALA A O   
2212 C CB  . ALA A 283 ? 0.4848 0.3950 0.4147 -0.0632 0.0713  -0.0307 283 ALA A CB  
2213 N N   . PHE A 284 ? 0.4975 0.3791 0.3937 -0.0646 0.0718  -0.0334 284 PHE A N   
2214 C CA  . PHE A 284 ? 0.5383 0.4065 0.4216 -0.0623 0.0675  -0.0345 284 PHE A CA  
2215 C C   . PHE A 284 ? 0.5649 0.4341 0.4504 -0.0621 0.0626  -0.0342 284 PHE A C   
2216 O O   . PHE A 284 ? 0.5666 0.4432 0.4578 -0.0645 0.0646  -0.0328 284 PHE A O   
2217 C CB  . PHE A 284 ? 0.5312 0.3864 0.3975 -0.0629 0.0723  -0.0349 284 PHE A CB  
2218 C CG  . PHE A 284 ? 0.6201 0.4743 0.4841 -0.0636 0.0789  -0.0355 284 PHE A CG  
2219 C CD1 . PHE A 284 ? 0.5841 0.4434 0.4552 -0.0619 0.0775  -0.0364 284 PHE A CD1 
2220 C CD2 . PHE A 284 ? 0.6493 0.4972 0.5044 -0.0661 0.0869  -0.0353 284 PHE A CD2 
2221 C CE1 . PHE A 284 ? 0.5656 0.4243 0.4349 -0.0624 0.0835  -0.0373 284 PHE A CE1 
2222 C CE2 . PHE A 284 ? 0.6239 0.4713 0.4779 -0.0669 0.0937  -0.0362 284 PHE A CE2 
2223 C CZ  . PHE A 284 ? 0.6202 0.4732 0.4811 -0.0649 0.0917  -0.0374 284 PHE A CZ  
2224 N N   . PRO A 285 ? 0.5570 0.4191 0.4390 -0.0590 0.0558  -0.0359 285 PRO A N   
2225 C CA  . PRO A 285 ? 0.5993 0.4609 0.4821 -0.0586 0.0511  -0.0363 285 PRO A CA  
2226 C C   . PRO A 285 ? 0.6769 0.5295 0.5460 -0.0599 0.0533  -0.0357 285 PRO A C   
2227 O O   . PRO A 285 ? 0.6974 0.5414 0.5543 -0.0605 0.0583  -0.0353 285 PRO A O   
2228 C CB  . PRO A 285 ? 0.6201 0.4744 0.5015 -0.0544 0.0431  -0.0396 285 PRO A CB  
2229 C CG  . PRO A 285 ? 0.6045 0.4610 0.4912 -0.0532 0.0436  -0.0403 285 PRO A CG  
2230 C CD  . PRO A 285 ? 0.6294 0.4856 0.5096 -0.0554 0.0513  -0.0384 285 PRO A CD  
2231 N N   . SER A 286 ? 0.6693 0.5234 0.5405 -0.0602 0.0501  -0.0358 286 SER A N   
2232 C CA  . SER A 286 ? 0.6652 0.5106 0.5243 -0.0613 0.0518  -0.0353 286 SER A CA  
2233 C C   . SER A 286 ? 0.7053 0.5317 0.5440 -0.0582 0.0504  -0.0364 286 SER A C   
2234 O O   . SER A 286 ? 0.6840 0.5038 0.5186 -0.0539 0.0440  -0.0389 286 SER A O   
2235 C CB  . SER A 286 ? 0.6974 0.5463 0.5617 -0.0611 0.0467  -0.0359 286 SER A CB  
2236 O OG  . SER A 286 ? 0.7786 0.6434 0.6585 -0.0636 0.0490  -0.0345 286 SER A OG  
2237 N N   . ALA A 287 ? 0.7233 0.5403 0.5492 -0.0601 0.0566  -0.0349 287 ALA A N   
2238 C CA  . ALA A 287 ? 0.7495 0.5460 0.5526 -0.0569 0.0569  -0.0352 287 ALA A CA  
2239 C C   . ALA A 287 ? 0.7205 0.5120 0.5173 -0.0544 0.0585  -0.0360 287 ALA A C   
2240 O O   . ALA A 287 ? 0.8315 0.6067 0.6104 -0.0494 0.0550  -0.0375 287 ALA A O   
2241 C CB  . ALA A 287 ? 0.7906 0.5764 0.5843 -0.0521 0.0471  -0.0375 287 ALA A CB  
2242 N N   . CYS A 288 ? 0.7448 0.5495 0.5555 -0.0572 0.0632  -0.0354 288 CYS A N   
2243 C CA  . CYS A 288 ? 0.6885 0.4900 0.4951 -0.0551 0.0650  -0.0364 288 CYS A CA  
2244 C C   . CYS A 288 ? 0.6887 0.4917 0.4945 -0.0589 0.0762  -0.0348 288 CYS A C   
2245 O O   . CYS A 288 ? 0.6470 0.4490 0.4511 -0.0576 0.0785  -0.0357 288 CYS A O   
2246 C CB  . CYS A 288 ? 0.7585 0.5736 0.5829 -0.0540 0.0595  -0.0379 288 CYS A CB  
2247 S SG  . CYS A 288 ? 0.7905 0.6024 0.6171 -0.0488 0.0466  -0.0414 288 CYS A SG  
2248 N N   . GLY A 289 ? 0.7117 0.5174 0.5202 -0.0635 0.0830  -0.0331 289 GLY A N   
2249 C CA  . GLY A 289 ? 0.6338 0.4376 0.4400 -0.0670 0.0942  -0.0323 289 GLY A CA  
2250 C C   . GLY A 289 ? 0.6391 0.4613 0.4664 -0.0717 0.0994  -0.0327 289 GLY A C   
2251 O O   . GLY A 289 ? 0.6293 0.4516 0.4577 -0.0742 0.1083  -0.0332 289 GLY A O   
2252 N N   . LYS A 290 ? 0.6460 0.4831 0.4897 -0.0727 0.0943  -0.0328 290 LYS A N   
2253 C CA  . LYS A 290 ? 0.6118 0.4655 0.4742 -0.0761 0.0981  -0.0336 290 LYS A CA  
2254 C C   . LYS A 290 ? 0.6254 0.4773 0.4887 -0.0804 0.1069  -0.0342 290 LYS A C   
2255 O O   . LYS A 290 ? 0.6099 0.4676 0.4815 -0.0829 0.1139  -0.0359 290 LYS A O   
2256 C CB  . LYS A 290 ? 0.5705 0.4378 0.4468 -0.0755 0.0911  -0.0334 290 LYS A CB  
2257 C CG  . LYS A 290 ? 0.5556 0.4277 0.4365 -0.0721 0.0845  -0.0331 290 LYS A CG  
2258 C CD  . LYS A 290 ? 0.5506 0.4376 0.4469 -0.0719 0.0806  -0.0326 290 LYS A CD  
2259 C CE  . LYS A 290 ? 0.5723 0.4590 0.4679 -0.0724 0.0773  -0.0320 290 LYS A CE  
2260 N NZ  . LYS A 290 ? 0.5925 0.4671 0.4764 -0.0702 0.0722  -0.0320 290 LYS A NZ  
2261 N N   . THR A 291 ? 0.6655 0.5093 0.5213 -0.0814 0.1066  -0.0331 291 THR A N   
2262 C CA  . THR A 291 ? 0.6802 0.5223 0.5388 -0.0859 0.1151  -0.0338 291 THR A CA  
2263 C C   . THR A 291 ? 0.6347 0.4636 0.4819 -0.0874 0.1256  -0.0337 291 THR A C   
2264 O O   . THR A 291 ? 0.7081 0.5409 0.5649 -0.0915 0.1346  -0.0356 291 THR A O   
2265 C CB  . THR A 291 ? 0.6451 0.4800 0.4971 -0.0863 0.1122  -0.0326 291 THR A CB  
2266 O OG1 . THR A 291 ? 0.6612 0.5106 0.5270 -0.0856 0.1044  -0.0333 291 THR A OG1 
2267 C CG2 . THR A 291 ? 0.6708 0.4999 0.5233 -0.0909 0.1219  -0.0331 291 THR A CG2 
2268 N N   . ASN A 292 ? 0.7051 0.5180 0.5320 -0.0838 0.1248  -0.0320 292 ASN A N   
2269 C CA  . ASN A 292 ? 0.6874 0.4863 0.5009 -0.0844 0.1353  -0.0316 292 ASN A CA  
2270 C C   . ASN A 292 ? 0.6676 0.4780 0.4941 -0.0857 0.1401  -0.0340 292 ASN A C   
2271 O O   . ASN A 292 ? 0.6978 0.5054 0.5259 -0.0890 0.1515  -0.0351 292 ASN A O   
2272 C CB  . ASN A 292 ? 0.7709 0.5500 0.5586 -0.0788 0.1316  -0.0297 292 ASN A CB  
2273 C CG  . ASN A 292 ? 0.8549 0.6147 0.6232 -0.0783 0.1336  -0.0272 292 ASN A CG  
2274 O OD1 . ASN A 292 ? 0.8367 0.5780 0.5861 -0.0778 0.1424  -0.0256 292 ASN A OD1 
2275 N ND2 . ASN A 292 ? 0.8314 0.5945 0.6036 -0.0781 0.1257  -0.0269 292 ASN A ND2 
2276 N N   . LEU A 293 ? 0.6629 0.4859 0.4992 -0.0830 0.1318  -0.0350 293 LEU A N   
2277 C CA  . LEU A 293 ? 0.6530 0.4870 0.5017 -0.0836 0.1353  -0.0375 293 LEU A CA  
2278 C C   . LEU A 293 ? 0.6113 0.4615 0.4825 -0.0881 0.1395  -0.0404 293 LEU A C   
2279 O O   . LEU A 293 ? 0.6170 0.4707 0.4960 -0.0905 0.1480  -0.0431 293 LEU A O   
2280 C CB  . LEU A 293 ? 0.5764 0.4182 0.4294 -0.0794 0.1252  -0.0376 293 LEU A CB  
2281 C CG  . LEU A 293 ? 0.5976 0.4488 0.4609 -0.0790 0.1274  -0.0400 293 LEU A CG  
2282 C CD1 . LEU A 293 ? 0.6724 0.5101 0.5211 -0.0784 0.1356  -0.0405 293 LEU A CD1 
2283 C CD2 . LEU A 293 ? 0.5959 0.4544 0.4644 -0.0751 0.1173  -0.0397 293 LEU A CD2 
2284 N N   . ALA A 294 ? 0.6332 0.4935 0.5155 -0.0888 0.1336  -0.0404 294 ALA A N   
2285 C CA  . ALA A 294 ? 0.5250 0.4013 0.4289 -0.0918 0.1357  -0.0439 294 ALA A CA  
2286 C C   . ALA A 294 ? 0.6452 0.5168 0.5524 -0.0967 0.1468  -0.0460 294 ALA A C   
2287 O O   . ALA A 294 ? 0.6340 0.5174 0.5597 -0.0993 0.1510  -0.0505 294 ALA A O   
2288 C CB  . ALA A 294 ? 0.5863 0.4728 0.4987 -0.0906 0.1265  -0.0435 294 ALA A CB  
2289 N N   . MET A 295 ? 0.6347 0.4888 0.5247 -0.0979 0.1516  -0.0432 295 MET A N   
2290 C CA  . MET A 295 ? 0.6996 0.5463 0.5910 -0.1028 0.1637  -0.0446 295 MET A CA  
2291 C C   . MET A 295 ? 0.6988 0.5283 0.5730 -0.1032 0.1744  -0.0430 295 MET A C   
2292 O O   . MET A 295 ? 0.6903 0.5070 0.5578 -0.1066 0.1851  -0.0423 295 MET A O   
2293 C CB  . MET A 295 ? 0.6443 0.4828 0.5293 -0.1042 0.1624  -0.0424 295 MET A CB  
2294 C CG  . MET A 295 ? 0.6936 0.5476 0.5946 -0.1041 0.1531  -0.0441 295 MET A CG  
2295 S SD  . MET A 295 ? 0.7650 0.6071 0.6573 -0.1059 0.1530  -0.0419 295 MET A SD  
2296 C CE  . MET A 295 ? 0.7303 0.5931 0.6424 -0.1047 0.1414  -0.0446 295 MET A CE  
2297 N N   A MET A 296 ? 0.7204 0.5488 0.5870 -0.0995 0.1721  -0.0425 296 MET A N   
2298 N N   B MET A 296 ? 0.7052 0.5336 0.5717 -0.0995 0.1720  -0.0425 296 MET A N   
2299 C CA  A MET A 296 ? 0.7266 0.5367 0.5724 -0.0983 0.1807  -0.0406 296 MET A CA  
2300 C CA  B MET A 296 ? 0.7261 0.5370 0.5730 -0.0984 0.1809  -0.0408 296 MET A CA  
2301 C C   A MET A 296 ? 0.7370 0.5453 0.5909 -0.1034 0.1964  -0.0434 296 MET A C   
2302 C C   B MET A 296 ? 0.7368 0.5452 0.5914 -0.1038 0.1968  -0.0434 296 MET A C   
2303 O O   A MET A 296 ? 0.7307 0.5561 0.6091 -0.1066 0.1990  -0.0482 296 MET A O   
2304 O O   B MET A 296 ? 0.7438 0.5688 0.6234 -0.1075 0.1997  -0.0482 296 MET A O   
2305 C CB  A MET A 296 ? 0.7256 0.5378 0.5659 -0.0934 0.1746  -0.0408 296 MET A CB  
2306 C CB  B MET A 296 ? 0.7250 0.5401 0.5695 -0.0940 0.1759  -0.0416 296 MET A CB  
2307 C CG  A MET A 296 ? 0.7545 0.5472 0.5711 -0.0907 0.1818  -0.0390 296 MET A CG  
2308 C CG  B MET A 296 ? 0.7464 0.5465 0.5743 -0.0929 0.1860  -0.0412 296 MET A CG  
2309 S SD  A MET A 296 ? 0.7250 0.5230 0.5404 -0.0855 0.1757  -0.0407 296 MET A SD  
2310 S SD  B MET A 296 ? 0.7689 0.5794 0.6031 -0.0893 0.1820  -0.0440 296 MET A SD  
2311 C CE  A MET A 296 ? 0.7417 0.5616 0.5876 -0.0902 0.1819  -0.0461 296 MET A CE  
2312 C CE  B MET A 296 ? 0.6790 0.4923 0.5078 -0.0834 0.1640  -0.0418 296 MET A CE  
2313 N N   . ASN A 297 ? 0.7356 0.5222 0.5682 -0.1039 0.2072  -0.0405 297 ASN A N   
2314 C CA  . ASN A 297 ? 0.7866 0.5678 0.6231 -0.1084 0.2242  -0.0425 297 ASN A CA  
2315 C C   . ASN A 297 ? 0.7309 0.5056 0.5543 -0.1047 0.2276  -0.0425 297 ASN A C   
2316 O O   . ASN A 297 ? 0.8089 0.5624 0.6032 -0.1006 0.2295  -0.0384 297 ASN A O   
2317 C CB  . ASN A 297 ? 0.7874 0.5468 0.6070 -0.1111 0.2355  -0.0389 297 ASN A CB  
2318 C CG  . ASN A 297 ? 0.9034 0.6577 0.7303 -0.1167 0.2548  -0.0412 297 ASN A CG  
2319 O OD1 . ASN A 297 ? 0.9752 0.7466 0.8268 -0.1198 0.2589  -0.0469 297 ASN A OD1 
2320 N ND2 . ASN A 297 ? 0.9616 0.6919 0.7672 -0.1178 0.2670  -0.0370 297 ASN A ND2 
2321 N N   . PRO A 298 ? 0.7310 0.5227 0.5739 -0.1054 0.2278  -0.0472 298 PRO A N   
2322 C CA  . PRO A 298 ? 0.7875 0.5746 0.6185 -0.1011 0.2285  -0.0475 298 PRO A CA  
2323 C C   . PRO A 298 ? 0.8041 0.5709 0.6166 -0.1020 0.2454  -0.0461 298 PRO A C   
2324 O O   . PRO A 298 ? 0.8003 0.5649 0.6220 -0.1078 0.2596  -0.0477 298 PRO A O   
2325 C CB  . PRO A 298 ? 0.7810 0.5919 0.6410 -0.1026 0.2261  -0.0535 298 PRO A CB  
2326 C CG  . PRO A 298 ? 0.8320 0.6550 0.7172 -0.1090 0.2315  -0.0573 298 PRO A CG  
2327 C CD  . PRO A 298 ? 0.7263 0.5416 0.6028 -0.1096 0.2272  -0.0532 298 PRO A CD  
2328 N N   . THR A 299 ? 0.8312 0.5827 0.6175 -0.0959 0.2439  -0.0435 299 THR A N   
2329 C CA  . THR A 299 ? 0.7735 0.5036 0.5375 -0.0951 0.2593  -0.0418 299 THR A CA  
2330 C C   . THR A 299 ? 0.8076 0.5462 0.5838 -0.0963 0.2683  -0.0466 299 THR A C   
2331 O O   . THR A 299 ? 0.9042 0.6277 0.6675 -0.0972 0.2844  -0.0461 299 THR A O   
2332 C CB  . THR A 299 ? 0.7979 0.5055 0.5253 -0.0868 0.2529  -0.0371 299 THR A CB  
2333 O OG1 . THR A 299 ? 0.7899 0.5073 0.5189 -0.0812 0.2392  -0.0392 299 THR A OG1 
2334 C CG2 . THR A 299 ? 0.8081 0.5059 0.5229 -0.0853 0.2443  -0.0329 299 THR A CG2 
2335 N N   . LEU A 300 ? 0.8024 0.5638 0.6021 -0.0961 0.2589  -0.0511 300 LEU A N   
2336 C CA  . LEU A 300 ? 0.8218 0.5928 0.6352 -0.0971 0.2664  -0.0563 300 LEU A CA  
2337 C C   . LEU A 300 ? 0.8027 0.5862 0.6450 -0.1051 0.2789  -0.0614 300 LEU A C   
2338 O O   . LEU A 300 ? 0.7972 0.5967 0.6625 -0.1086 0.2726  -0.0636 300 LEU A O   
2339 C CB  . LEU A 300 ? 0.7467 0.5363 0.5738 -0.0933 0.2512  -0.0594 300 LEU A CB  
2340 C CG  . LEU A 300 ? 0.7682 0.5481 0.5717 -0.0853 0.2390  -0.0562 300 LEU A CG  
2341 C CD1 . LEU A 300 ? 0.7497 0.5494 0.5715 -0.0827 0.2250  -0.0593 300 LEU A CD1 
2342 C CD2 . LEU A 300 ? 0.7905 0.5507 0.5683 -0.0814 0.2490  -0.0554 300 LEU A CD2 
2343 N N   . PRO A 301 ? 0.7722 0.5489 0.6147 -0.1080 0.2965  -0.0638 301 PRO A N   
2344 C CA  . PRO A 301 ? 0.8017 0.5912 0.6750 -0.1157 0.3086  -0.0699 301 PRO A CA  
2345 C C   . PRO A 301 ? 0.7471 0.5646 0.6538 -0.1163 0.2994  -0.0775 301 PRO A C   
2346 O O   . PRO A 301 ? 0.7501 0.5742 0.6553 -0.1115 0.2911  -0.0789 301 PRO A O   
2347 C CB  . PRO A 301 ? 0.7739 0.5478 0.6361 -0.1174 0.3295  -0.0704 301 PRO A CB  
2348 C CG  . PRO A 301 ? 0.8383 0.6011 0.6730 -0.1096 0.3243  -0.0675 301 PRO A CG  
2349 C CD  . PRO A 301 ? 0.8832 0.6401 0.6982 -0.1040 0.3064  -0.0616 301 PRO A CD  
2350 N N   . GLY A 302 ? 0.6875 0.5207 0.6242 -0.1218 0.3006  -0.0827 302 GLY A N   
2351 C CA  . GLY A 302 ? 0.7135 0.5725 0.6817 -0.1218 0.2913  -0.0903 302 GLY A CA  
2352 C C   . GLY A 302 ? 0.7640 0.6347 0.7345 -0.1175 0.2705  -0.0883 302 GLY A C   
2353 O O   . GLY A 302 ? 0.7502 0.6411 0.7445 -0.1165 0.2617  -0.0941 302 GLY A O   
2354 N N   . TRP A 303 ? 0.7663 0.6245 0.7130 -0.1147 0.2628  -0.0806 303 TRP A N   
2355 C CA  . TRP A 303 ? 0.6809 0.5487 0.6290 -0.1110 0.2445  -0.0783 303 TRP A CA  
2356 C C   . TRP A 303 ? 0.7640 0.6328 0.7181 -0.1142 0.2423  -0.0770 303 TRP A C   
2357 O O   . TRP A 303 ? 0.7010 0.5542 0.6427 -0.1173 0.2520  -0.0737 303 TRP A O   
2358 C CB  . TRP A 303 ? 0.6665 0.5213 0.5858 -0.1049 0.2356  -0.0716 303 TRP A CB  
2359 C CG  . TRP A 303 ? 0.6948 0.5531 0.6120 -0.1006 0.2327  -0.0735 303 TRP A CG  
2360 C CD1 . TRP A 303 ? 0.7164 0.5639 0.6215 -0.0997 0.2433  -0.0742 303 TRP A CD1 
2361 C CD2 . TRP A 303 ? 0.6562 0.5291 0.5835 -0.0965 0.2186  -0.0750 303 TRP A CD2 
2362 N NE1 . TRP A 303 ? 0.6735 0.5287 0.5813 -0.0953 0.2360  -0.0764 303 TRP A NE1 
2363 C CE2 . TRP A 303 ? 0.6470 0.5176 0.5686 -0.0934 0.2209  -0.0768 303 TRP A CE2 
2364 C CE3 . TRP A 303 ? 0.5918 0.4787 0.5317 -0.0949 0.2047  -0.0748 303 TRP A CE3 
2365 C CZ2 . TRP A 303 ? 0.6434 0.5253 0.5725 -0.0891 0.2096  -0.0784 303 TRP A CZ2 
2366 C CZ3 . TRP A 303 ? 0.6192 0.5163 0.5653 -0.0906 0.1943  -0.0761 303 TRP A CZ3 
2367 C CH2 . TRP A 303 ? 0.6170 0.5116 0.5582 -0.0879 0.1967  -0.0778 303 TRP A CH2 
2368 N N   . LYS A 304 ? 0.6522 0.5385 0.6245 -0.1132 0.2297  -0.0794 304 LYS A N   
2369 C CA  . LYS A 304 ? 0.6528 0.5428 0.6335 -0.1156 0.2261  -0.0792 304 LYS A CA  
2370 C C   . LYS A 304 ? 0.7155 0.6117 0.6913 -0.1108 0.2089  -0.0755 304 LYS A C   
2371 O O   . LYS A 304 ? 0.6815 0.5913 0.6673 -0.1072 0.1993  -0.0778 304 LYS A O   
2372 C CB  . LYS A 304 ? 0.6264 0.5335 0.6398 -0.1196 0.2297  -0.0880 304 LYS A CB  
2373 C CG  . LYS A 304 ? 0.7642 0.6740 0.7875 -0.1227 0.2281  -0.0888 304 LYS A CG  
2374 C CD  . LYS A 304 ? 0.8151 0.7429 0.8726 -0.1256 0.2303  -0.0989 304 LYS A CD  
2375 C CE  . LYS A 304 ? 0.8528 0.7833 0.9214 -0.1286 0.2289  -0.1005 304 LYS A CE  
2376 N NZ  . LYS A 304 ? 0.8928 0.8067 0.9547 -0.1347 0.2442  -0.0983 304 LYS A NZ  
2377 N N   . VAL A 305 ? 0.7109 0.5966 0.6714 -0.1107 0.2055  -0.0700 305 VAL A N   
2378 C CA  . VAL A 305 ? 0.6858 0.5768 0.6427 -0.1069 0.1906  -0.0666 305 VAL A CA  
2379 C C   . VAL A 305 ? 0.6523 0.5519 0.6246 -0.1095 0.1880  -0.0690 305 VAL A C   
2380 O O   . VAL A 305 ? 0.7052 0.5970 0.6777 -0.1139 0.1968  -0.0692 305 VAL A O   
2381 C CB  . VAL A 305 ? 0.7058 0.5792 0.6342 -0.1039 0.1868  -0.0593 305 VAL A CB  
2382 C CG1 . VAL A 305 ? 0.7226 0.6012 0.6503 -0.1012 0.1734  -0.0565 305 VAL A CG1 
2383 C CG2 . VAL A 305 ? 0.6654 0.5331 0.5805 -0.0998 0.1855  -0.0578 305 VAL A CG2 
2384 N N   . GLU A 306 ? 0.6088 0.5237 0.5935 -0.1065 0.1762  -0.0706 306 GLU A N   
2385 C CA  . GLU A 306 ? 0.6394 0.5637 0.6384 -0.1076 0.1717  -0.0732 306 GLU A CA  
2386 C C   . GLU A 306 ? 0.5883 0.5154 0.5793 -0.1031 0.1583  -0.0688 306 GLU A C   
2387 O O   . GLU A 306 ? 0.5828 0.5134 0.5692 -0.0988 0.1511  -0.0668 306 GLU A O   
2388 C CB  . GLU A 306 ? 0.6116 0.5538 0.6382 -0.1081 0.1716  -0.0819 306 GLU A CB  
2389 C CG  . GLU A 306 ? 0.6315 0.5721 0.6710 -0.1136 0.1858  -0.0876 306 GLU A CG  
2390 C CD  . GLU A 306 ? 0.6438 0.6023 0.7109 -0.1131 0.1851  -0.0971 306 GLU A CD  
2391 O OE1 . GLU A 306 ? 0.6382 0.6028 0.7072 -0.1097 0.1817  -0.0985 306 GLU A OE1 
2392 O OE2 . GLU A 306 ? 0.7385 0.7048 0.8261 -0.1159 0.1875  -0.1038 306 GLU A OE2 
2393 N N   . CYS A 307 ? 0.6130 0.5381 0.6027 -0.1043 0.1557  -0.0674 307 CYS A N   
2394 C CA  . CYS A 307 ? 0.6154 0.5406 0.5955 -0.1006 0.1447  -0.0628 307 CYS A CA  
2395 C C   . CYS A 307 ? 0.6138 0.5557 0.6109 -0.0980 0.1361  -0.0666 307 CYS A C   
2396 O O   . CYS A 307 ? 0.5782 0.5264 0.5896 -0.1002 0.1377  -0.0713 307 CYS A O   
2397 C CB  . CYS A 307 ? 0.6366 0.5479 0.6026 -0.1027 0.1465  -0.0588 307 CYS A CB  
2398 S SG  . CYS A 307 ? 0.6349 0.5466 0.5913 -0.0986 0.1336  -0.0541 307 CYS A SG  
2399 N N   . VAL A 308 ? 0.5850 0.5336 0.5805 -0.0931 0.1273  -0.0647 308 VAL A N   
2400 C CA  . VAL A 308 ? 0.5149 0.4765 0.5208 -0.0893 0.1184  -0.0667 308 VAL A CA  
2401 C C   . VAL A 308 ? 0.5972 0.5547 0.5923 -0.0878 0.1121  -0.0618 308 VAL A C   
2402 O O   . VAL A 308 ? 0.5307 0.4950 0.5329 -0.0866 0.1076  -0.0638 308 VAL A O   
2403 C CB  . VAL A 308 ? 0.5209 0.4912 0.5311 -0.0844 0.1130  -0.0672 308 VAL A CB  
2404 C CG1 . VAL A 308 ? 0.5135 0.4945 0.5302 -0.0795 0.1039  -0.0683 308 VAL A CG1 
2405 C CG2 . VAL A 308 ? 0.5068 0.4824 0.5298 -0.0856 0.1186  -0.0732 308 VAL A CG2 
2406 N N   . GLY A 309 ? 0.5526 0.4990 0.5310 -0.0875 0.1115  -0.0560 309 GLY A N   
2407 C CA  . GLY A 309 ? 0.5216 0.4634 0.4899 -0.0861 0.1058  -0.0517 309 GLY A CA  
2408 C C   . GLY A 309 ? 0.5434 0.4715 0.4945 -0.0861 0.1065  -0.0470 309 GLY A C   
2409 O O   . GLY A 309 ? 0.5726 0.4966 0.5196 -0.0860 0.1097  -0.0466 309 GLY A O   
2410 N N   . ASP A 310 ? 0.5062 0.4272 0.4474 -0.0857 0.1028  -0.0439 310 ASP A N   
2411 C CA  . ASP A 310 ? 0.5026 0.4092 0.4269 -0.0853 0.1026  -0.0404 310 ASP A CA  
2412 C C   . ASP A 310 ? 0.5393 0.4459 0.4589 -0.0818 0.0942  -0.0375 310 ASP A C   
2413 O O   . ASP A 310 ? 0.5690 0.4637 0.4754 -0.0808 0.0924  -0.0355 310 ASP A O   
2414 C CB  . ASP A 310 ? 0.5622 0.4555 0.4763 -0.0883 0.1074  -0.0399 310 ASP A CB  
2415 C CG  . ASP A 310 ? 0.6228 0.5155 0.5353 -0.0879 0.1021  -0.0390 310 ASP A CG  
2416 O OD1 . ASP A 310 ? 0.5388 0.4443 0.4628 -0.0866 0.0971  -0.0401 310 ASP A OD1 
2417 O OD2 . ASP A 310 ? 0.6341 0.5130 0.5332 -0.0886 0.1029  -0.0372 310 ASP A OD2 
2418 N N   . ASP A 311 ? 0.5447 0.4635 0.4744 -0.0795 0.0892  -0.0375 311 ASP A N   
2419 C CA  . ASP A 311 ? 0.5193 0.4375 0.4455 -0.0768 0.0825  -0.0350 311 ASP A CA  
2420 C C   . ASP A 311 ? 0.5308 0.4604 0.4663 -0.0736 0.0789  -0.0342 311 ASP A C   
2421 O O   . ASP A 311 ? 0.5095 0.4375 0.4431 -0.0715 0.0757  -0.0321 311 ASP A O   
2422 C CB  . ASP A 311 ? 0.5304 0.4466 0.4543 -0.0775 0.0800  -0.0349 311 ASP A CB  
2423 C CG  . ASP A 311 ? 0.5447 0.4589 0.4649 -0.0749 0.0738  -0.0330 311 ASP A CG  
2424 O OD1 . ASP A 311 ? 0.5052 0.4107 0.4175 -0.0739 0.0721  -0.0319 311 ASP A OD1 
2425 O OD2 . ASP A 311 ? 0.6455 0.5667 0.5711 -0.0738 0.0704  -0.0329 311 ASP A OD2 
2426 N N   . ILE A 312 ? 0.5225 0.4629 0.4680 -0.0730 0.0793  -0.0360 312 ILE A N   
2427 C CA  . ILE A 312 ? 0.5085 0.4583 0.4604 -0.0692 0.0759  -0.0349 312 ILE A CA  
2428 C C   . ILE A 312 ? 0.4837 0.4413 0.4438 -0.0679 0.0777  -0.0373 312 ILE A C   
2429 O O   . ILE A 312 ? 0.4898 0.4510 0.4555 -0.0694 0.0800  -0.0412 312 ILE A O   
2430 C CB  . ILE A 312 ? 0.5476 0.5026 0.5018 -0.0676 0.0725  -0.0349 312 ILE A CB  
2431 C CG1 . ILE A 312 ? 0.5540 0.5016 0.5011 -0.0685 0.0701  -0.0329 312 ILE A CG1 
2432 C CG2 . ILE A 312 ? 0.5491 0.5123 0.5079 -0.0630 0.0700  -0.0335 312 ILE A CG2 
2433 C CD1 . ILE A 312 ? 0.7050 0.6575 0.6541 -0.0668 0.0668  -0.0329 312 ILE A CD1 
2434 N N   . ALA A 313 ? 0.5178 0.4779 0.4795 -0.0649 0.0764  -0.0355 313 ALA A N   
2435 C CA  . ALA A 313 ? 0.5146 0.4817 0.4833 -0.0627 0.0770  -0.0377 313 ALA A CA  
2436 C C   . ALA A 313 ? 0.5014 0.4740 0.4719 -0.0575 0.0734  -0.0354 313 ALA A C   
2437 O O   . ALA A 313 ? 0.4924 0.4616 0.4591 -0.0563 0.0723  -0.0313 313 ALA A O   
2438 C CB  . ALA A 313 ? 0.4865 0.4495 0.4542 -0.0637 0.0798  -0.0377 313 ALA A CB  
2439 N N   . TRP A 314 ? 0.4846 0.4650 0.4608 -0.0543 0.0718  -0.0385 314 TRP A N   
2440 C CA  . TRP A 314 ? 0.5871 0.5715 0.5632 -0.0483 0.0688  -0.0366 314 TRP A CA  
2441 C C   . TRP A 314 ? 0.5403 0.5277 0.5211 -0.0459 0.0690  -0.0389 314 TRP A C   
2442 O O   . TRP A 314 ? 0.5061 0.4985 0.4939 -0.0463 0.0692  -0.0446 314 TRP A O   
2443 C CB  . TRP A 314 ? 0.5126 0.5028 0.4898 -0.0447 0.0656  -0.0387 314 TRP A CB  
2444 C CG  . TRP A 314 ? 0.4568 0.4445 0.4290 -0.0458 0.0649  -0.0359 314 TRP A CG  
2445 C CD1 . TRP A 314 ? 0.5105 0.4916 0.4784 -0.0495 0.0665  -0.0323 314 TRP A CD1 
2446 C CD2 . TRP A 314 ? 0.5444 0.5361 0.5158 -0.0426 0.0619  -0.0370 314 TRP A CD2 
2447 N NE1 . TRP A 314 ? 0.5055 0.4865 0.4706 -0.0491 0.0649  -0.0312 314 TRP A NE1 
2448 C CE2 . TRP A 314 ? 0.4781 0.4656 0.4450 -0.0450 0.0623  -0.0338 314 TRP A CE2 
2449 C CE3 . TRP A 314 ? 0.5394 0.5380 0.5137 -0.0374 0.0583  -0.0410 314 TRP A CE3 
2450 C CZ2 . TRP A 314 ? 0.5665 0.5565 0.5315 -0.0428 0.0599  -0.0342 314 TRP A CZ2 
2451 C CZ3 . TRP A 314 ? 0.5818 0.5824 0.5534 -0.0349 0.0557  -0.0414 314 TRP A CZ3 
2452 C CH2 . TRP A 314 ? 0.5622 0.5587 0.5293 -0.0378 0.0568  -0.0378 314 TRP A CH2 
2453 N N   . MET A 315 ? 0.5203 0.5046 0.4982 -0.0435 0.0690  -0.0350 315 MET A N   
2454 C CA  . MET A 315 ? 0.5473 0.5330 0.5290 -0.0416 0.0693  -0.0368 315 MET A CA  
2455 C C   . MET A 315 ? 0.5610 0.5472 0.5402 -0.0348 0.0667  -0.0341 315 MET A C   
2456 O O   . MET A 315 ? 0.6019 0.5847 0.5753 -0.0327 0.0666  -0.0289 315 MET A O   
2457 C CB  . MET A 315 ? 0.5364 0.5161 0.5171 -0.0456 0.0723  -0.0351 315 MET A CB  
2458 C CG  . MET A 315 ? 0.5775 0.5539 0.5572 -0.0516 0.0753  -0.0370 315 MET A CG  
2459 S SD  . MET A 315 ? 0.6212 0.5900 0.5982 -0.0549 0.0783  -0.0363 315 MET A SD  
2460 C CE  . MET A 315 ? 0.6475 0.6108 0.6202 -0.0531 0.0761  -0.0302 315 MET A CE  
2461 N N   . LYS A 316 ? 0.6127 0.6027 0.5961 -0.0311 0.0649  -0.0377 316 LYS A N   
2462 C CA  . LYS A 316 ? 0.6006 0.5899 0.5803 -0.0237 0.0622  -0.0356 316 LYS A CA  
2463 C C   . LYS A 316 ? 0.6189 0.6112 0.6047 -0.0214 0.0608  -0.0402 316 LYS A C   
2464 O O   . LYS A 316 ? 0.6013 0.5995 0.5956 -0.0234 0.0605  -0.0470 316 LYS A O   
2465 C CB  . LYS A 316 ? 0.6897 0.6824 0.6658 -0.0178 0.0583  -0.0368 316 LYS A CB  
2466 C CG  . LYS A 316 ? 0.6927 0.6830 0.6622 -0.0088 0.0553  -0.0347 316 LYS A CG  
2467 C CD  . LYS A 316 ? 0.7766 0.7682 0.7394 -0.0025 0.0518  -0.0351 316 LYS A CD  
2468 C CE  . LYS A 316 ? 0.8225 0.8231 0.7936 -0.0019 0.0475  -0.0440 316 LYS A CE  
2469 N NZ  . LYS A 316 ? 0.8395 0.8446 0.8181 0.0018  0.0437  -0.0509 316 LYS A NZ  
2470 N N   . PHE A 317 ? 0.6490 0.6367 0.6312 -0.0176 0.0604  -0.0365 317 PHE A N   
2471 C CA  . PHE A 317 ? 0.6858 0.6760 0.6731 -0.0142 0.0582  -0.0409 317 PHE A CA  
2472 C C   . PHE A 317 ? 0.7007 0.6962 0.6888 -0.0065 0.0525  -0.0460 317 PHE A C   
2473 O O   . PHE A 317 ? 0.6769 0.6698 0.6562 -0.0007 0.0501  -0.0429 317 PHE A O   
2474 C CB  . PHE A 317 ? 0.6966 0.6796 0.6793 -0.0116 0.0590  -0.0353 317 PHE A CB  
2475 C CG  . PHE A 317 ? 0.7119 0.6906 0.6966 -0.0182 0.0633  -0.0326 317 PHE A CG  
2476 C CD1 . PHE A 317 ? 0.6980 0.6792 0.6898 -0.0218 0.0645  -0.0372 317 PHE A CD1 
2477 C CD2 . PHE A 317 ? 0.7153 0.6875 0.6951 -0.0205 0.0661  -0.0258 317 PHE A CD2 
2478 C CE1 . PHE A 317 ? 0.6642 0.6408 0.6564 -0.0269 0.0677  -0.0351 317 PHE A CE1 
2479 C CE2 . PHE A 317 ? 0.6935 0.6616 0.6755 -0.0258 0.0688  -0.0243 317 PHE A CE2 
2480 C CZ  . PHE A 317 ? 0.6947 0.6648 0.6821 -0.0286 0.0694  -0.0289 317 PHE A CZ  
2481 N N   . ASP A 318 ? 0.6882 0.6909 0.6869 -0.0063 0.0504  -0.0545 318 ASP A N   
2482 C CA  . ASP A 318 ? 0.7003 0.7087 0.7020 0.0014  0.0440  -0.0612 318 ASP A CA  
2483 C C   . ASP A 318 ? 0.7613 0.7666 0.7594 0.0095  0.0398  -0.0612 318 ASP A C   
2484 O O   . ASP A 318 ? 0.6860 0.6843 0.6788 0.0090  0.0424  -0.0551 318 ASP A O   
2485 C CB  . ASP A 318 ? 0.7495 0.7678 0.7669 -0.0025 0.0439  -0.0713 318 ASP A CB  
2486 C CG  . ASP A 318 ? 0.6955 0.7162 0.7232 -0.0060 0.0466  -0.0756 318 ASP A CG  
2487 O OD1 . ASP A 318 ? 0.7183 0.7338 0.7412 -0.0044 0.0471  -0.0715 318 ASP A OD1 
2488 O OD2 . ASP A 318 ? 0.6793 0.7071 0.7204 -0.0104 0.0487  -0.0832 318 ASP A OD2 
2489 N N   . ALA A 319 ? 0.7779 0.7880 0.7792 0.0176  0.0328  -0.0685 319 ALA A N   
2490 C CA  . ALA A 319 ? 0.7962 0.8022 0.7924 0.0266  0.0279  -0.0687 319 ALA A CA  
2491 C C   . ALA A 319 ? 0.7825 0.7893 0.7873 0.0231  0.0301  -0.0706 319 ALA A C   
2492 O O   . ALA A 319 ? 0.7757 0.7753 0.7734 0.0274  0.0293  -0.0663 319 ALA A O   
2493 C CB  . ALA A 319 ? 0.7962 0.8079 0.7957 0.0363  0.0188  -0.0781 319 ALA A CB  
2494 N N   . GLN A 320 ? 0.7502 0.7649 0.7699 0.0154  0.0335  -0.0769 320 GLN A N   
2495 C CA  . GLN A 320 ? 0.7405 0.7568 0.7691 0.0123  0.0358  -0.0799 320 GLN A CA  
2496 C C   . GLN A 320 ? 0.7194 0.7284 0.7423 0.0054  0.0426  -0.0715 320 GLN A C   
2497 O O   . GLN A 320 ? 0.7192 0.7285 0.7479 0.0030  0.0447  -0.0733 320 GLN A O   
2498 C CB  . GLN A 320 ? 0.7440 0.7711 0.7907 0.0072  0.0376  -0.0904 320 GLN A CB  
2499 C CG  . GLN A 320 ? 0.7866 0.8222 0.8421 0.0127  0.0311  -0.0999 320 GLN A CG  
2500 C CD  . GLN A 320 ? 0.8389 0.8746 0.8931 0.0244  0.0219  -0.1044 320 GLN A CD  
2501 O OE1 . GLN A 320 ? 0.8493 0.8818 0.9025 0.0269  0.0210  -0.1037 320 GLN A OE1 
2502 N NE2 . GLN A 320 ? 0.8786 0.9172 0.9320 0.0321  0.0144  -0.1093 320 GLN A NE2 
2503 N N   . GLY A 321 ? 0.7428 0.7456 0.7554 0.0025  0.0458  -0.0631 321 GLY A N   
2504 C CA  . GLY A 321 ? 0.7032 0.6992 0.7115 -0.0035 0.0514  -0.0560 321 GLY A CA  
2505 C C   . GLY A 321 ? 0.7190 0.7170 0.7319 -0.0128 0.0571  -0.0570 321 GLY A C   
2506 O O   . GLY A 321 ? 0.6670 0.6593 0.6767 -0.0174 0.0610  -0.0522 321 GLY A O   
2507 N N   . ASN A 322 ? 0.6646 0.6698 0.6849 -0.0154 0.0576  -0.0632 322 ASN A N   
2508 C CA  . ASN A 322 ? 0.6226 0.6281 0.6456 -0.0239 0.0635  -0.0637 322 ASN A CA  
2509 C C   . ASN A 322 ? 0.6643 0.6656 0.6785 -0.0263 0.0645  -0.0577 322 ASN A C   
2510 O O   . ASN A 322 ? 0.6239 0.6264 0.6344 -0.0219 0.0609  -0.0566 322 ASN A O   
2511 C CB  . ASN A 322 ? 0.6667 0.6809 0.7024 -0.0261 0.0646  -0.0730 322 ASN A CB  
2512 C CG  . ASN A 322 ? 0.7191 0.7389 0.7657 -0.0232 0.0631  -0.0804 322 ASN A CG  
2513 O OD1 . ASN A 322 ? 0.7326 0.7512 0.7825 -0.0269 0.0675  -0.0817 322 ASN A OD1 
2514 N ND2 . ASN A 322 ? 0.7666 0.7922 0.8187 -0.0162 0.0566  -0.0859 322 ASN A ND2 
2515 N N   . LEU A 323 ? 0.6699 0.6660 0.6803 -0.0326 0.0692  -0.0542 323 LEU A N   
2516 C CA  . LEU A 323 ? 0.5917 0.5842 0.5952 -0.0355 0.0703  -0.0495 323 LEU A CA  
2517 C C   . LEU A 323 ? 0.5773 0.5745 0.5859 -0.0391 0.0720  -0.0545 323 LEU A C   
2518 O O   . LEU A 323 ? 0.6277 0.6244 0.6397 -0.0444 0.0766  -0.0574 323 LEU A O   
2519 C CB  . LEU A 323 ? 0.5698 0.5542 0.5673 -0.0399 0.0736  -0.0446 323 LEU A CB  
2520 C CG  . LEU A 323 ? 0.6067 0.5866 0.5975 -0.0425 0.0742  -0.0399 323 LEU A CG  
2521 C CD1 . LEU A 323 ? 0.5460 0.5255 0.5328 -0.0378 0.0711  -0.0354 323 LEU A CD1 
2522 C CD2 . LEU A 323 ? 0.5443 0.5164 0.5306 -0.0462 0.0764  -0.0368 323 LEU A CD2 
2523 N N   . ARG A 324 ? 0.5002 0.5014 0.5091 -0.0361 0.0686  -0.0555 324 ARG A N   
2524 C CA  . ARG A 324 ? 0.5914 0.5976 0.6067 -0.0390 0.0696  -0.0607 324 ARG A CA  
2525 C C   . ARG A 324 ? 0.6003 0.6021 0.6081 -0.0423 0.0707  -0.0562 324 ARG A C   
2526 O O   . ARG A 324 ? 0.6043 0.6030 0.6040 -0.0394 0.0683  -0.0507 324 ARG A O   
2527 C CB  . ARG A 324 ? 0.6337 0.6481 0.6562 -0.0328 0.0641  -0.0667 324 ARG A CB  
2528 C CG  . ARG A 324 ? 0.6391 0.6585 0.6708 -0.0294 0.0624  -0.0729 324 ARG A CG  
2529 C CD  . ARG A 324 ? 0.6345 0.6635 0.6792 -0.0262 0.0586  -0.0825 324 ARG A CD  
2530 N NE  . ARG A 324 ? 0.7324 0.7667 0.7894 -0.0254 0.0587  -0.0899 324 ARG A NE  
2531 C CZ  . ARG A 324 ? 0.7072 0.7460 0.7778 -0.0310 0.0640  -0.0966 324 ARG A CZ  
2532 N NH1 . ARG A 324 ? 0.7101 0.7483 0.7834 -0.0378 0.0694  -0.0971 324 ARG A NH1 
2533 N NH2 . ARG A 324 ? 0.8313 0.8749 0.9132 -0.0297 0.0642  -0.1032 324 ARG A NH2 
2534 N N   . ALA A 325 ? 0.5700 0.5709 0.5805 -0.0482 0.0749  -0.0585 325 ALA A N   
2535 C CA  . ALA A 325 ? 0.5541 0.5499 0.5575 -0.0518 0.0762  -0.0548 325 ALA A CA  
2536 C C   . ALA A 325 ? 0.5905 0.5909 0.6010 -0.0539 0.0768  -0.0599 325 ALA A C   
2537 O O   . ALA A 325 ? 0.5401 0.5451 0.5613 -0.0556 0.0792  -0.0664 325 ALA A O   
2538 C CB  . ALA A 325 ? 0.4848 0.4716 0.4814 -0.0571 0.0810  -0.0515 325 ALA A CB  
2539 N N   . ILE A 326 ? 0.5235 0.5225 0.5290 -0.0539 0.0747  -0.0574 326 ILE A N   
2540 C CA  . ILE A 326 ? 0.5358 0.5372 0.5466 -0.0567 0.0755  -0.0614 326 ILE A CA  
2541 C C   . ILE A 326 ? 0.4868 0.4797 0.4878 -0.0608 0.0775  -0.0566 326 ILE A C   
2542 O O   . ILE A 326 ? 0.4985 0.4865 0.4900 -0.0597 0.0759  -0.0507 326 ILE A O   
2543 C CB  . ILE A 326 ? 0.5644 0.5740 0.5803 -0.0510 0.0693  -0.0651 326 ILE A CB  
2544 C CG1 . ILE A 326 ? 0.5784 0.5856 0.5832 -0.0469 0.0652  -0.0589 326 ILE A CG1 
2545 C CG2 . ILE A 326 ? 0.6081 0.6255 0.6334 -0.0459 0.0662  -0.0708 326 ILE A CG2 
2546 C CD1 . ILE A 326 ? 0.7025 0.7158 0.7093 -0.0418 0.0598  -0.0620 326 ILE A CD1 
2547 N N   . ASN A 327 ? 0.5294 0.5204 0.5336 -0.0655 0.0810  -0.0594 327 ASN A N   
2548 C CA  . ASN A 327 ? 0.5492 0.5327 0.5446 -0.0686 0.0816  -0.0558 327 ASN A CA  
2549 C C   . ASN A 327 ? 0.5022 0.4914 0.5001 -0.0656 0.0764  -0.0570 327 ASN A C   
2550 O O   . ASN A 327 ? 0.5845 0.5798 0.5928 -0.0658 0.0761  -0.0629 327 ASN A O   
2551 C CB  . ASN A 327 ? 0.5535 0.5303 0.5494 -0.0747 0.0884  -0.0577 327 ASN A CB  
2552 C CG  . ASN A 327 ? 0.5242 0.4935 0.5122 -0.0772 0.0882  -0.0552 327 ASN A CG  
2553 O OD1 . ASN A 327 ? 0.5388 0.5063 0.5191 -0.0750 0.0836  -0.0512 327 ASN A OD1 
2554 N ND2 . ASN A 327 ? 0.5648 0.5294 0.5552 -0.0819 0.0937  -0.0577 327 ASN A ND2 
2555 N N   . PRO A 328 ? 0.4915 0.4794 0.4813 -0.0626 0.0723  -0.0523 328 PRO A N   
2556 C CA  . PRO A 328 ? 0.5502 0.5435 0.5415 -0.0591 0.0675  -0.0537 328 PRO A CA  
2557 C C   . PRO A 328 ? 0.5557 0.5461 0.5474 -0.0630 0.0683  -0.0553 328 PRO A C   
2558 O O   . PRO A 328 ? 0.5616 0.5572 0.5564 -0.0603 0.0643  -0.0577 328 PRO A O   
2559 C CB  . PRO A 328 ? 0.5293 0.5205 0.5114 -0.0555 0.0648  -0.0476 328 PRO A CB  
2560 C CG  . PRO A 328 ? 0.5044 0.4866 0.4799 -0.0594 0.0682  -0.0434 328 PRO A CG  
2561 C CD  . PRO A 328 ? 0.5156 0.4968 0.4954 -0.0623 0.0723  -0.0461 328 PRO A CD  
2562 N N   . GLU A 329 ? 0.5285 0.5101 0.5164 -0.0686 0.0731  -0.0540 329 GLU A N   
2563 C CA  . GLU A 329 ? 0.5438 0.5203 0.5301 -0.0722 0.0741  -0.0548 329 GLU A CA  
2564 C C   . GLU A 329 ? 0.5227 0.5019 0.5208 -0.0754 0.0778  -0.0610 329 GLU A C   
2565 O O   . GLU A 329 ? 0.5950 0.5791 0.6023 -0.0756 0.0803  -0.0648 329 GLU A O   
2566 C CB  . GLU A 329 ? 0.5770 0.5405 0.5510 -0.0758 0.0772  -0.0501 329 GLU A CB  
2567 C CG  . GLU A 329 ? 0.5367 0.4975 0.5016 -0.0730 0.0733  -0.0450 329 GLU A CG  
2568 C CD  . GLU A 329 ? 0.5818 0.5297 0.5351 -0.0757 0.0743  -0.0419 329 GLU A CD  
2569 O OE1 . GLU A 329 ? 0.5965 0.5367 0.5448 -0.0780 0.0785  -0.0411 329 GLU A OE1 
2570 O OE2 . GLU A 329 ? 0.6173 0.5626 0.5661 -0.0750 0.0707  -0.0405 329 GLU A OE2 
2571 N N   . ASN A 330 ? 0.5105 0.4865 0.5093 -0.0781 0.0781  -0.0623 330 ASN A N   
2572 C CA  . ASN A 330 ? 0.5081 0.4858 0.5194 -0.0816 0.0820  -0.0684 330 ASN A CA  
2573 C C   . ASN A 330 ? 0.5434 0.5076 0.5485 -0.0880 0.0896  -0.0665 330 ASN A C   
2574 O O   . ASN A 330 ? 0.4698 0.4336 0.4854 -0.0919 0.0948  -0.0711 330 ASN A O   
2575 C CB  . ASN A 330 ? 0.5546 0.5403 0.5742 -0.0790 0.0761  -0.0728 330 ASN A CB  
2576 C CG  . ASN A 330 ? 0.5377 0.5295 0.5757 -0.0811 0.0786  -0.0810 330 ASN A CG  
2577 O OD1 . ASN A 330 ? 0.5316 0.5261 0.5789 -0.0828 0.0832  -0.0845 330 ASN A OD1 
2578 N ND2 . ASN A 330 ? 0.5251 0.5195 0.5697 -0.0811 0.0756  -0.0848 330 ASN A ND2 
2579 N N   . GLY A 331 ? 0.5079 0.4605 0.4965 -0.0888 0.0904  -0.0603 331 GLY A N   
2580 C CA  . GLY A 331 ? 0.5173 0.4549 0.4965 -0.0936 0.0971  -0.0581 331 GLY A CA  
2581 C C   . GLY A 331 ? 0.5488 0.4753 0.5104 -0.0929 0.0973  -0.0521 331 GLY A C   
2582 O O   . GLY A 331 ? 0.5474 0.4787 0.5068 -0.0894 0.0932  -0.0502 331 GLY A O   
2583 N N   . PHE A 332 ? 0.5362 0.4468 0.4850 -0.0958 0.1021  -0.0496 332 PHE A N   
2584 C CA  . PHE A 332 ? 0.5852 0.4832 0.5162 -0.0946 0.1019  -0.0448 332 PHE A CA  
2585 C C   . PHE A 332 ? 0.5568 0.4446 0.4751 -0.0935 0.0971  -0.0421 332 PHE A C   
2586 O O   . PHE A 332 ? 0.5999 0.4811 0.5169 -0.0959 0.0994  -0.0428 332 PHE A O   
2587 C CB  . PHE A 332 ? 0.6417 0.5274 0.5651 -0.0977 0.1117  -0.0441 332 PHE A CB  
2588 C CG  . PHE A 332 ? 0.6405 0.5359 0.5781 -0.0993 0.1174  -0.0477 332 PHE A CG  
2589 C CD1 . PHE A 332 ? 0.5547 0.4603 0.4972 -0.0963 0.1137  -0.0480 332 PHE A CD1 
2590 C CD2 . PHE A 332 ? 0.5983 0.4924 0.5451 -0.1039 0.1265  -0.0512 332 PHE A CD2 
2591 C CE1 . PHE A 332 ? 0.6194 0.5339 0.5751 -0.0973 0.1182  -0.0518 332 PHE A CE1 
2592 C CE2 . PHE A 332 ? 0.6309 0.5347 0.5926 -0.1052 0.1314  -0.0554 332 PHE A CE2 
2593 C CZ  . PHE A 332 ? 0.6961 0.6101 0.6618 -0.1017 0.1269  -0.0558 332 PHE A CZ  
2594 N N   . PHE A 333 ? 0.5320 0.4187 0.4422 -0.0898 0.0905  -0.0394 333 PHE A N   
2595 C CA  . PHE A 333 ? 0.5927 0.4703 0.4914 -0.0879 0.0847  -0.0375 333 PHE A CA  
2596 C C   . PHE A 333 ? 0.6365 0.4999 0.5186 -0.0861 0.0845  -0.0348 333 PHE A C   
2597 O O   . PHE A 333 ? 0.5885 0.4540 0.4686 -0.0827 0.0785  -0.0339 333 PHE A O   
2598 C CB  . PHE A 333 ? 0.6139 0.5042 0.5206 -0.0846 0.0764  -0.0379 333 PHE A CB  
2599 C CG  . PHE A 333 ? 0.5846 0.4680 0.4832 -0.0828 0.0702  -0.0370 333 PHE A CG  
2600 C CD1 . PHE A 333 ? 0.6095 0.4886 0.5072 -0.0844 0.0701  -0.0382 333 PHE A CD1 
2601 C CD2 . PHE A 333 ? 0.6440 0.5257 0.5375 -0.0795 0.0644  -0.0357 333 PHE A CD2 
2602 C CE1 . PHE A 333 ? 0.6328 0.5057 0.5234 -0.0825 0.0640  -0.0379 333 PHE A CE1 
2603 C CE2 . PHE A 333 ? 0.6292 0.5052 0.5168 -0.0776 0.0583  -0.0359 333 PHE A CE2 
2604 C CZ  . PHE A 333 ? 0.5807 0.4523 0.4664 -0.0789 0.0579  -0.0369 333 PHE A CZ  
2605 N N   . GLY A 334 ? 0.6651 0.5136 0.5356 -0.0881 0.0915  -0.0339 334 GLY A N   
2606 C CA  . GLY A 334 ? 0.7173 0.5517 0.5711 -0.0860 0.0924  -0.0319 334 GLY A CA  
2607 C C   . GLY A 334 ? 0.7149 0.5306 0.5493 -0.0836 0.0890  -0.0303 334 GLY A C   
2608 O O   . GLY A 334 ? 0.6867 0.4971 0.5186 -0.0849 0.0890  -0.0303 334 GLY A O   
2609 N N   . VAL A 335 ? 0.7011 0.5067 0.5216 -0.0796 0.0855  -0.0294 335 VAL A N   
2610 C CA  . VAL A 335 ? 0.7384 0.5245 0.5383 -0.0760 0.0813  -0.0285 335 VAL A CA  
2611 C C   . VAL A 335 ? 0.7572 0.5247 0.5410 -0.0780 0.0911  -0.0265 335 VAL A C   
2612 O O   . VAL A 335 ? 0.7281 0.4928 0.5099 -0.0800 0.1001  -0.0258 335 VAL A O   
2613 C CB  . VAL A 335 ? 0.7723 0.5528 0.5627 -0.0706 0.0747  -0.0291 335 VAL A CB  
2614 C CG1 . VAL A 335 ? 0.7677 0.5276 0.5363 -0.0656 0.0689  -0.0291 335 VAL A CG1 
2615 C CG2 . VAL A 335 ? 0.8359 0.6348 0.6443 -0.0693 0.0668  -0.0309 335 VAL A CG2 
2616 N N   . ALA A 336 ? 0.7749 0.5291 0.5473 -0.0774 0.0898  -0.0257 336 ALA A N   
2617 C CA  . ALA A 336 ? 0.7779 0.5133 0.5355 -0.0796 0.0999  -0.0233 336 ALA A CA  
2618 C C   . ALA A 336 ? 0.8061 0.5183 0.5362 -0.0747 0.1014  -0.0213 336 ALA A C   
2619 O O   . ALA A 336 ? 0.8111 0.5151 0.5338 -0.0764 0.1122  -0.0198 336 ALA A O   
2620 C CB  . ALA A 336 ? 0.7859 0.5148 0.5411 -0.0805 0.0978  -0.0231 336 ALA A CB  
2621 N N   . PRO A 337 ? 0.8461 0.5470 0.5605 -0.0682 0.0908  -0.0218 337 PRO A N   
2622 C CA  . PRO A 337 ? 0.8408 0.5179 0.5268 -0.0622 0.0910  -0.0205 337 PRO A CA  
2623 C C   . PRO A 337 ? 0.8695 0.5498 0.5556 -0.0618 0.0959  -0.0206 337 PRO A C   
2624 O O   . PRO A 337 ? 0.8800 0.5810 0.5862 -0.0632 0.0927  -0.0227 337 PRO A O   
2625 C CB  . PRO A 337 ? 0.8352 0.5085 0.5142 -0.0550 0.0756  -0.0232 337 PRO A CB  
2626 C CG  . PRO A 337 ? 0.8482 0.5345 0.5443 -0.0580 0.0705  -0.0244 337 PRO A CG  
2627 C CD  . PRO A 337 ? 0.8511 0.5600 0.5732 -0.0655 0.0779  -0.0242 337 PRO A CD  
2628 N N   . GLY A 338 ? 0.8279 0.4868 0.4902 -0.0596 0.1041  -0.0182 338 GLY A N   
2629 C CA  . GLY A 338 ? 0.8657 0.5256 0.5264 -0.0596 0.1108  -0.0182 338 GLY A CA  
2630 C C   . GLY A 338 ? 0.8628 0.5324 0.5388 -0.0676 0.1255  -0.0171 338 GLY A C   
2631 O O   . GLY A 338 ? 0.8943 0.5608 0.5656 -0.0678 0.1335  -0.0167 338 GLY A O   
2632 N N   . THR A 339 ? 0.8366 0.5180 0.5314 -0.0739 0.1289  -0.0172 339 THR A N   
2633 C CA  . THR A 339 ? 0.8789 0.5695 0.5903 -0.0814 0.1424  -0.0173 339 THR A CA  
2634 C C   . THR A 339 ? 0.8850 0.5515 0.5769 -0.0832 0.1561  -0.0139 339 THR A C   
2635 O O   . THR A 339 ? 0.8700 0.5248 0.5540 -0.0837 0.1565  -0.0122 339 THR A O   
2636 C CB  . THR A 339 ? 0.8139 0.5263 0.5533 -0.0866 0.1396  -0.0195 339 THR A CB  
2637 O OG1 . THR A 339 ? 0.8099 0.5414 0.5636 -0.0841 0.1269  -0.0219 339 THR A OG1 
2638 C CG2 . THR A 339 ? 0.8117 0.5365 0.5718 -0.0936 0.1517  -0.0212 339 THR A CG2 
2639 N N   . SER A 340 ? 0.9036 0.5620 0.5875 -0.0840 0.1679  -0.0130 340 SER A N   
2640 C CA  . SER A 340 ? 0.9835 0.6182 0.6486 -0.0857 0.1833  -0.0095 340 SER A CA  
2641 C C   . SER A 340 ? 0.9452 0.5895 0.6279 -0.0925 0.1985  -0.0110 340 SER A C   
2642 O O   . SER A 340 ? 0.9436 0.6119 0.6510 -0.0949 0.1958  -0.0148 340 SER A O   
2643 C CB  . SER A 340 ? 1.0069 0.6136 0.6343 -0.0774 0.1827  -0.0064 340 SER A CB  
2644 O OG  . SER A 340 ? 1.0637 0.6760 0.6892 -0.0737 0.1799  -0.0082 340 SER A OG  
2645 N N   . VAL A 341 ? 0.9751 0.5998 0.6450 -0.0954 0.2150  -0.0082 341 VAL A N   
2646 C CA  . VAL A 341 ? 1.0584 0.6906 0.7454 -0.1020 0.2309  -0.0102 341 VAL A CA  
2647 C C   . VAL A 341 ? 1.0347 0.6677 0.7140 -0.0983 0.2324  -0.0110 341 VAL A C   
2648 O O   . VAL A 341 ? 1.0255 0.6752 0.7270 -0.1027 0.2391  -0.0146 341 VAL A O   
2649 C CB  . VAL A 341 ? 1.1338 0.7433 0.8093 -0.1063 0.2495  -0.0068 341 VAL A CB  
2650 C CG1 . VAL A 341 ? 1.0718 0.6868 0.7626 -0.1124 0.2671  -0.0091 341 VAL A CG1 
2651 C CG2 . VAL A 341 ? 1.0993 0.7125 0.7896 -0.1112 0.2486  -0.0072 341 VAL A CG2 
2652 N N   . LYS A 342 ? 1.0306 0.6457 0.6793 -0.0898 0.2257  -0.0083 342 LYS A N   
2653 C CA  . LYS A 342 ? 1.0722 0.6869 0.7124 -0.0857 0.2266  -0.0094 342 LYS A CA  
2654 C C   . LYS A 342 ? 1.0972 0.7370 0.7565 -0.0834 0.2106  -0.0134 342 LYS A C   
2655 O O   . LYS A 342 ? 1.1574 0.8077 0.8254 -0.0833 0.2127  -0.0159 342 LYS A O   
2656 C CB  . LYS A 342 ? 1.1964 0.7800 0.7947 -0.0767 0.2264  -0.0054 342 LYS A CB  
2657 C CG  . LYS A 342 ? 1.2990 0.8784 0.8828 -0.0683 0.2067  -0.0055 342 LYS A CG  
2658 C CD  . LYS A 342 ? 1.3985 0.9466 0.9404 -0.0585 0.2064  -0.0027 342 LYS A CD  
2659 C CE  . LYS A 342 ? 1.5108 1.0576 1.0419 -0.0495 0.1855  -0.0046 342 LYS A CE  
2660 N NZ  . LYS A 342 ? 1.4487 1.0193 1.0002 -0.0484 0.1751  -0.0093 342 LYS A NZ  
2661 N N   . THR A 343 ? 0.9911 0.6404 0.6576 -0.0816 0.1953  -0.0141 343 THR A N   
2662 C CA  . THR A 343 ? 0.9947 0.6667 0.6794 -0.0796 0.1811  -0.0175 343 THR A CA  
2663 C C   . THR A 343 ? 0.9826 0.6825 0.7034 -0.0868 0.1824  -0.0208 343 THR A C   
2664 O O   . THR A 343 ? 0.8953 0.6113 0.6319 -0.0876 0.1822  -0.0237 343 THR A O   
2665 C CB  . THR A 343 ? 0.9841 0.6538 0.6607 -0.0741 0.1646  -0.0171 343 THR A CB  
2666 O OG1 . THR A 343 ? 0.8814 0.5522 0.5651 -0.0778 0.1640  -0.0161 343 THR A OG1 
2667 C CG2 . THR A 343 ? 1.0257 0.6684 0.6669 -0.0655 0.1611  -0.0151 343 THR A CG2 
2668 N N   . ASN A 344 ? 0.8920 0.5973 0.6257 -0.0914 0.1833  -0.0208 344 ASN A N   
2669 C CA  . ASN A 344 ? 0.7860 0.5170 0.5529 -0.0971 0.1826  -0.0246 344 ASN A CA  
2670 C C   . ASN A 344 ? 0.8566 0.5846 0.6329 -0.1038 0.1950  -0.0249 344 ASN A C   
2671 O O   . ASN A 344 ? 0.8657 0.5988 0.6517 -0.1060 0.1909  -0.0254 344 ASN A O   
2672 C CB  . ASN A 344 ? 0.7837 0.5294 0.5613 -0.0949 0.1668  -0.0255 344 ASN A CB  
2673 C CG  . ASN A 344 ? 0.7689 0.5418 0.5772 -0.0979 0.1633  -0.0295 344 ASN A CG  
2674 O OD1 . ASN A 344 ? 0.7464 0.5281 0.5713 -0.1026 0.1726  -0.0323 344 ASN A OD1 
2675 N ND2 . ASN A 344 ? 0.7983 0.5841 0.6143 -0.0950 0.1501  -0.0301 344 ASN A ND2 
2676 N N   . PRO A 345 ? 0.8723 0.5922 0.6473 -0.1074 0.2107  -0.0251 345 PRO A N   
2677 C CA  . PRO A 345 ? 0.8914 0.6090 0.6788 -0.1144 0.2237  -0.0262 345 PRO A CA  
2678 C C   . PRO A 345 ? 0.8790 0.6231 0.7019 -0.1191 0.2201  -0.0318 345 PRO A C   
2679 O O   . PRO A 345 ? 0.8408 0.5850 0.6747 -0.1236 0.2241  -0.0329 345 PRO A O   
2680 C CB  . PRO A 345 ? 0.9161 0.6229 0.6978 -0.1168 0.2410  -0.0262 345 PRO A CB  
2681 C CG  . PRO A 345 ? 0.8703 0.5852 0.6495 -0.1123 0.2352  -0.0274 345 PRO A CG  
2682 C CD  . PRO A 345 ? 0.9025 0.6153 0.6660 -0.1052 0.2179  -0.0249 345 PRO A CD  
2683 N N   . ASN A 346 ? 0.8187 0.5845 0.6594 -0.1179 0.2123  -0.0355 346 ASN A N   
2684 C CA  . ASN A 346 ? 0.7770 0.5672 0.6493 -0.1209 0.2076  -0.0411 346 ASN A CA  
2685 C C   . ASN A 346 ? 0.8063 0.6017 0.6805 -0.1192 0.1949  -0.0403 346 ASN A C   
2686 O O   . ASN A 346 ? 0.7915 0.5992 0.6869 -0.1225 0.1940  -0.0441 346 ASN A O   
2687 C CB  . ASN A 346 ? 0.7593 0.5691 0.6467 -0.1189 0.2018  -0.0448 346 ASN A CB  
2688 C CG  . ASN A 346 ? 0.8143 0.6259 0.7115 -0.1222 0.2150  -0.0483 346 ASN A CG  
2689 O OD1 . ASN A 346 ? 0.7649 0.5759 0.6757 -0.1278 0.2267  -0.0515 346 ASN A OD1 
2690 N ND2 . ASN A 346 ? 0.7455 0.5593 0.6371 -0.1188 0.2132  -0.0482 346 ASN A ND2 
2691 N N   . ALA A 347 ? 0.7778 0.5641 0.6309 -0.1139 0.1849  -0.0359 347 ALA A N   
2692 C CA  . ALA A 347 ? 0.7092 0.4982 0.5625 -0.1123 0.1740  -0.0350 347 ALA A CA  
2693 C C   . ALA A 347 ? 0.7818 0.5557 0.6288 -0.1157 0.1810  -0.0335 347 ALA A C   
2694 O O   . ALA A 347 ? 0.7716 0.5539 0.6323 -0.1176 0.1768  -0.0356 347 ALA A O   
2695 C CB  . ALA A 347 ? 0.6917 0.4738 0.5250 -0.1058 0.1622  -0.0314 347 ALA A CB  
2696 N N   . ILE A 348 ? 0.8457 0.5962 0.6712 -0.1162 0.1919  -0.0298 348 ILE A N   
2697 C CA  . ILE A 348 ? 0.8348 0.5681 0.6525 -0.1194 0.2000  -0.0277 348 ILE A CA  
2698 C C   . ILE A 348 ? 0.8254 0.5718 0.6725 -0.1265 0.2080  -0.0328 348 ILE A C   
2699 O O   . ILE A 348 ? 0.8097 0.5561 0.6642 -0.1287 0.2064  -0.0336 348 ILE A O   
2700 C CB  . ILE A 348 ? 0.8266 0.5320 0.6159 -0.1185 0.2125  -0.0230 348 ILE A CB  
2701 C CG1 . ILE A 348 ? 0.8788 0.5704 0.6385 -0.1104 0.2027  -0.0189 348 ILE A CG1 
2702 C CG2 . ILE A 348 ? 1.0041 0.6903 0.7858 -0.1223 0.2230  -0.0205 348 ILE A CG2 
2703 C CD1 . ILE A 348 ? 0.9003 0.5876 0.6502 -0.1064 0.1891  -0.0173 348 ILE A CD1 
2704 N N   . LYS A 349 ? 0.8293 0.5874 0.6946 -0.1298 0.2161  -0.0369 349 LYS A N   
2705 C CA  . LYS A 349 ? 0.7783 0.5500 0.6743 -0.1361 0.2232  -0.0431 349 LYS A CA  
2706 C C   . LYS A 349 ? 0.7848 0.5792 0.7030 -0.1352 0.2094  -0.0478 349 LYS A C   
2707 O O   . LYS A 349 ? 0.7352 0.5369 0.6744 -0.1393 0.2120  -0.0524 349 LYS A O   
2708 C CB  . LYS A 349 ? 0.7745 0.5559 0.6864 -0.1388 0.2329  -0.0475 349 LYS A CB  
2709 C CG  . LYS A 349 ? 1.0442 0.8037 0.9358 -0.1401 0.2486  -0.0436 349 LYS A CG  
2710 C CD  . LYS A 349 ? 1.0561 0.8270 0.9670 -0.1432 0.2585  -0.0489 349 LYS A CD  
2711 C CE  . LYS A 349 ? 1.1175 0.8658 1.0082 -0.1446 0.2758  -0.0451 349 LYS A CE  
2712 N NZ  . LYS A 349 ? 1.1634 0.9234 1.0752 -0.1481 0.2865  -0.0510 349 LYS A NZ  
2713 N N   . THR A 350 ? 0.7698 0.5747 0.6835 -0.1295 0.1949  -0.0468 350 THR A N   
2714 C CA  . THR A 350 ? 0.6806 0.5070 0.6140 -0.1279 0.1823  -0.0510 350 THR A CA  
2715 C C   . THR A 350 ? 0.6845 0.5053 0.6115 -0.1269 0.1752  -0.0491 350 THR A C   
2716 O O   . THR A 350 ? 0.6751 0.5095 0.6215 -0.1279 0.1702  -0.0537 350 THR A O   
2717 C CB  . THR A 350 ? 0.7075 0.5466 0.6391 -0.1224 0.1710  -0.0505 350 THR A CB  
2718 O OG1 . THR A 350 ? 0.7641 0.6098 0.7040 -0.1232 0.1771  -0.0530 350 THR A OG1 
2719 C CG2 . THR A 350 ? 0.6572 0.5166 0.6063 -0.1200 0.1587  -0.0542 350 THR A CG2 
2720 N N   . ILE A 351 ? 0.7064 0.5073 0.6064 -0.1245 0.1741  -0.0429 351 ILE A N   
2721 C CA  . ILE A 351 ? 0.6752 0.4718 0.5670 -0.1221 0.1644  -0.0410 351 ILE A CA  
2722 C C   . ILE A 351 ? 0.7482 0.5302 0.6382 -0.1263 0.1725  -0.0404 351 ILE A C   
2723 O O   . ILE A 351 ? 0.7661 0.5396 0.6455 -0.1245 0.1662  -0.0382 351 ILE A O   
2724 C CB  . ILE A 351 ? 0.7026 0.4863 0.5672 -0.1163 0.1568  -0.0355 351 ILE A CB  
2725 C CG1 . ILE A 351 ? 0.7413 0.4994 0.5810 -0.1164 0.1673  -0.0309 351 ILE A CG1 
2726 C CG2 . ILE A 351 ? 0.6393 0.4384 0.5082 -0.1123 0.1484  -0.0363 351 ILE A CG2 
2727 C CD1 . ILE A 351 ? 0.7849 0.5284 0.5971 -0.1099 0.1593  -0.0264 351 ILE A CD1 
2728 N N   . GLN A 352 ? 0.7205 0.4992 0.6218 -0.1321 0.1866  -0.0427 352 GLN A N   
2729 C CA  . GLN A 352 ? 0.8187 0.5814 0.7185 -0.1366 0.1963  -0.0420 352 GLN A CA  
2730 C C   . GLN A 352 ? 0.7658 0.5435 0.6923 -0.1395 0.1924  -0.0480 352 GLN A C   
2731 O O   . GLN A 352 ? 0.7697 0.5356 0.6982 -0.1436 0.1999  -0.0480 352 GLN A O   
2732 C CB  . GLN A 352 ? 0.8070 0.5575 0.7071 -0.1418 0.2150  -0.0416 352 GLN A CB  
2733 C CG  . GLN A 352 ? 0.9412 0.6700 0.8094 -0.1388 0.2208  -0.0349 352 GLN A CG  
2734 C CD  . GLN A 352 ? 1.0616 0.7770 0.9290 -0.1439 0.2407  -0.0343 352 GLN A CD  
2735 O OE1 . GLN A 352 ? 1.1521 0.8771 1.0464 -0.1502 0.2501  -0.0398 352 GLN A OE1 
2736 N NE2 . GLN A 352 ? 1.1920 0.8848 1.0289 -0.1410 0.2472  -0.0281 352 GLN A NE2 
2737 N N   . LYS A 353 ? 0.6843 0.4867 0.6304 -0.1372 0.1809  -0.0532 353 LYS A N   
2738 C CA  . LYS A 353 ? 0.7078 0.5248 0.6782 -0.1387 0.1758  -0.0595 353 LYS A CA  
2739 C C   . LYS A 353 ? 0.6949 0.5333 0.6733 -0.1331 0.1599  -0.0622 353 LYS A C   
2740 O O   . LYS A 353 ? 0.7057 0.5523 0.6802 -0.1296 0.1556  -0.0612 353 LYS A O   
2741 C CB  . LYS A 353 ? 0.7522 0.5780 0.7512 -0.1446 0.1865  -0.0669 353 LYS A CB  
2742 C CG  . LYS A 353 ? 0.7732 0.6191 0.7899 -0.1435 0.1850  -0.0721 353 LYS A CG  
2743 C CD  . LYS A 353 ? 0.8305 0.6861 0.8784 -0.1490 0.1944  -0.0809 353 LYS A CD  
2744 C CE  . LYS A 353 ? 0.8285 0.7046 0.8949 -0.1471 0.1914  -0.0870 353 LYS A CE  
2745 N NZ  . LYS A 353 ? 0.9328 0.8198 1.0326 -0.1520 0.1991  -0.0971 353 LYS A NZ  
2746 N N   . ASN A 354 ? 0.6330 0.4798 0.6224 -0.1321 0.1516  -0.0657 354 ASN A N   
2747 C CA  . ASN A 354 ? 0.5935 0.4606 0.5920 -0.1267 0.1375  -0.0689 354 ASN A CA  
2748 C C   . ASN A 354 ? 0.5691 0.4344 0.5465 -0.1213 0.1294  -0.0629 354 ASN A C   
2749 O O   . ASN A 354 ? 0.5989 0.4796 0.5817 -0.1172 0.1218  -0.0643 354 ASN A O   
2750 C CB  . ASN A 354 ? 0.5643 0.4520 0.5883 -0.1268 0.1373  -0.0764 354 ASN A CB  
2751 C CG  . ASN A 354 ? 0.6352 0.5265 0.6839 -0.1319 0.1445  -0.0839 354 ASN A CG  
2752 O OD1 . ASN A 354 ? 0.6904 0.5781 0.7440 -0.1334 0.1433  -0.0857 354 ASN A OD1 
2753 N ND2 . ASN A 354 ? 0.6596 0.5581 0.7252 -0.1346 0.1521  -0.0889 354 ASN A ND2 
2754 N N   . THR A 355 ? 0.5862 0.4317 0.5395 -0.1209 0.1310  -0.0564 355 THR A N   
2755 C CA  . THR A 355 ? 0.6032 0.4444 0.5366 -0.1161 0.1246  -0.0512 355 THR A CA  
2756 C C   . THR A 355 ? 0.6233 0.4554 0.5420 -0.1131 0.1163  -0.0483 355 THR A C   
2757 O O   . THR A 355 ? 0.6525 0.4700 0.5644 -0.1153 0.1198  -0.0472 355 THR A O   
2758 C CB  . THR A 355 ? 0.6392 0.4638 0.5550 -0.1172 0.1337  -0.0467 355 THR A CB  
2759 O OG1 . THR A 355 ? 0.5887 0.4229 0.5192 -0.1199 0.1412  -0.0498 355 THR A OG1 
2760 C CG2 . THR A 355 ? 0.6066 0.4270 0.5033 -0.1118 0.1260  -0.0422 355 THR A CG2 
2761 N N   . ILE A 356 ? 0.5946 0.4350 0.5088 -0.1080 0.1056  -0.0472 356 ILE A N   
2762 C CA  . ILE A 356 ? 0.6194 0.4531 0.5211 -0.1045 0.0967  -0.0451 356 ILE A CA  
2763 C C   . ILE A 356 ? 0.6198 0.4399 0.4995 -0.1013 0.0950  -0.0404 356 ILE A C   
2764 O O   . ILE A 356 ? 0.6391 0.4664 0.5188 -0.0992 0.0934  -0.0396 356 ILE A O   
2765 C CB  . ILE A 356 ? 0.6352 0.4883 0.5494 -0.1009 0.0861  -0.0481 356 ILE A CB  
2766 C CG1 . ILE A 356 ? 0.6205 0.4867 0.5559 -0.1030 0.0866  -0.0536 356 ILE A CG1 
2767 C CG2 . ILE A 356 ? 0.5888 0.4354 0.4909 -0.0972 0.0772  -0.0463 356 ILE A CG2 
2768 C CD1 . ILE A 356 ? 0.6226 0.5057 0.5678 -0.0988 0.0764  -0.0566 356 ILE A CD1 
2769 N N   . PHE A 357 ? 0.6183 0.4182 0.4792 -0.1005 0.0950  -0.0375 357 PHE A N   
2770 C CA  . PHE A 357 ? 0.6346 0.4196 0.4732 -0.0964 0.0920  -0.0338 357 PHE A CA  
2771 C C   . PHE A 357 ? 0.6715 0.4572 0.5050 -0.0916 0.0797  -0.0343 357 PHE A C   
2772 O O   . PHE A 357 ? 0.6903 0.4776 0.5290 -0.0920 0.0760  -0.0360 357 PHE A O   
2773 C CB  . PHE A 357 ? 0.6542 0.4132 0.4720 -0.0976 0.1006  -0.0304 357 PHE A CB  
2774 C CG  . PHE A 357 ? 0.7157 0.4723 0.5379 -0.1024 0.1141  -0.0299 357 PHE A CG  
2775 C CD1 . PHE A 357 ? 0.6468 0.4066 0.4843 -0.1081 0.1225  -0.0321 357 PHE A CD1 
2776 C CD2 . PHE A 357 ? 0.7445 0.4960 0.5566 -0.1012 0.1185  -0.0279 357 PHE A CD2 
2777 C CE1 . PHE A 357 ? 0.7178 0.4759 0.5614 -0.1127 0.1354  -0.0324 357 PHE A CE1 
2778 C CE2 . PHE A 357 ? 0.7300 0.4795 0.5467 -0.1056 0.1314  -0.0279 357 PHE A CE2 
2779 C CZ  . PHE A 357 ? 0.7246 0.4776 0.5576 -0.1115 0.1401  -0.0302 357 PHE A CZ  
2780 N N   . THR A 358 ? 0.6766 0.4616 0.5015 -0.0872 0.0733  -0.0334 358 THR A N   
2781 C CA  . THR A 358 ? 0.7257 0.5120 0.5474 -0.0825 0.0618  -0.0345 358 THR A CA  
2782 C C   . THR A 358 ? 0.6915 0.4581 0.4905 -0.0779 0.0582  -0.0327 358 THR A C   
2783 O O   . THR A 358 ? 0.7102 0.4754 0.5040 -0.0762 0.0592  -0.0318 358 THR A O   
2784 C CB  . THR A 358 ? 0.6952 0.5037 0.5336 -0.0809 0.0560  -0.0365 358 THR A CB  
2785 O OG1 . THR A 358 ? 0.6315 0.4570 0.4891 -0.0841 0.0588  -0.0385 358 THR A OG1 
2786 C CG2 . THR A 358 ? 0.7033 0.5136 0.5408 -0.0765 0.0451  -0.0383 358 THR A CG2 
2787 N N   . ASN A 359 ? 0.7693 0.5203 0.5547 -0.0754 0.0537  -0.0327 359 ASN A N   
2788 C CA  . ASN A 359 ? 0.8019 0.5343 0.5657 -0.0694 0.0473  -0.0322 359 ASN A CA  
2789 C C   . ASN A 359 ? 0.8072 0.5181 0.5492 -0.0688 0.0551  -0.0288 359 ASN A C   
2790 O O   . ASN A 359 ? 0.8789 0.5767 0.6037 -0.0631 0.0501  -0.0288 359 ASN A O   
2791 C CB  . ASN A 359 ? 0.7871 0.5311 0.5575 -0.0652 0.0380  -0.0348 359 ASN A CB  
2792 C CG  . ASN A 359 ? 0.7588 0.5186 0.5453 -0.0642 0.0294  -0.0382 359 ASN A CG  
2793 O OD1 . ASN A 359 ? 0.7584 0.5150 0.5447 -0.0646 0.0271  -0.0391 359 ASN A OD1 
2794 N ND2 . ASN A 359 ? 0.7818 0.5581 0.5821 -0.0629 0.0250  -0.0402 359 ASN A ND2 
2795 N N   . VAL A 360 ? 0.7892 0.4958 0.5316 -0.0741 0.0675  -0.0263 360 VAL A N   
2796 C CA  . VAL A 360 ? 0.8329 0.5161 0.5525 -0.0735 0.0764  -0.0227 360 VAL A CA  
2797 C C   . VAL A 360 ? 0.8437 0.5039 0.5451 -0.0725 0.0778  -0.0207 360 VAL A C   
2798 O O   . VAL A 360 ? 0.8913 0.5566 0.6022 -0.0739 0.0737  -0.0223 360 VAL A O   
2799 C CB  . VAL A 360 ? 0.8097 0.4992 0.5394 -0.0798 0.0903  -0.0213 360 VAL A CB  
2800 C CG1 . VAL A 360 ? 0.7490 0.4613 0.4967 -0.0804 0.0883  -0.0233 360 VAL A CG1 
2801 C CG2 . VAL A 360 ? 0.7391 0.4352 0.4851 -0.0863 0.0973  -0.0219 360 VAL A CG2 
2802 N N   . ALA A 361 ? 0.9092 0.5430 0.5835 -0.0697 0.0836  -0.0172 361 ALA A N   
2803 C CA  . ALA A 361 ? 0.9238 0.5325 0.5779 -0.0684 0.0860  -0.0146 361 ALA A CA  
2804 C C   . ALA A 361 ? 0.8648 0.4731 0.5296 -0.0766 0.1004  -0.0126 361 ALA A C   
2805 O O   . ALA A 361 ? 0.8229 0.4428 0.5025 -0.0823 0.1108  -0.0125 361 ALA A O   
2806 C CB  . ALA A 361 ? 0.9482 0.5267 0.5671 -0.0617 0.0877  -0.0113 361 ALA A CB  
2807 N N   . GLU A 362 ? 0.8665 0.4610 0.5245 -0.0770 0.1007  -0.0116 362 GLU A N   
2808 C CA  . GLU A 362 ? 0.9239 0.5145 0.5909 -0.0845 0.1141  -0.0100 362 GLU A CA  
2809 C C   . GLU A 362 ? 0.9284 0.4835 0.5641 -0.0827 0.1239  -0.0045 362 GLU A C   
2810 O O   . GLU A 362 ? 0.9734 0.5075 0.5835 -0.0756 0.1160  -0.0030 362 GLU A O   
2811 C CB  . GLU A 362 ? 0.8393 0.4433 0.5265 -0.0872 0.1077  -0.0134 362 GLU A CB  
2812 C CG  . GLU A 362 ? 0.9427 0.5438 0.6425 -0.0950 0.1208  -0.0128 362 GLU A CG  
2813 C CD  . GLU A 362 ? 0.9959 0.6087 0.7139 -0.0967 0.1134  -0.0165 362 GLU A CD  
2814 O OE1 . GLU A 362 ? 0.9516 0.5779 0.6749 -0.0924 0.0988  -0.0197 362 GLU A OE1 
2815 O OE2 . GLU A 362 ? 0.9752 0.5836 0.7029 -0.1024 0.1224  -0.0166 362 GLU A OE2 
2816 N N   . THR A 363 ? 0.9642 0.5120 0.6017 -0.0889 0.1413  -0.0018 363 THR A N   
2817 C CA  . THR A 363 ? 0.9447 0.4582 0.5538 -0.0882 0.1535  0.0039  363 THR A CA  
2818 C C   . THR A 363 ? 0.9824 0.4891 0.5995 -0.0930 0.1579  0.0042  363 THR A C   
2819 O O   . THR A 363 ? 0.9405 0.4710 0.5895 -0.0990 0.1565  -0.0001 363 THR A O   
2820 C CB  . THR A 363 ? 0.9672 0.4743 0.5737 -0.0926 0.1716  0.0067  363 THR A CB  
2821 O OG1 . THR A 363 ? 0.9892 0.5195 0.6315 -0.1023 0.1807  0.0034  363 THR A OG1 
2822 C CG2 . THR A 363 ? 0.9949 0.5080 0.5930 -0.0876 0.1668  0.0062  363 THR A CG2 
2823 N N   . SER A 364 ? 0.9955 0.4683 0.5823 -0.0898 0.1632  0.0093  364 SER A N   
2824 C CA  . SER A 364 ? 1.0138 0.4763 0.6046 -0.0934 0.1667  0.0101  364 SER A CA  
2825 C C   . SER A 364 ? 0.9962 0.4703 0.6169 -0.1045 0.1827  0.0088  364 SER A C   
2826 O O   . SER A 364 ? 1.0421 0.5208 0.6800 -0.1088 0.1824  0.0066  364 SER A O   
2827 C CB  . SER A 364 ? 1.0188 0.4394 0.5686 -0.0876 0.1718  0.0166  364 SER A CB  
2828 O OG  . SER A 364 ? 1.1036 0.5038 0.6331 -0.0880 0.1882  0.0218  364 SER A OG  
2829 N N   . ASP A 365 ? 1.0014 0.4806 0.6296 -0.1091 0.1964  0.0094  365 ASP A N   
2830 C CA  . ASP A 365 ? 0.9445 0.4354 0.6031 -0.1195 0.2116  0.0070  365 ASP A CA  
2831 C C   . ASP A 365 ? 0.9606 0.4919 0.6590 -0.1236 0.2043  -0.0005 365 ASP A C   
2832 O O   . ASP A 365 ? 0.9897 0.5343 0.7144 -0.1313 0.2161  -0.0036 365 ASP A O   
2833 C CB  . ASP A 365 ? 0.9929 0.4657 0.6388 -0.1226 0.2321  0.0115  365 ASP A CB  
2834 C CG  . ASP A 365 ? 1.0431 0.5240 0.6806 -0.1185 0.2294  0.0116  365 ASP A CG  
2835 O OD1 . ASP A 365 ? 1.0068 0.5060 0.6475 -0.1132 0.2118  0.0085  365 ASP A OD1 
2836 O OD2 . ASP A 365 ? 1.0986 0.5674 0.7267 -0.1205 0.2453  0.0146  365 ASP A OD2 
2837 N N   . GLY A 366 ? 0.9409 0.4912 0.6441 -0.1183 0.1855  -0.0038 366 GLY A N   
2838 C CA  . GLY A 366 ? 0.9051 0.4916 0.6431 -0.1212 0.1778  -0.0106 366 GLY A CA  
2839 C C   . GLY A 366 ? 0.9404 0.5431 0.6844 -0.1206 0.1783  -0.0118 366 GLY A C   
2840 O O   . GLY A 366 ? 0.8720 0.5019 0.6463 -0.1245 0.1775  -0.0171 366 GLY A O   
2841 N N   . GLY A 367 ? 0.9598 0.5464 0.6758 -0.1153 0.1790  -0.0074 367 GLY A N   
2842 C CA  . GLY A 367 ? 0.9427 0.5427 0.6624 -0.1142 0.1791  -0.0083 367 GLY A CA  
2843 C C   . GLY A 367 ? 0.8822 0.4911 0.5931 -0.1065 0.1616  -0.0092 367 GLY A C   
2844 O O   . GLY A 367 ? 0.8519 0.4591 0.5564 -0.1020 0.1487  -0.0097 367 GLY A O   
2845 N N   . VAL A 368 ? 0.8566 0.4754 0.5688 -0.1051 0.1616  -0.0097 368 VAL A N   
2846 C CA  . VAL A 368 ? 0.8878 0.5157 0.5940 -0.0983 0.1467  -0.0108 368 VAL A CA  
2847 C C   . VAL A 368 ? 0.9009 0.5055 0.5750 -0.0923 0.1489  -0.0068 368 VAL A C   
2848 O O   . VAL A 368 ? 0.9402 0.5288 0.6024 -0.0944 0.1633  -0.0037 368 VAL A O   
2849 C CB  . VAL A 368 ? 0.7895 0.4489 0.5239 -0.1005 0.1429  -0.0151 368 VAL A CB  
2850 C CG1 . VAL A 368 ? 0.7505 0.4321 0.5143 -0.1049 0.1392  -0.0195 368 VAL A CG1 
2851 C CG2 . VAL A 368 ? 0.8172 0.4782 0.5566 -0.1045 0.1566  -0.0147 368 VAL A CG2 
2852 N N   . TYR A 369 ? 0.8974 0.5260 0.4981 -0.2122 0.0230  0.0032  369 TYR A N   
2853 C CA  . TYR A 369 ? 0.9499 0.5565 0.5003 -0.2239 0.0159  0.0141  369 TYR A CA  
2854 C C   . TYR A 369 ? 0.9121 0.5560 0.4600 -0.2356 -0.0045 0.0142  369 TYR A C   
2855 O O   . TYR A 369 ? 0.9293 0.6191 0.5145 -0.2286 -0.0152 0.0134  369 TYR A O   
2856 C CB  . TYR A 369 ? 0.9807 0.5697 0.5099 -0.2127 0.0092  0.0300  369 TYR A CB  
2857 C CG  . TYR A 369 ? 1.0725 0.6107 0.5392 -0.2210 0.0149  0.0388  369 TYR A CG  
2858 C CD1 . TYR A 369 ? 1.1147 0.6035 0.5667 -0.2213 0.0438  0.0373  369 TYR A CD1 
2859 C CD2 . TYR A 369 ? 1.0727 0.6115 0.4949 -0.2282 -0.0084 0.0487  369 TYR A CD2 
2860 C CE1 . TYR A 369 ? 1.1960 0.6325 0.5845 -0.2263 0.0536  0.0460  369 TYR A CE1 
2861 C CE2 . TYR A 369 ? 1.1502 0.6364 0.5040 -0.2348 -0.0036 0.0551  369 TYR A CE2 
2862 C CZ  . TYR A 369 ? 1.1926 0.6253 0.5267 -0.2326 0.0297  0.0540  369 TYR A CZ  
2863 O OH  . TYR A 369 ? 1.3508 0.7279 0.6141 -0.2356 0.0387  0.0602  369 TYR A OH  
2864 N N   . TRP A 370 ? 0.9445 0.5652 0.4480 -0.2537 -0.0076 0.0152  370 TRP A N   
2865 C CA  . TRP A 370 ? 1.0738 0.7239 0.5744 -0.2692 -0.0271 0.0149  370 TRP A CA  
2866 C C   . TRP A 370 ? 1.1457 0.7545 0.5825 -0.2875 -0.0338 0.0167  370 TRP A C   
2867 O O   . TRP A 370 ? 1.1126 0.6681 0.5062 -0.2869 -0.0172 0.0174  370 TRP A O   
2868 C CB  . TRP A 370 ? 0.8991 0.5715 0.4298 -0.2753 -0.0163 0.0039  370 TRP A CB  
2869 C CG  . TRP A 370 ? 0.8985 0.5322 0.4143 -0.2799 0.0100  -0.0046 370 TRP A CG  
2870 C CD1 . TRP A 370 ? 0.9424 0.5309 0.4117 -0.2955 0.0209  -0.0065 370 TRP A CD1 
2871 C CD2 . TRP A 370 ? 0.8877 0.5249 0.4374 -0.2682 0.0284  -0.0117 370 TRP A CD2 
2872 N NE1 . TRP A 370 ? 0.8834 0.4683 0.3710 -0.2796 0.0453  -0.0139 370 TRP A NE1 
2873 C CE2 . TRP A 370 ? 0.8980 0.5086 0.4330 -0.2679 0.0488  -0.0159 370 TRP A CE2 
2874 C CE3 . TRP A 370 ? 0.8281 0.4963 0.4226 -0.2513 0.0278  -0.0162 370 TRP A CE3 
2875 C CZ2 . TRP A 370 ? 0.8210 0.4424 0.3923 -0.2518 0.0651  -0.0219 370 TRP A CZ2 
2876 C CZ3 . TRP A 370 ? 0.7616 0.4239 0.3787 -0.2455 0.0436  -0.0248 370 TRP A CZ3 
2877 C CH2 . TRP A 370 ? 0.7975 0.4390 0.4060 -0.2465 0.0613  -0.0258 370 TRP A CH2 
2878 N N   . GLU A 371 ? 1.0611 0.6930 0.4921 -0.3039 -0.0575 0.0173  371 GLU A N   
2879 C CA  . GLU A 371 ? 1.1061 0.6978 0.4723 -0.3244 -0.0681 0.0151  371 GLU A CA  
2880 C C   . GLU A 371 ? 1.1346 0.6777 0.4697 -0.3359 -0.0390 0.0031  371 GLU A C   
2881 O O   . GLU A 371 ? 1.0911 0.6525 0.4631 -0.3384 -0.0239 -0.0039 371 GLU A O   
2882 C CB  . GLU A 371 ? 1.0912 0.7226 0.4699 -0.3428 -0.1010 0.0159  371 GLU A CB  
2883 C CG  . GLU A 371 ? 1.1197 0.7885 0.5121 -0.3346 -0.1345 0.0311  371 GLU A CG  
2884 C CD  . GLU A 371 ? 1.1542 0.8670 0.6093 -0.3077 -0.1282 0.0411  371 GLU A CD  
2885 O OE1 . GLU A 371 ? 1.0076 0.7403 0.5068 -0.3008 -0.1075 0.0344  371 GLU A OE1 
2886 O OE2 . GLU A 371 ? 1.1112 0.8359 0.5680 -0.2924 -0.1436 0.0558  371 GLU A OE2 
2887 N N   . GLY A 372 ? 1.1913 0.6780 0.4768 -0.3355 -0.0273 0.0045  372 GLY A N   
2888 C CA  . GLY A 372 ? 1.1634 0.6049 0.4350 -0.3405 0.0031  -0.0031 372 GLY A CA  
2889 C C   . GLY A 372 ? 1.1641 0.5943 0.4533 -0.3186 0.0323  -0.0146 372 GLY A C   
2890 O O   . GLY A 372 ? 1.2625 0.6815 0.5533 -0.3070 0.0553  -0.0247 372 GLY A O   
2891 N N   . ILE A 373 ? 1.1058 0.5578 0.4257 -0.3025 0.0346  -0.0053 373 ILE A N   
2892 C CA  . ILE A 373 ? 1.1216 0.5788 0.4819 -0.2775 0.0619  -0.0093 373 ILE A CA  
2893 C C   . ILE A 373 ? 1.1607 0.5695 0.4877 -0.2663 0.0821  -0.0113 373 ILE A C   
2894 O O   . ILE A 373 ? 1.0982 0.5113 0.4586 -0.2482 0.1071  -0.0146 373 ILE A O   
2895 C CB  . ILE A 373 ? 1.0710 0.5510 0.4719 -0.2675 0.0588  0.0007  373 ILE A CB  
2896 C CG1 . ILE A 373 ? 1.0640 0.5653 0.5244 -0.2482 0.0804  -0.0058 373 ILE A CG1 
2897 C CG2 . ILE A 373 ? 1.0828 0.5285 0.4477 -0.2623 0.0558  0.0148  373 ILE A CG2 
2898 C CD1 . ILE A 373 ? 1.0737 0.5922 0.5761 -0.2415 0.0769  -0.0016 373 ILE A CD1 
2899 N N   . ASP A 374 ? 1.2345 0.5995 0.4998 -0.2762 0.0711  -0.0070 374 ASP A N   
2900 C CA  . ASP A 374 ? 1.2790 0.5902 0.5025 -0.2673 0.0908  -0.0099 374 ASP A CA  
2901 C C   . ASP A 374 ? 1.3032 0.6123 0.5562 -0.2416 0.1173  -0.0028 374 ASP A C   
2902 O O   . ASP A 374 ? 1.3738 0.6571 0.6220 -0.2290 0.1441  -0.0068 374 ASP A O   
2903 C CB  . ASP A 374 ? 1.2899 0.5834 0.5030 -0.2721 0.1064  -0.0263 374 ASP A CB  
2904 C CG  . ASP A 374 ? 1.5142 0.7404 0.6683 -0.2696 0.1218  -0.0293 374 ASP A CG  
2905 O OD1 . ASP A 374 ? 1.6042 0.8008 0.7226 -0.2641 0.1179  -0.0177 374 ASP A OD1 
2906 O OD2 . ASP A 374 ? 1.6409 0.8437 0.7822 -0.2707 0.1392  -0.0420 374 ASP A OD2 
2907 N N   . GLU A 375 ? 1.2851 0.6198 0.5717 -0.2343 0.1112  0.0088  375 GLU A N   
2908 C CA  . GLU A 375 ? 1.2570 0.5928 0.5840 -0.2134 0.1352  0.0159  375 GLU A CA  
2909 C C   . GLU A 375 ? 1.3022 0.6200 0.6063 -0.2073 0.1269  0.0331  375 GLU A C   
2910 O O   . GLU A 375 ? 1.2849 0.6244 0.5958 -0.2140 0.1044  0.0404  375 GLU A O   
2911 C CB  . GLU A 375 ? 1.1813 0.5678 0.5882 -0.2087 0.1397  0.0114  375 GLU A CB  
2912 C CG  . GLU A 375 ? 1.3536 0.7449 0.8139 -0.1909 0.1646  0.0157  375 GLU A CG  
2913 C CD  . GLU A 375 ? 1.3391 0.7777 0.8738 -0.1888 0.1652  0.0090  375 GLU A CD  
2914 O OE1 . GLU A 375 ? 1.2420 0.7069 0.7820 -0.1977 0.1519  0.0007  375 GLU A OE1 
2915 O OE2 . GLU A 375 ? 1.3372 0.7856 0.9248 -0.1788 0.1779  0.0124  375 GLU A OE2 
2916 N N   . PRO A 376 ? 1.3751 0.6545 0.6519 -0.1927 0.1452  0.0419  376 PRO A N   
2917 C CA  . PRO A 376 ? 1.3725 0.6364 0.6292 -0.1823 0.1395  0.0610  376 PRO A CA  
2918 C C   . PRO A 376 ? 1.3241 0.6147 0.6501 -0.1735 0.1471  0.0668  376 PRO A C   
2919 O O   . PRO A 376 ? 1.3290 0.6420 0.7189 -0.1700 0.1646  0.0575  376 PRO A O   
2920 C CB  . PRO A 376 ? 1.2947 0.5118 0.5135 -0.1666 0.1645  0.0671  376 PRO A CB  
2921 C CG  . PRO A 376 ? 1.4485 0.6484 0.6450 -0.1739 0.1748  0.0504  376 PRO A CG  
2922 C CD  . PRO A 376 ? 1.4046 0.6513 0.6635 -0.1836 0.1729  0.0365  376 PRO A CD  
2923 N N   . LEU A 377 ? 1.3374 0.6259 0.6509 -0.1691 0.1320  0.0830  377 LEU A N   
2924 C CA  . LEU A 377 ? 1.2926 0.5941 0.6645 -0.1600 0.1395  0.0887  377 LEU A CA  
2925 C C   . LEU A 377 ? 1.3744 0.6454 0.7484 -0.1392 0.1640  0.1034  377 LEU A C   
2926 O O   . LEU A 377 ? 1.3803 0.6200 0.6952 -0.1304 0.1664  0.1158  377 LEU A O   
2927 C CB  . LEU A 377 ? 1.3032 0.6198 0.6654 -0.1650 0.1111  0.0996  377 LEU A CB  
2928 C CG  . LEU A 377 ? 1.2015 0.5700 0.5893 -0.1811 0.0864  0.0821  377 LEU A CG  
2929 C CD1 . LEU A 377 ? 1.2053 0.6258 0.6132 -0.1732 0.0535  0.0863  377 LEU A CD1 
2930 C CD2 . LEU A 377 ? 1.2173 0.6020 0.6709 -0.1860 0.1026  0.0640  377 LEU A CD2 
2931 N N   . ALA A 378 ? 1.3131 0.5944 0.7569 -0.1317 0.1814  0.1009  378 ALA A N   
2932 C CA  . ALA A 378 ? 1.3570 0.6139 0.8149 -0.1134 0.2061  0.1144  378 ALA A CA  
2933 C C   . ALA A 378 ? 1.3103 0.5447 0.7274 -0.1003 0.1964  0.1377  378 ALA A C   
2934 O O   . ALA A 378 ? 1.3463 0.5918 0.7477 -0.1050 0.1710  0.1424  378 ALA A O   
2935 C CB  . ALA A 378 ? 1.2521 0.5305 0.7996 -0.1118 0.2212  0.1040  378 ALA A CB  
2936 N N   . PRO A 379 ? 1.3823 0.5869 0.7816 -0.0820 0.2161  0.1547  379 PRO A N   
2937 C CA  . PRO A 379 ? 1.4111 0.5985 0.7798 -0.0646 0.2083  0.1798  379 PRO A CA  
2938 C C   . PRO A 379 ? 1.3015 0.5038 0.7276 -0.0619 0.2044  0.1798  379 PRO A C   
2939 O O   . PRO A 379 ? 1.2926 0.5064 0.7914 -0.0660 0.2205  0.1635  379 PRO A O   
2940 C CB  . PRO A 379 ? 1.4344 0.5907 0.7979 -0.0458 0.2393  0.1931  379 PRO A CB  
2941 C CG  . PRO A 379 ? 1.3833 0.5327 0.7334 -0.0538 0.2542  0.1790  379 PRO A CG  
2942 C CD  . PRO A 379 ? 1.3975 0.5828 0.7988 -0.0746 0.2462  0.1539  379 PRO A CD  
2943 N N   . GLY A 380 ? 1.2770 0.4808 0.6699 -0.0539 0.1807  0.1978  380 GLY A N   
2944 C CA  . GLY A 380 ? 1.2438 0.4654 0.6896 -0.0462 0.1759  0.1971  380 GLY A CA  
2945 C C   . GLY A 380 ? 1.2583 0.5398 0.7498 -0.0623 0.1503  0.1685  380 GLY A C   
2946 O O   . GLY A 380 ? 1.2196 0.5366 0.7528 -0.0526 0.1371  0.1648  380 GLY A O   
2947 N N   . VAL A 381 ? 1.2543 0.5454 0.7379 -0.0848 0.1457  0.1497  381 VAL A N   
2948 C CA  . VAL A 381 ? 1.1915 0.5374 0.7141 -0.0986 0.1233  0.1247  381 VAL A CA  
2949 C C   . VAL A 381 ? 1.1613 0.5542 0.6614 -0.0960 0.0861  0.1320  381 VAL A C   
2950 O O   . VAL A 381 ? 1.1894 0.5764 0.6301 -0.1002 0.0705  0.1443  381 VAL A O   
2951 C CB  . VAL A 381 ? 1.1477 0.4890 0.6665 -0.1212 0.1305  0.1065  381 VAL A CB  
2952 C CG1 . VAL A 381 ? 1.0590 0.4546 0.6180 -0.1328 0.1101  0.0825  381 VAL A CG1 
2953 C CG2 . VAL A 381 ? 1.2246 0.5251 0.7741 -0.1228 0.1669  0.1028  381 VAL A CG2 
2954 N N   . THR A 382 ? 1.1106 0.5491 0.6586 -0.0890 0.0718  0.1244  382 THR A N   
2955 C CA  . THR A 382 ? 1.1203 0.6112 0.6649 -0.0864 0.0386  0.1316  382 THR A CA  
2956 C C   . THR A 382 ? 1.0301 0.5646 0.6004 -0.1039 0.0252  0.1084  382 THR A C   
2957 O O   . THR A 382 ? 0.9754 0.5034 0.5716 -0.1134 0.0402  0.0868  382 THR A O   
2958 C CB  . THR A 382 ? 1.0571 0.5674 0.6369 -0.0610 0.0362  0.1457  382 THR A CB  
2959 O OG1 . THR A 382 ? 1.0936 0.6055 0.7279 -0.0568 0.0538  0.1256  382 THR A OG1 
2960 C CG2 . THR A 382 ? 1.1515 0.6183 0.7030 -0.0414 0.0498  0.1728  382 THR A CG2 
2961 N N   . ILE A 383 ? 1.0438 0.6243 0.6091 -0.1079 -0.0039 0.1143  383 ILE A N   
2962 C CA  . ILE A 383 ? 1.0483 0.6691 0.6321 -0.1247 -0.0163 0.0966  383 ILE A CA  
2963 C C   . ILE A 383 ? 1.0345 0.7118 0.6620 -0.1124 -0.0323 0.1020  383 ILE A C   
2964 O O   . ILE A 383 ? 1.1072 0.8052 0.7334 -0.1009 -0.0498 0.1240  383 ILE A O   
2965 C CB  . ILE A 383 ? 1.0733 0.6922 0.6091 -0.1470 -0.0334 0.0971  383 ILE A CB  
2966 C CG1 . ILE A 383 ? 1.1024 0.6613 0.5934 -0.1570 -0.0118 0.0922  383 ILE A CG1 
2967 C CG2 . ILE A 383 ? 1.0600 0.7213 0.6199 -0.1630 -0.0443 0.0816  383 ILE A CG2 
2968 C CD1 . ILE A 383 ? 1.1972 0.7431 0.6331 -0.1784 -0.0244 0.0903  383 ILE A CD1 
2969 N N   . THR A 384 ? 0.9969 0.6987 0.6625 -0.1134 -0.0257 0.0836  384 THR A N   
2970 C CA  . THR A 384 ? 0.9752 0.7300 0.6813 -0.1027 -0.0359 0.0872  384 THR A CA  
2971 C C   . THR A 384 ? 0.9343 0.7236 0.6420 -0.1229 -0.0490 0.0788  384 THR A C   
2972 O O   . THR A 384 ? 0.8950 0.6717 0.5962 -0.1363 -0.0388 0.0592  384 THR A O   
2973 C CB  . THR A 384 ? 0.9573 0.7089 0.6993 -0.0854 -0.0158 0.0730  384 THR A CB  
2974 O OG1 . THR A 384 ? 1.0102 0.7271 0.7541 -0.0671 -0.0022 0.0816  384 THR A OG1 
2975 C CG2 . THR A 384 ? 0.9429 0.7457 0.7223 -0.0724 -0.0214 0.0774  384 THR A CG2 
2976 N N   . SER A 385 ? 0.9405 0.7739 0.6608 -0.1249 -0.0713 0.0947  385 SER A N   
2977 C CA  . SER A 385 ? 0.9555 0.8206 0.6811 -0.1455 -0.0834 0.0888  385 SER A CA  
2978 C C   . SER A 385 ? 0.8914 0.7816 0.6541 -0.1388 -0.0678 0.0752  385 SER A C   
2979 O O   . SER A 385 ? 0.8854 0.7719 0.6691 -0.1175 -0.0515 0.0705  385 SER A O   
2980 C CB  . SER A 385 ? 0.9983 0.9078 0.7381 -0.1500 -0.1127 0.1101  385 SER A CB  
2981 O OG  . SER A 385 ? 0.9878 0.9410 0.7807 -0.1271 -0.1122 0.1248  385 SER A OG  
2982 N N   . TRP A 386 ? 0.8830 0.7949 0.6497 -0.1568 -0.0721 0.0687  386 TRP A N   
2983 C CA  . TRP A 386 ? 0.8609 0.7988 0.6582 -0.1492 -0.0579 0.0594  386 TRP A CA  
2984 C C   . TRP A 386 ? 0.8714 0.8544 0.7152 -0.1280 -0.0584 0.0755  386 TRP A C   
2985 O O   . TRP A 386 ? 0.8281 0.8242 0.6927 -0.1125 -0.0411 0.0687  386 TRP A O   
2986 C CB  . TRP A 386 ? 0.8463 0.7971 0.6390 -0.1724 -0.0608 0.0533  386 TRP A CB  
2987 C CG  . TRP A 386 ? 0.8173 0.8092 0.6325 -0.1853 -0.0815 0.0701  386 TRP A CG  
2988 C CD1 . TRP A 386 ? 0.8524 0.8400 0.6471 -0.2040 -0.1058 0.0788  386 TRP A CD1 
2989 C CD2 . TRP A 386 ? 0.8160 0.8594 0.6801 -0.1811 -0.0802 0.0802  386 TRP A CD2 
2990 N NE1 . TRP A 386 ? 0.8615 0.8976 0.6937 -0.2141 -0.1235 0.0924  386 TRP A NE1 
2991 C CE2 . TRP A 386 ? 0.8408 0.9128 0.7201 -0.2002 -0.1062 0.0948  386 TRP A CE2 
2992 C CE3 . TRP A 386 ? 0.7992 0.8656 0.6943 -0.1626 -0.0589 0.0787  386 TRP A CE3 
2993 C CZ2 . TRP A 386 ? 0.7755 0.9018 0.7101 -0.2027 -0.1107 0.1091  386 TRP A CZ2 
2994 C CZ3 . TRP A 386 ? 0.7211 0.8376 0.6647 -0.1624 -0.0595 0.0941  386 TRP A CZ3 
2995 C CH2 . TRP A 386 ? 0.7771 0.9249 0.7451 -0.1829 -0.0848 0.1098  386 TRP A CH2 
2996 N N   . LYS A 387 ? 0.9313 0.9378 0.7906 -0.1256 -0.0774 0.0976  387 LYS A N   
2997 C CA  . LYS A 387 ? 0.9612 1.0104 0.8701 -0.1023 -0.0766 0.1174  387 LYS A CA  
2998 C C   . LYS A 387 ? 1.0308 1.0552 0.9409 -0.0733 -0.0606 0.1188  387 LYS A C   
2999 O O   . LYS A 387 ? 1.0510 1.1042 0.9993 -0.0507 -0.0584 0.1383  387 LYS A O   
3000 C CB  . LYS A 387 ? 0.9524 1.0411 0.8827 -0.1115 -0.1070 0.1426  387 LYS A CB  
3001 C CG  . LYS A 387 ? 0.9034 1.0243 0.8472 -0.1398 -0.1232 0.1430  387 LYS A CG  
3002 C CD  . LYS A 387 ? 0.9809 1.1405 0.9466 -0.1509 -0.1590 0.1661  387 LYS A CD  
3003 C CE  . LYS A 387 ? 1.0076 1.1991 0.9940 -0.1813 -0.1753 0.1651  387 LYS A CE  
3004 N NZ  . LYS A 387 ? 0.9821 1.2175 1.0302 -0.1723 -0.1545 0.1705  387 LYS A NZ  
3005 N N   . ASN A 388 ? 0.9878 0.9589 0.8610 -0.0735 -0.0481 0.0997  388 ASN A N   
3006 C CA  . ASN A 388 ? 1.0038 0.9436 0.8780 -0.0489 -0.0309 0.0974  388 ASN A CA  
3007 C C   . ASN A 388 ? 1.0421 0.9859 0.9240 -0.0357 -0.0418 0.1244  388 ASN A C   
3008 O O   . ASN A 388 ? 1.0521 1.0036 0.9622 -0.0088 -0.0309 0.1371  388 ASN A O   
3009 C CB  . ASN A 388 ? 0.9364 0.8891 0.8384 -0.0258 -0.0096 0.0901  388 ASN A CB  
3010 C CG  . ASN A 388 ? 1.0053 0.9105 0.8970 -0.0076 0.0109  0.0745  388 ASN A CG  
3011 O OD1 . ASN A 388 ? 1.0172 0.8789 0.8816 -0.0186 0.0129  0.0586  388 ASN A OD1 
3012 N ND2 . ASN A 388 ? 1.0862 0.9979 1.0022 0.0203  0.0277  0.0791  388 ASN A ND2 
3013 N N   . LYS A 389 ? 0.9963 0.9321 0.8492 -0.0534 -0.0629 0.1339  389 LYS A N   
3014 C CA  . LYS A 389 ? 1.0523 0.9912 0.9032 -0.0418 -0.0778 0.1613  389 LYS A CA  
3015 C C   . LYS A 389 ? 1.1119 1.0001 0.9062 -0.0553 -0.0828 0.1586  389 LYS A C   
3016 O O   . LYS A 389 ? 1.0660 0.9314 0.8272 -0.0792 -0.0831 0.1402  389 LYS A O   
3017 C CB  . LYS A 389 ? 1.0810 1.0812 0.9606 -0.0475 -0.1078 0.1850  389 LYS A CB  
3018 C CG  . LYS A 389 ? 1.1090 1.1631 1.0506 -0.0337 -0.1003 0.1924  389 LYS A CG  
3019 C CD  . LYS A 389 ? 1.1214 1.2386 1.0995 -0.0439 -0.1319 0.2161  389 LYS A CD  
3020 C CE  . LYS A 389 ? 1.0941 1.2655 1.1393 -0.0308 -0.1195 0.2250  389 LYS A CE  
3021 N NZ  . LYS A 389 ? 1.0535 1.2902 1.1449 -0.0445 -0.1509 0.2478  389 LYS A NZ  
3022 N N   . GLU A 390 ? 1.1733 1.0423 0.9564 -0.0375 -0.0839 0.1793  390 GLU A N   
3023 C CA  . GLU A 390 ? 1.2580 1.0773 0.9838 -0.0462 -0.0866 0.1822  390 GLU A CA  
3024 C C   . GLU A 390 ? 1.2357 1.0706 0.9262 -0.0715 -0.1185 0.1862  390 GLU A C   
3025 O O   . GLU A 390 ? 1.2401 1.1245 0.9500 -0.0720 -0.1475 0.2044  390 GLU A O   
3026 C CB  . GLU A 390 ? 1.2894 1.0900 1.0112 -0.0188 -0.0824 0.2089  390 GLU A CB  
3027 C CG  . GLU A 390 ? 1.4367 1.1675 1.1106 -0.0180 -0.0627 0.2067  390 GLU A CG  
3028 C CD  . GLU A 390 ? 1.5020 1.1938 1.1916 -0.0183 -0.0281 0.1803  390 GLU A CD  
3029 O OE1 . GLU A 390 ? 1.4537 1.1696 1.1771 -0.0235 -0.0231 0.1595  390 GLU A OE1 
3030 O OE2 . GLU A 390 ? 1.5450 1.1821 1.2138 -0.0131 -0.0062 0.1809  390 GLU A OE2 
3031 N N   . TRP A 391 ? 1.2194 1.0111 0.8601 -0.0930 -0.1130 0.1691  391 TRP A N   
3032 C CA  . TRP A 391 ? 1.2975 1.0939 0.8991 -0.1202 -0.1387 0.1658  391 TRP A CA  
3033 C C   . TRP A 391 ? 1.3812 1.1183 0.9085 -0.1245 -0.1384 0.1708  391 TRP A C   
3034 O O   . TRP A 391 ? 1.3496 1.0340 0.8555 -0.1205 -0.1082 0.1621  391 TRP A O   
3035 C CB  . TRP A 391 ? 1.1643 0.9643 0.7737 -0.1434 -0.1293 0.1390  391 TRP A CB  
3036 C CG  . TRP A 391 ? 1.2567 1.0521 0.8242 -0.1726 -0.1505 0.1326  391 TRP A CG  
3037 C CD1 . TRP A 391 ? 1.2038 1.0463 0.7913 -0.1897 -0.1781 0.1344  391 TRP A CD1 
3038 C CD2 . TRP A 391 ? 1.3742 1.1107 0.8730 -0.1885 -0.1436 0.1228  391 TRP A CD2 
3039 N NE1 . TRP A 391 ? 1.2417 1.0559 0.7745 -0.2166 -0.1905 0.1241  391 TRP A NE1 
3040 C CE2 . TRP A 391 ? 1.3347 1.0825 0.8096 -0.2151 -0.1687 0.1170  391 TRP A CE2 
3041 C CE3 . TRP A 391 ? 1.3984 1.0722 0.8561 -0.1826 -0.1164 0.1189  391 TRP A CE3 
3042 C CZ2 . TRP A 391 ? 1.4089 1.1033 0.8133 -0.2346 -0.1665 0.1064  391 TRP A CZ2 
3043 C CZ3 . TRP A 391 ? 1.4352 1.0596 0.8271 -0.2006 -0.1126 0.1110  391 TRP A CZ3 
3044 C CH2 . TRP A 391 ? 1.4170 1.0499 0.7794 -0.2257 -0.1371 0.1042  391 TRP A CH2 
3045 N N   . ARG A 392 ? 1.4631 1.2083 0.9512 -0.1327 -0.1720 0.1851  392 ARG A N   
3046 C CA  . ARG A 392 ? 1.5957 1.2829 0.9998 -0.1385 -0.1749 0.1891  392 ARG A CA  
3047 C C   . ARG A 392 ? 1.6828 1.3670 1.0435 -0.1709 -0.1985 0.1743  392 ARG A C   
3048 O O   . ARG A 392 ? 1.6363 1.3748 1.0322 -0.1857 -0.2269 0.1721  392 ARG A O   
3049 C CB  . ARG A 392 ? 1.7023 1.3898 1.0800 -0.1169 -0.1961 0.2201  392 ARG A CB  
3050 C CG  . ARG A 392 ? 1.6549 1.3329 1.0654 -0.0832 -0.1696 0.2375  392 ARG A CG  
3051 C CD  . ARG A 392 ? 1.7080 1.3678 1.0714 -0.0618 -0.1849 0.2691  392 ARG A CD  
3052 N NE  . ARG A 392 ? 1.7238 1.4364 1.0841 -0.0673 -0.2361 0.2850  392 ARG A NE  
3053 C CZ  . ARG A 392 ? 1.7829 1.4898 1.0954 -0.0532 -0.2629 0.3122  392 ARG A CZ  
3054 N NH1 . ARG A 392 ? 1.7616 1.4090 1.0206 -0.0308 -0.2403 0.3287  392 ARG A NH1 
3055 N NH2 . ARG A 392 ? 1.7228 1.4855 1.0425 -0.0617 -0.3141 0.3243  392 ARG A NH2 
3056 N N   . PRO A 393 ? 1.8017 1.4206 1.0876 -0.1824 -0.1850 0.1644  393 PRO A N   
3057 C CA  . PRO A 393 ? 1.8601 1.4662 1.0964 -0.2132 -0.2053 0.1489  393 PRO A CA  
3058 C C   . PRO A 393 ? 1.9770 1.6114 1.1858 -0.2218 -0.2569 0.1616  393 PRO A C   
3059 O O   . PRO A 393 ? 2.0113 1.6450 1.1925 -0.2499 -0.2791 0.1467  393 PRO A O   
3060 C CB  . PRO A 393 ? 1.9508 1.4726 1.1065 -0.2150 -0.1749 0.1418  393 PRO A CB  
3061 C CG  . PRO A 393 ? 1.9090 1.4116 1.1009 -0.1921 -0.1325 0.1457  393 PRO A CG  
3062 C CD  . PRO A 393 ? 1.8564 1.4078 1.1049 -0.1683 -0.1455 0.1657  393 PRO A CD  
3063 N N   . GLN A 394 ? 2.0147 1.6743 1.2338 -0.1984 -0.2768 0.1883  394 GLN A N   
3064 C CA  . GLN A 394 ? 2.0845 1.7769 1.2822 -0.2053 -0.3307 0.2027  394 GLN A CA  
3065 C C   . GLN A 394 ? 2.0425 1.8209 1.3284 -0.2185 -0.3614 0.2033  394 GLN A C   
3066 O O   . GLN A 394 ? 2.0950 1.9037 1.3769 -0.2358 -0.4041 0.2032  394 GLN A O   
3067 C CB  . GLN A 394 ? 2.0751 1.7642 1.2526 -0.1724 -0.3404 0.2352  394 GLN A CB  
3068 C CG  . GLN A 394 ? 2.2037 1.8167 1.2940 -0.1591 -0.3176 0.2344  394 GLN A CG  
3069 C CD  . GLN A 394 ? 2.2172 1.7650 1.2873 -0.1547 -0.2621 0.2240  394 GLN A CD  
3070 O OE1 . GLN A 394 ? 2.1120 1.6769 1.2482 -0.1481 -0.2354 0.2217  394 GLN A OE1 
3071 N NE2 . GLN A 394 ? 2.3024 1.7879 1.3096 -0.1541 -0.2372 0.2116  394 GLN A NE2 
3072 N N   . ASP A 395 ? 1.9685 1.7874 1.3416 -0.2085 -0.3359 0.2015  395 ASP A N   
3073 C CA  . ASP A 395 ? 1.9591 1.8562 1.4181 -0.2193 -0.3570 0.2030  395 ASP A CA  
3074 C C   . ASP A 395 ? 1.9203 1.8142 1.3710 -0.2573 -0.3636 0.1765  395 ASP A C   
3075 O O   . ASP A 395 ? 1.9420 1.7751 1.3353 -0.2710 -0.3400 0.1546  395 ASP A O   
3076 C CB  . ASP A 395 ? 1.8491 1.7795 1.3915 -0.1960 -0.3224 0.2068  395 ASP A CB  
3077 C CG  . ASP A 395 ? 1.9055 1.8595 1.4801 -0.1598 -0.3231 0.2367  395 ASP A CG  
3078 O OD1 . ASP A 395 ? 1.9304 1.9277 1.5197 -0.1556 -0.3625 0.2603  395 ASP A OD1 
3079 O OD2 . ASP A 395 ? 1.8135 1.7426 1.4007 -0.1358 -0.2848 0.2369  395 ASP A OD2 
3080 N N   . GLU A 396 ? 1.9339 1.8944 1.4473 -0.2737 -0.3941 0.1803  396 GLU A N   
3081 C CA  . GLU A 396 ? 1.9070 1.8706 1.4281 -0.3090 -0.3974 0.1571  396 GLU A CA  
3082 C C   . GLU A 396 ? 1.8506 1.8266 1.4295 -0.3049 -0.3543 0.1451  396 GLU A C   
3083 O O   . GLU A 396 ? 1.8247 1.7810 1.3930 -0.3292 -0.3420 0.1237  396 GLU A O   
3084 C CB  . GLU A 396 ? 1.8874 1.9173 1.4581 -0.3307 -0.4472 0.1664  396 GLU A CB  
3085 C CG  . GLU A 396 ? 1.9038 1.9291 1.4871 -0.3641 -0.4437 0.1409  396 GLU A CG  
3086 C CD  . GLU A 396 ? 1.8699 1.9632 1.5262 -0.3793 -0.4798 0.1491  396 GLU A CD  
3087 O OE1 . GLU A 396 ? 1.8624 2.0241 1.5864 -0.3641 -0.5019 0.1766  396 GLU A OE1 
3088 O OE2 . GLU A 396 ? 1.8757 1.9537 1.5249 -0.4051 -0.4845 0.1294  396 GLU A OE2 
3089 N N   . GLU A 397 ? 1.5700 1.5750 1.2055 -0.2740 -0.3311 0.1586  397 GLU A N   
3090 C CA  . GLU A 397 ? 1.3991 1.4131 1.0815 -0.2664 -0.2916 0.1473  397 GLU A CA  
3091 C C   . GLU A 397 ? 1.3305 1.2744 0.9538 -0.2696 -0.2572 0.1247  397 GLU A C   
3092 O O   . GLU A 397 ? 1.3110 1.2092 0.8895 -0.2534 -0.2439 0.1266  397 GLU A O   
3093 C CB  . GLU A 397 ? 1.3354 1.3837 1.0766 -0.2304 -0.2745 0.1652  397 GLU A CB  
3094 C CG  . GLU A 397 ? 1.3339 1.4599 1.1539 -0.2236 -0.2984 0.1892  397 GLU A CG  
3095 C CD  . GLU A 397 ? 1.3275 1.4977 1.2141 -0.2327 -0.2850 0.1839  397 GLU A CD  
3096 O OE1 . GLU A 397 ? 1.2990 1.4428 1.1776 -0.2318 -0.2503 0.1649  397 GLU A OE1 
3097 O OE2 . GLU A 397 ? 1.2898 1.5221 1.2387 -0.2403 -0.3089 0.2003  397 GLU A OE2 
3098 N N   . PRO A 398 ? 1.2474 1.1811 0.8724 -0.2889 -0.2406 0.1052  398 PRO A N   
3099 C CA  . PRO A 398 ? 1.1876 1.0637 0.7721 -0.2875 -0.2049 0.0868  398 PRO A CA  
3100 C C   . PRO A 398 ? 1.0848 0.9666 0.7052 -0.2578 -0.1752 0.0884  398 PRO A C   
3101 O O   . PRO A 398 ? 1.0815 1.0127 0.7637 -0.2439 -0.1722 0.0959  398 PRO A O   
3102 C CB  . PRO A 398 ? 1.1128 0.9916 0.7069 -0.3122 -0.1966 0.0706  398 PRO A CB  
3103 C CG  . PRO A 398 ? 1.1286 1.0774 0.7936 -0.3165 -0.2152 0.0819  398 PRO A CG  
3104 C CD  . PRO A 398 ? 1.1972 1.1736 0.8676 -0.3115 -0.2516 0.1015  398 PRO A CD  
3105 N N   . CYS A 399 ? 1.0606 0.8890 0.6416 -0.2484 -0.1522 0.0811  399 CYS A N   
3106 C CA  . CYS A 399 ? 1.0962 0.9228 0.7073 -0.2230 -0.1261 0.0795  399 CYS A CA  
3107 C C   . CYS A 399 ? 0.9334 0.7732 0.5772 -0.2241 -0.1044 0.0635  399 CYS A C   
3108 O O   . CYS A 399 ? 0.9463 0.8010 0.6261 -0.2036 -0.0897 0.0618  399 CYS A O   
3109 C CB  . CYS A 399 ? 1.0287 0.7947 0.5947 -0.2149 -0.1081 0.0772  399 CYS A CB  
3110 S SG  . CYS A 399 ? 1.0604 0.7698 0.5795 -0.2349 -0.0853 0.0575  399 CYS A SG  
3111 N N   . ALA A 400 ? 0.9051 0.7367 0.5336 -0.2462 -0.1017 0.0517  400 ALA A N   
3112 C CA  . ALA A 400 ? 0.8716 0.7178 0.5278 -0.2470 -0.0830 0.0395  400 ALA A CA  
3113 C C   . ALA A 400 ? 0.9179 0.8018 0.5969 -0.2644 -0.0955 0.0424  400 ALA A C   
3114 O O   . ALA A 400 ? 0.9768 0.8525 0.6308 -0.2867 -0.1139 0.0441  400 ALA A O   
3115 C CB  . ALA A 400 ? 0.9414 0.7395 0.5637 -0.2552 -0.0613 0.0242  400 ALA A CB  
3116 N N   . HIS A 401 ? 0.8464 0.7689 0.5714 -0.2544 -0.0849 0.0427  401 HIS A N   
3117 C CA  . HIS A 401 ? 0.7916 0.7507 0.5465 -0.2699 -0.0917 0.0475  401 HIS A CA  
3118 C C   . HIS A 401 ? 0.8129 0.7392 0.5349 -0.2948 -0.0841 0.0350  401 HIS A C   
3119 O O   . HIS A 401 ? 0.8432 0.7342 0.5393 -0.2913 -0.0634 0.0231  401 HIS A O   
3120 C CB  . HIS A 401 ? 0.7381 0.7381 0.5429 -0.2505 -0.0748 0.0514  401 HIS A CB  
3121 C CG  . HIS A 401 ? 0.7529 0.7952 0.5993 -0.2635 -0.0789 0.0610  401 HIS A CG  
3122 N ND1 . HIS A 401 ? 0.7013 0.7388 0.5475 -0.2767 -0.0635 0.0544  401 HIS A ND1 
3123 C CD2 . HIS A 401 ? 0.6985 0.7896 0.5937 -0.2650 -0.0954 0.0786  401 HIS A CD2 
3124 C CE1 . HIS A 401 ? 0.7165 0.7954 0.6089 -0.2869 -0.0689 0.0667  401 HIS A CE1 
3125 N NE2 . HIS A 401 ? 0.6548 0.7689 0.5803 -0.2807 -0.0890 0.0815  401 HIS A NE2 
3126 N N   . PRO A 402 ? 0.7855 0.7217 0.5101 -0.3203 -0.1003 0.0376  402 PRO A N   
3127 C CA  . PRO A 402 ? 0.8036 0.7016 0.4937 -0.3442 -0.0906 0.0252  402 PRO A CA  
3128 C C   . PRO A 402 ? 0.7940 0.6912 0.4984 -0.3363 -0.0595 0.0193  402 PRO A C   
3129 O O   . PRO A 402 ? 0.9027 0.7577 0.5720 -0.3460 -0.0434 0.0090  402 PRO A O   
3130 C CB  . PRO A 402 ? 0.7775 0.6990 0.4859 -0.3714 -0.1150 0.0301  402 PRO A CB  
3131 C CG  . PRO A 402 ? 0.7823 0.7377 0.5102 -0.3645 -0.1454 0.0439  402 PRO A CG  
3132 C CD  . PRO A 402 ? 0.8070 0.7863 0.5653 -0.3296 -0.1300 0.0518  402 PRO A CD  
3133 N N   . ASN A 403 ? 0.7415 0.6824 0.4939 -0.3170 -0.0496 0.0268  403 ASN A N   
3134 C CA  . ASN A 403 ? 0.7807 0.7224 0.5421 -0.3052 -0.0219 0.0228  403 ASN A CA  
3135 C C   . ASN A 403 ? 0.7989 0.7300 0.5503 -0.2783 -0.0096 0.0161  403 ASN A C   
3136 O O   . ASN A 403 ? 0.6844 0.6232 0.4449 -0.2632 0.0090  0.0136  403 ASN A O   
3137 C CB  . ASN A 403 ? 0.7290 0.7199 0.5427 -0.2995 -0.0149 0.0349  403 ASN A CB  
3138 C CG  . ASN A 403 ? 0.8124 0.7988 0.6273 -0.2935 0.0131  0.0329  403 ASN A CG  
3139 O OD1 . ASN A 403 ? 0.8172 0.7679 0.6025 -0.3072 0.0230  0.0251  403 ASN A OD1 
3140 N ND2 . ASN A 403 ? 0.7171 0.7377 0.5636 -0.2708 0.0277  0.0414  403 ASN A ND2 
3141 N N   . SER A 404 ? 0.7123 0.6248 0.4450 -0.2720 -0.0201 0.0133  404 SER A N   
3142 C CA  . SER A 404 ? 0.7320 0.6304 0.4585 -0.2503 -0.0096 0.0051  404 SER A CA  
3143 C C   . SER A 404 ? 0.7618 0.6317 0.4686 -0.2527 0.0086  -0.0055 404 SER A C   
3144 O O   . SER A 404 ? 0.8151 0.6627 0.5021 -0.2717 0.0140  -0.0066 404 SER A O   
3145 C CB  . SER A 404 ? 0.7795 0.6539 0.4871 -0.2473 -0.0207 0.0051  404 SER A CB  
3146 O OG  . SER A 404 ? 0.8087 0.6440 0.4770 -0.2678 -0.0246 0.0032  404 SER A OG  
3147 N N   . ARG A 405 ? 0.7224 0.5920 0.4351 -0.2331 0.0176  -0.0134 405 ARG A N   
3148 C CA  . ARG A 405 ? 0.7163 0.5732 0.4220 -0.2308 0.0328  -0.0206 405 ARG A CA  
3149 C C   . ARG A 405 ? 0.6919 0.5292 0.3949 -0.2191 0.0346  -0.0316 405 ARG A C   
3150 O O   . ARG A 405 ? 0.7239 0.5645 0.4357 -0.2067 0.0272  -0.0354 405 ARG A O   
3151 C CB  . ARG A 405 ? 0.7290 0.6185 0.4520 -0.2172 0.0414  -0.0178 405 ARG A CB  
3152 C CG  . ARG A 405 ? 0.7052 0.6157 0.4403 -0.2291 0.0439  -0.0058 405 ARG A CG  
3153 C CD  . ARG A 405 ? 0.7147 0.6034 0.4351 -0.2463 0.0564  -0.0047 405 ARG A CD  
3154 N NE  . ARG A 405 ? 0.7770 0.6794 0.5105 -0.2631 0.0578  0.0052  405 ARG A NE  
3155 C CZ  . ARG A 405 ? 0.7602 0.6499 0.4888 -0.2755 0.0730  0.0084  405 ARG A CZ  
3156 N NH1 . ARG A 405 ? 0.7057 0.5716 0.4165 -0.2704 0.0888  0.0047  405 ARG A NH1 
3157 N NH2 . ARG A 405 ? 0.7413 0.6430 0.4872 -0.2934 0.0727  0.0163  405 ARG A NH2 
3158 N N   . PHE A 406 ? 0.6970 0.5136 0.3920 -0.2234 0.0455  -0.0360 406 PHE A N   
3159 C CA  . PHE A 406 ? 0.6724 0.4827 0.3773 -0.2113 0.0475  -0.0464 406 PHE A CA  
3160 C C   . PHE A 406 ? 0.6629 0.4938 0.3739 -0.2007 0.0532  -0.0479 406 PHE A C   
3161 O O   . PHE A 406 ? 0.7426 0.5776 0.4472 -0.2072 0.0632  -0.0394 406 PHE A O   
3162 C CB  . PHE A 406 ? 0.7263 0.4990 0.4248 -0.2221 0.0558  -0.0475 406 PHE A CB  
3163 C CG  . PHE A 406 ? 0.7515 0.5044 0.4329 -0.2368 0.0704  -0.0400 406 PHE A CG  
3164 C CD1 . PHE A 406 ? 0.7866 0.5467 0.4759 -0.2330 0.0813  -0.0387 406 PHE A CD1 
3165 C CD2 . PHE A 406 ? 0.7469 0.4751 0.4033 -0.2490 0.0726  -0.0345 406 PHE A CD2 
3166 C CE1 . PHE A 406 ? 0.7795 0.5235 0.4574 -0.2381 0.0955  -0.0325 406 PHE A CE1 
3167 C CE2 . PHE A 406 ? 0.8564 0.5756 0.5011 -0.2468 0.0827  -0.0323 406 PHE A CE2 
3168 C CZ  . PHE A 406 ? 0.8569 0.5840 0.5158 -0.2399 0.0942  -0.0321 406 PHE A CZ  
3169 N N   . CYS A 407 ? 0.6377 0.4796 0.3587 -0.1840 0.0464  -0.0588 407 CYS A N   
3170 C CA  . CYS A 407 ? 0.6777 0.5379 0.3988 -0.1704 0.0481  -0.0612 407 CYS A CA  
3171 C C   . CYS A 407 ? 0.6372 0.4869 0.3716 -0.1684 0.0425  -0.0715 407 CYS A C   
3172 O O   . CYS A 407 ? 0.6734 0.5221 0.4166 -0.1607 0.0298  -0.0857 407 CYS A O   
3173 C CB  . CYS A 407 ? 0.6499 0.5345 0.3660 -0.1504 0.0424  -0.0658 407 CYS A CB  
3174 S SG  . CYS A 407 ? 0.6600 0.5654 0.3631 -0.1301 0.0452  -0.0659 407 CYS A SG  
3175 N N   . THR A 408 ? 0.6855 0.5270 0.4250 -0.1755 0.0525  -0.0642 408 THR A N   
3176 C CA  . THR A 408 ? 0.6367 0.4683 0.3992 -0.1772 0.0494  -0.0698 408 THR A CA  
3177 C C   . THR A 408 ? 0.6101 0.4598 0.3801 -0.1672 0.0497  -0.0656 408 THR A C   
3178 O O   . THR A 408 ? 0.6887 0.5452 0.4444 -0.1648 0.0623  -0.0528 408 THR A O   
3179 C CB  . THR A 408 ? 0.7039 0.5027 0.4711 -0.1947 0.0648  -0.0617 408 THR A CB  
3180 O OG1 . THR A 408 ? 0.6652 0.4549 0.4639 -0.1958 0.0622  -0.0674 408 THR A OG1 
3181 C CG2 . THR A 408 ? 0.6383 0.4281 0.3938 -0.2014 0.0847  -0.0467 408 THR A CG2 
3182 N N   . PRO A 409 ? 0.6032 0.4614 0.3983 -0.1615 0.0354  -0.0752 409 PRO A N   
3183 C CA  . PRO A 409 ? 0.5941 0.4732 0.3993 -0.1505 0.0318  -0.0694 409 PRO A CA  
3184 C C   . PRO A 409 ? 0.6726 0.5381 0.4929 -0.1594 0.0549  -0.0508 409 PRO A C   
3185 O O   . PRO A 409 ? 0.6470 0.4892 0.4882 -0.1726 0.0654  -0.0486 409 PRO A O   
3186 C CB  . PRO A 409 ? 0.6575 0.5473 0.4920 -0.1467 0.0064  -0.0868 409 PRO A CB  
3187 C CG  . PRO A 409 ? 0.6762 0.5516 0.5049 -0.1511 -0.0026 -0.1039 409 PRO A CG  
3188 C CD  . PRO A 409 ? 0.6494 0.5005 0.4660 -0.1639 0.0194  -0.0924 409 PRO A CD  
3189 N N   . ALA A 410 ? 0.6278 0.5046 0.4359 -0.1503 0.0660  -0.0362 410 ALA A N   
3190 C CA  . ALA A 410 ? 0.6961 0.5563 0.5155 -0.1565 0.0918  -0.0176 410 ALA A CA  
3191 C C   . ALA A 410 ? 0.7121 0.5763 0.5781 -0.1562 0.0887  -0.0150 410 ALA A C   
3192 O O   . ALA A 410 ? 0.7442 0.5827 0.6261 -0.1660 0.1123  -0.0037 410 ALA A O   
3193 C CB  . ALA A 410 ? 0.6486 0.5214 0.4496 -0.1438 0.1043  -0.0018 410 ALA A CB  
3194 N N   . SER A 411 ? 0.6808 0.5759 0.5701 -0.1453 0.0600  -0.0256 411 SER A N   
3195 C CA  . SER A 411 ? 0.6846 0.5916 0.6290 -0.1454 0.0532  -0.0221 411 SER A CA  
3196 C C   . SER A 411 ? 0.6636 0.5421 0.6383 -0.1630 0.0649  -0.0253 411 SER A C   
3197 O O   . SER A 411 ? 0.7481 0.6277 0.7725 -0.1655 0.0738  -0.0149 411 SER A O   
3198 C CB  . SER A 411 ? 0.6644 0.6080 0.6247 -0.1340 0.0134  -0.0381 411 SER A CB  
3199 O OG  . SER A 411 ? 0.6877 0.6236 0.6387 -0.1407 -0.0057 -0.0625 411 SER A OG  
3200 N N   . GLN A 412 ? 0.6650 0.5187 0.6130 -0.1735 0.0669  -0.0371 412 GLN A N   
3201 C CA  . GLN A 412 ? 0.7243 0.5477 0.6944 -0.1877 0.0790  -0.0390 412 GLN A CA  
3202 C C   . GLN A 412 ? 0.7845 0.5679 0.7367 -0.1968 0.1165  -0.0216 412 GLN A C   
3203 O O   . GLN A 412 ? 0.8352 0.5895 0.8038 -0.2061 0.1323  -0.0188 412 GLN A O   
3204 C CB  . GLN A 412 ? 0.6852 0.4984 0.6331 -0.1925 0.0643  -0.0576 412 GLN A CB  
3205 C CG  . GLN A 412 ? 0.6600 0.5009 0.6237 -0.1852 0.0297  -0.0787 412 GLN A CG  
3206 C CD  . GLN A 412 ? 0.6785 0.5051 0.6175 -0.1875 0.0204  -0.0949 412 GLN A CD  
3207 O OE1 . GLN A 412 ? 0.7977 0.6355 0.7452 -0.1832 -0.0039 -0.1144 412 GLN A OE1 
3208 N NE2 . GLN A 412 ? 0.6705 0.4709 0.5777 -0.1940 0.0394  -0.0869 412 GLN A NE2 
3209 N N   . CYS A 413 ? 0.6677 0.4049 1.0121 -0.1531 0.1863  -0.1216 413 CYS A N   
3210 C CA  . CYS A 413 ? 0.6757 0.4086 0.9935 -0.1490 0.1851  -0.0891 413 CYS A CA  
3211 C C   . CYS A 413 ? 0.7261 0.4841 1.0397 -0.1693 0.1940  -0.0870 413 CYS A C   
3212 O O   . CYS A 413 ? 0.6826 0.4841 1.0051 -0.1782 0.1957  -0.1118 413 CYS A O   
3213 C CB  . CYS A 413 ? 0.6301 0.3837 0.9330 -0.1329 0.1777  -0.0893 413 CYS A CB  
3214 S SG  . CYS A 413 ? 0.6723 0.4189 0.9402 -0.1255 0.1758  -0.0503 413 CYS A SG  
3215 N N   . PRO A 414 ? 0.7417 0.4779 1.0413 -0.1768 0.1989  -0.0582 414 PRO A N   
3216 C CA  . PRO A 414 ? 0.7145 0.4793 1.0127 -0.1968 0.2090  -0.0579 414 PRO A CA  
3217 C C   . PRO A 414 ? 0.5957 0.4066 0.8819 -0.1937 0.2094  -0.0613 414 PRO A C   
3218 O O   . PRO A 414 ? 0.6562 0.5058 0.9502 -0.2079 0.2162  -0.0722 414 PRO A O   
3219 C CB  . PRO A 414 ? 0.7172 0.4457 0.9968 -0.2027 0.2130  -0.0224 414 PRO A CB  
3220 C CG  . PRO A 414 ? 0.8253 0.5192 1.0862 -0.1808 0.2020  0.0003  414 PRO A CG  
3221 C CD  . PRO A 414 ? 0.7362 0.4257 1.0188 -0.1673 0.1944  -0.0244 414 PRO A CD  
3222 N N   . ILE A 415 ? 0.5872 0.3965 0.8561 -0.1754 0.2020  -0.0525 415 ILE A N   
3223 C CA  . ILE A 415 ? 0.6046 0.4563 0.8585 -0.1685 0.1997  -0.0540 415 ILE A CA  
3224 C C   . ILE A 415 ? 0.6037 0.4845 0.8593 -0.1530 0.1858  -0.0772 415 ILE A C   
3225 O O   . ILE A 415 ? 0.5390 0.4450 0.7721 -0.1367 0.1762  -0.0729 415 ILE A O   
3226 C CB  . ILE A 415 ? 0.6440 0.4807 0.8614 -0.1545 0.1966  -0.0221 415 ILE A CB  
3227 C CG1 . ILE A 415 ? 0.6694 0.4669 0.8772 -0.1367 0.1857  -0.0090 415 ILE A CG1 
3228 C CG2 . ILE A 415 ? 0.6414 0.4621 0.8506 -0.1717 0.2111  0.0003  415 ILE A CG2 
3229 C CD1 . ILE A 415 ? 0.7260 0.5199 0.8973 -0.1201 0.1778  0.0160  415 ILE A CD1 
3230 N N   . ILE A 416 ? 0.5851 0.4615 0.8659 -0.1589 0.1851  -0.1019 416 ILE A N   
3231 C CA  . ILE A 416 ? 0.5768 0.4848 0.8566 -0.1474 0.1734  -0.1246 416 ILE A CA  
3232 C C   . ILE A 416 ? 0.5649 0.5298 0.8402 -0.1488 0.1688  -0.1352 416 ILE A C   
3233 O O   . ILE A 416 ? 0.5585 0.5456 0.8517 -0.1662 0.1764  -0.1444 416 ILE A O   
3234 C CB  . ILE A 416 ? 0.5389 0.4365 0.8476 -0.1571 0.1759  -0.1536 416 ILE A CB  
3235 C CG1 . ILE A 416 ? 0.5433 0.4653 0.8437 -0.1426 0.1646  -0.1718 416 ILE A CG1 
3236 C CG2 . ILE A 416 ? 0.5568 0.4796 0.8908 -0.1811 0.1834  -0.1765 416 ILE A CG2 
3237 C CD1 . ILE A 416 ? 0.5393 0.4359 0.8215 -0.1210 0.1582  -0.1532 416 ILE A CD1 
3238 N N   . ASP A 417 ? 0.5494 0.5381 0.8025 -0.1304 0.1562  -0.1333 417 ASP A N   
3239 C CA  . ASP A 417 ? 0.5413 0.5795 0.7887 -0.1271 0.1497  -0.1385 417 ASP A CA  
3240 C C   . ASP A 417 ? 0.5309 0.6083 0.8027 -0.1411 0.1478  -0.1689 417 ASP A C   
3241 O O   . ASP A 417 ? 0.5160 0.5905 0.7959 -0.1449 0.1453  -0.1883 417 ASP A O   
3242 C CB  . ASP A 417 ? 0.5331 0.5820 0.7518 -0.1053 0.1360  -0.1294 417 ASP A CB  
3243 C CG  . ASP A 417 ? 0.5309 0.6204 0.7419 -0.0976 0.1292  -0.1274 417 ASP A CG  
3244 O OD1 . ASP A 417 ? 0.5293 0.6146 0.7320 -0.0935 0.1340  -0.1113 417 ASP A OD1 
3245 O OD2 . ASP A 417 ? 0.5518 0.6781 0.7651 -0.0950 0.1187  -0.1421 417 ASP A OD2 
3246 N N   . PRO A 418 ? 0.5054 0.6233 0.7906 -0.1491 0.1488  -0.1757 418 PRO A N   
3247 C CA  . PRO A 418 ? 0.5446 0.7071 0.8533 -0.1625 0.1443  -0.2053 418 PRO A CA  
3248 C C   . PRO A 418 ? 0.5317 0.7242 0.8249 -0.1499 0.1272  -0.2169 418 PRO A C   
3249 O O   . PRO A 418 ? 0.6306 0.8596 0.9388 -0.1611 0.1217  -0.2427 418 PRO A O   
3250 C CB  . PRO A 418 ? 0.4955 0.6995 0.8196 -0.1679 0.1469  -0.2046 418 PRO A CB  
3251 C CG  . PRO A 418 ? 0.5585 0.7469 0.8582 -0.1497 0.1482  -0.1761 418 PRO A CG  
3252 C CD  . PRO A 418 ? 0.5780 0.7059 0.8593 -0.1466 0.1546  -0.1583 418 PRO A CD  
3253 N N   . ALA A 419 ? 0.5381 0.7174 0.8006 -0.1289 0.1188  -0.1987 419 ALA A N   
3254 C CA  . ALA A 419 ? 0.5862 0.7902 0.8294 -0.1182 0.1039  -0.2055 419 ALA A CA  
3255 C C   . ALA A 419 ? 0.5907 0.7598 0.8178 -0.1125 0.1052  -0.2037 419 ALA A C   
3256 O O   . ALA A 419 ? 0.6073 0.7894 0.8116 -0.1019 0.0949  -0.2020 419 ALA A O   
3257 C CB  . ALA A 419 ? 0.5596 0.7851 0.7819 -0.0990 0.0915  -0.1869 419 ALA A CB  
3258 N N   . TRP A 420 ? 0.5640 0.6899 0.8040 -0.1191 0.1178  -0.2032 420 TRP A N   
3259 C CA  . TRP A 420 ? 0.5929 0.6876 0.8233 -0.1113 0.1192  -0.2016 420 TRP A CA  
3260 C C   . TRP A 420 ? 0.5234 0.6408 0.7559 -0.1168 0.1161  -0.2302 420 TRP A C   
3261 O O   . TRP A 420 ? 0.4929 0.5996 0.7135 -0.1081 0.1152  -0.2305 420 TRP A O   
3262 C CB  . TRP A 420 ? 0.5341 0.5779 0.7819 -0.1160 0.1318  -0.1947 420 TRP A CB  
3263 C CG  . TRP A 420 ? 0.5582 0.5921 0.8373 -0.1339 0.1411  -0.2215 420 TRP A CG  
3264 C CD1 . TRP A 420 ? 0.5304 0.5718 0.8334 -0.1535 0.1482  -0.2336 420 TRP A CD1 
3265 C CD2 . TRP A 420 ? 0.5837 0.5967 0.8759 -0.1346 0.1454  -0.2412 420 TRP A CD2 
3266 N NE1 . TRP A 420 ? 0.5421 0.5654 0.8713 -0.1673 0.1561  -0.2597 420 TRP A NE1 
3267 C CE2 . TRP A 420 ? 0.5545 0.5596 0.8779 -0.1549 0.1547  -0.2654 420 TRP A CE2 
3268 C CE3 . TRP A 420 ? 0.5497 0.5518 0.8329 -0.1204 0.1431  -0.2425 420 TRP A CE3 
3269 C CZ2 . TRP A 420 ? 0.5862 0.5735 0.9267 -0.1555 0.1602  -0.2860 420 TRP A CZ2 
3270 C CZ3 . TRP A 420 ? 0.5443 0.5292 0.8504 -0.1245 0.1504  -0.2686 420 TRP A CZ3 
3271 C CH2 . TRP A 420 ? 0.5581 0.5362 0.8909 -0.1400 0.1581  -0.2879 420 TRP A CH2 
3272 N N   . GLU A 421 ? 0.5301 0.6827 0.7776 -0.1319 0.1146  -0.2555 421 GLU A N   
3273 C CA  . GLU A 421 ? 0.5461 0.7274 0.7922 -0.1393 0.1111  -0.2855 421 GLU A CA  
3274 C C   . GLU A 421 ? 0.6021 0.8399 0.8283 -0.1377 0.0955  -0.2886 421 GLU A C   
3275 O O   . GLU A 421 ? 0.5944 0.8646 0.8155 -0.1460 0.0910  -0.3138 421 GLU A O   
3276 C CB  . GLU A 421 ? 0.5797 0.7554 0.8597 -0.1604 0.1214  -0.3176 421 GLU A CB  
3277 C CG  . GLU A 421 ? 0.6236 0.7420 0.9230 -0.1606 0.1354  -0.3192 421 GLU A CG  
3278 C CD  . GLU A 421 ? 0.6284 0.7407 0.9545 -0.1743 0.1447  -0.3451 421 GLU A CD  
3279 O OE1 . GLU A 421 ? 0.6447 0.7656 0.9863 -0.1874 0.1473  -0.3486 421 GLU A OE1 
3280 O OE2 . GLU A 421 ? 0.5675 0.6691 0.8980 -0.1693 0.1494  -0.3586 421 GLU A OE2 
3281 N N   . SER A 422 ? 0.6368 0.8872 0.8514 -0.1267 0.0867  -0.2640 422 SER A N   
3282 C CA  . SER A 422 ? 0.6206 0.9214 0.8178 -0.1219 0.0697  -0.2627 422 SER A CA  
3283 C C   . SER A 422 ? 0.6120 0.9206 0.7749 -0.1136 0.0621  -0.2590 422 SER A C   
3284 O O   . SER A 422 ? 0.6044 0.8816 0.7493 -0.1009 0.0644  -0.2376 422 SER A O   
3285 C CB  . SER A 422 ? 0.6317 0.9362 0.8255 -0.1079 0.0631  -0.2357 422 SER A CB  
3286 O OG  . SER A 422 ? 0.6673 0.9727 0.8924 -0.1176 0.0715  -0.2403 422 SER A OG  
3287 N N   . PRO A 423 ? 0.6369 0.9886 0.7889 -0.1219 0.0532  -0.2793 423 PRO A N   
3288 C CA  . PRO A 423 ? 0.6933 1.0548 0.8094 -0.1167 0.0476  -0.2749 423 PRO A CA  
3289 C C   . PRO A 423 ? 0.6695 1.0315 0.7555 -0.0989 0.0346  -0.2398 423 PRO A C   
3290 O O   . PRO A 423 ? 0.7558 1.1121 0.8126 -0.0942 0.0335  -0.2290 423 PRO A O   
3291 C CB  . PRO A 423 ? 0.7337 1.1479 0.8443 -0.1316 0.0397  -0.3046 423 PRO A CB  
3292 C CG  . PRO A 423 ? 0.6613 1.1023 0.7998 -0.1385 0.0331  -0.3138 423 PRO A CG  
3293 C CD  . PRO A 423 ? 0.6588 1.0546 0.8298 -0.1385 0.0482  -0.3082 423 PRO A CD  
3294 N N   . GLU A 424 ? 0.6210 0.9897 0.7149 -0.0894 0.0255  -0.2227 424 GLU A N   
3295 C CA  . GLU A 424 ? 0.6234 0.9871 0.6921 -0.0713 0.0133  -0.1905 424 GLU A CA  
3296 C C   . GLU A 424 ? 0.6190 0.9311 0.6849 -0.0602 0.0229  -0.1682 424 GLU A C   
3297 O O   . GLU A 424 ? 0.5771 0.8774 0.6209 -0.0465 0.0148  -0.1429 424 GLU A O   
3298 C CB  . GLU A 424 ? 0.6131 1.0082 0.6943 -0.0631 -0.0010 -0.1836 424 GLU A CB  
3299 C CG  . GLU A 424 ? 0.6550 1.0419 0.7743 -0.0654 0.0089  -0.1898 424 GLU A CG  
3300 C CD  . GLU A 424 ? 0.7330 1.1419 0.8814 -0.0867 0.0164  -0.2225 424 GLU A CD  
3301 O OE1 . GLU A 424 ? 0.6845 1.0772 0.8319 -0.0993 0.0273  -0.2397 424 GLU A OE1 
3302 O OE2 . GLU A 424 ? 0.8192 1.2625 0.9939 -0.0910 0.0118  -0.2325 424 GLU A OE2 
3303 N N   . GLY A 425 ? 0.5949 0.8754 0.6821 -0.0661 0.0390  -0.1765 425 GLY A N   
3304 C CA  . GLY A 425 ? 0.5671 0.8023 0.6512 -0.0565 0.0467  -0.1562 425 GLY A CA  
3305 C C   . GLY A 425 ? 0.5589 0.7863 0.6515 -0.0463 0.0445  -0.1397 425 GLY A C   
3306 O O   . GLY A 425 ? 0.5512 0.8093 0.6545 -0.0448 0.0368  -0.1429 425 GLY A O   
3307 N N   . VAL A 426 ? 0.5230 0.7114 0.6114 -0.0390 0.0515  -0.1231 426 VAL A N   
3308 C CA  . VAL A 426 ? 0.5099 0.6877 0.6038 -0.0298 0.0523  -0.1089 426 VAL A CA  
3309 C C   . VAL A 426 ? 0.5595 0.7196 0.6269 -0.0146 0.0445  -0.0867 426 VAL A C   
3310 O O   . VAL A 426 ? 0.5044 0.6435 0.5536 -0.0140 0.0449  -0.0793 426 VAL A O   
3311 C CB  . VAL A 426 ? 0.4686 0.6160 0.5785 -0.0360 0.0675  -0.1085 426 VAL A CB  
3312 C CG1 . VAL A 426 ? 0.4465 0.6084 0.5852 -0.0524 0.0755  -0.1299 426 VAL A CG1 
3313 C CG2 . VAL A 426 ? 0.4887 0.5999 0.5861 -0.0347 0.0724  -0.1005 426 VAL A CG2 
3314 N N   . PRO A 427 ? 0.5162 0.6841 0.5831 -0.0025 0.0376  -0.0769 427 PRO A N   
3315 C CA  . PRO A 427 ? 0.5281 0.6746 0.5713 0.0116  0.0301  -0.0572 427 PRO A CA  
3316 C C   . PRO A 427 ? 0.5338 0.6409 0.5706 0.0132  0.0401  -0.0478 427 PRO A C   
3317 O O   . PRO A 427 ? 0.5445 0.6455 0.5948 0.0125  0.0493  -0.0499 427 PRO A O   
3318 C CB  . PRO A 427 ? 0.5632 0.7311 0.6158 0.0250  0.0211  -0.0540 427 PRO A CB  
3319 C CG  . PRO A 427 ? 0.5229 0.7132 0.6065 0.0174  0.0304  -0.0697 427 PRO A CG  
3320 C CD  . PRO A 427 ? 0.4941 0.6921 0.5853 -0.0010 0.0367  -0.0852 427 PRO A CD  
3321 N N   . ILE A 428 ? 0.5416 0.6249 0.5568 0.0140  0.0380  -0.0374 428 ILE A N   
3322 C CA  . ILE A 428 ? 0.4832 0.5324 0.4901 0.0152  0.0445  -0.0283 428 ILE A CA  
3323 C C   . ILE A 428 ? 0.5328 0.5665 0.5260 0.0279  0.0388  -0.0161 428 ILE A C   
3324 O O   . ILE A 428 ? 0.5516 0.5832 0.5298 0.0337  0.0287  -0.0075 428 ILE A O   
3325 C CB  . ILE A 428 ? 0.4811 0.5168 0.4766 0.0087  0.0455  -0.0259 428 ILE A CB  
3326 C CG1 . ILE A 428 ? 0.4937 0.5442 0.5054 -0.0022 0.0517  -0.0415 428 ILE A CG1 
3327 C CG2 . ILE A 428 ? 0.4630 0.4681 0.4516 0.0101  0.0498  -0.0167 428 ILE A CG2 
3328 C CD1 . ILE A 428 ? 0.4824 0.5250 0.5156 -0.0068 0.0620  -0.0483 428 ILE A CD1 
3329 N N   . GLU A 429 ? 0.5079 0.5296 0.5057 0.0317  0.0457  -0.0155 429 GLU A N   
3330 C CA  . GLU A 429 ? 0.5406 0.5454 0.5273 0.0436  0.0426  -0.0081 429 GLU A CA  
3331 C C   . GLU A 429 ? 0.5507 0.5237 0.5202 0.0413  0.0462  -0.0012 429 GLU A C   
3332 O O   . GLU A 429 ? 0.5377 0.4928 0.4954 0.0495  0.0434  0.0030  429 GLU A O   
3333 C CB  . GLU A 429 ? 0.5143 0.5353 0.5182 0.0506  0.0481  -0.0156 429 GLU A CB  
3334 C CG  . GLU A 429 ? 0.5988 0.6569 0.6235 0.0546  0.0425  -0.0233 429 GLU A CG  
3335 C CD  . GLU A 429 ? 0.5740 0.6521 0.6193 0.0628  0.0483  -0.0315 429 GLU A CD  
3336 O OE1 . GLU A 429 ? 0.5726 0.6349 0.6117 0.0741  0.0500  -0.0292 429 GLU A OE1 
3337 O OE2 . GLU A 429 ? 0.6022 0.7134 0.6714 0.0570  0.0519  -0.0422 429 GLU A OE2 
3338 N N   . GLY A 430 ? 0.5252 0.4914 0.4946 0.0309  0.0513  -0.0010 430 GLY A N   
3339 C CA  . GLY A 430 ? 0.5267 0.4681 0.4812 0.0286  0.0524  0.0058  430 GLY A CA  
3340 C C   . GLY A 430 ? 0.5231 0.4625 0.4809 0.0197  0.0531  0.0069  430 GLY A C   
3341 O O   . GLY A 430 ? 0.5108 0.4627 0.4849 0.0145  0.0576  0.0007  430 GLY A O   
3342 N N   . ILE A 431 ? 0.4947 0.4189 0.4395 0.0181  0.0487  0.0133  431 ILE A N   
3343 C CA  . ILE A 431 ? 0.5043 0.4286 0.4550 0.0118  0.0488  0.0139  431 ILE A CA  
3344 C C   . ILE A 431 ? 0.4940 0.4018 0.4367 0.0114  0.0479  0.0206  431 ILE A C   
3345 O O   . ILE A 431 ? 0.5617 0.4570 0.4876 0.0132  0.0441  0.0244  431 ILE A O   
3346 C CB  . ILE A 431 ? 0.5020 0.4321 0.4472 0.0082  0.0438  0.0147  431 ILE A CB  
3347 C CG1 . ILE A 431 ? 0.4678 0.4179 0.4174 0.0077  0.0435  0.0089  431 ILE A CG1 
3348 C CG2 . ILE A 431 ? 0.4753 0.4090 0.4300 0.0028  0.0449  0.0134  431 ILE A CG2 
3349 C CD1 . ILE A 431 ? 0.5530 0.5102 0.4915 0.0026  0.0393  0.0120  431 ILE A CD1 
3350 N N   . ILE A 432 ? 0.5062 0.4137 0.4612 0.0094  0.0506  0.0217  432 ILE A N   
3351 C CA  . ILE A 432 ? 0.5208 0.4160 0.4685 0.0096  0.0480  0.0301  432 ILE A CA  
3352 C C   . ILE A 432 ? 0.4629 0.3620 0.4222 0.0084  0.0432  0.0314  432 ILE A C   
3353 O O   . ILE A 432 ? 0.4957 0.4034 0.4758 0.0081  0.0464  0.0257  432 ILE A O   
3354 C CB  . ILE A 432 ? 0.4922 0.3816 0.4440 0.0095  0.0546  0.0342  432 ILE A CB  
3355 C CG1 . ILE A 432 ? 0.5190 0.4132 0.4672 0.0098  0.0618  0.0292  432 ILE A CG1 
3356 C CG2 . ILE A 432 ? 0.5668 0.4444 0.5027 0.0097  0.0504  0.0454  432 ILE A CG2 
3357 C CD1 . ILE A 432 ? 0.5379 0.4298 0.4927 0.0061  0.0710  0.0325  432 ILE A CD1 
3358 N N   . PHE A 433 ? 0.4700 0.3648 0.4179 0.0074  0.0356  0.0367  433 PHE A N   
3359 C CA  . PHE A 433 ? 0.4635 0.3656 0.4249 0.0073  0.0298  0.0388  433 PHE A CA  
3360 C C   . PHE A 433 ? 0.5055 0.3992 0.4603 0.0102  0.0237  0.0496  433 PHE A C   
3361 O O   . PHE A 433 ? 0.5020 0.3854 0.4340 0.0094  0.0233  0.0541  433 PHE A O   
3362 C CB  . PHE A 433 ? 0.4743 0.3840 0.4303 0.0015  0.0246  0.0361  433 PHE A CB  
3363 C CG  . PHE A 433 ? 0.5227 0.4409 0.4807 -0.0026 0.0296  0.0292  433 PHE A CG  
3364 C CD1 . PHE A 433 ? 0.5223 0.4564 0.5009 -0.0024 0.0352  0.0216  433 PHE A CD1 
3365 C CD2 . PHE A 433 ? 0.5379 0.4474 0.4761 -0.0064 0.0283  0.0302  433 PHE A CD2 
3366 C CE1 . PHE A 433 ? 0.5284 0.4735 0.5042 -0.0074 0.0393  0.0159  433 PHE A CE1 
3367 C CE2 . PHE A 433 ? 0.5785 0.4954 0.5152 -0.0101 0.0313  0.0275  433 PHE A CE2 
3368 C CZ  . PHE A 433 ? 0.5108 0.4475 0.4644 -0.0113 0.0367  0.0207  433 PHE A CZ  
3369 N N   . GLY A 434 ? 0.5057 0.4053 0.4805 0.0142  0.0189  0.0534  434 GLY A N   
3370 C CA  . GLY A 434 ? 0.5230 0.4158 0.4912 0.0180  0.0107  0.0668  434 GLY A CA  
3371 C C   . GLY A 434 ? 0.5242 0.4247 0.5222 0.0256  0.0045  0.0705  434 GLY A C   
3372 O O   . GLY A 434 ? 0.5177 0.4261 0.5435 0.0284  0.0100  0.0608  434 GLY A O   
3373 N N   . GLY A 435 ? 0.5794 0.4791 0.5714 0.0297  -0.0075 0.0840  435 GLY A N   
3374 C CA  . GLY A 435 ? 0.5169 0.4226 0.5382 0.0402  -0.0162 0.0908  435 GLY A CA  
3375 C C   . GLY A 435 ? 0.5431 0.4427 0.5468 0.0442  -0.0299 0.1110  435 GLY A C   
3376 O O   . GLY A 435 ? 0.5214 0.4117 0.4890 0.0375  -0.0299 0.1181  435 GLY A O   
3377 N N   . ARG A 436 ? 0.4788 0.3860 0.5086 0.0559  -0.0420 0.1197  436 ARG A N   
3378 C CA  . ARG A 436 ? 0.5830 0.4874 0.5973 0.0613  -0.0585 0.1418  436 ARG A CA  
3379 C C   . ARG A 436 ? 0.5603 0.4923 0.5621 0.0563  -0.0731 0.1383  436 ARG A C   
3380 O O   . ARG A 436 ? 0.5990 0.5569 0.6313 0.0617  -0.0827 0.1320  436 ARG A O   
3381 C CB  . ARG A 436 ? 0.5897 0.4880 0.6400 0.0783  -0.0668 0.1546  436 ARG A CB  
3382 C CG  . ARG A 436 ? 0.6031 0.4686 0.6639 0.0811  -0.0529 0.1589  436 ARG A CG  
3383 C CD  . ARG A 436 ? 0.6618 0.5169 0.7645 0.0993  -0.0602 0.1683  436 ARG A CD  
3384 N NE  . ARG A 436 ? 0.7036 0.5224 0.8141 0.0991  -0.0466 0.1726  436 ARG A NE  
3385 C CZ  . ARG A 436 ? 0.7038 0.4915 0.7954 0.0991  -0.0490 0.1987  436 ARG A CZ  
3386 N NH1 . ARG A 436 ? 0.6760 0.4653 0.7372 0.1005  -0.0651 0.2239  436 ARG A NH1 
3387 N NH2 . ARG A 436 ? 0.7784 0.5335 0.8804 0.0959  -0.0346 0.1996  436 ARG A NH2 
3388 N N   . ARG A 437 ? 0.5052 0.4336 0.4638 0.0450  -0.0741 0.1402  437 ARG A N   
3389 C CA  . ARG A 437 ? 0.6072 0.5584 0.5486 0.0383  -0.0892 0.1373  437 ARG A CA  
3390 C C   . ARG A 437 ? 0.6235 0.5703 0.5296 0.0389  -0.1020 0.1577  437 ARG A C   
3391 O O   . ARG A 437 ? 0.6230 0.5522 0.4908 0.0311  -0.0928 0.1608  437 ARG A O   
3392 C CB  . ARG A 437 ? 0.5060 0.4572 0.4258 0.0231  -0.0795 0.1178  437 ARG A CB  
3393 C CG  . ARG A 437 ? 0.6061 0.5653 0.5550 0.0200  -0.0693 0.0999  437 ARG A CG  
3394 C CD  . ARG A 437 ? 0.5892 0.5787 0.5774 0.0248  -0.0801 0.0964  437 ARG A CD  
3395 N NE  . ARG A 437 ? 0.5579 0.5708 0.5375 0.0171  -0.0966 0.0943  437 ARG A NE  
3396 C CZ  . ARG A 437 ? 0.5771 0.6003 0.5514 0.0020  -0.0952 0.0791  437 ARG A CZ  
3397 N NH1 . ARG A 437 ? 0.4359 0.4470 0.4100 -0.0060 -0.0790 0.0672  437 ARG A NH1 
3398 N NH2 . ARG A 437 ? 0.5379 0.5836 0.5066 -0.0059 -0.1113 0.0764  437 ARG A NH2 
3399 N N   . PRO A 438 ? 0.6439 0.6085 0.5607 0.0482  -0.1232 0.1724  438 PRO A N   
3400 C CA  . PRO A 438 ? 0.7269 0.6884 0.6054 0.0485  -0.1369 0.1951  438 PRO A CA  
3401 C C   . PRO A 438 ? 0.6641 0.6395 0.4977 0.0329  -0.1425 0.1857  438 PRO A C   
3402 O O   . PRO A 438 ? 0.7210 0.6934 0.5134 0.0296  -0.1496 0.2016  438 PRO A O   
3403 C CB  . PRO A 438 ? 0.6609 0.6420 0.5709 0.0649  -0.1605 0.2118  438 PRO A CB  
3404 C CG  . PRO A 438 ? 0.6100 0.6196 0.5649 0.0663  -0.1620 0.1892  438 PRO A CG  
3405 C CD  . PRO A 438 ? 0.5663 0.5577 0.5314 0.0594  -0.1359 0.1691  438 PRO A CD  
3406 N N   . ALA A 439 ? 0.6713 0.6606 0.5102 0.0222  -0.1389 0.1604  439 ALA A N   
3407 C CA  . ALA A 439 ? 0.6666 0.6681 0.4674 0.0071  -0.1453 0.1481  439 ALA A CA  
3408 C C   . ALA A 439 ? 0.6374 0.6313 0.4401 -0.0051 -0.1295 0.1210  439 ALA A C   
3409 O O   . ALA A 439 ? 0.6611 0.6529 0.4994 -0.0026 -0.1200 0.1122  439 ALA A O   
3410 C CB  . ALA A 439 ? 0.5994 0.6380 0.4080 0.0069  -0.1720 0.1501  439 ALA A CB  
3411 N N   . GLY A 440 ? 0.6696 0.6589 0.4327 -0.0182 -0.1267 0.1081  440 GLY A N   
3412 C CA  . GLY A 440 ? 0.6693 0.6517 0.4322 -0.0305 -0.1170 0.0829  440 GLY A CA  
3413 C C   . GLY A 440 ? 0.7072 0.6600 0.4693 -0.0297 -0.0936 0.0748  440 GLY A C   
3414 O O   . GLY A 440 ? 0.7656 0.7048 0.5073 -0.0386 -0.0850 0.0575  440 GLY A O   
3415 N N   . VAL A 441 ? 0.6685 0.6118 0.4542 -0.0187 -0.0838 0.0858  441 VAL A N   
3416 C CA  . VAL A 441 ? 0.6790 0.6007 0.4717 -0.0174 -0.0639 0.0778  441 VAL A CA  
3417 C C   . VAL A 441 ? 0.6649 0.5706 0.4291 -0.0152 -0.0521 0.0840  441 VAL A C   
3418 O O   . VAL A 441 ? 0.6497 0.5555 0.4120 -0.0091 -0.0540 0.1024  441 VAL A O   
3419 C CB  . VAL A 441 ? 0.6078 0.5311 0.4412 -0.0088 -0.0590 0.0826  441 VAL A CB  
3420 C CG1 . VAL A 441 ? 0.5642 0.4697 0.4026 -0.0088 -0.0408 0.0734  441 VAL A CG1 
3421 C CG2 . VAL A 441 ? 0.5929 0.5385 0.4551 -0.0117 -0.0697 0.0769  441 VAL A CG2 
3422 N N   . PRO A 442 ? 0.6774 0.5697 0.4224 -0.0199 -0.0397 0.0693  442 PRO A N   
3423 C CA  . PRO A 442 ? 0.7097 0.5932 0.4285 -0.0192 -0.0272 0.0725  442 PRO A CA  
3424 C C   . PRO A 442 ? 0.6744 0.5490 0.4144 -0.0120 -0.0137 0.0815  442 PRO A C   
3425 O O   . PRO A 442 ? 0.6456 0.5192 0.4185 -0.0071 -0.0131 0.0827  442 PRO A O   
3426 C CB  . PRO A 442 ? 0.7789 0.6531 0.4798 -0.0244 -0.0185 0.0499  442 PRO A CB  
3427 C CG  . PRO A 442 ? 0.6781 0.5466 0.4052 -0.0250 -0.0208 0.0393  442 PRO A CG  
3428 C CD  . PRO A 442 ? 0.7081 0.5926 0.4549 -0.0261 -0.0365 0.0491  442 PRO A CD  
3429 N N   . LEU A 443 ? 0.6959 0.5661 0.4156 -0.0131 -0.0019 0.0864  443 LEU A N   
3430 C CA  . LEU A 443 ? 0.6578 0.5210 0.3955 -0.0092 0.0108  0.0959  443 LEU A CA  
3431 C C   . LEU A 443 ? 0.6452 0.5041 0.4117 -0.0053 0.0202  0.0819  443 LEU A C   
3432 O O   . LEU A 443 ? 0.6459 0.5025 0.4408 -0.0014 0.0230  0.0873  443 LEU A O   
3433 C CB  . LEU A 443 ? 0.6589 0.5216 0.3686 -0.0144 0.0243  0.1002  443 LEU A CB  
3434 C CG  . LEU A 443 ? 0.6992 0.5560 0.4263 -0.0141 0.0398  0.1077  443 LEU A CG  
3435 C CD1 . LEU A 443 ? 0.6936 0.5420 0.4395 -0.0112 0.0325  0.1297  443 LEU A CD1 
3436 C CD2 . LEU A 443 ? 0.7423 0.6035 0.4405 -0.0218 0.0553  0.1088  443 LEU A CD2 
3437 N N   . VAL A 444 ? 0.5914 0.4485 0.3505 -0.0061 0.0246  0.0638  444 VAL A N   
3438 C CA  . VAL A 444 ? 0.5622 0.4155 0.3444 -0.0017 0.0319  0.0528  444 VAL A CA  
3439 C C   . VAL A 444 ? 0.6271 0.4737 0.3994 -0.0023 0.0297  0.0363  444 VAL A C   
3440 O O   . VAL A 444 ? 0.6206 0.4651 0.3675 -0.0051 0.0312  0.0276  444 VAL A O   
3441 C CB  . VAL A 444 ? 0.6128 0.4681 0.4014 0.0005  0.0478  0.0515  444 VAL A CB  
3442 C CG1 . VAL A 444 ? 0.5981 0.4558 0.3594 -0.0019 0.0572  0.0435  444 VAL A CG1 
3443 C CG2 . VAL A 444 ? 0.5365 0.3919 0.3498 0.0059  0.0521  0.0416  444 VAL A CG2 
3444 N N   . TYR A 445 ? 0.6332 0.4754 0.4250 -0.0003 0.0265  0.0317  445 TYR A N   
3445 C CA  . TYR A 445 ? 0.6406 0.4701 0.4276 0.0002  0.0265  0.0180  445 TYR A CA  
3446 C C   . TYR A 445 ? 0.5930 0.4200 0.4027 0.0056  0.0295  0.0178  445 TYR A C   
3447 O O   . TYR A 445 ? 0.5779 0.4149 0.4063 0.0065  0.0300  0.0258  445 TYR A O   
3448 C CB  . TYR A 445 ? 0.6207 0.4447 0.3981 -0.0081 0.0145  0.0140  445 TYR A CB  
3449 C CG  . TYR A 445 ? 0.5871 0.4197 0.3835 -0.0126 0.0053  0.0222  445 TYR A CG  
3450 C CD1 . TYR A 445 ? 0.5948 0.4433 0.3949 -0.0148 -0.0026 0.0323  445 TYR A CD1 
3451 C CD2 . TYR A 445 ? 0.6853 0.5113 0.4960 -0.0147 0.0045  0.0202  445 TYR A CD2 
3452 C CE1 . TYR A 445 ? 0.5582 0.4186 0.3799 -0.0175 -0.0100 0.0372  445 TYR A CE1 
3453 C CE2 . TYR A 445 ? 0.6456 0.4841 0.4740 -0.0202 -0.0016 0.0257  445 TYR A CE2 
3454 C CZ  . TYR A 445 ? 0.6207 0.4778 0.4566 -0.0210 -0.0084 0.0326  445 TYR A CZ  
3455 O OH  . TYR A 445 ? 0.6191 0.4925 0.4771 -0.0250 -0.0134 0.0356  445 TYR A OH  
3456 N N   . GLU A 446 ? 0.6157 0.4286 0.4228 0.0094  0.0311  0.0082  446 GLU A N   
3457 C CA  . GLU A 446 ? 0.5653 0.3752 0.3891 0.0157  0.0326  0.0090  446 GLU A CA  
3458 C C   . GLU A 446 ? 0.5910 0.3838 0.4131 0.0106  0.0247  0.0090  446 GLU A C   
3459 O O   . GLU A 446 ? 0.6406 0.4166 0.4486 0.0062  0.0213  0.0016  446 GLU A O   
3460 C CB  . GLU A 446 ? 0.6019 0.4096 0.4274 0.0269  0.0408  0.0002  446 GLU A CB  
3461 C CG  . GLU A 446 ? 0.6777 0.4814 0.5180 0.0352  0.0391  0.0015  446 GLU A CG  
3462 C CD  . GLU A 446 ? 0.6785 0.4810 0.5238 0.0487  0.0452  -0.0087 446 GLU A CD  
3463 O OE1 . GLU A 446 ? 0.6555 0.4695 0.4975 0.0505  0.0545  -0.0165 446 GLU A OE1 
3464 O OE2 . GLU A 446 ? 0.6980 0.4891 0.5510 0.0577  0.0409  -0.0085 446 GLU A OE2 
3465 N N   . ALA A 447 ? 0.6173 0.4147 0.4526 0.0096  0.0224  0.0168  447 ALA A N   
3466 C CA  . ALA A 447 ? 0.5896 0.3721 0.4225 0.0019  0.0163  0.0198  447 ALA A CA  
3467 C C   . ALA A 447 ? 0.6600 0.4149 0.4860 0.0086  0.0157  0.0157  447 ALA A C   
3468 O O   . ALA A 447 ? 0.6893 0.4437 0.5195 0.0220  0.0197  0.0124  447 ALA A O   
3469 C CB  . ALA A 447 ? 0.5710 0.3686 0.4169 -0.0017 0.0157  0.0290  447 ALA A CB  
3470 N N   . LEU A 448 ? 0.6716 0.4032 0.4895 -0.0008 0.0107  0.0156  448 LEU A N   
3471 C CA  . LEU A 448 ? 0.7196 0.4172 0.5319 0.0051  0.0092  0.0122  448 LEU A CA  
3472 C C   . LEU A 448 ? 0.7347 0.4256 0.5535 0.0118  0.0068  0.0255  448 LEU A C   
3473 O O   . LEU A 448 ? 0.6568 0.3236 0.4759 0.0241  0.0054  0.0246  448 LEU A O   
3474 C CB  . LEU A 448 ? 0.6622 0.3338 0.4640 -0.0101 0.0047  0.0075  448 LEU A CB  
3475 C CG  . LEU A 448 ? 0.7574 0.4370 0.5498 -0.0184 0.0042  -0.0061 448 LEU A CG  
3476 C CD1 . LEU A 448 ? 0.7471 0.4045 0.5323 -0.0363 -0.0013 -0.0115 448 LEU A CD1 
3477 C CD2 . LEU A 448 ? 0.7323 0.4076 0.5173 -0.0052 0.0098  -0.0211 448 LEU A CD2 
3478 N N   . SER A 449 ? 0.6291 0.3416 0.4530 0.0048  0.0060  0.0372  449 SER A N   
3479 C CA  . SER A 449 ? 0.6518 0.3620 0.4768 0.0081  0.0028  0.0512  449 SER A CA  
3480 C C   . SER A 449 ? 0.6150 0.3613 0.4465 0.0006  0.0051  0.0570  449 SER A C   
3481 O O   . SER A 449 ? 0.6074 0.3752 0.4453 -0.0056 0.0086  0.0507  449 SER A O   
3482 C CB  . SER A 449 ? 0.7420 0.4163 0.5558 -0.0017 -0.0021 0.0608  449 SER A CB  
3483 O OG  . SER A 449 ? 0.7197 0.3992 0.5300 -0.0230 -0.0011 0.0621  449 SER A OG  
3484 N N   . TRP A 450 ? 0.6516 0.4042 0.4813 0.0018  0.0024  0.0688  450 TRP A N   
3485 C CA  . TRP A 450 ? 0.6555 0.4424 0.4901 -0.0066 0.0055  0.0716  450 TRP A CA  
3486 C C   . TRP A 450 ? 0.6253 0.4166 0.4580 -0.0259 0.0082  0.0726  450 TRP A C   
3487 O O   . TRP A 450 ? 0.6034 0.4226 0.4478 -0.0310 0.0128  0.0656  450 TRP A O   
3488 C CB  . TRP A 450 ? 0.6475 0.4412 0.4753 -0.0034 0.0013  0.0841  450 TRP A CB  
3489 C CG  . TRP A 450 ? 0.6887 0.5203 0.5208 -0.0115 0.0056  0.0826  450 TRP A CG  
3490 C CD1 . TRP A 450 ? 0.6362 0.4791 0.4584 -0.0269 0.0075  0.0907  450 TRP A CD1 
3491 C CD2 . TRP A 450 ? 0.6662 0.5292 0.5142 -0.0058 0.0100  0.0704  450 TRP A CD2 
3492 N NE1 . TRP A 450 ? 0.6526 0.5333 0.4838 -0.0297 0.0129  0.0820  450 TRP A NE1 
3493 C CE2 . TRP A 450 ? 0.6133 0.5045 0.4611 -0.0169 0.0140  0.0696  450 TRP A CE2 
3494 C CE3 . TRP A 450 ? 0.6684 0.5382 0.5310 0.0063  0.0120  0.0596  450 TRP A CE3 
3495 C CZ2 . TRP A 450 ? 0.6020 0.5243 0.4652 -0.0154 0.0191  0.0568  450 TRP A CZ2 
3496 C CZ3 . TRP A 450 ? 0.5678 0.4674 0.4449 0.0062  0.0171  0.0496  450 TRP A CZ3 
3497 C CH2 . TRP A 450 ? 0.6157 0.5395 0.4938 -0.0041 0.0201  0.0476  450 TRP A CH2 
3498 N N   . GLN A 451 ? 0.6403 0.4042 0.4609 -0.0369 0.0055  0.0809  451 GLN A N   
3499 C CA  . GLN A 451 ? 0.6452 0.4171 0.4667 -0.0574 0.0084  0.0813  451 GLN A CA  
3500 C C   . GLN A 451 ? 0.6220 0.4038 0.4553 -0.0594 0.0092  0.0673  451 GLN A C   
3501 O O   . GLN A 451 ? 0.6359 0.4462 0.4812 -0.0690 0.0123  0.0632  451 GLN A O   
3502 C CB  . GLN A 451 ? 0.7080 0.4440 0.5147 -0.0705 0.0056  0.0928  451 GLN A CB  
3503 C CG  . GLN A 451 ? 0.7907 0.5169 0.5823 -0.0711 0.0036  0.1118  451 GLN A CG  
3504 C CD  . GLN A 451 ? 0.8199 0.5252 0.6075 -0.0485 -0.0033 0.1162  451 GLN A CD  
3505 O OE1 . GLN A 451 ? 0.7729 0.4598 0.5668 -0.0353 -0.0054 0.1055  451 GLN A OE1 
3506 N NE2 . GLN A 451 ? 0.7961 0.5078 0.5737 -0.0440 -0.0069 0.1313  451 GLN A NE2 
3507 N N   . HIS A 452 ? 0.5928 0.3536 0.4230 -0.0501 0.0062  0.0596  452 HIS A N   
3508 C CA  . HIS A 452 ? 0.6046 0.3772 0.4416 -0.0512 0.0055  0.0480  452 HIS A CA  
3509 C C   . HIS A 452 ? 0.6177 0.4227 0.4684 -0.0420 0.0088  0.0448  452 HIS A C   
3510 O O   . HIS A 452 ? 0.5251 0.3509 0.3866 -0.0463 0.0082  0.0407  452 HIS A O   
3511 C CB  . HIS A 452 ? 0.6163 0.3613 0.4430 -0.0437 0.0029  0.0392  452 HIS A CB  
3512 C CG  . HIS A 452 ? 0.6236 0.3810 0.4511 -0.0458 0.0009  0.0288  452 HIS A CG  
3513 N ND1 . HIS A 452 ? 0.6005 0.3592 0.4235 -0.0334 0.0025  0.0215  452 HIS A ND1 
3514 C CD2 . HIS A 452 ? 0.5843 0.3561 0.4161 -0.0593 -0.0032 0.0254  452 HIS A CD2 
3515 C CE1 . HIS A 452 ? 0.6281 0.3991 0.4487 -0.0391 -0.0012 0.0158  452 HIS A CE1 
3516 N NE2 . HIS A 452 ? 0.5919 0.3719 0.4192 -0.0539 -0.0057 0.0177  452 HIS A NE2 
3517 N N   . GLY A 453 ? 0.6210 0.4304 0.4735 -0.0292 0.0116  0.0466  453 GLY A N   
3518 C CA  . GLY A 453 ? 0.5480 0.3845 0.4148 -0.0226 0.0156  0.0431  453 GLY A CA  
3519 C C   . GLY A 453 ? 0.5575 0.4205 0.4377 -0.0316 0.0183  0.0436  453 GLY A C   
3520 O O   . GLY A 453 ? 0.5680 0.4492 0.4631 -0.0306 0.0196  0.0390  453 GLY A O   
3521 N N   . VAL A 454 ? 0.5380 0.4037 0.4130 -0.0404 0.0195  0.0494  454 VAL A N   
3522 C CA  . VAL A 454 ? 0.5216 0.4159 0.4089 -0.0507 0.0241  0.0474  454 VAL A CA  
3523 C C   . VAL A 454 ? 0.5563 0.4588 0.4549 -0.0594 0.0223  0.0434  454 VAL A C   
3524 O O   . VAL A 454 ? 0.5404 0.4701 0.4598 -0.0596 0.0251  0.0369  454 VAL A O   
3525 C CB  . VAL A 454 ? 0.5470 0.4417 0.4206 -0.0616 0.0263  0.0563  454 VAL A CB  
3526 C CG1 . VAL A 454 ? 0.5416 0.4700 0.4275 -0.0740 0.0336  0.0519  454 VAL A CG1 
3527 C CG2 . VAL A 454 ? 0.5407 0.4338 0.4046 -0.0515 0.0255  0.0605  454 VAL A CG2 
3528 N N   . PHE A 455 ? 0.5619 0.4418 0.4492 -0.0661 0.0170  0.0458  455 PHE A N   
3529 C CA  . PHE A 455 ? 0.5669 0.4574 0.4649 -0.0751 0.0130  0.0409  455 PHE A CA  
3530 C C   . PHE A 455 ? 0.5213 0.4226 0.4308 -0.0628 0.0091  0.0356  455 PHE A C   
3531 O O   . PHE A 455 ? 0.5466 0.4724 0.4753 -0.0651 0.0064  0.0320  455 PHE A O   
3532 C CB  . PHE A 455 ? 0.5723 0.4335 0.4541 -0.0856 0.0077  0.0421  455 PHE A CB  
3533 C CG  . PHE A 455 ? 0.5692 0.4414 0.4598 -0.0936 0.0010  0.0349  455 PHE A CG  
3534 C CD1 . PHE A 455 ? 0.5684 0.4658 0.4752 -0.1098 0.0014  0.0330  455 PHE A CD1 
3535 C CD2 . PHE A 455 ? 0.5563 0.4178 0.4389 -0.0856 -0.0058 0.0297  455 PHE A CD2 
3536 C CE1 . PHE A 455 ? 0.5317 0.4445 0.4492 -0.1170 -0.0068 0.0259  455 PHE A CE1 
3537 C CE2 . PHE A 455 ? 0.6099 0.4853 0.4984 -0.0932 -0.0141 0.0234  455 PHE A CE2 
3538 C CZ  . PHE A 455 ? 0.5648 0.4663 0.4720 -0.1085 -0.0156 0.0215  455 PHE A CZ  
3539 N N   . VAL A 456 ? 0.4995 0.3839 0.3985 -0.0497 0.0085  0.0360  456 VAL A N   
3540 C CA  . VAL A 456 ? 0.5168 0.4087 0.4226 -0.0396 0.0057  0.0343  456 VAL A CA  
3541 C C   . VAL A 456 ? 0.5123 0.4296 0.4428 -0.0341 0.0096  0.0332  456 VAL A C   
3542 O O   . VAL A 456 ? 0.5091 0.4411 0.4550 -0.0308 0.0050  0.0330  456 VAL A O   
3543 C CB  . VAL A 456 ? 0.5354 0.4071 0.4255 -0.0287 0.0076  0.0346  456 VAL A CB  
3544 C CG1 . VAL A 456 ? 0.5436 0.4238 0.4403 -0.0198 0.0072  0.0360  456 VAL A CG1 
3545 C CG2 . VAL A 456 ? 0.5302 0.3774 0.3987 -0.0324 0.0037  0.0318  456 VAL A CG2 
3546 N N   . GLY A 457 ? 0.4866 0.4097 0.4219 -0.0325 0.0173  0.0319  457 GLY A N   
3547 C CA  . GLY A 457 ? 0.4408 0.3872 0.4007 -0.0283 0.0223  0.0269  457 GLY A CA  
3548 C C   . GLY A 457 ? 0.4818 0.4538 0.4618 -0.0359 0.0220  0.0228  457 GLY A C   
3549 O O   . GLY A 457 ? 0.4272 0.4167 0.4325 -0.0294 0.0216  0.0185  457 GLY A O   
3550 N N   . ALA A 458 ? 0.4213 0.3957 0.3922 -0.0499 0.0224  0.0240  458 ALA A N   
3551 C CA  . ALA A 458 ? 0.4237 0.4276 0.4156 -0.0597 0.0237  0.0189  458 ALA A CA  
3552 C C   . ALA A 458 ? 0.4135 0.4258 0.4196 -0.0575 0.0132  0.0186  458 ALA A C   
3553 O O   . ALA A 458 ? 0.4588 0.5023 0.4940 -0.0576 0.0128  0.0126  458 ALA A O   
3554 C CB  . ALA A 458 ? 0.4626 0.4645 0.4392 -0.0785 0.0273  0.0224  458 ALA A CB  
3555 N N   . ALA A 459 ? 0.4327 0.4210 0.4194 -0.0549 0.0042  0.0240  459 ALA A N   
3556 C CA  . ALA A 459 ? 0.4519 0.4494 0.4460 -0.0543 -0.0080 0.0244  459 ALA A CA  
3557 C C   . ALA A 459 ? 0.4411 0.4416 0.4468 -0.0368 -0.0134 0.0281  459 ALA A C   
3558 O O   . ALA A 459 ? 0.4742 0.4827 0.4832 -0.0343 -0.0256 0.0312  459 ALA A O   
3559 C CB  . ALA A 459 ? 0.4625 0.4342 0.4271 -0.0623 -0.0148 0.0263  459 ALA A CB  
3560 N N   . MET A 460 ? 0.4228 0.4167 0.4342 -0.0259 -0.0054 0.0286  460 MET A N   
3561 C CA  . MET A 460 ? 0.4479 0.4373 0.4686 -0.0108 -0.0094 0.0343  460 MET A CA  
3562 C C   . MET A 460 ? 0.4512 0.4666 0.5032 -0.0042 -0.0188 0.0348  460 MET A C   
3563 O O   . MET A 460 ? 0.4634 0.5063 0.5434 -0.0066 -0.0156 0.0259  460 MET A O   
3564 C CB  . MET A 460 ? 0.4307 0.4130 0.4603 -0.0033 0.0022  0.0311  460 MET A CB  
3565 C CG  . MET A 460 ? 0.4293 0.3869 0.4312 -0.0048 0.0085  0.0330  460 MET A CG  
3566 S SD  . MET A 460 ? 0.5188 0.4743 0.5349 0.0017  0.0207  0.0267  460 MET A SD  
3567 C CE  . MET A 460 ? 0.4042 0.3565 0.4446 0.0146  0.0164  0.0324  460 MET A CE  
3568 N N   . ARG A 461 ? 0.4079 0.4169 0.4549 0.0044  -0.0307 0.0455  461 ARG A N   
3569 C CA  . ARG A 461 ? 0.4335 0.4646 0.5109 0.0152  -0.0426 0.0496  461 ARG A CA  
3570 C C   . ARG A 461 ? 0.4685 0.4784 0.5415 0.0296  -0.0474 0.0642  461 ARG A C   
3571 O O   . ARG A 461 ? 0.4512 0.4341 0.4921 0.0275  -0.0438 0.0714  461 ARG A O   
3572 C CB  . ARG A 461 ? 0.4163 0.4692 0.4909 0.0074  -0.0579 0.0503  461 ARG A CB  
3573 C CG  . ARG A 461 ? 0.4855 0.5540 0.5600 -0.0112 -0.0525 0.0376  461 ARG A CG  
3574 C CD  . ARG A 461 ? 0.4583 0.5455 0.5280 -0.0217 -0.0679 0.0368  461 ARG A CD  
3575 N NE  . ARG A 461 ? 0.4299 0.5548 0.5375 -0.0124 -0.0813 0.0377  461 ARG A NE  
3576 C CZ  . ARG A 461 ? 0.4427 0.5875 0.5494 -0.0148 -0.1002 0.0408  461 ARG A CZ  
3577 N NH1 . ARG A 461 ? 0.4724 0.6018 0.5405 -0.0273 -0.1070 0.0415  461 ARG A NH1 
3578 N NH2 . ARG A 461 ? 0.4754 0.6582 0.6221 -0.0037 -0.1131 0.0419  461 ARG A NH2 
3579 N N   . SER A 462 ? 0.4566 0.4789 0.5637 0.0443  -0.0551 0.0689  462 SER A N   
3580 C CA  . SER A 462 ? 0.5217 0.5202 0.6292 0.0582  -0.0588 0.0849  462 SER A CA  
3581 C C   . SER A 462 ? 0.6095 0.6271 0.7540 0.0748  -0.0744 0.0925  462 SER A C   
3582 O O   . SER A 462 ? 0.5370 0.5866 0.7186 0.0780  -0.0755 0.0796  462 SER A O   
3583 C CB  . SER A 462 ? 0.5280 0.5043 0.6447 0.0612  -0.0412 0.0786  462 SER A CB  
3584 O OG  . SER A 462 ? 0.5927 0.5414 0.7083 0.0715  -0.0435 0.0949  462 SER A OG  
3585 N N   . GLU A 463 ? 0.5706 0.5696 0.7052 0.0853  -0.0862 0.1143  463 GLU A N   
3586 C CA  . GLU A 463 ? 0.7229 0.7367 0.8910 0.1038  -0.1044 0.1262  463 GLU A CA  
3587 C C   . GLU A 463 ? 0.7075 0.7120 0.9229 0.1203  -0.0957 0.1201  463 GLU A C   
3588 O O   . GLU A 463 ? 0.6863 0.6616 0.8983 0.1180  -0.0787 0.1151  463 GLU A O   
3589 C CB  . GLU A 463 ? 0.7612 0.7561 0.8982 0.1091  -0.1210 0.1550  463 GLU A CB  
3590 C CG  . GLU A 463 ? 0.8533 0.8024 0.9740 0.1121  -0.1108 0.1703  463 GLU A CG  
3591 C CD  . GLU A 463 ? 0.9542 0.8873 1.0569 0.1218  -0.1290 0.2026  463 GLU A CD  
3592 O OE1 . GLU A 463 ? 0.9027 0.8597 0.9881 0.1213  -0.1489 0.2127  463 GLU A OE1 
3593 O OE2 . GLU A 463 ? 0.9889 0.8859 1.0943 0.1289  -0.1239 0.2184  463 GLU A OE2 
3594 N N   . ALA A 464 ? 0.7736 0.8050 1.0356 0.1373  -0.1079 0.1185  464 ALA A N   
3595 C CA  . ALA A 464 ? 0.9569 0.9826 1.2701 0.1551  -0.1002 0.1087  464 ALA A CA  
3596 C C   . ALA A 464 ? 1.0956 1.0703 1.4027 0.1655  -0.0994 0.1286  464 ALA A C   
3597 O O   . ALA A 464 ? 1.1628 1.1208 1.4527 0.1733  -0.1169 0.1572  464 ALA A O   
3598 C CB  . ALA A 464 ? 1.0399 1.1054 1.4059 0.1744  -0.1164 0.1060  464 ALA A CB  
3599 N N   . THR A 465 ? 1.2252 1.1757 1.5452 0.1642  -0.0791 0.1136  465 THR A N   
3600 C CA  . THR A 465 ? 1.3228 1.2231 1.6413 0.1703  -0.0742 0.1279  465 THR A CA  
3601 C C   . THR A 465 ? 1.4948 1.3883 1.8748 0.1925  -0.0722 0.1167  465 THR A C   
3602 O O   . THR A 465 ? 1.4454 1.3713 1.8642 0.2089  -0.0838 0.1112  465 THR A O   
3603 C CB  . THR A 465 ? 1.2454 1.1240 1.5299 0.1493  -0.0532 0.1179  465 THR A CB  
3604 O OG1 . THR A 465 ? 1.2514 1.1513 1.5580 0.1436  -0.0360 0.0847  465 THR A OG1 
3605 C CG2 . THR A 465 ? 1.1588 1.0449 1.3875 0.1309  -0.0561 0.1278  465 THR A CG2 
3606 N N   . ALA A 466 ? 1.6050 1.4604 1.9875 0.1897  -0.0562 0.1090  466 ALA A N   
3607 C CA  . ALA A 466 ? 1.6858 1.5320 2.1067 0.2030  -0.0499 0.0918  466 ALA A CA  
3608 C C   . ALA A 466 ? 1.6925 1.5343 2.1253 0.1914  -0.0255 0.0593  466 ALA A C   
3609 O O   . ALA A 466 ? 1.6180 1.4245 2.0499 0.1877  -0.0153 0.0546  466 ALA A O   
3610 C CB  . ALA A 466 ? 1.6531 1.4539 2.0604 0.2103  -0.0579 0.1164  466 ALA A CB  
3611 N N   . ALA A 467 ? 1.5675 1.4480 2.0106 0.1845  -0.0163 0.0363  467 ALA A N   
3612 C CA  . ALA A 467 ? 1.4384 1.3239 1.8887 0.1725  0.0062  0.0034  467 ALA A CA  
3613 C C   . ALA A 467 ? 1.4324 1.3555 1.9249 0.1813  0.0135  -0.0282 467 ALA A C   
3614 O O   . ALA A 467 ? 1.2466 1.1561 1.7572 0.1840  0.0232  -0.0465 467 ALA A O   
3615 C CB  . ALA A 467 ? 1.2315 1.1360 1.6357 0.1488  0.0136  -0.0002 467 ALA A CB  
3616 N N   . ALA A 468 ? 1.3878 1.3599 1.8963 0.1842  0.0096  -0.0359 468 ALA A N   
3617 C CA  . ALA A 468 ? 1.3356 1.3486 1.8821 0.1912  0.0169  -0.0645 468 ALA A CA  
3618 C C   . ALA A 468 ? 1.3807 1.3981 1.9568 0.2137  -0.0006 -0.0515 468 ALA A C   
3619 O O   . ALA A 468 ? 1.3990 1.3745 1.9688 0.2243  -0.0121 -0.0283 468 ALA A O   
3620 C CB  . ALA A 468 ? 1.2166 1.2850 1.7629 0.1788  0.0239  -0.0806 468 ALA A CB  
3621 N N   . GLU A 469 ? 1.3620 1.4316 1.9691 0.2203  -0.0023 -0.0658 469 GLU A N   
3622 C CA  . GLU A 469 ? 1.3699 1.4526 2.0080 0.2425  -0.0195 -0.0551 469 GLU A CA  
3623 C C   . GLU A 469 ? 1.4047 1.5157 2.0372 0.2447  -0.0415 -0.0311 469 GLU A C   
3624 O O   . GLU A 469 ? 1.3795 1.5274 2.0422 0.2583  -0.0536 -0.0306 469 GLU A O   
3625 C CB  . GLU A 469 ? 1.3168 1.4411 1.9967 0.2495  -0.0074 -0.0874 469 GLU A CB  
3626 C CG  . GLU A 469 ? 1.2388 1.4231 1.9229 0.2327  0.0048  -0.1101 469 GLU A CG  
3627 C CD  . GLU A 469 ? 1.0131 1.1950 1.6759 0.2114  0.0296  -0.1356 469 GLU A CD  
3628 O OE1 . GLU A 469 ? 1.0672 1.2049 1.7001 0.2034  0.0332  -0.1280 469 GLU A OE1 
3629 O OE2 . GLU A 469 ? 0.8717 1.0974 1.5456 0.2016  0.0452  -0.1625 469 GLU A OE2 
3630 N N   . HIS A 470 ? 1.4862 1.5822 2.0809 0.2309  -0.0475 -0.0116 470 HIS A N   
3631 C CA  . HIS A 470 ? 1.5336 1.6541 2.1178 0.2298  -0.0700 0.0113  470 HIS A CA  
3632 C C   . HIS A 470 ? 1.5600 1.6410 2.1209 0.2422  -0.0920 0.0480  470 HIS A C   
3633 O O   . HIS A 470 ? 1.5637 1.5903 2.0970 0.2407  -0.0875 0.0616  470 HIS A O   
3634 C CB  . HIS A 470 ? 1.5092 1.6305 2.0328 0.1985  -0.0618 0.0127  470 HIS A CB  
3635 C CG  . HIS A 470 ? 1.4735 1.6287 1.9998 0.1803  -0.0394 -0.0188 470 HIS A CG  
3636 N ND1 . HIS A 470 ? 1.4630 1.5994 1.9828 0.1722  -0.0167 -0.0383 470 HIS A ND1 
3637 C CD2 . HIS A 470 ? 1.4351 1.6426 1.9682 0.1672  -0.0362 -0.0331 470 HIS A CD2 
3638 C CE1 . HIS A 470 ? 1.3578 1.5336 1.8775 0.1556  -0.0011 -0.0618 470 HIS A CE1 
3639 N NE2 . HIS A 470 ? 1.3538 1.5716 1.8818 0.1518  -0.0117 -0.0585 470 HIS A NE2 
3640 N N   . LYS A 471 ? 1.4954 1.6071 2.0653 0.2523  -0.1152 0.0633  471 LYS A N   
3641 C CA  . LYS A 471 ? 1.4899 1.5718 2.0343 0.2639  -0.1372 0.0981  471 LYS A CA  
3642 C C   . LYS A 471 ? 1.5195 1.6299 2.0373 0.2554  -0.1602 0.1185  471 LYS A C   
3643 O O   . LYS A 471 ? 1.4199 1.5657 1.9344 0.2378  -0.1576 0.1058  471 LYS A O   
3644 C CB  . LYS A 471 ? 1.4245 1.5115 2.0065 0.2900  -0.1452 0.0980  471 LYS A CB  
3645 C CG  . LYS A 471 ? 1.3852 1.4435 1.9938 0.2984  -0.1240 0.0768  471 LYS A CG  
3646 C CD  . LYS A 471 ? 1.3360 1.4006 1.9843 0.3259  -0.1334 0.0773  471 LYS A CD  
3647 C CE  . LYS A 471 ? 1.2452 1.2810 1.9201 0.3329  -0.1126 0.0540  471 LYS A CE  
3648 N NZ  . LYS A 471 ? 1.0892 1.1300 1.8061 0.3615  -0.1212 0.0535  471 LYS A NZ  
3649 N N   . GLY A 472 ? 1.6126 1.7073 2.1050 0.2652  -0.1817 0.1484  472 GLY A N   
3650 C CA  . GLY A 472 ? 1.5343 1.6573 1.9970 0.2569  -0.2051 0.1666  472 GLY A CA  
3651 C C   . GLY A 472 ? 1.5044 1.6056 1.9121 0.2322  -0.2015 0.1776  472 GLY A C   
3652 O O   . GLY A 472 ? 1.4738 1.5400 1.8629 0.2201  -0.1788 0.1694  472 GLY A O   
3653 N N   . LYS A 473 ? 1.4443 1.5680 1.8176 0.2223  -0.2221 0.1927  473 LYS A N   
3654 C CA  . LYS A 473 ? 1.3795 1.4861 1.6833 0.1947  -0.2147 0.1962  473 LYS A CA  
3655 C C   . LYS A 473 ? 1.1922 1.3430 1.4940 0.1732  -0.2084 0.1685  473 LYS A C   
3656 O O   . LYS A 473 ? 1.1113 1.3010 1.4075 0.1677  -0.2279 0.1700  473 LYS A O   
3657 C CB  . LYS A 473 ? 1.4758 1.5727 1.7338 0.1956  -0.2389 0.2296  473 LYS A CB  
3658 C CG  . LYS A 473 ? 1.5520 1.6043 1.7999 0.2129  -0.2394 0.2513  473 LYS A CG  
3659 C CD  . LYS A 473 ? 1.5525 1.5502 1.7898 0.2076  -0.2135 0.2507  473 LYS A CD  
3660 C CE  . LYS A 473 ? 1.4539 1.4320 1.6324 0.1830  -0.2039 0.2573  473 LYS A CE  
3661 N NZ  . LYS A 473 ? 1.3935 1.3226 1.5631 0.1769  -0.1786 0.2556  473 LYS A NZ  
3662 N N   . VAL A 474 ? 1.0139 1.1578 1.3197 0.1600  -0.1815 0.1437  474 VAL A N   
3663 C CA  . VAL A 474 ? 0.7904 0.9691 1.0951 0.1384  -0.1720 0.1185  474 VAL A CA  
3664 C C   . VAL A 474 ? 0.6356 0.7802 0.8976 0.1176  -0.1477 0.1090  474 VAL A C   
3665 O O   . VAL A 474 ? 0.6931 0.7998 0.9499 0.1223  -0.1327 0.1112  474 VAL A O   
3666 C CB  . VAL A 474 ? 0.6785 0.8996 1.0478 0.1465  -0.1648 0.0948  474 VAL A CB  
3667 C CG1 . VAL A 474 ? 0.6204 0.8673 0.9828 0.1204  -0.1487 0.0703  474 VAL A CG1 
3668 C CG2 . VAL A 474 ? 0.6966 0.9621 1.1110 0.1658  -0.1909 0.1016  474 VAL A CG2 
3669 N N   . ILE A 475 ? 0.7512 0.6877 0.7997 0.0362  -0.0730 0.1928  475 ILE A N   
3670 C CA  . ILE A 475 ? 0.6731 0.5876 0.6978 0.0238  -0.0659 0.1703  475 ILE A CA  
3671 C C   . ILE A 475 ? 0.6683 0.5853 0.7139 0.0181  -0.0602 0.1555  475 ILE A C   
3672 O O   . ILE A 475 ? 0.7238 0.6637 0.7812 0.0129  -0.0717 0.1538  475 ILE A O   
3673 C CB  . ILE A 475 ? 0.5787 0.4987 0.5671 0.0125  -0.0807 0.1625  475 ILE A CB  
3674 C CG1 . ILE A 475 ? 0.6425 0.5648 0.6077 0.0184  -0.0862 0.1788  475 ILE A CG1 
3675 C CG2 . ILE A 475 ? 0.6073 0.5040 0.5753 0.0023  -0.0720 0.1415  475 ILE A CG2 
3676 C CD1 . ILE A 475 ? 0.7694 0.6983 0.6965 0.0077  -0.0997 0.1694  475 ILE A CD1 
3677 N N   . MET A 476 ? 0.5751 0.4703 0.6253 0.0183  -0.0423 0.1447  476 MET A N   
3678 C CA  . MET A 476 ? 0.6165 0.5142 0.6842 0.0140  -0.0343 0.1320  476 MET A CA  
3679 C C   . MET A 476 ? 0.6068 0.4871 0.6511 0.0034  -0.0286 0.1140  476 MET A C   
3680 O O   . MET A 476 ? 0.5921 0.4561 0.6123 0.0013  -0.0272 0.1106  476 MET A O   
3681 C CB  . MET A 476 ? 0.6530 0.5455 0.7511 0.0248  -0.0172 0.1349  476 MET A CB  
3682 C CG  . MET A 476 ? 0.7539 0.6186 0.8453 0.0290  -0.0021 0.1325  476 MET A CG  
3683 S SD  . MET A 476 ? 1.1415 0.9982 1.2724 0.0425  0.0181  0.1359  476 MET A SD  
3684 C CE  . MET A 476 ? 1.0400 0.8621 1.1584 0.0422  0.0334  0.1308  476 MET A CE  
3685 N N   . HIS A 477 ? 0.5556 0.4415 0.6085 -0.0026 -0.0249 0.1039  477 HIS A N   
3686 C CA  . HIS A 477 ? 0.5567 0.4298 0.5905 -0.0112 -0.0200 0.0896  477 HIS A CA  
3687 C C   . HIS A 477 ? 0.5656 0.4251 0.6026 -0.0081 -0.0029 0.0814  477 HIS A C   
3688 O O   . HIS A 477 ? 0.5981 0.4612 0.6578 -0.0019 0.0076  0.0822  477 HIS A O   
3689 C CB  . HIS A 477 ? 0.5268 0.4125 0.5667 -0.0195 -0.0235 0.0848  477 HIS A CB  
3690 C CG  . HIS A 477 ? 0.5477 0.4445 0.5838 -0.0263 -0.0401 0.0883  477 HIS A CG  
3691 N ND1 . HIS A 477 ? 0.4686 0.3560 0.4830 -0.0355 -0.0468 0.0808  477 HIS A ND1 
3692 C CD2 . HIS A 477 ? 0.5338 0.4515 0.5865 -0.0257 -0.0514 0.0973  477 HIS A CD2 
3693 C CE1 . HIS A 477 ? 0.5957 0.4954 0.6122 -0.0415 -0.0609 0.0829  477 HIS A CE1 
3694 N NE2 . HIS A 477 ? 0.5046 0.4249 0.5437 -0.0362 -0.0650 0.0930  477 HIS A NE2 
3695 N N   . ASP A 478 ? 0.4839 0.3289 0.4994 -0.0126 0.0002  0.0725  478 ASP A N   
3696 C CA  . ASP A 478 ? 0.5428 0.3773 0.5589 -0.0126 0.0145  0.0618  478 ASP A CA  
3697 C C   . ASP A 478 ? 0.5227 0.3530 0.5170 -0.0203 0.0129  0.0519  478 ASP A C   
3698 O O   . ASP A 478 ? 0.5332 0.3526 0.5153 -0.0214 0.0152  0.0480  478 ASP A O   
3699 C CB  . ASP A 478 ? 0.5928 0.4129 0.6134 -0.0067 0.0219  0.0657  478 ASP A CB  
3700 C CG  . ASP A 478 ? 0.5486 0.3593 0.5792 -0.0069 0.0383  0.0534  478 ASP A CG  
3701 O OD1 . ASP A 478 ? 0.5488 0.3650 0.5739 -0.0130 0.0421  0.0401  478 ASP A OD1 
3702 O OD2 . ASP A 478 ? 0.5748 0.3729 0.6188 -0.0014 0.0475  0.0568  478 ASP A OD2 
3703 N N   . PRO A 479 ? 0.5230 0.3627 0.5139 -0.0253 0.0094  0.0491  479 PRO A N   
3704 C CA  . PRO A 479 ? 0.5372 0.3737 0.5094 -0.0307 0.0067  0.0432  479 PRO A CA  
3705 C C   . PRO A 479 ? 0.5068 0.3400 0.4740 -0.0317 0.0160  0.0329  479 PRO A C   
3706 O O   . PRO A 479 ? 0.5146 0.3526 0.4910 -0.0315 0.0257  0.0262  479 PRO A O   
3707 C CB  . PRO A 479 ? 0.5281 0.3760 0.5037 -0.0348 0.0048  0.0447  479 PRO A CB  
3708 C CG  . PRO A 479 ? 0.5194 0.3781 0.5158 -0.0320 0.0114  0.0466  479 PRO A CG  
3709 C CD  . PRO A 479 ? 0.5504 0.4048 0.5571 -0.0258 0.0092  0.0526  479 PRO A CD  
3710 N N   . PHE A 480 ? 0.5410 0.3674 0.4943 -0.0332 0.0134  0.0302  480 PHE A N   
3711 C CA  . PHE A 480 ? 0.5396 0.3659 0.4894 -0.0354 0.0202  0.0202  480 PHE A CA  
3712 C C   . PHE A 480 ? 0.5342 0.3535 0.4967 -0.0342 0.0305  0.0155  480 PHE A C   
3713 O O   . PHE A 480 ? 0.4839 0.3047 0.4481 -0.0380 0.0379  0.0041  480 PHE A O   
3714 C CB  . PHE A 480 ? 0.5218 0.3621 0.4676 -0.0391 0.0218  0.0137  480 PHE A CB  
3715 C CG  . PHE A 480 ? 0.5747 0.4192 0.5092 -0.0398 0.0134  0.0195  480 PHE A CG  
3716 C CD1 . PHE A 480 ? 0.5172 0.3614 0.4530 -0.0396 0.0081  0.0282  480 PHE A CD1 
3717 C CD2 . PHE A 480 ? 0.5400 0.3889 0.4657 -0.0406 0.0114  0.0163  480 PHE A CD2 
3718 C CE1 . PHE A 480 ? 0.5454 0.3891 0.4736 -0.0404 0.0022  0.0337  480 PHE A CE1 
3719 C CE2 . PHE A 480 ? 0.5641 0.4146 0.4825 -0.0394 0.0050  0.0232  480 PHE A CE2 
3720 C CZ  . PHE A 480 ? 0.5322 0.3779 0.4517 -0.0394 0.0010  0.0318  480 PHE A CZ  
3721 N N   . ALA A 481 ? 0.4820 0.2940 0.4549 -0.0290 0.0312  0.0244  481 ALA A N   
3722 C CA  . ALA A 481 ? 0.5587 0.3611 0.5480 -0.0261 0.0425  0.0228  481 ALA A CA  
3723 C C   . ALA A 481 ? 0.5391 0.3469 0.5400 -0.0278 0.0530  0.0102  481 ALA A C   
3724 O O   . ALA A 481 ? 0.5284 0.3271 0.5409 -0.0287 0.0649  0.0010  481 ALA A O   
3725 C CB  . ALA A 481 ? 0.5174 0.3078 0.5037 -0.0287 0.0478  0.0196  481 ALA A CB  
3726 N N   . MET A 482 ? 0.5254 0.3478 0.5235 -0.0289 0.0498  0.0091  482 MET A N   
3727 C CA  . MET A 482 ? 0.4885 0.3203 0.4916 -0.0314 0.0598  -0.0039 482 MET A CA  
3728 C C   . MET A 482 ? 0.5066 0.3453 0.5268 -0.0258 0.0644  0.0011  482 MET A C   
3729 O O   . MET A 482 ? 0.5556 0.4038 0.5791 -0.0275 0.0741  -0.0096 482 MET A O   
3730 C CB  . MET A 482 ? 0.5746 0.4218 0.5583 -0.0380 0.0547  -0.0095 482 MET A CB  
3731 C CG  . MET A 482 ? 0.5708 0.4181 0.5427 -0.0439 0.0536  -0.0194 482 MET A CG  
3732 S SD  . MET A 482 ? 0.5838 0.4344 0.5607 -0.0504 0.0676  -0.0429 482 MET A SD  
3733 C CE  . MET A 482 ? 0.5696 0.4448 0.5339 -0.0531 0.0689  -0.0483 482 MET A CE  
3734 N N   . ARG A 483 ? 0.4768 0.3137 0.5078 -0.0195 0.0577  0.0167  483 ARG A N   
3735 C CA  . ARG A 483 ? 0.4951 0.3435 0.5460 -0.0142 0.0607  0.0228  483 ARG A CA  
3736 C C   . ARG A 483 ? 0.5526 0.3995 0.6227 -0.0101 0.0786  0.0116  483 ARG A C   
3737 O O   . ARG A 483 ? 0.5528 0.4147 0.6309 -0.0098 0.0851  0.0081  483 ARG A O   
3738 C CB  . ARG A 483 ? 0.5392 0.3871 0.6027 -0.0072 0.0509  0.0406  483 ARG A CB  
3739 C CG  . ARG A 483 ? 0.5401 0.4066 0.6248 -0.0033 0.0497  0.0490  483 ARG A CG  
3740 C CD  . ARG A 483 ? 0.5465 0.4154 0.6511 0.0062  0.0433  0.0653  483 ARG A CD  
3741 N NE  . ARG A 483 ? 0.7204 0.5756 0.8436 0.0160  0.0564  0.0657  483 ARG A NE  
3742 C CZ  . ARG A 483 ? 0.8328 0.6704 0.9515 0.0196  0.0557  0.0717  483 ARG A CZ  
3743 N NH1 . ARG A 483 ? 0.7802 0.6136 0.8748 0.0147  0.0428  0.0772  483 ARG A NH1 
3744 N NH2 . ARG A 483 ? 0.8332 0.6561 0.9728 0.0283  0.0699  0.0725  483 ARG A NH2 
3745 N N   . PRO A 484 ? 0.6274 0.4562 0.7068 -0.0072 0.0887  0.0051  484 PRO A N   
3746 C CA  . PRO A 484 ? 0.5538 0.3781 0.6529 -0.0036 0.1077  -0.0086 484 PRO A CA  
3747 C C   . PRO A 484 ? 0.5288 0.3580 0.6119 -0.0135 0.1169  -0.0323 484 PRO A C   
3748 O O   . PRO A 484 ? 0.6025 0.4294 0.6988 -0.0120 0.1338  -0.0478 484 PRO A O   
3749 C CB  . PRO A 484 ? 0.5989 0.3982 0.7144 0.0023  0.1147  -0.0053 484 PRO A CB  
3750 C CG  . PRO A 484 ? 0.5871 0.3824 0.6906 0.0029  0.0982  0.0135  484 PRO A CG  
3751 C CD  . PRO A 484 ? 0.5555 0.3659 0.6311 -0.0063 0.0845  0.0116  484 PRO A CD  
3752 N N   . PHE A 485 ? 0.5303 0.3677 0.5860 -0.0230 0.1065  -0.0358 485 PHE A N   
3753 C CA  . PHE A 485 ? 0.5848 0.4276 0.6241 -0.0329 0.1128  -0.0577 485 PHE A CA  
3754 C C   . PHE A 485 ? 0.5809 0.4482 0.5964 -0.0391 0.1063  -0.0590 485 PHE A C   
3755 O O   . PHE A 485 ? 0.5973 0.4744 0.5964 -0.0473 0.1093  -0.0758 485 PHE A O   
3756 C CB  . PHE A 485 ? 0.5641 0.3942 0.5952 -0.0391 0.1084  -0.0628 485 PHE A CB  
3757 C CG  . PHE A 485 ? 0.5838 0.3886 0.6366 -0.0337 0.1150  -0.0583 485 PHE A CG  
3758 C CD1 . PHE A 485 ? 0.5599 0.3501 0.6354 -0.0306 0.1329  -0.0702 485 PHE A CD1 
3759 C CD2 . PHE A 485 ? 0.5728 0.3674 0.6231 -0.0314 0.1047  -0.0416 485 PHE A CD2 
3760 C CE1 . PHE A 485 ? 0.5804 0.3453 0.6777 -0.0247 0.1400  -0.0628 485 PHE A CE1 
3761 C CE2 . PHE A 485 ? 0.5514 0.3236 0.6200 -0.0262 0.1114  -0.0342 485 PHE A CE2 
3762 C CZ  . PHE A 485 ? 0.5982 0.3549 0.6912 -0.0226 0.1288  -0.0434 485 PHE A CZ  
3763 N N   . PHE A 486 ? 0.5218 0.4000 0.5354 -0.0360 0.0976  -0.0416 486 PHE A N   
3764 C CA  . PHE A 486 ? 0.5770 0.4760 0.5694 -0.0415 0.0927  -0.0397 486 PHE A CA  
3765 C C   . PHE A 486 ? 0.5524 0.4669 0.5403 -0.0445 0.1077  -0.0562 486 PHE A C   
3766 O O   . PHE A 486 ? 0.5487 0.4642 0.5552 -0.0395 0.1206  -0.0594 486 PHE A O   
3767 C CB  . PHE A 486 ? 0.5297 0.4351 0.5270 -0.0385 0.0840  -0.0191 486 PHE A CB  
3768 C CG  . PHE A 486 ? 0.5019 0.3956 0.4961 -0.0377 0.0682  -0.0053 486 PHE A CG  
3769 C CD1 . PHE A 486 ? 0.5082 0.4002 0.4824 -0.0420 0.0591  -0.0056 486 PHE A CD1 
3770 C CD2 . PHE A 486 ? 0.5433 0.4300 0.5547 -0.0323 0.0627  0.0075  486 PHE A CD2 
3771 C CE1 . PHE A 486 ? 0.5218 0.4027 0.4928 -0.0408 0.0468  0.0051  486 PHE A CE1 
3772 C CE2 . PHE A 486 ? 0.4931 0.3702 0.4984 -0.0324 0.0490  0.0177  486 PHE A CE2 
3773 C CZ  . PHE A 486 ? 0.5208 0.3936 0.5056 -0.0365 0.0421  0.0157  486 PHE A CZ  
3774 N N   . GLY A 487 ? 0.5353 0.4643 0.4983 -0.0524 0.1061  -0.0666 487 GLY A N   
3775 C CA  . GLY A 487 ? 0.5621 0.5103 0.5136 -0.0565 0.1191  -0.0825 487 GLY A CA  
3776 C C   . GLY A 487 ? 0.5358 0.5052 0.4774 -0.0562 0.1199  -0.0688 487 GLY A C   
3777 O O   . GLY A 487 ? 0.5222 0.5087 0.4559 -0.0584 0.1334  -0.0802 487 GLY A O   
3778 N N   . TYR A 488 ? 0.5212 0.4897 0.4635 -0.0542 0.1071  -0.0454 488 TYR A N   
3779 C CA  . TYR A 488 ? 0.5738 0.5605 0.5079 -0.0554 0.1077  -0.0301 488 TYR A CA  
3780 C C   . TYR A 488 ? 0.5787 0.5547 0.5277 -0.0525 0.0960  -0.0075 488 TYR A C   
3781 O O   . TYR A 488 ? 0.5429 0.4999 0.5059 -0.0490 0.0881  -0.0049 488 TYR A O   
3782 C CB  . TYR A 488 ? 0.6084 0.6146 0.5101 -0.0613 0.1027  -0.0291 488 TYR A CB  
3783 C CG  . TYR A 488 ? 0.5816 0.5796 0.4738 -0.0619 0.0852  -0.0206 488 TYR A CG  
3784 C CD1 . TYR A 488 ? 0.5875 0.5778 0.4773 -0.0636 0.0808  -0.0359 488 TYR A CD1 
3785 C CD2 . TYR A 488 ? 0.5545 0.5519 0.4426 -0.0608 0.0745  0.0022  488 TYR A CD2 
3786 C CE1 . TYR A 488 ? 0.5921 0.5773 0.4757 -0.0635 0.0662  -0.0282 488 TYR A CE1 
3787 C CE2 . TYR A 488 ? 0.5615 0.5510 0.4431 -0.0600 0.0603  0.0092  488 TYR A CE2 
3788 C CZ  . TYR A 488 ? 0.6603 0.6453 0.5397 -0.0609 0.0562  -0.0059 488 TYR A CZ  
3789 O OH  . TYR A 488 ? 0.5694 0.5490 0.4448 -0.0594 0.0435  0.0011  488 TYR A OH  
3790 N N   . ASN A 489 ? 0.5808 0.5694 0.5255 -0.0548 0.0956  0.0085  489 ASN A N   
3791 C CA  . ASN A 489 ? 0.5658 0.5459 0.5255 -0.0545 0.0861  0.0279  489 ASN A CA  
3792 C C   . ASN A 489 ? 0.5430 0.5033 0.4989 -0.0536 0.0697  0.0322  489 ASN A C   
3793 O O   . ASN A 489 ? 0.5142 0.4743 0.4497 -0.0551 0.0630  0.0328  489 ASN A O   
3794 C CB  . ASN A 489 ? 0.5546 0.5493 0.5048 -0.0591 0.0881  0.0441  489 ASN A CB  
3795 C CG  . ASN A 489 ? 0.5480 0.5363 0.5196 -0.0611 0.0823  0.0612  489 ASN A CG  
3796 O OD1 . ASN A 489 ? 0.6037 0.5745 0.5778 -0.0614 0.0686  0.0676  489 ASN A OD1 
3797 N ND2 . ASN A 489 ? 0.5622 0.5656 0.5497 -0.0633 0.0934  0.0674  489 ASN A ND2 
3798 N N   . PHE A 490 ? 0.5369 0.4830 0.5127 -0.0507 0.0635  0.0355  490 PHE A N   
3799 C CA  . PHE A 490 ? 0.5731 0.5008 0.5446 -0.0498 0.0497  0.0383  490 PHE A CA  
3800 C C   . PHE A 490 ? 0.5562 0.4804 0.5174 -0.0533 0.0405  0.0516  490 PHE A C   
3801 O O   . PHE A 490 ? 0.5433 0.4575 0.4918 -0.0525 0.0324  0.0516  490 PHE A O   
3802 C CB  . PHE A 490 ? 0.5485 0.4658 0.5411 -0.0462 0.0450  0.0404  490 PHE A CB  
3803 C CG  . PHE A 490 ? 0.5916 0.4917 0.5780 -0.0458 0.0316  0.0439  490 PHE A CG  
3804 C CD1 . PHE A 490 ? 0.5414 0.4320 0.5131 -0.0445 0.0294  0.0365  490 PHE A CD1 
3805 C CD2 . PHE A 490 ? 0.5764 0.4719 0.5725 -0.0475 0.0220  0.0530  490 PHE A CD2 
3806 C CE1 . PHE A 490 ? 0.5522 0.4283 0.5181 -0.0437 0.0192  0.0392  490 PHE A CE1 
3807 C CE2 . PHE A 490 ? 0.6084 0.4889 0.5962 -0.0473 0.0110  0.0540  490 PHE A CE2 
3808 C CZ  . PHE A 490 ? 0.5361 0.4065 0.5084 -0.0448 0.0104  0.0475  490 PHE A CZ  
3809 N N   . GLY A 491 ? 0.5882 0.5200 0.5577 -0.0571 0.0429  0.0632  491 GLY A N   
3810 C CA  . GLY A 491 ? 0.4904 0.4162 0.4526 -0.0606 0.0367  0.0767  491 GLY A CA  
3811 C C   . GLY A 491 ? 0.5524 0.4845 0.4910 -0.0593 0.0373  0.0786  491 GLY A C   
3812 O O   . GLY A 491 ? 0.5297 0.4507 0.4599 -0.0578 0.0291  0.0845  491 GLY A O   
3813 N N   . LYS A 492 ? 0.5431 0.4952 0.4711 -0.0594 0.0473  0.0734  492 LYS A N   
3814 C CA  . LYS A 492 ? 0.5469 0.5111 0.4510 -0.0584 0.0463  0.0736  492 LYS A CA  
3815 C C   . LYS A 492 ? 0.5689 0.5256 0.4665 -0.0553 0.0385  0.0608  492 LYS A C   
3816 O O   . LYS A 492 ? 0.5590 0.5213 0.4422 -0.0537 0.0322  0.0646  492 LYS A O   
3817 C CB  . LYS A 492 ? 0.5294 0.5188 0.4215 -0.0605 0.0588  0.0668  492 LYS A CB  
3818 C CG  . LYS A 492 ? 0.6308 0.6302 0.5317 -0.0638 0.0696  0.0783  492 LYS A CG  
3819 C CD  . LYS A 492 ? 0.6842 0.6781 0.5850 -0.0656 0.0651  0.1024  492 LYS A CD  
3820 C CE  . LYS A 492 ? 0.7572 0.7618 0.6697 -0.0704 0.0772  0.1145  492 LYS A CE  
3821 N NZ  . LYS A 492 ? 0.7571 0.7488 0.6786 -0.0737 0.0734  0.1370  492 LYS A NZ  
3822 N N   . TYR A 493 ? 0.5219 0.4676 0.4316 -0.0543 0.0392  0.0473  493 TYR A N   
3823 C CA  . TYR A 493 ? 0.5350 0.4714 0.4419 -0.0523 0.0331  0.0366  493 TYR A CA  
3824 C C   . TYR A 493 ? 0.5446 0.4650 0.4520 -0.0497 0.0220  0.0469  493 TYR A C   
3825 O O   . TYR A 493 ? 0.5570 0.4783 0.4561 -0.0479 0.0166  0.0446  493 TYR A O   
3826 C CB  . TYR A 493 ? 0.5508 0.4766 0.4728 -0.0512 0.0380  0.0241  493 TYR A CB  
3827 C CG  . TYR A 493 ? 0.5323 0.4450 0.4552 -0.0497 0.0335  0.0154  493 TYR A CG  
3828 C CD1 . TYR A 493 ? 0.5748 0.4696 0.5043 -0.0470 0.0258  0.0218  493 TYR A CD1 
3829 C CD2 . TYR A 493 ? 0.5470 0.4663 0.4647 -0.0520 0.0379  -0.0004 493 TYR A CD2 
3830 C CE1 . TYR A 493 ? 0.5299 0.4139 0.4597 -0.0458 0.0236  0.0153  493 TYR A CE1 
3831 C CE2 . TYR A 493 ? 0.5064 0.4141 0.4277 -0.0517 0.0354  -0.0074 493 TYR A CE2 
3832 C CZ  . TYR A 493 ? 0.5258 0.4160 0.4529 -0.0482 0.0288  0.0016  493 TYR A CZ  
3833 O OH  . TYR A 493 ? 0.5470 0.4267 0.4769 -0.0480 0.0280  -0.0040 493 TYR A OH  
3834 N N   . LEU A 494 ? 0.5475 0.4544 0.4659 -0.0501 0.0191  0.0569  494 LEU A N   
3835 C CA  . LEU A 494 ? 0.5247 0.4147 0.4433 -0.0482 0.0102  0.0644  494 LEU A CA  
3836 C C   . LEU A 494 ? 0.5809 0.4764 0.4892 -0.0463 0.0080  0.0763  494 LEU A C   
3837 O O   . LEU A 494 ? 0.5652 0.4553 0.4690 -0.0421 0.0025  0.0771  494 LEU A O   
3838 C CB  . LEU A 494 ? 0.5920 0.4687 0.5246 -0.0512 0.0078  0.0703  494 LEU A CB  
3839 C CG  . LEU A 494 ? 0.5406 0.4121 0.4844 -0.0514 0.0068  0.0622  494 LEU A CG  
3840 C CD1 . LEU A 494 ? 0.5386 0.4044 0.4967 -0.0558 0.0028  0.0684  494 LEU A CD1 
3841 C CD2 . LEU A 494 ? 0.5035 0.3629 0.4410 -0.0477 0.0018  0.0545  494 LEU A CD2 
3842 N N   . ALA A 495 ? 0.5798 0.4874 0.4856 -0.0487 0.0130  0.0874  495 ALA A N   
3843 C CA  . ALA A 495 ? 0.5527 0.4677 0.4486 -0.0458 0.0115  0.1027  495 ALA A CA  
3844 C C   . ALA A 495 ? 0.6036 0.5372 0.4849 -0.0419 0.0082  0.0968  495 ALA A C   
3845 O O   . ALA A 495 ? 0.5959 0.5311 0.4734 -0.0364 0.0025  0.1070  495 ALA A O   
3846 C CB  . ALA A 495 ? 0.5402 0.4688 0.4337 -0.0496 0.0194  0.1159  495 ALA A CB  
3847 N N   . HIS A 496 ? 0.5628 0.5115 0.4383 -0.0448 0.0119  0.0800  496 HIS A N   
3848 C CA  . HIS A 496 ? 0.5546 0.5224 0.4187 -0.0438 0.0081  0.0705  496 HIS A CA  
3849 C C   . HIS A 496 ? 0.5917 0.5462 0.4634 -0.0396 0.0006  0.0666  496 HIS A C   
3850 O O   . HIS A 496 ? 0.5521 0.5191 0.4193 -0.0355 -0.0057 0.0713  496 HIS A O   
3851 C CB  . HIS A 496 ? 0.5686 0.5486 0.4292 -0.0494 0.0154  0.0497  496 HIS A CB  
3852 C CG  . HIS A 496 ? 0.5951 0.5983 0.4439 -0.0515 0.0122  0.0370  496 HIS A CG  
3853 N ND1 . HIS A 496 ? 0.6235 0.6547 0.4554 -0.0508 0.0076  0.0455  496 HIS A ND1 
3854 C CD2 . HIS A 496 ? 0.5455 0.5498 0.3982 -0.0551 0.0128  0.0165  496 HIS A CD2 
3855 C CE1 . HIS A 496 ? 0.5706 0.6216 0.3963 -0.0546 0.0041  0.0292  496 HIS A CE1 
3856 N NE2 . HIS A 496 ? 0.5768 0.6105 0.4159 -0.0579 0.0079  0.0108  496 HIS A NE2 
3857 N N   . TRP A 497 ? 0.5245 0.4560 0.4080 -0.0401 0.0015  0.0589  497 TRP A N   
3858 C CA  . TRP A 497 ? 0.5408 0.4590 0.4302 -0.0363 -0.0036 0.0555  497 TRP A CA  
3859 C C   . TRP A 497 ? 0.6305 0.5391 0.5221 -0.0300 -0.0086 0.0712  497 TRP A C   
3860 O O   . TRP A 497 ? 0.6188 0.5313 0.5117 -0.0246 -0.0128 0.0723  497 TRP A O   
3861 C CB  . TRP A 497 ? 0.4872 0.3839 0.3856 -0.0380 -0.0014 0.0471  497 TRP A CB  
3862 C CG  . TRP A 497 ? 0.5552 0.4554 0.4557 -0.0410 0.0024  0.0312  497 TRP A CG  
3863 C CD1 . TRP A 497 ? 0.5416 0.4491 0.4433 -0.0452 0.0094  0.0214  497 TRP A CD1 
3864 C CD2 . TRP A 497 ? 0.5566 0.4514 0.4604 -0.0400 0.0014  0.0234  497 TRP A CD2 
3865 N NE1 . TRP A 497 ? 0.5398 0.4443 0.4463 -0.0473 0.0126  0.0080  497 TRP A NE1 
3866 C CE2 . TRP A 497 ? 0.5895 0.4871 0.4972 -0.0446 0.0078  0.0098  497 TRP A CE2 
3867 C CE3 . TRP A 497 ? 0.5661 0.4537 0.4714 -0.0357 -0.0027 0.0264  497 TRP A CE3 
3868 C CZ2 . TRP A 497 ? 0.5976 0.4907 0.5109 -0.0461 0.0099  0.0007  497 TRP A CZ2 
3869 C CZ3 . TRP A 497 ? 0.5506 0.4365 0.4603 -0.0368 -0.0004 0.0170  497 TRP A CZ3 
3870 C CH2 . TRP A 497 ? 0.5839 0.4724 0.4977 -0.0424 0.0056  0.0051  497 TRP A CH2 
3871 N N   . LEU A 498 ? 0.5733 0.4688 0.4682 -0.0305 -0.0072 0.0832  498 LEU A N   
3872 C CA  . LEU A 498 ? 0.6251 0.5064 0.5250 -0.0249 -0.0099 0.0977  498 LEU A CA  
3873 C C   . LEU A 498 ? 0.6463 0.5479 0.5403 -0.0185 -0.0126 0.1115  498 LEU A C   
3874 O O   . LEU A 498 ? 0.6579 0.5523 0.5581 -0.0104 -0.0157 0.1203  498 LEU A O   
3875 C CB  . LEU A 498 ? 0.6114 0.4757 0.5179 -0.0293 -0.0069 0.1071  498 LEU A CB  
3876 C CG  . LEU A 498 ? 0.5898 0.4341 0.5045 -0.0347 -0.0070 0.0963  498 LEU A CG  
3877 C CD1 . LEU A 498 ? 0.5682 0.4073 0.4912 -0.0418 -0.0037 0.1040  498 LEU A CD1 
3878 C CD2 . LEU A 498 ? 0.5858 0.4072 0.5048 -0.0309 -0.0104 0.0925  498 LEU A CD2 
3879 N N   . SER A 499 ? 0.5999 0.5286 0.4822 -0.0214 -0.0114 0.1136  499 SER A N   
3880 C CA  . SER A 499 ? 0.6681 0.6215 0.5422 -0.0156 -0.0153 0.1290  499 SER A CA  
3881 C C   . SER A 499 ? 0.6525 0.6222 0.5284 -0.0098 -0.0225 0.1231  499 SER A C   
3882 O O   . SER A 499 ? 0.6645 0.6514 0.5396 -0.0018 -0.0278 0.1390  499 SER A O   
3883 C CB  . SER A 499 ? 0.6569 0.6387 0.5141 -0.0214 -0.0120 0.1295  499 SER A CB  
3884 O OG  . SER A 499 ? 0.6695 0.6670 0.5205 -0.0276 -0.0115 0.1062  499 SER A OG  
3885 N N   A MET A 500 ? 0.6636 0.6298 0.5439 -0.0135 -0.0225 0.1023  500 MET A N   
3886 N N   B MET A 500 ? 0.6875 0.6539 0.5676 -0.0137 -0.0225 0.1021  500 MET A N   
3887 C CA  A MET A 500 ? 0.6771 0.6605 0.5625 -0.0095 -0.0283 0.0960  500 MET A CA  
3888 C CA  B MET A 500 ? 0.6577 0.6402 0.5434 -0.0097 -0.0281 0.0955  500 MET A CA  
3889 C C   A MET A 500 ? 0.7024 0.6734 0.6012 0.0023  -0.0310 0.1098  500 MET A C   
3890 C C   B MET A 500 ? 0.6838 0.6550 0.5824 0.0023  -0.0310 0.1102  500 MET A C   
3891 O O   A MET A 500 ? 0.7238 0.7170 0.6286 0.0089  -0.0368 0.1136  500 MET A O   
3892 O O   B MET A 500 ? 0.7264 0.7207 0.6303 0.0090  -0.0370 0.1150  500 MET A O   
3893 C CB  A MET A 500 ? 0.6458 0.6222 0.5358 -0.0163 -0.0253 0.0730  500 MET A CB  
3894 C CB  B MET A 500 ? 0.6474 0.6199 0.5384 -0.0160 -0.0248 0.0732  500 MET A CB  
3895 C CG  A MET A 500 ? 0.6408 0.6265 0.5215 -0.0268 -0.0208 0.0578  500 MET A CG  
3896 C CG  B MET A 500 ? 0.6407 0.6233 0.5231 -0.0266 -0.0206 0.0569  500 MET A CG  
3897 S SD  A MET A 500 ? 0.7458 0.7771 0.6121 -0.0311 -0.0255 0.0546  500 MET A SD  
3898 S SD  B MET A 500 ? 0.5756 0.5358 0.4671 -0.0326 -0.0142 0.0367  500 MET A SD  
3899 C CE  A MET A 500 ? 0.6431 0.6724 0.5000 -0.0422 -0.0155 0.0367  500 MET A CE  
3900 C CE  B MET A 500 ? 0.5916 0.5629 0.4939 -0.0299 -0.0182 0.0307  500 MET A CE  
3901 N N   . ALA A 501 ? 0.6493 0.5862 0.5547 0.0049  -0.0268 0.1163  501 ALA A N   
3902 C CA  . ALA A 501 ? 0.7008 0.6217 0.6199 0.0164  -0.0271 0.1279  501 ALA A CA  
3903 C C   . ALA A 501 ? 0.8312 0.7670 0.7519 0.0259  -0.0305 0.1531  501 ALA A C   
3904 O O   . ALA A 501 ? 0.8405 0.7706 0.7754 0.0381  -0.0313 0.1645  501 ALA A O   
3905 C CB  . ALA A 501 ? 0.7463 0.6265 0.6711 0.0146  -0.0213 0.1255  501 ALA A CB  
3906 N N   . HIS A 502 ? 0.8266 0.7816 0.7333 0.0214  -0.0316 0.1630  502 HIS A N   
3907 C CA  . HIS A 502 ? 0.8913 0.8645 0.7960 0.0302  -0.0349 0.1899  502 HIS A CA  
3908 C C   . HIS A 502 ? 0.9086 0.9289 0.8070 0.0341  -0.0447 0.1919  502 HIS A C   
3909 O O   . HIS A 502 ? 1.0129 1.0548 0.9093 0.0432  -0.0495 0.2162  502 HIS A O   
3910 C CB  . HIS A 502 ? 0.8812 0.8535 0.7722 0.0232  -0.0300 0.2018  502 HIS A CB  
3911 C CG  . HIS A 502 ? 0.9215 0.8536 0.8200 0.0164  -0.0215 0.1978  502 HIS A CG  
3912 N ND1 . HIS A 502 ? 1.0039 0.9347 0.8931 0.0058  -0.0156 0.1972  502 HIS A ND1 
3913 C CD2 . HIS A 502 ? 0.9118 0.8063 0.8266 0.0182  -0.0181 0.1930  502 HIS A CD2 
3914 C CE1 . HIS A 502 ? 0.9975 0.8934 0.8990 0.0009  -0.0102 0.1932  502 HIS A CE1 
3915 N NE2 . HIS A 502 ? 1.0157 0.8888 0.9312 0.0078  -0.0119 0.1897  502 HIS A NE2 
3916 N N   . ARG A 503 ? 0.8571 0.8948 0.7535 0.0271  -0.0477 0.1679  503 ARG A N   
3917 C CA  . ARG A 503 ? 0.9217 1.0065 0.8143 0.0281  -0.0578 0.1662  503 ARG A CA  
3918 C C   . ARG A 503 ? 1.0586 1.1529 0.9725 0.0437  -0.0637 0.1807  503 ARG A C   
3919 O O   . ARG A 503 ? 1.0011 1.0672 0.9337 0.0493  -0.0588 0.1756  503 ARG A O   
3920 C CB  . ARG A 503 ? 0.9287 1.0245 0.8185 0.0153  -0.0577 0.1352  503 ARG A CB  
3921 C CG  . ARG A 503 ? 0.8414 0.9330 0.7126 0.0012  -0.0515 0.1198  503 ARG A CG  
3922 C CD  . ARG A 503 ? 1.0392 1.1707 0.8885 -0.0029 -0.0565 0.1248  503 ARG A CD  
3923 N NE  . ARG A 503 ? 1.0667 1.2404 0.9149 -0.0069 -0.0660 0.1120  503 ARG A NE  
3924 C CZ  . ARG A 503 ? 0.9742 1.1623 0.8145 -0.0208 -0.0646 0.0846  503 ARG A CZ  
3925 N NH1 . ARG A 503 ? 0.8601 1.0244 0.6933 -0.0302 -0.0536 0.0683  503 ARG A NH1 
3926 N NH2 . ARG A 503 ? 0.8931 1.1210 0.7352 -0.0254 -0.0742 0.0731  503 ARG A NH2 
3927 N N   . PRO A 504 ? 1.2758 1.4110 1.1877 0.0516  -0.0738 0.1993  504 PRO A N   
3928 C CA  . PRO A 504 ? 1.2788 1.4276 1.2152 0.0682  -0.0797 0.2144  504 PRO A CA  
3929 C C   . PRO A 504 ? 1.2790 1.4452 1.2309 0.0645  -0.0828 0.1908  504 PRO A C   
3930 O O   . PRO A 504 ? 1.2676 1.4624 1.2089 0.0508  -0.0875 0.1704  504 PRO A O   
3931 C CB  . PRO A 504 ? 1.2771 1.4733 1.2035 0.0754  -0.0917 0.2399  504 PRO A CB  
3932 C CG  . PRO A 504 ? 1.2947 1.4880 1.1910 0.0650  -0.0881 0.2438  504 PRO A CG  
3933 C CD  . PRO A 504 ? 1.2789 1.4498 1.1660 0.0473  -0.0799 0.2104  504 PRO A CD  
3934 N N   . ALA A 505 ? 1.0861 1.2339 1.0643 0.0765  -0.0785 0.1931  505 ALA A N   
3935 C CA  . ALA A 505 ? 0.9205 1.0839 0.9180 0.0750  -0.0792 0.1743  505 ALA A CA  
3936 C C   . ALA A 505 ? 0.8551 1.0013 0.8424 0.0566  -0.0723 0.1433  505 ALA A C   
3937 O O   . ALA A 505 ? 0.7916 0.9576 0.7902 0.0502  -0.0734 0.1257  505 ALA A O   
3938 C CB  . ALA A 505 ? 0.9267 1.1527 0.9321 0.0771  -0.0940 0.1792  505 ALA A CB  
3939 N N   . ALA A 506 ? 0.8658 0.9761 0.8343 0.0480  -0.0648 0.1374  506 ALA A N   
3940 C CA  . ALA A 506 ? 0.8131 0.9059 0.7732 0.0325  -0.0581 0.1113  506 ALA A CA  
3941 C C   . ALA A 506 ? 0.7329 0.7977 0.7092 0.0357  -0.0492 0.1011  506 ALA A C   
3942 O O   . ALA A 506 ? 0.7249 0.7576 0.7073 0.0455  -0.0433 0.1100  506 ALA A O   
3943 C CB  . ALA A 506 ? 0.7680 0.8328 0.7073 0.0246  -0.0527 0.1105  506 ALA A CB  
3944 N N   . LYS A 507 ? 0.6876 0.7645 0.6706 0.0268  -0.0474 0.0819  507 LYS A N   
3945 C CA  . LYS A 507 ? 0.6309 0.6846 0.6260 0.0281  -0.0378 0.0714  507 LYS A CA  
3946 C C   . LYS A 507 ? 0.6090 0.6289 0.5879 0.0165  -0.0300 0.0577  507 LYS A C   
3947 O O   . LYS A 507 ? 0.6793 0.7053 0.6555 0.0041  -0.0278 0.0421  507 LYS A O   
3948 C CB  . LYS A 507 ? 0.5855 0.6724 0.6000 0.0250  -0.0389 0.0611  507 LYS A CB  
3949 C CG  . LYS A 507 ? 0.6368 0.7652 0.6700 0.0364  -0.0487 0.0752  507 LYS A CG  
3950 C CD  . LYS A 507 ? 0.6671 0.8354 0.7203 0.0291  -0.0516 0.0626  507 LYS A CD  
3951 C CE  . LYS A 507 ? 0.6557 0.8722 0.7295 0.0407  -0.0635 0.0776  507 LYS A CE  
3952 N NZ  . LYS A 507 ? 0.7570 1.0181 0.8517 0.0306  -0.0680 0.0638  507 LYS A NZ  
3953 N N   . LEU A 508 ? 0.6355 0.6200 0.6056 0.0206  -0.0258 0.0640  508 LEU A N   
3954 C CA  . LEU A 508 ? 0.6083 0.5640 0.5640 0.0109  -0.0204 0.0540  508 LEU A CA  
3955 C C   . LEU A 508 ? 0.6312 0.5734 0.5912 0.0078  -0.0124 0.0409  508 LEU A C   
3956 O O   . LEU A 508 ? 0.5853 0.5183 0.5542 0.0162  -0.0079 0.0423  508 LEU A O   
3957 C CB  . LEU A 508 ? 0.5974 0.5225 0.5456 0.0151  -0.0190 0.0640  508 LEU A CB  
3958 C CG  . LEU A 508 ? 0.6196 0.5545 0.5634 0.0184  -0.0247 0.0804  508 LEU A CG  
3959 C CD1 . LEU A 508 ? 0.6566 0.5583 0.5983 0.0219  -0.0217 0.0900  508 LEU A CD1 
3960 C CD2 . LEU A 508 ? 0.5974 0.5507 0.5281 0.0074  -0.0275 0.0755  508 LEU A CD2 
3961 N N   . PRO A 509 ? 0.6217 0.5616 0.5759 -0.0035 -0.0091 0.0288  509 PRO A N   
3962 C CA  . PRO A 509 ? 0.5516 0.4773 0.5081 -0.0064 -0.0006 0.0196  509 PRO A CA  
3963 C C   . PRO A 509 ? 0.6407 0.5327 0.5859 -0.0031 0.0032  0.0215  509 PRO A C   
3964 O O   . PRO A 509 ? 0.6131 0.4904 0.5488 -0.0029 -0.0002 0.0268  509 PRO A O   
3965 C CB  . PRO A 509 ? 0.5719 0.5019 0.5258 -0.0189 0.0016  0.0091  509 PRO A CB  
3966 C CG  . PRO A 509 ? 0.5600 0.4910 0.5034 -0.0218 -0.0039 0.0121  509 PRO A CG  
3967 C CD  . PRO A 509 ? 0.5769 0.5252 0.5223 -0.0136 -0.0115 0.0235  509 PRO A CD  
3968 N N   . LYS A 510 ? 0.5874 0.4693 0.5336 -0.0014 0.0108  0.0167  510 LYS A N   
3969 C CA  . LYS A 510 ? 0.5737 0.4268 0.5058 -0.0007 0.0142  0.0153  510 LYS A CA  
3970 C C   . LYS A 510 ? 0.5407 0.3839 0.4616 -0.0098 0.0135  0.0131  510 LYS A C   
3971 O O   . LYS A 510 ? 0.5560 0.4101 0.4814 -0.0164 0.0150  0.0097  510 LYS A O   
3972 C CB  . LYS A 510 ? 0.5851 0.4332 0.5179 0.0029  0.0237  0.0102  510 LYS A CB  
3973 C CG  . LYS A 510 ? 0.6743 0.5209 0.6158 0.0144  0.0262  0.0120  510 LYS A CG  
3974 C CD  . LYS A 510 ? 0.6589 0.4973 0.5969 0.0177  0.0376  0.0050  510 LYS A CD  
3975 C CE  . LYS A 510 ? 0.6297 0.4612 0.5765 0.0303  0.0421  0.0048  510 LYS A CE  
3976 N NZ  . LYS A 510 ? 0.7491 0.5553 0.6866 0.0324  0.0372  0.0063  510 LYS A NZ  
3977 N N   . ILE A 511 ? 0.5757 0.3984 0.4842 -0.0100 0.0113  0.0146  511 ILE A N   
3978 C CA  . ILE A 511 ? 0.5349 0.3497 0.4354 -0.0166 0.0095  0.0147  511 ILE A CA  
3979 C C   . ILE A 511 ? 0.5713 0.3704 0.4587 -0.0169 0.0124  0.0127  511 ILE A C   
3980 O O   . ILE A 511 ? 0.5947 0.3816 0.4740 -0.0139 0.0113  0.0110  511 ILE A O   
3981 C CB  . ILE A 511 ? 0.6198 0.4307 0.5189 -0.0180 0.0025  0.0196  511 ILE A CB  
3982 C CG1 . ILE A 511 ? 0.5890 0.4190 0.4966 -0.0193 0.0004  0.0218  511 ILE A CG1 
3983 C CG2 . ILE A 511 ? 0.5187 0.3201 0.4111 -0.0228 0.0005  0.0202  511 ILE A CG2 
3984 C CD1 . ILE A 511 ? 0.6086 0.4376 0.5149 -0.0206 -0.0044 0.0281  511 ILE A CD1 
3985 N N   . PHE A 512 ? 0.5315 0.3312 0.4167 -0.0207 0.0166  0.0128  512 PHE A N   
3986 C CA  . PHE A 512 ? 0.5546 0.3434 0.4251 -0.0210 0.0191  0.0137  512 PHE A CA  
3987 C C   . PHE A 512 ? 0.5629 0.3479 0.4305 -0.0245 0.0147  0.0192  512 PHE A C   
3988 O O   . PHE A 512 ? 0.5637 0.3541 0.4430 -0.0268 0.0139  0.0209  512 PHE A O   
3989 C CB  . PHE A 512 ? 0.5345 0.3276 0.4060 -0.0211 0.0298  0.0131  512 PHE A CB  
3990 C CG  . PHE A 512 ? 0.5507 0.3526 0.4308 -0.0172 0.0353  0.0081  512 PHE A CG  
3991 C CD1 . PHE A 512 ? 0.4890 0.3074 0.3884 -0.0184 0.0363  0.0065  512 PHE A CD1 
3992 C CD2 . PHE A 512 ? 0.5354 0.3312 0.4053 -0.0122 0.0395  0.0043  512 PHE A CD2 
3993 C CE1 . PHE A 512 ? 0.5201 0.3511 0.4310 -0.0138 0.0402  0.0035  512 PHE A CE1 
3994 C CE2 . PHE A 512 ? 0.5229 0.3282 0.4048 -0.0068 0.0456  0.0004  512 PHE A CE2 
3995 C CZ  . PHE A 512 ? 0.4839 0.3079 0.3876 -0.0072 0.0454  0.0012  512 PHE A CZ  
3996 N N   . HIS A 513 ? 0.5393 0.3167 0.3913 -0.0244 0.0121  0.0217  513 HIS A N   
3997 C CA  . HIS A 513 ? 0.5776 0.3543 0.4279 -0.0259 0.0082  0.0296  513 HIS A CA  
3998 C C   . HIS A 513 ? 0.6022 0.3766 0.4383 -0.0248 0.0133  0.0352  513 HIS A C   
3999 O O   . HIS A 513 ? 0.5734 0.3452 0.3912 -0.0240 0.0134  0.0315  513 HIS A O   
4000 C CB  . HIS A 513 ? 0.5335 0.3089 0.3792 -0.0275 -0.0033 0.0298  513 HIS A CB  
4001 C CG  . HIS A 513 ? 0.5414 0.3209 0.3917 -0.0279 -0.0082 0.0390  513 HIS A CG  
4002 N ND1 . HIS A 513 ? 0.5519 0.3328 0.3893 -0.0268 -0.0113 0.0463  513 HIS A ND1 
4003 C CD2 . HIS A 513 ? 0.5598 0.3443 0.4273 -0.0282 -0.0100 0.0428  513 HIS A CD2 
4004 C CE1 . HIS A 513 ? 0.5887 0.3754 0.4377 -0.0256 -0.0156 0.0554  513 HIS A CE1 
4005 N NE2 . HIS A 513 ? 0.6181 0.4063 0.4862 -0.0265 -0.0140 0.0526  513 HIS A NE2 
4006 N N   . VAL A 514 ? 0.5720 0.3465 0.4162 -0.0247 0.0185  0.0441  514 VAL A N   
4007 C CA  . VAL A 514 ? 0.5824 0.3547 0.4147 -0.0233 0.0250  0.0535  514 VAL A CA  
4008 C C   . VAL A 514 ? 0.5948 0.3676 0.4261 -0.0210 0.0188  0.0670  514 VAL A C   
4009 O O   . VAL A 514 ? 0.6422 0.4167 0.4889 -0.0206 0.0132  0.0686  514 VAL A O   
4010 C CB  . VAL A 514 ? 0.6079 0.3785 0.4538 -0.0249 0.0394  0.0549  514 VAL A CB  
4011 C CG1 . VAL A 514 ? 0.5442 0.3198 0.3951 -0.0265 0.0441  0.0425  514 VAL A CG1 
4012 C CG2 . VAL A 514 ? 0.6120 0.3799 0.4815 -0.0264 0.0420  0.0578  514 VAL A CG2 
4013 N N   . ASN A 515 ? 0.5706 0.3440 0.3837 -0.0189 0.0202  0.0779  515 ASN A N   
4014 C CA  . ASN A 515 ? 0.6094 0.3862 0.4213 -0.0150 0.0144  0.0948  515 ASN A CA  
4015 C C   . ASN A 515 ? 0.6876 0.4611 0.4892 -0.0125 0.0254  0.1099  515 ASN A C   
4016 O O   . ASN A 515 ? 0.6745 0.4529 0.4483 -0.0125 0.0249  0.1120  515 ASN A O   
4017 C CB  . ASN A 515 ? 0.6473 0.4348 0.4412 -0.0153 -0.0020 0.0939  515 ASN A CB  
4018 C CG  . ASN A 515 ? 0.6646 0.4612 0.4594 -0.0103 -0.0100 0.1130  515 ASN A CG  
4019 O OD1 . ASN A 515 ? 0.6511 0.4434 0.4669 -0.0055 -0.0037 0.1262  515 ASN A OD1 
4020 N ND2 . ASN A 515 ? 0.6780 0.4881 0.4515 -0.0113 -0.0239 0.1143  515 ASN A ND2 
4021 N N   . TRP A 516 ? 0.6845 0.4489 0.5082 -0.0109 0.0366  0.1198  516 TRP A N   
4022 C CA  . TRP A 516 ? 0.6929 0.4520 0.5109 -0.0087 0.0485  0.1377  516 TRP A CA  
4023 C C   . TRP A 516 ? 0.7218 0.4873 0.5283 -0.0014 0.0405  0.1606  516 TRP A C   
4024 O O   . TRP A 516 ? 0.7349 0.4977 0.5317 0.0015  0.0493  0.1795  516 TRP A O   
4025 C CB  . TRP A 516 ? 0.7284 0.4729 0.5774 -0.0104 0.0643  0.1406  516 TRP A CB  
4026 C CG  . TRP A 516 ? 0.6736 0.4154 0.5394 -0.0179 0.0712  0.1195  516 TRP A CG  
4027 C CD1 . TRP A 516 ? 0.6831 0.4167 0.5786 -0.0215 0.0783  0.1119  516 TRP A CD1 
4028 C CD2 . TRP A 516 ? 0.6777 0.4273 0.5325 -0.0225 0.0716  0.1034  516 TRP A CD2 
4029 N NE1 . TRP A 516 ? 0.6308 0.3697 0.5327 -0.0285 0.0813  0.0928  516 TRP A NE1 
4030 C CE2 . TRP A 516 ? 0.6198 0.3684 0.4989 -0.0283 0.0773  0.0886  516 TRP A CE2 
4031 C CE3 . TRP A 516 ? 0.6741 0.4319 0.5015 -0.0218 0.0680  0.0993  516 TRP A CE3 
4032 C CZ2 . TRP A 516 ? 0.5898 0.3475 0.4685 -0.0322 0.0784  0.0731  516 TRP A CZ2 
4033 C CZ3 . TRP A 516 ? 0.6933 0.4564 0.5220 -0.0252 0.0712  0.0827  516 TRP A CZ3 
4034 C CH2 . TRP A 516 ? 0.6605 0.4245 0.5156 -0.0297 0.0757  0.0713  516 TRP A CH2 
4035 N N   . PHE A 517 ? 0.6995 0.4755 0.5081 0.0016  0.0241  0.1609  517 PHE A N   
4036 C CA  . PHE A 517 ? 0.7575 0.5411 0.5693 0.0101  0.0166  0.1845  517 PHE A CA  
4037 C C   . PHE A 517 ? 0.7220 0.5278 0.5057 0.0108  -0.0027 0.1875  517 PHE A C   
4038 O O   . PHE A 517 ? 0.7254 0.5443 0.5159 0.0174  -0.0141 0.2038  517 PHE A O   
4039 C CB  . PHE A 517 ? 0.7379 0.5170 0.5868 0.0141  0.0157  0.1852  517 PHE A CB  
4040 C CG  . PHE A 517 ? 0.7311 0.4892 0.6077 0.0124  0.0343  0.1803  517 PHE A CG  
4041 C CD1 . PHE A 517 ? 0.7771 0.5208 0.6690 0.0179  0.0480  0.2000  517 PHE A CD1 
4042 C CD2 . PHE A 517 ? 0.7164 0.4694 0.6040 0.0049  0.0379  0.1561  517 PHE A CD2 
4043 C CE1 . PHE A 517 ? 0.7523 0.4758 0.6710 0.0142  0.0654  0.1925  517 PHE A CE1 
4044 C CE2 . PHE A 517 ? 0.6989 0.4359 0.6107 0.0016  0.0537  0.1492  517 PHE A CE2 
4045 C CZ  . PHE A 517 ? 0.7059 0.4274 0.6337 0.0054  0.0676  0.1657  517 PHE A CZ  
4046 N N   . ARG A 518 ? 0.7336 0.5451 0.4875 0.0041  -0.0067 0.1713  518 ARG A N   
4047 C CA  . ARG A 518 ? 0.8040 0.6366 0.5285 0.0029  -0.0243 0.1717  518 ARG A CA  
4048 C C   . ARG A 518 ? 0.8514 0.6951 0.5545 0.0094  -0.0245 0.1988  518 ARG A C   
4049 O O   . ARG A 518 ? 0.8353 0.6682 0.5312 0.0115  -0.0081 0.2102  518 ARG A O   
4050 C CB  . ARG A 518 ? 0.8118 0.6441 0.5092 -0.0057 -0.0251 0.1467  518 ARG A CB  
4051 C CG  . ARG A 518 ? 0.8002 0.6524 0.4720 -0.0103 -0.0445 0.1385  518 ARG A CG  
4052 C CD  . ARG A 518 ? 0.8126 0.6586 0.4644 -0.0186 -0.0430 0.1103  518 ARG A CD  
4053 N NE  . ARG A 518 ? 0.8236 0.6852 0.4582 -0.0255 -0.0616 0.0973  518 ARG A NE  
4054 C CZ  . ARG A 518 ? 0.9142 0.7690 0.5391 -0.0336 -0.0634 0.0709  518 ARG A CZ  
4055 N NH1 . ARG A 518 ? 0.8381 0.6726 0.4691 -0.0341 -0.0484 0.0563  518 ARG A NH1 
4056 N NH2 . ARG A 518 ? 0.8995 0.7686 0.5109 -0.0415 -0.0806 0.0590  518 ARG A NH2 
4057 N N   . LYS A 519 ? 0.8843 0.7515 0.5784 0.0126  -0.0433 0.2105  519 LYS A N   
4058 C CA  . LYS A 519 ? 0.9277 0.8108 0.6012 0.0202  -0.0469 0.2398  519 LYS A CA  
4059 C C   . LYS A 519 ? 0.9938 0.9043 0.6243 0.0146  -0.0647 0.2328  519 LYS A C   
4060 O O   . LYS A 519 ? 1.0174 0.9371 0.6449 0.0062  -0.0787 0.2090  519 LYS A O   
4061 C CB  . LYS A 519 ? 0.9644 0.8556 0.6705 0.0317  -0.0539 0.2665  519 LYS A CB  
4062 C CG  . LYS A 519 ? 0.8822 0.7456 0.6297 0.0379  -0.0346 0.2750  519 LYS A CG  
4063 C CD  . LYS A 519 ? 0.8966 0.7681 0.6773 0.0508  -0.0406 0.3008  519 LYS A CD  
4064 C CE  . LYS A 519 ? 0.9095 0.7504 0.7304 0.0568  -0.0193 0.3080  519 LYS A CE  
4065 N NZ  . LYS A 519 ? 0.9547 0.8013 0.8097 0.0715  -0.0225 0.3343  519 LYS A NZ  
4066 N N   . ASP A 520 ? 1.0591 0.9824 0.6557 0.0185  -0.0635 0.2533  520 ASP A N   
4067 C CA  . ASP A 520 ? 1.1396 1.0923 0.6908 0.0131  -0.0803 0.2476  520 ASP A CA  
4068 C C   . ASP A 520 ? 1.2134 1.1991 0.7705 0.0190  -0.1046 0.2683  520 ASP A C   
4069 O O   . ASP A 520 ? 1.1806 1.1649 0.7796 0.0277  -0.1073 0.2851  520 ASP A O   
4070 C CB  . ASP A 520 ? 1.2133 1.1680 0.7208 0.0141  -0.0671 0.2592  520 ASP A CB  
4071 C CG  . ASP A 520 ? 1.2224 1.1768 0.7373 0.0270  -0.0581 0.3019  520 ASP A CG  
4072 O OD1 . ASP A 520 ? 1.2231 1.1782 0.7755 0.0363  -0.0643 0.3224  520 ASP A OD1 
4073 O OD2 . ASP A 520 ? 1.2238 1.1767 0.7083 0.0283  -0.0434 0.3155  520 ASP A OD2 
4074 N N   . LYS A 521 ? 1.2835 1.3015 0.7986 0.0142  -0.1223 0.2665  521 LYS A N   
4075 C CA  . LYS A 521 ? 1.2983 1.3550 0.8173 0.0187  -0.1482 0.2853  521 LYS A CA  
4076 C C   . LYS A 521 ? 1.3471 1.4080 0.8848 0.0366  -0.1442 0.3290  521 LYS A C   
4077 O O   . LYS A 521 ? 1.4036 1.4864 0.9679 0.0445  -0.1604 0.3425  521 LYS A O   
4078 C CB  . LYS A 521 ? 1.3938 1.4860 0.8588 0.0089  -0.1670 0.2738  521 LYS A CB  
4079 C CG  . LYS A 521 ? 1.5560 1.6442 1.0092 -0.0090 -0.1733 0.2273  521 LYS A CG  
4080 C CD  . LYS A 521 ? 1.7305 1.8563 1.1325 -0.0196 -0.1937 0.2145  521 LYS A CD  
4081 C CE  . LYS A 521 ? 1.7840 1.9023 1.1788 -0.0380 -0.1991 0.1671  521 LYS A CE  
4082 N NZ  . LYS A 521 ? 1.8569 2.0088 1.2074 -0.0487 -0.2173 0.1483  521 LYS A NZ  
4083 N N   . ASN A 522 ? 1.3008 1.3352 0.8330 0.0431  -0.1201 0.3439  522 ASN A N   
4084 C CA  . ASN A 522 ? 1.3033 1.3292 0.8588 0.0584  -0.1113 0.3763  522 ASN A CA  
4085 C C   . ASN A 522 ? 1.2357 1.2303 0.8468 0.0661  -0.0953 0.3859  522 ASN A C   
4086 O O   . ASN A 522 ? 1.2599 1.2401 0.8942 0.0771  -0.0836 0.4093  522 ASN A O   
4087 C CB  . ASN A 522 ? 1.3908 1.4055 0.9104 0.0588  -0.0940 0.3871  522 ASN A CB  
4088 C CG  . ASN A 522 ? 1.4261 1.4695 0.8880 0.0512  -0.1071 0.3753  522 ASN A CG  
4089 O OD1 . ASN A 522 ? 1.4490 1.5249 0.9011 0.0484  -0.1319 0.3659  522 ASN A OD1 
4090 N ND2 . ASN A 522 ? 1.3769 1.4092 0.8018 0.0470  -0.0897 0.3741  522 ASN A ND2 
4091 N N   . GLY A 523 ? 1.2532 1.2365 0.8862 0.0598  -0.0942 0.3672  523 GLY A N   
4092 C CA  . GLY A 523 ? 1.2162 1.1685 0.8998 0.0659  -0.0777 0.3718  523 GLY A CA  
4093 C C   . GLY A 523 ? 1.1818 1.0968 0.8677 0.0649  -0.0489 0.3730  523 GLY A C   
4094 O O   . GLY A 523 ? 1.1827 1.0712 0.9102 0.0708  -0.0333 0.3792  523 GLY A O   
4095 N N   . LYS A 524 ? 1.1368 1.0499 0.7812 0.0563  -0.0408 0.3635  524 LYS A N   
4096 C CA  . LYS A 524 ? 1.0821 0.9647 0.7277 0.0538  -0.0134 0.3647  524 LYS A CA  
4097 C C   . LYS A 524 ? 1.0162 0.8806 0.6674 0.0410  -0.0050 0.3245  524 LYS A C   
4098 O O   . LYS A 524 ? 0.9998 0.8775 0.6281 0.0324  -0.0172 0.2977  524 LYS A O   
4099 C CB  . LYS A 524 ? 1.0975 0.9891 0.6992 0.0518  -0.0079 0.3746  524 LYS A CB  
4100 C CG  . LYS A 524 ? 1.1406 1.0043 0.7492 0.0486  0.0203  0.3791  524 LYS A CG  
4101 C CD  . LYS A 524 ? 1.2016 1.0771 0.7711 0.0478  0.0247  0.3940  524 LYS A CD  
4102 C CE  . LYS A 524 ? 1.1513 1.0021 0.7325 0.0435  0.0526  0.4003  524 LYS A CE  
4103 N NZ  . LYS A 524 ? 1.2156 1.0783 0.7597 0.0429  0.0577  0.4172  524 LYS A NZ  
4104 N N   . PHE A 525 ? 0.9801 0.8145 0.6634 0.0398  0.0159  0.3206  525 PHE A N   
4105 C CA  . PHE A 525 ? 0.9090 0.7283 0.6006 0.0289  0.0243  0.2859  525 PHE A CA  
4106 C C   . PHE A 525 ? 0.9581 0.7844 0.6079 0.0211  0.0293  0.2714  525 PHE A C   
4107 O O   . PHE A 525 ? 0.9736 0.8000 0.6016 0.0223  0.0423  0.2889  525 PHE A O   
4108 C CB  . PHE A 525 ? 0.9305 0.7205 0.6609 0.0282  0.0462  0.2869  525 PHE A CB  
4109 C CG  . PHE A 525 ? 0.9020 0.6816 0.6763 0.0333  0.0434  0.2879  525 PHE A CG  
4110 C CD1 . PHE A 525 ? 0.8566 0.6453 0.6415 0.0313  0.0278  0.2669  525 PHE A CD1 
4111 C CD2 . PHE A 525 ? 0.9236 0.6834 0.7294 0.0401  0.0582  0.3096  525 PHE A CD2 
4112 C CE1 . PHE A 525 ? 0.8880 0.6688 0.7122 0.0361  0.0272  0.2672  525 PHE A CE1 
4113 C CE2 . PHE A 525 ? 0.8577 0.6074 0.7038 0.0452  0.0576  0.3083  525 PHE A CE2 
4114 C CZ  . PHE A 525 ? 0.8377 0.5992 0.6921 0.0434  0.0422  0.2869  525 PHE A CZ  
4115 N N   . LEU A 526 ? 0.9256 0.7571 0.5653 0.0134  0.0202  0.2398  526 LEU A N   
4116 C CA  . LEU A 526 ? 0.9738 0.8095 0.5784 0.0066  0.0266  0.2216  526 LEU A CA  
4117 C C   . LEU A 526 ? 0.9644 0.7807 0.5849 0.0024  0.0497  0.2111  526 LEU A C   
4118 O O   . LEU A 526 ? 1.0056 0.8250 0.6000 -0.0008 0.0614  0.2047  526 LEU A O   
4119 C CB  . LEU A 526 ? 0.9378 0.7830 0.5298 0.0004  0.0099  0.1916  526 LEU A CB  
4120 C CG  . LEU A 526 ? 0.9833 0.8535 0.5520 0.0008  -0.0140 0.1955  526 LEU A CG  
4121 C CD1 . LEU A 526 ? 1.0169 0.8904 0.5826 -0.0075 -0.0277 0.1633  526 LEU A CD1 
4122 C CD2 . LEU A 526 ? 1.0906 0.9794 0.6114 0.0018  -0.0136 0.2091  526 LEU A CD2 
4123 N N   . TRP A 527 ? 0.9193 0.7184 0.5824 0.0021  0.0565  0.2085  527 TRP A N   
4124 C CA  . TRP A 527 ? 0.8720 0.6565 0.5555 -0.0032 0.0755  0.1962  527 TRP A CA  
4125 C C   . TRP A 527 ? 0.8738 0.6427 0.5868 -0.0015 0.0913  0.2176  527 TRP A C   
4126 O O   . TRP A 527 ? 0.8049 0.5664 0.5432 0.0030  0.0859  0.2282  527 TRP A O   
4127 C CB  . TRP A 527 ? 0.8139 0.5934 0.5216 -0.0073 0.0688  0.1687  527 TRP A CB  
4128 C CG  . TRP A 527 ? 0.7614 0.5324 0.4896 -0.0129 0.0847  0.1538  527 TRP A CG  
4129 C CD1 . TRP A 527 ? 0.7380 0.4982 0.5037 -0.0158 0.0907  0.1483  527 TRP A CD1 
4130 C CD2 . TRP A 527 ? 0.7905 0.5662 0.5038 -0.0162 0.0962  0.1415  527 TRP A CD2 
4131 N NE1 . TRP A 527 ? 0.7204 0.4808 0.4960 -0.0213 0.1034  0.1343  527 TRP A NE1 
4132 C CE2 . TRP A 527 ? 0.7333 0.5030 0.4791 -0.0208 0.1075  0.1307  527 TRP A CE2 
4133 C CE3 . TRP A 527 ? 0.7995 0.5855 0.4757 -0.0157 0.0984  0.1376  527 TRP A CE3 
4134 C CZ2 . TRP A 527 ? 0.7462 0.5213 0.4918 -0.0240 0.1204  0.1183  527 TRP A CZ2 
4135 C CZ3 . TRP A 527 ? 0.8261 0.6145 0.5012 -0.0184 0.1133  0.1241  527 TRP A CZ3 
4136 C CH2 . TRP A 527 ? 0.7073 0.4911 0.4186 -0.0220 0.1239  0.1156  527 TRP A CH2 
4137 N N   . PRO A 528 ? 0.8775 0.6404 0.5904 -0.0052 0.1121  0.2241  528 PRO A N   
4138 C CA  . PRO A 528 ? 0.8514 0.5965 0.5950 -0.0052 0.1287  0.2441  528 PRO A CA  
4139 C C   . PRO A 528 ? 0.8249 0.5549 0.6131 -0.0098 0.1314  0.2278  528 PRO A C   
4140 O O   . PRO A 528 ? 0.8795 0.5932 0.6962 -0.0077 0.1379  0.2420  528 PRO A O   
4141 C CB  . PRO A 528 ? 0.8239 0.5697 0.5562 -0.0106 0.1504  0.2498  528 PRO A CB  
4142 C CG  . PRO A 528 ? 0.8735 0.6340 0.5842 -0.0145 0.1468  0.2226  528 PRO A CG  
4143 C CD  . PRO A 528 ? 0.8495 0.6217 0.5360 -0.0095 0.1227  0.2137  528 PRO A CD  
4144 N N   . GLY A 529 ? 0.7691 0.5041 0.5642 -0.0157 0.1272  0.1988  529 GLY A N   
4145 C CA  . GLY A 529 ? 0.7419 0.4673 0.5741 -0.0200 0.1270  0.1823  529 GLY A CA  
4146 C C   . GLY A 529 ? 0.8100 0.5216 0.6738 -0.0281 0.1476  0.1833  529 GLY A C   
4147 O O   . GLY A 529 ? 0.8082 0.5197 0.6674 -0.0321 0.1635  0.1924  529 GLY A O   
4148 N N   . PHE A 530 ? 0.7227 0.4236 0.6196 -0.0315 0.1478  0.1723  530 PHE A N   
4149 C CA  . PHE A 530 ? 0.7474 0.4344 0.6792 -0.0413 0.1657  0.1680  530 PHE A CA  
4150 C C   . PHE A 530 ? 0.8060 0.5072 0.7386 -0.0510 0.1729  0.1512  530 PHE A C   
4151 O O   . PHE A 530 ? 0.7236 0.4411 0.6478 -0.0512 0.1611  0.1316  530 PHE A O   
4152 C CB  . PHE A 530 ? 0.8324 0.4999 0.7727 -0.0388 0.1812  0.1968  530 PHE A CB  
4153 C CG  . PHE A 530 ? 0.8541 0.5092 0.8001 -0.0276 0.1740  0.2133  530 PHE A CG  
4154 C CD1 . PHE A 530 ? 0.7960 0.4402 0.7732 -0.0284 0.1722  0.1995  530 PHE A CD1 
4155 C CD2 . PHE A 530 ? 0.8728 0.5338 0.7937 -0.0159 0.1670  0.2400  530 PHE A CD2 
4156 C CE1 . PHE A 530 ? 0.7697 0.4103 0.7557 -0.0168 0.1636  0.2109  530 PHE A CE1 
4157 C CE2 . PHE A 530 ? 0.8852 0.5444 0.8158 -0.0049 0.1564  0.2523  530 PHE A CE2 
4158 C CZ  . PHE A 530 ? 0.8270 0.4752 0.7914 -0.0048 0.1556  0.2380  530 PHE A CZ  
4159 N N   . GLY A 531 ? 0.7654 0.4620 0.7104 -0.0588 0.1925  0.1592  531 GLY A N   
4160 C CA  . GLY A 531 ? 0.7181 0.4317 0.6695 -0.0677 0.2001  0.1438  531 GLY A CA  
4161 C C   . GLY A 531 ? 0.7655 0.4992 0.6829 -0.0614 0.1924  0.1396  531 GLY A C   
4162 O O   . GLY A 531 ? 0.7726 0.5235 0.6967 -0.0655 0.1926  0.1214  531 GLY A O   
4163 N N   . GLU A 532 ? 0.7187 0.4517 0.6009 -0.0512 0.1856  0.1554  532 GLU A N   
4164 C CA  . GLU A 532 ? 0.7448 0.4946 0.5930 -0.0459 0.1789  0.1487  532 GLU A CA  
4165 C C   . GLU A 532 ? 0.7530 0.5116 0.6005 -0.0433 0.1606  0.1253  532 GLU A C   
4166 O O   . GLU A 532 ? 0.7328 0.5041 0.5624 -0.0406 0.1577  0.1137  532 GLU A O   
4167 C CB  . GLU A 532 ? 0.7760 0.5248 0.5856 -0.0372 0.1741  0.1696  532 GLU A CB  
4168 C CG  . GLU A 532 ? 0.7437 0.4848 0.5491 -0.0381 0.1924  0.1974  532 GLU A CG  
4169 C CD  . GLU A 532 ? 0.7641 0.5148 0.5696 -0.0446 0.2132  0.1958  532 GLU A CD  
4170 O OE1 . GLU A 532 ? 0.8164 0.5807 0.6267 -0.0474 0.2127  0.1726  532 GLU A OE1 
4171 O OE2 . GLU A 532 ? 0.8871 0.6325 0.6896 -0.0465 0.2307  0.2193  532 GLU A OE2 
4172 N N   . ASN A 533 ? 0.6913 0.4427 0.5586 -0.0439 0.1498  0.1185  533 ASN A N   
4173 C CA  . ASN A 533 ? 0.6846 0.4442 0.5534 -0.0422 0.1339  0.0985  533 ASN A CA  
4174 C C   . ASN A 533 ? 0.6910 0.4653 0.5760 -0.0471 0.1386  0.0805  533 ASN A C   
4175 O O   . ASN A 533 ? 0.6619 0.4449 0.5447 -0.0442 0.1269  0.0662  533 ASN A O   
4176 C CB  . ASN A 533 ? 0.6650 0.4156 0.5539 -0.0428 0.1250  0.0954  533 ASN A CB  
4177 C CG  . ASN A 533 ? 0.7134 0.4537 0.5891 -0.0356 0.1174  0.1125  533 ASN A CG  
4178 O OD1 . ASN A 533 ? 0.6908 0.4354 0.5373 -0.0296 0.1111  0.1216  533 ASN A OD1 
4179 N ND2 . ASN A 533 ? 0.6742 0.4026 0.5726 -0.0360 0.1181  0.1160  533 ASN A ND2 
4180 N N   . SER A 534 ? 0.7498 0.5281 0.6532 -0.0544 0.1555  0.0822  534 SER A N   
4181 C CA  . SER A 534 ? 0.7231 0.5206 0.6434 -0.0581 0.1598  0.0669  534 SER A CA  
4182 C C   . SER A 534 ? 0.6338 0.4419 0.5295 -0.0497 0.1576  0.0619  534 SER A C   
4183 O O   . SER A 534 ? 0.6460 0.4693 0.5532 -0.0482 0.1546  0.0479  534 SER A O   
4184 C CB  . SER A 534 ? 0.6640 0.4656 0.6085 -0.0682 0.1798  0.0715  534 SER A CB  
4185 O OG  . SER A 534 ? 0.6975 0.4924 0.6215 -0.0662 0.1936  0.0897  534 SER A OG  
4186 N N   . ARG A 535 ? 0.6529 0.4536 0.5152 -0.0441 0.1593  0.0731  535 ARG A N   
4187 C CA  . ARG A 535 ? 0.7114 0.5192 0.5474 -0.0367 0.1575  0.0654  535 ARG A CA  
4188 C C   . ARG A 535 ? 0.7080 0.5139 0.5386 -0.0313 0.1384  0.0524  535 ARG A C   
4189 O O   . ARG A 535 ? 0.6181 0.4311 0.4453 -0.0264 0.1373  0.0397  535 ARG A O   
4190 C CB  . ARG A 535 ? 0.6605 0.4627 0.4587 -0.0334 0.1625  0.0794  535 ARG A CB  
4191 C CG  . ARG A 535 ? 0.7172 0.5191 0.5184 -0.0385 0.1822  0.0971  535 ARG A CG  
4192 C CD  . ARG A 535 ? 0.8141 0.6108 0.5758 -0.0346 0.1831  0.1153  535 ARG A CD  
4193 N NE  . ARG A 535 ? 0.8263 0.6205 0.5911 -0.0390 0.2023  0.1368  535 ARG A NE  
4194 C CZ  . ARG A 535 ? 0.8565 0.6606 0.6065 -0.0399 0.2211  0.1422  535 ARG A CZ  
4195 N NH1 . ARG A 535 ? 0.8472 0.6643 0.5780 -0.0360 0.2240  0.1261  535 ARG A NH1 
4196 N NH2 . ARG A 535 ? 0.7820 0.5820 0.5376 -0.0446 0.2390  0.1646  535 ARG A NH2 
4197 N N   . VAL A 536 ? 0.6928 0.4886 0.5245 -0.0318 0.1246  0.0561  536 VAL A N   
4198 C CA  . VAL A 536 ? 0.6609 0.4553 0.4912 -0.0282 0.1077  0.0453  536 VAL A CA  
4199 C C   . VAL A 536 ? 0.6198 0.4246 0.4802 -0.0300 0.1058  0.0337  536 VAL A C   
4200 O O   . VAL A 536 ? 0.6344 0.4437 0.4952 -0.0253 0.0988  0.0235  536 VAL A O   
4201 C CB  . VAL A 536 ? 0.6868 0.4706 0.5117 -0.0282 0.0951  0.0535  536 VAL A CB  
4202 C CG1 . VAL A 536 ? 0.7370 0.5205 0.5648 -0.0260 0.0793  0.0430  536 VAL A CG1 
4203 C CG2 . VAL A 536 ? 0.6286 0.4075 0.4225 -0.0254 0.0940  0.0659  536 VAL A CG2 
4204 N N   . LEU A 537 ? 0.6248 0.4339 0.5111 -0.0370 0.1118  0.0353  537 LEU A N   
4205 C CA  . LEU A 537 ? 0.6123 0.4367 0.5261 -0.0399 0.1092  0.0241  537 LEU A CA  
4206 C C   . LEU A 537 ? 0.5811 0.4219 0.5013 -0.0359 0.1160  0.0173  537 LEU A C   
4207 O O   . LEU A 537 ? 0.5677 0.4212 0.5008 -0.0324 0.1086  0.0090  537 LEU A O   
4208 C CB  . LEU A 537 ? 0.5878 0.4147 0.5277 -0.0504 0.1164  0.0246  537 LEU A CB  
4209 C CG  . LEU A 537 ? 0.6277 0.4377 0.5682 -0.0539 0.1125  0.0300  537 LEU A CG  
4210 C CD1 . LEU A 537 ? 0.6655 0.4763 0.6347 -0.0653 0.1221  0.0267  537 LEU A CD1 
4211 C CD2 . LEU A 537 ? 0.5659 0.3751 0.5014 -0.0499 0.0961  0.0240  537 LEU A CD2 
4212 N N   . GLU A 538 ? 0.5683 0.4103 0.4808 -0.0356 0.1309  0.0220  538 GLU A N   
4213 C CA  . GLU A 538 ? 0.5718 0.4298 0.4915 -0.0305 0.1396  0.0153  538 GLU A CA  
4214 C C   . GLU A 538 ? 0.5929 0.4467 0.4976 -0.0197 0.1302  0.0077  538 GLU A C   
4215 O O   . GLU A 538 ? 0.5768 0.4446 0.4995 -0.0139 0.1293  0.0003  538 GLU A O   
4216 C CB  . GLU A 538 ? 0.6180 0.4763 0.5257 -0.0315 0.1584  0.0221  538 GLU A CB  
4217 C CG  . GLU A 538 ? 0.6616 0.5364 0.5762 -0.0249 0.1701  0.0146  538 GLU A CG  
4218 C CD  . GLU A 538 ? 0.7059 0.5824 0.6060 -0.0262 0.1907  0.0214  538 GLU A CD  
4219 O OE1 . GLU A 538 ? 0.6567 0.5174 0.5256 -0.0276 0.1922  0.0312  538 GLU A OE1 
4220 O OE2 . GLU A 538 ? 0.7324 0.6285 0.6529 -0.0255 0.2055  0.0179  538 GLU A OE2 
4221 N N   . TRP A 539 ? 0.6191 0.4541 0.4931 -0.0169 0.1231  0.0097  539 TRP A N   
4222 C CA  . TRP A 539 ? 0.6139 0.4413 0.4749 -0.0087 0.1147  0.0011  539 TRP A CA  
4223 C C   . TRP A 539 ? 0.6239 0.4546 0.5046 -0.0070 0.1006  -0.0021 539 TRP A C   
4224 O O   . TRP A 539 ? 0.6134 0.4480 0.5034 0.0006  0.0990  -0.0084 539 TRP A O   
4225 C CB  . TRP A 539 ? 0.6719 0.4814 0.4979 -0.0090 0.1083  0.0032  539 TRP A CB  
4226 C CG  . TRP A 539 ? 0.6746 0.4738 0.4876 -0.0029 0.1009  -0.0076 539 TRP A CG  
4227 C CD1 . TRP A 539 ? 0.7095 0.5063 0.5117 0.0032  0.1099  -0.0183 539 TRP A CD1 
4228 C CD2 . TRP A 539 ? 0.6716 0.4603 0.4830 -0.0031 0.0846  -0.0095 539 TRP A CD2 
4229 N NE1 . TRP A 539 ? 0.7215 0.5043 0.5163 0.0064  0.1001  -0.0275 539 TRP A NE1 
4230 C CE2 . TRP A 539 ? 0.6913 0.4696 0.4919 0.0022  0.0844  -0.0213 539 TRP A CE2 
4231 C CE3 . TRP A 539 ? 0.6438 0.4305 0.4631 -0.0075 0.0718  -0.0029 539 TRP A CE3 
4232 C CZ2 . TRP A 539 ? 0.6769 0.4426 0.4756 0.0021  0.0713  -0.0255 539 TRP A CZ2 
4233 C CZ3 . TRP A 539 ? 0.6247 0.4016 0.4411 -0.0069 0.0591  -0.0064 539 TRP A CZ3 
4234 C CH2 . TRP A 539 ? 0.6377 0.4040 0.4445 -0.0027 0.0587  -0.0171 539 TRP A CH2 
4235 N N   . MET A 540 ? 0.5832 0.4125 0.4705 -0.0135 0.0915  0.0029  540 MET A N   
4236 C CA  . MET A 540 ? 0.5991 0.4350 0.5031 -0.0127 0.0794  0.0005  540 MET A CA  
4237 C C   . MET A 540 ? 0.5459 0.4055 0.4781 -0.0107 0.0831  -0.0030 540 MET A C   
4238 O O   . MET A 540 ? 0.5662 0.4329 0.5083 -0.0039 0.0760  -0.0049 540 MET A O   
4239 C CB  . MET A 540 ? 0.5409 0.3738 0.4484 -0.0206 0.0725  0.0046  540 MET A CB  
4240 C CG  . MET A 540 ? 0.5615 0.3756 0.4467 -0.0220 0.0682  0.0104  540 MET A CG  
4241 S SD  . MET A 540 ? 0.6337 0.4455 0.5304 -0.0298 0.0647  0.0149  540 MET A SD  
4242 C CE  . MET A 540 ? 0.6243 0.4186 0.4974 -0.0276 0.0565  0.0227  540 MET A CE  
4243 N N   . PHE A 541 ? 0.4804 0.3537 0.4275 -0.0165 0.0940  -0.0027 541 PHE A N   
4244 C CA  . PHE A 541 ? 0.5483 0.4495 0.5255 -0.0159 0.0972  -0.0062 541 PHE A CA  
4245 C C   . PHE A 541 ? 0.5618 0.4686 0.5428 -0.0028 0.1006  -0.0087 541 PHE A C   
4246 O O   . PHE A 541 ? 0.5864 0.5105 0.5868 0.0036  0.0937  -0.0093 541 PHE A O   
4247 C CB  . PHE A 541 ? 0.5046 0.4170 0.4966 -0.0254 0.1114  -0.0056 541 PHE A CB  
4248 C CG  . PHE A 541 ? 0.5585 0.5040 0.5861 -0.0293 0.1120  -0.0101 541 PHE A CG  
4249 C CD1 . PHE A 541 ? 0.5250 0.4920 0.5704 -0.0204 0.1172  -0.0119 541 PHE A CD1 
4250 C CD2 . PHE A 541 ? 0.5475 0.5040 0.5922 -0.0421 0.1077  -0.0135 541 PHE A CD2 
4251 C CE1 . PHE A 541 ? 0.5042 0.5070 0.5851 -0.0241 0.1162  -0.0152 541 PHE A CE1 
4252 C CE2 . PHE A 541 ? 0.5318 0.5227 0.6094 -0.0476 0.1067  -0.0193 541 PHE A CE2 
4253 C CZ  . PHE A 541 ? 0.5139 0.5298 0.6101 -0.0386 0.1101  -0.0192 541 PHE A CZ  
4254 N N   . GLY A 542 ? 0.5303 0.4229 0.4924 0.0020  0.1118  -0.0100 542 GLY A N   
4255 C CA  . GLY A 542 ? 0.5872 0.4810 0.5526 0.0149  0.1174  -0.0147 542 GLY A CA  
4256 C C   . GLY A 542 ? 0.6137 0.4930 0.5730 0.0230  0.1046  -0.0157 542 GLY A C   
4257 O O   . GLY A 542 ? 0.6114 0.4989 0.5890 0.0340  0.1044  -0.0165 542 GLY A O   
4258 N N   . ARG A 543 ? 0.5945 0.4525 0.5305 0.0179  0.0943  -0.0142 543 ARG A N   
4259 C CA  . ARG A 543 ? 0.6055 0.4487 0.5368 0.0235  0.0829  -0.0143 543 ARG A CA  
4260 C C   . ARG A 543 ? 0.6317 0.4934 0.5878 0.0261  0.0725  -0.0082 543 ARG A C   
4261 O O   . ARG A 543 ? 0.5963 0.4530 0.5593 0.0351  0.0676  -0.0061 543 ARG A O   
4262 C CB  . ARG A 543 ? 0.5602 0.3820 0.4651 0.0159  0.0742  -0.0135 543 ARG A CB  
4263 C CG  . ARG A 543 ? 0.6245 0.4270 0.5012 0.0158  0.0804  -0.0201 543 ARG A CG  
4264 C CD  . ARG A 543 ? 0.7075 0.4970 0.5835 0.0254  0.0842  -0.0289 543 ARG A CD  
4265 N NE  . ARG A 543 ? 0.6575 0.4358 0.5401 0.0273  0.0721  -0.0267 543 ARG A NE  
4266 C CZ  . ARG A 543 ? 0.7627 0.5309 0.6565 0.0368  0.0740  -0.0302 543 ARG A CZ  
4267 N NH1 . ARG A 543 ? 0.7999 0.5684 0.7016 0.0464  0.0875  -0.0374 543 ARG A NH1 
4268 N NH2 . ARG A 543 ? 0.7727 0.5297 0.6718 0.0370  0.0635  -0.0255 543 ARG A NH2 
4269 N N   . ILE A 544 ? 0.5973 0.4803 0.5665 0.0179  0.0694  -0.0054 544 ILE A N   
4270 C CA  . ILE A 544 ? 0.6281 0.5344 0.6184 0.0195  0.0590  -0.0007 544 ILE A CA  
4271 C C   . ILE A 544 ? 0.5880 0.5179 0.6052 0.0306  0.0636  0.0007  544 ILE A C   
4272 O O   . ILE A 544 ? 0.5606 0.5029 0.5919 0.0391  0.0552  0.0073  544 ILE A O   
4273 C CB  . ILE A 544 ? 0.5865 0.5092 0.5827 0.0061  0.0551  -0.0018 544 ILE A CB  
4274 C CG1 . ILE A 544 ? 0.5306 0.4311 0.5046 -0.0017 0.0492  -0.0013 544 ILE A CG1 
4275 C CG2 . ILE A 544 ? 0.5774 0.5323 0.5957 0.0068  0.0453  0.0007  544 ILE A CG2 
4276 C CD1 . ILE A 544 ? 0.5578 0.4669 0.5367 -0.0147 0.0491  -0.0044 544 ILE A CD1 
4277 N N   . GLU A 545 ? 0.5550 0.4931 0.5810 0.0314  0.0776  -0.0040 545 GLU A N   
4278 C CA  . GLU A 545 ? 0.5958 0.5572 0.6502 0.0433  0.0841  -0.0029 545 GLU A CA  
4279 C C   . GLU A 545 ? 0.5787 0.5192 0.6299 0.0593  0.0886  -0.0029 545 GLU A C   
4280 O O   . GLU A 545 ? 0.5989 0.5566 0.6766 0.0725  0.0934  -0.0003 545 GLU A O   
4281 C CB  . GLU A 545 ? 0.5966 0.5733 0.6624 0.0388  0.1001  -0.0081 545 GLU A CB  
4282 C CG  . GLU A 545 ? 0.5412 0.5432 0.6216 0.0234  0.0976  -0.0087 545 GLU A CG  
4283 C CD  . GLU A 545 ? 0.6265 0.6506 0.7285 0.0201  0.1140  -0.0118 545 GLU A CD  
4284 O OE1 . GLU A 545 ? 0.7213 0.7334 0.8152 0.0269  0.1297  -0.0141 545 GLU A OE1 
4285 O OE2 . GLU A 545 ? 0.6647 0.7191 0.7920 0.0099  0.1119  -0.0129 545 GLU A OE2 
4286 N N   . GLY A 546 ? 0.6017 0.5063 0.6238 0.0582  0.0877  -0.0063 546 GLY A N   
4287 C CA  . GLY A 546 ? 0.6911 0.5714 0.7096 0.0709  0.0925  -0.0092 546 GLY A CA  
4288 C C   . GLY A 546 ? 0.6632 0.5263 0.6671 0.0736  0.1098  -0.0216 546 GLY A C   
4289 O O   . GLY A 546 ? 0.6373 0.4847 0.6460 0.0860  0.1176  -0.0267 546 GLY A O   
4290 N N   . GLU A 547 ? 0.6610 0.5258 0.6469 0.0628  0.1167  -0.0264 547 GLU A N   
4291 C CA  . GLU A 547 ? 0.7335 0.5857 0.7013 0.0648  0.1338  -0.0376 547 GLU A CA  
4292 C C   . GLU A 547 ? 0.7510 0.5676 0.6869 0.0639  0.1312  -0.0467 547 GLU A C   
4293 O O   . GLU A 547 ? 0.6997 0.5030 0.6175 0.0548  0.1175  -0.0436 547 GLU A O   
4294 C CB  . GLU A 547 ? 0.6479 0.5118 0.6032 0.0529  0.1415  -0.0367 547 GLU A CB  
4295 C CG  . GLU A 547 ? 0.7613 0.6606 0.7503 0.0525  0.1487  -0.0315 547 GLU A CG  
4296 C CD  . GLU A 547 ? 0.9035 0.8105 0.8821 0.0397  0.1581  -0.0292 547 GLU A CD  
4297 O OE1 . GLU A 547 ? 0.9398 0.8261 0.8834 0.0342  0.1617  -0.0311 547 GLU A OE1 
4298 O OE2 . GLU A 547 ? 0.9247 0.8594 0.9312 0.0347  0.1617  -0.0248 547 GLU A OE2 
4299 N N   . ASP A 548 ? 0.9035 0.7060 0.8342 0.0730  0.1453  -0.0593 548 ASP A N   
4300 C CA  . ASP A 548 ? 0.9191 0.6885 0.8212 0.0714  0.1444  -0.0721 548 ASP A CA  
4301 C C   . ASP A 548 ? 0.9163 0.6807 0.7780 0.0591  0.1470  -0.0786 548 ASP A C   
4302 O O   . ASP A 548 ? 0.9291 0.6844 0.7687 0.0604  0.1604  -0.0930 548 ASP A O   
4303 C CB  . ASP A 548 ? 0.9796 0.7352 0.8932 0.0858  0.1598  -0.0853 548 ASP A CB  
4304 C CG  . ASP A 548 ? 1.0696 0.7892 0.9582 0.0831  0.1586  -0.1013 548 ASP A CG  
4305 O OD1 . ASP A 548 ? 1.1077 0.8160 0.9735 0.0705  0.1436  -0.0999 548 ASP A OD1 
4306 O OD2 . ASP A 548 ? 1.0961 0.7992 0.9896 0.0933  0.1732  -0.1162 548 ASP A OD2 
4307 N N   . SER A 549 ? 0.7865 0.5579 0.6384 0.0476  0.1341  -0.0671 549 SER A N   
4308 C CA  . SER A 549 ? 0.8020 0.5729 0.6196 0.0369  0.1346  -0.0670 549 SER A CA  
4309 C C   . SER A 549 ? 0.7440 0.4983 0.5383 0.0278  0.1174  -0.0667 549 SER A C   
4310 O O   . SER A 549 ? 0.7490 0.5060 0.5189 0.0192  0.1138  -0.0617 549 SER A O   
4311 C CB  . SER A 549 ? 0.7688 0.5627 0.5972 0.0313  0.1369  -0.0527 549 SER A CB  
4312 O OG  . SER A 549 ? 0.7313 0.5315 0.5809 0.0279  0.1223  -0.0417 549 SER A OG  
4313 N N   . ALA A 550 ? 0.7842 0.5225 0.5874 0.0297  0.1072  -0.0704 550 ALA A N   
4314 C CA  . ALA A 550 ? 0.7885 0.5147 0.5768 0.0205  0.0905  -0.0689 550 ALA A CA  
4315 C C   . ALA A 550 ? 0.8166 0.5198 0.5857 0.0188  0.0902  -0.0868 550 ALA A C   
4316 O O   . ALA A 550 ? 0.7398 0.4302 0.5189 0.0270  0.1002  -0.0987 550 ALA A O   
4317 C CB  . ALA A 550 ? 0.7782 0.5059 0.5930 0.0209  0.0779  -0.0570 550 ALA A CB  
4318 N N   . LYS A 551 ? 0.8537 0.5526 0.5972 0.0081  0.0787  -0.0892 551 LYS A N   
4319 C CA  . LYS A 551 ? 0.8249 0.5041 0.5508 0.0025  0.0743  -0.1070 551 LYS A CA  
4320 C C   . LYS A 551 ? 0.7829 0.4554 0.5192 -0.0050 0.0566  -0.1004 551 LYS A C   
4321 O O   . LYS A 551 ? 0.7367 0.4231 0.4762 -0.0092 0.0460  -0.0843 551 LYS A O   
4322 C CB  . LYS A 551 ? 0.8415 0.5262 0.5264 -0.0050 0.0750  -0.1169 551 LYS A CB  
4323 C CG  . LYS A 551 ? 0.9392 0.6081 0.6037 -0.0144 0.0669  -0.1368 551 LYS A CG  
4324 C CD  . LYS A 551 ? 1.0712 0.7517 0.6920 -0.0220 0.0658  -0.1454 551 LYS A CD  
4325 C CE  . LYS A 551 ? 1.0438 0.7477 0.6547 -0.0256 0.0552  -0.1221 551 LYS A CE  
4326 N NZ  . LYS A 551 ? 1.1890 0.9067 0.7562 -0.0325 0.0518  -0.1267 551 LYS A NZ  
4327 N N   . LEU A 552 ? 0.8507 0.5010 0.5941 -0.0068 0.0549  -0.1130 552 LEU A N   
4328 C CA  . LEU A 552 ? 0.8090 0.4523 0.5654 -0.0144 0.0402  -0.1068 552 LEU A CA  
4329 C C   . LEU A 552 ? 0.8422 0.4892 0.5734 -0.0285 0.0271  -0.1143 552 LEU A C   
4330 O O   . LEU A 552 ? 0.8535 0.4932 0.5605 -0.0338 0.0295  -0.1342 552 LEU A O   
4331 C CB  . LEU A 552 ? 0.8130 0.4299 0.5915 -0.0109 0.0449  -0.1149 552 LEU A CB  
4332 C CG  . LEU A 552 ? 0.8509 0.4578 0.6453 -0.0192 0.0326  -0.1085 552 LEU A CG  
4333 C CD1 . LEU A 552 ? 0.8566 0.4818 0.6695 -0.0163 0.0253  -0.0838 552 LEU A CD1 
4334 C CD2 . LEU A 552 ? 0.7985 0.3746 0.6129 -0.0159 0.0403  -0.1177 552 LEU A CD2 
4335 N N   . THR A 553 ? 0.7627 0.4231 0.4997 -0.0344 0.0133  -0.0989 553 THR A N   
4336 C CA  . THR A 553 ? 0.7612 0.4297 0.4824 -0.0471 -0.0018 -0.1020 553 THR A CA  
4337 C C   . THR A 553 ? 0.7835 0.4489 0.5298 -0.0530 -0.0125 -0.0934 553 THR A C   
4338 O O   . THR A 553 ? 0.6990 0.3588 0.4706 -0.0466 -0.0085 -0.0822 553 THR A O   
4339 C CB  . THR A 553 ? 0.7857 0.4793 0.4890 -0.0473 -0.0070 -0.0885 553 THR A CB  
4340 O OG1 . THR A 553 ? 0.6911 0.3955 0.4168 -0.0438 -0.0108 -0.0674 553 THR A OG1 
4341 C CG2 . THR A 553 ? 0.7408 0.4389 0.4251 -0.0396 0.0072  -0.0908 553 THR A CG2 
4342 N N   . PRO A 554 ? 0.7412 0.4129 0.4813 -0.0654 -0.0264 -0.0977 554 PRO A N   
4343 C CA  . PRO A 554 ? 0.7595 0.4302 0.5251 -0.0720 -0.0355 -0.0893 554 PRO A CA  
4344 C C   . PRO A 554 ? 0.7787 0.4656 0.5620 -0.0659 -0.0374 -0.0658 554 PRO A C   
4345 O O   . PRO A 554 ? 0.7805 0.4637 0.5874 -0.0675 -0.0391 -0.0573 554 PRO A O   
4346 C CB  . PRO A 554 ? 0.8434 0.5259 0.5967 -0.0865 -0.0506 -0.0988 554 PRO A CB  
4347 C CG  . PRO A 554 ? 0.8225 0.5003 0.5441 -0.0890 -0.0472 -0.1200 554 PRO A CG  
4348 C CD  . PRO A 554 ? 0.7654 0.4455 0.4753 -0.0748 -0.0340 -0.1128 554 PRO A CD  
4349 N N   . ILE A 555 ? 0.6368 0.3407 0.4093 -0.0595 -0.0361 -0.0554 555 ILE A N   
4350 C CA  . ILE A 555 ? 0.7058 0.4237 0.4944 -0.0546 -0.0369 -0.0362 555 ILE A CA  
4351 C C   . ILE A 555 ? 0.6937 0.4080 0.4921 -0.0440 -0.0247 -0.0301 555 ILE A C   
4352 O O   . ILE A 555 ? 0.6402 0.3651 0.4524 -0.0407 -0.0242 -0.0170 555 ILE A O   
4353 C CB  . ILE A 555 ? 0.7014 0.4397 0.4775 -0.0547 -0.0429 -0.0267 555 ILE A CB  
4354 C CG1 . ILE A 555 ? 0.7487 0.4881 0.5021 -0.0489 -0.0342 -0.0290 555 ILE A CG1 
4355 C CG2 . ILE A 555 ? 0.6731 0.4217 0.4420 -0.0648 -0.0574 -0.0307 555 ILE A CG2 
4356 C CD1 . ILE A 555 ? 0.7150 0.4715 0.4614 -0.0459 -0.0359 -0.0138 555 ILE A CD1 
4357 N N   . GLY A 556 ? 0.6897 0.3912 0.4827 -0.0388 -0.0149 -0.0400 556 GLY A N   
4358 C CA  . GLY A 556 ? 0.7188 0.4211 0.5229 -0.0287 -0.0041 -0.0349 556 GLY A CA  
4359 C C   . GLY A 556 ? 0.7497 0.4497 0.5377 -0.0235 0.0066  -0.0444 556 GLY A C   
4360 O O   . GLY A 556 ? 0.7520 0.4468 0.5182 -0.0276 0.0064  -0.0568 556 GLY A O   
4361 N N   . TYR A 557 ? 0.7258 0.4323 0.5247 -0.0148 0.0162  -0.0392 557 TYR A N   
4362 C CA  . TYR A 557 ? 0.7292 0.4369 0.5174 -0.0092 0.0288  -0.0466 557 TYR A CA  
4363 C C   . TYR A 557 ? 0.7088 0.4313 0.4800 -0.0120 0.0300  -0.0405 557 TYR A C   
4364 O O   . TYR A 557 ? 0.7259 0.4603 0.5066 -0.0133 0.0265  -0.0274 557 TYR A O   
4365 C CB  . TYR A 557 ? 0.7152 0.4278 0.5265 0.0010  0.0384  -0.0427 557 TYR A CB  
4366 C CG  . TYR A 557 ? 0.7764 0.4740 0.6057 0.0069  0.0396  -0.0458 557 TYR A CG  
4367 C CD1 . TYR A 557 ? 0.8488 0.5265 0.6720 0.0097  0.0469  -0.0611 557 TYR A CD1 
4368 C CD2 . TYR A 557 ? 0.7615 0.4645 0.6138 0.0099  0.0344  -0.0332 557 TYR A CD2 
4369 C CE1 . TYR A 557 ? 0.7914 0.4520 0.6344 0.0159  0.0495  -0.0624 557 TYR A CE1 
4370 C CE2 . TYR A 557 ? 0.7629 0.4520 0.6324 0.0163  0.0361  -0.0322 557 TYR A CE2 
4371 C CZ  . TYR A 557 ? 0.8790 0.5454 0.7455 0.0197  0.0439  -0.0461 557 TYR A CZ  
4372 O OH  . TYR A 557 ? 0.9114 0.5606 0.7981 0.0269  0.0469  -0.0436 557 TYR A OH  
4373 N N   . VAL A 558 ? 0.7173 0.4383 0.4635 -0.0127 0.0361  -0.0498 558 VAL A N   
4374 C CA  . VAL A 558 ? 0.7382 0.4724 0.4665 -0.0141 0.0401  -0.0420 558 VAL A CA  
4375 C C   . VAL A 558 ? 0.7165 0.4533 0.4403 -0.0078 0.0578  -0.0480 558 VAL A C   
4376 O O   . VAL A 558 ? 0.7452 0.4725 0.4742 -0.0027 0.0656  -0.0612 558 VAL A O   
4377 C CB  . VAL A 558 ? 0.7603 0.4963 0.4583 -0.0214 0.0305  -0.0444 558 VAL A CB  
4378 C CG1 . VAL A 558 ? 0.6965 0.4344 0.4043 -0.0271 0.0136  -0.0365 558 VAL A CG1 
4379 C CG2 . VAL A 558 ? 0.7795 0.5042 0.4564 -0.0233 0.0331  -0.0657 558 VAL A CG2 
4380 N N   . PRO A 559 ? 0.7845 0.5340 0.5011 -0.0078 0.0658  -0.0379 559 PRO A N   
4381 C CA  . PRO A 559 ? 0.7218 0.4768 0.4360 -0.0025 0.0844  -0.0426 559 PRO A CA  
4382 C C   . PRO A 559 ? 0.7614 0.5093 0.4447 -0.0021 0.0910  -0.0597 559 PRO A C   
4383 O O   . PRO A 559 ? 0.8147 0.5605 0.4687 -0.0082 0.0821  -0.0630 559 PRO A O   
4384 C CB  . PRO A 559 ? 0.7240 0.4924 0.4344 -0.0053 0.0902  -0.0259 559 PRO A CB  
4385 C CG  . PRO A 559 ? 0.7157 0.4844 0.4388 -0.0097 0.0757  -0.0127 559 PRO A CG  
4386 C CD  . PRO A 559 ? 0.7461 0.5048 0.4608 -0.0121 0.0600  -0.0205 559 PRO A CD  
4387 N N   . LYS A 560 ? 0.7628 0.5086 0.4537 0.0052  0.1067  -0.0714 560 LYS A N   
4388 C CA  . LYS A 560 ? 0.8767 0.6168 0.5378 0.0060  0.1175  -0.0898 560 LYS A CA  
4389 C C   . LYS A 560 ? 0.9608 0.7154 0.5888 0.0021  0.1249  -0.0823 560 LYS A C   
4390 O O   . LYS A 560 ? 0.8612 0.6287 0.4966 0.0006  0.1264  -0.0626 560 LYS A O   
4391 C CB  . LYS A 560 ? 0.8718 0.6085 0.5528 0.0167  0.1357  -0.1023 560 LYS A CB  
4392 C CG  . LYS A 560 ? 0.8491 0.5689 0.5591 0.0225  0.1307  -0.1103 560 LYS A CG  
4393 C CD  . LYS A 560 ? 0.8132 0.5312 0.5432 0.0351  0.1504  -0.1213 560 LYS A CD  
4394 C CE  . LYS A 560 ? 0.9749 0.6734 0.7331 0.0426  0.1470  -0.1278 560 LYS A CE  
4395 N NZ  . LYS A 560 ? 0.9144 0.6110 0.6935 0.0570  0.1674  -0.1383 560 LYS A NZ  
4396 N N   . GLU A 561 ? 0.9645 0.7165 0.5552 0.0000  0.1303  -0.0985 561 GLU A N   
4397 C CA  . GLU A 561 ? 1.0217 0.7891 0.5779 -0.0023 0.1407  -0.0915 561 GLU A CA  
4398 C C   . GLU A 561 ? 1.0500 0.8290 0.6261 0.0042  0.1627  -0.0829 561 GLU A C   
4399 O O   . GLU A 561 ? 1.0872 0.8627 0.6881 0.0119  0.1757  -0.0947 561 GLU A O   
4400 C CB  . GLU A 561 ? 1.1711 0.9354 0.6839 -0.0050 0.1459  -0.1149 561 GLU A CB  
4401 C CG  . GLU A 561 ? 1.2576 1.0398 0.7315 -0.0063 0.1601  -0.1084 561 GLU A CG  
4402 C CD  . GLU A 561 ? 1.3942 1.1745 0.8264 -0.0079 0.1697  -0.1362 561 GLU A CD  
4403 O OE1 . GLU A 561 ? 1.4374 1.1998 0.8721 -0.0090 0.1642  -0.1613 561 GLU A OE1 
4404 O OE2 . GLU A 561 ? 1.4720 1.2680 0.8685 -0.0085 0.1838  -0.1333 561 GLU A OE2 
4405 N N   . ASP A 562 ? 1.0217 0.8152 0.5904 0.0011  0.1671  -0.0611 562 ASP A N   
4406 C CA  . ASP A 562 ? 1.0725 0.8792 0.6608 0.0043  0.1879  -0.0503 562 ASP A CA  
4407 C C   . ASP A 562 ? 1.0023 0.8099 0.6439 0.0077  0.1867  -0.0452 562 ASP A C   
4408 O O   . ASP A 562 ? 1.0091 0.8298 0.6746 0.0099  0.2033  -0.0393 562 ASP A O   
4409 C CB  . ASP A 562 ? 1.2110 1.0232 0.7831 0.0096  0.2117  -0.0673 562 ASP A CB  
4410 C CG  . ASP A 562 ? 1.3378 1.1548 0.8531 0.0054  0.2158  -0.0710 562 ASP A CG  
4411 O OD1 . ASP A 562 ? 1.3792 1.2031 0.8724 -0.0006 0.2071  -0.0507 562 ASP A OD1 
4412 O OD2 . ASP A 562 ? 1.3793 1.1940 0.8720 0.0085  0.2280  -0.0942 562 ASP A OD2 
4413 N N   . ALA A 563 ? 1.0198 0.8162 0.6803 0.0075  0.1675  -0.0473 563 ALA A N   
4414 C CA  . ALA A 563 ? 0.9414 0.7418 0.6482 0.0098  0.1641  -0.0413 563 ALA A CA  
4415 C C   . ALA A 563 ? 0.8588 0.6676 0.5793 0.0030  0.1607  -0.0203 563 ALA A C   
4416 O O   . ALA A 563 ? 0.8694 0.6886 0.6256 0.0031  0.1651  -0.0151 563 ALA A O   
4417 C CB  . ALA A 563 ? 0.8696 0.6557 0.5895 0.0116  0.1461  -0.0493 563 ALA A CB  
4418 N N   . LEU A 564 ? 0.8529 0.6578 0.5471 -0.0028 0.1528  -0.0086 564 LEU A N   
4419 C CA  . LEU A 564 ? 0.8777 0.6868 0.5842 -0.0084 0.1524  0.0118  564 LEU A CA  
4420 C C   . LEU A 564 ? 0.8508 0.6706 0.5494 -0.0102 0.1737  0.0223  564 LEU A C   
4421 O O   . LEU A 564 ? 0.9017 0.7237 0.5640 -0.0092 0.1819  0.0214  564 LEU A O   
4422 C CB  . LEU A 564 ? 0.8349 0.6360 0.5207 -0.0119 0.1354  0.0226  564 LEU A CB  
4423 C CG  . LEU A 564 ? 0.8602 0.6534 0.5657 -0.0131 0.1159  0.0222  564 LEU A CG  
4424 C CD1 . LEU A 564 ? 0.8599 0.6498 0.5498 -0.0160 0.1036  0.0375  564 LEU A CD1 
4425 C CD2 . LEU A 564 ? 0.8012 0.5981 0.5482 -0.0144 0.1188  0.0246  564 LEU A CD2 
4426 N N   . ASN A 565 ? 0.8234 0.6507 0.5554 -0.0139 0.1831  0.0317  565 ASN A N   
4427 C CA  . ASN A 565 ? 0.8326 0.6689 0.5620 -0.0177 0.2039  0.0453  565 ASN A CA  
4428 C C   . ASN A 565 ? 0.8573 0.6854 0.5601 -0.0212 0.1998  0.0661  565 ASN A C   
4429 O O   . ASN A 565 ? 0.8657 0.6860 0.5864 -0.0251 0.1916  0.0784  565 ASN A O   
4430 C CB  . ASN A 565 ? 0.8111 0.6572 0.5873 -0.0230 0.2133  0.0489  565 ASN A CB  
4431 C CG  . ASN A 565 ? 0.9281 0.7841 0.7069 -0.0280 0.2373  0.0622  565 ASN A CG  
4432 O OD1 . ASN A 565 ? 0.9202 0.7731 0.6641 -0.0281 0.2455  0.0749  565 ASN A OD1 
4433 N ND2 . ASN A 565 ? 0.9599 0.8301 0.7801 -0.0328 0.2487  0.0601  565 ASN A ND2 
4434 N N   . LEU A 566 ? 0.9227 0.7534 0.5823 -0.0191 0.2055  0.0700  566 LEU A N   
4435 C CA  . LEU A 566 ? 0.9584 0.7855 0.5889 -0.0206 0.2011  0.0922  566 LEU A CA  
4436 C C   . LEU A 566 ? 1.0633 0.8986 0.6800 -0.0230 0.2243  0.1115  566 LEU A C   
4437 O O   . LEU A 566 ? 1.1320 0.9667 0.7202 -0.0230 0.2229  0.1331  566 LEU A O   
4438 C CB  . LEU A 566 ? 0.9566 0.7833 0.5432 -0.0173 0.1848  0.0840  566 LEU A CB  
4439 C CG  . LEU A 566 ? 0.9759 0.7935 0.5727 -0.0161 0.1609  0.0688  566 LEU A CG  
4440 C CD1 . LEU A 566 ? 0.9995 0.8193 0.5528 -0.0151 0.1475  0.0585  566 LEU A CD1 
4441 C CD2 . LEU A 566 ? 0.9385 0.7480 0.5614 -0.0179 0.1480  0.0850  566 LEU A CD2 
4442 N N   . LYS A 567 ? 1.0619 0.9067 0.6992 -0.0248 0.2457  0.1059  567 LYS A N   
4443 C CA  . LYS A 567 ? 1.0671 0.9204 0.6944 -0.0282 0.2702  0.1251  567 LYS A CA  
4444 C C   . LYS A 567 ? 1.0761 0.9188 0.7224 -0.0338 0.2719  0.1534  567 LYS A C   
4445 O O   . LYS A 567 ? 1.0081 0.8396 0.6903 -0.0366 0.2604  0.1529  567 LYS A O   
4446 C CB  . LYS A 567 ? 1.0883 0.9557 0.7446 -0.0299 0.2928  0.1133  567 LYS A CB  
4447 C CG  . LYS A 567 ? 1.2538 1.1327 0.8969 -0.0334 0.3210  0.1314  567 LYS A CG  
4448 C CD  . LYS A 567 ? 1.3004 1.1974 0.9734 -0.0343 0.3435  0.1178  567 LYS A CD  
4449 C CE  . LYS A 567 ? 1.3467 1.2564 1.0057 -0.0385 0.3735  0.1366  567 LYS A CE  
4450 N NZ  . LYS A 567 ? 1.2783 1.1923 0.8727 -0.0328 0.3780  0.1391  567 LYS A NZ  
4451 N N   . GLY A 568 ? 1.0989 0.9446 0.7205 -0.0352 0.2875  0.1787  568 GLY A N   
4452 C CA  . GLY A 568 ? 1.1412 0.9736 0.7752 -0.0386 0.2894  0.2091  568 GLY A CA  
4453 C C   . GLY A 568 ? 1.1977 1.0208 0.8068 -0.0327 0.2662  0.2223  568 GLY A C   
4454 O O   . GLY A 568 ? 1.2696 1.0833 0.8789 -0.0326 0.2693  0.2525  568 GLY A O   
4455 N N   . LEU A 569 ? 1.2338 1.0594 0.8248 -0.0277 0.2436  0.2015  569 LEU A N   
4456 C CA  . LEU A 569 ? 1.3494 1.1728 0.9132 -0.0223 0.2209  0.2125  569 LEU A CA  
4457 C C   . LEU A 569 ? 1.4676 1.3082 0.9723 -0.0188 0.2179  0.2091  569 LEU A C   
4458 O O   . LEU A 569 ? 1.4262 1.2752 0.8980 -0.0172 0.2256  0.2346  569 LEU A O   
4459 C CB  . LEU A 569 ? 1.2810 1.0962 0.8672 -0.0210 0.1970  0.1921  569 LEU A CB  
4460 C CG  . LEU A 569 ? 1.0905 0.8909 0.7320 -0.0250 0.1980  0.1896  569 LEU A CG  
4461 C CD1 . LEU A 569 ? 0.9845 0.7801 0.6401 -0.0232 0.1747  0.1699  569 LEU A CD1 
4462 C CD2 . LEU A 569 ? 1.0944 0.8821 0.7529 -0.0256 0.2046  0.2206  569 LEU A CD2 
4463 N N   . GLY A 570 ? 1.5409 1.3868 1.0315 -0.0179 0.2072  0.1778  570 GLY A N   
4464 C CA  . GLY A 570 ? 1.5305 1.3920 0.9653 -0.0161 0.2042  0.1677  570 GLY A CA  
4465 C C   . GLY A 570 ? 1.5747 1.4444 0.9733 -0.0137 0.1818  0.1819  570 GLY A C   
4466 O O   . GLY A 570 ? 1.5526 1.4308 0.9197 -0.0140 0.1664  0.1612  570 GLY A O   
4467 N N   . ASP A 571 ? 1.4862 1.3540 0.8909 -0.0113 0.1795  0.2170  571 ASP A N   
4468 C CA  . ASP A 571 ? 1.4559 1.3343 0.8337 -0.0074 0.1571  0.2359  571 ASP A CA  
4469 C C   . ASP A 571 ? 1.4173 1.2888 0.8204 -0.0065 0.1306  0.2229  571 ASP A C   
4470 O O   . ASP A 571 ? 1.3718 1.2530 0.7632 -0.0028 0.1107  0.2399  571 ASP A O   
4471 C CB  . ASP A 571 ? 1.4474 1.3234 0.8315 -0.0032 0.1656  0.2803  571 ASP A CB  
4472 C CG  . ASP A 571 ? 1.4782 1.3293 0.9232 -0.0042 0.1763  0.2890  571 ASP A CG  
4473 O OD1 . ASP A 571 ? 1.4565 1.2972 0.9325 -0.0092 0.1844  0.2630  571 ASP A OD1 
4474 O OD2 . ASP A 571 ? 1.5871 1.4325 1.0568 -0.0021 0.1730  0.3168  571 ASP A OD2 
4475 N N   . VAL A 572 ? 1.4067 1.2641 0.8447 -0.0095 0.1298  0.1951  572 VAL A N   
4476 C CA  . VAL A 572 ? 1.3675 1.2179 0.8320 -0.0092 0.1071  0.1834  572 VAL A CA  
4477 C C   . VAL A 572 ? 1.3139 1.1764 0.7458 -0.0117 0.0888  0.1581  572 VAL A C   
4478 O O   . VAL A 572 ? 1.2903 1.1542 0.7031 -0.0149 0.0968  0.1323  572 VAL A O   
4479 C CB  . VAL A 572 ? 1.2373 1.0693 0.7513 -0.0115 0.1143  0.1665  572 VAL A CB  
4480 C CG1 . VAL A 572 ? 1.2063 1.0327 0.7433 -0.0115 0.0922  0.1531  572 VAL A CG1 
4481 C CG2 . VAL A 572 ? 1.2733 1.0934 0.8216 -0.0112 0.1312  0.1892  572 VAL A CG2 
4482 N N   . ASN A 573 ? 1.2395 1.1109 0.6675 -0.0107 0.0647  0.1646  573 ASN A N   
4483 C CA  . ASN A 573 ? 1.2268 1.1092 0.6304 -0.0153 0.0452  0.1393  573 ASN A CA  
4484 C C   . ASN A 573 ? 1.2133 1.0781 0.6494 -0.0188 0.0424  0.1093  573 ASN A C   
4485 O O   . ASN A 573 ? 1.1830 1.0416 0.6522 -0.0185 0.0289  0.1104  573 ASN A O   
4486 C CB  . ASN A 573 ? 1.2481 1.1485 0.6445 -0.0137 0.0198  0.1566  573 ASN A CB  
4487 C CG  . ASN A 573 ? 1.3005 1.2147 0.6731 -0.0209 -0.0012 0.1297  573 ASN A CG  
4488 O OD1 . ASN A 573 ? 1.3170 1.2256 0.6730 -0.0269 0.0046  0.0986  573 ASN A OD1 
4489 N ND2 . ASN A 573 ? 1.3103 1.2430 0.6835 -0.0206 -0.0251 0.1414  573 ASN A ND2 
4490 N N   . VAL A 574 ? 1.2089 1.0665 0.6365 -0.0214 0.0561  0.0834  574 VAL A N   
4491 C CA  . VAL A 574 ? 1.2020 1.0425 0.6615 -0.0232 0.0556  0.0580  574 VAL A CA  
4492 C C   . VAL A 574 ? 1.1596 1.0018 0.6128 -0.0285 0.0335  0.0384  574 VAL A C   
4493 O O   . VAL A 574 ? 1.0858 0.9160 0.5726 -0.0295 0.0256  0.0292  574 VAL A O   
4494 C CB  . VAL A 574 ? 1.1884 1.0216 0.6434 -0.0225 0.0776  0.0381  574 VAL A CB  
4495 C CG1 . VAL A 574 ? 1.1582 0.9891 0.6332 -0.0188 0.0991  0.0565  574 VAL A CG1 
4496 C CG2 . VAL A 574 ? 1.2392 1.0844 0.6423 -0.0252 0.0814  0.0237  574 VAL A CG2 
4497 N N   . GLU A 575 ? 1.2423 1.1008 0.6526 -0.0329 0.0234  0.0315  575 GLU A N   
4498 C CA  . GLU A 575 ? 1.2772 1.1389 0.6820 -0.0404 0.0025  0.0107  575 GLU A CA  
4499 C C   . GLU A 575 ? 1.1523 1.0172 0.5901 -0.0403 -0.0169 0.0262  575 GLU A C   
4500 O O   . GLU A 575 ? 1.1146 0.9670 0.5821 -0.0434 -0.0240 0.0123  575 GLU A O   
4501 C CB  . GLU A 575 ? 1.3598 1.2442 0.7109 -0.0462 -0.0064 0.0032  575 GLU A CB  
4502 C CG  . GLU A 575 ? 1.5224 1.3990 0.8453 -0.0514 0.0048  -0.0322 575 GLU A CG  
4503 C CD  . GLU A 575 ? 1.6198 1.4790 0.9639 -0.0585 -0.0042 -0.0628 575 GLU A CD  
4504 O OE1 . GLU A 575 ? 1.5955 1.4605 0.9561 -0.0637 -0.0259 -0.0600 575 GLU A OE1 
4505 O OE2 . GLU A 575 ? 1.7013 1.5408 1.0479 -0.0584 0.0114  -0.0884 575 GLU A OE2 
4506 N N   . GLU A 576 ? 1.1793 1.0612 0.6132 -0.0359 -0.0245 0.0564  576 GLU A N   
4507 C CA  . GLU A 576 ? 1.1252 1.0126 0.5913 -0.0343 -0.0416 0.0721  576 GLU A CA  
4508 C C   . GLU A 576 ? 1.0899 0.9557 0.6044 -0.0295 -0.0316 0.0780  576 GLU A C   
4509 O O   . GLU A 576 ? 1.0420 0.9076 0.5874 -0.0296 -0.0436 0.0814  576 GLU A O   
4510 C CB  . GLU A 576 ? 1.2014 1.1123 0.6529 -0.0286 -0.0504 0.1050  576 GLU A CB  
4511 C CG  . GLU A 576 ? 1.2547 1.1765 0.7380 -0.0257 -0.0691 0.1217  576 GLU A CG  
4512 C CD  . GLU A 576 ? 1.2734 1.2215 0.7403 -0.0188 -0.0793 0.1546  576 GLU A CD  
4513 O OE1 . GLU A 576 ? 1.2898 1.2474 0.7180 -0.0169 -0.0718 0.1651  576 GLU A OE1 
4514 O OE2 . GLU A 576 ? 1.2644 1.2250 0.7577 -0.0145 -0.0943 0.1713  576 GLU A OE2 
4515 N N   . LEU A 577 ? 1.0945 0.9446 0.6163 -0.0260 -0.0099 0.0783  577 LEU A N   
4516 C CA  . LEU A 577 ? 1.0284 0.8614 0.5939 -0.0226 -0.0009 0.0830  577 LEU A CA  
4517 C C   . LEU A 577 ? 0.9576 0.7770 0.5446 -0.0264 -0.0027 0.0579  577 LEU A C   
4518 O O   . LEU A 577 ? 0.8842 0.6954 0.5065 -0.0252 -0.0042 0.0606  577 LEU A O   
4519 C CB  . LEU A 577 ? 0.9970 0.8220 0.5652 -0.0188 0.0221  0.0927  577 LEU A CB  
4520 C CG  . LEU A 577 ? 0.9106 0.7210 0.5221 -0.0166 0.0323  0.0980  577 LEU A CG  
4521 C CD1 . LEU A 577 ? 0.9330 0.7441 0.5690 -0.0136 0.0222  0.1169  577 LEU A CD1 
4522 C CD2 . LEU A 577 ? 0.9080 0.7140 0.5208 -0.0151 0.0546  0.1076  577 LEU A CD2 
4523 N N   . PHE A 578 ? 0.9605 0.7767 0.5270 -0.0307 -0.0016 0.0340  578 PHE A N   
4524 C CA  . PHE A 578 ? 0.9178 0.7196 0.5038 -0.0337 -0.0029 0.0119  578 PHE A CA  
4525 C C   . PHE A 578 ? 0.9456 0.7510 0.5187 -0.0416 -0.0199 -0.0051 578 PHE A C   
4526 O O   . PHE A 578 ? 0.9658 0.7572 0.5514 -0.0449 -0.0202 -0.0245 578 PHE A O   
4527 C CB  . PHE A 578 ? 0.9478 0.7379 0.5306 -0.0312 0.0160  -0.0036 578 PHE A CB  
4528 C CG  . PHE A 578 ? 0.9222 0.7062 0.5347 -0.0256 0.0304  0.0065  578 PHE A CG  
4529 C CD1 . PHE A 578 ? 0.8747 0.6496 0.5226 -0.0247 0.0283  0.0036  578 PHE A CD1 
4530 C CD2 . PHE A 578 ? 0.8232 0.6123 0.4282 -0.0223 0.0461  0.0187  578 PHE A CD2 
4531 C CE1 . PHE A 578 ? 0.8350 0.6080 0.5093 -0.0210 0.0398  0.0108  578 PHE A CE1 
4532 C CE2 . PHE A 578 ? 0.8596 0.6451 0.4945 -0.0194 0.0587  0.0259  578 PHE A CE2 
4533 C CZ  . PHE A 578 ? 0.8616 0.6399 0.5307 -0.0190 0.0547  0.0209  578 PHE A CZ  
4534 N N   . GLY A 579 ? 0.9889 0.8137 0.5390 -0.0451 -0.0343 0.0025  579 GLY A N   
4535 C CA  . GLY A 579 ? 0.9378 0.7695 0.4778 -0.0548 -0.0518 -0.0147 579 GLY A CA  
4536 C C   . GLY A 579 ? 0.9642 0.7884 0.5431 -0.0579 -0.0614 -0.0168 579 GLY A C   
4537 O O   . GLY A 579 ? 0.9320 0.7592 0.5388 -0.0529 -0.0635 0.0026  579 GLY A O   
4538 N N   . ILE A 580 ? 0.9126 0.7259 0.4937 -0.0664 -0.0657 -0.0412 580 ILE A N   
4539 C CA  . ILE A 580 ? 0.8910 0.6976 0.5061 -0.0714 -0.0744 -0.0446 580 ILE A CA  
4540 C C   . ILE A 580 ? 0.9048 0.7254 0.5088 -0.0845 -0.0932 -0.0583 580 ILE A C   
4541 O O   . ILE A 580 ? 0.9755 0.7870 0.5606 -0.0929 -0.0925 -0.0837 580 ILE A O   
4542 C CB  . ILE A 580 ? 0.8964 0.6749 0.5312 -0.0701 -0.0612 -0.0589 580 ILE A CB  
4543 C CG1 . ILE A 580 ? 0.9034 0.6743 0.5542 -0.0582 -0.0457 -0.0442 580 ILE A CG1 
4544 C CG2 . ILE A 580 ? 0.8883 0.6606 0.5534 -0.0771 -0.0705 -0.0629 580 ILE A CG2 
4545 C CD1 . ILE A 580 ? 0.8470 0.5952 0.5169 -0.0549 -0.0333 -0.0550 580 ILE A CD1 
4546 N N   . SER A 581 ? 0.8587 0.7021 0.4766 -0.0866 -0.1094 -0.0428 581 SER A N   
4547 C CA  . SER A 581 ? 0.8493 0.7142 0.4601 -0.0995 -0.1299 -0.0527 581 SER A CA  
4548 C C   . SER A 581 ? 0.8798 0.7361 0.5269 -0.1086 -0.1358 -0.0616 581 SER A C   
4549 O O   . SER A 581 ? 0.8675 0.7233 0.5483 -0.1032 -0.1343 -0.0449 581 SER A O   
4550 C CB  . SER A 581 ? 0.8640 0.7640 0.4708 -0.0953 -0.1449 -0.0279 581 SER A CB  
4551 O OG  . SER A 581 ? 0.9532 0.8785 0.5655 -0.1076 -0.1666 -0.0344 581 SER A OG  
4552 N N   . LYS A 582 ? 0.9184 0.7677 0.5585 -0.1231 -0.1412 -0.0885 582 LYS A N   
4553 C CA  . LYS A 582 ? 0.9121 0.7545 0.5868 -0.1342 -0.1472 -0.0966 582 LYS A CA  
4554 C C   . LYS A 582 ? 0.8774 0.7531 0.5759 -0.1367 -0.1647 -0.0779 582 LYS A C   
4555 O O   . LYS A 582 ? 0.8232 0.6957 0.5588 -0.1361 -0.1632 -0.0678 582 LYS A O   
4556 C CB  . LYS A 582 ? 0.9131 0.7448 0.5750 -0.1515 -0.1515 -0.1296 582 LYS A CB  
4557 C CG  . LYS A 582 ? 0.9248 0.7482 0.6237 -0.1652 -0.1569 -0.1383 582 LYS A CG  
4558 C CD  . LYS A 582 ? 0.9836 0.7911 0.6716 -0.1832 -0.1588 -0.1733 582 LYS A CD  
4559 C CE  . LYS A 582 ? 0.9462 0.7404 0.6748 -0.1972 -0.1608 -0.1802 582 LYS A CE  
4560 N NZ  . LYS A 582 ? 0.9573 0.7292 0.6794 -0.2153 -0.1599 -0.2158 582 LYS A NZ  
4561 N N   . GLU A 583 ? 0.8841 0.7943 0.5619 -0.1386 -0.1810 -0.0722 583 GLU A N   
4562 C CA  . GLU A 583 ? 0.8576 0.8038 0.5601 -0.1400 -0.1987 -0.0542 583 GLU A CA  
4563 C C   . GLU A 583 ? 0.8336 0.7791 0.5648 -0.1235 -0.1898 -0.0250 583 GLU A C   
4564 O O   . GLU A 583 ? 0.8264 0.7839 0.5951 -0.1247 -0.1949 -0.0150 583 GLU A O   
4565 C CB  . GLU A 583 ? 0.9019 0.8871 0.5739 -0.1419 -0.2174 -0.0495 583 GLU A CB  
4566 C CG  . GLU A 583 ? 1.0460 1.0381 0.6877 -0.1605 -0.2287 -0.0811 583 GLU A CG  
4567 C CD  . GLU A 583 ? 1.1209 1.0802 0.7256 -0.1597 -0.2113 -0.1021 583 GLU A CD  
4568 O OE1 . GLU A 583 ? 1.0698 1.0126 0.6642 -0.1436 -0.1944 -0.0874 583 GLU A OE1 
4569 O OE2 . GLU A 583 ? 1.1786 1.1285 0.7670 -0.1755 -0.2135 -0.1342 583 GLU A OE2 
4570 N N   . PHE A 584 ? 0.8140 0.7459 0.5294 -0.1085 -0.1755 -0.0121 584 PHE A N   
4571 C CA  . PHE A 584 ? 0.7489 0.6775 0.4909 -0.0940 -0.1656 0.0122  584 PHE A CA  
4572 C C   . PHE A 584 ? 0.7688 0.6721 0.5412 -0.0951 -0.1532 0.0066  584 PHE A C   
4573 O O   . PHE A 584 ? 0.7073 0.6181 0.5126 -0.0912 -0.1527 0.0202  584 PHE A O   
4574 C CB  . PHE A 584 ? 0.7892 0.7071 0.5084 -0.0803 -0.1520 0.0248  584 PHE A CB  
4575 C CG  . PHE A 584 ? 0.7630 0.6704 0.5091 -0.0673 -0.1386 0.0441  584 PHE A CG  
4576 C CD1 . PHE A 584 ? 0.7228 0.6501 0.4859 -0.0578 -0.1434 0.0685  584 PHE A CD1 
4577 C CD2 . PHE A 584 ? 0.7180 0.5965 0.4732 -0.0646 -0.1213 0.0373  584 PHE A CD2 
4578 C CE1 . PHE A 584 ? 0.7509 0.6666 0.5389 -0.0469 -0.1299 0.0828  584 PHE A CE1 
4579 C CE2 . PHE A 584 ? 0.7360 0.6068 0.5141 -0.0545 -0.1097 0.0518  584 PHE A CE2 
4580 C CZ  . PHE A 584 ? 0.7107 0.5985 0.5048 -0.0463 -0.1133 0.0732  584 PHE A CZ  
4581 N N   . TRP A 585 ? 0.7660 0.6405 0.5279 -0.0997 -0.1425 -0.0124 585 TRP A N   
4582 C CA  . TRP A 585 ? 0.7713 0.6220 0.5585 -0.0984 -0.1296 -0.0141 585 TRP A CA  
4583 C C   . TRP A 585 ? 0.7772 0.6313 0.5922 -0.1110 -0.1371 -0.0211 585 TRP A C   
4584 O O   . TRP A 585 ? 0.7200 0.5665 0.5623 -0.1088 -0.1296 -0.0136 585 TRP A O   
4585 C CB  . TRP A 585 ? 0.7260 0.5462 0.4953 -0.0964 -0.1150 -0.0286 585 TRP A CB  
4586 C CG  . TRP A 585 ? 0.7652 0.5807 0.5209 -0.0828 -0.1030 -0.0174 585 TRP A CG  
4587 C CD1 . TRP A 585 ? 0.7851 0.6039 0.5090 -0.0790 -0.1008 -0.0186 585 TRP A CD1 
4588 C CD2 . TRP A 585 ? 0.7764 0.5848 0.5505 -0.0724 -0.0912 -0.0033 585 TRP A CD2 
4589 N NE1 . TRP A 585 ? 0.7601 0.5730 0.4845 -0.0673 -0.0876 -0.0053 585 TRP A NE1 
4590 C CE2 . TRP A 585 ? 0.6993 0.5058 0.4544 -0.0635 -0.0821 0.0029  585 TRP A CE2 
4591 C CE3 . TRP A 585 ? 0.7153 0.5198 0.5192 -0.0706 -0.0869 0.0038  585 TRP A CE3 
4592 C CZ2 . TRP A 585 ? 0.6966 0.4969 0.4640 -0.0541 -0.0698 0.0144  585 TRP A CZ2 
4593 C CZ3 . TRP A 585 ? 0.7877 0.5872 0.6001 -0.0608 -0.0751 0.0143  585 TRP A CZ3 
4594 C CH2 . TRP A 585 ? 0.7179 0.5151 0.5135 -0.0532 -0.0671 0.0187  585 TRP A CH2 
4595 N N   . GLU A 586 ? 0.7636 0.6303 0.5722 -0.1253 -0.1515 -0.0355 586 GLU A N   
4596 C CA  . GLU A 586 ? 0.7528 0.6294 0.5924 -0.1386 -0.1601 -0.0393 586 GLU A CA  
4597 C C   . GLU A 586 ? 0.7522 0.6558 0.6219 -0.1320 -0.1644 -0.0164 586 GLU A C   
4598 O O   . GLU A 586 ? 0.7138 0.6155 0.6153 -0.1348 -0.1597 -0.0114 586 GLU A O   
4599 C CB  . GLU A 586 ? 0.7995 0.6928 0.6273 -0.1558 -0.1775 -0.0585 586 GLU A CB  
4600 C CG  . GLU A 586 ? 0.8166 0.6796 0.6242 -0.1663 -0.1717 -0.0865 586 GLU A CG  
4601 C CD  . GLU A 586 ? 0.9544 0.8354 0.7519 -0.1860 -0.1894 -0.1086 586 GLU A CD  
4602 O OE1 . GLU A 586 ? 0.9103 0.8302 0.6991 -0.1873 -0.2069 -0.1015 586 GLU A OE1 
4603 O OE2 . GLU A 586 ? 1.0689 0.9258 0.8683 -0.2001 -0.1859 -0.1329 586 GLU A OE2 
4604 N N   . LYS A 587 ? 0.7242 0.6528 0.5846 -0.1224 -0.1721 -0.0014 587 LYS A N   
4605 C CA  . LYS A 587 ? 0.6669 0.6194 0.5570 -0.1133 -0.1742 0.0208  587 LYS A CA  
4606 C C   . LYS A 587 ? 0.6715 0.6026 0.5748 -0.1006 -0.1548 0.0317  587 LYS A C   
4607 O O   . LYS A 587 ? 0.7096 0.6496 0.6450 -0.0982 -0.1510 0.0416  587 LYS A O   
4608 C CB  . LYS A 587 ? 0.7590 0.7397 0.6353 -0.1041 -0.1857 0.0361  587 LYS A CB  
4609 C CG  . LYS A 587 ? 0.8323 0.8388 0.7424 -0.0932 -0.1880 0.0595  587 LYS A CG  
4610 C CD  . LYS A 587 ? 0.8805 0.9214 0.8203 -0.1047 -0.2048 0.0585  587 LYS A CD  
4611 C CE  . LYS A 587 ? 0.8534 0.9130 0.8358 -0.0941 -0.2008 0.0784  587 LYS A CE  
4612 N NZ  . LYS A 587 ? 0.8115 0.8433 0.8115 -0.0924 -0.1805 0.0757  587 LYS A NZ  
4613 N N   . GLU A 588 ? 0.6821 0.5875 0.5613 -0.0929 -0.1422 0.0291  588 GLU A N   
4614 C CA  . GLU A 588 ? 0.6864 0.5749 0.5760 -0.0818 -0.1252 0.0379  588 GLU A CA  
4615 C C   . GLU A 588 ? 0.6484 0.5238 0.5594 -0.0878 -0.1173 0.0323  588 GLU A C   
4616 O O   . GLU A 588 ? 0.6445 0.5237 0.5782 -0.0825 -0.1096 0.0423  588 GLU A O   
4617 C CB  . GLU A 588 ? 0.6750 0.5415 0.5360 -0.0746 -0.1143 0.0343  588 GLU A CB  
4618 C CG  . GLU A 588 ? 0.6761 0.5306 0.5464 -0.0634 -0.0987 0.0437  588 GLU A CG  
4619 C CD  . GLU A 588 ? 0.6798 0.5493 0.5605 -0.0531 -0.0983 0.0617  588 GLU A CD  
4620 O OE1 . GLU A 588 ? 0.6264 0.5147 0.5006 -0.0521 -0.1098 0.0693  588 GLU A OE1 
4621 O OE2 . GLU A 588 ? 0.5985 0.4614 0.4940 -0.0458 -0.0864 0.0681  588 GLU A OE2 
4622 N N   . VAL A 589 ? 0.6851 0.5443 0.5888 -0.0987 -0.1181 0.0166  589 VAL A N   
4623 C CA  . VAL A 589 ? 0.7120 0.5571 0.6354 -0.1042 -0.1101 0.0140  589 VAL A CA  
4624 C C   . VAL A 589 ? 0.6563 0.5243 0.6122 -0.1102 -0.1152 0.0222  589 VAL A C   
4625 O O   . VAL A 589 ? 0.6731 0.5391 0.6486 -0.1082 -0.1052 0.0298  589 VAL A O   
4626 C CB  . VAL A 589 ? 0.6982 0.5203 0.6111 -0.1150 -0.1101 -0.0039 589 VAL A CB  
4627 C CG1 . VAL A 589 ? 0.7594 0.5575 0.6462 -0.1066 -0.1004 -0.0105 589 VAL A CG1 
4628 C CG2 . VAL A 589 ? 0.7660 0.6021 0.6728 -0.1282 -0.1260 -0.0165 589 VAL A CG2 
4629 N N   . GLU A 590 ? 0.6610 0.5545 0.6234 -0.1176 -0.1306 0.0210  590 GLU A N   
4630 C CA  . GLU A 590 ? 0.6375 0.5569 0.6349 -0.1240 -0.1358 0.0284  590 GLU A CA  
4631 C C   . GLU A 590 ? 0.6788 0.6125 0.6945 -0.1099 -0.1277 0.0461  590 GLU A C   
4632 O O   . GLU A 590 ? 0.6854 0.6264 0.7285 -0.1116 -0.1204 0.0522  590 GLU A O   
4633 C CB  . GLU A 590 ? 0.7187 0.6676 0.7194 -0.1341 -0.1560 0.0237  590 GLU A CB  
4634 C CG  . GLU A 590 ? 0.8527 0.7882 0.8348 -0.1500 -0.1640 0.0021  590 GLU A CG  
4635 C CD  . GLU A 590 ? 1.0131 0.9229 1.0100 -0.1620 -0.1544 -0.0076 590 GLU A CD  
4636 O OE1 . GLU A 590 ? 0.9787 0.8945 1.0062 -0.1633 -0.1473 0.0028  590 GLU A OE1 
4637 O OE2 . GLU A 590 ? 1.0477 0.9309 1.0261 -0.1698 -0.1526 -0.0250 590 GLU A OE2 
4638 N N   . GLU A 591 ? 0.6438 0.5810 0.6454 -0.0962 -0.1275 0.0543  591 GLU A N   
4639 C CA  . GLU A 591 ? 0.6549 0.6009 0.6744 -0.0825 -0.1177 0.0689  591 GLU A CA  
4640 C C   . GLU A 591 ? 0.6051 0.5283 0.6242 -0.0786 -0.0995 0.0675  591 GLU A C   
4641 O O   . GLU A 591 ? 0.6183 0.5501 0.6603 -0.0747 -0.0901 0.0743  591 GLU A O   
4642 C CB  . GLU A 591 ? 0.5886 0.5383 0.5931 -0.0695 -0.1200 0.0781  591 GLU A CB  
4643 C CG  . GLU A 591 ? 0.6580 0.6388 0.6679 -0.0699 -0.1381 0.0857  591 GLU A CG  
4644 C CD  . GLU A 591 ? 0.7046 0.7166 0.7557 -0.0697 -0.1422 0.0955  591 GLU A CD  
4645 O OE1 . GLU A 591 ? 0.7023 0.7135 0.7753 -0.0597 -0.1285 0.1040  591 GLU A OE1 
4646 O OE2 . GLU A 591 ? 0.6563 0.6949 0.7188 -0.0798 -0.1586 0.0937  591 GLU A OE2 
4647 N N   . ILE A 592 ? 0.5428 0.4393 0.5362 -0.0793 -0.0941 0.0587  592 ILE A N   
4648 C CA  . ILE A 592 ? 0.5614 0.4402 0.5537 -0.0764 -0.0792 0.0578  592 ILE A CA  
4649 C C   . ILE A 592 ? 0.6342 0.5159 0.6464 -0.0861 -0.0763 0.0578  592 ILE A C   
4650 O O   . ILE A 592 ? 0.6095 0.4938 0.6336 -0.0830 -0.0649 0.0633  592 ILE A O   
4651 C CB  . ILE A 592 ? 0.6428 0.4960 0.6070 -0.0751 -0.0756 0.0492  592 ILE A CB  
4652 C CG1 . ILE A 592 ? 0.6854 0.5372 0.6305 -0.0667 -0.0773 0.0504  592 ILE A CG1 
4653 C CG2 . ILE A 592 ? 0.6029 0.4430 0.5668 -0.0715 -0.0622 0.0499  592 ILE A CG2 
4654 C CD1 . ILE A 592 ? 0.6662 0.4968 0.5849 -0.0661 -0.0743 0.0411  592 ILE A CD1 
4655 N N   . ASP A 593 ? 0.6118 0.4932 0.6275 -0.0988 -0.0857 0.0512  593 ASP A N   
4656 C CA  . ASP A 593 ? 0.5487 0.4318 0.5860 -0.1099 -0.0824 0.0522  593 ASP A CA  
4657 C C   . ASP A 593 ? 0.6463 0.5579 0.7139 -0.1089 -0.0797 0.0627  593 ASP A C   
4658 O O   . ASP A 593 ? 0.6304 0.5430 0.7100 -0.1082 -0.0672 0.0691  593 ASP A O   
4659 C CB  . ASP A 593 ? 0.6344 0.5136 0.6732 -0.1253 -0.0940 0.0412  593 ASP A CB  
4660 C CG  . ASP A 593 ? 0.7408 0.6131 0.8004 -0.1380 -0.0883 0.0418  593 ASP A CG  
4661 O OD1 . ASP A 593 ? 0.7900 0.6594 0.8577 -0.1337 -0.0750 0.0520  593 ASP A OD1 
4662 O OD2 . ASP A 593 ? 0.7480 0.6177 0.8153 -0.1530 -0.0967 0.0320  593 ASP A OD2 
4663 N N   . LYS A 594 ? 0.5713 0.5084 0.6519 -0.1082 -0.0911 0.0653  594 LYS A N   
4664 C CA  . LYS A 594 ? 0.5677 0.5343 0.6813 -0.1055 -0.0881 0.0756  594 LYS A CA  
4665 C C   . LYS A 594 ? 0.6056 0.5692 0.7193 -0.0912 -0.0717 0.0822  594 LYS A C   
4666 O O   . LYS A 594 ? 0.5255 0.5018 0.6612 -0.0909 -0.0605 0.0877  594 LYS A O   
4667 C CB  . LYS A 594 ? 0.5482 0.5436 0.6742 -0.1035 -0.1039 0.0794  594 LYS A CB  
4668 C CG  . LYS A 594 ? 0.6231 0.6302 0.7533 -0.1199 -0.1216 0.0711  594 LYS A CG  
4669 C CD  . LYS A 594 ? 0.6317 0.6748 0.7758 -0.1167 -0.1384 0.0777  594 LYS A CD  
4670 C CE  . LYS A 594 ? 0.6339 0.6709 0.7510 -0.1012 -0.1415 0.0827  594 LYS A CE  
4671 N NZ  . LYS A 594 ? 0.6519 0.7240 0.7776 -0.0983 -0.1603 0.0908  594 LYS A NZ  
4672 N N   . TYR A 595 ? 0.5624 0.5100 0.6519 -0.0802 -0.0691 0.0807  595 TYR A N   
4673 C CA  . TYR A 595 ? 0.5308 0.4743 0.6199 -0.0681 -0.0539 0.0838  595 TYR A CA  
4674 C C   . TYR A 595 ? 0.5931 0.5244 0.6755 -0.0715 -0.0406 0.0813  595 TYR A C   
4675 O O   . TYR A 595 ? 0.5567 0.4992 0.6541 -0.0690 -0.0283 0.0846  595 TYR A O   
4676 C CB  . TYR A 595 ? 0.5421 0.4699 0.6076 -0.0583 -0.0544 0.0821  595 TYR A CB  
4677 C CG  . TYR A 595 ? 0.5322 0.4525 0.5962 -0.0480 -0.0388 0.0819  595 TYR A CG  
4678 C CD1 . TYR A 595 ? 0.5414 0.4742 0.6264 -0.0380 -0.0326 0.0878  595 TYR A CD1 
4679 C CD2 . TYR A 595 ? 0.5664 0.4677 0.6093 -0.0484 -0.0304 0.0751  595 TYR A CD2 
4680 C CE1 . TYR A 595 ? 0.5209 0.4447 0.6051 -0.0301 -0.0174 0.0843  595 TYR A CE1 
4681 C CE2 . TYR A 595 ? 0.5739 0.4704 0.6152 -0.0412 -0.0171 0.0721  595 TYR A CE2 
4682 C CZ  . TYR A 595 ? 0.5310 0.4375 0.5924 -0.0328 -0.0102 0.0755  595 TYR A CZ  
4683 O OH  . TYR A 595 ? 0.7075 0.6073 0.7681 -0.0270 0.0040  0.0694  595 TYR A OH  
4684 N N   . LEU A 596 ? 0.5787 0.4880 0.6383 -0.0764 -0.0423 0.0759  596 LEU A N   
4685 C CA  . LEU A 596 ? 0.6187 0.5177 0.6705 -0.0784 -0.0311 0.0765  596 LEU A CA  
4686 C C   . LEU A 596 ? 0.6249 0.5375 0.6991 -0.0873 -0.0262 0.0828  596 LEU A C   
4687 O O   . LEU A 596 ? 0.6046 0.5221 0.6803 -0.0859 -0.0133 0.0871  596 LEU A O   
4688 C CB  . LEU A 596 ? 0.6386 0.5129 0.6674 -0.0812 -0.0348 0.0716  596 LEU A CB  
4689 C CG  . LEU A 596 ? 0.6626 0.5234 0.6682 -0.0725 -0.0359 0.0658  596 LEU A CG  
4690 C CD1 . LEU A 596 ? 0.7021 0.5408 0.6900 -0.0752 -0.0388 0.0609  596 LEU A CD1 
4691 C CD2 . LEU A 596 ? 0.6517 0.5157 0.6524 -0.0641 -0.0244 0.0664  596 LEU A CD2 
4692 N N   . GLU A 597 ? 0.5832 0.5039 0.6750 -0.0975 -0.0359 0.0832  597 GLU A N   
4693 C CA  . GLU A 597 ? 0.5968 0.5308 0.7134 -0.1079 -0.0306 0.0897  597 GLU A CA  
4694 C C   . GLU A 597 ? 0.6190 0.5803 0.7583 -0.1022 -0.0203 0.0958  597 GLU A C   
4695 O O   . GLU A 597 ? 0.6369 0.6056 0.7845 -0.1048 -0.0068 0.1020  597 GLU A O   
4696 C CB  . GLU A 597 ? 0.6497 0.5891 0.7833 -0.1218 -0.0442 0.0864  597 GLU A CB  
4697 C CG  . GLU A 597 ? 0.7070 0.6599 0.8701 -0.1349 -0.0383 0.0932  597 GLU A CG  
4698 C CD  . GLU A 597 ? 0.7277 0.6980 0.9163 -0.1486 -0.0526 0.0890  597 GLU A CD  
4699 O OE1 . GLU A 597 ? 0.7217 0.6991 0.9048 -0.1459 -0.0675 0.0823  597 GLU A OE1 
4700 O OE2 . GLU A 597 ? 0.8419 0.8204 1.0562 -0.1627 -0.0490 0.0928  597 GLU A OE2 
4701 N N   . ASP A 598 ? 0.5977 0.5744 0.7474 -0.0937 -0.0254 0.0949  598 ASP A N   
4702 C CA  . ASP A 598 ? 0.6065 0.6088 0.7824 -0.0868 -0.0148 0.1000  598 ASP A CA  
4703 C C   . ASP A 598 ? 0.5793 0.5738 0.7395 -0.0758 0.0016  0.0974  598 ASP A C   
4704 O O   . ASP A 598 ? 0.6119 0.6193 0.7827 -0.0752 0.0170  0.0999  598 ASP A O   
4705 C CB  . ASP A 598 ? 0.5972 0.6185 0.7927 -0.0800 -0.0260 0.1021  598 ASP A CB  
4706 C CG  . ASP A 598 ? 0.6794 0.7244 0.9037 -0.0693 -0.0135 0.1071  598 ASP A CG  
4707 O OD1 . ASP A 598 ? 0.6041 0.6677 0.8517 -0.0744 -0.0030 0.1108  598 ASP A OD1 
4708 O OD2 . ASP A 598 ? 0.6838 0.7283 0.9089 -0.0556 -0.0129 0.1076  598 ASP A OD2 
4709 N N   . GLN A 599 ? 0.5726 0.5471 0.7069 -0.0680 -0.0010 0.0915  599 GLN A N   
4710 C CA  . GLN A 599 ? 0.5516 0.5209 0.6745 -0.0580 0.0130  0.0863  599 GLN A CA  
4711 C C   . GLN A 599 ? 0.5617 0.5212 0.6613 -0.0619 0.0224  0.0840  599 GLN A C   
4712 O O   . GLN A 599 ? 0.5971 0.5627 0.6931 -0.0575 0.0368  0.0799  599 GLN A O   
4713 C CB  . GLN A 599 ? 0.5350 0.4885 0.6433 -0.0494 0.0069  0.0817  599 GLN A CB  
4714 C CG  . GLN A 599 ? 0.5583 0.5240 0.6896 -0.0416 0.0011  0.0867  599 GLN A CG  
4715 C CD  . GLN A 599 ? 0.5344 0.5178 0.6938 -0.0333 0.0157  0.0880  599 GLN A CD  
4716 O OE1 . GLN A 599 ? 0.5218 0.4983 0.6746 -0.0282 0.0310  0.0805  599 GLN A OE1 
4717 N NE2 . GLN A 599 ? 0.5347 0.5424 0.7266 -0.0322 0.0114  0.0964  599 GLN A NE2 
4718 N N   . VAL A 600 ? 0.5410 0.4861 0.6244 -0.0695 0.0148  0.0862  600 VAL A N   
4719 C CA  . VAL A 600 ? 0.5597 0.4975 0.6223 -0.0719 0.0222  0.0877  600 VAL A CA  
4720 C C   . VAL A 600 ? 0.5570 0.5026 0.6307 -0.0818 0.0267  0.0982  600 VAL A C   
4721 O O   . VAL A 600 ? 0.5388 0.4889 0.6015 -0.0825 0.0377  0.1030  600 VAL A O   
4722 C CB  . VAL A 600 ? 0.5768 0.4913 0.6141 -0.0711 0.0133  0.0844  600 VAL A CB  
4723 C CG1 . VAL A 600 ? 0.5367 0.4489 0.5518 -0.0689 0.0211  0.0849  600 VAL A CG1 
4724 C CG2 . VAL A 600 ? 0.6415 0.5475 0.6732 -0.0641 0.0062  0.0762  600 VAL A CG2 
4725 N N   . ASN A 601 ? 0.5594 0.5078 0.6545 -0.0902 0.0187  0.1023  601 ASN A N   
4726 C CA  . ASN A 601 ? 0.5870 0.5458 0.7012 -0.1010 0.0249  0.1125  601 ASN A CA  
4727 C C   . ASN A 601 ? 0.5726 0.5185 0.6682 -0.1046 0.0320  0.1213  601 ASN A C   
4728 O O   . ASN A 601 ? 0.5789 0.5013 0.6596 -0.1060 0.0243  0.1214  601 ASN A O   
4729 C CB  . ASN A 601 ? 0.6537 0.6416 0.7907 -0.0988 0.0379  0.1150  601 ASN A CB  
4730 C CG  . ASN A 601 ? 0.6719 0.6760 0.8387 -0.1111 0.0421  0.1248  601 ASN A CG  
4731 O OD1 . ASN A 601 ? 0.6819 0.6749 0.8557 -0.1225 0.0337  0.1285  601 ASN A OD1 
4732 N ND2 . ASN A 601 ? 0.5922 0.6226 0.7784 -0.1093 0.0566  0.1282  601 ASN A ND2 
4733 N N   . ALA A 602 ? 0.5359 0.4981 0.6331 -0.1054 0.0473  0.1297  602 ALA A N   
4734 C CA  . ALA A 602 ? 0.5543 0.5090 0.6363 -0.1088 0.0550  0.1428  602 ALA A CA  
4735 C C   . ALA A 602 ? 0.5886 0.5323 0.6361 -0.0995 0.0538  0.1405  602 ALA A C   
4736 O O   . ALA A 602 ? 0.5998 0.5337 0.6338 -0.1006 0.0559  0.1527  602 ALA A O   
4737 C CB  . ALA A 602 ? 0.6401 0.6198 0.7316 -0.1123 0.0728  0.1531  602 ALA A CB  
4738 N N   . ASP A 603 ? 0.5290 0.4750 0.5645 -0.0904 0.0507  0.1262  603 ASP A N   
4739 C CA  . ASP A 603 ? 0.6132 0.5537 0.6192 -0.0828 0.0495  0.1222  603 ASP A CA  
4740 C C   . ASP A 603 ? 0.5716 0.4887 0.5693 -0.0794 0.0355  0.1156  603 ASP A C   
4741 O O   . ASP A 603 ? 0.5694 0.4836 0.5470 -0.0729 0.0333  0.1096  603 ASP A O   
4742 C CB  . ASP A 603 ? 0.5529 0.5105 0.5511 -0.0765 0.0577  0.1092  603 ASP A CB  
4743 C CG  . ASP A 603 ? 0.6933 0.6748 0.6892 -0.0784 0.0739  0.1144  603 ASP A CG  
4744 O OD1 . ASP A 603 ? 0.6627 0.6485 0.6422 -0.0806 0.0779  0.1272  603 ASP A OD1 
4745 O OD2 . ASP A 603 ? 0.6498 0.6464 0.6603 -0.0770 0.0834  0.1065  603 ASP A OD2 
4746 N N   . LEU A 604 ? 0.5499 0.4522 0.5626 -0.0845 0.0265  0.1156  604 LEU A N   
4747 C CA  . LEU A 604 ? 0.5879 0.4683 0.5915 -0.0817 0.0149  0.1089  604 LEU A CA  
4748 C C   . LEU A 604 ? 0.6078 0.4718 0.6003 -0.0814 0.0144  0.1188  604 LEU A C   
4749 O O   . LEU A 604 ? 0.5945 0.4513 0.5984 -0.0885 0.0170  0.1300  604 LEU A O   
4750 C CB  . LEU A 604 ? 0.5901 0.4629 0.6113 -0.0880 0.0054  0.1036  604 LEU A CB  
4751 C CG  . LEU A 604 ? 0.6352 0.4869 0.6466 -0.0862 -0.0059 0.0945  604 LEU A CG  
4752 C CD1 . LEU A 604 ? 0.5860 0.4402 0.5831 -0.0766 -0.0078 0.0851  604 LEU A CD1 
4753 C CD2 . LEU A 604 ? 0.6130 0.4621 0.6410 -0.0952 -0.0151 0.0898  604 LEU A CD2 
4754 N N   . PRO A 605 ? 0.5888 0.4470 0.5622 -0.0732 0.0118  0.1161  605 PRO A N   
4755 C CA  . PRO A 605 ? 0.6247 0.4683 0.5911 -0.0706 0.0112  0.1274  605 PRO A CA  
4756 C C   . PRO A 605 ? 0.6073 0.4240 0.5855 -0.0753 0.0056  0.1259  605 PRO A C   
4757 O O   . PRO A 605 ? 0.5936 0.4026 0.5756 -0.0775 -0.0014 0.1122  605 PRO A O   
4758 C CB  . PRO A 605 ? 0.5619 0.4087 0.5099 -0.0608 0.0078  0.1209  605 PRO A CB  
4759 C CG  . PRO A 605 ? 0.5682 0.4350 0.5115 -0.0598 0.0104  0.1091  605 PRO A CG  
4760 C CD  . PRO A 605 ? 0.5298 0.3959 0.4901 -0.0660 0.0102  0.1036  605 PRO A CD  
4761 N N   . TYR A 606 ? 0.6138 0.4161 0.5976 -0.0771 0.0092  0.1403  606 TYR A N   
4762 C CA  . TYR A 606 ? 0.7061 0.4797 0.7028 -0.0829 0.0058  0.1371  606 TYR A CA  
4763 C C   . TYR A 606 ? 0.6792 0.4365 0.6659 -0.0759 -0.0013 0.1229  606 TYR A C   
4764 O O   . TYR A 606 ? 0.6925 0.4345 0.6849 -0.0818 -0.0067 0.1094  606 TYR A O   
4765 C CB  . TYR A 606 ? 0.6448 0.4022 0.6502 -0.0842 0.0130  0.1566  606 TYR A CB  
4766 C CG  . TYR A 606 ? 0.7565 0.4790 0.7739 -0.0880 0.0110  0.1511  606 TYR A CG  
4767 C CD1 . TYR A 606 ? 0.7914 0.5028 0.8267 -0.1026 0.0088  0.1408  606 TYR A CD1 
4768 C CD2 . TYR A 606 ? 0.7487 0.4508 0.7609 -0.0772 0.0116  0.1547  606 TYR A CD2 
4769 C CE1 . TYR A 606 ? 0.9123 0.5908 0.9577 -0.1077 0.0076  0.1320  606 TYR A CE1 
4770 C CE2 . TYR A 606 ? 0.8077 0.4755 0.8317 -0.0803 0.0119  0.1471  606 TYR A CE2 
4771 C CZ  . TYR A 606 ? 0.8746 0.5297 0.9139 -0.0962 0.0101  0.1346  606 TYR A CZ  
4772 O OH  . TYR A 606 ? 1.0069 0.6271 1.0570 -0.1009 0.0110  0.1236  606 TYR A OH  
4773 N N   . GLU A 607 ? 0.6300 0.3925 0.6018 -0.0640 -0.0012 0.1253  607 GLU A N   
4774 C CA  . GLU A 607 ? 0.6890 0.4384 0.6529 -0.0569 -0.0060 0.1127  607 GLU A CA  
4775 C C   . GLU A 607 ? 0.6708 0.4254 0.6300 -0.0603 -0.0120 0.0944  607 GLU A C   
4776 O O   . GLU A 607 ? 0.6966 0.4352 0.6526 -0.0599 -0.0158 0.0821  607 GLU A O   
4777 C CB  . GLU A 607 ? 0.6894 0.4514 0.6413 -0.0444 -0.0052 0.1187  607 GLU A CB  
4778 C CG  . GLU A 607 ? 0.7651 0.5192 0.7216 -0.0376 -0.0011 0.1381  607 GLU A CG  
4779 C CD  . GLU A 607 ? 0.8120 0.5815 0.7589 -0.0248 -0.0028 0.1428  607 GLU A CD  
4780 O OE1 . GLU A 607 ? 0.8363 0.6283 0.7720 -0.0237 -0.0057 0.1333  607 GLU A OE1 
4781 O OE2 . GLU A 607 ? 1.0172 0.7765 0.9700 -0.0158 -0.0011 0.1560  607 GLU A OE2 
4782 N N   . ILE A 608 ? 0.6173 0.3939 0.5758 -0.0630 -0.0121 0.0929  608 ILE A N   
4783 C CA  . ILE A 608 ? 0.6169 0.3985 0.5739 -0.0656 -0.0176 0.0795  608 ILE A CA  
4784 C C   . ILE A 608 ? 0.6315 0.4034 0.6006 -0.0762 -0.0226 0.0745  608 ILE A C   
4785 O O   . ILE A 608 ? 0.6258 0.3909 0.5901 -0.0778 -0.0292 0.0627  608 ILE A O   
4786 C CB  . ILE A 608 ? 0.5851 0.3911 0.5423 -0.0644 -0.0148 0.0799  608 ILE A CB  
4787 C CG1 . ILE A 608 ? 0.5832 0.3988 0.5270 -0.0558 -0.0112 0.0794  608 ILE A CG1 
4788 C CG2 . ILE A 608 ? 0.5873 0.3982 0.5480 -0.0665 -0.0201 0.0704  608 ILE A CG2 
4789 C CD1 . ILE A 608 ? 0.6049 0.4124 0.5388 -0.0503 -0.0148 0.0694  608 ILE A CD1 
4790 N N   . GLU A 609 ? 0.5631 0.3363 0.5479 -0.0845 -0.0195 0.0834  609 GLU A N   
4791 C CA  . GLU A 609 ? 0.6362 0.4013 0.6359 -0.0970 -0.0246 0.0778  609 GLU A CA  
4792 C C   . GLU A 609 ? 0.6712 0.4072 0.6669 -0.0988 -0.0270 0.0689  609 GLU A C   
4793 O O   . GLU A 609 ? 0.6764 0.4061 0.6746 -0.1073 -0.0345 0.0556  609 GLU A O   
4794 C CB  . GLU A 609 ? 0.6300 0.4017 0.6500 -0.1062 -0.0185 0.0905  609 GLU A CB  
4795 C CG  . GLU A 609 ? 0.7427 0.5059 0.7825 -0.1216 -0.0231 0.0847  609 GLU A CG  
4796 C CD  . GLU A 609 ? 0.8860 0.6552 0.9482 -0.1315 -0.0149 0.0990  609 GLU A CD  
4797 O OE1 . GLU A 609 ? 0.9165 0.7031 0.9775 -0.1261 -0.0064 0.1125  609 GLU A OE1 
4798 O OE2 . GLU A 609 ? 1.0398 0.7970 1.1209 -0.1454 -0.0162 0.0962  609 GLU A OE2 
4799 N N   . ARG A 610 ? 0.6004 0.3198 0.5904 -0.0906 -0.0208 0.0756  610 ARG A N   
4800 C CA  . ARG A 610 ? 0.6064 0.2963 0.5945 -0.0900 -0.0206 0.0665  610 ARG A CA  
4801 C C   . ARG A 610 ? 0.6289 0.3177 0.5992 -0.0852 -0.0263 0.0493  610 ARG A C   
4802 O O   . ARG A 610 ? 0.6650 0.3369 0.6331 -0.0911 -0.0296 0.0341  610 ARG A O   
4803 C CB  . ARG A 610 ? 0.7168 0.3928 0.7059 -0.0794 -0.0121 0.0807  610 ARG A CB  
4804 C CG  . ARG A 610 ? 0.6733 0.3166 0.6644 -0.0765 -0.0092 0.0723  610 ARG A CG  
4805 C CD  . ARG A 610 ? 0.7337 0.3650 0.7319 -0.0653 -0.0007 0.0913  610 ARG A CD  
4806 N NE  . ARG A 610 ? 0.7547 0.4070 0.7398 -0.0507 -0.0009 0.0993  610 ARG A NE  
4807 C CZ  . ARG A 610 ? 0.7781 0.4347 0.7662 -0.0400 0.0037  0.1195  610 ARG A CZ  
4808 N NH1 . ARG A 610 ? 0.8655 0.5052 0.8687 -0.0409 0.0101  0.1368  610 ARG A NH1 
4809 N NH2 . ARG A 610 ? 0.8030 0.4827 0.7793 -0.0286 0.0016  0.1232  610 ARG A NH2 
4810 N N   . GLU A 611 ? 0.6236 0.3302 0.5806 -0.0752 -0.0267 0.0510  611 GLU A N   
4811 C CA  . GLU A 611 ? 0.6352 0.3426 0.5756 -0.0711 -0.0308 0.0372  611 GLU A CA  
4812 C C   . GLU A 611 ? 0.6716 0.3868 0.6105 -0.0812 -0.0398 0.0267  611 GLU A C   
4813 O O   . GLU A 611 ? 0.6576 0.3635 0.5848 -0.0834 -0.0437 0.0126  611 GLU A O   
4814 C CB  . GLU A 611 ? 0.5979 0.3239 0.5288 -0.0608 -0.0287 0.0421  611 GLU A CB  
4815 C CG  . GLU A 611 ? 0.6356 0.3588 0.5660 -0.0505 -0.0221 0.0506  611 GLU A CG  
4816 C CD  . GLU A 611 ? 0.6715 0.3731 0.5987 -0.0449 -0.0192 0.0434  611 GLU A CD  
4817 O OE1 . GLU A 611 ? 0.6493 0.3437 0.5665 -0.0465 -0.0213 0.0292  611 GLU A OE1 
4818 O OE2 . GLU A 611 ? 0.7774 0.4699 0.7122 -0.0382 -0.0142 0.0525  611 GLU A OE2 
4819 N N   . LEU A 612 ? 0.6477 0.3825 0.5982 -0.0870 -0.0431 0.0335  612 LEU A N   
4820 C CA  . LEU A 612 ? 0.6628 0.4096 0.6164 -0.0965 -0.0531 0.0260  612 LEU A CA  
4821 C C   . LEU A 612 ? 0.6712 0.4006 0.6294 -0.1089 -0.0575 0.0138  612 LEU A C   
4822 O O   . LEU A 612 ? 0.6419 0.3723 0.5890 -0.1140 -0.0660 0.0001  612 LEU A O   
4823 C CB  . LEU A 612 ? 0.6413 0.4121 0.6136 -0.1002 -0.0540 0.0367  612 LEU A CB  
4824 C CG  . LEU A 612 ? 0.7073 0.4971 0.6893 -0.1092 -0.0652 0.0323  612 LEU A CG  
4825 C CD1 . LEU A 612 ? 0.6428 0.4442 0.6086 -0.1018 -0.0715 0.0290  612 LEU A CD1 
4826 C CD2 . LEU A 612 ? 0.7587 0.5703 0.7657 -0.1131 -0.0630 0.0436  612 LEU A CD2 
4827 N N   . ARG A 613 ? 0.6677 0.3808 0.6418 -0.1144 -0.0513 0.0185  613 ARG A N   
4828 C CA  . ARG A 613 ? 0.7022 0.3937 0.6835 -0.1272 -0.0532 0.0053  613 ARG A CA  
4829 C C   . ARG A 613 ? 0.6607 0.3289 0.6223 -0.1221 -0.0515 -0.0106 613 ARG A C   
4830 O O   . ARG A 613 ? 0.6922 0.3518 0.6483 -0.1324 -0.0574 -0.0295 613 ARG A O   
4831 C CB  . ARG A 613 ? 0.7517 0.4264 0.7554 -0.1323 -0.0440 0.0167  613 ARG A CB  
4832 C CG  . ARG A 613 ? 0.6520 0.3485 0.6779 -0.1411 -0.0444 0.0298  613 ARG A CG  
4833 C CD  . ARG A 613 ? 0.8050 0.4810 0.8521 -0.1479 -0.0341 0.0410  613 ARG A CD  
4834 N NE  . ARG A 613 ? 0.8876 0.5838 0.9586 -0.1592 -0.0331 0.0520  613 ARG A NE  
4835 C CZ  . ARG A 613 ? 0.9959 0.6779 1.0908 -0.1715 -0.0261 0.0592  613 ARG A CZ  
4836 N NH1 . ARG A 613 ? 0.8508 0.4956 0.9500 -0.1740 -0.0196 0.0564  613 ARG A NH1 
4837 N NH2 . ARG A 613 ? 1.0676 0.7726 1.1846 -0.1814 -0.0241 0.0698  613 ARG A NH2 
4838 N N   . ALA A 614 ? 0.6657 0.3255 0.6170 -0.1068 -0.0432 -0.0043 614 ALA A N   
4839 C CA  . ALA A 614 ? 0.7231 0.3622 0.6585 -0.1004 -0.0391 -0.0185 614 ALA A CA  
4840 C C   . ALA A 614 ? 0.7134 0.3669 0.6251 -0.1004 -0.0467 -0.0320 614 ALA A C   
4841 O O   . ALA A 614 ? 0.7677 0.4075 0.6662 -0.1045 -0.0475 -0.0510 614 ALA A O   
4842 C CB  . ALA A 614 ? 0.6589 0.2919 0.5932 -0.0836 -0.0290 -0.0064 614 ALA A CB  
4843 N N   . LEU A 615 ? 0.6777 0.3583 0.5833 -0.0956 -0.0515 -0.0221 615 LEU A N   
4844 C CA  . LEU A 615 ? 0.7129 0.4085 0.5970 -0.0954 -0.0587 -0.0305 615 LEU A CA  
4845 C C   . LEU A 615 ? 0.7596 0.4619 0.6423 -0.1106 -0.0708 -0.0433 615 LEU A C   
4846 O O   . LEU A 615 ? 0.7181 0.4192 0.5795 -0.1138 -0.0751 -0.0588 615 LEU A O   
4847 C CB  . LEU A 615 ? 0.7379 0.4585 0.6216 -0.0877 -0.0604 -0.0155 615 LEU A CB  
4848 C CG  . LEU A 615 ? 0.7133 0.4509 0.5778 -0.0864 -0.0676 -0.0184 615 LEU A CG  
4849 C CD1 . LEU A 615 ? 0.7110 0.4361 0.5514 -0.0809 -0.0620 -0.0295 615 LEU A CD1 
4850 C CD2 . LEU A 615 ? 0.5929 0.3503 0.4627 -0.0785 -0.0669 -0.0027 615 LEU A CD2 
4851 N N   . LYS A 616 ? 0.7565 0.4687 0.6619 -0.1208 -0.0764 -0.0374 616 LYS A N   
4852 C CA  . LYS A 616 ? 0.7473 0.4694 0.6562 -0.1372 -0.0890 -0.0500 616 LYS A CA  
4853 C C   . LYS A 616 ? 0.7606 0.4555 0.6613 -0.1467 -0.0872 -0.0730 616 LYS A C   
4854 O O   . LYS A 616 ? 0.7804 0.4830 0.6660 -0.1567 -0.0975 -0.0905 616 LYS A O   
4855 C CB  . LYS A 616 ? 0.7394 0.4741 0.6800 -0.1470 -0.0920 -0.0394 616 LYS A CB  
4856 C CG  . LYS A 616 ? 0.8519 0.6034 0.8023 -0.1653 -0.1064 -0.0512 616 LYS A CG  
4857 C CD  . LYS A 616 ? 0.8894 0.6622 0.8729 -0.1720 -0.1085 -0.0367 616 LYS A CD  
4858 C CE  . LYS A 616 ? 0.9279 0.7254 0.9133 -0.1573 -0.1071 -0.0168 616 LYS A CE  
4859 N NZ  . LYS A 616 ? 0.9155 0.7350 0.9336 -0.1626 -0.1069 -0.0034 616 LYS A NZ  
4860 N N   . GLN A 617 ? 0.7856 0.4488 0.6957 -0.1432 -0.0740 -0.0735 617 GLN A N   
4861 C CA  . GLN A 617 ? 0.8096 0.4420 0.7161 -0.1513 -0.0696 -0.0962 617 GLN A CA  
4862 C C   . GLN A 617 ? 0.7896 0.4170 0.6634 -0.1438 -0.0674 -0.1124 617 GLN A C   
4863 O O   . GLN A 617 ? 0.8153 0.4379 0.6739 -0.1550 -0.0723 -0.1364 617 GLN A O   
4864 C CB  . GLN A 617 ? 0.7671 0.3666 0.6951 -0.1465 -0.0546 -0.0885 617 GLN A CB  
4865 C CG  . GLN A 617 ? 0.7817 0.3448 0.7155 -0.1568 -0.0484 -0.1109 617 GLN A CG  
4866 C CD  . GLN A 617 ? 0.8218 0.3885 0.7708 -0.1805 -0.0584 -0.1243 617 GLN A CD  
4867 O OE1 . GLN A 617 ? 0.9371 0.5328 0.8987 -0.1881 -0.0684 -0.1121 617 GLN A OE1 
4868 N NE2 . GLN A 617 ? 0.9146 0.4527 0.8644 -0.1929 -0.0552 -0.1506 617 GLN A NE2 
4869 N N   . ARG A 618 ? 0.7680 0.3981 0.6304 -0.1259 -0.0595 -0.1005 618 ARG A N   
4870 C CA  . ARG A 618 ? 0.7822 0.4086 0.6153 -0.1182 -0.0548 -0.1139 618 ARG A CA  
4871 C C   . ARG A 618 ? 0.8001 0.4528 0.6073 -0.1259 -0.0683 -0.1233 618 ARG A C   
4872 O O   . ARG A 618 ? 0.8474 0.4945 0.6291 -0.1291 -0.0675 -0.1441 618 ARG A O   
4873 C CB  . ARG A 618 ? 0.7184 0.3490 0.5484 -0.0992 -0.0451 -0.0970 618 ARG A CB  
4874 C CG  . ARG A 618 ? 0.7007 0.3085 0.5523 -0.0893 -0.0321 -0.0879 618 ARG A CG  
4875 C CD  . ARG A 618 ? 0.6669 0.2825 0.5131 -0.0719 -0.0235 -0.0760 618 ARG A CD  
4876 N NE  . ARG A 618 ? 0.7156 0.3599 0.5605 -0.0691 -0.0300 -0.0587 618 ARG A NE  
4877 C CZ  . ARG A 618 ? 0.7751 0.4281 0.6383 -0.0658 -0.0302 -0.0402 618 ARG A CZ  
4878 N NH1 . ARG A 618 ? 0.7760 0.4138 0.6592 -0.0641 -0.0249 -0.0330 618 ARG A NH1 
4879 N NH2 . ARG A 618 ? 0.7033 0.3806 0.5645 -0.0638 -0.0349 -0.0283 618 ARG A NH2 
4880 N N   . ILE A 619 ? 0.8013 0.4841 0.6142 -0.1283 -0.0805 -0.1076 619 ILE A N   
4881 C CA  . ILE A 619 ? 0.8316 0.5432 0.6226 -0.1343 -0.0949 -0.1119 619 ILE A CA  
4882 C C   . ILE A 619 ? 0.8628 0.5743 0.6508 -0.1539 -0.1059 -0.1354 619 ILE A C   
4883 O O   . ILE A 619 ? 0.8781 0.5987 0.6363 -0.1594 -0.1123 -0.1523 619 ILE A O   
4884 C CB  . ILE A 619 ? 0.8459 0.5885 0.6500 -0.1305 -0.1041 -0.0879 619 ILE A CB  
4885 C CG1 . ILE A 619 ? 0.7303 0.4743 0.5310 -0.1126 -0.0936 -0.0693 619 ILE A CG1 
4886 C CG2 . ILE A 619 ? 0.8269 0.6016 0.6152 -0.1380 -0.1216 -0.0902 619 ILE A CG2 
4887 C CD1 . ILE A 619 ? 0.8399 0.6102 0.6546 -0.1077 -0.0998 -0.0474 619 ILE A CD1 
4888 N N   . SER A 620 ? 0.8508 0.5534 0.6694 -0.1658 -0.1079 -0.1372 620 SER A N   
4889 C CA  . SER A 620 ? 0.8632 0.5654 0.6843 -0.1871 -0.1182 -0.1610 620 SER A CA  
4890 C C   . SER A 620 ? 0.8956 0.5683 0.6942 -0.1915 -0.1098 -0.1910 620 SER A C   
4891 O O   . SER A 620 ? 0.9128 0.5909 0.6997 -0.2089 -0.1199 -0.2160 620 SER A O   
4892 C CB  . SER A 620 ? 0.9111 0.6031 0.7732 -0.1986 -0.1173 -0.1562 620 SER A CB  
4893 O OG  . SER A 620 ? 0.9456 0.5971 0.8217 -0.1922 -0.0989 -0.1553 620 SER A OG  
4894 N N   . GLN A 621 ? 0.9016 0.5451 0.6950 -0.1764 -0.0915 -0.1902 621 GLN A N   
4895 C CA  . GLN A 621 ? 0.9833 0.5981 0.7568 -0.1774 -0.0802 -0.2183 621 GLN A CA  
4896 C C   . GLN A 621 ? 1.0358 0.6683 0.7659 -0.1706 -0.0813 -0.2267 621 GLN A C   
4897 O O   . GLN A 621 ? 1.0924 0.7042 0.8021 -0.1701 -0.0704 -0.2508 621 GLN A O   
4898 C CB  . GLN A 621 ? 1.0111 0.5877 0.8033 -0.1629 -0.0592 -0.2123 621 GLN A CB  
4899 C CG  . GLN A 621 ? 0.9605 0.5140 0.7931 -0.1701 -0.0554 -0.2055 621 GLN A CG  
4900 C CD  . GLN A 621 ? 1.0513 0.5909 0.8919 -0.1939 -0.0611 -0.2331 621 GLN A CD  
4901 O OE1 . GLN A 621 ? 1.1082 0.6215 0.9369 -0.1989 -0.0530 -0.2621 621 GLN A OE1 
4902 N NE2 . GLN A 621 ? 1.0515 0.6097 0.9136 -0.2092 -0.0744 -0.2256 621 GLN A NE2 
4903 N N   . MET A 622 ? 1.0407 0.7100 0.7572 -0.1652 -0.0927 -0.2070 622 MET A N   
4904 C CA  . MET A 622 ? 1.0206 0.7091 0.6954 -0.1594 -0.0939 -0.2111 622 MET A CA  
4905 C C   . MET A 622 ? 1.0375 0.7412 0.6846 -0.1778 -0.1078 -0.2384 622 MET A C   
4906 O O   . MET A 622 ? 1.1386 0.8529 0.8013 -0.1949 -0.1228 -0.2460 622 MET A O   
4907 C CB  . MET A 622 ? 0.9607 0.6821 0.6326 -0.1482 -0.1014 -0.1797 622 MET A CB  
4908 C CG  . MET A 622 ? 0.9120 0.6226 0.6067 -0.1310 -0.0883 -0.1549 622 MET A CG  
4909 S SD  . MET A 622 ? 0.9426 0.6871 0.6306 -0.1186 -0.0942 -0.1232 622 MET A SD  
4910 C CE  . MET A 622 ? 0.9417 0.6984 0.5796 -0.1163 -0.0924 -0.1337 622 MET A CE  
4911 O OXT . MET A 622 ? 1.2042 0.9124 0.8125 -0.1767 -0.1044 -0.2540 622 MET A OXT 
# 
