data_9F84
# 
_entry.id   9F84 
# 
_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   9F84         pdb_00009f84 10.2210/pdb9f84/pdb 
WWPDB D_1292138057 ?            ?                   
# 
_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       2025-05-21 
_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                        9F84 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              fredrik.ekstrom@foi.se 
_pdbx_contact_author.name_first         Fredrik 
_pdbx_contact_author.name_last          Ekstrom 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2483-0124 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Forsgren, N.' 1 ? 
'Ekstrom, F.'  2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Structure of choline O-acetyltransferase in complex with 1-Methyl-4-[2-(1-naphthyl)-2-(propylthio)ethyl]pyridinium at 1.9 Angstrom resultion.
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Forsgren, N.' 1 ? 
primary 'Ekstrom, F.'  2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Choline O-acetyltransferase'                                            68113.352 1   2.3.1.6 
E225A,D226A,E227A,K518A,E519A,K582A,E583A ? 
;Engineered mutations: E225A, D226A, E227A, K518A, E519A, K582A, E583A Residues 346-358 from UniProt sequence replaced with PELVRSPMVP,Engineered mutations: E225A, D226A, E227A, K518A, E519A, K582A, E583A Residues 346-358 from UniProt sequence replaced with PELVRSPMVP,Engineered mutations: E225A, D226A, E227A, K518A, E519A, K582A, E583A Residues 346-358 from UniProt sequence replaced with PELVRSPMVP,Engineered mutations: E225A, D226A, E227A, K518A, E519A, K582A, E583A Residues 346-358 from UniProt sequence replaced with PELVRSPMVP
;
2 non-polymer syn '1-methyl-4-[(2S)-2-naphthalen-1-yl-2-propylsulfanyl-ethyl]-4H-pyridine' 323.495   1   ?       ? ? ? 
3 non-polymer syn 'SODIUM ION'                                                             22.990    1   ?       ? ? ? 
4 water       nat water                                                                    18.015    434 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CHOACTase,ChAT,Choline acetylase' 
# 
_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       
;AAAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYW
LNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFS
SYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNAAARLPPIGLLTSDGR
SEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGV
VCEHSPFDGIVLVQCTEHLLKHMTQPELVRSPMVPLPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGK
TFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLK
DAIRAQTAYTVMAITGMAIDNHLLALRELARAMCAALPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGAC
YNPQPETILFCISSFHSCAATSSSKFAKAVEESLIDMRDLCSLLPPTESKPL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AAAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYW
LNDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFS
SYRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNAAARLPPIGLLTSDGR
SEWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGV
VCEHSPFDGIVLVQCTEHLLKHMTQPELVRSPMVPLPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGK
TFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYESASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLK
DAIRAQTAYTVMAITGMAIDNHLLALRELARAMCAALPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGAC
YNPQPETILFCISSFHSCAATSSSKFAKAVEESLIDMRDLCSLLPPTESKPL
;
_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 '1-methyl-4-[(2S)-2-naphthalen-1-yl-2-propylsulfanyl-ethyl]-4H-pyridine' A1IAP 
3 'SODIUM ION'                                                             NA    
4 water                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ALA n 
1 3   ALA n 
1 4   LYS n 
1 5   THR n 
1 6   PRO n 
1 7   SER n 
1 8   SER n 
1 9   GLU n 
1 10  GLU n 
1 11  SER n 
1 12  GLY n 
1 13  LEU n 
1 14  PRO n 
1 15  LYS n 
1 16  LEU n 
1 17  PRO n 
1 18  VAL n 
1 19  PRO n 
1 20  PRO n 
1 21  LEU n 
1 22  GLN n 
1 23  GLN n 
1 24  THR n 
1 25  LEU n 
1 26  ALA n 
1 27  THR n 
1 28  TYR n 
1 29  LEU n 
1 30  GLN n 
1 31  CYS n 
1 32  MET n 
1 33  ARG n 
1 34  HIS n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  GLU n 
1 39  GLU n 
1 40  GLN n 
1 41  PHE n 
1 42  ARG n 
1 43  LYS n 
1 44  SER n 
1 45  GLN n 
1 46  ALA n 
1 47  ILE n 
1 48  VAL n 
1 49  GLN n 
1 50  GLN n 
1 51  PHE n 
1 52  GLY n 
1 53  ALA n 
1 54  PRO n 
1 55  GLY n 
1 56  GLY n 
1 57  LEU n 
1 58  GLY n 
1 59  GLU n 
1 60  THR n 
1 61  LEU n 
1 62  GLN n 
1 63  GLN n 
1 64  LYS n 
1 65  LEU n 
1 66  LEU n 
1 67  GLU n 
1 68  ARG n 
1 69  GLN n 
1 70  GLU n 
1 71  LYS n 
1 72  THR n 
1 73  ALA n 
1 74  ASN n 
1 75  TRP n 
1 76  VAL n 
1 77  SER n 
1 78  GLU n 
1 79  TYR n 
1 80  TRP n 
1 81  LEU n 
1 82  ASN n 
1 83  ASP n 
1 84  MET n 
1 85  TYR n 
1 86  LEU n 
1 87  ASN n 
1 88  ASN n 
1 89  ARG n 
1 90  LEU n 
1 91  ALA n 
1 92  LEU n 
1 93  PRO n 
1 94  VAL n 
1 95  ASN n 
1 96  SER n 
1 97  SER n 
1 98  PRO n 
1 99  ALA n 
1 100 VAL n 
1 101 ILE n 
1 102 PHE n 
1 103 ALA n 
1 104 ARG n 
1 105 GLN n 
1 106 HIS n 
1 107 PHE n 
1 108 PRO n 
1 109 GLY n 
1 110 THR n 
1 111 ASP n 
1 112 ASP n 
1 113 GLN n 
1 114 LEU n 
1 115 ARG n 
1 116 PHE n 
1 117 ALA n 
1 118 ALA n 
1 119 SER n 
1 120 LEU n 
1 121 ILE n 
1 122 SER n 
1 123 GLY n 
1 124 VAL n 
1 125 LEU n 
1 126 SER n 
1 127 TYR n 
1 128 LYS n 
1 129 ALA n 
1 130 LEU n 
1 131 LEU n 
1 132 ASP n 
1 133 SER n 
1 134 HIS n 
1 135 SER n 
1 136 ILE n 
1 137 PRO n 
1 138 THR n 
1 139 ASP n 
1 140 CYS n 
1 141 ALA n 
1 142 LYS n 
1 143 GLY n 
1 144 GLN n 
1 145 LEU n 
1 146 SER n 
1 147 GLY n 
1 148 GLN n 
1 149 PRO n 
1 150 LEU n 
1 151 CYS n 
1 152 MET n 
1 153 LYS n 
1 154 GLN n 
1 155 TYR n 
1 156 TYR n 
1 157 GLY n 
1 158 LEU n 
1 159 PHE n 
1 160 SER n 
1 161 SER n 
1 162 TYR n 
1 163 ARG n 
1 164 LEU n 
1 165 PRO n 
1 166 GLY n 
1 167 HIS n 
1 168 THR n 
1 169 GLN n 
1 170 ASP n 
1 171 THR n 
1 172 LEU n 
1 173 VAL n 
1 174 ALA n 
1 175 GLN n 
1 176 ASN n 
1 177 SER n 
1 178 SER n 
1 179 ILE n 
1 180 MET n 
1 181 PRO n 
1 182 GLU n 
1 183 PRO n 
1 184 GLU n 
1 185 HIS n 
1 186 VAL n 
1 187 ILE n 
1 188 VAL n 
1 189 ALA n 
1 190 CYS n 
1 191 CYS n 
1 192 ASN n 
1 193 GLN n 
1 194 PHE n 
1 195 PHE n 
1 196 VAL n 
1 197 LEU n 
1 198 ASP n 
1 199 VAL n 
1 200 VAL n 
1 201 ILE n 
1 202 ASN n 
1 203 PHE n 
1 204 ARG n 
1 205 ARG n 
1 206 LEU n 
1 207 SER n 
1 208 GLU n 
1 209 GLY n 
1 210 ASP n 
1 211 LEU n 
1 212 PHE n 
1 213 THR n 
1 214 GLN n 
1 215 LEU n 
1 216 ARG n 
1 217 LYS n 
1 218 ILE n 
1 219 VAL n 
1 220 LYS n 
1 221 MET n 
1 222 ALA n 
1 223 SER n 
1 224 ASN n 
1 225 ALA n 
1 226 ALA n 
1 227 ALA n 
1 228 ARG n 
1 229 LEU n 
1 230 PRO n 
1 231 PRO n 
1 232 ILE n 
1 233 GLY n 
1 234 LEU n 
1 235 LEU n 
1 236 THR n 
1 237 SER n 
1 238 ASP n 
1 239 GLY n 
1 240 ARG n 
1 241 SER n 
1 242 GLU n 
1 243 TRP n 
1 244 ALA n 
1 245 GLU n 
1 246 ALA n 
1 247 ARG n 
1 248 THR n 
1 249 VAL n 
1 250 LEU n 
1 251 VAL n 
1 252 LYS n 
1 253 ASP n 
1 254 SER n 
1 255 THR n 
1 256 ASN n 
1 257 ARG n 
1 258 ASP n 
1 259 SER n 
1 260 LEU n 
1 261 ASP n 
1 262 MET n 
1 263 ILE n 
1 264 GLU n 
1 265 ARG n 
1 266 CYS n 
1 267 ILE n 
1 268 CYS n 
1 269 LEU n 
1 270 VAL n 
1 271 CYS n 
1 272 LEU n 
1 273 ASP n 
1 274 ALA n 
1 275 PRO n 
1 276 GLY n 
1 277 GLY n 
1 278 VAL n 
1 279 GLU n 
1 280 LEU n 
1 281 SER n 
1 282 ASP n 
1 283 THR n 
1 284 HIS n 
1 285 ARG n 
1 286 ALA n 
1 287 LEU n 
1 288 GLN n 
1 289 LEU n 
1 290 LEU n 
1 291 HIS n 
1 292 GLY n 
1 293 GLY n 
1 294 GLY n 
1 295 TYR n 
1 296 SER n 
1 297 LYS n 
1 298 ASN n 
1 299 GLY n 
1 300 ALA n 
1 301 ASN n 
1 302 ARG n 
1 303 TRP n 
1 304 TYR n 
1 305 ASP n 
1 306 LYS n 
1 307 SER n 
1 308 LEU n 
1 309 GLN n 
1 310 PHE n 
1 311 VAL n 
1 312 VAL n 
1 313 GLY n 
1 314 ARG n 
1 315 ASP n 
1 316 GLY n 
1 317 THR n 
1 318 CYS n 
1 319 GLY n 
1 320 VAL n 
1 321 VAL n 
1 322 CYS n 
1 323 GLU n 
1 324 HIS n 
1 325 SER n 
1 326 PRO n 
1 327 PHE n 
1 328 ASP n 
1 329 GLY n 
1 330 ILE n 
1 331 VAL n 
1 332 LEU n 
1 333 VAL n 
1 334 GLN n 
1 335 CYS n 
1 336 THR n 
1 337 GLU n 
1 338 HIS n 
1 339 LEU n 
1 340 LEU n 
1 341 LYS n 
1 342 HIS n 
1 343 MET n 
1 344 THR n 
1 345 GLN n 
1 346 PRO n 
1 347 GLU n 
1 348 LEU n 
1 349 VAL n 
1 350 ARG n 
1 351 SER n 
1 352 PRO n 
1 353 MET n 
1 354 VAL n 
1 355 PRO n 
1 356 LEU n 
1 357 PRO n 
1 358 ALA n 
1 359 PRO n 
1 360 ARG n 
1 361 ARG n 
1 362 LEU n 
1 363 ARG n 
1 364 TRP n 
1 365 LYS n 
1 366 CYS n 
1 367 SER n 
1 368 PRO n 
1 369 GLU n 
1 370 ILE n 
1 371 GLN n 
1 372 GLY n 
1 373 HIS n 
1 374 LEU n 
1 375 ALA n 
1 376 SER n 
1 377 SER n 
1 378 ALA n 
1 379 GLU n 
1 380 LYS n 
1 381 LEU n 
1 382 GLN n 
1 383 ARG n 
1 384 ILE n 
1 385 VAL n 
1 386 LYS n 
1 387 ASN n 
1 388 LEU n 
1 389 ASP n 
1 390 PHE n 
1 391 ILE n 
1 392 VAL n 
1 393 TYR n 
1 394 LYS n 
1 395 PHE n 
1 396 ASP n 
1 397 ASN n 
1 398 TYR n 
1 399 GLY n 
1 400 LYS n 
1 401 THR n 
1 402 PHE n 
1 403 ILE n 
1 404 LYS n 
1 405 LYS n 
1 406 GLN n 
1 407 LYS n 
1 408 CYS n 
1 409 SER n 
1 410 PRO n 
1 411 ASP n 
1 412 ALA n 
1 413 PHE n 
1 414 ILE n 
1 415 GLN n 
1 416 VAL n 
1 417 ALA n 
1 418 LEU n 
1 419 GLN n 
1 420 LEU n 
1 421 ALA n 
1 422 PHE n 
1 423 TYR n 
1 424 ARG n 
1 425 LEU n 
1 426 HIS n 
1 427 ARG n 
1 428 ARG n 
1 429 LEU n 
1 430 VAL n 
1 431 PRO n 
1 432 THR n 
1 433 TYR n 
1 434 GLU n 
1 435 SER n 
1 436 ALA n 
1 437 SER n 
1 438 ILE n 
1 439 ARG n 
1 440 ARG n 
1 441 PHE n 
1 442 GLN n 
1 443 GLU n 
1 444 GLY n 
1 445 ARG n 
1 446 VAL n 
1 447 ASP n 
1 448 ASN n 
1 449 ILE n 
1 450 ARG n 
1 451 SER n 
1 452 ALA n 
1 453 THR n 
1 454 PRO n 
1 455 GLU n 
1 456 ALA n 
1 457 LEU n 
1 458 ALA n 
1 459 PHE n 
1 460 VAL n 
1 461 ARG n 
1 462 ALA n 
1 463 VAL n 
1 464 THR n 
1 465 ASP n 
1 466 HIS n 
1 467 LYS n 
1 468 ALA n 
1 469 ALA n 
1 470 VAL n 
1 471 PRO n 
1 472 ALA n 
1 473 SER n 
1 474 GLU n 
1 475 LYS n 
1 476 LEU n 
1 477 LEU n 
1 478 LEU n 
1 479 LEU n 
1 480 LYS n 
1 481 ASP n 
1 482 ALA n 
1 483 ILE n 
1 484 ARG n 
1 485 ALA n 
1 486 GLN n 
1 487 THR n 
1 488 ALA n 
1 489 TYR n 
1 490 THR n 
1 491 VAL n 
1 492 MET n 
1 493 ALA n 
1 494 ILE n 
1 495 THR n 
1 496 GLY n 
1 497 MET n 
1 498 ALA n 
1 499 ILE n 
1 500 ASP n 
1 501 ASN n 
1 502 HIS n 
1 503 LEU n 
1 504 LEU n 
1 505 ALA n 
1 506 LEU n 
1 507 ARG n 
1 508 GLU n 
1 509 LEU n 
1 510 ALA n 
1 511 ARG n 
1 512 ALA n 
1 513 MET n 
1 514 CYS n 
1 515 ALA n 
1 516 ALA n 
1 517 LEU n 
1 518 PRO n 
1 519 GLU n 
1 520 MET n 
1 521 PHE n 
1 522 MET n 
1 523 ASP n 
1 524 GLU n 
1 525 THR n 
1 526 TYR n 
1 527 LEU n 
1 528 MET n 
1 529 SER n 
1 530 ASN n 
1 531 ARG n 
1 532 PHE n 
1 533 VAL n 
1 534 LEU n 
1 535 SER n 
1 536 THR n 
1 537 SER n 
1 538 GLN n 
1 539 VAL n 
1 540 PRO n 
1 541 THR n 
1 542 THR n 
1 543 THR n 
1 544 GLU n 
1 545 MET n 
1 546 PHE n 
1 547 CYS n 
1 548 CYS n 
1 549 TYR n 
1 550 GLY n 
1 551 PRO n 
1 552 VAL n 
1 553 VAL n 
1 554 PRO n 
1 555 ASN n 
1 556 GLY n 
1 557 TYR n 
1 558 GLY n 
1 559 ALA n 
1 560 CYS n 
1 561 TYR n 
1 562 ASN n 
1 563 PRO n 
1 564 GLN n 
1 565 PRO n 
1 566 GLU n 
1 567 THR n 
1 568 ILE n 
1 569 LEU n 
1 570 PHE n 
1 571 CYS n 
1 572 ILE n 
1 573 SER n 
1 574 SER n 
1 575 PHE n 
1 576 HIS n 
1 577 SER n 
1 578 CYS n 
1 579 ALA n 
1 580 ALA n 
1 581 THR n 
1 582 SER n 
1 583 SER n 
1 584 SER n 
1 585 LYS n 
1 586 PHE n 
1 587 ALA n 
1 588 LYS n 
1 589 ALA n 
1 590 VAL n 
1 591 GLU n 
1 592 GLU n 
1 593 SER n 
1 594 LEU n 
1 595 ILE n 
1 596 ASP n 
1 597 MET n 
1 598 ARG n 
1 599 ASP n 
1 600 LEU n 
1 601 CYS n 
1 602 SER n 
1 603 LEU n 
1 604 LEU n 
1 605 PRO n 
1 606 PRO n 
1 607 THR n 
1 608 GLU n 
1 609 SER n 
1 610 LYS n 
1 611 PRO n 
1 612 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1   345 human ? CHAT ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 
469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? Plasmid ? ? ? pJ301 ? ? 
1 2 sample 'Biological sequence' 346 612 human ? CHAT ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Escherichia coli BL21(DE3)' 
469008 ? ? ? ? ? ? ? ? ? ? ? ? ? ? Plasmid ? ? ? pJ301 ? ? 
# 
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 
A1IAP non-polymer         . '1-methyl-4-[(2S)-2-naphthalen-1-yl-2-propylsulfanyl-ethyl]-4H-pyridine' CHITOTRIOSE 'C21 H25 N S'    
323.495 
ALA   'L-peptide linking' y ALANINE                                                                  ?           'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                 ?           'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                               ?           'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                          ?           'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                 ?           'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                ?           'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                          ?           'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                  ?           'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                ?           'C6 H10 N3 O2 1' 
156.162 
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 
NA    non-polymer         . 'SODIUM ION'                                                             ?           'Na 1'           
22.990  
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   ALA 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   ALA 3   3   ?   ?   ?   A . n 
A 1 4   LYS 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  PRO 19  19  19  PRO PRO A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  GLN 23  23  23  GLN GLN A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLN 30  30  30  GLN GLN A . n 
A 1 31  CYS 31  31  31  CYS CYS A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  GLU 38  38  38  GLU GLU A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  GLN 40  40  40  GLN GLN A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  LYS 43  43  43  LYS LYS A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  PHE 51  51  51  PHE PHE A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  TYR 79  79  79  TYR TYR A . n 
A 1 80  TRP 80  80  80  TRP TRP A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  MET 84  84  84  MET MET A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  ASN 88  88  88  ASN ASN A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 PHE 102 102 102 PHE PHE A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 GLN 105 105 105 GLN GLN A . n 
A 1 106 HIS 106 106 106 HIS HIS A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 GLN 113 113 113 GLN GLN A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 SER 119 119 119 SER SER A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ILE 121 121 121 ILE ILE A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 THR 138 138 138 THR THR A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 CYS 140 140 140 CYS CYS A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLN 144 144 ?   ?   ?   A . n 
A 1 145 LEU 145 145 ?   ?   ?   A . n 
A 1 146 SER 146 146 ?   ?   ?   A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 CYS 151 151 151 CYS CYS A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 TYR 156 156 156 TYR TYR A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 SER 161 161 161 SER SER A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 HIS 167 167 167 HIS HIS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 ASN 176 176 ?   ?   ?   A . n 
A 1 177 SER 177 177 ?   ?   ?   A . n 
A 1 178 SER 178 178 ?   ?   ?   A . n 
A 1 179 ILE 179 179 ?   ?   ?   A . n 
A 1 180 MET 180 180 ?   ?   ?   A . n 
A 1 181 PRO 181 181 181 PRO PRO A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 HIS 185 185 185 HIS HIS A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 CYS 190 190 190 CYS CYS A . n 
A 1 191 CYS 191 191 191 CYS CYS A . n 
A 1 192 ASN 192 192 192 ASN ASN A . n 
A 1 193 GLN 193 193 193 GLN GLN A . n 
A 1 194 PHE 194 194 194 PHE PHE A . n 
A 1 195 PHE 195 195 195 PHE PHE A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 ASP 198 198 198 ASP ASP A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 ASN 202 202 202 ASN ASN A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 PHE 212 212 212 PHE PHE A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 LYS 220 220 220 LYS LYS A . n 
A 1 221 MET 221 221 221 MET MET A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ALA 226 226 226 ALA ALA A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 ARG 228 228 228 ARG ARG A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 TRP 243 243 243 TRP TRP A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 VAL 251 251 251 VAL VAL A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 THR 255 255 255 THR THR A . n 
A 1 256 ASN 256 256 256 ASN ASN A . n 
A 1 257 ARG 257 257 257 ARG ARG A . n 
A 1 258 ASP 258 258 258 ASP ASP A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 CYS 266 266 266 CYS CYS A . n 
A 1 267 ILE 267 267 267 ILE ILE A . n 
A 1 268 CYS 268 268 268 CYS CYS A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 CYS 271 271 271 CYS CYS A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 ALA 274 274 274 ALA ALA A . n 
A 1 275 PRO 275 275 275 PRO PRO A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 THR 283 283 283 THR THR A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 ARG 285 285 285 ARG ARG A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 LEU 290 290 290 LEU LEU A . n 
A 1 291 HIS 291 291 291 HIS HIS A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 GLY 294 294 294 GLY GLY A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 SER 296 296 296 SER SER A . n 
A 1 297 LYS 297 297 297 LYS LYS A . n 
A 1 298 ASN 298 298 298 ASN ASN A . n 
A 1 299 GLY 299 299 299 GLY GLY A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 TRP 303 303 303 TRP TRP A . n 
A 1 304 TYR 304 304 304 TYR TYR A . n 
A 1 305 ASP 305 305 305 ASP ASP A . n 
A 1 306 LYS 306 306 306 LYS LYS A . n 
A 1 307 SER 307 307 307 SER SER A . n 
A 1 308 LEU 308 308 308 LEU LEU A . n 
A 1 309 GLN 309 309 309 GLN GLN A . n 
A 1 310 PHE 310 310 310 PHE PHE A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 VAL 312 312 312 VAL VAL A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 ASP 315 315 315 ASP ASP A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 THR 317 317 317 THR THR A . n 
A 1 318 CYS 318 318 318 CYS CYS A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 VAL 320 320 320 VAL VAL A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 CYS 322 322 322 CYS CYS A . n 
A 1 323 GLU 323 323 323 GLU GLU A . n 
A 1 324 HIS 324 324 324 HIS HIS A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 PRO 326 326 326 PRO PRO A . n 
A 1 327 PHE 327 327 327 PHE PHE A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 VAL 333 333 333 VAL VAL A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 CYS 335 335 335 CYS CYS A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 LYS 341 341 341 LYS LYS A . n 
A 1 342 HIS 342 342 342 HIS HIS A . n 
A 1 343 MET 343 343 343 MET MET A . n 
A 1 344 THR 344 344 344 THR THR A . n 
A 1 345 GLN 345 345 345 GLN GLN A . n 
A 1 346 PRO 346 349 ?   ?   ?   A . n 
A 1 347 GLU 347 350 ?   ?   ?   A . n 
A 1 348 LEU 348 351 ?   ?   ?   A . n 
A 1 349 VAL 349 352 ?   ?   ?   A . n 
A 1 350 ARG 350 353 ?   ?   ?   A . n 
A 1 351 SER 351 354 ?   ?   ?   A . n 
A 1 352 PRO 352 355 ?   ?   ?   A . n 
A 1 353 MET 353 356 ?   ?   ?   A . n 
A 1 354 VAL 354 357 ?   ?   ?   A . n 
A 1 355 PRO 355 358 ?   ?   ?   A . n 
A 1 356 LEU 356 359 359 LEU LEU A . n 
A 1 357 PRO 357 360 360 PRO PRO A . n 
A 1 358 ALA 358 361 361 ALA ALA A . n 
A 1 359 PRO 359 362 362 PRO PRO A . n 
A 1 360 ARG 360 363 363 ARG ARG A . n 
A 1 361 ARG 361 364 364 ARG ARG A . n 
A 1 362 LEU 362 365 365 LEU LEU A . n 
A 1 363 ARG 363 366 366 ARG ARG A . n 
A 1 364 TRP 364 367 367 TRP TRP A . n 
A 1 365 LYS 365 368 368 LYS LYS A . n 
A 1 366 CYS 366 369 369 CYS CYS A . n 
A 1 367 SER 367 370 370 SER SER A . n 
A 1 368 PRO 368 371 371 PRO PRO A . n 
A 1 369 GLU 369 372 372 GLU GLU A . n 
A 1 370 ILE 370 373 373 ILE ILE A . n 
A 1 371 GLN 371 374 374 GLN GLN A . n 
A 1 372 GLY 372 375 375 GLY GLY A . n 
A 1 373 HIS 373 376 376 HIS HIS A . n 
A 1 374 LEU 374 377 377 LEU LEU A . n 
A 1 375 ALA 375 378 378 ALA ALA A . n 
A 1 376 SER 376 379 379 SER SER A . n 
A 1 377 SER 377 380 380 SER SER A . n 
A 1 378 ALA 378 381 381 ALA ALA A . n 
A 1 379 GLU 379 382 382 GLU GLU A . n 
A 1 380 LYS 380 383 383 LYS LYS A . n 
A 1 381 LEU 381 384 384 LEU LEU A . n 
A 1 382 GLN 382 385 385 GLN GLN A . n 
A 1 383 ARG 383 386 386 ARG ARG A . n 
A 1 384 ILE 384 387 387 ILE ILE A . n 
A 1 385 VAL 385 388 388 VAL VAL A . n 
A 1 386 LYS 386 389 389 LYS LYS A . n 
A 1 387 ASN 387 390 390 ASN ASN A . n 
A 1 388 LEU 388 391 391 LEU LEU A . n 
A 1 389 ASP 389 392 392 ASP ASP A . n 
A 1 390 PHE 390 393 393 PHE PHE A . n 
A 1 391 ILE 391 394 394 ILE ILE A . n 
A 1 392 VAL 392 395 395 VAL VAL A . n 
A 1 393 TYR 393 396 396 TYR TYR A . n 
A 1 394 LYS 394 397 397 LYS LYS A . n 
A 1 395 PHE 395 398 398 PHE PHE A . n 
A 1 396 ASP 396 399 399 ASP ASP A . n 
A 1 397 ASN 397 400 400 ASN ASN A . n 
A 1 398 TYR 398 401 401 TYR TYR A . n 
A 1 399 GLY 399 402 402 GLY GLY A . n 
A 1 400 LYS 400 403 403 LYS LYS A . n 
A 1 401 THR 401 404 404 THR THR A . n 
A 1 402 PHE 402 405 405 PHE PHE A . n 
A 1 403 ILE 403 406 406 ILE ILE A . n 
A 1 404 LYS 404 407 407 LYS LYS A . n 
A 1 405 LYS 405 408 408 LYS LYS A . n 
A 1 406 GLN 406 409 409 GLN GLN A . n 
A 1 407 LYS 407 410 410 LYS LYS A . n 
A 1 408 CYS 408 411 411 CYS CYS A . n 
A 1 409 SER 409 412 412 SER SER A . n 
A 1 410 PRO 410 413 413 PRO PRO A . n 
A 1 411 ASP 411 414 414 ASP ASP A . n 
A 1 412 ALA 412 415 415 ALA ALA A . n 
A 1 413 PHE 413 416 416 PHE PHE A . n 
A 1 414 ILE 414 417 417 ILE ILE A . n 
A 1 415 GLN 415 418 418 GLN GLN A . n 
A 1 416 VAL 416 419 419 VAL VAL A . n 
A 1 417 ALA 417 420 420 ALA ALA A . n 
A 1 418 LEU 418 421 421 LEU LEU A . n 
A 1 419 GLN 419 422 422 GLN GLN A . n 
A 1 420 LEU 420 423 423 LEU LEU A . n 
A 1 421 ALA 421 424 424 ALA ALA A . n 
A 1 422 PHE 422 425 425 PHE PHE A . n 
A 1 423 TYR 423 426 426 TYR TYR A . n 
A 1 424 ARG 424 427 427 ARG ARG A . n 
A 1 425 LEU 425 428 428 LEU LEU A . n 
A 1 426 HIS 426 429 429 HIS HIS A . n 
A 1 427 ARG 427 430 430 ARG ARG A . n 
A 1 428 ARG 428 431 431 ARG ARG A . n 
A 1 429 LEU 429 432 432 LEU LEU A . n 
A 1 430 VAL 430 433 433 VAL VAL A . n 
A 1 431 PRO 431 434 434 PRO PRO A . n 
A 1 432 THR 432 435 435 THR THR A . n 
A 1 433 TYR 433 436 436 TYR TYR A . n 
A 1 434 GLU 434 437 437 GLU GLU A . n 
A 1 435 SER 435 438 438 SER SER A . n 
A 1 436 ALA 436 439 439 ALA ALA A . n 
A 1 437 SER 437 440 440 SER SER A . n 
A 1 438 ILE 438 441 441 ILE ILE A . n 
A 1 439 ARG 439 442 442 ARG ARG A . n 
A 1 440 ARG 440 443 443 ARG ARG A . n 
A 1 441 PHE 441 444 444 PHE PHE A . n 
A 1 442 GLN 442 445 445 GLN GLN A . n 
A 1 443 GLU 443 446 446 GLU GLU A . n 
A 1 444 GLY 444 447 447 GLY GLY A . n 
A 1 445 ARG 445 448 448 ARG ARG A . n 
A 1 446 VAL 446 449 449 VAL VAL A . n 
A 1 447 ASP 447 450 450 ASP ASP A . n 
A 1 448 ASN 448 451 451 ASN ASN A . n 
A 1 449 ILE 449 452 452 ILE ILE A . n 
A 1 450 ARG 450 453 453 ARG ARG A . n 
A 1 451 SER 451 454 454 SER SER A . n 
A 1 452 ALA 452 455 455 ALA ALA A . n 
A 1 453 THR 453 456 456 THR THR A . n 
A 1 454 PRO 454 457 457 PRO PRO A . n 
A 1 455 GLU 455 458 458 GLU GLU A . n 
A 1 456 ALA 456 459 459 ALA ALA A . n 
A 1 457 LEU 457 460 460 LEU LEU A . n 
A 1 458 ALA 458 461 461 ALA ALA A . n 
A 1 459 PHE 459 462 462 PHE PHE A . n 
A 1 460 VAL 460 463 463 VAL VAL A . n 
A 1 461 ARG 461 464 464 ARG ARG A . n 
A 1 462 ALA 462 465 465 ALA ALA A . n 
A 1 463 VAL 463 466 466 VAL VAL A . n 
A 1 464 THR 464 467 467 THR THR A . n 
A 1 465 ASP 465 468 468 ASP ASP A . n 
A 1 466 HIS 466 469 469 HIS HIS A . n 
A 1 467 LYS 467 470 470 LYS LYS A . n 
A 1 468 ALA 468 471 471 ALA ALA A . n 
A 1 469 ALA 469 472 472 ALA ALA A . n 
A 1 470 VAL 470 473 473 VAL VAL A . n 
A 1 471 PRO 471 474 474 PRO PRO A . n 
A 1 472 ALA 472 475 475 ALA ALA A . n 
A 1 473 SER 473 476 476 SER SER A . n 
A 1 474 GLU 474 477 477 GLU GLU A . n 
A 1 475 LYS 475 478 478 LYS LYS A . n 
A 1 476 LEU 476 479 479 LEU LEU A . n 
A 1 477 LEU 477 480 480 LEU LEU A . n 
A 1 478 LEU 478 481 481 LEU LEU A . n 
A 1 479 LEU 479 482 482 LEU LEU A . n 
A 1 480 LYS 480 483 483 LYS LYS A . n 
A 1 481 ASP 481 484 484 ASP ASP A . n 
A 1 482 ALA 482 485 485 ALA ALA A . n 
A 1 483 ILE 483 486 486 ILE ILE A . n 
A 1 484 ARG 484 487 487 ARG ARG A . n 
A 1 485 ALA 485 488 488 ALA ALA A . n 
A 1 486 GLN 486 489 489 GLN GLN A . n 
A 1 487 THR 487 490 490 THR THR A . n 
A 1 488 ALA 488 491 491 ALA ALA A . n 
A 1 489 TYR 489 492 492 TYR TYR A . n 
A 1 490 THR 490 493 493 THR THR A . n 
A 1 491 VAL 491 494 494 VAL VAL A . n 
A 1 492 MET 492 495 495 MET MET A . n 
A 1 493 ALA 493 496 496 ALA ALA A . n 
A 1 494 ILE 494 497 497 ILE ILE A . n 
A 1 495 THR 495 498 498 THR THR A . n 
A 1 496 GLY 496 499 499 GLY GLY A . n 
A 1 497 MET 497 500 500 MET MET A . n 
A 1 498 ALA 498 501 501 ALA ALA A . n 
A 1 499 ILE 499 502 502 ILE ILE A . n 
A 1 500 ASP 500 503 503 ASP ASP A . n 
A 1 501 ASN 501 504 504 ASN ASN A . n 
A 1 502 HIS 502 505 505 HIS HIS A . n 
A 1 503 LEU 503 506 506 LEU LEU A . n 
A 1 504 LEU 504 507 507 LEU LEU A . n 
A 1 505 ALA 505 508 508 ALA ALA A . n 
A 1 506 LEU 506 509 509 LEU LEU A . n 
A 1 507 ARG 507 510 510 ARG ARG A . n 
A 1 508 GLU 508 511 511 GLU GLU A . n 
A 1 509 LEU 509 512 512 LEU LEU A . n 
A 1 510 ALA 510 513 513 ALA ALA A . n 
A 1 511 ARG 511 514 514 ARG ARG A . n 
A 1 512 ALA 512 515 515 ALA ALA A . n 
A 1 513 MET 513 516 516 MET MET A . n 
A 1 514 CYS 514 517 517 CYS CYS A . n 
A 1 515 ALA 515 518 518 ALA ALA A . n 
A 1 516 ALA 516 519 519 ALA ALA A . n 
A 1 517 LEU 517 520 520 LEU LEU A . n 
A 1 518 PRO 518 521 521 PRO PRO A . n 
A 1 519 GLU 519 522 522 GLU GLU A . n 
A 1 520 MET 520 523 523 MET MET A . n 
A 1 521 PHE 521 524 524 PHE PHE A . n 
A 1 522 MET 522 525 525 MET MET A . n 
A 1 523 ASP 523 526 526 ASP ASP A . n 
A 1 524 GLU 524 527 527 GLU GLU A . n 
A 1 525 THR 525 528 528 THR THR A . n 
A 1 526 TYR 526 529 529 TYR TYR A . n 
A 1 527 LEU 527 530 530 LEU LEU A . n 
A 1 528 MET 528 531 531 MET MET A . n 
A 1 529 SER 529 532 532 SER SER A . n 
A 1 530 ASN 530 533 533 ASN ASN A . n 
A 1 531 ARG 531 534 534 ARG ARG A . n 
A 1 532 PHE 532 535 535 PHE PHE A . n 
A 1 533 VAL 533 536 536 VAL VAL A . n 
A 1 534 LEU 534 537 537 LEU LEU A . n 
A 1 535 SER 535 538 538 SER SER A . n 
A 1 536 THR 536 539 539 THR THR A . n 
A 1 537 SER 537 540 540 SER SER A . n 
A 1 538 GLN 538 541 541 GLN GLN A . n 
A 1 539 VAL 539 542 542 VAL VAL A . n 
A 1 540 PRO 540 543 543 PRO PRO A . n 
A 1 541 THR 541 544 544 THR THR A . n 
A 1 542 THR 542 545 545 THR THR A . n 
A 1 543 THR 543 546 546 THR THR A . n 
A 1 544 GLU 544 547 547 GLU GLU A . n 
A 1 545 MET 545 548 548 MET MET A . n 
A 1 546 PHE 546 549 549 PHE PHE A . n 
A 1 547 CYS 547 550 550 CYS CYS A . n 
A 1 548 CYS 548 551 551 CYS CYS A . n 
A 1 549 TYR 549 552 552 TYR TYR A . n 
A 1 550 GLY 550 553 553 GLY GLY A . n 
A 1 551 PRO 551 554 554 PRO PRO A . n 
A 1 552 VAL 552 555 555 VAL VAL A . n 
A 1 553 VAL 553 556 556 VAL VAL A . n 
A 1 554 PRO 554 557 557 PRO PRO A . n 
A 1 555 ASN 555 558 558 ASN ASN A . n 
A 1 556 GLY 556 559 559 GLY GLY A . n 
A 1 557 TYR 557 560 560 TYR TYR A . n 
A 1 558 GLY 558 561 561 GLY GLY A . n 
A 1 559 ALA 559 562 562 ALA ALA A . n 
A 1 560 CYS 560 563 563 CYS CYS A . n 
A 1 561 TYR 561 564 564 TYR TYR A . n 
A 1 562 ASN 562 565 565 ASN ASN A . n 
A 1 563 PRO 563 566 566 PRO PRO A . n 
A 1 564 GLN 564 567 567 GLN GLN A . n 
A 1 565 PRO 565 568 568 PRO PRO A . n 
A 1 566 GLU 566 569 569 GLU GLU A . n 
A 1 567 THR 567 570 570 THR THR A . n 
A 1 568 ILE 568 571 571 ILE ILE A . n 
A 1 569 LEU 569 572 572 LEU LEU A . n 
A 1 570 PHE 570 573 573 PHE PHE A . n 
A 1 571 CYS 571 574 574 CYS CYS A . n 
A 1 572 ILE 572 575 575 ILE ILE A . n 
A 1 573 SER 573 576 576 SER SER A . n 
A 1 574 SER 574 577 577 SER SER A . n 
A 1 575 PHE 575 578 578 PHE PHE A . n 
A 1 576 HIS 576 579 579 HIS HIS A . n 
A 1 577 SER 577 580 580 SER SER A . n 
A 1 578 CYS 578 581 581 CYS CYS A . n 
A 1 579 ALA 579 582 582 ALA ALA A . n 
A 1 580 ALA 580 583 583 ALA ALA A . n 
A 1 581 THR 581 584 584 THR THR A . n 
A 1 582 SER 582 585 585 SER SER A . n 
A 1 583 SER 583 586 586 SER SER A . n 
A 1 584 SER 584 587 587 SER SER A . n 
A 1 585 LYS 585 588 588 LYS LYS A . n 
A 1 586 PHE 586 589 589 PHE PHE A . n 
A 1 587 ALA 587 590 590 ALA ALA A . n 
A 1 588 LYS 588 591 591 LYS LYS A . n 
A 1 589 ALA 589 592 592 ALA ALA A . n 
A 1 590 VAL 590 593 593 VAL VAL A . n 
A 1 591 GLU 591 594 594 GLU GLU A . n 
A 1 592 GLU 592 595 595 GLU GLU A . n 
A 1 593 SER 593 596 596 SER SER A . n 
A 1 594 LEU 594 597 597 LEU LEU A . n 
A 1 595 ILE 595 598 598 ILE ILE A . n 
A 1 596 ASP 596 599 599 ASP ASP A . n 
A 1 597 MET 597 600 600 MET MET A . n 
A 1 598 ARG 598 601 601 ARG ARG A . n 
A 1 599 ASP 599 602 602 ASP ASP A . n 
A 1 600 LEU 600 603 603 LEU LEU A . n 
A 1 601 CYS 601 604 604 CYS CYS A . n 
A 1 602 SER 602 605 605 SER SER A . n 
A 1 603 LEU 603 606 606 LEU LEU A . n 
A 1 604 LEU 604 607 ?   ?   ?   A . n 
A 1 605 PRO 605 608 ?   ?   ?   A . n 
A 1 606 PRO 606 609 ?   ?   ?   A . n 
A 1 607 THR 607 610 ?   ?   ?   A . n 
A 1 608 GLU 608 611 ?   ?   ?   A . n 
A 1 609 SER 609 612 ?   ?   ?   A . n 
A 1 610 LYS 610 613 ?   ?   ?   A . n 
A 1 611 PRO 611 614 ?   ?   ?   A . n 
A 1 612 LEU 612 615 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IAP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IAP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1IAP 1   701  1   A1IAP CTO A . 
C 3 NA    1   702  1   NA    NA  A . 
D 4 HOH   1   801  349 HOH   HOH A . 
D 4 HOH   2   802  17  HOH   HOH A . 
D 4 HOH   3   803  424 HOH   HOH A . 
D 4 HOH   4   804  426 HOH   HOH A . 
D 4 HOH   5   805  389 HOH   HOH A . 
D 4 HOH   6   806  431 HOH   HOH A . 
D 4 HOH   7   807  385 HOH   HOH A . 
D 4 HOH   8   808  282 HOH   HOH A . 
D 4 HOH   9   809  451 HOH   HOH A . 
D 4 HOH   10  810  235 HOH   HOH A . 
D 4 HOH   11  811  60  HOH   HOH A . 
D 4 HOH   12  812  230 HOH   HOH A . 
D 4 HOH   13  813  37  HOH   HOH A . 
D 4 HOH   14  814  175 HOH   HOH A . 
D 4 HOH   15  815  416 HOH   HOH A . 
D 4 HOH   16  816  215 HOH   HOH A . 
D 4 HOH   17  817  91  HOH   HOH A . 
D 4 HOH   18  818  176 HOH   HOH A . 
D 4 HOH   19  819  333 HOH   HOH A . 
D 4 HOH   20  820  224 HOH   HOH A . 
D 4 HOH   21  821  387 HOH   HOH A . 
D 4 HOH   22  822  307 HOH   HOH A . 
D 4 HOH   23  823  34  HOH   HOH A . 
D 4 HOH   24  824  447 HOH   HOH A . 
D 4 HOH   25  825  405 HOH   HOH A . 
D 4 HOH   26  826  46  HOH   HOH A . 
D 4 HOH   27  827  263 HOH   HOH A . 
D 4 HOH   28  828  264 HOH   HOH A . 
D 4 HOH   29  829  251 HOH   HOH A . 
D 4 HOH   30  830  142 HOH   HOH A . 
D 4 HOH   31  831  185 HOH   HOH A . 
D 4 HOH   32  832  137 HOH   HOH A . 
D 4 HOH   33  833  206 HOH   HOH A . 
D 4 HOH   34  834  166 HOH   HOH A . 
D 4 HOH   35  835  273 HOH   HOH A . 
D 4 HOH   36  836  73  HOH   HOH A . 
D 4 HOH   37  837  134 HOH   HOH A . 
D 4 HOH   38  838  346 HOH   HOH A . 
D 4 HOH   39  839  38  HOH   HOH A . 
D 4 HOH   40  840  362 HOH   HOH A . 
D 4 HOH   41  841  420 HOH   HOH A . 
D 4 HOH   42  842  159 HOH   HOH A . 
D 4 HOH   43  843  233 HOH   HOH A . 
D 4 HOH   44  844  298 HOH   HOH A . 
D 4 HOH   45  845  271 HOH   HOH A . 
D 4 HOH   46  846  12  HOH   HOH A . 
D 4 HOH   47  847  432 HOH   HOH A . 
D 4 HOH   48  848  406 HOH   HOH A . 
D 4 HOH   49  849  41  HOH   HOH A . 
D 4 HOH   50  850  146 HOH   HOH A . 
D 4 HOH   51  851  425 HOH   HOH A . 
D 4 HOH   52  852  153 HOH   HOH A . 
D 4 HOH   53  853  403 HOH   HOH A . 
D 4 HOH   54  854  439 HOH   HOH A . 
D 4 HOH   55  855  24  HOH   HOH A . 
D 4 HOH   56  856  21  HOH   HOH A . 
D 4 HOH   57  857  108 HOH   HOH A . 
D 4 HOH   58  858  35  HOH   HOH A . 
D 4 HOH   59  859  147 HOH   HOH A . 
D 4 HOH   60  860  92  HOH   HOH A . 
D 4 HOH   61  861  256 HOH   HOH A . 
D 4 HOH   62  862  286 HOH   HOH A . 
D 4 HOH   63  863  71  HOH   HOH A . 
D 4 HOH   64  864  247 HOH   HOH A . 
D 4 HOH   65  865  303 HOH   HOH A . 
D 4 HOH   66  866  221 HOH   HOH A . 
D 4 HOH   67  867  278 HOH   HOH A . 
D 4 HOH   68  868  415 HOH   HOH A . 
D 4 HOH   69  869  65  HOH   HOH A . 
D 4 HOH   70  870  63  HOH   HOH A . 
D 4 HOH   71  871  59  HOH   HOH A . 
D 4 HOH   72  872  450 HOH   HOH A . 
D 4 HOH   73  873  243 HOH   HOH A . 
D 4 HOH   74  874  121 HOH   HOH A . 
D 4 HOH   75  875  326 HOH   HOH A . 
D 4 HOH   76  876  408 HOH   HOH A . 
D 4 HOH   77  877  115 HOH   HOH A . 
D 4 HOH   78  878  79  HOH   HOH A . 
D 4 HOH   79  879  332 HOH   HOH A . 
D 4 HOH   80  880  419 HOH   HOH A . 
D 4 HOH   81  881  209 HOH   HOH A . 
D 4 HOH   82  882  259 HOH   HOH A . 
D 4 HOH   83  883  129 HOH   HOH A . 
D 4 HOH   84  884  414 HOH   HOH A . 
D 4 HOH   85  885  89  HOH   HOH A . 
D 4 HOH   86  886  94  HOH   HOH A . 
D 4 HOH   87  887  144 HOH   HOH A . 
D 4 HOH   88  888  331 HOH   HOH A . 
D 4 HOH   89  889  113 HOH   HOH A . 
D 4 HOH   90  890  61  HOH   HOH A . 
D 4 HOH   91  891  138 HOH   HOH A . 
D 4 HOH   92  892  125 HOH   HOH A . 
D 4 HOH   93  893  136 HOH   HOH A . 
D 4 HOH   94  894  266 HOH   HOH A . 
D 4 HOH   95  895  58  HOH   HOH A . 
D 4 HOH   96  896  309 HOH   HOH A . 
D 4 HOH   97  897  161 HOH   HOH A . 
D 4 HOH   98  898  15  HOH   HOH A . 
D 4 HOH   99  899  398 HOH   HOH A . 
D 4 HOH   100 900  6   HOH   HOH A . 
D 4 HOH   101 901  148 HOH   HOH A . 
D 4 HOH   102 902  109 HOH   HOH A . 
D 4 HOH   103 903  75  HOH   HOH A . 
D 4 HOH   104 904  19  HOH   HOH A . 
D 4 HOH   105 905  25  HOH   HOH A . 
D 4 HOH   106 906  239 HOH   HOH A . 
D 4 HOH   107 907  255 HOH   HOH A . 
D 4 HOH   108 908  84  HOH   HOH A . 
D 4 HOH   109 909  173 HOH   HOH A . 
D 4 HOH   110 910  31  HOH   HOH A . 
D 4 HOH   111 911  191 HOH   HOH A . 
D 4 HOH   112 912  238 HOH   HOH A . 
D 4 HOH   113 913  103 HOH   HOH A . 
D 4 HOH   114 914  28  HOH   HOH A . 
D 4 HOH   115 915  227 HOH   HOH A . 
D 4 HOH   116 916  437 HOH   HOH A . 
D 4 HOH   117 917  169 HOH   HOH A . 
D 4 HOH   118 918  130 HOH   HOH A . 
D 4 HOH   119 919  141 HOH   HOH A . 
D 4 HOH   120 920  178 HOH   HOH A . 
D 4 HOH   121 921  413 HOH   HOH A . 
D 4 HOH   122 922  291 HOH   HOH A . 
D 4 HOH   123 923  23  HOH   HOH A . 
D 4 HOH   124 924  293 HOH   HOH A . 
D 4 HOH   125 925  276 HOH   HOH A . 
D 4 HOH   126 926  20  HOH   HOH A . 
D 4 HOH   127 927  345 HOH   HOH A . 
D 4 HOH   128 928  219 HOH   HOH A . 
D 4 HOH   129 929  202 HOH   HOH A . 
D 4 HOH   130 930  128 HOH   HOH A . 
D 4 HOH   131 931  88  HOH   HOH A . 
D 4 HOH   132 932  223 HOH   HOH A . 
D 4 HOH   133 933  123 HOH   HOH A . 
D 4 HOH   134 934  434 HOH   HOH A . 
D 4 HOH   135 935  67  HOH   HOH A . 
D 4 HOH   136 936  145 HOH   HOH A . 
D 4 HOH   137 937  78  HOH   HOH A . 
D 4 HOH   138 938  33  HOH   HOH A . 
D 4 HOH   139 939  272 HOH   HOH A . 
D 4 HOH   140 940  199 HOH   HOH A . 
D 4 HOH   141 941  32  HOH   HOH A . 
D 4 HOH   142 942  217 HOH   HOH A . 
D 4 HOH   143 943  234 HOH   HOH A . 
D 4 HOH   144 944  435 HOH   HOH A . 
D 4 HOH   145 945  302 HOH   HOH A . 
D 4 HOH   146 946  53  HOH   HOH A . 
D 4 HOH   147 947  43  HOH   HOH A . 
D 4 HOH   148 948  189 HOH   HOH A . 
D 4 HOH   149 949  410 HOH   HOH A . 
D 4 HOH   150 950  76  HOH   HOH A . 
D 4 HOH   151 951  312 HOH   HOH A . 
D 4 HOH   152 952  26  HOH   HOH A . 
D 4 HOH   153 953  56  HOH   HOH A . 
D 4 HOH   154 954  388 HOH   HOH A . 
D 4 HOH   155 955  18  HOH   HOH A . 
D 4 HOH   156 956  14  HOH   HOH A . 
D 4 HOH   157 957  400 HOH   HOH A . 
D 4 HOH   158 958  124 HOH   HOH A . 
D 4 HOH   159 959  390 HOH   HOH A . 
D 4 HOH   160 960  187 HOH   HOH A . 
D 4 HOH   161 961  213 HOH   HOH A . 
D 4 HOH   162 962  216 HOH   HOH A . 
D 4 HOH   163 963  422 HOH   HOH A . 
D 4 HOH   164 964  436 HOH   HOH A . 
D 4 HOH   165 965  7   HOH   HOH A . 
D 4 HOH   166 966  98  HOH   HOH A . 
D 4 HOH   167 967  10  HOH   HOH A . 
D 4 HOH   168 968  260 HOH   HOH A . 
D 4 HOH   169 969  336 HOH   HOH A . 
D 4 HOH   170 970  192 HOH   HOH A . 
D 4 HOH   171 971  177 HOH   HOH A . 
D 4 HOH   172 972  40  HOH   HOH A . 
D 4 HOH   173 973  101 HOH   HOH A . 
D 4 HOH   174 974  49  HOH   HOH A . 
D 4 HOH   175 975  62  HOH   HOH A . 
D 4 HOH   176 976  444 HOH   HOH A . 
D 4 HOH   177 977  104 HOH   HOH A . 
D 4 HOH   178 978  36  HOH   HOH A . 
D 4 HOH   179 979  229 HOH   HOH A . 
D 4 HOH   180 980  325 HOH   HOH A . 
D 4 HOH   181 981  164 HOH   HOH A . 
D 4 HOH   182 982  275 HOH   HOH A . 
D 4 HOH   183 983  155 HOH   HOH A . 
D 4 HOH   184 984  22  HOH   HOH A . 
D 4 HOH   185 985  111 HOH   HOH A . 
D 4 HOH   186 986  300 HOH   HOH A . 
D 4 HOH   187 987  401 HOH   HOH A . 
D 4 HOH   188 988  68  HOH   HOH A . 
D 4 HOH   189 989  9   HOH   HOH A . 
D 4 HOH   190 990  131 HOH   HOH A . 
D 4 HOH   191 991  366 HOH   HOH A . 
D 4 HOH   192 992  154 HOH   HOH A . 
D 4 HOH   193 993  39  HOH   HOH A . 
D 4 HOH   194 994  301 HOH   HOH A . 
D 4 HOH   195 995  203 HOH   HOH A . 
D 4 HOH   196 996  116 HOH   HOH A . 
D 4 HOH   197 997  54  HOH   HOH A . 
D 4 HOH   198 998  117 HOH   HOH A . 
D 4 HOH   199 999  241 HOH   HOH A . 
D 4 HOH   200 1000 196 HOH   HOH A . 
D 4 HOH   201 1001 66  HOH   HOH A . 
D 4 HOH   202 1002 179 HOH   HOH A . 
D 4 HOH   203 1003 52  HOH   HOH A . 
D 4 HOH   204 1004 423 HOH   HOH A . 
D 4 HOH   205 1005 281 HOH   HOH A . 
D 4 HOH   206 1006 74  HOH   HOH A . 
D 4 HOH   207 1007 139 HOH   HOH A . 
D 4 HOH   208 1008 207 HOH   HOH A . 
D 4 HOH   209 1009 338 HOH   HOH A . 
D 4 HOH   210 1010 44  HOH   HOH A . 
D 4 HOH   211 1011 220 HOH   HOH A . 
D 4 HOH   212 1012 225 HOH   HOH A . 
D 4 HOH   213 1013 265 HOH   HOH A . 
D 4 HOH   214 1014 42  HOH   HOH A . 
D 4 HOH   215 1015 82  HOH   HOH A . 
D 4 HOH   216 1016 418 HOH   HOH A . 
D 4 HOH   217 1017 64  HOH   HOH A . 
D 4 HOH   218 1018 162 HOH   HOH A . 
D 4 HOH   219 1019 262 HOH   HOH A . 
D 4 HOH   220 1020 163 HOH   HOH A . 
D 4 HOH   221 1021 170 HOH   HOH A . 
D 4 HOH   222 1022 391 HOH   HOH A . 
D 4 HOH   223 1023 252 HOH   HOH A . 
D 4 HOH   224 1024 172 HOH   HOH A . 
D 4 HOH   225 1025 386 HOH   HOH A . 
D 4 HOH   226 1026 181 HOH   HOH A . 
D 4 HOH   227 1027 204 HOH   HOH A . 
D 4 HOH   228 1028 8   HOH   HOH A . 
D 4 HOH   229 1029 16  HOH   HOH A . 
D 4 HOH   230 1030 193 HOH   HOH A . 
D 4 HOH   231 1031 114 HOH   HOH A . 
D 4 HOH   232 1032 280 HOH   HOH A . 
D 4 HOH   233 1033 308 HOH   HOH A . 
D 4 HOH   234 1034 232 HOH   HOH A . 
D 4 HOH   235 1035 359 HOH   HOH A . 
D 4 HOH   236 1036 208 HOH   HOH A . 
D 4 HOH   237 1037 269 HOH   HOH A . 
D 4 HOH   238 1038 226 HOH   HOH A . 
D 4 HOH   239 1039 244 HOH   HOH A . 
D 4 HOH   240 1040 356 HOH   HOH A . 
D 4 HOH   241 1041 190 HOH   HOH A . 
D 4 HOH   242 1042 253 HOH   HOH A . 
D 4 HOH   243 1043 70  HOH   HOH A . 
D 4 HOH   244 1044 90  HOH   HOH A . 
D 4 HOH   245 1045 143 HOH   HOH A . 
D 4 HOH   246 1046 341 HOH   HOH A . 
D 4 HOH   247 1047 156 HOH   HOH A . 
D 4 HOH   248 1048 417 HOH   HOH A . 
D 4 HOH   249 1049 314 HOH   HOH A . 
D 4 HOH   250 1050 72  HOH   HOH A . 
D 4 HOH   251 1051 122 HOH   HOH A . 
D 4 HOH   252 1052 27  HOH   HOH A . 
D 4 HOH   253 1053 313 HOH   HOH A . 
D 4 HOH   254 1054 45  HOH   HOH A . 
D 4 HOH   255 1055 95  HOH   HOH A . 
D 4 HOH   256 1056 429 HOH   HOH A . 
D 4 HOH   257 1057 399 HOH   HOH A . 
D 4 HOH   258 1058 394 HOH   HOH A . 
D 4 HOH   259 1059 57  HOH   HOH A . 
D 4 HOH   260 1060 198 HOH   HOH A . 
D 4 HOH   261 1061 107 HOH   HOH A . 
D 4 HOH   262 1062 183 HOH   HOH A . 
D 4 HOH   263 1063 165 HOH   HOH A . 
D 4 HOH   264 1064 311 HOH   HOH A . 
D 4 HOH   265 1065 393 HOH   HOH A . 
D 4 HOH   266 1066 86  HOH   HOH A . 
D 4 HOH   267 1067 306 HOH   HOH A . 
D 4 HOH   268 1068 288 HOH   HOH A . 
D 4 HOH   269 1069 99  HOH   HOH A . 
D 4 HOH   270 1070 5   HOH   HOH A . 
D 4 HOH   271 1071 112 HOH   HOH A . 
D 4 HOH   272 1072 337 HOH   HOH A . 
D 4 HOH   273 1073 140 HOH   HOH A . 
D 4 HOH   274 1074 30  HOH   HOH A . 
D 4 HOH   275 1075 249 HOH   HOH A . 
D 4 HOH   276 1076 51  HOH   HOH A . 
D 4 HOH   277 1077 151 HOH   HOH A . 
D 4 HOH   278 1078 4   HOH   HOH A . 
D 4 HOH   279 1079 409 HOH   HOH A . 
D 4 HOH   280 1080 205 HOH   HOH A . 
D 4 HOH   281 1081 344 HOH   HOH A . 
D 4 HOH   282 1082 277 HOH   HOH A . 
D 4 HOH   283 1083 421 HOH   HOH A . 
D 4 HOH   284 1084 102 HOH   HOH A . 
D 4 HOH   285 1085 85  HOH   HOH A . 
D 4 HOH   286 1086 214 HOH   HOH A . 
D 4 HOH   287 1087 210 HOH   HOH A . 
D 4 HOH   288 1088 258 HOH   HOH A . 
D 4 HOH   289 1089 100 HOH   HOH A . 
D 4 HOH   290 1090 428 HOH   HOH A . 
D 4 HOH   291 1091 340 HOH   HOH A . 
D 4 HOH   292 1092 195 HOH   HOH A . 
D 4 HOH   293 1093 237 HOH   HOH A . 
D 4 HOH   294 1094 11  HOH   HOH A . 
D 4 HOH   295 1095 361 HOH   HOH A . 
D 4 HOH   296 1096 351 HOH   HOH A . 
D 4 HOH   297 1097 150 HOH   HOH A . 
D 4 HOH   298 1098 1   HOH   HOH A . 
D 4 HOH   299 1099 50  HOH   HOH A . 
D 4 HOH   300 1100 13  HOH   HOH A . 
D 4 HOH   301 1101 110 HOH   HOH A . 
D 4 HOH   302 1102 348 HOH   HOH A . 
D 4 HOH   303 1103 48  HOH   HOH A . 
D 4 HOH   304 1104 441 HOH   HOH A . 
D 4 HOH   305 1105 106 HOH   HOH A . 
D 4 HOH   306 1106 158 HOH   HOH A . 
D 4 HOH   307 1107 305 HOH   HOH A . 
D 4 HOH   308 1108 310 HOH   HOH A . 
D 4 HOH   309 1109 318 HOH   HOH A . 
D 4 HOH   310 1110 171 HOH   HOH A . 
D 4 HOH   311 1111 442 HOH   HOH A . 
D 4 HOH   312 1112 47  HOH   HOH A . 
D 4 HOH   313 1113 320 HOH   HOH A . 
D 4 HOH   314 1114 440 HOH   HOH A . 
D 4 HOH   315 1115 160 HOH   HOH A . 
D 4 HOH   316 1116 283 HOH   HOH A . 
D 4 HOH   317 1117 254 HOH   HOH A . 
D 4 HOH   318 1118 120 HOH   HOH A . 
D 4 HOH   319 1119 358 HOH   HOH A . 
D 4 HOH   320 1120 404 HOH   HOH A . 
D 4 HOH   321 1121 135 HOH   HOH A . 
D 4 HOH   322 1122 188 HOH   HOH A . 
D 4 HOH   323 1123 322 HOH   HOH A . 
D 4 HOH   324 1124 354 HOH   HOH A . 
D 4 HOH   325 1125 411 HOH   HOH A . 
D 4 HOH   326 1126 296 HOH   HOH A . 
D 4 HOH   327 1127 287 HOH   HOH A . 
D 4 HOH   328 1128 407 HOH   HOH A . 
D 4 HOH   329 1129 449 HOH   HOH A . 
D 4 HOH   330 1130 2   HOH   HOH A . 
D 4 HOH   331 1131 380 HOH   HOH A . 
D 4 HOH   332 1132 317 HOH   HOH A . 
D 4 HOH   333 1133 197 HOH   HOH A . 
D 4 HOH   334 1134 97  HOH   HOH A . 
D 4 HOH   335 1135 367 HOH   HOH A . 
D 4 HOH   336 1136 295 HOH   HOH A . 
D 4 HOH   337 1137 257 HOH   HOH A . 
D 4 HOH   338 1138 315 HOH   HOH A . 
D 4 HOH   339 1139 343 HOH   HOH A . 
D 4 HOH   340 1140 433 HOH   HOH A . 
D 4 HOH   341 1141 118 HOH   HOH A . 
D 4 HOH   342 1142 289 HOH   HOH A . 
D 4 HOH   343 1143 186 HOH   HOH A . 
D 4 HOH   344 1144 55  HOH   HOH A . 
D 4 HOH   345 1145 294 HOH   HOH A . 
D 4 HOH   346 1146 373 HOH   HOH A . 
D 4 HOH   347 1147 149 HOH   HOH A . 
D 4 HOH   348 1148 126 HOH   HOH A . 
D 4 HOH   349 1149 218 HOH   HOH A . 
D 4 HOH   350 1150 430 HOH   HOH A . 
D 4 HOH   351 1151 375 HOH   HOH A . 
D 4 HOH   352 1152 77  HOH   HOH A . 
D 4 HOH   353 1153 83  HOH   HOH A . 
D 4 HOH   354 1154 297 HOH   HOH A . 
D 4 HOH   355 1155 167 HOH   HOH A . 
D 4 HOH   356 1156 285 HOH   HOH A . 
D 4 HOH   357 1157 152 HOH   HOH A . 
D 4 HOH   358 1158 222 HOH   HOH A . 
D 4 HOH   359 1159 329 HOH   HOH A . 
D 4 HOH   360 1160 250 HOH   HOH A . 
D 4 HOH   361 1161 353 HOH   HOH A . 
D 4 HOH   362 1162 245 HOH   HOH A . 
D 4 HOH   363 1163 330 HOH   HOH A . 
D 4 HOH   364 1164 274 HOH   HOH A . 
D 4 HOH   365 1165 438 HOH   HOH A . 
D 4 HOH   366 1166 335 HOH   HOH A . 
D 4 HOH   367 1167 355 HOH   HOH A . 
D 4 HOH   368 1168 184 HOH   HOH A . 
D 4 HOH   369 1169 279 HOH   HOH A . 
D 4 HOH   370 1170 180 HOH   HOH A . 
D 4 HOH   371 1171 231 HOH   HOH A . 
D 4 HOH   372 1172 377 HOH   HOH A . 
D 4 HOH   373 1173 396 HOH   HOH A . 
D 4 HOH   374 1174 360 HOH   HOH A . 
D 4 HOH   375 1175 446 HOH   HOH A . 
D 4 HOH   376 1176 157 HOH   HOH A . 
D 4 HOH   377 1177 327 HOH   HOH A . 
D 4 HOH   378 1178 324 HOH   HOH A . 
D 4 HOH   379 1179 350 HOH   HOH A . 
D 4 HOH   380 1180 369 HOH   HOH A . 
D 4 HOH   381 1181 267 HOH   HOH A . 
D 4 HOH   382 1182 402 HOH   HOH A . 
D 4 HOH   383 1183 29  HOH   HOH A . 
D 4 HOH   384 1184 371 HOH   HOH A . 
D 4 HOH   385 1185 392 HOH   HOH A . 
D 4 HOH   386 1186 261 HOH   HOH A . 
D 4 HOH   387 1187 379 HOH   HOH A . 
D 4 HOH   388 1188 383 HOH   HOH A . 
D 4 HOH   389 1189 321 HOH   HOH A . 
D 4 HOH   390 1190 284 HOH   HOH A . 
D 4 HOH   391 1191 133 HOH   HOH A . 
D 4 HOH   392 1192 382 HOH   HOH A . 
D 4 HOH   393 1193 246 HOH   HOH A . 
D 4 HOH   394 1194 236 HOH   HOH A . 
D 4 HOH   395 1195 376 HOH   HOH A . 
D 4 HOH   396 1196 319 HOH   HOH A . 
D 4 HOH   397 1197 381 HOH   HOH A . 
D 4 HOH   398 1198 378 HOH   HOH A . 
D 4 HOH   399 1199 201 HOH   HOH A . 
D 4 HOH   400 1200 292 HOH   HOH A . 
D 4 HOH   401 1201 374 HOH   HOH A . 
D 4 HOH   402 1202 268 HOH   HOH A . 
D 4 HOH   403 1203 69  HOH   HOH A . 
D 4 HOH   404 1204 368 HOH   HOH A . 
D 4 HOH   405 1205 81  HOH   HOH A . 
D 4 HOH   406 1206 316 HOH   HOH A . 
D 4 HOH   407 1207 200 HOH   HOH A . 
D 4 HOH   408 1208 328 HOH   HOH A . 
D 4 HOH   409 1209 119 HOH   HOH A . 
D 4 HOH   410 1210 194 HOH   HOH A . 
D 4 HOH   411 1211 412 HOH   HOH A . 
D 4 HOH   412 1212 105 HOH   HOH A . 
D 4 HOH   413 1213 370 HOH   HOH A . 
D 4 HOH   414 1214 347 HOH   HOH A . 
D 4 HOH   415 1215 357 HOH   HOH A . 
D 4 HOH   416 1216 174 HOH   HOH A . 
D 4 HOH   417 1217 168 HOH   HOH A . 
D 4 HOH   418 1218 290 HOH   HOH A . 
D 4 HOH   419 1219 132 HOH   HOH A . 
D 4 HOH   420 1220 395 HOH   HOH A . 
D 4 HOH   421 1221 93  HOH   HOH A . 
D 4 HOH   422 1222 397 HOH   HOH A . 
D 4 HOH   423 1223 372 HOH   HOH A . 
D 4 HOH   424 1224 299 HOH   HOH A . 
D 4 HOH   425 1225 363 HOH   HOH A . 
D 4 HOH   426 1226 248 HOH   HOH A . 
D 4 HOH   427 1227 80  HOH   HOH A . 
D 4 HOH   428 1228 240 HOH   HOH A . 
D 4 HOH   429 1229 228 HOH   HOH A . 
D 4 HOH   430 1230 342 HOH   HOH A . 
D 4 HOH   431 1231 339 HOH   HOH A . 
D 4 HOH   432 1232 211 HOH   HOH A . 
D 4 HOH   433 1233 270 HOH   HOH A . 
D 4 HOH   434 1234 304 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 10  ? CG  ? A GLU 10  CG  
2  1 Y 1 A GLU 10  ? CD  ? A GLU 10  CD  
3  1 Y 1 A GLU 10  ? OE1 ? A GLU 10  OE1 
4  1 Y 1 A GLU 10  ? OE2 ? A GLU 10  OE2 
5  1 Y 1 A GLN 175 ? CG  ? A GLN 175 CG  
6  1 Y 1 A GLN 175 ? CD  ? A GLN 175 CD  
7  1 Y 1 A GLN 175 ? OE1 ? A GLN 175 OE1 
8  1 Y 1 A GLN 175 ? NE2 ? A GLN 175 NE2 
9  1 Y 1 A GLU 182 ? CG  ? A GLU 182 CG  
10 1 Y 1 A GLU 182 ? CD  ? A GLU 182 CD  
11 1 Y 1 A GLU 182 ? OE1 ? A GLU 182 OE1 
12 1 Y 1 A GLU 182 ? OE2 ? A GLU 182 OE2 
13 1 Y 1 A ILE 201 ? CG1 ? A ILE 201 CG1 
14 1 Y 1 A ILE 201 ? CG2 ? A ILE 201 CG2 
15 1 Y 1 A ILE 201 ? CD1 ? A ILE 201 CD1 
16 1 Y 1 A ASN 202 ? CG  ? A ASN 202 CG  
17 1 Y 1 A ASN 202 ? OD1 ? A ASN 202 OD1 
18 1 Y 1 A ASN 202 ? ND2 ? A ASN 202 ND2 
19 1 Y 1 A ARG 204 ? CG  ? A ARG 204 CG  
20 1 Y 1 A ARG 204 ? CD  ? A ARG 204 CD  
21 1 Y 1 A ARG 204 ? NE  ? A ARG 204 NE  
22 1 Y 1 A ARG 204 ? CZ  ? A ARG 204 CZ  
23 1 Y 1 A ARG 204 ? NH1 ? A ARG 204 NH1 
24 1 Y 1 A ARG 204 ? NH2 ? A ARG 204 NH2 
25 1 Y 1 A GLU 279 ? CD  ? A GLU 279 CD  
26 1 Y 1 A GLU 279 ? OE1 ? A GLU 279 OE1 
27 1 Y 1 A GLU 279 ? OE2 ? A GLU 279 OE2 
28 1 Y 1 A GLN 345 ? CG  ? A GLN 345 CG  
29 1 Y 1 A GLN 345 ? CD  ? A GLN 345 CD  
30 1 Y 1 A GLN 345 ? OE1 ? A GLN 345 OE1 
31 1 Y 1 A GLN 345 ? NE2 ? A GLN 345 NE2 
32 1 Y 1 A LYS 470 ? CD  ? A LYS 467 CD  
33 1 Y 1 A LYS 470 ? CE  ? A LYS 467 CE  
34 1 Y 1 A LYS 470 ? NZ  ? A LYS 467 NZ  
# 
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_5207 1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .         2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .         3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .         4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .         5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F84 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.660 
_cell.length_a_esd                 ? 
_cell.length_b                     76.766 
_cell.length_b_esd                 ? 
_cell.length_c                     164.324 
_cell.length_c_esd                 ? 
_cell.volume                       689508.361 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9F84 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9F84 
_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             2.53 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.4 
_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              ? 
_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 Tris-HCl pH 8.5
10 %(w/v) PEG3350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER 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         2023-11-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9762 
_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                        'MAX IV BEAMLINE BioMAX' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9762 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BioMAX 
_diffrn_source.pdbx_synchrotron_site       'MAX IV' 
# 
_reflns.B_iso_Wilson_estimate                          25.05 
_reflns.entry_id                                       9F84 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.9 
_reflns.d_resolution_low                               82.16 
_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                                     55320 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.3 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.9 
_reflns_shell.d_res_low                                     1.94 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3496 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.719 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_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                               31.55 
_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                                 9F84 
_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                            1.90 
_refine.ls_d_res_low                             34.78 
_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                     55230 
_refine.ls_number_reflns_R_free                  1135 
_refine.ls_number_reflns_R_work                  54095 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.69 
_refine.ls_percent_reflns_R_free                 2.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1686 
_refine.ls_R_factor_R_free                       0.1970 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1680 
_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                          1.34 
_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          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 20.1016 
_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                            0.1770 
_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                       1.90 
_refine_hist.d_res_low                        34.78 
_refine_hist.number_atoms_solvent             434 
_refine_hist.number_atoms_total               4946 
_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        4488 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_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' ? 0.0092  ? 4702 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9103  ? 6387 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0603  ? 718  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0091  ? 827  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.9086 ? 1738 ? f_dihedral_angle_d ? ? 
# 
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' 1.90 1.99  . . 144 6626 99.25 . . . . 0.2300 . . . . . . . . . . . 0.2962 
'X-RAY DIFFRACTION' 1.99 2.09  . . 137 6669 99.44 . . . . 0.1844 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.09 2.22  . . 135 6660 99.52 . . . . 0.1607 . . . . . . . . . . . 0.2006 
'X-RAY DIFFRACTION' 2.22 2.39  . . 155 6691 99.69 . . . . 0.1582 . . . . . . . . . . . 0.1958 
'X-RAY DIFFRACTION' 2.39 2.63  . . 130 6736 99.77 . . . . 0.1647 . . . . . . . . . . . 0.2119 
'X-RAY DIFFRACTION' 2.63 3.02  . . 145 6771 99.94 . . . . 0.1788 . . . . . . . . . . . 0.2030 
'X-RAY DIFFRACTION' 3.02 3.80  . . 140 6845 99.97 . . . . 0.1673 . . . . . . . . . . . 0.2136 
'X-RAY DIFFRACTION' 3.80 34.78 . . 149 7097 99.90 . . . . 0.1566 . . . . . . . . . . . 0.1609 
# 
_struct.entry_id                     9F84 
_struct.title                        
;Structure of Choline O-acetyltransferase in complex with 1-Methyl-4-[2-(1-naphthyl)-2-(propylthio)ethyl]pyridinium at 1.9 Angstrom resolution
;
_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        9F84 
_struct_keywords.text            'ChAT, complex, inhibitor, reversible, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP CLAT_HUMAN P28329 ? 1 
;AAKTPSSEESGLPKLPVPPLQQTLATYLQCMRHLVSEEQFRKSQAIVQQFGAPGGLGETLQQKLLERQEKTANWVSEYWL
NDMYLNNRLALPVNSSPAVIFARQHFPGTDDQLRFAASLISGVLSYKALLDSHSIPTDCAKGQLSGQPLCMKQYYGLFSS
YRLPGHTQDTLVAQNSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRS
EWAEARTVLVKDSTNRDSLDMIERCICLVCLDAPGGVELSDTHRALQLLHGGGYSKNGANRWYDKSLQFVVGRDGTCGVV
CEHSPFDGIVLVQCTEHLLKHVTQ
;
120 
2 UNP CLAT_HUMAN P28329 ? 1 
;LPAPRRLRWKCSPEIQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDAFIQVALQLAFYRLHRRLVPTYES
ASIRRFQEGRVDNIRSATPEALAFVRAVTDHKAAVPASEKLLLLKDAIRAQTAYTVMAITGMAIDNHLLALRELARAMCK
ELPEMFMDETYLMSNRFVLSTSQVPTTTEMFCCYGPVVPNGYGACYNPQPETILFCISSFHSCKETSSSKFAKAVEESLI
DMRDLCSLLPPTESKPL
;
477 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9F84 A 2   ? 345 ? P28329 120 ? 463 ? 2   345 
2 2 9F84 A 356 ? 612 ? P28329 477 ? 733 ? 359 615 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9F84 ALA A 1   ? UNP P28329 ?   ?   'expression tag'      1   1  
1 9F84 ALA A 225 ? UNP P28329 GLU 343 'engineered mutation' 225 2  
1 9F84 ALA A 226 ? UNP P28329 ASP 344 'engineered mutation' 226 3  
1 9F84 ALA A 227 ? UNP P28329 GLU 345 'engineered mutation' 227 4  
1 9F84 MET A 343 ? UNP P28329 VAL 461 conflict              343 5  
1 9F84 PRO A 346 ? UNP P28329 ?   ?   linker                349 6  
1 9F84 GLU A 347 ? UNP P28329 ?   ?   linker                350 7  
1 9F84 LEU A 348 ? UNP P28329 ?   ?   linker                351 8  
1 9F84 VAL A 349 ? UNP P28329 ?   ?   linker                352 9  
1 9F84 ARG A 350 ? UNP P28329 ?   ?   linker                353 10 
1 9F84 SER A 351 ? UNP P28329 ?   ?   linker                354 11 
1 9F84 PRO A 352 ? UNP P28329 ?   ?   linker                355 12 
1 9F84 MET A 353 ? UNP P28329 ?   ?   linker                356 13 
1 9F84 VAL A 354 ? UNP P28329 ?   ?   linker                357 14 
1 9F84 PRO A 355 ? UNP P28329 ?   ?   linker                358 15 
2 9F84 ALA A 515 ? UNP P28329 LYS 636 'engineered mutation' 518 16 
2 9F84 ALA A 516 ? UNP P28329 GLU 637 'engineered mutation' 519 17 
2 9F84 ALA A 579 ? UNP P28329 LYS 700 'engineered mutation' 582 18 
2 9F84 ALA A 580 ? UNP P28329 GLU 701 'engineered mutation' 583 19 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 910   ? 
1 MORE         -14   ? 
1 'SSA (A^2)'  23300 ? 
# 
_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 
# 
_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 PRO A 20  ? ARG A 33  ? PRO A 20  ARG A 33  1 ? 14 
HELX_P HELX_P2  AA2 HIS A 34  ? VAL A 36  ? HIS A 34  VAL A 36  5 ? 3  
HELX_P HELX_P3  AA3 SER A 37  ? GLY A 52  ? SER A 37  GLY A 52  1 ? 16 
HELX_P HELX_P4  AA4 GLY A 56  ? THR A 72  ? GLY A 56  THR A 72  1 ? 17 
HELX_P HELX_P5  AA5 VAL A 76  ? TYR A 85  ? VAL A 76  TYR A 85  1 ? 10 
HELX_P HELX_P6  AA6 GLY A 109 ? SER A 133 ? GLY A 109 SER A 133 1 ? 25 
HELX_P HELX_P7  AA7 MET A 152 ? LEU A 158 ? MET A 152 LEU A 158 5 ? 7  
HELX_P HELX_P8  AA8 SER A 207 ? SER A 223 ? SER A 207 SER A 223 1 ? 17 
HELX_P HELX_P9  AA9 PRO A 231 ? ASP A 238 ? PRO A 231 ASP A 238 5 ? 8  
HELX_P HELX_P10 AB1 GLY A 239 ? VAL A 251 ? GLY A 239 VAL A 251 1 ? 13 
HELX_P HELX_P11 AB2 ASP A 253 ? ARG A 265 ? ASP A 253 ARG A 265 1 ? 13 
HELX_P HELX_P12 AB3 SER A 281 ? GLY A 292 ? SER A 281 GLY A 292 1 ? 12 
HELX_P HELX_P13 AB4 ASP A 328 ? THR A 344 ? ASP A 328 THR A 344 1 ? 17 
HELX_P HELX_P14 AB5 SER A 367 ? ASN A 387 ? SER A 370 ASN A 390 1 ? 21 
HELX_P HELX_P15 AB6 GLY A 399 ? LYS A 405 ? GLY A 402 LYS A 408 1 ? 7  
HELX_P HELX_P16 AB7 SER A 409 ? ARG A 427 ? SER A 412 ARG A 430 1 ? 19 
HELX_P HELX_P17 AB8 THR A 453 ? ASP A 465 ? THR A 456 ASP A 468 1 ? 13 
HELX_P HELX_P18 AB9 HIS A 466 ? ALA A 469 ? HIS A 469 ALA A 472 5 ? 4  
HELX_P HELX_P19 AC1 PRO A 471 ? THR A 495 ? PRO A 474 THR A 498 1 ? 25 
HELX_P HELX_P20 AC2 ILE A 499 ? CYS A 514 ? ILE A 502 CYS A 517 1 ? 16 
HELX_P HELX_P21 AC3 PRO A 518 ? ASP A 523 ? PRO A 521 ASP A 526 1 ? 6  
HELX_P HELX_P22 AC4 ASP A 523 ? ASN A 530 ? ASP A 526 ASN A 533 1 ? 8  
HELX_P HELX_P23 AC5 SER A 582 ? SER A 602 ? SER A 585 SER A 605 1 ? 21 
# 
_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 PHE 575 O   ? ? ? 1_555 C NA  . NA ? ? A PHE 578 A NA  702  1_555 ? ? ? ? ? ? ? 2.429 ? ? 
metalc2 metalc ? ? A CYS 578 O   ? ? ? 1_555 C NA  . NA ? ? A CYS 581 A NA  702  1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc3 metalc ? ? A THR 581 O   ? ? ? 1_555 C NA  . NA ? ? A THR 584 A NA  702  1_555 ? ? ? ? ? ? ? 2.502 ? ? 
metalc4 metalc ? ? A THR 581 OG1 ? ? ? 1_555 C NA  . NA ? ? A THR 584 A NA  702  1_555 ? ? ? ? ? ? ? 2.566 ? ? 
metalc5 metalc ? ? C NA  .   NA  ? ? ? 1_555 D HOH . O  ? ? A NA  702 A HOH 899  1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc6 metalc ? ? C NA  .   NA  ? ? ? 1_555 D HOH . O  ? ? A NA  702 A HOH 1057 1_555 ? ? ? ? ? ? ? 2.469 ? ? 
# 
_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  O   ? A PHE 575 ? A PHE 578 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? A CYS 578 ? A CYS 581  ? 1_555 98.7  ? 
2  O   ? A PHE 575 ? A PHE 578 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? A THR 581 ? A THR 584  ? 1_555 160.7 ? 
3  O   ? A CYS 578 ? A CYS 581 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? A THR 581 ? A THR 584  ? 1_555 91.9  ? 
4  O   ? A PHE 575 ? A PHE 578 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 OG1 ? A THR 581 ? A THR 584  ? 1_555 88.7  ? 
5  O   ? A CYS 578 ? A CYS 581 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 OG1 ? A THR 581 ? A THR 584  ? 1_555 90.0  ? 
6  O   ? A THR 581 ? A THR 584 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 OG1 ? A THR 581 ? A THR 584  ? 1_555 75.2  ? 
7  O   ? A PHE 575 ? A PHE 578 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 899  ? 1_555 84.8  ? 
8  O   ? A CYS 578 ? A CYS 581 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 899  ? 1_555 172.5 ? 
9  O   ? A THR 581 ? A THR 584 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 899  ? 1_555 86.6  ? 
10 OG1 ? A THR 581 ? A THR 584 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 899  ? 1_555 96.8  ? 
11 O   ? A PHE 575 ? A PHE 578 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 1057 ? 1_555 109.0 ? 
12 O   ? A CYS 578 ? A CYS 581 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 1057 ? 1_555 79.1  ? 
13 O   ? A THR 581 ? A THR 584 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 1057 ? 1_555 88.7  ? 
14 OG1 ? A THR 581 ? A THR 584 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 1057 ? 1_555 160.3 ? 
15 O   ? D HOH .   ? A HOH 899 ? 1_555 NA ? C NA . ? A NA 702 ? 1_555 O   ? D HOH .   ? A HOH 1057 ? 1_555 93.5  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           182 
_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           GLU 
_struct_mon_prot_cis.auth_seq_id            182 
_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    183 
_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     183 
_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       -4.12 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? 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 ARG A 360 ? ARG A 361 ? ARG A 363 ARG A 364 
AA1 2 GLN A 193 ? ASP A 198 ? GLN A 193 ASP A 198 
AA1 3 HIS A 185 ? CYS A 190 ? HIS A 185 CYS A 190 
AA1 4 LEU A 269 ? LEU A 272 ? LEU A 269 LEU A 272 
AA1 5 LEU A 308 ? VAL A 312 ? LEU A 308 VAL A 312 
AA1 6 CYS A 318 ? CYS A 322 ? CYS A 318 CYS A 322 
AA1 7 ALA A 99  ? ILE A 101 ? ALA A 99  ILE A 101 
AA1 8 PHE A 546 ? CYS A 548 ? PHE A 549 CYS A 551 
AA2 1 SER A 161 ? LEU A 164 ? SER A 161 LEU A 164 
AA2 2 THR A 171 ? ALA A 174 ? THR A 171 ALA A 174 
AA3 1 VAL A 200 ? ILE A 201 ? VAL A 200 ILE A 201 
AA3 2 ARG A 204 ? ARG A 205 ? ARG A 204 ARG A 205 
AA4 1 LEU A 388 ? PHE A 395 ? LEU A 391 PHE A 398 
AA4 2 ILE A 568 ? PHE A 575 ? ILE A 571 PHE A 578 
AA4 3 TYR A 557 ? PRO A 563 ? TYR A 560 PRO A 566 
AA4 4 LEU A 534 ? GLN A 538 ? LEU A 537 GLN A 541 
AA4 5 THR A 432 ? SER A 437 ? THR A 435 SER A 440 
AA4 6 VAL A 446 ? ASN A 448 ? VAL A 449 ASN A 451 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 360 ? O ARG A 363 N VAL A 196 ? N VAL A 196 
AA1 2 3 O LEU A 197 ? O LEU A 197 N VAL A 186 ? N VAL A 186 
AA1 3 4 N ALA A 189 ? N ALA A 189 O LEU A 272 ? O LEU A 272 
AA1 4 5 N CYS A 271 ? N CYS A 271 O PHE A 310 ? O PHE A 310 
AA1 5 6 N VAL A 311 ? N VAL A 311 O GLY A 319 ? O GLY A 319 
AA1 6 7 O VAL A 320 ? O VAL A 320 N VAL A 100 ? N VAL A 100 
AA1 7 8 N ILE A 101 ? N ILE A 101 O PHE A 546 ? O PHE A 549 
AA2 1 2 N TYR A 162 ? N TYR A 162 O VAL A 173 ? O VAL A 173 
AA3 1 2 N ILE A 201 ? N ILE A 201 O ARG A 204 ? O ARG A 204 
AA4 1 2 N TYR A 393 ? N TYR A 396 O PHE A 570 ? O PHE A 573 
AA4 2 3 O CYS A 571 ? O CYS A 574 N CYS A 560 ? N CYS A 563 
AA4 3 4 O ALA A 559 ? O ALA A 562 N SER A 535 ? N SER A 538 
AA4 4 5 O LEU A 534 ? O LEU A 537 N TYR A 433 ? N TYR A 436 
AA4 5 6 N ALA A 436 ? N ALA A 439 O ASP A 447 ? O ASP A 450 
# 
_pdbx_entry_details.entry_id                   9F84 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 85  ? ? -123.94 -65.57  
2 1 VAL A 94  ? ? 73.87   -52.45  
3 1 SER A 96  ? ? -132.25 -52.41  
4 1 LEU A 280 ? ? -89.11  47.09   
5 1 HIS A 291 ? ? -144.89 10.88   
6 1 LYS A 297 ? ? -117.14 -105.16 
7 1 GLU A 446 ? ? 57.84   15.72   
8 1 ARG A 448 ? ? -108.88 -99.54  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 4.09344368957 -5.41069804983 67.9240187751 0.119695591122 ? 0.00171346122282 ? -0.034972670602   ? 
0.158287369662 ? -0.000274864176945 ? 0.176753669111 ? 0.919991275932 ? 0.0889542404214 ? -0.309056020524 ? 1.1522451696   ? 
-0.166107737878 ? 1.78870128983  ? 0.0300690928948 ? -0.0345795638058 ? -0.102907698561   ? -0.135838705478 ? 0.00166609583175 ? 
0.0387468804772 ? 0.122198072464   ? 0.116139071963   ? -0.0203456947169 ? 
2 'X-RAY DIFFRACTION' ? refined 2.67184443769 7.39424142458  47.3878543462 0.357132819741 ? 0.0331718224155  ? -0.0480695620194  ? 
0.239769330269 ? 0.0145654679831    ? 0.170593262124 ? 1.13546203486  ? -0.106904386404 ? 0.0733650045251 ? 1.22899992022  ? 
0.232635427289  ? 1.54967921398  ? 0.0295275192209 ? 0.271967053837   ? -0.00421420341425 ? -0.502035428109 ? -0.0152297860893 ? 
0.107771239414  ? -0.12741259433   ? -0.0931865274138 ? -0.0226028162869 ? 
3 'X-RAY DIFFRACTION' ? refined 12.7103590714 4.79078629555  77.3258070976 0.160383727068 ? 0.00731937345525 ? -0.00102502443575 ? 
0.157164912498 ? -0.00253871286808  ? 0.16068511701  ? 0.795564026135 ? 0.185583118808  ? 0.336999059813  ? 0.716211834488 ? 
0.0189762189037 ? 0.542062563403 ? 0.0457603999735 ? -0.0358442903136 ? -0.0400018157616  ? 0.0437282360789 ? -0.0248513006712 ? 
-0.029514101974 ? -0.0138526659021 ? 0.00451985743069 ? -0.0176795605911 ? 
# 
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 A 1   A 8   ? A 142 A 152 ? ? 
;chain 'A' and (resid 8 through 152 )
;
2 'X-RAY DIFFRACTION' 2 A 143 A 153 ? A 370 A 398 ? ? 
;chain 'A' and (resid 153 through 398 )
;
3 'X-RAY DIFFRACTION' 3 A 371 A 399 ? A 578 A 606 ? ? 
;chain 'A' and (resid 399 through 606 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1231 ? 6.08 . 
2 1 O ? A HOH 1232 ? 6.35 . 
3 1 O ? A HOH 1233 ? 6.78 . 
4 1 O ? A HOH 1234 ? 6.94 . 
# 
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 ALA 1   ? A ALA 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A ALA 3   ? A ALA 3   
4  1 Y 1 A LYS 4   ? A LYS 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A PRO 6   ? A PRO 6   
7  1 Y 1 A SER 7   ? A SER 7   
8  1 Y 1 A GLN 144 ? A GLN 144 
9  1 Y 1 A LEU 145 ? A LEU 145 
10 1 Y 1 A SER 146 ? A SER 146 
11 1 Y 1 A ASN 176 ? A ASN 176 
12 1 Y 1 A SER 177 ? A SER 177 
13 1 Y 1 A SER 178 ? A SER 178 
14 1 Y 1 A ILE 179 ? A ILE 179 
15 1 Y 1 A MET 180 ? A MET 180 
16 1 Y 1 A PRO 349 ? A PRO 346 
17 1 Y 1 A GLU 350 ? A GLU 347 
18 1 Y 1 A LEU 351 ? A LEU 348 
19 1 Y 1 A VAL 352 ? A VAL 349 
20 1 Y 1 A ARG 353 ? A ARG 350 
21 1 Y 1 A SER 354 ? A SER 351 
22 1 Y 1 A PRO 355 ? A PRO 352 
23 1 Y 1 A MET 356 ? A MET 353 
24 1 Y 1 A VAL 357 ? A VAL 354 
25 1 Y 1 A PRO 358 ? A PRO 355 
26 1 Y 1 A LEU 607 ? A LEU 604 
27 1 Y 1 A PRO 608 ? A PRO 605 
28 1 Y 1 A PRO 609 ? A PRO 606 
29 1 Y 1 A THR 610 ? A THR 607 
30 1 Y 1 A GLU 611 ? A GLU 608 
31 1 Y 1 A SER 612 ? A SER 609 
32 1 Y 1 A LYS 613 ? A LYS 610 
33 1 Y 1 A PRO 614 ? A PRO 611 
34 1 Y 1 A LEU 615 ? A LEU 612 
# 
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 
A1IAP C13  C  N N 1   
A1IAP C23  C  Y N 2   
A1IAP C12  C  N N 3   
A1IAP C22  C  Y N 4   
A1IAP C11  C  N N 5   
A1IAP C21  C  Y N 6   
A1IAP C01  C  N N 7   
A1IAP C02  C  N N 8   
A1IAP C03  C  N N 9   
A1IAP C05  C  N S 10  
A1IAP C06  C  N N 11  
A1IAP C07  C  N N 12  
A1IAP C08  C  N N 13  
A1IAP C09  C  N N 14  
A1IAP C14  C  Y N 15  
A1IAP C15  C  Y N 16  
A1IAP C16  C  Y N 17  
A1IAP C17  C  Y N 18  
A1IAP C18  C  Y N 19  
A1IAP C19  C  Y N 20  
A1IAP C20  C  Y N 21  
A1IAP N10  N  N N 22  
A1IAP S04  S  N N 23  
A1IAP H131 H  N N 24  
A1IAP H121 H  N N 25  
A1IAP H221 H  N N 26  
A1IAP H113 H  N N 27  
A1IAP H111 H  N N 28  
A1IAP H112 H  N N 29  
A1IAP H211 H  N N 30  
A1IAP H012 H  N N 31  
A1IAP H011 H  N N 32  
A1IAP H013 H  N N 33  
A1IAP H021 H  N N 34  
A1IAP H022 H  N N 35  
A1IAP H031 H  N N 36  
A1IAP H032 H  N N 37  
A1IAP H051 H  N N 38  
A1IAP H062 H  N N 39  
A1IAP H061 H  N N 40  
A1IAP H081 H  N N 41  
A1IAP H091 H  N N 42  
A1IAP H151 H  N N 43  
A1IAP H161 H  N N 44  
A1IAP H171 H  N N 45  
A1IAP H191 H  N N 46  
A1IAP H201 H  N N 47  
A1IAP H1   H  N N 48  
ALA   N    N  N N 49  
ALA   CA   C  N S 50  
ALA   C    C  N N 51  
ALA   O    O  N N 52  
ALA   CB   C  N N 53  
ALA   OXT  O  N N 54  
ALA   H    H  N N 55  
ALA   H2   H  N N 56  
ALA   HA   H  N N 57  
ALA   HB1  H  N N 58  
ALA   HB2  H  N N 59  
ALA   HB3  H  N N 60  
ALA   HXT  H  N N 61  
ARG   N    N  N N 62  
ARG   CA   C  N S 63  
ARG   C    C  N N 64  
ARG   O    O  N N 65  
ARG   CB   C  N N 66  
ARG   CG   C  N N 67  
ARG   CD   C  N N 68  
ARG   NE   N  N N 69  
ARG   CZ   C  N N 70  
ARG   NH1  N  N N 71  
ARG   NH2  N  N N 72  
ARG   OXT  O  N N 73  
ARG   H    H  N N 74  
ARG   H2   H  N N 75  
ARG   HA   H  N N 76  
ARG   HB2  H  N N 77  
ARG   HB3  H  N N 78  
ARG   HG2  H  N N 79  
ARG   HG3  H  N N 80  
ARG   HD2  H  N N 81  
ARG   HD3  H  N N 82  
ARG   HE   H  N N 83  
ARG   HH11 H  N N 84  
ARG   HH12 H  N N 85  
ARG   HH21 H  N N 86  
ARG   HH22 H  N N 87  
ARG   HXT  H  N N 88  
ASN   N    N  N N 89  
ASN   CA   C  N S 90  
ASN   C    C  N N 91  
ASN   O    O  N N 92  
ASN   CB   C  N N 93  
ASN   CG   C  N N 94  
ASN   OD1  O  N N 95  
ASN   ND2  N  N N 96  
ASN   OXT  O  N N 97  
ASN   H    H  N N 98  
ASN   H2   H  N N 99  
ASN   HA   H  N N 100 
ASN   HB2  H  N N 101 
ASN   HB3  H  N N 102 
ASN   HD21 H  N N 103 
ASN   HD22 H  N N 104 
ASN   HXT  H  N N 105 
ASP   N    N  N N 106 
ASP   CA   C  N S 107 
ASP   C    C  N N 108 
ASP   O    O  N N 109 
ASP   CB   C  N N 110 
ASP   CG   C  N N 111 
ASP   OD1  O  N N 112 
ASP   OD2  O  N N 113 
ASP   OXT  O  N N 114 
ASP   H    H  N N 115 
ASP   H2   H  N N 116 
ASP   HA   H  N N 117 
ASP   HB2  H  N N 118 
ASP   HB3  H  N N 119 
ASP   HD2  H  N N 120 
ASP   HXT  H  N N 121 
CYS   N    N  N N 122 
CYS   CA   C  N R 123 
CYS   C    C  N N 124 
CYS   O    O  N N 125 
CYS   CB   C  N N 126 
CYS   SG   S  N N 127 
CYS   OXT  O  N N 128 
CYS   H    H  N N 129 
CYS   H2   H  N N 130 
CYS   HA   H  N N 131 
CYS   HB2  H  N N 132 
CYS   HB3  H  N N 133 
CYS   HG   H  N N 134 
CYS   HXT  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
NA    NA   NA N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
# 
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 
A1IAP C02 C01  sing N N 1   
A1IAP C03 C02  sing N N 2   
A1IAP S04 C03  sing N N 3   
A1IAP C05 S04  sing N N 4   
A1IAP C07 C06  sing N N 5   
A1IAP C08 C07  sing N N 6   
A1IAP C09 C08  doub N N 7   
A1IAP N10 C09  sing N N 8   
A1IAP C11 N10  sing N N 9   
A1IAP C12 N10  sing N N 10  
A1IAP C13 C12  doub N N 11  
A1IAP C06 C05  sing N N 12  
A1IAP C14 C05  sing N N 13  
A1IAP C15 C14  doub Y N 14  
A1IAP C16 C15  sing Y N 15  
A1IAP C17 C16  doub Y N 16  
A1IAP C18 C17  sing Y N 17  
A1IAP C19 C18  sing Y N 18  
A1IAP C20 C19  doub Y N 19  
A1IAP C21 C20  sing Y N 20  
A1IAP C22 C21  doub Y N 21  
A1IAP C23 C22  sing Y N 22  
A1IAP C07 C13  sing N N 23  
A1IAP C14 C23  sing Y N 24  
A1IAP C18 C23  doub Y N 25  
A1IAP C13 H131 sing N N 26  
A1IAP C12 H121 sing N N 27  
A1IAP C22 H221 sing N N 28  
A1IAP C11 H113 sing N N 29  
A1IAP C11 H111 sing N N 30  
A1IAP C11 H112 sing N N 31  
A1IAP C21 H211 sing N N 32  
A1IAP C01 H012 sing N N 33  
A1IAP C01 H011 sing N N 34  
A1IAP C01 H013 sing N N 35  
A1IAP C02 H021 sing N N 36  
A1IAP C02 H022 sing N N 37  
A1IAP C03 H031 sing N N 38  
A1IAP C03 H032 sing N N 39  
A1IAP C05 H051 sing N N 40  
A1IAP C06 H062 sing N N 41  
A1IAP C06 H061 sing N N 42  
A1IAP C08 H081 sing N N 43  
A1IAP C09 H091 sing N N 44  
A1IAP C15 H151 sing N N 45  
A1IAP C16 H161 sing N N 46  
A1IAP C17 H171 sing N N 47  
A1IAP C19 H191 sing N N 48  
A1IAP C20 H201 sing N N 49  
A1IAP C07 H1   sing N N 50  
ALA   N   CA   sing N N 51  
ALA   N   H    sing N N 52  
ALA   N   H2   sing N N 53  
ALA   CA  C    sing N N 54  
ALA   CA  CB   sing N N 55  
ALA   CA  HA   sing N N 56  
ALA   C   O    doub N N 57  
ALA   C   OXT  sing N N 58  
ALA   CB  HB1  sing N N 59  
ALA   CB  HB2  sing N N 60  
ALA   CB  HB3  sing N N 61  
ALA   OXT HXT  sing N N 62  
ARG   N   CA   sing N N 63  
ARG   N   H    sing N N 64  
ARG   N   H2   sing N N 65  
ARG   CA  C    sing N N 66  
ARG   CA  CB   sing N N 67  
ARG   CA  HA   sing N N 68  
ARG   C   O    doub N N 69  
ARG   C   OXT  sing N N 70  
ARG   CB  CG   sing N N 71  
ARG   CB  HB2  sing N N 72  
ARG   CB  HB3  sing N N 73  
ARG   CG  CD   sing N N 74  
ARG   CG  HG2  sing N N 75  
ARG   CG  HG3  sing N N 76  
ARG   CD  NE   sing N N 77  
ARG   CD  HD2  sing N N 78  
ARG   CD  HD3  sing N N 79  
ARG   NE  CZ   sing N N 80  
ARG   NE  HE   sing N N 81  
ARG   CZ  NH1  sing N N 82  
ARG   CZ  NH2  doub N N 83  
ARG   NH1 HH11 sing N N 84  
ARG   NH1 HH12 sing N N 85  
ARG   NH2 HH21 sing N N 86  
ARG   NH2 HH22 sing N N 87  
ARG   OXT HXT  sing N N 88  
ASN   N   CA   sing N N 89  
ASN   N   H    sing N N 90  
ASN   N   H2   sing N N 91  
ASN   CA  C    sing N N 92  
ASN   CA  CB   sing N N 93  
ASN   CA  HA   sing N N 94  
ASN   C   O    doub N N 95  
ASN   C   OXT  sing N N 96  
ASN   CB  CG   sing N N 97  
ASN   CB  HB2  sing N N 98  
ASN   CB  HB3  sing N N 99  
ASN   CG  OD1  doub N N 100 
ASN   CG  ND2  sing N N 101 
ASN   ND2 HD21 sing N N 102 
ASN   ND2 HD22 sing N N 103 
ASN   OXT HXT  sing N N 104 
ASP   N   CA   sing N N 105 
ASP   N   H    sing N N 106 
ASP   N   H2   sing N N 107 
ASP   CA  C    sing N N 108 
ASP   CA  CB   sing N N 109 
ASP   CA  HA   sing N N 110 
ASP   C   O    doub N N 111 
ASP   C   OXT  sing N N 112 
ASP   CB  CG   sing N N 113 
ASP   CB  HB2  sing N N 114 
ASP   CB  HB3  sing N N 115 
ASP   CG  OD1  doub N N 116 
ASP   CG  OD2  sing N N 117 
ASP   OD2 HD2  sing N N 118 
ASP   OXT HXT  sing N N 119 
CYS   N   CA   sing N N 120 
CYS   N   H    sing N N 121 
CYS   N   H2   sing N N 122 
CYS   CA  C    sing N N 123 
CYS   CA  CB   sing N N 124 
CYS   CA  HA   sing N N 125 
CYS   C   O    doub N N 126 
CYS   C   OXT  sing N N 127 
CYS   CB  SG   sing N N 128 
CYS   CB  HB2  sing N N 129 
CYS   CB  HB3  sing N N 130 
CYS   SG  HG   sing N N 131 
CYS   OXT HXT  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Sweden 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2fy2 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9F84 
_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]   0.018295 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013027 
_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]   0.006086 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? 9.38062 1.54875 ? ? 3.38349  72.32734 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . SER   A 1 8   ? 6.38420   -28.60369 57.72663  1.000 67.32092 ? 8    SER   A N   1 
ATOM   2    C  CA  . SER   A 1 8   ? 6.37235   -28.59455 56.26777  1.000 77.17038 ? 8    SER   A CA  1 
ATOM   3    C  C   . SER   A 1 8   ? 5.57781   -27.39783 55.74066  1.000 83.78172 ? 8    SER   A C   1 
ATOM   4    O  O   . SER   A 1 8   ? 6.13053   -26.50587 55.09500  1.000 72.47105 ? 8    SER   A O   1 
ATOM   5    C  CB  . SER   A 1 8   ? 5.79288   -29.91013 55.73292  1.000 77.17013 ? 8    SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 8   ? 4.61414   -30.26949 56.43355  1.000 91.39317 ? 8    SER   A OG  1 
ATOM   7    N  N   . GLU   A 1 9   ? 4.27446   -27.39088 56.02547  1.000 73.93723 ? 9    GLU   A N   1 
ATOM   8    C  CA  . GLU   A 1 9   ? 3.39517   -26.27965 55.68076  1.000 55.54787 ? 9    GLU   A CA  1 
ATOM   9    C  C   . GLU   A 1 9   ? 3.25252   -25.26699 56.80906  1.000 54.61435 ? 9    GLU   A C   1 
ATOM   10   O  O   . GLU   A 1 9   ? 2.90072   -24.11071 56.54964  1.000 60.68377 ? 9    GLU   A O   1 
ATOM   11   C  CB  . GLU   A 1 9   ? 2.00249   -26.80625 55.32226  1.000 50.83373 ? 9    GLU   A CB  1 
ATOM   12   C  CG  . GLU   A 1 9   ? 1.97308   -27.70521 54.09482  1.000 58.53794 ? 9    GLU   A CG  1 
ATOM   13   C  CD  . GLU   A 1 9   ? 2.07264   -26.90902 52.80325  1.000 54.73072 ? 9    GLU   A CD  1 
ATOM   14   O  OE1 . GLU   A 1 9   ? 1.57022   -25.76119 52.77430  1.000 48.98578 ? 9    GLU   A OE1 1 
ATOM   15   O  OE2 . GLU   A 1 9   ? 2.65802   -27.42530 51.82707  1.000 47.79401 ? 9    GLU   A OE2 1 
ATOM   16   N  N   . GLU   A 1 10  ? 3.48352   -25.68136 58.04707  1.000 60.69920 ? 10   GLU   A N   1 
ATOM   17   C  CA  . GLU   A 1 10  ? 3.32838   -24.81457 59.20258  1.000 66.41299 ? 10   GLU   A CA  1 
ATOM   18   C  C   . GLU   A 1 10  ? 4.68968   -24.39155 59.73606  1.000 59.07794 ? 10   GLU   A C   1 
ATOM   19   O  O   . GLU   A 1 10  ? 5.71330   -25.04186 59.50247  1.000 53.75485 ? 10   GLU   A O   1 
ATOM   20   C  CB  . GLU   A 1 10  ? 2.52797   -25.51438 60.30483  1.000 54.29151 ? 10   GLU   A CB  1 
ATOM   21   N  N   . SER   A 1 11  ? 4.67824   -23.28944 60.47668  1.000 53.75124 ? 11   SER   A N   1 
ATOM   22   C  CA  . SER   A 1 11  ? 5.88495   -22.75535 61.08730  1.000 47.08137 ? 11   SER   A CA  1 
ATOM   23   C  C   . SER   A 1 11  ? 6.46984   -23.72739 62.10889  1.000 48.63325 ? 11   SER   A C   1 
ATOM   24   O  O   . SER   A 1 11  ? 5.74770   -24.43092 62.82064  1.000 50.47963 ? 11   SER   A O   1 
ATOM   25   C  CB  . SER   A 1 11  ? 5.56785   -21.42336 61.76865  1.000 51.92327 ? 11   SER   A CB  1 
ATOM   26   O  OG  . SER   A 1 11  ? 6.74663   -20.76085 62.15314  1.000 38.56974 ? 11   SER   A OG  1 
ATOM   27   N  N   . GLY   A 1 12  ? 7.79881   -23.76945 62.17021  1.000 37.35451 ? 12   GLY   A N   1 
ATOM   28   C  CA  . GLY   A 1 12  ? 8.47063   -24.45202 63.25293  1.000 32.05090 ? 12   GLY   A CA  1 
ATOM   29   C  C   . GLY   A 1 12  ? 8.78025   -23.57872 64.45784  1.000 38.44260 ? 12   GLY   A C   1 
ATOM   30   O  O   . GLY   A 1 12  ? 9.29339   -24.07944 65.46353  1.000 36.01778 ? 12   GLY   A O   1 
ATOM   31   N  N   . LEU   A 1 13  ? 8.46723   -22.28722 64.39633  1.000 30.39333 ? 13   LEU   A N   1 
ATOM   32   C  CA  . LEU   A 1 13  ? 8.79273   -21.36166 65.47417  1.000 25.84984 ? 13   LEU   A CA  1 
ATOM   33   C  C   . LEU   A 1 13  ? 7.88577   -21.59580 66.68015  1.000 29.03976 ? 13   LEU   A C   1 
ATOM   34   O  O   . LEU   A 1 13  ? 6.73513   -21.99684 66.52718  1.000 29.57018 ? 13   LEU   A O   1 
ATOM   35   C  CB  . LEU   A 1 13  ? 8.62690   -19.91018 65.00877  1.000 24.04681 ? 13   LEU   A CB  1 
ATOM   36   C  CG  . LEU   A 1 13  ? 9.55188   -19.45914 63.87307  1.000 34.53812 ? 13   LEU   A CG  1 
ATOM   37   C  CD1 . LEU   A 1 13  ? 9.11685   -18.12537 63.34348  1.000 28.62238 ? 13   LEU   A CD1 1 
ATOM   38   C  CD2 . LEU   A 1 13  ? 10.97663  -19.36718 64.39082  1.000 30.26795 ? 13   LEU   A CD2 1 
ATOM   39   N  N   . PRO   A 1 14  ? 8.36488   -21.30221 67.88856  1.000 30.50065 ? 14   PRO   A N   1 
ATOM   40   C  CA  . PRO   A 1 14  ? 7.47566   -21.34514 69.05645  1.000 23.85930 ? 14   PRO   A CA  1 
ATOM   41   C  C   . PRO   A 1 14  ? 6.36888   -20.30994 68.94176  1.000 26.66366 ? 14   PRO   A C   1 
ATOM   42   O  O   . PRO   A 1 14  ? 6.53733   -19.24739 68.32908  1.000 23.36318 ? 14   PRO   A O   1 
ATOM   43   C  CB  . PRO   A 1 14  ? 8.41465   -21.00987 70.22227  1.000 29.40923 ? 14   PRO   A CB  1 
ATOM   44   C  CG  . PRO   A 1 14  ? 9.44727   -20.09150 69.58756  1.000 23.57437 ? 14   PRO   A CG  1 
ATOM   45   C  CD  . PRO   A 1 14  ? 9.70040   -20.76411 68.23140  1.000 26.11888 ? 14   PRO   A CD  1 
ATOM   46   N  N   . LYS   A 1 15  ? 5.23046   -20.61199 69.55755  1.000 22.53629 ? 15   LYS   A N   1 
ATOM   47   C  CA  . LYS   A 1 15  ? 4.19605   -19.59987 69.66910  1.000 23.06803 ? 15   LYS   A CA  1 
ATOM   48   C  C   . LYS   A 1 15  ? 4.56239   -18.60155 70.76841  1.000 21.09102 ? 15   LYS   A C   1 
ATOM   49   O  O   . LYS   A 1 15  ? 5.32768   -18.90269 71.69302  1.000 23.71692 ? 15   LYS   A O   1 
ATOM   50   C  CB  . LYS   A 1 15  ? 2.84052   -20.22673 69.99338  1.000 27.29895 ? 15   LYS   A CB  1 
ATOM   51   C  CG  . LYS   A 1 15  ? 2.20262   -20.99656 68.84498  1.000 28.10491 ? 15   LYS   A CG  1 
ATOM   52   C  CD  . LYS   A 1 15  ? 0.85178   -21.57083 69.25819  1.000 28.30072 ? 15   LYS   A CD  1 
ATOM   53   C  CE  . LYS   A 1 15  ? 0.17762   -22.26398 68.06582  1.000 32.05179 ? 15   LYS   A CE  1 
ATOM   54   N  NZ  . LYS   A 1 15  ? -1.17948  -22.70138 68.44350  1.000 26.84816 ? 15   LYS   A NZ  1 
ATOM   55   N  N   . LEU   A 1 16  ? 3.95835   -17.43971 70.68641  1.000 18.84570 ? 16   LEU   A N   1 
ATOM   56   C  CA  . LEU   A 1 16  ? 4.13003   -16.38121 71.68163  1.000 24.66058 ? 16   LEU   A CA  1 
ATOM   57   C  C   . LEU   A 1 16  ? 3.68361   -16.86883 73.05724  1.000 20.64530 ? 16   LEU   A C   1 
ATOM   58   O  O   . LEU   A 1 16  ? 2.53932   -17.33051 73.20253  1.000 21.48967 ? 16   LEU   A O   1 
ATOM   59   C  CB  . LEU   A 1 16  ? 3.31832   -15.15809 71.25399  1.000 22.28798 ? 16   LEU   A CB  1 
ATOM   60   C  CG  . LEU   A 1 16  ? 3.45647   -13.86461 72.06539  1.000 19.27865 ? 16   LEU   A CG  1 
ATOM   61   C  CD1 . LEU   A 1 16  ? 4.91657   -13.34424 72.02872  1.000 19.54194 ? 16   LEU   A CD1 1 
ATOM   62   C  CD2 . LEU   A 1 16  ? 2.44407   -12.79833 71.57282  1.000 19.20273 ? 16   LEU   A CD2 1 
ATOM   63   N  N   . PRO   A 1 17  ? 4.54176   -16.82471 74.07052  1.000 18.03502 ? 17   PRO   A N   1 
ATOM   64   C  CA  . PRO   A 1 17  ? 4.14239   -17.33012 75.38452  1.000 26.22670 ? 17   PRO   A CA  1 
ATOM   65   C  C   . PRO   A 1 17  ? 3.00590   -16.50813 75.96004  1.000 23.26381 ? 17   PRO   A C   1 
ATOM   66   O  O   . PRO   A 1 17  ? 2.83818   -15.33319 75.64357  1.000 23.73070 ? 17   PRO   A O   1 
ATOM   67   C  CB  . PRO   A 1 17  ? 5.40976   -17.17073 76.23814  1.000 24.40556 ? 17   PRO   A CB  1 
ATOM   68   C  CG  . PRO   A 1 17  ? 6.52638   -16.98619 75.28500  1.000 26.14992 ? 17   PRO   A CG  1 
ATOM   69   C  CD  . PRO   A 1 17  ? 5.94612   -16.38436 74.04231  1.000 22.74275 ? 17   PRO   A CD  1 
ATOM   70   N  N   . VAL   A 1 18  ? 2.22968   -17.13985 76.83580  1.000 20.92386 ? 18   VAL   A N   1 
ATOM   71   C  CA  . VAL   A 1 18  ? 1.28466   -16.42918 77.68952  1.000 23.95857 ? 18   VAL   A CA  1 
ATOM   72   C  C   . VAL   A 1 18  ? 1.92868   -16.31961 79.07049  1.000 21.47175 ? 18   VAL   A C   1 
ATOM   73   O  O   . VAL   A 1 18  ? 2.15262   -17.35711 79.71133  1.000 20.68343 ? 18   VAL   A O   1 
ATOM   74   C  CB  . VAL   A 1 18  ? -0.06335  -17.15743 77.76626  1.000 23.86459 ? 18   VAL   A CB  1 
ATOM   75   C  CG1 . VAL   A 1 18  ? -0.94699  -16.48280 78.80577  1.000 23.39610 ? 18   VAL   A CG1 1 
ATOM   76   C  CG2 . VAL   A 1 18  ? -0.75602  -17.18128 76.36625  1.000 21.30824 ? 18   VAL   A CG2 1 
ATOM   77   N  N   . PRO   A 1 19  ? 2.27170   -15.12400 79.54056  1.000 20.68069 ? 19   PRO   A N   1 
ATOM   78   C  CA  . PRO   A 1 19  ? 2.90460   -15.01549 80.86537  1.000 21.08765 ? 19   PRO   A CA  1 
ATOM   79   C  C   . PRO   A 1 19  ? 1.94222   -15.47248 81.94015  1.000 22.12492 ? 19   PRO   A C   1 
ATOM   80   O  O   . PRO   A 1 19  ? 0.71656   -15.41424 81.74545  1.000 23.72254 ? 19   PRO   A O   1 
ATOM   81   C  CB  . PRO   A 1 19  ? 3.18908   -13.51255 80.99766  1.000 22.28401 ? 19   PRO   A CB  1 
ATOM   82   C  CG  . PRO   A 1 19  ? 3.16757   -12.97015 79.54509  1.000 23.82839 ? 19   PRO   A CG  1 
ATOM   83   C  CD  . PRO   A 1 19  ? 2.08205   -13.80898 78.89920  1.000 21.09547 ? 19   PRO   A CD  1 
ATOM   84   N  N   A PRO   A 1 20  ? 2.44094   -15.92960 83.08765  0.051 23.49289 ? 20   PRO   A N   1 
ATOM   85   N  N   B PRO   A 1 20  ? 2.44637   -15.91660 83.09253  0.949 23.34388 ? 20   PRO   A N   1 
ATOM   86   C  CA  A PRO   A 1 20  ? 1.53499   -16.23146 84.20318  0.051 21.93880 ? 20   PRO   A CA  1 
ATOM   87   C  CA  B PRO   A 1 20  ? 1.54670   -16.21235 84.21416  0.949 21.61054 ? 20   PRO   A CA  1 
ATOM   88   C  C   A PRO   A 1 20  ? 0.81083   -14.97293 84.65990  0.051 25.76001 ? 20   PRO   A C   1 
ATOM   89   C  C   B PRO   A 1 20  ? 0.79383   -14.95612 84.62071  0.949 25.97966 ? 20   PRO   A C   1 
ATOM   90   O  O   A PRO   A 1 20  ? 1.37814   -13.87835 84.66479  0.051 24.41580 ? 20   PRO   A O   1 
ATOM   91   O  O   B PRO   A 1 20  ? 1.32044   -13.84473 84.55214  0.949 24.37208 ? 20   PRO   A O   1 
ATOM   92   C  CB  A PRO   A 1 20  ? 2.46828   -16.78174 85.28873  0.051 27.54526 ? 20   PRO   A CB  1 
ATOM   93   C  CB  B PRO   A 1 20  ? 2.49018   -16.68506 85.32718  0.949 27.75306 ? 20   PRO   A CB  1 
ATOM   94   C  CG  A PRO   A 1 20  ? 3.83862   -16.33087 84.90011  0.051 26.49383 ? 20   PRO   A CG  1 
ATOM   95   C  CG  B PRO   A 1 20  ? 3.77989   -17.06892 84.64270  0.949 26.21250 ? 20   PRO   A CG  1 
ATOM   96   C  CD  A PRO   A 1 20  ? 3.84504   -16.23752 83.40640  0.051 28.33804 ? 20   PRO   A CD  1 
ATOM   97   C  CD  B PRO   A 1 20  ? 3.86185   -16.11113 83.45100  0.949 28.68357 ? 20   PRO   A CD  1 
ATOM   98   N  N   . LEU   A 1 21  ? -0.46208  -15.13767 85.03457  1.000 25.28214 ? 21   LEU   A N   1 
ATOM   99   C  CA  . LEU   A 1 21  ? -1.29889  -13.97918 85.35955  1.000 22.82822 ? 21   LEU   A CA  1 
ATOM   100  C  C   . LEU   A 1 21  ? -0.72177  -13.17308 86.52173  1.000 25.97495 ? 21   LEU   A C   1 
ATOM   101  O  O   . LEU   A 1 21  ? -0.66288  -11.94110 86.46406  1.000 22.90224 ? 21   LEU   A O   1 
ATOM   102  C  CB  . LEU   A 1 21  ? -2.72413  -14.43511 85.67693  1.000 20.61337 ? 21   LEU   A CB  1 
ATOM   103  C  CG  . LEU   A 1 21  ? -3.64964  -13.33979 86.20129  1.000 20.89270 ? 21   LEU   A CG  1 
ATOM   104  C  CD1 . LEU   A 1 21  ? -3.97747  -12.32989 85.07145  1.000 24.83902 ? 21   LEU   A CD1 1 
ATOM   105  C  CD2 . LEU   A 1 21  ? -4.94448  -13.96888 86.77268  1.000 28.32892 ? 21   LEU   A CD2 1 
ATOM   106  N  N   . GLN   A 1 22  ? -0.29603  -13.84554 87.59454  1.000 25.13846 ? 22   GLN   A N   1 
ATOM   107  C  CA  . GLN   A 1 22  ? 0.14201   -13.09910 88.77708  1.000 23.63626 ? 22   GLN   A CA  1 
ATOM   108  C  C   . GLN   A 1 22  ? 1.45906   -12.37319 88.53583  1.000 26.29047 ? 22   GLN   A C   1 
ATOM   109  O  O   . GLN   A 1 22  ? 1.71084   -11.33121 89.15413  1.000 24.50653 ? 22   GLN   A O   1 
ATOM   110  C  CB  . GLN   A 1 22  ? 0.28957   -14.02377 89.99142  1.000 27.11203 ? 22   GLN   A CB  1 
ATOM   111  C  CG  . GLN   A 1 22  ? -0.99652  -14.70386 90.37843  1.000 26.69487 ? 22   GLN   A CG  1 
ATOM   112  C  CD  . GLN   A 1 22  ? -2.14907  -13.73395 90.64947  1.000 34.42638 ? 22   GLN   A CD  1 
ATOM   113  O  OE1 . GLN   A 1 22  ? -1.96596  -12.62265 91.18174  1.000 25.44410 ? 22   GLN   A OE1 1 
ATOM   114  N  NE2 . GLN   A 1 22  ? -3.36014  -14.17777 90.31664  1.000 30.96806 ? 22   GLN   A NE2 1 
ATOM   115  N  N   . GLN   A 1 23  ? 2.30567   -12.92036 87.66164  1.000 19.86033 ? 23   GLN   A N   1 
ATOM   116  C  CA  . GLN   A 1 23  ? 3.53676   -12.24402 87.26025  1.000 22.48345 ? 23   GLN   A CA  1 
ATOM   117  C  C   . GLN   A 1 23  ? 3.23810   -10.91399 86.57784  1.000 20.32385 ? 23   GLN   A C   1 
ATOM   118  O  O   . GLN   A 1 23  ? 3.87081   -9.88998  86.87235  1.000 21.00252 ? 23   GLN   A O   1 
ATOM   119  C  CB  . GLN   A 1 23  ? 4.33448   -13.15963 86.31968  1.000 31.29299 ? 23   GLN   A CB  1 
ATOM   120  C  CG  . GLN   A 1 23  ? 5.61222   -12.54950 85.71029  1.000 26.20803 ? 23   GLN   A CG  1 
ATOM   121  C  CD  . GLN   A 1 23  ? 6.29793   -13.48321 84.72241  1.000 32.11960 ? 23   GLN   A CD  1 
ATOM   122  O  OE1 . GLN   A 1 23  ? 6.71860   -14.58690 85.06774  1.000 31.47158 ? 23   GLN   A OE1 1 
ATOM   123  N  NE2 . GLN   A 1 23  ? 6.40548   -13.04190 83.47805  1.000 33.21801 ? 23   GLN   A NE2 1 
ATOM   124  N  N   . THR   A 1 24  ? 2.28720   -10.91811 85.64542  1.000 21.46119 ? 24   THR   A N   1 
ATOM   125  C  CA  . THR   A 1 24  ? 1.94139   -9.69965  84.91820  1.000 20.40992 ? 24   THR   A CA  1 
ATOM   126  C  C   . THR   A 1 24  ? 1.29181   -8.67964  85.84740  1.000 25.30702 ? 24   THR   A C   1 
ATOM   127  O  O   . THR   A 1 24  ? 1.59784   -7.48754  85.76720  1.000 21.50101 ? 24   THR   A O   1 
ATOM   128  C  CB  . THR   A 1 24  ? 1.03341   -10.05073 83.73259  1.000 23.84702 ? 24   THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 24  ? 1.84000   -10.61741 82.68310  1.000 21.25122 ? 24   THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 24  ? 0.26074   -8.81217  83.19074  1.000 20.34665 ? 24   THR   A CG2 1 
ATOM   131  N  N   . LEU   A 1 25  ? 0.41668   -9.12499  86.76365  1.000 19.82021 ? 25   LEU   A N   1 
ATOM   132  C  CA  . LEU   A 1 25  ? -0.24964  -8.15289  87.63594  1.000 24.92720 ? 25   LEU   A CA  1 
ATOM   133  C  C   . LEU   A 1 25  ? 0.74738   -7.51570  88.59832  1.000 20.82290 ? 25   LEU   A C   1 
ATOM   134  O  O   . LEU   A 1 25  ? 0.65516   -6.31698  88.89877  1.000 23.85590 ? 25   LEU   A O   1 
ATOM   135  C  CB  . LEU   A 1 25  ? -1.39779  -8.81286  88.41114  1.000 21.38744 ? 25   LEU   A CB  1 
ATOM   136  C  CG  . LEU   A 1 25  ? -2.47818  -9.44847  87.54709  1.000 20.53266 ? 25   LEU   A CG  1 
ATOM   137  C  CD1 . LEU   A 1 25  ? -3.60194  -10.04327 88.43339  1.000 22.54608 ? 25   LEU   A CD1 1 
ATOM   138  C  CD2 . LEU   A 1 25  ? -3.04110  -8.35466  86.63068  1.000 18.13203 ? 25   LEU   A CD2 1 
ATOM   139  N  N   . ALA   A 1 26  ? 1.71305   -8.30088  89.08158  1.000 19.41263 ? 26   ALA   A N   1 
ATOM   140  C  CA  . ALA   A 1 26  ? 2.72364   -7.76270  89.99303  1.000 22.82329 ? 26   ALA   A CA  1 
ATOM   141  C  C   . ALA   A 1 26  ? 3.63963   -6.78576  89.27432  1.000 25.55249 ? 26   ALA   A C   1 
ATOM   142  O  O   . ALA   A 1 26  ? 3.94564   -5.70684  89.79889  1.000 21.84530 ? 26   ALA   A O   1 
ATOM   143  C  CB  . ALA   A 1 26  ? 3.54706   -8.89069  90.60486  1.000 23.97518 ? 26   ALA   A CB  1 
ATOM   144  N  N   . THR   A 1 27  ? 4.08840   -7.14479  88.06948  1.000 20.91712 ? 27   THR   A N   1 
ATOM   145  C  CA  . THR   A 1 27  ? 4.93027   -6.23442  87.30179  1.000 24.39320 ? 27   THR   A CA  1 
ATOM   146  C  C   . THR   A 1 27  ? 4.18489   -4.94549  86.98300  1.000 23.15359 ? 27   THR   A C   1 
ATOM   147  O  O   . THR   A 1 27  ? 4.74508   -3.85323  87.08757  1.000 22.88901 ? 27   THR   A O   1 
ATOM   148  C  CB  . THR   A 1 27  ? 5.39464   -6.91435  86.02077  1.000 23.64426 ? 27   THR   A CB  1 
ATOM   149  O  OG1 . THR   A 1 27  ? 6.25310   -8.01356  86.35671  1.000 23.09594 ? 27   THR   A OG1 1 
ATOM   150  C  CG2 . THR   A 1 27  ? 6.18733   -5.93855  85.14325  1.000 23.08539 ? 27   THR   A CG2 1 
ATOM   151  N  N   . TYR   A 1 28  ? 2.92075   -5.06565  86.59667  1.000 18.19831 ? 28   TYR   A N   1 
ATOM   152  C  CA  . TYR   A 1 28  ? 2.09300   -3.90423  86.28375  1.000 17.73625 ? 28   TYR   A CA  1 
ATOM   153  C  C   . TYR   A 1 28  ? 2.02572   -2.92770  87.44909  1.000 25.12212 ? 28   TYR   A C   1 
ATOM   154  O  O   . TYR   A 1 28  ? 2.26528   -1.73283  87.27693  1.000 21.24652 ? 28   TYR   A O   1 
ATOM   155  C  CB  . TYR   A 1 28  ? 0.69115   -4.36102  85.88402  1.000 18.40699 ? 28   TYR   A CB  1 
ATOM   156  C  CG  . TYR   A 1 28  ? -0.36304  -3.25851  85.83332  1.000 19.23278 ? 28   TYR   A CG  1 
ATOM   157  C  CD1 . TYR   A 1 28  ? -0.31661  -2.26485  84.85415  1.000 20.70860 ? 28   TYR   A CD1 1 
ATOM   158  C  CD2 . TYR   A 1 28  ? -1.42751  -3.24423  86.73543  1.000 21.23105 ? 28   TYR   A CD2 1 
ATOM   159  C  CE1 . TYR   A 1 28  ? -1.28009  -1.26233  84.79674  1.000 18.41090 ? 28   TYR   A CE1 1 
ATOM   160  C  CE2 . TYR   A 1 28  ? -2.39824  -2.25388  86.67816  1.000 23.49926 ? 28   TYR   A CE2 1 
ATOM   161  C  CZ  . TYR   A 1 28  ? -2.32695  -1.27698  85.70826  1.000 23.31402 ? 28   TYR   A CZ  1 
ATOM   162  O  OH  . TYR   A 1 28  ? -3.28935  -0.29082  85.68029  1.000 21.26650 ? 28   TYR   A OH  1 
ATOM   163  N  N   . LEU   A 1 29  ? 1.70877   -3.41570  88.65012  1.000 21.26223 ? 29   LEU   A N   1 
ATOM   164  C  CA  . LEU   A 1 29  ? 1.62977   -2.52047  89.79290  1.000 22.55981 ? 29   LEU   A CA  1 
ATOM   165  C  C   . LEU   A 1 29  ? 2.99012   -1.88887  90.09569  1.000 27.03098 ? 29   LEU   A C   1 
ATOM   166  O  O   . LEU   A 1 29  ? 3.07932   -0.69975  90.41515  1.000 23.34955 ? 29   LEU   A O   1 
ATOM   167  C  CB  . LEU   A 1 29  ? 1.08626   -3.27845  91.01808  1.000 20.47898 ? 29   LEU   A CB  1 
ATOM   168  C  CG  . LEU   A 1 29  ? -0.42970  -3.52750  91.08358  1.000 22.74315 ? 29   LEU   A CG  1 
ATOM   169  C  CD1 . LEU   A 1 29  ? -0.74906  -4.36285  92.30632  1.000 22.12199 ? 29   LEU   A CD1 1 
ATOM   170  C  CD2 . LEU   A 1 29  ? -1.20819  -2.20632  91.14263  1.000 22.59750 ? 29   LEU   A CD2 1 
ATOM   171  N  N   . GLN   A 1 30  ? 4.06404   -2.65752  90.00467  1.000 20.84979 ? 30   GLN   A N   1 
ATOM   172  C  CA  . GLN   A 1 30  ? 5.35259   -2.06264  90.34934  1.000 24.98988 ? 30   GLN   A CA  1 
ATOM   173  C  C   . GLN   A 1 30  ? 5.84500   -1.09471  89.26594  1.000 27.86287 ? 30   GLN   A C   1 
ATOM   174  O  O   . GLN   A 1 30  ? 6.58816   -0.16704  89.58083  1.000 26.30000 ? 30   GLN   A O   1 
ATOM   175  C  CB  . GLN   A 1 30  ? 6.36046   -3.16513  90.64746  1.000 30.66072 ? 30   GLN   A CB  1 
ATOM   176  C  CG  . GLN   A 1 30  ? 6.70993   -3.98738  89.48499  1.000 40.91629 ? 30   GLN   A CG  1 
ATOM   177  C  CD  . GLN   A 1 30  ? 7.93705   -3.46556  88.82865  1.000 50.83066 ? 30   GLN   A CD  1 
ATOM   178  O  OE1 . GLN   A 1 30  ? 8.87986   -3.07842  89.51651  1.000 43.66636 ? 30   GLN   A OE1 1 
ATOM   179  N  NE2 . GLN   A 1 30  ? 7.93636   -3.41595  87.49193  1.000 32.40694 ? 30   GLN   A NE2 1 
ATOM   180  N  N   . CYS   A 1 31  ? 5.41408   -1.27628  88.00869  1.000 24.02315 ? 31   CYS   A N   1 
ATOM   181  C  CA  . CYS   A 1 31  ? 5.68573   -0.30849  86.93305  1.000 22.74457 ? 31   CYS   A CA  1 
ATOM   182  C  C   . CYS   A 1 31  ? 5.06538   1.04697   87.22583  1.000 27.03564 ? 31   CYS   A C   1 
ATOM   183  O  O   . CYS   A 1 31  ? 5.62706   2.08430   86.85803  1.000 24.24141 ? 31   CYS   A O   1 
ATOM   184  C  CB  . CYS   A 1 31  ? 5.10729   -0.80691  85.58639  1.000 20.81190 ? 31   CYS   A CB  1 
ATOM   185  S  SG  . CYS   A 1 31  ? 6.11776   -2.01115  84.76020  1.000 32.90069 ? 31   CYS   A SG  1 
ATOM   186  N  N   . MET   A 1 32  ? 3.84145   1.05499   87.76653  1.000 19.27516 ? 32   MET   A N   1 
ATOM   187  C  CA  . MET   A 1 32  ? 3.04380   2.27460   87.82427  1.000 23.19160 ? 32   MET   A CA  1 
ATOM   188  C  C   . MET   A 1 32  ? 3.10250   2.96967   89.17967  1.000 23.53848 ? 32   MET   A C   1 
ATOM   189  O  O   . MET   A 1 32  ? 2.66589   4.12805   89.28668  1.000 25.17524 ? 32   MET   A O   1 
ATOM   190  C  CB  . MET   A 1 32  ? 1.56682   1.95578   87.46265  1.000 24.26742 ? 32   MET   A CB  1 
ATOM   191  C  CG  . MET   A 1 32  ? 1.36376   1.56408   85.99054  1.000 27.13376 ? 32   MET   A CG  1 
ATOM   192  S  SD  . MET   A 1 32  ? 2.08219   2.77554   84.86833  1.000 29.36014 ? 32   MET   A SD  1 
ATOM   193  C  CE  . MET   A 1 32  ? 1.04826   4.20917   85.17711  1.000 26.08102 ? 32   MET   A CE  1 
ATOM   194  N  N   . ARG   A 1 33  ? 3.62045   2.30111   90.21965  1.000 20.67159 ? 33   ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 33  ? 3.54877   2.87574   91.56177  1.000 23.73220 ? 33   ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 33  ? 4.09562   4.30106   91.60406  1.000 25.08527 ? 33   ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 33  ? 3.47369   5.19831   92.18395  1.000 31.47991 ? 33   ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 33  ? 4.30367   1.99807   92.55775  1.000 31.24088 ? 33   ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 33  ? 4.10535   2.48591   93.98055  1.000 33.97299 ? 33   ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 33  ? 5.22356   2.06632   94.89987  1.000 44.94846 ? 33   ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 33  ? 4.98885   0.74588   95.45751  1.000 47.08088 ? 33   ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 33  ? 4.36231   0.51703   96.60274  1.000 52.55329 ? 33   ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 33  ? 3.87617   1.50647   97.33799  1.000 52.25035 ? 33   ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 33  ? 4.20855   -0.73676  97.01337  1.000 48.16979 ? 33   ARG   A NH2 1 
ATOM   205  N  N   . HIS   A 1 34  ? 5.25864   4.53549   90.99410  1.000 28.27315 ? 34   HIS   A N   1 
ATOM   206  C  CA  . HIS   A 1 34  ? 5.89512   5.84783   91.09424  1.000 27.36622 ? 34   HIS   A CA  1 
ATOM   207  C  C   . HIS   A 1 34  ? 5.35176   6.84857   90.08176  1.000 26.53293 ? 34   HIS   A C   1 
ATOM   208  O  O   . HIS   A 1 34  ? 5.78982   8.00291   90.07138  1.000 27.58920 ? 34   HIS   A O   1 
ATOM   209  C  CB  . HIS   A 1 34  ? 7.41603   5.70686   90.93744  1.000 25.35513 ? 34   HIS   A CB  1 
ATOM   210  C  CG  . HIS   A 1 34  ? 7.82033   5.03204   89.66324  1.000 26.23809 ? 34   HIS   A CG  1 
ATOM   211  N  ND1 . HIS   A 1 34  ? 7.67086   3.67593   89.45843  1.000 24.72396 ? 34   HIS   A ND1 1 
ATOM   212  C  CD2 . HIS   A 1 34  ? 8.33698   5.53345   88.51790  1.000 27.10746 ? 34   HIS   A CD2 1 
ATOM   213  C  CE1 . HIS   A 1 34  ? 8.08883   3.37307   88.24111  1.000 30.48398 ? 34   HIS   A CE1 1 
ATOM   214  N  NE2 . HIS   A 1 34  ? 8.50077   4.48121   87.65141  1.000 24.12420 ? 34   HIS   A NE2 1 
ATOM   215  N  N   . LEU   A 1 35  ? 4.39620   6.45268   89.25059  1.000 22.14005 ? 35   LEU   A N   1 
ATOM   216  C  CA  . LEU   A 1 35  ? 3.85500   7.31321   88.20598  1.000 29.61631 ? 35   LEU   A CA  1 
ATOM   217  C  C   . LEU   A 1 35  ? 2.41715   7.76241   88.46899  1.000 32.42323 ? 35   LEU   A C   1 
ATOM   218  O  O   . LEU   A 1 35  ? 1.81283   8.42385   87.60797  1.000 30.11091 ? 35   LEU   A O   1 
ATOM   219  C  CB  . LEU   A 1 35  ? 3.91955   6.58871   86.86816  1.000 24.53055 ? 35   LEU   A CB  1 
ATOM   220  C  CG  . LEU   A 1 35  ? 5.30140   6.11331   86.39314  1.000 24.58223 ? 35   LEU   A CG  1 
ATOM   221  C  CD1 . LEU   A 1 35  ? 5.10858   5.28924   85.12462  1.000 22.62729 ? 35   LEU   A CD1 1 
ATOM   222  C  CD2 . LEU   A 1 35  ? 6.15963   7.31697   86.10542  1.000 25.81432 ? 35   LEU   A CD2 1 
ATOM   223  N  N   . VAL   A 1 36  ? 1.84361   7.38628   89.60899  1.000 32.05270 ? 36   VAL   A N   1 
ATOM   224  C  CA  . VAL   A 1 36  ? 0.50486   7.79692   90.01621  1.000 33.27720 ? 36   VAL   A CA  1 
ATOM   225  C  C   . VAL   A 1 36  ? 0.59303   8.26297   91.46244  1.000 30.16143 ? 36   VAL   A C   1 
ATOM   226  O  O   . VAL   A 1 36  ? 1.57758   8.01370   92.16141  1.000 34.81647 ? 36   VAL   A O   1 
ATOM   227  C  CB  . VAL   A 1 36  ? -0.54067  6.66449   89.87958  1.000 34.89092 ? 36   VAL   A CB  1 
ATOM   228  C  CG1 . VAL   A 1 36  ? -0.63447  6.19269   88.46509  1.000 27.58526 ? 36   VAL   A CG1 1 
ATOM   229  C  CG2 . VAL   A 1 36  ? -0.18654  5.49369   90.80044  1.000 24.11071 ? 36   VAL   A CG2 1 
ATOM   230  N  N   . SER   A 1 37  ? -0.46552  8.93436   91.91723  1.000 39.25898 ? 37   SER   A N   1 
ATOM   231  C  CA  . SER   A 1 37  ? -0.48009  9.41623   93.28582  1.000 31.56267 ? 37   SER   A CA  1 
ATOM   232  C  C   . SER   A 1 37  ? -0.62095  8.24249   94.25817  1.000 40.57345 ? 37   SER   A C   1 
ATOM   233  O  O   . SER   A 1 37  ? -1.04875  7.15159   93.89205  1.000 30.76241 ? 37   SER   A O   1 
ATOM   234  C  CB  . SER   A 1 37  ? -1.62204  10.41992  93.49304  1.000 36.93118 ? 37   SER   A CB  1 
ATOM   235  O  OG  . SER   A 1 37  ? -2.87547  9.77122   93.63413  1.000 36.29150 ? 37   SER   A OG  1 
ATOM   236  N  N   . GLU   A 1 38  ? -0.25545  8.47397   95.51970  1.000 31.63378 ? 38   GLU   A N   1 
ATOM   237  C  CA  . GLU   A 1 38  ? -0.34187  7.39072   96.49703  1.000 35.06236 ? 38   GLU   A CA  1 
ATOM   238  C  C   . GLU   A 1 38  ? -1.78536  6.94424   96.69802  1.000 31.06660 ? 38   GLU   A C   1 
ATOM   239  O  O   . GLU   A 1 38  ? -2.05517  5.75795   96.91140  1.000 37.70246 ? 38   GLU   A O   1 
ATOM   240  C  CB  . GLU   A 1 38  ? 0.27901   7.82481   97.82389  1.000 44.61717 ? 38   GLU   A CB  1 
ATOM   241  C  CG  . GLU   A 1 38  ? 1.68628   7.30093   98.02867  1.000 52.61040 ? 38   GLU   A CG  1 
ATOM   242  C  CD  . GLU   A 1 38  ? 2.60898   8.32873   98.64649  1.000 74.13410 ? 38   GLU   A CD  1 
ATOM   243  O  OE1 . GLU   A 1 38  ? 2.10921   9.37760   99.10400  1.000 87.03403 ? 38   GLU   A OE1 1 
ATOM   244  O  OE2 . GLU   A 1 38  ? 3.83517   8.09113   98.66767  1.000 75.71080 ? 38   GLU   A OE2 1 
ATOM   245  N  N   . GLU   A 1 39  ? -2.72707  7.88309   96.63830  1.000 36.65116 ? 39   GLU   A N   1 
ATOM   246  C  CA  . GLU   A 1 39  ? -4.13373  7.53827   96.81210  1.000 37.92708 ? 39   GLU   A CA  1 
ATOM   247  C  C   . GLU   A 1 39  ? -4.64186  6.72686   95.62685  1.000 41.72424 ? 39   GLU   A C   1 
ATOM   248  O  O   . GLU   A 1 39  ? -5.31333  5.70441   95.79791  1.000 33.95606 ? 39   GLU   A O   1 
ATOM   249  C  CB  . GLU   A 1 39  ? -4.94653  8.82030   96.99716  1.000 55.51963 ? 39   GLU   A CB  1 
ATOM   250  C  CG  . GLU   A 1 39  ? -6.43782  8.69792   96.75380  1.000 68.29715 ? 39   GLU   A CG  1 
ATOM   251  C  CD  . GLU   A 1 39  ? -7.12873  10.05742  96.78168  1.000 90.27995 ? 39   GLU   A CD  1 
ATOM   252  O  OE1 . GLU   A 1 39  ? -7.02750  10.75795  97.81380  1.000 91.53684 ? 39   GLU   A OE1 1 
ATOM   253  O  OE2 . GLU   A 1 39  ? -7.75166  10.43596  95.76499  1.000 83.90941 ? 39   GLU   A OE2 1 
ATOM   254  N  N   . GLN   A 1 40  ? -4.31350  7.15972   94.41252  1.000 31.93332 ? 40   GLN   A N   1 
ATOM   255  C  CA  . GLN   A 1 40  ? -4.68850  6.38979   93.23868  1.000 32.94405 ? 40   GLN   A CA  1 
ATOM   256  C  C   . GLN   A 1 40  ? -4.00831  5.02723   93.23860  1.000 26.26984 ? 40   GLN   A C   1 
ATOM   257  O  O   . GLN   A 1 40  ? -4.61364  4.02425   92.83684  1.000 29.06164 ? 40   GLN   A O   1 
ATOM   258  C  CB  . GLN   A 1 40  ? -4.34203  7.17369   91.97825  1.000 30.77515 ? 40   GLN   A CB  1 
ATOM   259  C  CG  . GLN   A 1 40  ? -4.84349  6.55000   90.70842  1.000 36.04798 ? 40   GLN   A CG  1 
ATOM   260  C  CD  . GLN   A 1 40  ? -4.51870  7.39560   89.49535  1.000 48.95071 ? 40   GLN   A CD  1 
ATOM   261  O  OE1 . GLN   A 1 40  ? -4.63731  8.62952   89.52018  1.000 42.33186 ? 40   GLN   A OE1 1 
ATOM   262  N  NE2 . GLN   A 1 40  ? -4.09779  6.73895   88.42630  1.000 34.56226 ? 40   GLN   A NE2 1 
ATOM   263  N  N   . PHE   A 1 41  ? -2.75146  4.95820   93.69355  1.000 29.25655 ? 41   PHE   A N   1 
ATOM   264  C  CA  . PHE   A 1 41  ? -2.09590  3.65643   93.70053  1.000 29.17299 ? 41   PHE   A CA  1 
ATOM   265  C  C   . PHE   A 1 41  ? -2.76684  2.71806   94.68505  1.000 30.24157 ? 41   PHE   A C   1 
ATOM   266  O  O   . PHE   A 1 41  ? -2.96918  1.54029   94.37927  1.000 27.01251 ? 41   PHE   A O   1 
ATOM   267  C  CB  . PHE   A 1 41  ? -0.62113  3.76666   94.02860  1.000 29.22916 ? 41   PHE   A CB  1 
ATOM   268  C  CG  . PHE   A 1 41  ? 0.09364   2.44244   93.97350  1.000 28.08183 ? 41   PHE   A CG  1 
ATOM   269  C  CD1 . PHE   A 1 41  ? 0.30845   1.80648   92.74977  1.000 32.67641 ? 41   PHE   A CD1 1 
ATOM   270  C  CD2 . PHE   A 1 41  ? 0.56620   1.84722   95.12458  1.000 33.00642 ? 41   PHE   A CD2 1 
ATOM   271  C  CE1 . PHE   A 1 41  ? 0.97976   0.57870   92.69066  1.000 33.40206 ? 41   PHE   A CE1 1 
ATOM   272  C  CE2 . PHE   A 1 41  ? 1.23447   0.63025   95.07563  1.000 37.86381 ? 41   PHE   A CE2 1 
ATOM   273  C  CZ  . PHE   A 1 41  ? 1.43198   -0.00878  93.85926  1.000 30.39162 ? 41   PHE   A CZ  1 
ATOM   274  N  N   . ARG   A 1 42  ? -3.14313  3.22353   95.86412  1.000 26.58057 ? 42   ARG   A N   1 
ATOM   275  C  CA  . ARG   A 1 42  ? -3.82669  2.36894   96.82580  1.000 30.79046 ? 42   ARG   A CA  1 
ATOM   276  C  C   . ARG   A 1 42  ? -5.10001  1.77993   96.22032  1.000 28.78408 ? 42   ARG   A C   1 
ATOM   277  O  O   . ARG   A 1 42  ? -5.40339  0.59486   96.42128  1.000 31.98534 ? 42   ARG   A O   1 
ATOM   278  C  CB  . ARG   A 1 42  ? -4.14095  3.16459   98.09594  1.000 36.29960 ? 42   ARG   A CB  1 
ATOM   279  C  CG  . ARG   A 1 42  ? -4.43917  2.32019   99.30435  1.000 47.31341 ? 42   ARG   A CG  1 
ATOM   280  C  CD  . ARG   A 1 42  ? -3.74233  2.88864   100.55458 1.000 74.80893 ? 42   ARG   A CD  1 
ATOM   281  N  NE  . ARG   A 1 42  ? -3.90151  4.33480   100.68551 1.000 62.23162 ? 42   ARG   A NE  1 
ATOM   282  C  CZ  . ARG   A 1 42  ? -2.90045  5.19915   100.81348 1.000 74.14472 ? 42   ARG   A CZ  1 
ATOM   283  N  NH1 . ARG   A 1 42  ? -1.64034  4.79668   100.87929 1.000 68.32365 ? 42   ARG   A NH1 1 
ATOM   284  N  NH2 . ARG   A 1 42  ? -3.17125  6.50093   100.88540 1.000 73.17128 ? 42   ARG   A NH2 1 
ATOM   285  N  N   . LYS   A 1 43  ? -5.84317  2.58838   95.45480  1.000 29.75938 ? 43   LYS   A N   1 
ATOM   286  C  CA  . LYS   A 1 43  ? -7.07310  2.10271   94.82057  1.000 26.02874 ? 43   LYS   A CA  1 
ATOM   287  C  C   . LYS   A 1 43  ? -6.75852  1.08113   93.74572  1.000 28.56659 ? 43   LYS   A C   1 
ATOM   288  O  O   . LYS   A 1 43  ? -7.46903  0.07944   93.60917  1.000 25.88899 ? 43   LYS   A O   1 
ATOM   289  C  CB  . LYS   A 1 43  ? -7.86153  3.26555   94.21307  1.000 29.66453 ? 43   LYS   A CB  1 
ATOM   290  C  CG  . LYS   A 1 43  ? -8.62063  4.12898   95.25274  1.000 39.68289 ? 43   LYS   A CG  1 
ATOM   291  C  CD  . LYS   A 1 43  ? -9.38250  5.28166   94.57052  1.000 59.67457 ? 43   LYS   A CD  1 
ATOM   292  C  CE  . LYS   A 1 43  ? -10.31794 6.02229   95.52744  1.000 68.22287 ? 43   LYS   A CE  1 
ATOM   293  N  NZ  . LYS   A 1 43  ? -9.62887  7.06431   96.34837  1.000 51.15465 ? 43   LYS   A NZ  1 
ATOM   294  N  N   . SER   A 1 44  ? -5.70040  1.32630   92.96799  1.000 24.16170 ? 44   SER   A N   1 
ATOM   295  C  CA  . SER   A 1 44  ? -5.29992  0.37137   91.93715  1.000 26.53526 ? 44   SER   A CA  1 
ATOM   296  C  C   . SER   A 1 44  ? -4.84897  -0.95439  92.53971  1.000 24.61217 ? 44   SER   A C   1 
ATOM   297  O  O   . SER   A 1 44  ? -5.13682  -2.02379  91.98163  1.000 22.99874 ? 44   SER   A O   1 
ATOM   298  C  CB  . SER   A 1 44  ? -4.20069  0.97819   91.07615  1.000 29.23845 ? 44   SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 44  ? -4.73275  2.02600   90.29334  1.000 26.07364 ? 44   SER   A OG  1 
ATOM   300  N  N   . GLN   A 1 45  ? -4.14109  -0.90922  93.67722  1.000 25.85315 ? 45   GLN   A N   1 
ATOM   301  C  CA  . GLN   A 1 45  ? -3.75348  -2.14722  94.33994  1.000 23.68185 ? 45   GLN   A CA  1 
ATOM   302  C  C   . GLN   A 1 45  ? -4.97194  -3.00575  94.67657  1.000 29.37158 ? 45   GLN   A C   1 
ATOM   303  O  O   . GLN   A 1 45  ? -4.94958  -4.22980  94.48316  1.000 28.19658 ? 45   GLN   A O   1 
ATOM   304  C  CB  . GLN   A 1 45  ? -2.97763  -1.84805  95.61941  1.000 26.77232 ? 45   GLN   A CB  1 
ATOM   305  C  CG  . GLN   A 1 45  ? -1.54096  -1.41918  95.48794  1.000 32.76818 ? 45   GLN   A CG  1 
ATOM   306  C  CD  . GLN   A 1 45  ? -0.96008  -1.09252  96.87162  1.000 35.57667 ? 45   GLN   A CD  1 
ATOM   307  O  OE1 . GLN   A 1 45  ? -1.54721  -0.32344  97.62914  1.000 43.34747 ? 45   GLN   A OE1 1 
ATOM   308  N  NE2 . GLN   A 1 45  ? 0.16802   -1.69228  97.20513  1.000 36.42639 ? 45   GLN   A NE2 1 
ATOM   309  N  N   . ALA   A 1 46  ? -6.04362  -2.38727  95.19212  1.000 25.40544 ? 46   ALA   A N   1 
ATOM   310  C  CA  . ALA   A 1 46  ? -7.23283  -3.16083  95.54505  1.000 25.52594 ? 46   ALA   A CA  1 
ATOM   311  C  C   . ALA   A 1 46  ? -7.96506  -3.64851  94.29932  1.000 27.44922 ? 46   ALA   A C   1 
ATOM   312  O  O   . ALA   A 1 46  ? -8.52133  -4.75261  94.28706  1.000 25.23718 ? 46   ALA   A O   1 
ATOM   313  C  CB  . ALA   A 1 46  ? -8.16635  -2.33501  96.41618  1.000 33.14735 ? 46   ALA   A CB  1 
ATOM   314  N  N   . ILE   A 1 47  ? -7.97809  -2.83923  93.23942  1.000 26.32902 ? 47   ILE   A N   1 
ATOM   315  C  CA  . ILE   A 1 47  ? -8.61642  -3.26535  92.00065  1.000 28.71591 ? 47   ILE   A CA  1 
ATOM   316  C  C   . ILE   A 1 47  ? -7.90988  -4.49468  91.44337  1.000 27.70630 ? 47   ILE   A C   1 
ATOM   317  O  O   . ILE   A 1 47  ? -8.54830  -5.49274  91.07518  1.000 24.20601 ? 47   ILE   A O   1 
ATOM   318  C  CB  . ILE   A 1 47  ? -8.64474  -2.10228  90.98789  1.000 24.24809 ? 47   ILE   A CB  1 
ATOM   319  C  CG1 . ILE   A 1 47  ? -9.74388  -1.09514  91.37772  1.000 26.62403 ? 47   ILE   A CG1 1 
ATOM   320  C  CG2 . ILE   A 1 47  ? -8.79389  -2.64453  89.57012  1.000 22.88481 ? 47   ILE   A CG2 1 
ATOM   321  C  CD1 . ILE   A 1 47  ? -9.70039  0.22472   90.60958  1.000 31.24936 ? 47   ILE   A CD1 1 
ATOM   322  N  N   . VAL   A 1 48  ? -6.57818  -4.44568  91.39462  1.000 23.50439 ? 48   VAL   A N   1 
ATOM   323  C  CA  . VAL   A 1 48  ? -5.79581  -5.54626  90.84286  1.000 27.03276 ? 48   VAL   A CA  1 
ATOM   324  C  C   . VAL   A 1 48  ? -5.95286  -6.79667  91.70583  1.000 24.47214 ? 48   VAL   A C   1 
ATOM   325  O  O   . VAL   A 1 48  ? -6.09254  -7.91568  91.19561  1.000 29.53702 ? 48   VAL   A O   1 
ATOM   326  C  CB  . VAL   A 1 48  ? -4.32418  -5.10887  90.71212  1.000 23.32643 ? 48   VAL   A CB  1 
ATOM   327  C  CG1 . VAL   A 1 48  ? -3.39799  -6.31118  90.47788  1.000 19.44970 ? 48   VAL   A CG1 1 
ATOM   328  C  CG2 . VAL   A 1 48  ? -4.18702  -4.08439  89.57290  1.000 25.91709 ? 48   VAL   A CG2 1 
ATOM   329  N  N   . GLN   A 1 49  ? -5.95766  -6.62009  93.02608  1.000 24.49473 ? 49   GLN   A N   1 
ATOM   330  C  CA  . GLN   A 1 49  ? -6.16259  -7.74993  93.92257  1.000 25.74101 ? 49   GLN   A CA  1 
ATOM   331  C  C   . GLN   A 1 49  ? -7.49084  -8.43539  93.63461  1.000 30.30586 ? 49   GLN   A C   1 
ATOM   332  O  O   . GLN   A 1 49  ? -7.57440  -9.66787  93.58165  1.000 27.16102 ? 49   GLN   A O   1 
ATOM   333  C  CB  . GLN   A 1 49  ? -6.10492  -7.27412  95.37784  1.000 33.06182 ? 49   GLN   A CB  1 
ATOM   334  C  CG  . GLN   A 1 49  ? -6.13237  -8.41210  96.39586  1.000 36.65717 ? 49   GLN   A CG  1 
ATOM   335  C  CD  . GLN   A 1 49  ? -7.52210  -8.97090  96.64079  1.000 49.43469 ? 49   GLN   A CD  1 
ATOM   336  O  OE1 . GLN   A 1 49  ? -7.69576  -10.18115 96.78606  1.000 62.82237 ? 49   GLN   A OE1 1 
ATOM   337  N  NE2 . GLN   A 1 49  ? -8.52410  -8.08971  96.68836  1.000 59.23900 ? 49   GLN   A NE2 1 
ATOM   338  N  N   . GLN   A 1 50  ? -8.55479  -7.65209  93.47918  1.000 29.65717 ? 50   GLN   A N   1 
ATOM   339  C  CA  . GLN   A 1 50  ? -9.84370  -8.26730  93.20338  1.000 26.89923 ? 50   GLN   A CA  1 
ATOM   340  C  C   . GLN   A 1 50  ? -9.82061  -8.94707  91.84165  1.000 30.95671 ? 50   GLN   A C   1 
ATOM   341  O  O   . GLN   A 1 50  ? -10.35892 -10.04599 91.67666  1.000 27.01158 ? 50   GLN   A O   1 
ATOM   342  C  CB  . GLN   A 1 50  ? -10.94887 -7.21289  93.28067  1.000 30.14584 ? 50   GLN   A CB  1 
ATOM   343  C  CG  . GLN   A 1 50  ? -12.33535 -7.77346  93.51157  1.000 38.96205 ? 50   GLN   A CG  1 
ATOM   344  C  CD  . GLN   A 1 50  ? -13.12130 -8.05985  92.23142  1.000 69.40913 ? 50   GLN   A CD  1 
ATOM   345  O  OE1 . GLN   A 1 50  ? -12.79719 -7.56128  91.14282  1.000 49.25304 ? 50   GLN   A OE1 1 
ATOM   346  N  NE2 . GLN   A 1 50  ? -14.17543 -8.86849  92.36509  1.000 53.56003 ? 50   GLN   A NE2 1 
ATOM   347  N  N   . PHE   A 1 51  ? -9.18738  -8.30922  90.85608  1.000 25.80390 ? 51   PHE   A N   1 
ATOM   348  C  CA  . PHE   A 1 51  ? -9.17480  -8.86335  89.50370  1.000 25.93203 ? 51   PHE   A CA  1 
ATOM   349  C  C   . PHE   A 1 51  ? -8.42403  -10.19576 89.44654  1.000 29.82087 ? 51   PHE   A C   1 
ATOM   350  O  O   . PHE   A 1 51  ? -8.87336  -11.14764 88.79225  1.000 27.57803 ? 51   PHE   A O   1 
ATOM   351  C  CB  . PHE   A 1 51  ? -8.56491  -7.83543  88.55763  1.000 27.01900 ? 51   PHE   A CB  1 
ATOM   352  C  CG  . PHE   A 1 51  ? -8.39081  -8.32102  87.14453  1.000 26.93184 ? 51   PHE   A CG  1 
ATOM   353  C  CD1 . PHE   A 1 51  ? -9.46165  -8.35262  86.27993  1.000 23.94879 ? 51   PHE   A CD1 1 
ATOM   354  C  CD2 . PHE   A 1 51  ? -7.13297  -8.69206  86.68201  1.000 28.36901 ? 51   PHE   A CD2 1 
ATOM   355  C  CE1 . PHE   A 1 51  ? -9.29614  -8.77274  84.95745  1.000 25.22213 ? 51   PHE   A CE1 1 
ATOM   356  C  CE2 . PHE   A 1 51  ? -6.94971  -9.11604  85.37874  1.000 30.16942 ? 51   PHE   A CE2 1 
ATOM   357  C  CZ  . PHE   A 1 51  ? -8.04600  -9.15925  84.51009  1.000 23.48752 ? 51   PHE   A CZ  1 
ATOM   358  N  N   . GLY   A 1 52  ? -7.29903  -10.29179 90.14437  1.000 23.80793 ? 52   GLY   A N   1 
ATOM   359  C  CA  . GLY   A 1 52  ? -6.47438  -11.47946 90.15173  1.000 26.28243 ? 52   GLY   A CA  1 
ATOM   360  C  C   . GLY   A 1 52  ? -6.72274  -12.46572 91.27955  1.000 25.70925 ? 52   GLY   A C   1 
ATOM   361  O  O   . GLY   A 1 52  ? -5.91199  -13.38080 91.44939  1.000 30.05021 ? 52   GLY   A O   1 
ATOM   362  N  N   . ALA   A 1 53  ? -7.80455  -12.31648 92.04995  1.000 29.16959 ? 53   ALA   A N   1 
ATOM   363  C  CA  . ALA   A 1 53  ? -8.08494  -13.19560 93.19553  1.000 24.38779 ? 53   ALA   A CA  1 
ATOM   364  C  C   . ALA   A 1 53  ? -8.35992  -14.63509 92.74267  1.000 29.58404 ? 53   ALA   A C   1 
ATOM   365  O  O   . ALA   A 1 53  ? -8.81079  -14.86559 91.61591  1.000 29.07384 ? 53   ALA   A O   1 
ATOM   366  C  CB  . ALA   A 1 53  ? -9.29830  -12.67964 93.97278  1.000 28.51163 ? 53   ALA   A CB  1 
ATOM   367  N  N   . PRO   A 1 54  ? -8.13329  -15.61982 93.61851  1.000 30.91082 ? 54   PRO   A N   1 
ATOM   368  C  CA  . PRO   A 1 54  ? -8.40747  -17.01277 93.23946  1.000 32.15433 ? 54   PRO   A CA  1 
ATOM   369  C  C   . PRO   A 1 54  ? -9.85674  -17.17996 92.80152  1.000 33.48178 ? 54   PRO   A C   1 
ATOM   370  O  O   . PRO   A 1 54  ? -10.78279 -16.73035 93.47669  1.000 31.83027 ? 54   PRO   A O   1 
ATOM   371  C  CB  . PRO   A 1 54  ? -8.10929  -17.79791 94.52297  1.000 31.33665 ? 54   PRO   A CB  1 
ATOM   372  C  CG  . PRO   A 1 54  ? -7.17447  -16.92947 95.29183  1.000 36.53862 ? 54   PRO   A CG  1 
ATOM   373  C  CD  . PRO   A 1 54  ? -7.61445  -15.52253 94.99693  1.000 38.31718 ? 54   PRO   A CD  1 
ATOM   374  N  N   . GLY   A 1 55  ? -10.05168 -17.81995 91.65295  1.000 32.37916 ? 55   GLY   A N   1 
ATOM   375  C  CA  . GLY   A 1 55  ? -11.40682 -17.99695 91.16901  1.000 30.87231 ? 55   GLY   A CA  1 
ATOM   376  C  C   . GLY   A 1 55  ? -12.08033 -16.73827 90.65518  1.000 39.14377 ? 55   GLY   A C   1 
ATOM   377  O  O   . GLY   A 1 55  ? -13.29713 -16.75060 90.44413  1.000 35.26884 ? 55   GLY   A O   1 
ATOM   378  N  N   . GLY   A 1 56  ? -11.32785 -15.65798 90.44531  1.000 34.58261 ? 56   GLY   A N   1 
ATOM   379  C  CA  . GLY   A 1 56  ? -11.87821 -14.39103 90.01026  1.000 30.57181 ? 56   GLY   A CA  1 
ATOM   380  C  C   . GLY   A 1 56  ? -11.83541 -14.22349 88.50073  1.000 35.29072 ? 56   GLY   A C   1 
ATOM   381  O  O   . GLY   A 1 56  ? -11.53779 -15.14742 87.74189  1.000 27.52295 ? 56   GLY   A O   1 
ATOM   382  N  N   . LEU   A 1 57  ? -12.13372 -13.00241 88.06489  1.000 31.24819 ? 57   LEU   A N   1 
ATOM   383  C  CA  . LEU   A 1 57  ? -12.27330 -12.74135 86.63562  1.000 29.21010 ? 57   LEU   A CA  1 
ATOM   384  C  C   . LEU   A 1 57  ? -10.94109 -12.88944 85.89403  1.000 27.14043 ? 57   LEU   A C   1 
ATOM   385  O  O   . LEU   A 1 57  ? -10.89007 -13.48618 84.80799  1.000 27.16486 ? 57   LEU   A O   1 
ATOM   386  C  CB  . LEU   A 1 57  ? -12.85381 -11.34411 86.42152  1.000 32.54876 ? 57   LEU   A CB  1 
ATOM   387  C  CG  . LEU   A 1 57  ? -12.94700 -10.88033 84.96849  1.000 37.10397 ? 57   LEU   A CG  1 
ATOM   388  C  CD1 . LEU   A 1 57  ? -13.83617 -11.81967 84.17589  1.000 32.85416 ? 57   LEU   A CD1 1 
ATOM   389  C  CD2 . LEU   A 1 57  ? -13.47038 -9.45500  84.90902  1.000 42.04197 ? 57   LEU   A CD2 1 
ATOM   390  N  N   . GLY   A 1 58  ? -9.86227  -12.32184 86.43886  1.000 24.79973 ? 58   GLY   A N   1 
ATOM   391  C  CA  . GLY   A 1 58  ? -8.54900  -12.48126 85.80344  1.000 21.91887 ? 58   GLY   A CA  1 
ATOM   392  C  C   . GLY   A 1 58  ? -8.21168  -13.92946 85.49695  1.000 24.90206 ? 58   GLY   A C   1 
ATOM   393  O  O   . GLY   A 1 58  ? -7.74486  -14.24863 84.40615  1.000 26.24234 ? 58   GLY   A O   1 
ATOM   394  N  N   . GLU   A 1 59  ? -8.46323  -14.83581 86.44706  1.000 25.05708 ? 59   GLU   A N   1 
ATOM   395  C  CA  . GLU   A 1 59  ? -8.17992  -16.25226 86.19787  1.000 26.88721 ? 59   GLU   A CA  1 
ATOM   396  C  C   . GLU   A 1 59  ? -9.06009  -16.81414 85.09464  1.000 26.86847 ? 59   GLU   A C   1 
ATOM   397  O  O   . GLU   A 1 59  ? -8.61553  -17.65315 84.30049  1.000 27.85718 ? 59   GLU   A O   1 
ATOM   398  C  CB  . GLU   A 1 59  ? -8.35555  -17.06626 87.48446  1.000 26.37739 ? 59   GLU   A CB  1 
ATOM   399  C  CG  . GLU   A 1 59  ? -7.16519  -16.79969 88.42640  1.000 23.13002 ? 59   GLU   A CG  1 
ATOM   400  C  CD  . GLU   A 1 59  ? -7.10221  -17.72128 89.61771  1.000 33.78099 ? 59   GLU   A CD  1 
ATOM   401  O  OE1 . GLU   A 1 59  ? -8.03710  -18.52889 89.81218  1.000 40.43943 ? 59   GLU   A OE1 1 
ATOM   402  O  OE2 . GLU   A 1 59  ? -6.11041  -17.60058 90.37751  1.000 38.22125 ? 59   GLU   A OE2 1 
ATOM   403  N  N   . THR   A 1 60  ? -10.31777 -16.38517 85.04108  1.000 27.43298 ? 60   THR   A N   1 
ATOM   404  C  CA  . THR   A 1 60  ? -11.20021 -16.81507 83.96066  1.000 28.02591 ? 60   THR   A CA  1 
ATOM   405  C  C   . THR   A 1 60  ? -10.68560 -16.32521 82.61431  1.000 26.14519 ? 60   THR   A C   1 
ATOM   406  O  O   . THR   A 1 60  ? -10.66644 -17.07506 81.63605  1.000 26.26828 ? 60   THR   A O   1 
ATOM   407  C  CB  . THR   A 1 60  ? -12.62162 -16.29260 84.21487  1.000 31.91425 ? 60   THR   A CB  1 
ATOM   408  O  OG1 . THR   A 1 60  ? -13.18704 -16.96363 85.35522  1.000 30.72996 ? 60   THR   A OG1 1 
ATOM   409  C  CG2 . THR   A 1 60  ? -13.50001 -16.50900 82.99570  1.000 32.57876 ? 60   THR   A CG2 1 
ATOM   410  N  N   . LEU   A 1 61  ? -10.26759 -15.06500 82.54667  1.000 20.48076 ? 61   LEU   A N   1 
ATOM   411  C  CA  . LEU   A 1 61  ? -9.75278  -14.51996 81.29011  1.000 26.84731 ? 61   LEU   A CA  1 
ATOM   412  C  C   . LEU   A 1 61  ? -8.44176  -15.17956 80.89849  1.000 24.98990 ? 61   LEU   A C   1 
ATOM   413  O  O   . LEU   A 1 61  ? -8.18790  -15.41096 79.71445  1.000 25.80899 ? 61   LEU   A O   1 
ATOM   414  C  CB  . LEU   A 1 61  ? -9.57135  -13.00710 81.40640  1.000 21.03487 ? 61   LEU   A CB  1 
ATOM   415  C  CG  . LEU   A 1 61  ? -10.89274 -12.25492 81.62195  1.000 25.32493 ? 61   LEU   A CG  1 
ATOM   416  C  CD1 . LEU   A 1 61  ? -10.61377 -10.81959 82.01174  1.000 23.06502 ? 61   LEU   A CD1 1 
ATOM   417  C  CD2 . LEU   A 1 61  ? -11.74366 -12.29521 80.36565  1.000 26.54598 ? 61   LEU   A CD2 1 
ATOM   418  N  N   . GLN   A 1 62  ? -7.58165  -15.45639 81.87858  1.000 23.45981 ? 62   GLN   A N   1 
ATOM   419  C  CA  . GLN   A 1 62  ? -6.33836  -16.15628 81.59307  1.000 19.48125 ? 62   GLN   A CA  1 
ATOM   420  C  C   . GLN   A 1 62  ? -6.60470  -17.53622 80.97085  1.000 30.27589 ? 62   GLN   A C   1 
ATOM   421  O  O   . GLN   A 1 62  ? -5.96184  -17.91341 79.98220  1.000 24.59721 ? 62   GLN   A O   1 
ATOM   422  C  CB  . GLN   A 1 62  ? -5.52556  -16.27218 82.88528  1.000 26.24108 ? 62   GLN   A CB  1 
ATOM   423  C  CG  . GLN   A 1 62  ? -4.21250  -17.01406 82.72432  1.000 28.24596 ? 62   GLN   A CG  1 
ATOM   424  C  CD  . GLN   A 1 62  ? -3.11979  -16.12051 82.19511  1.000 27.19789 ? 62   GLN   A CD  1 
ATOM   425  O  OE1 . GLN   A 1 62  ? -3.38539  -14.98776 81.80336  1.000 23.29450 ? 62   GLN   A OE1 1 
ATOM   426  N  NE2 . GLN   A 1 62  ? -1.87765  -16.61696 82.19021  1.000 24.27149 ? 62   GLN   A NE2 1 
ATOM   427  N  N   . GLN   A 1 63  ? -7.56369  -18.29976 81.51844  1.000 22.36315 ? 63   GLN   A N   1 
ATOM   428  C  CA  . GLN   A 1 63  ? -7.90659  -19.57527 80.88938  1.000 29.99257 ? 63   GLN   A CA  1 
ATOM   429  C  C   . GLN   A 1 63  ? -8.38793  -19.37503 79.45342  1.000 27.60083 ? 63   GLN   A C   1 
ATOM   430  O  O   . GLN   A 1 63  ? -8.00221  -20.12814 78.55210  1.000 25.84474 ? 63   GLN   A O   1 
ATOM   431  C  CB  . GLN   A 1 63  ? -8.95101  -20.32250 81.71371  1.000 34.88995 ? 63   GLN   A CB  1 
ATOM   432  C  CG  . GLN   A 1 63  ? -8.91450  -21.83424 81.47351  1.000 58.38019 ? 63   GLN   A CG  1 
ATOM   433  C  CD  . GLN   A 1 63  ? -7.49379  -22.41706 81.56643  1.000 68.44207 ? 63   GLN   A CD  1 
ATOM   434  O  OE1 . GLN   A 1 63  ? -6.79590  -22.24798 82.57384  1.000 46.99947 ? 63   GLN   A OE1 1 
ATOM   435  N  NE2 . GLN   A 1 63  ? -7.06048  -23.09308 80.50108  1.000 49.49149 ? 63   GLN   A NE2 1 
ATOM   436  N  N   . LYS   A 1 64  ? -9.19880  -18.34444 79.20845  1.000 25.87419 ? 64   LYS   A N   1 
ATOM   437  C  CA  . LYS   A 1 64  ? -9.62802  -18.07675 77.83896  1.000 23.05236 ? 64   LYS   A CA  1 
ATOM   438  C  C   . LYS   A 1 64  ? -8.44882  -17.70025 76.94800  1.000 29.42712 ? 64   LYS   A C   1 
ATOM   439  O  O   . LYS   A 1 64  ? -8.44041  -17.98950 75.74030  1.000 24.01172 ? 64   LYS   A O   1 
ATOM   440  C  CB  . LYS   A 1 64  ? -10.68207 -16.97211 77.85095  1.000 26.71939 ? 64   LYS   A CB  1 
ATOM   441  C  CG  . LYS   A 1 64  ? -12.08784 -17.48816 78.28012  1.000 35.51708 ? 64   LYS   A CG  1 
ATOM   442  C  CD  . LYS   A 1 64  ? -13.08817 -16.33780 78.31231  1.000 49.79426 ? 64   LYS   A CD  1 
ATOM   443  C  CE  . LYS   A 1 64  ? -14.42619 -16.75697 78.92408  1.000 47.81350 ? 64   LYS   A CE  1 
ATOM   444  N  NZ  . LYS   A 1 64  ? -15.21585 -17.70499 78.07238  1.000 45.26225 ? 64   LYS   A NZ  1 
ATOM   445  N  N   . LEU   A 1 65  ? -7.45523  -17.03442 77.51195  1.000 23.43980 ? 65   LEU   A N   1 
ATOM   446  C  CA  . LEU   A 1 65  ? -6.30956  -16.66900 76.70078  1.000 22.26057 ? 65   LEU   A CA  1 
ATOM   447  C  C   . LEU   A 1 65  ? -5.45576  -17.88895 76.36477  1.000 23.99408 ? 65   LEU   A C   1 
ATOM   448  O  O   . LEU   A 1 65  ? -4.89026  -17.96849 75.26633  1.000 23.90185 ? 65   LEU   A O   1 
ATOM   449  C  CB  . LEU   A 1 65  ? -5.50230  -15.61103 77.43219  1.000 19.79151 ? 65   LEU   A CB  1 
ATOM   450  C  CG  . LEU   A 1 65  ? -4.24614  -15.11237 76.74584  1.000 20.58605 ? 65   LEU   A CG  1 
ATOM   451  C  CD1 . LEU   A 1 65  ? -4.59982  -14.61127 75.35859  1.000 22.91708 ? 65   LEU   A CD1 1 
ATOM   452  C  CD2 . LEU   A 1 65  ? -3.65193  -14.01572 77.60593  1.000 18.12573 ? 65   LEU   A CD2 1 
ATOM   453  N  N   . LEU   A 1 66  ? -5.36643  -18.85337 77.27452  1.000 25.43092 ? 66   LEU   A N   1 
ATOM   454  C  CA  . LEU   A 1 66  ? -4.61275  -20.05949 76.95207  1.000 29.58697 ? 66   LEU   A CA  1 
ATOM   455  C  C   . LEU   A 1 66  ? -5.33364  -20.90445 75.90345  1.000 30.17832 ? 66   LEU   A C   1 
ATOM   456  O  O   . LEU   A 1 66  ? -4.67301  -21.57629 75.10214  1.000 26.31986 ? 66   LEU   A O   1 
ATOM   457  C  CB  . LEU   A 1 66  ? -4.34980  -20.87946 78.21867  1.000 24.82075 ? 66   LEU   A CB  1 
ATOM   458  C  CG  . LEU   A 1 66  ? -3.46934  -20.19927 79.26775  1.000 30.13122 ? 66   LEU   A CG  1 
ATOM   459  C  CD1 . LEU   A 1 66  ? -3.60911  -20.94428 80.55716  1.000 33.02010 ? 66   LEU   A CD1 1 
ATOM   460  C  CD2 . LEU   A 1 66  ? -2.01203  -20.16296 78.81974  1.000 28.47281 ? 66   LEU   A CD2 1 
ATOM   461  N  N   . GLU   A 1 67  ? -6.67516  -20.90389 75.89403  1.000 27.56062 ? 67   GLU   A N   1 
ATOM   462  C  CA  . GLU   A 1 67  ? -7.39326  -21.57354 74.80309  1.000 25.57584 ? 67   GLU   A CA  1 
ATOM   463  C  C   . GLU   A 1 67  ? -7.15553  -20.85001 73.48210  1.000 22.89427 ? 67   GLU   A C   1 
ATOM   464  O  O   . GLU   A 1 67  ? -7.02829  -21.49212 72.43360  1.000 26.83667 ? 67   GLU   A O   1 
ATOM   465  C  CB  . GLU   A 1 67  ? -8.89301  -21.65118 75.10125  1.000 29.79681 ? 67   GLU   A CB  1 
ATOM   466  C  CG  . GLU   A 1 67  ? -9.22652  -22.33989 76.42324  1.000 36.05618 ? 67   GLU   A CG  1 
ATOM   467  C  CD  . GLU   A 1 67  ? -10.63227 -22.01592 76.95903  1.000 59.30357 ? 67   GLU   A CD  1 
ATOM   468  O  OE1 . GLU   A 1 67  ? -11.39158 -21.25242 76.31663  1.000 45.58476 ? 67   GLU   A OE1 1 
ATOM   469  O  OE2 . GLU   A 1 67  ? -10.97331 -22.52438 78.04834  1.000 52.54791 ? 67   GLU   A OE2 1 
ATOM   470  N  N   . ARG   A 1 68  ? -7.10306  -19.51513 73.51511  1.000 25.66472 ? 68   ARG   A N   1 
ATOM   471  C  CA  . ARG   A 1 68  ? -6.81569  -18.74039 72.30898  1.000 25.02716 ? 68   ARG   A CA  1 
ATOM   472  C  C   . ARG   A 1 68  ? -5.41217  -19.01952 71.78653  1.000 24.21511 ? 68   ARG   A C   1 
ATOM   473  O  O   . ARG   A 1 68  ? -5.20156  -19.11034 70.57090  1.000 27.63875 ? 68   ARG   A O   1 
ATOM   474  C  CB  . ARG   A 1 68  ? -6.97444  -17.24447 72.58828  1.000 26.85341 ? 68   ARG   A CB  1 
ATOM   475  C  CG  . ARG   A 1 68  ? -6.80870  -16.35816 71.35259  1.000 28.17084 ? 68   ARG   A CG  1 
ATOM   476  C  CD  . ARG   A 1 68  ? -7.09407  -14.88624 71.64994  1.000 23.58002 ? 68   ARG   A CD  1 
ATOM   477  N  NE  . ARG   A 1 68  ? -6.99034  -14.02500 70.47123  1.000 21.51027 ? 68   ARG   A NE  1 
ATOM   478  C  CZ  . ARG   A 1 68  ? -7.99301  -13.81035 69.62765  1.000 28.63204 ? 68   ARG   A CZ  1 
ATOM   479  N  NH1 . ARG   A 1 68  ? -9.15453  -14.44877 69.74830  1.000 24.17283 ? 68   ARG   A NH1 1 
ATOM   480  N  NH2 . ARG   A 1 68  ? -7.83358  -12.93199 68.64353  1.000 28.31650 ? 68   ARG   A NH2 1 
ATOM   481  N  N   . GLN   A 1 69  ? -4.43009  -19.12696 72.68348  1.000 24.92335 ? 69   GLN   A N   1 
ATOM   482  C  CA  . GLN   A 1 69  ? -3.07865  -19.45197 72.24390  1.000 21.89465 ? 69   GLN   A CA  1 
ATOM   483  C  C   . GLN   A 1 69  ? -3.04545  -20.80670 71.53812  1.000 25.37055 ? 69   GLN   A C   1 
ATOM   484  O  O   . GLN   A 1 69  ? -2.31696  -20.98934 70.55432  1.000 29.08645 ? 69   GLN   A O   1 
ATOM   485  C  CB  . GLN   A 1 69  ? -2.12500  -19.44158 73.44538  1.000 24.04615 ? 69   GLN   A CB  1 
ATOM   486  C  CG  . GLN   A 1 69  ? -0.71319  -19.93197 73.12997  1.000 25.66601 ? 69   GLN   A CG  1 
ATOM   487  C  CD  . GLN   A 1 69  ? 0.08790   -20.22997 74.38755  1.000 29.58791 ? 69   GLN   A CD  1 
ATOM   488  O  OE1 . GLN   A 1 69  ? -0.38295  -20.90537 75.30184  1.000 27.57501 ? 69   GLN   A OE1 1 
ATOM   489  N  NE2 . GLN   A 1 69  ? 1.29122   -19.69965 74.44825  1.000 29.50914 ? 69   GLN   A NE2 1 
ATOM   490  N  N   . GLU   A 1 70  ? -3.84865  -21.76829 72.00702  1.000 26.51558 ? 70   GLU   A N   1 
ATOM   491  C  CA  . GLU   A 1 70  ? -3.80598  -23.08713 71.38357  1.000 24.62672 ? 70   GLU   A CA  1 
ATOM   492  C  C   . GLU   A 1 70  ? -4.44385  -23.06103 70.00036  1.000 34.80404 ? 70   GLU   A C   1 
ATOM   493  O  O   . GLU   A 1 70  ? -3.94789  -23.72929 69.09278  1.000 33.06586 ? 70   GLU   A O   1 
ATOM   494  C  CB  . GLU   A 1 70  ? -4.47697  -24.12381 72.28675  1.000 32.90791 ? 70   GLU   A CB  1 
ATOM   495  C  CG  . GLU   A 1 70  ? -4.54628  -25.52558 71.68174  1.000 47.16821 ? 70   GLU   A CG  1 
ATOM   496  C  CD  . GLU   A 1 70  ? -4.65413  -26.61036 72.73852  1.000 72.00223 ? 70   GLU   A CD  1 
ATOM   497  O  OE1 . GLU   A 1 70  ? -3.89749  -26.55332 73.73342  1.000 90.91580 ? 70   GLU   A OE1 1 
ATOM   498  O  OE2 . GLU   A 1 70  ? -5.49371  -27.52005 72.57832  1.000 83.72175 ? 70   GLU   A OE2 1 
ATOM   499  N  N   . LYS   A 1 71  ? -5.48706  -22.24379 69.80392  1.000 32.14512 ? 71   LYS   A N   1 
ATOM   500  C  CA  . LYS   A 1 71  ? -6.27309  -22.20301 68.56800  1.000 31.80094 ? 71   LYS   A CA  1 
ATOM   501  C  C   . LYS   A 1 71  ? -5.72318  -21.25373 67.51043  1.000 34.72373 ? 71   LYS   A C   1 
ATOM   502  O  O   . LYS   A 1 71  ? -6.18775  -21.29444 66.37012  1.000 32.70891 ? 71   LYS   A O   1 
ATOM   503  C  CB  . LYS   A 1 71  ? -7.72161  -21.77531 68.86092  1.000 36.08551 ? 71   LYS   A CB  1 
ATOM   504  C  CG  . LYS   A 1 71  ? -8.52362  -22.72330 69.75446  1.000 45.41733 ? 71   LYS   A CG  1 
ATOM   505  C  CD  . LYS   A 1 71  ? -9.75872  -23.22715 69.02865  1.000 61.50226 ? 71   LYS   A CD  1 
ATOM   506  C  CE  . LYS   A 1 71  ? -10.91086 -23.48485 69.98754  1.000 73.16658 ? 71   LYS   A CE  1 
ATOM   507  N  NZ  . LYS   A 1 71  ? -12.08485 -24.10979 69.29811  1.000 61.71819 ? 71   LYS   A NZ  1 
ATOM   508  N  N   . THR   A 1 72  ? -4.78459  -20.37621 67.85506  1.000 31.37752 ? 72   THR   A N   1 
ATOM   509  C  CA  . THR   A 1 72  ? -4.28632  -19.36045 66.94487  1.000 24.58811 ? 72   THR   A CA  1 
ATOM   510  C  C   . THR   A 1 72  ? -2.77988  -19.51613 66.81104  1.000 31.37549 ? 72   THR   A C   1 
ATOM   511  O  O   . THR   A 1 72  ? -2.12166  -20.01130 67.72365  1.000 27.30901 ? 72   THR   A O   1 
ATOM   512  C  CB  . THR   A 1 72  ? -4.59560  -17.92959 67.46391  1.000 29.93716 ? 72   THR   A CB  1 
ATOM   513  O  OG1 . THR   A 1 72  ? -3.89504  -17.71079 68.69956  1.000 29.12780 ? 72   THR   A OG1 1 
ATOM   514  C  CG2 . THR   A 1 72  ? -6.11825  -17.72389 67.68393  1.000 32.01993 ? 72   THR   A CG2 1 
ATOM   515  N  N   . ALA   A 1 73  ? -2.22907  -19.06171 65.68036  1.000 26.96288 ? 73   ALA   A N   1 
ATOM   516  C  CA  . ALA   A 1 73  ? -0.77228  -19.02879 65.56297  1.000 29.84441 ? 73   ALA   A CA  1 
ATOM   517  C  C   . ALA   A 1 73  ? -0.17043  -18.01989 66.53773  1.000 27.96996 ? 73   ALA   A C   1 
ATOM   518  O  O   . ALA   A 1 73  ? 0.88758   -18.26751 67.11693  1.000 24.62719 ? 73   ALA   A O   1 
ATOM   519  C  CB  . ALA   A 1 73  ? -0.35985  -18.69719 64.12778  1.000 31.99113 ? 73   ALA   A CB  1 
ATOM   520  N  N   . ASN   A 1 74  ? -0.84759  -16.89327 66.75143  1.000 21.13130 ? 74   ASN   A N   1 
ATOM   521  C  CA  . ASN   A 1 74  ? -0.36830  -15.84331 67.65476  1.000 22.79825 ? 74   ASN   A CA  1 
ATOM   522  C  C   . ASN   A 1 74  ? -1.58387  -15.20263 68.31665  1.000 26.90840 ? 74   ASN   A C   1 
ATOM   523  O  O   . ASN   A 1 74  ? -2.36750  -14.53292 67.63594  1.000 23.49765 ? 74   ASN   A O   1 
ATOM   524  C  CB  . ASN   A 1 74  ? 0.43655   -14.80448 66.86848  1.000 21.70719 ? 74   ASN   A CB  1 
ATOM   525  C  CG  . ASN   A 1 74  ? 0.95344   -13.66576 67.72759  1.000 23.60619 ? 74   ASN   A CG  1 
ATOM   526  O  OD1 . ASN   A 1 74  ? 0.24828   -13.13887 68.57930  1.000 22.16704 ? 74   ASN   A OD1 1 
ATOM   527  N  ND2 . ASN   A 1 74  ? 2.20253   -13.26834 67.48644  1.000 23.25883 ? 74   ASN   A ND2 1 
ATOM   528  N  N   . TRP   A 1 75  ? -1.72125  -15.36839 69.63624  1.000 19.45855 ? 75   TRP   A N   1 
ATOM   529  C  CA  . TRP   A 1 75  ? -2.93446  -14.92314 70.32518  1.000 23.10349 ? 75   TRP   A CA  1 
ATOM   530  C  C   . TRP   A 1 75  ? -3.10072  -13.40427 70.35889  1.000 23.59144 ? 75   TRP   A C   1 
ATOM   531  O  O   . TRP   A 1 75  ? -4.20159  -12.92839 70.65456  1.000 21.11467 ? 75   TRP   A O   1 
ATOM   532  C  CB  . TRP   A 1 75  ? -2.96591  -15.46418 71.76021  1.000 19.91823 ? 75   TRP   A CB  1 
ATOM   533  C  CG  . TRP   A 1 75  ? -1.69404  -15.23299 72.54480  1.000 22.78079 ? 75   TRP   A CG  1 
ATOM   534  C  CD1 . TRP   A 1 75  ? -0.63951  -16.10290 72.67963  1.000 22.90946 ? 75   TRP   A CD1 1 
ATOM   535  C  CD2 . TRP   A 1 75  ? -1.34942  -14.06555 73.31456  1.000 18.92120 ? 75   TRP   A CD2 1 
ATOM   536  N  NE1 . TRP   A 1 75  ? 0.33983   -15.53871 73.47103  1.000 20.37471 ? 75   TRP   A NE1 1 
ATOM   537  C  CE2 . TRP   A 1 75  ? -0.08303  -14.30123 73.88910  1.000 20.80614 ? 75   TRP   A CE2 1 
ATOM   538  C  CE3 . TRP   A 1 75  ? -1.98755  -12.84512 73.56465  1.000 18.84047 ? 75   TRP   A CE3 1 
ATOM   539  C  CZ2 . TRP   A 1 75  ? 0.57019   -13.35234 74.70000  1.000 21.36089 ? 75   TRP   A CZ2 1 
ATOM   540  C  CZ3 . TRP   A 1 75  ? -1.33745  -11.90320 74.38253  1.000 20.15801 ? 75   TRP   A CZ3 1 
ATOM   541  C  CH2 . TRP   A 1 75  ? -0.07275  -12.16910 74.93100  1.000 21.20791 ? 75   TRP   A CH2 1 
ATOM   542  N  N   . VAL   A 1 76  ? -2.06283  -12.61632 70.07437  1.000 19.60511 ? 76   VAL   A N   1 
ATOM   543  C  CA  . VAL   A 1 76  ? -2.20492  -11.16634 70.16510  1.000 18.25842 ? 76   VAL   A CA  1 
ATOM   544  C  C   . VAL   A 1 76  ? -2.32279  -10.48376 68.80763  1.000 25.56662 ? 76   VAL   A C   1 
ATOM   545  O  O   . VAL   A 1 76  ? -2.72602  -9.31395  68.76616  1.000 24.00638 ? 76   VAL   A O   1 
ATOM   546  C  CB  . VAL   A 1 76  ? -1.06495  -10.52840 70.99121  1.000 19.96191 ? 76   VAL   A CB  1 
ATOM   547  C  CG1 . VAL   A 1 76  ? 0.17011   -10.19908 70.13806  1.000 17.80168 ? 76   VAL   A CG1 1 
ATOM   548  C  CG2 . VAL   A 1 76  ? -1.58424  -9.27180  71.72450  1.000 18.05673 ? 76   VAL   A CG2 1 
ATOM   549  N  N   . SER   A 1 77  ? -2.03599  -11.18049 67.70020  1.000 21.46146 ? 77   SER   A N   1 
ATOM   550  C  CA  . SER   A 1 77  ? -1.93391  -10.52144 66.39742  1.000 23.24236 ? 77   SER   A CA  1 
ATOM   551  C  C   . SER   A 1 77  ? -3.14117  -9.63635  66.10409  1.000 20.50970 ? 77   SER   A C   1 
ATOM   552  O  O   . SER   A 1 77  ? -2.98154  -8.46683  65.74307  1.000 22.62881 ? 77   SER   A O   1 
ATOM   553  C  CB  . SER   A 1 77  ? -1.79352  -11.55767 65.28291  1.000 24.33574 ? 77   SER   A CB  1 
ATOM   554  O  OG  . SER   A 1 77  ? -0.54573  -12.22656 65.37747  1.000 23.41624 ? 77   SER   A OG  1 
ATOM   555  N  N   . GLU   A 1 78  ? -4.35138  -10.19761 66.19936  1.000 21.28212 ? 78   GLU   A N   1 
ATOM   556  C  CA  . GLU   A 1 78  ? -5.55460  -9.44587  65.81987  1.000 21.45542 ? 78   GLU   A CA  1 
ATOM   557  C  C   . GLU   A 1 78  ? -5.74975  -8.24287  66.73448  1.000 26.35352 ? 78   GLU   A C   1 
ATOM   558  O  O   . GLU   A 1 78  ? -5.95404  -7.11843  66.26687  1.000 21.16700 ? 78   GLU   A O   1 
ATOM   559  C  CB  . GLU   A 1 78  ? -6.78578  -10.35479 65.86017  1.000 27.39139 ? 78   GLU   A CB  1 
ATOM   560  C  CG  . GLU   A 1 78  ? -8.10575  -9.63886  65.52706  1.000 26.82729 ? 78   GLU   A CG  1 
ATOM   561  C  CD  . GLU   A 1 78  ? -9.32894  -10.53732 65.68334  1.000 37.75735 ? 78   GLU   A CD  1 
ATOM   562  O  OE1 . GLU   A 1 78  ? -9.21665  -11.62288 66.30096  1.000 39.60384 ? 78   GLU   A OE1 1 
ATOM   563  O  OE2 . GLU   A 1 78  ? -10.40846 -10.14734 65.19359  1.000 51.24017 ? 78   GLU   A OE2 1 
ATOM   564  N  N   . TYR   A 1 79  ? -5.66050  -8.46012  68.04979  1.000 22.16943 ? 79   TYR   A N   1 
ATOM   565  C  CA  . TYR   A 1 79  ? -5.86079  -7.36603  68.99566  1.000 23.16233 ? 79   TYR   A CA  1 
ATOM   566  C  C   . TYR   A 1 79  ? -4.81701  -6.28971  68.81832  1.000 19.54165 ? 79   TYR   A C   1 
ATOM   567  O  O   . TYR   A 1 79  ? -5.12012  -5.09624  68.92601  1.000 21.04433 ? 79   TYR   A O   1 
ATOM   568  C  CB  . TYR   A 1 79  ? -5.77068  -7.86481  70.43517  1.000 20.18019 ? 79   TYR   A CB  1 
ATOM   569  C  CG  . TYR   A 1 79  ? -6.73067  -8.94023  70.80037  1.000 21.18429 ? 79   TYR   A CG  1 
ATOM   570  C  CD1 . TYR   A 1 79  ? -8.03961  -8.95159  70.30470  1.000 19.59479 ? 79   TYR   A CD1 1 
ATOM   571  C  CD2 . TYR   A 1 79  ? -6.34307  -9.94728  71.68186  1.000 23.04852 ? 79   TYR   A CD2 1 
ATOM   572  C  CE1 . TYR   A 1 79  ? -8.93778  -9.97113  70.67767  1.000 25.42179 ? 79   TYR   A CE1 1 
ATOM   573  C  CE2 . TYR   A 1 79  ? -7.24471  -10.95909 72.05231  1.000 22.17575 ? 79   TYR   A CE2 1 
ATOM   574  C  CZ  . TYR   A 1 79  ? -8.51108  -10.94828 71.55268  1.000 23.67039 ? 79   TYR   A CZ  1 
ATOM   575  O  OH  . TYR   A 1 79  ? -9.34598  -11.96024 71.93105  1.000 25.83611 ? 79   TYR   A OH  1 
ATOM   576  N  N   . TRP   A 1 80  ? -3.56873  -6.69394  68.60445  1.000 17.87857 ? 80   TRP   A N   1 
ATOM   577  C  CA  . TRP   A 1 80  ? -2.48397  -5.72457  68.51008  1.000 21.11757 ? 80   TRP   A CA  1 
ATOM   578  C  C   . TRP   A 1 80  ? -2.58545  -4.89163  67.23600  1.000 20.11487 ? 80   TRP   A C   1 
ATOM   579  O  O   . TRP   A 1 80  ? -2.35455  -3.67841  67.25578  1.000 20.41780 ? 80   TRP   A O   1 
ATOM   580  C  CB  . TRP   A 1 80  ? -1.13943  -6.45726  68.57404  1.000 20.14883 ? 80   TRP   A CB  1 
ATOM   581  C  CG  . TRP   A 1 80  ? 0.02543   -5.54368  68.53576  1.000 21.52516 ? 80   TRP   A CG  1 
ATOM   582  C  CD1 . TRP   A 1 80  ? 0.58454   -4.88113  69.58151  1.000 22.77475 ? 80   TRP   A CD1 1 
ATOM   583  C  CD2 . TRP   A 1 80  ? 0.78248   -5.17264  67.36557  1.000 21.05409 ? 80   TRP   A CD2 1 
ATOM   584  N  NE1 . TRP   A 1 80  ? 1.64927   -4.12546  69.13988  1.000 21.07424 ? 80   TRP   A NE1 1 
ATOM   585  C  CE2 . TRP   A 1 80  ? 1.78474   -4.29330  67.78279  1.000 19.84063 ? 80   TRP   A CE2 1 
ATOM   586  C  CE3 . TRP   A 1 80  ? 0.69580   -5.51500  66.00667  1.000 26.31028 ? 80   TRP   A CE3 1 
ATOM   587  C  CZ2 . TRP   A 1 80  ? 2.70564   -3.72988  66.89009  1.000 23.63021 ? 80   TRP   A CZ2 1 
ATOM   588  C  CZ3 . TRP   A 1 80  ? 1.60845   -4.96970  65.12219  1.000 19.67155 ? 80   TRP   A CZ3 1 
ATOM   589  C  CH2 . TRP   A 1 80  ? 2.60451   -4.08928  65.56666  1.000 24.55002 ? 80   TRP   A CH2 1 
ATOM   590  N  N   . LEU   A 1 81  ? -2.89282  -5.53058  66.10941  1.000 17.98365 ? 81   LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 81  ? -3.03785  -4.78461  64.86648  1.000 19.70855 ? 81   LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 81  ? -4.13296  -3.72927  64.98955  1.000 23.04645 ? 81   LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 81  ? -3.95934  -2.57921  64.55550  1.000 22.63948 ? 81   LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 81  ? -3.36493  -5.75207  63.72425  1.000 19.82943 ? 81   LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 81  ? -3.67906  -5.14728  62.36297  1.000 26.43100 ? 81   LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 81  ? -2.47753  -4.41445  61.82074  1.000 30.26232 ? 81   LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 81  ? -4.12796  -6.24577  61.39356  1.000 32.14095 ? 81   LEU   A CD2 1 
ATOM   598  N  N   . ASN   A 1 82  ? -5.27350  -4.10911  65.57209  1.000 20.32313 ? 82   ASN   A N   1 
ATOM   599  C  CA  . ASN   A 1 82  ? -6.36242  -3.15783  65.75524  1.000 22.92686 ? 82   ASN   A CA  1 
ATOM   600  C  C   . ASN   A 1 82  ? -5.98443  -2.07561  66.76223  1.000 24.72597 ? 82   ASN   A C   1 
ATOM   601  O  O   . ASN   A 1 82  ? -6.21969  -0.88930  66.52594  1.000 22.07337 ? 82   ASN   A O   1 
ATOM   602  C  CB  . ASN   A 1 82  ? -7.62734  -3.88434  66.20700  1.000 21.89435 ? 82   ASN   A CB  1 
ATOM   603  C  CG  . ASN   A 1 82  ? -8.22321  -4.74086  65.11714  1.000 28.87301 ? 82   ASN   A CG  1 
ATOM   604  O  OD1 . ASN   A 1 82  ? -7.97083  -4.51097  63.92975  1.000 26.80607 ? 82   ASN   A OD1 1 
ATOM   605  N  ND2 . ASN   A 1 82  ? -9.04759  -5.71633  65.50679  1.000 26.77545 ? 82   ASN   A ND2 1 
ATOM   606  N  N   . ASP   A 1 83  ? -5.39802  -2.46407  67.89886  1.000 20.72316 ? 83   ASP   A N   1 
ATOM   607  C  CA  . ASP   A 1 83  ? -5.10910  -1.48223  68.94485  1.000 17.63035 ? 83   ASP   A CA  1 
ATOM   608  C  C   . ASP   A 1 83  ? -4.00232  -0.50273  68.53845  1.000 24.85706 ? 83   ASP   A C   1 
ATOM   609  O  O   . ASP   A 1 83  ? -4.08416  0.69977   68.82043  1.000 20.06805 ? 83   ASP   A O   1 
ATOM   610  C  CB  . ASP   A 1 83  ? -4.71665  -2.22072  70.22815  1.000 26.92609 ? 83   ASP   A CB  1 
ATOM   611  C  CG  . ASP   A 1 83  ? -4.58813  -1.28191  71.40896  1.000 33.20659 ? 83   ASP   A CG  1 
ATOM   612  O  OD1 . ASP   A 1 83  ? -5.62480  -0.78693  71.88645  1.000 25.38703 ? 83   ASP   A OD1 1 
ATOM   613  O  OD2 . ASP   A 1 83  ? -3.45722  -1.03833  71.84952  1.000 25.61496 ? 83   ASP   A OD2 1 
ATOM   614  N  N   . MET   A 1 84  ? -2.93265  -0.99747  67.92297  1.000 19.36070 ? 84   MET   A N   1 
ATOM   615  C  CA  . MET   A 1 84  ? -1.80875  -0.12678  67.58344  1.000 17.93127 ? 84   MET   A CA  1 
ATOM   616  C  C   . MET   A 1 84  ? -2.08563  0.71623   66.33120  1.000 22.94900 ? 84   MET   A C   1 
ATOM   617  O  O   . MET   A 1 84  ? -1.66133  1.87721   66.25701  1.000 24.10689 ? 84   MET   A O   1 
ATOM   618  C  CB  . MET   A 1 84  ? -0.56102  -0.99890  67.41389  1.000 18.92330 ? 84   MET   A CB  1 
ATOM   619  C  CG  . MET   A 1 84  ? 0.67279   -0.27502  66.92818  1.000 38.24216 ? 84   MET   A CG  1 
ATOM   620  S  SD  . MET   A 1 84  ? 1.20696   0.93274   68.14239  1.000 47.77047 ? 84   MET   A SD  1 
ATOM   621  C  CE  . MET   A 1 84  ? 1.13130   -0.10022  69.57208  1.000 21.43457 ? 84   MET   A CE  1 
ATOM   622  N  N   . TYR   A 1 85  ? -2.79366  0.16014   65.34049  1.000 19.96522 ? 85   TYR   A N   1 
ATOM   623  C  CA  . TYR   A 1 85  ? -2.96497  0.80623   64.03509  1.000 22.57839 ? 85   TYR   A CA  1 
ATOM   624  C  C   . TYR   A 1 85  ? -4.41504  1.00739   63.62191  1.000 19.95365 ? 85   TYR   A C   1 
ATOM   625  O  O   . TYR   A 1 85  ? -4.82055  2.14683   63.39821  1.000 22.70964 ? 85   TYR   A O   1 
ATOM   626  C  CB  . TYR   A 1 85  ? -2.28943  -0.01695  62.94261  1.000 24.35291 ? 85   TYR   A CB  1 
ATOM   627  C  CG  . TYR   A 1 85  ? -0.85187  -0.26906  63.21093  1.000 25.25772 ? 85   TYR   A CG  1 
ATOM   628  C  CD1 . TYR   A 1 85  ? 0.09211   0.70375   62.97423  1.000 31.86102 ? 85   TYR   A CD1 1 
ATOM   629  C  CD2 . TYR   A 1 85  ? -0.43290  -1.50221  63.67563  1.000 25.88816 ? 85   TYR   A CD2 1 
ATOM   630  C  CE1 . TYR   A 1 85  ? 1.40925   0.46293   63.21481  1.000 46.28882 ? 85   TYR   A CE1 1 
ATOM   631  C  CE2 . TYR   A 1 85  ? 0.87524   -1.74950  63.90592  1.000 25.97778 ? 85   TYR   A CE2 1 
ATOM   632  C  CZ  . TYR   A 1 85  ? 1.79570   -0.77961  63.67449  1.000 36.37295 ? 85   TYR   A CZ  1 
ATOM   633  O  OH  . TYR   A 1 85  ? 3.11499   -1.05854  63.92136  1.000 43.05313 ? 85   TYR   A OH  1 
ATOM   634  N  N   . LEU   A 1 86  ? -5.17532  -0.06857  63.38667  1.000 18.36112 ? 86   LEU   A N   1 
ATOM   635  C  CA  . LEU   A 1 86  ? -6.38655  0.08120   62.59104  1.000 22.61611 ? 86   LEU   A CA  1 
ATOM   636  C  C   . LEU   A 1 86  ? -7.45973  0.86956   63.32340  1.000 23.73716 ? 86   LEU   A C   1 
ATOM   637  O  O   . LEU   A 1 86  ? -8.31960  1.47230   62.67795  1.000 26.27746 ? 86   LEU   A O   1 
ATOM   638  C  CB  . LEU   A 1 86  ? -6.91589  -1.29100  62.17712  1.000 30.42061 ? 86   LEU   A CB  1 
ATOM   639  C  CG  . LEU   A 1 86  ? -5.87158  -2.14137  61.44556  1.000 27.82713 ? 86   LEU   A CG  1 
ATOM   640  C  CD1 . LEU   A 1 86  ? -6.57042  -3.39560  60.93174  1.000 26.41234 ? 86   LEU   A CD1 1 
ATOM   641  C  CD2 . LEU   A 1 86  ? -5.17825  -1.36497  60.29964  1.000 29.50769 ? 86   LEU   A CD2 1 
ATOM   642  N  N   . ASN   A 1 87  ? -7.44806  0.87633   64.66495  1.000 23.10110 ? 87   ASN   A N   1 
ATOM   643  C  CA  . ASN   A 1 87  ? -8.42722  1.69588   65.38037  1.000 21.72313 ? 87   ASN   A CA  1 
ATOM   644  C  C   . ASN   A 1 87  ? -8.02377  3.16367   65.44876  1.000 24.69386 ? 87   ASN   A C   1 
ATOM   645  O  O   . ASN   A 1 87  ? -8.86729  4.01274   65.74708  1.000 24.33656 ? 87   ASN   A O   1 
ATOM   646  C  CB  . ASN   A 1 87  ? -8.63533  1.17341   66.81655  1.000 27.07547 ? 87   ASN   A CB  1 
ATOM   647  C  CG  . ASN   A 1 87  ? -9.36356  -0.16251  66.85821  1.000 28.92542 ? 87   ASN   A CG  1 
ATOM   648  O  OD1 . ASN   A 1 87  ? -10.01691 -0.55703  65.88347  1.000 28.94697 ? 87   ASN   A OD1 1 
ATOM   649  N  ND2 . ASN   A 1 87  ? -9.26747  -0.86157  67.99489  1.000 29.26871 ? 87   ASN   A ND2 1 
ATOM   650  N  N   . ASN   A 1 88  ? -6.75832  3.47816   65.18485  1.000 20.91597 ? 88   ASN   A N   1 
ATOM   651  C  CA  . ASN   A 1 88  ? -6.25357  4.82734   65.36442  1.000 22.72580 ? 88   ASN   A CA  1 
ATOM   652  C  C   . ASN   A 1 88  ? -6.86072  5.73696   64.29764  1.000 20.89777 ? 88   ASN   A C   1 
ATOM   653  O  O   . ASN   A 1 88  ? -6.75332  5.45597   63.10378  1.000 26.55895 ? 88   ASN   A O   1 
ATOM   654  C  CB  . ASN   A 1 88  ? -4.72081  4.81049   65.28507  1.000 21.59706 ? 88   ASN   A CB  1 
ATOM   655  C  CG  . ASN   A 1 88  ? -4.09207  6.15896   65.61946  1.000 27.34891 ? 88   ASN   A CG  1 
ATOM   656  O  OD1 . ASN   A 1 88  ? -4.78119  7.16851   65.75658  1.000 30.24412 ? 88   ASN   A OD1 1 
ATOM   657  N  ND2 . ASN   A 1 88  ? -2.76456  6.18139   65.72615  1.000 31.13274 ? 88   ASN   A ND2 1 
ATOM   658  N  N   . ARG   A 1 89  ? -7.52832  6.80539   64.72274  1.000 19.14572 ? 89   ARG   A N   1 
ATOM   659  C  CA  . ARG   A 1 89  ? -8.24062  7.67559   63.79124  1.000 18.90527 ? 89   ARG   A CA  1 
ATOM   660  C  C   . ARG   A 1 89  ? -7.36790  8.79653   63.24997  1.000 22.97462 ? 89   ARG   A C   1 
ATOM   661  O  O   . ARG   A 1 89  ? -7.78394  9.49542   62.32683  1.000 22.36478 ? 89   ARG   A O   1 
ATOM   662  C  CB  . ARG   A 1 89  ? -9.48959  8.28737   64.47364  1.000 24.83756 ? 89   ARG   A CB  1 
ATOM   663  C  CG  . ARG   A 1 89  ? -10.45048 7.25183   65.11993  1.000 28.94852 ? 89   ARG   A CG  1 
ATOM   664  C  CD  . ARG   A 1 89  ? -11.20719 6.47078   64.03323  1.000 29.06577 ? 89   ARG   A CD  1 
ATOM   665  N  NE  . ARG   A 1 89  ? -10.37153 5.45665   63.39887  1.000 27.45641 ? 89   ARG   A NE  1 
ATOM   666  C  CZ  . ARG   A 1 89  ? -10.54741 4.98669   62.16677  1.000 28.76485 ? 89   ARG   A CZ  1 
ATOM   667  N  NH1 . ARG   A 1 89  ? -11.47542 5.48282   61.34916  1.000 26.69224 ? 89   ARG   A NH1 1 
ATOM   668  N  NH2 . ARG   A 1 89  ? -9.77277  3.99778   61.74112  1.000 29.63330 ? 89   ARG   A NH2 1 
ATOM   669  N  N   . LEU   A 1 90  ? -6.18685  9.01210   63.81549  1.000 23.88105 ? 90   LEU   A N   1 
ATOM   670  C  CA  . LEU   A 1 90  ? -5.37034  10.14653  63.39303  1.000 23.29020 ? 90   LEU   A CA  1 
ATOM   671  C  C   . LEU   A 1 90  ? -4.86839  9.95115   61.96818  1.000 20.29515 ? 90   LEU   A C   1 
ATOM   672  O  O   . LEU   A 1 90  ? -4.64741  8.82253   61.51009  1.000 23.82804 ? 90   LEU   A O   1 
ATOM   673  C  CB  . LEU   A 1 90  ? -4.17194  10.30693  64.32917  1.000 21.42938 ? 90   LEU   A CB  1 
ATOM   674  C  CG  . LEU   A 1 90  ? -4.48421  10.80240  65.75727  1.000 24.72810 ? 90   LEU   A CG  1 
ATOM   675  C  CD1 . LEU   A 1 90  ? -3.24579  10.64919  66.62549  1.000 26.35036 ? 90   LEU   A CD1 1 
ATOM   676  C  CD2 . LEU   A 1 90  ? -4.93029  12.23254  65.74405  1.000 30.48325 ? 90   LEU   A CD2 1 
ATOM   677  N  N   . ALA   A 1 91  ? -4.65522  11.06269  61.27860  1.000 17.19124 ? 91   ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 91  ? -4.09263  11.00031  59.93369  1.000 20.58053 ? 91   ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 91  ? -2.73229  10.31076  59.96910  1.000 22.61293 ? 91   ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 91  ? -1.94620  10.52539  60.89181  1.000 23.43300 ? 91   ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 91  ? -3.95610  12.41393  59.36795  1.000 20.29507 ? 91   ALA   A CB  1 
ATOM   682  N  N   . LEU   A 1 92  ? -2.43365  9.52762   58.92909  1.000 20.86601 ? 92   LEU   A N   1 
ATOM   683  C  CA  . LEU   A 1 92  ? -1.17209  8.78565   58.90062  1.000 18.09184 ? 92   LEU   A CA  1 
ATOM   684  C  C   . LEU   A 1 92  ? 0.08874   9.65319   58.88292  1.000 22.86198 ? 92   LEU   A C   1 
ATOM   685  O  O   . LEU   A 1 92  ? 1.03725   9.30540   59.60383  1.000 21.78712 ? 92   LEU   A O   1 
ATOM   686  C  CB  . LEU   A 1 92  ? -1.17402  7.81201   57.71313  1.000 18.87867 ? 92   LEU   A CB  1 
ATOM   687  C  CG  . LEU   A 1 92  ? -2.28866  6.75761   57.72875  1.000 20.81142 ? 92   LEU   A CG  1 
ATOM   688  C  CD1 . LEU   A 1 92  ? -2.19341  5.80840   56.51210  1.000 21.11356 ? 92   LEU   A CD1 1 
ATOM   689  C  CD2 . LEU   A 1 92  ? -2.22560  5.96609   59.01925  1.000 22.66408 ? 92   LEU   A CD2 1 
ATOM   690  N  N   . PRO   A 1 93  ? 0.19330   10.74445  58.11579  1.000 22.34710 ? 93   PRO   A N   1 
ATOM   691  C  CA  . PRO   A 1 93  ? 1.43742   11.52261  58.13411  1.000 18.84843 ? 93   PRO   A CA  1 
ATOM   692  C  C   . PRO   A 1 93  ? 1.74204   12.00613  59.53887  1.000 21.55997 ? 93   PRO   A C   1 
ATOM   693  O  O   . PRO   A 1 93  ? 0.86882   12.54579  60.21150  1.000 19.47054 ? 93   PRO   A O   1 
ATOM   694  C  CB  . PRO   A 1 93  ? 1.13646   12.71037  57.20661  1.000 20.47657 ? 93   PRO   A CB  1 
ATOM   695  C  CG  . PRO   A 1 93  ? 0.03130   12.25027  56.34074  1.000 25.36771 ? 93   PRO   A CG  1 
ATOM   696  C  CD  . PRO   A 1 93  ? -0.77928  11.30721  57.15943  1.000 20.00717 ? 93   PRO   A CD  1 
ATOM   697  N  N   . VAL   A 1 94  ? 2.99951   11.81661  59.95882  1.000 24.08236 ? 94   VAL   A N   1 
ATOM   698  C  CA  . VAL   A 1 94  ? 3.57047   12.29717  61.22766  1.000 20.95382 ? 94   VAL   A CA  1 
ATOM   699  C  C   . VAL   A 1 94  ? 3.04194   11.46284  62.38310  1.000 24.45057 ? 94   VAL   A C   1 
ATOM   700  O  O   . VAL   A 1 94  ? 3.83084   10.91284  63.15759  1.000 22.49153 ? 94   VAL   A O   1 
ATOM   701  C  CB  . VAL   A 1 94  ? 3.32865   13.79857  61.47529  1.000 18.94736 ? 94   VAL   A CB  1 
ATOM   702  C  CG1 . VAL   A 1 94  ? 3.80988   14.19461  62.90675  1.000 18.05076 ? 94   VAL   A CG1 1 
ATOM   703  C  CG2 . VAL   A 1 94  ? 4.07564   14.66809  60.41281  1.000 17.93376 ? 94   VAL   A CG2 1 
ATOM   704  N  N   . ASN   A 1 95  ? 1.71511   11.32106  62.49199  1.000 19.96728 ? 95   ASN   A N   1 
ATOM   705  C  CA  . ASN   A 1 95  ? 1.15484   10.57682  63.62653  1.000 20.44052 ? 95   ASN   A CA  1 
ATOM   706  C  C   . ASN   A 1 95  ? 1.48975   9.09366   63.57297  1.000 19.59237 ? 95   ASN   A C   1 
ATOM   707  O  O   . ASN   A 1 95  ? 1.58818   8.44392   64.62231  1.000 24.10750 ? 95   ASN   A O   1 
ATOM   708  C  CB  . ASN   A 1 95  ? -0.37494  10.73595  63.69635  1.000 17.69292 ? 95   ASN   A CB  1 
ATOM   709  C  CG  . ASN   A 1 95  ? -0.80187  12.16283  63.84830  1.000 21.97183 ? 95   ASN   A CG  1 
ATOM   710  O  OD1 . ASN   A 1 95  ? -0.47765  12.82948  64.85042  1.000 20.55566 ? 95   ASN   A OD1 1 
ATOM   711  N  ND2 . ASN   A 1 95  ? -1.54537  12.66016  62.86209  1.000 19.38903 ? 95   ASN   A ND2 1 
ATOM   712  N  N   . SER   A 1 96  ? 1.63630   8.52352   62.37923  1.000 20.28623 ? 96   SER   A N   1 
ATOM   713  C  CA  . SER   A 1 96  ? 1.72135   7.07172   62.28617  1.000 23.19712 ? 96   SER   A CA  1 
ATOM   714  C  C   . SER   A 1 96  ? 2.87465   6.58068   61.41325  1.000 22.79213 ? 96   SER   A C   1 
ATOM   715  O  O   . SER   A 1 96  ? 3.64992   5.71295   61.82602  1.000 20.81691 ? 96   SER   A O   1 
ATOM   716  C  CB  . SER   A 1 96  ? 0.41177   6.52431   61.72484  1.000 22.25908 ? 96   SER   A CB  1 
ATOM   717  O  OG  . SER   A 1 96  ? 0.41700   5.09199   61.75641  1.000 23.87130 ? 96   SER   A OG  1 
ATOM   718  N  N   . SER   A 1 97  ? 2.96037   7.08800   60.18319  1.000 17.78542 ? 97   SER   A N   1 
ATOM   719  C  CA  . SER   A 1 97  ? 3.85515   6.54536   59.15900  1.000 17.43255 ? 97   SER   A CA  1 
ATOM   720  C  C   . SER   A 1 97  ? 5.28827   7.02142   59.34207  1.000 17.38354 ? 97   SER   A C   1 
ATOM   721  O  O   . SER   A 1 97  ? 5.57543   8.20440   59.09724  1.000 20.32531 ? 97   SER   A O   1 
ATOM   722  C  CB  . SER   A 1 97  ? 3.35552   6.95300   57.76115  1.000 20.24038 ? 97   SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 97  ? 2.15556   6.27849   57.44008  1.000 19.53684 ? 97   SER   A OG  1 
ATOM   724  N  N   A PRO   A 1 98  ? 6.21328   6.15882   59.75642  0.214 19.58626 ? 98   PRO   A N   1 
ATOM   725  N  N   B PRO   A 1 98  ? 6.21469   6.14977   59.75497  0.786 19.60053 ? 98   PRO   A N   1 
ATOM   726  C  CA  A PRO   A 1 98  ? 7.60701   6.59149   59.89768  0.214 15.47280 ? 98   PRO   A CA  1 
ATOM   727  C  CA  B PRO   A 1 98  ? 7.61517   6.57060   59.87984  0.786 15.16497 ? 98   PRO   A CA  1 
ATOM   728  C  C   A PRO   A 1 98  ? 8.24820   6.85966   58.54570  0.214 20.28435 ? 98   PRO   A C   1 
ATOM   729  C  C   B PRO   A 1 98  ? 8.22939   6.88569   58.52818  0.786 20.31273 ? 98   PRO   A C   1 
ATOM   730  O  O   A PRO   A 1 98  ? 7.84525   6.32421   57.51018  0.214 19.94765 ? 98   PRO   A O   1 
ATOM   731  O  O   B PRO   A 1 98  ? 7.80146   6.39610   57.47795  0.786 19.97232 ? 98   PRO   A O   1 
ATOM   732  C  CB  A PRO   A 1 98  ? 8.27714   5.40912   60.60067  0.214 20.79828 ? 98   PRO   A CB  1 
ATOM   733  C  CB  B PRO   A 1 98  ? 8.30524   5.36105   60.52014  0.786 20.79243 ? 98   PRO   A CB  1 
ATOM   734  C  CG  A PRO   A 1 98  ? 7.45134   4.24101   60.20045  0.214 21.96528 ? 98   PRO   A CG  1 
ATOM   735  C  CG  B PRO   A 1 98  ? 7.18538   4.57299   61.14741  0.786 23.24350 ? 98   PRO   A CG  1 
ATOM   736  C  CD  A PRO   A 1 98  ? 6.03892   4.73568   60.09991  0.214 21.52733 ? 98   PRO   A CD  1 
ATOM   737  C  CD  B PRO   A 1 98  ? 6.03053   4.74911   60.18736  0.786 21.55995 ? 98   PRO   A CD  1 
ATOM   738  N  N   . ALA   A 1 99  ? 9.27091   7.70787   58.57037  1.000 18.10833 ? 99   ALA   A N   1 
ATOM   739  C  CA  . ALA   A 1 99  ? 10.03927  8.04523   57.38238  1.000 19.91316 ? 99   ALA   A CA  1 
ATOM   740  C  C   . ALA   A 1 99  ? 11.45189  7.50651   57.56222  1.000 24.94468 ? 99   ALA   A C   1 
ATOM   741  O  O   . ALA   A 1 99  ? 12.00915  7.53579   58.66925  1.000 21.33349 ? 99   ALA   A O   1 
ATOM   742  C  CB  . ALA   A 1 99  ? 10.05186  9.56153   57.14563  1.000 24.19408 ? 99   ALA   A CB  1 
ATOM   743  N  N   . VAL   A 1 100 ? 12.00931  6.98392   56.47940  1.000 22.45810 ? 100  VAL   A N   1 
ATOM   744  C  CA  . VAL   A 1 100 ? 13.40824  6.58021   56.40815  1.000 21.58547 ? 100  VAL   A CA  1 
ATOM   745  C  C   . VAL   A 1 100 ? 14.07492  7.44458   55.35697  1.000 20.94200 ? 100  VAL   A C   1 
ATOM   746  O  O   . VAL   A 1 100 ? 13.64120  7.45423   54.19947  1.000 25.00758 ? 100  VAL   A O   1 
ATOM   747  C  CB  . VAL   A 1 100 ? 13.55218  5.09964   56.03593  1.000 26.58153 ? 100  VAL   A CB  1 
ATOM   748  C  CG1 . VAL   A 1 100 ? 15.05444  4.73867   55.94447  1.000 25.83210 ? 100  VAL   A CG1 1 
ATOM   749  C  CG2 . VAL   A 1 100 ? 12.77093  4.24321   57.03469  1.000 27.67417 ? 100  VAL   A CG2 1 
ATOM   750  N  N   . ILE   A 1 101 ? 15.11918  8.15841   55.74834  1.000 19.08764 ? 101  ILE   A N   1 
ATOM   751  C  CA  . ILE   A 1 101 ? 15.77968  9.12442   54.88630  1.000 20.38350 ? 101  ILE   A CA  1 
ATOM   752  C  C   . ILE   A 1 101 ? 17.08887  8.50176   54.40768  1.000 26.11279 ? 101  ILE   A C   1 
ATOM   753  O  O   . ILE   A 1 101 ? 17.89835  8.04251   55.22590  1.000 24.41218 ? 101  ILE   A O   1 
ATOM   754  C  CB  . ILE   A 1 101 ? 16.03929  10.44928  55.63179  1.000 23.26403 ? 101  ILE   A CB  1 
ATOM   755  C  CG1 . ILE   A 1 101 ? 14.71902  11.15773  56.01161  1.000 25.76514 ? 101  ILE   A CG1 1 
ATOM   756  C  CG2 . ILE   A 1 101 ? 16.96154  11.33739  54.77665  1.000 26.41396 ? 101  ILE   A CG2 1 
ATOM   757  C  CD1 . ILE   A 1 101 ? 13.92520  10.53260  57.16818  1.000 24.37219 ? 101  ILE   A CD1 1 
ATOM   758  N  N   . PHE   A 1 102 ? 17.30278  8.48238   53.09807  1.000 23.61642 ? 102  PHE   A N   1 
ATOM   759  C  CA  . PHE   A 1 102 ? 18.53700  7.89935   52.58529  1.000 26.48667 ? 102  PHE   A CA  1 
ATOM   760  C  C   . PHE   A 1 102 ? 19.63771  8.94220   52.57839  1.000 34.72005 ? 102  PHE   A C   1 
ATOM   761  O  O   . PHE   A 1 102 ? 19.40919  10.13219  52.82580  1.000 34.65546 ? 102  PHE   A O   1 
ATOM   762  C  CB  . PHE   A 1 102 ? 18.36935  7.35823   51.15664  1.000 25.90452 ? 102  PHE   A CB  1 
ATOM   763  C  CG  . PHE   A 1 102 ? 17.30819  6.31881   51.01485  1.000 24.18850 ? 102  PHE   A CG  1 
ATOM   764  C  CD1 . PHE   A 1 102 ? 16.88307  5.57994   52.11038  1.000 24.12891 ? 102  PHE   A CD1 1 
ATOM   765  C  CD2 . PHE   A 1 102 ? 16.71235  6.09067   49.78118  1.000 26.24964 ? 102  PHE   A CD2 1 
ATOM   766  C  CE1 . PHE   A 1 102 ? 15.89088  4.63691   51.98445  1.000 29.52205 ? 102  PHE   A CE1 1 
ATOM   767  C  CE2 . PHE   A 1 102 ? 15.71302  5.14072   49.65083  1.000 26.16316 ? 102  PHE   A CE2 1 
ATOM   768  C  CZ  . PHE   A 1 102 ? 15.29853  4.41635   50.74539  1.000 27.89950 ? 102  PHE   A CZ  1 
ATOM   769  N  N   . ALA   A 1 103 ? 20.84549  8.48422   52.24105  1.000 39.34027 ? 103  ALA   A N   1 
ATOM   770  C  CA  . ALA   A 1 103 ? 21.95911  9.39599   52.03126  1.000 45.13374 ? 103  ALA   A CA  1 
ATOM   771  C  C   . ALA   A 1 103 ? 21.57451  10.48881  51.04287  1.000 44.81726 ? 103  ALA   A C   1 
ATOM   772  O  O   . ALA   A 1 103 ? 20.76891  10.28547  50.12810  1.000 44.72149 ? 103  ALA   A O   1 
ATOM   773  C  CB  . ALA   A 1 103 ? 23.17966  8.63349   51.52282  1.000 49.48289 ? 103  ALA   A CB  1 
ATOM   774  N  N   . ARG   A 1 104 ? 22.12511  11.67206  51.26638  1.000 40.56917 ? 104  ARG   A N   1 
ATOM   775  C  CA  . ARG   A 1 104 ? 21.91739  12.79019  50.36426  1.000 47.52417 ? 104  ARG   A CA  1 
ATOM   776  C  C   . ARG   A 1 104 ? 22.41554  12.41712  48.97379  1.000 47.75044 ? 104  ARG   A C   1 
ATOM   777  O  O   . ARG   A 1 104 ? 23.47954  11.81292  48.83310  1.000 43.29905 ? 104  ARG   A O   1 
ATOM   778  C  CB  . ARG   A 1 104 ? 22.66916  14.01375  50.89605  1.000 48.56004 ? 104  ARG   A CB  1 
ATOM   779  C  CG  . ARG   A 1 104 ? 22.35831  15.33839  50.20857  1.000 60.41632 ? 104  ARG   A CG  1 
ATOM   780  C  CD  . ARG   A 1 104 ? 23.22888  16.47873  50.77692  1.000 74.72654 ? 104  ARG   A CD  1 
ATOM   781  N  NE  . ARG   A 1 104 ? 22.77037  16.95481  52.08168  1.000 59.57275 ? 104  ARG   A NE  1 
ATOM   782  C  CZ  . ARG   A 1 104 ? 23.18185  16.47957  53.25142  1.000 64.63385 ? 104  ARG   A CZ  1 
ATOM   783  N  NH1 . ARG   A 1 104 ? 24.07313  15.50468  53.32940  1.000 75.11493 ? 104  ARG   A NH1 1 
ATOM   784  N  NH2 . ARG   A 1 104 ? 22.68455  16.99405  54.37313  1.000 50.37437 ? 104  ARG   A NH2 1 
ATOM   785  N  N   . GLN   A 1 105 ? 21.63425  12.74705  47.94861  1.000 40.71928 ? 105  GLN   A N   1 
ATOM   786  C  CA  . GLN   A 1 105 ? 22.01208  12.46727  46.56854  1.000 44.67541 ? 105  GLN   A CA  1 
ATOM   787  C  C   . GLN   A 1 105 ? 22.21575  13.77586  45.82219  1.000 39.72097 ? 105  GLN   A C   1 
ATOM   788  O  O   . GLN   A 1 105 ? 21.71306  14.82601  46.22506  1.000 45.20211 ? 105  GLN   A O   1 
ATOM   789  C  CB  . GLN   A 1 105 ? 20.94325  11.62707  45.84879  1.000 37.63582 ? 105  GLN   A CB  1 
ATOM   790  C  CG  . GLN   A 1 105 ? 20.65212  10.26740  46.47456  1.000 37.71029 ? 105  GLN   A CG  1 
ATOM   791  C  CD  . GLN   A 1 105 ? 21.87507  9.37576   46.52566  1.000 43.65183 ? 105  GLN   A CD  1 
ATOM   792  O  OE1 . GLN   A 1 105 ? 22.70129  9.38704   45.61709  1.000 44.08252 ? 105  GLN   A OE1 1 
ATOM   793  N  NE2 . GLN   A 1 105 ? 22.00415  8.61164   47.60262  1.000 47.26710 ? 105  GLN   A NE2 1 
ATOM   794  N  N   . HIS   A 1 106 ? 22.93209  13.71118  44.70226  1.000 41.40589 ? 106  HIS   A N   1 
ATOM   795  C  CA  . HIS   A 1 106 ? 23.14485  14.89704  43.88694  1.000 43.09390 ? 106  HIS   A CA  1 
ATOM   796  C  C   . HIS   A 1 106 ? 22.79935  14.57517  42.44330  1.000 46.94425 ? 106  HIS   A C   1 
ATOM   797  O  O   . HIS   A 1 106 ? 23.42896  13.70978  41.82814  1.000 45.98278 ? 106  HIS   A O   1 
ATOM   798  C  CB  . HIS   A 1 106 ? 24.57608  15.41973  44.01017  1.000 51.98843 ? 106  HIS   A CB  1 
ATOM   799  C  CG  . HIS   A 1 106 ? 24.85065  16.59286  43.12641  1.000 74.32756 ? 106  HIS   A CG  1 
ATOM   800  N  ND1 . HIS   A 1 106 ? 25.90181  16.62519  42.23453  1.000 77.41473 ? 106  HIS   A ND1 1 
ATOM   801  C  CD2 . HIS   A 1 106 ? 24.18816  17.76436  42.97229  1.000 72.38748 ? 106  HIS   A CD2 1 
ATOM   802  C  CE1 . HIS   A 1 106 ? 25.88396  17.77241  41.57969  1.000 71.30092 ? 106  HIS   A CE1 1 
ATOM   803  N  NE2 . HIS   A 1 106 ? 24.85353  18.48146  42.00770  1.000 70.72557 ? 106  HIS   A NE2 1 
ATOM   804  N  N   . PHE   A 1 107 ? 21.79367  15.26771  41.91604  1.000 48.79393 ? 107  PHE   A N   1 
ATOM   805  C  CA  . PHE   A 1 107 ? 21.28618  15.05064  40.56203  1.000 43.49181 ? 107  PHE   A CA  1 
ATOM   806  C  C   . PHE   A 1 107 ? 21.47978  16.33909  39.77360  1.000 44.13521 ? 107  PHE   A C   1 
ATOM   807  O  O   . PHE   A 1 107 ? 20.65110  17.26151  39.88136  1.000 47.22231 ? 107  PHE   A O   1 
ATOM   808  C  CB  . PHE   A 1 107 ? 19.80555  14.65612  40.58419  1.000 42.87454 ? 107  PHE   A CB  1 
ATOM   809  C  CG  . PHE   A 1 107 ? 19.49542  13.41139  41.39346  1.000 35.57902 ? 107  PHE   A CG  1 
ATOM   810  C  CD1 . PHE   A 1 107 ? 20.38056  12.34386  41.43280  1.000 42.82876 ? 107  PHE   A CD1 1 
ATOM   811  C  CD2 . PHE   A 1 107 ? 18.30331  13.31524  42.10908  1.000 33.59695 ? 107  PHE   A CD2 1 
ATOM   812  C  CE1 . PHE   A 1 107 ? 20.08706  11.20719  42.16584  1.000 40.82125 ? 107  PHE   A CE1 1 
ATOM   813  C  CE2 . PHE   A 1 107 ? 18.00011  12.17774  42.84461  1.000 36.32344 ? 107  PHE   A CE2 1 
ATOM   814  C  CZ  . PHE   A 1 107 ? 18.89772  11.12307  42.87875  1.000 41.01274 ? 107  PHE   A CZ  1 
ATOM   815  N  N   . PRO   A 1 108 ? 22.56065  16.46891  38.99480  1.000 52.95130 ? 108  PRO   A N   1 
ATOM   816  C  CA  . PRO   A 1 108 ? 22.72094  17.68255  38.16608  1.000 47.65860 ? 108  PRO   A CA  1 
ATOM   817  C  C   . PRO   A 1 108 ? 21.52392  17.95884  37.26771  1.000 56.59913 ? 108  PRO   A C   1 
ATOM   818  O  O   . PRO   A 1 108 ? 21.03845  19.09477  37.20869  1.000 48.50617 ? 108  PRO   A O   1 
ATOM   819  C  CB  . PRO   A 1 108 ? 23.99410  17.38032  37.36130  1.000 49.36656 ? 108  PRO   A CB  1 
ATOM   820  C  CG  . PRO   A 1 108 ? 24.77646  16.43890  38.23165  1.000 54.20048 ? 108  PRO   A CG  1 
ATOM   821  C  CD  . PRO   A 1 108 ? 23.74277  15.58748  38.93235  1.000 51.98696 ? 108  PRO   A CD  1 
ATOM   822  N  N   . GLY   A 1 109 ? 21.02101  16.93477  36.57330  1.000 55.33044 ? 109  GLY   A N   1 
ATOM   823  C  CA  . GLY   A 1 109 ? 19.87088  17.07053  35.71306  1.000 40.56629 ? 109  GLY   A CA  1 
ATOM   824  C  C   . GLY   A 1 109 ? 18.75435  16.10908  36.09778  1.000 43.11844 ? 109  GLY   A C   1 
ATOM   825  O  O   . GLY   A 1 109 ? 18.90893  15.22535  36.95352  1.000 41.57621 ? 109  GLY   A O   1 
ATOM   826  N  N   . THR   A 1 110 ? 17.61392  16.30206  35.43892  1.000 41.86734 ? 110  THR   A N   1 
ATOM   827  C  CA  . THR   A 1 110 ? 16.47223  15.42028  35.63641  1.000 43.55162 ? 110  THR   A CA  1 
ATOM   828  C  C   . THR   A 1 110 ? 16.82537  13.97541  35.31148  1.000 38.70635 ? 110  THR   A C   1 
ATOM   829  O  O   . THR   A 1 110 ? 16.36830  13.05437  35.99333  1.000 44.19833 ? 110  THR   A O   1 
ATOM   830  C  CB  . THR   A 1 110 ? 15.30550  15.90162  34.77540  1.000 44.25873 ? 110  THR   A CB  1 
ATOM   831  O  OG1 . THR   A 1 110 ? 14.97645  17.23849  35.15381  1.000 49.12350 ? 110  THR   A OG1 1 
ATOM   832  C  CG2 . THR   A 1 110 ? 14.08693  15.01548  34.97178  1.000 51.24097 ? 110  THR   A CG2 1 
ATOM   833  N  N   . ASP   A 1 111 ? 17.63402  13.75213  34.26593  1.000 43.76459 ? 111  ASP   A N   1 
ATOM   834  C  CA  . ASP   A 1 111 ? 17.97009  12.38302  33.88548  1.000 38.80028 ? 111  ASP   A CA  1 
ATOM   835  C  C   . ASP   A 1 111 ? 18.76946  11.67760  34.97268  1.000 43.22446 ? 111  ASP   A C   1 
ATOM   836  O  O   . ASP   A 1 111 ? 18.73297  10.44732  35.06675  1.000 46.70528 ? 111  ASP   A O   1 
ATOM   837  C  CB  . ASP   A 1 111 ? 18.73450  12.36075  32.55988  1.000 43.15296 ? 111  ASP   A CB  1 
ATOM   838  C  CG  . ASP   A 1 111 ? 17.85713  12.74532  31.37457  1.000 58.92831 ? 111  ASP   A CG  1 
ATOM   839  O  OD1 . ASP   A 1 111 ? 16.61209  12.65265  31.48943  1.000 56.38847 ? 111  ASP   A OD1 1 
ATOM   840  O  OD2 . ASP   A 1 111 ? 18.41122  13.13128  30.32736  1.000 58.80928 ? 111  ASP   A OD2 1 
ATOM   841  N  N   . ASP   A 1 112 ? 19.47748  12.42911  35.81513  1.000 41.08752 ? 112  ASP   A N   1 
ATOM   842  C  CA  . ASP   A 1 112 ? 20.14930  11.80609  36.95302  1.000 45.53963 ? 112  ASP   A CA  1 
ATOM   843  C  C   . ASP   A 1 112 ? 19.14164  11.35264  38.00045  1.000 40.44068 ? 112  ASP   A C   1 
ATOM   844  O  O   . ASP   A 1 112 ? 19.22852  10.23003  38.51324  1.000 41.51364 ? 112  ASP   A O   1 
ATOM   845  C  CB  . ASP   A 1 112 ? 21.16476  12.77666  37.54467  1.000 47.55352 ? 112  ASP   A CB  1 
ATOM   846  C  CG  . ASP   A 1 112 ? 22.18395  13.22715  36.51766  1.000 51.69492 ? 112  ASP   A CG  1 
ATOM   847  O  OD1 . ASP   A 1 112 ? 22.84611  12.34965  35.93725  1.000 47.53232 ? 112  ASP   A OD1 1 
ATOM   848  O  OD2 . ASP   A 1 112 ? 22.30017  14.44569  36.26760  1.000 50.56200 ? 112  ASP   A OD2 1 
ATOM   849  N  N   . GLN   A 1 113 ? 18.16838  12.20571  38.31688  1.000 37.09010 ? 113  GLN   A N   1 
ATOM   850  C  CA  . GLN   A 1 113 ? 17.05557  11.78963  39.16088  1.000 33.56150 ? 113  GLN   A CA  1 
ATOM   851  C  C   . GLN   A 1 113 ? 16.36529  10.55076  38.59202  1.000 39.09435 ? 113  GLN   A C   1 
ATOM   852  O  O   . GLN   A 1 113 ? 16.10382  9.57684   39.30832  1.000 35.14532 ? 113  GLN   A O   1 
ATOM   853  C  CB  . GLN   A 1 113 ? 16.06348  12.94730  39.28696  1.000 37.59561 ? 113  GLN   A CB  1 
ATOM   854  C  CG  . GLN   A 1 113 ? 14.83225  12.63798  40.13293  1.000 31.11781 ? 113  GLN   A CG  1 
ATOM   855  C  CD  . GLN   A 1 113 ? 13.68047  13.56033  39.82183  1.000 38.00326 ? 113  GLN   A CD  1 
ATOM   856  O  OE1 . GLN   A 1 113 ? 13.70412  14.27458  38.82361  1.000 40.44908 ? 113  GLN   A OE1 1 
ATOM   857  N  NE2 . GLN   A 1 113 ? 12.66683  13.55555  40.67775  1.000 34.30607 ? 113  GLN   A NE2 1 
ATOM   858  N  N   . LEU   A 1 114 ? 16.05964  10.57154  37.29822  1.000 35.15207 ? 114  LEU   A N   1 
ATOM   859  C  CA  . LEU   A 1 114 ? 15.33270  9.46190   36.69270  1.000 40.66757 ? 114  LEU   A CA  1 
ATOM   860  C  C   . LEU   A 1 114 ? 16.16907  8.18832   36.66226  1.000 41.03894 ? 114  LEU   A C   1 
ATOM   861  O  O   . LEU   A 1 114 ? 15.63296  7.08672   36.84662  1.000 38.66546 ? 114  LEU   A O   1 
ATOM   862  C  CB  . LEU   A 1 114 ? 14.87354  9.84579   35.28323  1.000 39.93715 ? 114  LEU   A CB  1 
ATOM   863  C  CG  . LEU   A 1 114 ? 13.85356  10.99029  35.26589  1.000 34.88078 ? 114  LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A 1 114 ? 13.18370  11.06813  33.88614  1.000 38.62452 ? 114  LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A 1 114 ? 12.81766  10.85834  36.38927  1.000 33.28902 ? 114  LEU   A CD2 1 
ATOM   866  N  N   . ARG   A 1 115 ? 17.48074  8.30790   36.44199  1.000 39.58128 ? 115  ARG   A N   1 
ATOM   867  C  CA  . ARG   A 1 115 ? 18.32555  7.11555   36.47775  1.000 35.98303 ? 115  ARG   A CA  1 
ATOM   868  C  C   . ARG   A 1 115 ? 18.36241  6.50424   37.87383  1.000 36.56283 ? 115  ARG   A C   1 
ATOM   869  O  O   . ARG   A 1 115 ? 18.41535  5.27459   38.02066  1.000 37.00772 ? 115  ARG   A O   1 
ATOM   870  C  CB  . ARG   A 1 115 ? 19.73883  7.44663   35.99157  1.000 38.60574 ? 115  ARG   A CB  1 
ATOM   871  C  CG  . ARG   A 1 115 ? 19.88830  7.32534   34.47388  1.000 38.53526 ? 115  ARG   A CG  1 
ATOM   872  C  CD  . ARG   A 1 115 ? 21.32355  7.46377   34.00141  1.000 50.66434 ? 115  ARG   A CD  1 
ATOM   873  N  NE  . ARG   A 1 115 ? 21.83075  8.81559   34.19090  1.000 50.22440 ? 115  ARG   A NE  1 
ATOM   874  C  CZ  . ARG   A 1 115 ? 21.81862  9.76787   33.26849  1.000 55.22120 ? 115  ARG   A CZ  1 
ATOM   875  N  NH1 . ARG   A 1 115 ? 21.36186  9.54381   32.04420  1.000 42.80257 ? 115  ARG   A NH1 1 
ATOM   876  N  NH2 . ARG   A 1 115 ? 22.27946  10.97637  33.58171  1.000 50.12651 ? 115  ARG   A NH2 1 
ATOM   877  N  N   . PHE   A 1 116 ? 18.34888  7.34453   38.90971  1.000 32.05880 ? 116  PHE   A N   1 
ATOM   878  C  CA  . PHE   A 1 116 ? 18.28673  6.83540   40.27188  1.000 30.63242 ? 116  PHE   A CA  1 
ATOM   879  C  C   . PHE   A 1 116 ? 16.96987  6.11298   40.51339  1.000 33.10234 ? 116  PHE   A C   1 
ATOM   880  O  O   . PHE   A 1 116 ? 16.94078  5.01284   41.07871  1.000 30.24769 ? 116  PHE   A O   1 
ATOM   881  C  CB  . PHE   A 1 116 ? 18.47080  7.99253   41.26231  1.000 34.85697 ? 116  PHE   A CB  1 
ATOM   882  C  CG  . PHE   A 1 116 ? 18.66912  7.54627   42.68883  1.000 31.73315 ? 116  PHE   A CG  1 
ATOM   883  C  CD1 . PHE   A 1 116 ? 17.58438  7.23516   43.48573  1.000 29.93385 ? 116  PHE   A CD1 1 
ATOM   884  C  CD2 . PHE   A 1 116 ? 19.94306  7.44440   43.22906  1.000 42.25081 ? 116  PHE   A CD2 1 
ATOM   885  C  CE1 . PHE   A 1 116 ? 17.76120  6.81723   44.79270  1.000 32.48901 ? 116  PHE   A CE1 1 
ATOM   886  C  CE2 . PHE   A 1 116 ? 20.12232  7.02581   44.53737  1.000 36.30323 ? 116  PHE   A CE2 1 
ATOM   887  C  CZ  . PHE   A 1 116 ? 19.03229  6.71153   45.30940  1.000 33.24845 ? 116  PHE   A CZ  1 
ATOM   888  N  N   . ALA   A 1 117 ? 15.86156  6.71998   40.09009  1.000 36.84018 ? 117  ALA   A N   1 
ATOM   889  C  CA  . ALA   A 1 117 ? 14.56081  6.09091   40.28284  1.000 28.78482 ? 117  ALA   A CA  1 
ATOM   890  C  C   . ALA   A 1 117 ? 14.45396  4.78995   39.48950  1.000 32.70678 ? 117  ALA   A C   1 
ATOM   891  O  O   . ALA   A 1 117 ? 13.85736  3.81703   39.95772  1.000 35.18310 ? 117  ALA   A O   1 
ATOM   892  C  CB  . ALA   A 1 117 ? 13.45777  7.07152   39.88627  1.000 32.84441 ? 117  ALA   A CB  1 
ATOM   893  N  N   . ALA   A 1 118 ? 15.02871  4.75581   38.28641  1.000 31.33330 ? 118  ALA   A N   1 
ATOM   894  C  CA  . ALA   A 1 118 ? 15.04263  3.52584   37.49641  1.000 35.98779 ? 118  ALA   A CA  1 
ATOM   895  C  C   . ALA   A 1 118 ? 15.85008  2.43881   38.19596  1.000 39.46006 ? 118  ALA   A C   1 
ATOM   896  O  O   . ALA   A 1 118 ? 15.41457  1.28522   38.29896  1.000 33.86710 ? 118  ALA   A O   1 
ATOM   897  C  CB  . ALA   A 1 118 ? 15.61581  3.81575   36.10747  1.000 34.54532 ? 118  ALA   A CB  1 
ATOM   898  N  N   . SER   A 1 119 ? 17.03672  2.79693   38.68536  1.000 40.10177 ? 119  SER   A N   1 
ATOM   899  C  CA  . SER   A 1 119 ? 17.86328  1.85213   39.42910  1.000 38.34384 ? 119  SER   A CA  1 
ATOM   900  C  C   . SER   A 1 119 ? 17.14954  1.35533   40.68175  1.000 36.44231 ? 119  SER   A C   1 
ATOM   901  O  O   . SER   A 1 119 ? 17.16681  0.15543   40.98009  1.000 34.29136 ? 119  SER   A O   1 
ATOM   902  C  CB  . SER   A 1 119 ? 19.19310  2.51954   39.78274  1.000 43.62178 ? 119  SER   A CB  1 
ATOM   903  O  OG  . SER   A 1 119 ? 19.99938  1.69401   40.58745  1.000 40.74779 ? 119  SER   A OG  1 
ATOM   904  N  N   . LEU   A 1 120 ? 16.51358  2.26266   41.42766  1.000 29.65756 ? 120  LEU   A N   1 
ATOM   905  C  CA  . LEU   A 1 120 ? 15.76740  1.87018   42.62068  1.000 31.16669 ? 120  LEU   A CA  1 
ATOM   906  C  C   . LEU   A 1 120 ? 14.65045  0.88412   42.28218  1.000 41.02590 ? 120  LEU   A C   1 
ATOM   907  O  O   . LEU   A 1 120 ? 14.46415  -0.12293  42.97523  1.000 34.69520 ? 120  LEU   A O   1 
ATOM   908  C  CB  . LEU   A 1 120 ? 15.19084  3.11583   43.30695  1.000 26.78970 ? 120  LEU   A CB  1 
ATOM   909  C  CG  . LEU   A 1 120 ? 14.38146  2.89095   44.59039  1.000 34.07402 ? 120  LEU   A CG  1 
ATOM   910  C  CD1 . LEU   A 1 120 ? 15.20084  2.09209   45.61173  1.000 36.66044 ? 120  LEU   A CD1 1 
ATOM   911  C  CD2 . LEU   A 1 120 ? 13.94217  4.21987   45.20741  1.000 31.21368 ? 120  LEU   A CD2 1 
ATOM   912  N  N   . ILE   A 1 121 ? 13.86616  1.17596   41.24108  1.000 32.91675 ? 121  ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 121 ? 12.75464  0.29083   40.89189  1.000 34.63214 ? 121  ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 121 ? 13.27907  -1.08238  40.50020  1.000 34.96411 ? 121  ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 121 ? 12.73833  -2.11825  40.91484  1.000 32.84267 ? 121  ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 121 ? 11.90481  0.90046   39.76682  1.000 35.49960 ? 121  ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 121 ? 11.11029  2.07873   40.29082  1.000 26.96691 ? 121  ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 121 ? 10.95070  -0.14611  39.18000  1.000 28.55285 ? 121  ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 121 ? 10.62569  3.00664   39.14998  1.000 29.47517 ? 121  ILE   A CD1 1 
ATOM   920  N  N   . SER   A 1 122 ? 14.36076  -1.11420  39.72965  1.000 36.37685 ? 122  SER   A N   1 
ATOM   921  C  CA  . SER   A 1 122 ? 14.96033  -2.39256  39.36940  1.000 36.45917 ? 122  SER   A CA  1 
ATOM   922  C  C   . SER   A 1 122 ? 15.38512  -3.17227  40.61115  1.000 36.79945 ? 122  SER   A C   1 
ATOM   923  O  O   . SER   A 1 122 ? 15.14426  -4.38195  40.70161  1.000 34.83490 ? 122  SER   A O   1 
ATOM   924  C  CB  . SER   A 1 122 ? 16.13846  -2.16127  38.41961  1.000 35.35758 ? 122  SER   A CB  1 
ATOM   925  O  OG  . SER   A 1 122 ? 16.82769  -3.36740  38.17200  1.000 54.88813 ? 122  SER   A OG  1 
ATOM   926  N  N   . GLY   A 1 123 ? 15.98935  -2.49364  41.59905  1.000 32.70891 ? 123  GLY   A N   1 
ATOM   927  C  CA  . GLY   A 1 123 ? 16.34673  -3.17296  42.83476  1.000 32.09075 ? 123  GLY   A CA  1 
ATOM   928  C  C   . GLY   A 1 123 ? 15.14194  -3.66173  43.62378  1.000 43.33280 ? 123  GLY   A C   1 
ATOM   929  O  O   . GLY   A 1 123 ? 15.21135  -4.69164  44.30290  1.000 31.85376 ? 123  GLY   A O   1 
ATOM   930  N  N   . VAL   A 1 124 ? 14.02778  -2.92994  43.55575  1.000 33.66103 ? 124  VAL   A N   1 
ATOM   931  C  CA  . VAL   A 1 124 ? 12.79406  -3.37317  44.19689  1.000 29.92914 ? 124  VAL   A CA  1 
ATOM   932  C  C   . VAL   A 1 124 ? 12.28975  -4.65079  43.54270  1.000 31.96819 ? 124  VAL   A C   1 
ATOM   933  O  O   . VAL   A 1 124 ? 11.89953  -5.60564  44.22799  1.000 33.05352 ? 124  VAL   A O   1 
ATOM   934  C  CB  . VAL   A 1 124 ? 11.73497  -2.24918  44.15260  1.000 35.63462 ? 124  VAL   A CB  1 
ATOM   935  C  CG1 . VAL   A 1 124 ? 10.32777  -2.81908  44.33037  1.000 32.27346 ? 124  VAL   A CG1 1 
ATOM   936  C  CG2 . VAL   A 1 124 ? 12.02749  -1.18548  45.22440  1.000 25.10737 ? 124  VAL   A CG2 1 
ATOM   937  N  N   . LEU   A 1 125 ? 12.31159  -4.69726  42.20872  1.000 30.90616 ? 125  LEU   A N   1 
ATOM   938  C  CA  . LEU   A 1 125 ? 11.90918  -5.90408  41.48811  1.000 38.23579 ? 125  LEU   A CA  1 
ATOM   939  C  C   . LEU   A 1 125 ? 12.80089  -7.09452  41.83256  1.000 41.47043 ? 125  LEU   A C   1 
ATOM   940  O  O   . LEU   A 1 125 ? 12.31003  -8.21914  41.97949  1.000 34.06491 ? 125  LEU   A O   1 
ATOM   941  C  CB  . LEU   A 1 125 ? 11.93374  -5.64193  39.98320  1.000 40.26712 ? 125  LEU   A CB  1 
ATOM   942  C  CG  . LEU   A 1 125 ? 10.97949  -4.54965  39.51517  1.000 43.67735 ? 125  LEU   A CG  1 
ATOM   943  C  CD1 . LEU   A 1 125 ? 11.10773  -4.33556  38.01121  1.000 46.51716 ? 125  LEU   A CD1 1 
ATOM   944  C  CD2 . LEU   A 1 125 ? 9.55177   -4.91519  39.91418  1.000 42.88577 ? 125  LEU   A CD2 1 
ATOM   945  N  N   . SER   A 1 126 ? 14.11363  -6.87042  41.95862  1.000 36.84406 ? 126  SER   A N   1 
ATOM   946  C  CA  . SER   A 1 126 ? 15.02702  -7.96099  42.30683  1.000 42.70162 ? 126  SER   A CA  1 
ATOM   947  C  C   . SER   A 1 126 ? 14.78725  -8.45080  43.72291  1.000 35.33711 ? 126  SER   A C   1 
ATOM   948  O  O   . SER   A 1 126 ? 14.76611  -9.66123  43.97899  1.000 36.03012 ? 126  SER   A O   1 
ATOM   949  C  CB  . SER   A 1 126 ? 16.47974  -7.50960  42.16488  1.000 42.15164 ? 126  SER   A CB  1 
ATOM   950  O  OG  . SER   A 1 126 ? 16.82679  -7.38764  40.80188  1.000 58.67756 ? 126  SER   A OG  1 
ATOM   951  N  N   . TYR   A 1 127 ? 14.61325  -7.52130  44.65451  1.000 32.08003 ? 127  TYR   A N   1 
ATOM   952  C  CA  . TYR   A 1 127 ? 14.37174  -7.90099  46.03389  1.000 31.53529 ? 127  TYR   A CA  1 
ATOM   953  C  C   . TYR   A 1 127 ? 13.06534  -8.66756  46.16332  1.000 38.11185 ? 127  TYR   A C   1 
ATOM   954  O  O   . TYR   A 1 127 ? 12.99403  -9.66769  46.88692  1.000 36.21122 ? 127  TYR   A O   1 
ATOM   955  C  CB  . TYR   A 1 127 ? 14.34761  -6.65160  46.91099  1.000 31.57771 ? 127  TYR   A CB  1 
ATOM   956  C  CG  . TYR   A 1 127 ? 14.39272  -6.96881  48.39039  1.000 30.88337 ? 127  TYR   A CG  1 
ATOM   957  C  CD1 . TYR   A 1 127 ? 15.58613  -7.35921  48.99234  1.000 35.73108 ? 127  TYR   A CD1 1 
ATOM   958  C  CD2 . TYR   A 1 127 ? 13.24692  -6.91996  49.17273  1.000 32.48940 ? 127  TYR   A CD2 1 
ATOM   959  C  CE1 . TYR   A 1 127 ? 15.64500  -7.66391  50.32211  1.000 34.47953 ? 127  TYR   A CE1 1 
ATOM   960  C  CE2 . TYR   A 1 127 ? 13.29540  -7.22556  50.53168  1.000 32.91085 ? 127  TYR   A CE2 1 
ATOM   961  C  CZ  . TYR   A 1 127 ? 14.49860  -7.58978  51.09343  1.000 24.96914 ? 127  TYR   A CZ  1 
ATOM   962  O  OH  . TYR   A 1 127 ? 14.59302  -7.91165  52.42807  1.000 34.26230 ? 127  TYR   A OH  1 
ATOM   963  N  N   . LYS   A 1 128 ? 12.02104  -8.21400  45.45710  1.000 30.81999 ? 128  LYS   A N   1 
ATOM   964  C  CA  . LYS   A 1 128 ? 10.73804  -8.90297  45.49299  1.000 32.71669 ? 128  LYS   A CA  1 
ATOM   965  C  C   . LYS   A 1 128 ? 10.81509  -10.29887 44.88183  1.000 35.41863 ? 128  LYS   A C   1 
ATOM   966  O  O   . LYS   A 1 128 ? 10.08668  -11.19668 45.31506  1.000 36.13325 ? 128  LYS   A O   1 
ATOM   967  C  CB  . LYS   A 1 128 ? 9.67266   -8.06301  44.79186  1.000 35.52182 ? 128  LYS   A CB  1 
ATOM   968  C  CG  . LYS   A 1 128 ? 8.28179   -8.61458  44.94578  1.000 40.96332 ? 128  LYS   A CG  1 
ATOM   969  C  CD  . LYS   A 1 128 ? 7.23703   -7.67094  44.38543  1.000 48.47335 ? 128  LYS   A CD  1 
ATOM   970  C  CE  . LYS   A 1 128 ? 5.85532   -8.06140  44.87572  1.000 47.29691 ? 128  LYS   A CE  1 
ATOM   971  N  NZ  . LYS   A 1 128 ? 5.45318   -9.39984  44.34459  1.000 60.18861 ? 128  LYS   A NZ  1 
ATOM   972  N  N   . ALA   A 1 129 ? 11.69961  -10.52150 43.90803  1.000 37.43594 ? 129  ALA   A N   1 
ATOM   973  C  CA  . ALA   A 1 129 ? 11.87910  -11.87630 43.38641  1.000 38.93996 ? 129  ALA   A CA  1 
ATOM   974  C  C   . ALA   A 1 129 ? 12.56601  -12.78070 44.40657  1.000 39.38394 ? 129  ALA   A C   1 
ATOM   975  O  O   . ALA   A 1 129 ? 12.27956  -13.98510 44.47340  1.000 41.09086 ? 129  ALA   A O   1 
ATOM   976  C  CB  . ALA   A 1 129 ? 12.67339  -11.84762 42.07687  1.000 39.05609 ? 129  ALA   A CB  1 
ATOM   977  N  N   . LEU   A 1 130 ? 13.51108  -12.23290 45.17223  1.000 40.99758 ? 130  LEU   A N   1 
ATOM   978  C  CA  . LEU   A 1 130 ? 14.11611  -12.98606 46.26954  1.000 44.07876 ? 130  LEU   A CA  1 
ATOM   979  C  C   . LEU   A 1 130 ? 13.06091  -13.36094 47.29580  1.000 42.34439 ? 130  LEU   A C   1 
ATOM   980  O  O   . LEU   A 1 130 ? 12.95233  -14.52152 47.71331  1.000 47.81076 ? 130  LEU   A O   1 
ATOM   981  C  CB  . LEU   A 1 130 ? 15.21249  -12.15308 46.93239  1.000 37.97589 ? 130  LEU   A CB  1 
ATOM   982  C  CG  . LEU   A 1 130 ? 16.45802  -11.83463 46.11214  1.000 49.24710 ? 130  LEU   A CG  1 
ATOM   983  C  CD1 . LEU   A 1 130 ? 17.31116  -10.79046 46.84272  1.000 42.82686 ? 130  LEU   A CD1 1 
ATOM   984  C  CD2 . LEU   A 1 130 ? 17.23993  -13.11001 45.86185  1.000 48.16817 ? 130  LEU   A CD2 1 
ATOM   985  N  N   . LEU   A 1 131 ? 12.28369  -12.36457 47.71506  1.000 41.56711 ? 131  LEU   A N   1 
ATOM   986  C  CA  . LEU   A 1 131 ? 11.15799  -12.54413 48.62134  1.000 34.76230 ? 131  LEU   A CA  1 
ATOM   987  C  C   . LEU   A 1 131 ? 10.21420  -13.63450 48.13004  1.000 51.29026 ? 131  LEU   A C   1 
ATOM   988  O  O   . LEU   A 1 131 ? 9.94685   -14.61059 48.83957  1.000 45.33859 ? 131  LEU   A O   1 
ATOM   989  C  CB  . LEU   A 1 131 ? 10.43317  -11.20513 48.73827  1.000 40.76395 ? 131  LEU   A CB  1 
ATOM   990  C  CG  . LEU   A 1 131 ? 9.58925   -10.81524 49.93056  1.000 52.79358 ? 131  LEU   A CG  1 
ATOM   991  C  CD1 . LEU   A 1 131 ? 9.57506   -9.29592  49.99574  1.000 47.03189 ? 131  LEU   A CD1 1 
ATOM   992  C  CD2 . LEU   A 1 131 ? 8.18929   -11.36140 49.75977  1.000 45.22410 ? 131  LEU   A CD2 1 
ATOM   993  N  N   . ASP   A 1 132 ? 9.71822   -13.48887 46.89377  1.000 49.34799 ? 132  ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 132 ? 8.65028   -14.35058 46.40110  1.000 37.20801 ? 132  ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 132 ? 9.10981   -15.78891 46.23654  1.000 51.09149 ? 132  ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 132 ? 8.28429   -16.70630 46.28423  1.000 54.48730 ? 132  ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 132 ? 8.10629   -13.82472 45.07044  1.000 43.06207 ? 132  ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 132 ? 7.28706   -12.55113 45.23454  1.000 55.68632 ? 132  ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 132 ? 6.91608   -12.19907 46.38387  1.000 67.83428 ? 132  ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 132 ? 7.02760   -11.89307 44.20604  1.000 72.28407 ? 132  ASP   A OD2 1 
ATOM   1001 N  N   . SER   A 1 133 ? 10.40479  -16.00552 46.02183  1.000 51.57067 ? 133  SER   A N   1 
ATOM   1002 C  CA  . SER   A 1 133 ? 10.97120  -17.34338 45.99410  1.000 38.64665 ? 133  SER   A CA  1 
ATOM   1003 C  C   . SER   A 1 133 ? 11.53933  -17.76442 47.35127  1.000 44.44379 ? 133  SER   A C   1 
ATOM   1004 O  O   . SER   A 1 133 ? 12.30472  -18.72848 47.41078  1.000 48.51901 ? 133  SER   A O   1 
ATOM   1005 C  CB  . SER   A 1 133 ? 12.06736  -17.43237 44.93398  1.000 48.34989 ? 133  SER   A CB  1 
ATOM   1006 O  OG  . SER   A 1 133 ? 13.19691  -16.67736 45.31977  1.000 46.90973 ? 133  SER   A OG  1 
ATOM   1007 N  N   . HIS   A 1 134 ? 11.21341  -17.04190 48.42704  1.000 47.89491 ? 134  HIS   A N   1 
ATOM   1008 C  CA  . HIS   A 1 134 ? 11.60943  -17.42819 49.78733  1.000 49.85607 ? 134  HIS   A CA  1 
ATOM   1009 C  C   . HIS   A 1 134 ? 13.12987  -17.62095 49.90560  1.000 43.84074 ? 134  HIS   A C   1 
ATOM   1010 O  O   . HIS   A 1 134 ? 13.60832  -18.56385 50.53411  1.000 46.87650 ? 134  HIS   A O   1 
ATOM   1011 C  CB  . HIS   A 1 134 ? 10.84654  -18.69123 50.21973  1.000 40.31979 ? 134  HIS   A CB  1 
ATOM   1012 C  CG  . HIS   A 1 134 ? 9.41713   -18.71490 49.76272  1.000 47.81208 ? 134  HIS   A CG  1 
ATOM   1013 N  ND1 . HIS   A 1 134 ? 8.45525   -17.86804 50.27447  1.000 45.89748 ? 134  HIS   A ND1 1 
ATOM   1014 C  CD2 . HIS   A 1 134 ? 8.79318   -19.46141 48.81920  1.000 42.17314 ? 134  HIS   A CD2 1 
ATOM   1015 C  CE1 . HIS   A 1 134 ? 7.29914   -18.10155 49.67883  1.000 45.31633 ? 134  HIS   A CE1 1 
ATOM   1016 N  NE2 . HIS   A 1 134 ? 7.47619   -19.06239 48.78997  1.000 43.12655 ? 134  HIS   A NE2 1 
ATOM   1017 N  N   . SER   A 1 135 ? 13.90148  -16.72674 49.28314  1.000 47.94270 ? 135  SER   A N   1 
ATOM   1018 C  CA  . SER   A 1 135 ? 15.35709  -16.84940 49.22150  1.000 50.41275 ? 135  SER   A CA  1 
ATOM   1019 C  C   . SER   A 1 135 ? 16.08156  -15.91685 50.18227  1.000 52.73588 ? 135  SER   A C   1 
ATOM   1020 O  O   . SER   A 1 135 ? 17.31734  -15.90361 50.19897  1.000 56.92688 ? 135  SER   A O   1 
ATOM   1021 C  CB  . SER   A 1 135 ? 15.85738  -16.57938 47.79832  1.000 48.00749 ? 135  SER   A CB  1 
ATOM   1022 O  OG  . SER   A 1 135 ? 15.10672  -17.31263 46.84647  1.000 62.57636 ? 135  SER   A OG  1 
ATOM   1023 N  N   . ILE   A 1 136 ? 15.35331  -15.12231 50.95553  1.000 37.90003 ? 136  ILE   A N   1 
ATOM   1024 C  CA  . ILE   A 1 136 ? 15.96893  -14.24795 51.94963  1.000 50.83430 ? 136  ILE   A CA  1 
ATOM   1025 C  C   . ILE   A 1 136 ? 16.44360  -15.13461 53.09497  1.000 47.98429 ? 136  ILE   A C   1 
ATOM   1026 O  O   . ILE   A 1 136 ? 15.63466  -15.88937 53.65554  1.000 44.58062 ? 136  ILE   A O   1 
ATOM   1027 C  CB  . ILE   A 1 136 ? 14.98340  -13.17453 52.42918  1.000 49.14345 ? 136  ILE   A CB  1 
ATOM   1028 C  CG1 . ILE   A 1 136 ? 14.53437  -12.31183 51.25008  1.000 47.41825 ? 136  ILE   A CG1 1 
ATOM   1029 C  CG2 . ILE   A 1 136 ? 15.60629  -12.31451 53.52402  1.000 48.02002 ? 136  ILE   A CG2 1 
ATOM   1030 C  CD1 . ILE   A 1 136 ? 15.59206  -11.34371 50.78561  1.000 43.63245 ? 136  ILE   A CD1 1 
ATOM   1031 N  N   . PRO   A 1 137 ? 17.72719  -15.10751 53.45852  1.000 48.75266 ? 137  PRO   A N   1 
ATOM   1032 C  CA  . PRO   A 1 137 ? 18.18980  -15.96525 54.55945  1.000 46.60560 ? 137  PRO   A CA  1 
ATOM   1033 C  C   . PRO   A 1 137 ? 17.46493  -15.61761 55.85370  1.000 43.57389 ? 137  PRO   A C   1 
ATOM   1034 O  O   . PRO   A 1 137 ? 17.23781  -14.44612 56.16738  1.000 36.94548 ? 137  PRO   A O   1 
ATOM   1035 C  CB  . PRO   A 1 137 ? 19.69375  -15.66170 54.64547  1.000 47.16659 ? 137  PRO   A CB  1 
ATOM   1036 C  CG  . PRO   A 1 137 ? 20.05139  -15.11189 53.27760  1.000 44.54213 ? 137  PRO   A CG  1 
ATOM   1037 C  CD  . PRO   A 1 137 ? 18.82929  -14.32319 52.86808  1.000 43.54848 ? 137  PRO   A CD  1 
ATOM   1038 N  N   . THR   A 1 138 ? 17.07281  -16.65636 56.58792  1.000 42.37737 ? 138  THR   A N   1 
ATOM   1039 C  CA  . THR   A 1 138 ? 16.37633  -16.46801 57.85270  1.000 36.06992 ? 138  THR   A CA  1 
ATOM   1040 C  C   . THR   A 1 138 ? 17.21500  -15.64253 58.82089  1.000 39.26378 ? 138  THR   A C   1 
ATOM   1041 O  O   . THR   A 1 138 ? 18.37503  -15.96664 59.09518  1.000 37.18083 ? 138  THR   A O   1 
ATOM   1042 C  CB  . THR   A 1 138 ? 16.04832  -17.82519 58.47106  1.000 43.53630 ? 138  THR   A CB  1 
ATOM   1043 O  OG1 . THR   A 1 138 ? 15.26009  -18.58207 57.54652  1.000 43.62656 ? 138  THR   A OG1 1 
ATOM   1044 C  CG2 . THR   A 1 138 ? 15.26597  -17.64204 59.77315  1.000 30.17519 ? 138  THR   A CG2 1 
ATOM   1045 N  N   . ASP   A 1 139 ? 16.63034  -14.55457 59.31515  1.000 33.91135 ? 139  ASP   A N   1 
ATOM   1046 C  CA  . ASP   A 1 139 ? 17.26223  -13.76611 60.36244  1.000 33.08186 ? 139  ASP   A CA  1 
ATOM   1047 C  C   . ASP   A 1 139 ? 17.38322  -14.60623 61.62215  1.000 36.10958 ? 139  ASP   A C   1 
ATOM   1048 O  O   . ASP   A 1 139 ? 16.51204  -15.42706 61.92167  1.000 35.51920 ? 139  ASP   A O   1 
ATOM   1049 C  CB  . ASP   A 1 139 ? 16.43333  -12.50443 60.65876  1.000 29.30581 ? 139  ASP   A CB  1 
ATOM   1050 C  CG  . ASP   A 1 139 ? 16.41751  -11.54063 59.48946  1.000 32.23605 ? 139  ASP   A CG  1 
ATOM   1051 O  OD1 . ASP   A 1 139 ? 17.45999  -11.43138 58.81461  1.000 34.68059 ? 139  ASP   A OD1 1 
ATOM   1052 O  OD2 . ASP   A 1 139 ? 15.37350  -10.91696 59.21880  1.000 28.97059 ? 139  ASP   A OD2 1 
ATOM   1053 N  N   . CYS   A 1 140 ? 18.47145  -14.39302 62.36464  1.000 33.63489 ? 140  CYS   A N   1 
ATOM   1054 C  CA  . CYS   A 1 140 ? 18.65917  -15.00255 63.67789  1.000 35.55060 ? 140  CYS   A CA  1 
ATOM   1055 C  C   . CYS   A 1 140 ? 18.78088  -13.91449 64.73391  1.000 37.73445 ? 140  CYS   A C   1 
ATOM   1056 O  O   . CYS   A 1 140 ? 19.23110  -12.80296 64.44302  1.000 35.80310 ? 140  CYS   A O   1 
ATOM   1057 C  CB  . CYS   A 1 140 ? 19.89982  -15.90079 63.71587  1.000 39.25732 ? 140  CYS   A CB  1 
ATOM   1058 S  SG  . CYS   A 1 140 ? 19.77994  -17.32084 62.60166  1.000 53.50438 ? 140  CYS   A SG  1 
ATOM   1059 N  N   . ALA   A 1 141 ? 18.38215  -14.25204 65.96514  1.000 30.51882 ? 141  ALA   A N   1 
ATOM   1060 C  CA  . ALA   A 1 141 ? 18.37133  -13.27812 67.04760  1.000 36.74682 ? 141  ALA   A CA  1 
ATOM   1061 C  C   . ALA   A 1 141 ? 19.77815  -12.72902 67.28311  1.000 39.01298 ? 141  ALA   A C   1 
ATOM   1062 O  O   . ALA   A 1 141 ? 20.76515  -13.46674 67.23121  1.000 41.15212 ? 141  ALA   A O   1 
ATOM   1063 C  CB  . ALA   A 1 141 ? 17.82514  -13.92492 68.32193  1.000 35.68591 ? 141  ALA   A CB  1 
ATOM   1064 N  N   . LYS   A 1 142 ? 19.86778  -11.41638 67.51630  1.000 49.39817 ? 142  LYS   A N   1 
ATOM   1065 C  CA  . LYS   A 1 142 ? 21.15712  -10.72923 67.70282  1.000 48.12015 ? 142  LYS   A CA  1 
ATOM   1066 C  C   . LYS   A 1 142 ? 22.11849  -10.97815 66.53956  1.000 59.26230 ? 142  LYS   A C   1 
ATOM   1067 O  O   . LYS   A 1 142 ? 23.33538  -11.06054 66.73048  1.000 68.48719 ? 142  LYS   A O   1 
ATOM   1068 C  CB  . LYS   A 1 142 ? 21.81894  -11.12686 69.03211  1.000 55.48518 ? 142  LYS   A CB  1 
ATOM   1069 C  CG  . LYS   A 1 142 ? 20.93388  -10.93923 70.27036  1.000 48.74581 ? 142  LYS   A CG  1 
ATOM   1070 C  CD  . LYS   A 1 142 ? 20.27852  -9.55568  70.29210  1.000 79.71625 ? 142  LYS   A CD  1 
ATOM   1071 C  CE  . LYS   A 1 142 ? 21.30685  -8.41975  70.35612  1.000 84.28410 ? 142  LYS   A CE  1 
ATOM   1072 N  NZ  . LYS   A 1 142 ? 20.73363  -7.13144  69.84782  1.000 66.52571 ? 142  LYS   A NZ  1 
ATOM   1073 N  N   . GLY   A 1 143 ? 21.58729  -11.09421 65.32313  1.000 52.25598 ? 143  GLY   A N   1 
ATOM   1074 C  CA  . GLY   A 1 143 ? 22.40549  -11.41129 64.16095  1.000 46.96166 ? 143  GLY   A CA  1 
ATOM   1075 C  C   . GLY   A 1 143 ? 23.15271  -12.73302 64.26704  1.000 56.58725 ? 143  GLY   A C   1 
ATOM   1076 O  O   . GLY   A 1 143 ? 23.72508  -13.21032 63.28661  1.000 65.39181 ? 143  GLY   A O   1 
ATOM   1077 N  N   . GLY   A 1 147 ? 22.31846  -18.60378 66.04734  1.000 52.32429 ? 147  GLY   A N   1 
ATOM   1078 C  CA  . GLY   A 1 147 ? 21.30573  -17.83763 66.75386  1.000 55.35472 ? 147  GLY   A CA  1 
ATOM   1079 C  C   . GLY   A 1 147 ? 19.89823  -18.38035 66.56090  1.000 34.36301 ? 147  GLY   A C   1 
ATOM   1080 O  O   . GLY   A 1 147 ? 19.62435  -19.12697 65.61479  1.000 52.71708 ? 147  GLY   A O   1 
ATOM   1081 N  N   . GLN   A 1 148 ? 19.01124  -17.99404 67.45805  1.000 39.93711 ? 148  GLN   A N   1 
ATOM   1082 C  CA  . GLN   A 1 148 ? 17.63169  -18.44430 67.39978  1.000 31.11685 ? 148  GLN   A CA  1 
ATOM   1083 C  C   . GLN   A 1 148 ? 16.92843  -17.86455 66.17078  1.000 29.30429 ? 148  GLN   A C   1 
ATOM   1084 O  O   . GLN   A 1 148 ? 16.94458  -16.64263 65.98408  1.000 32.53407 ? 148  GLN   A O   1 
ATOM   1085 C  CB  . GLN   A 1 148 ? 16.94208  -17.99563 68.67391  1.000 38.39917 ? 148  GLN   A CB  1 
ATOM   1086 C  CG  . GLN   A 1 148 ? 15.53732  -18.42629 68.81610  1.000 40.76747 ? 148  GLN   A CG  1 
ATOM   1087 C  CD  . GLN   A 1 148 ? 14.96820  -18.10386 70.18676  1.000 38.39464 ? 148  GLN   A CD  1 
ATOM   1088 O  OE1 . GLN   A 1 148 ? 15.69132  -17.71825 71.11431  1.000 37.61667 ? 148  GLN   A OE1 1 
ATOM   1089 N  NE2 . GLN   A 1 148 ? 13.67206  -18.29153 70.32813  1.000 30.80790 ? 148  GLN   A NE2 1 
ATOM   1090 N  N   . PRO   A 1 149 ? 16.27599  -18.69298 65.33702  1.000 37.77281 ? 149  PRO   A N   1 
ATOM   1091 C  CA  . PRO   A 1 149 ? 15.58499  -18.17129 64.13456  1.000 35.03176 ? 149  PRO   A CA  1 
ATOM   1092 C  C   . PRO   A 1 149 ? 14.45558  -17.21349 64.47171  1.000 34.78291 ? 149  PRO   A C   1 
ATOM   1093 O  O   . PRO   A 1 149 ? 13.75227  -17.38580 65.46972  1.000 28.35379 ? 149  PRO   A O   1 
ATOM   1094 C  CB  . PRO   A 1 149 ? 15.01507  -19.43287 63.46756  1.000 30.32674 ? 149  PRO   A CB  1 
ATOM   1095 C  CG  . PRO   A 1 149 ? 15.69308  -20.58399 64.12931  1.000 48.41762 ? 149  PRO   A CG  1 
ATOM   1096 C  CD  . PRO   A 1 149 ? 16.08767  -20.14325 65.49767  1.000 35.51733 ? 149  PRO   A CD  1 
ATOM   1097 N  N   . LEU   A 1 150 ? 14.23267  -16.23521 63.57685  1.000 24.96101 ? 150  LEU   A N   1 
ATOM   1098 C  CA  . LEU   A 1 150 ? 13.17380  -15.24593 63.73169  1.000 24.03245 ? 150  LEU   A CA  1 
ATOM   1099 C  C   . LEU   A 1 150 ? 12.11437  -15.41080 62.64793  1.000 25.65893 ? 150  LEU   A C   1 
ATOM   1100 O  O   . LEU   A 1 150 ? 12.39606  -15.88456 61.54131  1.000 24.45344 ? 150  LEU   A O   1 
ATOM   1101 C  CB  . LEU   A 1 150 ? 13.73486  -13.82098 63.65942  1.000 24.71854 ? 150  LEU   A CB  1 
ATOM   1102 C  CG  . LEU   A 1 150 ? 14.89858  -13.54638 64.61874  1.000 26.93768 ? 150  LEU   A CG  1 
ATOM   1103 C  CD1 . LEU   A 1 150 ? 15.51950  -12.17268 64.32537  1.000 30.89481 ? 150  LEU   A CD1 1 
ATOM   1104 C  CD2 . LEU   A 1 150 ? 14.39721  -13.59815 66.04230  1.000 21.21929 ? 150  LEU   A CD2 1 
ATOM   1105 N  N   . CYS   A 1 151 ? 10.89559  -15.01385 62.98589  1.000 23.49609 ? 151  CYS   A N   1 
ATOM   1106 C  CA  . CYS   A 1 151 ? 9.80070   -14.98912 62.02649  1.000 24.50484 ? 151  CYS   A CA  1 
ATOM   1107 C  C   . CYS   A 1 151 ? 10.14261  -14.11297 60.82076  1.000 31.86389 ? 151  CYS   A C   1 
ATOM   1108 O  O   . CYS   A 1 151 ? 10.66987  -13.00745 60.95866  1.000 24.51384 ? 151  CYS   A O   1 
ATOM   1109 C  CB  . CYS   A 1 151 ? 8.53924   -14.46087 62.70305  1.000 22.71696 ? 151  CYS   A CB  1 
ATOM   1110 S  SG  . CYS   A 1 151 ? 7.06294   -14.53809 61.60496  1.000 27.12154 ? 151  CYS   A SG  1 
ATOM   1111 N  N   . MET   A 1 152 ? 9.81777   -14.60579 59.63134  1.000 26.02845 ? 152  MET   A N   1 
ATOM   1112 C  CA  . MET   A 1 152 ? 10.08047  -13.87553 58.39929  1.000 25.10236 ? 152  MET   A CA  1 
ATOM   1113 C  C   . MET   A 1 152 ? 8.80752   -13.34050 57.75950  1.000 29.35500 ? 152  MET   A C   1 
ATOM   1114 O  O   . MET   A 1 152 ? 8.87777   -12.81925 56.64170  1.000 27.77455 ? 152  MET   A O   1 
ATOM   1115 C  CB  . MET   A 1 152 ? 10.83609  -14.75967 57.40384  1.000 25.90649 ? 152  MET   A CB  1 
ATOM   1116 C  CG  . MET   A 1 152 ? 12.21254  -15.23404 57.88467  1.000 23.44940 ? 152  MET   A CG  1 
ATOM   1117 S  SD  . MET   A 1 152 ? 13.45990  -13.95120 58.22090  1.000 28.28182 ? 152  MET   A SD  1 
ATOM   1118 C  CE  . MET   A 1 152 ? 14.11418  -13.74266 56.53458  1.000 30.02326 ? 152  MET   A CE  1 
ATOM   1119 N  N   . LYS   A 1 153 ? 7.65385   -13.41173 58.45134  1.000 27.48036 ? 153  LYS   A N   1 
ATOM   1120 C  CA  . LYS   A 1 153 ? 6.38659   -13.05405 57.79827  1.000 23.83447 ? 153  LYS   A CA  1 
ATOM   1121 C  C   . LYS   A 1 153 ? 6.28507   -11.57689 57.44325  1.000 23.71198 ? 153  LYS   A C   1 
ATOM   1122 O  O   . LYS   A 1 153 ? 5.56691   -11.23471 56.49449  1.000 25.42064 ? 153  LYS   A O   1 
ATOM   1123 C  CB  . LYS   A 1 153 ? 5.17437   -13.43133 58.65239  1.000 28.01289 ? 153  LYS   A CB  1 
ATOM   1124 C  CG  . LYS   A 1 153 ? 4.89272   -14.93460 58.76519  1.000 54.81314 ? 153  LYS   A CG  1 
ATOM   1125 C  CD  . LYS   A 1 153 ? 4.60397   -15.58430 57.41318  1.000 59.85372 ? 153  LYS   A CD  1 
ATOM   1126 C  CE  . LYS   A 1 153 ? 4.12260   -17.01662 57.58613  1.000 58.93214 ? 153  LYS   A CE  1 
ATOM   1127 N  NZ  . LYS   A 1 153 ? 2.80934   -17.03836 58.29449  1.000 74.92925 ? 153  LYS   A NZ  1 
ATOM   1128 N  N   . GLN   A 1 154 ? 6.93731   -10.67147 58.19028  1.000 23.95380 ? 154  GLN   A N   1 
ATOM   1129 C  CA  . GLN   A 1 154 ? 6.81017   -9.24839  57.85229  1.000 20.82422 ? 154  GLN   A CA  1 
ATOM   1130 C  C   . GLN   A 1 154 ? 7.38193   -8.94024  56.46956  1.000 25.24488 ? 154  GLN   A C   1 
ATOM   1131 O  O   . GLN   A 1 154 ? 6.97843   -7.95830  55.84127  1.000 21.46405 ? 154  GLN   A O   1 
ATOM   1132 C  CB  . GLN   A 1 154 ? 7.50579   -8.34995  58.88697  1.000 22.75726 ? 154  GLN   A CB  1 
ATOM   1133 C  CG  . GLN   A 1 154 ? 6.92042   -8.44937  60.28597  1.000 18.62582 ? 154  GLN   A CG  1 
ATOM   1134 C  CD  . GLN   A 1 154 ? 7.80960   -7.81380  61.32761  1.000 23.67273 ? 154  GLN   A CD  1 
ATOM   1135 O  OE1 . GLN   A 1 154 ? 8.42965   -6.77615  61.09038  1.000 23.12395 ? 154  GLN   A OE1 1 
ATOM   1136 N  NE2 . GLN   A 1 154 ? 7.88238   -8.44100  62.49572  1.000 18.58542 ? 154  GLN   A NE2 1 
ATOM   1137 N  N   . TYR   A 1 155 ? 8.35922   -9.72144  56.00091  1.000 21.91556 ? 155  TYR   A N   1 
ATOM   1138 C  CA  . TYR   A 1 155 ? 8.87943   -9.47451  54.65238  1.000 32.13807 ? 155  TYR   A CA  1 
ATOM   1139 C  C   . TYR   A 1 155 ? 7.77562   -9.58046  53.60041  1.000 28.71592 ? 155  TYR   A C   1 
ATOM   1140 O  O   . TYR   A 1 155 ? 7.77399   -8.83295  52.61414  1.000 27.76372 ? 155  TYR   A O   1 
ATOM   1141 C  CB  . TYR   A 1 155 ? 10.01863  -10.44298 54.33056  1.000 24.93938 ? 155  TYR   A CB  1 
ATOM   1142 C  CG  . TYR   A 1 155 ? 11.31647  -10.13670 55.08265  1.000 31.28153 ? 155  TYR   A CG  1 
ATOM   1143 C  CD1 . TYR   A 1 155 ? 11.58219  -10.71782 56.32947  1.000 24.62300 ? 155  TYR   A CD1 1 
ATOM   1144 C  CD2 . TYR   A 1 155 ? 12.27621  -9.27492  54.54207  1.000 24.30843 ? 155  TYR   A CD2 1 
ATOM   1145 C  CE1 . TYR   A 1 155 ? 12.80211  -10.46773 57.01989  1.000 24.67542 ? 155  TYR   A CE1 1 
ATOM   1146 C  CE2 . TYR   A 1 155 ? 13.49142  -9.01755  55.21703  1.000 27.44039 ? 155  TYR   A CE2 1 
ATOM   1147 C  CZ  . TYR   A 1 155 ? 13.73820  -9.62360  56.45461  1.000 33.82051 ? 155  TYR   A CZ  1 
ATOM   1148 O  OH  . TYR   A 1 155 ? 14.92172  -9.36281  57.12675  1.000 31.51252 ? 155  TYR   A OH  1 
ATOM   1149 N  N   . TYR   A 1 156 ? 6.81993   -10.48845 53.79455  1.000 26.83730 ? 156  TYR   A N   1 
ATOM   1150 C  CA  . TYR   A 1 156 ? 5.76571   -10.63978 52.79414  1.000 30.60959 ? 156  TYR   A CA  1 
ATOM   1151 C  C   . TYR   A 1 156 ? 4.74026   -9.52141  52.84412  1.000 32.66004 ? 156  TYR   A C   1 
ATOM   1152 O  O   . TYR   A 1 156 ? 3.83624   -9.49805  52.00464  1.000 36.58910 ? 156  TYR   A O   1 
ATOM   1153 C  CB  . TYR   A 1 156 ? 5.06007   -11.98277 52.95834  1.000 28.17336 ? 156  TYR   A CB  1 
ATOM   1154 C  CG  . TYR   A 1 156 ? 5.98161   -13.17298 52.78638  1.000 32.98769 ? 156  TYR   A CG  1 
ATOM   1155 C  CD1 . TYR   A 1 156 ? 6.31045   -13.65311 51.52427  1.000 35.73060 ? 156  TYR   A CD1 1 
ATOM   1156 C  CD2 . TYR   A 1 156 ? 6.51906   -13.81548 53.89154  1.000 38.94929 ? 156  TYR   A CD2 1 
ATOM   1157 C  CE1 . TYR   A 1 156 ? 7.16230   -14.74433 51.37297  1.000 31.11604 ? 156  TYR   A CE1 1 
ATOM   1158 C  CE2 . TYR   A 1 156 ? 7.37042   -14.89620 53.75512  1.000 41.63296 ? 156  TYR   A CE2 1 
ATOM   1159 C  CZ  . TYR   A 1 156 ? 7.68983   -15.35683 52.50327  1.000 47.95195 ? 156  TYR   A CZ  1 
ATOM   1160 O  OH  . TYR   A 1 156 ? 8.53292   -16.43392 52.40275  1.000 43.12645 ? 156  TYR   A OH  1 
ATOM   1161 N  N   . GLY   A 1 157 ? 4.84446   -8.61343  53.80510  1.000 24.69156 ? 157  GLY   A N   1 
ATOM   1162 C  CA  . GLY   A 1 157 ? 3.96111   -7.47976  53.91037  1.000 24.55408 ? 157  GLY   A CA  1 
ATOM   1163 C  C   . GLY   A 1 157 ? 4.54439   -6.21040  53.35158  1.000 25.41963 ? 157  GLY   A C   1 
ATOM   1164 O  O   . GLY   A 1 157 ? 3.85182   -5.18199  53.31726  1.000 27.34216 ? 157  GLY   A O   1 
ATOM   1165 N  N   . LEU   A 1 158 ? 5.80881   -6.24355  52.91446  1.000 24.57153 ? 158  LEU   A N   1 
ATOM   1166 C  CA  . LEU   A 1 158 ? 6.44751   -5.01582  52.44764  1.000 26.62171 ? 158  LEU   A CA  1 
ATOM   1167 C  C   . LEU   A 1 158 ? 5.79720   -4.49742  51.17150  1.000 25.00575 ? 158  LEU   A C   1 
ATOM   1168 O  O   . LEU   A 1 158 ? 5.56337   -3.29287  51.04098  1.000 24.95420 ? 158  LEU   A O   1 
ATOM   1169 C  CB  . LEU   A 1 158 ? 7.93774   -5.24528  52.22371  1.000 26.28338 ? 158  LEU   A CB  1 
ATOM   1170 C  CG  . LEU   A 1 158 ? 8.81401   -5.40835  53.46619  1.000 18.47540 ? 158  LEU   A CG  1 
ATOM   1171 C  CD1 . LEU   A 1 158 ? 10.10719  -6.11636  53.05655  1.000 23.29638 ? 158  LEU   A CD1 1 
ATOM   1172 C  CD2 . LEU   A 1 158 ? 9.14220   -4.02712  54.09325  1.000 19.67213 ? 158  LEU   A CD2 1 
ATOM   1173 N  N   . PHE   A 1 159 ? 5.47874   -5.38314  50.23478  1.000 22.68164 ? 159  PHE   A N   1 
ATOM   1174 C  CA  . PHE   A 1 159 ? 4.99347   -4.95834  48.92629  1.000 28.02904 ? 159  PHE   A CA  1 
ATOM   1175 C  C   . PHE   A 1 159 ? 3.56178   -5.36128  48.62057  1.000 40.13785 ? 159  PHE   A C   1 
ATOM   1176 O  O   . PHE   A 1 159 ? 3.01068   -4.91296  47.60022  1.000 39.83292 ? 159  PHE   A O   1 
ATOM   1177 C  CB  . PHE   A 1 159 ? 5.90102   -5.51848  47.82111  1.000 25.25954 ? 159  PHE   A CB  1 
ATOM   1178 C  CG  . PHE   A 1 159 ? 7.32119   -5.12689  47.97266  1.000 29.16264 ? 159  PHE   A CG  1 
ATOM   1179 C  CD1 . PHE   A 1 159 ? 7.72122   -3.81402  47.74807  1.000 28.88613 ? 159  PHE   A CD1 1 
ATOM   1180 C  CD2 . PHE   A 1 159 ? 8.26788   -6.06112  48.35676  1.000 37.29219 ? 159  PHE   A CD2 1 
ATOM   1181 C  CE1 . PHE   A 1 159 ? 9.05270   -3.44855  47.91288  1.000 29.12535 ? 159  PHE   A CE1 1 
ATOM   1182 C  CE2 . PHE   A 1 159 ? 9.58700   -5.69608  48.52841  1.000 35.58513 ? 159  PHE   A CE2 1 
ATOM   1183 C  CZ  . PHE   A 1 159 ? 9.97725   -4.38867  48.30769  1.000 33.07767 ? 159  PHE   A CZ  1 
ATOM   1184 N  N   . SER   A 1 160 ? 2.94468   -6.20281  49.44179  1.000 28.26447 ? 160  SER   A N   1 
ATOM   1185 C  CA  . SER   A 1 160 ? 1.64571   -6.77622  49.09848  1.000 45.29020 ? 160  SER   A CA  1 
ATOM   1186 C  C   . SER   A 1 160 ? 0.52430   -6.25726  49.99249  1.000 38.87419 ? 160  SER   A C   1 
ATOM   1187 O  O   . SER   A 1 160 ? -0.47599  -6.94866  50.20230  1.000 47.09343 ? 160  SER   A O   1 
ATOM   1188 C  CB  . SER   A 1 160 ? 1.71131   -8.29659  49.17697  1.000 54.96943 ? 160  SER   A CB  1 
ATOM   1189 O  OG  . SER   A 1 160 ? 1.93799   -8.67035  50.52003  1.000 51.02812 ? 160  SER   A OG  1 
ATOM   1190 N  N   . SER   A 1 161 ? 0.67182   -5.04242  50.51787  1.000 32.96768 ? 161  SER   A N   1 
ATOM   1191 C  CA  . SER   A 1 161 ? -0.19249  -4.55215  51.58637  1.000 31.69518 ? 161  SER   A CA  1 
ATOM   1192 C  C   . SER   A 1 161 ? -0.84405  -3.23145  51.20257  1.000 30.21347 ? 161  SER   A C   1 
ATOM   1193 O  O   . SER   A 1 161 ? -0.21472  -2.36733  50.58516  1.000 28.09819 ? 161  SER   A O   1 
ATOM   1194 C  CB  . SER   A 1 161 ? 0.59681   -4.35733  52.88399  1.000 30.46364 ? 161  SER   A CB  1 
ATOM   1195 O  OG  . SER   A 1 161 ? 1.14392   -5.58419  53.32299  1.000 39.23070 ? 161  SER   A OG  1 
ATOM   1196 N  N   . TYR   A 1 162 ? -2.10175  -3.06763  51.60247  1.000 25.76194 ? 162  TYR   A N   1 
ATOM   1197 C  CA  . TYR   A 1 162 ? -2.82082  -1.81566  51.39299  1.000 28.76518 ? 162  TYR   A CA  1 
ATOM   1198 C  C   . TYR   A 1 162 ? -3.73531  -1.60111  52.58775  1.000 24.71239 ? 162  TYR   A C   1 
ATOM   1199 O  O   . TYR   A 1 162 ? -4.52351  -2.49060  52.91781  1.000 29.53864 ? 162  TYR   A O   1 
ATOM   1200 C  CB  . TYR   A 1 162 ? -3.64967  -1.83756  50.08431  1.000 23.66744 ? 162  TYR   A CB  1 
ATOM   1201 C  CG  . TYR   A 1 162 ? -4.28940  -0.49347  49.82680  1.000 25.41264 ? 162  TYR   A CG  1 
ATOM   1202 C  CD1 . TYR   A 1 162 ? -5.52084  -0.16530  50.39257  1.000 24.44661 ? 162  TYR   A CD1 1 
ATOM   1203 C  CD2 . TYR   A 1 162 ? -3.62418  0.48220   49.08234  1.000 24.77891 ? 162  TYR   A CD2 1 
ATOM   1204 C  CE1 . TYR   A 1 162 ? -6.09572  1.11300   50.20376  1.000 25.38634 ? 162  TYR   A CE1 1 
ATOM   1205 C  CE2 . TYR   A 1 162 ? -4.18523  1.73681   48.88129  1.000 27.28057 ? 162  TYR   A CE2 1 
ATOM   1206 C  CZ  . TYR   A 1 162 ? -5.42008  2.04767   49.45124  1.000 27.17595 ? 162  TYR   A CZ  1 
ATOM   1207 O  OH  . TYR   A 1 162 ? -5.96994  3.29931   49.25686  1.000 28.58511 ? 162  TYR   A OH  1 
ATOM   1208 N  N   . ARG   A 1 163 ? -3.67295  -0.41834  53.20112  1.000 22.07646 ? 163  ARG   A N   1 
ATOM   1209 C  CA  . ARG   A 1 163 ? -4.49745  -0.10390  54.36917  1.000 23.04654 ? 163  ARG   A CA  1 
ATOM   1210 C  C   . ARG   A 1 163 ? -5.73696  0.70277   53.97049  1.000 29.45725 ? 163  ARG   A C   1 
ATOM   1211 O  O   . ARG   A 1 163 ? -5.65337  1.91255   53.72007  1.000 26.56150 ? 163  ARG   A O   1 
ATOM   1212 C  CB  . ARG   A 1 163 ? -3.68359  0.66296   55.40848  1.000 21.65038 ? 163  ARG   A CB  1 
ATOM   1213 C  CG  . ARG   A 1 163 ? -4.51293  0.98394   56.62549  1.000 22.51841 ? 163  ARG   A CG  1 
ATOM   1214 C  CD  . ARG   A 1 163 ? -3.64786  1.55590   57.71334  1.000 26.98626 ? 163  ARG   A CD  1 
ATOM   1215 N  NE  . ARG   A 1 163 ? -4.44014  2.24028   58.72650  1.000 21.71460 ? 163  ARG   A NE  1 
ATOM   1216 C  CZ  . ARG   A 1 163 ? -3.94368  2.65296   59.88630  1.000 23.37699 ? 163  ARG   A CZ  1 
ATOM   1217 N  NH1 . ARG   A 1 163 ? -2.67484  2.45541   60.20119  1.000 21.70374 ? 163  ARG   A NH1 1 
ATOM   1218 N  NH2 . ARG   A 1 163 ? -4.74455  3.25524   60.75929  1.000 22.10749 ? 163  ARG   A NH2 1 
ATOM   1219 N  N   . LEU   A 1 164 ? -6.88724  0.05853   53.97018  1.000 23.98811 ? 164  LEU   A N   1 
ATOM   1220 C  CA  . LEU   A 1 164 ? -8.10547  0.77930   53.58334  1.000 23.46067 ? 164  LEU   A CA  1 
ATOM   1221 C  C   . LEU   A 1 164 ? -8.61744  1.60360   54.76083  1.000 28.13899 ? 164  LEU   A C   1 
ATOM   1222 O  O   . LEU   A 1 164 ? -8.60018  1.12001   55.89293  1.000 27.02600 ? 164  LEU   A O   1 
ATOM   1223 C  CB  . LEU   A 1 164 ? -9.19422  -0.19698  53.15457  1.000 28.69116 ? 164  LEU   A CB  1 
ATOM   1224 C  CG  . LEU   A 1 164 ? -9.10093  -0.79289  51.76462  1.000 35.00167 ? 164  LEU   A CG  1 
ATOM   1225 C  CD1 . LEU   A 1 164 ? -9.96510  -2.02717  51.67935  1.000 38.36726 ? 164  LEU   A CD1 1 
ATOM   1226 C  CD2 . LEU   A 1 164 ? -9.56011  0.26053   50.75789  1.000 36.05415 ? 164  LEU   A CD2 1 
ATOM   1227 N  N   . PRO   A 1 165 ? -9.09867  2.82830   54.53247  1.000 27.16758 ? 165  PRO   A N   1 
ATOM   1228 C  CA  . PRO   A 1 165 ? -9.72809  3.57070   55.63027  1.000 26.67155 ? 165  PRO   A CA  1 
ATOM   1229 C  C   . PRO   A 1 165 ? -11.09470 2.99524   55.96331  1.000 29.53092 ? 165  PRO   A C   1 
ATOM   1230 O  O   . PRO   A 1 165 ? -11.79494 2.45538   55.10571  1.000 25.62360 ? 165  PRO   A O   1 
ATOM   1231 C  CB  . PRO   A 1 165 ? -9.84846  4.99127   55.07282  1.000 22.39245 ? 165  PRO   A CB  1 
ATOM   1232 C  CG  . PRO   A 1 165 ? -10.04503 4.75312   53.57056  1.000 25.48102 ? 165  PRO   A CG  1 
ATOM   1233 C  CD  . PRO   A 1 165 ? -9.18237  3.56580   53.24783  1.000 22.12818 ? 165  PRO   A CD  1 
ATOM   1234 N  N   . GLY   A 1 166 ? -11.48313 3.13163   57.22866  1.000 22.96600 ? 166  GLY   A N   1 
ATOM   1235 C  CA  . GLY   A 1 166 ? -12.82358 2.78235   57.64687  1.000 23.64469 ? 166  GLY   A CA  1 
ATOM   1236 C  C   . GLY   A 1 166 ? -13.39725 3.89059   58.50552  1.000 27.22054 ? 166  GLY   A C   1 
ATOM   1237 O  O   . GLY   A 1 166 ? -12.67401 4.73875   59.02620  1.000 30.75735 ? 166  GLY   A O   1 
ATOM   1238 N  N   . HIS   A 1 167 ? -14.72185 3.87654   58.65091  1.000 32.83903 ? 167  HIS   A N   1 
ATOM   1239 C  CA  . HIS   A 1 167 ? -15.34864 4.91788   59.45848  1.000 26.88831 ? 167  HIS   A CA  1 
ATOM   1240 C  C   . HIS   A 1 167 ? -14.91826 4.82354   60.91534  1.000 40.80191 ? 167  HIS   A C   1 
ATOM   1241 O  O   . HIS   A 1 167 ? -14.65810 5.84581   61.56322  1.000 41.84235 ? 167  HIS   A O   1 
ATOM   1242 C  CB  . HIS   A 1 167 ? -16.87067 4.85441   59.36160  1.000 44.96483 ? 167  HIS   A CB  1 
ATOM   1243 C  CG  . HIS   A 1 167 ? -17.54410 5.82844   60.27564  1.000 69.67154 ? 167  HIS   A CG  1 
ATOM   1244 N  ND1 . HIS   A 1 167 ? -17.27110 7.18057   60.24596  1.000 57.63770 ? 167  HIS   A ND1 1 
ATOM   1245 C  CD2 . HIS   A 1 167 ? -18.42960 5.64530   61.28331  1.000 71.69570 ? 167  HIS   A CD2 1 
ATOM   1246 C  CE1 . HIS   A 1 167 ? -17.98228 7.79150   61.17620  1.000 70.89888 ? 167  HIS   A CE1 1 
ATOM   1247 N  NE2 . HIS   A 1 167 ? -18.69485 6.88296   61.81888  1.000 87.77470 ? 167  HIS   A NE2 1 
ATOM   1248 N  N   . THR   A 1 168 ? -14.83640 3.60902   61.44961  1.000 33.24574 ? 168  THR   A N   1 
ATOM   1249 C  CA  . THR   A 1 168 ? -14.39048 3.39749   62.82072  1.000 31.72320 ? 168  THR   A CA  1 
ATOM   1250 C  C   . THR   A 1 168 ? -13.13603 2.53908   62.93161  1.000 36.14778 ? 168  THR   A C   1 
ATOM   1251 O  O   . THR   A 1 168 ? -12.34441 2.73571   63.85705  1.000 33.02415 ? 168  THR   A O   1 
ATOM   1252 C  CB  . THR   A 1 168 ? -15.52847 2.76049   63.64411  1.000 33.51356 ? 168  THR   A CB  1 
ATOM   1253 O  OG1 . THR   A 1 168 ? -16.05920 1.64497   62.92258  1.000 62.03574 ? 168  THR   A OG1 1 
ATOM   1254 C  CG2 . THR   A 1 168 ? -16.65757 3.77193   63.85264  1.000 40.10541 ? 168  THR   A CG2 1 
ATOM   1255 N  N   . GLN   A 1 169 ? -12.91598 1.60878   62.00542  1.000 25.08826 ? 169  GLN   A N   1 
ATOM   1256 C  CA  . GLN   A 1 169 ? -11.74279 0.74544   62.05408  1.000 25.96731 ? 169  GLN   A CA  1 
ATOM   1257 C  C   . GLN   A 1 169 ? -11.27378 0.53142   60.62414  1.000 27.84378 ? 169  GLN   A C   1 
ATOM   1258 O  O   . GLN   A 1 169 ? -12.10491 0.30158   59.73862  1.000 24.58103 ? 169  GLN   A O   1 
ATOM   1259 C  CB  . GLN   A 1 169 ? -12.08355 -0.58553  62.73271  1.000 30.09510 ? 169  GLN   A CB  1 
ATOM   1260 C  CG  . GLN   A 1 169 ? -10.91226 -1.54107  62.89990  1.000 24.51254 ? 169  GLN   A CG  1 
ATOM   1261 C  CD  . GLN   A 1 169 ? -11.32276 -2.79800  63.60392  1.000 35.22087 ? 169  GLN   A CD  1 
ATOM   1262 O  OE1 . GLN   A 1 169 ? -11.81702 -3.73353  62.98257  1.000 32.95421 ? 169  GLN   A OE1 1 
ATOM   1263 N  NE2 . GLN   A 1 169 ? -11.13963 -2.82407  64.92070  1.000 28.04487 ? 169  GLN   A NE2 1 
ATOM   1264 N  N   . ASP   A 1 170 ? -9.96772  0.67186   60.39292  1.000 25.71941 ? 170  ASP   A N   1 
ATOM   1265 C  CA  . ASP   A 1 170 ? -9.40026  0.45681   59.06805  1.000 25.09257 ? 170  ASP   A CA  1 
ATOM   1266 C  C   . ASP   A 1 170 ? -9.26024  -1.04281  58.80598  1.000 29.19733 ? 170  ASP   A C   1 
ATOM   1267 O  O   . ASP   A 1 170 ? -9.38442  -1.87386  59.70553  1.000 25.07587 ? 170  ASP   A O   1 
ATOM   1268 C  CB  . ASP   A 1 170 ? -8.02035  1.11158   58.93853  1.000 23.26491 ? 170  ASP   A CB  1 
ATOM   1269 C  CG  . ASP   A 1 170 ? -8.06340  2.62763   58.84891  1.000 26.29672 ? 170  ASP   A CG  1 
ATOM   1270 O  OD1 . ASP   A 1 170 ? -9.13861  3.22733   59.02147  1.000 24.55913 ? 170  ASP   A OD1 1 
ATOM   1271 O  OD2 . ASP   A 1 170 ? -6.98186  3.21724   58.60450  1.000 26.15161 ? 170  ASP   A OD2 1 
ATOM   1272 N  N   A THR   A 1 171 ? -9.00507  -1.38005  57.55056  0.545 30.93324 ? 171  THR   A N   1 
ATOM   1273 N  N   B THR   A 1 171 ? -8.98103  -1.40182  57.55505  0.455 30.91041 ? 171  THR   A N   1 
ATOM   1274 C  CA  A THR   A 1 171 ? -8.76511  -2.75457  57.14786  0.545 31.69768 ? 171  THR   A CA  1 
ATOM   1275 C  CA  B THR   A 1 171 ? -8.77652  -2.80363  57.20522  0.455 31.64166 ? 171  THR   A CA  1 
ATOM   1276 C  C   A THR   A 1 171 ? -7.37776  -2.83247  56.52184  0.545 32.59826 ? 171  THR   A C   1 
ATOM   1277 C  C   B THR   A 1 171 ? -7.48363  -2.94728  56.41086  0.455 32.63884 ? 171  THR   A C   1 
ATOM   1278 O  O   A THR   A 1 171 ? -6.95304  -1.91187  55.82298  0.545 27.52655 ? 171  THR   A O   1 
ATOM   1279 O  O   B THR   A 1 171 ? -7.24972  -2.20180  55.45694  0.455 30.18778 ? 171  THR   A O   1 
ATOM   1280 C  CB  A THR   A 1 171 ? -9.84904  -3.24586  56.16591  0.545 31.26453 ? 171  THR   A CB  1 
ATOM   1281 C  CB  B THR   A 1 171 ? -9.97012  -3.37782  56.41829  0.455 31.95246 ? 171  THR   A CB  1 
ATOM   1282 O  OG1 A THR   A 1 171 ? -11.14994 -3.06020  56.74761  0.545 30.71331 ? 171  THR   A OG1 1 
ATOM   1283 O  OG1 B THR   A 1 171 ? -10.17136 -2.63586  55.21202  0.455 27.83442 ? 171  THR   A OG1 1 
ATOM   1284 C  CG2 A THR   A 1 171 ? -9.66382  -4.71952  55.86963  0.545 27.21448 ? 171  THR   A CG2 1 
ATOM   1285 C  CG2 B THR   A 1 171 ? -11.25151 -3.33515  57.26434  0.455 25.80075 ? 171  THR   A CG2 1 
ATOM   1286 N  N   . LEU   A 1 172 ? -6.64696  -3.89961  56.81388  1.000 38.40539 ? 172  LEU   A N   1 
ATOM   1287 C  CA  . LEU   A 1 172 ? -5.33973  -4.12035  56.20822  1.000 32.95989 ? 172  LEU   A CA  1 
ATOM   1288 C  C   . LEU   A 1 172 ? -5.49936  -5.27153  55.23933  1.000 33.23645 ? 172  LEU   A C   1 
ATOM   1289 O  O   . LEU   A 1 172 ? -5.84956  -6.38235  55.65324  1.000 38.04610 ? 172  LEU   A O   1 
ATOM   1290 C  CB  . LEU   A 1 172 ? -4.25593  -4.41669  57.25548  1.000 36.80019 ? 172  LEU   A CB  1 
ATOM   1291 C  CG  . LEU   A 1 172 ? -2.83257  -4.72237  56.74566  1.000 37.44103 ? 172  LEU   A CG  1 
ATOM   1292 C  CD1 . LEU   A 1 172 ? -2.26685  -3.56543  55.89382  1.000 35.58033 ? 172  LEU   A CD1 1 
ATOM   1293 C  CD2 . LEU   A 1 172 ? -1.84275  -5.08229  57.88408  1.000 28.87883 ? 172  LEU   A CD2 1 
ATOM   1294 N  N   . VAL   A 1 173 ? -5.31884  -4.98700  53.94949  1.000 39.95087 ? 173  VAL   A N   1 
ATOM   1295 C  CA  . VAL   A 1 173 ? -5.58667  -5.93447  52.87416  1.000 43.02384 ? 173  VAL   A CA  1 
ATOM   1296 C  C   . VAL   A 1 173 ? -4.26302  -6.45354  52.32956  1.000 48.87185 ? 173  VAL   A C   1 
ATOM   1297 O  O   . VAL   A 1 173 ? -3.32246  -5.67818  52.10194  1.000 37.58754 ? 173  VAL   A O   1 
ATOM   1298 C  CB  . VAL   A 1 173 ? -6.41890  -5.29896  51.74744  1.000 36.66012 ? 173  VAL   A CB  1 
ATOM   1299 C  CG1 . VAL   A 1 173 ? -6.72537  -6.33969  50.70736  1.000 39.01583 ? 173  VAL   A CG1 1 
ATOM   1300 C  CG2 . VAL   A 1 173 ? -7.69760  -4.72567  52.30395  1.000 44.22910 ? 173  VAL   A CG2 1 
ATOM   1301 N  N   . ALA   A 1 174 ? -4.19045  -7.76349  52.12700  1.000 53.35957 ? 174  ALA   A N   1 
ATOM   1302 C  CA  . ALA   A 1 174 ? -3.07053  -8.39449  51.44900  1.000 61.20003 ? 174  ALA   A CA  1 
ATOM   1303 C  C   . ALA   A 1 174 ? -3.53568  -8.94057  50.10392  1.000 66.94945 ? 174  ALA   A C   1 
ATOM   1304 O  O   . ALA   A 1 174 ? -4.70212  -9.31531  49.93181  1.000 61.20592 ? 174  ALA   A O   1 
ATOM   1305 C  CB  . ALA   A 1 174 ? -2.46703  -9.51257  52.30202  1.000 54.34997 ? 174  ALA   A CB  1 
ATOM   1306 N  N   . GLN   A 1 175 ? -2.61874  -8.96483  49.14366  1.000 71.84274 ? 175  GLN   A N   1 
ATOM   1307 C  CA  . GLN   A 1 175 ? -2.94863  -9.43449  47.80589  1.000 73.20945 ? 175  GLN   A CA  1 
ATOM   1308 C  C   . GLN   A 1 175 ? -2.48711  -10.87612 47.61218  1.000 75.37384 ? 175  GLN   A C   1 
ATOM   1309 O  O   . GLN   A 1 175 ? -3.28586  -11.81309 47.70102  1.000 74.80164 ? 175  GLN   A O   1 
ATOM   1310 C  CB  . GLN   A 1 175 ? -2.32524  -8.52175  46.74640  1.000 72.58537 ? 175  GLN   A CB  1 
ATOM   1311 N  N   . PRO   A 1 181 ? -2.58063  -10.77363 40.00999  1.000 90.18614 ? 181  PRO   A N   1 
ATOM   1312 C  CA  . PRO   A 1 181 ? -1.61214  -9.68092  39.85694  1.000 91.32311 ? 181  PRO   A CA  1 
ATOM   1313 C  C   . PRO   A 1 181 ? -0.79281  -9.81447  38.57752  1.000 85.47417 ? 181  PRO   A C   1 
ATOM   1314 O  O   . PRO   A 1 181 ? 0.42284   -9.98641  38.65585  1.000 74.34189 ? 181  PRO   A O   1 
ATOM   1315 C  CB  . PRO   A 1 181 ? -0.71903  -9.83168  41.09176  1.000 77.33966 ? 181  PRO   A CB  1 
ATOM   1316 C  CG  . PRO   A 1 181 ? -0.76622  -11.29580 41.39770  1.000 87.64076 ? 181  PRO   A CG  1 
ATOM   1317 C  CD  . PRO   A 1 181 ? -2.15515  -11.75828 41.02208  1.000 85.71397 ? 181  PRO   A CD  1 
ATOM   1318 N  N   . GLU   A 1 182 ? -1.44109  -9.73290  37.42069  1.000 85.85237 ? 182  GLU   A N   1 
ATOM   1319 C  CA  . GLU   A 1 182 ? -0.78758  -10.01986 36.14398  1.000 92.46861 ? 182  GLU   A CA  1 
ATOM   1320 C  C   . GLU   A 1 182 ? -1.05189  -8.91879  35.12567  1.000 87.82905 ? 182  GLU   A C   1 
ATOM   1321 O  O   . GLU   A 1 182 ? -2.19641  -8.78089  34.64511  1.000 82.10232 ? 182  GLU   A O   1 
ATOM   1322 C  CB  . GLU   A 1 182 ? -1.24565  -11.37150 35.60486  1.000 68.91453 ? 182  GLU   A CB  1 
ATOM   1323 N  N   . PRO   A 1 183 ? -0.03793  -8.12901  34.75923  1.000 76.10845 ? 183  PRO   A N   1 
ATOM   1324 C  CA  . PRO   A 1 183 ? 1.32623   -8.15687  35.31058  1.000 61.33506 ? 183  PRO   A CA  1 
ATOM   1325 C  C   . PRO   A 1 183 ? 1.42692   -7.35582  36.61543  1.000 57.31853 ? 183  PRO   A C   1 
ATOM   1326 O  O   . PRO   A 1 183 ? 0.41643   -6.93231  37.17586  1.000 55.27291 ? 183  PRO   A O   1 
ATOM   1327 C  CB  . PRO   A 1 183 ? 2.16542   -7.54979  34.17700  1.000 72.02181 ? 183  PRO   A CB  1 
ATOM   1328 C  CG  . PRO   A 1 183 ? 1.22051   -6.60156  33.47918  1.000 80.55039 ? 183  PRO   A CG  1 
ATOM   1329 C  CD  . PRO   A 1 183 ? -0.14926  -7.23801  33.58820  1.000 81.34154 ? 183  PRO   A CD  1 
ATOM   1330 N  N   . GLU   A 1 184 ? 2.62696   -7.15315  37.14721  1.000 55.82708 ? 184  GLU   A N   1 
ATOM   1331 C  CA  . GLU   A 1 184 ? 2.79611   -6.27978  38.29883  1.000 34.66448 ? 184  GLU   A CA  1 
ATOM   1332 C  C   . GLU   A 1 184 ? 3.18456   -4.88726  37.82017  1.000 45.61423 ? 184  GLU   A C   1 
ATOM   1333 O  O   . GLU   A 1 184 ? 3.73694   -4.70874  36.73081  1.000 45.35627 ? 184  GLU   A O   1 
ATOM   1334 C  CB  . GLU   A 1 184 ? 3.84498   -6.83426  39.26136  1.000 43.37066 ? 184  GLU   A CB  1 
ATOM   1335 C  CG  . GLU   A 1 184 ? 3.38154   -8.05164  40.03747  1.000 58.02973 ? 184  GLU   A CG  1 
ATOM   1336 C  CD  . GLU   A 1 184 ? 4.52129   -8.76756  40.74771  1.000 73.02295 ? 184  GLU   A CD  1 
ATOM   1337 O  OE1 . GLU   A 1 184 ? 5.37017   -9.37495  40.05821  1.000 59.53366 ? 184  GLU   A OE1 1 
ATOM   1338 O  OE2 . GLU   A 1 184 ? 4.56774   -8.71858  41.99786  1.000 63.51610 ? 184  GLU   A OE2 1 
ATOM   1339 N  N   . HIS   A 1 185 ? 2.86350   -3.89319  38.63778  1.000 34.76625 ? 185  HIS   A N   1 
ATOM   1340 C  CA  . HIS   A 1 185 ? 3.07828   -2.50943  38.25864  1.000 33.46639 ? 185  HIS   A CA  1 
ATOM   1341 C  C   . HIS   A 1 185 ? 3.43783   -1.74596  39.51414  1.000 31.96544 ? 185  HIS   A C   1 
ATOM   1342 O  O   . HIS   A 1 185 ? 3.06097   -2.14281  40.61927  1.000 30.00519 ? 185  HIS   A O   1 
ATOM   1343 C  CB  . HIS   A 1 185 ? 1.82368   -1.89382  37.60205  1.000 33.60561 ? 185  HIS   A CB  1 
ATOM   1344 C  CG  . HIS   A 1 185 ? 0.62345   -1.85579  38.50454  1.000 31.92197 ? 185  HIS   A CG  1 
ATOM   1345 N  ND1 . HIS   A 1 185 ? -0.28091  -2.89424  38.59370  1.000 31.60487 ? 185  HIS   A ND1 1 
ATOM   1346 C  CD2 . HIS   A 1 185 ? 0.18833   -0.90823  39.37137  1.000 32.59950 ? 185  HIS   A CD2 1 
ATOM   1347 C  CE1 . HIS   A 1 185 ? -1.22179  -2.58673  39.46909  1.000 36.17284 ? 185  HIS   A CE1 1 
ATOM   1348 N  NE2 . HIS   A 1 185 ? -0.95799  -1.38841  39.95985  1.000 33.97486 ? 185  HIS   A NE2 1 
ATOM   1349 N  N   . VAL   A 1 186 ? 4.16957   -0.65653  39.34289  1.000 33.77310 ? 186  VAL   A N   1 
ATOM   1350 C  CA  . VAL   A 1 186 ? 4.30167   0.33623   40.39744  1.000 32.27067 ? 186  VAL   A CA  1 
ATOM   1351 C  C   . VAL   A 1 186 ? 3.44437   1.52426   39.99091  1.000 28.78240 ? 186  VAL   A C   1 
ATOM   1352 O  O   . VAL   A 1 186 ? 3.01826   1.65360   38.83719  1.000 31.27697 ? 186  VAL   A O   1 
ATOM   1353 C  CB  . VAL   A 1 186 ? 5.77115   0.74591   40.64948  1.000 36.69840 ? 186  VAL   A CB  1 
ATOM   1354 C  CG1 . VAL   A 1 186 ? 6.63182   -0.50498  40.89246  1.000 26.40183 ? 186  VAL   A CG1 1 
ATOM   1355 C  CG2 . VAL   A 1 186 ? 6.31661   1.51471   39.49282  1.000 35.96675 ? 186  VAL   A CG2 1 
ATOM   1356 N  N   . ILE   A 1 187 ? 3.15331   2.37946   40.95834  1.000 30.45017 ? 187  ILE   A N   1 
ATOM   1357 C  CA  . ILE   A 1 187 ? 2.50238   3.65977   40.70793  1.000 28.66089 ? 187  ILE   A CA  1 
ATOM   1358 C  C   . ILE   A 1 187 ? 3.56466   4.74077   40.84905  1.000 29.76497 ? 187  ILE   A C   1 
ATOM   1359 O  O   . ILE   A 1 187 ? 4.24916   4.81940   41.87859  1.000 28.71776 ? 187  ILE   A O   1 
ATOM   1360 C  CB  . ILE   A 1 187 ? 1.33171   3.91370   41.68010  1.000 29.52336 ? 187  ILE   A CB  1 
ATOM   1361 C  CG1 . ILE   A 1 187 ? 0.20546   2.90214   41.46951  1.000 30.48010 ? 187  ILE   A CG1 1 
ATOM   1362 C  CG2 . ILE   A 1 187 ? 0.78322   5.34691   41.50061  1.000 27.29444 ? 187  ILE   A CG2 1 
ATOM   1363 C  CD1 . ILE   A 1 187 ? -0.49226  3.02554   40.07959  1.000 33.81613 ? 187  ILE   A CD1 1 
ATOM   1364 N  N   . VAL   A 1 188 ? 3.70362   5.57147   39.82618  1.000 32.41610 ? 188  VAL   A N   1 
ATOM   1365 C  CA  . VAL   A 1 188 ? 4.61983   6.70075   39.87217  1.000 26.26698 ? 188  VAL   A CA  1 
ATOM   1366 C  C   . VAL   A 1 188 ? 3.78734   7.95074   40.08616  1.000 31.14352 ? 188  VAL   A C   1 
ATOM   1367 O  O   . VAL   A 1 188 ? 2.85318   8.22569   39.32359  1.000 34.89068 ? 188  VAL   A O   1 
ATOM   1368 C  CB  . VAL   A 1 188 ? 5.47025   6.80423   38.59826  1.000 32.39657 ? 188  VAL   A CB  1 
ATOM   1369 C  CG1 . VAL   A 1 188 ? 6.47195   7.95196   38.72159  1.000 27.53620 ? 188  VAL   A CG1 1 
ATOM   1370 C  CG2 . VAL   A 1 188 ? 6.19280   5.49103   38.36446  1.000 28.37789 ? 188  VAL   A CG2 1 
ATOM   1371 N  N   . ALA   A 1 189 ? 4.10975   8.67564   41.14982  1.000 27.24254 ? 189  ALA   A N   1 
ATOM   1372 C  CA  . ALA   A 1 189 ? 3.49185   9.94970   41.47864  1.000 25.42263 ? 189  ALA   A CA  1 
ATOM   1373 C  C   . ALA   A 1 189 ? 4.39866   11.06728  40.98682  1.000 32.94697 ? 189  ALA   A C   1 
ATOM   1374 O  O   . ALA   A 1 189 ? 5.58904   11.09079  41.31029  1.000 34.94958 ? 189  ALA   A O   1 
ATOM   1375 C  CB  . ALA   A 1 189 ? 3.26579   10.06563  42.99074  1.000 26.02450 ? 189  ALA   A CB  1 
ATOM   1376 N  N   . CYS   A 1 190 ? 3.83895   11.97534  40.18927  1.000 34.68848 ? 190  CYS   A N   1 
ATOM   1377 C  CA  . CYS   A 1 190 ? 4.57975   13.11648  39.66898  1.000 29.23989 ? 190  CYS   A CA  1 
ATOM   1378 C  C   . CYS   A 1 190 ? 3.60675   14.27731  39.49544  1.000 29.74962 ? 190  CYS   A C   1 
ATOM   1379 O  O   . CYS   A 1 190 ? 2.56354   14.11220  38.85514  1.000 32.68227 ? 190  CYS   A O   1 
ATOM   1380 C  CB  . CYS   A 1 190 ? 5.24738   12.75545  38.34342  1.000 33.41001 ? 190  CYS   A CB  1 
ATOM   1381 S  SG  . CYS   A 1 190 ? 6.45612   13.95890  37.75526  1.000 38.42784 ? 190  CYS   A SG  1 
ATOM   1382 N  N   . CYS   A 1 191 ? 3.93375   15.43511  40.07671  1.000 31.99566 ? 191  CYS   A N   1 
ATOM   1383 C  CA  . CYS   A 1 191 ? 3.06322   16.61280  39.97975  1.000 30.61975 ? 191  CYS   A CA  1 
ATOM   1384 C  C   . CYS   A 1 191 ? 1.65048   16.29056  40.44974  1.000 35.35781 ? 191  CYS   A C   1 
ATOM   1385 O  O   . CYS   A 1 191 ? 0.66682   16.75484  39.87667  1.000 36.35523 ? 191  CYS   A O   1 
ATOM   1386 C  CB  . CYS   A 1 191 ? 3.02476   17.15867  38.55668  1.000 41.97967 ? 191  CYS   A CB  1 
ATOM   1387 S  SG  . CYS   A 1 191 ? 4.61561   17.63738  37.92272  1.000 49.07449 ? 191  CYS   A SG  1 
ATOM   1388 N  N   . ASN   A 1 192 ? 1.55173   15.44941  41.47603  1.000 32.47564 ? 192  ASN   A N   1 
ATOM   1389 C  CA  . ASN   A 1 192 ? 0.29991   15.02787  42.09983  1.000 34.89793 ? 192  ASN   A CA  1 
ATOM   1390 C  C   . ASN   A 1 192 ? -0.53300  14.13352  41.20083  1.000 34.29016 ? 192  ASN   A C   1 
ATOM   1391 O  O   . ASN   A 1 192 ? -1.69118  13.83869  41.53831  1.000 32.19858 ? 192  ASN   A O   1 
ATOM   1392 C  CB  . ASN   A 1 192 ? -0.53367  16.22748  42.55983  1.000 31.49403 ? 192  ASN   A CB  1 
ATOM   1393 C  CG  . ASN   A 1 192 ? 0.22316   17.10184  43.53846  1.000 33.21737 ? 192  ASN   A CG  1 
ATOM   1394 O  OD1 . ASN   A 1 192 ? 1.14198   16.63469  44.20866  1.000 36.85338 ? 192  ASN   A OD1 1 
ATOM   1395 N  ND2 . ASN   A 1 192 ? -0.15281  18.37306  43.62669  1.000 32.07335 ? 192  ASN   A ND2 1 
ATOM   1396 N  N   . GLN   A 1 193 ? 0.02915   13.69296  40.07580  1.000 28.74371 ? 193  GLN   A N   1 
ATOM   1397 C  CA  . GLN   A 1 193 ? -0.58561  12.77982  39.12410  1.000 30.89690 ? 193  GLN   A CA  1 
ATOM   1398 C  C   . GLN   A 1 193 ? -0.01814  11.38540  39.34882  1.000 31.90009 ? 193  GLN   A C   1 
ATOM   1399 O  O   . GLN   A 1 193 ? 1.15663   11.23730  39.68385  1.000 34.85057 ? 193  GLN   A O   1 
ATOM   1400 C  CB  . GLN   A 1 193 ? -0.29391  13.21895  37.67868  1.000 31.17130 ? 193  GLN   A CB  1 
ATOM   1401 C  CG  . GLN   A 1 193 ? -0.43830  14.73453  37.41406  1.000 33.68247 ? 193  GLN   A CG  1 
ATOM   1402 C  CD  . GLN   A 1 193 ? -1.84831  15.21180  37.62174  1.000 33.22356 ? 193  GLN   A CD  1 
ATOM   1403 O  OE1 . GLN   A 1 193 ? -2.74724  14.81767  36.88764  1.000 35.93966 ? 193  GLN   A OE1 1 
ATOM   1404 N  NE2 . GLN   A 1 193 ? -2.06522  16.03926  38.65842  1.000 37.99203 ? 193  GLN   A NE2 1 
ATOM   1405 N  N   . PHE   A 1 194 ? -0.84990  10.36238  39.13406  1.000 34.09863 ? 194  PHE   A N   1 
ATOM   1406 C  CA  . PHE   A 1 194 ? -0.46239  8.96773   39.31656  1.000 32.87332 ? 194  PHE   A CA  1 
ATOM   1407 C  C   . PHE   A 1 194 ? -0.50482  8.21793   37.98813  1.000 35.00066 ? 194  PHE   A C   1 
ATOM   1408 O  O   . PHE   A 1 194 ? -1.46224  8.34240   37.21997  1.000 37.76370 ? 194  PHE   A O   1 
ATOM   1409 C  CB  . PHE   A 1 194 ? -1.37082  8.27741   40.33781  1.000 29.59906 ? 194  PHE   A CB  1 
ATOM   1410 C  CG  . PHE   A 1 194 ? -1.41764  8.98698   41.65166  1.000 34.52208 ? 194  PHE   A CG  1 
ATOM   1411 C  CD1 . PHE   A 1 194 ? -0.36895  8.86037   42.55767  1.000 31.75282 ? 194  PHE   A CD1 1 
ATOM   1412 C  CD2 . PHE   A 1 194 ? -2.48573  9.80338   41.97081  1.000 28.93238 ? 194  PHE   A CD2 1 
ATOM   1413 C  CE1 . PHE   A 1 194 ? -0.40592  9.53680   43.78743  1.000 32.49533 ? 194  PHE   A CE1 1 
ATOM   1414 C  CE2 . PHE   A 1 194 ? -2.53428  10.48212  43.16906  1.000 27.83955 ? 194  PHE   A CE2 1 
ATOM   1415 C  CZ  . PHE   A 1 194 ? -1.49790  10.35712  44.08353  1.000 28.07821 ? 194  PHE   A CZ  1 
ATOM   1416 N  N   . PHE   A 1 195 ? 0.53398   7.42183   37.74325  1.000 35.19080 ? 195  PHE   A N   1 
ATOM   1417 C  CA  . PHE   A 1 195 ? 0.71263   6.68212   36.50564  1.000 33.46436 ? 195  PHE   A CA  1 
ATOM   1418 C  C   . PHE   A 1 195 ? 0.97335   5.22220   36.82549  1.000 36.32370 ? 195  PHE   A C   1 
ATOM   1419 O  O   . PHE   A 1 195 ? 1.73353   4.90556   37.74488  1.000 32.69219 ? 195  PHE   A O   1 
ATOM   1420 C  CB  . PHE   A 1 195 ? 1.86632   7.24719   35.69370  1.000 37.19980 ? 195  PHE   A CB  1 
ATOM   1421 C  CG  . PHE   A 1 195 ? 1.59019   8.61306   35.14186  1.000 36.41656 ? 195  PHE   A CG  1 
ATOM   1422 C  CD1 . PHE   A 1 195 ? 1.82271   9.74580   35.91222  1.000 40.73941 ? 195  PHE   A CD1 1 
ATOM   1423 C  CD2 . PHE   A 1 195 ? 1.09195   8.76775   33.86835  1.000 42.24627 ? 195  PHE   A CD2 1 
ATOM   1424 C  CE1 . PHE   A 1 195 ? 1.55617   10.99854  35.40922  1.000 43.44873 ? 195  PHE   A CE1 1 
ATOM   1425 C  CE2 . PHE   A 1 195 ? 0.82278   10.02616  33.36287  1.000 46.48020 ? 195  PHE   A CE2 1 
ATOM   1426 C  CZ  . PHE   A 1 195 ? 1.05165   11.13241  34.13669  1.000 41.38035 ? 195  PHE   A CZ  1 
ATOM   1427 N  N   . VAL   A 1 196 ? 0.32251   4.34210   36.07870  1.000 34.25332 ? 196  VAL   A N   1 
ATOM   1428 C  CA  . VAL   A 1 196 ? 0.61243   2.91602   36.14338  1.000 36.27850 ? 196  VAL   A CA  1 
ATOM   1429 C  C   . VAL   A 1 196 ? 1.87499   2.64965   35.33355  1.000 38.34259 ? 196  VAL   A C   1 
ATOM   1430 O  O   . VAL   A 1 196 ? 1.90902   2.89329   34.12602  1.000 39.47511 ? 196  VAL   A O   1 
ATOM   1431 C  CB  . VAL   A 1 196 ? -0.56497  2.09043   35.60941  1.000 42.63104 ? 196  VAL   A CB  1 
ATOM   1432 C  CG1 . VAL   A 1 196 ? -0.24179  0.58913   35.69281  1.000 40.10004 ? 196  VAL   A CG1 1 
ATOM   1433 C  CG2 . VAL   A 1 196 ? -1.82723  2.41409   36.38167  1.000 43.42989 ? 196  VAL   A CG2 1 
ATOM   1434 N  N   . LEU   A 1 197 ? 2.91388   2.15077   35.98845  1.000 38.77514 ? 197  LEU   A N   1 
ATOM   1435 C  CA  . LEU   A 1 197 ? 4.13789   1.74248   35.29875  1.000 37.78587 ? 197  LEU   A CA  1 
ATOM   1436 C  C   . LEU   A 1 197 ? 4.24149   0.22242   35.36579  1.000 38.12089 ? 197  LEU   A C   1 
ATOM   1437 O  O   . LEU   A 1 197 ? 4.62442   -0.33466  36.39925  1.000 43.65674 ? 197  LEU   A O   1 
ATOM   1438 C  CB  . LEU   A 1 197 ? 5.35747   2.40366   35.92741  1.000 30.27485 ? 197  LEU   A CB  1 
ATOM   1439 C  CG  . LEU   A 1 197 ? 6.72024   1.94542   35.40602  1.000 34.27947 ? 197  LEU   A CG  1 
ATOM   1440 C  CD1 . LEU   A 1 197 ? 6.84444   2.25246   33.93102  1.000 36.35224 ? 197  LEU   A CD1 1 
ATOM   1441 C  CD2 . LEU   A 1 197 ? 7.83051   2.63390   36.19437  1.000 34.70825 ? 197  LEU   A CD2 1 
ATOM   1442 N  N   . ASP   A 1 198 ? 3.88463   -0.45520  34.27980  1.000 36.81633 ? 198  ASP   A N   1 
ATOM   1443 C  CA  . ASP   A 1 198 ? 4.09469   -1.89544  34.23751  1.000 38.17777 ? 198  ASP   A CA  1 
ATOM   1444 C  C   . ASP   A 1 198 ? 5.59242   -2.17181  34.24433  1.000 41.29501 ? 198  ASP   A C   1 
ATOM   1445 O  O   . ASP   A 1 198 ? 6.36146   -1.50723  33.54515  1.000 45.14863 ? 198  ASP   A O   1 
ATOM   1446 C  CB  . ASP   A 1 198 ? 3.43402   -2.51255  33.00339  1.000 38.88296 ? 198  ASP   A CB  1 
ATOM   1447 C  CG  . ASP   A 1 198 ? 1.91976   -2.41911  33.03952  1.000 52.39338 ? 198  ASP   A CG  1 
ATOM   1448 O  OD1 . ASP   A 1 198 ? 1.34757   -2.40729  34.14507  1.000 46.46249 ? 198  ASP   A OD1 1 
ATOM   1449 O  OD2 . ASP   A 1 198 ? 1.29499   -2.36292  31.95859  1.000 63.01724 ? 198  ASP   A OD2 1 
ATOM   1450 N  N   . VAL   A 1 199 ? 6.01981   -3.11705  35.06916  1.000 42.54025 ? 199  VAL   A N   1 
ATOM   1451 C  CA  . VAL   A 1 199 ? 7.43560   -3.41754  35.18197  1.000 43.58222 ? 199  VAL   A CA  1 
ATOM   1452 C  C   . VAL   A 1 199 ? 7.75731   -4.76902  34.54376  1.000 58.12272 ? 199  VAL   A C   1 
ATOM   1453 O  O   . VAL   A 1 199 ? 8.77723   -5.38715  34.85307  1.000 54.72113 ? 199  VAL   A O   1 
ATOM   1454 C  CB  . VAL   A 1 199 ? 7.89076   -3.32745  36.64408  1.000 42.44278 ? 199  VAL   A CB  1 
ATOM   1455 C  CG1 . VAL   A 1 199 ? 7.84919   -1.85399  37.09707  1.000 35.78006 ? 199  VAL   A CG1 1 
ATOM   1456 C  CG2 . VAL   A 1 199 ? 6.97814   -4.15254  37.51765  1.000 52.94857 ? 199  VAL   A CG2 1 
ATOM   1457 N  N   . VAL   A 1 200 ? 6.88398   -5.21390  33.63544  1.000 56.71240 ? 200  VAL   A N   1 
ATOM   1458 C  CA  . VAL   A 1 200 ? 7.00589   -6.46080  32.88821  1.000 49.68012 ? 200  VAL   A CA  1 
ATOM   1459 C  C   . VAL   A 1 200 ? 6.40105   -6.23966  31.50359  1.000 58.60796 ? 200  VAL   A C   1 
ATOM   1460 O  O   . VAL   A 1 200 ? 5.24704   -5.81471  31.38377  1.000 58.77004 ? 200  VAL   A O   1 
ATOM   1461 C  CB  . VAL   A 1 200 ? 6.30660   -7.62074  33.63088  1.000 62.10425 ? 200  VAL   A CB  1 
ATOM   1462 C  CG1 . VAL   A 1 200 ? 6.08957   -8.77517  32.70859  1.000 57.69918 ? 200  VAL   A CG1 1 
ATOM   1463 C  CG2 . VAL   A 1 200 ? 7.09870   -8.05610  34.87396  1.000 51.22167 ? 200  VAL   A CG2 1 
ATOM   1464 N  N   . ILE   A 1 201 ? 7.17739   -6.50231  30.45112  1.000 61.90130 ? 201  ILE   A N   1 
ATOM   1465 C  CA  . ILE   A 1 201 ? 6.69723   -6.48519  29.06943  1.000 63.55521 ? 201  ILE   A CA  1 
ATOM   1466 C  C   . ILE   A 1 201 ? 6.93695   -7.86638  28.48028  1.000 56.63015 ? 201  ILE   A C   1 
ATOM   1467 O  O   . ILE   A 1 201 ? 8.07837   -8.34902  28.46878  1.000 58.55612 ? 201  ILE   A O   1 
ATOM   1468 C  CB  . ILE   A 1 201 ? 7.39195   -5.40901  28.21763  1.000 56.88546 ? 201  ILE   A CB  1 
ATOM   1469 N  N   . ASN   A 1 202 ? 5.86418   -8.49322  27.98353  1.000 75.32498 ? 202  ASN   A N   1 
ATOM   1470 C  CA  . ASN   A 1 202 ? 5.91419   -9.84335  27.41021  1.000 67.78789 ? 202  ASN   A CA  1 
ATOM   1471 C  C   . ASN   A 1 202 ? 6.58057   -10.82864 28.37145  1.000 70.55209 ? 202  ASN   A C   1 
ATOM   1472 O  O   . ASN   A 1 202 ? 7.37831   -11.68099 27.96719  1.000 75.34381 ? 202  ASN   A O   1 
ATOM   1473 C  CB  . ASN   A 1 202 ? 6.61353   -9.84182  26.04575  1.000 72.76025 ? 202  ASN   A CB  1 
ATOM   1474 N  N   . PHE   A 1 203 ? 6.24251   -10.69908 29.65992  1.000 71.12648 ? 203  PHE   A N   1 
ATOM   1475 C  CA  . PHE   A 1 203 ? 6.72723   -11.51627 30.77316  1.000 79.81823 ? 203  PHE   A CA  1 
ATOM   1476 C  C   . PHE   A 1 203 ? 8.22196   -11.35390 31.02803  1.000 75.02502 ? 203  PHE   A C   1 
ATOM   1477 O  O   . PHE   A 1 203 ? 8.79973   -12.11704 31.81123  1.000 80.14969 ? 203  PHE   A O   1 
ATOM   1478 C  CB  . PHE   A 1 203 ? 6.36115   -12.99344 30.57773  1.000 55.28190 ? 203  PHE   A CB  1 
ATOM   1479 C  CG  . PHE   A 1 203 ? 4.88297   -13.21999 30.49643  1.000 52.48841 ? 203  PHE   A CG  1 
ATOM   1480 C  CD1 . PHE   A 1 203 ? 4.11799   -13.29080 31.64924  1.000 59.25433 ? 203  PHE   A CD1 1 
ATOM   1481 C  CD2 . PHE   A 1 203 ? 4.24946   -13.30831 29.26639  1.000 54.86661 ? 203  PHE   A CD2 1 
ATOM   1482 C  CE1 . PHE   A 1 203 ? 2.74895   -13.47674 31.57756  1.000 51.90380 ? 203  PHE   A CE1 1 
ATOM   1483 C  CE2 . PHE   A 1 203 ? 2.88629   -13.49814 29.19286  1.000 45.57219 ? 203  PHE   A CE2 1 
ATOM   1484 C  CZ  . PHE   A 1 203 ? 2.13634   -13.58142 30.35583  1.000 48.09381 ? 203  PHE   A CZ  1 
ATOM   1485 N  N   . ARG   A 1 204 ? 8.85433   -10.36285 30.40455  1.000 62.47418 ? 204  ARG   A N   1 
ATOM   1486 C  CA  . ARG   A 1 204 ? 10.26633  -10.05905 30.59228  1.000 72.36968 ? 204  ARG   A CA  1 
ATOM   1487 C  C   . ARG   A 1 204 ? 10.38030  -8.79157  31.43202  1.000 73.66070 ? 204  ARG   A C   1 
ATOM   1488 O  O   . ARG   A 1 204 ? 9.90851   -7.72909  31.01291  1.000 60.07142 ? 204  ARG   A O   1 
ATOM   1489 C  CB  . ARG   A 1 204 ? 10.96608  -9.88452  29.24109  1.000 58.85277 ? 204  ARG   A CB  1 
ATOM   1490 N  N   . ARG   A 1 205 ? 10.99082  -8.91256  32.61532  1.000 69.19201 ? 205  ARG   A N   1 
ATOM   1491 C  CA  . ARG   A 1 205 ? 11.20856  -7.77336  33.50560  1.000 57.23463 ? 205  ARG   A CA  1 
ATOM   1492 C  C   . ARG   A 1 205 ? 11.88869  -6.62074  32.77281  1.000 54.35991 ? 205  ARG   A C   1 
ATOM   1493 O  O   . ARG   A 1 205 ? 12.86673  -6.82120  32.04915  1.000 52.91055 ? 205  ARG   A O   1 
ATOM   1494 C  CB  . ARG   A 1 205 ? 12.05510  -8.22192  34.69958  1.000 52.91458 ? 205  ARG   A CB  1 
ATOM   1495 C  CG  . ARG   A 1 205 ? 12.51991  -7.11698  35.60389  1.000 58.63376 ? 205  ARG   A CG  1 
ATOM   1496 C  CD  . ARG   A 1 205 ? 12.36651  -7.51104  37.05532  1.000 64.36885 ? 205  ARG   A CD  1 
ATOM   1497 N  NE  . ARG   A 1 205 ? 13.39769  -8.41556  37.54701  1.000 63.86333 ? 205  ARG   A NE  1 
ATOM   1498 C  CZ  . ARG   A 1 205 ? 14.49154  -8.02968  38.19193  1.000 59.66643 ? 205  ARG   A CZ  1 
ATOM   1499 N  NH1 . ARG   A 1 205 ? 14.78582  -6.74681  38.35692  1.000 52.52076 ? 205  ARG   A NH1 1 
ATOM   1500 N  NH2 . ARG   A 1 205 ? 15.30500  -8.95254  38.69523  1.000 47.96506 ? 205  ARG   A NH2 1 
ATOM   1501 N  N   . LEU   A 1 206 ? 11.34306  -5.41418  32.93371  1.000 59.36396 ? 206  LEU   A N   1 
ATOM   1502 C  CA  . LEU   A 1 206 ? 11.91587  -4.24589  32.27345  1.000 49.28988 ? 206  LEU   A CA  1 
ATOM   1503 C  C   . LEU   A 1 206 ? 13.30826  -3.96492  32.81728  1.000 49.19821 ? 206  LEU   A C   1 
ATOM   1504 O  O   . LEU   A 1 206 ? 13.53651  -4.02277  34.02577  1.000 43.06980 ? 206  LEU   A O   1 
ATOM   1505 C  CB  . LEU   A 1 206 ? 11.03100  -3.01832  32.48193  1.000 40.13662 ? 206  LEU   A CB  1 
ATOM   1506 C  CG  . LEU   A 1 206 ? 10.14908  -2.59846  31.30848  1.000 59.55667 ? 206  LEU   A CG  1 
ATOM   1507 C  CD1 . LEU   A 1 206 ? 9.16075   -3.70063  30.95288  1.000 54.64576 ? 206  LEU   A CD1 1 
ATOM   1508 C  CD2 . LEU   A 1 206 ? 9.42839   -1.29569  31.62768  1.000 53.88834 ? 206  LEU   A CD2 1 
ATOM   1509 N  N   . SER   A 1 207 ? 14.24059  -3.66271  31.91709  1.000 45.98514 ? 207  SER   A N   1 
ATOM   1510 C  CA  . SER   A 1 207 ? 15.58614  -3.28830  32.32298  1.000 52.10434 ? 207  SER   A CA  1 
ATOM   1511 C  C   . SER   A 1 207 ? 15.60184  -1.86346  32.87430  1.000 42.96677 ? 207  SER   A C   1 
ATOM   1512 O  O   . SER   A 1 207 ? 14.64072  -1.10026  32.72474  1.000 42.10422 ? 207  SER   A O   1 
ATOM   1513 C  CB  . SER   A 1 207 ? 16.54268  -3.38648  31.14534  1.000 46.65118 ? 207  SER   A CB  1 
ATOM   1514 O  OG  . SER   A 1 207 ? 16.25623  -2.36399  30.21019  1.000 47.74562 ? 207  SER   A OG  1 
ATOM   1515 N  N   . GLU   A 1 208 ? 16.72810  -1.49993  33.50021  1.000 48.96164 ? 208  GLU   A N   1 
ATOM   1516 C  CA  . GLU   A 1 208 ? 16.90013  -0.13436  33.99692  1.000 55.49442 ? 208  GLU   A CA  1 
ATOM   1517 C  C   . GLU   A 1 208 ? 16.79679  0.89169   32.87229  1.000 44.87067 ? 208  GLU   A C   1 
ATOM   1518 O  O   . GLU   A 1 208 ? 16.29039  2.00128   33.08108  1.000 41.93787 ? 208  GLU   A O   1 
ATOM   1519 C  CB  . GLU   A 1 208 ? 18.24594  0.00915   34.70152  1.000 54.56706 ? 208  GLU   A CB  1 
ATOM   1520 C  CG  . GLU   A 1 208 ? 18.37126  -0.76132  35.98707  1.000 48.52424 ? 208  GLU   A CG  1 
ATOM   1521 C  CD  . GLU   A 1 208 ? 19.58048  -0.32340  36.78837  1.000 58.05174 ? 208  GLU   A CD  1 
ATOM   1522 O  OE1 . GLU   A 1 208 ? 19.93783  0.87162   36.69328  1.000 50.07421 ? 208  GLU   A OE1 1 
ATOM   1523 O  OE2 . GLU   A 1 208 ? 20.16861  -1.16220  37.51080  1.000 73.81135 ? 208  GLU   A OE2 1 
ATOM   1524 N  N   . GLY   A 1 209 ? 17.29829  0.54900   31.68355  1.000 45.16385 ? 209  GLY   A N   1 
ATOM   1525 C  CA  . GLY   A 1 209 ? 17.15162  1.43700   30.54268  1.000 39.40901 ? 209  GLY   A CA  1 
ATOM   1526 C  C   . GLY   A 1 209 ? 15.70422  1.61385   30.12170  1.000 48.68696 ? 209  GLY   A C   1 
ATOM   1527 O  O   . GLY   A 1 209 ? 15.27056  2.72688   29.81476  1.000 44.97870 ? 209  GLY   A O   1 
ATOM   1528 N  N   . ASP   A 1 210 ? 14.93528  0.52023   30.09779  1.000 51.25383 ? 210  ASP   A N   1 
ATOM   1529 C  CA  . ASP   A 1 210 ? 13.51562  0.62713   29.76889  1.000 41.24619 ? 210  ASP   A CA  1 
ATOM   1530 C  C   . ASP   A 1 210 ? 12.77594  1.44958   30.81184  1.000 47.08001 ? 210  ASP   A C   1 
ATOM   1531 O  O   . ASP   A 1 210 ? 11.86631  2.22145   30.47931  1.000 39.53772 ? 210  ASP   A O   1 
ATOM   1532 C  CB  . ASP   A 1 210 ? 12.88430  -0.76107  29.66521  1.000 50.54325 ? 210  ASP   A CB  1 
ATOM   1533 C  CG  . ASP   A 1 210 ? 13.50618  -1.61580  28.57893  1.000 55.57833 ? 210  ASP   A CG  1 
ATOM   1534 O  OD1 . ASP   A 1 210 ? 13.74146  -1.10323  27.46539  1.000 49.67035 ? 210  ASP   A OD1 1 
ATOM   1535 O  OD2 . ASP   A 1 210 ? 13.74662  -2.81217  28.84325  1.000 64.40694 ? 210  ASP   A OD2 1 
ATOM   1536 N  N   . LEU   A 1 211 ? 13.13574  1.27559   32.08658  1.000 43.09513 ? 211  LEU   A N   1 
ATOM   1537 C  CA  . LEU   A 1 211 ? 12.46856  2.01292   33.14895  1.000 44.90965 ? 211  LEU   A CA  1 
ATOM   1538 C  C   . LEU   A 1 211 ? 12.75219  3.50382   33.03560  1.000 38.32253 ? 211  LEU   A C   1 
ATOM   1539 O  O   . LEU   A 1 211 ? 11.84708  4.32665   33.22223  1.000 36.45117 ? 211  LEU   A O   1 
ATOM   1540 C  CB  . LEU   A 1 211 ? 12.90329  1.47371   34.51129  1.000 36.26669 ? 211  LEU   A CB  1 
ATOM   1541 C  CG  . LEU   A 1 211 ? 12.43333  0.05881   34.86082  1.000 48.06460 ? 211  LEU   A CG  1 
ATOM   1542 C  CD1 . LEU   A 1 211 ? 13.24938  -0.51368  36.01729  1.000 34.22448 ? 211  LEU   A CD1 1 
ATOM   1543 C  CD2 . LEU   A 1 211 ? 10.95560  0.05550   35.20814  1.000 41.36139 ? 211  LEU   A CD2 1 
ATOM   1544 N  N   . PHE   A 1 212 ? 14.00808  3.85940   32.74185  1.000 35.66349 ? 212  PHE   A N   1 
ATOM   1545 C  CA  . PHE   A 1 212 ? 14.38656  5.24387   32.45414  1.000 45.88228 ? 212  PHE   A CA  1 
ATOM   1546 C  C   . PHE   A 1 212 ? 13.52106  5.83549   31.34920  1.000 41.68990 ? 212  PHE   A C   1 
ATOM   1547 O  O   . PHE   A 1 212 ? 12.93407  6.91329   31.50514  1.000 47.20041 ? 212  PHE   A O   1 
ATOM   1548 C  CB  . PHE   A 1 212 ? 15.86722  5.29361   32.05329  1.000 36.95035 ? 212  PHE   A CB  1 
ATOM   1549 C  CG  . PHE   A 1 212 ? 16.35262  6.66178   31.62285  1.000 50.58812 ? 212  PHE   A CG  1 
ATOM   1550 C  CD1 . PHE   A 1 212 ? 16.62765  7.65098   32.56527  1.000 50.01399 ? 212  PHE   A CD1 1 
ATOM   1551 C  CD2 . PHE   A 1 212 ? 16.56636  6.94644   30.28381  1.000 44.20098 ? 212  PHE   A CD2 1 
ATOM   1552 C  CE1 . PHE   A 1 212 ? 17.09134  8.90567   32.17083  1.000 43.99343 ? 212  PHE   A CE1 1 
ATOM   1553 C  CE2 . PHE   A 1 212 ? 17.02971  8.20089   29.87747  1.000 50.69600 ? 212  PHE   A CE2 1 
ATOM   1554 C  CZ  . PHE   A 1 212 ? 17.29269  9.17901   30.81738  1.000 47.13718 ? 212  PHE   A CZ  1 
ATOM   1555 N  N   . THR   A 1 213 ? 13.43335  5.13226   30.22121  1.000 41.57125 ? 213  THR   A N   1 
ATOM   1556 C  CA  . THR   A 1 213 ? 12.63948  5.61248   29.09360  1.000 46.89191 ? 213  THR   A CA  1 
ATOM   1557 C  C   . THR   A 1 213 ? 11.19071  5.84779   29.49952  1.000 41.32768 ? 213  THR   A C   1 
ATOM   1558 O  O   . THR   A 1 213 ? 10.58309  6.85277   29.11161  1.000 43.68174 ? 213  THR   A O   1 
ATOM   1559 C  CB  . THR   A 1 213 ? 12.72257  4.60977   27.94275  1.000 45.20674 ? 213  THR   A CB  1 
ATOM   1560 O  OG1 . THR   A 1 213 ? 14.07709  4.52528   27.48532  1.000 46.67156 ? 213  THR   A OG1 1 
ATOM   1561 C  CG2 . THR   A 1 213 ? 11.82087  5.03945   26.78900  1.000 47.86944 ? 213  THR   A CG2 1 
ATOM   1562 N  N   . GLN   A 1 214 ? 10.62940  4.94183   30.30255  1.000 39.29035 ? 214  GLN   A N   1 
ATOM   1563 C  CA  . GLN   A 1 214 ? 9.24158   5.08085   30.73663  1.000 44.31592 ? 214  GLN   A CA  1 
ATOM   1564 C  C   . GLN   A 1 214 ? 9.06453   6.25936   31.68292  1.000 42.15665 ? 214  GLN   A C   1 
ATOM   1565 O  O   . GLN   A 1 214 ? 8.05969   6.98062   31.60505  1.000 40.53661 ? 214  GLN   A O   1 
ATOM   1566 C  CB  . GLN   A 1 214 ? 8.77825   3.78546   31.40241  1.000 39.00216 ? 214  GLN   A CB  1 
ATOM   1567 C  CG  . GLN   A 1 214 ? 8.68023   2.59356   30.42357  1.000 41.57384 ? 214  GLN   A CG  1 
ATOM   1568 C  CD  . GLN   A 1 214 ? 7.58686   2.76902   29.39076  1.000 46.57988 ? 214  GLN   A CD  1 
ATOM   1569 O  OE1 . GLN   A 1 214 ? 7.69585   3.59616   28.48330  1.000 48.10054 ? 214  GLN   A OE1 1 
ATOM   1570 N  NE2 . GLN   A 1 214 ? 6.51584   1.99605   29.52985  1.000 48.00662 ? 214  GLN   A NE2 1 
ATOM   1571 N  N   . LEU   A 1 215 ? 10.02390  6.45874   32.59010  1.000 34.69739 ? 215  LEU   A N   1 
ATOM   1572 C  CA  . LEU   A 1 215 ? 9.93612   7.55221   33.54978  1.000 37.69150 ? 215  LEU   A CA  1 
ATOM   1573 C  C   . LEU   A 1 215 ? 9.98635   8.90397   32.85020  1.000 37.29710 ? 215  LEU   A C   1 
ATOM   1574 O  O   . LEU   A 1 215 ? 9.30550   9.85235   33.26496  1.000 40.92606 ? 215  LEU   A O   1 
ATOM   1575 C  CB  . LEU   A 1 215 ? 11.05906  7.42365   34.58645  1.000 36.16661 ? 215  LEU   A CB  1 
ATOM   1576 C  CG  . LEU   A 1 215 ? 10.89506  6.24243   35.56890  1.000 39.48375 ? 215  LEU   A CG  1 
ATOM   1577 C  CD1 . LEU   A 1 215 ? 12.16869  5.97120   36.35901  1.000 35.93243 ? 215  LEU   A CD1 1 
ATOM   1578 C  CD2 . LEU   A 1 215 ? 9.72822   6.46759   36.51774  1.000 33.25319 ? 215  LEU   A CD2 1 
ATOM   1579 N  N   . ARG   A 1 216 ? 10.79938  9.01711   31.79687  1.000 39.70210 ? 216  ARG   A N   1 
ATOM   1580 C  CA  . ARG   A 1 216 ? 10.77887  10.22585  30.97780  1.000 53.52667 ? 216  ARG   A CA  1 
ATOM   1581 C  C   . ARG   A 1 216 ? 9.39325   10.47875  30.39863  1.000 46.73083 ? 216  ARG   A C   1 
ATOM   1582 O  O   . ARG   A 1 216 ? 8.91922   11.61847  30.39453  1.000 43.62585 ? 216  ARG   A O   1 
ATOM   1583 C  CB  . ARG   A 1 216 ? 11.80161  10.12326  29.85020  1.000 53.12844 ? 216  ARG   A CB  1 
ATOM   1584 C  CG  . ARG   A 1 216 ? 13.16142  10.73050  30.15210  1.000 53.71752 ? 216  ARG   A CG  1 
ATOM   1585 C  CD  . ARG   A 1 216 ? 14.14228  10.24570  29.09844  1.000 68.76033 ? 216  ARG   A CD  1 
ATOM   1586 N  NE  . ARG   A 1 216 ? 15.33393  11.07419  28.96740  1.000 55.43058 ? 216  ARG   A NE  1 
ATOM   1587 C  CZ  . ARG   A 1 216 ? 16.18280  10.99090  27.95212  1.000 67.00506 ? 216  ARG   A CZ  1 
ATOM   1588 N  NH1 . ARG   A 1 216 ? 15.99018  10.13425  26.95848  1.000 54.41636 ? 216  ARG   A NH1 1 
ATOM   1589 N  NH2 . ARG   A 1 216 ? 17.24622  11.79125  27.92816  1.000 63.76056 ? 216  ARG   A NH2 1 
ATOM   1590 N  N   . LYS   A 1 217 ? 8.73580   9.43658   29.87449  1.000 43.87651 ? 217  LYS   A N   1 
ATOM   1591 C  CA  . LYS   A 1 217 ? 7.38874   9.63477   29.34826  1.000 44.10475 ? 217  LYS   A CA  1 
ATOM   1592 C  C   . LYS   A 1 217 ? 6.46587   10.17694  30.42859  1.000 46.34303 ? 217  LYS   A C   1 
ATOM   1593 O  O   . LYS   A 1 217 ? 5.65024   11.07011  30.16827  1.000 41.24640 ? 217  LYS   A O   1 
ATOM   1594 C  CB  . LYS   A 1 217 ? 6.82335   8.33131   28.77774  1.000 42.57782 ? 217  LYS   A CB  1 
ATOM   1595 C  CG  . LYS   A 1 217 ? 7.57668   7.75174   27.57258  1.000 46.76055 ? 217  LYS   A CG  1 
ATOM   1596 C  CD  . LYS   A 1 217 ? 6.91221   6.44702   27.12367  1.000 42.93351 ? 217  LYS   A CD  1 
ATOM   1597 C  CE  . LYS   A 1 217 ? 7.75767   5.69085   26.11885  1.000 49.25064 ? 217  LYS   A CE  1 
ATOM   1598 N  NZ  . LYS   A 1 217 ? 7.09270   4.40425   25.76852  1.000 59.05724 ? 217  LYS   A NZ  1 
ATOM   1599 N  N   . ILE   A 1 218 ? 6.60955   9.66746   31.65624  1.000 39.84486 ? 218  ILE   A N   1 
ATOM   1600 C  CA  . ILE   A 1 218 ? 5.74851   10.07495  32.76082  1.000 39.77250 ? 218  ILE   A CA  1 
ATOM   1601 C  C   . ILE   A 1 218 ? 5.96943   11.54620  33.10198  1.000 45.38376 ? 218  ILE   A C   1 
ATOM   1602 O  O   . ILE   A 1 218 ? 5.01116   12.31688  33.23202  1.000 41.71355 ? 218  ILE   A O   1 
ATOM   1603 C  CB  . ILE   A 1 218 ? 5.99297   9.15521   33.97191  1.000 46.10157 ? 218  ILE   A CB  1 
ATOM   1604 C  CG1 . ILE   A 1 218 ? 5.51685   7.74138   33.64631  1.000 35.10064 ? 218  ILE   A CG1 1 
ATOM   1605 C  CG2 . ILE   A 1 218 ? 5.29478   9.67134   35.21229  1.000 40.34552 ? 218  ILE   A CG2 1 
ATOM   1606 C  CD1 . ILE   A 1 218 ? 5.88864   6.70197   34.69709  1.000 33.51590 ? 218  ILE   A CD1 1 
ATOM   1607 N  N   . VAL   A 1 219 ? 7.23455   11.96161  33.23541  1.000 35.00031 ? 219  VAL   A N   1 
ATOM   1608 C  CA  . VAL   A 1 219 ? 7.53281   13.34741  33.58913  1.000 38.61975 ? 219  VAL   A CA  1 
ATOM   1609 C  C   . VAL   A 1 219 ? 6.97463   14.29545  32.53678  1.000 42.87355 ? 219  VAL   A C   1 
ATOM   1610 O  O   . VAL   A 1 219 ? 6.48748   15.38746  32.85425  1.000 40.61091 ? 219  VAL   A O   1 
ATOM   1611 C  CB  . VAL   A 1 219 ? 9.05118   13.53485  33.79177  1.000 37.26736 ? 219  VAL   A CB  1 
ATOM   1612 C  CG1 . VAL   A 1 219 ? 9.40971   15.00764  33.90332  1.000 39.62183 ? 219  VAL   A CG1 1 
ATOM   1613 C  CG2 . VAL   A 1 219 ? 9.50871   12.80045  35.04181  1.000 33.39315 ? 219  VAL   A CG2 1 
ATOM   1614 N  N   . LYS   A 1 220 ? 6.99978   13.88100  31.27159  1.000 42.96365 ? 220  LYS   A N   1 
ATOM   1615 C  CA  . LYS   A 1 220 ? 6.47102   14.73389  30.21401  1.000 40.20802 ? 220  LYS   A CA  1 
ATOM   1616 C  C   . LYS   A 1 220 ? 4.95305   14.85220  30.30634  1.000 46.96119 ? 220  LYS   A C   1 
ATOM   1617 O  O   . LYS   A 1 220 ? 4.39765   15.94715  30.16451  1.000 50.74550 ? 220  LYS   A O   1 
ATOM   1618 C  CB  . LYS   A 1 220 ? 6.89702   14.19012  28.84626  1.000 41.89376 ? 220  LYS   A CB  1 
ATOM   1619 C  CG  . LYS   A 1 220 ? 6.37509   15.01323  27.66586  1.000 44.02545 ? 220  LYS   A CG  1 
ATOM   1620 C  CD  . LYS   A 1 220 ? 7.04670   14.60725  26.37679  1.000 58.64034 ? 220  LYS   A CD  1 
ATOM   1621 C  CE  . LYS   A 1 220 ? 8.07561   15.64488  25.93288  1.000 84.53956 ? 220  LYS   A CE  1 
ATOM   1622 N  NZ  . LYS   A 1 220 ? 8.98422   15.13319  24.86256  1.000 67.04664 ? 220  LYS   A NZ  1 
ATOM   1623 N  N   . MET   A 1 221 ? 4.26075   13.72597  30.51074  1.000 39.53490 ? 221  MET   A N   1 
ATOM   1624 C  CA  . MET   A 1 221 ? 2.80554   13.75758  30.64010  1.000 46.02878 ? 221  MET   A CA  1 
ATOM   1625 C  C   . MET   A 1 221 ? 2.38210   14.52193  31.88819  1.000 50.44515 ? 221  MET   A C   1 
ATOM   1626 O  O   . MET   A 1 221 ? 1.39090   15.26159  31.86501  1.000 44.10589 ? 221  MET   A O   1 
ATOM   1627 C  CB  . MET   A 1 221 ? 2.23603   12.33300  30.68802  1.000 42.50219 ? 221  MET   A CB  1 
ATOM   1628 C  CG  . MET   A 1 221 ? 2.07537   11.62671  29.33330  1.000 43.96561 ? 221  MET   A CG  1 
ATOM   1629 S  SD  . MET   A 1 221 ? 1.34328   9.97595   29.51484  1.000 54.00938 ? 221  MET   A SD  1 
ATOM   1630 C  CE  . MET   A 1 221 ? 2.71902   9.02873   30.17842  1.000 52.82495 ? 221  MET   A CE  1 
ATOM   1631 N  N   . ALA   A 1 222 ? 3.11317   14.34411  32.99281  1.000 41.19082 ? 222  ALA   A N   1 
ATOM   1632 C  CA  . ALA   A 1 222 ? 2.73167   14.98559  34.24598  1.000 41.85970 ? 222  ALA   A CA  1 
ATOM   1633 C  C   . ALA   A 1 222 ? 2.82936   16.50608  34.17718  1.000 44.99351 ? 222  ALA   A C   1 
ATOM   1634 O  O   . ALA   A 1 222 ? 2.15259   17.19289  34.95315  1.000 47.74460 ? 222  ALA   A O   1 
ATOM   1635 C  CB  . ALA   A 1 222 ? 3.59008   14.44305  35.39216  1.000 37.35708 ? 222  ALA   A CB  1 
ATOM   1636 N  N   . SER   A 1 223 ? 3.63700   17.03906  33.26035  1.000 51.69954 ? 223  SER   A N   1 
ATOM   1637 C  CA  . SER   A 1 223 ? 3.83408   18.47239  33.08358  1.000 60.30142 ? 223  SER   A CA  1 
ATOM   1638 C  C   . SER   A 1 223 ? 2.79285   19.11946  32.18062  1.000 49.38564 ? 223  SER   A C   1 
ATOM   1639 O  O   . SER   A 1 223 ? 2.85530   20.33130  31.95716  1.000 74.26361 ? 223  SER   A O   1 
ATOM   1640 C  CB  . SER   A 1 223 ? 5.22974   18.73534  32.51352  1.000 48.92988 ? 223  SER   A CB  1 
ATOM   1641 O  OG  . SER   A 1 223 ? 6.20736   18.04399  33.27319  1.000 61.60663 ? 223  SER   A OG  1 
ATOM   1642 N  N   . ASN   A 1 224 ? 1.84182   18.35690  31.65830  1.000 54.57054 ? 224  ASN   A N   1 
ATOM   1643 C  CA  . ASN   A 1 224 ? 0.86128   18.88346  30.71434  1.000 52.91934 ? 224  ASN   A CA  1 
ATOM   1644 C  C   . ASN   A 1 224 ? -0.35203  19.38816  31.48767  1.000 63.45436 ? 224  ASN   A C   1 
ATOM   1645 O  O   . ASN   A 1 224 ? -1.10644  18.59858  32.06668  1.000 53.39365 ? 224  ASN   A O   1 
ATOM   1646 C  CB  . ASN   A 1 224 ? 0.46583   17.81566  29.69806  1.000 53.58160 ? 224  ASN   A CB  1 
ATOM   1647 C  CG  . ASN   A 1 224 ? -0.53421  18.32396  28.68097  1.000 53.31089 ? 224  ASN   A CG  1 
ATOM   1648 O  OD1 . ASN   A 1 224 ? -0.89535  19.50177  28.68217  1.000 57.56363 ? 224  ASN   A OD1 1 
ATOM   1649 N  ND2 . ASN   A 1 224 ? -0.97569  17.43851  27.79160  1.000 63.44257 ? 224  ASN   A ND2 1 
ATOM   1650 N  N   . ALA   A 1 225 ? -0.55968  20.70415  31.47208  1.000 71.03220 ? 225  ALA   A N   1 
ATOM   1651 C  CA  . ALA   A 1 225 ? -1.65861  21.27002  32.24039  1.000 63.17902 ? 225  ALA   A CA  1 
ATOM   1652 C  C   . ALA   A 1 225 ? -3.02016  20.93669  31.64267  1.000 53.57092 ? 225  ALA   A C   1 
ATOM   1653 O  O   . ALA   A 1 225 ? -4.02234  20.98374  32.35999  1.000 52.20097 ? 225  ALA   A O   1 
ATOM   1654 C  CB  . ALA   A 1 225 ? -1.48986  22.78284  32.36434  1.000 52.68040 ? 225  ALA   A CB  1 
ATOM   1655 N  N   . ALA   A 1 226 ? -3.09386  20.59661  30.35507  1.000 48.95868 ? 226  ALA   A N   1 
ATOM   1656 C  CA  . ALA   A 1 226 ? -4.40034  20.27647  29.79268  1.000 61.98980 ? 226  ALA   A CA  1 
ATOM   1657 C  C   . ALA   A 1 226 ? -4.87760  18.89083  30.21308  1.000 57.71061 ? 226  ALA   A C   1 
ATOM   1658 O  O   . ALA   A 1 226 ? -6.07316  18.59766  30.09403  1.000 53.63811 ? 226  ALA   A O   1 
ATOM   1659 C  CB  . ALA   A 1 226 ? -4.37731  20.40293  28.26615  1.000 49.64442 ? 226  ALA   A CB  1 
ATOM   1660 N  N   . ALA   A 1 227 ? -3.98001  18.04413  30.72143  1.000 45.21325 ? 227  ALA   A N   1 
ATOM   1661 C  CA  . ALA   A 1 227 ? -4.33758  16.72169  31.21306  1.000 51.38245 ? 227  ALA   A CA  1 
ATOM   1662 C  C   . ALA   A 1 227 ? -4.28334  16.62433  32.73227  1.000 50.22863 ? 227  ALA   A C   1 
ATOM   1663 O  O   . ALA   A 1 227 ? -4.54898  15.54890  33.28146  1.000 43.40111 ? 227  ALA   A O   1 
ATOM   1664 C  CB  . ALA   A 1 227 ? -3.42056  15.66202  30.59049  1.000 50.98609 ? 227  ALA   A CB  1 
ATOM   1665 N  N   . ARG   A 1 228 ? -3.96932  17.71969  33.42168  1.000 40.42549 ? 228  ARG   A N   1 
ATOM   1666 C  CA  . ARG   A 1 228 ? -3.78135  17.68172  34.86936  1.000 44.45765 ? 228  ARG   A CA  1 
ATOM   1667 C  C   . ARG   A 1 228 ? -5.09055  17.37591  35.58771  1.000 38.38127 ? 228  ARG   A C   1 
ATOM   1668 O  O   . ARG   A 1 228 ? -6.12795  17.98217  35.30491  1.000 39.73547 ? 228  ARG   A O   1 
ATOM   1669 C  CB  . ARG   A 1 228 ? -3.21813  19.01214  35.35985  1.000 40.46369 ? 228  ARG   A CB  1 
ATOM   1670 C  CG  . ARG   A 1 228 ? -2.80846  18.99623  36.83836  1.000 49.22376 ? 228  ARG   A CG  1 
ATOM   1671 C  CD  . ARG   A 1 228 ? -2.16835  20.32125  37.25977  1.000 48.31412 ? 228  ARG   A CD  1 
ATOM   1672 N  NE  . ARG   A 1 228 ? -1.79636  20.29463  38.67057  1.000 67.39005 ? 228  ARG   A NE  1 
ATOM   1673 C  CZ  . ARG   A 1 228 ? -0.57892  20.02728  39.12516  1.000 67.52472 ? 228  ARG   A CZ  1 
ATOM   1674 N  NH1 . ARG   A 1 228 ? 0.43165   19.80640  38.30210  1.000 64.56334 ? 228  ARG   A NH1 1 
ATOM   1675 N  NH2 . ARG   A 1 228 ? -0.36796  19.99531  40.44002  1.000 44.86184 ? 228  ARG   A NH2 1 
ATOM   1676 N  N   . LEU   A 1 229 ? -5.04259  16.43400  36.51628  1.000 36.50014 ? 229  LEU   A N   1 
ATOM   1677 C  CA  . LEU   A 1 229 ? -6.20198  16.03057  37.28926  1.000 39.30824 ? 229  LEU   A CA  1 
ATOM   1678 C  C   . LEU   A 1 229 ? -6.07279  16.50929  38.73106  1.000 42.26118 ? 229  LEU   A C   1 
ATOM   1679 O  O   . LEU   A 1 229 ? -4.98294  16.89644  39.17608  1.000 36.35494 ? 229  LEU   A O   1 
ATOM   1680 C  CB  . LEU   A 1 229 ? -6.36353  14.49953  37.24970  1.000 35.76890 ? 229  LEU   A CB  1 
ATOM   1681 C  CG  . LEU   A 1 229 ? -6.64386  13.87732  35.87528  1.000 39.50509 ? 229  LEU   A CG  1 
ATOM   1682 C  CD1 . LEU   A 1 229 ? -6.57824  12.37386  35.93695  1.000 40.28990 ? 229  LEU   A CD1 1 
ATOM   1683 C  CD2 . LEU   A 1 229 ? -8.00290  14.31827  35.32412  1.000 49.99421 ? 229  LEU   A CD2 1 
ATOM   1684 N  N   . PRO   A 1 230 ? -7.16859  16.51353  39.48864  1.000 33.81933 ? 230  PRO   A N   1 
ATOM   1685 C  CA  . PRO   A 1 230 ? -7.10810  16.98399  40.87942  1.000 32.62939 ? 230  PRO   A CA  1 
ATOM   1686 C  C   . PRO   A 1 230 ? -6.15374  16.14223  41.70805  1.000 31.85225 ? 230  PRO   A C   1 
ATOM   1687 O  O   . PRO   A 1 230 ? -5.89835  14.97026  41.39559  1.000 35.37203 ? 230  PRO   A O   1 
ATOM   1688 C  CB  . PRO   A 1 230 ? -8.55264  16.81712  41.36711  1.000 34.57718 ? 230  PRO   A CB  1 
ATOM   1689 C  CG  . PRO   A 1 230 ? -9.36873  17.02377  40.10714  1.000 47.35681 ? 230  PRO   A CG  1 
ATOM   1690 C  CD  . PRO   A 1 230 ? -8.56177  16.34482  39.03016  1.000 38.66944 ? 230  PRO   A CD  1 
ATOM   1691 N  N   . PRO   A 1 231 ? -5.62897  16.69459  42.79740  1.000 29.82763 ? 231  PRO   A N   1 
ATOM   1692 C  CA  . PRO   A 1 231 ? -4.62806  15.95149  43.59272  1.000 28.23264 ? 231  PRO   A CA  1 
ATOM   1693 C  C   . PRO   A 1 231 ? -5.25530  14.98944  44.59818  1.000 30.60804 ? 231  PRO   A C   1 
ATOM   1694 O  O   . PRO   A 1 231 ? -5.20894  15.19158  45.81356  1.000 33.84830 ? 231  PRO   A O   1 
ATOM   1695 C  CB  . PRO   A 1 231 ? -3.84605  17.08208  44.26562  1.000 30.93214 ? 231  PRO   A CB  1 
ATOM   1696 C  CG  . PRO   A 1 231 ? -4.86258  18.19370  44.42934  1.000 28.83880 ? 231  PRO   A CG  1 
ATOM   1697 C  CD  . PRO   A 1 231 ? -5.78383  18.09815  43.23608  1.000 35.23226 ? 231  PRO   A CD  1 
ATOM   1698 N  N   . ILE   A 1 232 ? -5.80924  13.88565  44.08191  1.000 28.17193 ? 232  ILE   A N   1 
ATOM   1699 C  CA  . ILE   A 1 232 ? -6.57497  12.94244  44.89761  1.000 26.92714 ? 232  ILE   A CA  1 
ATOM   1700 C  C   . ILE   A 1 232 ? -5.74192  12.39041  46.05771  1.000 29.56423 ? 232  ILE   A C   1 
ATOM   1701 O  O   . ILE   A 1 232 ? -6.28196  12.09018  47.12891  1.000 28.31249 ? 232  ILE   A O   1 
ATOM   1702 C  CB  . ILE   A 1 232 ? -7.11673  11.81188  43.99715  1.000 32.36181 ? 232  ILE   A CB  1 
ATOM   1703 C  CG1 . ILE   A 1 232 ? -7.96918  12.39808  42.86788  1.000 37.42230 ? 232  ILE   A CG1 1 
ATOM   1704 C  CG2 . ILE   A 1 232 ? -7.94987  10.80721  44.78920  1.000 29.20779 ? 232  ILE   A CG2 1 
ATOM   1705 C  CD1 . ILE   A 1 232 ? -9.12205  13.27072  43.35541  1.000 34.08900 ? 232  ILE   A CD1 1 
ATOM   1706 N  N   . GLY   A 1 233 ? -4.42116  12.26678  45.88097  1.000 26.06921 ? 233  GLY   A N   1 
ATOM   1707 C  CA  . GLY   A 1 233 ? -3.58287  11.73258  46.95407  1.000 24.73639 ? 233  GLY   A CA  1 
ATOM   1708 C  C   . GLY   A 1 233 ? -3.63714  12.54242  48.23761  1.000 30.30273 ? 233  GLY   A C   1 
ATOM   1709 O  O   . GLY   A 1 233 ? -3.40526  12.00796  49.33356  1.000 28.29636 ? 233  GLY   A O   1 
ATOM   1710 N  N   . LEU   A 1 234 ? -3.92545  13.84018  48.12570  1.000 30.09714 ? 234  LEU   A N   1 
ATOM   1711 C  CA  . LEU   A 1 234 ? -4.10099  14.67636  49.30938  1.000 30.47226 ? 234  LEU   A CA  1 
ATOM   1712 C  C   . LEU   A 1 234 ? -5.15616  14.10947  50.26384  1.000 27.64414 ? 234  LEU   A C   1 
ATOM   1713 O  O   . LEU   A 1 234 ? -5.04647  14.25976  51.48566  1.000 23.59088 ? 234  LEU   A O   1 
ATOM   1714 C  CB  . LEU   A 1 234 ? -4.49137  16.07742  48.85673  1.000 25.94566 ? 234  LEU   A CB  1 
ATOM   1715 C  CG  . LEU   A 1 234 ? -4.48599  17.16441  49.90948  1.000 33.74781 ? 234  LEU   A CG  1 
ATOM   1716 C  CD1 . LEU   A 1 234 ? -3.09840  17.28277  50.52082  1.000 28.30485 ? 234  LEU   A CD1 1 
ATOM   1717 C  CD2 . LEU   A 1 234 ? -4.90646  18.45380  49.24681  1.000 33.77270 ? 234  LEU   A CD2 1 
ATOM   1718 N  N   . LEU   A 1 235 ? -6.19473  13.47409  49.72691  1.000 23.42671 ? 235  LEU   A N   1 
ATOM   1719 C  CA  . LEU   A 1 235 ? -7.23845  12.92389  50.57928  1.000 29.64947 ? 235  LEU   A CA  1 
ATOM   1720 C  C   . LEU   A 1 235 ? -6.70279  11.81178  51.48704  1.000 22.11876 ? 235  LEU   A C   1 
ATOM   1721 O  O   . LEU   A 1 235 ? -7.21018  11.62835  52.60143  1.000 26.63264 ? 235  LEU   A O   1 
ATOM   1722 C  CB  . LEU   A 1 235 ? -8.40154  12.41918  49.70645  1.000 29.02654 ? 235  LEU   A CB  1 
ATOM   1723 C  CG  . LEU   A 1 235 ? -9.12331  13.42587  48.79923  1.000 26.36353 ? 235  LEU   A CG  1 
ATOM   1724 C  CD1 . LEU   A 1 235 ? -10.10127 12.67630  47.88750  1.000 30.98405 ? 235  LEU   A CD1 1 
ATOM   1725 C  CD2 . LEU   A 1 235 ? -9.86833  14.49188  49.56673  1.000 26.26849 ? 235  LEU   A CD2 1 
ATOM   1726 N  N   . THR   A 1 236 ? -5.66337  11.07875  51.05406  1.000 22.59008 ? 236  THR   A N   1 
ATOM   1727 C  CA  . THR   A 1 236 ? -5.11751  10.01865  51.89570  1.000 20.57669 ? 236  THR   A CA  1 
ATOM   1728 C  C   . THR   A 1 236 ? -4.29567  10.54157  53.07252  1.000 25.06778 ? 236  THR   A C   1 
ATOM   1729 O  O   . THR   A 1 236 ? -3.88684  9.73813   53.91627  1.000 22.39664 ? 236  THR   A O   1 
ATOM   1730 C  CB  . THR   A 1 236 ? -4.23898  9.05820   51.08493  1.000 25.13454 ? 236  THR   A CB  1 
ATOM   1731 O  OG1 . THR   A 1 236 ? -2.97981  9.67288   50.80229  1.000 22.96197 ? 236  THR   A OG1 1 
ATOM   1732 C  CG2 . THR   A 1 236 ? -4.89700  8.68743   49.76649  1.000 21.46447 ? 236  THR   A CG2 1 
ATOM   1733 N  N   . SER   A 1 237 ? -4.00650  11.83600  53.12128  1.000 24.40400 ? 237  SER   A N   1 
ATOM   1734 C  CA  . SER   A 1 237 ? -3.26945  12.45121  54.21798  1.000 25.45376 ? 237  SER   A CA  1 
ATOM   1735 C  C   . SER   A 1 237 ? -4.16533  12.87499  55.37608  1.000 23.74594 ? 237  SER   A C   1 
ATOM   1736 O  O   . SER   A 1 237 ? -3.63898  13.32893  56.39662  1.000 20.29710 ? 237  SER   A O   1 
ATOM   1737 C  CB  . SER   A 1 237 ? -2.50466  13.68568  53.71733  1.000 20.90713 ? 237  SER   A CB  1 
ATOM   1738 O  OG  . SER   A 1 237 ? -3.39437  14.77112  53.49392  1.000 26.66963 ? 237  SER   A OG  1 
ATOM   1739 N  N   . ASP   A 1 238 ? -5.48860  12.74696  55.24452  1.000 24.67695 ? 238  ASP   A N   1 
ATOM   1740 C  CA  . ASP   A 1 238 ? -6.45235  13.23772  56.22625  1.000 24.89816 ? 238  ASP   A CA  1 
ATOM   1741 C  C   . ASP   A 1 238 ? -6.67372  12.22157  57.34556  1.000 24.26282 ? 238  ASP   A C   1 
ATOM   1742 O  O   . ASP   A 1 238 ? -6.16566  11.09822  57.30412  1.000 24.45969 ? 238  ASP   A O   1 
ATOM   1743 C  CB  . ASP   A 1 238 ? -7.78499  13.55094  55.53652  1.000 24.35835 ? 238  ASP   A CB  1 
ATOM   1744 C  CG  . ASP   A 1 238 ? -8.52520  14.72473  56.17747  1.000 36.38864 ? 238  ASP   A CG  1 
ATOM   1745 O  OD1 . ASP   A 1 238 ? -8.39976  14.92454  57.41719  1.000 29.21975 ? 238  ASP   A OD1 1 
ATOM   1746 O  OD2 . ASP   A 1 238 ? -9.24202  15.43459  55.43565  1.000 31.84556 ? 238  ASP   A OD2 1 
ATOM   1747 N  N   . GLY   A 1 239 ? -7.46613  12.60590  58.35092  1.000 24.30163 ? 239  GLY   A N   1 
ATOM   1748 C  CA  . GLY   A 1 239 ? -7.86202  11.64637  59.37733  1.000 24.04320 ? 239  GLY   A CA  1 
ATOM   1749 C  C   . GLY   A 1 239 ? -8.55436  10.43699  58.77035  1.000 25.47337 ? 239  GLY   A C   1 
ATOM   1750 O  O   . GLY   A 1 239 ? -9.15877  10.51702  57.70753  1.000 24.66511 ? 239  GLY   A O   1 
ATOM   1751 N  N   . ARG   A 1 240 ? -8.46507  9.28819   59.44801  1.000 24.97588 ? 240  ARG   A N   1 
ATOM   1752 C  CA  . ARG   A 1 240 ? -8.89369  8.05282   58.78414  1.000 23.07099 ? 240  ARG   A CA  1 
ATOM   1753 C  C   . ARG   A 1 240 ? -10.38952 8.03402   58.54409  1.000 25.98614 ? 240  ARG   A C   1 
ATOM   1754 O  O   . ARG   A 1 240 ? -10.84031 7.53609   57.50566  1.000 29.69619 ? 240  ARG   A O   1 
ATOM   1755 C  CB  . ARG   A 1 240 ? -8.45547  6.82182   59.58312  1.000 20.80665 ? 240  ARG   A CB  1 
ATOM   1756 C  CG  . ARG   A 1 240 ? -6.94734  6.80058   59.86629  1.000 20.51355 ? 240  ARG   A CG  1 
ATOM   1757 C  CD  . ARG   A 1 240 ? -6.13760  6.88541   58.55729  1.000 24.37975 ? 240  ARG   A CD  1 
ATOM   1758 N  NE  . ARG   A 1 240 ? -6.38735  5.71301   57.72020  1.000 22.48521 ? 240  ARG   A NE  1 
ATOM   1759 C  CZ  . ARG   A 1 240 ? -5.97056  5.57526   56.47099  1.000 30.18092 ? 240  ARG   A CZ  1 
ATOM   1760 N  NH1 . ARG   A 1 240 ? -5.35942  6.56568   55.84036  1.000 22.46373 ? 240  ARG   A NH1 1 
ATOM   1761 N  NH2 . ARG   A 1 240 ? -6.17212  4.41061   55.83961  1.000 21.33333 ? 240  ARG   A NH2 1 
ATOM   1762 N  N   . SER   A 1 241 ? -11.18606 8.58909   59.47019  1.000 24.61155 ? 241  SER   A N   1 
ATOM   1763 C  CA  . SER   A 1 241 ? -12.62477 8.63144   59.22621  1.000 27.01545 ? 241  SER   A CA  1 
ATOM   1764 C  C   . SER   A 1 241 ? -12.97047 9.64753   58.14402  1.000 28.98377 ? 241  SER   A C   1 
ATOM   1765 O  O   . SER   A 1 241 ? -13.94093 9.45732   57.40545  1.000 28.00832 ? 241  SER   A O   1 
ATOM   1766 C  CB  . SER   A 1 241 ? -13.37708 8.93861   60.52183  1.000 34.13414 ? 241  SER   A CB  1 
ATOM   1767 O  OG  . SER   A 1 241 ? -13.14462 7.91588   61.49190  1.000 37.82917 ? 241  SER   A OG  1 
ATOM   1768 N  N   . GLU   A 1 242 ? -12.18351 10.71998  58.03011  1.000 29.11081 ? 242  GLU   A N   1 
ATOM   1769 C  CA  . GLU   A 1 242 ? -12.40580 11.71107  56.97931  1.000 25.42760 ? 242  GLU   A CA  1 
ATOM   1770 C  C   . GLU   A 1 242 ? -12.11912 11.11405  55.61404  1.000 23.89100 ? 242  GLU   A C   1 
ATOM   1771 O  O   . GLU   A 1 242 ? -12.89720 11.27747  54.67457  1.000 28.35373 ? 242  GLU   A O   1 
ATOM   1772 C  CB  . GLU   A 1 242 ? -11.51644 12.93219  57.22840  1.000 29.48307 ? 242  GLU   A CB  1 
ATOM   1773 C  CG  . GLU   A 1 242 ? -11.99765 13.83667  58.39349  1.000 30.61228 ? 242  GLU   A CG  1 
ATOM   1774 C  CD  . GLU   A 1 242 ? -11.60146 13.33596  59.77809  1.000 34.14098 ? 242  GLU   A CD  1 
ATOM   1775 O  OE1 . GLU   A 1 242 ? -10.96391 12.26480  59.90945  1.000 31.11290 ? 242  GLU   A OE1 1 
ATOM   1776 O  OE2 . GLU   A 1 242 ? -11.95364 14.02194  60.76729  1.000 39.67844 ? 242  GLU   A OE2 1 
ATOM   1777 N  N   . TRP   A 1 243 ? -10.99258 10.41411  55.48783  1.000 26.23817 ? 243  TRP   A N   1 
ATOM   1778 C  CA  . TRP   A 1 243 ? -10.67236 9.77301   54.21848  1.000 26.49354 ? 243  TRP   A CA  1 
ATOM   1779 C  C   . TRP   A 1 243 ? -11.63096 8.61547   53.90515  1.000 30.55503 ? 243  TRP   A C   1 
ATOM   1780 O  O   . TRP   A 1 243 ? -11.99718 8.41683   52.74490  1.000 32.91798 ? 243  TRP   A O   1 
ATOM   1781 C  CB  . TRP   A 1 243 ? -9.20613  9.33899   54.24902  1.000 22.96421 ? 243  TRP   A CB  1 
ATOM   1782 C  CG  . TRP   A 1 243 ? -8.69847  8.41686   53.15603  1.000 23.98812 ? 243  TRP   A CG  1 
ATOM   1783 C  CD1 . TRP   A 1 243 ? -7.81941  7.39154   53.33499  1.000 25.29418 ? 243  TRP   A CD1 1 
ATOM   1784 C  CD2 . TRP   A 1 243 ? -9.00155  8.44394   51.74257  1.000 26.55828 ? 243  TRP   A CD2 1 
ATOM   1785 N  NE1 . TRP   A 1 243 ? -7.54161  6.77951   52.13374  1.000 24.71102 ? 243  TRP   A NE1 1 
ATOM   1786 C  CE2 . TRP   A 1 243 ? -8.25496  7.40414   51.14133  1.000 24.31289 ? 243  TRP   A CE2 1 
ATOM   1787 C  CE3 . TRP   A 1 243 ? -9.83276  9.24113   50.92874  1.000 27.94220 ? 243  TRP   A CE3 1 
ATOM   1788 C  CZ2 . TRP   A 1 243 ? -8.32863  7.11731   49.77540  1.000 26.35217 ? 243  TRP   A CZ2 1 
ATOM   1789 C  CZ3 . TRP   A 1 243 ? -9.88722  8.97387   49.56343  1.000 30.82168 ? 243  TRP   A CZ3 1 
ATOM   1790 C  CH2 . TRP   A 1 243 ? -9.13654  7.91872   48.99988  1.000 25.93278 ? 243  TRP   A CH2 1 
ATOM   1791 N  N   . ALA   A 1 244 ? -12.07669 7.85273   54.90729  1.000 26.34071 ? 244  ALA   A N   1 
ATOM   1792 C  CA  . ALA   A 1 244 ? -13.13890 6.88279   54.62250  1.000 24.64533 ? 244  ALA   A CA  1 
ATOM   1793 C  C   . ALA   A 1 244 ? -14.35216 7.57464   54.01663  1.000 29.40080 ? 244  ALA   A C   1 
ATOM   1794 O  O   . ALA   A 1 244 ? -14.94264 7.08090   53.04686  1.000 32.26434 ? 244  ALA   A O   1 
ATOM   1795 C  CB  . ALA   A 1 244 ? -13.54383 6.13448   55.88856  1.000 31.01046 ? 244  ALA   A CB  1 
ATOM   1796 N  N   . GLU   A 1 245 ? -14.73034 8.73662   54.55403  1.000 26.29818 ? 245  GLU   A N   1 
ATOM   1797 C  CA  . GLU   A 1 245 ? -15.90162 9.40836   53.99877  1.000 27.78739 ? 245  GLU   A CA  1 
ATOM   1798 C  C   . GLU   A 1 245 ? -15.64496 9.86720   52.56424  1.000 33.39462 ? 245  GLU   A C   1 
ATOM   1799 O  O   . GLU   A 1 245 ? -16.48878 9.66364   51.68932  1.000 35.35751 ? 245  GLU   A O   1 
ATOM   1800 C  CB  . GLU   A 1 245 ? -16.31417 10.58154  54.88192  1.000 33.47359 ? 245  GLU   A CB  1 
ATOM   1801 C  CG  . GLU   A 1 245 ? -17.49745 11.37990  54.29972  1.000 40.86917 ? 245  GLU   A CG  1 
ATOM   1802 C  CD  . GLU   A 1 245 ? -17.85118 12.57559  55.16461  1.000 58.16176 ? 245  GLU   A CD  1 
ATOM   1803 O  OE1 . GLU   A 1 245 ? -17.68985 13.72085  54.69397  1.000 73.16815 ? 245  GLU   A OE1 1 
ATOM   1804 O  OE2 . GLU   A 1 245 ? -18.26792 12.36799  56.32510  1.000 74.67947 ? 245  GLU   A OE2 1 
ATOM   1805 N  N   . ALA   A 1 246 ? -14.47357 10.45090  52.28808  1.000 30.24021 ? 246  ALA   A N   1 
ATOM   1806 C  CA  . ALA   A 1 246 ? -14.21523 10.96296  50.93767  1.000 33.47546 ? 246  ALA   A CA  1 
ATOM   1807 C  C   . ALA   A 1 246 ? -14.03420 9.82702   49.93699  1.000 29.98331 ? 246  ALA   A C   1 
ATOM   1808 O  O   . ALA   A 1 246 ? -14.43802 9.94046   48.77708  1.000 31.99693 ? 246  ALA   A O   1 
ATOM   1809 C  CB  . ALA   A 1 246 ? -12.98529 11.87176  50.94220  1.000 31.81190 ? 246  ALA   A CB  1 
ATOM   1810 N  N   . ARG   A 1 247 ? -13.42484 8.72441   50.36526  1.000 30.64624 ? 247  ARG   A N   1 
ATOM   1811 C  CA  . ARG   A 1 247 ? -13.28429 7.57753   49.48107  1.000 29.49743 ? 247  ARG   A CA  1 
ATOM   1812 C  C   . ARG   A 1 247 ? -14.64624 6.99731   49.13041  1.000 39.27817 ? 247  ARG   A C   1 
ATOM   1813 O  O   . ARG   A 1 247 ? -14.88892 6.61705   47.97974  1.000 38.73257 ? 247  ARG   A O   1 
ATOM   1814 C  CB  . ARG   A 1 247 ? -12.38737 6.52165   50.13696  1.000 26.65240 ? 247  ARG   A CB  1 
ATOM   1815 C  CG  . ARG   A 1 247 ? -12.03885 5.33018   49.19987  1.000 29.97193 ? 247  ARG   A CG  1 
ATOM   1816 C  CD  . ARG   A 1 247 ? -11.17188 4.26481   49.92111  1.000 32.94897 ? 247  ARG   A CD  1 
ATOM   1817 N  NE  . ARG   A 1 247 ? -10.94128 3.10517   49.06240  1.000 34.75449 ? 247  ARG   A NE  1 
ATOM   1818 C  CZ  . ARG   A 1 247 ? -11.87335 2.21857   48.73985  1.000 34.19494 ? 247  ARG   A CZ  1 
ATOM   1819 N  NH1 . ARG   A 1 247 ? -13.09730 2.29489   49.23311  1.000 39.76404 ? 247  ARG   A NH1 1 
ATOM   1820 N  NH2 . ARG   A 1 247 ? -11.56821 1.22786   47.90634  1.000 30.63239 ? 247  ARG   A NH2 1 
ATOM   1821 N  N   . THR   A 1 248 ? -15.56839 6.95529   50.09883  1.000 31.50704 ? 248  THR   A N   1 
ATOM   1822 C  CA  . THR   A 1 248 ? -16.92077 6.49019   49.77971  1.000 37.56344 ? 248  THR   A CA  1 
ATOM   1823 C  C   . THR   A 1 248 ? -17.56812 7.33860   48.69001  1.000 39.59758 ? 248  THR   A C   1 
ATOM   1824 O  O   . THR   A 1 248 ? -18.32907 6.81565   47.85968  1.000 37.42092 ? 248  THR   A O   1 
ATOM   1825 C  CB  . THR   A 1 248 ? -17.78115 6.48863   51.04104  1.000 35.09153 ? 248  THR   A CB  1 
ATOM   1826 O  OG1 . THR   A 1 248 ? -17.20995 5.58565   52.00003  1.000 39.82167 ? 248  THR   A OG1 1 
ATOM   1827 C  CG2 . THR   A 1 248 ? -19.20544 6.05490   50.72342  1.000 43.54240 ? 248  THR   A CG2 1 
ATOM   1828 N  N   . VAL   A 1 249 ? -17.28422 8.64231   48.66525  1.000 32.18731 ? 249  VAL   A N   1 
ATOM   1829 C  CA  . VAL   A 1 249 ? -17.77591 9.46041   47.55754  1.000 36.67889 ? 249  VAL   A CA  1 
ATOM   1830 C  C   . VAL   A 1 249 ? -17.14527 9.00356   46.25040  1.000 42.09366 ? 249  VAL   A C   1 
ATOM   1831 O  O   . VAL   A 1 249 ? -17.83403 8.84146   45.23511  1.000 46.39487 ? 249  VAL   A O   1 
ATOM   1832 C  CB  . VAL   A 1 249 ? -17.51810 10.95924  47.80950  1.000 40.57578 ? 249  VAL   A CB  1 
ATOM   1833 C  CG1 . VAL   A 1 249 ? -17.98803 11.77703  46.59953  1.000 41.70213 ? 249  VAL   A CG1 1 
ATOM   1834 C  CG2 . VAL   A 1 249 ? -18.22790 11.44325  49.06895  1.000 36.74388 ? 249  VAL   A CG2 1 
ATOM   1835 N  N   . LEU   A 1 250 ? -15.82701 8.78773   46.25315  1.000 41.91883 ? 250  LEU   A N   1 
ATOM   1836 C  CA  . LEU   A 1 250 ? -15.12934 8.41134   45.02487  1.000 33.89213 ? 250  LEU   A CA  1 
ATOM   1837 C  C   . LEU   A 1 250 ? -15.67900 7.11583   44.42974  1.000 36.83519 ? 250  LEU   A C   1 
ATOM   1838 O  O   . LEU   A 1 250 ? -15.85711 7.01301   43.21216  1.000 41.09122 ? 250  LEU   A O   1 
ATOM   1839 C  CB  . LEU   A 1 250 ? -13.63124 8.26856   45.29608  1.000 35.90639 ? 250  LEU   A CB  1 
ATOM   1840 C  CG  . LEU   A 1 250 ? -12.78541 9.50280   45.58521  1.000 35.51926 ? 250  LEU   A CG  1 
ATOM   1841 C  CD1 . LEU   A 1 250 ? -11.34366 9.09896   45.90897  1.000 29.07489 ? 250  LEU   A CD1 1 
ATOM   1842 C  CD2 . LEU   A 1 250 ? -12.84667 10.42275  44.38138  1.000 38.39050 ? 250  LEU   A CD2 1 
ATOM   1843 N  N   . VAL   A 1 251 ? -15.93937 6.10392   45.26254  1.000 38.66843 ? 251  VAL   A N   1 
ATOM   1844 C  CA  . VAL   A 1 251 ? -16.24298 4.77993   44.72021  1.000 39.96538 ? 251  VAL   A CA  1 
ATOM   1845 C  C   . VAL   A 1 251 ? -17.63883 4.72343   44.08686  1.000 49.01478 ? 251  VAL   A C   1 
ATOM   1846 O  O   . VAL   A 1 251 ? -18.02629 3.70292   43.50354  1.000 50.47489 ? 251  VAL   A O   1 
ATOM   1847 C  CB  . VAL   A 1 251 ? -16.05741 3.70113   45.80252  1.000 42.62324 ? 251  VAL   A CB  1 
ATOM   1848 C  CG1 . VAL   A 1 251 ? -14.58569 3.62521   46.20194  1.000 33.89944 ? 251  VAL   A CG1 1 
ATOM   1849 C  CG2 . VAL   A 1 251 ? -16.89923 4.00822   47.01128  1.000 53.77677 ? 251  VAL   A CG2 1 
ATOM   1850 N  N   . LYS   A 1 252 ? -18.39081 5.82550   44.14659  1.000 44.44670 ? 252  LYS   A N   1 
ATOM   1851 C  CA  . LYS   A 1 252 ? -19.65804 5.88805   43.41881  1.000 47.63264 ? 252  LYS   A CA  1 
ATOM   1852 C  C   . LYS   A 1 252 ? -19.46331 5.84494   41.90828  1.000 53.26741 ? 252  LYS   A C   1 
ATOM   1853 O  O   . LYS   A 1 252 ? -20.41477 5.54568   41.18302  1.000 58.57649 ? 252  LYS   A O   1 
ATOM   1854 C  CB  . LYS   A 1 252 ? -20.43045 7.15717   43.77801  1.000 42.46004 ? 252  LYS   A CB  1 
ATOM   1855 C  CG  . LYS   A 1 252 ? -20.99380 7.19367   45.19067  1.000 55.85867 ? 252  LYS   A CG  1 
ATOM   1856 C  CD  . LYS   A 1 252 ? -21.04894 8.63058   45.69998  1.000 56.30166 ? 252  LYS   A CD  1 
ATOM   1857 C  CE  . LYS   A 1 252 ? -22.44537 9.06815   46.06572  1.000 65.38204 ? 252  LYS   A CE  1 
ATOM   1858 N  NZ  . LYS   A 1 252 ? -22.40789 10.46511  46.58800  1.000 75.18661 ? 252  LYS   A NZ  1 
ATOM   1859 N  N   . ASP   A 1 253 ? -18.26094 6.12745   41.42100  1.000 46.45990 ? 253  ASP   A N   1 
ATOM   1860 C  CA  . ASP   A 1 253 ? -17.98274 6.21545   39.99829  1.000 49.09591 ? 253  ASP   A CA  1 
ATOM   1861 C  C   . ASP   A 1 253 ? -17.02983 5.10710   39.57062  1.000 54.97418 ? 253  ASP   A C   1 
ATOM   1862 O  O   . ASP   A 1 253 ? -16.03123 4.84969   40.24069  1.000 42.49147 ? 253  ASP   A O   1 
ATOM   1863 C  CB  . ASP   A 1 253 ? -17.39074 7.58268   39.66511  1.000 47.91311 ? 253  ASP   A CB  1 
ATOM   1864 C  CG  . ASP   A 1 253 ? -17.00359 7.69923   38.21859  1.000 67.03013 ? 253  ASP   A CG  1 
ATOM   1865 O  OD1 . ASP   A 1 253 ? -15.90822 7.21690   37.87601  1.000 60.25736 ? 253  ASP   A OD1 1 
ATOM   1866 O  OD2 . ASP   A 1 253 ? -17.80125 8.24584   37.42338  1.000 69.98968 ? 253  ASP   A OD2 1 
ATOM   1867 N  N   . SER   A 1 254 ? -17.32736 4.46708   38.43406  1.000 48.96025 ? 254  SER   A N   1 
ATOM   1868 C  CA  . SER   A 1 254 ? -16.52737 3.32196   37.98933  1.000 50.87325 ? 254  SER   A CA  1 
ATOM   1869 C  C   . SER   A 1 254 ? -15.10795 3.71436   37.58695  1.000 51.55968 ? 254  SER   A C   1 
ATOM   1870 O  O   . SER   A 1 254 ? -14.18486 2.91223   37.75737  1.000 46.95232 ? 254  SER   A O   1 
ATOM   1871 C  CB  . SER   A 1 254 ? -17.20797 2.61249   36.81476  1.000 41.98967 ? 254  SER   A CB  1 
ATOM   1872 O  OG  . SER   A 1 254 ? -17.35951 3.51558   35.74698  1.000 50.33434 ? 254  SER   A OG  1 
ATOM   1873 N  N   . THR   A 1 255 ? -14.90805 4.90842   37.01696  1.000 41.57328 ? 255  THR   A N   1 
ATOM   1874 C  CA  . THR   A 1 255 ? -13.54238 5.35141   36.72900  1.000 42.97724 ? 255  THR   A CA  1 
ATOM   1875 C  C   . THR   A 1 255 ? -12.70744 5.43102   38.00468  1.000 43.34782 ? 255  THR   A C   1 
ATOM   1876 O  O   . THR   A 1 255 ? -11.55257 4.97762   38.03736  1.000 40.21406 ? 255  THR   A O   1 
ATOM   1877 C  CB  . THR   A 1 255 ? -13.56083 6.70977   36.01558  1.000 43.60127 ? 255  THR   A CB  1 
ATOM   1878 O  OG1 . THR   A 1 255 ? -14.17657 6.56642   34.72621  1.000 51.13809 ? 255  THR   A OG1 1 
ATOM   1879 C  CG2 . THR   A 1 255 ? -12.13879 7.25703   35.85076  1.000 47.01528 ? 255  THR   A CG2 1 
ATOM   1880 N  N   . ASN   A 1 256 ? -13.27339 5.99575   39.07299  1.000 40.22350 ? 256  ASN   A N   1 
ATOM   1881 C  CA  . ASN   A 1 256 ? -12.51427 6.07782   40.32121  1.000 36.93833 ? 256  ASN   A CA  1 
ATOM   1882 C  C   . ASN   A 1 256 ? -12.25833 4.69760   40.90180  1.000 40.27581 ? 256  ASN   A C   1 
ATOM   1883 O  O   . ASN   A 1 256 ? -11.18460 4.44808   41.45994  1.000 37.22665 ? 256  ASN   A O   1 
ATOM   1884 C  CB  . ASN   A 1 256 ? -13.24073 6.95255   41.33653  1.000 35.14270 ? 256  ASN   A CB  1 
ATOM   1885 C  CG  . ASN   A 1 256 ? -13.44310 8.37993   40.83974  1.000 46.98010 ? 256  ASN   A CG  1 
ATOM   1886 O  OD1 . ASN   A 1 256 ? -12.61977 8.91357   40.09807  1.000 42.47285 ? 256  ASN   A OD1 1 
ATOM   1887 N  ND2 . ASN   A 1 256 ? -14.54610 8.99962   41.24857  1.000 39.88498 ? 256  ASN   A ND2 1 
ATOM   1888 N  N   . ARG   A 1 257 ? -13.22975 3.78587   40.79904  1.000 37.76642 ? 257  ARG   A N   1 
ATOM   1889 C  CA  . ARG   A 1 257 ? -12.99751 2.44872   41.33514  1.000 40.56299 ? 257  ARG   A CA  1 
ATOM   1890 C  C   . ARG   A 1 257 ? -11.83275 1.77530   40.62160  1.000 43.21891 ? 257  ARG   A C   1 
ATOM   1891 O  O   . ARG   A 1 257 ? -10.96403 1.16959   41.26884  1.000 42.53712 ? 257  ARG   A O   1 
ATOM   1892 C  CB  . ARG   A 1 257 ? -14.26731 1.59501   41.24720  1.000 40.21705 ? 257  ARG   A CB  1 
ATOM   1893 C  CG  . ARG   A 1 257 ? -15.39060 2.08943   42.16125  1.000 43.83408 ? 257  ARG   A CG  1 
ATOM   1894 C  CD  . ARG   A 1 257 ? -16.53160 1.07143   42.31948  1.000 44.98222 ? 257  ARG   A CD  1 
ATOM   1895 N  NE  . ARG   A 1 257 ? -17.17320 0.74318   41.05140  1.000 45.66489 ? 257  ARG   A NE  1 
ATOM   1896 C  CZ  . ARG   A 1 257 ? -18.16655 1.42315   40.49441  1.000 53.47920 ? 257  ARG   A CZ  1 
ATOM   1897 N  NH1 . ARG   A 1 257 ? -18.69707 2.48753   41.07647  1.000 43.55512 ? 257  ARG   A NH1 1 
ATOM   1898 N  NH2 . ARG   A 1 257 ? -18.64669 1.02009   39.32254  1.000 54.55617 ? 257  ARG   A NH2 1 
ATOM   1899 N  N   . ASP   A 1 258 ? -11.78816 1.88752   39.29009  1.000 43.04391 ? 258  ASP   A N   1 
ATOM   1900 C  CA  . ASP   A 1 258 ? -10.67304 1.32740   38.53345  1.000 42.13360 ? 258  ASP   A CA  1 
ATOM   1901 C  C   . ASP   A 1 258 ? -9.34630  1.93392   38.97638  1.000 40.77462 ? 258  ASP   A C   1 
ATOM   1902 O  O   . ASP   A 1 258 ? -8.34300  1.22158   39.11733  1.000 40.14788 ? 258  ASP   A O   1 
ATOM   1903 C  CB  . ASP   A 1 258 ? -10.88124 1.55596   37.03878  1.000 38.13762 ? 258  ASP   A CB  1 
ATOM   1904 C  CG  . ASP   A 1 258 ? -12.18588 0.94939   36.51422  1.000 66.76953 ? 258  ASP   A CG  1 
ATOM   1905 O  OD1 . ASP   A 1 258 ? -12.74959 0.02052   37.14590  1.000 51.92579 ? 258  ASP   A OD1 1 
ATOM   1906 O  OD2 . ASP   A 1 258 ? -12.64423 1.40759   35.44574  1.000 60.43386 ? 258  ASP   A OD2 1 
ATOM   1907 N  N   . SER   A 1 259 ? -9.31805  3.24609   39.21324  1.000 36.69306 ? 259  SER   A N   1 
ATOM   1908 C  CA  . SER   A 1 259 ? -8.05263  3.87985   39.57839  1.000 39.74616 ? 259  SER   A CA  1 
ATOM   1909 C  C   . SER   A 1 259 ? -7.62881  3.49866   40.98741  1.000 37.52354 ? 259  SER   A C   1 
ATOM   1910 O  O   . SER   A 1 259 ? -6.44830  3.22770   41.23294  1.000 34.46503 ? 259  SER   A O   1 
ATOM   1911 C  CB  . SER   A 1 259 ? -8.15889  5.39266   39.43476  1.000 33.77222 ? 259  SER   A CB  1 
ATOM   1912 O  OG  . SER   A 1 259 ? -8.29923  5.71980   38.06262  1.000 37.15748 ? 259  SER   A OG  1 
ATOM   1913 N  N   . LEU   A 1 260 ? -8.56992  3.49869   41.93141  1.000 36.21223 ? 260  LEU   A N   1 
ATOM   1914 C  CA  . LEU   A 1 260 ? -8.25255  3.04746   43.28391  1.000 35.53959 ? 260  LEU   A CA  1 
ATOM   1915 C  C   . LEU   A 1 260 ? -7.74960  1.61284   43.26914  1.000 32.10653 ? 260  LEU   A C   1 
ATOM   1916 O  O   . LEU   A 1 260 ? -6.80376  1.26712   43.98098  1.000 33.13235 ? 260  LEU   A O   1 
ATOM   1917 C  CB  . LEU   A 1 260 ? -9.48715  3.17012   44.16953  1.000 33.64245 ? 260  LEU   A CB  1 
ATOM   1918 C  CG  . LEU   A 1 260 ? -9.91974  4.61621   44.40030  1.000 37.62358 ? 260  LEU   A CG  1 
ATOM   1919 C  CD1 . LEU   A 1 260 ? -11.28375 4.66602   45.03988  1.000 30.34265 ? 260  LEU   A CD1 1 
ATOM   1920 C  CD2 . LEU   A 1 260 ? -8.87470  5.28532   45.27174  1.000 28.52615 ? 260  LEU   A CD2 1 
ATOM   1921 N  N   . ASP   A 1 261 ? -8.36380  0.76824   42.44276  1.000 32.20862 ? 261  ASP   A N   1 
ATOM   1922 C  CA  . ASP   A 1 261 ? -7.95446  -0.62944  42.37346  1.000 37.62546 ? 261  ASP   A CA  1 
ATOM   1923 C  C   . ASP   A 1 261 ? -6.51607  -0.75100  41.89273  1.000 34.85971 ? 261  ASP   A C   1 
ATOM   1924 O  O   . ASP   A 1 261 ? -5.76405  -1.61683  42.35615  1.000 36.50921 ? 261  ASP   A O   1 
ATOM   1925 C  CB  . ASP   A 1 261 ? -8.90221  -1.40437  41.45243  1.000 41.37891 ? 261  ASP   A CB  1 
ATOM   1926 C  CG  . ASP   A 1 261 ? -8.36242  -2.77017  41.08273  1.000 52.28126 ? 261  ASP   A CG  1 
ATOM   1927 O  OD1 . ASP   A 1 261 ? -8.24632  -3.62090  41.99199  1.000 51.02386 ? 261  ASP   A OD1 1 
ATOM   1928 O  OD2 . ASP   A 1 261 ? -8.04753  -2.98919  39.88640  1.000 52.66143 ? 261  ASP   A OD2 1 
ATOM   1929 N  N   . MET   A 1 262 ? -6.10803  0.12110   40.97661  1.000 35.26261 ? 262  MET   A N   1 
ATOM   1930 C  CA  . MET   A 1 262 ? -4.74514  0.04741   40.47571  1.000 33.82383 ? 262  MET   A CA  1 
ATOM   1931 C  C   . MET   A 1 262 ? -3.74614  0.43316   41.55981  1.000 32.01495 ? 262  MET   A C   1 
ATOM   1932 O  O   . MET   A 1 262 ? -2.66384  -0.15268  41.64208  1.000 32.79210 ? 262  MET   A O   1 
ATOM   1933 C  CB  . MET   A 1 262 ? -4.59222  0.93167   39.24478  1.000 29.74593 ? 262  MET   A CB  1 
ATOM   1934 C  CG  . MET   A 1 262 ? -5.42596  0.42604   38.02628  1.000 31.84246 ? 262  MET   A CG  1 
ATOM   1935 S  SD  . MET   A 1 262 ? -4.99045  -1.27358  37.54733  1.000 44.93425 ? 262  MET   A SD  1 
ATOM   1936 C  CE  . MET   A 1 262 ? -3.31515  -1.00859  36.96926  1.000 37.73947 ? 262  MET   A CE  1 
ATOM   1937 N  N   . ILE   A 1 263 ? -4.09021  1.40890   42.40248  1.000 29.32440 ? 263  ILE   A N   1 
ATOM   1938 C  CA  . ILE   A 1 263 ? -3.18755  1.78426   43.48955  1.000 25.09688 ? 263  ILE   A CA  1 
ATOM   1939 C  C   . ILE   A 1 263 ? -3.16205  0.69524   44.54390  1.000 32.64531 ? 263  ILE   A C   1 
ATOM   1940 O  O   . ILE   A 1 263 ? -2.09046  0.30160   45.02841  1.000 31.55698 ? 263  ILE   A O   1 
ATOM   1941 C  CB  . ILE   A 1 263 ? -3.60136  3.13835   44.08241  1.000 25.28211 ? 263  ILE   A CB  1 
ATOM   1942 C  CG1 . ILE   A 1 263 ? -3.53417  4.21796   43.00407  1.000 31.37942 ? 263  ILE   A CG1 1 
ATOM   1943 C  CG2 . ILE   A 1 263 ? -2.72443  3.50743   45.28369  1.000 26.34200 ? 263  ILE   A CG2 1 
ATOM   1944 C  CD1 . ILE   A 1 263 ? -4.28008  5.49763   43.39379  1.000 36.15802 ? 263  ILE   A CD1 1 
ATOM   1945 N  N   . GLU   A 1 264 ? -4.33738  0.15348   44.87930  1.000 27.86632 ? 264  GLU   A N   1 
ATOM   1946 C  CA  . GLU   A 1 264 ? -4.41730  -0.88242  45.90947  1.000 29.44179 ? 264  GLU   A CA  1 
ATOM   1947 C  C   . GLU   A 1 264 ? -3.59954  -2.11253  45.54740  1.000 35.91006 ? 264  GLU   A C   1 
ATOM   1948 O  O   . GLU   A 1 264 ? -3.10237  -2.80031  46.44046  1.000 34.88896 ? 264  GLU   A O   1 
ATOM   1949 C  CB  . GLU   A 1 264 ? -5.88235  -1.26417  46.15931  1.000 28.86343 ? 264  GLU   A CB  1 
ATOM   1950 C  CG  . GLU   A 1 264 ? -6.67416  -0.09585  46.75801  1.000 32.72821 ? 264  GLU   A CG  1 
ATOM   1951 C  CD  . GLU   A 1 264 ? -8.16032  -0.34313  46.79517  1.000 40.68731 ? 264  GLU   A CD  1 
ATOM   1952 O  OE1 . GLU   A 1 264 ? -8.56933  -1.51972  46.67718  1.000 45.89074 ? 264  GLU   A OE1 1 
ATOM   1953 O  OE2 . GLU   A 1 264 ? -8.91700  0.64119   46.94441  1.000 37.91512 ? 264  GLU   A OE2 1 
ATOM   1954 N  N   . ARG   A 1 265 ? -3.41945  -2.39934  44.25916  1.000 33.87207 ? 265  ARG   A N   1 
ATOM   1955 C  CA  . ARG   A 1 265 ? -2.70471  -3.60776  43.85848  1.000 34.40399 ? 265  ARG   A CA  1 
ATOM   1956 C  C   . ARG   A 1 265 ? -1.30064  -3.33433  43.34054  1.000 34.99719 ? 265  ARG   A C   1 
ATOM   1957 O  O   . ARG   A 1 265 ? -0.68029  -4.23071  42.76113  1.000 35.58953 ? 265  ARG   A O   1 
ATOM   1958 C  CB  . ARG   A 1 265 ? -3.50347  -4.38168  42.80296  1.000 36.93139 ? 265  ARG   A CB  1 
ATOM   1959 C  CG  . ARG   A 1 265 ? -4.82515  -4.94645  43.33293  1.000 53.73177 ? 265  ARG   A CG  1 
ATOM   1960 C  CD  . ARG   A 1 265 ? -5.58587  -5.78593  42.28902  1.000 54.43378 ? 265  ARG   A CD  1 
ATOM   1961 N  NE  . ARG   A 1 265 ? -5.85840  -5.04768  41.06141  1.000 48.69904 ? 265  ARG   A NE  1 
ATOM   1962 C  CZ  . ARG   A 1 265 ? -5.14607  -5.15139  39.94514  1.000 65.51198 ? 265  ARG   A CZ  1 
ATOM   1963 N  NH1 . ARG   A 1 265 ? -4.12281  -5.98741  39.85073  1.000 52.68353 ? 265  ARG   A NH1 1 
ATOM   1964 N  NH2 . ARG   A 1 265 ? -5.46624  -4.39514  38.89829  1.000 64.22203 ? 265  ARG   A NH2 1 
ATOM   1965 N  N   . CYS   A 1 266 ? -0.78454  -2.12558  43.50522  1.000 32.77249 ? 266  CYS   A N   1 
ATOM   1966 C  CA  . CYS   A 1 266 ? 0.55523   -1.88521  42.99539  1.000 28.81171 ? 266  CYS   A CA  1 
ATOM   1967 C  C   . CYS   A 1 266 ? 1.59722   -2.44963  43.96428  1.000 30.29192 ? 266  CYS   A C   1 
ATOM   1968 O  O   . CYS   A 1 266 ? 1.29934   -2.79785  45.11114  1.000 31.43388 ? 266  CYS   A O   1 
ATOM   1969 C  CB  . CYS   A 1 266 ? 0.78414   -0.38804  42.74989  1.000 26.84114 ? 266  CYS   A CB  1 
ATOM   1970 S  SG  . CYS   A 1 266 ? 1.01799   0.62769   44.24304  1.000 33.65200 ? 266  CYS   A SG  1 
ATOM   1971 N  N   . ILE   A 1 267 ? 2.83112   -2.56874  43.47593  1.000 30.22910 ? 267  ILE   A N   1 
ATOM   1972 C  CA  . ILE   A 1 267 ? 3.92822   -3.03224  44.32488  1.000 31.14932 ? 267  ILE   A CA  1 
ATOM   1973 C  C   . ILE   A 1 267 ? 4.27751   -1.98326  45.36979  1.000 35.76777 ? 267  ILE   A C   1 
ATOM   1974 O  O   . ILE   A 1 267 ? 4.41481   -2.27866  46.56787  1.000 26.58781 ? 267  ILE   A O   1 
ATOM   1975 C  CB  . ILE   A 1 267 ? 5.15043   -3.35901  43.45611  1.000 29.02908 ? 267  ILE   A CB  1 
ATOM   1976 C  CG1 . ILE   A 1 267 ? 4.85887   -4.58988  42.60416  1.000 30.35726 ? 267  ILE   A CG1 1 
ATOM   1977 C  CG2 . ILE   A 1 267 ? 6.41756   -3.49166  44.33335  1.000 30.87845 ? 267  ILE   A CG2 1 
ATOM   1978 C  CD1 . ILE   A 1 267 ? 5.89620   -4.83491  41.51937  1.000 33.74245 ? 267  ILE   A CD1 1 
ATOM   1979 N  N   . CYS   A 1 268 ? 4.46975   -0.75015  44.91664  1.000 27.36451 ? 268  CYS   A N   1 
ATOM   1980 C  CA  . CYS   A 1 268 ? 4.82175   0.37994   45.76312  1.000 25.27897 ? 268  CYS   A CA  1 
ATOM   1981 C  C   . CYS   A 1 268 ? 4.56665   1.63238   44.93769  1.000 25.52170 ? 268  CYS   A C   1 
ATOM   1982 O  O   . CYS   A 1 268 ? 4.25683   1.55658   43.74293  1.000 26.53579 ? 268  CYS   A O   1 
ATOM   1983 C  CB  . CYS   A 1 268 ? 6.28800   0.30488   46.23505  1.000 24.25340 ? 268  CYS   A CB  1 
ATOM   1984 S  SG  . CYS   A 1 268 ? 7.51658   0.37942   44.88056  1.000 31.09794 ? 268  CYS   A SG  1 
ATOM   1985 N  N   . LEU   A 1 269 ? 4.65642   2.78483   45.60361  1.000 24.00229 ? 269  LEU   A N   1 
ATOM   1986 C  CA  . LEU   A 1 269 ? 4.70986   4.06679   44.92943  1.000 23.84977 ? 269  LEU   A CA  1 
ATOM   1987 C  C   . LEU   A 1 269 ? 6.15972   4.49898   44.77261  1.000 26.19764 ? 269  LEU   A C   1 
ATOM   1988 O  O   . LEU   A 1 269 ? 7.00846   4.20733   45.61463  1.000 23.30835 ? 269  LEU   A O   1 
ATOM   1989 C  CB  . LEU   A 1 269 ? 3.95955   5.15029   45.70596  1.000 25.14839 ? 269  LEU   A CB  1 
ATOM   1990 C  CG  . LEU   A 1 269 ? 2.59275   5.58846   45.18569  1.000 32.46971 ? 269  LEU   A CG  1 
ATOM   1991 C  CD1 . LEU   A 1 269 ? 1.56341   4.47260   45.44807  1.000 29.57565 ? 269  LEU   A CD1 1 
ATOM   1992 C  CD2 . LEU   A 1 269 ? 2.19639   6.87804   45.88050  1.000 29.27693 ? 269  LEU   A CD2 1 
ATOM   1993 N  N   . VAL   A 1 270 ? 6.42930   5.20693   43.68265  1.000 29.36056 ? 270  VAL   A N   1 
ATOM   1994 C  CA  . VAL   A 1 270 ? 7.66667   5.95343   43.50363  1.000 30.48213 ? 270  VAL   A CA  1 
ATOM   1995 C  C   . VAL   A 1 270 ? 7.25540   7.39899   43.28012  1.000 30.59780 ? 270  VAL   A C   1 
ATOM   1996 O  O   . VAL   A 1 270 ? 6.46886   7.68009   42.37219  1.000 27.34124 ? 270  VAL   A O   1 
ATOM   1997 C  CB  . VAL   A 1 270 ? 8.49123   5.41347   42.32451  1.000 32.98837 ? 270  VAL   A CB  1 
ATOM   1998 C  CG1 . VAL   A 1 270 ? 9.79868   6.17863   42.17940  1.000 36.33382 ? 270  VAL   A CG1 1 
ATOM   1999 C  CG2 . VAL   A 1 270 ? 8.76072   3.94294   42.52473  1.000 33.00171 ? 270  VAL   A CG2 1 
ATOM   2000 N  N   . CYS   A 1 271 ? 7.73797   8.30669   44.13563  1.000 27.30420 ? 271  CYS   A N   1 
ATOM   2001 C  CA  . CYS   A 1 271 ? 7.30418   9.69964   44.12341  1.000 31.58590 ? 271  CYS   A CA  1 
ATOM   2002 C  C   . CYS   A 1 271 ? 8.45070   10.56373  43.61835  1.000 29.83091 ? 271  CYS   A C   1 
ATOM   2003 O  O   . CYS   A 1 271 ? 9.48695   10.66857  44.28350  1.000 28.51016 ? 271  CYS   A O   1 
ATOM   2004 C  CB  . CYS   A 1 271 ? 6.85700   10.14483  45.51775  1.000 24.70993 ? 271  CYS   A CB  1 
ATOM   2005 S  SG  . CYS   A 1 271 ? 5.64909   9.03677   46.26489  1.000 29.38128 ? 271  CYS   A SG  1 
ATOM   2006 N  N   . LEU   A 1 272 ? 8.26984   11.15423  42.43003  1.000 28.19033 ? 272  LEU   A N   1 
ATOM   2007 C  CA  . LEU   A 1 272 ? 9.23603   12.08144  41.83255  1.000 28.01774 ? 272  LEU   A CA  1 
ATOM   2008 C  C   . LEU   A 1 272 ? 8.90677   13.48346  42.33428  1.000 35.38574 ? 272  LEU   A C   1 
ATOM   2009 O  O   . LEU   A 1 272 ? 8.20625   14.25568  41.68849  1.000 32.41456 ? 272  LEU   A O   1 
ATOM   2010 C  CB  . LEU   A 1 272 ? 9.18531   12.01482  40.30622  1.000 28.02169 ? 272  LEU   A CB  1 
ATOM   2011 C  CG  . LEU   A 1 272 ? 9.32111   10.61868  39.68217  1.000 34.82372 ? 272  LEU   A CG  1 
ATOM   2012 C  CD1 . LEU   A 1 272 ? 9.24287   10.65119  38.12142  1.000 37.20999 ? 272  LEU   A CD1 1 
ATOM   2013 C  CD2 . LEU   A 1 272 ? 10.60930  9.96273   40.15612  1.000 29.47002 ? 272  LEU   A CD2 1 
ATOM   2014 N  N   . ASP   A 1 273 ? 9.42161   13.80247  43.51723  1.000 37.20244 ? 273  ASP   A N   1 
ATOM   2015 C  CA  . ASP   A 1 273 ? 9.11539   15.06751  44.16695  1.000 27.72356 ? 273  ASP   A CA  1 
ATOM   2016 C  C   . ASP   A 1 273 ? 9.78549   16.22902  43.45813  1.000 34.13500 ? 273  ASP   A C   1 
ATOM   2017 O  O   . ASP   A 1 273 ? 10.86742  16.09533  42.87565  1.000 33.53720 ? 273  ASP   A O   1 
ATOM   2018 C  CB  . ASP   A 1 273 ? 9.59503   15.06760  45.62041  1.000 23.59743 ? 273  ASP   A CB  1 
ATOM   2019 C  CG  . ASP   A 1 273 ? 8.59621   14.41961  46.57506  1.000 25.12514 ? 273  ASP   A CG  1 
ATOM   2020 O  OD1 . ASP   A 1 273 ? 7.61228   13.80448  46.08147  1.000 31.94921 ? 273  ASP   A OD1 1 
ATOM   2021 O  OD2 . ASP   A 1 273 ? 8.80597   14.52019  47.81566  1.000 28.66273 ? 273  ASP   A OD2 1 
ATOM   2022 N  N   . ALA   A 1 274 ? 9.15969   17.39120  43.58317  1.000 34.91763 ? 274  ALA   A N   1 
ATOM   2023 C  CA  . ALA   A 1 274 ? 9.70439   18.64443  43.09418  1.000 30.59924 ? 274  ALA   A CA  1 
ATOM   2024 C  C   . ALA   A 1 274 ? 10.77711  19.15073  44.05582  1.000 38.48887 ? 274  ALA   A C   1 
ATOM   2025 O  O   . ALA   A 1 274 ? 10.84308  18.71110  45.21227  1.000 39.72603 ? 274  ALA   A O   1 
ATOM   2026 C  CB  . ALA   A 1 274 ? 8.58739   19.66867  42.96104  1.000 40.74578 ? 274  ALA   A CB  1 
ATOM   2027 N  N   . PRO   A 1 275 ? 11.64342  20.06190  43.60177  1.000 38.86737 ? 275  PRO   A N   1 
ATOM   2028 C  CA  . PRO   A 1 275 ? 12.63971  20.64440  44.51177  1.000 41.36397 ? 275  PRO   A CA  1 
ATOM   2029 C  C   . PRO   A 1 275 ? 11.97428  21.33136  45.69207  1.000 56.21561 ? 275  PRO   A C   1 
ATOM   2030 O  O   . PRO   A 1 275 ? 10.92187  21.95822  45.55721  1.000 46.24013 ? 275  PRO   A O   1 
ATOM   2031 C  CB  . PRO   A 1 275 ? 13.38938  21.64460  43.62332  1.000 43.56001 ? 275  PRO   A CB  1 
ATOM   2032 C  CG  . PRO   A 1 275 ? 13.25877  21.09204  42.26292  1.000 38.75149 ? 275  PRO   A CG  1 
ATOM   2033 C  CD  . PRO   A 1 275 ? 11.88754  20.46891  42.20369  1.000 46.94002 ? 275  PRO   A CD  1 
ATOM   2034 N  N   . GLY   A 1 276 ? 12.59401  21.18059  46.86657  1.000 52.55628 ? 276  GLY   A N   1 
ATOM   2035 C  CA  . GLY   A 1 276 ? 11.99596  21.68935  48.08505  1.000 57.32122 ? 276  GLY   A CA  1 
ATOM   2036 C  C   . GLY   A 1 276 ? 12.17216  23.17762  48.26885  1.000 59.87317 ? 276  GLY   A C   1 
ATOM   2037 O  O   . GLY   A 1 276 ? 11.31786  23.83150  48.87503  1.000 70.34765 ? 276  GLY   A O   1 
ATOM   2038 N  N   . GLY   A 1 277 ? 13.26559  23.73566  47.75589  1.000 66.32874 ? 277  GLY   A N   1 
ATOM   2039 C  CA  . GLY   A 1 277 ? 13.55057  25.14166  47.93461  1.000 67.26430 ? 277  GLY   A CA  1 
ATOM   2040 C  C   . GLY   A 1 277 ? 14.12403  25.52001  49.28454  1.000 70.63467 ? 277  GLY   A C   1 
ATOM   2041 O  O   . GLY   A 1 277 ? 14.42152  26.70210  49.49915  1.000 66.52030 ? 277  GLY   A O   1 
ATOM   2042 N  N   . VAL   A 1 278 ? 14.28007  24.56984  50.20574  1.000 50.91037 ? 278  VAL   A N   1 
ATOM   2043 C  CA  . VAL   A 1 278 ? 14.91519  24.83193  51.49259  1.000 57.58298 ? 278  VAL   A CA  1 
ATOM   2044 C  C   . VAL   A 1 278 ? 16.27038  24.13066  51.50998  1.000 57.13292 ? 278  VAL   A C   1 
ATOM   2045 O  O   . VAL   A 1 278 ? 16.50814  23.16793  50.77326  1.000 58.85586 ? 278  VAL   A O   1 
ATOM   2046 C  CB  . VAL   A 1 278 ? 14.03963  24.38895  52.69443  1.000 57.84605 ? 278  VAL   A CB  1 
ATOM   2047 C  CG1 . VAL   A 1 278 ? 12.79829  25.27124  52.82723  1.000 58.68502 ? 278  VAL   A CG1 1 
ATOM   2048 C  CG2 . VAL   A 1 278 ? 13.63929  22.91037  52.58176  1.000 58.02636 ? 278  VAL   A CG2 1 
ATOM   2049 N  N   . GLU   A 1 279 ? 17.17899  24.64321  52.34741  1.000 56.22866 ? 279  GLU   A N   1 
ATOM   2050 C  CA  . GLU   A 1 279 ? 18.47295  23.99444  52.55503  1.000 57.39312 ? 279  GLU   A CA  1 
ATOM   2051 C  C   . GLU   A 1 279 ? 18.28033  22.50417  52.81405  1.000 46.67457 ? 279  GLU   A C   1 
ATOM   2052 O  O   . GLU   A 1 279 ? 17.34451  22.09294  53.50220  1.000 44.55104 ? 279  GLU   A O   1 
ATOM   2053 C  CB  . GLU   A 1 279 ? 19.21288  24.64569  53.73163  1.000 65.94058 ? 279  GLU   A CB  1 
ATOM   2054 C  CG  . GLU   A 1 279 ? 20.54511  23.98911  54.09502  1.000 50.83968 ? 279  GLU   A CG  1 
ATOM   2055 N  N   . LEU   A 1 280 ? 19.15052  21.68515  52.23843  1.000 41.12595 ? 280  LEU   A N   1 
ATOM   2056 C  CA  . LEU   A 1 280 ? 18.94584  20.24158  52.30840  1.000 44.97031 ? 280  LEU   A CA  1 
ATOM   2057 C  C   . LEU   A 1 280 ? 19.59660  19.62246  53.55124  1.000 41.09553 ? 280  LEU   A C   1 
ATOM   2058 O  O   . LEU   A 1 280 ? 20.28049  18.60711  53.47236  1.000 39.01117 ? 280  LEU   A O   1 
ATOM   2059 C  CB  . LEU   A 1 280 ? 19.45283  19.59192  51.02649  1.000 47.86606 ? 280  LEU   A CB  1 
ATOM   2060 C  CG  . LEU   A 1 280 ? 18.41200  19.50246  49.90240  1.000 47.37657 ? 280  LEU   A CG  1 
ATOM   2061 C  CD1 . LEU   A 1 280 ? 18.22529  20.84258  49.22418  1.000 55.22077 ? 280  LEU   A CD1 1 
ATOM   2062 C  CD2 . LEU   A 1 280 ? 18.78847  18.44372  48.88889  1.000 64.45180 ? 280  LEU   A CD2 1 
ATOM   2063 N  N   . SER   A 1 281 ? 19.37867  20.23778  54.71363  1.000 34.89835 ? 281  SER   A N   1 
ATOM   2064 C  CA  . SER   A 1 281 ? 19.81896  19.66322  55.97749  1.000 34.48253 ? 281  SER   A CA  1 
ATOM   2065 C  C   . SER   A 1 281 ? 19.10883  18.33837  56.25765  1.000 32.87981 ? 281  SER   A C   1 
ATOM   2066 O  O   . SER   A 1 281 ? 18.06052  18.02573  55.69040  1.000 33.42480 ? 281  SER   A O   1 
ATOM   2067 C  CB  . SER   A 1 281 ? 19.52728  20.61911  57.12539  1.000 40.29238 ? 281  SER   A CB  1 
ATOM   2068 O  OG  . SER   A 1 281 ? 18.12836  20.66265  57.34619  1.000 32.65544 ? 281  SER   A OG  1 
ATOM   2069 N  N   . ASP   A 1 282 ? 19.68865  17.55009  57.16666  1.000 33.18961 ? 282  ASP   A N   1 
ATOM   2070 C  CA  . ASP   A 1 282 ? 19.05166  16.29336  57.54124  1.000 28.93829 ? 282  ASP   A CA  1 
ATOM   2071 C  C   . ASP   A 1 282 ? 17.64745  16.53646  58.08002  1.000 24.38701 ? 282  ASP   A C   1 
ATOM   2072 O  O   . ASP   A 1 282 ? 16.71714  15.78031  57.77896  1.000 25.36436 ? 282  ASP   A O   1 
ATOM   2073 C  CB  . ASP   A 1 282 ? 19.90434  15.55149  58.57829  1.000 29.75686 ? 282  ASP   A CB  1 
ATOM   2074 C  CG  . ASP   A 1 282 ? 21.12673  14.87160  57.95798  1.000 39.76850 ? 282  ASP   A CG  1 
ATOM   2075 O  OD1 . ASP   A 1 282 ? 21.22435  14.83437  56.70767  1.000 38.64454 ? 282  ASP   A OD1 1 
ATOM   2076 O  OD2 . ASP   A 1 282 ? 21.98182  14.36866  58.72070  1.000 41.18361 ? 282  ASP   A OD2 1 
ATOM   2077 N  N   . THR   A 1 283 ? 17.47379  17.59274  58.86923  1.000 22.73507 ? 283  THR   A N   1 
ATOM   2078 C  CA  . THR   A 1 283 ? 16.14492  17.91173  59.38728  1.000 24.03760 ? 283  THR   A CA  1 
ATOM   2079 C  C   . THR   A 1 283 ? 15.16631  18.20365  58.25553  1.000 26.63954 ? 283  THR   A C   1 
ATOM   2080 O  O   . THR   A 1 283 ? 14.02707  17.72787  58.27138  1.000 26.82890 ? 283  THR   A O   1 
ATOM   2081 C  CB  . THR   A 1 283 ? 16.23676  19.10642  60.33550  1.000 31.44806 ? 283  THR   A CB  1 
ATOM   2082 O  OG1 . THR   A 1 283 ? 17.10508  18.75981  61.41458  1.000 26.57576 ? 283  THR   A OG1 1 
ATOM   2083 C  CG2 . THR   A 1 283 ? 14.85826  19.47744  60.88955  1.000 25.02267 ? 283  THR   A CG2 1 
ATOM   2084 N  N   . HIS   A 1 284 ? 15.59406  18.98066  57.26146  1.000 22.78763 ? 284  HIS   A N   1 
ATOM   2085 C  CA  . HIS   A 1 284 ? 14.68257  19.34885  56.18475  1.000 29.34960 ? 284  HIS   A CA  1 
ATOM   2086 C  C   . HIS   A 1 284 ? 14.35415  18.16147  55.28188  1.000 23.28267 ? 284  HIS   A C   1 
ATOM   2087 O  O   . HIS   A 1 284 ? 13.20183  17.99846  54.85964  1.000 26.43450 ? 284  HIS   A O   1 
ATOM   2088 C  CB  . HIS   A 1 284 ? 15.27611  20.52345  55.40476  1.000 28.90592 ? 284  HIS   A CB  1 
ATOM   2089 C  CG  . HIS   A 1 284 ? 15.13263  21.83255  56.12579  1.000 46.44134 ? 284  HIS   A CG  1 
ATOM   2090 N  ND1 . HIS   A 1 284 ? 15.75998  22.99155  55.71781  1.000 47.62871 ? 284  HIS   A ND1 1 
ATOM   2091 C  CD2 . HIS   A 1 284 ? 14.42565  22.15915  57.23684  1.000 39.00850 ? 284  HIS   A CD2 1 
ATOM   2092 C  CE1 . HIS   A 1 284 ? 15.44885  23.97357  56.54713  1.000 44.72183 ? 284  HIS   A CE1 1 
ATOM   2093 N  NE2 . HIS   A 1 284 ? 14.64201  23.49426  57.47825  1.000 51.17167 ? 284  HIS   A NE2 1 
ATOM   2094 N  N   A ARG   A 1 285 ? 15.34538  17.32036  54.97821  0.498 26.41059 ? 285  ARG   A N   1 
ATOM   2095 N  N   B ARG   A 1 285 ? 15.34738  17.32497  54.96203  0.502 26.40958 ? 285  ARG   A N   1 
ATOM   2096 C  CA  A ARG   A 1 285 ? 15.07501  16.13347  54.17320  0.498 26.53473 ? 285  ARG   A CA  1 
ATOM   2097 C  CA  B ARG   A 1 285 ? 15.05993  16.13160  54.17005  0.502 26.52631 ? 285  ARG   A CA  1 
ATOM   2098 C  C   A ARG   A 1 285 ? 14.09608  15.20734  54.88274  0.498 27.06725 ? 285  ARG   A C   1 
ATOM   2099 C  C   B ARG   A 1 285 ? 14.06321  15.23588  54.88886  0.502 27.07982 ? 285  ARG   A C   1 
ATOM   2100 O  O   A ARG   A 1 285 ? 13.21928  14.61077  54.24682  0.498 29.30742 ? 285  ARG   A O   1 
ATOM   2101 O  O   B ARG   A 1 285 ? 13.14897  14.68276  54.26649  0.502 29.26381 ? 285  ARG   A O   1 
ATOM   2102 C  CB  A ARG   A 1 285 ? 16.38773  15.41732  53.84957  0.498 29.90326 ? 285  ARG   A CB  1 
ATOM   2103 C  CB  B ARG   A 1 285 ? 16.34849  15.36486  53.86509  0.502 29.86088 ? 285  ARG   A CB  1 
ATOM   2104 C  CG  A ARG   A 1 285 ? 17.36905  16.32835  53.10711  0.498 33.16973 ? 285  ARG   A CG  1 
ATOM   2105 C  CG  B ARG   A 1 285 ? 17.40102  16.20807  53.15654  0.502 33.16974 ? 285  ARG   A CG  1 
ATOM   2106 C  CD  A ARG   A 1 285 ? 18.62566  15.61745  52.58437  0.498 37.51532 ? 285  ARG   A CD  1 
ATOM   2107 C  CD  B ARG   A 1 285 ? 18.21497  15.42356  52.11001  0.502 37.08068 ? 285  ARG   A CD  1 
ATOM   2108 N  NE  A ARG   A 1 285 ? 19.42329  15.02771  53.64989  0.498 34.16792 ? 285  ARG   A NE  1 
ATOM   2109 N  NE  B ARG   A 1 285 ? 18.75040  14.16050  52.60544  0.502 22.08261 ? 285  ARG   A NE  1 
ATOM   2110 C  CZ  A ARG   A 1 285 ? 19.76422  13.74776  53.70726  0.498 31.94245 ? 285  ARG   A CZ  1 
ATOM   2111 C  CZ  B ARG   A 1 285 ? 19.69017  14.05191  53.53462  0.502 32.10919 ? 285  ARG   A CZ  1 
ATOM   2112 N  NH1 A ARG   A 1 285 ? 19.47987  12.91036  52.72105  0.498 26.73856 ? 285  ARG   A NH1 1 
ATOM   2113 N  NH1 B ARG   A 1 285 ? 20.24032  15.12002  54.09069  0.502 40.97091 ? 285  ARG   A NH1 1 
ATOM   2114 N  NH2 A ARG   A 1 285 ? 20.41336  13.29888  54.77653  0.498 30.55021 ? 285  ARG   A NH2 1 
ATOM   2115 N  NH2 B ARG   A 1 285 ? 20.07693  12.84062  53.92679  0.502 27.76070 ? 285  ARG   A NH2 1 
ATOM   2116 N  N   . ALA   A 1 286 ? 14.20886  15.10464  56.20758  1.000 22.10995 ? 286  ALA   A N   1 
ATOM   2117 C  CA  . ALA   A 1 286 ? 13.25899  14.32185  56.98390  1.000 22.56705 ? 286  ALA   A CA  1 
ATOM   2118 C  C   . ALA   A 1 286 ? 11.86093  14.91169  56.92296  1.000 24.10753 ? 286  ALA   A C   1 
ATOM   2119 O  O   . ALA   A 1 286 ? 10.87856  14.16731  56.84822  1.000 20.85166 ? 286  ALA   A O   1 
ATOM   2120 C  CB  . ALA   A 1 286 ? 13.72609  14.23613  58.43053  1.000 22.43289 ? 286  ALA   A CB  1 
ATOM   2121 N  N   . LEU   A 1 287 ? 11.73951  16.24272  57.00593  1.000 24.78909 ? 287  LEU   A N   1 
ATOM   2122 C  CA  . LEU   A 1 287 ? 10.40500  16.83002  56.91826  1.000 23.58420 ? 287  LEU   A CA  1 
ATOM   2123 C  C   . LEU   A 1 287 ? 9.73690   16.46727  55.59626  1.000 26.19414 ? 287  LEU   A C   1 
ATOM   2124 O  O   . LEU   A 1 287 ? 8.54057   16.15829  55.56599  1.000 23.19675 ? 287  LEU   A O   1 
ATOM   2125 C  CB  . LEU   A 1 287 ? 10.47056  18.34684  57.08104  1.000 21.93606 ? 287  LEU   A CB  1 
ATOM   2126 C  CG  . LEU   A 1 287 ? 10.92652  18.78872  58.47761  1.000 23.47712 ? 287  LEU   A CG  1 
ATOM   2127 C  CD1 . LEU   A 1 287 ? 10.90276  20.29375  58.54323  1.000 31.50630 ? 287  LEU   A CD1 1 
ATOM   2128 C  CD2 . LEU   A 1 287 ? 10.08359  18.15499  59.55018  1.000 22.72525 ? 287  LEU   A CD2 1 
ATOM   2129 N  N   . GLN   A 1 288 ? 10.48953  16.52500  54.48670  1.000 22.06617 ? 288  GLN   A N   1 
ATOM   2130 C  CA  . GLN   A 1 288 ? 9.91239   16.17119  53.19242  1.000 25.74948 ? 288  GLN   A CA  1 
ATOM   2131 C  C   . GLN   A 1 288 ? 9.44352   14.72274  53.16048  1.000 24.91183 ? 288  GLN   A C   1 
ATOM   2132 O  O   . GLN   A 1 288 ? 8.39264   14.42028  52.58916  1.000 23.87839 ? 288  GLN   A O   1 
ATOM   2133 C  CB  . GLN   A 1 288 ? 10.91142  16.42603  52.06616  1.000 28.69391 ? 288  GLN   A CB  1 
ATOM   2134 C  CG  . GLN   A 1 288 ? 10.34591  16.02738  50.69751  1.000 31.54936 ? 288  GLN   A CG  1 
ATOM   2135 C  CD  . GLN   A 1 288 ? 11.19915  16.51764  49.56295  1.000 37.54678 ? 288  GLN   A CD  1 
ATOM   2136 O  OE1 . GLN   A 1 288 ? 11.93228  17.49726  49.71588  1.000 39.10235 ? 288  GLN   A OE1 1 
ATOM   2137 N  NE2 . GLN   A 1 288 ? 11.11562  15.83926  48.40670  1.000 29.83046 ? 288  GLN   A NE2 1 
ATOM   2138 N  N   . LEU   A 1 289 ? 10.20537  13.80383  53.75319  1.000 23.31325 ? 289  LEU   A N   1 
ATOM   2139 C  CA  . LEU   A 1 289 ? 9.74299   12.41890  53.80521  1.000 21.17335 ? 289  LEU   A CA  1 
ATOM   2140 C  C   . LEU   A 1 289 ? 8.56105   12.24871  54.75859  1.000 22.93955 ? 289  LEU   A C   1 
ATOM   2141 O  O   . LEU   A 1 289 ? 7.70064   11.39621  54.52709  1.000 23.28939 ? 289  LEU   A O   1 
ATOM   2142 C  CB  . LEU   A 1 289 ? 10.88131  11.48742  54.22447  1.000 20.12336 ? 289  LEU   A CB  1 
ATOM   2143 C  CG  . LEU   A 1 289 ? 11.71475  10.87476  53.08470  1.000 24.17945 ? 289  LEU   A CG  1 
ATOM   2144 C  CD1 . LEU   A 1 289 ? 10.84005  9.93323   52.24572  1.000 23.67819 ? 289  LEU   A CD1 1 
ATOM   2145 C  CD2 . LEU   A 1 289 ? 12.27678  11.95938  52.19125  1.000 35.39875 ? 289  LEU   A CD2 1 
ATOM   2146 N  N   . LEU   A 1 290 ? 8.47733   13.05147  55.82239  1.000 18.47189 ? 290  LEU   A N   1 
ATOM   2147 C  CA  . LEU   A 1 290 ? 7.38643   12.83691  56.77636  1.000 18.50146 ? 290  LEU   A CA  1 
ATOM   2148 C  C   . LEU   A 1 290 ? 6.03497   13.32993  56.25340  1.000 25.90844 ? 290  LEU   A C   1 
ATOM   2149 O  O   . LEU   A 1 290 ? 5.01005   12.65867  56.44856  1.000 23.50041 ? 290  LEU   A O   1 
ATOM   2150 C  CB  . LEU   A 1 290 ? 7.70967   13.52365  58.11117  1.000 18.67808 ? 290  LEU   A CB  1 
ATOM   2151 C  CG  . LEU   A 1 290 ? 8.66894   12.76294  59.04096  1.000 19.16114 ? 290  LEU   A CG  1 
ATOM   2152 C  CD1 . LEU   A 1 290 ? 9.18586   13.70532  60.11911  1.000 21.36746 ? 290  LEU   A CD1 1 
ATOM   2153 C  CD2 . LEU   A 1 290 ? 8.05954   11.47834  59.66578  1.000 21.82683 ? 290  LEU   A CD2 1 
ATOM   2154 N  N   . HIS   A 1 291 ? 5.99368   14.51757  55.62336  1.000 22.81339 ? 291  HIS   A N   1 
ATOM   2155 C  CA  . HIS   A 1 291 ? 4.71027   15.07066  55.20387  1.000 30.69431 ? 291  HIS   A CA  1 
ATOM   2156 C  C   . HIS   A 1 291 ? 4.78633   15.84086  53.89286  1.000 24.34407 ? 291  HIS   A C   1 
ATOM   2157 O  O   . HIS   A 1 291 ? 3.80551   16.51127  53.52964  1.000 23.08238 ? 291  HIS   A O   1 
ATOM   2158 C  CB  . HIS   A 1 291 ? 4.11099   15.97675  56.30310  1.000 20.37914 ? 291  HIS   A CB  1 
ATOM   2159 C  CG  . HIS   A 1 291 ? 5.03789   17.04152  56.80625  1.000 19.20800 ? 291  HIS   A CG  1 
ATOM   2160 N  ND1 . HIS   A 1 291 ? 5.73962   17.89134  55.97152  1.000 19.20722 ? 291  HIS   A ND1 1 
ATOM   2161 C  CD2 . HIS   A 1 291 ? 5.33417   17.42805  58.06992  1.000 18.43138 ? 291  HIS   A CD2 1 
ATOM   2162 C  CE1 . HIS   A 1 291 ? 6.45016   18.73222  56.70147  1.000 23.99065 ? 291  HIS   A CE1 1 
ATOM   2163 N  NE2 . HIS   A 1 291 ? 6.21883   18.47336  57.97995  1.000 19.62173 ? 291  HIS   A NE2 1 
ATOM   2164 N  N   . GLY   A 1 292 ? 5.89960   15.75207  53.16906  1.000 22.30925 ? 292  GLY   A N   1 
ATOM   2165 C  CA  . GLY   A 1 292 ? 6.07221   16.40570  51.88933  1.000 25.72412 ? 292  GLY   A CA  1 
ATOM   2166 C  C   . GLY   A 1 292 ? 6.07896   17.91209  51.93175  1.000 29.20178 ? 292  GLY   A C   1 
ATOM   2167 O  O   . GLY   A 1 292 ? 6.11411   18.54151  50.86436  1.000 29.01722 ? 292  GLY   A O   1 
ATOM   2168 N  N   . GLY   A 1 293 ? 6.05706   18.51219  53.11965  1.000 25.12060 ? 293  GLY   A N   1 
ATOM   2169 C  CA  . GLY   A 1 293 ? 5.94361   19.94895  53.25025  1.000 24.72953 ? 293  GLY   A CA  1 
ATOM   2170 C  C   . GLY   A 1 293 ? 4.55621   20.49842  53.01757  1.000 26.49630 ? 293  GLY   A C   1 
ATOM   2171 O  O   . GLY   A 1 293 ? 4.41267   21.71497  52.86654  1.000 30.16639 ? 293  GLY   A O   1 
ATOM   2172 N  N   . GLY   A 1 294 ? 3.51797   19.65244  52.99536  1.000 29.11789 ? 294  GLY   A N   1 
ATOM   2173 C  CA  . GLY   A 1 294 ? 2.16210   20.14578  52.77630  1.000 24.76294 ? 294  GLY   A CA  1 
ATOM   2174 C  C   . GLY   A 1 294 ? 1.80676   20.29414  51.30105  1.000 33.64986 ? 294  GLY   A C   1 
ATOM   2175 O  O   . GLY   A 1 294 ? 2.61657   20.07450  50.39497  1.000 26.79719 ? 294  GLY   A O   1 
ATOM   2176 N  N   . TYR   A 1 295 ? 0.55825   20.71128  51.05792  1.000 29.11023 ? 295  TYR   A N   1 
ATOM   2177 C  CA  . TYR   A 1 295 ? 0.03470   20.71043  49.69237  1.000 32.16106 ? 295  TYR   A CA  1 
ATOM   2178 C  C   . TYR   A 1 295 ? 0.83063   21.62727  48.76675  1.000 38.94523 ? 295  TYR   A C   1 
ATOM   2179 O  O   . TYR   A 1 295 ? 1.04649   21.29354  47.59541  1.000 38.23959 ? 295  TYR   A O   1 
ATOM   2180 C  CB  . TYR   A 1 295 ? -1.44156  21.11220  49.67902  1.000 31.63061 ? 295  TYR   A CB  1 
ATOM   2181 C  CG  . TYR   A 1 295 ? -1.96004  21.27285  48.27108  1.000 41.46169 ? 295  TYR   A CG  1 
ATOM   2182 C  CD1 . TYR   A 1 295 ? -1.86080  20.23493  47.35274  1.000 36.98414 ? 295  TYR   A CD1 1 
ATOM   2183 C  CD2 . TYR   A 1 295 ? -2.52195  22.47163  47.84929  1.000 41.19770 ? 295  TYR   A CD2 1 
ATOM   2184 C  CE1 . TYR   A 1 295 ? -2.32589  20.39106  46.03715  1.000 38.91274 ? 295  TYR   A CE1 1 
ATOM   2185 C  CE2 . TYR   A 1 295 ? -2.98793  22.62766  46.56346  1.000 43.66770 ? 295  TYR   A CE2 1 
ATOM   2186 C  CZ  . TYR   A 1 295 ? -2.87993  21.58941  45.66246  1.000 45.18246 ? 295  TYR   A CZ  1 
ATOM   2187 O  OH  . TYR   A 1 295 ? -3.34189  21.76182  44.37342  1.000 50.16911 ? 295  TYR   A OH  1 
ATOM   2188 N  N   . SER   A 1 296 ? 1.27254   22.78664  49.26299  1.000 34.15728 ? 296  SER   A N   1 
ATOM   2189 C  CA  . SER   A 1 296 ? 1.99413   23.74177  48.42280  1.000 42.61721 ? 296  SER   A CA  1 
ATOM   2190 C  C   . SER   A 1 296 ? 3.34785   23.22083  47.95953  1.000 40.73097 ? 296  SER   A C   1 
ATOM   2191 O  O   . SER   A 1 296 ? 3.96420   23.82588  47.07578  1.000 42.06851 ? 296  SER   A O   1 
ATOM   2192 C  CB  . SER   A 1 296 ? 2.18637   25.06180  49.17104  1.000 39.89845 ? 296  SER   A CB  1 
ATOM   2193 O  OG  . SER   A 1 296 ? 3.16299   24.91829  50.18605  1.000 46.66059 ? 296  SER   A OG  1 
ATOM   2194 N  N   . LYS   A 1 297 ? 3.82365   22.12398  48.52570  1.000 32.90601 ? 297  LYS   A N   1 
ATOM   2195 C  CA  . LYS   A 1 297 ? 5.11391   21.56193  48.14642  1.000 30.35963 ? 297  LYS   A CA  1 
ATOM   2196 C  C   . LYS   A 1 297 ? 4.92071   20.17088  47.55246  1.000 33.44643 ? 297  LYS   A C   1 
ATOM   2197 O  O   . LYS   A 1 297 ? 4.44443   20.04344  46.42461  1.000 35.90234 ? 297  LYS   A O   1 
ATOM   2198 C  CB  . LYS   A 1 297 ? 6.04254   21.54513  49.36308  1.000 33.05159 ? 297  LYS   A CB  1 
ATOM   2199 C  CG  . LYS   A 1 297 ? 6.43342   22.96024  49.81517  1.000 36.84239 ? 297  LYS   A CG  1 
ATOM   2200 C  CD  . LYS   A 1 297 ? 7.18215   23.65175  48.67063  1.000 42.88631 ? 297  LYS   A CD  1 
ATOM   2201 C  CE  . LYS   A 1 297 ? 7.73950   25.01642  49.08081  1.000 71.26686 ? 297  LYS   A CE  1 
ATOM   2202 N  NZ  . LYS   A 1 297 ? 8.55830   25.63617  47.99155  1.000 65.69606 ? 297  LYS   A NZ  1 
ATOM   2203 N  N   . ASN   A 1 298 ? 5.24903   19.11585  48.29718  1.000 26.51237 ? 298  ASN   A N   1 
ATOM   2204 C  CA  . ASN   A 1 298 ? 5.10374   17.75584  47.77889  1.000 34.67663 ? 298  ASN   A CA  1 
ATOM   2205 C  C   . ASN   A 1 298 ? 4.06312   16.93015  48.53083  1.000 26.40968 ? 298  ASN   A C   1 
ATOM   2206 O  O   . ASN   A 1 298 ? 3.99646   15.71701  48.32508  1.000 29.51607 ? 298  ASN   A O   1 
ATOM   2207 C  CB  . ASN   A 1 298 ? 6.44703   17.01130  47.80812  1.000 27.44698 ? 298  ASN   A CB  1 
ATOM   2208 C  CG  . ASN   A 1 298 ? 7.43864   17.53506  46.76011  1.000 36.69153 ? 298  ASN   A CG  1 
ATOM   2209 O  OD1 . ASN   A 1 298 ? 7.24159   17.35377  45.54831  1.000 33.30331 ? 298  ASN   A OD1 1 
ATOM   2210 N  ND2 . ASN   A 1 298 ? 8.50709   18.17484  47.22329  1.000 26.65638 ? 298  ASN   A ND2 1 
ATOM   2211 N  N   . GLY   A 1 299 ? 3.25521   17.54148  49.39988  1.000 28.65950 ? 299  GLY   A N   1 
ATOM   2212 C  CA  . GLY   A 1 299 ? 2.39228   16.75433  50.27762  1.000 28.20999 ? 299  GLY   A CA  1 
ATOM   2213 C  C   . GLY   A 1 299 ? 1.26659   15.99377  49.58072  1.000 29.15130 ? 299  GLY   A C   1 
ATOM   2214 O  O   . GLY   A 1 299 ? 0.75628   15.01983  50.14437  1.000 27.34078 ? 299  GLY   A O   1 
ATOM   2215 N  N   . ALA   A 1 300 ? 0.85419   16.41550  48.38476  1.000 24.45728 ? 300  ALA   A N   1 
ATOM   2216 C  CA  . ALA   A 1 300 ? -0.16005  15.67658  47.63896  1.000 26.25970 ? 300  ALA   A CA  1 
ATOM   2217 C  C   . ALA   A 1 300 ? 0.44303   14.64567  46.69450  1.000 33.56402 ? 300  ALA   A C   1 
ATOM   2218 O  O   . ALA   A 1 300 ? -0.29770  13.89382  46.05196  1.000 28.22044 ? 300  ALA   A O   1 
ATOM   2219 C  CB  . ALA   A 1 300 ? -1.05964  16.64571  46.84945  1.000 27.57582 ? 300  ALA   A CB  1 
ATOM   2220 N  N   . ASN   A 1 301 ? 1.76473   14.58457  46.60172  1.000 26.04786 ? 301  ASN   A N   1 
ATOM   2221 C  CA  . ASN   A 1 301 ? 2.44356   13.65948  45.69985  1.000 28.70791 ? 301  ASN   A CA  1 
ATOM   2222 C  C   . ASN   A 1 301 ? 2.66640   12.31521  46.38602  1.000 26.77530 ? 301  ASN   A C   1 
ATOM   2223 O  O   . ASN   A 1 301 ? 3.77080   11.76662  46.39226  1.000 26.73527 ? 301  ASN   A O   1 
ATOM   2224 C  CB  . ASN   A 1 301 ? 3.75989   14.28100  45.24971  1.000 34.07617 ? 301  ASN   A CB  1 
ATOM   2225 C  CG  . ASN   A 1 301 ? 4.22794   13.75648  43.92252  1.000 31.78090 ? 301  ASN   A CG  1 
ATOM   2226 O  OD1 . ASN   A 1 301 ? 3.46512   13.69041  42.95880  1.000 27.17319 ? 301  ASN   A OD1 1 
ATOM   2227 N  ND2 . ASN   A 1 301 ? 5.50487   13.39470  43.85487  1.000 34.64964 ? 301  ASN   A ND2 1 
ATOM   2228 N  N   . ARG   A 1 302 ? 1.58765   11.78317  46.96385  1.000 26.22515 ? 302  ARG   A N   1 
ATOM   2229 C  CA  . ARG   A 1 302 ? 1.64797   10.73561  47.97556  1.000 25.57224 ? 302  ARG   A CA  1 
ATOM   2230 C  C   . ARG   A 1 302 ? 0.36564   9.91468   47.93050  1.000 29.27914 ? 302  ARG   A C   1 
ATOM   2231 O  O   . ARG   A 1 302 ? -0.68691  10.39491  47.50838  1.000 26.78936 ? 302  ARG   A O   1 
ATOM   2232 C  CB  . ARG   A 1 302 ? 1.78172   11.33620  49.38271  1.000 28.03300 ? 302  ARG   A CB  1 
ATOM   2233 C  CG  . ARG   A 1 302 ? 3.03330   12.16264  49.63843  1.000 25.94866 ? 302  ARG   A CG  1 
ATOM   2234 C  CD  . ARG   A 1 302 ? 4.24694   11.28647  49.83950  1.000 23.18778 ? 302  ARG   A CD  1 
ATOM   2235 N  NE  . ARG   A 1 302 ? 5.39782   12.08194  50.25915  1.000 26.11137 ? 302  ARG   A NE  1 
ATOM   2236 C  CZ  . ARG   A 1 302 ? 6.23205   12.68655  49.42849  1.000 33.25780 ? 302  ARG   A CZ  1 
ATOM   2237 N  NH1 . ARG   A 1 302 ? 6.08019   12.60152  48.10941  1.000 24.39156 ? 302  ARG   A NH1 1 
ATOM   2238 N  NH2 . ARG   A 1 302 ? 7.22519   13.42362  49.93154  1.000 25.79515 ? 302  ARG   A NH2 1 
ATOM   2239 N  N   . TRP   A 1 303 ? 0.44710   8.68850   48.42728  1.000 27.48762 ? 303  TRP   A N   1 
ATOM   2240 C  CA  . TRP   A 1 303 ? -0.74331  7.87031   48.67650  1.000 24.09862 ? 303  TRP   A CA  1 
ATOM   2241 C  C   . TRP   A 1 303 ? -0.47117  7.10199   49.96974  1.000 24.34641 ? 303  TRP   A C   1 
ATOM   2242 O  O   . TRP   A 1 303 ? 0.14628   6.03824   49.93882  1.000 21.58672 ? 303  TRP   A O   1 
ATOM   2243 C  CB  . TRP   A 1 303 ? -1.04058  6.92553   47.51299  1.000 25.64320 ? 303  TRP   A CB  1 
ATOM   2244 C  CG  . TRP   A 1 303 ? -2.46268  6.43944   47.55017  1.000 24.74546 ? 303  TRP   A CG  1 
ATOM   2245 C  CD1 . TRP   A 1 303 ? -2.95284  5.38691   48.28019  1.000 25.58436 ? 303  TRP   A CD1 1 
ATOM   2246 C  CD2 . TRP   A 1 303 ? -3.58606  7.02465   46.88021  1.000 22.55399 ? 303  TRP   A CD2 1 
ATOM   2247 N  NE1 . TRP   A 1 303 ? -4.32220  5.26897   48.08299  1.000 26.43396 ? 303  TRP   A NE1 1 
ATOM   2248 C  CE2 . TRP   A 1 303 ? -4.72834  6.27031   47.23221  1.000 23.94810 ? 303  TRP   A CE2 1 
ATOM   2249 C  CE3 . TRP   A 1 303 ? -3.73480  8.10687   46.00172  1.000 27.96158 ? 303  TRP   A CE3 1 
ATOM   2250 C  CZ2 . TRP   A 1 303 ? -6.00642  6.57321   46.74229  1.000 26.48423 ? 303  TRP   A CZ2 1 
ATOM   2251 C  CZ3 . TRP   A 1 303 ? -4.99674  8.40684   45.52327  1.000 29.31695 ? 303  TRP   A CZ3 1 
ATOM   2252 C  CH2 . TRP   A 1 303 ? -6.11942  7.63843   45.88883  1.000 27.60856 ? 303  TRP   A CH2 1 
ATOM   2253 N  N   . TYR   A 1 304 ? -0.93753  7.62826   51.10471  1.000 22.34207 ? 304  TYR   A N   1 
ATOM   2254 C  CA  . TYR   A 1 304 ? -0.44234  7.11158   52.37501  1.000 20.39352 ? 304  TYR   A CA  1 
ATOM   2255 C  C   . TYR   A 1 304 ? -0.97168  5.73347   52.73295  1.000 25.17999 ? 304  TYR   A C   1 
ATOM   2256 O  O   . TYR   A 1 304 ? -0.41284  5.10628   53.64057  1.000 20.07794 ? 304  TYR   A O   1 
ATOM   2257 C  CB  . TYR   A 1 304 ? -0.75060  8.09128   53.50479  1.000 21.24616 ? 304  TYR   A CB  1 
ATOM   2258 C  CG  . TYR   A 1 304 ? 0.18700   9.28009   53.50205  1.000 22.33828 ? 304  TYR   A CG  1 
ATOM   2259 C  CD1 . TYR   A 1 304 ? 1.41242   9.21947   54.17667  1.000 20.65154 ? 304  TYR   A CD1 1 
ATOM   2260 C  CD2 . TYR   A 1 304 ? -0.14123  10.45478  52.81880  1.000 22.30914 ? 304  TYR   A CD2 1 
ATOM   2261 C  CE1 . TYR   A 1 304 ? 2.29102   10.31526  54.18062  1.000 18.63387 ? 304  TYR   A CE1 1 
ATOM   2262 C  CE2 . TYR   A 1 304 ? 0.72455   11.56144  52.82317  1.000 26.61935 ? 304  TYR   A CE2 1 
ATOM   2263 C  CZ  . TYR   A 1 304 ? 1.94722   11.46480  53.49496  1.000 23.77483 ? 304  TYR   A CZ  1 
ATOM   2264 O  OH  . TYR   A 1 304 ? 2.83372   12.52199  53.51720  1.000 24.98340 ? 304  TYR   A OH  1 
ATOM   2265 N  N   . ASP   A 1 305 ? -2.00841  5.24474   52.06381  1.000 21.57752 ? 305  ASP   A N   1 
ATOM   2266 C  CA  . ASP   A 1 305 ? -2.51220  3.90683   52.38310  1.000 23.81111 ? 305  ASP   A CA  1 
ATOM   2267 C  C   . ASP   A 1 305 ? -1.57369  2.80895   51.91734  1.000 24.06277 ? 305  ASP   A C   1 
ATOM   2268 O  O   . ASP   A 1 305 ? -1.65433  1.67651   52.41461  1.000 21.07592 ? 305  ASP   A O   1 
ATOM   2269 C  CB  . ASP   A 1 305 ? -3.86155  3.65153   51.71722  1.000 24.22496 ? 305  ASP   A CB  1 
ATOM   2270 C  CG  . ASP   A 1 305 ? -5.00469  4.47579   52.29516  1.000 29.94364 ? 305  ASP   A CG  1 
ATOM   2271 O  OD1 . ASP   A 1 305 ? -4.85361  5.09816   53.36996  1.000 28.20285 ? 305  ASP   A OD1 1 
ATOM   2272 O  OD2 . ASP   A 1 305 ? -6.08979  4.45760   51.66424  1.000 26.61612 ? 305  ASP   A OD2 1 
ATOM   2273 N  N   . LYS   A 1 306 ? -0.71461  3.09878   50.95156  1.000 21.49940 ? 306  LYS   A N   1 
ATOM   2274 C  CA  . LYS   A 1 306 ? 0.15497   2.07033   50.39768  1.000 23.69610 ? 306  LYS   A CA  1 
ATOM   2275 C  C   . LYS   A 1 306 ? 1.40940   1.94391   51.26269  1.000 23.64474 ? 306  LYS   A C   1 
ATOM   2276 O  O   . LYS   A 1 306 ? 1.93541   2.93740   51.76366  1.000 24.52641 ? 306  LYS   A O   1 
ATOM   2277 C  CB  . LYS   A 1 306 ? 0.51626   2.41891   48.94969  1.000 24.76448 ? 306  LYS   A CB  1 
ATOM   2278 C  CG  . LYS   A 1 306 ? 1.31144   1.33509   48.22439  1.000 30.76899 ? 306  LYS   A CG  1 
ATOM   2279 C  CD  . LYS   A 1 306 ? 0.53605   -0.00682  48.15734  1.000 34.60200 ? 306  LYS   A CD  1 
ATOM   2280 C  CE  . LYS   A 1 306 ? 1.48472   -1.12699  47.68588  1.000 48.98143 ? 306  LYS   A CE  1 
ATOM   2281 N  NZ  . LYS   A 1 306 ? 1.15258   -2.53713  48.12680  1.000 41.27412 ? 306  LYS   A NZ  1 
ATOM   2282 N  N   . SER   A 1 307 ? 1.90653   0.71842   51.41968  1.000 18.89471 ? 307  SER   A N   1 
ATOM   2283 C  CA  . SER   A 1 307 ? 2.86057   0.46055   52.50143  1.000 23.55497 ? 307  SER   A CA  1 
ATOM   2284 C  C   . SER   A 1 307 ? 4.19975   1.14849   52.28135  1.000 24.21388 ? 307  SER   A C   1 
ATOM   2285 O  O   . SER   A 1 307 ? 4.84108   1.59118   53.24788  1.000 22.94102 ? 307  SER   A O   1 
ATOM   2286 C  CB  . SER   A 1 307 ? 3.06246   -1.04078  52.65762  1.000 28.92649 ? 307  SER   A CB  1 
ATOM   2287 O  OG  . SER   A 1 307 ? 1.85888   -1.59598  53.12078  1.000 31.98097 ? 307  SER   A OG  1 
ATOM   2288 N  N   . LEU   A 1 308 ? 4.67216   1.22273   51.04100  1.000 24.14051 ? 308  LEU   A N   1 
ATOM   2289 C  CA  . LEU   A 1 308 ? 5.97334   1.83875   50.78132  1.000 23.57350 ? 308  LEU   A CA  1 
ATOM   2290 C  C   . LEU   A 1 308 ? 5.82184   2.89780   49.71208  1.000 25.31533 ? 308  LEU   A C   1 
ATOM   2291 O  O   . LEU   A 1 308 ? 5.32063   2.60897   48.61778  1.000 22.63829 ? 308  LEU   A O   1 
ATOM   2292 C  CB  . LEU   A 1 308 ? 7.01919   0.80937   50.34948  1.000 18.56508 ? 308  LEU   A CB  1 
ATOM   2293 C  CG  . LEU   A 1 308 ? 7.41266   -0.24313  51.37729  1.000 22.08593 ? 308  LEU   A CG  1 
ATOM   2294 C  CD1 . LEU   A 1 308 ? 8.41896   -1.17724  50.73079  1.000 27.02603 ? 308  LEU   A CD1 1 
ATOM   2295 C  CD2 . LEU   A 1 308 ? 7.98718   0.39844   52.63777  1.000 24.50640 ? 308  LEU   A CD2 1 
ATOM   2296 N  N   . GLN   A 1 309 ? 6.27003   4.11330   50.02277  1.000 19.74037 ? 309  GLN   A N   1 
ATOM   2297 C  CA  . GLN   A 1 309 ? 6.30960   5.21098   49.05664  1.000 23.90353 ? 309  GLN   A CA  1 
ATOM   2298 C  C   . GLN   A 1 309 ? 7.75907   5.67248   48.99961  1.000 22.09062 ? 309  GLN   A C   1 
ATOM   2299 O  O   . GLN   A 1 309 ? 8.21816   6.41787   49.87412  1.000 22.55643 ? 309  GLN   A O   1 
ATOM   2300 C  CB  . GLN   A 1 309 ? 5.40974   6.37131   49.45419  1.000 23.30563 ? 309  GLN   A CB  1 
ATOM   2301 C  CG  . GLN   A 1 309 ? 3.94293   6.09221   49.65743  1.000 19.93293 ? 309  GLN   A CG  1 
ATOM   2302 C  CD  . GLN   A 1 309 ? 3.28502   7.29303   50.27808  1.000 27.59967 ? 309  GLN   A CD  1 
ATOM   2303 O  OE1 . GLN   A 1 309 ? 3.03161   8.28273   49.60730  1.000 23.80968 ? 309  GLN   A OE1 1 
ATOM   2304 N  NE2 . GLN   A 1 309 ? 3.06998   7.24313   51.58421  1.000 21.97073 ? 309  GLN   A NE2 1 
ATOM   2305 N  N   . PHE   A 1 310 ? 8.47838   5.20945   47.99021  1.000 25.65913 ? 310  PHE   A N   1 
ATOM   2306 C  CA  . PHE   A 1 310 ? 9.83781   5.66125   47.77051  1.000 24.96709 ? 310  PHE   A CA  1 
ATOM   2307 C  C   . PHE   A 1 310 ? 9.80901   7.05892   47.17961  1.000 33.91178 ? 310  PHE   A C   1 
ATOM   2308 O  O   . PHE   A 1 310 ? 9.11969   7.31004   46.18977  1.000 34.56065 ? 310  PHE   A O   1 
ATOM   2309 C  CB  . PHE   A 1 310 ? 10.56313  4.70223   46.83465  1.000 21.49515 ? 310  PHE   A CB  1 
ATOM   2310 C  CG  . PHE   A 1 310 ? 10.79379  3.35347   47.44122  1.000 24.41093 ? 310  PHE   A CG  1 
ATOM   2311 C  CD1 . PHE   A 1 310 ? 11.88331  3.13110   48.26449  1.000 20.90178 ? 310  PHE   A CD1 1 
ATOM   2312 C  CD2 . PHE   A 1 310 ? 9.91971   2.30784   47.20660  1.000 27.09265 ? 310  PHE   A CD2 1 
ATOM   2313 C  CE1 . PHE   A 1 310 ? 12.09085  1.89648   48.83297  1.000 26.27655 ? 310  PHE   A CE1 1 
ATOM   2314 C  CE2 . PHE   A 1 310 ? 10.14165  1.05860   47.77895  1.000 21.53089 ? 310  PHE   A CE2 1 
ATOM   2315 C  CZ  . PHE   A 1 310 ? 11.22976  0.85914   48.57110  1.000 27.65486 ? 310  PHE   A CZ  1 
ATOM   2316 N  N   . VAL   A 1 311 ? 10.54681  7.97130   47.78652  1.000 25.20135 ? 311  VAL   A N   1 
ATOM   2317 C  CA  . VAL   A 1 311 ? 10.63531  9.33190   47.28541  1.000 25.83194 ? 311  VAL   A CA  1 
ATOM   2318 C  C   . VAL   A 1 311 ? 11.99086  9.49453   46.61484  1.000 28.58247 ? 311  VAL   A C   1 
ATOM   2319 O  O   . VAL   A 1 311 ? 13.01700  9.12542   47.18914  1.000 24.15479 ? 311  VAL   A O   1 
ATOM   2320 C  CB  . VAL   A 1 311 ? 10.42640  10.34165  48.42692  1.000 25.17455 ? 311  VAL   A CB  1 
ATOM   2321 C  CG1 . VAL   A 1 311 ? 10.62452  11.77241  47.92473  1.000 27.84066 ? 311  VAL   A CG1 1 
ATOM   2322 C  CG2 . VAL   A 1 311 ? 9.02536   10.15583  48.99546  1.000 24.84222 ? 311  VAL   A CG2 1 
ATOM   2323 N  N   . VAL   A 1 312 ? 11.99435  9.98226   45.37487  1.000 27.31064 ? 312  VAL   A N   1 
ATOM   2324 C  CA  . VAL   A 1 312 ? 13.22446  10.32579  44.66081  1.000 26.12283 ? 312  VAL   A CA  1 
ATOM   2325 C  C   . VAL   A 1 312 ? 13.03872  11.77042  44.20639  1.000 35.03684 ? 312  VAL   A C   1 
ATOM   2326 O  O   . VAL   A 1 312 ? 12.44484  12.04300  43.15536  1.000 30.21907 ? 312  VAL   A O   1 
ATOM   2327 C  CB  . VAL   A 1 312 ? 13.51727  9.38931   43.47979  1.000 32.74118 ? 312  VAL   A CB  1 
ATOM   2328 C  CG1 . VAL   A 1 312 ? 14.80499  9.81197   42.77503  1.000 27.40892 ? 312  VAL   A CG1 1 
ATOM   2329 C  CG2 . VAL   A 1 312 ? 13.64474  7.91316   43.96016  1.000 25.23622 ? 312  VAL   A CG2 1 
ATOM   2330 N  N   . GLY   A 1 313 ? 13.50141  12.71177  45.02350  1.000 33.73256 ? 313  GLY   A N   1 
ATOM   2331 C  CA  . GLY   A 1 313 ? 13.24294  14.11352  44.74692  1.000 35.71546 ? 313  GLY   A CA  1 
ATOM   2332 C  C   . GLY   A 1 313 ? 14.19354  14.68268  43.70859  1.000 29.89325 ? 313  GLY   A C   1 
ATOM   2333 O  O   . GLY   A 1 313 ? 15.34555  14.26451  43.58754  1.000 33.01509 ? 313  GLY   A O   1 
ATOM   2334 N  N   . ARG   A 1 314 ? 13.69509  15.67003  42.95236  1.000 31.63688 ? 314  ARG   A N   1 
ATOM   2335 C  CA  . ARG   A 1 314 ? 14.50968  16.27344  41.89739  1.000 37.39395 ? 314  ARG   A CA  1 
ATOM   2336 C  C   . ARG   A 1 314 ? 15.81708  16.85067  42.44507  1.000 42.72278 ? 314  ARG   A C   1 
ATOM   2337 O  O   . ARG   A 1 314 ? 16.84762  16.81888  41.75742  1.000 43.83952 ? 314  ARG   A O   1 
ATOM   2338 C  CB  . ARG   A 1 314 ? 13.70071  17.35350  41.15886  1.000 32.54635 ? 314  ARG   A CB  1 
ATOM   2339 C  CG  . ARG   A 1 314 ? 14.51223  18.20862  40.17570  1.000 37.64629 ? 314  ARG   A CG  1 
ATOM   2340 C  CD  . ARG   A 1 314 ? 14.95643  17.41184  38.96925  1.000 32.75544 ? 314  ARG   A CD  1 
ATOM   2341 N  NE  . ARG   A 1 314 ? 15.81300  18.19752  38.08665  1.000 42.65501 ? 314  ARG   A NE  1 
ATOM   2342 C  CZ  . ARG   A 1 314 ? 17.09675  18.45689  38.30890  1.000 41.52663 ? 314  ARG   A CZ  1 
ATOM   2343 N  NH1 . ARG   A 1 314 ? 17.72170  17.99718  39.38153  1.000 39.17746 ? 314  ARG   A NH1 1 
ATOM   2344 N  NH2 . ARG   A 1 314 ? 17.77274  19.19481  37.42839  1.000 47.08193 ? 314  ARG   A NH2 1 
ATOM   2345 N  N   . ASP   A 1 315 ? 15.80829  17.35639  43.67658  1.000 37.02629 ? 315  ASP   A N   1 
ATOM   2346 C  CA  . ASP   A 1 315 ? 17.00220  17.94240  44.27865  1.000 38.89948 ? 315  ASP   A CA  1 
ATOM   2347 C  C   . ASP   A 1 315 ? 17.88478  16.93458  45.02467  1.000 45.62535 ? 315  ASP   A C   1 
ATOM   2348 O  O   . ASP   A 1 315 ? 18.89047  17.33260  45.62448  1.000 38.55491 ? 315  ASP   A O   1 
ATOM   2349 C  CB  . ASP   A 1 315 ? 16.59464  19.08616  45.21596  1.000 42.39648 ? 315  ASP   A CB  1 
ATOM   2350 C  CG  . ASP   A 1 315 ? 15.58954  18.65711  46.28693  1.000 50.44598 ? 315  ASP   A CG  1 
ATOM   2351 O  OD1 . ASP   A 1 315 ? 15.22033  17.46101  46.35201  1.000 40.34244 ? 315  ASP   A OD1 1 
ATOM   2352 O  OD2 . ASP   A 1 315 ? 15.16144  19.53861  47.06894  1.000 41.53115 ? 315  ASP   A OD2 1 
ATOM   2353 N  N   . GLY   A 1 316 ? 17.56402  15.64621  44.99467  1.000 33.40511 ? 316  GLY   A N   1 
ATOM   2354 C  CA  . GLY   A 1 316 ? 18.40005  14.65511  45.64075  1.000 31.21011 ? 316  GLY   A CA  1 
ATOM   2355 C  C   . GLY   A 1 316 ? 17.93803  14.22466  47.02128  1.000 30.44061 ? 316  GLY   A C   1 
ATOM   2356 O  O   . GLY   A 1 316 ? 18.66863  13.50272  47.70452  1.000 34.74065 ? 316  GLY   A O   1 
ATOM   2357 N  N   . THR   A 1 317 ? 16.75993  14.64532  47.45418  1.000 30.82530 ? 317  THR   A N   1 
ATOM   2358 C  CA  . THR   A 1 317 ? 16.19623  14.12138  48.68940  1.000 29.31184 ? 317  THR   A CA  1 
ATOM   2359 C  C   . THR   A 1 317 ? 15.48145  12.81324  48.37154  1.000 30.27329 ? 317  THR   A C   1 
ATOM   2360 O  O   . THR   A 1 317 ? 14.54423  12.78868  47.56317  1.000 29.62702 ? 317  THR   A O   1 
ATOM   2361 C  CB  . THR   A 1 317 ? 15.25171  15.13940  49.32211  1.000 35.11576 ? 317  THR   A CB  1 
ATOM   2362 O  OG1 . THR   A 1 317 ? 16.00774  16.29196  49.72277  1.000 35.34229 ? 317  THR   A OG1 1 
ATOM   2363 C  CG2 . THR   A 1 317 ? 14.57341  14.53932  50.55728  1.000 36.94759 ? 317  THR   A CG2 1 
ATOM   2364 N  N   . CYS   A 1 318 ? 15.95410  11.72425  48.97275  1.000 25.93675 ? 318  CYS   A N   1 
ATOM   2365 C  CA  . CYS   A 1 318 ? 15.44103  10.38837  48.70766  1.000 27.59717 ? 318  CYS   A CA  1 
ATOM   2366 C  C   . CYS   A 1 318 ? 15.19299  9.66677   50.02355  1.000 28.21514 ? 318  CYS   A C   1 
ATOM   2367 O  O   . CYS   A 1 318 ? 15.93246  9.84955   50.99883  1.000 24.95181 ? 318  CYS   A O   1 
ATOM   2368 C  CB  . CYS   A 1 318 ? 16.41693  9.56857   47.86663  1.000 27.34975 ? 318  CYS   A CB  1 
ATOM   2369 S  SG  . CYS   A 1 318 ? 16.79135  10.30508  46.24267  1.000 35.34794 ? 318  CYS   A SG  1 
ATOM   2370 N  N   . GLY   A 1 319 ? 14.16094  8.83307   50.03360  1.000 23.41972 ? 319  GLY   A N   1 
ATOM   2371 C  CA  . GLY   A 1 319 ? 13.89841  7.99631   51.19807  1.000 21.52009 ? 319  GLY   A CA  1 
ATOM   2372 C  C   . GLY   A 1 319 ? 12.66097  7.17015   50.95126  1.000 26.89757 ? 319  GLY   A C   1 
ATOM   2373 O  O   . GLY   A 1 319 ? 12.22967  7.00539   49.80959  1.000 21.60888 ? 319  GLY   A O   1 
ATOM   2374 N  N   . VAL   A 1 320 ? 12.06060  6.66560   52.01621  1.000 24.71025 ? 320  VAL   A N   1 
ATOM   2375 C  CA  . VAL   A 1 320 ? 10.83175  5.90359   51.84540  1.000 21.85186 ? 320  VAL   A CA  1 
ATOM   2376 C  C   . VAL   A 1 320 ? 9.90679   6.23185   53.00870  1.000 21.00912 ? 320  VAL   A C   1 
ATOM   2377 O  O   . VAL   A 1 320 ? 10.34961  6.33766   54.16093  1.000 20.97737 ? 320  VAL   A O   1 
ATOM   2378 C  CB  . VAL   A 1 320 ? 11.11718  4.38713   51.69912  1.000 21.59477 ? 320  VAL   A CB  1 
ATOM   2379 C  CG1 . VAL   A 1 320 ? 11.87444  3.80722   52.93526  1.000 17.68406 ? 320  VAL   A CG1 1 
ATOM   2380 C  CG2 . VAL   A 1 320 ? 9.83699   3.60188   51.41773  1.000 21.73734 ? 320  VAL   A CG2 1 
ATOM   2381 N  N   . VAL   A 1 321 ? 8.63760   6.47133   52.69812  1.000 19.37159 ? 321  VAL   A N   1 
ATOM   2382 C  CA  . VAL   A 1 321 ? 7.59855   6.69369   53.70977  1.000 18.06741 ? 321  VAL   A CA  1 
ATOM   2383 C  C   . VAL   A 1 321 ? 6.88966   5.36950   53.92797  1.000 22.38915 ? 321  VAL   A C   1 
ATOM   2384 O  O   . VAL   A 1 321 ? 6.45231   4.73742   52.95907  1.000 20.58142 ? 321  VAL   A O   1 
ATOM   2385 C  CB  . VAL   A 1 321 ? 6.56392   7.76035   53.27414  1.000 25.41891 ? 321  VAL   A CB  1 
ATOM   2386 C  CG1 . VAL   A 1 321 ? 5.74175   8.22272   54.49634  1.000 26.70515 ? 321  VAL   A CG1 1 
ATOM   2387 C  CG2 . VAL   A 1 321 ? 7.17805   8.93541   52.54620  1.000 28.79686 ? 321  VAL   A CG2 1 
ATOM   2388 N  N   . CYS   A 1 322 ? 6.72580   4.95909   55.18908  1.000 22.70779 ? 322  CYS   A N   1 
ATOM   2389 C  CA  . CYS   A 1 322 ? 6.30202   3.59304   55.50075  1.000 23.26087 ? 322  CYS   A CA  1 
ATOM   2390 C  C   . CYS   A 1 322 ? 4.96091   3.60230   56.21637  1.000 22.04402 ? 322  CYS   A C   1 
ATOM   2391 O  O   . CYS   A 1 322 ? 4.84966   4.17283   57.30231  1.000 25.26622 ? 322  CYS   A O   1 
ATOM   2392 C  CB  . CYS   A 1 322 ? 7.33809   2.89590   56.38657  1.000 24.42205 ? 322  CYS   A CB  1 
ATOM   2393 S  SG  . CYS   A 1 322 ? 8.97119   2.84690   55.65097  1.000 24.76647 ? 322  CYS   A SG  1 
ATOM   2394 N  N   . GLU   A 1 323 ? 3.95979   2.92641   55.65024  1.000 23.07081 ? 323  GLU   A N   1 
ATOM   2395 C  CA  . GLU   A 1 323 ? 2.75324   2.63816   56.41793  1.000 19.78769 ? 323  GLU   A CA  1 
ATOM   2396 C  C   . GLU   A 1 323 ? 3.08233   1.40844   57.25381  1.000 29.03044 ? 323  GLU   A C   1 
ATOM   2397 O  O   . GLU   A 1 323 ? 3.28249   0.32278   56.70896  1.000 31.62713 ? 323  GLU   A O   1 
ATOM   2398 C  CB  . GLU   A 1 323 ? 1.54194   2.40806   55.51295  1.000 22.29766 ? 323  GLU   A CB  1 
ATOM   2399 C  CG  . GLU   A 1 323 ? 0.21873   2.74391   56.20368  1.000 24.66358 ? 323  GLU   A CG  1 
ATOM   2400 C  CD  . GLU   A 1 323 ? -0.18957  1.69466   57.21810  1.000 26.69015 ? 323  GLU   A CD  1 
ATOM   2401 O  OE1 . GLU   A 1 323 ? -0.34647  0.51757   56.82791  1.000 29.07723 ? 323  GLU   A OE1 1 
ATOM   2402 O  OE2 . GLU   A 1 323 ? -0.36038  2.04274   58.40946  1.000 28.27044 ? 323  GLU   A OE2 1 
ATOM   2403 N  N   A HIS   A 1 324 ? 3.05919   1.61923   58.58162  0.447 26.82870 ? 324  HIS   A N   1 
ATOM   2404 N  N   B HIS   A 1 324 ? 3.22260   1.53768   58.56451  0.553 26.96485 ? 324  HIS   A N   1 
ATOM   2405 C  CA  A HIS   A 1 324 ? 3.63163   0.77285   59.63018  0.447 29.10858 ? 324  HIS   A CA  1 
ATOM   2406 C  CA  B HIS   A 1 324 ? 3.83932   0.41241   59.25536  0.553 28.03024 ? 324  HIS   A CA  1 
ATOM   2407 C  C   A HIS   A 1 324 ? 2.85238   -0.51622  59.86277  0.447 24.30263 ? 324  HIS   A C   1 
ATOM   2408 C  C   B HIS   A 1 324 ? 2.83703   -0.52327  59.93833  0.553 24.25604 ? 324  HIS   A C   1 
ATOM   2409 O  O   A HIS   A 1 324 ? 3.42308   -1.49710  60.35410  0.447 20.99097 ? 324  HIS   A O   1 
ATOM   2410 O  O   B HIS   A 1 324 ? 3.23773   -1.30385  60.80890  0.553 22.19136 ? 324  HIS   A O   1 
ATOM   2411 C  CB  A HIS   A 1 324 ? 3.67814   1.60508   60.92920  0.447 24.94115 ? 324  HIS   A CB  1 
ATOM   2412 C  CB  B HIS   A 1 324 ? 4.91379   0.89938   60.23721  0.553 19.29212 ? 324  HIS   A CB  1 
ATOM   2413 C  CG  A HIS   A 1 324 ? 4.55055   1.04347   62.01552  0.447 21.87106 ? 324  HIS   A CG  1 
ATOM   2414 C  CG  B HIS   A 1 324 ? 4.38946   1.67641   61.40553  0.553 26.55502 ? 324  HIS   A CG  1 
ATOM   2415 N  ND1 A HIS   A 1 324 ? 4.99908   -0.25747  62.02849  0.447 23.36990 ? 324  HIS   A ND1 1 
ATOM   2416 N  ND1 B HIS   A 1 324 ? 3.32602   2.54461   61.31242  0.553 18.50079 ? 324  HIS   A ND1 1 
ATOM   2417 C  CD2 A HIS   A 1 324 ? 5.06670   1.62710   63.12424  0.447 27.77285 ? 324  HIS   A CD2 1 
ATOM   2418 C  CD2 B HIS   A 1 324 ? 4.81282   1.73575   62.69007  0.553 28.80276 ? 324  HIS   A CD2 1 
ATOM   2419 C  CE1 A HIS   A 1 324 ? 5.74877   -0.45609  63.09836  0.447 25.06406 ? 324  HIS   A CE1 1 
ATOM   2420 C  CE1 B HIS   A 1 324 ? 3.10346   3.09176   62.49317  0.553 26.83907 ? 324  HIS   A CE1 1 
ATOM   2421 N  NE2 A HIS   A 1 324 ? 5.80639   0.67366   63.77980  0.447 29.50229 ? 324  HIS   A NE2 1 
ATOM   2422 N  NE2 B HIS   A 1 324 ? 4.00190   2.62811   63.34350  0.553 21.95489 ? 324  HIS   A NE2 1 
ATOM   2423 N  N   . SER   A 1 325 ? 1.57108   -0.54923  59.51204  1.000 22.63702 ? 325  SER   A N   1 
ATOM   2424 C  CA  . SER   A 1 325 ? 0.70834   -1.62453  60.00083  1.000 20.05166 ? 325  SER   A CA  1 
ATOM   2425 C  C   . SER   A 1 325 ? 1.17671   -3.03394  59.62567  1.000 25.11912 ? 325  SER   A C   1 
ATOM   2426 O  O   . SER   A 1 325 ? 0.96098   -3.93741  60.45401  1.000 23.57677 ? 325  SER   A O   1 
ATOM   2427 C  CB  . SER   A 1 325 ? -0.76149  -1.39329  59.58214  1.000 21.00276 ? 325  SER   A CB  1 
ATOM   2428 O  OG  . SER   A 1 325 ? -0.98102  -1.57807  58.20439  1.000 26.86838 ? 325  SER   A OG  1 
ATOM   2429 N  N   . PRO   A 1 326 ? 1.81734   -3.30041  58.47286  1.000 20.77502 ? 326  PRO   A N   1 
ATOM   2430 C  CA  . PRO   A 1 326 ? 2.24927   -4.66999  58.16437  1.000 19.49531 ? 326  PRO   A CA  1 
ATOM   2431 C  C   . PRO   A 1 326 ? 3.67056   -5.06599  58.53649  1.000 22.57729 ? 326  PRO   A C   1 
ATOM   2432 O  O   . PRO   A 1 326 ? 3.99817   -6.24173  58.35182  1.000 22.27213 ? 326  PRO   A O   1 
ATOM   2433 C  CB  . PRO   A 1 326 ? 2.10994   -4.74494  56.62213  1.000 27.15879 ? 326  PRO   A CB  1 
ATOM   2434 C  CG  . PRO   A 1 326 ? 1.77740   -3.37116  56.15868  1.000 27.38696 ? 326  PRO   A CG  1 
ATOM   2435 C  CD  . PRO   A 1 326 ? 1.99986   -2.43928  57.29215  1.000 25.18603 ? 326  PRO   A CD  1 
ATOM   2436 N  N   . PHE   A 1 327 ? 4.53912   -4.16230  58.99335  1.000 18.69517 ? 327  PHE   A N   1 
ATOM   2437 C  CA  . PHE   A 1 327 ? 5.90626   -4.55550  59.31216  1.000 21.90160 ? 327  PHE   A CA  1 
ATOM   2438 C  C   . PHE   A 1 327 ? 6.51849   -3.50946  60.22714  1.000 21.57061 ? 327  PHE   A C   1 
ATOM   2439 O  O   . PHE   A 1 327 ? 6.09366   -2.34813  60.24678  1.000 20.21838 ? 327  PHE   A O   1 
ATOM   2440 C  CB  . PHE   A 1 327 ? 6.77195   -4.71153  58.04310  1.000 21.61045 ? 327  PHE   A CB  1 
ATOM   2441 C  CG  . PHE   A 1 327 ? 6.63606   -3.55191  57.09274  1.000 20.14853 ? 327  PHE   A CG  1 
ATOM   2442 C  CD1 . PHE   A 1 327 ? 7.34616   -2.36668  57.30340  1.000 20.66156 ? 327  PHE   A CD1 1 
ATOM   2443 C  CD2 . PHE   A 1 327 ? 5.77204   -3.63739  55.99490  1.000 24.32565 ? 327  PHE   A CD2 1 
ATOM   2444 C  CE1 . PHE   A 1 327 ? 7.18054   -1.27245  56.45416  1.000 26.49394 ? 327  PHE   A CE1 1 
ATOM   2445 C  CE2 . PHE   A 1 327 ? 5.61033   -2.55049  55.14052  1.000 22.22013 ? 327  PHE   A CE2 1 
ATOM   2446 C  CZ  . PHE   A 1 327 ? 6.32279   -1.37163  55.37536  1.000 22.93289 ? 327  PHE   A CZ  1 
ATOM   2447 N  N   . ASP   A 1 328 ? 7.56010   -3.92663  60.94965  1.000 24.04261 ? 328  ASP   A N   1 
ATOM   2448 C  CA  . ASP   A 1 328 ? 8.30719   -3.02508  61.81210  1.000 23.36741 ? 328  ASP   A CA  1 
ATOM   2449 C  C   . ASP   A 1 328 ? 9.63820   -2.66194  61.16226  1.000 22.26648 ? 328  ASP   A C   1 
ATOM   2450 O  O   . ASP   A 1 328 ? 9.94759   -3.06407  60.03688  1.000 20.31569 ? 328  ASP   A O   1 
ATOM   2451 C  CB  . ASP   A 1 328 ? 8.49209   -3.64248  63.20060  1.000 18.49750 ? 328  ASP   A CB  1 
ATOM   2452 C  CG  . ASP   A 1 328 ? 7.17804   -4.07659  63.79688  1.000 19.98261 ? 328  ASP   A CG  1 
ATOM   2453 O  OD1 . ASP   A 1 328 ? 6.24079   -3.26678  63.78881  1.000 23.61466 ? 328  ASP   A OD1 1 
ATOM   2454 O  OD2 . ASP   A 1 328 ? 7.07171   -5.23277  64.23789  1.000 21.02316 ? 328  ASP   A OD2 1 
ATOM   2455 N  N   . GLY   A 1 329 ? 10.43867  -1.88153  61.89553  1.000 22.65277 ? 329  GLY   A N   1 
ATOM   2456 C  CA  . GLY   A 1 329 ? 11.51749  -1.13919  61.26067  1.000 24.26366 ? 329  GLY   A CA  1 
ATOM   2457 C  C   . GLY   A 1 329 ? 12.76233  -1.94454  60.96438  1.000 24.65946 ? 329  GLY   A C   1 
ATOM   2458 O  O   . GLY   A 1 329 ? 13.51822  -1.59408  60.05754  1.000 19.81391 ? 329  GLY   A O   1 
ATOM   2459 N  N   . ILE   A 1 330 ? 13.00578  -3.01677  61.71524  1.000 18.91189 ? 330  ILE   A N   1 
ATOM   2460 C  CA  . ILE   A 1 330 ? 14.19898  -3.82755  61.48473  1.000 19.26926 ? 330  ILE   A CA  1 
ATOM   2461 C  C   . ILE   A 1 330 ? 14.12038  -4.49151  60.11456  1.000 22.71636 ? 330  ILE   A C   1 
ATOM   2462 O  O   . ILE   A 1 330 ? 15.09476  -4.51107  59.35467  1.000 20.72161 ? 330  ILE   A O   1 
ATOM   2463 C  CB  . ILE   A 1 330 ? 14.35954  -4.88811  62.59148  1.000 21.41115 ? 330  ILE   A CB  1 
ATOM   2464 C  CG1 . ILE   A 1 330 ? 14.48382  -4.23989  64.00133  1.000 27.08256 ? 330  ILE   A CG1 1 
ATOM   2465 C  CG2 . ILE   A 1 330 ? 15.50088  -5.84329  62.26342  1.000 26.32701 ? 330  ILE   A CG2 1 
ATOM   2466 C  CD1 . ILE   A 1 330 ? 15.50531  -3.13158  64.08774  1.000 34.20903 ? 330  ILE   A CD1 1 
ATOM   2467 N  N   . VAL   A 1 331 ? 12.97105  -5.08916  59.80522  1.000 18.40932 ? 331  VAL   A N   1 
ATOM   2468 C  CA  . VAL   A 1 331 ? 12.78262  -5.72917  58.50173  1.000 20.39816 ? 331  VAL   A CA  1 
ATOM   2469 C  C   . VAL   A 1 331 ? 12.82257  -4.68629  57.38658  1.000 21.77290 ? 331  VAL   A C   1 
ATOM   2470 O  O   . VAL   A 1 331 ? 13.41918  -4.90291  56.32068  1.000 25.85672 ? 331  VAL   A O   1 
ATOM   2471 C  CB  . VAL   A 1 331 ? 11.46011  -6.51075  58.48952  1.000 26.96658 ? 331  VAL   A CB  1 
ATOM   2472 C  CG1 . VAL   A 1 331 ? 10.99482  -6.74664  57.04548  1.000 25.26374 ? 331  VAL   A CG1 1 
ATOM   2473 C  CG2 . VAL   A 1 331 ? 11.63340  -7.85365  59.21208  1.000 27.24951 ? 331  VAL   A CG2 1 
ATOM   2474 N  N   . LEU   A 1 332 ? 12.20114  -3.53211  57.62355  1.000 17.50312 ? 332  LEU   A N   1 
ATOM   2475 C  CA  . LEU   A 1 332 ? 12.18873  -2.48962  56.60973  1.000 20.97294 ? 332  LEU   A CA  1 
ATOM   2476 C  C   . LEU   A 1 332 ? 13.60238  -2.03199  56.29721  1.000 24.87098 ? 332  LEU   A C   1 
ATOM   2477 O  O   . LEU   A 1 332 ? 13.96169  -1.87685  55.13140  1.000 26.15049 ? 332  LEU   A O   1 
ATOM   2478 C  CB  . LEU   A 1 332 ? 11.29412  -1.32438  57.06835  1.000 16.34987 ? 332  LEU   A CB  1 
ATOM   2479 C  CG  . LEU   A 1 332 ? 11.10464  -0.09790  56.17804  1.000 22.03696 ? 332  LEU   A CG  1 
ATOM   2480 C  CD1 . LEU   A 1 332 ? 12.31587  0.83101   56.25812  1.000 26.23531 ? 332  LEU   A CD1 1 
ATOM   2481 C  CD2 . LEU   A 1 332 ? 10.85212  -0.51245  54.74833  1.000 24.33185 ? 332  LEU   A CD2 1 
ATOM   2482 N  N   . VAL   A 1 333 ? 14.43656  -1.85415  57.32495  1.000 21.04768 ? 333  VAL   A N   1 
ATOM   2483 C  CA  . VAL   A 1 333 ? 15.80514  -1.40753  57.09664  1.000 20.43438 ? 333  VAL   A CA  1 
ATOM   2484 C  C   . VAL   A 1 333 ? 16.63507  -2.49263  56.40115  1.000 23.53654 ? 333  VAL   A C   1 
ATOM   2485 O  O   . VAL   A 1 333 ? 17.49839  -2.18570  55.57259  1.000 23.55124 ? 333  VAL   A O   1 
ATOM   2486 C  CB  . VAL   A 1 333 ? 16.42440  -0.95854  58.43621  1.000 22.38323 ? 333  VAL   A CB  1 
ATOM   2487 C  CG1 . VAL   A 1 333 ? 17.95350  -1.03826  58.38479  1.000 28.85146 ? 333  VAL   A CG1 1 
ATOM   2488 C  CG2 . VAL   A 1 333 ? 15.94167  0.46167   58.76585  1.000 27.97055 ? 333  VAL   A CG2 1 
ATOM   2489 N  N   . GLN   A 1 334 ? 16.41035  -3.77030  56.72585  1.000 22.54136 ? 334  GLN   A N   1 
ATOM   2490 C  CA  . GLN   A 1 334 ? 17.05717  -4.83520  55.95556  1.000 25.97646 ? 334  GLN   A CA  1 
ATOM   2491 C  C   . GLN   A 1 334 ? 16.74776  -4.69520  54.47258  1.000 27.24360 ? 334  GLN   A C   1 
ATOM   2492 O  O   . GLN   A 1 334 ? 17.63324  -4.80827  53.62277  1.000 24.26785 ? 334  GLN   A O   1 
ATOM   2493 C  CB  . GLN   A 1 334 ? 16.59305  -6.21210  56.42860  1.000 30.23856 ? 334  GLN   A CB  1 
ATOM   2494 C  CG  . GLN   A 1 334 ? 17.09161  -6.62081  57.77767  1.000 31.52437 ? 334  GLN   A CG  1 
ATOM   2495 C  CD  . GLN   A 1 334 ? 18.57911  -6.76409  57.80163  1.000 51.01631 ? 334  GLN   A CD  1 
ATOM   2496 O  OE1 . GLN   A 1 334 ? 19.13494  -7.69101  57.21243  1.000 48.54593 ? 334  GLN   A OE1 1 
ATOM   2497 N  NE2 . GLN   A 1 334 ? 19.24563  -5.83993  58.48060  1.000 44.10805 ? 334  GLN   A NE2 1 
ATOM   2498 N  N   . CYS   A 1 335 ? 15.47312  -4.51331  54.15037  1.000 24.20666 ? 335  CYS   A N   1 
ATOM   2499 C  CA  . CYS   A 1 335 ? 15.05512  -4.29233  52.77046  1.000 27.85785 ? 335  CYS   A CA  1 
ATOM   2500 C  C   . CYS   A 1 335 ? 15.74569  -3.07738  52.16423  1.000 23.37507 ? 335  CYS   A C   1 
ATOM   2501 O  O   . CYS   A 1 335 ? 16.34380  -3.17067  51.08999  1.000 26.61475 ? 335  CYS   A O   1 
ATOM   2502 C  CB  . CYS   A 1 335 ? 13.53462  -4.11795  52.71839  1.000 25.40214 ? 335  CYS   A CB  1 
ATOM   2503 S  SG  . CYS   A 1 335 ? 12.92862  -3.66618  51.03624  1.000 31.85696 ? 335  CYS   A SG  1 
ATOM   2504 N  N   . THR   A 1 336 ? 15.67402  -1.92023  52.83219  1.000 24.97281 ? 336  THR   A N   1 
ATOM   2505 C  CA  . THR   A 1 336 ? 16.18999  -0.70541  52.19366  1.000 24.12683 ? 336  THR   A CA  1 
ATOM   2506 C  C   . THR   A 1 336 ? 17.70433  -0.73370  52.05322  1.000 28.30296 ? 336  THR   A C   1 
ATOM   2507 O  O   . THR   A 1 336 ? 18.24924  -0.21997  51.06937  1.000 30.64879 ? 336  THR   A O   1 
ATOM   2508 C  CB  . THR   A 1 336 ? 15.77073  0.54871   52.95324  1.000 23.89361 ? 336  THR   A CB  1 
ATOM   2509 O  OG1 . THR   A 1 336 ? 16.26404  0.50933   54.29288  1.000 34.11408 ? 336  THR   A OG1 1 
ATOM   2510 C  CG2 . THR   A 1 336 ? 14.25732  0.68110   52.96308  1.000 36.92904 ? 336  THR   A CG2 1 
ATOM   2511 N  N   . GLU   A 1 337 ? 18.41354  -1.30880  53.02125  1.000 28.55002 ? 337  GLU   A N   1 
ATOM   2512 C  CA  . GLU   A 1 337 ? 19.86194  -1.40004  52.84852  1.000 27.61800 ? 337  GLU   A CA  1 
ATOM   2513 C  C   . GLU   A 1 337 ? 20.22173  -2.33430  51.70282  1.000 29.19239 ? 337  GLU   A C   1 
ATOM   2514 O  O   . GLU   A 1 337 ? 21.20058  -2.09893  50.98130  1.000 29.94334 ? 337  GLU   A O   1 
ATOM   2515 C  CB  . GLU   A 1 337 ? 20.51355  -1.83784  54.15967  1.000 29.52965 ? 337  GLU   A CB  1 
ATOM   2516 C  CG  . GLU   A 1 337 ? 20.33889  -0.74997  55.19196  1.000 35.55370 ? 337  GLU   A CG  1 
ATOM   2517 C  CD  . GLU   A 1 337 ? 21.23058  -0.90155  56.38698  1.000 56.76376 ? 337  GLU   A CD  1 
ATOM   2518 O  OE1 . GLU   A 1 337 ? 21.28182  -2.01586  56.96505  1.000 53.27143 ? 337  GLU   A OE1 1 
ATOM   2519 O  OE2 . GLU   A 1 337 ? 21.87606  0.11351   56.73423  1.000 42.99285 ? 337  GLU   A OE2 1 
ATOM   2520 N  N   . HIS   A 1 338 ? 19.45528  -3.40658  51.51541  1.000 32.64640 ? 338  HIS   A N   1 
ATOM   2521 C  CA  . HIS   A 1 338 ? 19.72150  -4.29252  50.38295  1.000 29.47240 ? 338  HIS   A CA  1 
ATOM   2522 C  C   . HIS   A 1 338 ? 19.48381  -3.56890  49.06241  1.000 30.99831 ? 338  HIS   A C   1 
ATOM   2523 O  O   . HIS   A 1 338 ? 20.28879  -3.66341  48.13250  1.000 34.30964 ? 338  HIS   A O   1 
ATOM   2524 C  CB  . HIS   A 1 338 ? 18.83996  -5.53754  50.47954  1.000 28.51922 ? 338  HIS   A CB  1 
ATOM   2525 C  CG  . HIS   A 1 338 ? 19.10924  -6.55466  49.40754  1.000 34.69522 ? 338  HIS   A CG  1 
ATOM   2526 N  ND1 . HIS   A 1 338 ? 18.66187  -6.41064  48.11083  1.000 48.82662 ? 338  HIS   A ND1 1 
ATOM   2527 C  CD2 . HIS   A 1 338 ? 19.75354  -7.74446  49.45105  1.000 43.30670 ? 338  HIS   A CD2 1 
ATOM   2528 C  CE1 . HIS   A 1 338 ? 19.04088  -7.45515  47.39481  1.000 31.67442 ? 338  HIS   A CE1 1 
ATOM   2529 N  NE2 . HIS   A 1 338 ? 19.69997  -8.28297  48.18612  1.000 49.87835 ? 338  HIS   A NE2 1 
ATOM   2530 N  N   . LEU   A 1 339 ? 18.36514  -2.84793  48.96466  1.000 28.86316 ? 339  LEU   A N   1 
ATOM   2531 C  CA  . LEU   A 1 339 ? 18.08958  -2.02258  47.79200  1.000 30.59286 ? 339  LEU   A CA  1 
ATOM   2532 C  C   . LEU   A 1 339 ? 19.24879  -1.08073  47.48254  1.000 29.43114 ? 339  LEU   A C   1 
ATOM   2533 O  O   . LEU   A 1 339 ? 19.75301  -1.04579  46.35870  1.000 33.44401 ? 339  LEU   A O   1 
ATOM   2534 C  CB  . LEU   A 1 339 ? 16.81188  -1.20913  48.02819  1.000 33.75562 ? 339  LEU   A CB  1 
ATOM   2535 C  CG  . LEU   A 1 339 ? 15.48602  -1.96098  48.14594  1.000 36.87892 ? 339  LEU   A CG  1 
ATOM   2536 C  CD1 . LEU   A 1 339 ? 14.34821  -0.95531  48.28014  1.000 30.16013 ? 339  LEU   A CD1 1 
ATOM   2537 C  CD2 . LEU   A 1 339 ? 15.26780  -2.84671  46.94187  1.000 39.62641 ? 339  LEU   A CD2 1 
ATOM   2538 N  N   A LEU   A 1 340 ? 19.67682  -0.29689  48.47336  0.559 31.71128 ? 340  LEU   A N   1 
ATOM   2539 N  N   B LEU   A 1 340 ? 19.69003  -0.30866  48.47648  0.441 31.73577 ? 340  LEU   A N   1 
ATOM   2540 C  CA  A LEU   A 1 340 ? 20.70984  0.70365   48.21863  0.559 32.36705 ? 340  LEU   A CA  1 
ATOM   2541 C  CA  B LEU   A 1 340 ? 20.70855  0.70523   48.21197  0.441 32.39930 ? 340  LEU   A CA  1 
ATOM   2542 C  C   A LEU   A 1 340 ? 22.04666  0.05828   47.89074  0.559 37.07140 ? 340  LEU   A C   1 
ATOM   2543 C  C   B LEU   A 1 340 ? 22.06020  0.07547   47.90933  0.441 37.06281 ? 340  LEU   A C   1 
ATOM   2544 O  O   A LEU   A 1 340 ? 22.76331  0.52009   46.99382  0.559 35.47004 ? 340  LEU   A O   1 
ATOM   2545 O  O   B LEU   A 1 340 ? 22.79973  0.56340   47.04587  0.441 35.50136 ? 340  LEU   A O   1 
ATOM   2546 C  CB  A LEU   A 1 340 ? 20.84565  1.62593   49.42456  0.559 33.92958 ? 340  LEU   A CB  1 
ATOM   2547 C  CB  B LEU   A 1 340 ? 20.81423  1.66104   49.39746  0.441 33.98043 ? 340  LEU   A CB  1 
ATOM   2548 C  CG  A LEU   A 1 340 ? 19.67374  2.58849   49.60726  0.559 37.70989 ? 340  LEU   A CG  1 
ATOM   2549 C  CG  B LEU   A 1 340 ? 19.95462  2.92690   49.31963  0.441 37.64539 ? 340  LEU   A CG  1 
ATOM   2550 C  CD1 A LEU   A 1 340 ? 19.93946  3.45013   50.79363  0.559 41.83574 ? 340  LEU   A CD1 1 
ATOM   2551 C  CD1 B LEU   A 1 340 ? 18.55564  2.62561   48.80508  0.441 31.84400 ? 340  LEU   A CD1 1 
ATOM   2552 C  CD2 A LEU   A 1 340 ? 19.49879  3.43678   48.36017  0.559 34.82249 ? 340  LEU   A CD2 1 
ATOM   2553 C  CD2 B LEU   A 1 340 ? 19.88168  3.54927   50.68226  0.441 41.71847 ? 340  LEU   A CD2 1 
ATOM   2554 N  N   . LYS   A 1 341 ? 22.40217  -1.00828  48.60628  1.000 36.99152 ? 341  LYS   A N   1 
ATOM   2555 C  CA  . LYS   A 1 341 ? 23.67286  -1.66920  48.35217  1.000 36.36076 ? 341  LYS   A CA  1 
ATOM   2556 C  C   . LYS   A 1 341 ? 23.72560  -2.25222  46.95025  1.000 39.88040 ? 341  LYS   A C   1 
ATOM   2557 O  O   . LYS   A 1 341 ? 24.78853  -2.27284  46.31949  1.000 45.87050 ? 341  LYS   A O   1 
ATOM   2558 C  CB  . LYS   A 1 341 ? 23.90552  -2.75721  49.39527  1.000 48.17215 ? 341  LYS   A CB  1 
ATOM   2559 C  CG  . LYS   A 1 341 ? 25.16888  -3.60155  49.16998  1.000 44.56316 ? 341  LYS   A CG  1 
ATOM   2560 C  CD  . LYS   A 1 341 ? 25.42582  -4.47621  50.39505  1.000 61.65507 ? 341  LYS   A CD  1 
ATOM   2561 C  CE  . LYS   A 1 341 ? 26.52117  -5.49786  50.15687  1.000 63.62208 ? 341  LYS   A CE  1 
ATOM   2562 N  NZ  . LYS   A 1 341 ? 26.78019  -6.29145  51.39293  1.000 60.60220 ? 341  LYS   A NZ  1 
ATOM   2563 N  N   . HIS   A 1 342 ? 22.59887  -2.71051  46.43193  1.000 40.33545 ? 342  HIS   A N   1 
ATOM   2564 C  CA  . HIS   A 1 342 ? 22.63751  -3.35520  45.13124  1.000 47.26217 ? 342  HIS   A CA  1 
ATOM   2565 C  C   . HIS   A 1 342 ? 22.37942  -2.38615  43.98751  1.000 44.58279 ? 342  HIS   A C   1 
ATOM   2566 O  O   . HIS   A 1 342 ? 22.52038  -2.77555  42.82742  1.000 45.97472 ? 342  HIS   A O   1 
ATOM   2567 C  CB  . HIS   A 1 342 ? 21.66012  -4.53211  45.11305  1.000 64.87750 ? 342  HIS   A CB  1 
ATOM   2568 C  CG  . HIS   A 1 342 ? 22.11001  -5.68135  45.96685  1.000 71.20486 ? 342  HIS   A CG  1 
ATOM   2569 N  ND1 . HIS   A 1 342 ? 22.26510  -5.57703  47.33459  1.000 61.46417 ? 342  HIS   A ND1 1 
ATOM   2570 C  CD2 . HIS   A 1 342 ? 22.47359  -6.94568  45.64340  1.000 70.22943 ? 342  HIS   A CD2 1 
ATOM   2571 C  CE1 . HIS   A 1 342 ? 22.69056  -6.73122  47.81724  1.000 71.75981 ? 342  HIS   A CE1 1 
ATOM   2572 N  NE2 . HIS   A 1 342 ? 22.82385  -7.57906  46.81205  1.000 86.21903 ? 342  HIS   A NE2 1 
ATOM   2573 N  N   . MET   A 1 343 ? 22.04057  -1.12995  44.29199  1.000 38.09639 ? 343  MET   A N   1 
ATOM   2574 C  CA  . MET   A 1 343 ? 22.14868  -0.07184  43.29286  1.000 53.30613 ? 343  MET   A CA  1 
ATOM   2575 C  C   . MET   A 1 343 ? 23.60863  0.22099   42.97575  1.000 56.93795 ? 343  MET   A C   1 
ATOM   2576 O  O   . MET   A 1 343 ? 23.93867  0.57654   41.83949  1.000 65.76384 ? 343  MET   A O   1 
ATOM   2577 C  CB  . MET   A 1 343 ? 21.44761  1.20154   43.78490  1.000 42.14210 ? 343  MET   A CB  1 
ATOM   2578 C  CG  . MET   A 1 343 ? 19.93576  1.09156   43.86896  1.000 40.62457 ? 343  MET   A CG  1 
ATOM   2579 S  SD  . MET   A 1 343 ? 19.16153  2.56074   44.57159  1.000 44.32624 ? 343  MET   A SD  1 
ATOM   2580 C  CE  . MET   A 1 343 ? 19.62594  3.82067   43.39753  1.000 42.49842 ? 343  MET   A CE  1 
ATOM   2581 N  N   . THR   A 1 344 ? 24.48773  0.07292   43.97411  1.000 70.44503 ? 344  THR   A N   1 
ATOM   2582 C  CA  . THR   A 1 344 ? 25.92091  0.28388   43.78465  1.000 88.29779 ? 344  THR   A CA  1 
ATOM   2583 C  C   . THR   A 1 344 ? 26.52201  -0.71879  42.80299  1.000 78.49657 ? 344  THR   A C   1 
ATOM   2584 O  O   . THR   A 1 344 ? 27.51288  -0.40909  42.13225  1.000 87.44604 ? 344  THR   A O   1 
ATOM   2585 C  CB  . THR   A 1 344 ? 26.64258  0.19869   45.13558  1.000 82.28030 ? 344  THR   A CB  1 
ATOM   2586 O  OG1 . THR   A 1 344 ? 26.64199  -1.15749  45.60229  1.000 78.75806 ? 344  THR   A OG1 1 
ATOM   2587 C  CG2 . THR   A 1 344 ? 25.94278  1.06504   46.17281  1.000 57.12861 ? 344  THR   A CG2 1 
ATOM   2588 N  N   . GLN   A 1 345 ? 25.94734  -1.91311  42.70665  1.000 74.09882 ? 345  GLN   A N   1 
ATOM   2589 C  CA  . GLN   A 1 345 ? 26.43600  -2.92851  41.78561  1.000 71.32856 ? 345  GLN   A CA  1 
ATOM   2590 C  C   . GLN   A 1 345 ? 25.64490  -2.89237  40.47820  1.000 81.41849 ? 345  GLN   A C   1 
ATOM   2591 O  O   . GLN   A 1 345 ? 25.24892  -1.82034  40.00629  1.000 71.16766 ? 345  GLN   A O   1 
ATOM   2592 C  CB  . GLN   A 1 345 ? 26.35334  -4.31762  42.42782  1.000 62.67423 ? 345  GLN   A CB  1 
ATOM   2593 N  N   . LEU   A 1 356 ? 7.22611   -1.04863  23.58685  1.000 50.82252 ? 359  LEU   A N   1 
ATOM   2594 C  CA  . LEU   A 1 356 ? 7.17461   -0.37277  24.89204  1.000 58.19158 ? 359  LEU   A CA  1 
ATOM   2595 C  C   . LEU   A 1 356 ? 6.02542   0.65247   24.99380  1.000 60.44248 ? 359  LEU   A C   1 
ATOM   2596 O  O   . LEU   A 1 356 ? 6.16697   1.81008   24.59627  1.000 56.35191 ? 359  LEU   A O   1 
ATOM   2597 C  CB  . LEU   A 1 356 ? 8.51539   0.30816   25.17407  1.000 67.84083 ? 359  LEU   A CB  1 
ATOM   2598 C  CG  . LEU   A 1 356 ? 8.98982   0.37771   26.62395  1.000 66.00916 ? 359  LEU   A CG  1 
ATOM   2599 C  CD1 . LEU   A 1 356 ? 8.90037   -0.99048  27.27966  1.000 69.63955 ? 359  LEU   A CD1 1 
ATOM   2600 C  CD2 . LEU   A 1 356 ? 10.41373  0.90502   26.69678  1.000 65.48249 ? 359  LEU   A CD2 1 
ATOM   2601 N  N   . PRO   A 1 357 ? 4.88991   0.22757   25.54043  1.000 63.66989 ? 360  PRO   A N   1 
ATOM   2602 C  CA  . PRO   A 1 357 ? 3.71833   1.10749   25.58784  1.000 49.01411 ? 360  PRO   A CA  1 
ATOM   2603 C  C   . PRO   A 1 357 ? 3.88600   2.18360   26.64861  1.000 56.44728 ? 360  PRO   A C   1 
ATOM   2604 O  O   . PRO   A 1 357 ? 4.71290   2.08064   27.55425  1.000 47.94079 ? 360  PRO   A O   1 
ATOM   2605 C  CB  . PRO   A 1 357 ? 2.56639   0.15706   25.94284  1.000 74.54642 ? 360  PRO   A CB  1 
ATOM   2606 C  CG  . PRO   A 1 357 ? 3.20438   -1.21633  26.18003  1.000 74.18114 ? 360  PRO   A CG  1 
ATOM   2607 C  CD  . PRO   A 1 357 ? 4.67676   -1.00307  26.31526  1.000 72.13480 ? 360  PRO   A CD  1 
ATOM   2608 N  N   . ALA   A 1 358 ? 3.08179   3.22714   26.52473  1.000 47.99367 ? 361  ALA   A N   1 
ATOM   2609 C  CA  . ALA   A 1 358 ? 3.24125   4.36265   27.41367  1.000 46.19389 ? 361  ALA   A CA  1 
ATOM   2610 C  C   . ALA   A 1 358 ? 2.58333   4.08156   28.76207  1.000 44.42529 ? 361  ALA   A C   1 
ATOM   2611 O  O   . ALA   A 1 358 ? 1.55907   3.39765   28.83662  1.000 42.90700 ? 361  ALA   A O   1 
ATOM   2612 C  CB  . ALA   A 1 358 ? 2.63191   5.61558   26.79470  1.000 47.66468 ? 361  ALA   A CB  1 
ATOM   2613 N  N   . PRO   A 1 359 ? 3.15217   4.58816   29.84610  1.000 44.45760 ? 362  PRO   A N   1 
ATOM   2614 C  CA  . PRO   A 1 359 ? 2.47481   4.45712   31.13916  1.000 36.46845 ? 362  PRO   A CA  1 
ATOM   2615 C  C   . PRO   A 1 359 ? 1.12972   5.16991   31.11029  1.000 45.03943 ? 362  PRO   A C   1 
ATOM   2616 O  O   . PRO   A 1 359 ? 0.95780   6.18496   30.43716  1.000 43.19759 ? 362  PRO   A O   1 
ATOM   2617 C  CB  . PRO   A 1 359 ? 3.45155   5.11577   32.12780  1.000 40.37788 ? 362  PRO   A CB  1 
ATOM   2618 C  CG  . PRO   A 1 359 ? 4.80560   5.03986   31.44275  1.000 40.70306 ? 362  PRO   A CG  1 
ATOM   2619 C  CD  . PRO   A 1 359 ? 4.48882   5.19813   29.96044  1.000 43.81496 ? 362  PRO   A CD  1 
ATOM   2620 N  N   . ARG   A 1 360 ? 0.16609   4.63068   31.85192  1.000 37.54169 ? 363  ARG   A N   1 
ATOM   2621 C  CA  . ARG   A 1 360 ? -1.20827  5.12080   31.81314  1.000 42.32353 ? 363  ARG   A CA  1 
ATOM   2622 C  C   . ARG   A 1 360 ? -1.46768  6.03028   33.00406  1.000 45.85917 ? 363  ARG   A C   1 
ATOM   2623 O  O   . ARG   A 1 360 ? -1.28775  5.61637   34.15416  1.000 42.02268 ? 363  ARG   A O   1 
ATOM   2624 C  CB  . ARG   A 1 360 ? -2.20304  3.96204   31.82496  1.000 44.39664 ? 363  ARG   A CB  1 
ATOM   2625 C  CG  . ARG   A 1 360 ? -2.10612  3.03915   30.63216  1.000 55.49860 ? 363  ARG   A CG  1 
ATOM   2626 C  CD  . ARG   A 1 360 ? -2.75363  1.72234   30.96325  1.000 60.86220 ? 363  ARG   A CD  1 
ATOM   2627 N  NE  . ARG   A 1 360 ? -1.82081  0.82342   31.63073  1.000 58.39157 ? 363  ARG   A NE  1 
ATOM   2628 C  CZ  . ARG   A 1 360 ? -2.17339  -0.10312  32.50927  1.000 51.43911 ? 363  ARG   A CZ  1 
ATOM   2629 N  NH1 . ARG   A 1 360 ? -3.41512  -0.18965  32.96064  1.000 78.90735 ? 363  ARG   A NH1 1 
ATOM   2630 N  NH2 . ARG   A 1 360 ? -1.26123  -0.97351  32.93668  1.000 61.03597 ? 363  ARG   A NH2 1 
ATOM   2631 N  N   . ARG   A 1 361 ? -1.90610  7.25543   32.72957  1.000 35.90736 ? 364  ARG   A N   1 
ATOM   2632 C  CA  . ARG   A 1 361 ? -2.37244  8.13075   33.79701  1.000 45.14052 ? 364  ARG   A CA  1 
ATOM   2633 C  C   . ARG   A 1 361 ? -3.64430  7.55106   34.40142  1.000 38.04186 ? 364  ARG   A C   1 
ATOM   2634 O  O   . ARG   A 1 361 ? -4.55656  7.14017   33.67422  1.000 36.50626 ? 364  ARG   A O   1 
ATOM   2635 C  CB  . ARG   A 1 361 ? -2.64019  9.53931   33.26256  1.000 42.93787 ? 364  ARG   A CB  1 
ATOM   2636 C  CG  . ARG   A 1 361 ? -2.80761  10.58629  34.37469  1.000 43.33517 ? 364  ARG   A CG  1 
ATOM   2637 C  CD  . ARG   A 1 361 ? -3.39237  11.88257  33.85128  1.000 43.72869 ? 364  ARG   A CD  1 
ATOM   2638 N  NE  . ARG   A 1 361 ? -2.55960  12.48413  32.81743  1.000 43.09006 ? 364  ARG   A NE  1 
ATOM   2639 C  CZ  . ARG   A 1 361 ? -1.74540  13.51546  33.00643  1.000 46.34010 ? 364  ARG   A CZ  1 
ATOM   2640 N  NH1 . ARG   A 1 361 ? -1.64847  14.11701  34.18381  1.000 37.97312 ? 364  ARG   A NH1 1 
ATOM   2641 N  NH2 . ARG   A 1 361 ? -0.99531  13.94245  31.99428  1.000 40.09404 ? 364  ARG   A NH2 1 
ATOM   2642 N  N   . LEU   A 1 362 ? -3.70065  7.49145   35.72802  1.000 33.07608 ? 365  LEU   A N   1 
ATOM   2643 C  CA  . LEU   A 1 362 ? -4.94641  7.13642   36.39437  1.000 36.95660 ? 365  LEU   A CA  1 
ATOM   2644 C  C   . LEU   A 1 362 ? -5.90526  8.31140   36.30919  1.000 44.30325 ? 365  LEU   A C   1 
ATOM   2645 O  O   . LEU   A 1 362 ? -5.57278  9.42989   36.71651  1.000 41.30477 ? 365  LEU   A O   1 
ATOM   2646 C  CB  . LEU   A 1 362 ? -4.69942  6.76337   37.84916  1.000 32.56248 ? 365  LEU   A CB  1 
ATOM   2647 C  CG  . LEU   A 1 362 ? -3.90623  5.47170   38.05184  1.000 36.26725 ? 365  LEU   A CG  1 
ATOM   2648 C  CD1 . LEU   A 1 362 ? -3.68401  5.20253   39.53099  1.000 41.01241 ? 365  LEU   A CD1 1 
ATOM   2649 C  CD2 . LEU   A 1 362 ? -4.65601  4.30456   37.39364  1.000 44.52596 ? 365  LEU   A CD2 1 
ATOM   2650 N  N   . ARG   A 1 363 ? -7.09012  8.06286   35.79085  1.000 36.29908 ? 366  ARG   A N   1 
ATOM   2651 C  CA  . ARG   A 1 363 ? -8.05892  9.13316   35.65047  1.000 45.28885 ? 366  ARG   A CA  1 
ATOM   2652 C  C   . ARG   A 1 363 ? -8.98550  9.17856   36.86098  1.000 39.99889 ? 366  ARG   A C   1 
ATOM   2653 O  O   . ARG   A 1 363 ? -9.16598  8.19018   37.57706  1.000 41.24018 ? 366  ARG   A O   1 
ATOM   2654 C  CB  . ARG   A 1 363 ? -8.84047  8.95889   34.34901  1.000 41.29359 ? 366  ARG   A CB  1 
ATOM   2655 C  CG  . ARG   A 1 363 ? -8.08358  9.54585   33.15350  1.000 66.63503 ? 366  ARG   A CG  1 
ATOM   2656 C  CD  . ARG   A 1 363 ? -8.34910  8.79401   31.85876  1.000 76.97563 ? 366  ARG   A CD  1 
ATOM   2657 N  NE  . ARG   A 1 363 ? -9.55154  7.97459   31.94162  1.000 91.44880 ? 366  ARG   A NE  1 
ATOM   2658 C  CZ  . ARG   A 1 363 ? -9.58492  6.66456   31.73578  1.000 85.22053 ? 366  ARG   A CZ  1 
ATOM   2659 N  NH1 . ARG   A 1 363 ? -8.50066  5.99133   31.38123  1.000 86.72313 ? 366  ARG   A NH1 1 
ATOM   2660 N  NH2 . ARG   A 1 363 ? -10.73865 6.01589   31.87507  1.000 76.67740 ? 366  ARG   A NH2 1 
ATOM   2661 N  N   . TRP   A 1 364 ? -9.55509  10.35592  37.10047  1.000 42.08234 ? 367  TRP   A N   1 
ATOM   2662 C  CA  . TRP   A 1 364 ? -10.47265 10.55929  38.21063  1.000 37.21128 ? 367  TRP   A CA  1 
ATOM   2663 C  C   . TRP   A 1 364 ? -11.69248 11.32505  37.73604  1.000 54.16268 ? 367  TRP   A C   1 
ATOM   2664 O  O   . TRP   A 1 364 ? -11.58944 12.19766  36.87568  1.000 41.41003 ? 367  TRP   A O   1 
ATOM   2665 C  CB  . TRP   A 1 364 ? -9.82929  11.34913  39.35679  1.000 39.05892 ? 367  TRP   A CB  1 
ATOM   2666 C  CG  . TRP   A 1 364 ? -8.57175  10.75253  39.88431  1.000 42.36526 ? 367  TRP   A CG  1 
ATOM   2667 C  CD1 . TRP   A 1 364 ? -7.30000  11.17467  39.64046  1.000 40.75816 ? 367  TRP   A CD1 1 
ATOM   2668 C  CD2 . TRP   A 1 364 ? -8.46508  9.63154   40.76157  1.000 42.95564 ? 367  TRP   A CD2 1 
ATOM   2669 N  NE1 . TRP   A 1 364 ? -6.40323  10.38123  40.31578  1.000 41.58434 ? 367  TRP   A NE1 1 
ATOM   2670 C  CE2 . TRP   A 1 364 ? -7.09300  9.42489   41.01027  1.000 38.02499 ? 367  TRP   A CE2 1 
ATOM   2671 C  CE3 . TRP   A 1 364 ? -9.39575  8.77911   41.35775  1.000 33.22285 ? 367  TRP   A CE3 1 
ATOM   2672 C  CZ2 . TRP   A 1 364 ? -6.62630  8.40595   41.83900  1.000 36.57711 ? 367  TRP   A CZ2 1 
ATOM   2673 C  CZ3 . TRP   A 1 364 ? -8.93078  7.77003   42.18727  1.000 38.72042 ? 367  TRP   A CZ3 1 
ATOM   2674 C  CH2 . TRP   A 1 364 ? -7.55723  7.58763   42.41548  1.000 36.09178 ? 367  TRP   A CH2 1 
ATOM   2675 N  N   . LYS   A 1 365 ? -12.84298 11.00592  38.32702  1.000 41.91325 ? 368  LYS   A N   1 
ATOM   2676 C  CA  . LYS   A 1 365 ? -14.09148 11.73354  38.10005  1.000 48.42044 ? 368  LYS   A CA  1 
ATOM   2677 C  C   . LYS   A 1 365 ? -14.49216 12.38356  39.42261  1.000 57.73933 ? 368  LYS   A C   1 
ATOM   2678 O  O   . LYS   A 1 365 ? -14.98077 11.70898  40.33534  1.000 56.63988 ? 368  LYS   A O   1 
ATOM   2679 C  CB  . LYS   A 1 365 ? -15.17466 10.80701  37.56533  1.000 48.19289 ? 368  LYS   A CB  1 
ATOM   2680 C  CG  . LYS   A 1 365 ? -14.85385 10.23615  36.17582  1.000 66.35282 ? 368  LYS   A CG  1 
ATOM   2681 C  CD  . LYS   A 1 365 ? -14.15045 11.28894  35.31767  1.000 68.84850 ? 368  LYS   A CD  1 
ATOM   2682 C  CE  . LYS   A 1 365 ? -14.15006 10.96537  33.83339  1.000 68.75662 ? 368  LYS   A CE  1 
ATOM   2683 N  NZ  . LYS   A 1 365 ? -14.10511 12.23580  33.04185  1.000 70.10001 ? 368  LYS   A NZ  1 
ATOM   2684 N  N   . CYS   A 1 366 ? -14.26563 13.68891  39.52790  1.000 47.70724 ? 369  CYS   A N   1 
ATOM   2685 C  CA  . CYS   A 1 366 ? -14.54394 14.44760  40.73621  1.000 63.72550 ? 369  CYS   A CA  1 
ATOM   2686 C  C   . CYS   A 1 366 ? -15.88882 15.15386  40.64309  1.000 60.99704 ? 369  CYS   A C   1 
ATOM   2687 O  O   . CYS   A 1 366 ? -16.49235 15.26443  39.57674  1.000 56.93247 ? 369  CYS   A O   1 
ATOM   2688 C  CB  . CYS   A 1 366 ? -13.43985 15.47157  40.99179  1.000 69.79275 ? 369  CYS   A CB  1 
ATOM   2689 S  SG  . CYS   A 1 366 ? -11.81615 14.71636  41.07357  1.000 70.93435 ? 369  CYS   A SG  1 
ATOM   2690 N  N   . SER   A 1 367 ? -16.35402 15.62027  41.78931  1.000 61.95440 ? 370  SER   A N   1 
ATOM   2691 C  CA  . SER   A 1 367 ? -17.62178 16.31625  41.93665  1.000 63.73894 ? 370  SER   A CA  1 
ATOM   2692 C  C   . SER   A 1 367 ? -17.38170 17.53870  42.80025  1.000 72.08632 ? 370  SER   A C   1 
ATOM   2693 O  O   . SER   A 1 367 ? -16.28162 17.73111  43.33094  1.000 59.17294 ? 370  SER   A O   1 
ATOM   2694 C  CB  . SER   A 1 367 ? -18.68843 15.39034  42.55749  1.000 68.72203 ? 370  SER   A CB  1 
ATOM   2695 O  OG  . SER   A 1 367 ? -18.31014 14.87101  43.82447  1.000 65.21992 ? 370  SER   A OG  1 
ATOM   2696 N  N   . PRO   A 1 368 ? -18.37457 18.42501  42.91887  1.000 70.20875 ? 371  PRO   A N   1 
ATOM   2697 C  CA  . PRO   A 1 368 ? -18.24577 19.51230  43.89836  1.000 59.79734 ? 371  PRO   A CA  1 
ATOM   2698 C  C   . PRO   A 1 368 ? -18.01060 19.00803  45.30481  1.000 44.89437 ? 371  PRO   A C   1 
ATOM   2699 O  O   . PRO   A 1 368 ? -17.32757 19.68584  46.08737  1.000 60.60445 ? 371  PRO   A O   1 
ATOM   2700 C  CB  . PRO   A 1 368 ? -19.58429 20.25230  43.77678  1.000 64.21342 ? 371  PRO   A CB  1 
ATOM   2701 C  CG  . PRO   A 1 368 ? -20.02034 19.99127  42.38213  1.000 64.53584 ? 371  PRO   A CG  1 
ATOM   2702 C  CD  . PRO   A 1 368 ? -19.55345 18.60527  42.05027  1.000 61.75668 ? 371  PRO   A CD  1 
ATOM   2703 N  N   . GLU   A 1 369 ? -18.55324 17.83570  45.65523  1.000 51.34612 ? 372  GLU   A N   1 
ATOM   2704 C  CA  . GLU   A 1 369 ? -18.23148 17.22709  46.94335  1.000 46.61427 ? 372  GLU   A CA  1 
ATOM   2705 C  C   . GLU   A 1 369 ? -16.72845 17.03385  47.09198  1.000 44.54235 ? 372  GLU   A C   1 
ATOM   2706 O  O   . GLU   A 1 369 ? -16.15259 17.31915  48.15038  1.000 48.35276 ? 372  GLU   A O   1 
ATOM   2707 C  CB  . GLU   A 1 369 ? -18.91940 15.87185  47.09376  1.000 54.89119 ? 372  GLU   A CB  1 
ATOM   2708 C  CG  . GLU   A 1 369 ? -20.40760 15.84314  47.32590  1.000 72.69193 ? 372  GLU   A CG  1 
ATOM   2709 C  CD  . GLU   A 1 369 ? -20.90834 14.40179  47.37311  1.000 79.55855 ? 372  GLU   A CD  1 
ATOM   2710 O  OE1 . GLU   A 1 369 ? -21.07776 13.78996  46.28908  1.000 62.10475 ? 372  GLU   A OE1 1 
ATOM   2711 O  OE2 . GLU   A 1 369 ? -21.08004 13.86469  48.49228  1.000 55.00639 ? 372  GLU   A OE2 1 
ATOM   2712 N  N   . ILE   A 1 370 ? -16.07906 16.51797  46.04492  1.000 46.44993 ? 373  ILE   A N   1 
ATOM   2713 C  CA  . ILE   A 1 370 ? -14.67444 16.13482  46.16369  1.000 42.21568 ? 373  ILE   A CA  1 
ATOM   2714 C  C   . ILE   A 1 370 ? -13.79417 17.36767  46.30788  1.000 42.65362 ? 373  ILE   A C   1 
ATOM   2715 O  O   . ILE   A 1 370 ? -12.80272 17.35882  47.04918  1.000 34.69347 ? 373  ILE   A O   1 
ATOM   2716 C  CB  . ILE   A 1 370 ? -14.25344 15.26560  44.96398  1.000 50.10426 ? 373  ILE   A CB  1 
ATOM   2717 C  CG1 . ILE   A 1 370 ? -14.94029 13.89228  45.03386  1.000 45.68821 ? 373  ILE   A CG1 1 
ATOM   2718 C  CG2 . ILE   A 1 370 ? -12.72365 15.10928  44.91259  1.000 41.19577 ? 373  ILE   A CG2 1 
ATOM   2719 C  CD1 . ILE   A 1 370 ? -14.64209 13.09613  46.30730  1.000 40.84197 ? 373  ILE   A CD1 1 
ATOM   2720 N  N   . GLN   A 1 371 ? -14.14551 18.45051  45.61461  1.000 39.61689 ? 374  GLN   A N   1 
ATOM   2721 C  CA  . GLN   A 1 371 ? -13.39032 19.69069  45.75538  1.000 46.10198 ? 374  GLN   A CA  1 
ATOM   2722 C  C   . GLN   A 1 371 ? -13.41383 20.18596  47.19386  1.000 38.58584 ? 374  GLN   A C   1 
ATOM   2723 O  O   . GLN   A 1 371 ? -12.39000 20.65063  47.71420  1.000 38.67485 ? 374  GLN   A O   1 
ATOM   2724 C  CB  . GLN   A 1 371 ? -13.94585 20.75309  44.79666  1.000 47.69482 ? 374  GLN   A CB  1 
ATOM   2725 C  CG  . GLN   A 1 371 ? -12.86083 21.45609  43.98933  1.000 57.81615 ? 374  GLN   A CG  1 
ATOM   2726 C  CD  . GLN   A 1 371 ? -11.86394 20.48342  43.35755  1.000 59.93631 ? 374  GLN   A CD  1 
ATOM   2727 O  OE1 . GLN   A 1 371 ? -12.24595 19.44909  42.80038  1.000 69.63254 ? 374  GLN   A OE1 1 
ATOM   2728 N  NE2 . GLN   A 1 371 ? -10.57933 20.81445  43.44669  1.000 63.96833 ? 374  GLN   A NE2 1 
ATOM   2729 N  N   . GLY   A 1 372 ? -14.56576 20.06860  47.86620  1.000 40.19864 ? 375  GLY   A N   1 
ATOM   2730 C  CA  . GLY   A 1 372 ? -14.62999 20.44588  49.27332  1.000 39.06170 ? 375  GLY   A CA  1 
ATOM   2731 C  C   . GLY   A 1 372 ? -13.77561 19.55443  50.16083  1.000 38.38142 ? 375  GLY   A C   1 
ATOM   2732 O  O   . GLY   A 1 372 ? -13.14266 20.02626  51.11694  1.000 33.60835 ? 375  GLY   A O   1 
ATOM   2733 N  N   . HIS   A 1 373 ? -13.75994 18.25283  49.87237  1.000 34.78894 ? 376  HIS   A N   1 
ATOM   2734 C  CA  . HIS   A 1 373 ? -12.91312 17.33927  50.63061  1.000 32.29387 ? 376  HIS   A CA  1 
ATOM   2735 C  C   . HIS   A 1 373 ? -11.43978 17.64393  50.41356  1.000 31.41333 ? 376  HIS   A C   1 
ATOM   2736 O  O   . HIS   A 1 373 ? -10.62921 17.51128  51.33646  1.000 31.06681 ? 376  HIS   A O   1 
ATOM   2737 C  CB  . HIS   A 1 373 ? -13.21117 15.89422  50.24168  1.000 36.35826 ? 376  HIS   A CB  1 
ATOM   2738 C  CG  . HIS   A 1 373 ? -14.44402 15.34119  50.87935  1.000 38.99910 ? 376  HIS   A CG  1 
ATOM   2739 N  ND1 . HIS   A 1 373 ? -15.59448 15.08339  50.17251  1.000 42.05961 ? 376  HIS   A ND1 1 
ATOM   2740 C  CD2 . HIS   A 1 373 ? -14.70512 14.99368  52.16129  1.000 40.94799 ? 376  HIS   A CD2 1 
ATOM   2741 C  CE1 . HIS   A 1 373 ? -16.51536 14.60419  50.98942  1.000 41.24239 ? 376  HIS   A CE1 1 
ATOM   2742 N  NE2 . HIS   A 1 373 ? -16.00280 14.54409  52.20341  1.000 47.95160 ? 376  HIS   A NE2 1 
ATOM   2743 N  N   . LEU   A 1 374 ? -11.07351 18.03064  49.19123  1.000 33.39854 ? 377  LEU   A N   1 
ATOM   2744 C  CA  . LEU   A 1 374 ? -9.67871  18.34062  48.88964  1.000 30.53489 ? 377  LEU   A CA  1 
ATOM   2745 C  C   . LEU   A 1 374 ? -9.22047  19.58115  49.64461  1.000 35.61441 ? 377  LEU   A C   1 
ATOM   2746 O  O   . LEU   A 1 374 ? -8.14833  19.57655  50.25463  1.000 33.26521 ? 377  LEU   A O   1 
ATOM   2747 C  CB  . LEU   A 1 374 ? -9.50427  18.52876  47.38261  1.000 29.93235 ? 377  LEU   A CB  1 
ATOM   2748 C  CG  . LEU   A 1 374 ? -9.49713  17.24428  46.56035  1.000 31.41742 ? 377  LEU   A CG  1 
ATOM   2749 C  CD1 . LEU   A 1 374 ? -9.69727  17.61295  45.08125  1.000 42.93780 ? 377  LEU   A CD1 1 
ATOM   2750 C  CD2 . LEU   A 1 374 ? -8.19819  16.45697  46.76024  1.000 28.86481 ? 377  LEU   A CD2 1 
ATOM   2751 N  N   . ALA   A 1 375 ? -10.02975 20.65612  49.62269  1.000 31.60191 ? 378  ALA   A N   1 
ATOM   2752 C  CA  . ALA   A 1 375 ? -9.67935  21.86822  50.36467  1.000 33.54078 ? 378  ALA   A CA  1 
ATOM   2753 C  C   . ALA   A 1 375 ? -9.55765  21.58965  51.85665  1.000 35.07802 ? 378  ALA   A C   1 
ATOM   2754 O  O   . ALA   A 1 375 ? -8.62553  22.07191  52.52061  1.000 31.00038 ? 378  ALA   A O   1 
ATOM   2755 C  CB  . ALA   A 1 375 ? -10.72167 22.96246  50.10980  1.000 36.47348 ? 378  ALA   A CB  1 
ATOM   2756 N  N   . SER   A 1 376 ? -10.48570 20.80316  52.40526  1.000 31.71012 ? 379  SER   A N   1 
ATOM   2757 C  CA  . SER   A 1 376 ? -10.40088 20.45795  53.82373  1.000 31.33603 ? 379  SER   A CA  1 
ATOM   2758 C  C   . SER   A 1 376 ? -9.15813  19.62446  54.12545  1.000 28.60188 ? 379  SER   A C   1 
ATOM   2759 O  O   . SER   A 1 376 ? -8.51184  19.80956  55.16856  1.000 33.08989 ? 379  SER   A O   1 
ATOM   2760 C  CB  . SER   A 1 376 ? -11.66861 19.72803  54.25712  1.000 35.76505 ? 379  SER   A CB  1 
ATOM   2761 O  OG  . SER   A 1 376 ? -11.55768 19.28525  55.59252  1.000 47.15558 ? 379  SER   A OG  1 
ATOM   2762 N  N   . SER   A 1 377 ? -8.79608  18.69563  53.23871  1.000 29.90523 ? 380  SER   A N   1 
ATOM   2763 C  CA  . SER   A 1 377 ? -7.59812  17.89615  53.50501  1.000 26.88253 ? 380  SER   A CA  1 
ATOM   2764 C  C   . SER   A 1 377 ? -6.33422  18.74305  53.42774  1.000 27.32006 ? 380  SER   A C   1 
ATOM   2765 O  O   . SER   A 1 377 ? -5.38154  18.50915  54.17565  1.000 26.78374 ? 380  SER   A O   1 
ATOM   2766 C  CB  . SER   A 1 377 ? -7.50832  16.72111  52.52677  1.000 27.65908 ? 380  SER   A CB  1 
ATOM   2767 O  OG  . SER   A 1 377 ? -8.57402  15.82059  52.77372  1.000 38.29326 ? 380  SER   A OG  1 
ATOM   2768 N  N   . ALA   A 1 378 ? -6.28778  19.69730  52.49341  1.000 25.09601 ? 381  ALA   A N   1 
ATOM   2769 C  CA  . ALA   A 1 378 ? -5.13472  20.58685  52.39591  1.000 28.05384 ? 381  ALA   A CA  1 
ATOM   2770 C  C   . ALA   A 1 378 ? -4.95755  21.38955  53.67750  1.000 27.98485 ? 381  ALA   A C   1 
ATOM   2771 O  O   . ALA   A 1 378 ? -3.83190  21.55404  54.16910  1.000 29.35149 ? 381  ALA   A O   1 
ATOM   2772 C  CB  . ALA   A 1 378 ? -5.30038  21.53161  51.19705  1.000 32.79367 ? 381  ALA   A CB  1 
ATOM   2773 N  N   . GLU   A 1 379 ? -6.06759  21.90994  54.21869  1.000 30.39398 ? 382  GLU   A N   1 
ATOM   2774 C  CA  . GLU   A 1 379 ? -6.04689  22.65652  55.47548  1.000 31.21827 ? 382  GLU   A CA  1 
ATOM   2775 C  C   . GLU   A 1 379 ? -5.63418  21.76278  56.64660  1.000 31.31600 ? 382  GLU   A C   1 
ATOM   2776 O  O   . GLU   A 1 379 ? -4.78027  22.13980  57.45952  1.000 30.34397 ? 382  GLU   A O   1 
ATOM   2777 C  CB  . GLU   A 1 379 ? -7.43069  23.27059  55.70590  1.000 31.32771 ? 382  GLU   A CB  1 
ATOM   2778 C  CG  . GLU   A 1 379 ? -7.51180  24.30281  56.82283  1.000 48.90332 ? 382  GLU   A CG  1 
ATOM   2779 C  CD  . GLU   A 1 379 ? -7.70051  23.67635  58.19179  1.000 70.75487 ? 382  GLU   A CD  1 
ATOM   2780 O  OE1 . GLU   A 1 379 ? -7.24598  24.28076  59.18993  1.000 67.13446 ? 382  GLU   A OE1 1 
ATOM   2781 O  OE2 . GLU   A 1 379 ? -8.30228  22.58019  58.26448  1.000 73.87092 ? 382  GLU   A OE2 1 
ATOM   2782 N  N   . LYS   A 1 380 ? -6.22332  20.56608  56.74893  1.000 27.75151 ? 383  LYS   A N   1 
ATOM   2783 C  CA  . LYS   A 1 380 ? -5.84030  19.65380  57.82155  1.000 22.65332 ? 383  LYS   A CA  1 
ATOM   2784 C  C   . LYS   A 1 380 ? -4.36907  19.26834  57.72029  1.000 29.60545 ? 383  LYS   A C   1 
ATOM   2785 O  O   . LYS   A 1 380 ? -3.68208  19.15843  58.73807  1.000 24.41215 ? 383  LYS   A O   1 
ATOM   2786 C  CB  . LYS   A 1 380 ? -6.71098  18.39230  57.79351  1.000 28.52753 ? 383  LYS   A CB  1 
ATOM   2787 C  CG  . LYS   A 1 380 ? -8.17491  18.63429  58.06113  1.000 34.81350 ? 383  LYS   A CG  1 
ATOM   2788 C  CD  . LYS   A 1 380 ? -8.39511  19.33930  59.37766  1.000 45.65890 ? 383  LYS   A CD  1 
ATOM   2789 C  CE  . LYS   A 1 380 ? -9.66100  18.82240  60.04402  1.000 53.13509 ? 383  LYS   A CE  1 
ATOM   2790 N  NZ  . LYS   A 1 380 ? -10.73719 18.51963  59.06621  1.000 41.46027 ? 383  LYS   A NZ  1 
ATOM   2791 N  N   . LEU   A 1 381 ? -3.87051  19.01330  56.50403  1.000 23.86838 ? 384  LEU   A N   1 
ATOM   2792 C  CA  . LEU   A 1 381 ? -2.46574  18.62486  56.38523  1.000 24.27317 ? 384  LEU   A CA  1 
ATOM   2793 C  C   . LEU   A 1 381 ? -1.55202  19.77875  56.77474  1.000 21.51821 ? 384  LEU   A C   1 
ATOM   2794 O  O   . LEU   A 1 381 ? -0.49479  19.56779  57.39156  1.000 25.76616 ? 384  LEU   A O   1 
ATOM   2795 C  CB  . LEU   A 1 381 ? -2.15895  18.15195  54.96216  1.000 23.38679 ? 384  LEU   A CB  1 
ATOM   2796 C  CG  . LEU   A 1 381 ? -0.71691  17.76536  54.66848  1.000 25.69790 ? 384  LEU   A CG  1 
ATOM   2797 C  CD1 . LEU   A 1 381 ? -0.27012  16.58699  55.56133  1.000 24.85920 ? 384  LEU   A CD1 1 
ATOM   2798 C  CD2 . LEU   A 1 381 ? -0.55929  17.40441  53.16479  1.000 24.70966 ? 384  LEU   A CD2 1 
ATOM   2799 N  N   . GLN   A 1 382 ? -1.95613  21.01190  56.45274  1.000 22.53746 ? 385  GLN   A N   1 
ATOM   2800 C  CA  . GLN   A 1 382 ? -1.11178  22.14961  56.79592  1.000 27.35128 ? 385  GLN   A CA  1 
ATOM   2801 C  C   . GLN   A 1 382 ? -1.00778  22.33062  58.30521  1.000 25.30652 ? 385  GLN   A C   1 
ATOM   2802 O  O   . GLN   A 1 382 ? 0.03867   22.75585  58.79828  1.000 24.71791 ? 385  GLN   A O   1 
ATOM   2803 C  CB  . GLN   A 1 382 ? -1.62773  23.43178  56.14767  1.000 30.61615 ? 385  GLN   A CB  1 
ATOM   2804 C  CG  . GLN   A 1 382 ? -0.59970  24.58112  56.17017  1.000 31.37606 ? 385  GLN   A CG  1 
ATOM   2805 C  CD  . GLN   A 1 382 ? 0.65843   24.23767  55.37136  1.000 48.75268 ? 385  GLN   A CD  1 
ATOM   2806 O  OE1 . GLN   A 1 382 ? 0.63572   23.36855  54.49827  1.000 42.03861 ? 385  GLN   A OE1 1 
ATOM   2807 N  NE2 . GLN   A 1 382 ? 1.75981   24.91136  55.67714  1.000 45.34195 ? 385  GLN   A NE2 1 
ATOM   2808 N  N   . ARG   A 1 383 ? -2.07392  22.01909  59.05299  1.000 25.73114 ? 386  ARG   A N   1 
ATOM   2809 C  CA  . ARG   A 1 383 ? -1.97534  22.04447  60.51260  1.000 26.01473 ? 386  ARG   A CA  1 
ATOM   2810 C  C   . ARG   A 1 383 ? -0.92414  21.06428  61.01250  1.000 21.99974 ? 386  ARG   A C   1 
ATOM   2811 O  O   . ARG   A 1 383 ? -0.22087  21.35137  61.98447  1.000 22.32935 ? 386  ARG   A O   1 
ATOM   2812 C  CB  . ARG   A 1 383 ? -3.32599  21.72443  61.15888  1.000 25.43385 ? 386  ARG   A CB  1 
ATOM   2813 C  CG  . ARG   A 1 383 ? -4.39819  22.79398  61.02440  1.000 29.77784 ? 386  ARG   A CG  1 
ATOM   2814 C  CD  . ARG   A 1 383 ? -5.71232  22.23072  61.56352  1.000 37.97346 ? 386  ARG   A CD  1 
ATOM   2815 N  NE  . ARG   A 1 383 ? -6.84128  23.12984  61.35783  1.000 44.39466 ? 386  ARG   A NE  1 
ATOM   2816 C  CZ  . ARG   A 1 383 ? -8.10904  22.79901  61.56774  1.000 61.29405 ? 386  ARG   A CZ  1 
ATOM   2817 N  NH1 . ARG   A 1 383 ? -8.46031  21.55912  61.88338  1.000 40.45893 ? 386  ARG   A NH1 1 
ATOM   2818 N  NH2 . ARG   A 1 383 ? -9.04743  23.73647  61.46498  1.000 66.28033 ? 386  ARG   A NH2 1 
ATOM   2819 N  N   . ILE   A 1 384 ? -0.82786  19.88025  60.38527  1.000 21.71142 ? 387  ILE   A N   1 
ATOM   2820 C  CA  . ILE   A 1 384 ? 0.17650   18.90424  60.79411  1.000 24.64342 ? 387  ILE   A CA  1 
ATOM   2821 C  C   . ILE   A 1 384 ? 1.58260   19.41156  60.48367  1.000 21.36205 ? 387  ILE   A C   1 
ATOM   2822 O  O   . ILE   A 1 384 ? 2.51175   19.27350  61.30476  1.000 22.53857 ? 387  ILE   A O   1 
ATOM   2823 C  CB  . ILE   A 1 384 ? -0.10461  17.55239  60.11246  1.000 26.61815 ? 387  ILE   A CB  1 
ATOM   2824 C  CG1 . ILE   A 1 384 ? -1.33129  16.89071  60.74512  1.000 28.09686 ? 387  ILE   A CG1 1 
ATOM   2825 C  CG2 . ILE   A 1 384 ? 1.11149   16.62877  60.21150  1.000 25.34539 ? 387  ILE   A CG2 1 
ATOM   2826 C  CD1 . ILE   A 1 384 ? -1.71369  15.58357  60.08506  1.000 27.62800 ? 387  ILE   A CD1 1 
ATOM   2827 N  N   . VAL   A 1 385 ? 1.77090   19.96424  59.28058  1.000 22.74426 ? 388  VAL   A N   1 
ATOM   2828 C  CA  . VAL   A 1 385 ? 3.06040   20.54096  58.89398  1.000 19.10719 ? 388  VAL   A CA  1 
ATOM   2829 C  C   . VAL   A 1 385 ? 3.49851   21.59821  59.89881  1.000 22.50980 ? 388  VAL   A C   1 
ATOM   2830 O  O   . VAL   A 1 385 ? 4.63486   21.58955  60.38716  1.000 23.46435 ? 388  VAL   A O   1 
ATOM   2831 C  CB  . VAL   A 1 385 ? 2.96682   21.14140  57.47603  1.000 24.41881 ? 388  VAL   A CB  1 
ATOM   2832 C  CG1 . VAL   A 1 385 ? 4.23978   21.90641  57.13569  1.000 27.71845 ? 388  VAL   A CG1 1 
ATOM   2833 C  CG2 . VAL   A 1 385 ? 2.67765   20.04626  56.42525  1.000 23.38509 ? 388  VAL   A CG2 1 
ATOM   2834 N  N   A LYS   A 1 386 ? 2.60586   22.54866  60.19809  0.408 20.14796 ? 389  LYS   A N   1 
ATOM   2835 N  N   B LYS   A 1 386 ? 2.60862   22.53808  60.21624  0.592 20.13477 ? 389  LYS   A N   1 
ATOM   2836 C  CA  A LYS   A 1 386 ? 2.94813   23.64095  61.10791  0.408 20.65561 ? 389  LYS   A CA  1 
ATOM   2837 C  CA  B LYS   A 1 386 ? 2.99619   23.63199  61.10597  0.592 20.64160 ? 389  LYS   A CA  1 
ATOM   2838 C  C   A LYS   A 1 386 ? 3.19874   23.14577  62.52718  0.408 21.68810 ? 389  LYS   A C   1 
ATOM   2839 C  C   B LYS   A 1 386 ? 3.17511   23.17057  62.54917  0.592 21.70244 ? 389  LYS   A C   1 
ATOM   2840 O  O   A LYS   A 1 386 ? 4.01371   23.72714  63.25300  0.408 22.18700 ? 389  LYS   A O   1 
ATOM   2841 O  O   B LYS   A 1 386 ? 3.90450   23.80966  63.31776  0.592 21.89175 ? 389  LYS   A O   1 
ATOM   2842 C  CB  A LYS   A 1 386 ? 1.82453   24.68006  61.13506  0.408 23.72143 ? 389  LYS   A CB  1 
ATOM   2843 C  CB  B LYS   A 1 386 ? 1.94714   24.73375  61.04971  0.592 23.94987 ? 389  LYS   A CB  1 
ATOM   2844 C  CG  A LYS   A 1 386 ? 1.47575   25.31247  59.78708  0.408 32.92383 ? 389  LYS   A CG  1 
ATOM   2845 C  CG  B LYS   A 1 386 ? 1.91853   25.48581  59.72508  0.592 33.46395 ? 389  LYS   A CG  1 
ATOM   2846 C  CD  A LYS   A 1 386 ? 0.62390   26.57309  59.98068  0.408 38.57465 ? 389  LYS   A CD  1 
ATOM   2847 C  CD  B LYS   A 1 386 ? 0.72991   26.42246  59.69260  0.592 38.28670 ? 389  LYS   A CD  1 
ATOM   2848 C  CE  A LYS   A 1 386 ? -0.64954  26.58695  59.12265  0.408 38.92185 ? 389  LYS   A CE  1 
ATOM   2849 C  CE  B LYS   A 1 386 ? 0.66745   27.24159  58.42121  0.592 35.12072 ? 389  LYS   A CE  1 
ATOM   2850 N  NZ  A LYS   A 1 386 ? -1.71258  25.63133  59.57929  0.408 25.59586 ? 389  LYS   A NZ  1 
ATOM   2851 N  NZ  B LYS   A 1 386 ? -0.63561  27.93747  58.37737  0.592 34.96872 ? 389  LYS   A NZ  1 
ATOM   2852 N  N   . ASN   A 1 387 ? 2.47787   22.11082  62.95353  1.000 19.23310 ? 390  ASN   A N   1 
ATOM   2853 C  CA  . ASN   A 1 387 ? 2.52400   21.66403  64.34368  1.000 21.44170 ? 390  ASN   A CA  1 
ATOM   2854 C  C   . ASN   A 1 387 ? 3.76833   20.84602  64.66829  1.000 23.42592 ? 390  ASN   A C   1 
ATOM   2855 O  O   . ASN   A 1 387 ? 4.12893   20.71152  65.84811  1.000 19.73145 ? 390  ASN   A O   1 
ATOM   2856 C  CB  . ASN   A 1 387 ? 1.29802   20.79326  64.65392  1.000 21.68952 ? 390  ASN   A CB  1 
ATOM   2857 C  CG  . ASN   A 1 387 ? 0.99433   20.71983  66.13732  1.000 23.63655 ? 390  ASN   A CG  1 
ATOM   2858 O  OD1 . ASN   A 1 387 ? 1.32429   21.63128  66.88350  1.000 23.06822 ? 390  ASN   A OD1 1 
ATOM   2859 N  ND2 . ASN   A 1 387 ? 0.30484   19.66628  66.55019  1.000 22.82870 ? 390  ASN   A ND2 1 
ATOM   2860 N  N   . LEU   A 1 388 ? 4.41990   20.26675  63.67081  1.000 21.54373 ? 391  LEU   A N   1 
ATOM   2861 C  CA  . LEU   A 1 388 ? 5.48380   19.32003  63.96360  1.000 19.28181 ? 391  LEU   A CA  1 
ATOM   2862 C  C   . LEU   A 1 388 ? 6.74950   20.08249  64.33196  1.000 24.01823 ? 391  LEU   A C   1 
ATOM   2863 O  O   . LEU   A 1 388 ? 7.22074   20.92482  63.56481  1.000 18.52684 ? 391  LEU   A O   1 
ATOM   2864 C  CB  . LEU   A 1 388 ? 5.71430   18.37834  62.78069  1.000 17.29136 ? 391  LEU   A CB  1 
ATOM   2865 C  CG  . LEU   A 1 388 ? 6.95243   17.49478  62.90398  1.000 20.11752 ? 391  LEU   A CG  1 
ATOM   2866 C  CD1 . LEU   A 1 388 ? 6.80254   16.48663  64.08520  1.000 16.50024 ? 391  LEU   A CD1 1 
ATOM   2867 C  CD2 . LEU   A 1 388 ? 7.22094   16.73940  61.56671  1.000 18.58832 ? 391  LEU   A CD2 1 
ATOM   2868 N  N   . ASP   A 1 389 ? 7.26956   19.81915  65.53706  1.000 19.22101 ? 392  ASP   A N   1 
ATOM   2869 C  CA  . ASP   A 1 389 ? 8.55291   20.34386  65.99437  1.000 18.08986 ? 392  ASP   A CA  1 
ATOM   2870 C  C   . ASP   A 1 389 ? 9.55305   19.19809  65.85340  1.000 22.69572 ? 392  ASP   A C   1 
ATOM   2871 O  O   . ASP   A 1 389 ? 9.50571   18.24047  66.62953  1.000 19.95611 ? 392  ASP   A O   1 
ATOM   2872 C  CB  . ASP   A 1 389 ? 8.42062   20.82246  67.44867  1.000 17.64399 ? 392  ASP   A CB  1 
ATOM   2873 C  CG  . ASP   A 1 389 ? 9.70429   21.42024  68.01487  1.000 24.01571 ? 392  ASP   A CG  1 
ATOM   2874 O  OD1 . ASP   A 1 389 ? 10.66767  21.54787  67.25125  1.000 23.10303 ? 392  ASP   A OD1 1 
ATOM   2875 O  OD2 . ASP   A 1 389 ? 9.73543   21.79068  69.22202  1.000 20.31145 ? 392  ASP   A OD2 1 
ATOM   2876 N  N   . PHE   A 1 390 ? 10.46242  19.28049  64.87293  1.000 20.54529 ? 393  PHE   A N   1 
ATOM   2877 C  CA  . PHE   A 1 390 ? 11.32815  18.14219  64.57437  1.000 20.38372 ? 393  PHE   A CA  1 
ATOM   2878 C  C   . PHE   A 1 390 ? 12.80125  18.53805  64.50078  1.000 25.66163 ? 393  PHE   A C   1 
ATOM   2879 O  O   . PHE   A 1 390 ? 13.15893  19.52583  63.85676  1.000 19.36992 ? 393  PHE   A O   1 
ATOM   2880 C  CB  . PHE   A 1 390 ? 10.93503  17.48210  63.25646  1.000 21.78204 ? 393  PHE   A CB  1 
ATOM   2881 C  CG  . PHE   A 1 390 ? 11.74037  16.24761  62.94326  1.000 21.12780 ? 393  PHE   A CG  1 
ATOM   2882 C  CD1 . PHE   A 1 390 ? 11.57481  15.09546  63.70819  1.000 24.04282 ? 393  PHE   A CD1 1 
ATOM   2883 C  CD2 . PHE   A 1 390 ? 12.69299  16.25430  61.91948  1.000 20.61445 ? 393  PHE   A CD2 1 
ATOM   2884 C  CE1 . PHE   A 1 390 ? 12.31972  13.96294  63.46904  1.000 21.86526 ? 393  PHE   A CE1 1 
ATOM   2885 C  CE2 . PHE   A 1 390 ? 13.42574  15.11503  61.65649  1.000 21.27867 ? 393  PHE   A CE2 1 
ATOM   2886 C  CZ  . PHE   A 1 390 ? 13.24715  13.97104  62.43653  1.000 23.21947 ? 393  PHE   A CZ  1 
ATOM   2887 N  N   . ILE   A 1 391 ? 13.67461  17.72113  65.07942  1.000 18.05567 ? 394  ILE   A N   1 
ATOM   2888 C  CA  . ILE   A 1 391 ? 15.10021  18.02863  65.03081  1.000 17.60824 ? 394  ILE   A CA  1 
ATOM   2889 C  C   . ILE   A 1 391 ? 15.88310  16.73380  64.87759  1.000 24.15906 ? 394  ILE   A C   1 
ATOM   2890 O  O   . ILE   A 1 391 ? 15.57394  15.73018  65.52885  1.000 17.02532 ? 394  ILE   A O   1 
ATOM   2891 C  CB  . ILE   A 1 391 ? 15.56849  18.81044  66.27810  1.000 22.89108 ? 394  ILE   A CB  1 
ATOM   2892 C  CG1 . ILE   A 1 391 ? 17.07654  19.09065  66.19009  1.000 36.32981 ? 394  ILE   A CG1 1 
ATOM   2893 C  CG2 . ILE   A 1 391 ? 15.29823  18.04519  67.53828  1.000 28.89304 ? 394  ILE   A CG2 1 
ATOM   2894 C  CD1 . ILE   A 1 391 ? 17.55171  20.20756  67.11914  1.000 45.15002 ? 394  ILE   A CD1 1 
ATOM   2895 N  N   . VAL   A 1 392 ? 16.87963  16.74760  63.99438  1.000 21.42082 ? 395  VAL   A N   1 
ATOM   2896 C  CA  . VAL   A 1 392 ? 17.84593  15.66277  63.89883  1.000 22.37058 ? 395  VAL   A CA  1 
ATOM   2897 C  C   . VAL   A 1 392 ? 19.07565  16.13330  64.65009  1.000 25.10717 ? 395  VAL   A C   1 
ATOM   2898 O  O   . VAL   A 1 392 ? 19.65523  17.15937  64.29793  1.000 21.72950 ? 395  VAL   A O   1 
ATOM   2899 C  CB  . VAL   A 1 392 ? 18.19991  15.32597  62.44265  1.000 24.86045 ? 395  VAL   A CB  1 
ATOM   2900 C  CG1 . VAL   A 1 392 ? 19.23081  14.19225  62.42574  1.000 26.88189 ? 395  VAL   A CG1 1 
ATOM   2901 C  CG2 . VAL   A 1 392 ? 16.94700  14.93562  61.66351  1.000 24.34784 ? 395  VAL   A CG2 1 
ATOM   2902 N  N   . TYR   A 1 393 ? 19.46543  15.41430  65.69416  1.000 19.40571 ? 396  TYR   A N   1 
ATOM   2903 C  CA  . TYR   A 1 393 ? 20.58821  15.82821  66.53130  1.000 19.99235 ? 396  TYR   A CA  1 
ATOM   2904 C  C   . TYR   A 1 393 ? 21.59549  14.68894  66.55182  1.000 22.72111 ? 396  TYR   A C   1 
ATOM   2905 O  O   . TYR   A 1 393 ? 21.25387  13.55887  66.92744  1.000 20.12518 ? 396  TYR   A O   1 
ATOM   2906 C  CB  . TYR   A 1 393 ? 20.11597  16.17249  67.95157  1.000 22.31983 ? 396  TYR   A CB  1 
ATOM   2907 C  CG  . TYR   A 1 393 ? 21.27736  16.28099  68.92027  1.000 23.19216 ? 396  TYR   A CG  1 
ATOM   2908 C  CD1 . TYR   A 1 393 ? 22.26654  17.22596  68.74053  1.000 31.44632 ? 396  TYR   A CD1 1 
ATOM   2909 C  CD2 . TYR   A 1 393 ? 21.39463  15.40391  69.98707  1.000 27.25196 ? 396  TYR   A CD2 1 
ATOM   2910 C  CE1 . TYR   A 1 393 ? 23.35481  17.30650  69.60964  1.000 32.99727 ? 396  TYR   A CE1 1 
ATOM   2911 C  CE2 . TYR   A 1 393 ? 22.45563  15.47624  70.85131  1.000 23.92102 ? 396  TYR   A CE2 1 
ATOM   2912 C  CZ  . TYR   A 1 393 ? 23.43665  16.42173  70.65774  1.000 24.69470 ? 396  TYR   A CZ  1 
ATOM   2913 O  OH  . TYR   A 1 393 ? 24.51503  16.47271  71.52004  1.000 33.44799 ? 396  TYR   A OH  1 
ATOM   2914 N  N   . LYS   A 1 394 ? 22.81438  14.98011  66.13566  1.000 22.04533 ? 397  LYS   A N   1 
ATOM   2915 C  CA  . LYS   A 1 394 ? 23.89331  14.01177  66.11354  1.000 25.61368 ? 397  LYS   A CA  1 
ATOM   2916 C  C   . LYS   A 1 394 ? 24.75570  14.24467  67.34962  1.000 25.66858 ? 397  LYS   A C   1 
ATOM   2917 O  O   . LYS   A 1 394 ? 25.44895  15.26030  67.45418  1.000 24.49901 ? 397  LYS   A O   1 
ATOM   2918 C  CB  . LYS   A 1 394 ? 24.73541  14.13647  64.84580  1.000 33.52939 ? 397  LYS   A CB  1 
ATOM   2919 C  CG  . LYS   A 1 394 ? 25.67505  12.95173  64.69078  1.000 36.93835 ? 397  LYS   A CG  1 
ATOM   2920 C  CD  . LYS   A 1 394 ? 26.52031  13.03760  63.41683  1.000 44.43190 ? 397  LYS   A CD  1 
ATOM   2921 C  CE  . LYS   A 1 394 ? 27.03159  11.65336  63.05150  1.000 52.82296 ? 397  LYS   A CE  1 
ATOM   2922 N  NZ  . LYS   A 1 394 ? 25.90959  10.63965  63.09515  1.000 57.98369 ? 397  LYS   A NZ  1 
ATOM   2923 N  N   . PHE   A 1 395 ? 24.69137  13.32460  68.29764  1.000 21.12816 ? 398  PHE   A N   1 
ATOM   2924 C  CA  . PHE   A 1 395 ? 25.58964  13.39073  69.44187  1.000 21.92064 ? 398  PHE   A CA  1 
ATOM   2925 C  C   . PHE   A 1 395 ? 26.93703  12.82787  69.01235  1.000 22.74537 ? 398  PHE   A C   1 
ATOM   2926 O  O   . PHE   A 1 395 ? 27.01088  11.67862  68.57457  1.000 26.65199 ? 398  PHE   A O   1 
ATOM   2927 C  CB  . PHE   A 1 395 ? 24.99258  12.59413  70.60299  1.000 24.07747 ? 398  PHE   A CB  1 
ATOM   2928 C  CG  . PHE   A 1 395 ? 25.88750  12.50406  71.79796  1.000 22.86349 ? 398  PHE   A CG  1 
ATOM   2929 C  CD1 . PHE   A 1 395 ? 25.92609  13.54630  72.73682  1.000 22.59001 ? 398  PHE   A CD1 1 
ATOM   2930 C  CD2 . PHE   A 1 395 ? 26.68582  11.38214  71.99581  1.000 22.49043 ? 398  PHE   A CD2 1 
ATOM   2931 C  CE1 . PHE   A 1 395 ? 26.73951  13.46046  73.84188  1.000 23.49703 ? 398  PHE   A CE1 1 
ATOM   2932 C  CE2 . PHE   A 1 395 ? 27.49843  11.28180  73.10617  1.000 23.40436 ? 398  PHE   A CE2 1 
ATOM   2933 C  CZ  . PHE   A 1 395 ? 27.53460  12.32261  74.03495  1.000 24.50721 ? 398  PHE   A CZ  1 
ATOM   2934 N  N   . ASP   A 1 396 ? 28.01224  13.62366  69.10714  1.000 23.87370 ? 399  ASP   A N   1 
ATOM   2935 C  CA  . ASP   A 1 396 ? 29.28365  13.18233  68.54050  1.000 32.80399 ? 399  ASP   A CA  1 
ATOM   2936 C  C   . ASP   A 1 396 ? 30.39438  12.98123  69.56883  1.000 27.35347 ? 399  ASP   A C   1 
ATOM   2937 O  O   . ASP   A 1 396 ? 31.55694  12.77149  69.18197  1.000 23.56321 ? 399  ASP   A O   1 
ATOM   2938 C  CB  . ASP   A 1 396 ? 29.74842  14.16057  67.46346  1.000 37.50778 ? 399  ASP   A CB  1 
ATOM   2939 C  CG  . ASP   A 1 396 ? 30.00675  15.54397  67.99906  1.000 38.40242 ? 399  ASP   A CG  1 
ATOM   2940 O  OD1 . ASP   A 1 396 ? 30.03509  15.75154  69.22927  1.000 60.99309 ? 399  ASP   A OD1 1 
ATOM   2941 O  OD2 . ASP   A 1 396 ? 30.19934  16.44237  67.15683  1.000 61.69898 ? 399  ASP   A OD2 1 
ATOM   2942 N  N   . ASN   A 1 397 ? 30.09692  13.06845  70.86249  1.000 19.45403 ? 400  ASN   A N   1 
ATOM   2943 C  CA  . ASN   A 1 397 ? 31.18348  12.91094  71.82818  1.000 23.88500 ? 400  ASN   A CA  1 
ATOM   2944 C  C   . ASN   A 1 397 ? 31.60591  11.44842  71.97732  1.000 29.36967 ? 400  ASN   A C   1 
ATOM   2945 O  O   . ASN   A 1 397 ? 32.78183  11.16748  72.23950  1.000 23.62569 ? 400  ASN   A O   1 
ATOM   2946 C  CB  . ASN   A 1 397 ? 30.78081  13.50578  73.18413  1.000 24.73187 ? 400  ASN   A CB  1 
ATOM   2947 C  CG  . ASN   A 1 397 ? 31.95216  13.54242  74.18144  1.000 34.27741 ? 400  ASN   A CG  1 
ATOM   2948 O  OD1 . ASN   A 1 397 ? 31.98991  12.77523  75.12480  1.000 26.26753 ? 400  ASN   A OD1 1 
ATOM   2949 N  ND2 . ASN   A 1 397 ? 32.89837  14.44251  73.96808  1.000 26.34689 ? 400  ASN   A ND2 1 
ATOM   2950 N  N   . TYR   A 1 398 ? 30.67992  10.50855  71.81304  1.000 21.68274 ? 401  TYR   A N   1 
ATOM   2951 C  CA  . TYR   A 1 398 ? 30.99870  9.08251   71.89219  1.000 22.71782 ? 401  TYR   A CA  1 
ATOM   2952 C  C   . TYR   A 1 398 ? 29.79951  8.30052   71.37975  1.000 20.00909 ? 401  TYR   A C   1 
ATOM   2953 O  O   . TYR   A 1 398 ? 28.72718  8.86267   71.12712  1.000 19.76527 ? 401  TYR   A O   1 
ATOM   2954 C  CB  . TYR   A 1 398 ? 31.35477  8.63776   73.32207  1.000 22.20299 ? 401  TYR   A CB  1 
ATOM   2955 C  CG  . TYR   A 1 398 ? 30.23441  8.78203   74.36124  1.000 21.65595 ? 401  TYR   A CG  1 
ATOM   2956 C  CD1 . TYR   A 1 398 ? 29.25946  7.78885   74.51730  1.000 18.09717 ? 401  TYR   A CD1 1 
ATOM   2957 C  CD2 . TYR   A 1 398 ? 30.18195  9.89341   75.20577  1.000 16.60630 ? 401  TYR   A CD2 1 
ATOM   2958 C  CE1 . TYR   A 1 398 ? 28.24988  7.90633   75.47242  1.000 19.00181 ? 401  TYR   A CE1 1 
ATOM   2959 C  CE2 . TYR   A 1 398 ? 29.17783  10.02713  76.16402  1.000 18.71129 ? 401  TYR   A CE2 1 
ATOM   2960 C  CZ  . TYR   A 1 398 ? 28.21638  9.02864   76.29149  1.000 20.46859 ? 401  TYR   A CZ  1 
ATOM   2961 O  OH  . TYR   A 1 398 ? 27.23077  9.13204   77.24909  1.000 18.14176 ? 401  TYR   A OH  1 
ATOM   2962 N  N   . GLY   A 1 399 ? 29.97209  6.97999   71.28818  1.000 19.74520 ? 402  GLY   A N   1 
ATOM   2963 C  CA  . GLY   A 1 399 ? 28.89619  6.09107   70.86564  1.000 20.87401 ? 402  GLY   A CA  1 
ATOM   2964 C  C   . GLY   A 1 399 ? 29.01940  4.73619   71.50584  1.000 23.67791 ? 402  GLY   A C   1 
ATOM   2965 O  O   . GLY   A 1 399 ? 29.35410  4.63045   72.69181  1.000 19.33013 ? 402  GLY   A O   1 
ATOM   2966 N  N   . LYS   A 1 400 ? 28.77149  3.68502   70.71805  1.000 19.07094 ? 403  LYS   A N   1 
ATOM   2967 C  CA  . LYS   A 1 400 ? 28.76835  2.32499   71.25874  1.000 20.07098 ? 403  LYS   A CA  1 
ATOM   2968 C  C   . LYS   A 1 400 ? 30.11119  1.94241   71.88239  1.000 21.03128 ? 403  LYS   A C   1 
ATOM   2969 O  O   . LYS   A 1 400 ? 30.14763  1.23658   72.89646  1.000 22.70757 ? 403  LYS   A O   1 
ATOM   2970 C  CB  . LYS   A 1 400 ? 28.39599  1.33508   70.14783  1.000 20.26223 ? 403  LYS   A CB  1 
ATOM   2971 C  CG  . LYS   A 1 400 ? 26.90843  1.43813   69.77719  1.000 24.78613 ? 403  LYS   A CG  1 
ATOM   2972 C  CD  . LYS   A 1 400 ? 26.52965  0.64989   68.49058  1.000 28.01615 ? 403  LYS   A CD  1 
ATOM   2973 C  CE  . LYS   A 1 400 ? 27.40915  -0.50260  68.15350  1.000 46.13021 ? 403  LYS   A CE  1 
ATOM   2974 N  NZ  . LYS   A 1 400 ? 27.24002  -0.89921  66.68908  1.000 36.15446 ? 403  LYS   A NZ  1 
ATOM   2975 N  N   . THR   A 1 401 ? 31.22662  2.33894   71.26465  1.000 23.56185 ? 404  THR   A N   1 
ATOM   2976 C  CA  . THR   A 1 401 ? 32.52289  1.87043   71.75839  1.000 20.56992 ? 404  THR   A CA  1 
ATOM   2977 C  C   . THR   A 1 401 ? 32.73007  2.27545   73.21297  1.000 23.72982 ? 404  THR   A C   1 
ATOM   2978 O  O   . THR   A 1 401 ? 33.11383  1.45040   74.05309  1.000 24.58766 ? 404  THR   A O   1 
ATOM   2979 C  CB  . THR   A 1 401 ? 33.65342  2.40392   70.87654  1.000 28.18883 ? 404  THR   A CB  1 
ATOM   2980 O  OG1 . THR   A 1 401 ? 33.44632  1.92883   69.54395  1.000 31.51564 ? 404  THR   A OG1 1 
ATOM   2981 C  CG2 . THR   A 1 401 ? 35.02635  1.91672   71.38584  1.000 27.82998 ? 404  THR   A CG2 1 
ATOM   2982 N  N   . PHE   A 1 402 ? 32.46852  3.53869   73.53565  1.000 20.86186 ? 405  PHE   A N   1 
ATOM   2983 C  CA  . PHE   A 1 402 ? 32.60735  3.97391   74.92752  1.000 22.90112 ? 405  PHE   A CA  1 
ATOM   2984 C  C   . PHE   A 1 402 ? 31.61077  3.25801   75.84156  1.000 25.39204 ? 405  PHE   A C   1 
ATOM   2985 O  O   . PHE   A 1 402 ? 31.95583  2.85248   76.95962  1.000 20.74076 ? 405  PHE   A O   1 
ATOM   2986 C  CB  . PHE   A 1 402 ? 32.41940  5.49621   75.03399  1.000 19.33089 ? 405  PHE   A CB  1 
ATOM   2987 C  CG  . PHE   A 1 402 ? 32.44921  5.99370   76.45513  1.000 23.01849 ? 405  PHE   A CG  1 
ATOM   2988 C  CD1 . PHE   A 1 402 ? 33.65837  6.25363   77.07658  1.000 25.89649 ? 405  PHE   A CD1 1 
ATOM   2989 C  CD2 . PHE   A 1 402 ? 31.26652  6.12884   77.19392  1.000 23.41507 ? 405  PHE   A CD2 1 
ATOM   2990 C  CE1 . PHE   A 1 402 ? 33.69989  6.68956   78.39090  1.000 29.67367 ? 405  PHE   A CE1 1 
ATOM   2991 C  CE2 . PHE   A 1 402 ? 31.29921  6.55399   78.50670  1.000 19.41626 ? 405  PHE   A CE2 1 
ATOM   2992 C  CZ  . PHE   A 1 402 ? 32.53075  6.84215   79.10160  1.000 21.72976 ? 405  PHE   A CZ  1 
ATOM   2993 N  N   . ILE   A 1 403 ? 30.36449  3.09705   75.38704  1.000 20.40431 ? 406  ILE   A N   1 
ATOM   2994 C  CA  . ILE   A 1 403 ? 29.32657  2.51377   76.24259  1.000 19.14459 ? 406  ILE   A CA  1 
ATOM   2995 C  C   . ILE   A 1 403 ? 29.65038  1.06962   76.56198  1.000 20.68669 ? 406  ILE   A C   1 
ATOM   2996 O  O   . ILE   A 1 403 ? 29.53314  0.63370   77.71289  1.000 22.54535 ? 406  ILE   A O   1 
ATOM   2997 C  CB  . ILE   A 1 403 ? 27.93606  2.63416   75.57970  1.000 15.65255 ? 406  ILE   A CB  1 
ATOM   2998 C  CG1 . ILE   A 1 403 ? 27.50910  4.10687   75.50094  1.000 19.52092 ? 406  ILE   A CG1 1 
ATOM   2999 C  CG2 . ILE   A 1 403 ? 26.93796  1.81110   76.39230  1.000 15.49729 ? 406  ILE   A CG2 1 
ATOM   3000 C  CD1 . ILE   A 1 403 ? 26.28471  4.37604   74.52078  1.000 19.80405 ? 406  ILE   A CD1 1 
ATOM   3001 N  N   . LYS   A 1 404 ? 30.10812  0.30899   75.56109  1.000 18.39846 ? 407  LYS   A N   1 
ATOM   3002 C  CA  . LYS   A 1 404 ? 30.46872  -1.08062  75.82244  1.000 19.69353 ? 407  LYS   A CA  1 
ATOM   3003 C  C   . LYS   A 1 404 ? 31.64354  -1.19347  76.78907  1.000 22.97719 ? 407  LYS   A C   1 
ATOM   3004 O  O   . LYS   A 1 404 ? 31.73442  -2.17546  77.53037  1.000 22.22693 ? 407  LYS   A O   1 
ATOM   3005 C  CB  . LYS   A 1 404 ? 30.77350  -1.80705  74.50908  1.000 22.83450 ? 407  LYS   A CB  1 
ATOM   3006 C  CG  . LYS   A 1 404 ? 29.49718  -2.09009  73.67501  1.000 23.22254 ? 407  LYS   A CG  1 
ATOM   3007 C  CD  . LYS   A 1 404 ? 29.87306  -2.62437  72.29564  1.000 34.53659 ? 407  LYS   A CD  1 
ATOM   3008 C  CE  . LYS   A 1 404 ? 28.60320  -3.02792  71.53667  1.000 39.35707 ? 407  LYS   A CE  1 
ATOM   3009 N  NZ  . LYS   A 1 404 ? 28.84843  -3.23925  70.08290  1.000 57.16289 ? 407  LYS   A NZ  1 
ATOM   3010 N  N   . LYS   A 1 405 ? 32.55427  -0.21896  76.79287  1.000 20.35561 ? 408  LYS   A N   1 
ATOM   3011 C  CA  . LYS   A 1 405 ? 33.64784  -0.22140  77.76047  1.000 28.02170 ? 408  LYS   A CA  1 
ATOM   3012 C  C   . LYS   A 1 405 ? 33.17716  0.00704   79.19433  1.000 27.18230 ? 408  LYS   A C   1 
ATOM   3013 O  O   . LYS   A 1 405 ? 33.98041  -0.12819  80.13301  1.000 21.50117 ? 408  LYS   A O   1 
ATOM   3014 C  CB  . LYS   A 1 405 ? 34.67790  0.84482   77.38662  1.000 23.81332 ? 408  LYS   A CB  1 
ATOM   3015 C  CG  . LYS   A 1 405 ? 35.47253  0.50569   76.13701  1.000 24.10634 ? 408  LYS   A CG  1 
ATOM   3016 C  CD  . LYS   A 1 405 ? 36.32539  1.65752   75.71598  1.000 28.54306 ? 408  LYS   A CD  1 
ATOM   3017 C  CE  . LYS   A 1 405 ? 37.23957  1.25157   74.56998  1.000 38.92615 ? 408  LYS   A CE  1 
ATOM   3018 N  NZ  . LYS   A 1 405 ? 37.97622  2.44614   74.11629  1.000 37.57137 ? 408  LYS   A NZ  1 
ATOM   3019 N  N   . GLN   A 1 406 ? 31.90931  0.34236   79.38314  1.000 22.74849 ? 409  GLN   A N   1 
ATOM   3020 C  CA  . GLN   A 1 406 ? 31.31127  0.48216   80.69834  1.000 23.83807 ? 409  GLN   A CA  1 
ATOM   3021 C  C   . GLN   A 1 406 ? 30.49842  -0.73525  81.10141  1.000 25.75034 ? 409  GLN   A C   1 
ATOM   3022 O  O   . GLN   A 1 406 ? 29.74943  -0.66484  82.08856  1.000 26.88760 ? 409  GLN   A O   1 
ATOM   3023 C  CB  . GLN   A 1 406 ? 30.43111  1.73802   80.73892  1.000 23.92398 ? 409  GLN   A CB  1 
ATOM   3024 C  CG  . GLN   A 1 406 ? 31.05238  2.94612   80.03567  1.000 19.13587 ? 409  GLN   A CG  1 
ATOM   3025 C  CD  . GLN   A 1 406 ? 32.49555  3.21732   80.45800  1.000 22.97819 ? 409  GLN   A CD  1 
ATOM   3026 O  OE1 . GLN   A 1 406 ? 32.82850  3.19184   81.64001  1.000 23.56074 ? 409  GLN   A OE1 1 
ATOM   3027 N  NE2 . GLN   A 1 406 ? 33.35478  3.47206   79.48394  1.000 23.55761 ? 409  GLN   A NE2 1 
ATOM   3028 N  N   . LYS   A 1 407 ? 30.65033  -1.85561  80.37799  1.000 24.18275 ? 410  LYS   A N   1 
ATOM   3029 C  CA  . LYS   A 1 407 ? 29.88919  -3.08966  80.62906  1.000 20.52977 ? 410  LYS   A CA  1 
ATOM   3030 C  C   . LYS   A 1 407 ? 28.38327  -2.82196  80.57123  1.000 24.57786 ? 410  LYS   A C   1 
ATOM   3031 O  O   . LYS   A 1 407 ? 27.60978  -3.36170  81.36554  1.000 25.64439 ? 410  LYS   A O   1 
ATOM   3032 C  CB  . LYS   A 1 407 ? 30.26252  -3.72352  81.96991  1.000 27.30251 ? 410  LYS   A CB  1 
ATOM   3033 C  CG  . LYS   A 1 407 ? 31.69661  -4.19940  82.10395  1.000 34.81874 ? 410  LYS   A CG  1 
ATOM   3034 C  CD  . LYS   A 1 407 ? 31.86457  -5.08276  83.33139  1.000 42.56417 ? 410  LYS   A CD  1 
ATOM   3035 C  CE  . LYS   A 1 407 ? 31.64925  -4.31123  84.62644  1.000 49.67666 ? 410  LYS   A CE  1 
ATOM   3036 N  NZ  . LYS   A 1 407 ? 32.69568  -3.27110  84.88498  1.000 65.43991 ? 410  LYS   A NZ  1 
ATOM   3037 N  N   . CYS   A 1 408 ? 27.96542  -1.99156  79.61702  1.000 22.33324 ? 411  CYS   A N   1 
ATOM   3038 C  CA  . CYS   A 1 408 ? 26.56224  -1.63891  79.40357  1.000 24.69911 ? 411  CYS   A CA  1 
ATOM   3039 C  C   . CYS   A 1 408 ? 26.16216  -1.94133  77.96886  1.000 28.11062 ? 411  CYS   A C   1 
ATOM   3040 O  O   . CYS   A 1 408 ? 26.93229  -1.71326  77.03615  1.000 23.13564 ? 411  CYS   A O   1 
ATOM   3041 C  CB  . CYS   A 1 408 ? 26.29347  -0.11670  79.67141  1.000 18.35908 ? 411  CYS   A CB  1 
ATOM   3042 S  SG  . CYS   A 1 408 ? 26.57629  0.33707   81.41666  1.000 31.00934 ? 411  CYS   A SG  1 
ATOM   3043 N  N   . SER   A 1 409 ? 24.94786  -2.42226  77.80616  1.000 20.79920 ? 412  SER   A N   1 
ATOM   3044 C  CA  . SER   A 1 409 ? 24.30876  -2.44586  76.50335  1.000 25.89664 ? 412  SER   A CA  1 
ATOM   3045 C  C   . SER   A 1 409 ? 24.11044  -1.01305  75.99562  1.000 23.42732 ? 412  SER   A C   1 
ATOM   3046 O  O   . SER   A 1 409 ? 23.59193  -0.16264  76.73883  1.000 23.07410 ? 412  SER   A O   1 
ATOM   3047 C  CB  . SER   A 1 409 ? 22.98199  -3.19043  76.68654  1.000 28.37770 ? 412  SER   A CB  1 
ATOM   3048 O  OG  . SER   A 1 409 ? 21.95355  -2.69198  75.91224  1.000 28.31549 ? 412  SER   A OG  1 
ATOM   3049 N  N   . PRO   A 1 410 ? 24.50077  -0.69420  74.75137  1.000 17.83520 ? 413  PRO   A N   1 
ATOM   3050 C  CA  . PRO   A 1 410 ? 24.21120  0.66005   74.24383  1.000 20.63601 ? 413  PRO   A CA  1 
ATOM   3051 C  C   . PRO   A 1 410 ? 22.73442  1.02145   74.31078  1.000 21.38699 ? 413  PRO   A C   1 
ATOM   3052 O  O   . PRO   A 1 410 ? 22.39768  2.15152   74.69356  1.000 18.54289 ? 413  PRO   A O   1 
ATOM   3053 C  CB  . PRO   A 1 410 ? 24.72733  0.61528   72.80083  1.000 22.91066 ? 413  PRO   A CB  1 
ATOM   3054 C  CG  . PRO   A 1 410 ? 25.86908  -0.35974  72.86685  1.000 27.27051 ? 413  PRO   A CG  1 
ATOM   3055 C  CD  . PRO   A 1 410 ? 25.38635  -1.44021  73.83754  1.000 25.99772 ? 413  PRO   A CD  1 
ATOM   3056 N  N   . ASP   A 1 411 ? 21.83672  0.09241   73.98091  1.000 19.14256 ? 414  ASP   A N   1 
ATOM   3057 C  CA  . ASP   A 1 411 ? 20.41579  0.42858   74.02346  1.000 18.84423 ? 414  ASP   A CA  1 
ATOM   3058 C  C   . ASP   A 1 411 ? 19.98595  0.81764   75.42062  1.000 18.81254 ? 414  ASP   A C   1 
ATOM   3059 O  O   . ASP   A 1 411 ? 19.25669  1.78644   75.60256  1.000 15.23647 ? 414  ASP   A O   1 
ATOM   3060 C  CB  . ASP   A 1 411 ? 19.55019  -0.73178  73.56310  1.000 21.17220 ? 414  ASP   A CB  1 
ATOM   3061 C  CG  . ASP   A 1 411 ? 18.11989  -0.28667  73.35213  1.000 28.63604 ? 414  ASP   A CG  1 
ATOM   3062 O  OD1 . ASP   A 1 411 ? 17.92293  0.55166   72.45516  1.000 24.80574 ? 414  ASP   A OD1 1 
ATOM   3063 O  OD2 . ASP   A 1 411 ? 17.21951  -0.70401  74.11303  1.000 22.64027 ? 414  ASP   A OD2 1 
ATOM   3064 N  N   . ALA   A 1 412 ? 20.40471  0.04289   76.42460  1.000 18.04754 ? 415  ALA   A N   1 
ATOM   3065 C  CA  . ALA   A 1 412 ? 19.95912  0.31649   77.78676  1.000 21.53184 ? 415  ALA   A CA  1 
ATOM   3066 C  C   . ALA   A 1 412 ? 20.54905  1.62412   78.29189  1.000 18.63806 ? 415  ALA   A C   1 
ATOM   3067 O  O   . ALA   A 1 412 ? 19.87453  2.39764   78.96865  1.000 17.24405 ? 415  ALA   A O   1 
ATOM   3068 C  CB  . ALA   A 1 412 ? 20.36742  -0.83019  78.71264  1.000 16.57500 ? 415  ALA   A CB  1 
ATOM   3069 N  N   . PHE   A 1 413 ? 21.81582  1.87842   77.96520  1.000 14.53032 ? 416  PHE   A N   1 
ATOM   3070 C  CA  . PHE   A 1 413 ? 22.45404  3.13256   78.35975  1.000 14.00111 ? 416  PHE   A CA  1 
ATOM   3071 C  C   . PHE   A 1 413 ? 21.70956  4.32576   77.76643  1.000 18.21710 ? 416  PHE   A C   1 
ATOM   3072 O  O   . PHE   A 1 413 ? 21.38259  5.29483   78.47058  1.000 17.68010 ? 416  PHE   A O   1 
ATOM   3073 C  CB  . PHE   A 1 413 ? 23.91460  3.05809   77.90340  1.000 18.45416 ? 416  PHE   A CB  1 
ATOM   3074 C  CG  . PHE   A 1 413 ? 24.78450  4.20099   78.32099  1.000 19.57640 ? 416  PHE   A CG  1 
ATOM   3075 C  CD1 . PHE   A 1 413 ? 24.73241  5.41655   77.65156  1.000 16.77659 ? 416  PHE   A CD1 1 
ATOM   3076 C  CD2 . PHE   A 1 413 ? 25.72523  4.03053   79.33753  1.000 18.91493 ? 416  PHE   A CD2 1 
ATOM   3077 C  CE1 . PHE   A 1 413 ? 25.58809  6.46425   78.00828  1.000 17.38786 ? 416  PHE   A CE1 1 
ATOM   3078 C  CE2 . PHE   A 1 413 ? 26.60141  5.07719   79.68570  1.000 21.95294 ? 416  PHE   A CE2 1 
ATOM   3079 C  CZ  . PHE   A 1 413 ? 26.52540  6.28256   79.03129  1.000 16.78209 ? 416  PHE   A CZ  1 
ATOM   3080 N  N   . ILE   A 1 414 ? 21.36433  4.24467   76.48316  1.000 17.00720 ? 417  ILE   A N   1 
ATOM   3081 C  CA  . ILE   A 1 414 ? 20.64940  5.36211   75.84681  1.000 16.81254 ? 417  ILE   A CA  1 
ATOM   3082 C  C   . ILE   A 1 414 ? 19.24574  5.52378   76.42655  1.000 17.56267 ? 417  ILE   A C   1 
ATOM   3083 O  O   . ILE   A 1 414 ? 18.77839  6.65189   76.67389  1.000 16.42632 ? 417  ILE   A O   1 
ATOM   3084 C  CB  . ILE   A 1 414 ? 20.62122  5.16254   74.31950  1.000 18.83346 ? 417  ILE   A CB  1 
ATOM   3085 C  CG1 . ILE   A 1 414 ? 22.03558  5.33127   73.74892  1.000 20.14852 ? 417  ILE   A CG1 1 
ATOM   3086 C  CG2 . ILE   A 1 414 ? 19.64067  6.16411   73.66754  1.000 18.87071 ? 417  ILE   A CG2 1 
ATOM   3087 C  CD1 . ILE   A 1 414 ? 22.22935  4.65161   72.34869  1.000 16.90711 ? 417  ILE   A CD1 1 
ATOM   3088 N  N   . GLN   A 1 415 ? 18.54604  4.41496   76.66377  1.000 15.55473 ? 418  GLN   A N   1 
ATOM   3089 C  CA  . GLN   A 1 415 ? 17.22693  4.52514   77.28550  1.000 14.29603 ? 418  GLN   A CA  1 
ATOM   3090 C  C   . GLN   A 1 415 ? 17.29484  5.23457   78.63432  1.000 15.94149 ? 418  GLN   A C   1 
ATOM   3091 O  O   . GLN   A 1 415 ? 16.42648  6.05811   78.96225  1.000 15.49711 ? 418  GLN   A O   1 
ATOM   3092 C  CB  . GLN   A 1 415 ? 16.61031  3.12687   77.43386  1.000 14.42307 ? 418  GLN   A CB  1 
ATOM   3093 C  CG  . GLN   A 1 415 ? 16.07714  2.58514   76.09282  1.000 15.68308 ? 418  GLN   A CG  1 
ATOM   3094 C  CD  . GLN   A 1 415 ? 14.77621  3.26317   75.67035  1.000 19.74532 ? 418  GLN   A CD  1 
ATOM   3095 O  OE1 . GLN   A 1 415 ? 13.94733  3.62410   76.50767  1.000 18.33629 ? 418  GLN   A OE1 1 
ATOM   3096 N  NE2 . GLN   A 1 415 ? 14.59025  3.43001   74.36561  1.000 15.40540 ? 418  GLN   A NE2 1 
ATOM   3097 N  N   . VAL   A 1 416 ? 18.28805  4.89728   79.45459  1.000 14.40892 ? 419  VAL   A N   1 
ATOM   3098 C  CA  . VAL   A 1 416 ? 18.42019  5.58288   80.73742  1.000 15.85736 ? 419  VAL   A CA  1 
ATOM   3099 C  C   . VAL   A 1 416 ? 18.73284  7.06609   80.52489  1.000 14.27567 ? 419  VAL   A C   1 
ATOM   3100 O  O   . VAL   A 1 416 ? 18.22486  7.92077   81.24997  1.000 14.98047 ? 419  VAL   A O   1 
ATOM   3101 C  CB  . VAL   A 1 416 ? 19.48618  4.87074   81.60181  1.000 18.42124 ? 419  VAL   A CB  1 
ATOM   3102 C  CG1 . VAL   A 1 416 ? 19.81350  5.66215   82.84190  1.000 19.48417 ? 419  VAL   A CG1 1 
ATOM   3103 C  CG2 . VAL   A 1 416 ? 18.97460  3.48549   81.98198  1.000 16.59779 ? 419  VAL   A CG2 1 
ATOM   3104 N  N   . ALA   A 1 417 ? 19.56322  7.38900   79.52648  1.000 16.89088 ? 420  ALA   A N   1 
ATOM   3105 C  CA  . ALA   A 1 417 ? 19.84304  8.78546   79.19123  1.000 17.35804 ? 420  ALA   A CA  1 
ATOM   3106 C  C   . ALA   A 1 417 ? 18.57741  9.54292   78.82827  1.000 13.31096 ? 420  ALA   A C   1 
ATOM   3107 O  O   . ALA   A 1 417 ? 18.41567  10.71164  79.19760  1.000 17.84824 ? 420  ALA   A O   1 
ATOM   3108 C  CB  . ALA   A 1 417 ? 20.82640  8.85574   78.03020  1.000 14.35273 ? 420  ALA   A CB  1 
ATOM   3109 N  N   . LEU   A 1 418 ? 17.67266  8.90614   78.07411  1.000 13.36416 ? 421  LEU   A N   1 
ATOM   3110 C  CA  . LEU   A 1 418 ? 16.43314  9.59217   77.72466  1.000 16.55454 ? 421  LEU   A CA  1 
ATOM   3111 C  C   . LEU   A 1 418 ? 15.55218  9.80648   78.95307  1.000 15.34973 ? 421  LEU   A C   1 
ATOM   3112 O  O   . LEU   A 1 418 ? 14.84287  10.81531  79.03190  1.000 16.88609 ? 421  LEU   A O   1 
ATOM   3113 C  CB  . LEU   A 1 418 ? 15.66784  8.80622   76.65027  1.000 15.94581 ? 421  LEU   A CB  1 
ATOM   3114 C  CG  . LEU   A 1 418 ? 16.39726  8.68802   75.31043  1.000 18.59907 ? 421  LEU   A CG  1 
ATOM   3115 C  CD1 . LEU   A 1 418 ? 15.78134  7.55312   74.50782  1.000 16.69699 ? 421  LEU   A CD1 1 
ATOM   3116 C  CD2 . LEU   A 1 418 ? 16.28216  10.00970  74.56369  1.000 16.46826 ? 421  LEU   A CD2 1 
ATOM   3117 N  N   . GLN   A 1 419 ? 15.55254  8.87512   79.90072  1.000 17.08644 ? 422  GLN   A N   1 
ATOM   3118 C  CA  . GLN   A 1 419 ? 14.81711  9.12350   81.14282  1.000 14.93708 ? 422  GLN   A CA  1 
ATOM   3119 C  C   . GLN   A 1 419 ? 15.40404  10.30868  81.90657  1.000 14.62540 ? 422  GLN   A C   1 
ATOM   3120 O  O   . GLN   A 1 419 ? 14.66195  11.14026  82.43163  1.000 16.15912 ? 422  GLN   A O   1 
ATOM   3121 C  CB  . GLN   A 1 419 ? 14.80914  7.87347   82.03907  1.000 13.80419 ? 422  GLN   A CB  1 
ATOM   3122 C  CG  . GLN   A 1 419 ? 14.08891  6.64825   81.43377  1.000 18.10651 ? 422  GLN   A CG  1 
ATOM   3123 C  CD  . GLN   A 1 419 ? 12.60206  6.91529   81.27813  1.000 18.41596 ? 422  GLN   A CD  1 
ATOM   3124 O  OE1 . GLN   A 1 419 ? 11.96331  7.40079   82.21520  1.000 18.67677 ? 422  GLN   A OE1 1 
ATOM   3125 N  NE2 . GLN   A 1 419 ? 12.04974  6.63707   80.08230  1.000 16.59219 ? 422  GLN   A NE2 1 
ATOM   3126 N  N   . LEU   A 1 420 ? 16.73715  10.38771  82.01154  1.000 13.50930 ? 423  LEU   A N   1 
ATOM   3127 C  CA  . LEU   A 1 420 ? 17.35944  11.53287  82.68195  1.000 15.10379 ? 423  LEU   A CA  1 
ATOM   3128 C  C   . LEU   A 1 420 ? 17.08857  12.83040  81.92174  1.000 16.49923 ? 423  LEU   A C   1 
ATOM   3129 O  O   . LEU   A 1 420 ? 16.83615  13.86866  82.53075  1.000 16.87450 ? 423  LEU   A O   1 
ATOM   3130 C  CB  . LEU   A 1 420 ? 18.87862  11.28581  82.82899  1.000 13.91558 ? 423  LEU   A CB  1 
ATOM   3131 C  CG  . LEU   A 1 420 ? 19.69191  12.43574  83.46266  1.000 17.49538 ? 423  LEU   A CG  1 
ATOM   3132 C  CD1 . LEU   A 1 420 ? 19.11818  12.79435  84.83152  1.000 17.95250 ? 423  LEU   A CD1 1 
ATOM   3133 C  CD2 . LEU   A 1 420 ? 21.21098  12.06278  83.60456  1.000 14.42440 ? 423  LEU   A CD2 1 
ATOM   3134 N  N   . ALA   A 1 421 ? 17.10897  12.78893  80.58578  1.000 15.20634 ? 424  ALA   A N   1 
ATOM   3135 C  CA  . ALA   A 1 421 ? 16.78458  13.98676  79.80164  1.000 14.85143 ? 424  ALA   A CA  1 
ATOM   3136 C  C   . ALA   A 1 421 ? 15.36287  14.44807  80.06348  1.000 21.00667 ? 424  ALA   A C   1 
ATOM   3137 O  O   . ALA   A 1 421 ? 15.10396  15.64590  80.23978  1.000 18.26247 ? 424  ALA   A O   1 
ATOM   3138 C  CB  . ALA   A 1 421 ? 16.93828  13.72417  78.28965  1.000 13.57066 ? 424  ALA   A CB  1 
ATOM   3139 N  N   . PHE   A 1 422 ? 14.41107  13.51820  80.01442  1.000 18.93275 ? 425  PHE   A N   1 
ATOM   3140 C  CA  . PHE   A 1 422 ? 13.02310  13.89977  80.26346  1.000 19.16534 ? 425  PHE   A CA  1 
ATOM   3141 C  C   . PHE   A 1 422 ? 12.85118  14.44150  81.68129  1.000 17.13065 ? 425  PHE   A C   1 
ATOM   3142 O  O   . PHE   A 1 422 ? 12.16603  15.44868  81.89806  1.000 16.31177 ? 425  PHE   A O   1 
ATOM   3143 C  CB  . PHE   A 1 422 ? 12.10512  12.68881  80.02253  1.000 18.74920 ? 425  PHE   A CB  1 
ATOM   3144 C  CG  . PHE   A 1 422 ? 10.65778  13.06788  79.94890  1.000 13.44907 ? 425  PHE   A CG  1 
ATOM   3145 C  CD1 . PHE   A 1 422 ? 9.93258   13.31976  81.11687  1.000 20.05174 ? 425  PHE   A CD1 1 
ATOM   3146 C  CD2 . PHE   A 1 422 ? 10.03801  13.23381  78.72074  1.000 15.85023 ? 425  PHE   A CD2 1 
ATOM   3147 C  CE1 . PHE   A 1 422 ? 8.62484   13.72765  81.06263  1.000 20.62423 ? 425  PHE   A CE1 1 
ATOM   3148 C  CE2 . PHE   A 1 422 ? 8.69525   13.65106  78.66410  1.000 19.01441 ? 425  PHE   A CE2 1 
ATOM   3149 C  CZ  . PHE   A 1 422 ? 8.00519   13.89906  79.81142  1.000 19.31665 ? 425  PHE   A CZ  1 
ATOM   3150 N  N   . TYR   A 1 423 ? 13.46288  13.78433  82.66908  1.000 18.58848 ? 426  TYR   A N   1 
ATOM   3151 C  CA  . TYR   A 1 423 ? 13.30837  14.23897  84.05579  1.000 16.38055 ? 426  TYR   A CA  1 
ATOM   3152 C  C   . TYR   A 1 423 ? 13.94737  15.60669  84.28062  1.000 21.92022 ? 426  TYR   A C   1 
ATOM   3153 O  O   . TYR   A 1 423 ? 13.39834  16.44558  85.00489  1.000 18.65818 ? 426  TYR   A O   1 
ATOM   3154 C  CB  . TYR   A 1 423 ? 13.93021  13.23215  85.01870  1.000 16.23169 ? 426  TYR   A CB  1 
ATOM   3155 C  CG  . TYR   A 1 423 ? 13.50825  13.48378  86.44691  1.000 21.39197 ? 426  TYR   A CG  1 
ATOM   3156 C  CD1 . TYR   A 1 423 ? 12.34791  12.91240  86.94153  1.000 20.44087 ? 426  TYR   A CD1 1 
ATOM   3157 C  CD2 . TYR   A 1 423 ? 14.26263  14.29154  87.29806  1.000 19.18252 ? 426  TYR   A CD2 1 
ATOM   3158 C  CE1 . TYR   A 1 423 ? 11.93500  13.13503  88.26925  1.000 25.36600 ? 426  TYR   A CE1 1 
ATOM   3159 C  CE2 . TYR   A 1 423 ? 13.85185  14.53055  88.61775  1.000 26.46184 ? 426  TYR   A CE2 1 
ATOM   3160 C  CZ  . TYR   A 1 423 ? 12.69438  13.93524  89.08106  1.000 29.01021 ? 426  TYR   A CZ  1 
ATOM   3161 O  OH  . TYR   A 1 423 ? 12.26999  14.15454  90.36698  1.000 35.21557 ? 426  TYR   A OH  1 
ATOM   3162 N  N   . ARG   A 1 424 ? 15.12046  15.85452  83.70820  1.000 18.34234 ? 427  ARG   A N   1 
ATOM   3163 C  CA  . ARG   A 1 424 ? 15.76857  17.13173  84.04183  1.000 21.46655 ? 427  ARG   A CA  1 
ATOM   3164 C  C   . ARG   A 1 424 ? 15.06280  18.29546  83.36437  1.000 22.99599 ? 427  ARG   A C   1 
ATOM   3165 O  O   . ARG   A 1 424 ? 15.10218  19.42579  83.86002  1.000 22.19637 ? 427  ARG   A O   1 
ATOM   3166 C  CB  . ARG   A 1 424 ? 17.24334  17.09441  83.65799  1.000 22.06229 ? 427  ARG   A CB  1 
ATOM   3167 C  CG  . ARG   A 1 424 ? 17.51087  17.15574  82.13623  1.000 19.69374 ? 427  ARG   A CG  1 
ATOM   3168 C  CD  . ARG   A 1 424 ? 18.97475  16.73449  81.82332  1.000 23.73747 ? 427  ARG   A CD  1 
ATOM   3169 N  NE  . ARG   A 1 424 ? 19.96555  17.51861  82.56130  1.000 21.93203 ? 427  ARG   A NE  1 
ATOM   3170 C  CZ  . ARG   A 1 424 ? 21.15319  17.04691  82.92426  1.000 31.38293 ? 427  ARG   A CZ  1 
ATOM   3171 N  NH1 . ARG   A 1 424 ? 21.53657  15.82156  82.60728  1.000 19.94162 ? 427  ARG   A NH1 1 
ATOM   3172 N  NH2 . ARG   A 1 424 ? 21.97576  17.81909  83.62431  1.000 26.39693 ? 427  ARG   A NH2 1 
ATOM   3173 N  N   . LEU   A 1 425 ? 14.36731  18.02992  82.27742  1.000 18.59627 ? 428  LEU   A N   1 
ATOM   3174 C  CA  . LEU   A 1 425 ? 13.59913  19.06093  81.59031  1.000 20.46381 ? 428  LEU   A CA  1 
ATOM   3175 C  C   . LEU   A 1 425 ? 12.19441  19.21541  82.17000  1.000 23.36469 ? 428  LEU   A C   1 
ATOM   3176 O  O   . LEU   A 1 425 ? 11.72900  20.33856  82.41361  1.000 21.40217 ? 428  LEU   A O   1 
ATOM   3177 C  CB  . LEU   A 1 425 ? 13.53756  18.72752  80.08903  1.000 19.74967 ? 428  LEU   A CB  1 
ATOM   3178 C  CG  . LEU   A 1 425 ? 12.94560  19.79738  79.16287  1.000 28.81750 ? 428  LEU   A CG  1 
ATOM   3179 C  CD1 . LEU   A 1 425 ? 13.68291  21.13309  79.26115  1.000 26.69923 ? 428  LEU   A CD1 1 
ATOM   3180 C  CD2 . LEU   A 1 425 ? 12.95385  19.25759  77.70895  1.000 22.86324 ? 428  LEU   A CD2 1 
ATOM   3181 N  N   . HIS   A 1 426 ? 11.51643  18.11052  82.45424  1.000 21.04666 ? 429  HIS   A N   1 
ATOM   3182 C  CA  . HIS   A 1 426 ? 10.11174  18.16702  82.82551  1.000 21.44830 ? 429  HIS   A CA  1 
ATOM   3183 C  C   . HIS   A 1 426 ? 9.84518   17.84737  84.28420  1.000 26.95790 ? 429  HIS   A C   1 
ATOM   3184 O  O   . HIS   A 1 426 ? 8.72348   18.06086  84.74209  1.000 24.84682 ? 429  HIS   A O   1 
ATOM   3185 C  CB  . HIS   A 1 426 ? 9.30860   17.22621  81.91492  1.000 20.74175 ? 429  HIS   A CB  1 
ATOM   3186 C  CG  . HIS   A 1 426 ? 9.33727   17.67208  80.48929  1.000 24.51822 ? 429  HIS   A CG  1 
ATOM   3187 N  ND1 . HIS   A 1 426 ? 8.84944   18.90269  80.09805  1.000 29.57322 ? 429  HIS   A ND1 1 
ATOM   3188 C  CD2 . HIS   A 1 426 ? 9.84210   17.09612  79.37905  1.000 18.34880 ? 429  HIS   A CD2 1 
ATOM   3189 C  CE1 . HIS   A 1 426 ? 9.03530   19.05113  78.79834  1.000 34.01216 ? 429  HIS   A CE1 1 
ATOM   3190 N  NE2 . HIS   A 1 426 ? 9.63604   17.96891  78.33678  1.000 22.01578 ? 429  HIS   A NE2 1 
ATOM   3191 N  N   . ARG   A 1 427 ? 10.84427  17.38524  85.02910  1.000 22.26353 ? 430  ARG   A N   1 
ATOM   3192 C  CA  . ARG   A 1 427 ? 10.79149  17.22725  86.48129  1.000 20.05057 ? 430  ARG   A CA  1 
ATOM   3193 C  C   . ARG   A 1 427 ? 9.84612   16.11335  86.91184  1.000 24.59040 ? 430  ARG   A C   1 
ATOM   3194 O  O   . ARG   A 1 427 ? 9.33331   16.12977  88.02835  1.000 23.61751 ? 430  ARG   A O   1 
ATOM   3195 C  CB  . ARG   A 1 427 ? 10.42587  18.54148  87.18909  1.000 28.33613 ? 430  ARG   A CB  1 
ATOM   3196 C  CG  . ARG   A 1 427 ? 11.12910  19.80025  86.63477  1.000 27.17733 ? 430  ARG   A CG  1 
ATOM   3197 C  CD  . ARG   A 1 427 ? 12.63668  19.59732  86.41532  1.000 39.96622 ? 430  ARG   A CD  1 
ATOM   3198 N  NE  . ARG   A 1 427 ? 13.36748  19.46307  87.67028  1.000 49.43880 ? 430  ARG   A NE  1 
ATOM   3199 C  CZ  . ARG   A 1 427 ? 14.68522  19.55044  87.79501  1.000 52.57139 ? 430  ARG   A CZ  1 
ATOM   3200 N  NH1 . ARG   A 1 427 ? 15.47133  19.73570  86.74406  1.000 39.46405 ? 430  ARG   A NH1 1 
ATOM   3201 N  NH2 . ARG   A 1 427 ? 15.22688  19.46252  89.00880  1.000 44.36510 ? 430  ARG   A NH2 1 
ATOM   3202 N  N   . ARG   A 1 428 ? 9.59585   15.15090  86.03225  1.000 23.16160 ? 431  ARG   A N   1 
ATOM   3203 C  CA  . ARG   A 1 428 ? 8.89031   13.91718  86.35728  1.000 20.58887 ? 431  ARG   A CA  1 
ATOM   3204 C  C   . ARG   A 1 428 ? 9.30058   12.89338  85.31424  1.000 19.14145 ? 431  ARG   A C   1 
ATOM   3205 O  O   . ARG   A 1 428 ? 9.78025   13.25487  84.23915  1.000 21.61664 ? 431  ARG   A O   1 
ATOM   3206 C  CB  . ARG   A 1 428 ? 7.36209   14.09921  86.34806  1.000 28.23376 ? 431  ARG   A CB  1 
ATOM   3207 C  CG  . ARG   A 1 428 ? 6.81492   14.46521  84.97957  1.000 26.51247 ? 431  ARG   A CG  1 
ATOM   3208 C  CD  . ARG   A 1 428 ? 5.27872   14.56028  84.97316  1.000 38.66890 ? 431  ARG   A CD  1 
ATOM   3209 N  NE  . ARG   A 1 428 ? 4.80143   14.85524  83.62598  1.000 39.68893 ? 431  ARG   A NE  1 
ATOM   3210 C  CZ  . ARG   A 1 428 ? 3.70263   14.34687  83.08563  1.000 57.02601 ? 431  ARG   A CZ  1 
ATOM   3211 N  NH1 . ARG   A 1 428 ? 2.89612   13.55914  83.77744  1.000 39.43405 ? 431  ARG   A NH1 1 
ATOM   3212 N  NH2 . ARG   A 1 428 ? 3.42164   14.61361  81.80944  1.000 41.35550 ? 431  ARG   A NH2 1 
ATOM   3213 N  N   . LEU   A 1 429 ? 9.10881   11.61373  85.63556  1.000 19.20239 ? 432  LEU   A N   1 
ATOM   3214 C  CA  . LEU   A 1 429 ? 9.12068   10.58541  84.60592  1.000 20.54200 ? 432  LEU   A CA  1 
ATOM   3215 C  C   . LEU   A 1 429 ? 7.68965   10.34697  84.13688  1.000 21.29161 ? 432  LEU   A C   1 
ATOM   3216 O  O   . LEU   A 1 429 ? 6.72950   10.69329  84.82099  1.000 18.20857 ? 432  LEU   A O   1 
ATOM   3217 C  CB  . LEU   A 1 429 ? 9.74220   9.27323   85.12554  1.000 21.25277 ? 432  LEU   A CB  1 
ATOM   3218 C  CG  . LEU   A 1 429 ? 11.23801  9.34741   85.49939  1.000 21.12624 ? 432  LEU   A CG  1 
ATOM   3219 C  CD1 . LEU   A 1 429 ? 11.83464  7.92587   85.72846  1.000 23.35738 ? 432  LEU   A CD1 1 
ATOM   3220 C  CD2 . LEU   A 1 429 ? 12.04564  10.08897  84.42821  1.000 19.43191 ? 432  LEU   A CD2 1 
ATOM   3221 N  N   . VAL   A 1 430 ? 7.55385   9.74215   82.96275  1.000 20.08432 ? 433  VAL   A N   1 
ATOM   3222 C  CA  . VAL   A 1 430 ? 6.23204   9.49807   82.37933  1.000 19.30225 ? 433  VAL   A CA  1 
ATOM   3223 C  C   . VAL   A 1 430 ? 6.21951   8.09040   81.81505  1.000 21.73114 ? 433  VAL   A C   1 
ATOM   3224 O  O   . VAL   A 1 430 ? 7.28161   7.52991   81.51054  1.000 18.87542 ? 433  VAL   A O   1 
ATOM   3225 C  CB  . VAL   A 1 430 ? 5.91337   10.50451  81.26246  1.000 21.20323 ? 433  VAL   A CB  1 
ATOM   3226 C  CG1 . VAL   A 1 430 ? 5.71504   11.92562  81.83269  1.000 24.46959 ? 433  VAL   A CG1 1 
ATOM   3227 C  CG2 . VAL   A 1 430 ? 7.05229   10.46285  80.17459  1.000 17.54426 ? 433  VAL   A CG2 1 
ATOM   3228 N  N   . PRO   A 1 431 ? 5.03218   7.50691   81.62735  1.000 19.85703 ? 434  PRO   A N   1 
ATOM   3229 C  CA  . PRO   A 1 431 ? 4.96118   6.23274   80.91165  1.000 18.89075 ? 434  PRO   A CA  1 
ATOM   3230 C  C   . PRO   A 1 431 ? 5.68396   6.33828   79.58282  1.000 18.71028 ? 434  PRO   A C   1 
ATOM   3231 O  O   . PRO   A 1 431 ? 5.40836   7.22763   78.76518  1.000 17.45855 ? 434  PRO   A O   1 
ATOM   3232 C  CB  . PRO   A 1 431 ? 3.44649   6.00303   80.72789  1.000 17.53326 ? 434  PRO   A CB  1 
ATOM   3233 C  CG  . PRO   A 1 431 ? 2.82749   6.73246   81.94053  1.000 20.62207 ? 434  PRO   A CG  1 
ATOM   3234 C  CD  . PRO   A 1 431 ? 3.68765   7.98540   82.04696  1.000 19.64610 ? 434  PRO   A CD  1 
ATOM   3235 N  N   . THR   A 1 432 ? 6.61931   5.42024   79.36702  1.000 18.88954 ? 435  THR   A N   1 
ATOM   3236 C  CA  . THR   A 1 432 ? 7.51977   5.46720   78.21742  1.000 15.84848 ? 435  THR   A CA  1 
ATOM   3237 C  C   . THR   A 1 432 ? 7.35962   4.17541   77.44382  1.000 18.42533 ? 435  THR   A C   1 
ATOM   3238 O  O   . THR   A 1 432 ? 7.19731   3.11281   78.03068  1.000 17.39799 ? 435  THR   A O   1 
ATOM   3239 C  CB  . THR   A 1 432 ? 8.98498   5.65604   78.67904  1.000 15.85435 ? 435  THR   A CB  1 
ATOM   3240 O  OG1 . THR   A 1 432 ? 9.05657   6.88688   79.40132  1.000 18.31044 ? 435  THR   A OG1 1 
ATOM   3241 C  CG2 . THR   A 1 432 ? 9.98858   5.69973   77.46326  1.000 14.91285 ? 435  THR   A CG2 1 
ATOM   3242 N  N   . TYR   A 1 433 ? 7.36347   4.28814   76.12908  1.000 15.66049 ? 436  TYR   A N   1 
ATOM   3243 C  CA  . TYR   A 1 433 ? 7.27192   3.15967   75.21166  1.000 15.91492 ? 436  TYR   A CA  1 
ATOM   3244 C  C   . TYR   A 1 433 ? 8.62921   2.95922   74.55990  1.000 18.90728 ? 436  TYR   A C   1 
ATOM   3245 O  O   . TYR   A 1 433 ? 9.25264   3.92966   74.11495  1.000 18.48978 ? 436  TYR   A O   1 
ATOM   3246 C  CB  . TYR   A 1 433 ? 6.21915   3.43597   74.13191  1.000 15.18061 ? 436  TYR   A CB  1 
ATOM   3247 C  CG  . TYR   A 1 433 ? 6.00516   2.30178   73.13496  1.000 21.15953 ? 436  TYR   A CG  1 
ATOM   3248 C  CD1 . TYR   A 1 433 ? 6.83042   2.15781   72.01228  1.000 21.48000 ? 436  TYR   A CD1 1 
ATOM   3249 C  CD2 . TYR   A 1 433 ? 4.98656   1.36169   73.33648  1.000 18.89332 ? 436  TYR   A CD2 1 
ATOM   3250 C  CE1 . TYR   A 1 433 ? 6.62255   1.12852   71.10198  1.000 22.03425 ? 436  TYR   A CE1 1 
ATOM   3251 C  CE2 . TYR   A 1 433 ? 4.76903   0.33016   72.43466  1.000 18.12505 ? 436  TYR   A CE2 1 
ATOM   3252 C  CZ  . TYR   A 1 433 ? 5.58128   0.22241   71.32666  1.000 21.77161 ? 436  TYR   A CZ  1 
ATOM   3253 O  OH  . TYR   A 1 433 ? 5.34390   -0.80995  70.45355  1.000 20.60695 ? 436  TYR   A OH  1 
ATOM   3254 N  N   . GLU   A 1 434 ? 9.08210   1.71403   74.49817  1.000 18.61128 ? 437  GLU   A N   1 
ATOM   3255 C  CA  . GLU   A 1 434 ? 10.22501  1.34208   73.66617  1.000 15.26227 ? 437  GLU   A CA  1 
ATOM   3256 C  C   . GLU   A 1 434 ? 9.87880   0.04118   72.95931  1.000 20.10420 ? 437  GLU   A C   1 
ATOM   3257 O  O   . GLU   A 1 434 ? 9.57947   -0.95923  73.61828  1.000 16.04927 ? 437  GLU   A O   1 
ATOM   3258 C  CB  . GLU   A 1 434 ? 11.53053  1.15497   74.47665  1.000 15.57688 ? 437  GLU   A CB  1 
ATOM   3259 C  CG  . GLU   A 1 434 ? 12.66476  0.77410   73.52863  1.000 16.29895 ? 437  GLU   A CG  1 
ATOM   3260 C  CD  . GLU   A 1 434 ? 13.96250  0.33679   74.18197  1.000 24.91996 ? 437  GLU   A CD  1 
ATOM   3261 O  OE1 . GLU   A 1 434 ? 14.05040  0.18471   75.41736  1.000 19.20371 ? 437  GLU   A OE1 1 
ATOM   3262 O  OE2 . GLU   A 1 434 ? 14.93388  0.16529   73.41500  1.000 22.48467 ? 437  GLU   A OE2 1 
ATOM   3263 N  N   . SER   A 1 435 ? 9.94462   0.05675   71.62633  1.000 16.71690 ? 438  SER   A N   1 
ATOM   3264 C  CA  . SER   A 1 435 ? 9.68751   -1.12858  70.81541  1.000 18.98907 ? 438  SER   A CA  1 
ATOM   3265 C  C   . SER   A 1 435 ? 10.62767  -2.25737  71.18574  1.000 21.02239 ? 438  SER   A C   1 
ATOM   3266 O  O   . SER   A 1 435 ? 11.84433  -2.06619  71.23394  1.000 21.46385 ? 438  SER   A O   1 
ATOM   3267 C  CB  . SER   A 1 435 ? 9.88344   -0.79468  69.32335  1.000 21.24378 ? 438  SER   A CB  1 
ATOM   3268 O  OG  . SER   A 1 435 ? 9.07196   0.29009   68.93831  1.000 35.57830 ? 438  SER   A OG  1 
ATOM   3269 N  N   . ALA   A 1 436 ? 10.07217  -3.45103  71.40338  1.000 15.76386 ? 439  ALA   A N   1 
ATOM   3270 C  CA  . ALA   A 1 436 ? 10.87495  -4.65718  71.63075  1.000 15.26757 ? 439  ALA   A CA  1 
ATOM   3271 C  C   . ALA   A 1 436 ? 10.39238  -5.71488  70.66161  1.000 25.10363 ? 439  ALA   A C   1 
ATOM   3272 O  O   . ALA   A 1 436 ? 9.20908   -6.05887  70.67877  1.000 22.54381 ? 439  ALA   A O   1 
ATOM   3273 C  CB  . ALA   A 1 436 ? 10.71841  -5.17767  73.05712  1.000 19.03230 ? 439  ALA   A CB  1 
ATOM   3274 N  N   . SER   A 1 437 ? 11.28930  -6.24556  69.83627  1.000 18.70776 ? 440  SER   A N   1 
ATOM   3275 C  CA  . SER   A 1 437 ? 10.85106  -7.22612  68.84210  1.000 18.23702 ? 440  SER   A CA  1 
ATOM   3276 C  C   . SER   A 1 437 ? 10.56134  -8.58498  69.47624  1.000 22.85202 ? 440  SER   A C   1 
ATOM   3277 O  O   . SER   A 1 437 ? 11.38604  -9.11082  70.22934  1.000 19.50976 ? 440  SER   A O   1 
ATOM   3278 C  CB  . SER   A 1 437 ? 11.90961  -7.38308  67.76460  1.000 23.15853 ? 440  SER   A CB  1 
ATOM   3279 O  OG  . SER   A 1 437 ? 11.63656  -8.55516  67.00626  1.000 20.56953 ? 440  SER   A OG  1 
ATOM   3280 N  N   . ILE   A 1 438 ? 9.40546   -9.17377  69.13382  1.000 19.19825 ? 441  ILE   A N   1 
ATOM   3281 C  CA  . ILE   A 1 438 ? 9.07652   -10.54586 69.52925  1.000 18.32434 ? 441  ILE   A CA  1 
ATOM   3282 C  C   . ILE   A 1 438 ? 9.03614   -11.46352 68.30769  1.000 17.45212 ? 441  ILE   A C   1 
ATOM   3283 O  O   . ILE   A 1 438 ? 8.27882   -12.44286 68.27191  1.000 17.27172 ? 441  ILE   A O   1 
ATOM   3284 C  CB  . ILE   A 1 438 ? 7.75463   -10.60029 70.32474  1.000 18.53486 ? 441  ILE   A CB  1 
ATOM   3285 C  CG1 . ILE   A 1 438 ? 6.65709   -9.77931  69.62368  1.000 16.90015 ? 441  ILE   A CG1 1 
ATOM   3286 C  CG2 . ILE   A 1 438 ? 7.98661   -10.03356 71.73056  1.000 20.11721 ? 441  ILE   A CG2 1 
ATOM   3287 C  CD1 . ILE   A 1 438 ? 5.21701   -10.04036 70.18468  1.000 17.11127 ? 441  ILE   A CD1 1 
ATOM   3288 N  N   . ARG   A 1 439 ? 9.90544   -11.19114 67.32486  1.000 20.10619 ? 442  ARG   A N   1 
ATOM   3289 C  CA  . ARG   A 1 439 ? 10.05032  -12.03503 66.13456  1.000 22.29539 ? 442  ARG   A CA  1 
ATOM   3290 C  C   . ARG   A 1 439 ? 10.59040  -13.42022 66.44327  1.000 23.11291 ? 442  ARG   A C   1 
ATOM   3291 O  O   . ARG   A 1 439 ? 10.63933  -14.26188 65.54361  1.000 24.50867 ? 442  ARG   A O   1 
ATOM   3292 C  CB  . ARG   A 1 439 ? 10.98560  -11.36393 65.11069  1.000 18.94034 ? 442  ARG   A CB  1 
ATOM   3293 C  CG  . ARG   A 1 439 ? 10.29128  -10.27878 64.30373  1.000 18.23626 ? 442  ARG   A CG  1 
ATOM   3294 C  CD  . ARG   A 1 439 ? 11.24802  -9.63195  63.35443  1.000 24.10173 ? 442  ARG   A CD  1 
ATOM   3295 N  NE  . ARG   A 1 439 ? 11.73337  -10.55744 62.34432  1.000 26.47005 ? 442  ARG   A NE  1 
ATOM   3296 C  CZ  . ARG   A 1 439 ? 12.88495  -10.42690 61.70564  1.000 25.33503 ? 442  ARG   A CZ  1 
ATOM   3297 N  NH1 . ARG   A 1 439 ? 13.74376  -9.46215  62.01256  1.000 24.54310 ? 442  ARG   A NH1 1 
ATOM   3298 N  NH2 . ARG   A 1 439 ? 13.17785  -11.27480 60.72602  1.000 26.53858 ? 442  ARG   A NH2 1 
ATOM   3299 N  N   . ARG   A 1 440 ? 11.01887  -13.68578 67.67310  1.000 19.55947 ? 443  ARG   A N   1 
ATOM   3300 C  CA  . ARG   A 1 440 ? 11.33389  -15.06670 68.03212  1.000 19.54248 ? 443  ARG   A CA  1 
ATOM   3301 C  C   . ARG   A 1 440 ? 10.12920  -15.99219 67.87841  1.000 19.50480 ? 443  ARG   A C   1 
ATOM   3302 O  O   . ARG   A 1 440 ? 10.30254  -17.21170 67.77096  1.000 21.11542 ? 443  ARG   A O   1 
ATOM   3303 C  CB  . ARG   A 1 440 ? 11.83490  -15.12847 69.48793  1.000 20.88160 ? 443  ARG   A CB  1 
ATOM   3304 C  CG  . ARG   A 1 440 ? 13.28131  -14.67288 69.71386  1.000 28.33556 ? 443  ARG   A CG  1 
ATOM   3305 C  CD  . ARG   A 1 440 ? 13.57340  -14.50902 71.23100  1.000 28.29540 ? 443  ARG   A CD  1 
ATOM   3306 N  NE  . ARG   A 1 440 ? 14.98284  -14.22421 71.49773  1.000 31.80478 ? 443  ARG   A NE  1 
ATOM   3307 C  CZ  . ARG   A 1 440 ? 15.55475  -13.04936 71.26660  1.000 36.31148 ? 443  ARG   A CZ  1 
ATOM   3308 N  NH1 . ARG   A 1 440 ? 14.86009  -12.02038 70.79656  1.000 32.25298 ? 443  ARG   A NH1 1 
ATOM   3309 N  NH2 . ARG   A 1 440 ? 16.85468  -12.90059 71.50504  1.000 37.73376 ? 443  ARG   A NH2 1 
ATOM   3310 N  N   . PHE   A 1 441 ? 8.91516   -15.44647 67.89920  1.000 20.73979 ? 444  PHE   A N   1 
ATOM   3311 C  CA  . PHE   A 1 441 ? 7.68284   -16.22163 67.96167  1.000 20.52640 ? 444  PHE   A CA  1 
ATOM   3312 C  C   . PHE   A 1 441 ? 6.90733   -16.05818 66.66353  1.000 22.48950 ? 444  PHE   A C   1 
ATOM   3313 O  O   . PHE   A 1 441 ? 7.06577   -15.06424 65.95269  1.000 21.95142 ? 444  PHE   A O   1 
ATOM   3314 C  CB  . PHE   A 1 441 ? 6.86125   -15.76522 69.17863  1.000 18.21697 ? 444  PHE   A CB  1 
ATOM   3315 C  CG  . PHE   A 1 441 ? 7.66954   -15.80095 70.44733  1.000 18.29779 ? 444  PHE   A CG  1 
ATOM   3316 C  CD1 . PHE   A 1 441 ? 7.99265   -17.02126 71.01323  1.000 20.08380 ? 444  PHE   A CD1 1 
ATOM   3317 C  CD2 . PHE   A 1 441 ? 8.13114   -14.63933 71.03660  1.000 20.26172 ? 444  PHE   A CD2 1 
ATOM   3318 C  CE1 . PHE   A 1 441 ? 8.79469   -17.08464 72.14968  1.000 24.12836 ? 444  PHE   A CE1 1 
ATOM   3319 C  CE2 . PHE   A 1 441 ? 8.92929   -14.69926 72.18009  1.000 21.37779 ? 444  PHE   A CE2 1 
ATOM   3320 C  CZ  . PHE   A 1 441 ? 9.24732   -15.93041 72.72388  1.000 23.01810 ? 444  PHE   A CZ  1 
ATOM   3321 N  N   . GLN   A 1 442 ? 6.07310   -17.04847 66.35709  1.000 21.81683 ? 445  GLN   A N   1 
ATOM   3322 C  CA  . GLN   A 1 442 ? 5.25037   -17.00327 65.14354  1.000 18.65396 ? 445  GLN   A CA  1 
ATOM   3323 C  C   . GLN   A 1 442 ? 4.47829   -15.69153 65.03314  1.000 23.74885 ? 445  GLN   A C   1 
ATOM   3324 O  O   . GLN   A 1 442 ? 3.82367   -15.25495 65.99031  1.000 22.28149 ? 445  GLN   A O   1 
ATOM   3325 C  CB  . GLN   A 1 442 ? 4.27118   -18.18202 65.14694  1.000 18.94276 ? 445  GLN   A CB  1 
ATOM   3326 C  CG  . GLN   A 1 442 ? 4.89040   -19.52322 65.06611  1.000 28.18807 ? 445  GLN   A CG  1 
ATOM   3327 C  CD  . GLN   A 1 442 ? 3.84307   -20.60751 64.90862  1.000 35.44483 ? 445  GLN   A CD  1 
ATOM   3328 O  OE1 . GLN   A 1 442 ? 2.76221   -20.36918 64.35834  1.000 28.66099 ? 445  GLN   A OE1 1 
ATOM   3329 N  NE2 . GLN   A 1 442 ? 4.15090   -21.80320 65.40384  1.000 27.96101 ? 445  GLN   A NE2 1 
ATOM   3330 N  N   . GLU   A 1 443 ? 4.53782   -15.07280 63.84050  1.000 21.18117 ? 446  GLU   A N   1 
ATOM   3331 C  CA  . GLU   A 1 443 ? 3.87237   -13.81706 63.50417  1.000 17.33585 ? 446  GLU   A CA  1 
ATOM   3332 C  C   . GLU   A 1 443 ? 4.28036   -12.67579 64.42065  1.000 17.82356 ? 446  GLU   A C   1 
ATOM   3333 O  O   . GLU   A 1 443 ? 3.60382   -11.63629 64.44607  1.000 18.39090 ? 446  GLU   A O   1 
ATOM   3334 C  CB  . GLU   A 1 443 ? 2.33334   -13.94506 63.51328  1.000 23.71007 ? 446  GLU   A CB  1 
ATOM   3335 C  CG  . GLU   A 1 443 ? 1.76447   -14.96221 62.56576  1.000 33.25950 ? 446  GLU   A CG  1 
ATOM   3336 C  CD  . GLU   A 1 443 ? 0.21465   -14.99577 62.58262  1.000 45.28853 ? 446  GLU   A CD  1 
ATOM   3337 O  OE1 . GLU   A 1 443 ? -0.45941  -14.20655 63.31729  1.000 42.50814 ? 446  GLU   A OE1 1 
ATOM   3338 O  OE2 . GLU   A 1 443 ? -0.32982  -15.83546 61.85629  1.000 44.19555 ? 446  GLU   A OE2 1 
ATOM   3339 N  N   . GLY   A 1 444 ? 5.37713   -12.83485 65.16934  1.000 20.05689 ? 447  GLY   A N   1 
ATOM   3340 C  CA  . GLY   A 1 444 ? 5.69373   -11.89021 66.21605  1.000 20.50450 ? 447  GLY   A CA  1 
ATOM   3341 C  C   . GLY   A 1 444 ? 5.98453   -10.50433 65.68632  1.000 20.44175 ? 447  GLY   A C   1 
ATOM   3342 O  O   . GLY   A 1 444 ? 6.74042   -10.36063 64.71941  1.000 20.09835 ? 447  GLY   A O   1 
ATOM   3343 N  N   . ARG   A 1 445 ? 5.39348   -9.47589  66.31378  1.000 18.60535 ? 448  ARG   A N   1 
ATOM   3344 C  CA  . ARG   A 1 445 ? 5.67015   -8.09878  65.95591  1.000 18.40453 ? 448  ARG   A CA  1 
ATOM   3345 C  C   . ARG   A 1 445 ? 6.48080   -7.48997  67.08635  1.000 16.58774 ? 448  ARG   A C   1 
ATOM   3346 O  O   . ARG   A 1 445 ? 7.71939   -7.70816  67.14335  1.000 17.48908 ? 448  ARG   A O   1 
ATOM   3347 C  CB  . ARG   A 1 445 ? 4.36546   -7.36891  65.60958  1.000 16.11198 ? 448  ARG   A CB  1 
ATOM   3348 C  CG  . ARG   A 1 445 ? 3.73603   -7.93917  64.33014  1.000 18.49104 ? 448  ARG   A CG  1 
ATOM   3349 C  CD  . ARG   A 1 445 ? 4.54892   -7.54755  63.06184  1.000 18.63945 ? 448  ARG   A CD  1 
ATOM   3350 N  NE  . ARG   A 1 445 ? 4.63408   -6.09235  62.93476  1.000 20.67762 ? 448  ARG   A NE  1 
ATOM   3351 C  CZ  . ARG   A 1 445 ? 3.75207   -5.34794  62.27536  1.000 25.22391 ? 448  ARG   A CZ  1 
ATOM   3352 N  NH1 . ARG   A 1 445 ? 2.70590   -5.88640  61.65453  1.000 22.31871 ? 448  ARG   A NH1 1 
ATOM   3353 N  NH2 . ARG   A 1 445 ? 3.91633   -4.03220  62.24017  1.000 19.66962 ? 448  ARG   A NH2 1 
ATOM   3354 N  N   . VAL   A 1 446 ? 5.86715   -6.72191  68.00885  1.000 14.66886 ? 449  VAL   A N   1 
ATOM   3355 C  CA  . VAL   A 1 446 ? 6.59103   -6.06590  69.09584  1.000 17.89694 ? 449  VAL   A CA  1 
ATOM   3356 C  C   . VAL   A 1 446 ? 5.78507   -6.18249  70.38597  1.000 24.42369 ? 449  VAL   A C   1 
ATOM   3357 O  O   . VAL   A 1 446 ? 4.57323   -6.40059  70.37731  1.000 20.92694 ? 449  VAL   A O   1 
ATOM   3358 C  CB  . VAL   A 1 446 ? 6.89352   -4.56293  68.81852  1.000 27.76276 ? 449  VAL   A CB  1 
ATOM   3359 C  CG1 . VAL   A 1 446 ? 7.86827   -4.36015  67.63823  1.000 21.78666 ? 449  VAL   A CG1 1 
ATOM   3360 C  CG2 . VAL   A 1 446 ? 5.63431   -3.81501  68.54600  1.000 30.56857 ? 449  VAL   A CG2 1 
ATOM   3361 N  N   . ASP   A 1 447 ? 6.48608   -6.06158  71.50538  1.000 18.29499 ? 450  ASP   A N   1 
ATOM   3362 C  CA  . ASP   A 1 447 ? 5.87669   -5.73180  72.79488  1.000 21.85731 ? 450  ASP   A CA  1 
ATOM   3363 C  C   . ASP   A 1 447 ? 6.58324   -4.47614  73.31251  1.000 18.80778 ? 450  ASP   A C   1 
ATOM   3364 O  O   . ASP   A 1 447 ? 7.42068   -3.90061  72.61886  1.000 21.66963 ? 450  ASP   A O   1 
ATOM   3365 C  CB  . ASP   A 1 447 ? 5.96892   -6.92518  73.75620  1.000 23.58599 ? 450  ASP   A CB  1 
ATOM   3366 C  CG  . ASP   A 1 447 ? 4.87819   -6.89937  74.85836  1.000 27.18822 ? 450  ASP   A CG  1 
ATOM   3367 O  OD1 . ASP   A 1 447 ? 4.17083   -5.88827  75.03792  1.000 20.22192 ? 450  ASP   A OD1 1 
ATOM   3368 O  OD2 . ASP   A 1 447 ? 4.74189   -7.90272  75.55961  1.000 21.57402 ? 450  ASP   A OD2 1 
ATOM   3369 N  N   . ASN   A 1 448 ? 6.22131   -4.01939  74.50859  1.000 20.29445 ? 451  ASN   A N   1 
ATOM   3370 C  CA  . ASN   A 1 448 ? 6.68807   -2.74499  75.05333  1.000 17.15689 ? 451  ASN   A CA  1 
ATOM   3371 C  C   . ASN   A 1 448 ? 7.71228   -2.98476  76.16046  1.000 17.47868 ? 451  ASN   A C   1 
ATOM   3372 O  O   . ASN   A 1 448 ? 7.44301   -3.74784  77.08073  1.000 16.66530 ? 451  ASN   A O   1 
ATOM   3373 C  CB  . ASN   A 1 448 ? 5.51071   -1.95209  75.63828  1.000 16.47982 ? 451  ASN   A CB  1 
ATOM   3374 C  CG  . ASN   A 1 448 ? 5.89681   -0.55530  76.04552  1.000 19.22308 ? 451  ASN   A CG  1 
ATOM   3375 O  OD1 . ASN   A 1 448 ? 6.89951   -0.01656  75.57696  1.000 16.46506 ? 451  ASN   A OD1 1 
ATOM   3376 N  ND2 . ASN   A 1 448 ? 5.08006   0.06492   76.86788  1.000 18.74206 ? 451  ASN   A ND2 1 
ATOM   3377 N  N   . ILE   A 1 449 ? 8.84875   -2.29373  76.09397  1.000 18.11907 ? 452  ILE   A N   1 
ATOM   3378 C  CA  . ILE   A 1 449 ? 9.78359   -2.18127  77.22143  1.000 16.71062 ? 452  ILE   A CA  1 
ATOM   3379 C  C   . ILE   A 1 449 ? 9.42875   -0.89924  77.97357  1.000 16.73050 ? 452  ILE   A C   1 
ATOM   3380 O  O   . ILE   A 1 449 ? 9.45205   0.18763   77.38795  1.000 17.78780 ? 452  ILE   A O   1 
ATOM   3381 C  CB  . ILE   A 1 449 ? 11.24099  -2.13968  76.72616  1.000 18.86039 ? 452  ILE   A CB  1 
ATOM   3382 C  CG1 . ILE   A 1 449 ? 11.63981  -3.46574  76.08028  1.000 13.38530 ? 452  ILE   A CG1 1 
ATOM   3383 C  CG2 . ILE   A 1 449 ? 12.22961  -1.76228  77.88607  1.000 17.22089 ? 452  ILE   A CG2 1 
ATOM   3384 C  CD1 . ILE   A 1 449 ? 12.86836  -3.31965  75.15085  1.000 17.79611 ? 452  ILE   A CD1 1 
ATOM   3385 N  N   . ARG   A 1 450 ? 9.05969   -1.01220  79.25775  1.000 15.76963 ? 453  ARG   A N   1 
ATOM   3386 C  CA  . ARG   A 1 450 ? 8.62692   0.16107   80.01496  1.000 15.03089 ? 453  ARG   A CA  1 
ATOM   3387 C  C   . ARG   A 1 450 ? 9.85162   0.77732   80.68962  1.000 20.26347 ? 453  ARG   A C   1 
ATOM   3388 O  O   . ARG   A 1 450 ? 10.18755  0.45118   81.82322  1.000 18.27764 ? 453  ARG   A O   1 
ATOM   3389 C  CB  . ARG   A 1 450 ? 7.54156   -0.21215  81.01913  1.000 15.59486 ? 453  ARG   A CB  1 
ATOM   3390 C  CG  . ARG   A 1 450 ? 6.17740   -0.38688  80.29159  1.000 20.55483 ? 453  ARG   A CG  1 
ATOM   3391 C  CD  . ARG   A 1 450 ? 5.02272   -0.75566  81.22728  1.000 20.35790 ? 453  ARG   A CD  1 
ATOM   3392 N  NE  . ARG   A 1 450 ? 3.79428   -0.72218  80.43913  1.000 19.86351 ? 453  ARG   A NE  1 
ATOM   3393 C  CZ  . ARG   A 1 450 ? 3.00645   0.33519   80.32488  1.000 20.95342 ? 453  ARG   A CZ  1 
ATOM   3394 N  NH1 . ARG   A 1 450 ? 3.24539   1.46166   80.99764  1.000 16.36839 ? 453  ARG   A NH1 1 
ATOM   3395 N  NH2 . ARG   A 1 450 ? 1.94914   0.26956   79.51249  1.000 19.32585 ? 453  ARG   A NH2 1 
ATOM   3396 N  N   . SER   A 1 451 ? 10.52188  1.69563   79.98125  1.000 16.19155 ? 454  SER   A N   1 
ATOM   3397 C  CA  . SER   A 1 451 ? 11.81750  2.21454   80.44274  1.000 16.28924 ? 454  SER   A CA  1 
ATOM   3398 C  C   . SER   A 1 451 ? 11.72645  3.16109   81.63954  1.000 13.19451 ? 454  SER   A C   1 
ATOM   3399 O  O   . SER   A 1 451 ? 12.77691  3.48742   82.23033  1.000 17.47572 ? 454  SER   A O   1 
ATOM   3400 C  CB  . SER   A 1 451 ? 12.51230  2.94378   79.27903  1.000 19.04088 ? 454  SER   A CB  1 
ATOM   3401 O  OG  . SER   A 1 451 ? 12.59062  2.08462   78.14490  1.000 20.82296 ? 454  SER   A OG  1 
ATOM   3402 N  N   . ALA   A 1 452 ? 10.53484  3.61320   82.02511  1.000 16.04549 ? 455  ALA   A N   1 
ATOM   3403 C  CA  . ALA   A 1 452 ? 10.41270  4.48680   83.20212  1.000 16.91195 ? 455  ALA   A CA  1 
ATOM   3404 C  C   . ALA   A 1 452 ? 10.34029  3.61543   84.46135  1.000 18.83974 ? 455  ALA   A C   1 
ATOM   3405 O  O   . ALA   A 1 452 ? 9.31907   3.51495   85.14447  1.000 19.22589 ? 455  ALA   A O   1 
ATOM   3406 C  CB  . ALA   A 1 452 ? 9.20223   5.41387   83.07546  1.000 20.49981 ? 455  ALA   A CB  1 
ATOM   3407 N  N   . THR   A 1 453 ? 11.46510  2.97644   84.77129  1.000 15.82894 ? 456  THR   A N   1 
ATOM   3408 C  CA  . THR   A 1 453 ? 11.50391  2.00996   85.86781  1.000 19.88662 ? 456  THR   A CA  1 
ATOM   3409 C  C   . THR   A 1 453 ? 11.65016  2.72196   87.21635  1.000 19.02783 ? 456  THR   A C   1 
ATOM   3410 O  O   . THR   A 1 453 ? 12.03336  3.89631   87.27877  1.000 19.07074 ? 456  THR   A O   1 
ATOM   3411 C  CB  . THR   A 1 453 ? 12.69347  1.06310   85.68316  1.000 15.99472 ? 456  THR   A CB  1 
ATOM   3412 O  OG1 . THR   A 1 453 ? 13.89534  1.84987   85.76553  1.000 18.00325 ? 456  THR   A OG1 1 
ATOM   3413 C  CG2 . THR   A 1 453 ? 12.65321  0.36822   84.30249  1.000 18.57245 ? 456  THR   A CG2 1 
ATOM   3414 N  N   . PRO   A 1 454 ? 11.36502  2.02231   88.31215  1.000 19.48543 ? 457  PRO   A N   1 
ATOM   3415 C  CA  . PRO   A 1 454 ? 11.68240  2.57513   89.63450  1.000 19.43571 ? 457  PRO   A CA  1 
ATOM   3416 C  C   . PRO   A 1 454 ? 13.15719  2.88783   89.78910  1.000 21.63678 ? 457  PRO   A C   1 
ATOM   3417 O  O   . PRO   A 1 454 ? 13.51743  3.87127   90.44047  1.000 20.48541 ? 457  PRO   A O   1 
ATOM   3418 C  CB  . PRO   A 1 454 ? 11.23544  1.45616   90.58883  1.000 25.52758 ? 457  PRO   A CB  1 
ATOM   3419 C  CG  . PRO   A 1 454 ? 10.18095  0.71146   89.81140  1.000 26.12254 ? 457  PRO   A CG  1 
ATOM   3420 C  CD  . PRO   A 1 454 ? 10.64623  0.72915   88.39978  1.000 22.14663 ? 457  PRO   A CD  1 
ATOM   3421 N  N   . GLU   A 1 455 ? 14.02453  2.07327   89.18801  1.000 18.93069 ? 458  GLU   A N   1 
ATOM   3422 C  CA  . GLU   A 1 455 ? 15.46434  2.32470   89.27352  1.000 18.96642 ? 458  GLU   A CA  1 
ATOM   3423 C  C   . GLU   A 1 455 ? 15.85123  3.57516   88.49832  1.000 19.06531 ? 458  GLU   A C   1 
ATOM   3424 O  O   . GLU   A 1 455 ? 16.70487  4.35616   88.94063  1.000 17.44098 ? 458  GLU   A O   1 
ATOM   3425 C  CB  . GLU   A 1 455 ? 16.21736  1.11079   88.75066  1.000 15.38402 ? 458  GLU   A CB  1 
ATOM   3426 C  CG  . GLU   A 1 455 ? 16.06712  -0.12337  89.67159  1.000 24.41466 ? 458  GLU   A CG  1 
ATOM   3427 C  CD  . GLU   A 1 455 ? 14.78932  -0.94390  89.42858  1.000 28.99654 ? 458  GLU   A CD  1 
ATOM   3428 O  OE1 . GLU   A 1 455 ? 14.01540  -0.63610  88.50467  1.000 20.58483 ? 458  GLU   A OE1 1 
ATOM   3429 O  OE2 . GLU   A 1 455 ? 14.56573  -1.92578  90.15949  1.000 30.97772 ? 458  GLU   A OE2 1 
ATOM   3430 N  N   . ALA   A 1 456 ? 15.23112  3.78603   87.34240  1.000 17.19633 ? 459  ALA   A N   1 
ATOM   3431 C  CA  . ALA   A 1 456 ? 15.47944  5.01705   86.60490  1.000 18.09933 ? 459  ALA   A CA  1 
ATOM   3432 C  C   . ALA   A 1 456 ? 15.04897  6.23045   87.41149  1.000 17.68425 ? 459  ALA   A C   1 
ATOM   3433 O  O   . ALA   A 1 456 ? 15.72005  7.26230   87.39476  1.000 18.66333 ? 459  ALA   A O   1 
ATOM   3434 C  CB  . ALA   A 1 456 ? 14.74293  4.99843   85.26541  1.000 17.05667 ? 459  ALA   A CB  1 
ATOM   3435 N  N   . LEU   A 1 457 ? 13.93726  6.12349   88.13546  1.000 20.92649 ? 460  LEU   A N   1 
ATOM   3436 C  CA  . LEU   A 1 457 ? 13.51740  7.23107   88.98035  1.000 20.15065 ? 460  LEU   A CA  1 
ATOM   3437 C  C   . LEU   A 1 457 ? 14.54551  7.50672   90.07561  1.000 19.56223 ? 460  LEU   A C   1 
ATOM   3438 O  O   . LEU   A 1 457 ? 14.90422  8.66522   90.33173  1.000 18.01106 ? 460  LEU   A O   1 
ATOM   3439 C  CB  . LEU   A 1 457 ? 12.13798  6.93727   89.58139  1.000 22.35636 ? 460  LEU   A CB  1 
ATOM   3440 C  CG  . LEU   A 1 457 ? 11.62369  8.10998   90.42767  1.000 25.57389 ? 460  LEU   A CG  1 
ATOM   3441 C  CD1 . LEU   A 1 457 ? 11.44952  9.36608   89.55660  1.000 24.12718 ? 460  LEU   A CD1 1 
ATOM   3442 C  CD2 . LEU   A 1 457 ? 10.29435  7.75908   91.13785  1.000 26.44727 ? 460  LEU   A CD2 1 
ATOM   3443 N  N   . ALA   A 1 458 ? 15.03448  6.45582   90.74582  1.000 17.84290 ? 461  ALA   A N   1 
ATOM   3444 C  CA  . ALA   A 1 458 ? 16.02071  6.69471   91.79784  1.000 18.42499 ? 461  ALA   A CA  1 
ATOM   3445 C  C   . ALA   A 1 458 ? 17.25684  7.39206   91.23169  1.000 22.99985 ? 461  ALA   A C   1 
ATOM   3446 O  O   . ALA   A 1 458 ? 17.82409  8.30415   91.85817  1.000 19.33460 ? 461  ALA   A O   1 
ATOM   3447 C  CB  . ALA   A 1 458 ? 16.41547  5.36936   92.46436  1.000 21.53658 ? 461  ALA   A CB  1 
ATOM   3448 N  N   . PHE   A 1 459 ? 17.67287  6.99042   90.03339  1.000 17.72369 ? 462  PHE   A N   1 
ATOM   3449 C  CA  . PHE   A 1 459 ? 18.86127  7.58208   89.41159  1.000 17.55009 ? 462  PHE   A CA  1 
ATOM   3450 C  C   . PHE   A 1 459 ? 18.63940  9.04052   89.02370  1.000 21.95400 ? 462  PHE   A C   1 
ATOM   3451 O  O   . PHE   A 1 459 ? 19.47402  9.90470   89.32187  1.000 19.13822 ? 462  PHE   A O   1 
ATOM   3452 C  CB  . PHE   A 1 459 ? 19.25854  6.76064   88.19350  1.000 15.01479 ? 462  PHE   A CB  1 
ATOM   3453 C  CG  . PHE   A 1 459 ? 20.30430  7.41687   87.33602  1.000 19.71089 ? 462  PHE   A CG  1 
ATOM   3454 C  CD1 . PHE   A 1 459 ? 21.57306  7.69189   87.85576  1.000 20.60686 ? 462  PHE   A CD1 1 
ATOM   3455 C  CD2 . PHE   A 1 459 ? 20.02873  7.75427   86.02127  1.000 17.21049 ? 462  PHE   A CD2 1 
ATOM   3456 C  CE1 . PHE   A 1 459 ? 22.54887  8.28720   87.06076  1.000 23.80237 ? 462  PHE   A CE1 1 
ATOM   3457 C  CE2 . PHE   A 1 459 ? 21.01710  8.33883   85.21004  1.000 20.05123 ? 462  PHE   A CE2 1 
ATOM   3458 C  CZ  . PHE   A 1 459 ? 22.25504  8.61097   85.73724  1.000 19.12874 ? 462  PHE   A CZ  1 
ATOM   3459 N  N   . VAL   A 1 460 ? 17.53250  9.34460   88.34065  1.000 18.69214 ? 463  VAL   A N   1 
ATOM   3460 C  CA  . VAL   A 1 460 ? 17.35525  10.72210  87.87116  1.000 15.91142 ? 463  VAL   A CA  1 
ATOM   3461 C  C   . VAL   A 1 460 ? 17.13067  11.68497  89.03115  1.000 18.89556 ? 463  VAL   A C   1 
ATOM   3462 O  O   . VAL   A 1 460 ? 17.52384  12.85836  88.95368  1.000 21.02448 ? 463  VAL   A O   1 
ATOM   3463 C  CB  . VAL   A 1 460 ? 16.19663  10.81591  86.84998  1.000 18.47735 ? 463  VAL   A CB  1 
ATOM   3464 C  CG1 . VAL   A 1 460 ? 16.41973  9.82552   85.72926  1.000 17.78760 ? 463  VAL   A CG1 1 
ATOM   3465 C  CG2 . VAL   A 1 460 ? 14.83849  10.56291  87.52899  1.000 17.27398 ? 463  VAL   A CG2 1 
ATOM   3466 N  N   . ARG   A 1 461 ? 16.49065  11.23802  90.11478  1.000 20.71220 ? 464  ARG   A N   1 
ATOM   3467 C  CA  . ARG   A 1 461 ? 16.34182  12.12568  91.26074  1.000 21.18784 ? 464  ARG   A CA  1 
ATOM   3468 C  C   . ARG   A 1 461 ? 17.68891  12.41354  91.91359  1.000 20.75687 ? 464  ARG   A C   1 
ATOM   3469 O  O   . ARG   A 1 461 ? 17.97006  13.55593  92.31037  1.000 21.30751 ? 464  ARG   A O   1 
ATOM   3470 C  CB  . ARG   A 1 461 ? 15.38874  11.52281  92.28758  1.000 20.23854 ? 464  ARG   A CB  1 
ATOM   3471 C  CG  . ARG   A 1 461 ? 13.94339  11.42675  91.83288  1.000 28.88177 ? 464  ARG   A CG  1 
ATOM   3472 C  CD  . ARG   A 1 461 ? 13.15736  10.64317  92.87111  1.000 34.75743 ? 464  ARG   A CD  1 
ATOM   3473 N  NE  . ARG   A 1 461 ? 11.76874  11.07992  92.93398  1.000 54.89160 ? 464  ARG   A NE  1 
ATOM   3474 C  CZ  . ARG   A 1 461 ? 10.80312  10.44674  93.58951  1.000 55.12722 ? 464  ARG   A CZ  1 
ATOM   3475 N  NH1 . ARG   A 1 461 ? 11.02689  9.30224   94.22535  1.000 42.26952 ? 464  ARG   A NH1 1 
ATOM   3476 N  NH2 . ARG   A 1 461 ? 9.57955   10.97100  93.60146  1.000 52.99166 ? 464  ARG   A NH2 1 
ATOM   3477 N  N   . ALA   A 1 462 ? 18.53099  11.39125  92.05394  1.000 20.13327 ? 465  ALA   A N   1 
ATOM   3478 C  CA  . ALA   A 1 462 ? 19.85250  11.62416  92.63873  1.000 18.51922 ? 465  ALA   A CA  1 
ATOM   3479 C  C   . ALA   A 1 462 ? 20.64321  12.63485  91.82490  1.000 18.96081 ? 465  ALA   A C   1 
ATOM   3480 O  O   . ALA   A 1 462 ? 21.32462  13.51293  92.38827  1.000 23.12826 ? 465  ALA   A O   1 
ATOM   3481 C  CB  . ALA   A 1 462 ? 20.62746  10.31276  92.72911  1.000 22.01620 ? 465  ALA   A CB  1 
ATOM   3482 N  N   . VAL   A 1 463 ? 20.57674  12.52639  90.49628  1.000 20.01423 ? 466  VAL   A N   1 
ATOM   3483 C  CA  . VAL   A 1 463 ? 21.37742  13.39202  89.63153  1.000 23.22287 ? 466  VAL   A CA  1 
ATOM   3484 C  C   . VAL   A 1 463 ? 20.88338  14.83575  89.69379  1.000 33.44496 ? 466  VAL   A C   1 
ATOM   3485 O  O   . VAL   A 1 463 ? 21.68461  15.77476  89.73585  1.000 32.33333 ? 466  VAL   A O   1 
ATOM   3486 C  CB  . VAL   A 1 463 ? 21.37191  12.85608  88.18940  1.000 23.92777 ? 466  VAL   A CB  1 
ATOM   3487 C  CG1 . VAL   A 1 463 ? 21.98258  13.89090  87.24991  1.000 24.69372 ? 466  VAL   A CG1 1 
ATOM   3488 C  CG2 . VAL   A 1 463 ? 22.15079  11.54507  88.11482  1.000 19.29328 ? 466  VAL   A CG2 1 
ATOM   3489 N  N   . THR   A 1 464 ? 19.56373  15.03991  89.71803  1.000 21.96482 ? 467  THR   A N   1 
ATOM   3490 C  CA  . THR   A 1 464 ? 18.99938  16.37587  89.55205  1.000 29.35640 ? 467  THR   A CA  1 
ATOM   3491 C  C   . THR   A 1 464 ? 18.75108  17.11191  90.86808  1.000 34.35184 ? 467  THR   A C   1 
ATOM   3492 O  O   . THR   A 1 464 ? 18.65239  18.34035  90.86496  1.000 36.85279 ? 467  THR   A O   1 
ATOM   3493 C  CB  . THR   A 1 464 ? 17.68193  16.30077  88.76764  1.000 32.09869 ? 467  THR   A CB  1 
ATOM   3494 O  OG1 . THR   A 1 464 ? 16.77279  15.44014  89.45374  1.000 36.11783 ? 467  THR   A OG1 1 
ATOM   3495 C  CG2 . THR   A 1 464 ? 17.91578  15.73738  87.35849  1.000 27.56478 ? 467  THR   A CG2 1 
ATOM   3496 N  N   . ASP   A 1 465 ? 18.65157  16.41182  91.98905  1.000 33.09591 ? 468  ASP   A N   1 
ATOM   3497 C  CA  . ASP   A 1 465 ? 18.27847  17.04542  93.25866  1.000 35.86977 ? 468  ASP   A CA  1 
ATOM   3498 C  C   . ASP   A 1 465 ? 19.55838  17.49965  93.94670  1.000 34.90116 ? 468  ASP   A C   1 
ATOM   3499 O  O   . ASP   A 1 465 ? 20.16802  16.76230  94.72830  1.000 34.79451 ? 468  ASP   A O   1 
ATOM   3500 C  CB  . ASP   A 1 465 ? 17.47116  16.06720  94.10524  1.000 37.14972 ? 468  ASP   A CB  1 
ATOM   3501 C  CG  . ASP   A 1 465 ? 17.05164  16.63650  95.44680  1.000 46.58303 ? 468  ASP   A CG  1 
ATOM   3502 O  OD1 . ASP   A 1 465 ? 17.32321  17.82485  95.73765  1.000 42.19077 ? 468  ASP   A OD1 1 
ATOM   3503 O  OD2 . ASP   A 1 465 ? 16.44406  15.86621  96.21757  1.000 34.28790 ? 468  ASP   A OD2 1 
ATOM   3504 N  N   . HIS   A 1 466 ? 19.98675  18.73270  93.64548  1.000 39.14475 ? 469  HIS   A N   1 
ATOM   3505 C  CA  . HIS   A 1 466 ? 21.28285  19.19646  94.14087  1.000 45.94139 ? 469  HIS   A CA  1 
ATOM   3506 C  C   . HIS   A 1 466 ? 21.32235  19.24479  95.66230  1.000 40.99437 ? 469  HIS   A C   1 
ATOM   3507 O  O   . HIS   A 1 466 ? 22.35734  18.94026  96.26986  1.000 41.72376 ? 469  HIS   A O   1 
ATOM   3508 C  CB  . HIS   A 1 466 ? 21.61757  20.56882  93.55336  1.000 53.56221 ? 469  HIS   A CB  1 
ATOM   3509 C  CG  . HIS   A 1 466 ? 21.77909  20.55464  92.06612  1.000 61.72502 ? 469  HIS   A CG  1 
ATOM   3510 N  ND1 . HIS   A 1 466 ? 21.02921  21.35111  91.22809  1.000 64.35263 ? 469  HIS   A ND1 1 
ATOM   3511 C  CD2 . HIS   A 1 466 ? 22.58691  19.81916  91.26507  1.000 61.74980 ? 469  HIS   A CD2 1 
ATOM   3512 C  CE1 . HIS   A 1 466 ? 21.37499  21.11240  89.97451  1.000 68.37183 ? 469  HIS   A CE1 1 
ATOM   3513 N  NE2 . HIS   A 1 466 ? 22.32000  20.18929  89.96939  1.000 67.91397 ? 469  HIS   A NE2 1 
ATOM   3514 N  N   . LYS   A 1 467 ? 20.20795  19.61810  96.29688  1.000 36.19407 ? 470  LYS   A N   1 
ATOM   3515 C  CA  . LYS   A 1 467 ? 20.22277  19.78707  97.74584  1.000 54.01124 ? 470  LYS   A CA  1 
ATOM   3516 C  C   . LYS   A 1 467 ? 20.43198  18.45493  98.45841  1.000 55.52383 ? 470  LYS   A C   1 
ATOM   3517 O  O   . LYS   A 1 467 ? 21.03086  18.42212  99.53798  1.000 46.72727 ? 470  LYS   A O   1 
ATOM   3518 C  CB  . LYS   A 1 467 ? 18.93336  20.47125  98.21964  1.000 44.16850 ? 470  LYS   A CB  1 
ATOM   3519 C  CG  . LYS   A 1 467 ? 17.74041  19.54634  98.44865  1.000 48.95344 ? 470  LYS   A CG  1 
ATOM   3520 N  N   . ALA   A 1 468 ? 19.98235  17.34836  97.85612  1.000 37.93457 ? 471  ALA   A N   1 
ATOM   3521 C  CA  . ALA   A 1 468 ? 20.24354  16.02951  98.42303  1.000 30.29497 ? 471  ALA   A CA  1 
ATOM   3522 C  C   . ALA   A 1 468 ? 21.73598  15.71006  98.45006  1.000 36.21563 ? 471  ALA   A C   1 
ATOM   3523 O  O   . ALA   A 1 468 ? 22.18581  14.94570  99.30623  1.000 33.33280 ? 471  ALA   A O   1 
ATOM   3524 C  CB  . ALA   A 1 468 ? 19.47796  14.96371  97.63200  1.000 32.95586 ? 471  ALA   A CB  1 
ATOM   3525 N  N   . ALA   A 1 469 ? 22.52379  16.27120  97.52456  1.000 30.59800 ? 472  ALA   A N   1 
ATOM   3526 C  CA  . ALA   A 1 469 ? 23.98922  16.15124  97.59631  1.000 28.96555 ? 472  ALA   A CA  1 
ATOM   3527 C  C   . ALA   A 1 469 ? 24.43928  14.69090  97.59459  1.000 24.36501 ? 472  ALA   A C   1 
ATOM   3528 O  O   . ALA   A 1 469 ? 25.34546  14.29378  98.34498  1.000 27.49773 ? 472  ALA   A O   1 
ATOM   3529 C  CB  . ALA   A 1 469 ? 24.54596  16.89025  98.82232  1.000 28.23377 ? 472  ALA   A CB  1 
ATOM   3530 N  N   . VAL   A 1 470 ? 23.80397  13.88504  96.74539  1.000 24.83480 ? 473  VAL   A N   1 
ATOM   3531 C  CA  . VAL   A 1 470 ? 24.21405  12.48174  96.59695  1.000 20.16200 ? 473  VAL   A CA  1 
ATOM   3532 C  C   . VAL   A 1 470 ? 25.63701  12.43371  96.04686  1.000 22.14895 ? 473  VAL   A C   1 
ATOM   3533 O  O   . VAL   A 1 470 ? 25.91405  13.06504  95.00912  1.000 22.88211 ? 473  VAL   A O   1 
ATOM   3534 C  CB  . VAL   A 1 470 ? 23.25300  11.74765  95.65065  1.000 21.87339 ? 473  VAL   A CB  1 
ATOM   3535 C  CG1 . VAL   A 1 470 ? 23.73788  10.29980  95.41741  1.000 23.70471 ? 473  VAL   A CG1 1 
ATOM   3536 C  CG2 . VAL   A 1 470 ? 21.78958  11.81418  96.19929  1.000 22.90640 ? 473  VAL   A CG2 1 
ATOM   3537 N  N   . PRO   A 1 471 ? 26.54988  11.68417  96.65729  1.000 25.94148 ? 474  PRO   A N   1 
ATOM   3538 C  CA  . PRO   A 1 471 ? 27.91648  11.58501  96.11935  1.000 21.67022 ? 474  PRO   A CA  1 
ATOM   3539 C  C   . PRO   A 1 471 ? 27.91419  11.00595  94.71240  1.000 24.49494 ? 474  PRO   A C   1 
ATOM   3540 O  O   . PRO   A 1 471 ? 27.10201  10.14279  94.36904  1.000 21.10813 ? 474  PRO   A O   1 
ATOM   3541 C  CB  . PRO   A 1 471 ? 28.61520  10.63786  97.09363  1.000 23.60681 ? 474  PRO   A CB  1 
ATOM   3542 C  CG  . PRO   A 1 471 ? 27.76048  10.66440  98.35047  1.000 31.09778 ? 474  PRO   A CG  1 
ATOM   3543 C  CD  . PRO   A 1 471 ? 26.35795  10.88237  97.88446  1.000 26.76576 ? 474  PRO   A CD  1 
ATOM   3544 N  N   . ALA   A 1 472 ? 28.85688  11.47831  93.90000  1.000 20.99203 ? 475  ALA   A N   1 
ATOM   3545 C  CA  . ALA   A 1 472 ? 28.98039  10.95348  92.54547  1.000 22.39391 ? 475  ALA   A CA  1 
ATOM   3546 C  C   . ALA   A 1 472 ? 29.17521  9.44826   92.56099  1.000 18.43477 ? 475  ALA   A C   1 
ATOM   3547 O  O   . ALA   A 1 472 ? 28.66721  8.74092   91.68989  1.000 24.30493 ? 475  ALA   A O   1 
ATOM   3548 C  CB  . ALA   A 1 472 ? 30.14009  11.64679  91.83188  1.000 21.84539 ? 475  ALA   A CB  1 
ATOM   3549 N  N   . SER   A 1 473 ? 29.89343  8.92429   93.56289  1.000 19.86737 ? 476  SER   A N   1 
ATOM   3550 C  CA  . SER   A 1 473 ? 30.08747  7.48076   93.60633  1.000 24.93729 ? 476  SER   A CA  1 
ATOM   3551 C  C   . SER   A 1 473 ? 28.75025  6.75768   93.76051  1.000 24.17911 ? 476  SER   A C   1 
ATOM   3552 O  O   . SER   A 1 473 ? 28.53886  5.69607   93.16343  1.000 21.43514 ? 476  SER   A O   1 
ATOM   3553 C  CB  . SER   A 1 473 ? 31.04746  7.11750   94.74156  1.000 27.91281 ? 476  SER   A CB  1 
ATOM   3554 O  OG  . SER   A 1 473 ? 30.49002  7.47967   95.98890  1.000 24.12467 ? 476  SER   A OG  1 
ATOM   3555 N  N   . GLU   A 1 474 ? 27.82655  7.33372   94.53759  1.000 22.66969 ? 477  GLU   A N   1 
ATOM   3556 C  CA  . GLU   A 1 474 ? 26.49559  6.74707   94.68273  1.000 21.82857 ? 477  GLU   A CA  1 
ATOM   3557 C  C   . GLU   A 1 474 ? 25.63322  6.95017   93.43471  1.000 23.35692 ? 477  GLU   A C   1 
ATOM   3558 O  O   . GLU   A 1 474 ? 24.83771  6.07183   93.06939  1.000 23.25877 ? 477  GLU   A O   1 
ATOM   3559 C  CB  . GLU   A 1 474 ? 25.80712  7.33961   95.91204  1.000 25.26486 ? 477  GLU   A CB  1 
ATOM   3560 C  CG  . GLU   A 1 474 ? 24.36205  6.85804   96.11787  1.000 36.25905 ? 477  GLU   A CG  1 
ATOM   3561 C  CD  . GLU   A 1 474 ? 24.25904  5.37320   96.44738  1.000 53.61922 ? 477  GLU   A CD  1 
ATOM   3562 O  OE1 . GLU   A 1 474 ? 25.14783  4.84030   97.15888  1.000 50.20146 ? 477  GLU   A OE1 1 
ATOM   3563 O  OE2 . GLU   A 1 474 ? 23.28688  4.73571   95.98662  1.000 49.71132 ? 477  GLU   A OE2 1 
ATOM   3564 N  N   . LYS   A 1 475 ? 25.73850  8.11158   92.78200  1.000 20.85632 ? 478  LYS   A N   1 
ATOM   3565 C  CA  . LYS   A 1 475 ? 25.04254  8.28776   91.51458  1.000 18.35133 ? 478  LYS   A CA  1 
ATOM   3566 C  C   . LYS   A 1 475 ? 25.46352  7.22991   90.51217  1.000 18.96674 ? 478  LYS   A C   1 
ATOM   3567 O  O   . LYS   A 1 475 ? 24.66417  6.82249   89.65785  1.000 20.93125 ? 478  LYS   A O   1 
ATOM   3568 C  CB  . LYS   A 1 475 ? 25.32976  9.68696   90.93997  1.000 18.25628 ? 478  LYS   A CB  1 
ATOM   3569 C  CG  . LYS   A 1 475 ? 24.70515  10.83628  91.72825  1.000 22.22975 ? 478  LYS   A CG  1 
ATOM   3570 C  CD  . LYS   A 1 475 ? 25.22674  12.17382  91.20989  1.000 20.58224 ? 478  LYS   A CD  1 
ATOM   3571 C  CE  . LYS   A 1 475 ? 24.61360  13.34334  91.95711  1.000 21.65562 ? 478  LYS   A CE  1 
ATOM   3572 N  NZ  . LYS   A 1 475 ? 25.04597  14.64073  91.31042  1.000 24.23823 ? 478  LYS   A NZ  1 
ATOM   3573 N  N   . LEU   A 1 476 ? 26.73279  6.82790   90.55067  1.000 20.46096 ? 479  LEU   A N   1 
ATOM   3574 C  CA  . LEU   A 1 476 ? 27.20520  5.83086   89.59731  1.000 18.99595 ? 479  LEU   A CA  1 
ATOM   3575 C  C   . LEU   A 1 476 ? 26.59849  4.46089   89.90187  1.000 20.32617 ? 479  LEU   A C   1 
ATOM   3576 O  O   . LEU   A 1 476 ? 26.18283  3.74913   88.98653  1.000 19.47212 ? 479  LEU   A O   1 
ATOM   3577 C  CB  . LEU   A 1 476 ? 28.73508  5.78628   89.61469  1.000 18.70443 ? 479  LEU   A CB  1 
ATOM   3578 C  CG  . LEU   A 1 476 ? 29.37982  4.62281   88.84459  1.000 22.38609 ? 479  LEU   A CG  1 
ATOM   3579 C  CD1 . LEU   A 1 476 ? 29.05648  4.65922   87.36309  1.000 18.11079 ? 479  LEU   A CD1 1 
ATOM   3580 C  CD2 . LEU   A 1 476 ? 30.92282  4.59522   89.07822  1.000 25.85708 ? 479  LEU   A CD2 1 
ATOM   3581 N  N   . LEU   A 1 477 ? 26.53095  4.07981   91.17939  1.000 20.83889 ? 480  LEU   A N   1 
ATOM   3582 C  CA  . LEU   A 1 477 ? 25.82712  2.84924   91.54007  1.000 21.54196 ? 480  LEU   A CA  1 
ATOM   3583 C  C   . LEU   A 1 477 ? 24.37537  2.88654   91.08516  1.000 21.15298 ? 480  LEU   A C   1 
ATOM   3584 O  O   . LEU   A 1 477 ? 23.83091  1.87744   90.61973  1.000 22.68928 ? 480  LEU   A O   1 
ATOM   3585 C  CB  . LEU   A 1 477 ? 25.88731  2.63708   93.05029  1.000 18.98551 ? 480  LEU   A CB  1 
ATOM   3586 C  CG  . LEU   A 1 477 ? 27.28344  2.41887   93.60912  1.000 24.01752 ? 480  LEU   A CG  1 
ATOM   3587 C  CD1 . LEU   A 1 477 ? 27.13303  2.30719   95.13629  1.000 32.72054 ? 480  LEU   A CD1 1 
ATOM   3588 C  CD2 . LEU   A 1 477 ? 27.88745  1.14598   93.03371  1.000 28.41830 ? 480  LEU   A CD2 1 
ATOM   3589 N  N   . LEU   A 1 478 ? 23.71581  4.03304   91.24293  1.000 20.21268 ? 481  LEU   A N   1 
ATOM   3590 C  CA  . LEU   A 1 478 ? 22.32111  4.14044   90.80475  1.000 21.32909 ? 481  LEU   A CA  1 
ATOM   3591 C  C   . LEU   A 1 478 ? 22.22262  4.09220   89.28359  1.000 18.05783 ? 481  LEU   A C   1 
ATOM   3592 O  O   . LEU   A 1 478 ? 21.24558  3.56213   88.73151  1.000 20.76805 ? 481  LEU   A O   1 
ATOM   3593 C  CB  . LEU   A 1 478 ? 21.70309  5.43840   91.34633  1.000 17.10561 ? 481  LEU   A CB  1 
ATOM   3594 C  CG  . LEU   A 1 478 ? 21.55123  5.50749   92.86821  1.000 19.29223 ? 481  LEU   A CG  1 
ATOM   3595 C  CD1 . LEU   A 1 478 ? 21.09260  6.88824   93.30129  1.000 22.60201 ? 481  LEU   A CD1 1 
ATOM   3596 C  CD2 . LEU   A 1 478 ? 20.53313  4.47117   93.36614  1.000 21.58905 ? 481  LEU   A CD2 1 
ATOM   3597 N  N   . LEU   A 1 479 ? 23.20786  4.66879   88.58657  1.000 22.37876 ? 482  LEU   A N   1 
ATOM   3598 C  CA  . LEU   A 1 479 ? 23.23139  4.59637   87.12492  1.000 18.45192 ? 482  LEU   A CA  1 
ATOM   3599 C  C   . LEU   A 1 479 ? 23.31527  3.14713   86.67631  1.000 22.75872 ? 482  LEU   A C   1 
ATOM   3600 O  O   . LEU   A 1 479 ? 22.56528  2.71144   85.79885  1.000 21.73282 ? 482  LEU   A O   1 
ATOM   3601 C  CB  . LEU   A 1 479 ? 24.43053  5.38849   86.56691  1.000 17.58477 ? 482  LEU   A CB  1 
ATOM   3602 C  CG  . LEU   A 1 479 ? 24.65189  5.49305   85.04587  1.000 23.37484 ? 482  LEU   A CG  1 
ATOM   3603 C  CD1 . LEU   A 1 479 ? 25.74158  6.53302   84.75250  1.000 22.66883 ? 482  LEU   A CD1 1 
ATOM   3604 C  CD2 . LEU   A 1 479 ? 25.14703  4.21981   84.46895  1.000 29.71695 ? 482  LEU   A CD2 1 
ATOM   3605 N  N   . LYS   A 1 480 ? 24.24422  2.38616   87.26249  1.000 19.31761 ? 483  LYS   A N   1 
ATOM   3606 C  CA  . LYS   A 1 480 ? 24.42181  1.01896   86.82007  1.000 21.22743 ? 483  LYS   A CA  1 
ATOM   3607 C  C   . LYS   A 1 480 ? 23.21666  0.16161   87.18967  1.000 20.98023 ? 483  LYS   A C   1 
ATOM   3608 O  O   . LYS   A 1 480 ? 22.85171  -0.73265  86.42925  1.000 19.83956 ? 483  LYS   A O   1 
ATOM   3609 C  CB  . LYS   A 1 480 ? 25.72959  0.45260   87.38361  1.000 25.61614 ? 483  LYS   A CB  1 
ATOM   3610 C  CG  . LYS   A 1 480 ? 26.97744  1.05916   86.72345  1.000 26.77831 ? 483  LYS   A CG  1 
ATOM   3611 C  CD  . LYS   A 1 480 ? 26.87543  1.06045   85.17679  1.000 31.62715 ? 483  LYS   A CD  1 
ATOM   3612 C  CE  . LYS   A 1 480 ? 28.12013  1.64865   84.50769  1.000 28.55858 ? 483  LYS   A CE  1 
ATOM   3613 N  NZ  . LYS   A 1 480 ? 29.31617  0.86093   84.86421  1.000 26.51738 ? 483  LYS   A NZ  1 
ATOM   3614 N  N   . ASP   A 1 481 ? 22.57461  0.42864   88.32790  1.000 19.37438 ? 484  ASP   A N   1 
ATOM   3615 C  CA  . ASP   A 1 481 ? 21.36139  -0.30965  88.65876  1.000 19.99008 ? 484  ASP   A CA  1 
ATOM   3616 C  C   . ASP   A 1 481 ? 20.21619  0.05393   87.72648  1.000 23.38796 ? 484  ASP   A C   1 
ATOM   3617 O  O   . ASP   A 1 481 ? 19.38077  -0.79622  87.42245  1.000 21.57549 ? 484  ASP   A O   1 
ATOM   3618 C  CB  . ASP   A 1 481 ? 20.94680  -0.04573  90.11127  1.000 22.28474 ? 484  ASP   A CB  1 
ATOM   3619 C  CG  . ASP   A 1 481 ? 19.91758  -1.05968  90.62352  1.000 30.83303 ? 484  ASP   A CG  1 
ATOM   3620 O  OD1 . ASP   A 1 481 ? 20.03868  -2.25915  90.29633  1.000 34.99951 ? 484  ASP   A OD1 1 
ATOM   3621 O  OD2 . ASP   A 1 481 ? 19.00988  -0.66257  91.37591  1.000 31.04835 ? 484  ASP   A OD2 1 
ATOM   3622 N  N   . ALA   A 1 482 ? 20.14012  1.30313   87.26880  1.000 17.57276 ? 485  ALA   A N   1 
ATOM   3623 C  CA  . ALA   A 1 482 ? 19.08136  1.61914   86.30818  1.000 17.43939 ? 485  ALA   A CA  1 
ATOM   3624 C  C   . ALA   A 1 482 ? 19.35138  0.92780   84.97900  1.000 16.50730 ? 485  ALA   A C   1 
ATOM   3625 O  O   . ALA   A 1 482 ? 18.42404  0.45022   84.31562  1.000 17.06854 ? 485  ALA   A O   1 
ATOM   3626 C  CB  . ALA   A 1 482 ? 18.96370  3.13616   86.12015  1.000 19.13162 ? 485  ALA   A CB  1 
ATOM   3627 N  N   . ILE   A 1 483 ? 20.62052  0.88025   84.56223  1.000 18.34492 ? 486  ILE   A N   1 
ATOM   3628 C  CA  . ILE   A 1 483 ? 20.94919  0.18332   83.32138  1.000 18.83459 ? 486  ILE   A CA  1 
ATOM   3629 C  C   . ILE   A 1 483 ? 20.66713  -1.30490  83.45688  1.000 17.60085 ? 486  ILE   A C   1 
ATOM   3630 O  O   . ILE   A 1 483 ? 20.13989  -1.93697  82.52303  1.000 19.27513 ? 486  ILE   A O   1 
ATOM   3631 C  CB  . ILE   A 1 483 ? 22.40543  0.49695   82.91762  1.000 21.26531 ? 486  ILE   A CB  1 
ATOM   3632 C  CG1 . ILE   A 1 483 ? 22.43026  1.92441   82.35273  1.000 18.08044 ? 486  ILE   A CG1 1 
ATOM   3633 C  CG2 . ILE   A 1 483 ? 22.93129  -0.51417  81.86037  1.000 22.27577 ? 486  ILE   A CG2 1 
ATOM   3634 C  CD1 . ILE   A 1 483 ? 23.80772  2.42685   81.95116  1.000 26.55810 ? 486  ILE   A CD1 1 
ATOM   3635 N  N   . ARG   A 1 484 ? 20.98338  -1.88528  84.62841  1.000 17.52396 ? 487  ARG   A N   1 
ATOM   3636 C  CA  . ARG   A 1 484 ? 20.65227  -3.28346  84.88903  1.000 20.01785 ? 487  ARG   A CA  1 
ATOM   3637 C  C   . ARG   A 1 484 ? 19.15496  -3.53659  84.76465  1.000 16.41291 ? 487  ARG   A C   1 
ATOM   3638 O  O   . ARG   A 1 484 ? 18.72748  -4.49549  84.10438  1.000 20.04779 ? 487  ARG   A O   1 
ATOM   3639 C  CB  . ARG   A 1 484 ? 21.14449  -3.69815  86.28839  1.000 22.56663 ? 487  ARG   A CB  1 
ATOM   3640 C  CG  . ARG   A 1 484 ? 20.93004  -5.18807  86.57599  1.000 25.82077 ? 487  ARG   A CG  1 
ATOM   3641 C  CD  . ARG   A 1 484 ? 20.84587  -5.53250  88.07367  1.000 29.91935 ? 487  ARG   A CD  1 
ATOM   3642 N  NE  . ARG   A 1 484 ? 19.89389  -4.66140  88.74903  1.000 32.59876 ? 487  ARG   A NE  1 
ATOM   3643 C  CZ  . ARG   A 1 484 ? 18.57601  -4.77563  88.67548  1.000 34.92919 ? 487  ARG   A CZ  1 
ATOM   3644 N  NH1 . ARG   A 1 484 ? 17.99931  -5.77439  88.01014  1.000 24.55900 ? 487  ARG   A NH1 1 
ATOM   3645 N  NH2 . ARG   A 1 484 ? 17.81843  -3.85992  89.27319  1.000 27.01021 ? 487  ARG   A NH2 1 
ATOM   3646 N  N   . ALA   A 1 485 ? 18.34056  -2.69850  85.41341  1.000 18.27762 ? 488  ALA   A N   1 
ATOM   3647 C  CA  . ALA   A 1 485 ? 16.88461  -2.86351  85.34562  1.000 20.67762 ? 488  ALA   A CA  1 
ATOM   3648 C  C   . ALA   A 1 485 ? 16.36223  -2.70277  83.91954  1.000 20.63912 ? 488  ALA   A C   1 
ATOM   3649 O  O   . ALA   A 1 485 ? 15.43172  -3.40959  83.51696  1.000 20.22777 ? 488  ALA   A O   1 
ATOM   3650 C  CB  . ALA   A 1 485 ? 16.19146  -1.85948  86.27783  1.000 18.08370 ? 488  ALA   A CB  1 
ATOM   3651 N  N   . GLN   A 1 486 ? 16.93885  -1.76858  83.15198  1.000 14.49507 ? 489  GLN   A N   1 
ATOM   3652 C  CA  . GLN   A 1 486 ? 16.53937  -1.55176  81.75687  1.000 16.23595 ? 489  GLN   A CA  1 
ATOM   3653 C  C   . GLN   A 1 486 ? 16.83427  -2.78165  80.91524  1.000 17.86596 ? 489  GLN   A C   1 
ATOM   3654 O  O   . GLN   A 1 486 ? 15.99102  -3.22868  80.11913  1.000 18.84361 ? 489  GLN   A O   1 
ATOM   3655 C  CB  . GLN   A 1 486 ? 17.27814  -0.31748  81.19838  1.000 15.67972 ? 489  GLN   A CB  1 
ATOM   3656 C  CG  . GLN   A 1 486 ? 17.01049  -0.02778  79.70478  1.000 17.50938 ? 489  GLN   A CG  1 
ATOM   3657 C  CD  . GLN   A 1 486 ? 15.57511  0.40599   79.45039  1.000 19.36833 ? 489  GLN   A CD  1 
ATOM   3658 O  OE1 . GLN   A 1 486 ? 14.94648  1.02429   80.30966  1.000 24.37176 ? 489  GLN   A OE1 1 
ATOM   3659 N  NE2 . GLN   A 1 486 ? 15.05711  0.09604   78.25583  1.000 19.12839 ? 489  GLN   A NE2 1 
ATOM   3660 N  N   . THR   A 1 487 ? 18.04067  -3.34901  81.09117  1.000 19.42023 ? 490  THR   A N   1 
ATOM   3661 C  CA  . THR   A 1 487 ? 18.43315  -4.56628  80.38803  1.000 19.00628 ? 490  THR   A CA  1 
ATOM   3662 C  C   . THR   A 1 487 ? 17.53121  -5.73720  80.77251  1.000 18.38259 ? 490  THR   A C   1 
ATOM   3663 O  O   . THR   A 1 487 ? 17.12980  -6.53106  79.91776  1.000 16.20708 ? 490  THR   A O   1 
ATOM   3664 C  CB  . THR   A 1 487 ? 19.89445  -4.89730  80.72127  1.000 22.99726 ? 490  THR   A CB  1 
ATOM   3665 O  OG1 . THR   A 1 487 ? 20.73157  -3.80183  80.32977  1.000 22.87970 ? 490  THR   A OG1 1 
ATOM   3666 C  CG2 . THR   A 1 487 ? 20.36464  -6.18299  80.01602  1.000 22.30233 ? 490  THR   A CG2 1 
ATOM   3667 N  N   . ALA   A 1 488 ? 17.21396  -5.85968  82.06119  1.000 17.67857 ? 491  ALA   A N   1 
ATOM   3668 C  CA  . ALA   A 1 488 ? 16.32667  -6.92309  82.51930  1.000 21.30162 ? 491  ALA   A CA  1 
ATOM   3669 C  C   . ALA   A 1 488 ? 14.94929  -6.81535  81.87839  1.000 18.57161 ? 491  ALA   A C   1 
ATOM   3670 O  O   . ALA   A 1 488 ? 14.37855  -7.82585  81.44864  1.000 16.87189 ? 491  ALA   A O   1 
ATOM   3671 C  CB  . ALA   A 1 488 ? 16.20645  -6.88875  84.04589  1.000 20.15601 ? 491  ALA   A CB  1 
ATOM   3672 N  N   . TYR   A 1 489 ? 14.38617  -5.60775  81.82408  1.000 17.58532 ? 492  TYR   A N   1 
ATOM   3673 C  CA  . TYR   A 1 489 ? 13.07645  -5.43959  81.18656  1.000 18.09197 ? 492  TYR   A CA  1 
ATOM   3674 C  C   . TYR   A 1 489 ? 13.15752  -5.78276  79.70917  1.000 18.05352 ? 492  TYR   A C   1 
ATOM   3675 O  O   . TYR   A 1 489 ? 12.24130  -6.39230  79.15295  1.000 18.08486 ? 492  TYR   A O   1 
ATOM   3676 C  CB  . TYR   A 1 489 ? 12.55295  -3.99650  81.36171  1.000 16.35613 ? 492  TYR   A CB  1 
ATOM   3677 C  CG  . TYR   A 1 489 ? 11.01771  -3.93236  81.36473  1.000 19.23930 ? 492  TYR   A CG  1 
ATOM   3678 C  CD1 . TYR   A 1 489 ? 10.28288  -4.24628  80.20804  1.000 16.90377 ? 492  TYR   A CD1 1 
ATOM   3679 C  CD2 . TYR   A 1 489 ? 10.31013  -3.58435  82.51595  1.000 20.96305 ? 492  TYR   A CD2 1 
ATOM   3680 C  CE1 . TYR   A 1 489 ? 8.86539   -4.21622  80.19862  1.000 15.98080 ? 492  TYR   A CE1 1 
ATOM   3681 C  CE2 . TYR   A 1 489 ? 8.89099   -3.57398  82.52499  1.000 18.33122 ? 492  TYR   A CE2 1 
ATOM   3682 C  CZ  . TYR   A 1 489 ? 8.19436   -3.88844  81.36292  1.000 21.60976 ? 492  TYR   A CZ  1 
ATOM   3683 O  OH  . TYR   A 1 489 ? 6.82328   -3.85158  81.34839  1.000 23.29407 ? 492  TYR   A OH  1 
ATOM   3684 N  N   . THR   A 1 490 ? 14.25188  -5.39287  79.05649  1.000 17.32800 ? 493  THR   A N   1 
ATOM   3685 C  CA  . THR   A 1 490 ? 14.45139  -5.71690  77.64481  1.000 18.61418 ? 493  THR   A CA  1 
ATOM   3686 C  C   . THR   A 1 490 ? 14.42027  -7.22533  77.40838  1.000 16.92669 ? 493  THR   A C   1 
ATOM   3687 O  O   . THR   A 1 490 ? 13.72911  -7.70021  76.51293  1.000 18.48903 ? 493  THR   A O   1 
ATOM   3688 C  CB  . THR   A 1 490 ? 15.79296  -5.11935  77.18329  1.000 18.23694 ? 493  THR   A CB  1 
ATOM   3689 O  OG1 . THR   A 1 490 ? 15.72705  -3.70132  77.34671  1.000 19.86945 ? 493  THR   A OG1 1 
ATOM   3690 C  CG2 . THR   A 1 490 ? 16.10476  -5.47846  75.68987  1.000 19.72513 ? 493  THR   A CG2 1 
ATOM   3691 N  N   . VAL   A 1 491 ? 15.16871  -8.00120  78.20363  1.000 18.94626 ? 494  VAL   A N   1 
ATOM   3692 C  CA  . VAL   A 1 491 ? 15.15164  -9.47088  78.05906  1.000 17.35818 ? 494  VAL   A CA  1 
ATOM   3693 C  C   . VAL   A 1 491 ? 13.75339  -10.01299 78.28872  1.000 21.16413 ? 494  VAL   A C   1 
ATOM   3694 O  O   . VAL   A 1 491 ? 13.28540  -10.88939 77.55282  1.000 19.94856 ? 494  VAL   A O   1 
ATOM   3695 C  CB  . VAL   A 1 491 ? 16.14894  -10.13428 79.03014  1.000 21.01169 ? 494  VAL   A CB  1 
ATOM   3696 C  CG1 . VAL   A 1 491 ? 15.95203  -11.65469 79.03739  1.000 24.20016 ? 494  VAL   A CG1 1 
ATOM   3697 C  CG2 . VAL   A 1 491 ? 17.57455  -9.77763  78.66716  1.000 22.59645 ? 494  VAL   A CG2 1 
ATOM   3698 N  N   . MET   A 1 492 ? 13.06942  -9.50377  79.32332  1.000 17.41459 ? 495  MET   A N   1 
ATOM   3699 C  CA  . MET   A 1 492 ? 11.68987  -9.89993  79.60625  1.000 21.41276 ? 495  MET   A CA  1 
ATOM   3700 C  C   . MET   A 1 492 ? 10.79101  -9.66312  78.40132  1.000 16.64564 ? 495  MET   A C   1 
ATOM   3701 O  O   . MET   A 1 492 ? 10.00896  -10.53581 78.01538  1.000 19.17138 ? 495  MET   A O   1 
ATOM   3702 C  CB  . MET   A 1 492 ? 11.15791  -9.11279  80.81222  1.000 20.47949 ? 495  MET   A CB  1 
ATOM   3703 C  CG  . MET   A 1 492 ? 9.77429   -9.56258  81.33284  1.000 21.50608 ? 495  MET   A CG  1 
ATOM   3704 S  SD  . MET   A 1 492 ? 9.36471   -8.73193  82.91280  1.000 27.04179 ? 495  MET   A SD  1 
ATOM   3705 C  CE  . MET   A 1 492 ? 9.08357   -7.09023  82.31025  1.000 19.96587 ? 495  MET   A CE  1 
ATOM   3706 N  N   . ALA   A 1 493 ? 10.89192  -8.48943  77.78203  1.000 15.84861 ? 496  ALA   A N   1 
ATOM   3707 C  CA  . ALA   A 1 493 ? 9.98518   -8.17485  76.67797  1.000 19.91308 ? 496  ALA   A CA  1 
ATOM   3708 C  C   . ALA   A 1 493 ? 10.28066  -9.03566  75.44681  1.000 18.89039 ? 496  ALA   A C   1 
ATOM   3709 O  O   . ALA   A 1 493 ? 9.35755   -9.56637  74.82394  1.000 20.74139 ? 496  ALA   A O   1 
ATOM   3710 C  CB  . ALA   A 1 493 ? 10.04981  -6.68295  76.33441  1.000 19.86965 ? 496  ALA   A CB  1 
ATOM   3711 N  N   . ILE   A 1 494 ? 11.55439  -9.17073  75.05541  1.000 18.48161 ? 497  ILE   A N   1 
ATOM   3712 C  CA  . ILE   A 1 494 ? 11.81936  -9.88933  73.80868  1.000 16.76774 ? 497  ILE   A CA  1 
ATOM   3713 C  C   . ILE   A 1 494 ? 11.56997  -11.38886 73.95137  1.000 20.20655 ? 497  ILE   A C   1 
ATOM   3714 O  O   . ILE   A 1 494 ? 11.42544  -12.08567 72.93686  1.000 20.24751 ? 497  ILE   A O   1 
ATOM   3715 C  CB  . ILE   A 1 494 ? 13.25384  -9.62980  73.29812  1.000 20.71102 ? 497  ILE   A CB  1 
ATOM   3716 C  CG1 . ILE   A 1 494 ? 14.28521  -10.23014 74.26584  1.000 21.81079 ? 497  ILE   A CG1 1 
ATOM   3717 C  CG2 . ILE   A 1 494 ? 13.46922  -8.11845  73.04058  1.000 16.58175 ? 497  ILE   A CG2 1 
ATOM   3718 C  CD1 . ILE   A 1 494 ? 15.75066  -9.98942  73.87928  1.000 27.29956 ? 497  ILE   A CD1 1 
ATOM   3719 N  N   . THR   A 1 495 ? 11.53291  -11.92072 75.17504  1.000 17.98163 ? 498  THR   A N   1 
ATOM   3720 C  CA  . THR   A 1 495 ? 11.18445  -13.32486 75.39133  1.000 17.11283 ? 498  THR   A CA  1 
ATOM   3721 C  C   . THR   A 1 495 ? 9.68778   -13.53003 75.65056  1.000 21.25594 ? 498  THR   A C   1 
ATOM   3722 O  O   . THR   A 1 495 ? 9.28576   -14.62957 76.02959  1.000 21.17399 ? 498  THR   A O   1 
ATOM   3723 C  CB  . THR   A 1 495 ? 12.01292  -13.91293 76.54238  1.000 24.14057 ? 498  THR   A CB  1 
ATOM   3724 O  OG1 . THR   A 1 495 ? 11.71904  -13.22342 77.77196  1.000 22.87079 ? 498  THR   A OG1 1 
ATOM   3725 C  CG2 . THR   A 1 495 ? 13.52393  -13.80944 76.22828  1.000 28.16212 ? 498  THR   A CG2 1 
ATOM   3726 N  N   . GLY   A 1 496 ? 8.85665   -12.51259 75.42142  1.000 23.94215 ? 499  GLY   A N   1 
ATOM   3727 C  CA  . GLY   A 1 496 ? 7.41194   -12.66988 75.55911  1.000 23.50501 ? 499  GLY   A CA  1 
ATOM   3728 C  C   . GLY   A 1 496 ? 6.90132   -12.64485 76.98449  1.000 24.75916 ? 499  GLY   A C   1 
ATOM   3729 O  O   . GLY   A 1 496 ? 5.78384   -13.08883 77.23530  1.000 22.39868 ? 499  GLY   A O   1 
ATOM   3730 N  N   . MET   A 1 497 ? 7.68717   -12.13257 77.93303  1.000 17.02976 ? 500  MET   A N   1 
ATOM   3731 C  CA  . MET   A 1 497 ? 7.33477   -12.18939 79.34889  1.000 18.64961 ? 500  MET   A CA  1 
ATOM   3732 C  C   . MET   A 1 497 ? 6.95797   -10.82899 79.92685  1.000 21.69612 ? 500  MET   A C   1 
ATOM   3733 O  O   . MET   A 1 497 ? 6.73683   -10.73459 81.13606  1.000 23.72144 ? 500  MET   A O   1 
ATOM   3734 C  CB  . MET   A 1 497 ? 8.47585   -12.79386 80.17787  1.000 18.93500 ? 500  MET   A CB  1 
ATOM   3735 C  CG  . MET   A 1 497 ? 8.70460   -14.29514 79.97299  1.000 27.26736 ? 500  MET   A CG  1 
ATOM   3736 S  SD  . MET   A 1 497 ? 7.36887   -15.30289 80.64320  1.000 31.75677 ? 500  MET   A SD  1 
ATOM   3737 C  CE  . MET   A 1 497 ? 6.61677   -15.87063 79.16701  1.000 25.18735 ? 500  MET   A CE  1 
ATOM   3738 N  N   . ALA   A 1 498 ? 6.84185   -9.78379  79.10841  1.000 15.45307 ? 501  ALA   A N   1 
ATOM   3739 C  CA  . ALA   A 1 498 ? 6.47044   -8.48040  79.64099  1.000 19.49556 ? 501  ALA   A CA  1 
ATOM   3740 C  C   . ALA   A 1 498 ? 4.94011   -8.39194  79.65631  1.000 22.59149 ? 501  ALA   A C   1 
ATOM   3741 O  O   . ALA   A 1 498 ? 4.26870   -9.42418  79.57443  1.000 23.43572 ? 501  ALA   A O   1 
ATOM   3742 C  CB  . ALA   A 1 498 ? 7.17542   -7.36984  78.85019  1.000 17.03220 ? 501  ALA   A CB  1 
ATOM   3743 N  N   . ILE   A 1 499 ? 4.36032   -7.19654  79.78950  1.000 14.93391 ? 502  ILE   A N   1 
ATOM   3744 C  CA  . ILE   A 1 499 ? 2.96702   -7.10568  80.23538  1.000 17.95806 ? 502  ILE   A CA  1 
ATOM   3745 C  C   . ILE   A 1 499 ? 2.00752   -6.49301  79.22334  1.000 18.76674 ? 502  ILE   A C   1 
ATOM   3746 O  O   . ILE   A 1 499 ? 0.78713   -6.72885  79.35039  1.000 19.52130 ? 502  ILE   A O   1 
ATOM   3747 C  CB  . ILE   A 1 499 ? 2.83639   -6.35043  81.57535  1.000 18.19192 ? 502  ILE   A CB  1 
ATOM   3748 C  CG1 . ILE   A 1 499 ? 3.30155   -4.87860  81.43427  1.000 19.88501 ? 502  ILE   A CG1 1 
ATOM   3749 C  CG2 . ILE   A 1 499 ? 3.62498   -7.09242  82.67314  1.000 21.71429 ? 502  ILE   A CG2 1 
ATOM   3750 C  CD1 . ILE   A 1 499 ? 2.84286   -3.94562  82.62134  1.000 18.54416 ? 502  ILE   A CD1 1 
ATOM   3751 N  N   . ASP   A 1 500 ? 2.44573   -5.65534  78.28505  1.000 16.62533 ? 503  ASP   A N   1 
ATOM   3752 C  CA  . ASP   A 1 500 ? 1.45201   -4.87827  77.52935  1.000 17.77204 ? 503  ASP   A CA  1 
ATOM   3753 C  C   . ASP   A 1 500 ? 0.57536   -5.77797  76.65895  1.000 21.45562 ? 503  ASP   A C   1 
ATOM   3754 O  O   . ASP   A 1 500 ? -0.65416  -5.68820  76.71327  1.000 21.18195 ? 503  ASP   A O   1 
ATOM   3755 C  CB  . ASP   A 1 500 ? 2.13443   -3.80104  76.68045  1.000 18.33015 ? 503  ASP   A CB  1 
ATOM   3756 C  CG  . ASP   A 1 500 ? 2.66527   -2.64932  77.51433  1.000 24.73078 ? 503  ASP   A CG  1 
ATOM   3757 O  OD1 . ASP   A 1 500 ? 3.31064   -2.89215  78.56207  1.000 19.92312 ? 503  ASP   A OD1 1 
ATOM   3758 O  OD2 . ASP   A 1 500 ? 2.47162   -1.49116  77.10623  1.000 23.14659 ? 503  ASP   A OD2 1 
ATOM   3759 N  N   . ASN   A 1 501 ? 1.17777   -6.67042  75.86328  1.000 20.77907 ? 504  ASN   A N   1 
ATOM   3760 C  CA  . ASN   A 1 501 ? 0.36717   -7.57018  75.02918  1.000 20.19842 ? 504  ASN   A CA  1 
ATOM   3761 C  C   . ASN   A 1 501 ? -0.54774  -8.43968  75.87653  1.000 16.89352 ? 504  ASN   A C   1 
ATOM   3762 O  O   . ASN   A 1 501 ? -1.69894  -8.69418  75.50289  1.000 19.39309 ? 504  ASN   A O   1 
ATOM   3763 C  CB  . ASN   A 1 501 ? 1.26203   -8.46683  74.16295  1.000 15.10377 ? 504  ASN   A CB  1 
ATOM   3764 C  CG  . ASN   A 1 501 ? 1.86055   -7.70327  72.96140  1.000 21.09781 ? 504  ASN   A CG  1 
ATOM   3765 O  OD1 . ASN   A 1 501 ? 1.38895   -6.63228  72.60902  1.000 22.02090 ? 504  ASN   A OD1 1 
ATOM   3766 N  ND2 . ASN   A 1 501 ? 2.90946   -8.23413  72.38613  1.000 20.07993 ? 504  ASN   A ND2 1 
ATOM   3767 N  N   . HIS   A 1 502 ? -0.03838  -8.92865  77.00574  1.000 19.03275 ? 505  HIS   A N   1 
ATOM   3768 C  CA  . HIS   A 1 502 ? -0.82742  -9.79312  77.87652  1.000 17.53319 ? 505  HIS   A CA  1 
ATOM   3769 C  C   . HIS   A 1 502 ? -2.06272  -9.06721  78.40296  1.000 16.78665 ? 505  HIS   A C   1 
ATOM   3770 O  O   . HIS   A 1 502 ? -3.17951  -9.59301  78.33555  1.000 20.55764 ? 505  HIS   A O   1 
ATOM   3771 C  CB  . HIS   A 1 502 ? 0.06658   -10.29746 79.01355  1.000 17.12010 ? 505  HIS   A CB  1 
ATOM   3772 C  CG  . HIS   A 1 502 ? -0.55957  -11.34385 79.88396  1.000 18.68228 ? 505  HIS   A CG  1 
ATOM   3773 N  ND1 . HIS   A 1 502 ? 0.00838   -11.74760 81.07680  1.000 18.34450 ? 505  HIS   A ND1 1 
ATOM   3774 C  CD2 . HIS   A 1 502 ? -1.67341  -12.09452 79.72666  1.000 18.98788 ? 505  HIS   A CD2 1 
ATOM   3775 C  CE1 . HIS   A 1 502 ? -0.73848  -12.69014 81.61942  1.000 17.86041 ? 505  HIS   A CE1 1 
ATOM   3776 N  NE2 . HIS   A 1 502 ? -1.76770  -12.91857 80.82216  1.000 20.49491 ? 505  HIS   A NE2 1 
ATOM   3777 N  N   . LEU   A 1 503 ? -1.88789  -7.85297  78.92619  1.000 17.95117 ? 506  LEU   A N   1 
ATOM   3778 C  CA  . LEU   A 1 503 ? -3.04333  -7.08188  79.40289  1.000 18.11709 ? 506  LEU   A CA  1 
ATOM   3779 C  C   . LEU   A 1 503 ? -3.98980  -6.73019  78.26060  1.000 18.94478 ? 506  LEU   A C   1 
ATOM   3780 O  O   . LEU   A 1 503 ? -5.21347  -6.74129  78.42776  1.000 18.49166 ? 506  LEU   A O   1 
ATOM   3781 C  CB  . LEU   A 1 503 ? -2.56632  -5.80772  80.09546  1.000 18.64387 ? 506  LEU   A CB  1 
ATOM   3782 C  CG  . LEU   A 1 503 ? -1.80800  -6.05712  81.42330  1.000 21.66142 ? 506  LEU   A CG  1 
ATOM   3783 C  CD1 . LEU   A 1 503 ? -1.21080  -4.75468  81.94143  1.000 17.56004 ? 506  LEU   A CD1 1 
ATOM   3784 C  CD2 . LEU   A 1 503 ? -2.77284  -6.65976  82.44820  1.000 19.96040 ? 506  LEU   A CD2 1 
ATOM   3785 N  N   . LEU   A 1 504 ? -3.44157  -6.39521  77.09710  1.000 16.35087 ? 507  LEU   A N   1 
ATOM   3786 C  CA  . LEU   A 1 504 ? -4.29398  -6.07941  75.94828  1.000 19.88524 ? 507  LEU   A CA  1 
ATOM   3787 C  C   . LEU   A 1 504 ? -5.22679  -7.23813  75.63152  1.000 18.63561 ? 507  LEU   A C   1 
ATOM   3788 O  O   . LEU   A 1 504 ? -6.44145  -7.05182  75.45238  1.000 19.36749 ? 507  LEU   A O   1 
ATOM   3789 C  CB  . LEU   A 1 504 ? -3.41799  -5.74565  74.73993  1.000 17.91231 ? 507  LEU   A CB  1 
ATOM   3790 C  CG  . LEU   A 1 504 ? -4.18382  -5.69465  73.40229  1.000 19.66907 ? 507  LEU   A CG  1 
ATOM   3791 C  CD1 . LEU   A 1 504 ? -5.17471  -4.57939  73.39754  1.000 17.47024 ? 507  LEU   A CD1 1 
ATOM   3792 C  CD2 . LEU   A 1 504 ? -3.17648  -5.48586  72.25252  1.000 22.99461 ? 507  LEU   A CD2 1 
ATOM   3793 N  N   . ALA   A 1 505 ? -4.67243  -8.45754  75.57933  1.000 16.34479 ? 508  ALA   A N   1 
ATOM   3794 C  CA  . ALA   A 1 505 ? -5.48395  -9.64026  75.29771  1.000 20.02872 ? 508  ALA   A CA  1 
ATOM   3795 C  C   . ALA   A 1 505 ? -6.49331  -9.91796  76.40172  1.000 22.70313 ? 508  ALA   A C   1 
ATOM   3796 O  O   . ALA   A 1 505 ? -7.62925  -10.29553 76.11327  1.000 19.17168 ? 508  ALA   A O   1 
ATOM   3797 C  CB  . ALA   A 1 505 ? -4.59598  -10.86203 75.09380  1.000 16.94226 ? 508  ALA   A CB  1 
ATOM   3798 N  N   . LEU   A 1 506 ? -6.09754  -9.78953  77.67326  1.000 20.70449 ? 509  LEU   A N   1 
ATOM   3799 C  CA  . LEU   A 1 506 ? -7.08460  -9.96990  78.73814  1.000 22.70399 ? 509  LEU   A CA  1 
ATOM   3800 C  C   . LEU   A 1 506 ? -8.21167  -8.95069  78.60600  1.000 18.11141 ? 509  LEU   A C   1 
ATOM   3801 O  O   . LEU   A 1 506 ? -9.39281  -9.28713  78.77385  1.000 21.49771 ? 509  LEU   A O   1 
ATOM   3802 C  CB  . LEU   A 1 506 ? -6.40841  -9.85783  80.10419  1.000 19.48656 ? 509  LEU   A CB  1 
ATOM   3803 C  CG  . LEU   A 1 506 ? -5.32171  -10.90251 80.45048  1.000 22.19511 ? 509  LEU   A CG  1 
ATOM   3804 C  CD1 . LEU   A 1 506 ? -4.62831  -10.54101 81.79069  1.000 21.98959 ? 509  LEU   A CD1 1 
ATOM   3805 C  CD2 . LEU   A 1 506 ? -5.88281  -12.31466 80.51159  1.000 21.86529 ? 509  LEU   A CD2 1 
ATOM   3806 N  N   . ARG   A 1 507 ? -7.86131  -7.70213  78.28449  1.000 17.65873 ? 510  ARG   A N   1 
ATOM   3807 C  CA  . ARG   A 1 507 ? -8.86077  -6.64748  78.10579  1.000 20.43527 ? 510  ARG   A CA  1 
ATOM   3808 C  C   . ARG   A 1 507 ? -9.82630  -6.97491  76.97267  1.000 22.42405 ? 510  ARG   A C   1 
ATOM   3809 O  O   . ARG   A 1 507 ? -11.04300 -6.79764  77.10163  1.000 20.14441 ? 510  ARG   A O   1 
ATOM   3810 C  CB  . ARG   A 1 507 ? -8.16051  -5.31913  77.81578  1.000 20.17010 ? 510  ARG   A CB  1 
ATOM   3811 C  CG  . ARG   A 1 507 ? -9.12034  -4.13968  77.64053  1.000 19.87015 ? 510  ARG   A CG  1 
ATOM   3812 C  CD  . ARG   A 1 507 ? -8.31836  -2.91046  77.23150  1.000 21.90479 ? 510  ARG   A CD  1 
ATOM   3813 N  NE  . ARG   A 1 507 ? -8.10127  -2.92046  75.78965  1.000 20.86654 ? 510  ARG   A NE  1 
ATOM   3814 C  CZ  . ARG   A 1 507 ? -7.20945  -2.18370  75.14321  1.000 25.64055 ? 510  ARG   A CZ  1 
ATOM   3815 N  NH1 . ARG   A 1 507 ? -6.24880  -1.54019  75.78608  1.000 27.21861 ? 510  ARG   A NH1 1 
ATOM   3816 N  NH2 . ARG   A 1 507 ? -7.27126  -2.11275  73.81502  1.000 17.27747 ? 510  ARG   A NH2 1 
ATOM   3817 N  N   . GLU   A 1 508 ? -9.29761  -7.41587  75.83012  1.000 19.99991 ? 511  GLU   A N   1 
ATOM   3818 C  CA  . GLU   A 1 508 ? -10.17637 -7.63276  74.69165  1.000 20.58841 ? 511  GLU   A CA  1 
ATOM   3819 C  C   . GLU   A 1 508 ? -10.97482 -8.91277  74.84583  1.000 23.26735 ? 511  GLU   A C   1 
ATOM   3820 O  O   . GLU   A 1 508 ? -12.09829 -8.99804  74.34565  1.000 21.90275 ? 511  GLU   A O   1 
ATOM   3821 C  CB  . GLU   A 1 508 ? -9.35887  -7.61787  73.40450  1.000 22.73040 ? 511  GLU   A CB  1 
ATOM   3822 C  CG  . GLU   A 1 508 ? -8.77339  -6.23785  73.13001  1.000 22.25957 ? 511  GLU   A CG  1 
ATOM   3823 C  CD  . GLU   A 1 508 ? -9.81756  -5.14096  73.10982  1.000 25.48749 ? 511  GLU   A CD  1 
ATOM   3824 O  OE1 . GLU   A 1 508 ? -10.89485 -5.29131  72.47431  1.000 22.04800 ? 511  GLU   A OE1 1 
ATOM   3825 O  OE2 . GLU   A 1 508 ? -9.56711  -4.10584  73.73717  1.000 24.01551 ? 511  GLU   A OE2 1 
ATOM   3826 N  N   . LEU   A 1 509 ? -10.43609 -9.90171  75.55554  1.000 24.27692 ? 512  LEU   A N   1 
ATOM   3827 C  CA  . LEU   A 1 509 ? -11.23186 -11.08221 75.89171  1.000 24.55002 ? 512  LEU   A CA  1 
ATOM   3828 C  C   . LEU   A 1 509 ? -12.35380 -10.73532 76.86865  1.000 25.62215 ? 512  LEU   A C   1 
ATOM   3829 O  O   . LEU   A 1 509 ? -13.47015 -11.25216 76.75078  1.000 27.92165 ? 512  LEU   A O   1 
ATOM   3830 C  CB  . LEU   A 1 509 ? -10.32136 -12.17495 76.46478  1.000 25.34583 ? 512  LEU   A CB  1 
ATOM   3831 C  CG  . LEU   A 1 509 ? -9.49303  -12.96867 75.43927  1.000 24.29135 ? 512  LEU   A CG  1 
ATOM   3832 C  CD1 . LEU   A 1 509 ? -8.39351  -13.75527 76.13728  1.000 26.64490 ? 512  LEU   A CD1 1 
ATOM   3833 C  CD2 . LEU   A 1 509 ? -10.41300 -13.94450 74.67080  1.000 25.07795 ? 512  LEU   A CD2 1 
ATOM   3834 N  N   . ALA   A 1 510 ? -12.08197 -9.85048  77.82917  1.000 21.04463 ? 513  ALA   A N   1 
ATOM   3835 C  CA  . ALA   A 1 510 ? -13.14580 -9.33724  78.68996  1.000 23.40302 ? 513  ALA   A CA  1 
ATOM   3836 C  C   . ALA   A 1 510 ? -14.22628 -8.65912  77.85872  1.000 20.88794 ? 513  ALA   A C   1 
ATOM   3837 O  O   . ALA   A 1 510 ? -15.42689 -8.91449  78.04306  1.000 23.36629 ? 513  ALA   A O   1 
ATOM   3838 C  CB  . ALA   A 1 510 ? -12.56184 -8.35734  79.71589  1.000 20.00034 ? 513  ALA   A CB  1 
ATOM   3839 N  N   . ARG   A 1 511 ? -13.81078 -7.80871  76.90867  1.000 23.35796 ? 514  ARG   A N   1 
ATOM   3840 C  CA  . ARG   A 1 511 ? -14.78124 -7.06676  76.10321  1.000 25.76590 ? 514  ARG   A CA  1 
ATOM   3841 C  C   . ARG   A 1 511 ? -15.70043 -7.99774  75.32273  1.000 30.96329 ? 514  ARG   A C   1 
ATOM   3842 O  O   . ARG   A 1 511 ? -16.87839 -7.67339  75.12502  1.000 26.56072 ? 514  ARG   A O   1 
ATOM   3843 C  CB  . ARG   A 1 511 ? -14.06859 -6.10092  75.14546  1.000 19.22492 ? 514  ARG   A CB  1 
ATOM   3844 C  CG  . ARG   A 1 511 ? -15.01398 -5.02539  74.58271  1.000 28.88211 ? 514  ARG   A CG  1 
ATOM   3845 C  CD  . ARG   A 1 511 ? -14.39188 -4.19136  73.46009  1.000 27.03055 ? 514  ARG   A CD  1 
ATOM   3846 N  NE  . ARG   A 1 511 ? -13.05374 -3.70474  73.77574  1.000 25.96245 ? 514  ARG   A NE  1 
ATOM   3847 C  CZ  . ARG   A 1 511 ? -12.76840 -2.57755  74.42211  1.000 25.18962 ? 514  ARG   A CZ  1 
ATOM   3848 N  NH1 . ARG   A 1 511 ? -13.71596 -1.80910  74.93915  1.000 24.12603 ? 514  ARG   A NH1 1 
ATOM   3849 N  NH2 . ARG   A 1 511 ? -11.49538 -2.20632  74.54541  1.000 24.18712 ? 514  ARG   A NH2 1 
ATOM   3850 N  N   . ALA   A 1 512 ? -15.18814 -9.15596  74.87533  1.000 29.11302 ? 515  ALA   A N   1 
ATOM   3851 C  CA  . ALA   A 1 512 ? -16.03178 -10.13509 74.19101  1.000 31.99116 ? 515  ALA   A CA  1 
ATOM   3852 C  C   . ALA   A 1 512 ? -17.04882 -10.76898 75.12229  1.000 28.99365 ? 515  ALA   A C   1 
ATOM   3853 O  O   . ALA   A 1 512 ? -18.09758 -11.22041 74.66056  1.000 36.87676 ? 515  ALA   A O   1 
ATOM   3854 C  CB  . ALA   A 1 512 ? -15.18676 -11.23401 73.54782  1.000 29.62737 ? 515  ALA   A CB  1 
ATOM   3855 N  N   . MET   A 1 513 ? -16.75792 -10.84598 76.41748  1.000 26.69613 ? 516  MET   A N   1 
ATOM   3856 C  CA  . MET   A 1 513 ? -17.75703 -11.32902 77.36847  1.000 25.85176 ? 516  MET   A CA  1 
ATOM   3857 C  C   . MET   A 1 513 ? -18.82298 -10.27611 77.64366  1.000 40.16721 ? 516  MET   A C   1 
ATOM   3858 O  O   . MET   A 1 513 ? -20.01535 -10.59639 77.73841  1.000 33.99507 ? 516  MET   A O   1 
ATOM   3859 C  CB  . MET   A 1 513 ? -17.10454 -11.72432 78.69281  1.000 33.20797 ? 516  MET   A CB  1 
ATOM   3860 C  CG  . MET   A 1 513 ? -16.05970 -12.81385 78.62149  1.000 45.78434 ? 516  MET   A CG  1 
ATOM   3861 S  SD  . MET   A 1 513 ? -15.29168 -13.10580 80.24992  1.000 54.23851 ? 516  MET   A SD  1 
ATOM   3862 C  CE  . MET   A 1 513 ? -16.44450 -12.33126 81.38901  1.000 47.48153 ? 516  MET   A CE  1 
ATOM   3863 N  N   . CYS   A 1 514 ? -18.41352 -9.01716  77.78728  1.000 27.86239 ? 517  CYS   A N   1 
ATOM   3864 C  CA  . CYS   A 1 514 ? -19.34408 -7.95672  78.15530  1.000 28.25636 ? 517  CYS   A CA  1 
ATOM   3865 C  C   . CYS   A 1 514 ? -18.74497 -6.63502  77.71884  1.000 28.19766 ? 517  CYS   A C   1 
ATOM   3866 O  O   . CYS   A 1 514 ? -17.56569 -6.38478  77.98255  1.000 24.95775 ? 517  CYS   A O   1 
ATOM   3867 C  CB  . CYS   A 1 514 ? -19.58977 -7.95570  79.66739  1.000 30.30299 ? 517  CYS   A CB  1 
ATOM   3868 S  SG  . CYS   A 1 514 ? -20.74343 -6.67029  80.22739  1.000 35.17667 ? 517  CYS   A SG  1 
ATOM   3869 N  N   . ALA   A 1 515 ? -19.54720 -5.78111  77.07823  1.000 27.41483 ? 518  ALA   A N   1 
ATOM   3870 C  CA  . ALA   A 1 515 ? -18.98813 -4.51446  76.60267  1.000 27.98054 ? 518  ALA   A CA  1 
ATOM   3871 C  C   . ALA   A 1 515 ? -18.53808 -3.60992  77.74667  1.000 21.74260 ? 518  ALA   A C   1 
ATOM   3872 O  O   . ALA   A 1 515 ? -17.73817 -2.69749  77.52015  1.000 23.00300 ? 518  ALA   A O   1 
ATOM   3873 C  CB  . ALA   A 1 515 ? -20.00164 -3.77292  75.72672  1.000 29.50415 ? 518  ALA   A CB  1 
ATOM   3874 N  N   . ALA   A 1 516 ? -19.05891 -3.81637  78.95407  1.000 23.96540 ? 519  ALA   A N   1 
ATOM   3875 C  CA  . ALA   A 1 516 ? -18.61582 -3.06660  80.12543  1.000 22.40537 ? 519  ALA   A CA  1 
ATOM   3876 C  C   . ALA   A 1 516 ? -17.34344 -3.71160  80.64249  1.000 23.64960 ? 519  ALA   A C   1 
ATOM   3877 O  O   . ALA   A 1 516 ? -17.39114 -4.79176  81.23384  1.000 23.38069 ? 519  ALA   A O   1 
ATOM   3878 C  CB  . ALA   A 1 516 ? -19.69194 -3.04881  81.21021  1.000 25.35797 ? 519  ALA   A CB  1 
ATOM   3879 N  N   . LEU   A 1 517 ? -16.21379 -3.04899  80.42038  1.000 24.58735 ? 520  LEU   A N   1 
ATOM   3880 C  CA  . LEU   A 1 517 ? -14.92673 -3.57784  80.83451  1.000 25.02834 ? 520  LEU   A CA  1 
ATOM   3881 C  C   . LEU   A 1 517 ? -14.85517 -3.62950  82.35706  1.000 26.86547 ? 520  LEU   A C   1 
ATOM   3882 O  O   . LEU   A 1 517 ? -15.47511 -2.81173  83.03905  1.000 27.07559 ? 520  LEU   A O   1 
ATOM   3883 C  CB  . LEU   A 1 517 ? -13.79537 -2.69472  80.31081  1.000 21.03597 ? 520  LEU   A CB  1 
ATOM   3884 C  CG  . LEU   A 1 517 ? -13.47998 -2.73617  78.81943  1.000 29.24384 ? 520  LEU   A CG  1 
ATOM   3885 C  CD1 . LEU   A 1 517 ? -12.29657 -1.80429  78.54243  1.000 24.90702 ? 520  LEU   A CD1 1 
ATOM   3886 C  CD2 . LEU   A 1 517 ? -13.15343 -4.14954  78.37341  1.000 31.18426 ? 520  LEU   A CD2 1 
ATOM   3887 N  N   . PRO   A 1 518 ? -14.09391 -4.56338  82.91578  1.000 23.92732 ? 521  PRO   A N   1 
ATOM   3888 C  CA  . PRO   A 1 518 ? -13.96540 -4.61276  84.37248  1.000 30.60604 ? 521  PRO   A CA  1 
ATOM   3889 C  C   . PRO   A 1 518 ? -13.15335 -3.42270  84.85542  1.000 24.59624 ? 521  PRO   A C   1 
ATOM   3890 O  O   . PRO   A 1 518 ? -12.45513 -2.76173  84.08377  1.000 24.18627 ? 521  PRO   A O   1 
ATOM   3891 C  CB  . PRO   A 1 518 ? -13.24094 -5.94001  84.63115  1.000 32.79659 ? 521  PRO   A CB  1 
ATOM   3892 C  CG  . PRO   A 1 518 ? -12.52357 -6.24172  83.37984  1.000 31.65841 ? 521  PRO   A CG  1 
ATOM   3893 C  CD  . PRO   A 1 518 ? -13.33992 -5.63647  82.24123  1.000 24.75077 ? 521  PRO   A CD  1 
ATOM   3894 N  N   . GLU   A 1 519 ? -13.26513 -3.15039  86.15341  1.000 23.41519 ? 522  GLU   A N   1 
ATOM   3895 C  CA  . GLU   A 1 519 ? -12.60069 -1.98819  86.73493  1.000 27.82057 ? 522  GLU   A CA  1 
ATOM   3896 C  C   . GLU   A 1 519 ? -11.10871 -2.01176  86.49665  1.000 23.72712 ? 522  GLU   A C   1 
ATOM   3897 O  O   . GLU   A 1 519 ? -10.48598 -0.94990  86.38430  1.000 25.56166 ? 522  GLU   A O   1 
ATOM   3898 C  CB  . GLU   A 1 519 ? -12.86083 -1.92345  88.22953  1.000 26.45675 ? 522  GLU   A CB  1 
ATOM   3899 C  CG  . GLU   A 1 519 ? -14.27865 -1.62667  88.56748  1.000 34.39002 ? 522  GLU   A CG  1 
ATOM   3900 C  CD  . GLU   A 1 519 ? -14.60934 -2.18841  89.91905  1.000 72.00318 ? 522  GLU   A CD  1 
ATOM   3901 O  OE1 . GLU   A 1 519 ? -14.00072 -1.71105  90.90511  1.000 57.46883 ? 522  GLU   A OE1 1 
ATOM   3902 O  OE2 . GLU   A 1 519 ? -15.42861 -3.13582  89.98484  1.000 77.57850 ? 522  GLU   A OE2 1 
ATOM   3903 N  N   . MET   A 1 520 ? -10.52720 -3.21222  86.42357  1.000 20.78632 ? 523  MET   A N   1 
ATOM   3904 C  CA  . MET   A 1 520 ? -9.10560  -3.35677  86.11993  1.000 19.72315 ? 523  MET   A CA  1 
ATOM   3905 C  C   . MET   A 1 520 ? -8.68582  -2.48625  84.93473  1.000 22.20105 ? 523  MET   A C   1 
ATOM   3906 O  O   . MET   A 1 520 ? -7.65914  -1.80211  84.98571  1.000 21.74062 ? 523  MET   A O   1 
ATOM   3907 C  CB  . MET   A 1 520 ? -8.81129  -4.82990  85.82727  1.000 25.12962 ? 523  MET   A CB  1 
ATOM   3908 C  CG  . MET   A 1 520 ? -7.44005  -5.03319  85.24604  1.000 25.24851 ? 523  MET   A CG  1 
ATOM   3909 S  SD  . MET   A 1 520 ? -6.17736  -4.95464  86.54116  1.000 24.90863 ? 523  MET   A SD  1 
ATOM   3910 C  CE  . MET   A 1 520 ? -4.72052  -4.71365  85.49164  1.000 20.36984 ? 523  MET   A CE  1 
ATOM   3911 N  N   . PHE   A 1 521 ? -9.47610  -2.48425  83.86449  1.000 23.58028 ? 524  PHE   A N   1 
ATOM   3912 C  CA  . PHE   A 1 521 ? -9.13072  -1.74734  82.65253  1.000 18.27913 ? 524  PHE   A CA  1 
ATOM   3913 C  C   . PHE   A 1 521 ? -9.81472  -0.39151  82.52895  1.000 20.43178 ? 524  PHE   A C   1 
ATOM   3914 O  O   . PHE   A 1 521 ? -9.43012  0.39366   81.65696  1.000 24.92559 ? 524  PHE   A O   1 
ATOM   3915 C  CB  . PHE   A 1 521 ? -9.44774  -2.62672  81.43127  1.000 23.13235 ? 524  PHE   A CB  1 
ATOM   3916 C  CG  . PHE   A 1 521 ? -8.69064  -3.90902  81.44809  1.000 21.73432 ? 524  PHE   A CG  1 
ATOM   3917 C  CD1 . PHE   A 1 521 ? -7.30624  -3.88927  81.35324  1.000 19.00791 ? 524  PHE   A CD1 1 
ATOM   3918 C  CD2 . PHE   A 1 521 ? -9.33593  -5.11840  81.64662  1.000 24.07458 ? 524  PHE   A CD2 1 
ATOM   3919 C  CE1 . PHE   A 1 521 ? -6.56922  -5.05579  81.40502  1.000 21.17818 ? 524  PHE   A CE1 1 
ATOM   3920 C  CE2 . PHE   A 1 521 ? -8.60727  -6.31107  81.68226  1.000 22.41250 ? 524  PHE   A CE2 1 
ATOM   3921 C  CZ  . PHE   A 1 521 ? -7.21761  -6.27974  81.58623  1.000 20.52494 ? 524  PHE   A CZ  1 
ATOM   3922 N  N   . MET   A 1 522 ? -10.80954 -0.08594  83.37615  1.000 20.25818 ? 525  MET   A N   1 
ATOM   3923 C  CA  . MET   A 1 522 ? -11.36382 1.26290   83.44212  1.000 24.30454 ? 525  MET   A CA  1 
ATOM   3924 C  C   . MET   A 1 522 ? -10.57800 2.16895   84.38413  1.000 30.49106 ? 525  MET   A C   1 
ATOM   3925 O  O   . MET   A 1 522 ? -10.68390 3.40275   84.28483  1.000 24.22353 ? 525  MET   A O   1 
ATOM   3926 C  CB  . MET   A 1 522 ? -12.82727 1.20462   83.88808  1.000 21.54302 ? 525  MET   A CB  1 
ATOM   3927 C  CG  . MET   A 1 522 ? -13.66183 0.32540   82.98026  1.000 27.52840 ? 525  MET   A CG  1 
ATOM   3928 S  SD  . MET   A 1 522 ? -13.72312 0.95810   81.30735  1.000 33.76952 ? 525  MET   A SD  1 
ATOM   3929 C  CE  . MET   A 1 522 ? -14.87966 2.32147   81.51325  1.000 29.81007 ? 525  MET   A CE  1 
ATOM   3930 N  N   . ASP   A 1 523 ? -9.80216  1.56459   85.28331  1.000 25.11979 ? 526  ASP   A N   1 
ATOM   3931 C  CA  . ASP   A 1 523 ? -8.92263  2.25536   86.21878  1.000 23.29926 ? 526  ASP   A CA  1 
ATOM   3932 C  C   . ASP   A 1 523 ? -8.10711  3.34335   85.53050  1.000 27.23392 ? 526  ASP   A C   1 
ATOM   3933 O  O   . ASP   A 1 523 ? -7.44293  3.08783   84.52566  1.000 22.58056 ? 526  ASP   A O   1 
ATOM   3934 C  CB  . ASP   A 1 523 ? -7.99995  1.19454   86.81642  1.000 27.38771 ? 526  ASP   A CB  1 
ATOM   3935 C  CG  . ASP   A 1 523 ? -7.16492  1.68631   87.97364  1.000 32.49667 ? 526  ASP   A CG  1 
ATOM   3936 O  OD1 . ASP   A 1 523 ? -7.22909  2.87228   88.36167  1.000 27.70929 ? 526  ASP   A OD1 1 
ATOM   3937 O  OD2 . ASP   A 1 523 ? -6.41649  0.83276   88.48154  1.000 30.78438 ? 526  ASP   A OD2 1 
ATOM   3938 N  N   . GLU   A 1 524 ? -8.10896  4.55012   86.11041  1.000 21.49794 ? 527  GLU   A N   1 
ATOM   3939 C  CA  . GLU   A 1 524 ? -7.28715  5.63129   85.54926  1.000 26.37465 ? 527  GLU   A CA  1 
ATOM   3940 C  C   . GLU   A 1 524 ? -5.80544  5.25693   85.50375  1.000 24.73212 ? 527  GLU   A C   1 
ATOM   3941 O  O   . GLU   A 1 524 ? -5.07400  5.69599   84.60646  1.000 22.84163 ? 527  GLU   A O   1 
ATOM   3942 C  CB  . GLU   A 1 524 ? -7.49743  6.92193   86.34533  1.000 32.53454 ? 527  GLU   A CB  1 
ATOM   3943 C  CG  . GLU   A 1 524 ? -6.74986  8.16425   85.78373  1.000 34.10225 ? 527  GLU   A CG  1 
ATOM   3944 C  CD  . GLU   A 1 524 ? -7.10197  8.51493   84.33482  1.000 41.12773 ? 527  GLU   A CD  1 
ATOM   3945 O  OE1 . GLU   A 1 524 ? -8.17697  8.12920   83.83877  1.000 37.20626 ? 527  GLU   A OE1 1 
ATOM   3946 O  OE2 . GLU   A 1 524 ? -6.28638  9.19171   83.67372  1.000 39.97181 ? 527  GLU   A OE2 1 
ATOM   3947 N  N   . THR   A 1 525 ? -5.34098  4.44659   86.44740  1.000 20.17087 ? 528  THR   A N   1 
ATOM   3948 C  CA  . THR   A 1 525 ? -3.94933  3.99559   86.38695  1.000 23.52309 ? 528  THR   A CA  1 
ATOM   3949 C  C   . THR   A 1 525 ? -3.68523  3.23083   85.10153  1.000 25.84308 ? 528  THR   A C   1 
ATOM   3950 O  O   . THR   A 1 525 ? -2.63402  3.39350   84.48261  1.000 20.99385 ? 528  THR   A O   1 
ATOM   3951 C  CB  . THR   A 1 525 ? -3.61483  3.11579   87.59208  1.000 22.36590 ? 528  THR   A CB  1 
ATOM   3952 O  OG1 . THR   A 1 525 ? -3.75355  3.87711   88.80124  1.000 26.02062 ? 528  THR   A OG1 1 
ATOM   3953 C  CG2 . THR   A 1 525 ? -2.19010  2.58018   87.48052  1.000 26.42690 ? 528  THR   A CG2 1 
ATOM   3954 N  N   . TYR   A 1 526 ? -4.61643  2.36705   84.69807  1.000 20.19879 ? 529  TYR   A N   1 
ATOM   3955 C  CA  . TYR   A 1 526 ? -4.40301  1.62410   83.46134  1.000 20.99088 ? 529  TYR   A CA  1 
ATOM   3956 C  C   . TYR   A 1 526 ? -4.44417  2.54753   82.24863  1.000 21.52104 ? 529  TYR   A C   1 
ATOM   3957 O  O   . TYR   A 1 526 ? -3.60522  2.42629   81.34166  1.000 19.32439 ? 529  TYR   A O   1 
ATOM   3958 C  CB  . TYR   A 1 526 ? -5.43653  0.50467   83.33616  1.000 19.35970 ? 529  TYR   A CB  1 
ATOM   3959 C  CG  . TYR   A 1 526 ? -5.30572  -0.25790  82.02474  1.000 20.29933 ? 529  TYR   A CG  1 
ATOM   3960 C  CD1 . TYR   A 1 526 ? -4.27893  -1.18077  81.83000  1.000 22.00730 ? 529  TYR   A CD1 1 
ATOM   3961 C  CD2 . TYR   A 1 526 ? -6.19831  -0.04192  80.98677  1.000 19.96076 ? 529  TYR   A CD2 1 
ATOM   3962 C  CE1 . TYR   A 1 526 ? -4.14853  -1.87854  80.63471  1.000 19.60203 ? 529  TYR   A CE1 1 
ATOM   3963 C  CE2 . TYR   A 1 526 ? -6.06964  -0.71590  79.77815  1.000 20.82926 ? 529  TYR   A CE2 1 
ATOM   3964 C  CZ  . TYR   A 1 526 ? -5.04601  -1.63760  79.60718  1.000 19.87879 ? 529  TYR   A CZ  1 
ATOM   3965 O  OH  . TYR   A 1 526 ? -4.91586  -2.32937  78.41363  1.000 20.62020 ? 529  TYR   A OH  1 
ATOM   3966 N  N   . LEU   A 1 527 ? -5.40589  3.47744   82.20201  1.000 19.94764 ? 530  LEU   A N   1 
ATOM   3967 C  CA  . LEU   A 1 527 ? -5.45755  4.39730   81.05879  1.000 21.72456 ? 530  LEU   A CA  1 
ATOM   3968 C  C   . LEU   A 1 527 ? -4.19393  5.24302   80.99592  1.000 18.48708 ? 530  LEU   A C   1 
ATOM   3969 O  O   . LEU   A 1 527 ? -3.59256  5.40913   79.92938  1.000 22.00823 ? 530  LEU   A O   1 
ATOM   3970 C  CB  . LEU   A 1 527 ? -6.68470  5.30348   81.15018  1.000 18.96232 ? 530  LEU   A CB  1 
ATOM   3971 C  CG  . LEU   A 1 527 ? -8.02442  4.56035   81.27984  1.000 25.78308 ? 530  LEU   A CG  1 
ATOM   3972 C  CD1 . LEU   A 1 527 ? -9.19602  5.54665   81.41502  1.000 28.61633 ? 530  LEU   A CD1 1 
ATOM   3973 C  CD2 . LEU   A 1 527 ? -8.19872  3.67980   80.07658  1.000 23.57236 ? 530  LEU   A CD2 1 
ATOM   3974 N  N   A MET   A 1 528 ? -3.74396  5.76094   82.13195  0.389 19.97217 ? 531  MET   A N   1 
ATOM   3975 N  N   B MET   A 1 528 ? -3.77463  5.76767   82.15025  0.611 19.91257 ? 531  MET   A N   1 
ATOM   3976 C  CA  A MET   A 1 528 ? -2.56346  6.60956   82.07925  0.389 22.49041 ? 531  MET   A CA  1 
ATOM   3977 C  CA  B MET   A 1 528 ? -2.56221  6.57355   82.22119  0.611 22.70984 ? 531  MET   A CA  1 
ATOM   3978 C  C   A MET   A 1 528 ? -1.29994  5.80201   81.81376  0.389 22.10369 ? 531  MET   A C   1 
ATOM   3979 C  C   B MET   A 1 528 ? -1.37025  5.78045   81.71957  0.611 22.18643 ? 531  MET   A C   1 
ATOM   3980 O  O   A MET   A 1 528 ? -0.30237  6.36810   81.35751  0.389 23.02992 ? 531  MET   A O   1 
ATOM   3981 O  O   B MET   A 1 528 ? -0.52218  6.30745   80.98945  0.611 21.06154 ? 531  MET   A O   1 
ATOM   3982 C  CB  A MET   A 1 528 ? -2.43867  7.41555   83.37437  0.389 24.59954 ? 531  MET   A CB  1 
ATOM   3983 C  CB  B MET   A 1 528 ? -2.32113  7.03812   83.66777  0.611 22.59132 ? 531  MET   A CB  1 
ATOM   3984 C  CG  A MET   A 1 528 ? -1.49330  8.60622   83.27112  0.389 22.94168 ? 531  MET   A CG  1 
ATOM   3985 C  CG  B MET   A 1 528 ? -3.19883  8.20418   84.14747  0.611 25.60217 ? 531  MET   A CG  1 
ATOM   3986 S  SD  A MET   A 1 528 ? 0.14346   8.16756   83.85389  0.389 48.03977 ? 531  MET   A SD  1 
ATOM   3987 S  SD  B MET   A 1 528 ? -2.98540  8.58808   85.91858  0.611 31.85826 ? 531  MET   A SD  1 
ATOM   3988 C  CE  A MET   A 1 528 ? -0.26865  7.63527   85.48390  0.389 36.63716 ? 531  MET   A CE  1 
ATOM   3989 C  CE  B MET   A 1 528 ? -1.22047  8.95120   85.94643  0.611 33.59506 ? 531  MET   A CE  1 
ATOM   3990 N  N   . SER   A 1 529 ? -1.33351  4.48713   82.05257  1.000 18.66727 ? 532  SER   A N   1 
ATOM   3991 C  CA  . SER   A 1 529 ? -0.18167  3.64117   81.75595  1.000 19.90379 ? 532  SER   A CA  1 
ATOM   3992 C  C   . SER   A 1 529 ? 0.06986   3.48122   80.26495  1.000 19.45962 ? 532  SER   A C   1 
ATOM   3993 O  O   . SER   A 1 529 ? 1.18435   3.12250   79.87643  1.000 17.92507 ? 532  SER   A O   1 
ATOM   3994 C  CB  . SER   A 1 529 ? -0.37625  2.26785   82.40639  1.000 20.09540 ? 532  SER   A CB  1 
ATOM   3995 O  OG  . SER   A 1 529 ? -1.16219  1.40595   81.58956  1.000 20.45441 ? 532  SER   A OG  1 
ATOM   3996 N  N   . ASN   A 1 530 ? -0.91977  3.75916   79.42046  1.000 16.54328 ? 533  ASN   A N   1 
ATOM   3997 C  CA  . ASN   A 1 530 ? -0.83967  3.50534   77.98745  1.000 16.51547 ? 533  ASN   A CA  1 
ATOM   3998 C  C   . ASN   A 1 530 ? -0.80875  4.78401   77.15984  1.000 19.54000 ? 533  ASN   A C   1 
ATOM   3999 O  O   . ASN   A 1 530 ? -0.90985  4.72184   75.93053  1.000 20.78988 ? 533  ASN   A O   1 
ATOM   4000 C  CB  . ASN   A 1 530 ? -2.01386  2.60833   77.56048  1.000 20.42959 ? 533  ASN   A CB  1 
ATOM   4001 C  CG  . ASN   A 1 530 ? -1.82954  1.18053   78.02313  1.000 25.12710 ? 533  ASN   A CG  1 
ATOM   4002 O  OD1 . ASN   A 1 530 ? -0.69857  0.67000   78.03589  1.000 23.21695 ? 533  ASN   A OD1 1 
ATOM   4003 N  ND2 . ASN   A 1 530 ? -2.91938  0.52767   78.41884  1.000 26.23192 ? 533  ASN   A ND2 1 
ATOM   4004 N  N   . ARG   A 1 531 ? -0.67125  5.92983   77.80356  1.000 19.40669 ? 534  ARG   A N   1 
ATOM   4005 C  CA  . ARG   A 1 531 ? -0.46265  7.21395   77.14476  1.000 15.18849 ? 534  ARG   A CA  1 
ATOM   4006 C  C   . ARG   A 1 531 ? 1.03606   7.48034   77.17211  1.000 20.60240 ? 534  ARG   A C   1 
ATOM   4007 O  O   . ARG   A 1 531 ? 1.56754   7.96548   78.17284  1.000 17.69575 ? 534  ARG   A O   1 
ATOM   4008 C  CB  . ARG   A 1 531 ? -1.22688  8.31790   77.86308  1.000 20.82620 ? 534  ARG   A CB  1 
ATOM   4009 C  CG  . ARG   A 1 531 ? -2.74177  8.14675   77.73451  1.000 20.20065 ? 534  ARG   A CG  1 
ATOM   4010 C  CD  . ARG   A 1 531 ? -3.45036  9.17069   78.60625  1.000 24.46234 ? 534  ARG   A CD  1 
ATOM   4011 N  NE  . ARG   A 1 531 ? -4.85671  8.82511   78.67006  1.000 37.81353 ? 534  ARG   A NE  1 
ATOM   4012 C  CZ  . ARG   A 1 531 ? -5.59345  8.91445   79.76142  1.000 33.03502 ? 534  ARG   A CZ  1 
ATOM   4013 N  NH1 . ARG   A 1 531 ? -5.07593  9.32721   80.90777  1.000 31.02937 ? 534  ARG   A NH1 1 
ATOM   4014 N  NH2 . ARG   A 1 531 ? -6.87423  8.56447   79.70043  1.000 32.81839 ? 534  ARG   A NH2 1 
ATOM   4015 N  N   . PHE   A 1 532 ? 1.71713   7.17526   76.07117  1.000 17.84110 ? 535  PHE   A N   1 
ATOM   4016 C  CA  . PHE   A 1 532 ? 3.18761   7.20030   76.07516  1.000 17.65845 ? 535  PHE   A CA  1 
ATOM   4017 C  C   . PHE   A 1 532 ? 3.71262   8.57712   75.68752  1.000 20.04365 ? 535  PHE   A C   1 
ATOM   4018 O  O   . PHE   A 1 532 ? 3.99411   8.87127   74.52015  1.000 19.15596 ? 535  PHE   A O   1 
ATOM   4019 C  CB  . PHE   A 1 532 ? 3.70060   6.09785   75.16198  1.000 17.55524 ? 535  PHE   A CB  1 
ATOM   4020 C  CG  . PHE   A 1 532 ? 3.27690   4.72920   75.62944  1.000 21.19102 ? 535  PHE   A CG  1 
ATOM   4021 C  CD1 . PHE   A 1 532 ? 3.71594   4.24439   76.85207  1.000 17.66566 ? 535  PHE   A CD1 1 
ATOM   4022 C  CD2 . PHE   A 1 532 ? 2.42914   3.94182   74.86304  1.000 21.76065 ? 535  PHE   A CD2 1 
ATOM   4023 C  CE1 . PHE   A 1 532 ? 3.33284   2.99695   77.30273  1.000 19.69585 ? 535  PHE   A CE1 1 
ATOM   4024 C  CE2 . PHE   A 1 532 ? 2.05461   2.68971   75.29501  1.000 23.04840 ? 535  PHE   A CE2 1 
ATOM   4025 C  CZ  . PHE   A 1 532 ? 2.48568   2.21556   76.51389  1.000 16.81973 ? 535  PHE   A CZ  1 
ATOM   4026 N  N   . VAL   A 1 533 ? 3.88396   9.42128   76.70757  1.000 16.54348 ? 536  VAL   A N   1 
ATOM   4027 C  CA  . VAL   A 1 533 ? 4.39417   10.77068  76.53430  1.000 17.26082 ? 536  VAL   A CA  1 
ATOM   4028 C  C   . VAL   A 1 533 ? 5.81227   10.74150  75.97979  1.000 19.98293 ? 536  VAL   A C   1 
ATOM   4029 O  O   . VAL   A 1 533 ? 6.23690   11.68659  75.30621  1.000 17.57443 ? 536  VAL   A O   1 
ATOM   4030 C  CB  . VAL   A 1 533 ? 4.31263   11.51838  77.88723  1.000 17.99671 ? 536  VAL   A CB  1 
ATOM   4031 C  CG1 . VAL   A 1 533 ? 4.93757   12.92107  77.79882  1.000 19.29796 ? 536  VAL   A CG1 1 
ATOM   4032 C  CG2 . VAL   A 1 533 ? 2.84081   11.64010  78.32383  1.000 20.04856 ? 536  VAL   A CG2 1 
ATOM   4033 N  N   . LEU   A 1 534 ? 6.54720   9.65505   76.19723  1.000 19.53483 ? 537  LEU   A N   1 
ATOM   4034 C  CA  . LEU   A 1 534 ? 7.83616   9.45036   75.52256  1.000 15.79291 ? 537  LEU   A CA  1 
ATOM   4035 C  C   . LEU   A 1 534 ? 7.77324   8.13554   74.75260  1.000 16.33043 ? 537  LEU   A C   1 
ATOM   4036 O  O   . LEU   A 1 534 ? 7.61166   7.06900   75.34884  1.000 16.69574 ? 537  LEU   A O   1 
ATOM   4037 C  CB  . LEU   A 1 534 ? 8.98085   9.45060   76.53847  1.000 17.78477 ? 537  LEU   A CB  1 
ATOM   4038 C  CG  . LEU   A 1 534 ? 10.41774  9.23259   76.05136  1.000 18.37682 ? 537  LEU   A CG  1 
ATOM   4039 C  CD1 . LEU   A 1 534 ? 10.78069  10.22776  74.94658  1.000 17.76377 ? 537  LEU   A CD1 1 
ATOM   4040 C  CD2 . LEU   A 1 534 ? 11.40543  9.29569   77.23899  1.000 22.77505 ? 537  LEU   A CD2 1 
ATOM   4041 N  N   . SER   A 1 535 ? 7.90070   8.19675   73.42908  1.000 16.01409 ? 538  SER   A N   1 
ATOM   4042 C  CA  . SER   A 1 535 ? 7.73768   7.01593   72.58540  1.000 14.85136 ? 538  SER   A CA  1 
ATOM   4043 C  C   . SER   A 1 535 ? 9.00482   6.84287   71.76425  1.000 15.59700 ? 538  SER   A C   1 
ATOM   4044 O  O   . SER   A 1 535 ? 9.39923   7.76015   71.04377  1.000 18.31323 ? 538  SER   A O   1 
ATOM   4045 C  CB  . SER   A 1 535 ? 6.50983   7.15814   71.67345  1.000 18.14422 ? 538  SER   A CB  1 
ATOM   4046 O  OG  . SER   A 1 535 ? 6.37805   5.99038   70.87187  1.000 23.21777 ? 538  SER   A OG  1 
ATOM   4047 N  N   . THR   A 1 536 ? 9.66498   5.68661   71.89281  1.000 18.41708 ? 539  THR   A N   1 
ATOM   4048 C  CA  . THR   A 1 536 ? 11.06640  5.56476   71.49157  1.000 18.93756 ? 539  THR   A CA  1 
ATOM   4049 C  C   . THR   A 1 536 ? 11.30626  4.25468   70.74076  1.000 18.96989 ? 539  THR   A C   1 
ATOM   4050 O  O   . THR   A 1 536 ? 10.51791  3.30774   70.80913  1.000 17.91043 ? 539  THR   A O   1 
ATOM   4051 C  CB  . THR   A 1 536 ? 12.03461  5.61001   72.71435  1.000 19.06128 ? 539  THR   A CB  1 
ATOM   4052 O  OG1 . THR   A 1 536 ? 11.93918  4.37791   73.44713  1.000 20.03787 ? 539  THR   A OG1 1 
ATOM   4053 C  CG2 . THR   A 1 536 ? 11.67129  6.75679   73.71036  1.000 19.74518 ? 539  THR   A CG2 1 
ATOM   4054 N  N   . SER   A 1 537 ? 12.43801  4.20233   70.04177  1.000 16.85928 ? 540  SER   A N   1 
ATOM   4055 C  CA  . SER   A 1 537 ? 12.88817  2.96144   69.43520  1.000 16.43478 ? 540  SER   A CA  1 
ATOM   4056 C  C   . SER   A 1 537 ? 14.31949  3.15812   68.98397  1.000 20.71265 ? 540  SER   A C   1 
ATOM   4057 O  O   . SER   A 1 537 ? 14.74179  4.28121   68.68877  1.000 17.99874 ? 540  SER   A O   1 
ATOM   4058 C  CB  . SER   A 1 537 ? 12.02728  2.55391   68.23332  1.000 18.21377 ? 540  SER   A CB  1 
ATOM   4059 O  OG  . SER   A 1 537 ? 12.03630  3.57996   67.27598  1.000 25.15679 ? 540  SER   A OG  1 
ATOM   4060 N  N   A GLN   A 1 538 ? 15.07341  2.06770   68.99473  0.635 17.51869 ? 541  GLN   A N   1 
ATOM   4061 N  N   B GLN   A 1 538 ? 15.04952  2.04581   68.91565  0.365 17.58647 ? 541  GLN   A N   1 
ATOM   4062 C  CA  A GLN   A 1 538 ? 16.38312  2.01363   68.36493  0.635 20.68296 ? 541  GLN   A CA  1 
ATOM   4063 C  CA  B GLN   A 1 538 ? 16.40645  1.99045   68.38227  0.365 20.76376 ? 541  GLN   A CA  1 
ATOM   4064 C  C   A GLN   A 1 538 ? 16.20225  1.40713   66.98701  0.635 23.04282 ? 541  GLN   A C   1 
ATOM   4065 C  C   B GLN   A 1 538 ? 16.35149  1.34372   67.00563  0.365 22.92351 ? 541  GLN   A C   1 
ATOM   4066 O  O   A GLN   A 1 538 ? 15.59808  0.33752   66.84883  0.635 20.16762 ? 541  GLN   A O   1 
ATOM   4067 O  O   B GLN   A 1 538 ? 15.99738  0.16590   66.88595  0.365 19.82718 ? 541  GLN   A O   1 
ATOM   4068 C  CB  A GLN   A 1 538 ? 17.37436  1.16447   69.16869  0.635 21.68320 ? 541  GLN   A CB  1 
ATOM   4069 C  CB  B GLN   A 1 538 ? 17.32131  1.17616   69.30296  0.365 21.64511 ? 541  GLN   A CB  1 
ATOM   4070 C  CG  A GLN   A 1 538 ? 18.80776  1.33493   68.67036  0.635 21.73230 ? 541  GLN   A CG  1 
ATOM   4071 C  CG  B GLN   A 1 538 ? 18.75819  1.02190   68.79885  0.365 23.26209 ? 541  GLN   A CG  1 
ATOM   4072 C  CD  A GLN   A 1 538 ? 19.75422  0.25572   69.15798  0.635 28.49006 ? 541  GLN   A CD  1 
ATOM   4073 C  CD  B GLN   A 1 538 ? 19.57859  0.04394   69.63872  0.365 29.45534 ? 541  GLN   A CD  1 
ATOM   4074 O  OE1 A GLN   A 1 538 ? 19.69074  -0.18929  70.30829  0.635 30.07088 ? 541  GLN   A OE1 1 
ATOM   4075 O  OE1 B GLN   A 1 538 ? 20.47409  0.44226   70.38635  0.365 19.46424 ? 541  GLN   A OE1 1 
ATOM   4076 N  NE2 A GLN   A 1 538 ? 20.63493  -0.17379  68.27984  0.635 23.82270 ? 541  GLN   A NE2 1 
ATOM   4077 N  NE2 B GLN   A 1 538 ? 19.27135  -1.24168  69.51587  0.365 21.51150 ? 541  GLN   A NE2 1 
ATOM   4078 N  N   . VAL   A 1 539 ? 16.68633  2.10293   65.97000  1.000 21.58507 ? 542  VAL   A N   1 
ATOM   4079 C  CA  . VAL   A 1 539 ? 16.73524  1.51819   64.64171  1.000 21.01432 ? 542  VAL   A CA  1 
ATOM   4080 C  C   . VAL   A 1 539 ? 18.14711  1.70270   64.12021  1.000 22.63310 ? 542  VAL   A C   1 
ATOM   4081 O  O   . VAL   A 1 539 ? 18.46364  2.74662   63.53887  1.000 23.29906 ? 542  VAL   A O   1 
ATOM   4082 C  CB  . VAL   A 1 539 ? 15.71079  2.12201   63.68175  1.000 29.11862 ? 542  VAL   A CB  1 
ATOM   4083 C  CG1 . VAL   A 1 539 ? 15.75867  1.32266   62.36535  1.000 26.64513 ? 542  VAL   A CG1 1 
ATOM   4084 C  CG2 . VAL   A 1 539 ? 14.31585  2.07275   64.31240  1.000 29.16830 ? 542  VAL   A CG2 1 
ATOM   4085 N  N   . PRO   A 1 540 ? 19.01980  0.72602   64.32516  1.000 22.35168 ? 543  PRO   A N   1 
ATOM   4086 C  CA  . PRO   A 1 540 ? 20.39887  0.86172   63.86071  1.000 24.75717 ? 543  PRO   A CA  1 
ATOM   4087 C  C   . PRO   A 1 540 ? 20.49775  0.65639   62.35933  1.000 30.10771 ? 543  PRO   A C   1 
ATOM   4088 O  O   . PRO   A 1 540 ? 19.78925  -0.16486  61.77749  1.000 28.25809 ? 543  PRO   A O   1 
ATOM   4089 C  CB  . PRO   A 1 540 ? 21.13636  -0.25083  64.62287  1.000 34.50962 ? 543  PRO   A CB  1 
ATOM   4090 C  CG  . PRO   A 1 540 ? 20.08098  -1.28003  64.90552  1.000 29.71936 ? 543  PRO   A CG  1 
ATOM   4091 C  CD  . PRO   A 1 540 ? 18.79161  -0.51574  65.08670  1.000 28.19188 ? 543  PRO   A CD  1 
ATOM   4092 N  N   . THR   A 1 541 ? 21.39269  1.41059   61.72200  1.000 24.04673 ? 544  THR   A N   1 
ATOM   4093 C  CA  . THR   A 1 541 ? 21.64512  1.22497   60.29766  1.000 28.09077 ? 544  THR   A CA  1 
ATOM   4094 C  C   . THR   A 1 541 ? 23.14814  1.16403   60.08465  1.000 34.08034 ? 544  THR   A C   1 
ATOM   4095 O  O   . THR   A 1 541 ? 23.92709  1.56108   60.94769  1.000 32.13561 ? 544  THR   A O   1 
ATOM   4096 C  CB  . THR   A 1 541 ? 21.06484  2.35554   59.43331  1.000 35.79801 ? 544  THR   A CB  1 
ATOM   4097 O  OG1 . THR   A 1 541 ? 21.75690  3.58273   59.73035  1.000 39.52675 ? 544  THR   A OG1 1 
ATOM   4098 C  CG2 . THR   A 1 541 ? 19.59779  2.53634   59.69653  1.000 29.57417 ? 544  THR   A CG2 1 
ATOM   4099 N  N   . THR   A 1 542 ? 23.54763  0.67531   58.91101  1.000 33.10516 ? 545  THR   A N   1 
ATOM   4100 C  CA  . THR   A 1 542 ? 24.96199  0.57027   58.56185  1.000 44.01801 ? 545  THR   A CA  1 
ATOM   4101 C  C   . THR   A 1 542 ? 25.41873  1.65763   57.60140  1.000 39.56825 ? 545  THR   A C   1 
ATOM   4102 O  O   . THR   A 1 542 ? 26.61868  1.93730   57.52755  1.000 47.91309 ? 545  THR   A O   1 
ATOM   4103 C  CB  . THR   A 1 542 ? 25.26332  -0.79557  57.93206  1.000 38.15589 ? 545  THR   A CB  1 
ATOM   4104 O  OG1 . THR   A 1 542 ? 25.06421  -0.72496  56.51642  1.000 74.87682 ? 545  THR   A OG1 1 
ATOM   4105 C  CG2 . THR   A 1 542 ? 24.33223  -1.86809  58.49869  1.000 52.44588 ? 545  THR   A CG2 1 
ATOM   4106 N  N   . THR   A 1 543 ? 24.49904  2.25087   56.85882  1.000 31.32492 ? 546  THR   A N   1 
ATOM   4107 C  CA  . THR   A 1 543 ? 24.76832  3.35676   55.96694  1.000 41.45281 ? 546  THR   A CA  1 
ATOM   4108 C  C   . THR   A 1 543 ? 24.40054  4.66481   56.66018  1.000 47.28728 ? 546  THR   A C   1 
ATOM   4109 O  O   . THR   A 1 543 ? 24.14373  4.70760   57.86990  1.000 41.41609 ? 546  THR   A O   1 
ATOM   4110 C  CB  . THR   A 1 543 ? 23.99265  3.16881   54.66411  1.000 50.19480 ? 546  THR   A CB  1 
ATOM   4111 O  OG1 . THR   A 1 543 ? 22.63622  2.83534   54.97325  1.000 54.49495 ? 546  THR   A OG1 1 
ATOM   4112 C  CG2 . THR   A 1 543 ? 24.60127  2.04579   53.84227  1.000 46.24068 ? 546  THR   A CG2 1 
ATOM   4113 N  N   . GLU   A 1 544 ? 24.36398  5.74484   55.88641  1.000 32.41334 ? 547  GLU   A N   1 
ATOM   4114 C  CA  . GLU   A 1 544 ? 23.97579  7.04756   56.40395  1.000 41.37789 ? 547  GLU   A CA  1 
ATOM   4115 C  C   . GLU   A 1 544 ? 22.46235  7.20691   56.55181  1.000 44.33201 ? 547  GLU   A C   1 
ATOM   4116 O  O   . GLU   A 1 544 ? 22.00694  8.31144   56.87156  1.000 42.64182 ? 547  GLU   A O   1 
ATOM   4117 C  CB  . GLU   A 1 544 ? 24.51601  8.14980   55.49000  1.000 60.46276 ? 547  GLU   A CB  1 
ATOM   4118 C  CG  . GLU   A 1 544 ? 25.94214  7.89890   55.00174  1.000 73.04641 ? 547  GLU   A CG  1 
ATOM   4119 C  CD  . GLU   A 1 544 ? 25.99828  7.31150   53.59369  1.000 76.89623 ? 547  GLU   A CD  1 
ATOM   4120 O  OE1 . GLU   A 1 544 ? 26.45214  8.02993   52.67152  1.000 63.91881 ? 547  GLU   A OE1 1 
ATOM   4121 O  OE2 . GLU   A 1 544 ? 25.58574  6.13874   53.40984  1.000 62.99283 ? 547  GLU   A OE2 1 
ATOM   4122 N  N   . MET   A 1 545 ? 21.66996  6.15790   56.34067  1.000 28.11886 ? 548  MET   A N   1 
ATOM   4123 C  CA  . MET   A 1 545 ? 20.22540  6.34408   56.42387  1.000 27.47036 ? 548  MET   A CA  1 
ATOM   4124 C  C   . MET   A 1 545 ? 19.77677  6.49247   57.87940  1.000 30.89461 ? 548  MET   A C   1 
ATOM   4125 O  O   . MET   A 1 545 ? 20.46613  6.06494   58.80333  1.000 25.03855 ? 548  MET   A O   1 
ATOM   4126 C  CB  . MET   A 1 545 ? 19.49829  5.19535   55.72694  1.000 36.22498 ? 548  MET   A CB  1 
ATOM   4127 C  CG  . MET   A 1 545 ? 19.19366  3.98969   56.55120  1.000 46.39192 ? 548  MET   A CG  1 
ATOM   4128 S  SD  . MET   A 1 545 ? 18.18573  2.77922   55.65230  1.000 43.93853 ? 548  MET   A SD  1 
ATOM   4129 C  CE  . MET   A 1 545 ? 18.71366  3.03928   53.99866  1.000 41.95458 ? 548  MET   A CE  1 
ATOM   4130 N  N   . PHE   A 1 546 ? 18.61094  7.12373   58.08487  1.000 24.60968 ? 549  PHE   A N   1 
ATOM   4131 C  CA  . PHE   A 1 546 ? 18.07936  7.29232   59.44498  1.000 21.42840 ? 549  PHE   A CA  1 
ATOM   4132 C  C   . PHE   A 1 546 ? 16.55193  7.35019   59.39869  1.000 22.67252 ? 549  PHE   A C   1 
ATOM   4133 O  O   . PHE   A 1 546 ? 15.95022  7.63347   58.35913  1.000 21.53272 ? 549  PHE   A O   1 
ATOM   4134 C  CB  . PHE   A 1 546 ? 18.65260  8.52634   60.17196  1.000 24.94645 ? 549  PHE   A CB  1 
ATOM   4135 C  CG  . PHE   A 1 546 ? 18.30916  9.84400   59.54245  1.000 25.34805 ? 549  PHE   A CG  1 
ATOM   4136 C  CD1 . PHE   A 1 546 ? 17.13624  10.51611  59.89533  1.000 29.65138 ? 549  PHE   A CD1 1 
ATOM   4137 C  CD2 . PHE   A 1 546 ? 19.16673  10.43215  58.61279  1.000 26.69105 ? 549  PHE   A CD2 1 
ATOM   4138 C  CE1 . PHE   A 1 546 ? 16.81598  11.73448  59.32604  1.000 24.69423 ? 549  PHE   A CE1 1 
ATOM   4139 C  CE2 . PHE   A 1 546 ? 18.85015  11.66329  58.04281  1.000 26.92434 ? 549  PHE   A CE2 1 
ATOM   4140 C  CZ  . PHE   A 1 546 ? 17.67185  12.31024  58.40357  1.000 28.34727 ? 549  PHE   A CZ  1 
ATOM   4141 N  N   . CYS   A 1 547 ? 15.93722  7.03254   60.53833  1.000 20.13927 ? 550  CYS   A N   1 
ATOM   4142 C  CA  . CYS   A 1 547 ? 14.49791  6.82344   60.65986  1.000 19.82592 ? 550  CYS   A CA  1 
ATOM   4143 C  C   . CYS   A 1 547 ? 13.92169  7.83748   61.64060  1.000 24.15570 ? 550  CYS   A C   1 
ATOM   4144 O  O   . CYS   A 1 547 ? 14.58992  8.22086   62.60084  1.000 21.28271 ? 550  CYS   A O   1 
ATOM   4145 C  CB  . CYS   A 1 547 ? 14.21523  5.40243   61.16214  1.000 23.69543 ? 550  CYS   A CB  1 
ATOM   4146 S  SG  . CYS   A 1 547 ? 14.96088  4.12245   60.14289  1.000 31.13989 ? 550  CYS   A SG  1 
ATOM   4147 N  N   . CYS   A 1 548 ? 12.67818  8.26495   61.41282  1.000 19.29834 ? 551  CYS   A N   1 
ATOM   4148 C  CA  . CYS   A 1 548 ? 12.05372  9.20594   62.33204  1.000 21.24055 ? 551  CYS   A CA  1 
ATOM   4149 C  C   . CYS   A 1 548 ? 10.53910  9.04461   62.28679  1.000 23.22726 ? 551  CYS   A C   1 
ATOM   4150 O  O   . CYS   A 1 548 ? 9.99149   8.42446   61.37161  1.000 20.50054 ? 551  CYS   A O   1 
ATOM   4151 C  CB  . CYS   A 1 548 ? 12.44055  10.64345  62.00507  1.000 22.35185 ? 551  CYS   A CB  1 
ATOM   4152 S  SG  . CYS   A 1 548 ? 12.04673  11.09617  60.32045  1.000 24.04863 ? 551  CYS   A SG  1 
ATOM   4153 N  N   . TYR   A 1 549 ? 9.87140   9.59953   63.30101  1.000 17.02072 ? 552  TYR   A N   1 
ATOM   4154 C  CA  . TYR   A 1 549 ? 8.40923   9.59792   63.35394  1.000 20.07696 ? 552  TYR   A CA  1 
ATOM   4155 C  C   . TYR   A 1 549 ? 7.95129   10.64754  64.35513  1.000 19.22707 ? 552  TYR   A C   1 
ATOM   4156 O  O   . TYR   A 1 549 ? 8.74644   11.17134  65.15053  1.000 20.76572 ? 552  TYR   A O   1 
ATOM   4157 C  CB  . TYR   A 1 549 ? 7.85189   8.22054   63.73354  1.000 18.67726 ? 552  TYR   A CB  1 
ATOM   4158 C  CG  . TYR   A 1 549 ? 8.61843   7.61197   64.88253  1.000 18.09085 ? 552  TYR   A CG  1 
ATOM   4159 C  CD1 . TYR   A 1 549 ? 8.37822   8.01255   66.19036  1.000 20.52470 ? 552  TYR   A CD1 1 
ATOM   4160 C  CD2 . TYR   A 1 549 ? 9.58629   6.65602   64.65102  1.000 20.51880 ? 552  TYR   A CD2 1 
ATOM   4161 C  CE1 . TYR   A 1 549 ? 9.08289   7.43960   67.25529  1.000 24.78592 ? 552  TYR   A CE1 1 
ATOM   4162 C  CE2 . TYR   A 1 549 ? 10.30983  6.10601   65.68561  1.000 22.56546 ? 552  TYR   A CE2 1 
ATOM   4163 C  CZ  . TYR   A 1 549 ? 10.05373  6.49777   66.97946  1.000 23.40887 ? 552  TYR   A CZ  1 
ATOM   4164 O  OH  . TYR   A 1 549 ? 10.76899  5.92495   68.00271  1.000 26.74435 ? 552  TYR   A OH  1 
ATOM   4165 N  N   . GLY   A 1 550 ? 6.63737   10.93820  64.32427  1.000 19.57305 ? 553  GLY   A N   1 
ATOM   4166 C  CA  . GLY   A 1 550 ? 6.07764   11.91772  65.23389  1.000 16.61771 ? 553  GLY   A CA  1 
ATOM   4167 C  C   . GLY   A 1 550 ? 5.75915   11.29852  66.58897  1.000 16.49725 ? 553  GLY   A C   1 
ATOM   4168 O  O   . GLY   A 1 550 ? 5.91470   10.09836  66.80918  1.000 18.82085 ? 553  GLY   A O   1 
ATOM   4169 N  N   . PRO   A 1 551 ? 5.31296   12.14258  67.52546  1.000 18.36722 ? 554  PRO   A N   1 
ATOM   4170 C  CA  . PRO   A 1 551 ? 4.83556   11.64223  68.82572  1.000 17.12654 ? 554  PRO   A CA  1 
ATOM   4171 C  C   . PRO   A 1 551 ? 3.50520   10.91266  68.67781  1.000 20.50598 ? 554  PRO   A C   1 
ATOM   4172 O  O   . PRO   A 1 551 ? 2.80656   11.04054  67.66695  1.000 21.68058 ? 554  PRO   A O   1 
ATOM   4173 C  CB  . PRO   A 1 551 ? 4.65080   12.91452  69.65204  1.000 18.12737 ? 554  PRO   A CB  1 
ATOM   4174 C  CG  . PRO   A 1 551 ? 5.25923   14.04403  68.82199  1.000 17.96033 ? 554  PRO   A CG  1 
ATOM   4175 C  CD  . PRO   A 1 551 ? 5.17064   13.60102  67.41078  1.000 18.05545 ? 554  PRO   A CD  1 
ATOM   4176 N  N   . VAL   A 1 552 ? 3.11433   10.19628  69.73632  1.000 16.68382 ? 555  VAL   A N   1 
ATOM   4177 C  CA  . VAL   A 1 552 ? 1.84165   9.46163   69.72315  1.000 16.31218 ? 555  VAL   A CA  1 
ATOM   4178 C  C   . VAL   A 1 552 ? 0.78092   10.06178  70.63143  1.000 22.26647 ? 555  VAL   A C   1 
ATOM   4179 O  O   . VAL   A 1 552 ? -0.36839  9.59108   70.59992  1.000 18.68878 ? 555  VAL   A O   1 
ATOM   4180 C  CB  . VAL   A 1 552 ? 2.03995   7.96905   70.05888  1.000 18.11416 ? 555  VAL   A CB  1 
ATOM   4181 C  CG1 . VAL   A 1 552 ? 3.01479   7.34316   69.03370  1.000 19.19560 ? 555  VAL   A CG1 1 
ATOM   4182 C  CG2 . VAL   A 1 552 ? 2.56649   7.76687   71.51812  1.000 20.52965 ? 555  VAL   A CG2 1 
ATOM   4183 N  N   . VAL   A 1 553 ? 1.11899   11.04950  71.45391  1.000 18.62444 ? 556  VAL   A N   1 
ATOM   4184 C  CA  . VAL   A 1 553 ? 0.13309   11.81119  72.22264  1.000 20.25426 ? 556  VAL   A CA  1 
ATOM   4185 C  C   . VAL   A 1 553 ? 0.44895   13.28613  72.03313  1.000 17.65126 ? 556  VAL   A C   1 
ATOM   4186 O  O   . VAL   A 1 553 ? 1.59520   13.63947  71.70581  1.000 20.48303 ? 556  VAL   A O   1 
ATOM   4187 C  CB  . VAL   A 1 553 ? 0.14756   11.43914  73.72104  1.000 19.16857 ? 556  VAL   A CB  1 
ATOM   4188 C  CG1 . VAL   A 1 553 ? -0.28705  9.97044   73.90754  1.000 26.14877 ? 556  VAL   A CG1 1 
ATOM   4189 C  CG2 . VAL   A 1 553 ? 1.54110   11.72121  74.32328  1.000 18.67927 ? 556  VAL   A CG2 1 
ATOM   4190 N  N   . PRO   A 1 554 ? -0.54550  14.16894  72.22329  1.000 18.21252 ? 557  PRO   A N   1 
ATOM   4191 C  CA  . PRO   A 1 554 ? -0.32644  15.59642  71.92951  1.000 19.66191 ? 557  PRO   A CA  1 
ATOM   4192 C  C   . PRO   A 1 554 ? 0.73521   16.24024  72.78943  1.000 19.97705 ? 557  PRO   A C   1 
ATOM   4193 O  O   . PRO   A 1 554 ? 1.40462   17.17143  72.32923  1.000 18.94152 ? 557  PRO   A O   1 
ATOM   4194 C  CB  . PRO   A 1 554 ? -1.71289  16.22639  72.17549  1.000 24.71795 ? 557  PRO   A CB  1 
ATOM   4195 C  CG  . PRO   A 1 554 ? -2.68030  15.10249  71.99652  1.000 29.02785 ? 557  PRO   A CG  1 
ATOM   4196 C  CD  . PRO   A 1 554 ? -1.96387  13.88264  72.54239  1.000 19.79095 ? 557  PRO   A CD  1 
ATOM   4197 N  N   . ASN   A 1 555 ? 0.94099   15.77049  74.02109  1.000 19.38410 ? 558  ASN   A N   1 
ATOM   4198 C  CA  . ASN   A 1 555 ? 1.95671   16.34057  74.89615  1.000 16.35340 ? 558  ASN   A CA  1 
ATOM   4199 C  C   . ASN   A 1 555 ? 3.20832   15.47412  74.92750  1.000 19.13805 ? 558  ASN   A C   1 
ATOM   4200 O  O   . ASN   A 1 555 ? 3.96637   15.50455  75.89632  1.000 19.19245 ? 558  ASN   A O   1 
ATOM   4201 C  CB  . ASN   A 1 555 ? 1.40243   16.55404  76.32266  1.000 18.66964 ? 558  ASN   A CB  1 
ATOM   4202 C  CG  . ASN   A 1 555 ? 1.07162   15.23208  77.05210  1.000 27.33938 ? 558  ASN   A CG  1 
ATOM   4203 O  OD1 . ASN   A 1 555 ? 0.70372   14.23231  76.42240  1.000 22.73363 ? 558  ASN   A OD1 1 
ATOM   4204 N  ND2 . ASN   A 1 555 ? 1.18673   15.23673  78.39518  1.000 24.71721 ? 558  ASN   A ND2 1 
ATOM   4205 N  N   . GLY   A 1 556 ? 3.47204   14.71429  73.86518  1.000 16.56213 ? 559  GLY   A N   1 
ATOM   4206 C  CA  . GLY   A 1 556 ? 4.52819   13.73469  73.90190  1.000 15.97014 ? 559  GLY   A CA  1 
ATOM   4207 C  C   . GLY   A 1 556 ? 5.70103   14.05629  72.98304  1.000 18.55762 ? 559  GLY   A C   1 
ATOM   4208 O  O   . GLY   A 1 556 ? 5.71621   15.03831  72.23902  1.000 16.05896 ? 559  GLY   A O   1 
ATOM   4209 N  N   . TYR   A 1 557 ? 6.67455   13.15510  73.03397  1.000 16.15194 ? 560  TYR   A N   1 
ATOM   4210 C  CA  . TYR   A 1 557 ? 7.83201   13.13106  72.15421  1.000 17.16317 ? 560  TYR   A CA  1 
ATOM   4211 C  C   . TYR   A 1 557 ? 7.87942   11.81372  71.39828  1.000 17.16289 ? 560  TYR   A C   1 
ATOM   4212 O  O   . TYR   A 1 557 ? 7.50965   10.77129  71.93316  1.000 16.48675 ? 560  TYR   A O   1 
ATOM   4213 C  CB  . TYR   A 1 557 ? 9.16120   13.23988  72.94449  1.000 15.54260 ? 560  TYR   A CB  1 
ATOM   4214 C  CG  . TYR   A 1 557 ? 9.39004   14.54048  73.66331  1.000 16.01755 ? 560  TYR   A CG  1 
ATOM   4215 C  CD1 . TYR   A 1 557 ? 9.93299   15.63589  72.99908  1.000 19.29047 ? 560  TYR   A CD1 1 
ATOM   4216 C  CD2 . TYR   A 1 557 ? 9.04560   14.68490  75.00169  1.000 17.55248 ? 560  TYR   A CD2 1 
ATOM   4217 C  CE1 . TYR   A 1 557 ? 10.14338  16.86033  73.66974  1.000 18.82430 ? 560  TYR   A CE1 1 
ATOM   4218 C  CE2 . TYR   A 1 557 ? 9.26941   15.87375  75.67081  1.000 16.63385 ? 560  TYR   A CE2 1 
ATOM   4219 C  CZ  . TYR   A 1 557 ? 9.80378   16.96104  74.99194  1.000 16.32118 ? 560  TYR   A CZ  1 
ATOM   4220 O  OH  . TYR   A 1 557 ? 10.02980  18.13652  75.66396  1.000 19.51803 ? 560  TYR   A OH  1 
ATOM   4221 N  N   . GLY   A 1 558 ? 8.39508   11.84921  70.17087  1.000 16.43888 ? 561  GLY   A N   1 
ATOM   4222 C  CA  . GLY   A 1 558 ? 8.93177   10.66938  69.51516  1.000 14.90700 ? 561  GLY   A CA  1 
ATOM   4223 C  C   . GLY   A 1 558 ? 10.44933  10.77563  69.49765  1.000 18.22379 ? 561  GLY   A C   1 
ATOM   4224 O  O   . GLY   A 1 558 ? 11.00036  11.85095  69.23869  1.000 17.72146 ? 561  GLY   A O   1 
ATOM   4225 N  N   . ALA   A 1 559 ? 11.12148  9.67663   69.83301  1.000 16.75399 ? 562  ALA   A N   1 
ATOM   4226 C  CA  . ALA   A 1 559 ? 12.58571  9.71544   69.84882  1.000 17.90138 ? 562  ALA   A CA  1 
ATOM   4227 C  C   . ALA   A 1 559 ? 13.12979  8.42687   69.25050  1.000 20.96041 ? 562  ALA   A C   1 
ATOM   4228 O  O   . ALA   A 1 559 ? 13.06184  7.37216   69.88963  1.000 23.12028 ? 562  ALA   A O   1 
ATOM   4229 C  CB  . ALA   A 1 559 ? 13.09628  9.93298   71.27564  1.000 18.33788 ? 562  ALA   A CB  1 
ATOM   4230 N  N   . CYS   A 1 560 ? 13.69743  8.50709   68.04874  1.000 14.39174 ? 563  CYS   A N   1 
ATOM   4231 C  CA  . CYS   A 1 560 ? 14.24588  7.34246   67.36169  1.000 13.57347 ? 563  CYS   A CA  1 
ATOM   4232 C  C   . CYS   A 1 560 ? 15.75216  7.55699   67.26388  1.000 21.18093 ? 563  CYS   A C   1 
ATOM   4233 O  O   . CYS   A 1 560 ? 16.18497  8.62923   66.84020  1.000 24.62971 ? 563  CYS   A O   1 
ATOM   4234 C  CB  . CYS   A 1 560 ? 13.61552  7.18618   65.96315  1.000 18.55041 ? 563  CYS   A CB  1 
ATOM   4235 S  SG  . CYS   A 1 560 ? 14.05639  5.60518   65.14849  1.000 22.78042 ? 563  CYS   A SG  1 
ATOM   4236 N  N   . TYR   A 1 561 ? 16.56132  6.56899   67.68669  1.000 18.71246 ? 564  TYR   A N   1 
ATOM   4237 C  CA  . TYR   A 1 561 ? 18.00190  6.80130   67.70966  1.000 19.29322 ? 564  TYR   A CA  1 
ATOM   4238 C  C   . TYR   A 1 561 ? 18.75194  5.67895   67.00703  1.000 21.81051 ? 564  TYR   A C   1 
ATOM   4239 O  O   . TYR   A 1 561 ? 18.29422  4.53302   66.93427  1.000 17.20729 ? 564  TYR   A O   1 
ATOM   4240 C  CB  . TYR   A 1 561 ? 18.54894  6.98361   69.14093  1.000 17.32633 ? 564  TYR   A CB  1 
ATOM   4241 C  CG  . TYR   A 1 561 ? 18.09008  5.89758   70.08149  1.000 19.57409 ? 564  TYR   A CG  1 
ATOM   4242 C  CD1 . TYR   A 1 561 ? 16.86821  5.99076   70.72380  1.000 19.25110 ? 564  TYR   A CD1 1 
ATOM   4243 C  CD2 . TYR   A 1 561 ? 18.87598  4.76668   70.30823  1.000 21.09094 ? 564  TYR   A CD2 1 
ATOM   4244 C  CE1 . TYR   A 1 561 ? 16.42824  4.97873   71.57805  1.000 20.34173 ? 564  TYR   A CE1 1 
ATOM   4245 C  CE2 . TYR   A 1 561 ? 18.46070  3.76167   71.17919  1.000 18.33497 ? 564  TYR   A CE2 1 
ATOM   4246 C  CZ  . TYR   A 1 561 ? 17.23372  3.87042   71.79490  1.000 19.94267 ? 564  TYR   A CZ  1 
ATOM   4247 O  OH  . TYR   A 1 561 ? 16.78290  2.85888   72.62931  1.000 21.86284 ? 564  TYR   A OH  1 
ATOM   4248 N  N   . ASN   A 1 562 ? 19.91729  6.04128   66.46969  1.000 17.43386 ? 565  ASN   A N   1 
ATOM   4249 C  CA  . ASN   A 1 562 ? 20.74470  5.15280   65.65437  1.000 19.73282 ? 565  ASN   A CA  1 
ATOM   4250 C  C   . ASN   A 1 562 ? 22.15948  5.24246   66.22363  1.000 22.65633 ? 565  ASN   A C   1 
ATOM   4251 O  O   . ASN   A 1 562 ? 22.90951  6.17496   65.89174  1.000 21.13439 ? 565  ASN   A O   1 
ATOM   4252 C  CB  . ASN   A 1 562 ? 20.67674  5.58591   64.19234  1.000 19.75414 ? 565  ASN   A CB  1 
ATOM   4253 C  CG  . ASN   A 1 562 ? 21.44005  4.67170   63.24642  1.000 29.38362 ? 565  ASN   A CG  1 
ATOM   4254 O  OD1 . ASN   A 1 562 ? 22.17599  3.78939   63.65999  1.000 26.43474 ? 565  ASN   A OD1 1 
ATOM   4255 N  ND2 . ASN   A 1 562 ? 21.27537  4.91205   61.95985  1.000 38.72791 ? 565  ASN   A ND2 1 
ATOM   4256 N  N   . PRO   A 1 563 ? 22.54912  4.31193   67.09319  1.000 19.55319 ? 566  PRO   A N   1 
ATOM   4257 C  CA  . PRO   A 1 563 ? 23.87691  4.36507   67.72030  1.000 25.84176 ? 566  PRO   A CA  1 
ATOM   4258 C  C   . PRO   A 1 563 ? 24.93523  3.77845   66.79822  1.000 27.39643 ? 566  PRO   A C   1 
ATOM   4259 O  O   . PRO   A 1 563 ? 24.73788  2.71654   66.19949  1.000 25.03195 ? 566  PRO   A O   1 
ATOM   4260 C  CB  . PRO   A 1 563 ? 23.70983  3.50869   68.98219  1.000 24.38928 ? 566  PRO   A CB  1 
ATOM   4261 C  CG  . PRO   A 1 563 ? 22.63050  2.56586   68.64795  1.000 31.22118 ? 566  PRO   A CG  1 
ATOM   4262 C  CD  . PRO   A 1 563 ? 21.73099  3.19745   67.59690  1.000 25.95238 ? 566  PRO   A CD  1 
ATOM   4263 N  N   . GLN   A 1 564 ? 26.04474  4.47821   66.68410  1.000 21.42401 ? 567  GLN   A N   1 
ATOM   4264 C  CA  . GLN   A 1 564 ? 27.15588  4.08531   65.82656  1.000 22.52802 ? 567  GLN   A CA  1 
ATOM   4265 C  C   . GLN   A 1 564 ? 28.37342  3.92969   66.74213  1.000 24.38876 ? 567  GLN   A C   1 
ATOM   4266 O  O   . GLN   A 1 564 ? 28.26996  4.23372   67.93391  1.000 21.20904 ? 567  GLN   A O   1 
ATOM   4267 C  CB  . GLN   A 1 564 ? 27.37292  5.13215   64.72762  1.000 27.14695 ? 567  GLN   A CB  1 
ATOM   4268 C  CG  . GLN   A 1 564 ? 26.19611  5.23560   63.74356  1.000 26.11601 ? 567  GLN   A CG  1 
ATOM   4269 C  CD  . GLN   A 1 564 ? 26.05031  3.98041   62.93624  1.000 34.35034 ? 567  GLN   A CD  1 
ATOM   4270 O  OE1 . GLN   A 1 564 ? 27.04904  3.37395   62.57211  1.000 29.03130 ? 567  GLN   A OE1 1 
ATOM   4271 N  NE2 . GLN   A 1 564 ? 24.81231  3.54811   62.68649  1.000 36.27798 ? 567  GLN   A NE2 1 
ATOM   4272 N  N   . PRO   A 1 565 ? 29.52020  3.44326   66.25697  1.000 26.02791 ? 568  PRO   A N   1 
ATOM   4273 C  CA  . PRO   A 1 565 ? 30.65760  3.24455   67.17866  1.000 24.65744 ? 568  PRO   A CA  1 
ATOM   4274 C  C   . PRO   A 1 565 ? 31.06774  4.49261   67.95643  1.000 25.74567 ? 568  PRO   A C   1 
ATOM   4275 O  O   . PRO   A 1 565 ? 31.39084  4.37692   69.14770  1.000 24.44394 ? 568  PRO   A O   1 
ATOM   4276 C  CB  . PRO   A 1 565 ? 31.77286  2.74233   66.24095  1.000 30.52766 ? 568  PRO   A CB  1 
ATOM   4277 C  CG  . PRO   A 1 565 ? 31.01168  1.96348   65.18059  1.000 29.79310 ? 568  PRO   A CG  1 
ATOM   4278 C  CD  . PRO   A 1 565 ? 29.74955  2.79098   64.95015  1.000 32.45509 ? 568  PRO   A CD  1 
ATOM   4279 N  N   . GLU   A 1 566 ? 31.04076  5.67997   67.33327  1.000 21.29218 ? 569  GLU   A N   1 
ATOM   4280 C  CA  . GLU   A 1 566 ? 31.57540  6.91502   67.92301  1.000 22.96659 ? 569  GLU   A CA  1 
ATOM   4281 C  C   . GLU   A 1 566 ? 30.56237  8.05589   68.00360  1.000 22.96918 ? 569  GLU   A C   1 
ATOM   4282 O  O   . GLU   A 1 566 ? 30.90402  9.13048   68.51113  1.000 23.79223 ? 569  GLU   A O   1 
ATOM   4283 C  CB  . GLU   A 1 566 ? 32.80242  7.41468   67.13576  1.000 23.26223 ? 569  GLU   A CB  1 
ATOM   4284 C  CG  . GLU   A 1 566 ? 33.90313  6.35929   66.97143  1.000 27.24642 ? 569  GLU   A CG  1 
ATOM   4285 C  CD  . GLU   A 1 566 ? 34.34400  5.78932   68.30341  1.000 42.21579 ? 569  GLU   A CD  1 
ATOM   4286 O  OE1 . GLU   A 1 566 ? 34.41707  6.56567   69.28083  1.000 49.61503 ? 569  GLU   A OE1 1 
ATOM   4287 O  OE2 . GLU   A 1 566 ? 34.59271  4.56403   68.37832  1.000 60.30216 ? 569  GLU   A OE2 1 
ATOM   4288 N  N   . THR   A 1 567 ? 29.32784  7.84934   67.54761  1.000 24.74044 ? 570  THR   A N   1 
ATOM   4289 C  CA  . THR   A 1 567 ? 28.29280  8.88214   67.53903  1.000 20.52573 ? 570  THR   A CA  1 
ATOM   4290 C  C   . THR   A 1 567 ? 26.95448  8.22574   67.84473  1.000 22.12393 ? 570  THR   A C   1 
ATOM   4291 O  O   . THR   A 1 567 ? 26.80828  6.99887   67.78098  1.000 21.62489 ? 570  THR   A O   1 
ATOM   4292 C  CB  . THR   A 1 567 ? 28.17246  9.58290   66.16993  1.000 21.61088 ? 570  THR   A CB  1 
ATOM   4293 O  OG1 . THR   A 1 567 ? 27.83925  8.59369   65.18735  1.000 22.91919 ? 570  THR   A OG1 1 
ATOM   4294 C  CG2 . THR   A 1 567 ? 29.46761  10.27692  65.75106  1.000 29.51399 ? 570  THR   A CG2 1 
ATOM   4295 N  N   . ILE   A 1 568 ? 25.96327  9.04860   68.17250  1.000 19.83045 ? 571  ILE   A N   1 
ATOM   4296 C  CA  . ILE   A 1 568 ? 24.58538  8.56518   68.28930  1.000 17.23144 ? 571  ILE   A CA  1 
ATOM   4297 C  C   . ILE   A 1 568 ? 23.68092  9.59052   67.62993  1.000 20.45413 ? 571  ILE   A C   1 
ATOM   4298 O  O   . ILE   A 1 568 ? 23.69487  10.75871  68.01867  1.000 24.18449 ? 571  ILE   A O   1 
ATOM   4299 C  CB  . ILE   A 1 568 ? 24.13985  8.36870   69.74827  1.000 19.87924 ? 571  ILE   A CB  1 
ATOM   4300 C  CG1 . ILE   A 1 568 ? 25.14123  7.51512   70.56048  1.000 19.04956 ? 571  ILE   A CG1 1 
ATOM   4301 C  CG2 . ILE   A 1 568 ? 22.72200  7.77024   69.76602  1.000 18.54763 ? 571  ILE   A CG2 1 
ATOM   4302 C  CD1 . ILE   A 1 568 ? 24.90326  7.62219   72.08756  1.000 22.83274 ? 571  ILE   A CD1 1 
ATOM   4303 N  N   . LEU   A 1 569 ? 22.86946  9.16076   66.67008  1.000 20.35997 ? 572  LEU   A N   1 
ATOM   4304 C  CA  . LEU   A 1 569 ? 21.92980  10.05731  66.00057  1.000 16.72022 ? 572  LEU   A CA  1 
ATOM   4305 C  C   . LEU   A 1 569 ? 20.57289  9.96602   66.68013  1.000 18.00866 ? 572  LEU   A C   1 
ATOM   4306 O  O   . LEU   A 1 569 ? 20.03881  8.86820   66.84625  1.000 25.38515 ? 572  LEU   A O   1 
ATOM   4307 C  CB  . LEU   A 1 569 ? 21.77824  9.67559   64.52071  1.000 19.52711 ? 572  LEU   A CB  1 
ATOM   4308 C  CG  . LEU   A 1 569 ? 21.06674  10.75931  63.69107  1.000 26.16218 ? 572  LEU   A CG  1 
ATOM   4309 C  CD1 . LEU   A 1 569 ? 22.00402  11.92654  63.41461  1.000 29.64561 ? 572  LEU   A CD1 1 
ATOM   4310 C  CD2 . LEU   A 1 569 ? 20.58773  10.19153  62.39895  1.000 36.85104 ? 572  LEU   A CD2 1 
ATOM   4311 N  N   . PHE   A 1 570 ? 20.02095  11.10860  67.07401  1.000 22.52234 ? 573  PHE   A N   1 
ATOM   4312 C  CA  . PHE   A 1 570 ? 18.69129  11.19876  67.66869  1.000 19.66880 ? 573  PHE   A CA  1 
ATOM   4313 C  C   . PHE   A 1 570 ? 17.77180  11.97971  66.73329  1.000 19.85891 ? 573  PHE   A C   1 
ATOM   4314 O  O   . PHE   A 1 570 ? 18.11076  13.09123  66.31726  1.000 23.48418 ? 573  PHE   A O   1 
ATOM   4315 C  CB  . PHE   A 1 570 ? 18.74937  11.90790  69.02887  1.000 16.31814 ? 573  PHE   A CB  1 
ATOM   4316 C  CG  . PHE   A 1 570 ? 19.48253  11.12909  70.10322  1.000 20.89724 ? 573  PHE   A CG  1 
ATOM   4317 C  CD1 . PHE   A 1 570 ? 20.85043  11.29836  70.29127  1.000 19.73927 ? 573  PHE   A CD1 1 
ATOM   4318 C  CD2 . PHE   A 1 570 ? 18.79508  10.24072  70.92107  1.000 18.80112 ? 573  PHE   A CD2 1 
ATOM   4319 C  CE1 . PHE   A 1 570 ? 21.52393  10.58516  71.26030  1.000 20.19508 ? 573  PHE   A CE1 1 
ATOM   4320 C  CE2 . PHE   A 1 570 ? 19.46656  9.50805   71.91741  1.000 19.16947 ? 573  PHE   A CE2 1 
ATOM   4321 C  CZ  . PHE   A 1 570 ? 20.83515  9.69063   72.08827  1.000 14.70070 ? 573  PHE   A CZ  1 
ATOM   4322 N  N   . CYS   A 1 571 ? 16.61764  11.41059  66.40585  1.000 18.95975 ? 574  CYS   A N   1 
ATOM   4323 C  CA  . CYS   A 1 571 ? 15.55750  12.14152  65.70450  1.000 18.34183 ? 574  CYS   A CA  1 
ATOM   4324 C  C   . CYS   A 1 571 ? 14.44391  12.36934  66.70689  1.000 18.82112 ? 574  CYS   A C   1 
ATOM   4325 O  O   . CYS   A 1 571 ? 13.79270  11.40733  67.13887  1.000 18.82429 ? 574  CYS   A O   1 
ATOM   4326 C  CB  . CYS   A 1 571 ? 15.03530  11.37408  64.50531  1.000 20.81305 ? 574  CYS   A CB  1 
ATOM   4327 S  SG  . CYS   A 1 571 ? 16.26554  11.21893  63.20382  1.000 24.12800 ? 574  CYS   A SG  1 
ATOM   4328 N  N   . ILE   A 1 572 ? 14.22091  13.63088  67.06991  1.000 17.04339 ? 575  ILE   A N   1 
ATOM   4329 C  CA  . ILE   A 1 572 ? 13.30357  13.96826  68.15355  1.000 15.47948 ? 575  ILE   A CA  1 
ATOM   4330 C  C   . ILE   A 1 572 ? 12.14932  14.78088  67.59925  1.000 15.80559 ? 575  ILE   A C   1 
ATOM   4331 O  O   . ILE   A 1 572 ? 12.36409  15.80181  66.94320  1.000 18.02556 ? 575  ILE   A O   1 
ATOM   4332 C  CB  . ILE   A 1 572 ? 14.02040  14.72209  69.26992  1.000 19.67982 ? 575  ILE   A CB  1 
ATOM   4333 C  CG1 . ILE   A 1 572 ? 15.07742  13.77821  69.87644  1.000 20.18834 ? 575  ILE   A CG1 1 
ATOM   4334 C  CG2 . ILE   A 1 572 ? 12.96635  15.18634  70.33550  1.000 18.60030 ? 575  ILE   A CG2 1 
ATOM   4335 C  CD1 . ILE   A 1 572 ? 16.17395  14.50319  70.58097  1.000 24.75742 ? 575  ILE   A CD1 1 
ATOM   4336 N  N   . SER   A 1 573 ? 10.92301  14.32485  67.86708  1.000 13.83041 ? 576  SER   A N   1 
ATOM   4337 C  CA  . SER   A 1 573 ? 9.72612   15.03683  67.44726  1.000 13.88599 ? 576  SER   A CA  1 
ATOM   4338 C  C   . SER   A 1 573 ? 8.88296   15.41285  68.65374  1.000 17.48857 ? 576  SER   A C   1 
ATOM   4339 O  O   . SER   A 1 573 ? 8.94518   14.77035  69.70421  1.000 18.45344 ? 576  SER   A O   1 
ATOM   4340 C  CB  . SER   A 1 573 ? 8.88350   14.18237  66.50478  1.000 14.96129 ? 576  SER   A CB  1 
ATOM   4341 O  OG  . SER   A 1 573 ? 8.54375   12.96077  67.14314  1.000 16.01870 ? 576  SER   A OG  1 
ATOM   4342 N  N   . SER   A 1 574 ? 8.10233   16.47441  68.48782  1.000 16.26057 ? 577  SER   A N   1 
ATOM   4343 C  CA  . SER   A 1 574 ? 7.10364   16.88606  69.46848  1.000 18.08381 ? 577  SER   A CA  1 
ATOM   4344 C  C   . SER   A 1 574 ? 6.15878   17.81265  68.71898  1.000 19.91570 ? 577  SER   A C   1 
ATOM   4345 O  O   . SER   A 1 574 ? 6.34140   18.06848  67.52853  1.000 23.09678 ? 577  SER   A O   1 
ATOM   4346 C  CB  . SER   A 1 574 ? 7.75166   17.55414  70.68374  1.000 17.11541 ? 577  SER   A CB  1 
ATOM   4347 O  OG  . SER   A 1 574 ? 8.44361   18.74313  70.30762  1.000 20.60389 ? 577  SER   A OG  1 
ATOM   4348 N  N   . PHE   A 1 575 ? 5.12682   18.28283  69.39175  1.000 15.91392 ? 578  PHE   A N   1 
ATOM   4349 C  CA  . PHE   A 1 575 ? 4.14980   19.17244  68.75749  1.000 15.20181 ? 578  PHE   A CA  1 
ATOM   4350 C  C   . PHE   A 1 575 ? 4.24615   20.58438  69.31357  1.000 19.23229 ? 578  PHE   A C   1 
ATOM   4351 O  O   . PHE   A 1 575 ? 4.21406   20.77594  70.53384  1.000 19.09003 ? 578  PHE   A O   1 
ATOM   4352 C  CB  . PHE   A 1 575 ? 2.73884   18.64602  68.96729  1.000 18.13115 ? 578  PHE   A CB  1 
ATOM   4353 C  CG  . PHE   A 1 575 ? 2.46742   17.35493  68.26605  1.000 18.72614 ? 578  PHE   A CG  1 
ATOM   4354 C  CD1 . PHE   A 1 575 ? 2.58418   17.26600  66.88398  1.000 19.74237 ? 578  PHE   A CD1 1 
ATOM   4355 C  CD2 . PHE   A 1 575 ? 2.04862   16.24288  68.98359  1.000 17.19076 ? 578  PHE   A CD2 1 
ATOM   4356 C  CE1 . PHE   A 1 575 ? 2.29408   16.05775  66.22428  1.000 21.87920 ? 578  PHE   A CE1 1 
ATOM   4357 C  CE2 . PHE   A 1 575 ? 1.75904   15.04414  68.34174  1.000 23.98637 ? 578  PHE   A CE2 1 
ATOM   4358 C  CZ  . PHE   A 1 575 ? 1.87525   14.96099  66.94701  1.000 21.89081 ? 578  PHE   A CZ  1 
ATOM   4359 N  N   . HIS   A 1 576 ? 4.29854   21.57377  68.40448  1.000 16.55705 ? 579  HIS   A N   1 
ATOM   4360 C  CA  . HIS   A 1 576 ? 4.37504   22.98121  68.79686  1.000 21.88399 ? 579  HIS   A CA  1 
ATOM   4361 C  C   . HIS   A 1 576 ? 3.15474   23.43008  69.58616  1.000 18.02297 ? 579  HIS   A C   1 
ATOM   4362 O  O   . HIS   A 1 576 ? 3.23630   24.42029  70.31441  1.000 22.82360 ? 579  HIS   A O   1 
ATOM   4363 C  CB  . HIS   A 1 576 ? 4.50080   23.88139  67.55969  1.000 20.09589 ? 579  HIS   A CB  1 
ATOM   4364 C  CG  . HIS   A 1 576 ? 5.86643   23.88294  66.94040  1.000 21.40934 ? 579  HIS   A CG  1 
ATOM   4365 N  ND1 . HIS   A 1 576 ? 6.98216   24.33155  67.60992  1.000 22.01611 ? 579  HIS   A ND1 1 
ATOM   4366 C  CD2 . HIS   A 1 576 ? 6.28514   23.53371  65.69890  1.000 19.51912 ? 579  HIS   A CD2 1 
ATOM   4367 C  CE1 . HIS   A 1 576 ? 8.03639   24.23876  66.81618  1.000 31.48596 ? 579  HIS   A CE1 1 
ATOM   4368 N  NE2 . HIS   A 1 576 ? 7.63452   23.78386  65.64095  1.000 20.87012 ? 579  HIS   A NE2 1 
ATOM   4369 N  N   A SER   A 1 577 ? 2.03091   22.73973  69.45268  0.603 21.53087 ? 580  SER   A N   1 
ATOM   4370 N  N   B SER   A 1 577 ? 2.03732   22.70041  69.48210  0.397 21.50463 ? 580  SER   A N   1 
ATOM   4371 C  CA  A SER   A 1 577 ? 0.84336   23.14465  70.19441  0.603 21.95069 ? 580  SER   A CA  1 
ATOM   4372 C  CA  B SER   A 1 577 ? 0.79667   23.07069  70.16487  0.397 22.04232 ? 580  SER   A CA  1 
ATOM   4373 C  C   A SER   A 1 577 ? 1.05180   23.00904  71.70167  0.603 23.16079 ? 580  SER   A C   1 
ATOM   4374 C  C   B SER   A 1 577 ? 0.83705   22.79557  71.66803  0.397 23.53146 ? 580  SER   A C   1 
ATOM   4375 O  O   A SER   A 1 577 ? 0.56230   23.83468  72.47938  0.603 22.10544 ? 580  SER   A O   1 
ATOM   4376 O  O   B SER   A 1 577 ? -0.01155  23.31205  72.40625  0.397 22.28572 ? 580  SER   A O   1 
ATOM   4377 C  CB  A SER   A 1 577 ? -0.34281  22.30586  69.73576  0.603 21.85654 ? 580  SER   A CB  1 
ATOM   4378 C  CB  B SER   A 1 577 ? -0.38425  22.31971  69.53706  0.397 21.95372 ? 580  SER   A CB  1 
ATOM   4379 O  OG  A SER   A 1 577 ? 0.07299   20.97515  69.56013  0.603 19.80381 ? 580  SER   A OG  1 
ATOM   4380 O  OG  B SER   A 1 577 ? -1.62956  22.78195  70.04656  0.397 20.14121 ? 580  SER   A OG  1 
ATOM   4381 N  N   . CYS   A 1 578 ? 1.77913   21.98267  72.12687  1.000 22.69871 ? 581  CYS   A N   1 
ATOM   4382 C  CA  . CYS   A 1 578 ? 1.97440   21.69950  73.54442  1.000 24.53022 ? 581  CYS   A CA  1 
ATOM   4383 C  C   . CYS   A 1 578 ? 3.09170   22.59094  74.08263  1.000 25.32274 ? 581  CYS   A C   1 
ATOM   4384 O  O   . CYS   A 1 578 ? 4.25356   22.43451  73.69782  1.000 21.85334 ? 581  CYS   A O   1 
ATOM   4385 C  CB  . CYS   A 1 578 ? 2.32139   20.22570  73.73277  1.000 24.67379 ? 581  CYS   A CB  1 
ATOM   4386 S  SG  . CYS   A 1 578 ? 2.77848   19.88016  75.45026  1.000 24.66193 ? 581  CYS   A SG  1 
ATOM   4387 N  N   . ALA   A 1 579 ? 2.73962   23.53503  74.96586  1.000 24.47650 ? 582  ALA   A N   1 
ATOM   4388 C  CA  . ALA   A 1 579 ? 3.71197   24.46531  75.53083  1.000 17.16329 ? 582  ALA   A CA  1 
ATOM   4389 C  C   . ALA   A 1 579 ? 4.77774   23.76862  76.36791  1.000 20.57409 ? 582  ALA   A C   1 
ATOM   4390 O  O   . ALA   A 1 579 ? 5.87906   24.30973  76.53425  1.000 26.16577 ? 582  ALA   A O   1 
ATOM   4391 C  CB  . ALA   A 1 579 ? 2.98985   25.50413  76.39941  1.000 24.51353 ? 582  ALA   A CB  1 
ATOM   4392 N  N   . ALA   A 1 580 ? 4.48644   22.59414  76.91501  1.000 21.78233 ? 583  ALA   A N   1 
ATOM   4393 C  CA  . ALA   A 1 580 ? 5.49797   21.94730  77.75680  1.000 24.61463 ? 583  ALA   A CA  1 
ATOM   4394 C  C   . ALA   A 1 580 ? 6.65762   21.37503  76.93000  1.000 29.08945 ? 583  ALA   A C   1 
ATOM   4395 O  O   . ALA   A 1 580 ? 7.82738   21.51479  77.31078  1.000 27.52505 ? 583  ALA   A O   1 
ATOM   4396 C  CB  . ALA   A 1 580 ? 4.84864   20.86644  78.61194  1.000 24.53767 ? 583  ALA   A CB  1 
ATOM   4397 N  N   . THR   A 1 581 ? 6.37799   20.78219  75.78015  1.000 24.70739 ? 584  THR   A N   1 
ATOM   4398 C  CA  . THR   A 1 581 ? 7.43476   20.07331  75.07152  1.000 18.02621 ? 584  THR   A CA  1 
ATOM   4399 C  C   . THR   A 1 581 ? 8.19360   21.01615  74.15679  1.000 20.55741 ? 584  THR   A C   1 
ATOM   4400 O  O   . THR   A 1 581 ? 7.66994   22.03046  73.71343  1.000 20.69823 ? 584  THR   A O   1 
ATOM   4401 C  CB  . THR   A 1 581 ? 6.86080   18.92766  74.23481  1.000 22.23934 ? 584  THR   A CB  1 
ATOM   4402 O  OG1 . THR   A 1 581 ? 5.96137   19.49029  73.27065  1.000 18.02341 ? 584  THR   A OG1 1 
ATOM   4403 C  CG2 . THR   A 1 581 ? 6.11839   17.91450  75.14320  1.000 20.16576 ? 584  THR   A CG2 1 
ATOM   4404 N  N   . SER   A 1 582 ? 9.43609   20.63677  73.84976  1.000 19.20542 ? 585  SER   A N   1 
ATOM   4405 C  CA  . SER   A 1 582 ? 10.27450  21.36641  72.89484  1.000 18.21867 ? 585  SER   A CA  1 
ATOM   4406 C  C   . SER   A 1 582 ? 11.31073  20.38778  72.37630  1.000 18.20751 ? 585  SER   A C   1 
ATOM   4407 O  O   . SER   A 1 582 ? 12.07682  19.83699  73.16525  1.000 18.61420 ? 585  SER   A O   1 
ATOM   4408 C  CB  . SER   A 1 582 ? 10.95998  22.56151  73.55109  1.000 24.10112 ? 585  SER   A CB  1 
ATOM   4409 O  OG  . SER   A 1 582 ? 12.04715  23.00203  72.76054  1.000 20.75305 ? 585  SER   A OG  1 
ATOM   4410 N  N   . SER   A 1 583 ? 11.35800  20.17346  71.05818  1.000 19.24085 ? 586  SER   A N   1 
ATOM   4411 C  CA  . SER   A 1 583 ? 12.31922  19.19741  70.56035  1.000 20.11150 ? 586  SER   A CA  1 
ATOM   4412 C  C   . SER   A 1 583 ? 13.75151  19.69289  70.74870  1.000 20.44002 ? 586  SER   A C   1 
ATOM   4413 O  O   . SER   A 1 583 ? 14.64383  18.90251  71.09573  1.000 20.37846 ? 586  SER   A O   1 
ATOM   4414 C  CB  . SER   A 1 583 ? 11.99714  18.85835  69.09858  1.000 20.06830 ? 586  SER   A CB  1 
ATOM   4415 O  OG  . SER   A 1 583 ? 10.72937  18.17965  69.05959  1.000 17.92098 ? 586  SER   A OG  1 
ATOM   4416 N  N   . SER   A 1 584 ? 13.98386  21.00675  70.56127  1.000 18.68092 ? 587  SER   A N   1 
ATOM   4417 C  CA  . SER   A 1 584 ? 15.30818  21.60295  70.78324  1.000 26.91078 ? 587  SER   A CA  1 
ATOM   4418 C  C   . SER   A 1 584 ? 15.76588  21.42661  72.22231  1.000 24.26493 ? 587  SER   A C   1 
ATOM   4419 O  O   . SER   A 1 584 ? 16.93015  21.06688  72.49439  1.000 21.86215 ? 587  SER   A O   1 
ATOM   4420 C  CB  . SER   A 1 584 ? 15.26749  23.10867  70.44943  1.000 19.57274 ? 587  SER   A CB  1 
ATOM   4421 O  OG  . SER   A 1 584 ? 15.23634  23.28588  69.06038  1.000 45.91477 ? 587  SER   A OG  1 
ATOM   4422 N  N   . LYS   A 1 585 ? 14.89149  21.78025  73.16523  1.000 19.23257 ? 588  LYS   A N   1 
ATOM   4423 C  CA  . LYS   A 1 585 ? 15.25854  21.65489  74.57176  1.000 19.77509 ? 588  LYS   A CA  1 
ATOM   4424 C  C   . LYS   A 1 585 ? 15.46771  20.20235  74.95290  1.000 22.49149 ? 588  LYS   A C   1 
ATOM   4425 O  O   . LYS   A 1 585 ? 16.36291  19.89328  75.75283  1.000 18.74535 ? 588  LYS   A O   1 
ATOM   4426 C  CB  . LYS   A 1 585 ? 14.18849  22.28150  75.45670  1.000 21.19921 ? 588  LYS   A CB  1 
ATOM   4427 C  CG  . LYS   A 1 585 ? 14.16193  23.81219  75.40841  1.000 32.01393 ? 588  LYS   A CG  1 
ATOM   4428 C  CD  . LYS   A 1 585 ? 13.10845  24.35389  76.36891  1.000 34.72379 ? 588  LYS   A CD  1 
ATOM   4429 C  CE  . LYS   A 1 585 ? 13.11795  25.89240  76.37187  1.000 45.32198 ? 588  LYS   A CE  1 
ATOM   4430 N  NZ  . LYS   A 1 585 ? 12.13925  26.48206  77.33474  1.000 57.28948 ? 588  LYS   A NZ  1 
ATOM   4431 N  N   . PHE   A 1 586 ? 14.64154  19.28790  74.41358  1.000 16.70860 ? 589  PHE   A N   1 
ATOM   4432 C  CA  . PHE   A 1 586 ? 14.84889  17.87514  74.74760  1.000 20.33120 ? 589  PHE   A CA  1 
ATOM   4433 C  C   . PHE   A 1 586 ? 16.17748  17.35925  74.19596  1.000 18.93274 ? 589  PHE   A C   1 
ATOM   4434 O  O   . PHE   A 1 586 ? 16.89898  16.62826  74.88577  1.000 19.88410 ? 589  PHE   A O   1 
ATOM   4435 C  CB  . PHE   A 1 586 ? 13.67619  17.02669  74.24588  1.000 18.80467 ? 589  PHE   A CB  1 
ATOM   4436 C  CG  . PHE   A 1 586 ? 13.71202  15.59312  74.72794  1.000 18.75085 ? 589  PHE   A CG  1 
ATOM   4437 C  CD1 . PHE   A 1 586 ? 13.34413  15.27655  76.02332  1.000 22.35507 ? 589  PHE   A CD1 1 
ATOM   4438 C  CD2 . PHE   A 1 586 ? 14.12257  14.57348  73.88604  1.000 17.77085 ? 589  PHE   A CD2 1 
ATOM   4439 C  CE1 . PHE   A 1 586 ? 13.38827  13.97609  76.47936  1.000 21.28246 ? 589  PHE   A CE1 1 
ATOM   4440 C  CE2 . PHE   A 1 586 ? 14.16264  13.24196  74.33815  1.000 18.71307 ? 589  PHE   A CE2 1 
ATOM   4441 C  CZ  . PHE   A 1 586 ? 13.77759  12.95629  75.64111  1.000 18.11004 ? 589  PHE   A CZ  1 
ATOM   4442 N  N   . ALA   A 1 587 ? 16.54709  17.74835  72.96799  1.000 17.28842 ? 590  ALA   A N   1 
ATOM   4443 C  CA  . ALA   A 1 587 ? 17.83812  17.31318  72.42866  1.000 18.83914 ? 590  ALA   A CA  1 
ATOM   4444 C  C   . ALA   A 1 587 ? 19.00101  17.84765  73.26882  1.000 21.55727 ? 590  ALA   A C   1 
ATOM   4445 O  O   . ALA   A 1 587 ? 20.00557  17.15076  73.49654  1.000 17.91217 ? 590  ALA   A O   1 
ATOM   4446 C  CB  . ALA   A 1 587 ? 17.96917  17.77053  70.96855  1.000 26.04211 ? 590  ALA   A CB  1 
ATOM   4447 N  N   . LYS   A 1 588 ? 18.88487  19.08026  73.74487  1.000 20.16815 ? 591  LYS   A N   1 
ATOM   4448 C  CA  . LYS   A 1 588 ? 19.91805  19.61584  74.62961  1.000 24.46320 ? 591  LYS   A CA  1 
ATOM   4449 C  C   . LYS   A 1 588 ? 19.97033  18.84000  75.94575  1.000 21.35114 ? 591  LYS   A C   1 
ATOM   4450 O  O   . LYS   A 1 588 ? 21.05199  18.60778  76.50035  1.000 17.37032 ? 591  LYS   A O   1 
ATOM   4451 C  CB  . LYS   A 1 588 ? 19.65813  21.09356  74.89264  1.000 22.88203 ? 591  LYS   A CB  1 
ATOM   4452 C  CG  . LYS   A 1 588 ? 20.77733  21.75273  75.66696  1.000 33.45938 ? 591  LYS   A CG  1 
ATOM   4453 C  CD  . LYS   A 1 588 ? 22.12472  21.50145  74.96424  1.000 40.86360 ? 591  LYS   A CD  1 
ATOM   4454 C  CE  . LYS   A 1 588 ? 23.16659  22.51040  75.38735  1.000 60.29468 ? 591  LYS   A CE  1 
ATOM   4455 N  NZ  . LYS   A 1 588 ? 23.20304  22.68078  76.86457  1.000 56.13596 ? 591  LYS   A NZ  1 
ATOM   4456 N  N   . ALA   A 1 589 ? 18.81541  18.44665  76.46895  1.000 18.16825 ? 592  ALA   A N   1 
ATOM   4457 C  CA  . ALA   A 1 589 ? 18.79866  17.64980  77.70363  1.000 20.47068 ? 592  ALA   A CA  1 
ATOM   4458 C  C   . ALA   A 1 589 ? 19.39314  16.25748  77.48575  1.000 17.33300 ? 592  ALA   A C   1 
ATOM   4459 O  O   . ALA   A 1 589 ? 20.02908  15.69960  78.39537  1.000 16.15395 ? 592  ALA   A O   1 
ATOM   4460 C  CB  . ALA   A 1 589 ? 17.37115  17.55630  78.24666  1.000 21.72508 ? 592  ALA   A CB  1 
ATOM   4461 N  N   . VAL   A 1 590 ? 19.16928  15.66949  76.30536  1.000 15.79357 ? 593  VAL   A N   1 
ATOM   4462 C  CA  . VAL   A 1 590 ? 19.80517  14.39852  75.94656  1.000 16.51591 ? 593  VAL   A CA  1 
ATOM   4463 C  C   . VAL   A 1 590 ? 21.32569  14.53172  75.95656  1.000 19.27490 ? 593  VAL   A C   1 
ATOM   4464 O  O   . VAL   A 1 590 ? 22.04075  13.69151  76.52501  1.000 17.51081 ? 593  VAL   A O   1 
ATOM   4465 C  CB  . VAL   A 1 590 ? 19.29299  13.91351  74.57637  1.000 18.16254 ? 593  VAL   A CB  1 
ATOM   4466 C  CG1 . VAL   A 1 590 ? 20.17454  12.76321  74.02466  1.000 18.76238 ? 593  VAL   A CG1 1 
ATOM   4467 C  CG2 . VAL   A 1 590 ? 17.80651  13.48054  74.70560  1.000 18.15220 ? 593  VAL   A CG2 1 
ATOM   4468 N  N   . GLU   A 1 591 ? 21.84318  15.58061  75.31006  1.000 19.90732 ? 594  GLU   A N   1 
ATOM   4469 C  CA  . GLU   A 1 591 ? 23.28655  15.84312  75.32547  1.000 19.99132 ? 594  GLU   A CA  1 
ATOM   4470 C  C   . GLU   A 1 591 ? 23.82263  15.98865  76.74781  1.000 17.90788 ? 594  GLU   A C   1 
ATOM   4471 O  O   . GLU   A 1 591 ? 24.85309  15.40411  77.10725  1.000 18.85299 ? 594  GLU   A O   1 
ATOM   4472 C  CB  . GLU   A 1 591 ? 23.58391  17.11470  74.51451  1.000 17.27081 ? 594  GLU   A CB  1 
ATOM   4473 C  CG  . GLU   A 1 591 ? 25.06882  17.47268  74.47519  1.000 22.25479 ? 594  GLU   A CG  1 
ATOM   4474 C  CD  . GLU   A 1 591 ? 25.29922  18.82651  73.81622  1.000 35.85615 ? 594  GLU   A CD  1 
ATOM   4475 O  OE1 . GLU   A 1 591 ? 25.10889  18.92629  72.58928  1.000 50.83266 ? 594  GLU   A OE1 1 
ATOM   4476 O  OE2 . GLU   A 1 591 ? 25.62520  19.78551  74.52974  1.000 49.60524 ? 594  GLU   A OE2 1 
ATOM   4477 N  N   . GLU   A 1 592 ? 23.16566  16.79947  77.56996  1.000 19.79686 ? 595  GLU   A N   1 
ATOM   4478 C  CA  . GLU   A 1 592 ? 23.67996  16.97485  78.92580  1.000 19.81415 ? 595  GLU   A CA  1 
ATOM   4479 C  C   . GLU   A 1 592 ? 23.63680  15.66945  79.71255  1.000 19.49138 ? 595  GLU   A C   1 
ATOM   4480 O  O   . GLU   A 1 592 ? 24.51032  15.41480  80.55338  1.000 19.46592 ? 595  GLU   A O   1 
ATOM   4481 C  CB  . GLU   A 1 592 ? 22.87283  18.05679  79.63463  1.000 21.56143 ? 595  GLU   A CB  1 
ATOM   4482 C  CG  . GLU   A 1 592 ? 23.07410  19.43702  79.01079  1.000 26.68579 ? 595  GLU   A CG  1 
ATOM   4483 C  CD  . GLU   A 1 592 ? 22.16760  20.50758  79.64301  1.000 53.61011 ? 595  GLU   A CD  1 
ATOM   4484 O  OE1 . GLU   A 1 592 ? 21.16806  20.15758  80.31585  1.000 43.71364 ? 595  GLU   A OE1 1 
ATOM   4485 O  OE2 . GLU   A 1 592 ? 22.45430  21.70436  79.45633  1.000 59.77327 ? 595  GLU   A OE2 1 
ATOM   4486 N  N   . SER   A 1 593 ? 22.61491  14.84290  79.46845  1.000 18.47088 ? 596  SER   A N   1 
ATOM   4487 C  CA  . SER   A 1 593 ? 22.49470  13.56834  80.17204  1.000 16.78855 ? 596  SER   A CA  1 
ATOM   4488 C  C   . SER   A 1 593 ? 23.58371  12.59878  79.75130  1.000 16.66086 ? 596  SER   A C   1 
ATOM   4489 O  O   . SER   A 1 593 ? 24.18707  11.92916  80.59455  1.000 17.09323 ? 596  SER   A O   1 
ATOM   4490 C  CB  . SER   A 1 593 ? 21.11420  12.95524  79.90227  1.000 18.58782 ? 596  SER   A CB  1 
ATOM   4491 O  OG  . SER   A 1 593 ? 20.12623  13.80844  80.45627  1.000 19.76635 ? 596  SER   A OG  1 
ATOM   4492 N  N   . LEU   A 1 594 ? 23.85427  12.50905  78.45307  1.000 14.99079 ? 597  LEU   A N   1 
ATOM   4493 C  CA  . LEU   A 1 594 ? 24.94133  11.63692  78.00415  1.000 16.84214 ? 597  LEU   A CA  1 
ATOM   4494 C  C   . LEU   A 1 594 ? 26.29424  12.11249  78.52106  1.000 17.27807 ? 597  LEU   A C   1 
ATOM   4495 O  O   . LEU   A 1 594 ? 27.16114  11.29025  78.81059  1.000 18.05551 ? 597  LEU   A O   1 
ATOM   4496 C  CB  . LEU   A 1 594 ? 24.95498  11.55818  76.47633  1.000 16.46785 ? 597  LEU   A CB  1 
ATOM   4497 C  CG  . LEU   A 1 594 ? 23.71835  10.85100  75.88073  1.000 17.65698 ? 597  LEU   A CG  1 
ATOM   4498 C  CD1 . LEU   A 1 594 ? 23.67509  11.11044  74.37750  1.000 18.87658 ? 597  LEU   A CD1 1 
ATOM   4499 C  CD2 . LEU   A 1 594 ? 23.72556  9.34508   76.18739  1.000 19.60914 ? 597  LEU   A CD2 1 
ATOM   4500 N  N   . ILE   A 1 595 ? 26.49656  13.42819  78.63196  1.000 20.67090 ? 598  ILE   A N   1 
ATOM   4501 C  CA  . ILE   A 1 595 ? 27.75403  13.91923  79.20207  1.000 18.40142 ? 598  ILE   A CA  1 
ATOM   4502 C  C   . ILE   A 1 595 ? 27.82010  13.59860  80.68456  1.000 20.96525 ? 598  ILE   A C   1 
ATOM   4503 O  O   . ILE   A 1 595 ? 28.86122  13.17901  81.18920  1.000 20.75788 ? 598  ILE   A O   1 
ATOM   4504 C  CB  . ILE   A 1 595 ? 27.91653  15.42588  78.94656  1.000 20.47382 ? 598  ILE   A CB  1 
ATOM   4505 C  CG1 . ILE   A 1 595 ? 28.02803  15.69116  77.44665  1.000 19.59229 ? 598  ILE   A CG1 1 
ATOM   4506 C  CG2 . ILE   A 1 595 ? 29.13557  15.96509  79.67098  1.000 25.52099 ? 598  ILE   A CG2 1 
ATOM   4507 C  CD1 . ILE   A 1 595 ? 29.23099  15.07081  76.79053  1.000 29.71893 ? 598  ILE   A CD1 1 
ATOM   4508 N  N   . ASP   A 1 596 ? 26.71764  13.80381  81.41134  1.000 20.91926 ? 599  ASP   A N   1 
ATOM   4509 C  CA  . ASP   A 1 596 ? 26.69958  13.45590  82.83600  1.000 20.50620 ? 599  ASP   A CA  1 
ATOM   4510 C  C   . ASP   A 1 596 ? 27.02461  11.98767  83.05654  1.000 19.23233 ? 599  ASP   A C   1 
ATOM   4511 O  O   . ASP   A 1 596 ? 27.77926  11.63930  83.97618  1.000 17.89138 ? 599  ASP   A O   1 
ATOM   4512 C  CB  . ASP   A 1 596 ? 25.32168  13.74810  83.43213  1.000 16.31951 ? 599  ASP   A CB  1 
ATOM   4513 C  CG  . ASP   A 1 596 ? 25.07483  15.22136  83.65217  1.000 33.20454 ? 599  ASP   A CG  1 
ATOM   4514 O  OD1 . ASP   A 1 596 ? 26.05228  15.98625  83.52662  1.000 28.01810 ? 599  ASP   A OD1 1 
ATOM   4515 O  OD2 . ASP   A 1 596 ? 23.90343  15.60490  83.95405  1.000 28.33081 ? 599  ASP   A OD2 1 
ATOM   4516 N  N   . MET   A 1 597 ? 26.42921  11.10281  82.24089  1.000 15.92036 ? 600  MET   A N   1 
ATOM   4517 C  CA  . MET   A 1 597 ? 26.63365  9.66678   82.40403  1.000 17.23698 ? 600  MET   A CA  1 
ATOM   4518 C  C   . MET   A 1 597 ? 28.05324  9.27810   82.05726  1.000 15.87399 ? 600  MET   A C   1 
ATOM   4519 O  O   . MET   A 1 597 ? 28.65317  8.43511   82.72826  1.000 18.53763 ? 600  MET   A O   1 
ATOM   4520 C  CB  . MET   A 1 597 ? 25.62756  8.88954   81.54055  1.000 18.05782 ? 600  MET   A CB  1 
ATOM   4521 C  CG  . MET   A 1 597 ? 24.19767  9.02807   82.08211  1.000 15.55113 ? 600  MET   A CG  1 
ATOM   4522 S  SD  . MET   A 1 597 ? 22.92668  8.39802   80.94091  1.000 22.58102 ? 600  MET   A SD  1 
ATOM   4523 C  CE  . MET   A 1 597 ? 23.27537  6.66178   81.01081  1.000 17.98593 ? 600  MET   A CE  1 
ATOM   4524 N  N   . ARG   A 1 598 ? 28.62271  9.90596   81.03437  1.000 18.31280 ? 601  ARG   A N   1 
ATOM   4525 C  CA  . ARG   A 1 598 ? 30.04133  9.71240   80.74050  1.000 18.74658 ? 601  ARG   A CA  1 
ATOM   4526 C  C   . ARG   A 1 598 ? 30.90686  10.08198  81.94035  1.000 20.30889 ? 601  ARG   A C   1 
ATOM   4527 O  O   . ARG   A 1 598 ? 31.79064  9.31425   82.34230  1.000 20.81039 ? 601  ARG   A O   1 
ATOM   4528 C  CB  . ARG   A 1 598 ? 30.42788  10.56401  79.53237  1.000 17.70279 ? 601  ARG   A CB  1 
ATOM   4529 C  CG  . ARG   A 1 598 ? 31.91111  10.49632  79.19455  1.000 21.01227 ? 601  ARG   A CG  1 
ATOM   4530 C  CD  . ARG   A 1 598 ? 32.29097  11.71434  78.33298  1.000 25.76263 ? 601  ARG   A CD  1 
ATOM   4531 N  NE  . ARG   A 1 598 ? 32.25865  12.94484  79.12979  1.000 23.61353 ? 601  ARG   A NE  1 
ATOM   4532 C  CZ  . ARG   A 1 598 ? 32.56467  14.14912  78.66409  1.000 30.50354 ? 601  ARG   A CZ  1 
ATOM   4533 N  NH1 . ARG   A 1 598 ? 32.87795  14.33863  77.39020  1.000 27.96355 ? 601  ARG   A NH1 1 
ATOM   4534 N  NH2 . ARG   A 1 598 ? 32.54285  15.19162  79.49304  1.000 23.85503 ? 601  ARG   A NH2 1 
ATOM   4535 N  N   . ASP   A 1 599 ? 30.66173  11.25855  82.53907  1.000 21.83196 ? 602  ASP   A N   1 
ATOM   4536 C  CA  . ASP   A 1 599 ? 31.48550  11.67824  83.68364  1.000 21.69689 ? 602  ASP   A CA  1 
ATOM   4537 C  C   . ASP   A 1 599 ? 31.33518  10.71543  84.86044  1.000 25.14925 ? 602  ASP   A C   1 
ATOM   4538 O  O   . ASP   A 1 599 ? 32.30988  10.42792  85.56512  1.000 21.83370 ? 602  ASP   A O   1 
ATOM   4539 C  CB  . ASP   A 1 599 ? 31.13106  13.10837  84.12123  1.000 22.77999 ? 602  ASP   A CB  1 
ATOM   4540 C  CG  . ASP   A 1 599 ? 31.38521  14.14647  83.03333  1.000 25.05371 ? 602  ASP   A CG  1 
ATOM   4541 O  OD1 . ASP   A 1 599 ? 32.15525  13.84302  82.09557  1.000 25.96069 ? 602  ASP   A OD1 1 
ATOM   4542 O  OD2 . ASP   A 1 599 ? 30.81047  15.26396  83.10560  1.000 23.01106 ? 602  ASP   A OD2 1 
ATOM   4543 N  N   . LEU   A 1 600 ? 30.11802  10.22037  85.10761  1.000 20.04052 ? 603  LEU   A N   1 
ATOM   4544 C  CA  . LEU   A 1 600 ? 29.92124  9.23837   86.18108  1.000 20.03175 ? 603  LEU   A CA  1 
ATOM   4545 C  C   . LEU   A 1 600 ? 30.69228  7.95261   85.91279  1.000 21.91479 ? 603  LEU   A C   1 
ATOM   4546 O  O   . LEU   A 1 600 ? 31.24760  7.34439   86.84220  1.000 19.37560 ? 603  LEU   A O   1 
ATOM   4547 C  CB  . LEU   A 1 600 ? 28.42159  8.92333   86.35628  1.000 18.71899 ? 603  LEU   A CB  1 
ATOM   4548 C  CG  . LEU   A 1 600 ? 27.63655  10.01829  87.07884  1.000 21.48356 ? 603  LEU   A CG  1 
ATOM   4549 C  CD1 . LEU   A 1 600 ? 26.10613  9.86734   86.87723  1.000 18.35805 ? 603  LEU   A CD1 1 
ATOM   4550 C  CD2 . LEU   A 1 600 ? 27.99474  10.07969  88.59437  1.000 19.48632 ? 603  LEU   A CD2 1 
ATOM   4551 N  N   . CYS   A 1 601 ? 30.71010  7.49240   84.65981  1.000 20.40623 ? 604  CYS   A N   1 
ATOM   4552 C  CA  . CYS   A 1 601 ? 31.46381  6.28258   84.33009  1.000 28.56572 ? 604  CYS   A CA  1 
ATOM   4553 C  C   . CYS   A 1 601 ? 32.96684  6.52052   84.27885  1.000 27.62618 ? 604  CYS   A C   1 
ATOM   4554 O  O   . CYS   A 1 601 ? 33.72980  5.56035   84.12779  1.000 34.92865 ? 604  CYS   A O   1 
ATOM   4555 C  CB  . CYS   A 1 601 ? 30.98020  5.70078   82.98281  1.000 22.55607 ? 604  CYS   A CB  1 
ATOM   4556 S  SG  . CYS   A 1 601 ? 29.26682  5.14401   82.97299  1.000 27.61301 ? 604  CYS   A SG  1 
ATOM   4557 N  N   . SER   A 1 602 ? 33.42120  7.77025   84.38363  1.000 25.11648 ? 605  SER   A N   1 
ATOM   4558 C  CA  . SER   A 1 602 ? 34.84200  8.09447   84.34984  1.000 24.48773 ? 605  SER   A CA  1 
ATOM   4559 C  C   . SER   A 1 602 ? 35.37128  8.48006   85.72426  1.000 35.32110 ? 605  SER   A C   1 
ATOM   4560 O  O   . SER   A 1 602 ? 36.37499  9.18480   85.81404  1.000 40.49686 ? 605  SER   A O   1 
ATOM   4561 C  CB  . SER   A 1 602 ? 35.12859  9.23644   83.35526  1.000 24.07326 ? 605  SER   A CB  1 
ATOM   4562 O  OG  . SER   A 1 602 ? 34.63119  8.94259   82.05462  1.000 30.31928 ? 605  SER   A OG  1 
ATOM   4563 N  N   . LEU   A 1 603 ? 34.66467  8.11734   86.78868  1.000 31.86079 ? 606  LEU   A N   1 
ATOM   4564 C  CA  . LEU   A 1 603 ? 35.15042  8.35277   88.13896  1.000 32.78003 ? 606  LEU   A CA  1 
ATOM   4565 C  C   . LEU   A 1 603 ? 36.28030  7.37959   88.44289  1.000 39.74406 ? 606  LEU   A C   1 
ATOM   4566 O  O   . LEU   A 1 603 ? 37.38573  7.80049   88.71151  1.000 44.06799 ? 606  LEU   A O   1 
ATOM   4567 C  CB  . LEU   A 1 603 ? 34.03758  8.17658   89.17266  1.000 35.27778 ? 606  LEU   A CB  1 
ATOM   4568 C  CG  . LEU   A 1 603 ? 32.91491  9.20739   89.20679  1.000 32.04388 ? 606  LEU   A CG  1 
ATOM   4569 C  CD1 . LEU   A 1 603 ? 31.91427  8.80711   90.26734  1.000 44.67640 ? 606  LEU   A CD1 1 
ATOM   4570 C  CD2 . LEU   A 1 603 ? 33.46217  10.61419  89.48985  1.000 33.47506 ? 606  LEU   A CD2 1 
HETATM 4571 C  C13 . A1IAP B 2 .   ? 7.64240   3.60311   65.53851  1.000 22.02002 ? 701  A1IAP A C13 1 
HETATM 4572 C  C23 . A1IAP B 2 .   ? 9.47021   1.64168   62.15379  1.000 23.12835 ? 701  A1IAP A C23 1 
HETATM 4573 C  C12 . A1IAP B 2 .   ? 6.83427   4.67268   65.92921  1.000 24.24894 ? 701  A1IAP A C12 1 
HETATM 4574 C  C22 . A1IAP B 2 .   ? 8.53849   0.67516   61.71783  1.000 20.87331 ? 701  A1IAP A C22 1 
HETATM 4575 C  C11 . A1IAP B 2 .   ? 5.87629   6.15753   67.63008  1.000 26.26906 ? 701  A1IAP A C11 1 
HETATM 4576 C  C21 . A1IAP B 2 .   ? 8.32095   0.44659   60.37732  1.000 18.46909 ? 701  A1IAP A C21 1 
HETATM 4577 C  C01 . A1IAP B 2 .   ? 11.25883  -3.00434  66.36849  1.000 33.37059 ? 701  A1IAP A C01 1 
HETATM 4578 C  C02 . A1IAP B 2 .   ? 12.11416  -1.94730  65.60717  1.000 46.27097 ? 701  A1IAP A C02 1 
HETATM 4579 C  C03 . A1IAP B 2 .   ? 11.44647  -0.56021  65.47280  1.000 27.44772 ? 701  A1IAP A C03 1 
HETATM 4580 C  C05 . A1IAP B 2 .   ? 8.97289   1.13740   64.64303  1.000 24.99074 ? 701  A1IAP A C05 1 
HETATM 4581 C  C06 . A1IAP B 2 .   ? 9.23795   1.75184   66.03502  1.000 24.90382 ? 701  A1IAP A C06 1 
HETATM 4582 C  C07 . A1IAP B 2 .   ? 8.38825   2.86010   66.46311  1.000 32.63006 ? 701  A1IAP A C07 1 
HETATM 4583 C  C08 . A1IAP B 2 .   ? 8.28988   3.25975   67.82153  1.000 26.61492 ? 701  A1IAP A C08 1 
HETATM 4584 C  C09 . A1IAP B 2 .   ? 7.48513   4.32443   68.19678  1.000 24.25890 ? 701  A1IAP A C09 1 
HETATM 4585 C  C14 . A1IAP B 2 .   ? 9.69969   1.91134   63.56621  1.000 23.17810 ? 701  A1IAP A C14 1 
HETATM 4586 C  C15 . A1IAP B 2 .   ? 10.63433  2.86964   63.86161  1.000 22.22472 ? 701  A1IAP A C15 1 
HETATM 4587 C  C16 . A1IAP B 2 .   ? 11.33697  3.58180   62.84362  1.000 22.78581 ? 701  A1IAP A C16 1 
HETATM 4588 C  C17 . A1IAP B 2 .   ? 11.10535  3.34199   61.52492  1.000 23.44973 ? 701  A1IAP A C17 1 
HETATM 4589 C  C18 . A1IAP B 2 .   ? 10.15705  2.35907   61.15599  1.000 22.30909 ? 701  A1IAP A C18 1 
HETATM 4590 C  C19 . A1IAP B 2 .   ? 9.95107   2.10160   59.75365  1.000 20.66203 ? 701  A1IAP A C19 1 
HETATM 4591 C  C20 . A1IAP B 2 .   ? 9.02903   1.16264   59.38642  1.000 22.13021 ? 701  A1IAP A C20 1 
HETATM 4592 N  N10 . A1IAP B 2 .   ? 6.75680   5.03548   67.23498  1.000 29.22345 ? 701  A1IAP A N10 1 
HETATM 4593 S  S04 . A1IAP B 2 .   ? 9.71012   -0.60540  64.81448  1.000 35.41307 ? 701  A1IAP A S04 1 
HETATM 4594 NA NA  . NA    C 3 .   ? 5.75875   21.77479  72.11965  1.000 20.50042 ? 702  NA    A NA  1 
HETATM 4595 O  O   . HOH   D 4 .   ? 35.46352  10.22968  80.25415  1.000 46.00743 ? 801  HOH   A O   1 
HETATM 4596 O  O   . HOH   D 4 .   ? -0.15042  19.18787  71.10529  1.000 27.67953 ? 802  HOH   A O   1 
HETATM 4597 O  O   . HOH   D 4 .   ? 10.40042  13.03016  91.30465  1.000 55.64405 ? 803  HOH   A O   1 
HETATM 4598 O  O   . HOH   D 4 .   ? 17.47824  -2.37773  92.21157  1.000 43.80184 ? 804  HOH   A O   1 
HETATM 4599 O  O   . HOH   D 4 .   ? 12.75058  17.13103  46.26693  1.000 34.45147 ? 805  HOH   A O   1 
HETATM 4600 O  O   . HOH   D 4 .   ? -8.75493  9.00277   81.57578  1.000 43.63613 ? 806  HOH   A O   1 
HETATM 4601 O  O   . HOH   D 4 .   ? -11.132   -16.188   95.888    1.000 40.29464 ? 807  HOH   A O   1 
HETATM 4602 O  O   . HOH   D 4 .   ? -10.94362 16.91885  56.52742  1.000 40.03583 ? 808  HOH   A O   1 
HETATM 4603 O  O   . HOH   D 4 .   ? 9.94424   22.86435  77.30499  1.000 41.39332 ? 809  HOH   A O   1 
HETATM 4604 O  O   . HOH   D 4 .   ? -1.14090  3.99340   65.00298  1.000 31.09371 ? 810  HOH   A O   1 
HETATM 4605 O  O   . HOH   D 4 .   ? 1.98112   5.85784   54.96045  1.000 21.43209 ? 811  HOH   A O   1 
HETATM 4606 O  O   . HOH   D 4 .   ? -12.86536 -8.73035  71.94875  1.000 29.52722 ? 812  HOH   A O   1 
HETATM 4607 O  O   . HOH   D 4 .   ? 15.93172  1.61280   84.27904  1.000 17.81633 ? 813  HOH   A O   1 
HETATM 4608 O  O   . HOH   D 4 .   ? -12.31395 4.98176   83.15650  1.000 32.73100 ? 814  HOH   A O   1 
HETATM 4609 O  O   . HOH   D 4 .   ? -8.71157  -1.48469  37.95399  1.000 51.29814 ? 815  HOH   A O   1 
HETATM 4610 O  O   . HOH   D 4 .   ? -5.34408  -16.02566 92.21387  1.000 37.47266 ? 816  HOH   A O   1 
HETATM 4611 O  O   . HOH   D 4 .   ? 8.94007   20.77509  61.70216  1.000 35.69504 ? 817  HOH   A O   1 
HETATM 4612 O  O   . HOH   D 4 .   ? 4.27733   10.99421  85.41454  1.000 40.63546 ? 818  HOH   A O   1 
HETATM 4613 O  O   . HOH   D 4 .   ? 2.59150   -8.27559  57.76054  1.000 33.75420 ? 819  HOH   A O   1 
HETATM 4614 O  O   . HOH   D 4 .   ? 16.97624  -8.44996  53.14126  1.000 37.99511 ? 820  HOH   A O   1 
HETATM 4615 O  O   . HOH   D 4 .   ? 18.23169  -11.91620 56.43118  1.000 35.98392 ? 821  HOH   A O   1 
HETATM 4616 O  O   . HOH   D 4 .   ? -0.31590  4.33699   98.12279  1.000 44.40930 ? 822  HOH   A O   1 
HETATM 4617 O  O   . HOH   D 4 .   ? 28.69940  16.05199  84.31563  1.000 29.14333 ? 823  HOH   A O   1 
HETATM 4618 O  O   . HOH   D 4 .   ? -11.82167 -6.95810  70.76930  1.000 39.58819 ? 824  HOH   A O   1 
HETATM 4619 O  O   . HOH   D 4 .   ? 14.80041  14.42447  31.13130  1.000 54.29108 ? 825  HOH   A O   1 
HETATM 4620 O  O   . HOH   D 4 .   ? -11.77008 -11.84140 71.11062  1.000 27.35884 ? 826  HOH   A O   1 
HETATM 4621 O  O   . HOH   D 4 .   ? 14.81473  -4.44935  89.78264  1.000 46.92659 ? 827  HOH   A O   1 
HETATM 4622 O  O   . HOH   D 4 .   ? 6.24321   -20.53739 73.44462  1.000 40.20118 ? 828  HOH   A O   1 
HETATM 4623 O  O   . HOH   D 4 .   ? 31.80318  8.50257   97.95428  1.000 43.30321 ? 829  HOH   A O   1 
HETATM 4624 O  O   . HOH   D 4 .   ? 18.33521  1.66244   92.25529  1.000 27.45178 ? 830  HOH   A O   1 
HETATM 4625 O  O   . HOH   D 4 .   ? -6.13392  1.43668   73.09888  1.000 34.49475 ? 831  HOH   A O   1 
HETATM 4626 O  O   . HOH   D 4 .   ? -2.28833  -22.65490 75.39239  1.000 26.74427 ? 832  HOH   A O   1 
HETATM 4627 O  O   . HOH   D 4 .   ? 10.05784  -17.03340 76.61397  1.000 34.14450 ? 833  HOH   A O   1 
HETATM 4628 O  O   . HOH   D 4 .   ? -7.10267  3.97001   90.70848  1.000 31.66813 ? 834  HOH   A O   1 
HETATM 4629 O  O   . HOH   D 4 .   ? -12.54842 -3.47110  92.14331  1.000 42.75337 ? 835  HOH   A O   1 
HETATM 4630 O  O   . HOH   D 4 .   ? -5.65147  -1.12553  86.95670  1.000 23.54619 ? 836  HOH   A O   1 
HETATM 4631 O  O   . HOH   D 4 .   ? 6.91761   20.54741  59.71717  1.000 25.25868 ? 837  HOH   A O   1 
HETATM 4632 O  O   . HOH   D 4 .   ? 21.51889  9.14416   39.08864  1.000 41.96126 ? 838  HOH   A O   1 
HETATM 4633 O  O   . HOH   D 4 .   ? 15.43135  2.97985   81.95421  1.000 19.06333 ? 839  HOH   A O   1 
HETATM 4634 O  O   . HOH   D 4 .   ? 29.39443  7.53035   63.39126  1.000 39.85497 ? 840  HOH   A O   1 
HETATM 4635 O  O   . HOH   D 4 .   ? 9.31762   23.82937  63.64573  1.000 36.35696 ? 841  HOH   A O   1 
HETATM 4636 O  O   . HOH   D 4 .   ? -10.52249 -17.97277 74.16406  1.000 37.10823 ? 842  HOH   A O   1 
HETATM 4637 O  O   . HOH   D 4 .   ? 3.10288   -10.37118 56.39499  1.000 35.63316 ? 843  HOH   A O   1 
HETATM 4638 O  O   . HOH   D 4 .   ? -14.38695 21.82219  52.55275  1.000 42.58626 ? 844  HOH   A O   1 
HETATM 4639 O  O   . HOH   D 4 .   ? 2.07165   5.91004   94.27461  1.000 38.38994 ? 845  HOH   A O   1 
HETATM 4640 O  O   . HOH   D 4 .   ? 8.99705   -6.90201  64.85377  1.000 21.32266 ? 846  HOH   A O   1 
HETATM 4641 O  O   . HOH   D 4 .   ? 18.53155  -2.43602  62.16554  1.000 35.05234 ? 847  HOH   A O   1 
HETATM 4642 O  O   . HOH   D 4 .   ? 15.99393  -11.17684 39.90835  1.000 53.31213 ? 848  HOH   A O   1 
HETATM 4643 O  O   . HOH   D 4 .   ? 6.44784   -9.44108  84.16063  1.000 21.03229 ? 849  HOH   A O   1 
HETATM 4644 O  O   . HOH   D 4 .   ? 0.80210   8.96396   80.47939  1.000 26.98857 ? 850  HOH   A O   1 
HETATM 4645 O  O   . HOH   D 4 .   ? 30.42120  1.02211   87.24396  1.000 36.01583 ? 851  HOH   A O   1 
HETATM 4646 O  O   . HOH   D 4 .   ? 22.05962  14.87452  94.51487  1.000 30.11594 ? 852  HOH   A O   1 
HETATM 4647 O  O   . HOH   D 4 .   ? -8.63010  -6.50238  62.34180  1.000 47.55693 ? 853  HOH   A O   1 
HETATM 4648 O  O   . HOH   D 4 .   ? 10.96536  23.95700  70.55875  1.000 42.21317 ? 854  HOH   A O   1 
HETATM 4649 O  O   . HOH   D 4 .   ? 7.20100   2.05847   84.57358  1.000 23.42080 ? 855  HOH   A O   1 
HETATM 4650 O  O   . HOH   D 4 .   ? 5.48622   -4.34613  78.86524  1.000 20.79281 ? 856  HOH   A O   1 
HETATM 4651 O  O   . HOH   D 4 .   ? -0.18343  -0.32035  54.19496  1.000 27.52171 ? 857  HOH   A O   1 
HETATM 4652 O  O   . HOH   D 4 .   ? -4.30898  9.32640   56.48807  1.000 21.73765 ? 858  HOH   A O   1 
HETATM 4653 O  O   . HOH   D 4 .   ? 14.37337  -10.08274 82.81716  1.000 24.36110 ? 859  HOH   A O   1 
HETATM 4654 O  O   . HOH   D 4 .   ? 2.63134   -7.45835  68.93356  1.000 21.63609 ? 860  HOH   A O   1 
HETATM 4655 O  O   . HOH   D 4 .   ? 12.449    -19.070   72.538    1.000 42.28330 ? 861  HOH   A O   1 
HETATM 4656 O  O   . HOH   D 4 .   ? -2.32857  9.82169   90.00239  1.000 37.84349 ? 862  HOH   A O   1 
HETATM 4657 O  O   . HOH   D 4 .   ? 2.86843   -16.87142 68.17142  1.000 22.68909 ? 863  HOH   A O   1 
HETATM 4658 O  O   . HOH   D 4 .   ? 12.56796  -18.56732 67.64426  1.000 26.00775 ? 864  HOH   A O   1 
HETATM 4659 O  O   . HOH   D 4 .   ? -4.92789  11.43900  93.64445  1.000 50.80491 ? 865  HOH   A O   1 
HETATM 4660 O  O   . HOH   D 4 .   ? 20.63918  19.35648  65.39360  1.000 38.50805 ? 866  HOH   A O   1 
HETATM 4661 O  O   . HOH   D 4 .   ? 6.02036   -0.32515  31.19591  1.000 39.33380 ? 867  HOH   A O   1 
HETATM 4662 O  O   . HOH   D 4 .   ? -20.20351 4.94026   47.80372  1.000 45.84268 ? 868  HOH   A O   1 
HETATM 4663 O  O   . HOH   D 4 .   ? 3.74272   -5.49181  92.43624  1.000 23.99152 ? 869  HOH   A O   1 
HETATM 4664 O  O   . HOH   D 4 .   ? 23.36265  -3.61862  80.02640  1.000 23.20263 ? 870  HOH   A O   1 
HETATM 4665 O  O   . HOH   D 4 .   ? 17.42591  -1.82747  76.53720  1.000 21.24049 ? 871  HOH   A O   1 
HETATM 4666 O  O   . HOH   D 4 .   ? 7.06750   25.62812  69.92620  1.000 35.61360 ? 872  HOH   A O   1 
HETATM 4667 O  O   . HOH   D 4 .   ? -2.83225  -5.80939  94.76431  1.000 36.51230 ? 873  HOH   A O   1 
HETATM 4668 O  O   . HOH   D 4 .   ? 36.50417  0.57665   80.57318  1.000 28.05267 ? 874  HOH   A O   1 
HETATM 4669 O  O   . HOH   D 4 .   ? 22.60017  15.09245  61.20286  1.000 43.24106 ? 875  HOH   A O   1 
HETATM 4670 O  O   . HOH   D 4 .   ? 2.54407   -3.15170  50.63775  1.000 40.44572 ? 876  HOH   A O   1 
HETATM 4671 O  O   . HOH   D 4 .   ? -8.45944  3.04986   47.98730  1.000 29.14806 ? 877  HOH   A O   1 
HETATM 4672 O  O   . HOH   D 4 .   ? 4.52772   -10.79401 82.62797  1.000 24.72061 ? 878  HOH   A O   1 
HETATM 4673 O  O   . HOH   D 4 .   ? 33.12871  -0.80339  83.96560  1.000 48.69329 ? 879  HOH   A O   1 
HETATM 4674 O  O   . HOH   D 4 .   ? -1.89135  25.85227  62.23443  1.000 31.83986 ? 880  HOH   A O   1 
HETATM 4675 O  O   . HOH   D 4 .   ? 12.66604  22.64680  68.64689  1.000 34.33437 ? 881  HOH   A O   1 
HETATM 4676 O  O   . HOH   D 4 .   ? 4.44795   -18.55024 80.38756  1.000 42.07860 ? 882  HOH   A O   1 
HETATM 4677 O  O   . HOH   D 4 .   ? 3.22804   25.70391  65.08563  1.000 32.40999 ? 883  HOH   A O   1 
HETATM 4678 O  O   . HOH   D 4 .   ? -12.89033 2.49650   52.66080  1.000 45.48264 ? 884  HOH   A O   1 
HETATM 4679 O  O   . HOH   D 4 .   ? 34.03887  -0.94376  73.28355  1.000 27.05889 ? 885  HOH   A O   1 
HETATM 4680 O  O   . HOH   D 4 .   ? 0.45431   -0.68561  75.53313  1.000 28.06767 ? 886  HOH   A O   1 
HETATM 4681 O  O   . HOH   D 4 .   ? -5.27335  16.09114  55.33518  1.000 25.21422 ? 887  HOH   A O   1 
HETATM 4682 O  O   . HOH   D 4 .   ? -0.62669  16.81579  34.01576  1.000 41.23563 ? 888  HOH   A O   1 
HETATM 4683 O  O   . HOH   D 4 .   ? 17.66580  -4.16151  60.04899  1.000 29.27199 ? 889  HOH   A O   1 
HETATM 4684 O  O   . HOH   D 4 .   ? 4.63251   10.49627  57.99721  1.000 20.59034 ? 890  HOH   A O   1 
HETATM 4685 O  O   . HOH   D 4 .   ? 1.60355   14.78318  52.74432  1.000 26.46317 ? 891  HOH   A O   1 
HETATM 4686 O  O   . HOH   D 4 .   ? 19.56827  -3.80503  76.46431  1.000 26.40989 ? 892  HOH   A O   1 
HETATM 4687 O  O   . HOH   D 4 .   ? 20.06317  -5.85059  54.11575  1.000 36.40976 ? 893  HOH   A O   1 
HETATM 4688 O  O   . HOH   D 4 .   ? -17.15877 -0.73804  82.72372  1.000 31.94437 ? 894  HOH   A O   1 
HETATM 4689 O  O   . HOH   D 4 .   ? 1.26475   4.10420   59.40260  1.000 20.99126 ? 895  HOH   A O   1 
HETATM 4690 O  O   . HOH   D 4 .   ? 17.72303  18.51882  33.91884  1.000 53.01436 ? 896  HOH   A O   1 
HETATM 4691 O  O   . HOH   D 4 .   ? -12.06144 -17.78552 87.68374  1.000 37.49710 ? 897  HOH   A O   1 
HETATM 4692 O  O   . HOH   D 4 .   ? 0.20682   11.55933  67.19394  1.000 18.75952 ? 898  HOH   A O   1 
HETATM 4693 O  O   . HOH   D 4 .   ? 7.37435   21.39382  70.46305  1.000 17.60570 ? 899  HOH   A O   1 
HETATM 4694 O  O   . HOH   D 4 .   ? 13.83977  5.91920   77.91980  1.000 17.01833 ? 900  HOH   A O   1 
HETATM 4695 O  O   . HOH   D 4 .   ? 0.939     24.222    66.239    1.000 28.03052 ? 901  HOH   A O   1 
HETATM 4696 O  O   . HOH   D 4 .   ? 17.43765  8.71363   94.49688  1.000 27.07132 ? 902  HOH   A O   1 
HETATM 4697 O  O   . HOH   D 4 .   ? 6.94442   -9.59466  76.03117  1.000 21.97701 ? 903  HOH   A O   1 
HETATM 4698 O  O   . HOH   D 4 .   ? 6.56560   -11.43997 62.24828  1.000 22.87571 ? 904  HOH   A O   1 
HETATM 4699 O  O   . HOH   D 4 .   ? 24.86461  -0.60664  90.88735  1.000 29.11460 ? 905  HOH   A O   1 
HETATM 4700 O  O   . HOH   D 4 .   ? 1.05871   -5.35581  41.02245  1.000 36.62590 ? 906  HOH   A O   1 
HETATM 4701 O  O   . HOH   D 4 .   ? -16.25138 8.08197   57.71300  1.000 34.55414 ? 907  HOH   A O   1 
HETATM 4702 O  O   . HOH   D 4 .   ? 13.73066  -4.38570  85.38415  1.000 22.08568 ? 908  HOH   A O   1 
HETATM 4703 O  O   . HOH   D 4 .   ? 3.74779   -12.37307 75.59559  1.000 33.94736 ? 909  HOH   A O   1 
HETATM 4704 O  O   . HOH   D 4 .   ? -0.69513  12.03950  77.19615  1.000 20.49802 ? 910  HOH   A O   1 
HETATM 4705 O  O   . HOH   D 4 .   ? -2.48700  13.79889  44.45122  1.000 28.32975 ? 911  HOH   A O   1 
HETATM 4706 O  O   . HOH   D 4 .   ? 6.57870   -0.21232  67.98776  1.000 30.73149 ? 912  HOH   A O   1 
HETATM 4707 O  O   . HOH   D 4 .   ? -8.79201  -13.89489 88.97279  1.000 28.01052 ? 913  HOH   A O   1 
HETATM 4708 O  O   . HOH   D 4 .   ? -2.43552  -3.17821  77.70512  1.000 22.19826 ? 914  HOH   A O   1 
HETATM 4709 O  O   . HOH   D 4 .   ? -3.61853  -0.93338  74.55852  1.000 28.90130 ? 915  HOH   A O   1 
HETATM 4710 O  O   . HOH   D 4 .   ? -19.17643 9.38107   51.97456  1.000 39.46636 ? 916  HOH   A O   1 
HETATM 4711 O  O   . HOH   D 4 .   ? 6.938     26.124    78.259    1.000 29.63767 ? 917  HOH   A O   1 
HETATM 4712 O  O   . HOH   D 4 .   ? 5.56857   12.33988  53.12851  1.000 24.26013 ? 918  HOH   A O   1 
HETATM 4713 O  O   . HOH   D 4 .   ? 12.63014  -14.23261 80.12650  1.000 32.45931 ? 919  HOH   A O   1 
HETATM 4714 O  O   . HOH   D 4 .   ? -1.03501  21.27805  53.19008  1.000 30.11290 ? 920  HOH   A O   1 
HETATM 4715 O  O   . HOH   D 4 .   ? 10.49789  13.79917  29.99521  1.000 42.51919 ? 921  HOH   A O   1 
HETATM 4716 O  O   . HOH   D 4 .   ? 23.64381  16.54098  92.66627  1.000 41.51614 ? 922  HOH   A O   1 
HETATM 4717 O  O   . HOH   D 4 .   ? -1.42285  15.26167  65.63204  1.000 22.89840 ? 923  HOH   A O   1 
HETATM 4718 O  O   . HOH   D 4 .   ? 26.13204  17.78198  81.47984  1.000 43.82515 ? 924  HOH   A O   1 
HETATM 4719 O  O   . HOH   D 4 .   ? 5.37413   17.15268  43.57500  1.000 35.61059 ? 925  HOH   A O   1 
HETATM 4720 O  O   . HOH   D 4 .   ? 10.07234  9.25835   81.57634  1.000 17.22759 ? 926  HOH   A O   1 
HETATM 4721 O  O   . HOH   D 4 .   ? 16.42433  -11.32511 42.59467  1.000 45.80241 ? 927  HOH   A O   1 
HETATM 4722 O  O   . HOH   D 4 .   ? 21.39723  10.92762  55.69543  1.000 43.94793 ? 928  HOH   A O   1 
HETATM 4723 O  O   . HOH   D 4 .   ? 11.71699  -18.31968 60.51078  1.000 32.18188 ? 929  HOH   A O   1 
HETATM 4724 O  O   . HOH   D 4 .   ? 8.76220   -7.27059  87.13861  1.000 35.54315 ? 930  HOH   A O   1 
HETATM 4725 O  O   . HOH   D 4 .   ? 1.38319   -10.28995 65.29528  1.000 24.06933 ? 931  HOH   A O   1 
HETATM 4726 O  O   . HOH   D 4 .   ? 15.26200  16.20505  91.59804  1.000 44.22202 ? 932  HOH   A O   1 
HETATM 4727 O  O   . HOH   D 4 .   ? -13.91614 -13.86754 76.09518  1.000 34.60480 ? 933  HOH   A O   1 
HETATM 4728 O  O   . HOH   D 4 .   ? -3.87025  -16.91940 88.96349  1.000 36.03116 ? 934  HOH   A O   1 
HETATM 4729 O  O   . HOH   D 4 .   ? 2.91161   -9.18098  77.21085  1.000 21.78477 ? 935  HOH   A O   1 
HETATM 4730 O  O   . HOH   D 4 .   ? 0.30927   -10.71582 91.42256  1.000 28.68896 ? 936  HOH   A O   1 
HETATM 4731 O  O   . HOH   D 4 .   ? 8.83183   -11.06221 60.37565  1.000 26.16631 ? 937  HOH   A O   1 
HETATM 4732 O  O   . HOH   D 4 .   ? 31.72324  2.24240   83.96228  1.000 30.07622 ? 938  HOH   A O   1 
HETATM 4733 O  O   . HOH   D 4 .   ? 12.45524  4.51451   92.88752  1.000 30.43447 ? 939  HOH   A O   1 
HETATM 4734 O  O   . HOH   D 4 .   ? 18.33771  -7.19015  60.69086  1.000 43.68290 ? 940  HOH   A O   1 
HETATM 4735 O  O   . HOH   D 4 .   ? 9.01201   -0.15625  84.23000  1.000 18.30892 ? 941  HOH   A O   1 
HETATM 4736 O  O   . HOH   D 4 .   ? 2.40228   17.55013  63.44065  1.000 26.27600 ? 942  HOH   A O   1 
HETATM 4737 O  O   . HOH   D 4 .   ? -10.03065 0.42849   94.54055  1.000 34.52500 ? 943  HOH   A O   1 
HETATM 4738 O  O   . HOH   D 4 .   ? -11.19704 -5.24929  90.38228  1.000 30.67396 ? 944  HOH   A O   1 
HETATM 4739 O  O   . HOH   D 4 .   ? -9.88491  0.43319   78.94548  1.000 26.90749 ? 945  HOH   A O   1 
HETATM 4740 O  O   . HOH   D 4 .   ? 5.58220   9.35972   61.71467  1.000 22.01608 ? 946  HOH   A O   1 
HETATM 4741 O  O   . HOH   D 4 .   ? -2.11478  4.29158   62.47867  1.000 21.28245 ? 947  HOH   A O   1 
HETATM 4742 O  O   . HOH   D 4 .   ? -8.09419  15.41602  60.10994  1.000 39.30228 ? 948  HOH   A O   1 
HETATM 4743 O  O   . HOH   D 4 .   ? 19.63516  3.72621   36.09699  1.000 46.90709 ? 949  HOH   A O   1 
HETATM 4744 O  O   . HOH   D 4 .   ? -5.01604  4.88243   77.63024  1.000 21.45609 ? 950  HOH   A O   1 
HETATM 4745 O  O   . HOH   D 4 .   ? 30.70241  -4.72572  77.36638  1.000 37.90525 ? 951  HOH   A O   1 
HETATM 4746 O  O   . HOH   D 4 .   ? 3.21684   -2.45917  71.04702  1.000 28.02994 ? 952  HOH   A O   1 
HETATM 4747 O  O   . HOH   D 4 .   ? 4.31234   17.40400  72.05822  1.000 18.44953 ? 953  HOH   A O   1 
HETATM 4748 O  O   . HOH   D 4 .   ? 21.00783  -4.70041  56.39960  1.000 48.29465 ? 954  HOH   A O   1 
HETATM 4749 O  O   . HOH   D 4 .   ? -4.60026  -13.03487 67.01251  1.000 23.23429 ? 955  HOH   A O   1 
HETATM 4750 O  O   . HOH   D 4 .   ? -4.75516  18.20989  61.09761  1.000 22.27098 ? 956  HOH   A O   1 
HETATM 4751 O  O   . HOH   D 4 .   ? 9.94225   -2.24017  86.00124  1.000 27.74504 ? 957  HOH   A O   1 
HETATM 4752 O  O   . HOH   D 4 .   ? 17.22428  21.60226  77.74489  1.000 27.40177 ? 958  HOH   A O   1 
HETATM 4753 O  O   . HOH   D 4 .   ? 6.23085   16.18369  41.56016  1.000 31.85352 ? 959  HOH   A O   1 
HETATM 4754 O  O   . HOH   D 4 .   ? -5.48142  -11.37590 94.18030  1.000 29.57872 ? 960  HOH   A O   1 
HETATM 4755 O  O   . HOH   D 4 .   ? 16.18846  13.12414  95.94647  1.000 40.85865 ? 961  HOH   A O   1 
HETATM 4756 O  O   . HOH   D 4 .   ? 7.18994   24.75807  74.13869  1.000 28.21723 ? 962  HOH   A O   1 
HETATM 4757 O  O   . HOH   D 4 .   ? 11.37925  21.06826  62.40174  1.000 42.76347 ? 963  HOH   A O   1 
HETATM 4758 O  O   . HOH   D 4 .   ? 18.39238  11.75847  50.28592  1.000 41.92311 ? 964  HOH   A O   1 
HETATM 4759 O  O   . HOH   D 4 .   ? 18.92473  3.33452   90.24451  1.000 18.67441 ? 965  HOH   A O   1 
HETATM 4760 O  O   . HOH   D 4 .   ? 4.59133   -1.10317  49.07130  1.000 28.54776 ? 966  HOH   A O   1 
HETATM 4761 O  O   . HOH   D 4 .   ? -4.24992  15.67147  57.74776  1.000 23.15719 ? 967  HOH   A O   1 
HETATM 4762 O  O   . HOH   D 4 .   ? 4.48031   5.96056   64.46016  1.000 38.95036 ? 968  HOH   A O   1 
HETATM 4763 O  O   . HOH   D 4 .   ? 7.58374   0.28682   92.13150  1.000 35.37487 ? 969  HOH   A O   1 
HETATM 4764 O  O   . HOH   D 4 .   ? -11.91584 3.74143   66.40851  1.000 39.49722 ? 970  HOH   A O   1 
HETATM 4765 O  O   . HOH   D 4 .   ? -5.53512  -11.32295 68.82257  1.000 30.71229 ? 971  HOH   A O   1 
HETATM 4766 O  O   . HOH   D 4 .   ? 3.67298   4.75182   53.01477  1.000 21.93207 ? 972  HOH   A O   1 
HETATM 4767 O  O   . HOH   D 4 .   ? 4.22590   8.26594   65.48303  1.000 26.10488 ? 973  HOH   A O   1 
HETATM 4768 O  O   . HOH   D 4 .   ? -10.49518 10.21482  61.73211  1.000 25.91804 ? 974  HOH   A O   1 
HETATM 4769 O  O   . HOH   D 4 .   ? 11.62075  10.89094  65.47674  1.000 21.24705 ? 975  HOH   A O   1 
HETATM 4770 O  O   . HOH   D 4 .   ? 13.91439  -5.33236  69.61838  1.000 32.40664 ? 976  HOH   A O   1 
HETATM 4771 O  O   . HOH   D 4 .   ? -3.96573  6.24960   62.34657  1.000 27.28870 ? 977  HOH   A O   1 
HETATM 4772 O  O   . HOH   D 4 .   ? -10.24858 -16.43619 71.37362  1.000 30.94250 ? 978  HOH   A O   1 
HETATM 4773 O  O   . HOH   D 4 .   ? -1.32390  -19.21606 83.05786  1.000 41.37801 ? 979  HOH   A O   1 
HETATM 4774 O  O   . HOH   D 4 .   ? 1.79969   18.24309  46.49225  1.000 42.09117 ? 980  HOH   A O   1 
HETATM 4775 O  O   . HOH   D 4 .   ? 1.62995   -8.43279  61.23585  1.000 36.96609 ? 981  HOH   A O   1 
HETATM 4776 O  O   . HOH   D 4 .   ? 16.98959  7.71840   63.94972  1.000 29.85736 ? 982  HOH   A O   1 
HETATM 4777 O  O   . HOH   D 4 .   ? 12.03221  -11.83144 70.12279  1.000 23.48997 ? 983  HOH   A O   1 
HETATM 4778 O  O   . HOH   D 4 .   ? 7.59507   3.25251   80.84516  1.000 17.53548 ? 984  HOH   A O   1 
HETATM 4779 O  O   . HOH   D 4 .   ? 0.59642   -22.12304 64.04865  1.000 39.17679 ? 985  HOH   A O   1 
HETATM 4780 O  O   . HOH   D 4 .   ? -6.39228  -19.12697 85.17765  1.000 33.21252 ? 986  HOH   A O   1 
HETATM 4781 O  O   . HOH   D 4 .   ? -0.48224  1.97902   98.83709  1.000 44.22850 ? 987  HOH   A O   1 
HETATM 4782 O  O   . HOH   D 4 .   ? 30.65101  3.84820   92.93030  1.000 24.83703 ? 988  HOH   A O   1 
HETATM 4783 O  O   . HOH   D 4 .   ? -16.36450 -0.56927  78.75114  1.000 23.24935 ? 989  HOH   A O   1 
HETATM 4784 O  O   . HOH   D 4 .   ? -0.45185  8.34645   66.56190  1.000 34.48399 ? 990  HOH   A O   1 
HETATM 4785 O  O   . HOH   D 4 .   ? 2.82897   -18.98696 61.90379  1.000 39.26940 ? 991  HOH   A O   1 
HETATM 4786 O  O   . HOH   D 4 .   ? 17.34901  -9.72827  55.73989  1.000 35.77248 ? 992  HOH   A O   1 
HETATM 4787 O  O   . HOH   D 4 .   ? 32.46167  5.68080   71.54199  1.000 22.52857 ? 993  HOH   A O   1 
HETATM 4788 O  O   . HOH   D 4 .   ? -2.97944  11.18321  81.24220  1.000 39.79274 ? 994  HOH   A O   1 
HETATM 4789 O  O   . HOH   D 4 .   ? 13.03151  7.34008   93.92384  1.000 39.64359 ? 995  HOH   A O   1 
HETATM 4790 O  O   . HOH   D 4 .   ? 0.09499   6.18030   73.73443  1.000 22.25439 ? 996  HOH   A O   1 
HETATM 4791 O  O   . HOH   D 4 .   ? 10.86218  -5.59810  61.90783  1.000 21.26537 ? 997  HOH   A O   1 
HETATM 4792 O  O   . HOH   D 4 .   ? -16.62054 -2.13633  74.98832  1.000 25.52864 ? 998  HOH   A O   1 
HETATM 4793 O  O   . HOH   D 4 .   ? 23.41975  17.62533  65.35315  1.000 31.51378 ? 999  HOH   A O   1 
HETATM 4794 O  O   . HOH   D 4 .   ? 13.88233  -0.26551  70.47225  1.000 28.02782 ? 1000 HOH   A O   1 
HETATM 4795 O  O   . HOH   D 4 .   ? -7.65223  -4.66942  70.10873  1.000 22.17923 ? 1001 HOH   A O   1 
HETATM 4796 O  O   . HOH   D 4 .   ? 2.46620   9.42762   85.04038  1.000 39.24968 ? 1002 HOH   A O   1 
HETATM 4797 O  O   . HOH   D 4 .   ? 26.47786  14.64427  100.91827 1.000 26.89390 ? 1003 HOH   A O   1 
HETATM 4798 O  O   . HOH   D 4 .   ? 25.13710  7.96256   64.60627  1.000 39.09862 ? 1004 HOH   A O   1 
HETATM 4799 O  O   . HOH   D 4 .   ? -3.94193  -18.23141 63.57859  1.000 45.73513 ? 1005 HOH   A O   1 
HETATM 4800 O  O   . HOH   D 4 .   ? -12.50337 -10.96849 90.00642  1.000 30.18199 ? 1006 HOH   A O   1 
HETATM 4801 O  O   . HOH   D 4 .   ? -0.87857  -2.18655  71.56986  1.000 27.33515 ? 1007 HOH   A O   1 
HETATM 4802 O  O   . HOH   D 4 .   ? 34.54569  12.43524  81.49832  1.000 34.62490 ? 1008 HOH   A O   1 
HETATM 4803 O  O   . HOH   D 4 .   ? -11.60721 -2.97224  70.99667  1.000 31.84854 ? 1009 HOH   A O   1 
HETATM 4804 O  O   . HOH   D 4 .   ? -1.58134  -17.71690 85.44878  1.000 25.98991 ? 1010 HOH   A O   1 
HETATM 4805 O  O   . HOH   D 4 .   ? -3.78136  10.63280  38.56657  1.000 33.98010 ? 1011 HOH   A O   1 
HETATM 4806 O  O   . HOH   D 4 .   ? -4.20544  12.94714  40.33655  1.000 32.46890 ? 1012 HOH   A O   1 
HETATM 4807 O  O   . HOH   D 4 .   ? 24.70941  -0.04179  65.50365  1.000 46.66983 ? 1013 HOH   A O   1 
HETATM 4808 O  O   . HOH   D 4 .   ? 4.63143   10.51916  72.28865  1.000 17.24828 ? 1014 HOH   A O   1 
HETATM 4809 O  O   . HOH   D 4 .   ? -15.93571 -7.03544  80.25035  1.000 23.41386 ? 1015 HOH   A O   1 
HETATM 4810 O  O   . HOH   D 4 .   ? 11.47355  20.07469  53.94893  1.000 33.16207 ? 1016 HOH   A O   1 
HETATM 4811 O  O   . HOH   D 4 .   ? 4.27649   -10.24490 73.99779  1.000 22.93458 ? 1017 HOH   A O   1 
HETATM 4812 O  O   . HOH   D 4 .   ? -0.13388  -1.25586  81.56034  1.000 26.36046 ? 1018 HOH   A O   1 
HETATM 4813 O  O   . HOH   D 4 .   ? 27.10647  -2.43677  84.01972  1.000 38.16054 ? 1019 HOH   A O   1 
HETATM 4814 O  O   . HOH   D 4 .   ? 1.74780   -3.46396  95.61675  1.000 42.61304 ? 1020 HOH   A O   1 
HETATM 4815 O  O   . HOH   D 4 .   ? -9.87890  5.46553   88.15744  1.000 32.89981 ? 1021 HOH   A O   1 
HETATM 4816 O  O   . HOH   D 4 .   ? 8.83766   18.87823  50.06778  1.000 35.97400 ? 1022 HOH   A O   1 
HETATM 4817 O  O   . HOH   D 4 .   ? -1.46463  7.60210   68.86431  1.000 32.63499 ? 1023 HOH   A O   1 
HETATM 4818 O  O   . HOH   D 4 .   ? 3.78656   0.96767   31.80202  1.000 36.09417 ? 1024 HOH   A O   1 
HETATM 4819 O  O   . HOH   D 4 .   ? 14.31987  -9.36932  69.85447  1.000 37.25287 ? 1025 HOH   A O   1 
HETATM 4820 O  O   . HOH   D 4 .   ? 7.72125   -16.94441 83.78223  1.000 40.05998 ? 1026 HOH   A O   1 
HETATM 4821 O  O   . HOH   D 4 .   ? 4.98740   11.10640  27.37784  1.000 42.96745 ? 1027 HOH   A O   1 
HETATM 4822 O  O   . HOH   D 4 .   ? -7.95602  7.20007   67.53342  1.000 26.96762 ? 1028 HOH   A O   1 
HETATM 4823 O  O   . HOH   D 4 .   ? 19.98462  -7.06187  83.82405  1.000 21.34054 ? 1029 HOH   A O   1 
HETATM 4824 O  O   . HOH   D 4 .   ? 17.47446  23.66436  67.29451  1.000 46.31031 ? 1030 HOH   A O   1 
HETATM 4825 O  O   . HOH   D 4 .   ? -0.59153  17.78576  64.56731  1.000 29.50013 ? 1031 HOH   A O   1 
HETATM 4826 O  O   . HOH   D 4 .   ? -15.27358 0.90979   60.25259  1.000 32.21997 ? 1032 HOH   A O   1 
HETATM 4827 O  O   . HOH   D 4 .   ? -2.41918  3.34100   68.61923  1.000 36.29085 ? 1033 HOH   A O   1 
HETATM 4828 O  O   . HOH   D 4 .   ? -7.72804  -5.90868  58.57802  1.000 36.88971 ? 1034 HOH   A O   1 
HETATM 4829 O  O   . HOH   D 4 .   ? -22.16396 -6.82091  76.45378  1.000 41.69008 ? 1035 HOH   A O   1 
HETATM 4830 O  O   . HOH   D 4 .   ? 30.91470  5.80836   64.45400  1.000 31.81350 ? 1036 HOH   A O   1 
HETATM 4831 O  O   . HOH   D 4 .   ? 26.00814  -3.67512  69.80540  1.000 44.84887 ? 1037 HOH   A O   1 
HETATM 4832 O  O   . HOH   D 4 .   ? 33.37415  17.06141  76.54837  1.000 43.05532 ? 1038 HOH   A O   1 
HETATM 4833 O  O   . HOH   D 4 .   ? -5.13986  -1.33635  98.56734  1.000 40.54092 ? 1039 HOH   A O   1 
HETATM 4834 O  O   . HOH   D 4 .   ? 0.87119   11.07602  96.12523  1.000 44.36651 ? 1040 HOH   A O   1 
HETATM 4835 O  O   . HOH   D 4 .   ? 15.17177  -5.84887  87.36851  1.000 28.10551 ? 1041 HOH   A O   1 
HETATM 4836 O  O   . HOH   D 4 .   ? -9.94654  12.55454  52.86790  1.000 29.97464 ? 1042 HOH   A O   1 
HETATM 4837 O  O   . HOH   D 4 .   ? 4.10764   4.22371   71.25032  1.000 24.13400 ? 1043 HOH   A O   1 
HETATM 4838 O  O   . HOH   D 4 .   ? -0.54604  -2.01349  79.13256  1.000 24.84086 ? 1044 HOH   A O   1 
HETATM 4839 O  O   . HOH   D 4 .   ? -3.68174  -10.54489 92.26939  1.000 34.48023 ? 1045 HOH   A O   1 
HETATM 4840 O  O   . HOH   D 4 .   ? 8.02885   14.27188  89.85074  1.000 46.69123 ? 1046 HOH   A O   1 
HETATM 4841 O  O   . HOH   D 4 .   ? 19.15741  -8.03380  86.57821  1.000 26.40470 ? 1047 HOH   A O   1 
HETATM 4842 O  O   . HOH   D 4 .   ? 15.70046  22.47843  46.75370  1.000 50.66430 ? 1048 HOH   A O   1 
HETATM 4843 O  O   . HOH   D 4 .   ? -10.56346 -7.51600  63.77845  1.000 47.94698 ? 1049 HOH   A O   1 
HETATM 4844 O  O   . HOH   D 4 .   ? -0.94622  -18.30141 69.77830  1.000 28.01942 ? 1050 HOH   A O   1 
HETATM 4845 O  O   . HOH   D 4 .   ? 0.12720   -4.11824  73.40530  1.000 25.44776 ? 1051 HOH   A O   1 
HETATM 4846 O  O   . HOH   D 4 .   ? 2.89102   -10.14968 67.66691  1.000 20.99852 ? 1052 HOH   A O   1 
HETATM 4847 O  O   . HOH   D 4 .   ? 18.50679  -16.92561 71.11786  1.000 49.22497 ? 1053 HOH   A O   1 
HETATM 4848 O  O   . HOH   D 4 .   ? 17.63503  5.36241   62.49319  1.000 28.96924 ? 1054 HOH   A O   1 
HETATM 4849 O  O   . HOH   D 4 .   ? -0.20723  -16.78580 87.72042  1.000 28.28023 ? 1055 HOH   A O   1 
HETATM 4850 O  O   . HOH   D 4 .   ? -8.21526  0.75161   70.22267  1.000 46.94856 ? 1056 HOH   A O   1 
HETATM 4851 O  O   . HOH   D 4 .   ? 5.77871   24.22175  71.79001  1.000 22.32060 ? 1057 HOH   A O   1 
HETATM 4852 O  O   . HOH   D 4 .   ? 5.25590   -1.46755  65.90627  1.000 41.38891 ? 1058 HOH   A O   1 
HETATM 4853 O  O   . HOH   D 4 .   ? 5.37456   2.56134   82.71646  1.000 23.67229 ? 1059 HOH   A O   1 
HETATM 4854 O  O   . HOH   D 4 .   ? 24.70063  -2.55816  85.02957  1.000 26.65594 ? 1060 HOH   A O   1 
HETATM 4855 O  O   . HOH   D 4 .   ? 36.24739  3.51620   80.06908  1.000 33.39375 ? 1061 HOH   A O   1 
HETATM 4856 O  O   . HOH   D 4 .   ? 31.80038  10.58212  95.08843  1.000 25.37005 ? 1062 HOH   A O   1 
HETATM 4857 O  O   . HOH   D 4 .   ? 6.41487   -9.98352  88.54949  1.000 28.18207 ? 1063 HOH   A O   1 
HETATM 4858 O  O   . HOH   D 4 .   ? 27.50590  16.45625  70.58044  1.000 46.11073 ? 1064 HOH   A O   1 
HETATM 4859 O  O   . HOH   D 4 .   ? 3.38739   3.91400   65.93744  1.000 40.79545 ? 1065 HOH   A O   1 
HETATM 4860 O  O   . HOH   D 4 .   ? 19.90150  18.98897  60.47090  1.000 35.82047 ? 1066 HOH   A O   1 
HETATM 4861 O  O   . HOH   D 4 .   ? 9.13376   -17.46214 59.24336  1.000 34.45081 ? 1067 HOH   A O   1 
HETATM 4862 O  O   . HOH   D 4 .   ? -4.30564  25.00065  58.06865  1.000 38.35266 ? 1068 HOH   A O   1 
HETATM 4863 O  O   . HOH   D 4 .   ? -6.21298  9.08259   76.04238  1.000 44.87264 ? 1069 HOH   A O   1 
HETATM 4864 O  O   . HOH   D 4 .   ? 2.79476   -20.04983 77.00480  1.000 30.43329 ? 1070 HOH   A O   1 
HETATM 4865 O  O   . HOH   D 4 .   ? 2.48180   -24.23368 65.76227  1.000 51.04203 ? 1071 HOH   A O   1 
HETATM 4866 O  O   . HOH   D 4 .   ? -15.20977 -15.15551 86.57402  1.000 44.32398 ? 1072 HOH   A O   1 
HETATM 4867 O  O   . HOH   D 4 .   ? -8.15933  -1.94116  70.82169  1.000 33.43425 ? 1073 HOH   A O   1 
HETATM 4868 O  O   . HOH   D 4 .   ? -9.53148  -5.84510  68.44724  1.000 23.77882 ? 1074 HOH   A O   1 
HETATM 4869 O  O   . HOH   D 4 .   ? -13.07848 -8.34480  88.27493  1.000 46.47316 ? 1075 HOH   A O   1 
HETATM 4870 O  O   . HOH   D 4 .   ? 12.30005  -2.56291  86.98723  1.000 26.62626 ? 1076 HOH   A O   1 
HETATM 4871 O  O   . HOH   D 4 .   ? -0.34004  -8.30548  64.33851  1.000 30.18642 ? 1077 HOH   A O   1 
HETATM 4872 O  O   . HOH   D 4 .   ? 7.59041   21.10354  81.70713  1.000 31.60393 ? 1078 HOH   A O   1 
HETATM 4873 O  O   . HOH   D 4 .   ? 18.94986  -3.51993  33.61288  1.000 48.47143 ? 1079 HOH   A O   1 
HETATM 4874 O  O   . HOH   D 4 .   ? 2.84973   -3.70794  73.44383  1.000 28.01449 ? 1080 HOH   A O   1 
HETATM 4875 O  O   . HOH   D 4 .   ? 25.44623  6.41872   59.98484  1.000 53.81942 ? 1081 HOH   A O   1 
HETATM 4876 O  O   . HOH   D 4 .   ? -22.56622 -9.23852  76.86832  1.000 45.25274 ? 1082 HOH   A O   1 
HETATM 4877 O  O   . HOH   D 4 .   ? 6.62372   24.31825  61.84460  1.000 44.41509 ? 1083 HOH   A O   1 
HETATM 4878 O  O   . HOH   D 4 .   ? -4.98165  13.86944  62.39360  1.000 29.65855 ? 1084 HOH   A O   1 
HETATM 4879 O  O   . HOH   D 4 .   ? 22.49112  18.13485  58.19933  1.000 36.53325 ? 1085 HOH   A O   1 
HETATM 4880 O  O   . HOH   D 4 .   ? -7.19918  6.68255   77.32989  1.000 40.76485 ? 1086 HOH   A O   1 
HETATM 4881 O  O   . HOH   D 4 .   ? 0.55407   13.55635  80.86826  1.000 33.97762 ? 1087 HOH   A O   1 
HETATM 4882 O  O   . HOH   D 4 .   ? -14.86103 -5.29545  87.63482  1.000 40.04709 ? 1088 HOH   A O   1 
HETATM 4883 O  O   . HOH   D 4 .   ? -1.23143  18.09695  68.68854  1.000 31.03785 ? 1089 HOH   A O   1 
HETATM 4884 O  O   . HOH   D 4 .   ? -11.57016 0.67651   75.58734  1.000 54.57882 ? 1090 HOH   A O   1 
HETATM 4885 O  O   . HOH   D 4 .   ? -2.90126  -15.85319 64.72499  1.000 32.41033 ? 1091 HOH   A O   1 
HETATM 4886 O  O   . HOH   D 4 .   ? 21.35887  17.47914  61.76369  1.000 34.44913 ? 1092 HOH   A O   1 
HETATM 4887 O  O   . HOH   D 4 .   ? 6.09595   -1.69474  93.91487  1.000 41.61456 ? 1093 HOH   A O   1 
HETATM 4888 O  O   . HOH   D 4 .   ? -10.91869 -3.46412  68.31402  1.000 23.79591 ? 1094 HOH   A O   1 
HETATM 4889 O  O   . HOH   D 4 .   ? -12.93655 -0.17540  66.88550  1.000 42.74334 ? 1095 HOH   A O   1 
HETATM 4890 O  O   . HOH   D 4 .   ? -2.24347  3.02421   73.68500  1.000 52.10336 ? 1096 HOH   A O   1 
HETATM 4891 O  O   . HOH   D 4 .   ? 31.98117  16.32031  71.64791  1.000 45.04151 ? 1097 HOH   A O   1 
HETATM 4892 O  O   . HOH   D 4 .   ? 14.04763  -8.16308  65.05674  1.000 10.67062 ? 1098 HOH   A O   1 
HETATM 4893 O  O   . HOH   D 4 .   ? 21.79683  5.49659   52.32636  1.000 34.27763 ? 1099 HOH   A O   1 
HETATM 4894 O  O   . HOH   D 4 .   ? 22.28273  -2.28569  71.97168  1.000 25.08401 ? 1100 HOH   A O   1 
HETATM 4895 O  O   . HOH   D 4 .   ? -5.42419  2.20376   77.49857  1.000 22.26144 ? 1101 HOH   A O   1 
HETATM 4896 O  O   . HOH   D 4 .   ? 7.80027   22.28831  45.83788  1.000 51.41089 ? 1102 HOH   A O   1 
HETATM 4897 O  O   . HOH   D 4 .   ? 33.04530  3.19466   86.10234  1.000 35.00922 ? 1103 HOH   A O   1 
HETATM 4898 O  O   . HOH   D 4 .   ? 16.86683  21.50111  82.26457  1.000 43.27737 ? 1104 HOH   A O   1 
HETATM 4899 O  O   . HOH   D 4 .   ? -2.80121  -23.02787 65.74161  1.000 50.00212 ? 1105 HOH   A O   1 
HETATM 4900 O  O   . HOH   D 4 .   ? -2.35612  1.91667   71.27680  1.000 34.98258 ? 1106 HOH   A O   1 
HETATM 4901 O  O   . HOH   D 4 .   ? 35.93820  4.91543   73.91210  1.000 34.41309 ? 1107 HOH   A O   1 
HETATM 4902 O  O   . HOH   D 4 .   ? 21.91387  17.99662  87.42522  1.000 43.33290 ? 1108 HOH   A O   1 
HETATM 4903 O  O   . HOH   D 4 .   ? -14.38933 4.03278   51.77135  1.000 49.49698 ? 1109 HOH   A O   1 
HETATM 4904 O  O   . HOH   D 4 .   ? -20.48834 4.04903   37.83138  1.000 57.61284 ? 1110 HOH   A O   1 
HETATM 4905 O  O   . HOH   D 4 .   ? 7.91438   10.82616  88.55204  1.000 29.06291 ? 1111 HOH   A O   1 
HETATM 4906 O  O   . HOH   D 4 .   ? -1.27411  12.89875  69.32173  1.000 24.60828 ? 1112 HOH   A O   1 
HETATM 4907 O  O   . HOH   D 4 .   ? 19.62429  -1.65915  31.15184  1.000 53.12272 ? 1113 HOH   A O   1 
HETATM 4908 O  O   . HOH   D 4 .   ? 22.57065  20.21534  70.99476  1.000 53.08472 ? 1114 HOH   A O   1 
HETATM 4909 O  O   . HOH   D 4 .   ? -3.98401  5.46131   75.08864  1.000 39.78391 ? 1115 HOH   A O   1 
HETATM 4910 O  O   . HOH   D 4 .   ? 31.30778  -0.36340  68.55369  1.000 44.11832 ? 1116 HOH   A O   1 
HETATM 4911 O  O   . HOH   D 4 .   ? 1.64825   10.75434  82.58981  1.000 41.97676 ? 1117 HOH   A O   1 
HETATM 4912 O  O   . HOH   D 4 .   ? 4.12360   -10.90617 61.26000  1.000 29.11542 ? 1118 HOH   A O   1 
HETATM 4913 O  O   . HOH   D 4 .   ? -10.22658 -0.51549  71.99719  1.000 47.96785 ? 1119 HOH   A O   1 
HETATM 4914 O  O   . HOH   D 4 .   ? -3.40954  15.35325  63.57992  1.000 41.12027 ? 1120 HOH   A O   1 
HETATM 4915 O  O   . HOH   D 4 .   ? 9.90284   -5.36541  85.58220  1.000 29.61713 ? 1121 HOH   A O   1 
HETATM 4916 O  O   . HOH   D 4 .   ? 2.50649   4.53578   96.76926  1.000 44.90881 ? 1122 HOH   A O   1 
HETATM 4917 O  O   . HOH   D 4 .   ? 12.43801  -22.81609 65.74983  1.000 42.91261 ? 1123 HOH   A O   1 
HETATM 4918 O  O   . HOH   D 4 .   ? 5.69536   -17.37902 61.62250  1.000 46.89307 ? 1124 HOH   A O   1 
HETATM 4919 O  O   . HOH   D 4 .   ? 9.56792   10.80559  26.86638  1.000 51.09669 ? 1125 HOH   A O   1 
HETATM 4920 O  O   . HOH   D 4 .   ? 12.19556  18.62650  90.76517  1.000 54.42912 ? 1126 HOH   A O   1 
HETATM 4921 O  O   . HOH   D 4 .   ? -0.29307  -7.07573  59.84889  1.000 38.25227 ? 1127 HOH   A O   1 
HETATM 4922 O  O   . HOH   D 4 .   ? 12.21333  -15.11625 52.37983  1.000 44.17041 ? 1128 HOH   A O   1 
HETATM 4923 O  O   . HOH   D 4 .   ? 23.03875  11.09143  58.99743  1.000 56.43187 ? 1129 HOH   A O   1 
HETATM 4924 O  O   . HOH   D 4 .   ? -11.73288 -5.94224  88.17524  1.000 24.67318 ? 1130 HOH   A O   1 
HETATM 4925 O  O   . HOH   D 4 .   ? 24.80625  -1.05227  63.04313  1.000 37.33751 ? 1131 HOH   A O   1 
HETATM 4926 O  O   . HOH   D 4 .   ? 27.47762  -5.66973  78.77395  1.000 54.44280 ? 1132 HOH   A O   1 
HETATM 4927 O  O   . HOH   D 4 .   ? 14.63366  -10.19381 67.63373  1.000 34.95489 ? 1133 HOH   A O   1 
HETATM 4928 O  O   . HOH   D 4 .   ? 12.05923  -6.26550  84.32000  1.000 25.78423 ? 1134 HOH   A O   1 
HETATM 4929 O  O   . HOH   D 4 .   ? 23.19152  7.67014   61.06597  1.000 40.68181 ? 1135 HOH   A O   1 
HETATM 4930 O  O   . HOH   D 4 .   ? 21.34871  -14.09844 60.43594  1.000 51.52089 ? 1136 HOH   A O   1 
HETATM 4931 O  O   . HOH   D 4 .   ? -12.57068 0.03510   44.15129  1.000 55.23977 ? 1137 HOH   A O   1 
HETATM 4932 O  O   . HOH   D 4 .   ? 25.316    20.585    88.180    1.000 49.69890 ? 1138 HOH   A O   1 
HETATM 4933 O  O   . HOH   D 4 .   ? -16.41100 3.84861   54.95414  1.000 45.73594 ? 1139 HOH   A O   1 
HETATM 4934 O  O   . HOH   D 4 .   ? 21.45408  -2.96732  60.43620  1.000 54.47942 ? 1140 HOH   A O   1 
HETATM 4935 O  O   . HOH   D 4 .   ? 23.55511  -2.74631  89.54875  1.000 30.52031 ? 1141 HOH   A O   1 
HETATM 4936 O  O   . HOH   D 4 .   ? 5.41984   -9.62261  48.31465  1.000 43.52972 ? 1142 HOH   A O   1 
HETATM 4937 O  O   . HOH   D 4 .   ? -12.19219 10.45666  63.78792  1.000 32.69752 ? 1143 HOH   A O   1 
HETATM 4938 O  O   . HOH   D 4 .   ? 11.52730  -6.08152  64.42158  1.000 23.09204 ? 1144 HOH   A O   1 
HETATM 4939 O  O   . HOH   D 4 .   ? -5.21083  -3.79885  98.38712  1.000 38.15141 ? 1145 HOH   A O   1 
HETATM 4940 O  O   . HOH   D 4 .   ? -0.24040  -8.21463  92.10411  1.000 29.15545 ? 1146 HOH   A O   1 
HETATM 4941 O  O   . HOH   D 4 .   ? 3.63753   -2.67886  93.58520  1.000 34.29072 ? 1147 HOH   A O   1 
HETATM 4942 O  O   . HOH   D 4 .   ? 19.01680  -8.98408  82.16992  1.000 25.23636 ? 1148 HOH   A O   1 
HETATM 4943 O  O   . HOH   D 4 .   ? 18.20333  11.15836  95.65567  1.000 36.98521 ? 1149 HOH   A O   1 
HETATM 4944 O  O   . HOH   D 4 .   ? -8.71265  1.19148   74.36662  1.000 44.29493 ? 1150 HOH   A O   1 
HETATM 4945 O  O   . HOH   D 4 .   ? -5.18144  12.45780  78.93995  1.000 45.99696 ? 1151 HOH   A O   1 
HETATM 4946 O  O   . HOH   D 4 .   ? 23.937    20.244    100.814   1.000 31.33393 ? 1152 HOH   A O   1 
HETATM 4947 O  O   . HOH   D 4 .   ? -1.41832  -2.39834  75.25585  1.000 27.15131 ? 1153 HOH   A O   1 
HETATM 4948 O  O   . HOH   D 4 .   ? 8.83770   -11.17726 85.55465  1.000 41.81331 ? 1154 HOH   A O   1 
HETATM 4949 O  O   . HOH   D 4 .   ? -4.23534  1.57640   75.12056  1.000 38.28200 ? 1155 HOH   A O   1 
HETATM 4950 O  O   . HOH   D 4 .   ? 25.00946  -3.61821  87.39426  1.000 32.44591 ? 1156 HOH   A O   1 
HETATM 4951 O  O   . HOH   D 4 .   ? 5.01845   27.27662  66.41829  1.000 28.34065 ? 1157 HOH   A O   1 
HETATM 4952 O  O   . HOH   D 4 .   ? -15.55977 -9.23164  81.76433  1.000 38.13644 ? 1158 HOH   A O   1 
HETATM 4953 O  O   . HOH   D 4 .   ? 12.66948  -12.15936 81.92279  1.000 36.96126 ? 1159 HOH   A O   1 
HETATM 4954 O  O   . HOH   D 4 .   ? 7.27447   27.63230  65.80496  1.000 42.84522 ? 1160 HOH   A O   1 
HETATM 4955 O  O   . HOH   D 4 .   ? 23.21510  9.96347   41.26112  1.000 51.62480 ? 1161 HOH   A O   1 
HETATM 4956 O  O   . HOH   D 4 .   ? -8.08310  1.50635   77.13030  1.000 30.23584 ? 1162 HOH   A O   1 
HETATM 4957 O  O   . HOH   D 4 .   ? 23.59067  -4.21211  83.12363  1.000 35.17438 ? 1163 HOH   A O   1 
HETATM 4958 O  O   . HOH   D 4 .   ? 0.98618   5.01771   66.18171  1.000 46.15827 ? 1164 HOH   A O   1 
HETATM 4959 O  O   . HOH   D 4 .   ? -17.59320 6.49261   55.78610  1.000 43.63057 ? 1165 HOH   A O   1 
HETATM 4960 O  O   . HOH   D 4 .   ? -11.86376 2.47867   88.40610  1.000 53.70810 ? 1166 HOH   A O   1 
HETATM 4961 O  O   . HOH   D 4 .   ? -14.20706 -2.28152  70.38369  1.000 45.03147 ? 1167 HOH   A O   1 
HETATM 4962 O  O   . HOH   D 4 .   ? -2.51368  -8.37887  93.57951  1.000 29.61085 ? 1168 HOH   A O   1 
HETATM 4963 O  O   . HOH   D 4 .   ? 15.44453  1.44118   92.82879  1.000 42.25232 ? 1169 HOH   A O   1 
HETATM 4964 O  O   . HOH   D 4 .   ? -3.55475  11.84237  70.18539  1.000 30.53195 ? 1170 HOH   A O   1 
HETATM 4965 O  O   . HOH   D 4 .   ? -14.50758 1.05340   77.51132  1.000 35.38845 ? 1171 HOH   A O   1 
HETATM 4966 O  O   . HOH   D 4 .   ? 13.20894  -21.13593 67.63942  1.000 31.83888 ? 1172 HOH   A O   1 
HETATM 4967 O  O   . HOH   D 4 .   ? -2.98686  7.15702   73.62849  1.000 44.21887 ? 1173 HOH   A O   1 
HETATM 4968 O  O   . HOH   D 4 .   ? 32.98592  -1.91165  70.41961  1.000 45.74818 ? 1174 HOH   A O   1 
HETATM 4969 O  O   . HOH   D 4 .   ? 10.36783  -12.66932 83.41248  1.000 38.37991 ? 1175 HOH   A O   1 
HETATM 4970 O  O   . HOH   D 4 .   ? -5.55562  15.55386  60.27976  1.000 26.31478 ? 1176 HOH   A O   1 
HETATM 4971 O  O   . HOH   D 4 .   ? -8.60464  11.62355  65.70535  1.000 41.98230 ? 1177 HOH   A O   1 
HETATM 4972 O  O   . HOH   D 4 .   ? 1.94864   -11.49065 93.20753  1.000 43.63043 ? 1178 HOH   A O   1 
HETATM 4973 O  O   . HOH   D 4 .   ? -5.42361  -14.38233 64.95414  1.000 54.74895 ? 1179 HOH   A O   1 
HETATM 4974 O  O   . HOH   D 4 .   ? 12.86255  -8.89776  85.07919  1.000 27.02821 ? 1180 HOH   A O   1 
HETATM 4975 O  O   . HOH   D 4 .   ? 28.80543  16.59580  73.05271  1.000 47.77421 ? 1181 HOH   A O   1 
HETATM 4976 O  O   . HOH   D 4 .   ? -9.77512  -18.50665 69.89329  1.000 42.16359 ? 1182 HOH   A O   1 
HETATM 4977 O  O   . HOH   D 4 .   ? 26.180    18.773    89.743    1.000 32.71083 ? 1183 HOH   A O   1 
HETATM 4978 O  O   . HOH   D 4 .   ? 16.97885  -10.46100 83.34939  1.000 28.15582 ? 1184 HOH   A O   1 
HETATM 4979 O  O   . HOH   D 4 .   ? 7.88080   21.61670  55.76163  1.000 35.14440 ? 1185 HOH   A O   1 
HETATM 4980 O  O   . HOH   D 4 .   ? 29.22227  0.95066   89.69085  1.000 29.94648 ? 1186 HOH   A O   1 
HETATM 4981 O  O   . HOH   D 4 .   ? 26.38667  -4.88983  74.33166  1.000 41.92114 ? 1187 HOH   A O   1 
HETATM 4982 O  O   . HOH   D 4 .   ? 28.80820  18.93777  82.31476  1.000 49.61689 ? 1188 HOH   A O   1 
HETATM 4983 O  O   . HOH   D 4 .   ? 7.46828   11.29333  25.73726  1.000 49.61587 ? 1189 HOH   A O   1 
HETATM 4984 O  O   . HOH   D 4 .   ? 14.98668  8.21938   95.24859  1.000 40.18941 ? 1190 HOH   A O   1 
HETATM 4985 O  O   . HOH   D 4 .   ? 30.84701  3.06763   95.54816  1.000 30.09305 ? 1191 HOH   A O   1 
HETATM 4986 O  O   . HOH   D 4 .   ? 18.65620  -10.99399 42.96358  1.000 52.22597 ? 1192 HOH   A O   1 
HETATM 4987 O  O   . HOH   D 4 .   ? 7.90978   22.50236  57.85979  1.000 34.22708 ? 1193 HOH   A O   1 
HETATM 4988 O  O   . HOH   D 4 .   ? 0.10116   -5.52438  95.35248  1.000 36.18857 ? 1194 HOH   A O   1 
HETATM 4989 O  O   . HOH   D 4 .   ? 12.58321  -17.17959 74.30805  1.000 41.23080 ? 1195 HOH   A O   1 
HETATM 4990 O  O   . HOH   D 4 .   ? 2.64303   27.92446  63.04702  1.000 37.06490 ? 1196 HOH   A O   1 
HETATM 4991 O  O   . HOH   D 4 .   ? 10.48053  23.63834  58.62442  1.000 42.02536 ? 1197 HOH   A O   1 
HETATM 4992 O  O   . HOH   D 4 .   ? -11.84339 1.74982   78.33178  1.000 37.39678 ? 1198 HOH   A O   1 
HETATM 4993 O  O   . HOH   D 4 .   ? -13.24302 -13.83098 72.13459  1.000 36.09639 ? 1199 HOH   A O   1 
HETATM 4994 O  O   . HOH   D 4 .   ? -0.70039  11.20482  79.95300  1.000 28.73960 ? 1200 HOH   A O   1 
HETATM 4995 O  O   . HOH   D 4 .   ? 6.15217   25.03182  58.20610  1.000 50.25412 ? 1201 HOH   A O   1 
HETATM 4996 O  O   . HOH   D 4 .   ? -3.11179  12.07311  76.12189  1.000 37.68167 ? 1202 HOH   A O   1 
HETATM 4997 O  O   . HOH   D 4 .   ? -1.88122  15.59293  68.27379  1.000 30.10256 ? 1203 HOH   A O   1 
HETATM 4998 O  O   . HOH   D 4 .   ? 14.84708  -8.69672  86.95273  1.000 29.27913 ? 1204 HOH   A O   1 
HETATM 4999 O  O   . HOH   D 4 .   ? -4.08759  -17.70041 86.44086  1.000 30.80898 ? 1205 HOH   A O   1 
HETATM 5000 O  O   . HOH   D 4 .   ? 32.80721  -0.87960  66.15572  1.000 39.30069 ? 1206 HOH   A O   1 
HETATM 5001 O  O   . HOH   D 4 .   ? 32.85261  5.52075   92.08305  1.000 35.74003 ? 1207 HOH   A O   1 
HETATM 5002 O  O   . HOH   D 4 .   ? 8.91371   -20.47314 73.81063  1.000 50.95729 ? 1208 HOH   A O   1 
HETATM 5003 O  O   . HOH   D 4 .   ? -0.17367  4.99748   69.16840  1.000 35.25409 ? 1209 HOH   A O   1 
HETATM 5004 O  O   . HOH   D 4 .   ? 1.71572   -6.93285  93.47383  1.000 28.41957 ? 1210 HOH   A O   1 
HETATM 5005 O  O   . HOH   D 4 .   ? 4.91069   8.06422   24.40290  1.000 53.55567 ? 1211 HOH   A O   1 
HETATM 5006 O  O   . HOH   D 4 .   ? 22.65995  -6.61218  83.54854  1.000 28.46645 ? 1212 HOH   A O   1 
HETATM 5007 O  O   . HOH   D 4 .   ? 17.25188  -9.84166  86.14736  1.000 26.62760 ? 1213 HOH   A O   1 
HETATM 5008 O  O   . HOH   D 4 .   ? 3.87734   8.76436   26.67732  1.000 53.07243 ? 1214 HOH   A O   1 
HETATM 5009 O  O   . HOH   D 4 .   ? -2.48403  -21.27711 83.74481  1.000 46.25376 ? 1215 HOH   A O   1 
HETATM 5010 O  O   . HOH   D 4 .   ? -5.854    -29.329   76.821    1.000 40.15819 ? 1216 HOH   A O   1 
HETATM 5011 O  O   . HOH   D 4 .   ? 1.03102   -0.46282  72.63814  1.000 32.51261 ? 1217 HOH   A O   1 
HETATM 5012 O  O   . HOH   D 4 .   ? 10.04180  4.20607   93.45297  1.000 37.14934 ? 1218 HOH   A O   1 
HETATM 5013 O  O   . HOH   D 4 .   ? 34.17183  4.67733   89.91229  1.000 34.68536 ? 1219 HOH   A O   1 
HETATM 5014 O  O   . HOH   D 4 .   ? 0.02270   2.01692   72.17796  1.000 41.32939 ? 1220 HOH   A O   1 
HETATM 5015 O  O   . HOH   D 4 .   ? 27.48632  -1.19113  90.32162  1.000 27.90915 ? 1221 HOH   A O   1 
HETATM 5016 O  O   . HOH   D 4 .   ? 19.00710  -4.30387  64.07872  1.000 32.55762 ? 1222 HOH   A O   1 
HETATM 5017 O  O   . HOH   D 4 .   ? 20.92794  -9.70655  80.38272  1.000 34.37947 ? 1223 HOH   A O   1 
HETATM 5018 O  O   . HOH   D 4 .   ? 24.61656  -6.12406  87.74880  1.000 42.23120 ? 1224 HOH   A O   1 
HETATM 5019 O  O   . HOH   D 4 .   ? 18.80562  -6.77074  63.44544  1.000 45.82234 ? 1225 HOH   A O   1 
HETATM 5020 O  O   . HOH   D 4 .   ? 30.95522  1.54995   91.47719  1.000 28.99681 ? 1226 HOH   A O   1 
HETATM 5021 O  O   . HOH   D 4 .   ? 1.32131   4.39449   71.27927  1.000 31.30359 ? 1227 HOH   A O   1 
HETATM 5022 O  O   . HOH   D 4 .   ? -11.17583 11.04085  65.95315  1.000 42.94289 ? 1228 HOH   A O   1 
HETATM 5023 O  O   . HOH   D 4 .   ? 27.45015  -2.90363  88.25523  1.000 38.54046 ? 1229 HOH   A O   1 
HETATM 5024 O  O   . HOH   D 4 .   ? -2.32507  -9.03377  59.01076  1.000 46.94803 ? 1230 HOH   A O   1 
HETATM 5025 O  O   . HOH   D 4 .   ? 24.10608  -7.91325  85.79789  1.000 43.30594 ? 1231 HOH   A O   1 
HETATM 5026 O  O   . HOH   D 4 .   ? 30.66970  0.40354   95.94988  1.000 38.24952 ? 1232 HOH   A O   1 
HETATM 5027 O  O   . HOH   D 4 .   ? 33.30406  1.79818   90.26859  1.000 38.81654 ? 1233 HOH   A O   1 
HETATM 5028 O  O   . HOH   D 4 .   ? 31.02196  -0.78228  93.27651  1.000 42.73356 ? 1234 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   . SER A 8   ? 1.06667 0.63134 0.85988 0.06338  0.00646  -0.06727 8   SER A N   
2    C CA  . SER A 8   ? 1.20000 0.75651 0.97561 0.05916  0.00735  -0.07839 8   SER A CA  
3    C C   . SER A 8   ? 1.27677 0.85190 1.05465 0.04494  -0.00264 -0.08213 8   SER A C   
4    O O   . SER A 8   ? 1.12568 0.72207 0.90582 0.04998  -0.00100 -0.08407 8   SER A O   
5    C CB  . SER A 8   ? 1.21603 0.74180 0.97429 0.04975  0.00797  -0.08433 8   SER A CB  
6    O OG  . SER A 8   ? 1.39658 0.91589 1.16006 0.03375  0.00042  -0.08100 8   SER A OG  
7    N N   . GLU A 9   ? 1.15093 0.72560 0.93274 0.02637  -0.01277 -0.08146 9   GLU A N   
8    C CA  . GLU A 9   ? 0.90566 0.50769 0.69722 0.01211  -0.02323 -0.08198 9   GLU A CA  
9    C C   . GLU A 9   ? 0.87102 0.51163 0.69245 0.01198  -0.02693 -0.07090 9   GLU A C   
10   O O   . GLU A 9   ? 0.93510 0.60354 0.76706 0.00634  -0.03287 -0.06999 9   GLU A O   
11   C CB  . GLU A 9   ? 0.85583 0.43912 0.63650 -0.00853 -0.03264 -0.08761 9   GLU A CB  
12   C CG  . GLU A 9   ? 0.96828 0.52936 0.72653 -0.01184 -0.02974 -0.09717 9   GLU A CG  
13   C CD  . GLU A 9   ? 0.92056 0.49151 0.66745 -0.01313 -0.03254 -0.10421 9   GLU A CD  
14   O OE1 . GLU A 9   ? 0.83672 0.43123 0.59329 -0.01982 -0.04123 -0.10238 9   GLU A OE1 
15   O OE2 . GLU A 9   ? 0.84415 0.39947 0.57233 -0.00718 -0.02592 -0.11109 9   GLU A OE2 
16   N N   . GLU A 10  ? 0.94383 0.58501 0.77745 0.01786  -0.02360 -0.06252 10  GLU A N   
17   C CA  . GLU A 10  ? 0.99634 0.67110 0.85595 0.01732  -0.02668 -0.05240 10  GLU A CA  
18   C C   . GLU A 10  ? 0.89335 0.58719 0.76414 0.03548  -0.01916 -0.04648 10  GLU A C   
19   O O   . GLU A 10  ? 0.83441 0.51286 0.69517 0.04967  -0.01084 -0.04807 10  GLU A O   
20   C CB  . GLU A 10  ? 0.84402 0.50895 0.70986 0.00916  -0.02910 -0.04636 10  GLU A CB  
21   N N   . SER A 11  ? 0.80734 0.53554 0.69942 0.03477  -0.02215 -0.03963 11  SER A N   
22   C CA  . SER A 11  ? 0.71071 0.46213 0.61604 0.04920  -0.01665 -0.03361 11  SER A CA  
23   C C   . SER A 11  ? 0.73366 0.47367 0.64051 0.06026  -0.01150 -0.02689 11  SER A C   
24   O O   . SER A 11  ? 0.76243 0.48736 0.66821 0.05405  -0.01377 -0.02326 11  SER A O   
25   C CB  . SER A 11  ? 0.75336 0.54012 0.67937 0.04338  -0.02172 -0.02806 11  SER A CB  
26   O OG  . SER A 11  ? 0.57241 0.38320 0.50986 0.05507  -0.01712 -0.02397 11  SER A OG  
27   N N   . GLY A 12  ? 0.58734 0.33521 0.49675 0.07698  -0.00436 -0.02477 12  GLY A N   
28   C CA  . GLY A 12  ? 0.51905 0.26487 0.43386 0.08944  -0.00036 -0.01639 12  GLY A CA  
29   C C   . GLY A 12  ? 0.58096 0.36228 0.51740 0.09122  -0.00301 -0.00723 12  GLY A C   
30   O O   . GLY A 12  ? 0.54807 0.33083 0.48961 0.10092  -0.00099 0.00083  12  GLY A O   
31   N N   . LEU A 13  ? 0.46601 0.27479 0.41401 0.08206  -0.00762 -0.00816 13  LEU A N   
32   C CA  . LEU A 13  ? 0.39118 0.23306 0.35794 0.08287  -0.00985 -0.00088 13  LEU A CA  
33   C C   . LEU A 13  ? 0.43073 0.27032 0.40233 0.07497  -0.01431 0.00578  13  LEU A C   
34   O O   . LEU A 13  ? 0.44596 0.26693 0.41065 0.06349  -0.01751 0.00357  13  LEU A O   
35   C CB  . LEU A 13  ? 0.35713 0.22419 0.33235 0.07449  -0.01293 -0.00438 13  LEU A CB  
36   C CG  . LEU A 13  ? 0.48870 0.36301 0.46058 0.08094  -0.00816 -0.01008 13  LEU A CG  
37   C CD1 . LEU A 13  ? 0.40661 0.29804 0.38287 0.07038  -0.01177 -0.01341 13  LEU A CD1 
38   C CD2 . LEU A 13  ? 0.42412 0.31929 0.40663 0.09503  -0.00303 -0.00525 13  LEU A CD2 
39   N N   . PRO A 14  ? 0.43837 0.29854 0.42198 0.07999  -0.01473 0.01391  14  PRO A N   
40   C CA  . PRO A 14  ? 0.35229 0.21371 0.34054 0.07150  -0.01858 0.02022  14  PRO A CA  
41   C C   . PRO A 14  ? 0.38139 0.25547 0.37624 0.05602  -0.02357 0.01698  14  PRO A C   
42   O O   . PRO A 14  ? 0.33200 0.22357 0.33213 0.05367  -0.02459 0.01246  14  PRO A O   
43   C CB  . PRO A 14  ? 0.41075 0.29671 0.40995 0.08087  -0.01814 0.02836  14  PRO A CB  
44   C CG  . PRO A 14  ? 0.32647 0.23618 0.33307 0.08666  -0.01651 0.02439  14  PRO A CG  
45   C CD  . PRO A 14  ? 0.37030 0.25744 0.36466 0.09190  -0.01222 0.01734  14  PRO A CD  
46   N N   . LYS A 15  ? 0.33196 0.19751 0.32681 0.04573  -0.02627 0.01987  15  LYS A N   
47   C CA  . LYS A 15  ? 0.33037 0.21186 0.33425 0.03286  -0.03056 0.01844  15  LYS A CA  
48   C C   . LYS A 15  ? 0.29169 0.20163 0.30804 0.03466  -0.03096 0.02367  15  LYS A C   
49   O O   . LYS A 15  ? 0.32280 0.23793 0.34040 0.04307  -0.02908 0.02994  15  LYS A O   
50   C CB  . LYS A 15  ? 0.38980 0.25599 0.39145 0.02083  -0.03272 0.01997  15  LYS A CB  
51   C CG  . LYS A 15  ? 0.41242 0.25300 0.40244 0.01418  -0.03404 0.01327  15  LYS A CG  
52   C CD  . LYS A 15  ? 0.41866 0.24779 0.40885 0.00055  -0.03632 0.01529  15  LYS A CD  
53   C CE  . LYS A 15  ? 0.47795 0.28336 0.45651 -0.00825 -0.03881 0.00765  15  LYS A CE  
54   N NZ  . LYS A 15  ? 0.41313 0.21231 0.39466 -0.02344 -0.04152 0.00943  15  LYS A NZ  
55   N N   . LEU A 16  ? 0.25480 0.18189 0.27936 0.02649  -0.03363 0.02118  16  LEU A N   
56   C CA  . LEU A 16  ? 0.31675 0.26867 0.35158 0.02588  -0.03399 0.02467  16  LEU A CA  
57   C C   . LEU A 16  ? 0.26586 0.21670 0.30186 0.02389  -0.03357 0.03209  16  LEU A C   
58   O O   . LEU A 16  ? 0.28064 0.22024 0.31563 0.01543  -0.03433 0.03309  16  LEU A O   
59   C CB  . LEU A 16  ? 0.28040 0.24465 0.32179 0.01694  -0.03648 0.02039  16  LEU A CB  
60   C CG  . LEU A 16  ? 0.23149 0.21919 0.28182 0.01547  -0.03637 0.02189  16  LEU A CG  
61   C CD1 . LEU A 16  ? 0.22993 0.23125 0.28132 0.02351  -0.03462 0.02127  16  LEU A CD1 
62   C CD2 . LEU A 16  ? 0.22653 0.22103 0.28206 0.00720  -0.03848 0.01808  16  LEU A CD2 
63   N N   . PRO A 17  ? 0.22842 0.19078 0.26605 0.03099  -0.03241 0.03762  17  PRO A N   
64   C CA  . PRO A 17  ? 0.33340 0.29345 0.36964 0.02944  -0.03180 0.04528  17  PRO A CA  
65   C C   . PRO A 17  ? 0.29007 0.26108 0.33277 0.01842  -0.03245 0.04517  17  PRO A C   
66   O O   . PRO A 17  ? 0.28877 0.27479 0.33810 0.01462  -0.03347 0.04042  17  PRO A O   
67   C CB  . PRO A 17  ? 0.30472 0.28060 0.34198 0.03945  -0.03160 0.05023  17  PRO A CB  
68   C CG  . PRO A 17  ? 0.32457 0.30581 0.36320 0.04771  -0.03127 0.04583  17  PRO A CG  
69   C CD  . PRO A 17  ? 0.28187 0.26010 0.32214 0.04069  -0.03171 0.03747  17  PRO A CD  
70   N N   . VAL A 18  ? 0.26399 0.22677 0.30426 0.01371  -0.03117 0.05086  18  VAL A N   
71   C CA  . VAL A 18  ? 0.29626 0.27168 0.34238 0.00529  -0.03034 0.05245  18  VAL A CA  
72   C C   . VAL A 18  ? 0.26216 0.24844 0.30523 0.01012  -0.02915 0.05903  18  VAL A C   
73   O O   . VAL A 18  ? 0.25876 0.23305 0.29407 0.01396  -0.02801 0.06609  18  VAL A O   
74   C CB  . VAL A 18  ? 0.29972 0.26127 0.34576 -0.00450 -0.02910 0.05448  18  VAL A CB  
75   C CG1 . VAL A 18  ? 0.28688 0.26308 0.33898 -0.01149 -0.02680 0.05720  18  VAL A CG1 
76   C CG2 . VAL A 18  ? 0.26893 0.22250 0.31819 -0.01056 -0.03163 0.04737  18  VAL A CG2 
77   N N   . PRO A 19  ? 0.24375 0.25092 0.29111 0.01015  -0.02956 0.05706  19  PRO A N   
78   C CA  . PRO A 19  ? 0.24676 0.26489 0.28958 0.01395  -0.02926 0.06287  19  PRO A CA  
79   C C   . PRO A 19  ? 0.26321 0.27559 0.30184 0.00826  -0.02625 0.06913  19  PRO A C   
80   O O   . PRO A 19  ? 0.28349 0.29132 0.32655 -0.00027 -0.02408 0.06744  19  PRO A O   
81   C CB  . PRO A 19  ? 0.25314 0.29236 0.30120 0.01167  -0.02993 0.05734  19  PRO A CB  
82   C CG  . PRO A 19  ? 0.27080 0.30916 0.32541 0.01064  -0.03104 0.04941  19  PRO A CG  
83   C CD  . PRO A 19  ? 0.24205 0.26238 0.29710 0.00633  -0.03034 0.04953  19  PRO A CD  
84   N N   A PRO A 20  ? 0.28292 0.29650 0.31320 0.01258  -0.02597 0.07680  20  PRO A N   
85   N N   B PRO A 20  ? 0.28094 0.29476 0.31126 0.01258  -0.02599 0.07676  20  PRO A N   
86   C CA  A PRO A 20  ? 0.26621 0.27611 0.29125 0.00655  -0.02223 0.08295  20  PRO A CA  
87   C CA  B PRO A 20  ? 0.26193 0.27221 0.28697 0.00659  -0.02226 0.08291  20  PRO A CA  
88   C C   A PRO A 20  ? 0.30748 0.33362 0.33766 -0.00105 -0.01979 0.07842  20  PRO A C   
89   C C   B PRO A 20  ? 0.31014 0.33628 0.34069 -0.00118 -0.01980 0.07816  20  PRO A C   
90   O O   A PRO A 20  ? 0.28433 0.32628 0.31708 0.00031  -0.02152 0.07319  20  PRO A O   
91   O O   B PRO A 20  ? 0.28354 0.32521 0.31727 -0.00005 -0.02150 0.07254  20  PRO A O   
92   C CB  A PRO A 20  ? 0.34056 0.35168 0.35435 0.01447  -0.02356 0.09169  20  PRO A CB  
93   C CB  B PRO A 20  ? 0.34255 0.35540 0.35654 0.01435  -0.02364 0.09138  20  PRO A CB  
94   C CG  A PRO A 20  ? 0.32187 0.34645 0.33833 0.02324  -0.02830 0.08853  20  PRO A CG  
95   C CG  B PRO A 20  ? 0.32318 0.33519 0.33758 0.02544  -0.02782 0.09111  20  PRO A CG  
96   C CD  A PRO A 20  ? 0.34419 0.36314 0.36939 0.02347  -0.02906 0.08083  20  PRO A CD  
97   C CD  B PRO A 20  ? 0.34773 0.36882 0.37329 0.02315  -0.02915 0.08044  20  PRO A CD  
98   N N   . LEU A 21  ? 0.30242 0.32404 0.33415 -0.00923 -0.01518 0.08039  21  LEU A N   
99   C CA  . LEU A 21  ? 0.26459 0.30024 0.30254 -0.01565 -0.01168 0.07580  21  LEU A CA  
100  C C   . LEU A 21  ? 0.30245 0.35212 0.33236 -0.01366 -0.01088 0.07630  21  LEU A C   
101  O O   . LEU A 21  ? 0.25815 0.32031 0.29173 -0.01476 -0.01064 0.06950  21  LEU A O   
102  C CB  . LEU A 21  ? 0.23722 0.26737 0.27862 -0.02419 -0.00617 0.07921  21  LEU A CB  
103  C CG  . LEU A 21  ? 0.23386 0.27876 0.28121 -0.02949 -0.00096 0.07588  21  LEU A CG  
104  C CD1 . LEU A 21  ? 0.27675 0.32967 0.33735 -0.03020 -0.00293 0.06694  21  LEU A CD1 
105  C CD2 . LEU A 21  ? 0.32849 0.36977 0.37811 -0.03752 0.00552  0.08145  21  LEU A CD2 
106  N N   . GLN A 22  ? 0.29698 0.34370 0.31447 -0.01097 -0.01054 0.08435  22  GLN A N   
107  C CA  . GLN A 22  ? 0.27670 0.33677 0.28459 -0.01054 -0.00993 0.08475  22  GLN A CA  
108  C C   . GLN A 22  ? 0.30627 0.37870 0.31395 -0.00526 -0.01598 0.07985  22  GLN A C   
109  O O   . GLN A 22  ? 0.28081 0.36608 0.28424 -0.00740 -0.01572 0.07563  22  GLN A O   
110  C CB  . GLN A 22  ? 0.32766 0.38180 0.32068 -0.00879 -0.00872 0.09541  22  GLN A CB  
111  C CG  . GLN A 22  ? 0.32648 0.36935 0.31845 -0.01544 -0.00168 0.10087  22  GLN A CG  
112  C CD  . GLN A 22  ? 0.41921 0.47156 0.41727 -0.02331 0.00518  0.09545  22  GLN A CD  
113  O OE1 . GLN A 22  ? 0.30225 0.36771 0.29680 -0.02367 0.00622  0.09031  22  GLN A OE1 
114  N NE2 . GLN A 22  ? 0.37473 0.42028 0.38164 -0.02978 0.01024  0.09673  22  GLN A NE2 
115  N N   . GLN A 23  ? 0.22478 0.29331 0.23652 0.00121  -0.02097 0.08023  23  GLN A N   
116  C CA  . GLN A 23  ? 0.25262 0.33445 0.26720 0.00557  -0.02619 0.07530  23  GLN A CA  
117  C C   . GLN A 23  ? 0.21991 0.30919 0.24311 0.00028  -0.02489 0.06498  23  GLN A C   
118  O O   . GLN A 23  ? 0.22460 0.32739 0.24601 -0.00114 -0.02650 0.06017  23  GLN A O   
119  C CB  . GLN A 23  ? 0.36526 0.43984 0.38388 0.01386  -0.02999 0.07755  23  GLN A CB  
120  C CG  . GLN A 23  ? 0.29413 0.38327 0.31838 0.01853  -0.03462 0.07255  23  GLN A CG  
121  C CD  . GLN A 23  ? 0.37037 0.45127 0.39876 0.02739  -0.03673 0.07441  23  GLN A CD  
122  O OE1 . GLN A 23  ? 0.36647 0.44002 0.38929 0.03511  -0.03797 0.08245  23  GLN A OE1 
123  N NE2 . GLN A 23  ? 0.38143 0.46222 0.41849 0.02682  -0.03667 0.06709  23  GLN A NE2 
124  N N   . THR A 24  ? 0.23443 0.31451 0.26648 -0.00288 -0.02227 0.06164  24  THR A N   
125  C CA  . THR A 24  ? 0.21678 0.30200 0.25670 -0.00675 -0.02108 0.05289  24  THR A CA  
126  C C   . THR A 24  ? 0.27773 0.36985 0.31397 -0.01216 -0.01644 0.05012  24  THR A C   
127  O O   . THR A 24  ? 0.22696 0.32661 0.26337 -0.01395 -0.01629 0.04349  24  THR A O   
128  C CB  . THR A 24  ? 0.26069 0.33513 0.31025 -0.00840 -0.02024 0.05109  24  THR A CB  
129  O OG1 . THR A 24  ? 0.22881 0.29795 0.28069 -0.00323 -0.02440 0.05048  24  THR A OG1 
130  C CG2 . THR A 24  ? 0.21236 0.29117 0.26954 -0.01270 -0.01784 0.04392  24  THR A CG2 
131  N N   . LEU A 25  ? 0.21089 0.29958 0.24261 -0.01490 -0.01193 0.05508  25  LEU A N   
132  C CA  . LEU A 25  ? 0.27497 0.36956 0.30259 -0.01936 -0.00621 0.05198  25  LEU A CA  
133  C C   . LEU A 25  ? 0.22412 0.32798 0.23907 -0.01923 -0.00803 0.05030  25  LEU A C   
134  O O   . LEU A 25  ? 0.26194 0.37071 0.27376 -0.02236 -0.00520 0.04363  25  LEU A O   
135  C CB  . LEU A 25  ? 0.23235 0.32234 0.25793 -0.02256 -0.00006 0.05803  25  LEU A CB  
136  C CG  . LEU A 25  ? 0.21967 0.30227 0.25821 -0.02475 0.00167  0.05964  25  LEU A CG  
137  C CD1 . LEU A 25  ? 0.24652 0.32687 0.28326 -0.02937 0.00869  0.06583  25  LEU A CD1 
138  C CD2 . LEU A 25  ? 0.18375 0.27084 0.23435 -0.02580 0.00269  0.05168  25  LEU A CD2 
139  N N   . ALA A 26  ? 0.20814 0.31418 0.21527 -0.01557 -0.01297 0.05627  26  ALA A N   
140  C CA  . ALA A 26  ? 0.25150 0.36890 0.24679 -0.01592 -0.01627 0.05510  26  ALA A CA  
141  C C   . ALA A 26  ? 0.28150 0.40738 0.28200 -0.01649 -0.02034 0.04708  26  ALA A C   
142  O O   . ALA A 26  ? 0.23451 0.36753 0.22798 -0.02106 -0.01988 0.04100  26  ALA A O   
143  C CB  . ALA A 26  ? 0.26815 0.38743 0.25537 -0.01056 -0.02143 0.06450  26  ALA A CB  
144  N N   . THR A 27  ? 0.21962 0.34380 0.23133 -0.01248 -0.02386 0.04674  27  THR A N   
145  C CA  . THR A 27  ? 0.25927 0.39112 0.27644 -0.01356 -0.02680 0.03955  27  THR A CA  
146  C C   . THR A 27  ? 0.24421 0.37215 0.26338 -0.01927 -0.02172 0.03118  27  THR A C   
147  O O   . THR A 27  ? 0.23997 0.37411 0.25560 -0.02350 -0.02219 0.02472  27  THR A O   
148  C CB  . THR A 27  ? 0.24719 0.37600 0.27519 -0.00787 -0.02996 0.04091  27  THR A CB  
149  O OG1 . THR A 27  ? 0.23965 0.37271 0.26518 -0.00118 -0.03455 0.04843  27  THR A OG1 
150  C CG2 . THR A 27  ? 0.23567 0.37190 0.26957 -0.00969 -0.03175 0.03360  27  THR A CG2 
151  N N   . TYR A 28  ? 0.18299 0.30062 0.20785 -0.01947 -0.01686 0.03145  28  TYR A N   
152  C CA  . TYR A 28  ? 0.17757 0.29107 0.20526 -0.02295 -0.01167 0.02470  28  TYR A CA  
153  C C   . TYR A 28  ? 0.27418 0.39062 0.28972 -0.02746 -0.00767 0.02052  28  TYR A C   
154  O O   . TYR A 28  ? 0.22604 0.34212 0.23911 -0.03063 -0.00629 0.01323  28  TYR A O   
155  C CB  . TYR A 28  ? 0.18581 0.29140 0.22218 -0.02205 -0.00752 0.02732  28  TYR A CB  
156  C CG  . TYR A 28  ? 0.19620 0.29912 0.23544 -0.02409 -0.00113 0.02213  28  TYR A CG  
157  C CD1 . TYR A 28  ? 0.21404 0.31437 0.25842 -0.02391 -0.00130 0.01615  28  TYR A CD1 
158  C CD2 . TYR A 28  ? 0.22235 0.32504 0.25930 -0.02543 0.00560  0.02386  28  TYR A CD2 
159  C CE1 . TYR A 28  ? 0.18523 0.28216 0.23214 -0.02409 0.00464  0.01215  28  TYR A CE1 
160  C CE2 . TYR A 28  ? 0.25037 0.35141 0.29108 -0.02561 0.01204  0.01946  28  TYR A CE2 
161  C CZ  . TYR A 28  ? 0.24741 0.34523 0.29319 -0.02443 0.01131  0.01380  28  TYR A CZ  
162  O OH  . TYR A 28  ? 0.22120 0.31656 0.27027 -0.02309 0.01791  0.01012  28  TYR A OH  
163  N N   . LEU A 29  ? 0.22798 0.34576 0.23413 -0.02813 -0.00537 0.02495  29  LEU A N   
164  C CA  . LEU A 29  ? 0.24856 0.36797 0.24064 -0.03254 -0.00114 0.02050  29  LEU A CA  
165  C C   . LEU A 29  ? 0.30548 0.43313 0.28844 -0.03609 -0.00673 0.01595  29  LEU A C   
166  O O   . LEU A 29  ? 0.26214 0.38817 0.23686 -0.04107 -0.00388 0.00806  29  LEU A O   
167  C CB  . LEU A 29  ? 0.22546 0.34499 0.20766 -0.03255 0.00228  0.02705  29  LEU A CB  
168  C CG  . LEU A 29  ? 0.25422 0.36741 0.24251 -0.03193 0.01071  0.02960  29  LEU A CG  
169  C CD1 . LEU A 29  ? 0.24996 0.36373 0.22685 -0.03260 0.01366  0.03701  29  LEU A CD1 
170  C CD2 . LEU A 29  ? 0.25368 0.36344 0.24148 -0.03373 0.01866  0.02142  29  LEU A CD2 
171  N N   . GLN A 30  ? 0.22372 0.36039 0.20809 -0.03373 -0.01455 0.02069  30  GLN A N   
172  C CA  . GLN A 30  ? 0.27468 0.42295 0.25187 -0.03793 -0.02025 0.01666  30  GLN A CA  
173  C C   . GLN A 30  ? 0.30842 0.45649 0.29375 -0.04090 -0.02099 0.00907  30  GLN A C   
174  O O   . GLN A 30  ? 0.28916 0.44297 0.26715 -0.04759 -0.02272 0.00273  30  GLN A O   
175  C CB  . GLN A 30  ? 0.34244 0.50304 0.31949 -0.03344 -0.02829 0.02474  30  GLN A CB  
176  C CG  . GLN A 30  ? 0.46725 0.62803 0.45935 -0.02665 -0.03162 0.02899  30  GLN A CG  
177  C CD  . GLN A 30  ? 0.58662 0.75953 0.58519 -0.02820 -0.03675 0.02468  30  GLN A CD  
178  O OE1 . GLN A 30  ? 0.49335 0.68064 0.48514 -0.03220 -0.04147 0.02310  30  GLN A OE1 
179  N NE2 . GLN A 30  ? 0.35063 0.51871 0.36198 -0.02587 -0.03583 0.02255  30  GLN A NE2 
180  N N   . CYS A 31  ? 0.25764 0.39839 0.25674 -0.03687 -0.01953 0.00956  31  CYS A N   
181  C CA  . CYS A 31  ? 0.24046 0.37787 0.24586 -0.03954 -0.01879 0.00286  31  CYS A CA  
182  C C   . CYS A 31  ? 0.30093 0.42818 0.29812 -0.04507 -0.01225 -0.00504 31  CYS A C   
183  O O   . CYS A 31  ? 0.26676 0.39259 0.26171 -0.05040 -0.01209 -0.01163 31  CYS A O   
184  C CB  . CYS A 31  ? 0.21399 0.34348 0.23330 -0.03377 -0.01798 0.00539  31  CYS A CB  
185  S SG  . CYS A 31  ? 0.36098 0.49894 0.39015 -0.02775 -0.02479 0.01118  31  CYS A SG  
186  N N   . MET A 32  ? 0.20667 0.32533 0.20037 -0.04337 -0.00593 -0.00432 32  MET A N   
187  C CA  . MET A 32  ? 0.26199 0.36847 0.25071 -0.04565 0.00173  -0.01117 32  MET A CA  
188  C C   . MET A 32  ? 0.27295 0.37803 0.24338 -0.05135 0.00534  -0.01624 32  MET A C   
189  O O   . MET A 32  ? 0.29994 0.39339 0.26322 -0.05384 0.01186  -0.02338 32  MET A O   
190  C CB  . MET A 32  ? 0.27487 0.37391 0.27328 -0.03955 0.00747  -0.00775 32  MET A CB  
191  C CG  . MET A 32  ? 0.30641 0.40358 0.32098 -0.03504 0.00456  -0.00492 32  MET A CG  
192  S SD  . MET A 32  ? 0.33636 0.42743 0.35176 -0.03771 0.00341  -0.01165 32  MET A SD  
193  C CE  . MET A 32  ? 0.30187 0.37867 0.31041 -0.03790 0.01298  -0.01803 32  MET A CE  
194  N N   . ARG A 33  ? 0.23626 0.35163 0.19753 -0.05312 0.00145  -0.01273 33  ARG A N   
195  C CA  . ARG A 33  ? 0.28223 0.39555 0.22393 -0.05843 0.00518  -0.01730 33  ARG A CA  
196  C C   . ARG A 33  ? 0.30524 0.41181 0.23607 -0.06657 0.00661  -0.02806 33  ARG A C   
197  O O   . ARG A 33  ? 0.39464 0.48866 0.31280 -0.06897 0.01459  -0.03464 33  ARG A O   
198  C CB  . ARG A 33  ? 0.37574 0.50302 0.30825 -0.05980 -0.00161 -0.01178 33  ARG A CB  
199  C CG  . ARG A 33  ? 0.41866 0.54322 0.32894 -0.06502 0.00253  -0.01591 33  ARG A CG  
200  C CD  . ARG A 33  ? 0.55679 0.69641 0.45463 -0.06926 -0.00638 -0.01343 33  ARG A CD  
201  N NE  . ARG A 33  ? 0.58190 0.72781 0.47916 -0.06326 -0.00836 -0.00238 33  ARG A NE  
202  C CZ  . ARG A 33  ? 0.65761 0.80013 0.53904 -0.06349 -0.00342 -0.00008 33  ARG A CZ  
203  N NH1 . ARG A 33  ? 0.66249 0.79564 0.52715 -0.06881 0.00420  -0.00854 33  ARG A NH1 
204  N NH2 . ARG A 33  ? 0.60056 0.74771 0.48197 -0.05813 -0.00545 0.01102  33  ARG A NH2 
205  N N   . HIS A 34  ? 0.34168 0.45568 0.27689 -0.07110 -0.00037 -0.03012 34  HIS A N   
206  C CA  . HIS A 34  ? 0.33604 0.44398 0.25977 -0.08102 0.00044  -0.04022 34  HIS A CA  
207  C C   . HIS A 34  ? 0.32984 0.41964 0.25865 -0.08013 0.00716  -0.04535 34  HIS A C   
208  O O   . HIS A 34  ? 0.34975 0.43002 0.26850 -0.08840 0.00915  -0.05381 34  HIS A O   
209  C CB  . HIS A 34  ? 0.30358 0.42967 0.23013 -0.08758 -0.00968 -0.04014 34  HIS A CB  
210  C CG  . HIS A 34  ? 0.30506 0.43962 0.25225 -0.08177 -0.01416 -0.03409 34  HIS A CG  
211  N ND1 . HIS A 34  ? 0.27893 0.42277 0.23769 -0.07235 -0.01774 -0.02433 34  HIS A ND1 
212  C CD2 . HIS A 34  ? 0.31334 0.44651 0.27011 -0.08407 -0.01482 -0.03662 34  HIS A CD2 
213  C CE1 . HIS A 34  ? 0.34540 0.49320 0.31965 -0.06886 -0.02045 -0.02172 34  HIS A CE1 
214  N NE2 . HIS A 34  ? 0.26691 0.40927 0.24043 -0.07579 -0.01874 -0.02884 34  HIS A NE2 
215  N N   . LEU A 35  ? 0.27134 0.35543 0.21445 -0.07069 0.01062  -0.04037 35  LEU A N   
216  C CA  . LEU A 35  ? 0.36936 0.43760 0.31832 -0.06818 0.01599  -0.04355 35  LEU A CA  
217  C C   . LEU A 35  ? 0.41072 0.46416 0.35705 -0.06189 0.02603  -0.04491 35  LEU A C   
218  O O   . LEU A 35  ? 0.38379 0.42437 0.33592 -0.05762 0.03061  -0.04624 35  LEU A O   
219  C CB  . LEU A 35  ? 0.29649 0.37081 0.26475 -0.06219 0.01135  -0.03699 35  LEU A CB  
220  C CG  . LEU A 35  ? 0.29014 0.37962 0.26425 -0.06622 0.00255  -0.03504 35  LEU A CG  
221  C CD1 . LEU A 35  ? 0.25857 0.35115 0.25002 -0.05848 -0.00030 -0.02851 35  LEU A CD1 
222  C CD2 . LEU A 35  ? 0.31009 0.39384 0.27690 -0.07566 0.00296  -0.04260 35  LEU A CD2 
223  N N   . VAL A 36  ? 0.40780 0.46385 0.34621 -0.06049 0.02968  -0.04386 36  VAL A N   
224  C CA  . VAL A 36  ? 0.42798 0.47277 0.36363 -0.05452 0.04026  -0.04528 36  VAL A CA  
225  C C   . VAL A 36  ? 0.39758 0.43785 0.31057 -0.06020 0.04506  -0.05152 36  VAL A C   
226  O O   . VAL A 36  ? 0.45736 0.50648 0.35903 -0.06794 0.03883  -0.05271 36  VAL A O   
227  C CB  . VAL A 36  ? 0.44003 0.49411 0.39155 -0.04591 0.04137  -0.03613 36  VAL A CB  
228  C CG1 . VAL A 36  ? 0.33960 0.39727 0.31124 -0.04114 0.03622  -0.03076 36  VAL A CG1 
229  C CG2 . VAL A 36  ? 0.30018 0.36851 0.24741 -0.04814 0.03679  -0.03051 36  VAL A CG2 
230  N N   . SER A 37  ? 0.51948 0.54655 0.42563 -0.05581 0.05632  -0.05539 37  SER A N   
231  C CA  . SER A 37  ? 0.43212 0.45250 0.31462 -0.06068 0.06236  -0.06209 37  SER A CA  
232  C C   . SER A 37  ? 0.54195 0.57804 0.42161 -0.06036 0.06051  -0.05541 37  SER A C   
233  O O   . SER A 37  ? 0.40785 0.45621 0.30477 -0.05462 0.05778  -0.04584 37  SER A O   
234  C CB  . SER A 37  ? 0.50845 0.51002 0.38475 -0.05437 0.07628  -0.06780 37  SER A CB  
235  O OG  . SER A 37  ? 0.49370 0.50262 0.38259 -0.04461 0.08279  -0.06102 37  SER A OG  
236  N N   . GLU A 38  ? 0.43720 0.47156 0.29317 -0.06712 0.06207  -0.06054 38  GLU A N   
237  C CA  . GLU A 38  ? 0.47801 0.52599 0.32821 -0.06707 0.06034  -0.05370 38  GLU A CA  
238  C C   . GLU A 38  ? 0.42455 0.47243 0.28341 -0.05790 0.07093  -0.04825 38  GLU A C   
239  O O   . GLU A 38  ? 0.50176 0.56237 0.36839 -0.05522 0.06865  -0.03855 38  GLU A O   
240  C CB  . GLU A 38  ? 0.60985 0.65500 0.43040 -0.07627 0.06028  -0.06084 38  GLU A CB  
241  C CG  . GLU A 38  ? 0.70749 0.76825 0.52321 -0.08436 0.04596  -0.05851 38  GLU A CG  
242  C CD  . GLU A 38  ? 0.99022 1.04442 0.78212 -0.09643 0.04335  -0.07002 38  GLU A CD  
243  O OE1 . GLU A 38  ? 1.16572 1.20072 0.94046 -0.09859 0.05364  -0.07998 38  GLU A OE1 
244  O OE2 . GLU A 38  ? 1.00594 1.07430 0.79643 -0.10383 0.03114  -0.06927 38  GLU A OE2 
245  N N   . GLU A 39  ? 0.50035 0.53403 0.35819 -0.05298 0.08292  -0.05414 39  GLU A N   
246  C CA  . GLU A 39  ? 0.51220 0.54839 0.38047 -0.04416 0.09376  -0.04923 39  GLU A CA  
247  C C   . GLU A 39  ? 0.54654 0.59370 0.44509 -0.03769 0.08943  -0.03970 39  GLU A C   
248  O O   . GLU A 39  ? 0.44063 0.49952 0.35003 -0.03468 0.09091  -0.03105 39  GLU A O   
249  C CB  . GLU A 39  ? 0.74355 0.76216 0.60378 -0.03929 0.10764  -0.05820 39  GLU A CB  
250  C CG  . GLU A 39  ? 0.89788 0.92030 0.77680 -0.02813 0.11862  -0.05349 39  GLU A CG  
251  C CD  . GLU A 39  ? 1.18466 1.18859 1.05697 -0.02150 0.13169  -0.06239 39  GLU A CD  
252  O OE1 . GLU A 39  ? 1.21375 1.20428 1.05996 -0.02451 0.13979  -0.07112 39  GLU A OE1 
253  O OE2 . GLU A 39  ? 1.09811 1.09994 0.99013 -0.01305 0.13371  -0.06073 39  GLU A OE2 
254  N N   . GLN A 40  ? 0.41974 0.46259 0.33099 -0.03634 0.08398  -0.04121 40  GLN A N   
255  C CA  . GLN A 40  ? 0.42050 0.47313 0.35809 -0.03126 0.07853  -0.03289 40  GLN A CA  
256  C C   . GLN A 40  ? 0.32979 0.39636 0.27199 -0.03506 0.06788  -0.02471 40  GLN A C   
257  O O   . GLN A 40  ? 0.35634 0.43234 0.31553 -0.03154 0.06645  -0.01633 40  GLN A O   
258  C CB  . GLN A 40  ? 0.39311 0.43699 0.33921 -0.02978 0.07457  -0.03649 40  GLN A CB  
259  C CG  . GLN A 40  ? 0.44880 0.50064 0.42022 -0.02406 0.06988  -0.02915 40  GLN A CG  
260  C CD  . GLN A 40  ? 0.61371 0.65554 0.59066 -0.02243 0.06672  -0.03255 40  GLN A CD  
261  O OE1 . GLN A 40  ? 0.53812 0.56461 0.50569 -0.02092 0.07324  -0.03956 40  GLN A OE1 
262  N NE2 . GLN A 40  ? 0.42460 0.47333 0.41527 -0.02266 0.05721  -0.02760 40  GLN A NE2 
263  N N   . PHE A 41  ? 0.37211 0.44019 0.29931 -0.04223 0.06028  -0.02687 41  PHE A N   
264  C CA  . PHE A 41  ? 0.36531 0.44620 0.29693 -0.04400 0.05048  -0.01844 41  PHE A CA  
265  C C   . PHE A 41  ? 0.37821 0.46525 0.30559 -0.04287 0.05500  -0.01142 41  PHE A C   
266  O O   . PHE A 41  ? 0.33066 0.42519 0.27051 -0.04063 0.05127  -0.00229 41  PHE A O   
267  C CB  . PHE A 41  ? 0.36942 0.45392 0.28724 -0.05110 0.04121  -0.02145 41  PHE A CB  
268  C CG  . PHE A 41  ? 0.34866 0.44628 0.27205 -0.05091 0.03114  -0.01228 41  PHE A CG  
269  C CD1 . PHE A 41  ? 0.39894 0.50065 0.34196 -0.04722 0.02475  -0.00730 41  PHE A CD1 
270  C CD2 . PHE A 41  ? 0.41384 0.51858 0.32167 -0.05384 0.02817  -0.00863 41  PHE A CD2 
271  C CE1 . PHE A 41  ? 0.40337 0.51503 0.35072 -0.04587 0.01626  0.00099  41  PHE A CE1 
272  C CE2 . PHE A 41  ? 0.47021 0.58570 0.38274 -0.05217 0.01913  0.00048  41  PHE A CE2 
273  C CZ  . PHE A 41  ? 0.36796 0.48628 0.30050 -0.04786 0.01358  0.00518  41  PHE A CZ  
274  N N   . ARG A 42  ? 0.33956 0.42205 0.24833 -0.04466 0.06376  -0.01564 42  ARG A N   
275  C CA  . ARG A 42  ? 0.39287 0.48071 0.29632 -0.04392 0.06944  -0.00868 42  ARG A CA  
276  C C   . ARG A 42  ? 0.35841 0.45039 0.28486 -0.03817 0.07516  -0.00200 42  ARG A C   
277  O O   . ARG A 42  ? 0.39480 0.49379 0.32671 -0.03819 0.07417  0.00746  42  ARG A O   
278  C CB  . ARG A 42  ? 0.47298 0.55376 0.35247 -0.04617 0.07987  -0.01562 42  ARG A CB  
279  C CG  . ARG A 42  ? 0.61528 0.70140 0.48101 -0.04774 0.08388  -0.00895 42  ARG A CG  
280  C CD  . ARG A 42  ? 0.97578 1.05716 0.80946 -0.05397 0.08433  -0.01570 42  ARG A CD  
281  N NE  . ARG A 42  ? 0.82470 0.89285 0.64696 -0.05477 0.09221  -0.02866 42  ARG A NE  
282  C CZ  . ARG A 42  ? 0.98328 1.04458 0.78930 -0.06111 0.08668  -0.03809 42  ARG A CZ  
283  N NH1 . ARG A 42  ? 0.90884 0.97846 0.70869 -0.06719 0.07294  -0.03612 42  ARG A NH1 
284  N NH2 . ARG A 42  ? 0.97953 1.02532 0.77532 -0.06140 0.09537  -0.04973 42  ARG A NH2 
285  N N   . LYS A 43  ? 0.36762 0.45534 0.30776 -0.03346 0.08075  -0.00651 43  LYS A N   
286  C CA  . LYS A 43  ? 0.31028 0.40465 0.27404 -0.02838 0.08530  -0.00056 43  LYS A CA  
287  C C   . LYS A 43  ? 0.33455 0.43475 0.31610 -0.02867 0.07419  0.00653  43  LYS A C   
288  O O   . LYS A 43  ? 0.29381 0.40130 0.28855 -0.02834 0.07502  0.01446  43  LYS A O   
289  C CB  . LYS A 43  ? 0.35465 0.44388 0.32858 -0.02218 0.09265  -0.00677 43  LYS A CB  
290  C CG  . LYS A 43  ? 0.48755 0.57171 0.44851 -0.01940 0.10738  -0.01242 43  LYS A CG  
291  C CD  . LYS A 43  ? 0.73908 0.81713 0.71115 -0.01129 0.11444  -0.01783 43  LYS A CD  
292  C CE  . LYS A 43  ? 0.85161 0.92595 0.81460 -0.00633 0.13068  -0.02240 43  LYS A CE  
293  N NZ  . LYS A 43  ? 0.65118 0.70776 0.58470 -0.00920 0.13500  -0.03305 43  LYS A NZ  
294  N N   . SER A 44  ? 0.27997 0.37648 0.26158 -0.02976 0.06429  0.00349  44  SER A N   
295  C CA  . SER A 44  ? 0.30384 0.40440 0.29998 -0.02963 0.05406  0.00940  44  SER A CA  
296  C C   . SER A 44  ? 0.27999 0.38510 0.27006 -0.03249 0.04940  0.01755  44  SER A C   
297  O O   . SER A 44  ? 0.25429 0.36219 0.25736 -0.03185 0.04588  0.02467  44  SER A O   
298  C CB  . SER A 44  ? 0.33977 0.43591 0.33524 -0.03026 0.04584  0.00410  44  SER A CB  
299  O OG  . SER A 44  ? 0.29877 0.38927 0.30264 -0.02674 0.04959  -0.00129 44  SER A OG  
300  N N   . GLN A 45  ? 0.30270 0.40763 0.27197 -0.03570 0.04913  0.01675  45  GLN A N   
301  C CA  . GLN A 45  ? 0.27656 0.38503 0.23822 -0.03731 0.04520  0.02553  45  GLN A CA  
302  C C   . GLN A 45  ? 0.34579 0.45585 0.31436 -0.03706 0.05274  0.03322  45  GLN A C   
303  O O   . GLN A 45  ? 0.32890 0.43936 0.30307 -0.03723 0.04864  0.04183  45  GLN A O   
304  C CB  . GLN A 45  ? 0.32382 0.43290 0.26051 -0.04076 0.04472  0.02338  45  GLN A CB  
305  C CG  . GLN A 45  ? 0.40180 0.51304 0.33020 -0.04289 0.03475  0.01879  45  GLN A CG  
306  C CD  . GLN A 45  ? 0.44542 0.55842 0.34792 -0.04735 0.03487  0.01641  45  GLN A CD  
307  O OE1 . GLN A 45  ? 0.54969 0.65779 0.43952 -0.04938 0.04402  0.01072  45  GLN A OE1 
308  N NE2 . GLN A 45  ? 0.45649 0.57676 0.35079 -0.04843 0.02487  0.02089  45  GLN A NE2 
309  N N   . ALA A 46  ? 0.29553 0.40615 0.26362 -0.03678 0.06436  0.03028  46  ALA A N   
310  C CA  . ALA A 46  ? 0.29315 0.40770 0.26901 -0.03750 0.07254  0.03758  46  ALA A CA  
311  C C   . ALA A 46  ? 0.30766 0.42551 0.30977 -0.03621 0.07044  0.04078  46  ALA A C   
312  O O   . ALA A 46  ? 0.27628 0.39629 0.28633 -0.03871 0.07132  0.04899  46  ALA A O   
313  C CB  . ALA A 46  ? 0.39133 0.50750 0.36063 -0.03682 0.08633  0.03332  46  ALA A CB  
314  N N   . ILE A 47  ? 0.28938 0.40692 0.30408 -0.03291 0.06752  0.03445  47  ILE A N   
315  C CA  . ILE A 47  ? 0.31062 0.43171 0.34874 -0.03191 0.06411  0.03706  47  ILE A CA  
316  C C   . ILE A 47  ? 0.29845 0.41577 0.33849 -0.03414 0.05377  0.04305  47  ILE A C   
317  O O   . ILE A 47  ? 0.24960 0.36855 0.30158 -0.03666 0.05325  0.04932  47  ILE A O   
318  C CB  . ILE A 47  ? 0.25116 0.37120 0.29895 -0.02736 0.06234  0.02941  47  ILE A CB  
319  C CG1 . ILE A 47  ? 0.27839 0.40273 0.33048 -0.02365 0.07417  0.02546  47  ILE A CG1 
320  C CG2 . ILE A 47  ? 0.22711 0.34862 0.29379 -0.02690 0.05416  0.03187  47  ILE A CG2 
321  C CD1 . ILE A 47  ? 0.33716 0.45692 0.39326 -0.01817 0.07397  0.01775  47  ILE A CD1 
322  N N   . VAL A 48  ? 0.25093 0.36312 0.27901 -0.03341 0.04578  0.04112  48  VAL A N   
323  C CA  . VAL A 48  ? 0.29663 0.40465 0.32584 -0.03367 0.03634  0.04629  48  VAL A CA  
324  C C   . VAL A 48  ? 0.26755 0.37326 0.28902 -0.03641 0.03824  0.05569  48  VAL A C   
325  O O   . VAL A 48  ? 0.33083 0.43194 0.35951 -0.03756 0.03483  0.06173  48  VAL A O   
326  C CB  . VAL A 48  ? 0.25375 0.36007 0.27247 -0.03178 0.02846  0.04208  48  VAL A CB  
327  C CG1 . VAL A 48  ? 0.20663 0.30957 0.22279 -0.03062 0.02004  0.04846  48  VAL A CG1 
328  C CG2 . VAL A 48  ? 0.28336 0.38941 0.31196 -0.02972 0.02589  0.03423  48  VAL A CG2 
329  N N   . GLN A 49  ? 0.27275 0.38000 0.27794 -0.03779 0.04413  0.05704  49  GLN A N   
330  C CA  . GLN A 49  ? 0.29273 0.39688 0.28844 -0.04048 0.04701  0.06669  49  GLN A CA  
331  C C   . GLN A 49  ? 0.34514 0.44997 0.35637 -0.04422 0.05321  0.07170  49  GLN A C   
332  O O   . GLN A 49  ? 0.30730 0.40548 0.31922 -0.04673 0.05143  0.07989  49  GLN A O   
333  C CB  . GLN A 49  ? 0.39157 0.49810 0.36653 -0.04166 0.05366  0.06633  49  GLN A CB  
334  C CG  . GLN A 49  ? 0.44330 0.54555 0.40395 -0.04404 0.05597  0.07710  49  GLN A CG  
335  C CD  . GLN A 49  ? 0.60205 0.70500 0.57124 -0.04845 0.06648  0.08277  49  GLN A CD  
336  O OE1 . GLN A 49  ? 0.77422 0.87062 0.74213 -0.05110 0.06644  0.09242  49  GLN A OE1 
337  N NE2 . GLN A 49  ? 0.72056 0.83144 0.69881 -0.04924 0.07594  0.07700  49  GLN A NE2 
338  N N   . GLN A 50  ? 0.33007 0.44301 0.35376 -0.04478 0.06084  0.06707  50  GLN A N   
339  C CA  . GLN A 50  ? 0.28796 0.40540 0.32868 -0.04914 0.06646  0.07175  50  GLN A CA  
340  C C   . GLN A 50  ? 0.33536 0.44884 0.39201 -0.05016 0.05760  0.07278  50  GLN A C   
341  O O   . GLN A 50  ? 0.28429 0.39451 0.34751 -0.05554 0.05797  0.07942  50  GLN A O   
342  C CB  . GLN A 50  ? 0.32111 0.45071 0.37358 -0.04788 0.07614  0.06649  50  GLN A CB  
343  C CG  . GLN A 50  ? 0.42504 0.56383 0.49152 -0.05315 0.08530  0.07224  50  GLN A CG  
344  C CD  . GLN A 50  ? 0.79964 0.94531 0.89228 -0.05530 0.08127  0.07243  50  GLN A CD  
345  O OE1 . GLN A 50  ? 0.54167 0.68673 0.64299 -0.05132 0.07326  0.06696  50  GLN A OE1 
346  N NE2 . GLN A 50  ? 0.59251 0.74524 0.69728 -0.06241 0.08688  0.07889  50  GLN A NE2 
347  N N   . PHE A 51  ? 0.26879 0.38130 0.33034 -0.04566 0.04986  0.06608  51  PHE A N   
348  C CA  . PHE A 51  ? 0.26717 0.37572 0.34241 -0.04636 0.04172  0.06602  51  PHE A CA  
349  C C   . PHE A 51  ? 0.32381 0.41910 0.39015 -0.04781 0.03564  0.07242  51  PHE A C   
350  O O   . PHE A 51  ? 0.29430 0.38403 0.36952 -0.05203 0.03328  0.07595  51  PHE A O   
351  C CB  . PHE A 51  ? 0.27934 0.38888 0.35838 -0.04093 0.03567  0.05779  51  PHE A CB  
352  C CG  . PHE A 51  ? 0.27637 0.38093 0.36598 -0.04094 0.02695  0.05692  51  PHE A CG  
353  C CD1 . PHE A 51  ? 0.23060 0.34106 0.33829 -0.04352 0.02680  0.05631  51  PHE A CD1 
354  C CD2 . PHE A 51  ? 0.30055 0.39570 0.38164 -0.03803 0.01895  0.05639  51  PHE A CD2 
355  C CE1 . PHE A 51  ? 0.24602 0.35117 0.36114 -0.04393 0.01846  0.05486  51  PHE A CE1 
356  C CE2 . PHE A 51  ? 0.32265 0.41217 0.41148 -0.03769 0.01178  0.05497  51  PHE A CE2 
357  C CZ  . PHE A 51  ? 0.23131 0.32492 0.33618 -0.04101 0.01143  0.05399  51  PHE A CZ  
358  N N   . GLY A 52  ? 0.25542 0.34530 0.30387 -0.04436 0.03312  0.07409  52  GLY A N   
359  C CA  . GLY A 52  ? 0.29413 0.37147 0.33301 -0.04329 0.02747  0.08052  52  GLY A CA  
360  C C   . GLY A 52  ? 0.29315 0.36388 0.31980 -0.04670 0.03260  0.09030  52  GLY A C   
361  O O   . GLY A 52  ? 0.35562 0.41503 0.37112 -0.04402 0.02810  0.09635  52  GLY A O   
362  N N   . ALA A 53  ? 0.33435 0.41155 0.36242 -0.05196 0.04226  0.09250  53  ALA A N   
363  C CA  . ALA A 53  ? 0.28032 0.35124 0.29507 -0.05588 0.04845  0.10229  53  ALA A CA  
364  C C   . ALA A 53  ? 0.35003 0.40596 0.36806 -0.06054 0.04681  0.10994  53  ALA A C   
365  O O   . ALA A 53  ? 0.33869 0.39299 0.37300 -0.06352 0.04374  0.10694  53  ALA A O   
366  C CB  . ALA A 53  ? 0.32739 0.41005 0.34587 -0.06098 0.06041  0.10223  53  ALA A CB  
367  N N   . PRO A 54  ? 0.37643 0.42011 0.37793 -0.06172 0.04906  0.11998  54  PRO A N   
368  C CA  . PRO A 54  ? 0.39792 0.42354 0.40026 -0.06671 0.04845  0.12747  54  PRO A CA  
369  C C   . PRO A 54  ? 0.40672 0.43760 0.42784 -0.07762 0.05469  0.12668  54  PRO A C   
370  O O   . PRO A 54  ? 0.37989 0.42417 0.40535 -0.08272 0.06396  0.12723  54  PRO A O   
371  C CB  . PRO A 54  ? 0.39887 0.41308 0.37870 -0.06648 0.05252  0.13893  54  PRO A CB  
372  C CG  . PRO A 54  ? 0.46608 0.49040 0.43182 -0.05827 0.05002  0.13660  54  PRO A CG  
373  C CD  . PRO A 54  ? 0.47738 0.52157 0.45692 -0.05874 0.05214  0.12520  54  PRO A CD  
374  N N   . GLY A 55  ? 0.39214 0.41349 0.42462 -0.08126 0.04960  0.12510  55  GLY A N   
375  C CA  . GLY A 55  ? 0.36432 0.39280 0.41588 -0.09252 0.05400  0.12413  55  GLY A CA  
376  C C   . GLY A 55  ? 0.45425 0.50707 0.52597 -0.09207 0.05471  0.11500  55  GLY A C   
377  O O   . GLY A 55  ? 0.39548 0.46010 0.48447 -0.10089 0.05946  0.11485  55  GLY A O   
378  N N   . GLY A 56  ? 0.39432 0.45509 0.46457 -0.08212 0.05018  0.10777  56  GLY A N   
379  C CA  . GLY A 56  ? 0.33129 0.41240 0.41790 -0.07994 0.05119  0.09955  56  GLY A CA  
380  C C   . GLY A 56  ? 0.38619 0.46763 0.48706 -0.07890 0.04201  0.09285  56  GLY A C   
381  O O   . GLY A 56  ? 0.29319 0.35966 0.39290 -0.08144 0.03559  0.09403  56  GLY A O   
382  N N   . LEU A 57  ? 0.32559 0.42313 0.43857 -0.07467 0.04175  0.08566  57  LEU A N   
383  C CA  . LEU A 57  ? 0.29406 0.39446 0.42133 -0.07406 0.03373  0.07970  57  LEU A CA  
384  C C   . LEU A 57  ? 0.27658 0.36179 0.39284 -0.06779 0.02423  0.07647  57  LEU A C   
385  O O   . LEU A 57  ? 0.27828 0.35491 0.39895 -0.07026 0.01733  0.07498  57  LEU A O   
386  C CB  . LEU A 57  ? 0.32539 0.44518 0.46613 -0.06944 0.03624  0.07374  57  LEU A CB  
387  C CG  . LEU A 57  ? 0.37748 0.50116 0.53114 -0.06718 0.02777  0.06775  57  LEU A CG  
388  C CD1 . LEU A 57  ? 0.31856 0.44357 0.48618 -0.07681 0.02410  0.06998  57  LEU A CD1 
389  C CD2 . LEU A 57  ? 0.43075 0.57147 0.59517 -0.06093 0.03130  0.06300  57  LEU A CD2 
390  N N   . GLY A 58  ? 0.25242 0.33524 0.35462 -0.05994 0.02385  0.07492  58  GLY A N   
391  C CA  . GLY A 58  ? 0.22301 0.29401 0.31580 -0.05381 0.01561  0.07245  58  GLY A CA  
392  C C   . GLY A 58  ? 0.26913 0.32159 0.35544 -0.05642 0.01192  0.07749  58  GLY A C   
393  O O   . GLY A 58  ? 0.28868 0.33221 0.37619 -0.05457 0.00517  0.07434  58  GLY A O   
394  N N   . GLU A 59  ? 0.27636 0.32114 0.35455 -0.06072 0.01690  0.08546  59  GLU A N   
395  C CA  . GLU A 59  ? 0.30922 0.33275 0.37963 -0.06310 0.01428  0.09078  59  GLU A CA  
396  C C   . GLU A 59  ? 0.30639 0.32500 0.38949 -0.07159 0.01177  0.08850  59  GLU A C   
397  O O   . GLU A 59  ? 0.32643 0.32717 0.40484 -0.07133 0.00662  0.08801  59  GLU A O   
398  C CB  . GLU A 59  ? 0.30957 0.32491 0.36773 -0.06655 0.02091  0.10062  59  GLU A CB  
399  C CG  . GLU A 59  ? 0.27418 0.28933 0.31532 -0.05697 0.02033  0.10351  59  GLU A CG  
400  C CD  . GLU A 59  ? 0.41834 0.42180 0.44338 -0.05838 0.02518  0.11427  59  GLU A CD  
401  O OE1 . GLU A 59  ? 0.50482 0.50007 0.53162 -0.06764 0.03048  0.11976  59  GLU A OE1 
402  O OE2 . GLU A 59  ? 0.47948 0.48293 0.48982 -0.05054 0.02357  0.11741  59  GLU A OE2 
403  N N   . THR A 60  ? 0.30294 0.33750 0.40189 -0.07921 0.01543  0.08707  60  THR A N   
404  C CA  . THR A 60  ? 0.30608 0.34013 0.41865 -0.08811 0.01186  0.08435  60  THR A CA  
405  C C   . THR A 60  ? 0.28116 0.31485 0.39739 -0.08262 0.00306  0.07623  60  THR A C   
406  O O   . THR A 60  ? 0.28755 0.30747 0.40306 -0.08652 -0.00247 0.07415  60  THR A O   
407  C CB  . THR A 60  ? 0.34147 0.39840 0.47272 -0.09578 0.01739  0.08461  60  THR A CB  
408  O OG1 . THR A 60  ? 0.32826 0.38336 0.45597 -0.10318 0.02612  0.09267  60  THR A OG1 
409  C CG2 . THR A 60  ? 0.34276 0.40481 0.49027 -0.10416 0.01179  0.08072  60  THR A CG2 
410  N N   . LEU A 61  ? 0.20401 0.25139 0.32277 -0.07402 0.00210  0.07144  61  LEU A N   
411  C CA  . LEU A 61  ? 0.28391 0.33111 0.40505 -0.06872 -0.00550 0.06423  61  LEU A CA  
412  C C   . LEU A 61  ? 0.27211 0.29931 0.37807 -0.06277 -0.01002 0.06377  61  LEU A C   
413  O O   . LEU A 61  ? 0.28534 0.30415 0.39114 -0.06231 -0.01607 0.05929  61  LEU A O   
414  C CB  . LEU A 61  ? 0.20319 0.26730 0.32875 -0.06124 -0.00438 0.05988  61  LEU A CB  
415  C CG  . LEU A 61  ? 0.24517 0.32971 0.38735 -0.06492 0.00011  0.05961  61  LEU A CG  
416  C CD1 . LEU A 61  ? 0.21269 0.30896 0.35471 -0.05674 0.00324  0.05606  61  LEU A CD1 
417  C CD2 . LEU A 61  ? 0.25379 0.34428 0.41055 -0.06984 -0.00575 0.05655  61  LEU A CD2 
418  N N   . GLN A 62  ? 0.25935 0.27979 0.35222 -0.05748 -0.00710 0.06838  62  GLN A N   
419  C CA  . GLN A 62  ? 0.21922 0.22217 0.29881 -0.05063 -0.01078 0.06909  62  GLN A CA  
420  C C   . GLN A 62  ? 0.36453 0.34557 0.44025 -0.05633 -0.01261 0.07084  62  GLN A C   
421  O O   . GLN A 62  ? 0.29845 0.26674 0.36940 -0.05248 -0.01732 0.06703  62  GLN A O   
422  C CB  . GLN A 62  ? 0.30932 0.31123 0.37649 -0.04461 -0.00745 0.07525  62  GLN A CB  
423  C CG  . GLN A 62  ? 0.34409 0.33052 0.39860 -0.03588 -0.01088 0.07737  62  GLN A CG  
424  C CD  . GLN A 62  ? 0.32744 0.32353 0.38242 -0.02705 -0.01510 0.07143  62  GLN A CD  
425  O OE1 . GLN A 62  ? 0.27016 0.28092 0.33401 -0.02818 -0.01581 0.06532  62  GLN A OE1 
426  N NE2 . GLN A 62  ? 0.29613 0.28432 0.34176 -0.01799 -0.01757 0.07359  62  GLN A NE2 
427  N N   . GLN A 63  ? 0.26569 0.24126 0.34275 -0.06612 -0.00841 0.07626  63  GLN A N   
428  C CA  . GLN A 63  ? 0.37111 0.32430 0.44416 -0.07360 -0.01001 0.07709  63  GLN A CA  
429  C C   . GLN A 63  ? 0.33693 0.29237 0.41940 -0.07845 -0.01614 0.06883  63  GLN A C   
430  O O   . GLN A 63  ? 0.32406 0.25939 0.39853 -0.07835 -0.02007 0.06574  63  GLN A O   
431  C CB  . GLN A 63  ? 0.43401 0.38319 0.50846 -0.08539 -0.00400 0.08415  63  GLN A CB  
432  C CG  . GLN A 63  ? 0.74595 0.66393 0.80831 -0.09097 -0.00395 0.08759  63  GLN A CG  
433  C CD  . GLN A 63  ? 0.88670 0.78305 0.93073 -0.07786 -0.00511 0.09022  63  GLN A CD  
434  O OE1 . GLN A 63  ? 0.61663 0.51629 0.65284 -0.06907 -0.00232 0.09609  63  GLN A OE1 
435  N NE2 . GLN A 63  ? 0.65609 0.53118 0.69318 -0.07618 -0.00932 0.08574  63  GLN A NE2 
436  N N   . LYS A 64  ? 0.30182 0.28112 0.40016 -0.08181 -0.01706 0.06514  64  LYS A N   
437  C CA  . LYS A 64  ? 0.26205 0.24528 0.36856 -0.08545 -0.02380 0.05785  64  LYS A CA  
438  C C   . LYS A 64  ? 0.34782 0.32439 0.44589 -0.07462 -0.02872 0.05212  64  LYS A C   
439  O O   . LYS A 64  ? 0.28310 0.25029 0.37894 -0.07674 -0.03433 0.04667  64  LYS A O   
440  C CB  . LYS A 64  ? 0.29276 0.30434 0.41811 -0.08881 -0.02345 0.05630  64  LYS A CB  
441  C CG  . LYS A 64  ? 0.39735 0.41714 0.53499 -0.10259 -0.02009 0.06041  64  LYS A CG  
442  C CD  . LYS A 64  ? 0.56138 0.61154 0.71903 -0.10343 -0.01916 0.05923  64  LYS A CD  
443  C CE  . LYS A 64  ? 0.52733 0.59033 0.69904 -0.11595 -0.01407 0.06416  64  LYS A CE  
444  N NZ  . LYS A 64  ? 0.49493 0.55241 0.67242 -0.13006 -0.01953 0.06280  64  LYS A NZ  
445  N N   . LEU A 65  ? 0.27176 0.25397 0.36487 -0.06365 -0.02663 0.05304  65  LEU A N   
446  C CA  . LEU A 65  ? 0.26057 0.23844 0.34679 -0.05398 -0.03047 0.04802  65  LEU A CA  
447  C C   . LEU A 65  ? 0.29597 0.24813 0.36757 -0.05041 -0.03130 0.04871  65  LEU A C   
448  O O   . LEU A 65  ? 0.29942 0.24285 0.36588 -0.04654 -0.03506 0.04324  65  LEU A O   
449  C CB  . LEU A 65  ? 0.22457 0.21703 0.31039 -0.04482 -0.02806 0.04870  65  LEU A CB  
450  C CG  . LEU A 65  ? 0.23676 0.22855 0.31686 -0.03519 -0.03097 0.04418  65  LEU A CG  
451  C CD1 . LEU A 65  ? 0.26378 0.25800 0.34896 -0.03723 -0.03573 0.03741  65  LEU A CD1 
452  C CD2 . LEU A 65  ? 0.19985 0.20796 0.28088 -0.02938 -0.02841 0.04490  65  LEU A CD2 
453  N N   . LEU A 66  ? 0.32123 0.25993 0.38510 -0.05120 -0.02736 0.05553  66  LEU A N   
454  C CA  . LEU A 66  ? 0.38767 0.29938 0.43713 -0.04691 -0.02756 0.05662  66  LEU A CA  
455  C C   . LEU A 66  ? 0.40210 0.29532 0.44922 -0.05681 -0.03038 0.05226  66  LEU A C   
456  O O   . LEU A 66  ? 0.36388 0.23641 0.39974 -0.05228 -0.03197 0.04885  66  LEU A O   
457  C CB  . LEU A 66  ? 0.33411 0.23444 0.37452 -0.04469 -0.02260 0.06606  66  LEU A CB  
458  C CG  . LEU A 66  ? 0.39658 0.31263 0.43564 -0.03436 -0.02069 0.07049  66  LEU A CG  
459  C CD1 . LEU A 66  ? 0.43867 0.34603 0.46992 -0.03561 -0.01595 0.08038  66  LEU A CD1 
460  C CD2 . LEU A 66  ? 0.37893 0.29173 0.41118 -0.02060 -0.02307 0.06841  66  LEU A CD2 
461  N N   . GLU A 67  ? 0.36312 0.26362 0.42044 -0.07046 -0.03089 0.05211  67  GLU A N   
462  C CA  . GLU A 67  ? 0.34303 0.22961 0.39912 -0.08141 -0.03507 0.04675  67  GLU A CA  
463  C C   . GLU A 67  ? 0.30597 0.19995 0.36396 -0.07796 -0.04126 0.03799  67  GLU A C   
464  O O   . GLU A 67  ? 0.36562 0.24029 0.41376 -0.08028 -0.04470 0.03240  67  GLU A O   
465  C CB  . GLU A 67  ? 0.38820 0.28635 0.45760 -0.09724 -0.03471 0.04881  67  GLU A CB  
466  C CG  . GLU A 67  ? 0.47033 0.36192 0.53772 -0.10214 -0.02766 0.05798  67  GLU A CG  
467  C CD  . GLU A 67  ? 0.75137 0.66546 0.83643 -0.11510 -0.02547 0.06095  67  GLU A CD  
468  O OE1 . GLU A 67  ? 0.56520 0.50128 0.66552 -0.11984 -0.02987 0.05616  67  GLU A OE1 
469  O OE2 . GLU A 67  ? 0.66750 0.57791 0.75118 -0.11999 -0.01894 0.06866  67  GLU A OE2 
470  N N   . ARG A 68  ? 0.32864 0.24883 0.39767 -0.07265 -0.04238 0.03669  68  ARG A N   
471  C CA  . ARG A 68  ? 0.31803 0.24520 0.38769 -0.06854 -0.04767 0.02942  68  ARG A CA  
472  C C   . ARG A 68  ? 0.31819 0.22885 0.37303 -0.05697 -0.04722 0.02655  68  ARG A C   
473  O O   . ARG A 68  ? 0.36688 0.26846 0.41481 -0.05657 -0.05112 0.02004  68  ARG A O   
474  C CB  . ARG A 68  ? 0.32719 0.28295 0.41016 -0.06436 -0.04764 0.02963  68  ARG A CB  
475  C CG  . ARG A 68  ? 0.34099 0.30448 0.42489 -0.06097 -0.05296 0.02313  68  ARG A CG  
476  C CD  . ARG A 68  ? 0.27011 0.25911 0.36671 -0.05749 -0.05243 0.02378  68  ARG A CD  
477  N NE  . ARG A 68  ? 0.24190 0.23692 0.33848 -0.05443 -0.05735 0.01857  68  ARG A NE  
478  C CZ  . ARG A 68  ? 0.32737 0.32979 0.43073 -0.06089 -0.06319 0.01619  68  ARG A CZ  
479  N NH1 . ARG A 68  ? 0.26724 0.27243 0.37878 -0.07168 -0.06523 0.01775  68  ARG A NH1 
480  N NH2 . ARG A 68  ? 0.32196 0.32998 0.42396 -0.05678 -0.06722 0.01255  68  ARG A NH2 
481  N N   . GLN A 69  ? 0.32958 0.23786 0.37953 -0.04714 -0.04249 0.03139  69  GLN A N   
482  C CA  . GLN A 69  ? 0.29973 0.19464 0.33753 -0.03536 -0.04150 0.02942  69  GLN A CA  
483  C C   . GLN A 69  ? 0.35876 0.22270 0.38250 -0.03779 -0.04176 0.02680  69  GLN A C   
484  O O   . GLN A 69  ? 0.41283 0.26527 0.42705 -0.03157 -0.04259 0.02129  69  GLN A O   
485  C CB  . GLN A 69  ? 0.32605 0.22545 0.36214 -0.02518 -0.03705 0.03626  69  GLN A CB  
486  C CG  . GLN A 69  ? 0.35440 0.24125 0.37953 -0.01207 -0.03546 0.03575  69  GLN A CG  
487  C CD  . GLN A 69  ? 0.40440 0.29293 0.42687 -0.00314 -0.03192 0.04398  69  GLN A CD  
488  O OE1 . GLN A 69  ? 0.38267 0.26251 0.40254 -0.00692 -0.02972 0.05056  69  GLN A OE1 
489  N NE2 . GLN A 69  ? 0.39897 0.30007 0.42218 0.00820  -0.03153 0.04396  69  GLN A NE2 
490  N N   . GLU A 70  ? 0.37905 0.22802 0.40040 -0.04740 -0.04050 0.03036  70  GLU A N   
491  C CA  . GLU A 70  ? 0.37137 0.18707 0.37726 -0.05029 -0.04014 0.02762  70  GLU A CA  
492  C C   . GLU A 70  ? 0.50253 0.31361 0.50626 -0.05962 -0.04592 0.01838  70  GLU A C   
493  O O   . GLU A 70  ? 0.49337 0.28087 0.48211 -0.05669 -0.04615 0.01272  70  GLU A O   
494  C CB  . GLU A 70  ? 0.48285 0.28192 0.48559 -0.05912 -0.03676 0.03434  70  GLU A CB  
495  C CG  . GLU A 70  ? 0.68196 0.44283 0.66738 -0.06412 -0.03597 0.03137  70  GLU A CG  
496  C CD  . GLU A 70  ? 1.00644 0.74536 0.98396 -0.06629 -0.03038 0.04014  70  GLU A CD  
497  O OE1 . GLU A 70  ? 1.24485 0.98795 1.22158 -0.05441 -0.02630 0.04807  70  GLU A OE1 
498  O OE2 . GLU A 70  ? 1.16410 0.88142 1.13553 -0.08036 -0.03024 0.03934  70  GLU A OE2 
499  N N   . LYS A 71  ? 0.45633 0.29065 0.47439 -0.06961 -0.05059 0.01669  71  LYS A N   
500  C CA  . LYS A 71  ? 0.45245 0.28594 0.46989 -0.08018 -0.05744 0.00896  71  LYS A CA  
501  C C   . LYS A 71  ? 0.48627 0.33085 0.50222 -0.07247 -0.06110 0.00277  71  LYS A C   
502  O O   . LYS A 71  ? 0.46379 0.30417 0.47483 -0.07942 -0.06698 -0.00400 71  LYS A O   
503  C CB  . LYS A 71  ? 0.49324 0.34925 0.52860 -0.09415 -0.06110 0.01103  71  LYS A CB  
504  C CG  . LYS A 71  ? 0.61374 0.46027 0.65164 -0.10597 -0.05791 0.01656  71  LYS A CG  
505  C CD  . LYS A 71  ? 0.81753 0.66116 0.85811 -0.12414 -0.06405 0.01211  71  LYS A CD  
506  C CE  . LYS A 71  ? 0.95654 0.81180 1.01166 -0.13747 -0.06176 0.01856  71  LYS A CE  
507  N NZ  . LYS A 71  ? 0.81178 0.66375 0.86948 -0.15673 -0.06774 0.01423  71  LYS A NZ  
508  N N   . THR A 72  ? 0.43772 0.29700 0.45748 -0.05937 -0.05804 0.00502  72  THR A N   
509  C CA  . THR A 72  ? 0.34772 0.21934 0.36718 -0.05282 -0.06065 0.00021  72  THR A CA  
510  C C   . THR A 72  ? 0.44095 0.30199 0.44919 -0.03853 -0.05567 -0.00068 72  THR A C   
511  O O   . THR A 72  ? 0.39209 0.24684 0.39869 -0.03163 -0.05047 0.00443  72  THR A O   
512  C CB  . THR A 72  ? 0.39922 0.30235 0.43590 -0.05123 -0.06138 0.00359  72  THR A CB  
513  O OG1 . THR A 72  ? 0.38508 0.29552 0.42613 -0.04312 -0.05547 0.00968  72  THR A OG1 
514  C CG2 . THR A 72  ? 0.41607 0.33368 0.46686 -0.06390 -0.06550 0.00536  72  THR A CG2 
515  N N   . ALA A 73  ? 0.38756 0.24840 0.38851 -0.03375 -0.05718 -0.00668 73  ALA A N   
516  C CA  . ALA A 73  ? 0.42771 0.28481 0.42142 -0.01975 -0.05185 -0.00720 73  ALA A CA  
517  C C   . ALA A 73  ? 0.39142 0.27318 0.39813 -0.01243 -0.04897 -0.00155 73  ALA A C   
518  O O   . ALA A 73  ? 0.34986 0.23074 0.35512 -0.00225 -0.04414 0.00171  73  ALA A O   
519  C CB  . ALA A 73  ? 0.45985 0.31281 0.44286 -0.01720 -0.05337 -0.01472 73  ALA A CB  
520  N N   . ASN A 74  ? 0.29333 0.19703 0.31254 -0.01748 -0.05199 -0.00029 74  ASN A N   
521  C CA  . ASN A 74  ? 0.30340 0.22928 0.33355 -0.01221 -0.04944 0.00401  74  ASN A CA  
522  C C   . ASN A 74  ? 0.34590 0.28732 0.38917 -0.02056 -0.05184 0.00706  74  ASN A C   
523  O O   . ASN A 74  ? 0.29871 0.24796 0.34614 -0.02589 -0.05606 0.00436  74  ASN A O   
524  C CB  . ASN A 74  ? 0.28658 0.22285 0.31534 -0.00640 -0.04901 0.00040  74  ASN A CB  
525  C CG  . ASN A 74  ? 0.30020 0.25787 0.33886 -0.00246 -0.04652 0.00381  74  ASN A CG  
526  O OD1 . ASN A 74  ? 0.27483 0.24429 0.32313 -0.00675 -0.04712 0.00711  74  ASN A OD1 
527  N ND2 . ASN A 74  ? 0.29496 0.25787 0.33090 0.00536  -0.04336 0.00262  74  ASN A ND2 
528  N N   . TRP A 75  ? 0.24768 0.19445 0.29720 -0.02087 -0.04890 0.01297  75  TRP A N   
529  C CA  . TRP A 75  ? 0.28536 0.24550 0.34696 -0.02876 -0.04983 0.01603  75  TRP A CA  
530  C C   . TRP A 75  ? 0.28131 0.26276 0.35229 -0.02741 -0.05028 0.01530  75  TRP A C   
531  O O   . TRP A 75  ? 0.24257 0.23569 0.32401 -0.03319 -0.05134 0.01675  75  TRP A O   
532  C CB  . TRP A 75  ? 0.24446 0.20422 0.30812 -0.02893 -0.04558 0.02271  75  TRP A CB  
533  C CG  . TRP A 75  ? 0.28023 0.24468 0.34066 -0.01894 -0.04180 0.02566  75  TRP A CG  
534  C CD1 . TRP A 75  ? 0.28942 0.24073 0.34031 -0.01133 -0.03979 0.02749  75  TRP A CD1 
535  C CD2 . TRP A 75  ? 0.22269 0.20684 0.28939 -0.01560 -0.03986 0.02715  75  TRP A CD2 
536  N NE1 . TRP A 75  ? 0.25245 0.21700 0.30470 -0.00372 -0.03753 0.03030  75  TRP A NE1 
537  C CE2 . TRP A 75  ? 0.24855 0.23237 0.30962 -0.00707 -0.03756 0.02981  75  TRP A CE2 
538  C CE3 . TRP A 75  ? 0.21283 0.21418 0.28884 -0.01879 -0.03978 0.02633  75  TRP A CE3 
539  C CZ2 . TRP A 75  ? 0.24890 0.24974 0.31298 -0.00328 -0.03587 0.03117  75  TRP A CZ2 
540  C CZ3 . TRP A 75  ? 0.22443 0.23952 0.30197 -0.01453 -0.03712 0.02738  75  TRP A CZ3 
541  C CH2 . TRP A 75  ? 0.23982 0.25477 0.31122 -0.00768 -0.03556 0.02953  75  TRP A CH2 
542  N N   . VAL A 76  ? 0.23009 0.21689 0.29792 -0.02004 -0.04902 0.01325  76  VAL A N   
543  C CA  . VAL A 76  ? 0.20499 0.20869 0.28006 -0.01912 -0.04871 0.01272  76  VAL A CA  
544  C C   . VAL A 76  ? 0.29830 0.30224 0.37087 -0.01917 -0.05241 0.00824  76  VAL A C   
545  O O   . VAL A 76  ? 0.27267 0.28821 0.35125 -0.01926 -0.05277 0.00818  76  VAL A O   
546  C CB  . VAL A 76  ? 0.22393 0.23620 0.29833 -0.01280 -0.04439 0.01416  76  VAL A CB  
547  C CG1 . VAL A 76  ? 0.19955 0.20997 0.26686 -0.00698 -0.04397 0.01062  76  VAL A CG1 
548  C CG2 . VAL A 76  ? 0.19192 0.21948 0.27468 -0.01432 -0.04256 0.01529  76  VAL A CG2 
549  N N   . SER A 77  ? 0.25416 0.24441 0.31687 -0.01901 -0.05498 0.00463  77  SER A N   
550  C CA  . SER A 77  ? 0.27880 0.26841 0.33589 -0.01807 -0.05793 0.00058  77  SER A CA  
551  C C   . SER A 77  ? 0.23773 0.23840 0.30315 -0.02239 -0.06219 0.00120  77  SER A C   
552  O O   . SER A 77  ? 0.26200 0.26998 0.32781 -0.01942 -0.06197 0.00082  77  SER A O   
553  C CB  . SER A 77  ? 0.30277 0.27465 0.34724 -0.01929 -0.06064 -0.00366 77  SER A CB  
554  O OG  . SER A 77  ? 0.29718 0.25917 0.33336 -0.01274 -0.05595 -0.00446 77  SER A OG  
555  N N   . GLU A 78  ? 0.24497 0.24671 0.31694 -0.02936 -0.06610 0.00232  78  GLU A N   
556  C CA  . GLU A 78  ? 0.23990 0.25415 0.32116 -0.03280 -0.07095 0.00322  78  GLU A CA  
557  C C   . GLU A 78  ? 0.29308 0.32279 0.38544 -0.02909 -0.06684 0.00669  78  GLU A C   
558  O O   . GLU A 78  ? 0.22445 0.26123 0.31857 -0.02596 -0.06812 0.00679  78  GLU A O   
559  C CB  . GLU A 78  ? 0.31242 0.32761 0.40071 -0.04196 -0.07552 0.00402  78  GLU A CB  
560  C CG  . GLU A 78  ? 0.29535 0.32761 0.39636 -0.04524 -0.08099 0.00571  78  GLU A CG  
561  C CD  . GLU A 78  ? 0.42896 0.46593 0.53972 -0.05564 -0.08509 0.00685  78  GLU A CD  
562  O OE1 . GLU A 78  ? 0.45640 0.48324 0.56512 -0.06044 -0.08219 0.00726  78  GLU A OE1 
563  O OE2 . GLU A 78  ? 0.59160 0.64293 0.71236 -0.05911 -0.09122 0.00776  78  GLU A OE2 
564  N N   . TYR A 79  ? 0.23694 0.27031 0.33509 -0.02908 -0.06151 0.00957  79  TYR A N   
565  C CA  . TYR A 79  ? 0.24232 0.28862 0.34913 -0.02598 -0.05689 0.01211  79  TYR A CA  
566  C C   . TYR A 79  ? 0.19910 0.24450 0.29889 -0.01976 -0.05399 0.01034  79  TYR A C   
567  O O   . TYR A 79  ? 0.21422 0.26712 0.31825 -0.01708 -0.05239 0.01094  79  TYR A O   
568  C CB  . TYR A 79  ? 0.20271 0.25103 0.31302 -0.02712 -0.05144 0.01517  79  TYR A CB  
569  C CG  . TYR A 79  ? 0.21322 0.26162 0.33006 -0.03415 -0.05260 0.01766  79  TYR A CG  
570  C CD1 . TYR A 79  ? 0.18680 0.24365 0.31406 -0.03947 -0.05703 0.01820  79  TYR A CD1 
571  C CD2 . TYR A 79  ? 0.24068 0.28145 0.35361 -0.03580 -0.04922 0.02007  79  TYR A CD2 
572  C CE1 . TYR A 79  ? 0.25796 0.31583 0.39212 -0.04779 -0.05772 0.02056  79  TYR A CE1 
573  C CE2 . TYR A 79  ? 0.22845 0.26754 0.34659 -0.04348 -0.04952 0.02283  79  TYR A CE2 
574  C CZ  . TYR A 79  ? 0.24090 0.28871 0.36976 -0.04992 -0.05351 0.02279  79  TYR A CZ  
575  O OH  . TYR A 79  ? 0.26704 0.31346 0.40116 -0.05886 -0.05342 0.02546  79  TYR A OH  
576  N N   . TRP A 80  ? 0.18456 0.22083 0.27391 -0.01739 -0.05260 0.00834  80  TRP A N   
577  C CA  . TRP A 80  ? 0.22735 0.26421 0.31081 -0.01289 -0.04926 0.00674  80  TRP A CA  
578  C C   . TRP A 80  ? 0.21693 0.25159 0.29575 -0.01156 -0.05213 0.00488  80  TRP A C   
579  O O   . TRP A 80  ? 0.21995 0.25773 0.29810 -0.00925 -0.04954 0.00483  80  TRP A O   
580  C CB  . TRP A 80  ? 0.21987 0.25037 0.29533 -0.01041 -0.04707 0.00554  80  TRP A CB  
581  C CG  . TRP A 80  ? 0.23771 0.27141 0.30874 -0.00717 -0.04350 0.00402  80  TRP A CG  
582  C CD1 . TRP A 80  ? 0.25012 0.29178 0.32343 -0.00652 -0.03941 0.00482  80  TRP A CD1 
583  C CD2 . TRP A 80  ? 0.23600 0.26514 0.29882 -0.00521 -0.04355 0.00122  80  TRP A CD2 
584  N NE1 . TRP A 80  ? 0.22988 0.27281 0.29803 -0.00503 -0.03716 0.00264  80  TRP A NE1 
585  C CE2 . TRP A 80  ? 0.21881 0.25427 0.28077 -0.00400 -0.03921 0.00071  80  TRP A CE2 
586  C CE3 . TRP A 80  ? 0.30809 0.32828 0.36330 -0.00501 -0.04674 -0.00100 80  TRP A CE3 
587  C CZ2 . TRP A 80  ? 0.26965 0.30352 0.32467 -0.00281 -0.03732 -0.00149 80  TRP A CZ2 
588  C CZ3 . TRP A 80  ? 0.22753 0.24540 0.27450 -0.00294 -0.04469 -0.00317 80  TRP A CZ3 
589  C CH2 . TRP A 80  ? 0.28674 0.31174 0.33431 -0.00193 -0.03972 -0.00317 80  TRP A CH2 
590  N N   . LEU A 81  ? 0.19396 0.22164 0.26769 -0.01325 -0.05738 0.00328  81  LEU A N   
591  C CA  . LEU A 81  ? 0.21867 0.24397 0.28620 -0.01199 -0.06071 0.00213  81  LEU A CA  
592  C C   . LEU A 81  ? 0.25477 0.28949 0.33140 -0.01124 -0.06229 0.00500  81  LEU A C   
593  O O   . LEU A 81  ? 0.25108 0.28530 0.32382 -0.00789 -0.06116 0.00550  81  LEU A O   
594  C CB  . LEU A 81  ? 0.22558 0.24225 0.28560 -0.01500 -0.06694 -0.00024 81  LEU A CB  
595  C CG  . LEU A 81  ? 0.31273 0.32683 0.36470 -0.01441 -0.07198 -0.00106 81  LEU A CG  
596  C CD1 . LEU A 81  ? 0.36698 0.37540 0.40745 -0.01019 -0.06742 -0.00242 81  LEU A CD1 
597  C CD2 . LEU A 81  ? 0.39036 0.39620 0.43465 -0.01902 -0.07876 -0.00401 81  LEU A CD2 
598  N N   . ASN A 82  ? 0.21341 0.25654 0.30224 -0.01407 -0.06441 0.00722  82  ASN A N   
599  C CA  . ASN A 82  ? 0.23913 0.29327 0.33871 -0.01206 -0.06522 0.01030  82  ASN A CA  
600  C C   . ASN A 82  ? 0.26026 0.31709 0.36213 -0.00792 -0.05752 0.01121  82  ASN A C   
601  O O   . ASN A 82  ? 0.22636 0.28414 0.32819 -0.00353 -0.05644 0.01243  82  ASN A O   
602  C CB  . ASN A 82  ? 0.21783 0.28263 0.33143 -0.01663 -0.06829 0.01247  82  ASN A CB  
603  C CG  . ASN A 82  ? 0.30727 0.37064 0.41913 -0.02181 -0.07707 0.01138  82  ASN A CG  
604  O OD1 . ASN A 82  ? 0.28677 0.34370 0.38804 -0.02048 -0.08169 0.00974  82  ASN A OD1 
605  N ND2 . ASN A 82  ? 0.27559 0.34476 0.39700 -0.02852 -0.07942 0.01224  82  ASN A ND2 
606  N N   . ASP A 83  ? 0.20928 0.26622 0.31189 -0.00926 -0.05217 0.01065  83  ASP A N   
607  C CA  . ASP A 83  ? 0.16882 0.22842 0.27264 -0.00661 -0.04517 0.01086  83  ASP A CA  
608  C C   . ASP A 83  ? 0.26673 0.31841 0.35931 -0.00420 -0.04235 0.00866  83  ASP A C   
609  O O   . ASP A 83  ? 0.20654 0.25747 0.29848 -0.00150 -0.03840 0.00877  83  ASP A O   
610  C CB  . ASP A 83  ? 0.28519 0.34718 0.39070 -0.00918 -0.04116 0.01104  83  ASP A CB  
611  C CG  . ASP A 83  ? 0.36331 0.42881 0.46958 -0.00752 -0.03432 0.01089  83  ASP A CG  
612  O OD1 . ASP A 83  ? 0.25928 0.33136 0.37395 -0.00607 -0.03205 0.01255  83  ASP A OD1 
613  O OD2 . ASP A 83  ? 0.27087 0.33309 0.36929 -0.00774 -0.03116 0.00892  83  ASP A OD2 
614  N N   . MET A 84  ? 0.20234 0.24755 0.28572 -0.00532 -0.04347 0.00657  84  MET A N   
615  C CA  . MET A 84  ? 0.18938 0.22888 0.26304 -0.00436 -0.04004 0.00462  84  MET A CA  
616  C C   . MET A 84  ? 0.25705 0.29026 0.32465 -0.00211 -0.04236 0.00527  84  MET A C   
617  O O   . MET A 84  ? 0.27521 0.30359 0.33715 -0.00107 -0.03846 0.00498  84  MET A O   
618  C CB  . MET A 84  ? 0.20468 0.24204 0.27228 -0.00563 -0.03962 0.00258  84  MET A CB  
619  C CG  . MET A 84  ? 0.45352 0.48732 0.51219 -0.00564 -0.03618 0.00060  84  MET A CG  
620  S SD  . MET A 84  ? 0.57269 0.61029 0.63207 -0.00753 -0.02985 -0.00029 84  MET A SD  
621  C CE  . MET A 84  ? 0.23362 0.28008 0.30071 -0.00826 -0.02975 0.00055  84  MET A CE  
622  N N   . TYR A 85  ? 0.21958 0.25192 0.28709 -0.00181 -0.04881 0.00627  85  TYR A N   
623  C CA  . TYR A 85  ? 0.25759 0.28358 0.31671 0.00037  -0.05206 0.00727  85  TYR A CA  
624  C C   . TYR A 85  ? 0.22021 0.25147 0.28647 0.00269  -0.05809 0.01062  85  TYR A C   
625  O O   . TYR A 85  ? 0.25596 0.28551 0.32140 0.00696  -0.05732 0.01327  85  TYR A O   
626  C CB  . TYR A 85  ? 0.28591 0.30530 0.33409 -0.00136 -0.05506 0.00494  85  TYR A CB  
627  C CG  . TYR A 85  ? 0.30019 0.31682 0.34267 -0.00256 -0.04940 0.00209  85  TYR A CG  
628  C CD1 . TYR A 85  ? 0.38784 0.40026 0.42247 -0.00225 -0.04423 0.00161  85  TYR A CD1 
629  C CD2 . TYR A 85  ? 0.30667 0.32517 0.35179 -0.00402 -0.04923 0.00025  85  TYR A CD2 
630  C CE1 . TYR A 85  ? 0.57123 0.58472 0.60281 -0.00363 -0.03933 -0.00077 85  TYR A CE1 
631  C CE2 . TYR A 85  ? 0.30909 0.32748 0.35047 -0.00387 -0.04445 -0.00172 85  TYR A CE2 
632  C CZ  . TYR A 85  ? 0.44299 0.46048 0.47853 -0.00380 -0.03970 -0.00231 85  TYR A CZ  
633  O OH  . TYR A 85  ? 0.52695 0.54790 0.56098 -0.00388 -0.03515 -0.00408 85  TYR A OH  
634  N N   . LEU A 86  ? 0.19615 0.23314 0.26834 -0.00006 -0.06448 0.01070  86  LEU A N   
635  C CA  . LEU A 86  ? 0.24677 0.28946 0.32308 0.00139  -0.07216 0.01364  86  LEU A CA  
636  C C   . LEU A 86  ? 0.25237 0.30622 0.34331 0.00562  -0.07075 0.01753  86  LEU A C   
637  O O   . LEU A 86  ? 0.28204 0.34057 0.37582 0.00980  -0.07558 0.02111  86  LEU A O   
638  C CB  . LEU A 86  ? 0.34365 0.38976 0.42243 -0.00442 -0.07947 0.01209  86  LEU A CB  
639  C CG  . LEU A 86  ? 0.32029 0.35350 0.38351 -0.00761 -0.08003 0.00770  86  LEU A CG  
640  C CD1 . LEU A 86  ? 0.30183 0.33594 0.36578 -0.01371 -0.08789 0.00591  86  LEU A CD1 
641  C CD2 . LEU A 86  ? 0.35042 0.37356 0.39718 -0.00429 -0.07996 0.00744  86  LEU A CD2 
642  N N   . ASN A 87  ? 0.23968 0.29836 0.33970 0.00524  -0.06412 0.01714  87  ASN A N   
643  C CA  . ASN A 87  ? 0.21478 0.28306 0.32754 0.01026  -0.06112 0.02040  87  ASN A CA  
644  C C   . ASN A 87  ? 0.25815 0.31677 0.36334 0.01664  -0.05505 0.02114  87  ASN A C   
645  O O   . ASN A 87  ? 0.24936 0.31285 0.36247 0.02297  -0.05293 0.02419  87  ASN A O   
646  C CB  . ASN A 87  ? 0.27620 0.35265 0.39990 0.00737  -0.05562 0.01970  87  ASN A CB  
647  C CG  . ASN A 87  ? 0.29270 0.37963 0.42671 0.00115  -0.06096 0.02026  87  ASN A CG  
648  O OD1 . ASN A 87  ? 0.29050 0.38223 0.42713 -0.00053 -0.06926 0.02143  87  ASN A OD1 
649  N ND2 . ASN A 87  ? 0.29436 0.38439 0.43333 -0.00290 -0.05633 0.01953  87  ASN A ND2 
650  N N   . ASN A 88  ? 0.21988 0.26474 0.31009 0.01505  -0.05174 0.01844  88  ASN A N   
651  C CA  . ASN A 88  ? 0.24942 0.28290 0.33116 0.01883  -0.04497 0.01843  88  ASN A CA  
652  C C   . ASN A 88  ? 0.22935 0.25782 0.30686 0.02553  -0.04853 0.02284  88  ASN A C   
653  O O   . ASN A 88  ? 0.30460 0.33016 0.37437 0.02482  -0.05492 0.02398  88  ASN A O   
654  C CB  . ASN A 88  ? 0.24322 0.26601 0.31136 0.01377  -0.04113 0.01456  88  ASN A CB  
655  C CG  . ASN A 88  ? 0.32319 0.33369 0.38225 0.01496  -0.03341 0.01366  88  ASN A CG  
656  O OD1 . ASN A 88  ? 0.36094 0.36707 0.42113 0.02066  -0.03085 0.01607  88  ASN A OD1 
657  N ND2 . ASN A 88  ? 0.37613 0.38078 0.42599 0.00950  -0.02952 0.01019  88  ASN A ND2 
658  N N   . ARG A 89  ? 0.20620 0.23326 0.28799 0.03263  -0.04440 0.02555  89  ARG A N   
659  C CA  . ARG A 89  ? 0.20526 0.22853 0.28452 0.04093  -0.04796 0.03103  89  ARG A CA  
660  C C   . ARG A 89  ? 0.27021 0.27199 0.33074 0.04246  -0.04334 0.03148  89  ARG A C   
661  O O   . ARG A 89  ? 0.26670 0.26197 0.32108 0.04905  -0.04656 0.03659  89  ARG A O   
662  C CB  . ARG A 89  ? 0.27238 0.30487 0.36647 0.04982  -0.04538 0.03455  89  ARG A CB  
663  C CG  . ARG A 89  ? 0.30992 0.36549 0.42451 0.04783  -0.04855 0.03462  89  ARG A CG  
664  C CD  . ARG A 89  ? 0.30449 0.37405 0.42583 0.04691  -0.06072 0.03801  89  ARG A CD  
665  N NE  . ARG A 89  ? 0.28911 0.35401 0.40009 0.03749  -0.06584 0.03441  89  ARG A NE  
666  C CZ  . ARG A 89  ? 0.30675 0.37357 0.41262 0.03568  -0.07569 0.03588  89  ARG A CZ  
667  N NH1 . ARG A 89  ? 0.27709 0.35079 0.38630 0.04249  -0.08270 0.04150  89  ARG A NH1 
668  N NH2 . ARG A 89  ? 0.32264 0.38422 0.41907 0.02732  -0.07861 0.03166  89  ARG A NH2 
669  N N   . LEU A 90  ? 0.28834 0.27934 0.33969 0.03636  -0.03591 0.02669  90  LEU A N   
670  C CA  . LEU A 90  ? 0.29349 0.26380 0.32763 0.03637  -0.03042 0.02702  90  LEU A CA  
671  C C   . LEU A 90  ? 0.26183 0.22617 0.28313 0.03438  -0.03571 0.02909  90  LEU A C   
672  O O   . LEU A 90  ? 0.30290 0.27675 0.32570 0.02983  -0.04146 0.02739  90  LEU A O   
673  C CB  . LEU A 90  ? 0.27395 0.23771 0.30256 0.02826  -0.02217 0.02093  90  LEU A CB  
674  C CG  . LEU A 90  ? 0.31362 0.27730 0.34864 0.02964  -0.01498 0.01821  90  LEU A CG  
675  C CD1 . LEU A 90  ? 0.33626 0.29848 0.36646 0.01981  -0.00959 0.01190  90  LEU A CD1 
676  C CD2 . LEU A 90  ? 0.39468 0.34100 0.42255 0.03703  -0.00939 0.02084  90  LEU A CD2 
677  N N   . ALA A 91  ? 0.23322 0.17983 0.24014 0.03765  -0.03297 0.03264  91  ALA A N   
678  C CA  . ALA A 91  ? 0.28386 0.22257 0.27554 0.03545  -0.03644 0.03480  91  ALA A CA  
679  C C   . ALA A 91  ? 0.31102 0.25079 0.29738 0.02501  -0.03332 0.02891  91  ALA A C   
680  O O   . ALA A 91  ? 0.32178 0.25937 0.30919 0.01952  -0.02602 0.02446  91  ALA A O   
681  C CB  . ALA A 91  ? 0.29302 0.20952 0.26858 0.03972  -0.03175 0.03969  91  ALA A CB  
682  N N   . LEU A 92  ? 0.29008 0.23297 0.26976 0.02259  -0.03872 0.02894  92  LEU A N   
683  C CA  . LEU A 92  ? 0.25535 0.20092 0.23114 0.01436  -0.03564 0.02365  92  LEU A CA  
684  C C   . LEU A 92  ? 0.32407 0.25682 0.28776 0.00876  -0.02632 0.02237  92  LEU A C   
685  O O   . LEU A 92  ? 0.30694 0.24579 0.27509 0.00236  -0.02155 0.01739  92  LEU A O   
686  C CB  . LEU A 92  ? 0.26638 0.21555 0.23537 0.01385  -0.04266 0.02373  92  LEU A CB  
687  C CG  . LEU A 92  ? 0.28229 0.24523 0.26322 0.01638  -0.05220 0.02369  92  LEU A CG  
688  C CD1 . LEU A 92  ? 0.28943 0.25271 0.26007 0.01455  -0.05873 0.02259  92  LEU A CD1 
689  C CD2 . LEU A 92  ? 0.29634 0.27134 0.29346 0.01330  -0.05038 0.01925  92  LEU A CD2 
690  N N   . PRO A 93  ? 0.32819 0.24405 0.27685 0.01022  -0.02339 0.02678  93  PRO A N   
691  C CA  . PRO A 93  ? 0.29134 0.19566 0.22915 0.00278  -0.01397 0.02522  93  PRO A CA  
692  C C   . PRO A 93  ? 0.32276 0.22747 0.26895 -0.00129 -0.00768 0.02112  93  PRO A C   
693  O O   . PRO A 93  ? 0.29585 0.19655 0.24739 0.00398  -0.00766 0.02238  93  PRO A O   
694  C CB  . PRO A 93  ? 0.32456 0.20804 0.24542 0.00675  -0.01244 0.03204  93  PRO A CB  
695  C CG  . PRO A 93  ? 0.38531 0.27297 0.30558 0.01533  -0.02245 0.03682  93  PRO A CG  
696  C CD  . PRO A 93  ? 0.30444 0.21110 0.24464 0.01830  -0.02862 0.03387  93  PRO A CD  
697  N N   . VAL A 94  ? 0.35263 0.26287 0.29952 -0.01056 -0.00225 0.01619  94  VAL A N   
698  C CA  . VAL A 94  ? 0.31113 0.22208 0.26294 -0.01716 0.00391  0.01153  94  VAL A CA  
699  C C   . VAL A 94  ? 0.34452 0.27171 0.31278 -0.01464 0.00011  0.00829  94  VAL A C   
700  O O   . VAL A 94  ? 0.31299 0.25315 0.28844 -0.02059 0.00154  0.00371  94  VAL A O   
701  C CB  . VAL A 94  ? 0.29644 0.18529 0.23818 -0.01737 0.00997  0.01326  94  VAL A CB  
702  C CG1 . VAL A 94  ? 0.28299 0.17327 0.22958 -0.02461 0.01541  0.00718  94  VAL A CG1 
703  C CG2 . VAL A 94  ? 0.29550 0.16661 0.21928 -0.02244 0.01540  0.01643  94  VAL A CG2 
704  N N   . ASN A 95  ? 0.28530 0.21339 0.25998 -0.00580 -0.00486 0.01111  95  ASN A N   
705  C CA  . ASN A 95  ? 0.28135 0.22412 0.27118 -0.00390 -0.00745 0.00853  95  ASN A CA  
706  C C   . ASN A 95  ? 0.26198 0.22225 0.26019 -0.00565 -0.01241 0.00657  95  ASN A C   
707  O O   . ASN A 95  ? 0.31187 0.28401 0.32009 -0.00757 -0.01252 0.00352  95  ASN A O   
708  C CB  . ASN A 95  ? 0.24451 0.18674 0.24100 0.00585  -0.01129 0.01244  95  ASN A CB  
709  C CG  . ASN A 95  ? 0.30727 0.23134 0.29622 0.00983  -0.00590 0.01458  95  ASN A CG  
710  O OD1 . ASN A 95  ? 0.29219 0.20952 0.27931 0.00626  0.00088  0.01086  95  ASN A OD1 
711  N ND2 . ASN A 95  ? 0.27947 0.19438 0.26285 0.01756  -0.00887 0.02062  95  ASN A ND2 
712  N N   . SER A 96  ? 0.27230 0.23309 0.26540 -0.00462 -0.01638 0.00834  96  SER A N   
713  C CA  . SER A 96  ? 0.30230 0.27654 0.30255 -0.00463 -0.02138 0.00661  96  SER A CA  
714  C C   . SER A 96  ? 0.29963 0.27455 0.29182 -0.00820 -0.01995 0.00505  96  SER A C   
715  O O   . SER A 96  ? 0.26930 0.25470 0.26694 -0.01083 -0.01904 0.00188  96  SER A O   
716  C CB  . SER A 96  ? 0.28836 0.26490 0.29248 0.00145  -0.02940 0.00971  96  SER A CB  
717  O OG  . SER A 96  ? 0.30303 0.29023 0.31374 0.00060  -0.03391 0.00754  96  SER A OG  
718  N N   . SER A 97  ? 0.24426 0.20831 0.22320 -0.00744 -0.01969 0.00769  97  SER A N   
719  C CA  . SER A 97  ? 0.24277 0.20696 0.21263 -0.00945 -0.01854 0.00660  97  SER A CA  
720  C C   . SER A 97  ? 0.24267 0.20830 0.20953 -0.01621 -0.01003 0.00441  97  SER A C   
721  O O   . SER A 97  ? 0.28664 0.24119 0.24445 -0.01948 -0.00498 0.00633  97  SER A O   
722  C CB  . SER A 97  ? 0.28748 0.23919 0.24237 -0.00626 -0.02144 0.01074  97  SER A CB  
723  O OG  . SER A 97  ? 0.27666 0.23094 0.23471 -0.00104 -0.03049 0.01219  97  SER A OG  
724  N N   A PRO A 98  ? 0.26364 0.24269 0.23787 -0.01857 -0.00811 0.00077  98  PRO A N   
725  N N   B PRO A 98  ? 0.26379 0.24290 0.23804 -0.01855 -0.00813 0.00075  98  PRO A N   
726  C CA  A PRO A 98  ? 0.21003 0.19444 0.18343 -0.02537 -0.00041 -0.00110 98  PRO A CA  
727  C CA  B PRO A 98  ? 0.20612 0.19062 0.17946 -0.02531 -0.00043 -0.00111 98  PRO A CA  
728  C C   A PRO A 98  ? 0.27794 0.25538 0.23740 -0.02700 0.00392  0.00032  98  PRO A C   
729  C C   B PRO A 98  ? 0.27856 0.25554 0.23769 -0.02699 0.00391  0.00042  98  PRO A C   
730  O O   A PRO A 98  ? 0.27837 0.25025 0.22929 -0.02236 0.00068  0.00151  98  PRO A O   
731  O O   B PRO A 98  ? 0.27927 0.25012 0.22947 -0.02237 0.00065  0.00176  98  PRO A O   
732  C CB  A PRO A 98  ? 0.26734 0.26969 0.25321 -0.02477 -0.00100 -0.00440 98  PRO A CB  
733  C CB  B PRO A 98  ? 0.26743 0.26976 0.25283 -0.02459 -0.00096 -0.00440 98  PRO A CB  
734  C CG  A PRO A 98  ? 0.28226 0.28351 0.26881 -0.01781 -0.00761 -0.00422 98  PRO A CG  
735  C CG  B PRO A 98  ? 0.29523 0.29918 0.28873 -0.01920 -0.00811 -0.00430 98  PRO A CG  
736  C CD  A PRO A 98  ? 0.28140 0.27142 0.26512 -0.01500 -0.01282 -0.00142 98  PRO A CD  
737  C CD  B PRO A 98  ? 0.28142 0.27187 0.26589 -0.01510 -0.01280 -0.00147 98  PRO A CD  
738  N N   . ALA A 99  ? 0.25125 0.22909 0.20769 -0.03458 0.01157  0.00003  99  ALA A N   
739  C CA  . ALA A 99  ? 0.28011 0.25279 0.22371 -0.03773 0.01766  0.00151  99  ALA A CA  
740  C C   . ALA A 99  ? 0.33450 0.32656 0.28673 -0.04188 0.02343  -0.00174 99  ALA A C   
741  O O   . ALA A 99  ? 0.27977 0.28571 0.24510 -0.04623 0.02456  -0.00421 99  ALA A O   
742  C CB  . ALA A 99  ? 0.34390 0.29962 0.27574 -0.04390 0.02277  0.00474  99  ALA A CB  
743  N N   . VAL A 100 ? 0.30484 0.29878 0.24968 -0.03992 0.02688  -0.00169 100 VAL A N   
744  C CA  . VAL A 100 ? 0.28537 0.29770 0.23708 -0.04304 0.03405  -0.00396 100 VAL A CA  
745  C C   . VAL A 100 ? 0.28431 0.28925 0.22214 -0.04946 0.04278  -0.00159 100 VAL A C   
746  O O   . VAL A 100 ? 0.34642 0.33631 0.26745 -0.04598 0.04283  0.00072  100 VAL A O   
747  C CB  . VAL A 100 ? 0.34470 0.36578 0.29949 -0.03407 0.03220  -0.00635 100 VAL A CB  
748  C CG1 . VAL A 100 ? 0.32553 0.36735 0.28861 -0.03596 0.04072  -0.00818 100 VAL A CG1 
749  C CG2 . VAL A 100 ? 0.35339 0.37827 0.31983 -0.02813 0.02350  -0.00789 100 VAL A CG2 
750  N N   . ILE A 101 ? 0.25519 0.27080 0.19926 -0.05943 0.04998  -0.00203 101 ILE A N   
751  C CA  . ILE A 101 ? 0.27825 0.28642 0.20981 -0.06797 0.05923  0.00062  101 ILE A CA  
752  C C   . ILE A 101 ? 0.34148 0.37128 0.27940 -0.06894 0.06733  -0.00106 101 ILE A C   
753  O O   . ILE A 101 ? 0.30540 0.35990 0.26226 -0.07043 0.06822  -0.00397 101 ILE A O   
754  C CB  . ILE A 101 ? 0.31568 0.31932 0.24893 -0.08041 0.06250  0.00115  101 ILE A CB  
755  C CG1 . ILE A 101 ? 0.35816 0.33768 0.28312 -0.07809 0.05605  0.00316  101 ILE A CG1 
756  C CG2 . ILE A 101 ? 0.36054 0.36012 0.28296 -0.09109 0.07363  0.00371  101 ILE A CG2 
757  C CD1 . ILE A 101 ? 0.33391 0.31981 0.27232 -0.07135 0.04673  0.00038  101 ILE A CD1 
758  N N   . PHE A 102 ? 0.31787 0.33941 0.24004 -0.06757 0.07335  0.00098  102 PHE A N   
759  C CA  . PHE A 102 ? 0.34550 0.38762 0.27326 -0.06755 0.08243  -0.00061 102 PHE A CA  
760  C C   . PHE A 102 ? 0.44559 0.49726 0.37636 -0.08176 0.09285  0.00092  102 PHE A C   
761  O O   . PHE A 102 ? 0.45162 0.48905 0.37608 -0.09173 0.09340  0.00326  102 PHE A O   
762  C CB  . PHE A 102 ? 0.34861 0.37871 0.25694 -0.06008 0.08565  0.00025  102 PHE A CB  
763  C CG  . PHE A 102 ? 0.33213 0.35169 0.23523 -0.04772 0.07574  -0.00166 102 PHE A CG  
764  C CD1 . PHE A 102 ? 0.32286 0.35124 0.24269 -0.04222 0.06705  -0.00450 102 PHE A CD1 
765  C CD2 . PHE A 102 ? 0.37225 0.37255 0.25257 -0.04246 0.07489  -0.00049 102 PHE A CD2 
766  C CE1 . PHE A 102 ? 0.39619 0.41430 0.31122 -0.03247 0.05823  -0.00618 102 PHE A CE1 
767  C CE2 . PHE A 102 ? 0.37596 0.36677 0.25135 -0.03279 0.06518  -0.00267 102 PHE A CE2 
768  C CZ  . PHE A 102 ? 0.38915 0.38865 0.28226 -0.02815 0.05708  -0.00551 102 PHE A CZ  
769  N N   . ALA A 103 ? 0.49315 0.56853 0.43307 -0.08263 0.10183  -0.00036 103 ALA A N   
770  C CA  . ALA A 103 ? 0.56199 0.64856 0.50433 -0.09678 0.11315  0.00133  103 ALA A CA  
771  C C   . ALA A 103 ? 0.57643 0.63349 0.49294 -0.10383 0.11825  0.00614  103 ALA A C   
772  O O   . ALA A 103 ? 0.58955 0.62409 0.48557 -0.09560 0.11600  0.00824  103 ALA A O   
773  C CB  . ALA A 103 ? 0.60417 0.71883 0.55713 -0.09373 0.12297  -0.00007 103 ALA A CB  
774  N N   . ARG A 104 ? 0.52280 0.57904 0.43960 -0.11957 0.12454  0.00804  104 ARG A N   
775  C CA  . ARG A 104 ? 0.62838 0.65661 0.52071 -0.12765 0.13101  0.01343  104 ARG A CA  
776  C C   . ARG A 104 ? 0.63546 0.66479 0.51405 -0.12429 0.14099  0.01575  104 ARG A C   
777  O O   . ARG A 104 ? 0.56485 0.62288 0.45743 -0.12451 0.14868  0.01344  104 ARG A O   
778  C CB  . ARG A 104 ? 0.63870 0.66998 0.53638 -0.14692 0.13783  0.01420  104 ARG A CB  
779  C CG  . ARG A 104 ? 0.80884 0.80586 0.68084 -0.15663 0.14370  0.02018  104 ARG A CG  
780  C CD  . ARG A 104 ? 0.98554 0.98679 0.86694 -0.17314 0.14744  0.01933  104 ARG A CD  
781  N NE  . ARG A 104 ? 0.79297 0.78829 0.68223 -0.17798 0.13964  0.01591  104 ARG A NE  
782  C CZ  . ARG A 104 ? 0.83963 0.86296 0.75321 -0.17958 0.13427  0.01008  104 ARG A CZ  
783  N NH1 . ARG A 104 ? 0.95312 1.01341 0.88749 -0.17603 0.13540  0.00737  104 ARG A NH1 
784  N NH2 . ARG A 104 ? 0.66134 0.67485 0.57781 -0.18377 0.12742  0.00708  104 ARG A NH2 
785  N N   . GLN A 105 ? 0.56578 0.56461 0.41676 -0.12026 0.14077  0.02040  105 GLN A N   
786  C CA  . GLN A 105 ? 0.62299 0.61856 0.45591 -0.11732 0.15020  0.02285  105 GLN A CA  
787  C C   . GLN A 105 ? 0.57478 0.54851 0.38592 -0.13007 0.15990  0.02975  105 GLN A C   
788  O O   . GLN A 105 ? 0.65355 0.60597 0.45796 -0.13732 0.15676  0.03311  105 GLN A O   
789  C CB  . GLN A 105 ? 0.54543 0.52377 0.36079 -0.10134 0.14159  0.02263  105 GLN A CB  
790  C CG  . GLN A 105 ? 0.53485 0.52993 0.36804 -0.08841 0.13225  0.01614  105 GLN A CG  
791  C CD  . GLN A 105 ? 0.59310 0.62069 0.44478 -0.08636 0.14092  0.01161  105 GLN A CD  
792  O OE1 . GLN A 105 ? 0.59920 0.63304 0.44269 -0.08897 0.15345  0.01274  105 GLN A OE1 
793  N NE2 . GLN A 105 ? 0.62343 0.67231 0.50020 -0.08123 0.13471  0.00690  105 GLN A NE2 
794  N N   . HIS A 106 ? 0.59876 0.57599 0.39848 -0.13134 0.17118  0.03200  106 HIS A N   
795  C CA  . HIS A 106 ? 0.63254 0.58950 0.41533 -0.13907 0.17652  0.03863  106 HIS A CA  
796  C C   . HIS A 106 ? 0.69632 0.63648 0.45087 -0.13019 0.17921  0.04227  106 HIS A C   
797  O O   . HIS A 106 ? 0.67742 0.63566 0.43406 -0.12445 0.18551  0.03947  106 HIS A O   
798  C CB  . HIS A 106 ? 0.73070 0.71135 0.53327 -0.15076 0.18569  0.03817  106 HIS A CB  
799  C CG  . HIS A 106 ? 1.02639 0.98666 0.81106 -0.15904 0.19225  0.04485  106 HIS A CG  
800  N ND1 . HIS A 106 ? 1.06102 1.03476 0.84563 -0.16205 0.20331  0.04681  106 HIS A ND1 
801  C CD2 . HIS A 106 ? 1.01944 0.94601 0.78494 -0.16407 0.18959  0.05034  106 HIS A CD2 
802  C CE1 . HIS A 106 ? 0.99789 0.94730 0.76392 -0.16962 0.20714  0.05319  106 HIS A CE1 
803  N NE2 . HIS A 106 ? 1.00434 0.92447 0.75844 -0.17060 0.19886  0.05541  106 HIS A NE2 
804  N N   . PHE A 107 ? 0.73997 0.64575 0.46823 -0.12828 0.17395  0.04846  107 PHE A N   
805  C CA  . PHE A 107 ? 0.68900 0.57572 0.38778 -0.11957 0.17359  0.05250  107 PHE A CA  
806  C C   . PHE A 107 ? 0.70959 0.57574 0.39160 -0.12702 0.17873  0.06048  107 PHE A C   
807  O O   . PHE A 107 ? 0.76201 0.60088 0.43134 -0.12805 0.17257  0.06599  107 PHE A O   
808  C CB  . PHE A 107 ? 0.69420 0.55905 0.37578 -0.10855 0.16049  0.05349  107 PHE A CB  
809  C CG  . PHE A 107 ? 0.58931 0.47283 0.28970 -0.09978 0.15248  0.04532  107 PHE A CG  
810  C CD1 . PHE A 107 ? 0.66613 0.57838 0.38279 -0.09687 0.15862  0.03825  107 PHE A CD1 
811  C CD2 . PHE A 107 ? 0.56522 0.43938 0.27193 -0.09211 0.13666  0.04447  107 PHE A CD2 
812  C CE1 . PHE A 107 ? 0.62833 0.55714 0.36555 -0.08674 0.14900  0.03082  107 PHE A CE1 
813  C CE2 . PHE A 107 ? 0.58674 0.47883 0.31455 -0.08299 0.12722  0.03688  107 PHE A CE2 
814  C CZ  . PHE A 107 ? 0.63250 0.55083 0.37497 -0.08043 0.13329  0.03018  107 PHE A CZ  
815  N N   . PRO A 108 ? 0.81736 0.69542 0.49913 -0.13199 0.19023  0.06161  108 PRO A N   
816  C CA  . PRO A 108 ? 0.76357 0.62034 0.42690 -0.13899 0.19550  0.06965  108 PRO A CA  
817  C C   . PRO A 108 ? 0.89866 0.72228 0.52958 -0.13026 0.18785  0.07625  108 PRO A C   
818  O O   . PRO A 108 ? 0.80885 0.60665 0.42751 -0.13378 0.18529  0.08291  108 PRO A O   
819  C CB  . PRO A 108 ? 0.77655 0.65543 0.44372 -0.14221 0.20870  0.06893  108 PRO A CB  
820  C CG  . PRO A 108 ? 0.81512 0.73064 0.51362 -0.14201 0.21133  0.06069  108 PRO A CG  
821  C CD  . PRO A 108 ? 0.78729 0.69994 0.48804 -0.13187 0.19951  0.05592  108 PRO A CD  
822  N N   . GLY A 109 ? 0.88721 0.71105 0.50404 -0.11838 0.18350  0.07435  109 GLY A N   
823  C CA  . GLY A 109 ? 0.71913 0.51562 0.30658 -0.10929 0.17438  0.08007  109 GLY A CA  
824  C C   . GLY A 109 ? 0.75274 0.54717 0.33840 -0.09760 0.16090  0.07600  109 GLY A C   
825  O O   . GLY A 109 ? 0.72010 0.53409 0.32552 -0.09593 0.15969  0.06833  109 GLY A O   
826  N N   . THR A 110 ? 0.75266 0.52368 0.31442 -0.08938 0.15031  0.08157  110 THR A N   
827  C CA  . THR A 110 ? 0.77652 0.54449 0.33376 -0.07811 0.13612  0.07852  110 THR A CA  
828  C C   . THR A 110 ? 0.70848 0.49524 0.26695 -0.07268 0.13774  0.06949  110 THR A C   
829  O O   . THR A 110 ? 0.77204 0.56702 0.34028 -0.06713 0.13034  0.06315  110 THR A O   
830  C CB  . THR A 110 ? 0.80240 0.54556 0.33366 -0.07040 0.12483  0.08661  110 THR A CB  
831  O OG1 . THR A 110 ? 0.86997 0.59497 0.40153 -0.07406 0.12384  0.09466  110 THR A OG1 
832  C CG2 . THR A 110 ? 0.89231 0.63421 0.42040 -0.05928 0.10872  0.08361  110 THR A CG2 
833  N N   . ASP A 111 ? 0.77399 0.56683 0.32204 -0.07381 0.14766  0.06867  111 ASP A N   
834  C CA  . ASP A 111 ? 0.70611 0.51446 0.25366 -0.06750 0.14984  0.05972  111 ASP A CA  
835  C C   . ASP A 111 ? 0.74353 0.57792 0.32088 -0.06951 0.15645  0.05150  111 ASP A C   
836  O O   . ASP A 111 ? 0.78287 0.62782 0.36389 -0.06212 0.15439  0.04322  111 ASP A O   
837  C CB  . ASP A 111 ? 0.76635 0.57612 0.29714 -0.06838 0.16047  0.06081  111 ASP A CB  
838  C CG  . ASP A 111 ? 0.98467 0.77071 0.48363 -0.06411 0.15228  0.06740  111 ASP A CG  
839  O OD1 . ASP A 111 ? 0.95993 0.73238 0.45020 -0.05780 0.13688  0.06887  111 ASP A OD1 
840  O OD2 . ASP A 111 ? 0.98957 0.77204 0.47287 -0.06694 0.16098  0.07129  111 ASP A OD2 
841  N N   . ASP A 112 ? 0.70570 0.55063 0.30481 -0.07932 0.16378  0.05340  112 ASP A N   
842  C CA  . ASP A 112 ? 0.74316 0.61450 0.37264 -0.08118 0.16809  0.04611  112 ASP A CA  
843  C C   . ASP A 112 ? 0.67738 0.54478 0.31439 -0.07635 0.15545  0.04293  112 ASP A C   
844  O O   . ASP A 112 ? 0.67970 0.56448 0.33315 -0.06972 0.15272  0.03480  112 ASP A O   
845  C CB  . ASP A 112 ? 0.75715 0.64177 0.40790 -0.09409 0.17789  0.04890  112 ASP A CB  
846  C CG  . ASP A 112 ? 0.81030 0.69979 0.45408 -0.09931 0.19064  0.05240  112 ASP A CG  
847  O OD1 . ASP A 112 ? 0.75194 0.65781 0.39627 -0.09410 0.19790  0.04787  112 ASP A OD1 
848  O OD2 . ASP A 112 ? 0.80292 0.67864 0.43957 -0.10804 0.19355  0.05968  112 ASP A OD2 
849  N N   . GLN A 113 ? 0.64464 0.49077 0.27384 -0.07782 0.14594  0.04920  113 GLN A N   
850  C CA  . GLN A 113 ? 0.59570 0.44078 0.23870 -0.06970 0.12889  0.04618  113 GLN A CA  
851  C C   . GLN A 113 ? 0.66972 0.51363 0.30206 -0.05768 0.11923  0.04089  113 GLN A C   
852  O O   . GLN A 113 ? 0.60826 0.46620 0.26090 -0.05137 0.11137  0.03351  113 GLN A O   
853  C CB  . GLN A 113 ? 0.65877 0.47892 0.29077 -0.07089 0.12052  0.05484  113 GLN A CB  
854  C CG  . GLN A 113 ? 0.57231 0.39137 0.21866 -0.06240 0.10318  0.05273  113 GLN A CG  
855  C CD  . GLN A 113 ? 0.67462 0.46716 0.30216 -0.05904 0.09401  0.06185  113 GLN A CD  
856  O OE1 . GLN A 113 ? 0.72140 0.49439 0.32109 -0.06121 0.09892  0.06980  113 GLN A OE1 
857  N NE2 . GLN A 113 ? 0.62296 0.41498 0.26553 -0.05318 0.08101  0.06124  113 GLN A NE2 
858  N N   . LEU A 114 ? 0.63682 0.46293 0.23586 -0.05498 0.11966  0.04458  114 LEU A N   
859  C CA  . LEU A 114 ? 0.71266 0.53468 0.29784 -0.04500 0.10958  0.03942  114 LEU A CA  
860  C C   . LEU A 114 ? 0.70774 0.54882 0.30273 -0.04143 0.11727  0.02916  114 LEU A C   
861  O O   . LEU A 114 ? 0.67466 0.51938 0.27507 -0.03364 0.10761  0.02193  114 LEU A O   
862  C CB  . LEU A 114 ? 0.72281 0.52325 0.27137 -0.04344 0.10766  0.04570  114 LEU A CB  
863  C CG  . LEU A 114 ? 0.66848 0.44932 0.20751 -0.04354 0.09720  0.05610  114 LEU A CG  
864  C CD1 . LEU A 114 ? 0.73003 0.49626 0.24126 -0.03852 0.08952  0.06031  114 LEU A CD1 
865  C CD2 . LEU A 114 ? 0.64117 0.42395 0.19971 -0.03909 0.08233  0.05499  114 LEU A CD2 
866  N N   . ARG A 115 ? 0.68419 0.53763 0.28208 -0.04687 0.13493  0.02849  115 ARG A N   
867  C CA  . ARG A 115 ? 0.62807 0.50123 0.23789 -0.04194 0.14318  0.01912  115 ARG A CA  
868  C C   . ARG A 115 ? 0.61609 0.50979 0.26335 -0.03881 0.13695  0.01326  115 ARG A C   
869  O O   . ARG A 115 ? 0.61625 0.51858 0.27130 -0.03044 0.13495  0.00513  115 ARG A O   
870  C CB  . ARG A 115 ? 0.65467 0.54315 0.26902 -0.04749 0.16141  0.02033  115 ARG A CB  
871  C CG  . ARG A 115 ? 0.66582 0.54449 0.25385 -0.04446 0.16534  0.02111  115 ARG A CG  
872  C CD  . ARG A 115 ? 0.81007 0.70818 0.40676 -0.04809 0.18269  0.02127  115 ARG A CD  
873  N NE  . ARG A 115 ? 0.80086 0.70163 0.40581 -0.05978 0.18891  0.02981  115 ARG A NE  
874  C CZ  . ARG A 115 ? 0.87569 0.76156 0.46090 -0.06504 0.19145  0.03760  115 ARG A CZ  
875  N NH1 . ARG A 115 ? 0.73371 0.60296 0.28964 -0.05985 0.18860  0.03834  115 ARG A NH1 
876  N NH2 . ARG A 115 ? 0.80750 0.69476 0.40232 -0.07607 0.19681  0.04467  115 ARG A NH2 
877  N N   . PHE A 116 ? 0.54954 0.44983 0.21872 -0.04547 0.13423  0.01728  116 PHE A N   
878  C CA  . PHE A 116 ? 0.51441 0.43260 0.21688 -0.04282 0.12709  0.01249  116 PHE A CA  
879  C C   . PHE A 116 ? 0.54994 0.45717 0.25063 -0.03421 0.10977  0.00941  116 PHE A C   
880  O O   . PHE A 116 ? 0.50467 0.42324 0.22137 -0.02741 0.10550  0.00255  116 PHE A O   
881  C CB  . PHE A 116 ? 0.55969 0.48358 0.28114 -0.05280 0.12756  0.01745  116 PHE A CB  
882  C CG  . PHE A 116 ? 0.50131 0.44721 0.25720 -0.05172 0.12299  0.01272  116 PHE A CG  
883  C CD1 . PHE A 116 ? 0.47703 0.41786 0.24245 -0.04640 0.10790  0.01116  116 PHE A CD1 
884  C CD2 . PHE A 116 ? 0.61793 0.59082 0.39659 -0.05615 0.13380  0.01026  116 PHE A CD2 
885  C CE1 . PHE A 116 ? 0.49314 0.45326 0.28803 -0.04539 0.10390  0.00725  116 PHE A CE1 
886  C CE2 . PHE A 116 ? 0.52574 0.51911 0.33451 -0.05480 0.12880  0.00646  116 PHE A CE2 
887  C CZ  . PHE A 116 ? 0.48727 0.47309 0.30293 -0.04941 0.11405  0.00500  116 PHE A CZ  
888  N N   . ALA A 117 ? 0.61094 0.49637 0.29245 -0.03439 0.09964  0.01487  117 ALA A N   
889  C CA  . ALA A 117 ? 0.51209 0.38901 0.19260 -0.02730 0.08286  0.01250  117 ALA A CA  
890  C C   . ALA A 117 ? 0.56807 0.44150 0.23314 -0.02005 0.08136  0.00524  117 ALA A C   
891  O O   . ALA A 117 ? 0.59520 0.47129 0.27031 -0.01448 0.07152  -0.00050 117 ALA A O   
892  C CB  . ALA A 117 ? 0.57637 0.43263 0.23893 -0.02847 0.07316  0.02077  117 ALA A CB  
893  N N   . ALA A 118 ? 0.56167 0.42782 0.20103 -0.02049 0.09157  0.00523  118 ALA A N   
894  C CA  . ALA A 118 ? 0.62800 0.48919 0.25019 -0.01391 0.09218  -0.00267 118 ALA A CA  
895  C C   . ALA A 118 ? 0.65776 0.53767 0.30387 -0.00896 0.09874  -0.01103 118 ALA A C   
896  O O   . ALA A 118 ? 0.58764 0.46470 0.23446 -0.00247 0.09179  -0.01827 118 ALA A O   
897  C CB  . ALA A 118 ? 0.62421 0.47462 0.21374 -0.01581 0.10414  -0.00066 118 ALA A CB  
898  N N   . SER A 119 ? 0.65285 0.55211 0.31873 -0.01213 0.11209  -0.00981 119 SER A N   
899  C CA  . SER A 119 ? 0.61516 0.53524 0.30649 -0.00667 0.11826  -0.01632 119 SER A CA  
900  C C   . SER A 119 ? 0.58111 0.50655 0.29699 -0.00354 0.10454  -0.01857 119 SER A C   
901  O O   . SER A 119 ? 0.55018 0.47897 0.27376 0.00429  0.10261  -0.02537 119 SER A O   
902  C CB  . SER A 119 ? 0.66821 0.61095 0.37827 -0.01240 0.13331  -0.01312 119 SER A CB  
903  O OG  . SER A 119 ? 0.61494 0.58096 0.35233 -0.00675 0.13830  -0.01812 119 SER A OG  
904  N N   . LEU A 120 ? 0.49151 0.41648 0.21886 -0.00938 0.09555  -0.01284 120 LEU A N   
905  C CA  . LEU A 120 ? 0.50178 0.43133 0.25109 -0.00697 0.08282  -0.01440 120 LEU A CA  
906  C C   . LEU A 120 ? 0.63636 0.55005 0.37238 -0.00095 0.07051  -0.01900 120 LEU A C   
907  O O   . LEU A 120 ? 0.54966 0.46840 0.30021 0.00425  0.06554  -0.02408 120 LEU A O   
908  C CB  . LEU A 120 ? 0.44383 0.37176 0.20229 -0.01409 0.07614  -0.00736 120 LEU A CB  
909  C CG  . LEU A 120 ? 0.52696 0.45987 0.30784 -0.01251 0.06377  -0.00810 120 LEU A CG  
910  C CD1 . LEU A 120 ? 0.54368 0.49818 0.35106 -0.00934 0.06790  -0.01276 120 LEU A CD1 
911  C CD2 . LEU A 120 ? 0.48927 0.41955 0.27715 -0.01929 0.05994  -0.00140 120 LEU A CD2 
912  N N   . ILE A 121 ? 0.54940 0.44369 0.25759 -0.00219 0.06485  -0.01691 121 ILE A N   
913  C CA  . ILE A 121 ? 0.58017 0.46036 0.27534 0.00168  0.05199  -0.02132 121 ILE A CA  
914  C C   . ILE A 121 ? 0.58737 0.46567 0.27543 0.00800  0.05788  -0.03053 121 ILE A C   
915  O O   . ILE A 121 ? 0.55945 0.43470 0.25373 0.01178  0.04993  -0.03612 121 ILE A O   
916  C CB  . ILE A 121 ? 0.60733 0.46903 0.27247 -0.00095 0.04495  -0.01692 121 ILE A CB  
917  C CG1 . ILE A 121 ? 0.49641 0.35769 0.17051 -0.00483 0.03613  -0.00823 121 ILE A CG1 
918  C CG2 . ILE A 121 ? 0.52973 0.37785 0.17729 0.00208  0.03339  -0.02303 121 ILE A CG2 
919  C CD1 . ILE A 121 ? 0.54344 0.38844 0.18805 -0.00723 0.03343  -0.00108 121 ILE A CD1 
920  N N   . SER A 122 ? 0.60903 0.48875 0.28438 0.00935  0.07277  -0.03221 122 SER A N   
921  C CA  . SER A 122 ? 0.61295 0.49060 0.28174 0.01678  0.08051  -0.04109 122 SER A CA  
922  C C   . SER A 122 ? 0.60150 0.49502 0.30169 0.02217  0.08153  -0.04442 122 SER A C   
923  O O   . SER A 122 ? 0.57986 0.46543 0.27828 0.02828  0.07828  -0.05143 122 SER A O   
924  C CB  . SER A 122 ? 0.60331 0.48358 0.25653 0.01754  0.09829  -0.04136 122 SER A CB  
925  O OG  . SER A 122 ? 0.85176 0.73198 0.50176 0.02621  0.10771  -0.04984 122 SER A OG  
926  N N   . GLY A 123 ? 0.53323 0.44814 0.26141 0.01961  0.08546  -0.03932 123 GLY A N   
927  C CA  . GLY A 123 ? 0.51025 0.44115 0.26790 0.02459  0.08499  -0.04141 123 GLY A CA  
928  C C   . GLY A 123 ? 0.65242 0.57552 0.41851 0.02483  0.06907  -0.04242 123 GLY A C   
929  O O   . GLY A 123 ? 0.50167 0.42775 0.28087 0.03109  0.06755  -0.04647 123 GLY A O   
930  N N   . VAL A 124 ? 0.53547 0.44891 0.29459 0.01837  0.05744  -0.03828 124 VAL A N   
931  C CA  . VAL A 124 ? 0.48821 0.39480 0.25417 0.01798  0.04245  -0.03908 124 VAL A CA  
932  C C   . VAL A 124 ? 0.52632 0.41482 0.27351 0.02209  0.03817  -0.04671 124 VAL A C   
933  O O   . VAL A 124 ? 0.53712 0.42372 0.29504 0.02504  0.03243  -0.05035 124 VAL A O   
934  C CB  . VAL A 124 ? 0.56352 0.46496 0.32547 0.01118  0.03192  -0.03251 124 VAL A CB  
935  C CG1 . VAL A 124 ? 0.52492 0.41612 0.28521 0.01076  0.01643  -0.03425 124 VAL A CG1 
936  C CG2 . VAL A 124 ? 0.41679 0.33445 0.20273 0.00724  0.03364  -0.02619 124 VAL A CG2 
937  N N   . LEU A 125 ? 0.52767 0.40145 0.24517 0.02185  0.04132  -0.04940 125 LEU A N   
938  C CA  . LEU A 125 ? 0.63420 0.48860 0.32998 0.02488  0.03824  -0.05781 125 LEU A CA  
939  C C   . LEU A 125 ? 0.67204 0.52792 0.37573 0.03353  0.04815  -0.06445 125 LEU A C   
940  O O   . LEU A 125 ? 0.58370 0.42664 0.28396 0.03605  0.04264  -0.07058 125 LEU A O   
941  C CB  . LEU A 125 ? 0.67655 0.51606 0.33735 0.02306  0.04163  -0.05936 125 LEU A CB  
942  C CG  . LEU A 125 ? 0.72514 0.56030 0.37409 0.01584  0.03084  -0.05244 125 LEU A CG  
943  C CD1 . LEU A 125 ? 0.77831 0.59861 0.39052 0.01461  0.03509  -0.05363 125 LEU A CD1 
944  C CD2 . LEU A 125 ? 0.71552 0.54495 0.36900 0.01255  0.01273  -0.05306 125 LEU A CD2 
945  N N   . SER A 126 ? 0.60465 0.47620 0.31905 0.03821  0.06294  -0.06309 126 SER A N   
946  C CA  . SER A 126 ? 0.67437 0.54984 0.39826 0.04833  0.07298  -0.06834 126 SER A CA  
947  C C   . SER A 126 ? 0.56858 0.45326 0.32081 0.05069  0.06608  -0.06693 126 SER A C   
948  O O   . SER A 126 ? 0.58071 0.45523 0.33304 0.05749  0.06601  -0.07235 126 SER A O   
949  C CB  . SER A 126 ? 0.65792 0.55325 0.39040 0.05239  0.08989  -0.06608 126 SER A CB  
950  O OG  . SER A 126 ? 0.88060 0.76476 0.58412 0.05253  0.09905  -0.06903 126 SER A OG  
951  N N   . TYR A 127 ? 0.51389 0.41620 0.28880 0.04515  0.06075  -0.05963 127 TYR A N   
952  C CA  . TYR A 127 ? 0.49519 0.40701 0.29600 0.04675  0.05423  -0.05770 127 TYR A CA  
953  C C   . TYR A 127 ? 0.58754 0.47980 0.38074 0.04453  0.04099  -0.06095 127 TYR A C   
954  O O   . TYR A 127 ? 0.56125 0.45029 0.36432 0.04945  0.03908  -0.06327 127 TYR A O   
955  C CB  . TYR A 127 ? 0.48188 0.41376 0.30417 0.03993  0.05091  -0.04987 127 TYR A CB  
956  C CG  . TYR A 127 ? 0.45917 0.40518 0.30908 0.04224  0.04703  -0.04753 127 TYR A CG  
957  C CD1 . TYR A 127 ? 0.50868 0.47278 0.37616 0.04959  0.05623  -0.04724 127 TYR A CD1 
958  C CD2 . TYR A 127 ? 0.47812 0.42019 0.33614 0.03761  0.03434  -0.04542 127 TYR A CD2 
959  C CE1 . TYR A 127 ? 0.48088 0.45771 0.37148 0.05198  0.05232  -0.04469 127 TYR A CE1 
960  C CE2 . TYR A 127 ? 0.47162 0.42592 0.35292 0.03967  0.03131  -0.04311 127 TYR A CE2 
961  C CZ  . TYR A 127 ? 0.36038 0.33141 0.25692 0.04675  0.04002  -0.04267 127 TYR A CZ  
962  O OH  . TYR A 127 ? 0.46681 0.45023 0.38477 0.04924  0.03682  -0.03994 127 TYR A OH  
963  N N   . LYS A 128 ? 0.50533 0.38480 0.28089 0.03696  0.03169  -0.06076 128 LYS A N   
964  C CA  . LYS A 128 ? 0.53724 0.40026 0.30559 0.03326  0.01860  -0.06390 128 LYS A CA  
965  C C   . LYS A 128 ? 0.58513 0.42652 0.33410 0.03813  0.02143  -0.07301 128 LYS A C   
966  O O   . LYS A 128 ? 0.59732 0.42744 0.34814 0.03702  0.01372  -0.07613 128 LYS A O   
967  C CB  . LYS A 128 ? 0.57958 0.43663 0.33346 0.02477  0.00812  -0.06120 128 LYS A CB  
968  C CG  . LYS A 128 ? 0.65283 0.49908 0.40450 0.01947  -0.00662 -0.06314 128 LYS A CG  
969  C CD  . LYS A 128 ? 0.75123 0.59699 0.49355 0.01226  -0.01762 -0.05877 128 LYS A CD  
970  C CE  . LYS A 128 ? 0.73428 0.57805 0.48473 0.00672  -0.03243 -0.05872 128 LYS A CE  
971  N NZ  . LYS A 128 ? 0.90995 0.73421 0.64274 0.00505  -0.03642 -0.06764 128 LYS A NZ  
972  N N   . ALA A 129 ? 0.61929 0.45372 0.34938 0.04344  0.03317  -0.07752 129 ALA A N   
973  C CA  . ALA A 129 ? 0.65198 0.46421 0.36336 0.04943  0.03775  -0.08681 129 ALA A CA  
974  C C   . ALA A 129 ? 0.64927 0.46621 0.38094 0.05918  0.04417  -0.08747 129 ALA A C   
975  O O   . ALA A 129 ? 0.68033 0.47709 0.40385 0.06231  0.04263  -0.09354 129 ALA A O   
976  C CB  . ALA A 129 ? 0.66501 0.46884 0.35011 0.05342  0.04999  -0.09153 129 ALA A CB  
977  N N   . LEU A 130 ? 0.65279 0.49540 0.40953 0.06412  0.05166  -0.08128 130 LEU A N   
978  C CA  . LEU A 130 ? 0.68172 0.53264 0.46044 0.07338  0.05584  -0.08006 130 LEU A CA  
979  C C   . LEU A 130 ? 0.65718 0.50335 0.44836 0.06842  0.04269  -0.07795 130 LEU A C   
980  O O   . LEU A 130 ? 0.73128 0.56298 0.52233 0.07373  0.04227  -0.08113 130 LEU A O   
981  C CB  . LEU A 130 ? 0.58511 0.46830 0.38950 0.07689  0.06375  -0.07307 130 LEU A CB  
982  C CG  . LEU A 130 ? 0.72631 0.62008 0.52478 0.08276  0.07902  -0.07414 130 LEU A CG  
983  C CD1 . LEU A 130 ? 0.62457 0.55243 0.45022 0.08138  0.08350  -0.06640 130 LEU A CD1 
984  C CD2 . LEU A 130 ? 0.71827 0.60171 0.51018 0.09694  0.09008  -0.08011 130 LEU A CD2 
985  N N   . LEU A 131 ? 0.63993 0.49777 0.44167 0.05841  0.03261  -0.07226 131 LEU A N   
986  C CA  . LEU A 131 ? 0.55070 0.40617 0.36394 0.05211  0.01996  -0.06977 131 LEU A CA  
987  C C   . LEU A 131 ? 0.77610 0.60323 0.56947 0.04886  0.01313  -0.07670 131 LEU A C   
988  O O   . LEU A 131 ? 0.70191 0.51944 0.50131 0.05090  0.01073  -0.07784 131 LEU A O   
989  C CB  . LEU A 131 ? 0.61987 0.48873 0.44024 0.04222  0.01156  -0.06389 131 LEU A CB  
990  C CG  . LEU A 131 ? 0.76143 0.64139 0.60310 0.03657  0.00166  -0.05814 131 LEU A CG  
991  C CD1 . LEU A 131 ? 0.67990 0.57734 0.52976 0.03148  0.00059  -0.05198 131 LEU A CD1 
992  C CD2 . LEU A 131 ? 0.67417 0.53749 0.50665 0.02944  -0.01036 -0.06086 131 LEU A CD2 
993  N N   . ASP A 132 ? 0.76469 0.57745 0.53286 0.04327  0.00999  -0.08139 132 ASP A N   
994  C CA  . ASP A 132 ? 0.62556 0.41351 0.37466 0.03672  0.00086  -0.08789 132 ASP A CA  
995  C C   . ASP A 132 ? 0.81379 0.57793 0.54953 0.04414  0.00812  -0.09574 132 ASP A C   
996  O O   . ASP A 132 ? 0.86648 0.61026 0.59352 0.03896  0.00101  -0.10038 132 ASP A O   
997  C CB  . ASP A 132 ? 0.71102 0.49056 0.43459 0.02944  -0.00422 -0.09096 132 ASP A CB  
998  C CG  . ASP A 132 ? 0.86128 0.65870 0.59585 0.02114  -0.01467 -0.08328 132 ASP A CG  
999  O OD1 . ASP A 132 ? 1.00126 0.81436 0.76178 0.01935  -0.01956 -0.07693 132 ASP A OD1 
1000 O OD2 . ASP A 132 ? 1.07840 0.87348 0.79459 0.01704  -0.01754 -0.08342 132 ASP A OD2 
1001 N N   . SER A 133 ? 0.82003 0.58582 0.55361 0.05609  0.02251  -0.09736 133 SER A N   
1002 C CA  . SER A 133 ? 0.66672 0.41113 0.39055 0.06612  0.03122  -0.10377 133 SER A CA  
1003 C C   . SER A 133 ? 0.72717 0.48342 0.47807 0.07531  0.03512  -0.09802 133 SER A C   
1004 O O   . SER A 133 ? 0.78415 0.52816 0.53119 0.08738  0.04501  -0.10129 133 SER A O   
1005 C CB  . SER A 133 ? 0.79774 0.53664 0.50269 0.07565  0.04571  -0.10914 133 SER A CB  
1006 O OG  . SER A 133 ? 0.76271 0.53101 0.48863 0.08365  0.05544  -0.10248 133 SER A OG  
1007 N N   . HIS A 134 ? 0.75425 0.53404 0.53150 0.07064  0.02797  -0.08938 134 HIS A N   
1008 C CA  . HIS A 134 ? 0.76717 0.55817 0.56896 0.07777  0.02954  -0.08339 134 HIS A CA  
1009 C C   . HIS A 134 ? 0.68409 0.48742 0.49424 0.09352  0.04383  -0.08209 134 HIS A C   
1010 O O   . HIS A 134 ? 0.72258 0.51956 0.53895 0.10412  0.04853  -0.08134 134 HIS A O   
1011 C CB  . HIS A 134 ? 0.65743 0.42170 0.45285 0.07610  0.02422  -0.08638 134 HIS A CB  
1012 C CG  . HIS A 134 ? 0.76224 0.51064 0.54376 0.06084  0.01175  -0.09020 134 HIS A CG  
1013 N ND1 . HIS A 134 ? 0.72756 0.49273 0.52361 0.04938  0.00033  -0.08462 134 HIS A ND1 
1014 C CD2 . HIS A 134 ? 0.70976 0.42840 0.46423 0.05505  0.00881  -0.09918 134 HIS A CD2 
1015 C CE1 . HIS A 134 ? 0.73082 0.47959 0.51140 0.03763  -0.00938 -0.08938 134 HIS A CE1 
1016 N NE2 . HIS A 134 ? 0.72112 0.44154 0.47595 0.04001  -0.00494 -0.09840 134 HIS A NE2 
1017 N N   . SER A 135 ? 0.72992 0.55140 0.54028 0.09526  0.05103  -0.08140 135 SER A N   
1018 C CA  . SER A 135 ? 0.75386 0.58984 0.57176 0.10944  0.06532  -0.08064 135 SER A CA  
1019 C C   . SER A 135 ? 0.76051 0.63434 0.60887 0.11068  0.06659  -0.07166 135 SER A C   
1020 O O   . SER A 135 ? 0.80404 0.69615 0.66277 0.12141  0.07777  -0.07005 135 SER A O   
1021 C CB  . SER A 135 ? 0.73257 0.56295 0.52854 0.11085  0.07484  -0.08658 135 SER A CB  
1022 O OG  . SER A 135 ? 0.93903 0.73449 0.70410 0.10729  0.07229  -0.09548 135 SER A OG  
1023 N N   . ILE A 136 ? 0.56364 0.45018 0.42620 0.09976  0.05571  -0.06610 136 ILE A N   
1024 C CA  . ILE A 136 ? 0.70709 0.62733 0.59705 0.09945  0.05592  -0.05824 136 ILE A CA  
1025 C C   . ILE A 136 ? 0.66351 0.58943 0.57025 0.11028  0.05696  -0.05459 136 ILE A C   
1026 O O   . ILE A 136 ? 0.62715 0.53516 0.53155 0.10928  0.04975  -0.05454 136 ILE A O   
1027 C CB  . ILE A 136 ? 0.68050 0.60879 0.57794 0.08513  0.04443  -0.05409 136 ILE A CB  
1028 C CG1 . ILE A 136 ? 0.66682 0.58847 0.54639 0.07594  0.04341  -0.05681 136 ILE A CG1 
1029 C CG2 . ILE A 136 ? 0.64672 0.60718 0.57065 0.08412  0.04453  -0.04685 136 ILE A CG2 
1030 C CD1 . ILE A 136 ? 0.61052 0.55315 0.49417 0.07637  0.05299  -0.05490 136 ILE A CD1 
1031 N N   . PRO A 137 ? 0.65954 0.60991 0.58293 0.12075  0.06567  -0.05115 137 PRO A N   
1032 C CA  . PRO A 137 ? 0.62517 0.58158 0.56405 0.13228  0.06599  -0.04670 137 PRO A CA  
1033 C C   . PRO A 137 ? 0.57894 0.54389 0.53278 0.12389  0.05426  -0.04059 137 PRO A C   
1034 O O   . PRO A 137 ? 0.48556 0.46899 0.44922 0.11267  0.04931  -0.03763 137 PRO A O   
1035 C CB  . PRO A 137 ? 0.61540 0.60461 0.57211 0.14237  0.07636  -0.04342 137 PRO A CB  
1036 C CG  . PRO A 137 ? 0.58701 0.57570 0.52970 0.13966  0.08507  -0.04872 137 PRO A CG  
1037 C CD  . PRO A 137 ? 0.58378 0.55818 0.51269 0.12268  0.07580  -0.05079 137 PRO A CD  
1038 N N   . THR A 138 ? 0.56914 0.51813 0.52288 0.12930  0.05039  -0.03886 138 THR A N   
1039 C CA  . THR A 138 ? 0.48300 0.43816 0.44933 0.12234  0.04023  -0.03299 138 THR A CA  
1040 C C   . THR A 138 ? 0.50270 0.49569 0.49345 0.12313  0.04004  -0.02609 138 THR A C   
1041 O O   . THR A 138 ? 0.46659 0.47727 0.46884 0.13558  0.04643  -0.02311 138 THR A O   
1042 C CB  . THR A 138 ? 0.58667 0.51896 0.54856 0.13018  0.03845  -0.03148 138 THR A CB  
1043 O OG1 . THR A 138 ? 0.60781 0.50390 0.54589 0.12759  0.03843  -0.03876 138 THR A OG1 
1044 C CG2 . THR A 138 ? 0.41182 0.34960 0.38510 0.12226  0.02847  -0.02527 138 THR A CG2 
1045 N N   . ASP A 139 ? 0.42811 0.43386 0.42651 0.10976  0.03275  -0.02377 139 ASP A N   
1046 C CA  . ASP A 139 ? 0.39956 0.43818 0.41922 0.10798  0.03092  -0.01776 139 ASP A CA  
1047 C C   . ASP A 139 ? 0.43369 0.47517 0.46314 0.11611  0.02746  -0.01186 139 ASP A C   
1048 O O   . ASP A 139 ? 0.43724 0.45444 0.45789 0.11639  0.02314  -0.01160 139 ASP A O   
1049 C CB  . ASP A 139 ? 0.34878 0.39364 0.37106 0.09196  0.02375  -0.01716 139 ASP A CB  
1050 C CG  . ASP A 139 ? 0.38887 0.43355 0.40240 0.08423  0.02718  -0.02142 139 ASP A CG  
1051 O OD1 . ASP A 139 ? 0.41567 0.47183 0.43020 0.08954  0.03577  -0.02285 139 ASP A OD1 
1052 O OD2 . ASP A 139 ? 0.35407 0.38723 0.35944 0.07349  0.02171  -0.02297 139 ASP A OD2 
1053 N N   . CYS A 140 ? 0.38619 0.45808 0.43370 0.12222  0.02921  -0.00676 140 CYS A N   
1054 C CA  . CYS A 140 ? 0.40429 0.48418 0.46229 0.12926  0.02488  0.00019  140 CYS A CA  
1055 C C   . CYS A 140 ? 0.41721 0.52594 0.49058 0.11945  0.01883  0.00437  140 CYS A C   
1056 O O   . CYS A 140 ? 0.38355 0.51297 0.46383 0.11160  0.02059  0.00260  140 CYS A O   
1057 C CB  . CYS A 140 ? 0.44508 0.53590 0.51062 0.14785  0.03163  0.00336  140 CYS A CB  
1058 S SG  . CYS A 140 ? 0.64512 0.69749 0.69031 0.16124  0.03960  -0.00178 140 CYS A SG  
1059 N N   . ALA A 141 ? 0.32462 0.43313 0.40183 0.11960  0.01209  0.00983  141 ALA A N   
1060 C CA  . ALA A 141 ? 0.39189 0.52384 0.48048 0.10972  0.00589  0.01319  141 ALA A CA  
1061 C C   . ALA A 141 ? 0.40235 0.57196 0.50800 0.11292  0.00839  0.01551  141 ALA A C   
1062 O O   . ALA A 141 ? 0.42329 0.60429 0.53602 0.12717  0.01251  0.01845  141 ALA A O   
1063 C CB  . ALA A 141 ? 0.38091 0.50582 0.46917 0.11180  -0.00060 0.01922  141 ALA A CB  
1064 N N   . LYS A 142 ? 0.52519 0.71415 0.63756 0.09944  0.00618  0.01407  142 LYS A N   
1065 C CA  . LYS A 142 ? 0.49111 0.71728 0.61996 0.09852  0.00821  0.01544  142 LYS A CA  
1066 C C   . LYS A 142 ? 0.62843 0.86264 0.76062 0.10729  0.01778  0.01314  142 LYS A C   
1067 O O   . LYS A 142 ? 0.72993 0.99456 0.87771 0.11452  0.02049  0.01623  142 LYS A O   
1068 C CB  . LYS A 142 ? 0.57202 0.82232 0.71384 0.10533  0.00277  0.02258  142 LYS A CB  
1069 C CG  . LYS A 142 ? 0.49036 0.73383 0.62792 0.09747  -0.00606 0.02528  142 LYS A CG  
1070 C CD  . LYS A 142 ? 0.88446 1.12626 1.01813 0.07885  -0.00818 0.02040  142 LYS A CD  
1071 C CE  . LYS A 142 ? 0.92711 1.20183 1.07347 0.06995  -0.00718 0.01893  142 LYS A CE  
1072 N NZ  . LYS A 142 ? 0.70755 0.97307 0.84706 0.05393  -0.00568 0.01302  142 LYS A NZ  
1073 N N   . GLY A 143 ? 0.55315 0.76156 0.67078 0.10674  0.02306  0.00776  143 GLY A N   
1074 C CA  . GLY A 143 ? 0.48512 0.69680 0.60240 0.11565  0.03317  0.00503  143 GLY A CA  
1075 C C   . GLY A 143 ? 0.60426 0.81906 0.72674 0.13570  0.03714  0.00859  143 GLY A C   
1076 O O   . GLY A 143 ? 0.71774 0.92958 0.83727 0.14574  0.04643  0.00597  143 GLY A O   
1077 N N   . GLY A 147 ? 0.59159 0.71165 0.68484 0.19543  0.03340  0.02480  147 GLY A N   
1078 C CA  . GLY A 147 ? 0.63009 0.75042 0.72272 0.18035  0.02446  0.02560  147 GLY A CA  
1079 C C   . GLY A 147 ? 0.38521 0.46291 0.45752 0.17345  0.02183  0.02229  147 GLY A C   
1080 O O   . GLY A 147 ? 0.63263 0.68053 0.68985 0.17854  0.02743  0.01721  147 GLY A O   
1081 N N   . GLN A 148 ? 0.45661 0.53230 0.52852 0.16134  0.01351  0.02489  148 GLN A N   
1082 C CA  . GLN A 148 ? 0.36221 0.40223 0.41785 0.15312  0.01031  0.02254  148 GLN A CA  
1083 C C   . GLN A 148 ? 0.34754 0.37320 0.39269 0.14130  0.01202  0.01327  148 GLN A C   
1084 O O   . GLN A 148 ? 0.37968 0.42500 0.43147 0.13061  0.01059  0.01069  148 GLN A O   
1085 C CB  . GLN A 148 ? 0.45028 0.49812 0.51059 0.14275  0.00188  0.02766  148 GLN A CB  
1086 C CG  . GLN A 148 ? 0.49499 0.51185 0.54214 0.13377  -0.00169 0.02669  148 GLN A CG  
1087 C CD  . GLN A 148 ? 0.46033 0.48616 0.51233 0.12605  -0.00861 0.03281  148 GLN A CD  
1088 O OE1 . GLN A 148 ? 0.43757 0.49064 0.50105 0.12914  -0.01116 0.03837  148 GLN A OE1 
1089 N NE2 . GLN A 148 ? 0.37474 0.37817 0.41766 0.11588  -0.01159 0.03179  148 GLN A NE2 
1090 N N   . PRO A 149 ? 0.47223 0.46302 0.49995 0.14225  0.01462  0.00825  149 PRO A N   
1091 C CA  . PRO A 149 ? 0.44583 0.42316 0.46206 0.13113  0.01529  -0.00032 149 PRO A CA  
1092 C C   . PRO A 149 ? 0.44103 0.42165 0.45891 0.11374  0.00749  -0.00083 149 PRO A C   
1093 O O   . PRO A 149 ? 0.36005 0.33695 0.38032 0.10910  0.00182  0.00364  149 PRO A O   
1094 C CB  . PRO A 149 ? 0.40607 0.34358 0.40262 0.13512  0.01782  -0.00456 149 PRO A CB  
1095 C CG  . PRO A 149 ? 0.63682 0.56788 0.63494 0.15141  0.02118  0.00135  149 PRO A CG  
1096 C CD  . PRO A 149 ? 0.45753 0.41808 0.47389 0.15259  0.01649  0.01038  149 PRO A CD  
1097 N N   . LEU A 150 ? 0.31596 0.30140 0.33104 0.10452  0.00778  -0.00631 150 LEU A N   
1098 C CA  . LEU A 150 ? 0.30295 0.29110 0.31907 0.08932  0.00122  -0.00717 150 LEU A CA  
1099 C C   . LEU A 150 ? 0.33758 0.29994 0.33740 0.08183  -0.00055 -0.01352 150 LEU A C   
1100 O O   . LEU A 150 ? 0.33134 0.27911 0.31867 0.08648  0.00424  -0.01875 150 LEU A O   
1101 C CB  . LEU A 150 ? 0.29896 0.31485 0.32538 0.08383  0.00210  -0.00731 150 LEU A CB  
1102 C CG  . LEU A 150 ? 0.31173 0.35709 0.35469 0.08977  0.00358  -0.00192 150 LEU A CG  
1103 C CD1 . LEU A 150 ? 0.35107 0.42083 0.40196 0.08311  0.00569  -0.00337 150 LEU A CD1 
1104 C CD2 . LEU A 150 ? 0.23538 0.28549 0.28536 0.08662  -0.00285 0.00375  150 LEU A CD2 
1105 N N   . CYS A 151 ? 0.31160 0.26955 0.31160 0.07030  -0.00748 -0.01302 151 CYS A N   
1106 C CA  . CYS A 151 ? 0.33497 0.27401 0.32209 0.06145  -0.01101 -0.01836 151 CYS A CA  
1107 C C   . CYS A 151 ? 0.42839 0.37289 0.40941 0.05945  -0.00827 -0.02299 151 CYS A C   
1108 O O   . CYS A 151 ? 0.32501 0.29113 0.31527 0.05783  -0.00681 -0.02121 151 CYS A O   
1109 C CB  . CYS A 151 ? 0.30928 0.25129 0.30257 0.05004  -0.01855 -0.01586 151 CYS A CB  
1110 S SG  . CYS A 151 ? 0.37652 0.29785 0.35612 0.03889  -0.02469 -0.02152 151 CYS A SG  
1111 N N   . MET A 152 ? 0.36717 0.29069 0.33110 0.05871  -0.00758 -0.02900 152 MET A N   
1112 C CA  . MET A 152 ? 0.35801 0.28328 0.31248 0.05681  -0.00484 -0.03332 152 MET A CA  
1113 C C   . MET A 152 ? 0.41756 0.33433 0.36347 0.04528  -0.01241 -0.03574 152 MET A C   
1114 O O   . MET A 152 ? 0.40223 0.31644 0.33663 0.04325  -0.01108 -0.03925 152 MET A O   
1115 C CB  . MET A 152 ? 0.37855 0.28802 0.31775 0.06594  0.00279  -0.03871 152 MET A CB  
1116 C CG  . MET A 152 ? 0.34059 0.26136 0.28902 0.07948  0.01129  -0.03611 152 MET A CG  
1117 S SD  . MET A 152 ? 0.38308 0.34139 0.35011 0.08164  0.01652  -0.03172 152 MET A SD  
1118 C CE  . MET A 152 ? 0.41268 0.36522 0.36284 0.08444  0.02549  -0.03829 152 MET A CE  
1119 N N   . LYS A 153 ? 0.42462 0.24123 0.37828 0.03129  -0.02968 -0.00955 153 LYS A N   
1120 C CA  . LYS A 153 ? 0.37792 0.19717 0.33051 0.02089  -0.03385 -0.01198 153 LYS A CA  
1121 C C   . LYS A 153 ? 0.36895 0.20968 0.32232 0.02039  -0.03230 -0.01235 153 LYS A C   
1122 O O   . LYS A 153 ? 0.39187 0.23363 0.34037 0.01556  -0.03575 -0.01712 153 LYS A O   
1123 C CB  . LYS A 153 ? 0.42869 0.24637 0.38930 0.01043  -0.03718 -0.00480 153 LYS A CB  
1124 C CG  . LYS A 153 ? 0.77736 0.56960 0.73568 0.00677  -0.04013 -0.00496 153 LYS A CG  
1125 C CD  . LYS A 153 ? 0.84997 0.62516 0.79903 0.00413  -0.04456 -0.01595 153 LYS A CD  
1126 C CE  . LYS A 153 ? 0.84734 0.59652 0.79529 -0.00213 -0.04811 -0.01585 153 LYS A CE  
1127 N NZ  . LYS A 153 ? 1.04435 0.79978 1.00285 -0.01578 -0.05050 -0.00856 153 LYS A NZ  
1128 N N   . GLN A 154 ? 0.36460 0.22194 0.32359 0.02495  -0.02784 -0.00734 154 GLN A N   
1129 C CA  . GLN A 154 ? 0.31912 0.19395 0.27816 0.02398  -0.02647 -0.00752 154 GLN A CA  
1130 C C   . GLN A 154 ? 0.37980 0.25193 0.32747 0.02776  -0.02481 -0.01560 154 GLN A C   
1131 O O   . GLN A 154 ? 0.33054 0.21077 0.27423 0.02524  -0.02553 -0.01671 154 GLN A O   
1132 C CB  . GLN A 154 ? 0.33560 0.22699 0.30208 0.02796  -0.02197 -0.00179 154 GLN A CB  
1133 C CG  . GLN A 154 ? 0.27840 0.17514 0.25416 0.02439  -0.02294 0.00649  154 GLN A CG  
1134 C CD  . GLN A 154 ? 0.33611 0.24612 0.31722 0.02967  -0.01908 0.01086  154 GLN A CD  
1135 O OE1 . GLN A 154 ? 0.32539 0.24683 0.30638 0.03250  -0.01617 0.00882  154 GLN A OE1 
1136 N NE2 . GLN A 154 ? 0.27101 0.17897 0.25618 0.03064  -0.01924 0.01701  154 GLN A NE2 
1137 N N   . TYR A 155 ? 0.34323 0.20445 0.28501 0.03450  -0.02211 -0.02103 155 TYR A N   
1138 C CA  . TYR A 155 ? 0.47761 0.33639 0.40710 0.03786  -0.01959 -0.02902 155 TYR A CA  
1139 C C   . TYR A 155 ? 0.44045 0.29069 0.35993 0.03141  -0.02566 -0.03381 155 TYR A C   
1140 O O   . TYR A 155 ? 0.43047 0.28465 0.33977 0.03132  -0.02492 -0.03722 155 TYR A O   
1141 C CB  . TYR A 155 ? 0.39143 0.23934 0.31681 0.04668  -0.01574 -0.03505 155 TYR A CB  
1142 C CG  . TYR A 155 ? 0.46449 0.32519 0.39887 0.05459  -0.00938 -0.03213 155 TYR A CG  
1143 C CD1 . TYR A 155 ? 0.37698 0.23682 0.32177 0.05773  -0.01035 -0.02642 155 TYR A CD1 
1144 C CD2 . TYR A 155 ? 0.37247 0.24640 0.30474 0.05856  -0.00260 -0.03498 155 TYR A CD2 
1145 C CE1 . TYR A 155 ? 0.37038 0.24331 0.32386 0.06558  -0.00573 -0.02433 155 TYR A CE1 
1146 C CE2 . TYR A 155 ? 0.40415 0.29183 0.34663 0.06525  0.00278  -0.03316 155 TYR A CE2 
1147 C CZ  . TYR A 155 ? 0.48139 0.36894 0.43470 0.06904  0.00058  -0.02815 155 TYR A CZ  
1148 O OH  . TYR A 155 ? 0.44363 0.34628 0.40741 0.07587  0.00460  -0.02672 155 TYR A OH  
1149 N N   . TYR A 156 ? 0.41968 0.25838 0.34163 0.02553  -0.03197 -0.03390 156 TYR A N   
1150 C CA  . TYR A 156 ? 0.47255 0.30434 0.38613 0.01903  -0.03889 -0.03934 156 TYR A CA  
1151 C C   . TYR A 156 ? 0.49182 0.33929 0.40983 0.01302  -0.04272 -0.03482 156 TYR A C   
1152 O O   . TYR A 156 ? 0.54445 0.38954 0.45624 0.00812  -0.04935 -0.03900 156 TYR A O   
1153 C CB  . TYR A 156 ? 0.44668 0.26114 0.36264 0.01338  -0.04462 -0.04150 156 TYR A CB  
1154 C CG  . TYR A 156 ? 0.51627 0.31109 0.42603 0.02001  -0.04200 -0.04709 156 TYR A CG  
1155 C CD1 . TYR A 156 ? 0.56068 0.34194 0.45498 0.02345  -0.04263 -0.05800 156 TYR A CD1 
1156 C CD2 . TYR A 156 ? 0.59065 0.38009 0.50915 0.02363  -0.03906 -0.04155 156 TYR A CD2 
1157 C CE1 . TYR A 156 ? 0.51016 0.27305 0.39906 0.03081  -0.03999 -0.06387 156 TYR A CE1 
1158 C CE2 . TYR A 156 ? 0.63258 0.40347 0.54582 0.03120  -0.03708 -0.04648 156 TYR A CE2 
1159 C CZ  . TYR A 156 ? 0.72169 0.47943 0.62084 0.03498  -0.03736 -0.05789 156 TYR A CZ  
1160 O OH  . TYR A 156 ? 0.66834 0.40738 0.56289 0.04362  -0.03521 -0.06326 156 TYR A OH  
1161 N N   . GLY A 157 ? 0.38216 0.24537 0.31064 0.01374  -0.03927 -0.02695 157 GLY A N   
1162 C CA  . GLY A 157 ? 0.37397 0.25196 0.30701 0.00988  -0.04217 -0.02280 157 GLY A CA  
1163 C C   . GLY A 157 ? 0.38490 0.27112 0.30982 0.01438  -0.03833 -0.02266 157 GLY A C   
1164 O O   . GLY A 157 ? 0.40528 0.30174 0.33186 0.01244  -0.04097 -0.01954 157 GLY A O   
1165 N N   . LEU A 158 ? 0.37838 0.26037 0.29486 0.02043  -0.03184 -0.02586 158 LEU A N   
1166 C CA  . LEU A 158 ? 0.40415 0.29388 0.31347 0.02354  -0.02683 -0.02487 158 LEU A CA  
1167 C C   . LEU A 158 ? 0.38984 0.27613 0.28414 0.02177  -0.03142 -0.02790 158 LEU A C   
1168 O O   . LEU A 158 ? 0.38751 0.28125 0.27939 0.02140  -0.03146 -0.02397 158 LEU A O   
1169 C CB  . LEU A 158 ? 0.40198 0.28975 0.30692 0.02975  -0.01833 -0.02813 158 LEU A CB  
1170 C CG  . LEU A 158 ? 0.29591 0.19101 0.21507 0.03317  -0.01329 -0.02439 158 LEU A CG  
1171 C CD1 . LEU A 158 ? 0.35989 0.25023 0.27503 0.03998  -0.00707 -0.03007 158 LEU A CD1 
1172 C CD2 . LEU A 158 ? 0.30376 0.21411 0.22958 0.03268  -0.00940 -0.01859 158 LEU A CD2 
1173 N N   . PHE A 159 ? 0.36812 0.24223 0.25145 0.02087  -0.03589 -0.03487 159 PHE A N   
1174 C CA  . PHE A 159 ? 0.44308 0.31305 0.30884 0.02016  -0.04044 -0.03848 159 PHE A CA  
1175 C C   . PHE A 159 ? 0.59696 0.46458 0.46351 0.01462  -0.05205 -0.04078 159 PHE A C   
1176 O O   . PHE A 159 ? 0.59820 0.46435 0.45092 0.01415  -0.05774 -0.04303 159 PHE A O   
1177 C CB  . PHE A 159 ? 0.41794 0.27634 0.26547 0.02431  -0.03586 -0.04642 159 PHE A CB  
1178 C CG  . PHE A 159 ? 0.46601 0.32893 0.31311 0.02953  -0.02422 -0.04514 159 PHE A CG  
1179 C CD1 . PHE A 159 ? 0.46162 0.33265 0.30328 0.03019  -0.01909 -0.04026 159 PHE A CD1 
1180 C CD2 . PHE A 159 ? 0.56823 0.42749 0.42122 0.03375  -0.01849 -0.04871 159 PHE A CD2 
1181 C CE1 . PHE A 159 ? 0.46203 0.33911 0.30550 0.03372  -0.00806 -0.03933 159 PHE A CE1 
1182 C CE2 . PHE A 159 ? 0.54334 0.41004 0.39870 0.03861  -0.00806 -0.04788 159 PHE A CE2 
1183 C CZ  . PHE A 159 ? 0.50970 0.38616 0.36094 0.03794  -0.00271 -0.04335 159 PHE A CZ  
1184 N N   . SER A 160 ? 0.44157 0.30895 0.32340 0.01015  -0.05591 -0.04027 160 SER A N   
1185 C CA  . SER A 160 ? 0.65731 0.52232 0.54119 0.00364  -0.06669 -0.04390 160 SER A CA  
1186 C C   . SER A 160 ? 0.56471 0.44518 0.46716 -0.00110 -0.07126 -0.03727 160 SER A C   
1187 O O   . SER A 160 ? 0.66517 0.54646 0.57770 -0.00794 -0.07810 -0.03880 160 SER A O   
1188 C CB  . SER A 160 ? 0.78428 0.63442 0.66989 0.00063  -0.06800 -0.04976 160 SER A CB  
1189 O OG  . SER A 160 ? 0.72786 0.58060 0.63038 -0.00030 -0.06333 -0.04377 160 SER A OG  
1190 N N   . SER A 161 ? 0.48409 0.37704 0.39149 0.00221  -0.06730 -0.03033 161 SER A N   
1191 C CA  . SER A 161 ? 0.45658 0.36482 0.38287 -0.00072 -0.06904 -0.02396 161 SER A CA  
1192 C C   . SER A 161 ? 0.43502 0.35396 0.35900 0.00171  -0.07336 -0.02123 161 SER A C   
1193 O O   . SER A 161 ? 0.41398 0.32975 0.32387 0.00690  -0.07048 -0.02045 161 SER A O   
1194 C CB  . SER A 161 ? 0.43582 0.34895 0.37271 0.00160  -0.05989 -0.01789 161 SER A CB  
1195 O OG  . SER A 161 ? 0.54929 0.45235 0.48894 0.00025  -0.05668 -0.01941 161 SER A OG  
1196 N N   . TYR A 162 ? 0.36955 0.30132 0.30797 -0.00193 -0.07991 -0.01945 162 TYR A N   
1197 C CA  . TYR A 162 ? 0.40351 0.34664 0.34279 0.00154  -0.08458 -0.01648 162 TYR A CA  
1198 C C   . TYR A 162 ? 0.33875 0.29927 0.30093 -0.00100 -0.08504 -0.01221 162 TYR A C   
1199 O O   . TYR A 162 ? 0.39370 0.35959 0.36904 -0.00784 -0.08874 -0.01394 162 TYR A O   
1200 C CB  . TYR A 162 ? 0.34300 0.28458 0.27167 0.00103  -0.09603 -0.02152 162 TYR A CB  
1201 C CG  . TYR A 162 ? 0.36223 0.31355 0.28978 0.00656  -0.10103 -0.01781 162 TYR A CG  
1202 C CD1 . TYR A 162 ? 0.33749 0.30686 0.28451 0.00555  -0.10692 -0.01594 162 TYR A CD1 
1203 C CD2 . TYR A 162 ? 0.36387 0.30623 0.27138 0.01314  -0.09894 -0.01566 162 TYR A CD2 
1204 C CE1 . TYR A 162 ? 0.34675 0.32449 0.29332 0.01237  -0.11156 -0.01248 162 TYR A CE1 
1205 C CE2 . TYR A 162 ? 0.39423 0.34261 0.29971 0.01890  -0.10353 -0.01150 162 TYR A CE2 
1206 C CZ  . TYR A 162 ? 0.38053 0.34631 0.30572 0.01914  -0.11014 -0.01011 162 TYR A CZ  
1207 O OH  . TYR A 162 ? 0.39732 0.36817 0.32062 0.02636  -0.11498 -0.00620 162 TYR A OH  
1208 N N   . ARG A 163 ? 0.30102 0.27016 0.26762 0.00411  -0.08127 -0.00703 163 ARG A N   
1209 C CA  . ARG A 163 ? 0.30064 0.28717 0.28785 0.00296  -0.08050 -0.00333 163 ARG A CA  
1210 C C   . ARG A 163 ? 0.37539 0.37524 0.36861 0.00579  -0.08934 -0.00357 163 ARG A C   
1211 O O   . ARG A 163 ? 0.34110 0.34088 0.32723 0.01307  -0.08987 -0.00129 163 ARG A O   
1212 C CB  . ARG A 163 ? 0.28173 0.26986 0.27103 0.00717  -0.07096 0.00153  163 ARG A CB  
1213 C CG  . ARG A 163 ? 0.28038 0.28620 0.28901 0.00652  -0.06943 0.00471  163 ARG A CG  
1214 C CD  . ARG A 163 ? 0.33652 0.34270 0.34613 0.00975  -0.06024 0.00848  163 ARG A CD  
1215 N NE  . ARG A 163 ? 0.25938 0.28213 0.28354 0.01161  -0.05890 0.01089  163 ARG A NE  
1216 C CZ  . ARG A 163 ? 0.27795 0.30446 0.30582 0.01351  -0.05155 0.01366  163 ARG A CZ  
1217 N NH1 . ARG A 163 ? 0.26288 0.27917 0.28260 0.01363  -0.04556 0.01466  163 ARG A NH1 
1218 N NH2 . ARG A 163 ? 0.25257 0.29449 0.29292 0.01555  -0.05035 0.01494  163 ARG A NH2 
1219 N N   . LEU A 164 ? 0.29745 0.30914 0.30485 0.00013  -0.09616 -0.00608 164 LEU A N   
1220 C CA  . LEU A 164 ? 0.28296 0.31008 0.29836 0.00349  -0.10550 -0.00684 164 LEU A CA  
1221 C C   . LEU A 164 ? 0.33043 0.37521 0.36351 0.00716  -0.10111 -0.00266 164 LEU A C   
1222 O O   . LEU A 164 ? 0.30967 0.36123 0.35597 0.00237  -0.09388 -0.00062 164 LEU A O   
1223 C CB  . LEU A 164 ? 0.34232 0.37880 0.36901 -0.00456 -0.11486 -0.01183 164 LEU A CB  
1224 C CG  . LEU A 164 ? 0.43247 0.45543 0.44200 -0.00671 -0.12346 -0.01776 164 LEU A CG  
1225 C CD1 . LEU A 164 ? 0.46827 0.49803 0.49148 -0.01775 -0.12986 -0.02295 164 LEU A CD1 
1226 C CD2 . LEU A 164 ? 0.44834 0.47428 0.44727 0.00186  -0.13310 -0.01824 164 LEU A CD2 
1227 N N   . PRO A 165 ? 0.31582 0.36767 0.34875 0.01594  -0.10537 -0.00137 165 PRO A N   
1228 C CA  . PRO A 165 ? 0.29745 0.36747 0.34848 0.01997  -0.10182 0.00121  165 PRO A CA  
1229 C C   . PRO A 165 ? 0.31757 0.41158 0.39289 0.01453  -0.10664 -0.00109 165 PRO A C   
1230 O O   . PRO A 165 ? 0.26557 0.36439 0.34362 0.01073  -0.11653 -0.00496 165 PRO A O   
1231 C CB  . PRO A 165 ? 0.24743 0.31448 0.28890 0.03159  -0.10653 0.00261  165 PRO A CB  
1232 C CG  . PRO A 165 ? 0.29420 0.35276 0.32121 0.03178  -0.11770 -0.00022 165 PRO A CG  
1233 C CD  . PRO A 165 ? 0.26037 0.30402 0.27639 0.02300  -0.11422 -0.00229 165 PRO A CD  
1234 N N   . GLY A 166 ? 0.22307 0.33327 0.31627 0.01389  -0.09946 0.00102  166 GLY A N   
1235 C CA  . GLY A 166 ? 0.21442 0.35107 0.33290 0.00949  -0.10243 -0.00070 166 GLY A CA  
1236 C C   . GLY A 166 ? 0.24920 0.40402 0.38104 0.01844  -0.09877 0.00074  166 GLY A C   
1237 O O   . GLY A 166 ? 0.30035 0.44576 0.42253 0.02571  -0.09207 0.00330  166 GLY A O   
1238 N N   . HIS A 167 ? 0.30363 0.48545 0.45865 0.01781  -0.10329 -0.00158 167 HIS A N   
1239 C CA  . HIS A 167 ? 0.21720 0.41814 0.38629 0.02739  -0.09973 -0.00119 167 HIS A CA  
1240 C C   . HIS A 167 ? 0.39130 0.59466 0.56432 0.02451  -0.08545 0.00193  167 HIS A C   
1241 O O   . HIS A 167 ? 0.40586 0.60838 0.57558 0.03410  -0.07991 0.00289  167 HIS A O   
1242 C CB  . HIS A 167 ? 0.42653 0.65950 0.62243 0.02712  -0.10676 -0.00474 167 HIS A CB  
1243 C CG  . HIS A 167 ? 0.72675 0.98143 0.93902 0.03707  -0.10178 -0.00504 167 HIS A CG  
1244 N ND1 . HIS A 167 ? 0.58083 0.82664 0.78251 0.05227  -0.10240 -0.00462 167 HIS A ND1 
1245 C CD2 . HIS A 167 ? 0.73439 1.01795 0.97177 0.03394  -0.09505 -0.00583 167 HIS A CD2 
1246 C CE1 . HIS A 167 ? 0.73531 1.00349 0.95503 0.05898  -0.09695 -0.00591 167 HIS A CE1 
1247 N NE2 . HIS A 167 ? 0.93362 1.22612 1.17529 0.04819  -0.09209 -0.00666 167 HIS A NE2 
1248 N N   . THR A 168 ? 0.29308 0.49819 0.47192 0.01148  -0.07965 0.00353  168 THR A N   
1249 C CA  . THR A 168 ? 0.27313 0.47911 0.45310 0.00808  -0.06654 0.00725  168 THR A CA  
1250 C C   . THR A 168 ? 0.34356 0.52428 0.50562 0.00082  -0.06170 0.01052  168 THR A C   
1251 O O   . THR A 168 ? 0.30929 0.48240 0.46307 0.00269  -0.05267 0.01359  168 THR A O   
1252 C CB  . THR A 168 ? 0.27794 0.51219 0.48323 -0.00045 -0.06180 0.00757  168 THR A CB  
1253 O OG1 . THR A 168 ? 0.63531 0.87269 0.84907 -0.01225 -0.06863 0.00602  168 THR A OG1 
1254 C CG2 . THR A 168 ? 0.34585 0.60793 0.57004 0.00929  -0.06348 0.00435  168 THR A CG2 
1255 N N   . GLN A 169 ? 0.21009 0.37757 0.36558 -0.00664 -0.06788 0.00939  169 GLN A N   
1256 C CA  . GLN A 169 ? 0.23456 0.37816 0.37392 -0.01244 -0.06375 0.01188  169 GLN A CA  
1257 C C   . GLN A 169 ? 0.26970 0.39448 0.39375 -0.01190 -0.07282 0.00852  169 GLN A C   
1258 O O   . GLN A 169 ? 0.22368 0.35584 0.35445 -0.01455 -0.08226 0.00468  169 GLN A O   
1259 C CB  . GLN A 169 ? 0.28172 0.42985 0.43190 -0.02568 -0.05893 0.01450  169 GLN A CB  
1260 C CG  . GLN A 169 ? 0.22442 0.34789 0.35906 -0.03076 -0.05453 0.01751  169 GLN A CG  
1261 C CD  . GLN A 169 ? 0.35571 0.48207 0.50045 -0.04350 -0.04986 0.02102  169 GLN A CD  
1262 O OE1 . GLN A 169 ? 0.32606 0.44978 0.47627 -0.05297 -0.05530 0.01876  169 GLN A OE1 
1263 N NE2 . GLN A 169 ? 0.26259 0.39383 0.40916 -0.04421 -0.03977 0.02662  169 GLN A NE2 
1264 N N   . ASP A 170 ? 0.25706 0.35937 0.36079 -0.00802 -0.07010 0.00958  170 ASP A N   
1265 C CA  . ASP A 170 ? 0.26100 0.34457 0.34782 -0.00728 -0.07690 0.00646  170 ASP A CA  
1266 C C   . ASP A 170 ? 0.31691 0.38991 0.40254 -0.01802 -0.07791 0.00508  170 ASP A C   
1267 O O   . ASP A 170 ? 0.26048 0.33668 0.35561 -0.02560 -0.07232 0.00780  170 ASP A O   
1268 C CB  . ASP A 170 ? 0.25071 0.31560 0.31764 -0.00003 -0.07236 0.00794  170 ASP A CB  
1269 C CG  . ASP A 170 ? 0.28913 0.35762 0.35241 0.01052  -0.07326 0.00849  170 ASP A CG  
1270 O OD1 . ASP A 170 ? 0.25682 0.34290 0.33342 0.01393  -0.07674 0.00791  170 ASP A OD1 
1271 O OD2 . ASP A 170 ? 0.29782 0.35089 0.34493 0.01543  -0.07022 0.00943  170 ASP A OD2 
1272 N N   A THR A 171 ? 0.34794 0.40694 0.42044 -0.01848 -0.08511 0.00081  171 THR A N   
1273 N N   B THR A 171 ? 0.34788 0.40644 0.42014 -0.01858 -0.08498 0.00083  171 THR A N   
1274 C CA  A THR A 171 ? 0.36389 0.40861 0.43187 -0.02734 -0.08675 -0.00186 171 THR A CA  
1275 C CA  B THR A 171 ? 0.36287 0.40780 0.43157 -0.02780 -0.08643 -0.00170 171 THR A CA  
1276 C C   A THR A 171 ? 0.39082 0.41178 0.43598 -0.02264 -0.08441 -0.00303 171 THR A C   
1277 C C   B THR A 171 ? 0.39123 0.41211 0.43679 -0.02362 -0.08560 -0.00373 171 THR A C   
1278 O O   A THR A 171 ? 0.33247 0.34887 0.36454 -0.01462 -0.08629 -0.00391 171 THR A O   
1279 O O   B THR A 171 ? 0.36616 0.38230 0.39853 -0.01690 -0.08998 -0.00601 171 THR A O   
1280 C CB  A THR A 171 ? 0.35413 0.40536 0.42841 -0.03340 -0.09831 -0.00775 171 THR A CB  
1281 C CB  B THR A 171 ? 0.36056 0.41441 0.43907 -0.03518 -0.09713 -0.00703 171 THR A CB  
1282 O OG1 A THR A 171 ? 0.33057 0.40784 0.42856 -0.03712 -0.10015 -0.00685 171 THR A OG1 
1283 O OG1 B THR A 171 ? 0.31178 0.36564 0.38016 -0.02838 -0.10650 -0.01107 171 THR A OG1 
1284 C CG2 A THR A 171 ? 0.30926 0.34465 0.38012 -0.04363 -0.09964 -0.01101 171 THR A CG2 
1285 C CG2 B THR A 171 ? 0.26512 0.34560 0.36958 -0.04049 -0.09675 -0.00513 171 THR A CG2 
1286 N N   . LEU A 172 ? 0.47092 0.47688 0.51143 -0.02723 -0.07967 -0.00262 172 LEU A N   
1287 C CA  . LEU A 172 ? 0.41549 0.40049 0.43635 -0.02292 -0.07715 -0.00463 172 LEU A CA  
1288 C C   . LEU A 172 ? 0.42571 0.39711 0.44001 -0.02901 -0.08358 -0.01104 172 LEU A C   
1289 O O   . LEU A 172 ? 0.48500 0.45275 0.50783 -0.03747 -0.08357 -0.01120 172 LEU A O   
1290 C CB  . LEU A 172 ? 0.46710 0.44461 0.48653 -0.02124 -0.06718 0.00008  172 LEU A CB  
1291 C CG  . LEU A 172 ? 0.48738 0.44570 0.48952 -0.01642 -0.06354 -0.00211 172 LEU A CG  
1292 C CD1 . LEU A 172 ? 0.46869 0.42586 0.45735 -0.00857 -0.06381 -0.00382 172 LEU A CD1 
1293 C CD2 . LEU A 172 ? 0.38001 0.33368 0.38357 -0.01457 -0.05491 0.00269  172 LEU A CD2 
1294 N N   . VAL A 173 ? 0.51847 0.48224 0.51724 -0.02515 -0.08935 -0.01636 173 VAL A N   
1295 C CA  . VAL A 173 ? 0.56406 0.51603 0.55462 -0.03025 -0.09713 -0.02404 173 VAL A CA  
1296 C C   . VAL A 173 ? 0.65204 0.58183 0.62304 -0.02628 -0.09255 -0.02739 173 VAL A C   
1297 O O   . VAL A 173 ? 0.51440 0.44072 0.47303 -0.01809 -0.08741 -0.02580 173 VAL A O   
1298 C CB  . VAL A 173 ? 0.48245 0.44247 0.46800 -0.02856 -0.10802 -0.02836 173 VAL A CB  
1299 C CG1 . VAL A 173 ? 0.51902 0.46723 0.49618 -0.03466 -0.11658 -0.03712 173 VAL A CG1 
1300 C CG2 . VAL A 173 ? 0.56316 0.54747 0.56988 -0.03081 -0.11230 -0.02531 173 VAL A CG2 
1301 N N   . ALA A 174 ? 0.71460 0.62943 0.68339 -0.03220 -0.09413 -0.03225 174 ALA A N   
1302 C CA  . ALA A 174 ? 0.82716 0.72069 0.77747 -0.02826 -0.09115 -0.03755 174 ALA A CA  
1303 C C   . ALA A 174 ? 0.90741 0.79119 0.84518 -0.03153 -0.10087 -0.04744 174 ALA A C   
1304 O O   . ALA A 174 ? 0.82947 0.71934 0.77673 -0.03983 -0.10978 -0.05047 174 ALA A O   
1305 C CB  . ALA A 174 ? 0.74320 0.62341 0.69845 -0.03061 -0.08486 -0.03578 174 ALA A CB  
1306 N N   . GLN A 175 ? 0.98115 0.85099 0.89756 -0.02510 -0.09907 -0.05286 175 GLN A N   
1307 C CA  . GLN A 175 ? 1.00725 0.86669 0.90769 -0.02699 -0.10792 -0.06299 175 GLN A CA  
1308 C C   . GLN A 175 ? 1.04427 0.88120 0.93840 -0.02991 -0.10704 -0.07055 175 GLN A C   
1309 O O   . GLN A 175 ? 1.03581 0.86759 0.93872 -0.03935 -0.11362 -0.07450 175 GLN A O   
1310 C CB  . GLN A 175 ? 1.00729 0.86532 0.88530 -0.01818 -0.10679 -0.06474 175 GLN A CB  
1311 N N   . PRO A 181 ? 1.29052 1.08471 1.05143 -0.01647 -0.14135 -0.11975 181 PRO A N   
1312 C CA  . PRO A 181 ? 1.30791 1.10614 1.05581 -0.00671 -0.13043 -0.11230 181 PRO A CA  
1313 C C   . PRO A 181 ? 1.24985 1.03332 0.96446 -0.00030 -0.12692 -0.12078 181 PRO A C   
1314 O O   . PRO A 181 ? 1.11375 0.88912 0.82179 0.00554  -0.11377 -0.12123 181 PRO A O   
1315 C CB  . PRO A 181 ? 1.12466 0.92301 0.89088 -0.00473 -0.11682 -0.10544 181 PRO A CB  
1316 C CG  . PRO A 181 ? 1.25741 1.04086 1.03168 -0.01010 -0.11837 -0.11344 181 PRO A CG  
1317 C CD  . PRO A 181 ? 1.23104 1.01603 1.00967 -0.01969 -0.13411 -0.11965 181 PRO A CD  
1318 N N   . GLU A 182 ? 1.26231 1.04350 0.95618 -0.00105 -0.13843 -0.12754 182 GLU A N   
1319 C CA  . GLU A 182 ? 1.36248 1.12843 1.02248 0.00414  -0.13630 -0.13747 182 GLU A CA  
1320 C C   . GLU A 182 ? 1.30910 1.08204 0.94597 0.00834  -0.14081 -0.13355 182 GLU A C   
1321 O O   . GLU A 182 ? 1.23261 1.01497 0.87193 0.00445  -0.15414 -0.13404 182 GLU A O   
1322 C CB  . GLU A 182 ? 1.06907 0.82282 0.72655 -0.00153 -0.14426 -0.15125 182 GLU A CB  
1323 N N   . PRO A 183 ? 1.16746 0.93877 0.78554 0.01588  -0.12861 -0.12821 183 PRO A N   
1324 C CA  . PRO A 183 ? 0.98032 0.74794 0.60219 0.02053  -0.11059 -0.12531 183 PRO A CA  
1325 C C   . PRO A 183 ? 0.91496 0.69738 0.56550 0.01998  -0.10428 -0.11136 183 PRO A C   
1326 O O   . PRO A 183 ? 0.87919 0.67312 0.54781 0.01591  -0.11368 -0.10522 183 PRO A O   
1327 C CB  . PRO A 183 ? 1.12805 0.89116 0.71729 0.02716  -0.10175 -0.12523 183 PRO A CB  
1328 C CG  . PRO A 183 ? 1.23623 1.00839 0.81592 0.02635  -0.11239 -0.11861 183 PRO A CG  
1329 C CD  . PRO A 183 ? 1.23978 1.01591 0.83491 0.01971  -0.12976 -0.12397 183 PRO A CD  
1330 N N   . GLU A 184 ? 0.89384 0.67729 0.55004 0.02408  -0.08856 -0.10677 184 GLU A N   
1331 C CA  . GLU A 184 ? 0.61348 0.41059 0.29302 0.02395  -0.08246 -0.09400 184 GLU A CA  
1332 C C   . GLU A 184 ? 0.75595 0.55789 0.41929 0.02776  -0.07677 -0.08507 184 GLU A C   
1333 O O   . GLU A 184 ? 0.76460 0.55896 0.39977 0.03131  -0.07218 -0.08826 184 GLU A O   
1334 C CB  . GLU A 184 ? 0.71783 0.51468 0.41538 0.02571  -0.06986 -0.09371 184 GLU A CB  
1335 C CG  . GLU A 184 ? 0.89810 0.69049 0.61628 0.02132  -0.07534 -0.09866 184 GLU A CG  
1336 C CD  . GLU A 184 ? 1.08569 0.87368 0.81517 0.02503  -0.06357 -0.10024 184 GLU A CD  
1337 O OE1 . GLU A 184 ? 0.92382 0.70086 0.63733 0.03008  -0.05713 -0.10892 184 GLU A OE1 
1338 O OE2 . GLU A 184 ? 0.95449 0.75041 0.70842 0.02354  -0.06089 -0.09293 184 GLU A OE2 
1339 N N   . HIS A 185 ? 0.60895 0.42266 0.28935 0.02683  -0.07707 -0.07381 185 HIS A N   
1340 C CA  . HIS A 185 ? 0.59622 0.41265 0.26271 0.02966  -0.07329 -0.06436 185 HIS A CA  
1341 C C   . HIS A 185 ? 0.56554 0.39265 0.25635 0.02926  -0.06561 -0.05428 185 HIS A C   
1342 O O   . HIS A 185 ? 0.52933 0.36386 0.24687 0.02658  -0.06810 -0.05353 185 HIS A O   
1343 C CB  . HIS A 185 ? 0.60153 0.41904 0.25629 0.02962  -0.08845 -0.06184 185 HIS A CB  
1344 C CG  . HIS A 185 ? 0.56717 0.39644 0.24928 0.02637  -0.09986 -0.05892 185 HIS A CG  
1345 N ND1 . HIS A 185 ? 0.55879 0.38977 0.25228 0.02191  -0.11123 -0.06705 185 HIS A ND1 
1346 C CD2 . HIS A 185 ? 0.56583 0.40618 0.26663 0.02671  -0.10096 -0.04912 185 HIS A CD2 
1347 C CE1 . HIS A 185 ? 0.60386 0.44812 0.32242 0.01943  -0.11830 -0.06200 185 HIS A CE1 
1348 N NE2 . HIS A 185 ? 0.57253 0.42266 0.29570 0.02288  -0.11225 -0.05139 185 HIS A NE2 
1349 N N   . VAL A 186 ? 0.59176 0.41905 0.27241 0.03143  -0.05614 -0.04665 186 VAL A N   
1350 C CA  . VAL A 186 ? 0.56326 0.39970 0.26318 0.03085  -0.05161 -0.03656 186 VAL A CA  
1351 C C   . VAL A 186 ? 0.52292 0.35861 0.21207 0.03217  -0.06007 -0.02880 186 VAL A C   
1352 O O   . VAL A 186 ? 0.56549 0.39337 0.22952 0.03395  -0.06688 -0.03024 186 VAL A O   
1353 C CB  . VAL A 186 ? 0.61881 0.45647 0.31909 0.03146  -0.03476 -0.03339 186 VAL A CB  
1354 C CG1 . VAL A 186 ? 0.48560 0.32349 0.19406 0.03206  -0.02728 -0.04206 186 VAL A CG1 
1355 C CG2 . VAL A 186 ? 0.62205 0.45161 0.29291 0.03282  -0.02851 -0.03040 186 VAL A CG2 
1356 N N   . ILE A 187 ? 0.53520 0.37871 0.24307 0.03195  -0.06040 -0.02083 187 ILE A N   
1357 C CA  . ILE A 187 ? 0.51596 0.35775 0.21527 0.03449  -0.06648 -0.01231 187 ILE A CA  
1358 C C   . ILE A 187 ? 0.53331 0.37089 0.22673 0.03446  -0.05328 -0.00442 187 ILE A C   
1359 O O   . ILE A 187 ? 0.51119 0.35548 0.22448 0.03239  -0.04423 -0.00293 187 ILE A O   
1360 C CB  . ILE A 187 ? 0.51464 0.36795 0.23917 0.03479  -0.07666 -0.00954 187 ILE A CB  
1361 C CG1 . ILE A 187 ? 0.52292 0.38149 0.25369 0.03351  -0.09024 -0.01709 187 ILE A CG1 
1362 C CG2 . ILE A 187 ? 0.48998 0.34051 0.20657 0.03900  -0.08163 -0.00031 187 ILE A CG2 
1363 C CD1 . ILE A 187 ? 0.57646 0.42781 0.28059 0.03638  -0.10203 -0.01896 187 ILE A CD1 
1364 N N   . VAL A 188 ? 0.57985 0.40612 0.24570 0.03632  -0.05238 0.00074  188 VAL A N   
1365 C CA  . VAL A 188 ? 0.50639 0.32677 0.16487 0.03514  -0.04046 0.00913  188 VAL A CA  
1366 C C   . VAL A 188 ? 0.56934 0.38595 0.22802 0.03808  -0.04839 0.01828  188 VAL A C   
1367 O O   . VAL A 188 ? 0.62429 0.43483 0.26657 0.04221  -0.06025 0.02029  188 VAL A O   
1368 C CB  . VAL A 188 ? 0.59866 0.40740 0.22487 0.03452  -0.03162 0.00958  188 VAL A CB  
1369 C CG1 . VAL A 188 ? 0.54043 0.34395 0.16187 0.03140  -0.01802 0.01841  188 VAL A CG1 
1370 C CG2 . VAL A 188 ? 0.54628 0.35914 0.17281 0.03324  -0.02487 -0.00101 188 VAL A CG2 
1371 N N   . ALA A 189 ? 0.51225 0.33277 0.19008 0.03651  -0.04251 0.02316  189 ALA A N   
1372 C CA  . ALA A 189 ? 0.49035 0.30581 0.16978 0.03959  -0.04774 0.03165  189 ALA A CA  
1373 C C   . ALA A 189 ? 0.59748 0.39780 0.25655 0.03734  -0.03712 0.03998  189 ALA A C   
1374 O O   . ALA A 189 ? 0.62059 0.42261 0.28473 0.03180  -0.02328 0.03970  189 ALA A O   
1375 C CB  . ALA A 189 ? 0.48276 0.31097 0.19509 0.03906  -0.04778 0.03109  189 ALA A CB  
1376 N N   . CYS A 190 ? 0.63213 0.41774 0.26813 0.04148  -0.04375 0.04750  190 CYS A N   
1377 C CA  . CYS A 190 ? 0.57631 0.34426 0.19041 0.03902  -0.03450 0.05693  190 CYS A CA  
1378 C C   . CYS A 190 ? 0.59070 0.34520 0.19445 0.04571  -0.04553 0.06578  190 CYS A C   
1379 O O   . CYS A 190 ? 0.63034 0.38536 0.22608 0.05208  -0.05897 0.06502  190 CYS A O   
1380 C CB  . CYS A 190 ? 0.64245 0.40163 0.22535 0.03664  -0.02778 0.05676  190 CYS A CB  
1381 S SG  . CYS A 190 ? 0.71925 0.46092 0.27991 0.03009  -0.01144 0.06727  190 CYS A SG  
1382 N N   . CYS A 191 ? 0.62082 0.36566 0.22922 0.04414  -0.03997 0.07296  191 CYS A N   
1383 C CA  . CYS A 191 ? 0.60807 0.34186 0.21348 0.05065  -0.04906 0.08019  191 CYS A CA  
1384 C C   . CYS A 191 ? 0.65789 0.40461 0.28094 0.05951  -0.06541 0.07597  191 CYS A C   
1385 O O   . CYS A 191 ? 0.67229 0.41742 0.29163 0.06635  -0.07623 0.07827  191 CYS A O   
1386 C CB  . CYS A 191 ? 0.76443 0.48586 0.34475 0.05140  -0.04952 0.08572  191 CYS A CB  
1387 S SG  . CYS A 191 ? 0.86526 0.57328 0.42607 0.04064  -0.03012 0.09130  191 CYS A SG  
1388 N N   . ASN A 192 ? 0.60670 0.37160 0.25563 0.05818  -0.06586 0.06831  192 ASN A N   
1389 C CA  . ASN A 192 ? 0.62398 0.40598 0.29600 0.06444  -0.07893 0.06312  192 ASN A CA  
1390 C C   . ASN A 192 ? 0.61712 0.40604 0.27971 0.06801  -0.09124 0.05861  192 ASN A C   
1391 O O   . ASN A 192 ? 0.58021 0.38332 0.25987 0.07328  -0.10362 0.05488  192 ASN A O   
1392 C CB  . ASN A 192 ? 0.58110 0.35672 0.25881 0.07271  -0.08664 0.06897  192 ASN A CB  
1393 C CG  . ASN A 192 ? 0.60161 0.37032 0.29018 0.06895  -0.07544 0.07198  192 ASN A CG  
1394 O OD1 . ASN A 192 ? 0.64029 0.41740 0.34257 0.06078  -0.06416 0.06769  192 ASN A OD1 
1395 N ND2 . ASN A 192 ? 0.59402 0.34752 0.27711 0.07500  -0.07883 0.07883  192 ASN A ND2 
1396 N N   . GLN A 193 ? 0.55852 0.33871 0.19490 0.06493  -0.08794 0.05830  193 GLN A N   
1397 C CA  . GLN A 193 ? 0.58616 0.37350 0.21427 0.06623  -0.09733 0.05214  193 GLN A CA  
1398 C C   . GLN A 193 ? 0.59294 0.39056 0.22856 0.05991  -0.09188 0.04252  193 GLN A C   
1399 O O   . GLN A 193 ? 0.62972 0.42603 0.26842 0.05366  -0.07705 0.04178  193 GLN A O   
1400 C CB  . GLN A 193 ? 0.60371 0.37761 0.20304 0.06605  -0.09473 0.05655  193 GLN A CB  
1401 C CG  . GLN A 193 ? 0.64273 0.40285 0.23420 0.06981  -0.09423 0.06711  193 GLN A CG  
1402 C CD  . GLN A 193 ? 0.62949 0.39726 0.23559 0.07851  -0.10918 0.06800  193 GLN A CD  
1403 O OE1 . GLN A 193 ? 0.66248 0.43785 0.26521 0.08251  -0.12092 0.06483  193 GLN A OE1 
1404 N NE2 . GLN A 193 ? 0.68415 0.45138 0.30799 0.08156  -0.10878 0.07157  193 GLN A NE2 
1405 N N   . PHE A 194 ? 0.61457 0.42416 0.25687 0.06094  -0.10320 0.03440  194 PHE A N   
1406 C CA  . PHE A 194 ? 0.59197 0.41166 0.24540 0.05496  -0.09897 0.02415  194 PHE A CA  
1407 C C   . PHE A 194 ? 0.63010 0.44341 0.25635 0.05497  -0.10408 0.01866  194 PHE A C   
1408 O O   . PHE A 194 ? 0.66878 0.48186 0.28421 0.05937  -0.11749 0.01876  194 PHE A O   
1409 C CB  . PHE A 194 ? 0.53275 0.37177 0.22011 0.05429  -0.10682 0.01816  194 PHE A CB  
1410 C CG  . PHE A 194 ? 0.58419 0.43039 0.29710 0.05494  -0.10248 0.02270  194 PHE A CG  
1411 C CD1 . PHE A 194 ? 0.54385 0.39209 0.27053 0.04984  -0.08831 0.02234  194 PHE A CD1 
1412 C CD2 . PHE A 194 ? 0.50859 0.35967 0.23104 0.06130  -0.11265 0.02696  194 PHE A CD2 
1413 C CE1 . PHE A 194 ? 0.54381 0.39836 0.29250 0.05046  -0.08464 0.02591  194 PHE A CE1 
1414 C CE2 . PHE A 194 ? 0.48552 0.34243 0.22983 0.06250  -0.10841 0.03034  194 PHE A CE2 
1415 C CZ  . PHE A 194 ? 0.48395 0.34219 0.24070 0.05679  -0.09447 0.02975  194 PHE A CZ  
1416 N N   . PHE A 195 ? 0.63577 0.44633 0.25498 0.05002  -0.09264 0.01305  195 PHE A N   
1417 C CA  . PHE A 195 ? 0.62558 0.42871 0.21721 0.04975  -0.09440 0.00674  195 PHE A CA  
1418 C C   . PHE A 195 ? 0.65393 0.46533 0.26087 0.04534  -0.09179 -0.00519 195 PHE A C   
1419 O O   . PHE A 195 ? 0.59909 0.41625 0.22682 0.04185  -0.08047 -0.00658 195 PHE A O   
1420 C CB  . PHE A 195 ? 0.68700 0.47608 0.25034 0.04876  -0.08048 0.01200  195 PHE A CB  
1421 C CG  . PHE A 195 ? 0.68320 0.46484 0.23562 0.05172  -0.08184 0.02335  195 PHE A CG  
1422 C CD1 . PHE A 195 ? 0.73641 0.51392 0.29758 0.05199  -0.07656 0.03301  195 PHE A CD1 
1423 C CD2 . PHE A 195 ? 0.76468 0.54256 0.29793 0.05432  -0.08865 0.02417  195 PHE A CD2 
1424 C CE1 . PHE A 195 ? 0.77707 0.54556 0.32822 0.05485  -0.07809 0.04302  195 PHE A CE1 
1425 C CE2 . PHE A 195 ? 0.82463 0.59430 0.34711 0.05751  -0.09033 0.03482  195 PHE A CE2 
1426 C CZ  . PHE A 195 ? 0.75872 0.52315 0.29040 0.05781  -0.08506 0.04410  195 PHE A CZ  
1427 N N   . VAL A 196 ? 0.63122 0.44252 0.22773 0.04570  -0.10303 -0.01383 196 VAL A N   
1428 C CA  . VAL A 196 ? 0.65341 0.46740 0.25761 0.04178  -0.10079 -0.02582 196 VAL A CA  
1429 C C   . VAL A 196 ? 0.69192 0.49465 0.27028 0.04155  -0.08705 -0.02891 196 VAL A C   
1430 O O   . VAL A 196 ? 0.71893 0.51307 0.26788 0.04368  -0.08833 -0.02849 196 VAL A O   
1431 C CB  . VAL A 196 ? 0.73359 0.55061 0.33559 0.04146  -0.11836 -0.03474 196 VAL A CB  
1432 C CG1 . VAL A 196 ? 0.69924 0.51570 0.30868 0.03701  -0.11578 -0.04744 196 VAL A CG1 
1433 C CG2 . VAL A 196 ? 0.73015 0.56113 0.35886 0.04178  -0.13129 -0.03146 196 VAL A CG2 
1434 N N   . LEU A 197 ? 0.69152 0.49708 0.28468 0.03898  -0.07302 -0.03178 197 LEU A N   
1435 C CA  . LEU A 197 ? 0.68809 0.48625 0.26135 0.03910  -0.05918 -0.03652 197 LEU A CA  
1436 C C   . LEU A 197 ? 0.68936 0.48807 0.27100 0.03802  -0.06011 -0.04997 197 LEU A C   
1437 O O   . LEU A 197 ? 0.74813 0.55370 0.35693 0.03628  -0.05468 -0.05218 197 LEU A O   
1438 C CB  . LEU A 197 ? 0.58860 0.39004 0.17167 0.03774  -0.04176 -0.02951 197 LEU A CB  
1439 C CG  . LEU A 197 ? 0.64473 0.44326 0.21448 0.03778  -0.02549 -0.03477 197 LEU A CG  
1440 C CD1 . LEU A 197 ? 0.68837 0.47512 0.21773 0.03963  -0.02410 -0.03458 197 LEU A CD1 
1441 C CD2 . LEU A 197 ? 0.64243 0.44799 0.22834 0.03547  -0.00993 -0.02775 197 LEU A CD2 
1442 N N   . ASP A 198 ? 0.68362 0.47395 0.24128 0.03921  -0.06755 -0.05903 198 ASP A N   
1443 C CA  . ASP A 198 ? 0.70050 0.48766 0.26242 0.03845  -0.06728 -0.07256 198 ASP A CA  
1444 C C   . ASP A 198 ? 0.74146 0.52703 0.30053 0.04029  -0.04827 -0.07523 198 ASP A C   
1445 O O   . ASP A 198 ? 0.79883 0.58120 0.33541 0.04218  -0.03758 -0.07130 198 ASP A O   
1446 C CB  . ASP A 198 ? 0.71879 0.49946 0.25913 0.03871  -0.07821 -0.08161 198 ASP A CB  
1447 C CG  . ASP A 198 ? 0.88499 0.67115 0.43457 0.03645  -0.09760 -0.08062 198 ASP A CG  
1448 O OD1 . ASP A 198 ? 0.79985 0.59213 0.37338 0.03425  -0.10410 -0.07826 198 ASP A OD1 
1449 O OD2 . ASP A 198 ? 1.02431 0.81075 0.55932 0.03679  -0.10599 -0.08216 198 ASP A OD2 
1450 N N   . VAL A 199 ? 0.74833 0.53690 0.33111 0.03978  -0.04368 -0.08120 199 VAL A N   
1451 C CA  . VAL A 199 ? 0.76050 0.55029 0.34514 0.04252  -0.02635 -0.08409 199 VAL A CA  
1452 C C   . VAL A 199 ? 0.95204 0.73181 0.52454 0.04555  -0.02530 -0.09916 199 VAL A C   
1453 O O   . VAL A 199 ? 0.90546 0.68654 0.48716 0.04871  -0.01367 -0.10423 199 VAL A O   
1454 C CB  . VAL A 199 ? 0.73049 0.53169 0.35046 0.04130  -0.02004 -0.07823 199 VAL A CB  
1455 C CG1 . VAL A 199 ? 0.64132 0.45073 0.26742 0.03906  -0.01759 -0.06416 199 VAL A CG1 
1456 C CG2 . VAL A 199 ? 0.85536 0.65717 0.49927 0.03871  -0.03204 -0.08136 199 VAL A CG2 
1457 N N   . VAL A 200 ? 0.94457 0.71424 0.49600 0.04504  -0.03795 -0.10676 200 VAL A N   
1458 C CA  . VAL A 200 ? 0.86061 0.62273 0.40427 0.04652  -0.03874 -0.12041 200 VAL A CA  
1459 C C   . VAL A 200 ? 0.98180 0.74291 0.50212 0.04533  -0.04601 -0.12156 200 VAL A C   
1460 O O   . VAL A 200 ? 0.98362 0.74638 0.50299 0.04209  -0.06038 -0.11733 200 VAL A O   
1461 C CB  . VAL A 200 ? 1.01392 0.76918 0.57657 0.04397  -0.05005 -0.12871 200 VAL A CB  
1462 C CG1 . VAL A 200 ? 0.96410 0.71088 0.51733 0.04372  -0.05479 -0.14169 200 VAL A CG1 
1463 C CG2 . VAL A 200 ? 0.86591 0.62434 0.45594 0.04576  -0.04038 -0.12761 200 VAL A CG2 
1464 N N   . ILE A 201 ? 1.03011 0.78982 0.53203 0.04832  -0.03613 -0.12720 201 ILE A N   
1465 C CA  . ILE A 201 ? 1.05976 0.81743 0.53762 0.04773  -0.04232 -0.13049 201 ILE A CA  
1466 C C   . ILE A 201 ? 0.97613 0.72647 0.44909 0.04931  -0.04163 -0.14631 201 ILE A C   
1467 O O   . ILE A 201 ? 1.00030 0.75038 0.47418 0.05341  -0.02730 -0.15187 201 ILE A O   
1468 C CB  . ILE A 201 ? 0.98074 0.74337 0.43728 0.04936  -0.03077 -0.12191 201 ILE A CB  
1469 N N   . ASN A 202 ? 1.21607 0.96121 0.68473 0.04612  -0.05707 -0.15377 202 ASN A N   
1470 C CA  . ASN A 202 ? 1.12517 0.86137 0.58909 0.04658  -0.05876 -0.16947 202 ASN A CA  
1471 C C   . ASN A 202 ? 1.15512 0.88535 0.64018 0.04872  -0.05174 -0.17615 202 ASN A C   
1472 O O   . ASN A 202 ? 1.21919 0.94403 0.69950 0.05280  -0.04278 -0.18654 202 ASN A O   
1473 C CB  . ASN A 202 ? 1.19731 0.93357 0.63367 0.05019  -0.04935 -0.17460 202 ASN A CB  
1474 N N   . PHE A 203 ? 1.15417 0.88548 0.66283 0.04636  -0.05600 -0.16994 203 PHE A N   
1475 C CA  . PHE A 203 ? 1.25857 0.98422 0.78994 0.04801  -0.05137 -0.17359 203 PHE A CA  
1476 C C   . PHE A 203 ? 1.19559 0.92583 0.72919 0.05530  -0.03224 -0.17202 203 PHE A C   
1477 O O   . PHE A 203 ? 1.25632 0.98198 0.80702 0.05863  -0.02686 -0.17615 203 PHE A O   
1478 C CB  . PHE A 203 ? 0.95097 0.66317 0.48632 0.04617  -0.05848 -0.18756 203 PHE A CB  
1479 C CG  . PHE A 203 ? 0.91525 0.62496 0.45410 0.03775  -0.07719 -0.18927 203 PHE A CG  
1480 C CD1 . PHE A 203 ? 0.99307 0.70290 0.55542 0.03209  -0.08641 -0.18456 203 PHE A CD1 
1481 C CD2 . PHE A 203 ? 0.95206 0.66133 0.47129 0.03523  -0.08548 -0.19525 203 PHE A CD2 
1482 C CE1 . PHE A 203 ? 0.89767 0.60850 0.46594 0.02369  -0.10319 -0.18607 203 PHE A CE1 
1483 C CE2 . PHE A 203 ? 0.83235 0.54219 0.35699 0.02734  -0.10276 -0.19697 203 PHE A CE2 
1484 C CZ  . PHE A 203 ? 0.85523 0.56666 0.40546 0.02140  -0.11140 -0.19236 203 PHE A CZ  
1485 N N   . ARG A 204 ? 1.03859 0.77853 0.55661 0.05762  -0.02192 -0.16559 204 ARG A N   
1486 C CA  . ARG A 204 ? 1.16005 0.90838 0.68129 0.06332  -0.00321 -0.16314 204 ARG A CA  
1487 C C   . ARG A 204 ? 1.17010 0.92828 0.70039 0.06159  0.00058  -0.14851 204 ARG A C   
1488 O O   . ARG A 204 ? 1.00093 0.76318 0.51833 0.05811  -0.00290 -0.13931 204 ARG A O   
1489 C CB  . ARG A 204 ? 0.99527 0.74809 0.49278 0.06597  0.00720  -0.16683 204 ARG A CB  
1490 N N   . ARG A 205 ? 1.10508 0.86644 0.65746 0.06425  0.00727  -0.14638 205 ARG A N   
1491 C CA  . ARG A 205 ? 0.94711 0.71786 0.50969 0.06279  0.01214  -0.13357 205 ARG A CA  
1492 C C   . ARG A 205 ? 0.91237 0.69356 0.45950 0.06217  0.02424  -0.12557 205 ARG A C   
1493 O O   . ARG A 205 ? 0.89482 0.68133 0.43422 0.06551  0.03693  -0.13036 205 ARG A O   
1494 C CB  . ARG A 205 ? 0.88252 0.65745 0.47054 0.06722  0.02062  -0.13451 205 ARG A CB  
1495 C CG  . ARG A 205 ? 0.94207 0.73442 0.55133 0.06446  0.02800  -0.12045 205 ARG A CG  
1496 C CD  . ARG A 205 ? 1.00152 0.79868 0.64552 0.06348  0.02332  -0.11668 205 ARG A CD  
1497 N NE  . ARG A 205 ? 0.98919 0.78855 0.64877 0.07049  0.03216  -0.12335 205 ARG A NE  
1498 C CZ  . ARG A 205 ? 0.92478 0.73992 0.60235 0.07327  0.04424  -0.11863 205 ARG A CZ  
1499 N NH1 . ARG A 205 ? 0.82856 0.65770 0.50928 0.06891  0.05046  -0.10786 205 ARG A NH1 
1500 N NH2 . ARG A 205 ? 0.77093 0.58746 0.46407 0.08062  0.04965  -0.12496 205 ARG A NH2 
1501 N N   . LEU A 206 ? 0.97634 0.76017 0.51905 0.05760  0.02003  -0.11332 206 LEU A N   
1502 C CA  . LEU A 206 ? 0.85099 0.64250 0.37930 0.05576  0.03078  -0.10403 206 LEU A CA  
1503 C C   . LEU A 206 ? 0.84118 0.64482 0.38330 0.05761  0.04930  -0.10155 206 LEU A C   
1504 O O   . LEU A 206 ? 0.75438 0.56236 0.31971 0.05837  0.05094  -0.09961 206 LEU A O   
1505 C CB  . LEU A 206 ? 0.73693 0.52719 0.26088 0.05100  0.02181  -0.09084 206 LEU A CB  
1506 C CG  . LEU A 206 ? 0.99253 0.77745 0.49290 0.04902  0.01147  -0.08811 206 LEU A CG  
1507 C CD1 . LEU A 206 ? 0.93381 0.71096 0.43152 0.04970  -0.00407 -0.09921 206 LEU A CD1 
1508 C CD2 . LEU A 206 ? 0.92103 0.70582 0.42066 0.04570  0.00433  -0.07396 206 LEU A CD2 
1509 N N   . SER A 207 ? 0.80181 0.61327 0.33214 0.05785  0.06301  -0.10146 207 SER A N   
1510 C CA  . SER A 207 ? 0.86963 0.69610 0.41399 0.05840  0.08100  -0.09865 207 SER A CA  
1511 C C   . SER A 207 ? 0.75102 0.58206 0.29946 0.05218  0.08435  -0.08366 207 SER A C   
1512 O O   . SER A 207 ? 0.74698 0.56932 0.28347 0.04815  0.07390  -0.07513 207 SER A O   
1513 C CB  . SER A 207 ? 0.80228 0.63718 0.33307 0.05964  0.09442  -0.10332 207 SER A CB  
1514 O OG  . SER A 207 ? 0.82461 0.65730 0.33221 0.05430  0.09446  -0.09419 207 SER A OG  
1515 N N   . GLU A 208 ? 0.81607 0.66158 0.38267 0.05146  0.09900  -0.08068 208 GLU A N   
1516 C CA  . GLU A 208 ? 0.89551 0.74586 0.46717 0.04453  0.10414  -0.06701 208 GLU A CA  
1517 C C   . GLU A 208 ? 0.77012 0.61705 0.31771 0.03888  0.10646  -0.05809 208 GLU A C   
1518 O O   . GLU A 208 ? 0.73637 0.57738 0.27969 0.03351  0.10221  -0.04616 208 GLU A O   
1519 C CB  . GLU A 208 ? 0.86938 0.73860 0.46532 0.04407  0.12043  -0.06690 208 GLU A CB  
1520 C CG  . GLU A 208 ? 0.77762 0.65633 0.40976 0.04797  0.11523  -0.07139 208 GLU A CG  
1521 C CD  . GLU A 208 ? 0.88183 0.78192 0.54195 0.04569  0.12810  -0.06821 208 GLU A CD  
1522 O OE1 . GLU A 208 ? 0.78015 0.68527 0.43718 0.03788  0.13604  -0.05866 208 GLU A OE1 
1523 O OE2 . GLU A 208 ? 1.06941 0.98074 0.75435 0.05155  0.12982  -0.07514 208 GLU A OE2 
1524 N N   . GLY A 209 ? 0.77796 0.62833 0.30973 0.04038  0.11342  -0.06358 209 GLY A N   
1525 C CA  . GLY A 209 ? 0.71504 0.56083 0.22150 0.03582  0.11484  -0.05540 209 GLY A CA  
1526 C C   . GLY A 209 ? 0.84477 0.67320 0.33191 0.03610  0.09646  -0.05194 209 GLY A C   
1527 O O   . GLY A 209 ? 0.80420 0.62593 0.27885 0.03168  0.09318  -0.03995 209 GLY A O   
1528 N N   . ASP A 210 ? 0.88018 0.70139 0.36584 0.04130  0.08379  -0.06246 210 ASP A N   
1529 C CA  . ASP A 210 ? 0.76265 0.57039 0.23413 0.04146  0.06504  -0.06011 210 ASP A CA  
1530 C C   . ASP A 210 ? 0.83380 0.63733 0.31770 0.03876  0.05596  -0.04964 210 ASP A C   
1531 O O   . ASP A 210 ? 0.74492 0.54061 0.21672 0.03719  0.04521  -0.04117 210 ASP A O   
1532 C CB  . ASP A 210 ? 0.88206 0.68426 0.35410 0.04629  0.05352  -0.07421 210 ASP A CB  
1533 C CG  . ASP A 210 ? 0.94965 0.75428 0.40779 0.04950  0.06094  -0.08564 210 ASP A CG  
1534 O OD1 . ASP A 210 ? 0.88187 0.68735 0.31802 0.04797  0.06623  -0.08216 210 ASP A OD1 
1535 O OD2 . ASP A 210 ? 1.05769 0.86275 0.52673 0.05377  0.06127  -0.09821 210 ASP A OD2 
1536 N N   . LEU A 211 ? 0.77330 0.58237 0.28175 0.03890  0.05971  -0.05046 211 LEU A N   
1537 C CA  . LEU A 211 ? 0.79314 0.59912 0.31411 0.03659  0.05165  -0.04143 211 LEU A CA  
1538 C C   . LEU A 211 ? 0.71166 0.51738 0.22704 0.03116  0.05843  -0.02706 211 LEU A C   
1539 O O   . LEU A 211 ? 0.69152 0.48965 0.20381 0.02986  0.04760  -0.01804 211 LEU A O   
1540 C CB  . LEU A 211 ? 0.66826 0.48538 0.22433 0.03721  0.05459  -0.04517 211 LEU A CB  
1541 C CG  . LEU A 211 ? 0.81344 0.62994 0.38285 0.04162  0.04480  -0.05717 211 LEU A CG  
1542 C CD1 . LEU A 211 ? 0.62231 0.45213 0.22594 0.04285  0.05195  -0.06062 211 LEU A CD1 
1543 C CD2 . LEU A 211 ? 0.72882 0.53926 0.30346 0.04071  0.02534  -0.05488 211 LEU A CD2 
1544 N N   . PHE A 212 ? 0.67501 0.48937 0.19067 0.02795  0.07613  -0.02505 212 PHE A N   
1545 C CA  . PHE A 212 ? 0.80723 0.62029 0.31580 0.02164  0.08387  -0.01190 212 PHE A CA  
1546 C C   . PHE A 212 ? 0.76705 0.56756 0.24942 0.02186  0.07390  -0.00533 212 PHE A C   
1547 O O   . PHE A 212 ? 0.84085 0.63259 0.31996 0.01954  0.06753  0.00597  212 PHE A O   
1548 C CB  . PHE A 212 ? 0.68877 0.51518 0.20000 0.01824  0.10398  -0.01334 212 PHE A CB  
1549 C CG  . PHE A 212 ? 0.86478 0.68970 0.36764 0.01065  0.11309  -0.00037 212 PHE A CG  
1550 C CD1 . PHE A 212 ? 0.85172 0.67758 0.37100 0.00444  0.11729  0.00878  212 PHE A CD1 
1551 C CD2 . PHE A 212 ? 0.79285 0.61510 0.27148 0.00939  0.11776  0.00237  212 PHE A CD2 
1552 C CE1 . PHE A 212 ? 0.77887 0.60160 0.29108 -0.00323 0.12552  0.02043  212 PHE A CE1 
1553 C CE2 . PHE A 212 ? 0.87872 0.69827 0.34923 0.00207  0.12634  0.01468  212 PHE A CE2 
1554 C CZ  . PHE A 212 ? 0.82805 0.64725 0.31570 -0.00441 0.13011  0.02365  212 PHE A CZ  
1555 N N   . THR A 213 ? 0.77209 0.57163 0.23580 0.02518  0.07225  -0.01269 213 THR A N   
1556 C CA  . THR A 213 ? 0.85167 0.64059 0.28942 0.02599  0.06278  -0.00735 213 THR A CA  
1557 C C   . THR A 213 ? 0.78362 0.56320 0.22344 0.02870  0.04275  -0.00377 213 THR A C   
1558 O O   . THR A 213 ? 0.82028 0.59118 0.24825 0.02809  0.03601  0.00683  213 THR A O   
1559 C CB  . THR A 213 ? 0.83583 0.62638 0.25544 0.02964  0.06293  -0.01846 213 THR A CB  
1560 O OG1 . THR A 213 ? 0.85179 0.65260 0.26892 0.02738  0.08211  -0.02080 213 THR A OG1 
1561 C CG2 . THR A 213 ? 0.88200 0.66225 0.27457 0.03098  0.05159  -0.01367 213 THR A CG2 
1562 N N   . GLN A 214 ? 0.75163 0.53348 0.20774 0.03187  0.03310  -0.01242 214 GLN A N   
1563 C CA  . GLN A 214 ? 0.81530 0.59172 0.27678 0.03432  0.01395  -0.01009 214 GLN A CA  
1564 C C   . GLN A 214 ? 0.78440 0.55850 0.25886 0.03204  0.01324  0.00206  214 GLN A C   
1565 O O   . GLN A 214 ? 0.76710 0.53508 0.23803 0.03373  0.00055  0.00938  214 GLN A O   
1566 C CB  . GLN A 214 ? 0.74155 0.52169 0.21866 0.03712  0.00518  -0.02253 214 GLN A CB  
1567 C CG  . GLN A 214 ? 0.77869 0.55834 0.24259 0.03970  0.00187  -0.03538 214 GLN A CG  
1568 C CD  . GLN A 214 ? 0.85019 0.62432 0.29530 0.04130  -0.01287 -0.03413 214 GLN A CD  
1569 O OE1 . GLN A 214 ? 0.87725 0.64775 0.30261 0.04079  -0.00984 -0.02627 214 GLN A OE1 
1570 N NE2 . GLN A 214 ? 0.86607 0.64002 0.31795 0.04295  -0.02913 -0.04178 214 GLN A NE2 
1571 N N   . LEU A 215 ? 0.68272 0.46229 0.17333 0.02856  0.02652  0.00378  215 LEU A N   
1572 C CA  . LEU A 215 ? 0.71703 0.49425 0.22083 0.02586  0.02675  0.01438  215 LEU A CA  
1573 C C   . LEU A 215 ? 0.72023 0.48830 0.20859 0.02307  0.02958  0.02702  215 LEU A C   
1574 O O   . LEU A 215 ? 0.76723 0.52824 0.25953 0.02356  0.02151  0.03592  215 LEU A O   
1575 C CB  . LEU A 215 ? 0.68800 0.47439 0.21178 0.02210  0.04147  0.01251  215 LEU A CB  
1576 C CG  . LEU A 215 ? 0.71522 0.51490 0.27008 0.02468  0.03611  0.00182  215 LEU A CG  
1577 C CD1 . LEU A 215 ? 0.65680 0.47136 0.23711 0.02162  0.05101  -0.00156 215 LEU A CD1 
1578 C CD2 . LEU A 215 ? 0.62880 0.42989 0.20478 0.02619  0.02051  0.00482  215 LEU A CD2 
1579 N N   . ARG A 216 ? 0.75650 0.52442 0.22757 0.02035  0.04120  0.02791  216 ARG A N   
1580 C CA  . ARG A 216 ? 0.94117 0.69865 0.39396 0.01798  0.04286  0.03975  216 ARG A CA  
1581 C C   . ARG A 216 ? 0.86281 0.61073 0.30203 0.02387  0.02424  0.04293  216 ARG A C   
1582 O O   . ARG A 216 ? 0.82809 0.56591 0.26358 0.02403  0.01916  0.05378  216 ARG A O   
1583 C CB  . ARG A 216 ? 0.94107 0.70163 0.37593 0.01467  0.05741  0.03884  216 ARG A CB  
1584 C CG  . ARG A 216 ? 0.94359 0.70994 0.38749 0.00662  0.07681  0.04369  216 ARG A CG  
1585 C CD  . ARG A 216 ? 1.13596 0.91072 0.56590 0.00485  0.09055  0.03888  216 ARG A CD  
1586 N NE  . ARG A 216 ? 0.96518 0.74413 0.39680 -0.00353 0.10817  0.04622  216 ARG A NE  
1587 C CZ  . ARG A 216 ? 1.11446 0.89976 0.53167 -0.00613 0.12090  0.04552  216 ARG A CZ  
1588 N NH1 . ARG A 216 ? 0.96058 0.74784 0.35915 -0.00075 0.11827  0.03766  216 ARG A NH1 
1589 N NH2 . ARG A 216 ? 1.07017 0.86043 0.49201 -0.01463 0.13657  0.05263  216 ARG A NH2 
1590 N N   . LYS A 217 ? 0.82792 0.57909 0.26010 0.02881  0.01380  0.03322  217 LYS A N   
1591 C CA  . LYS A 217 ? 0.83616 0.58129 0.25833 0.03429  -0.00463 0.03540  217 LYS A CA  
1592 C C   . LYS A 217 ? 0.85824 0.60217 0.30041 0.03682  -0.01659 0.04011  217 LYS A C   
1593 O O   . LYS A 217 ? 0.79806 0.53463 0.23448 0.04004  -0.02656 0.04839  217 LYS A O   
1594 C CB  . LYS A 217 ? 0.81704 0.56758 0.23315 0.03807  -0.01444 0.02259  217 LYS A CB  
1595 C CG  . LYS A 217 ? 0.87710 0.62862 0.27097 0.03697  -0.00472 0.01676  217 LYS A CG  
1596 C CD  . LYS A 217 ? 0.82846 0.58410 0.21872 0.04060  -0.01619 0.00311  217 LYS A CD  
1597 C CE  . LYS A 217 ? 0.91369 0.67172 0.28588 0.03988  -0.00532 -0.00532 217 LYS A CE  
1598 N NZ  . LYS A 217 ? 1.03761 0.79820 0.40810 0.04294  -0.01698 -0.01943 217 LYS A NZ  
1599 N N   . ILE A 218 ? 0.76551 0.51699 0.23142 0.03580  -0.01527 0.03497  218 ILE A N   
1600 C CA  . ILE A 218 ? 0.75735 0.50994 0.24389 0.03836  -0.02621 0.03825  218 ILE A CA  
1601 C C   . ILE A 218 ? 0.83093 0.57439 0.31905 0.03645  -0.02114 0.05114  218 ILE A C   
1602 O O   . ILE A 218 ? 0.78499 0.52370 0.27623 0.04076  -0.03277 0.05731  218 ILE A O   
1603 C CB  . ILE A 218 ? 0.82661 0.58912 0.33592 0.03714  -0.02417 0.02989  218 ILE A CB  
1604 C CG1 . ILE A 218 ? 0.68530 0.45432 0.19404 0.03957  -0.03275 0.01706  218 ILE A CG1 
1605 C CG2 . ILE A 218 ? 0.74574 0.51028 0.27692 0.03897  -0.03249 0.03417  218 ILE A CG2 
1606 C CD1 . ILE A 218 ? 0.65620 0.43320 0.18405 0.03832  -0.02939 0.00789  218 ILE A CD1 
1607 N N   . VAL A 219 ? 0.70052 0.44182 0.18751 0.02992  -0.00368 0.05488  219 VAL A N   
1608 C CA  . VAL A 219 ? 0.74884 0.48034 0.23819 0.02663  0.00199  0.06641  219 VAL A CA  
1609 C C   . VAL A 219 ? 0.81402 0.53249 0.28250 0.02947  -0.00429 0.07537  219 VAL A C   
1610 O O   . VAL A 219 ? 0.78740 0.49625 0.25938 0.03132  -0.00952 0.08384  219 VAL A O   
1611 C CB  . VAL A 219 ? 0.73005 0.46380 0.22214 0.01774  0.02242  0.06776  219 VAL A CB  
1612 C CG1 . VAL A 219 ? 0.76448 0.48593 0.25503 0.01291  0.02867  0.07971  219 VAL A CG1 
1613 C CG2 . VAL A 219 ? 0.66899 0.41498 0.18482 0.01578  0.02738  0.06040  219 VAL A CG2 
1614 N N   . LYS A 220 ? 0.82285 0.54055 0.26901 0.03054  -0.00443 0.07329  220 LYS A N   
1615 C CA  . LYS A 220 ? 0.79939 0.50480 0.22354 0.03364  -0.01065 0.08194  220 LYS A CA  
1616 C C   . LYS A 220 ? 0.88340 0.58838 0.31252 0.04250  -0.03106 0.08207  220 LYS A C   
1617 O O   . LYS A 220 ? 0.93654 0.63059 0.36097 0.04589  -0.03727 0.09139  220 LYS A O   
1618 C CB  . LYS A 220 ? 0.82906 0.53518 0.22753 0.03260  -0.00550 0.07899  220 LYS A CB  
1619 C CG  . LYS A 220 ? 0.86890 0.56237 0.24150 0.03592  -0.01186 0.08809  220 LYS A CG  
1620 C CD  . LYS A 220 ? 1.06257 0.75643 0.40907 0.03331  -0.00295 0.08640  220 LYS A CD  
1621 C CE  . LYS A 220 ? 1.39858 1.08225 0.73130 0.02634  0.01296  0.09761  220 LYS A CE  
1622 N NZ  . LYS A 220 ? 1.18239 0.87072 0.49436 0.02243  0.02569  0.09456  220 LYS A NZ  
1623 N N   . MET A 221 ? 0.78193 0.49924 0.22098 0.04633  -0.04173 0.07150  221 MET A N   
1624 C CA  . MET A 221 ? 0.86006 0.58106 0.30776 0.05413  -0.06103 0.07053  221 MET A CA  
1625 C C   . MET A 221 ? 0.90825 0.62882 0.37962 0.05622  -0.06476 0.07521  221 MET A C   
1626 O O   . MET A 221 ? 0.82811 0.54552 0.30219 0.06263  -0.07656 0.08032  221 MET A O   
1627 C CB  . MET A 221 ? 0.80777 0.54311 0.26401 0.05591  -0.07052 0.05747  221 MET A CB  
1628 C CG  . MET A 221 ? 0.83378 0.56991 0.26681 0.05696  -0.07463 0.05192  221 MET A CG  
1629 S SD  . MET A 221 ? 0.95134 0.70296 0.39781 0.05808  -0.08674 0.03583  221 MET A SD  
1630 C CE  . MET A 221 ? 0.93254 0.68757 0.38700 0.05151  -0.06934 0.02779  221 MET A CE  
1631 N N   . ALA A 222 ? 0.78387 0.50832 0.27288 0.05136  -0.05488 0.07309  222 ALA A N   
1632 C CA  . ALA A 222 ? 0.78442 0.50954 0.29652 0.05331  -0.05820 0.07634  222 ALA A CA  
1633 C C   . ALA A 222 ? 0.83159 0.54070 0.33726 0.05372  -0.05506 0.08809  222 ALA A C   
1634 O O   . ALA A 222 ? 0.86160 0.56954 0.38294 0.05830  -0.06214 0.09113  222 ALA A O   
1635 C CB  . ALA A 222 ? 0.71906 0.45142 0.24892 0.04753  -0.04754 0.07160  222 ALA A CB  
1636 N N   . SER A 223 ? 0.92813 0.62492 0.41130 0.04914  -0.04466 0.09444  223 SER A N   
1637 C CA  . SER A 223 ? 1.04592 0.72511 0.52015 0.04825  -0.04063 0.10588  223 SER A CA  
1638 C C   . SER A 223 ? 0.91567 0.58614 0.37462 0.05652  -0.05373 0.11177  223 SER A C   
1639 O O   . SER A 223 ? 1.23936 0.89334 0.68899 0.05685  -0.05182 0.12162  223 SER A O   
1640 C CB  . SER A 223 ? 0.91003 0.58116 0.36793 0.03843  -0.02255 0.11027  223 SER A CB  
1641 O OG  . SER A 223 ? 1.06225 0.74402 0.53450 0.03119  -0.01041 0.10398  223 SER A OG  
1642 N N   . ASN A 224 ? 0.97877 0.65960 0.43506 0.06301  -0.06712 0.10596  224 ASN A N   
1643 C CA  . ASN A 224 ? 0.96508 0.63965 0.40596 0.07097  -0.07995 0.11102  224 ASN A CA  
1644 C C   . ASN A 224 ? 1.09010 0.76877 0.55211 0.07985  -0.09392 0.11150  224 ASN A C   
1645 O O   . ASN A 224 ? 0.95015 0.64618 0.43239 0.08339  -0.10348 0.10301  224 ASN A O   
1646 C CB  . ASN A 224 ? 0.97480 0.65934 0.40172 0.07292  -0.08736 0.10402  224 ASN A CB  
1647 C CG  . ASN A 224 ? 0.97877 0.65799 0.38882 0.08106  -0.10102 0.10912  224 ASN A CG  
1648 O OD1 . ASN A 224 ? 1.03769 0.70451 0.44495 0.08561  -0.10437 0.11852  224 ASN A OD1 
1649 N ND2 . ASN A 224 ? 1.10812 0.79621 0.50620 0.08302  -0.10908 0.10274  224 ASN A ND2 
1650 N N   . ALA A 225 ? 1.19286 0.85580 0.65024 0.08356  -0.09507 0.12128  225 ALA A N   
1651 C CA  . ALA A 225 ? 1.08526 0.75190 0.56335 0.09257  -0.10695 0.12162  225 ALA A CA  
1652 C C   . ALA A 225 ? 0.95959 0.63799 0.43787 0.10234  -0.12486 0.11858  225 ALA A C   
1653 O O   . ALA A 225 ? 0.93055 0.62095 0.43189 0.10948  -0.13547 0.11512  225 ALA A O   
1654 C CB  . ALA A 225 ? 0.96149 0.60643 0.43369 0.09418  -0.10317 0.13244  225 ALA A CB  
1655 N N   . ALA A 226 ? 0.90990 0.58651 0.36380 0.10275  -0.12847 0.11944  226 ALA A N   
1656 C CA  . ALA A 226 ? 1.07048 0.75943 0.52542 0.11160  -0.14613 0.11615  226 ALA A CA  
1657 C C   . ALA A 226 ? 1.00142 0.71481 0.47651 0.11035  -0.15273 0.10324  226 ALA A C   
1658 O O   . ALA A 226 ? 0.94130 0.66952 0.42718 0.11716  -0.16792 0.09897  226 ALA A O   
1659 C CB  . ALA A 226 ? 0.92874 0.60753 0.34999 0.11282  -0.14891 0.12136  226 ALA A CB  
1660 N N   . ALA A 227 ? 0.83949 0.55763 0.32077 0.10167  -0.14174 0.09698  227 ALA A N   
1661 C CA  . ALA A 227 ? 0.90415 0.64328 0.40487 0.09959  -0.14684 0.08491  227 ALA A CA  
1662 C C   . ALA A 227 ? 0.87637 0.62439 0.40769 0.09808  -0.14327 0.08154  227 ALA A C   
1663 O O   . ALA A 227 ? 0.77822 0.54319 0.32764 0.09584  -0.14680 0.07203  227 ALA A O   
1664 C CB  . ALA A 227 ? 0.90479 0.64374 0.38870 0.09162  -0.13826 0.07893  227 ALA A CB  
1665 N N   . ARG A 228 ? 0.75403 0.49069 0.29126 0.09917  -0.13674 0.08893  228 ARG A N   
1666 C CA  . ARG A 228 ? 0.79395 0.53747 0.35776 0.09726  -0.13184 0.08610  228 ARG A CA  
1667 C C   . ARG A 228 ? 0.70060 0.46493 0.29278 0.10394  -0.14541 0.08023  228 ARG A C   
1668 O O   . ARG A 228 ? 0.71586 0.48286 0.31105 0.11242  -0.15657 0.08292  228 ARG A O   
1669 C CB  . ARG A 228 ? 0.74993 0.47534 0.31216 0.09718  -0.12278 0.09514  228 ARG A CB  
1670 C CG  . ARG A 228 ? 0.85118 0.58153 0.43757 0.09398  -0.11562 0.09238  228 ARG A CG  
1671 C CD  . ARG A 228 ? 0.84739 0.55798 0.43035 0.09264  -0.10620 0.10072  228 ARG A CD  
1672 N NE  . ARG A 228 ? 1.07974 0.79551 0.68526 0.08970  -0.09999 0.09756  228 ARG A NE  
1673 C CZ  . ARG A 228 ? 1.08297 0.79493 0.68774 0.08024  -0.08647 0.09691  228 ARG A CZ  
1674 N NH1 . ARG A 228 ? 1.05542 0.75866 0.63904 0.07250  -0.07645 0.09918  228 ARG A NH1 
1675 N NH2 . ARG A 228 ? 0.78684 0.50477 0.41293 0.07865  -0.08264 0.09383  228 ARG A NH2 
1676 N N   . LEU A 229 ? 0.66458 0.44433 0.27793 0.10009  -0.14423 0.07230  229 LEU A N   
1677 C CA  . LEU A 229 ? 0.68299 0.48490 0.32565 0.10464  -0.15532 0.06617  229 LEU A CA  
1678 C C   . LEU A 229 ? 0.71177 0.51633 0.37762 0.10543  -0.14972 0.06704  229 LEU A C   
1679 O O   . LEU A 229 ? 0.64361 0.43421 0.30351 0.10073  -0.13710 0.07072  229 LEU A O   
1680 C CB  . LEU A 229 ? 0.62998 0.44882 0.28025 0.09931  -0.15955 0.05582  229 LEU A CB  
1681 C CG  . LEU A 229 ? 0.68383 0.50319 0.31400 0.09863  -0.16689 0.05263  229 LEU A CG  
1682 C CD1 . LEU A 229 ? 0.68744 0.51933 0.32407 0.09192  -0.16857 0.04189  229 LEU A CD1 
1683 C CD2 . LEU A 229 ? 0.81215 0.64084 0.44656 0.10704  -0.18202 0.05381  229 LEU A CD2 
1684 N N   . PRO A 230 ? 0.58965 0.41279 0.28254 0.11116  -0.15852 0.06352  230 PRO A N   
1685 C CA  . PRO A 230 ? 0.56597 0.39270 0.28110 0.11267  -0.15336 0.06378  230 PRO A CA  
1686 C C   . PRO A 230 ? 0.55303 0.38237 0.27485 0.10409  -0.14367 0.05973  230 PRO A C   
1687 O O   . PRO A 230 ? 0.59666 0.43258 0.31474 0.09809  -0.14409 0.05428  230 PRO A O   
1688 C CB  . PRO A 230 ? 0.57302 0.42466 0.31609 0.11947  -0.16528 0.05886  230 PRO A CB  
1689 C CG  . PRO A 230 ? 0.73916 0.59098 0.46920 0.12491  -0.17645 0.06063  230 PRO A CG  
1690 C CD  . PRO A 230 ? 0.64201 0.48236 0.34489 0.11771  -0.17347 0.06042  230 PRO A CD  
1691 N N   . PRO A 231 ? 0.52565 0.34998 0.25769 0.10357  -0.13523 0.06179  231 PRO A N   
1692 C CA  . PRO A 231 ? 0.50346 0.32897 0.24027 0.09564  -0.12558 0.05878  231 PRO A CA  
1693 C C   . PRO A 231 ? 0.51553 0.36599 0.28144 0.09510  -0.13011 0.05109  231 PRO A C   
1694 O O   . PRO A 231 ? 0.54609 0.40529 0.33470 0.09430  -0.12408 0.04940  231 PRO A O   
1695 C CB  . PRO A 231 ? 0.54397 0.35269 0.27862 0.09535  -0.11515 0.06460  231 PRO A CB  
1696 C CG  . PRO A 231 ? 0.51419 0.32322 0.25834 0.10509  -0.12210 0.06719  231 PRO A CG  
1697 C CD  . PRO A 231 ? 0.59672 0.41005 0.33190 0.10987  -0.13331 0.06745  231 PRO A CD  
1698 N N   . ILE A 232 ? 0.47922 0.34348 0.24771 0.09302  -0.13828 0.04518  232 ILE A N   
1699 C CA  . ILE A 232 ? 0.44426 0.33497 0.24388 0.09045  -0.14203 0.03739  232 ILE A CA  
1700 C C   . ILE A 232 ? 0.46940 0.36665 0.28726 0.08159  -0.12798 0.03402  232 ILE A C   
1701 O O   . ILE A 232 ? 0.43816 0.35411 0.28348 0.08091  -0.12772 0.03042  232 ILE A O   
1702 C CB  . ILE A 232 ? 0.51173 0.41141 0.30646 0.08758  -0.15228 0.03147  232 ILE A CB  
1703 C CG1 . ILE A 232 ? 0.58095 0.47817 0.36275 0.09477  -0.16344 0.03409  232 ILE A CG1 
1704 C CG2 . ILE A 232 ? 0.45224 0.37846 0.27906 0.08346  -0.15629 0.02377  232 ILE A CG2 
1705 C CD1 . ILE A 232 ? 0.52733 0.43773 0.33017 0.10351  -0.16970 0.03590  232 ILE A CD1 
1706 N N   . GLY A 233 ? 0.43486 0.31775 0.23790 0.07503  -0.11607 0.03532  233 GLY A N   
1707 C CA  . GLY A 233 ? 0.41028 0.29968 0.22991 0.06744  -0.10367 0.03221  233 GLY A CA  
1708 C C   . GLY A 233 ? 0.47298 0.36718 0.31120 0.06998  -0.09884 0.03408  233 GLY A C   
1709 O O   . GLY A 233 ? 0.43672 0.34331 0.29511 0.06539  -0.09246 0.03055  233 GLY A O   
1710 N N   . LEU A 234 ? 0.47668 0.35984 0.30703 0.07760  -0.10183 0.03959  234 LEU A N   
1711 C CA  . LEU A 234 ? 0.47466 0.36146 0.32169 0.08137  -0.09849 0.04039  234 LEU A CA  
1712 C C   . LEU A 234 ? 0.42065 0.33313 0.29657 0.08317  -0.10305 0.03506  234 LEU A C   
1713 O O   . LEU A 234 ? 0.36069 0.28160 0.25406 0.08225  -0.09662 0.03322  234 LEU A O   
1714 C CB  . LEU A 234 ? 0.42765 0.29761 0.26055 0.09105  -0.10400 0.04668  234 LEU A CB  
1715 C CG  . LEU A 234 ? 0.52431 0.39027 0.36769 0.09550  -0.09971 0.04788  234 LEU A CG  
1716 C CD1 . LEU A 234 ? 0.45888 0.31594 0.30064 0.08631  -0.08564 0.04788  234 LEU A CD1 
1717 C CD2 . LEU A 234 ? 0.53713 0.38298 0.36309 0.10570  -0.10658 0.05448  234 LEU A CD2 
1718 N N   . LEU A 235 ? 0.36111 0.28678 0.24221 0.08542  -0.11405 0.03243  235 LEU A N   
1719 C CA  . LEU A 235 ? 0.42193 0.37339 0.33122 0.08606  -0.11797 0.02763  235 LEU A CA  
1720 C C   . LEU A 235 ? 0.31788 0.28036 0.24217 0.07578  -0.10870 0.02352  235 LEU A C   
1721 O O   . LEU A 235 ? 0.36158 0.34169 0.30865 0.07544  -0.10641 0.02107  235 LEU A O   
1722 C CB  . LEU A 235 ? 0.40931 0.37285 0.32071 0.08904  -0.13217 0.02528  235 LEU A CB  
1723 C CG  . LEU A 235 ? 0.38254 0.33845 0.28071 0.10077  -0.14405 0.02926  235 LEU A CG  
1724 C CD1 . LEU A 235 ? 0.43620 0.40541 0.33565 0.10124  -0.15811 0.02569  235 LEU A CD1 
1725 C CD2 . LEU A 235 ? 0.37388 0.33697 0.28723 0.11148  -0.14613 0.03062  235 LEU A CD2 
1726 N N   . THR A 236 ? 0.33164 0.28373 0.24295 0.06791  -0.10287 0.02290  236 THR A N   
1727 C CA  . THR A 236 ? 0.29899 0.25955 0.22328 0.05933  -0.09468 0.01952  236 THR A CA  
1728 C C   . THR A 236 ? 0.35437 0.31295 0.28514 0.05834  -0.08355 0.02098  236 THR A C   
1729 O O   . THR A 236 ? 0.31401 0.28056 0.25640 0.05242  -0.07715 0.01877  236 THR A O   
1730 C CB  . THR A 236 ? 0.36520 0.31547 0.27434 0.05256  -0.09191 0.01769  236 THR A CB  
1731 O OG1 . THR A 236 ? 0.34953 0.28210 0.24082 0.05204  -0.08348 0.02093  236 THR A OG1 
1732 C CG2 . THR A 236 ? 0.32367 0.27161 0.22027 0.05385  -0.10302 0.01600  236 THR A CG2 
1733 N N   . SER A 237 ? 0.35275 0.29952 0.27497 0.06370  -0.08144 0.02458  237 SER A N   
1734 C CA  . SER A 237 ? 0.36503 0.30933 0.29277 0.06287  -0.07205 0.02518  237 SER A CA  
1735 C C   . SER A 237 ? 0.33177 0.29113 0.27934 0.06793  -0.07307 0.02354  237 SER A C   
1736 O O   . SER A 237 ? 0.28636 0.24546 0.23938 0.06731  -0.06578 0.02300  237 SER A O   
1737 C CB  . SER A 237 ? 0.32120 0.24346 0.22971 0.06522  -0.06893 0.02948  237 SER A CB  
1738 O OG  . SER A 237 ? 0.39675 0.31401 0.30256 0.07461  -0.07608 0.03195  237 SER A OG  
1739 N N   . ASP A 238 ? 0.33520 0.30865 0.29377 0.07291  -0.08180 0.02227  238 ASP A N   
1740 C CA  . ASP A 238 ? 0.32652 0.31570 0.30380 0.07921  -0.08296 0.02048  238 ASP A CA  
1741 C C   . ASP A 238 ? 0.30484 0.31475 0.30229 0.07303  -0.07798 0.01727  238 ASP A C   
1742 O O   . ASP A 238 ? 0.30695 0.31821 0.30419 0.06437  -0.07503 0.01662  238 ASP A O   
1743 C CB  . ASP A 238 ? 0.31551 0.31297 0.29703 0.08771  -0.09480 0.02045  238 ASP A CB  
1744 C CG  . ASP A 238 ? 0.46315 0.46534 0.45411 0.09886  -0.09631 0.02003  238 ASP A CG  
1745 O OD1 . ASP A 238 ? 0.36600 0.37560 0.36862 0.09866  -0.08852 0.01781  238 ASP A OD1 
1746 O OD2 . ASP A 238 ? 0.40853 0.40689 0.39457 0.10844  -0.10562 0.02167  238 ASP A OD2 
1747 N N   . GLY A 239 ? 0.29435 0.32017 0.30884 0.07788  -0.07690 0.01534  239 GLY A N   
1748 C CA  . GLY A 239 ? 0.27774 0.32464 0.31115 0.07216  -0.07252 0.01307  239 GLY A CA  
1749 C C   . GLY A 239 ? 0.28914 0.34822 0.33051 0.06626  -0.07862 0.01215  239 GLY A C   
1750 O O   . GLY A 239 ? 0.28022 0.33879 0.31815 0.06947  -0.08811 0.01204  239 GLY A O   
1751 N N   . ARG A 240 ? 0.27611 0.34536 0.32750 0.05728  -0.07356 0.01147  240 ARG A N   
1752 C CA  . ARG A 240 ? 0.24864 0.32369 0.30427 0.04971  -0.07892 0.01039  240 ARG A CA  
1753 C C   . ARG A 240 ? 0.27277 0.36896 0.34562 0.05237  -0.08732 0.00821  240 ARG A C   
1754 O O   . ARG A 240 ? 0.32016 0.41695 0.39121 0.05013  -0.09633 0.00674  240 ARG A O   
1755 C CB  . ARG A 240 ? 0.21679 0.29524 0.27852 0.03952  -0.07159 0.01077  240 ARG A CB  
1756 C CG  . ARG A 240 ? 0.22419 0.28436 0.27087 0.03755  -0.06376 0.01255  240 ARG A CG  
1757 C CD  . ARG A 240 ? 0.28668 0.32648 0.31316 0.03806  -0.06731 0.01260  240 ARG A CD  
1758 N NE  . ARG A 240 ? 0.26348 0.30212 0.28874 0.03178  -0.07267 0.01078  240 ARG A NE  
1759 C CZ  . ARG A 240 ? 0.37120 0.39550 0.38004 0.03167  -0.07714 0.00979  240 ARG A CZ  
1760 N NH1 . ARG A 240 ? 0.28357 0.29402 0.27593 0.03730  -0.07708 0.01133  240 ARG A NH1 
1761 N NH2 . ARG A 240 ? 0.25982 0.28282 0.26793 0.02539  -0.08147 0.00708  240 ARG A NH2 
1762 N N   . SER A 241 ? 0.24349 0.35827 0.33336 0.05752  -0.08485 0.00738  241 SER A N   
1763 C CA  . SER A 241 ? 0.26001 0.39788 0.36857 0.06094  -0.09295 0.00489  241 SER A CA  
1764 C C   . SER A 241 ? 0.29046 0.42110 0.38969 0.07224  -0.10359 0.00477  241 SER A C   
1765 O O   . SER A 241 ? 0.27084 0.41457 0.37878 0.07376  -0.11411 0.00277  241 SER A O   
1766 C CB  . SER A 241 ? 0.33531 0.49661 0.46502 0.06395  -0.08636 0.00364  241 SER A CB  
1767 O OG  . SER A 241 ? 0.37720 0.54555 0.51459 0.05290  -0.07704 0.00463  241 SER A OG  
1768 N N   . GLU A 242 ? 0.30515 0.41459 0.38633 0.07990  -0.10139 0.00706  242 GLU A N   
1769 C CA  . GLU A 242 ? 0.26667 0.36441 0.33505 0.09063  -0.11108 0.00834  242 GLU A CA  
1770 C C   . GLU A 242 ? 0.25705 0.34191 0.30880 0.08593  -0.11901 0.00923  242 GLU A C   
1771 O O   . GLU A 242 ? 0.31233 0.40173 0.36325 0.09128  -0.13088 0.00866  242 GLU A O   
1772 C CB  . GLU A 242 ? 0.33120 0.40614 0.38288 0.09761  -0.10540 0.01102  242 GLU A CB  
1773 C CG  . GLU A 242 ? 0.33715 0.42304 0.40294 0.10638  -0.10047 0.00909  242 GLU A CG  
1774 C CD  . GLU A 242 ? 0.37512 0.47073 0.45136 0.09904  -0.08827 0.00741  242 GLU A CD  
1775 O OE1 . GLU A 242 ? 0.33794 0.43221 0.41199 0.08736  -0.08357 0.00819  242 GLU A OE1 
1776 O OE2 . GLU A 242 ? 0.43890 0.54353 0.52517 0.10573  -0.08347 0.00515  242 GLU A OE2 
1777 N N   . TRP A 243 ? 0.29665 0.36573 0.33455 0.07646  -0.11274 0.01026  243 TRP A N   
1778 C CA  . TRP A 243 ? 0.30958 0.36633 0.33073 0.07179  -0.11911 0.01016  243 TRP A CA  
1779 C C   . TRP A 243 ? 0.34953 0.42555 0.38588 0.06507  -0.12683 0.00600  243 TRP A C   
1780 O O   . TRP A 243 ? 0.38335 0.45673 0.41065 0.06584  -0.13759 0.00466  243 TRP A O   
1781 C CB  . TRP A 243 ? 0.27708 0.31382 0.28163 0.06435  -0.10940 0.01163  243 TRP A CB  
1782 C CG  . TRP A 243 ? 0.29939 0.32414 0.28790 0.05767  -0.11255 0.01033  243 TRP A CG  
1783 C CD1 . TRP A 243 ? 0.31922 0.33749 0.30435 0.04857  -0.10545 0.00906  243 TRP A CD1 
1784 C CD2 . TRP A 243 ? 0.33983 0.35693 0.31233 0.06034  -0.12337 0.00982  243 TRP A CD2 
1785 N NE1 . TRP A 243 ? 0.32119 0.32808 0.28964 0.04545  -0.11043 0.00717  243 TRP A NE1 
1786 C CE2 . TRP A 243 ? 0.31933 0.32540 0.27905 0.05216  -0.12140 0.00757  243 TRP A CE2 
1787 C CE3 . TRP A 243 ? 0.35883 0.37711 0.32573 0.06954  -0.13491 0.01097  243 TRP A CE3 
1788 C CZ2 . TRP A 243 ? 0.35440 0.35123 0.29562 0.05219  -0.13011 0.00582  243 TRP A CZ2 
1789 C CZ3 . TRP A 243 ? 0.40485 0.41364 0.35259 0.06963  -0.14416 0.01010  243 TRP A CZ3 
1790 C CH2 . TRP A 243 ? 0.35081 0.34906 0.28545 0.06070  -0.14145 0.00729  243 TRP A CH2 
1791 N N   . ALA A 244 ? 0.28218 0.37756 0.34108 0.05809  -0.12188 0.00391  244 ALA A N   
1792 C CA  . ALA A 244 ? 0.24832 0.36374 0.32435 0.05155  -0.12988 -0.00012 244 ALA A CA  
1793 C C   . ALA A 244 ? 0.30035 0.43155 0.38520 0.06106  -0.14264 -0.00171 244 ALA A C   
1794 O O   . ALA A 244 ? 0.33494 0.47142 0.41954 0.05875  -0.15424 -0.00480 244 ALA A O   
1795 C CB  . ALA A 244 ? 0.31427 0.44949 0.41449 0.04324  -0.12176 -0.00104 244 ALA A CB  
1796 N N   . GLU A 245 ? 0.25623 0.39464 0.34834 0.07253  -0.14137 -0.00007 245 GLU A N   
1797 C CA  . GLU A 245 ? 0.26663 0.42088 0.36829 0.08327  -0.15404 -0.00158 245 GLU A CA  
1798 C C   . GLU A 245 ? 0.35330 0.48687 0.42868 0.08970  -0.16520 0.00026  245 GLU A C   
1799 O O   . GLU A 245 ? 0.37323 0.51806 0.45214 0.09162  -0.17879 -0.00234 245 GLU A O   
1800 C CB  . GLU A 245 ? 0.33142 0.49534 0.44508 0.09557  -0.14992 -0.00059 245 GLU A CB  
1801 C CG  . GLU A 245 ? 0.41773 0.59534 0.53978 0.10781  -0.16148 -0.00139 245 GLU A CG  
1802 C CD  . GLU A 245 ? 0.63232 0.81434 0.76322 0.11926  -0.15476 -0.00037 245 GLU A CD  
1803 O OE1 . GLU A 245 ? 0.83471 0.99686 0.94849 0.12977  -0.15678 0.00302  245 GLU A OE1 
1804 O OE2 . GLU A 245 ? 0.82641 1.03063 0.98044 0.11737  -0.14697 -0.00309 245 GLU A OE2 
1805 N N   . ALA A 246 ? 0.33230 0.43601 0.38068 0.09235  -0.15970 0.00471  246 ALA A N   
1806 C CA  . ALA A 246 ? 0.38929 0.47222 0.41040 0.09865  -0.16916 0.00751  246 ALA A CA  
1807 C C   . ALA A 246 ? 0.35057 0.42875 0.35991 0.08881  -0.17507 0.00458  246 ALA A C   
1808 O O   . ALA A 246 ? 0.38161 0.45628 0.37785 0.09300  -0.18733 0.00436  246 ALA A O   
1809 C CB  . ALA A 246 ? 0.38653 0.43937 0.38281 0.10241  -0.16025 0.01319  246 ALA A CB  
1810 N N   . ARG A 247 ? 0.35826 0.43518 0.37097 0.07589  -0.16624 0.00219  247 ARG A N   
1811 C CA  . ARG A 247 ? 0.34859 0.42072 0.35145 0.06648  -0.17152 -0.00182 247 ARG A CA  
1812 C C   . ARG A 247 ? 0.45752 0.55491 0.47996 0.06438  -0.18504 -0.00735 247 ARG A C   
1813 O O   . ARG A 247 ? 0.45616 0.54981 0.46569 0.06332  -0.19656 -0.01042 247 ARG A O   
1814 C CB  . ARG A 247 ? 0.31410 0.37967 0.31889 0.05415  -0.15903 -0.00322 247 ARG A CB  
1815 C CG  . ARG A 247 ? 0.36438 0.41931 0.35511 0.04491  -0.16298 -0.00783 247 ARG A CG  
1816 C CD  . ARG A 247 ? 0.40325 0.45129 0.39737 0.03398  -0.15076 -0.00906 247 ARG A CD  
1817 N NE  . ARG A 247 ? 0.43328 0.47144 0.41580 0.02591  -0.15499 -0.01449 247 ARG A NE  
1818 C CZ  . ARG A 247 ? 0.41789 0.46877 0.41259 0.01902  -0.16461 -0.02039 247 ARG A CZ  
1819 N NH1 . ARG A 247 ? 0.47115 0.54756 0.49214 0.01838  -0.17035 -0.02138 247 ARG A NH1 
1820 N NH2 . ARG A 247 ? 0.38166 0.41985 0.36239 0.01237  -0.16834 -0.02596 247 ARG A NH2 
1821 N N   . THR A 248 ? 0.33963 0.46412 0.39337 0.06383  -0.18402 -0.00899 248 THR A N   
1822 C CA  . THR A 248 ? 0.39988 0.55193 0.47543 0.06186  -0.19708 -0.01440 248 THR A CA  
1823 C C   . THR A 248 ? 0.42975 0.58100 0.49378 0.07229  -0.20742 -0.01277 248 THR A C   
1824 O O   . THR A 248 ? 0.39793 0.55940 0.46450 0.06815  -0.21727 -0.01669 248 THR A O   
1825 C CB  . THR A 248 ? 0.34679 0.52890 0.45762 0.06065  -0.19173 -0.01545 248 THR A CB  
1826 O OG1 . THR A 248 ? 0.40504 0.58480 0.52320 0.04787  -0.17791 -0.01534 248 THR A OG1 
1827 C CG2 . THR A 248 ? 0.43627 0.64769 0.57045 0.05684  -0.20135 -0.02006 248 THR A CG2 
1828 N N   . VAL A 249 ? 0.34484 0.48261 0.39552 0.08486  -0.20426 -0.00673 249 VAL A N   
1829 C CA  . VAL A 249 ? 0.40875 0.54041 0.44447 0.09408  -0.21269 -0.00393 249 VAL A CA  
1830 C C   . VAL A 249 ? 0.49483 0.60466 0.49988 0.09013  -0.21827 -0.00447 249 VAL A C   
1831 O O   . VAL A 249 ? 0.54903 0.66442 0.54935 0.09037  -0.22871 -0.00647 249 VAL A O   
1832 C CB  . VAL A 249 ? 0.46599 0.58351 0.49220 0.10746  -0.20752 0.00284  249 VAL A CB  
1833 C CG1 . VAL A 249 ? 0.48892 0.59766 0.49791 0.11660  -0.21676 0.00629  249 VAL A CG1 
1834 C CG2 . VAL A 249 ? 0.40014 0.53983 0.45612 0.11233  -0.20208 0.00236  249 VAL A CG2 
1835 N N   . LEU A 250 ? 0.50800 0.59325 0.49147 0.08656  -0.21119 -0.00288 250 LEU A N   
1836 C CA  . LEU A 250 ? 0.42429 0.48725 0.37620 0.08339  -0.21447 -0.00329 250 LEU A CA  
1837 C C   . LEU A 250 ? 0.45563 0.53066 0.41328 0.07317  -0.22330 -0.01139 250 LEU A C   
1838 O O   . LEU A 250 ? 0.51798 0.58628 0.45702 0.07367  -0.23110 -0.01274 250 LEU A O   
1839 C CB  . LEU A 250 ? 0.46466 0.50286 0.39676 0.08006  -0.20410 -0.00100 250 LEU A CB  
1840 C CG  . LEU A 250 ? 0.47156 0.48967 0.38834 0.08826  -0.19492 0.00707  250 LEU A CG  
1841 C CD1 . LEU A 250 ? 0.40102 0.39980 0.30390 0.08103  -0.18179 0.00806  250 LEU A CD1 
1842 C CD2 . LEU A 250 ? 0.52145 0.52398 0.41323 0.09586  -0.19903 0.01212  250 LEU A CD2 
1843 N N   . VAL A 251 ? 0.46490 0.55679 0.44753 0.06321  -0.22202 -0.01697 251 VAL A N   
1844 C CA  . VAL A 251 ? 0.47868 0.57605 0.46378 0.05141  -0.22895 -0.02512 251 VAL A CA  
1845 C C   . VAL A 251 ? 0.58112 0.70129 0.57992 0.05167  -0.24068 -0.02852 251 VAL A C   
1846 O O   . VAL A 251 ? 0.59735 0.72284 0.59763 0.04215  -0.24782 -0.03564 251 VAL A O   
1847 C CB  . VAL A 251 ? 0.50226 0.60789 0.50933 0.03944  -0.22361 -0.02945 251 VAL A CB  
1848 C CG1 . VAL A 251 ? 0.40650 0.48607 0.39546 0.03724  -0.20791 -0.02556 251 VAL A CG1 
1849 C CG2 . VAL A 251 ? 0.62258 0.75587 0.66483 0.04049  -0.22021 -0.02796 251 VAL A CG2 
1850 N N   . LYS A 252 ? 0.51620 0.64873 0.52384 0.06266  -0.24311 -0.02368 252 LYS A N   
1851 C CA  . LYS A 252 ? 0.54676 0.69918 0.56389 0.06456  -0.25514 -0.02607 252 LYS A CA  
1852 C C   . LYS A 252 ? 0.63436 0.76955 0.62000 0.06622  -0.26372 -0.02697 252 LYS A C   
1853 O O   . LYS A 252 ? 0.69469 0.84512 0.68584 0.06443  -0.27498 -0.03099 252 LYS A O   
1854 C CB  . LYS A 252 ? 0.47206 0.63823 0.50299 0.07755  -0.25576 -0.02028 252 LYS A CB  
1855 C CG  . LYS A 252 ? 0.62162 0.81263 0.68813 0.07634  -0.24899 -0.02057 252 LYS A CG  
1856 C CD  . LYS A 252 ? 0.62765 0.81596 0.69559 0.09105  -0.24396 -0.01358 252 LYS A CD  
1857 C CE  . LYS A 252 ? 0.72246 0.94163 0.82013 0.09656  -0.24831 -0.01408 252 LYS A CE  
1858 N NZ  . LYS A 252 ? 0.84905 1.06163 0.94607 0.11110  -0.24270 -0.00803 252 LYS A NZ  
1859 N N   . ASP A 253 ? 0.56917 0.67397 0.52212 0.06924  -0.25839 -0.02338 253 ASP A N   
1860 C CA  . ASP A 253 ? 0.61945 0.70628 0.53968 0.07187  -0.26454 -0.02313 253 ASP A CA  
1861 C C   . ASP A 253 ? 0.70662 0.77511 0.60703 0.06171  -0.26146 -0.02900 253 ASP A C   
1862 O O   . ASP A 253 ? 0.55417 0.60926 0.45106 0.05812  -0.25105 -0.02835 253 ASP A O   
1863 C CB  . ASP A 253 ? 0.61957 0.68519 0.51572 0.08436  -0.26009 -0.01327 253 ASP A CB  
1864 C CG  . ASP A 253 ? 0.88019 0.92595 0.74070 0.08670  -0.26469 -0.01206 253 ASP A CG  
1865 O OD1 . ASP A 253 ? 0.80923 0.83389 0.64639 0.08163  -0.25822 -0.01336 253 ASP A OD1 
1866 O OD2 . ASP A 253 ? 0.91713 0.96908 0.77308 0.09359  -0.27469 -0.00999 253 ASP A OD2 
1867 N N   . SER A 254 ? 0.63544 0.70281 0.52201 0.05755  -0.27062 -0.03492 254 SER A N   
1868 C CA  . SER A 254 ? 0.67107 0.72194 0.53994 0.04775  -0.26822 -0.04216 254 SER A CA  
1869 C C   . SER A 254 ? 0.70164 0.72159 0.53580 0.05192  -0.25821 -0.03732 254 SER A C   
1870 O O   . SER A 254 ? 0.65108 0.65663 0.47626 0.04495  -0.25104 -0.04151 254 SER A O   
1871 C CB  . SER A 254 ? 0.55930 0.61600 0.42011 0.04300  -0.28046 -0.05004 254 SER A CB  
1872 O OG  . SER A 254 ? 0.67489 0.72503 0.51255 0.05310  -0.28611 -0.04476 254 SER A OG  
1873 N N   . THR A 255 ? 0.58555 0.59451 0.39953 0.06270  -0.25735 -0.02866 255 THR A N   
1874 C CA  . THR A 255 ? 0.62289 0.60388 0.40617 0.06571  -0.24607 -0.02314 255 THR A CA  
1875 C C   . THR A 255 ? 0.62581 0.60124 0.41996 0.06402  -0.23366 -0.02014 255 THR A C   
1876 O O   . THR A 255 ? 0.59746 0.55512 0.37538 0.05977  -0.22430 -0.02145 255 THR A O   
1877 C CB  . THR A 255 ? 0.64082 0.61174 0.40409 0.07690  -0.24698 -0.01330 255 THR A CB  
1878 O OG1 . THR A 255 ? 0.74060 0.71381 0.48860 0.07822  -0.25825 -0.01609 255 THR A OG1 
1879 C CG2 . THR A 255 ? 0.70273 0.64613 0.43750 0.07892  -0.23353 -0.00657 255 THR A CG2 
1880 N N   . ASN A 256 ? 0.57184 0.56299 0.39349 0.06754  -0.23321 -0.01640 256 ASN A N   
1881 C CA  . ASN A 256 ? 0.52797 0.51508 0.36044 0.06605  -0.22197 -0.01369 256 ASN A CA  
1882 C C   . ASN A 256 ? 0.56459 0.55590 0.40980 0.05463  -0.22028 -0.02207 256 ASN A C   
1883 O O   . ASN A 256 ? 0.53262 0.51042 0.37141 0.05162  -0.21048 -0.02135 256 ASN A O   
1884 C CB  . ASN A 256 ? 0.49043 0.49472 0.35011 0.07248  -0.22183 -0.00880 256 ASN A CB  
1885 C CG  . ASN A 256 ? 0.64710 0.64388 0.49406 0.08422  -0.22290 -0.00026 256 ASN A CG  
1886 O OD1 . ASN A 256 ? 0.60772 0.58130 0.42476 0.08730  -0.21850 0.00478  256 ASN A OD1 
1887 N ND2 . ASN A 256 ? 0.54308 0.55936 0.41301 0.09055  -0.22837 0.00138  256 ASN A ND2 
1888 N N   . ARG A 257 ? 0.52056 0.53011 0.38428 0.04772  -0.22963 -0.02999 257 ARG A N   
1889 C CA  . ARG A 257 ? 0.55154 0.56245 0.42722 0.03585  -0.22799 -0.03791 257 ARG A CA  
1890 C C   . ARG A 257 ? 0.60403 0.58908 0.44901 0.03202  -0.22309 -0.04185 257 ARG A C   
1891 O O   . ARG A 257 ? 0.59761 0.57323 0.44537 0.02607  -0.21115 -0.04282 257 ARG A O   
1892 C CB  . ARG A 257 ? 0.53146 0.56524 0.43137 0.02782  -0.23862 -0.04577 257 ARG A CB  
1893 C CG  . ARG A 257 ? 0.55592 0.61854 0.49104 0.02996  -0.24120 -0.04286 257 ARG A CG  
1894 C CD  . ARG A 257 ? 0.55310 0.63959 0.51643 0.01880  -0.24890 -0.05084 257 ARG A CD  
1895 N NE  . ARG A 257 ? 0.56455 0.65378 0.51673 0.01723  -0.26012 -0.05634 257 ARG A NE  
1896 C CZ  . ARG A 257 ? 0.65661 0.76218 0.61317 0.02406  -0.26901 -0.05444 257 ARG A CZ  
1897 N NH1 . ARG A 257 ? 0.52050 0.64128 0.49312 0.03341  -0.26793 -0.04743 257 ARG A NH1 
1898 N NH2 . ARG A 257 ? 0.67404 0.78045 0.61839 0.02169  -0.27941 -0.05998 257 ARG A NH2 
1899 N N   . ASP A 258 ? 0.61405 0.58887 0.43256 0.03504  -0.22716 -0.04312 258 ASP A N   
1900 C CA  . ASP A 258 ? 0.62066 0.57171 0.40852 0.03262  -0.22115 -0.04694 258 ASP A CA  
1901 C C   . ASP A 258 ? 0.61455 0.54770 0.38700 0.03682  -0.20738 -0.03984 258 ASP A C   
1902 O O   . ASP A 258 ? 0.61348 0.53348 0.37847 0.03182  -0.19666 -0.04322 258 ASP A O   
1903 C CB  . ASP A 258 ? 0.58082 0.52566 0.34257 0.03656  -0.22718 -0.04786 258 ASP A CB  
1904 C CG  . ASP A 258 ? 0.93291 0.89584 0.70818 0.03218  -0.24145 -0.05537 258 ASP A CG  
1905 O OD1 . ASP A 258 ? 0.73205 0.70801 0.53288 0.02327  -0.24533 -0.06233 258 ASP A OD1 
1906 O OD2 . ASP A 258 ? 0.85747 0.82142 0.61731 0.03722  -0.24873 -0.05410 258 ASP A OD2 
1907 N N   . SER A 259 ? 0.56303 0.49667 0.33447 0.04534  -0.20419 -0.02957 259 SER A N   
1908 C CA  . SER A 259 ? 0.61159 0.52889 0.36969 0.04815  -0.18927 -0.02239 259 SER A CA  
1909 C C   . SER A 259 ? 0.57158 0.49599 0.35815 0.04236  -0.17633 -0.02196 259 SER A C   
1910 O O   . SER A 259 ? 0.53902 0.45154 0.31895 0.03933  -0.16229 -0.02156 259 SER A O   
1911 C CB  . SER A 259 ? 0.53988 0.45377 0.28955 0.05795  -0.18909 -0.01170 259 SER A CB  
1912 O OG  . SER A 259 ? 0.59359 0.49945 0.31878 0.06136  -0.19316 -0.01055 259 SER A OG  
1913 N N   . LEU A 260 ? 0.53771 0.48234 0.35585 0.04122  -0.18071 -0.02184 260 LEU A N   
1914 C CA  . LEU A 260 ? 0.51804 0.47005 0.36226 0.03531  -0.16926 -0.02157 260 LEU A CA  
1915 C C   . LEU A 260 ? 0.47661 0.42224 0.32105 0.02585  -0.16488 -0.02933 260 LEU A C   
1916 O O   . LEU A 260 ? 0.49028 0.42948 0.33911 0.02266  -0.15168 -0.02826 260 LEU A O   
1917 C CB  . LEU A 260 ? 0.47506 0.45144 0.35176 0.03502  -0.17574 -0.02123 260 LEU A CB  
1918 C CG  . LEU A 260 ? 0.52246 0.50486 0.40220 0.04562  -0.17819 -0.01360 260 LEU A CG  
1919 C CD1 . LEU A 260 ? 0.41107 0.42009 0.32172 0.04627  -0.18680 -0.01502 260 LEU A CD1 
1920 C CD2 . LEU A 260 ? 0.41055 0.38338 0.28994 0.04755  -0.16250 -0.00703 260 LEU A CD2 
1921 N N   . ASP A 261 ? 0.47938 0.42595 0.31845 0.02168  -0.17643 -0.03754 261 ASP A N   
1922 C CA  . ASP A 261 ? 0.55101 0.48915 0.38943 0.01291  -0.17340 -0.04581 261 ASP A CA  
1923 C C   . ASP A 261 ? 0.53195 0.44832 0.34424 0.01488  -0.16168 -0.04609 261 ASP A C   
1924 O O   . ASP A 261 ? 0.55388 0.46270 0.37060 0.01017  -0.15214 -0.04912 261 ASP A O   
1925 C CB  . ASP A 261 ? 0.59860 0.54037 0.43324 0.00835  -0.18931 -0.05534 261 ASP A CB  
1926 C CG  . ASP A 261 ? 0.74486 0.67150 0.57009 0.00082  -0.18688 -0.06488 261 ASP A CG  
1927 O OD1 . ASP A 261 ? 0.72188 0.64965 0.56714 -0.00657 -0.18049 -0.06653 261 ASP A OD1 
1928 O OD2 . ASP A 261 ? 0.76386 0.67649 0.56054 0.00271  -0.19121 -0.07066 261 ASP A OD2 
1929 N N   . MET A 262 ? 0.54943 0.45583 0.33455 0.02210  -0.16187 -0.04257 262 MET A N   
1930 C CA  . MET A 262 ? 0.54552 0.43348 0.30615 0.02372  -0.14987 -0.04285 262 MET A CA  
1931 C C   . MET A 262 ? 0.51879 0.40614 0.29149 0.02425  -0.13383 -0.03618 262 MET A C   
1932 O O   . MET A 262 ? 0.53358 0.41139 0.30098 0.02246  -0.12271 -0.03888 262 MET A O   
1933 C CB  . MET A 262 ? 0.50817 0.38591 0.23613 0.03054  -0.15344 -0.03965 262 MET A CB  
1934 C CG  . MET A 262 ? 0.54109 0.41727 0.25151 0.03021  -0.16955 -0.04775 262 MET A CG  
1935 S SD  . MET A 262 ? 0.71323 0.57852 0.41555 0.02285  -0.16833 -0.06206 262 MET A SD  
1936 C CE  . MET A 262 ? 0.63881 0.48474 0.31038 0.02712  -0.15077 -0.05991 262 MET A CE  
1937 N N   . ILE A 263 ? 0.47570 0.37360 0.26489 0.02713  -0.13280 -0.02808 263 ILE A N   
1938 C CA  . ILE A 263 ? 0.41794 0.31628 0.21934 0.02721  -0.11867 -0.02245 263 ILE A CA  
1939 C C   . ILE A 263 ? 0.50318 0.40836 0.32883 0.02089  -0.11473 -0.02621 263 ILE A C   
1940 O O   . ILE A 263 ? 0.49079 0.39019 0.31804 0.01948  -0.10314 -0.02636 263 ILE A O   
1941 C CB  . ILE A 263 ? 0.41454 0.32075 0.22532 0.03232  -0.11924 -0.01371 263 ILE A CB  
1942 C CG1 . ILE A 263 ? 0.50437 0.39974 0.28816 0.03879  -0.12259 -0.00893 263 ILE A CG1 
1943 C CG2 . ILE A 263 ? 0.42285 0.33057 0.24746 0.03172  -0.10565 -0.00892 263 ILE A CG2 
1944 C CD1 . ILE A 263 ? 0.55993 0.46204 0.35187 0.04510  -0.12773 -0.00150 263 ILE A CD1 
1945 N N   . GLU A 264 ? 0.43227 0.34982 0.27671 0.01684  -0.12449 -0.02931 264 GLU A N   
1946 C CA  . GLU A 264 ? 0.44276 0.36598 0.30992 0.01002  -0.12099 -0.03177 264 GLU A CA  
1947 C C   . GLU A 264 ? 0.53307 0.44138 0.38997 0.00627  -0.11644 -0.03868 264 GLU A C   
1948 O O   . GLU A 264 ? 0.51635 0.42327 0.38600 0.00302  -0.10876 -0.03855 264 GLU A O   
1949 C CB  . GLU A 264 ? 0.42328 0.36253 0.31087 0.00514  -0.13266 -0.03431 264 GLU A CB  
1950 C CG  . GLU A 264 ? 0.46146 0.41790 0.36416 0.00976  -0.13553 -0.02764 264 GLU A CG  
1951 C CD  . GLU A 264 ? 0.54973 0.52474 0.47146 0.00614  -0.14797 -0.03062 264 GLU A CD  
1952 O OE1 . GLU A 264 ? 0.61302 0.58883 0.54179 -0.00235 -0.15259 -0.03715 264 GLU A OE1 
1953 O OE2 . GLU A 264 ? 0.50715 0.49602 0.43744 0.01180  -0.15311 -0.02668 264 GLU A OE2 
1954 N N   . ARG A 265 ? 0.51925 0.41558 0.35215 0.00743  -0.12087 -0.04477 265 ARG A N   
1955 C CA  . ARG A 265 ? 0.53435 0.41587 0.35698 0.00469  -0.11712 -0.05278 265 ARG A CA  
1956 C C   . ARG A 265 ? 0.55331 0.42216 0.35426 0.01024  -0.10568 -0.05243 265 ARG A C   
1957 O O   . ARG A 265 ? 0.56954 0.42546 0.35724 0.00994  -0.10285 -0.06004 265 ARG A O   
1958 C CB  . ARG A 265 ? 0.57162 0.44823 0.38337 0.00090  -0.13011 -0.06244 265 ARG A CB  
1959 C CG  . ARG A 265 ? 0.77207 0.66132 0.60817 -0.00693 -0.14068 -0.06465 265 ARG A CG  
1960 C CD  . ARG A 265 ? 0.78592 0.67018 0.61214 -0.01196 -0.15422 -0.07552 265 ARG A CD  
1961 N NE  . ARG A 265 ? 0.72130 0.60509 0.52395 -0.00637 -0.16293 -0.07686 265 ARG A NE  
1962 C CZ  . ARG A 265 ? 0.94982 0.81752 0.72181 -0.00232 -0.16156 -0.08199 265 ARG A CZ  
1963 N NH1 . ARG A 265 ? 0.79610 0.64747 0.55816 -0.00278 -0.15203 -0.08741 265 ARG A NH1 
1964 N NH2 . ARG A 265 ? 0.94064 0.80869 0.69081 0.00292  -0.16979 -0.08157 265 ARG A NH2 
1965 N N   . CYS A 266 ? 0.52539 0.39749 0.32233 0.01514  -0.09886 -0.04430 266 CYS A N   
1966 C CA  . CYS A 266 ? 0.48506 0.34686 0.26279 0.01914  -0.08732 -0.04412 266 CYS A CA  
1967 C C   . CYS A 266 ? 0.49915 0.36064 0.29116 0.01863  -0.07535 -0.04405 266 CYS A C   
1968 O O   . CYS A 266 ? 0.50331 0.37231 0.31872 0.01573  -0.07543 -0.04195 266 CYS A O   
1969 C CB  . CYS A 266 ? 0.46325 0.32659 0.23000 0.02353  -0.08405 -0.03544 266 CYS A CB  
1970 S SG  . CYS A 266 ? 0.53755 0.41258 0.32850 0.02418  -0.07652 -0.02528 266 CYS A SG  
1971 N N   . ILE A 267 ? 0.50601 0.35929 0.28327 0.02174  -0.06502 -0.04651 267 ILE A N   
1972 C CA  . ILE A 267 ? 0.51312 0.36730 0.30312 0.02274  -0.05375 -0.04646 267 ILE A CA  
1973 C C   . ILE A 267 ? 0.56283 0.42816 0.36802 0.02336  -0.04740 -0.03703 267 ILE A C   
1974 O O   . ILE A 267 ? 0.43743 0.30927 0.26352 0.02226  -0.04475 -0.03467 267 ILE A O   
1975 C CB  . ILE A 267 ? 0.49568 0.34080 0.26650 0.02658  -0.04417 -0.05206 267 ILE A CB  
1976 C CG1 . ILE A 267 ? 0.52088 0.35369 0.27887 0.02621  -0.05009 -0.06305 267 ILE A CG1 
1977 C CG2 . ILE A 267 ? 0.51285 0.36282 0.29757 0.02901  -0.03166 -0.05030 267 ILE A CG2 
1978 C CD1 . ILE A 267 ? 0.57463 0.39839 0.30904 0.03069  -0.04160 -0.06969 267 ILE A CD1 
1979 N N   . CYS A 268 ? 0.46007 0.32632 0.25333 0.02510  -0.04471 -0.03162 268 CYS A N   
1980 C CA  . CYS A 268 ? 0.42725 0.30169 0.23154 0.02546  -0.03888 -0.02331 268 CYS A CA  
1981 C C   . CYS A 268 ? 0.43772 0.30820 0.22379 0.02684  -0.04072 -0.01816 268 CYS A C   
1982 O O   . CYS A 268 ? 0.46052 0.32268 0.22504 0.02787  -0.04545 -0.02094 268 CYS A O   
1983 C CB  . CYS A 268 ? 0.41162 0.28852 0.22139 0.02653  -0.02562 -0.02330 268 CYS A CB  
1984 S SG  . CYS A 268 ? 0.50963 0.37828 0.29366 0.02873  -0.01523 -0.02695 268 CYS A SG  
1985 N N   . LEU A 269 ? 0.41416 0.28958 0.20824 0.02701  -0.03763 -0.01063 269 LEU A N   
1986 C CA  . LEU A 269 ? 0.42019 0.28920 0.19680 0.02837  -0.03650 -0.00449 269 LEU A CA  
1987 C C   . LEU A 269 ? 0.45333 0.31957 0.22249 0.02726  -0.02238 -0.00272 269 LEU A C   
1988 O O   . LEU A 269 ? 0.40894 0.28254 0.19413 0.02594  -0.01436 -0.00397 269 LEU A O   
1989 C CB  . LEU A 269 ? 0.43097 0.30485 0.21970 0.02936  -0.04130 0.00239  269 LEU A CB  
1990 C CG  . LEU A 269 ? 0.52659 0.39871 0.30840 0.03232  -0.05454 0.00445  269 LEU A CG  
1991 C CD1 . LEU A 269 ? 0.48229 0.36310 0.27834 0.03127  -0.06462 -0.00151 269 LEU A CD1 
1992 C CD2 . LEU A 269 ? 0.48250 0.35686 0.27303 0.03459  -0.05575 0.01169  269 LEU A CD2 
1993 N N   . VAL A 270 ? 0.50493 0.36110 0.24953 0.02767  -0.01953 0.00044  270 VAL A N   
1994 C CA  . VAL A 270 ? 0.52252 0.37616 0.25950 0.02539  -0.00619 0.00429  270 VAL A CA  
1995 C C   . VAL A 270 ? 0.53061 0.37560 0.25637 0.02540  -0.00858 0.01349  270 VAL A C   
1996 O O   . VAL A 270 ? 0.49920 0.33463 0.20501 0.02804  -0.01676 0.01573  270 VAL A O   
1997 C CB  . VAL A 270 ? 0.56341 0.41140 0.27860 0.02538  0.00168  -0.00028 270 VAL A CB  
1998 C CG1 . VAL A 270 ? 0.60749 0.45558 0.31745 0.02190  0.01669  0.00375  270 VAL A CG1 
1999 C CG2 . VAL A 270 ? 0.55805 0.41209 0.28378 0.02678  0.00228  -0.01001 270 VAL A CG2 
2000 N N   . CYS A 271 ? 0.48369 0.33141 0.22233 0.02286  -0.00252 0.01859  271 CYS A N   
2001 C CA  . CYS A 271 ? 0.54362 0.38164 0.27486 0.02324  -0.00531 0.02716  271 CYS A CA  
2002 C C   . CYS A 271 ? 0.52919 0.35855 0.24570 0.01843  0.00752  0.03231  271 CYS A C   
2003 O O   . CYS A 271 ? 0.50512 0.34219 0.23594 0.01382  0.01790  0.03140  271 CYS A O   
2004 C CB  . CYS A 271 ? 0.44542 0.29141 0.20204 0.02381  -0.00907 0.02860  271 CYS A CB  
2005 S SG  . CYS A 271 ? 0.49312 0.35251 0.27072 0.02755  -0.02124 0.02256  271 CYS A SG  
2006 N N   . LEU A 272 ? 0.52316 0.33707 0.21088 0.01919  0.00670  0.03774  272 LEU A N   
2007 C CA  . LEU A 272 ? 0.53057 0.33342 0.20056 0.01385  0.01877  0.04434  272 LEU A CA  
2008 C C   . LEU A 272 ? 0.62692 0.41877 0.29881 0.01315  0.01637  0.05296  272 LEU A C   
2009 O O   . LEU A 272 ? 0.60152 0.37704 0.25305 0.01650  0.00967  0.06004  272 LEU A O   
2010 C CB  . LEU A 272 ? 0.54645 0.33643 0.18182 0.01516  0.01921  0.04657  272 LEU A CB  
2011 C CG  . LEU A 272 ? 0.63195 0.42977 0.26143 0.01728  0.01944  0.03702  272 LEU A CG  
2012 C CD1 . LEU A 272 ? 0.67963 0.46336 0.27082 0.01880  0.01963  0.03929  272 LEU A CD1 
2013 C CD2 . LEU A 272 ? 0.55347 0.36585 0.20041 0.01294  0.03323  0.03064  272 LEU A CD2 
2014 N N   . ASP A 273 ? 0.63891 0.43935 0.33527 0.00927  0.02143  0.05198  273 ASP A N   
2015 C CA  . ASP A 273 ? 0.52043 0.31104 0.22190 0.00881  0.01896  0.05824  273 ASP A CA  
2016 C C   . ASP A 273 ? 0.61522 0.38680 0.29495 0.00287  0.02793  0.06707  273 ASP A C   
2017 O O   . ASP A 273 ? 0.61037 0.38289 0.28100 -0.00387 0.04039  0.06729  273 ASP A O   
2018 C CB  . ASP A 273 ? 0.45312 0.25828 0.18519 0.00549  0.02261  0.05385  273 ASP A CB  
2019 C CG  . ASP A 273 ? 0.46106 0.27931 0.21428 0.01196  0.01152  0.04852  273 ASP A CG  
2020 O OD1 . ASP A 273 ? 0.54949 0.36823 0.29621 0.01809  0.00168  0.04706  273 ASP A OD1 
2021 O OD2 . ASP A 273 ? 0.49483 0.32336 0.27086 0.01041  0.01282  0.04569  273 ASP A OD2 
2022 N N   . ALA A 274 ? 0.63306 0.38757 0.30607 0.00523  0.02211  0.07427  274 ALA A N   
2023 C CA  . ALA A 274 ? 0.59193 0.32475 0.24595 -0.00078 0.02974  0.08372  274 ALA A CA  
2024 C C   . ALA A 274 ? 0.68329 0.42162 0.35750 -0.01054 0.04073  0.08216  274 ALA A C   
2025 O O   . ALA A 274 ? 0.68358 0.44006 0.38577 -0.01020 0.03924  0.07469  274 ALA A O   
2026 C CB  . ALA A 274 ? 0.73186 0.44342 0.37287 0.00673  0.01818  0.09139  274 ALA A CB  
2027 N N   . PRO A 275 ? 0.69775 0.42101 0.35803 -0.01988 0.05185  0.08909  275 PRO A N   
2028 C CA  . PRO A 275 ? 0.72132 0.44917 0.40115 -0.03016 0.06141  0.08744  275 PRO A CA  
2029 C C   . PRO A 275 ? 0.90537 0.62857 0.60199 -0.02628 0.05243  0.08620  275 PRO A C   
2030 O O   . PRO A 275 ? 0.78895 0.49408 0.47389 -0.01833 0.04221  0.09127  275 PRO A O   
2031 C CB  . PRO A 275 ? 0.76422 0.47054 0.42033 -0.04024 0.07279  0.09725  275 PRO A CB  
2032 C CG  . PRO A 275 ? 0.71379 0.41597 0.34262 -0.03710 0.07421  0.10073  275 PRO A CG  
2033 C CD  . PRO A 275 ? 0.81773 0.52177 0.44401 -0.02291 0.05774  0.09807  275 PRO A CD  
2034 N N   . GLY A 276 ? 0.84392 0.58474 0.56824 -0.03115 0.05605  0.07886  276 GLY A N   
2035 C CA  . GLY A 276 ? 0.89878 0.63879 0.64038 -0.02708 0.04800  0.07578  276 GLY A CA  
2036 C C   . GLY A 276 ? 0.94176 0.65695 0.67620 -0.03283 0.05038  0.08158  276 GLY A C   
2037 O O   . GLY A 276 ? 1.07724 0.78116 0.81450 -0.02604 0.04148  0.08184  276 GLY A O   
2038 N N   . GLY A 277 ? 1.02959 0.73564 0.75496 -0.04540 0.06259  0.08604  277 GLY A N   
2039 C CA  . GLY A 277 ? 1.05192 0.73291 0.77090 -0.05307 0.06596  0.09140  277 GLY A CA  
2040 C C   . GLY A 277 ? 1.08272 0.77334 0.82774 -0.05986 0.06782  0.08368  277 GLY A C   
2041 O O   . GLY A 277 ? 1.03905 0.70829 0.78013 -0.06748 0.07075  0.08694  277 GLY A O   
2042 N N   . VAL A 278 ? 0.81446 0.53510 0.58481 -0.05737 0.06580  0.07359  278 VAL A N   
2043 C CA  . VAL A 278 ? 0.88677 0.61963 0.68148 -0.06397 0.06746  0.06559  278 VAL A CA  
2044 C C   . VAL A 278 ? 0.86737 0.62629 0.67713 -0.07444 0.07827  0.06083  278 VAL A C   
2045 O O   . VAL A 278 ? 0.88583 0.65856 0.69186 -0.07273 0.08223  0.06123  278 VAL A O   
2046 C CB  . VAL A 278 ? 0.87963 0.62627 0.69199 -0.05260 0.05623  0.05781  278 VAL A CB  
2047 C CG1 . VAL A 278 ? 0.90225 0.62415 0.70336 -0.04294 0.04646  0.06134  278 VAL A CG1 
2048 C CG2 . VAL A 278 ? 0.87161 0.64252 0.69060 -0.04365 0.05240  0.05433  278 VAL A CG2 
2049 N N   . GLU A 279 ? 0.84792 0.61359 0.67493 -0.08522 0.08293  0.05579  279 GLU A N   
2050 C CA  . GLU A 279 ? 0.84667 0.64110 0.69291 -0.09425 0.09187  0.04984  279 GLU A CA  
2051 C C   . GLU A 279 ? 0.69740 0.51986 0.55616 -0.08374 0.08769  0.04383  279 GLU A C   
2052 O O   . GLU A 279 ? 0.66760 0.49354 0.53160 -0.07255 0.07718  0.04058  279 GLU A O   
2053 C CB  . GLU A 279 ? 0.94567 0.74706 0.81272 -0.10402 0.09272  0.04291  279 GLU A CB  
2054 C CG  . GLU A 279 ? 0.73552 0.57002 0.62614 -0.11239 0.10021  0.03571  279 GLU A CG  
2055 N N   . LEU A 280 ? 0.61925 0.46104 0.48231 -0.08721 0.09632  0.04247  280 LEU A N   
2056 C CA  . LEU A 280 ? 0.65784 0.52171 0.52911 -0.07679 0.09270  0.03761  280 LEU A CA  
2057 C C   . LEU A 280 ? 0.58975 0.48202 0.48968 -0.07678 0.09099  0.02820  280 LEU A C   
2058 O O   . LEU A 280 ? 0.55195 0.46714 0.46316 -0.07538 0.09509  0.02388  280 LEU A O   
2059 C CB  . LEU A 280 ? 0.69681 0.56571 0.55618 -0.07802 0.10202  0.04028  280 LEU A CB  
2060 C CG  . LEU A 280 ? 0.70697 0.55486 0.53826 -0.07038 0.09826  0.04736  280 LEU A CG  
2061 C CD1 . LEU A 280 ? 0.82376 0.64168 0.63270 -0.07703 0.10124  0.05685  280 LEU A CD1 
2062 C CD2 . LEU A 280 ? 0.92208 0.78139 0.74539 -0.06778 0.10472  0.04644  280 LEU A CD2 
2063 N N   . SER A 281 ? 0.50829 0.39852 0.41917 -0.07758 0.08456  0.02483  281 SER A N   
2064 C CA  . SER A 281 ? 0.48657 0.40183 0.42178 -0.07583 0.08069  0.01633  281 SER A CA  
2065 C C   . SER A 281 ? 0.46091 0.38863 0.39974 -0.06236 0.07334  0.01399  281 SER A C   
2066 O O   . SER A 281 ? 0.47693 0.39217 0.40090 -0.05420 0.06888  0.01807  281 SER A O   
2067 C CB  . SER A 281 ? 0.56082 0.46778 0.50232 -0.07804 0.07430  0.01329  281 SER A CB  
2068 O OG  . SER A 281 ? 0.47257 0.36458 0.40361 -0.06712 0.06491  0.01547  281 SER A OG  
2069 N N   . ASP A 282 ? 0.44980 0.40237 0.40888 -0.06025 0.07161  0.00734  282 ASP A N   
2070 C CA  . ASP A 282 ? 0.39115 0.35417 0.35419 -0.04836 0.06471  0.00540  282 ASP A CA  
2071 C C   . ASP A 282 ? 0.34058 0.28956 0.29646 -0.04099 0.05496  0.00713  282 ASP A C   
2072 O O   . ASP A 282 ? 0.35639 0.30217 0.30516 -0.03233 0.05026  0.00912  282 ASP A O   
2073 C CB  . ASP A 282 ? 0.38523 0.37492 0.37048 -0.04720 0.06352  -0.00137 282 ASP A CB  
2074 C CG  . ASP A 282 ? 0.50313 0.51104 0.49685 -0.04988 0.07216  -0.00361 282 ASP A CG  
2075 O OD1 . ASP A 282 ? 0.49577 0.49579 0.47675 -0.05179 0.07927  -0.00005 282 ASP A OD1 
2076 O OD2 . ASP A 282 ? 0.50714 0.53778 0.51987 -0.04940 0.07173  -0.00906 282 ASP A OD2 
2077 N N   . THR A 283 ? 0.32161 0.26252 0.27971 -0.04443 0.05196  0.00587  283 THR A N   
2078 C CA  . THR A 283 ? 0.34431 0.27274 0.29626 -0.03698 0.04353  0.00698  283 THR A CA  
2079 C C   . THR A 283 ? 0.39102 0.29797 0.32319 -0.03318 0.04242  0.01378  283 THR A C   
2080 O O   . THR A 283 ? 0.39557 0.30021 0.32359 -0.02404 0.03580  0.01516  283 THR A O   
2081 C CB  . THR A 283 ? 0.43911 0.36049 0.39529 -0.04176 0.04160  0.00367  283 THR A CB  
2082 O OG1 . THR A 283 ? 0.36420 0.30729 0.33827 -0.04452 0.04123  -0.00305 283 THR A OG1 
2083 C CG2 . THR A 283 ? 0.36365 0.27310 0.31400 -0.03309 0.03361  0.00409  283 THR A CG2 
2084 N N   . HIS A 284 ? 0.35153 0.24308 0.27121 -0.04034 0.04871  0.01829  284 HIS A N   
2085 C CA  . HIS A 284 ? 0.44891 0.31857 0.34768 -0.03639 0.04686  0.02532  284 HIS A CA  
2086 C C   . HIS A 284 ? 0.37230 0.24829 0.26405 -0.03038 0.04641  0.02718  284 HIS A C   
2087 O O   . HIS A 284 ? 0.41893 0.28554 0.29992 -0.02238 0.03973  0.03029  284 HIS A O   
2088 C CB  . HIS A 284 ? 0.45430 0.30412 0.33987 -0.04628 0.05411  0.03042  284 HIS A CB  
2089 C CG  . HIS A 284 ? 0.68152 0.51531 0.56773 -0.04979 0.05181  0.02978  284 HIS A CG  
2090 N ND1 . HIS A 284 ? 0.70560 0.52078 0.58330 -0.06055 0.05819  0.03336  284 HIS A ND1 
2091 C CD2 . HIS A 284 ? 0.58517 0.41798 0.47899 -0.04396 0.04409  0.02559  284 HIS A CD2 
2092 C CE1 . HIS A 284 ? 0.67235 0.47445 0.55242 -0.06101 0.05391  0.03098  284 HIS A CE1 
2093 N NE2 . HIS A 284 ? 0.74716 0.56029 0.63684 -0.05061 0.04546  0.02595  284 HIS A NE2 
2094 N N   A ARG A 285 ? 0.40434 0.29661 0.30253 -0.03380 0.05309  0.02468  285 ARG A N   
2095 N N   B ARG A 285 ? 0.40446 0.29655 0.30243 -0.03385 0.05316  0.02475  285 ARG A N   
2096 C CA  A ARG A 285 ? 0.40621 0.30403 0.29795 -0.02788 0.05259  0.02502  285 ARG A CA  
2097 C CA  B ARG A 285 ? 0.40619 0.30388 0.29781 -0.02778 0.05250  0.02505  285 ARG A CA  
2098 C C   A ARG A 285 ? 0.40723 0.31381 0.30740 -0.01831 0.04310  0.02209  285 ARG A C   
2099 C C   B ARG A 285 ? 0.40763 0.31372 0.30757 -0.01823 0.04290  0.02220  285 ARG A C   
2100 O O   A ARG A 285 ? 0.44053 0.34222 0.33079 -0.01207 0.03830  0.02384  285 ARG A O   
2101 O O   B ARG A 285 ? 0.44046 0.34112 0.33032 -0.01193 0.03786  0.02408  285 ARG A O   
2102 C CB  A ARG A 285 ? 0.44064 0.35549 0.34006 -0.03248 0.06189  0.02166  285 ARG A CB  
2103 C CB  B ARG A 285 ? 0.43992 0.35511 0.33954 -0.03200 0.06151  0.02154  285 ARG A CB  
2104 C CG  A ARG A 285 ? 0.48691 0.39478 0.37861 -0.04327 0.07269  0.02485  285 ARG A CG  
2105 C CG  B ARG A 285 ? 0.48566 0.39571 0.37893 -0.04280 0.07258  0.02424  285 ARG A CG  
2106 C CD  A ARG A 285 ? 0.53391 0.45962 0.43188 -0.04721 0.08314  0.02166  285 ARG A CD  
2107 C CD  B ARG A 285 ? 0.53374 0.45310 0.42205 -0.04416 0.08184  0.02344  285 ARG A CD  
2108 N NE  A ARG A 285 ? 0.47486 0.42527 0.39809 -0.04714 0.08326  0.01456  285 ARG A NE  
2109 N NE  B ARG A 285 ? 0.32992 0.27297 0.23615 -0.03939 0.08193  0.01650  285 ARG A NE  
2110 C CZ  A ARG A 285 ? 0.43758 0.40570 0.37039 -0.04085 0.08349  0.00979  285 ARG A CZ  
2111 C CZ  B ARG A 285 ? 0.44290 0.40577 0.37133 -0.04257 0.08425  0.01134  285 ARG A CZ  
2112 N NH1 A ARG A 285 ? 0.37717 0.34178 0.29700 -0.03523 0.08483  0.01037  285 ARG A NH1 
2113 N NH1 B ARG A 285 ? 0.55224 0.51552 0.48895 -0.05167 0.08690  0.01143  285 ARG A NH1 
2114 N NH2 A ARG A 285 ? 0.40560 0.39450 0.36067 -0.03986 0.08195  0.00410  285 ARG A NH2 
2115 N NH2 B ARG A 285 ? 0.37676 0.35882 0.31920 -0.03628 0.08319  0.00581  285 ARG A NH2 
2116 N N   . ALA A 286 ? 0.33432 0.25361 0.25215 -0.01756 0.04017  0.01772  286 ALA A N   
2117 C CA  . ALA A 286 ? 0.33496 0.26193 0.26056 -0.00954 0.03197  0.01572  286 ALA A CA  
2118 C C   . ALA A 286 ? 0.36223 0.27496 0.27878 -0.00432 0.02463  0.01901  286 ALA A C   
2119 O O   . ALA A 286 ? 0.32047 0.23546 0.23634 0.00216  0.01858  0.01932  286 ALA A O   
2120 C CB  . ALA A 286 ? 0.32209 0.26439 0.26587 -0.01030 0.03095  0.01096  286 ALA A CB  
2121 N N   . LEU A 287 ? 0.37755 0.27596 0.28836 -0.00690 0.02476  0.02111  287 LEU A N   
2122 C CA  . LEU A 287 ? 0.36943 0.25455 0.27211 -0.00038 0.01749  0.02407  287 LEU A CA  
2123 C C   . LEU A 287 ? 0.41081 0.28678 0.29766 0.00351  0.01478  0.02860  287 LEU A C   
2124 O O   . LEU A 287 ? 0.37297 0.24932 0.25907 0.01089  0.00707  0.02922  287 LEU A O   
2125 C CB  . LEU A 287 ? 0.35642 0.22390 0.25315 -0.00346 0.01849  0.02581  287 LEU A CB  
2126 C CG  . LEU A 287 ? 0.36838 0.24374 0.27990 -0.00640 0.01921  0.02019  287 LEU A CG  
2127 C CD1 . LEU A 287 ? 0.47968 0.33393 0.38349 -0.00921 0.01965  0.02156  287 LEU A CD1 
2128 C CD2 . LEU A 287 ? 0.34998 0.23990 0.27357 0.00117  0.01304  0.01635  287 LEU A CD2 
2129 N N   . GLN A 288 ? 0.36540 0.23378 0.23923 -0.00158 0.02108  0.03159  288 GLN A N   
2130 C CA  . GLN A 288 ? 0.42089 0.28032 0.27716 0.00203  0.01839  0.03549  288 GLN A CA  
2131 C C   . GLN A 288 ? 0.40332 0.27728 0.26594 0.00690  0.01403  0.03184  288 GLN A C   
2132 O O   . GLN A 288 ? 0.39433 0.26411 0.24883 0.01265  0.00663  0.03336  288 GLN A O   
2133 C CB  . GLN A 288 ? 0.46637 0.31679 0.30708 -0.00486 0.02748  0.03890  288 GLN A CB  
2134 C CG  . GLN A 288 ? 0.51261 0.35368 0.33244 -0.00092 0.02459  0.04251  288 GLN A CG  
2135 C CD  . GLN A 288 ? 0.59918 0.42785 0.39958 -0.00746 0.03378  0.04729  288 GLN A CD  
2136 O OE1 . GLN A 288 ? 0.62177 0.44256 0.42139 -0.01474 0.04069  0.05002  288 GLN A OE1 
2137 N NE2 . GLN A 288 ? 0.50764 0.33423 0.29156 -0.00549 0.03425  0.04815  288 GLN A NE2 
2138 N N   . LEU A 289 ? 0.37271 0.26334 0.24975 0.00471  0.01804  0.02696  289 LEU A N   
2139 C CA  . LEU A 289 ? 0.33979 0.24167 0.22303 0.00911  0.01372  0.02362  289 LEU A CA  
2140 C C   . LEU A 289 ? 0.35630 0.26422 0.25108 0.01436  0.00519  0.02264  289 LEU A C   
2141 O O   . LEU A 289 ? 0.35957 0.27076 0.25456 0.01826  -0.00082 0.02177  289 LEU A O   
2142 C CB  . LEU A 289 ? 0.31753 0.23419 0.21288 0.00649  0.01994  0.01910  289 LEU A CB  
2143 C CG  . LEU A 289 ? 0.37256 0.28852 0.25764 0.00457  0.02657  0.01803  289 LEU A CG  
2144 C CD1 . LEU A 289 ? 0.37117 0.28271 0.24579 0.00941  0.02065  0.01728  289 LEU A CD1 
2145 C CD2 . LEU A 289 ? 0.52382 0.42759 0.39358 -0.00070 0.03327  0.02210  289 LEU A CD2 
2146 N N   . LEU A 290 ? 0.29596 0.20564 0.20025 0.01422  0.00472  0.02238  290 LEU A N   
2147 C CA  . LEU A 290 ? 0.28982 0.20758 0.20557 0.01924  -0.00202 0.02105  290 LEU A CA  
2148 C C   . LEU A 290 ? 0.38910 0.29819 0.29712 0.02485  -0.00963 0.02392  290 LEU A C   
2149 O O   . LEU A 290 ? 0.35364 0.27099 0.26828 0.02889  -0.01574 0.02296  290 LEU A O   
2150 C CB  . LEU A 290 ? 0.28647 0.20944 0.21377 0.01803  -0.00009 0.01893  290 LEU A CB  
2151 C CG  . LEU A 290 ? 0.28319 0.22127 0.22358 0.01504  0.00394  0.01526  290 LEU A CG  
2152 C CD1 . LEU A 290 ? 0.30821 0.24813 0.25552 0.01255  0.00614  0.01299  290 LEU A CD1 
2153 C CD2 . LEU A 290 ? 0.30921 0.26044 0.25967 0.01857  0.00015  0.01388  290 LEU A CD2 
2154 N N   . HIS A 291 ? 0.35978 0.25249 0.25453 0.02523  -0.00963 0.02760  291 HIS A N   
2155 C CA  . HIS A 291 ? 0.46438 0.34921 0.35265 0.03209  -0.01776 0.03040  291 HIS A CA  
2156 C C   . HIS A 291 ? 0.39789 0.26272 0.26436 0.03228  -0.01811 0.03580  291 HIS A C   
2157 O O   . HIS A 291 ? 0.38732 0.24297 0.24674 0.03878  -0.02517 0.03886  291 HIS A O   
2158 C CB  . HIS A 291 ? 0.33017 0.21576 0.22839 0.03634  -0.02019 0.02923  291 HIS A CB  
2159 C CG  . HIS A 291 ? 0.31910 0.19483 0.21589 0.03197  -0.01401 0.02905  291 HIS A CG  
2160 N ND1 . HIS A 291 ? 0.33065 0.18747 0.21166 0.02779  -0.00999 0.03310  291 HIS A ND1 
2161 C CD2 . HIS A 291 ? 0.30333 0.18495 0.21203 0.03074  -0.01147 0.02512  291 HIS A CD2 
2162 C CE1 . HIS A 291 ? 0.39169 0.24338 0.27646 0.02339  -0.00522 0.03141  291 HIS A CE1 
2163 N NE2 . HIS A 291 ? 0.32588 0.19252 0.22713 0.02542  -0.00644 0.02617  291 HIS A NE2 
2164 N N   . GLY A 292 ? 0.37795 0.23635 0.23336 0.02583  -0.01073 0.03726  292 GLY A N   
2165 C CA  . GLY A 292 ? 0.43525 0.27451 0.26764 0.02494  -0.00961 0.04306  292 GLY A CA  
2166 C C   . GLY A 292 ? 0.48860 0.30862 0.31231 0.02507  -0.00891 0.04782  292 GLY A C   
2167 O O   . GLY A 292 ? 0.49958 0.30091 0.30202 0.02493  -0.00864 0.05401  292 GLY A O   
2168 N N   . GLY A 293 ? 0.43134 0.25383 0.26930 0.02535  -0.00856 0.04517  293 GLY A N   
2169 C CA  . GLY A 293 ? 0.43552 0.23800 0.26609 0.02647  -0.00896 0.04872  293 GLY A CA  
2170 C C   . GLY A 293 ? 0.46298 0.25611 0.28766 0.03767  -0.01941 0.05165  293 GLY A C   
2171 O O   . GLY A 293 ? 0.52019 0.29192 0.33407 0.03995  -0.02050 0.05587  293 GLY A O   
2172 N N   . GLY A 294 ? 0.48858 0.29702 0.32075 0.04485  -0.02737 0.04943  294 GLY A N   
2173 C CA  . GLY A 294 ? 0.43613 0.23938 0.26537 0.05619  -0.03795 0.05164  294 GLY A CA  
2174 C C   . GLY A 294 ? 0.56146 0.34963 0.36746 0.05967  -0.04331 0.05842  294 GLY A C   
2175 O O   . GLY A 294 ? 0.48285 0.26268 0.27264 0.05303  -0.03802 0.06178  294 GLY A O   
2176 N N   . TYR A 295 ? 0.50571 0.29075 0.30960 0.07093  -0.05415 0.06042  295 TYR A N   
2177 C CA  . TYR A 295 ? 0.55485 0.32939 0.33773 0.07590  -0.06183 0.06621  295 TYR A CA  
2178 C C   . TYR A 295 ? 0.65977 0.40498 0.41500 0.07203  -0.05680 0.07467  295 TYR A C   
2179 O O   . TYR A 295 ? 0.65993 0.39818 0.39482 0.06994  -0.05718 0.07885  295 TYR A O   
2180 C CB  . TYR A 295 ? 0.54569 0.32298 0.33315 0.08968  -0.07501 0.06676  295 TYR A CB  
2181 C CG  . TYR A 295 ? 0.68253 0.44670 0.44612 0.09571  -0.08411 0.07337  295 TYR A CG  
2182 C CD1 . TYR A 295 ? 0.62651 0.39829 0.38044 0.09164  -0.08588 0.07283  295 TYR A CD1 
2183 C CD2 . TYR A 295 ? 0.68772 0.43571 0.44190 0.10364  -0.08923 0.07835  295 TYR A CD2 
2184 C CE1 . TYR A 295 ? 0.66050 0.42373 0.39428 0.09574  -0.09327 0.07738  295 TYR A CE1 
2185 C CE2 . TYR A 295 ? 0.72603 0.46890 0.46425 0.10666  -0.09544 0.08246  295 TYR A CE2 
2186 C CZ  . TYR A 295 ? 0.74604 0.49673 0.47396 0.10257  -0.09739 0.08192  295 TYR A CZ  
2187 O OH  . TYR A 295 ? 0.81670 0.56192 0.52758 0.10581  -0.10381 0.08574  295 TYR A OH  
2188 N N   . SER A 296 ? 0.60592 0.33290 0.35900 0.07059  -0.05181 0.07723  296 SER A N   
2189 C CA  . SER A 296 ? 0.73186 0.42877 0.45863 0.06605  -0.04660 0.08612  296 SER A CA  
2190 C C   . SER A 296 ? 0.71036 0.40823 0.42900 0.05215  -0.03424 0.08681  296 SER A C   
2191 O O   . SER A 296 ? 0.74271 0.41818 0.43752 0.04710  -0.02898 0.09470  296 SER A O   
2192 C CB  . SER A 296 ? 0.70335 0.38048 0.43213 0.06639  -0.04374 0.08747  296 SER A CB  
2193 O OG  . SER A 296 ? 0.77982 0.46720 0.52587 0.05578  -0.03346 0.08113  296 SER A OG  
2194 N N   . LYS A 297 ? 0.59659 0.31959 0.33410 0.04618  -0.02925 0.07903  297 LYS A N   
2195 C CA  . LYS A 297 ? 0.56444 0.29170 0.29738 0.03425  -0.01749 0.07848  297 LYS A CA  
2196 C C   . LYS A 297 ? 0.59758 0.34301 0.33022 0.03533  -0.02010 0.07481  297 LYS A C   
2197 O O   . LYS A 297 ? 0.63827 0.37542 0.35044 0.03961  -0.02563 0.07911  297 LYS A O   
2198 C CB  . LYS A 297 ? 0.58728 0.32627 0.34226 0.02586  -0.00849 0.07231  297 LYS A CB  
2199 C CG  . LYS A 297 ? 0.64336 0.36110 0.39538 0.02227  -0.00455 0.07563  297 LYS A CG  
2200 C CD  . LYS A 297 ? 0.73679 0.43024 0.46245 0.01490  0.00274  0.08470  297 LYS A CD  
2201 C CE  . LYS A 297 ? 1.10488 0.77555 0.82738 0.00845  0.00820  0.08800  297 LYS A CE  
2202 N NZ  . LYS A 297 ? 1.05027 0.69813 0.74775 -0.00090 0.01708  0.09731  297 LYS A NZ  
2203 N N   . ASN A 298 ? 0.49470 0.26378 0.24886 0.03197  -0.01697 0.06675  298 ASN A N   
2204 C CA  . ASN A 298 ? 0.59292 0.37734 0.34730 0.03258  -0.01920 0.06253  298 ASN A CA  
2205 C C   . ASN A 298 ? 0.47451 0.27881 0.25012 0.03883  -0.02848 0.05627  298 ASN A C   
2206 O O   . ASN A 298 ? 0.50780 0.32580 0.28788 0.03812  -0.02982 0.05155  298 ASN A O   
2207 C CB  . ASN A 298 ? 0.49645 0.29098 0.25543 0.02316  -0.00706 0.05866  298 ASN A CB  
2208 C CG  . ASN A 298 ? 0.62672 0.40511 0.36228 0.01639  0.00273  0.06450  298 ASN A CG  
2209 O OD1 . ASN A 298 ? 0.59443 0.36385 0.30710 0.01827  0.00088  0.06793  298 ASN A OD1 
2210 N ND2 . ASN A 298 ? 0.49881 0.27420 0.23982 0.00805  0.01327  0.06546  298 ASN A ND2 
2211 N N   . GLY A 299 ? 0.49803 0.30407 0.28683 0.04468  -0.03440 0.05590  299 GLY A N   
2212 C CA  . GLY A 299 ? 0.47759 0.30502 0.28924 0.04881  -0.04065 0.04981  299 GLY A CA  
2213 C C   . GLY A 299 ? 0.48773 0.32300 0.29689 0.05463  -0.05165 0.04869  299 GLY A C   
2214 O O   . GLY A 299 ? 0.45243 0.30680 0.27959 0.05492  -0.05488 0.04325  299 GLY A O   
2215 N N   . ALA A 300 ? 0.44041 0.26132 0.22754 0.05895  -0.05782 0.05378  300 ALA A N   
2216 C CA  . ALA A 300 ? 0.46181 0.29057 0.24536 0.06381  -0.06907 0.05206  300 ALA A CA  
2217 C C   . ALA A 300 ? 0.55894 0.38774 0.32860 0.05811  -0.06609 0.04987  300 ALA A C   
2218 O O   . ALA A 300 ? 0.49022 0.32564 0.25639 0.06065  -0.07514 0.04709  300 ALA A O   
2219 C CB  . ALA A 300 ? 0.48873 0.30340 0.25563 0.07327  -0.07965 0.05828  300 ALA A CB  
2220 N N   . ASN A 301 ? 0.46830 0.29072 0.23068 0.05052  -0.05370 0.05035  301 ASN A N   
2221 C CA  . ASN A 301 ? 0.50685 0.32871 0.25521 0.04575  -0.04923 0.04779  301 ASN A CA  
2222 C C   . ASN A 301 ? 0.46920 0.30976 0.23838 0.04191  -0.04662 0.03955  301 ASN A C   
2223 O O   . ASN A 301 ? 0.46803 0.31060 0.23719 0.03621  -0.03650 0.03683  301 ASN A O   
2224 C CB  . ASN A 301 ? 0.58533 0.39268 0.31673 0.03974  -0.03647 0.05237  301 ASN A CB  
2225 C CG  . ASN A 301 ? 0.56693 0.36719 0.27340 0.03761  -0.03355 0.05239  301 ASN A CG  
2226 O OD1 . ASN A 301 ? 0.51685 0.31056 0.20504 0.04252  -0.04294 0.05397  301 ASN A OD1 
2227 N ND2 . ASN A 301 ? 0.60303 0.40527 0.30824 0.03059  -0.02046 0.05030  301 ASN A ND2 
2228 N N   . ARG A 302 ? 0.45157 0.30598 0.23888 0.04530  -0.05589 0.03579  302 ARG A N   
2229 C CA  . ARG A 302 ? 0.42970 0.30105 0.24087 0.04205  -0.05371 0.02964  302 ARG A CA  
2230 C C   . ARG A 302 ? 0.46949 0.35253 0.29045 0.04467  -0.06546 0.02559  302 ARG A C   
2231 O O   . ARG A 302 ? 0.43955 0.32188 0.25645 0.05016  -0.07575 0.02763  302 ARG A O   
2232 C CB  . ARG A 302 ? 0.45187 0.33001 0.28325 0.04184  -0.04929 0.03061  302 ARG A CB  
2233 C CG  . ARG A 302 ? 0.43013 0.29912 0.25668 0.03801  -0.03806 0.03366  302 ARG A CG  
2234 C CD  . ARG A 302 ? 0.39166 0.26658 0.22279 0.03187  -0.02834 0.02978  302 ARG A CD  
2235 N NE  . ARG A 302 ? 0.43001 0.30045 0.26166 0.02758  -0.01815 0.03192  302 ARG A NE  
2236 C CZ  . ARG A 302 ? 0.53066 0.38841 0.34458 0.02427  -0.01135 0.03545  302 ARG A CZ  
2237 N NH1 . ARG A 302 ? 0.42924 0.27651 0.22102 0.02539  -0.01326 0.03759  302 ARG A NH1 
2238 N NH2 . ARG A 302 ? 0.43555 0.29108 0.25347 0.01928  -0.00248 0.03691  302 ARG A NH2 
2239 N N   . TRP A 303 ? 0.43826 0.33254 0.27360 0.04067  -0.06404 0.01994  303 TRP A N   
2240 C CA  . TRP A 303 ? 0.38588 0.29349 0.23628 0.04106  -0.07370 0.01593  303 TRP A CA  
2241 C C   . TRP A 303 ? 0.37748 0.29707 0.25050 0.03686  -0.06785 0.01316  303 TRP A C   
2242 O O   . TRP A 303 ? 0.34257 0.26170 0.21592 0.03265  -0.06371 0.00931  303 TRP A O   
2243 C CB  . TRP A 303 ? 0.41103 0.31525 0.24804 0.03971  -0.08043 0.01139  303 TRP A CB  
2244 C CG  . TRP A 303 ? 0.39108 0.30800 0.24113 0.04053  -0.09284 0.00828  303 TRP A CG  
2245 C CD1 . TRP A 303 ? 0.39036 0.32037 0.26136 0.03602  -0.09456 0.00380  303 TRP A CD1 
2246 C CD2 . TRP A 303 ? 0.36452 0.28338 0.20905 0.04603  -0.10517 0.00978  303 TRP A CD2 
2247 N NE1 . TRP A 303 ? 0.39432 0.33569 0.27436 0.03735  -0.10685 0.00195  303 TRP A NE1 
2248 C CE2 . TRP A 303 ? 0.36987 0.30555 0.23450 0.04408  -0.11394 0.00531  303 TRP A CE2 
2249 C CE3 . TRP A 303 ? 0.44352 0.35124 0.26766 0.05249  -0.10990 0.01478  303 TRP A CE3 
2250 C CZ2 . TRP A 303 ? 0.39828 0.34266 0.26534 0.04870  -0.12758 0.00494  303 TRP A CZ2 
2251 C CZ3 . TRP A 303 ? 0.45825 0.37262 0.28304 0.05808  -0.12386 0.01496  303 TRP A CZ3 
2252 C CH2 . TRP A 303 ? 0.42270 0.35656 0.26974 0.05630  -0.13281 0.00964  303 TRP A CH2 
2253 N N   . TYR A 304 ? 0.34280 0.27244 0.23366 0.03859  -0.06759 0.01508  304 TYR A N   
2254 C CA  . TYR A 304 ? 0.30947 0.24788 0.21751 0.03500  -0.06027 0.01387  304 TYR A CA  
2255 C C   . TYR A 304 ? 0.36221 0.31077 0.28374 0.03089  -0.06326 0.00992  304 TYR A C   
2256 O O   . TYR A 304 ? 0.29274 0.24554 0.22459 0.02768  -0.05702 0.00917  304 TYR A O   
2257 C CB  . TYR A 304 ? 0.31353 0.25910 0.23463 0.03809  -0.05850 0.01659  304 TYR A CB  
2258 C CG  . TYR A 304 ? 0.33478 0.26870 0.24527 0.03960  -0.05200 0.01989  304 TYR A CG  
2259 C CD1 . TYR A 304 ? 0.31274 0.24588 0.22605 0.03589  -0.04238 0.01954  304 TYR A CD1 
2260 C CD2 . TYR A 304 ? 0.34222 0.26552 0.23991 0.04448  -0.05580 0.02344  304 TYR A CD2 
2261 C CE1 . TYR A 304 ? 0.29332 0.21641 0.19827 0.03575  -0.03634 0.02211  304 TYR A CE1 
2262 C CE2 . TYR A 304 ? 0.40438 0.31491 0.29212 0.04458  -0.04946 0.02677  304 TYR A CE2 
2263 C CZ  . TYR A 304 ? 0.36678 0.27780 0.25876 0.03948  -0.03955 0.02577  304 TYR A CZ  
2264 O OH  . TYR A 304 ? 0.38865 0.28812 0.27249 0.03797  -0.03312 0.02847  304 TYR A OH  
2265 N N   . ASP A 305 ? 0.31541 0.26747 0.23696 0.03062  -0.07280 0.00749  305 ASP A N   
2266 C CA  . ASP A 305 ? 0.33675 0.29680 0.27117 0.02518  -0.07549 0.00366  305 ASP A CA  
2267 C C   . ASP A 305 ? 0.34684 0.29597 0.27146 0.02127  -0.07147 0.00003  305 ASP A C   
2268 O O   . ASP A 305 ? 0.30455 0.25664 0.23960 0.01653  -0.07079 -0.00240 305 ASP A O   
2269 C CB  . ASP A 305 ? 0.33852 0.30580 0.27612 0.02493  -0.08750 0.00106  305 ASP A CB  
2270 C CG  . ASP A 305 ? 0.40060 0.38337 0.35375 0.02888  -0.09237 0.00345  305 ASP A CG  
2271 O OD1 . ASP A 305 ? 0.37315 0.36181 0.33662 0.03101  -0.08611 0.00657  305 ASP A OD1 
2272 O OD2 . ASP A 305 ? 0.35522 0.34530 0.31077 0.03005  -0.10298 0.00150  305 ASP A OD2 
2273 N N   . LYS A 306 ? 0.32547 0.26156 0.22985 0.02328  -0.06869 -0.00042 306 LYS A N   
2274 C CA  . LYS A 306 ? 0.36004 0.28613 0.25418 0.02083  -0.06486 -0.00489 306 LYS A CA  
2275 C C   . LYS A 306 ? 0.35764 0.28327 0.25748 0.02051  -0.05367 -0.00354 306 LYS A C   
2276 O O   . LYS A 306 ? 0.36760 0.29531 0.26897 0.02255  -0.04807 0.00061  306 LYS A O   
2277 C CB  . LYS A 306 ? 0.38601 0.29982 0.25511 0.02326  -0.06610 -0.00626 306 LYS A CB  
2278 C CG  . LYS A 306 ? 0.46960 0.37318 0.32630 0.02163  -0.06270 -0.01231 306 LYS A CG  
2279 C CD  . LYS A 306 ? 0.51557 0.41980 0.37935 0.01760  -0.07030 -0.01849 306 LYS A CD  
2280 C CE  . LYS A 306 ? 0.70477 0.59760 0.55870 0.01687  -0.06512 -0.02486 306 LYS A CE  
2281 N NZ  . LYS A 306 ? 0.60370 0.49491 0.46962 0.01247  -0.06806 -0.02980 306 LYS A NZ  
2282 N N   . SER A 307 ? 0.29764 0.21994 0.20034 0.01816  -0.05090 -0.00736 307 SER A N   
2283 C CA  . SER A 307 ? 0.35209 0.27753 0.26536 0.01823  -0.04247 -0.00577 307 SER A CA  
2284 C C   . SER A 307 ? 0.36458 0.28666 0.26878 0.02092  -0.03361 -0.00475 307 SER A C   
2285 O O   . SER A 307 ? 0.34319 0.27160 0.25686 0.02153  -0.02777 -0.00178 307 SER A O   
2286 C CB  . SER A 307 ? 0.42044 0.34094 0.33770 0.01608  -0.04233 -0.00986 307 SER A CB  
2287 O OG  . SER A 307 ? 0.45350 0.37893 0.38271 0.01202  -0.04915 -0.00961 307 SER A OG  
2288 N N   . LEU A 308 ? 0.37277 0.28569 0.25877 0.02211  -0.03212 -0.00743 308 LEU A N   
2289 C CA  . LEU A 308 ? 0.36890 0.27984 0.24695 0.02355  -0.02258 -0.00653 308 LEU A CA  
2290 C C   . LEU A 308 ? 0.39930 0.30353 0.25904 0.02419  -0.02339 -0.00420 308 LEU A C   
2291 O O   . LEU A 308 ? 0.37298 0.26964 0.21753 0.02467  -0.02865 -0.00687 308 LEU A O   
2292 C CB  . LEU A 308 ? 0.30867 0.21510 0.18162 0.02476  -0.01663 -0.01206 308 LEU A CB  
2293 C CG  . LEU A 308 ? 0.34648 0.25716 0.23553 0.02536  -0.01483 -0.01380 308 LEU A CG  
2294 C CD1 . LEU A 308 ? 0.41361 0.31819 0.29506 0.02818  -0.00937 -0.01994 308 LEU A CD1 
2295 C CD2 . LEU A 308 ? 0.36848 0.29010 0.27255 0.02548  -0.00995 -0.00921 308 LEU A CD2 
2296 N N   . GLN A 309 ? 0.32804 0.23390 0.18810 0.02405  -0.01844 0.00074  309 GLN A N   
2297 C CA  . GLN A 309 ? 0.38995 0.28700 0.23128 0.02442  -0.01755 0.00433  309 GLN A CA  
2298 C C   . GLN A 309 ? 0.36827 0.26494 0.20613 0.02254  -0.00545 0.00526  309 GLN A C   
2299 O O   . GLN A 309 ? 0.36872 0.27056 0.21776 0.02099  -0.00103 0.00829  309 GLN A O   
2300 C CB  . GLN A 309 ? 0.38120 0.27844 0.22586 0.02562  -0.02325 0.00986  309 GLN A CB  
2301 C CG  . GLN A 309 ? 0.33440 0.23619 0.18677 0.02754  -0.03480 0.00935  309 GLN A CG  
2302 C CD  . GLN A 309 ? 0.42844 0.33255 0.28767 0.02981  -0.03800 0.01432  309 GLN A CD  
2303 O OE1 . GLN A 309 ? 0.38807 0.28320 0.23339 0.03219  -0.04042 0.01824  309 GLN A OE1 
2304 N NE2 . GLN A 309 ? 0.34670 0.26182 0.22627 0.02947  -0.03741 0.01432  309 GLN A NE2 
2305 N N   . PHE A 310 ? 0.42008 0.31169 0.24316 0.02245  -0.00000 0.00200  310 PHE A N   
2306 C CA  . PHE A 310 ? 0.41229 0.30500 0.23135 0.02017  0.01216  0.00271  310 PHE A CA  
2307 C C   . PHE A 310 ? 0.53393 0.41724 0.33733 0.01795  0.01420  0.00944  310 PHE A C   
2308 O O   . PHE A 310 ? 0.55240 0.42475 0.33600 0.01939  0.00896  0.01144  310 PHE A O   
2309 C CB  . PHE A 310 ? 0.37276 0.26363 0.18032 0.02144  0.01789  -0.00339 310 PHE A CB  
2310 C CG  . PHE A 310 ? 0.40221 0.30021 0.22508 0.02402  0.01726  -0.00983 310 PHE A CG  
2311 C CD1 . PHE A 310 ? 0.34836 0.25760 0.18822 0.02412  0.02494  -0.01132 310 PHE A CD1 
2312 C CD2 . PHE A 310 ? 0.43863 0.33163 0.25914 0.02625  0.00848  -0.01430 310 PHE A CD2 
2313 C CE1 . PHE A 310 ? 0.41059 0.32447 0.26333 0.02746  0.02379  -0.01641 310 PHE A CE1 
2314 C CE2 . PHE A 310 ? 0.36262 0.25918 0.19628 0.02845  0.00801  -0.01961 310 PHE A CE2 
2315 C CZ  . PHE A 310 ? 0.43192 0.33811 0.28072 0.02958  0.01569  -0.02032 310 PHE A CZ  
2316 N N   . VAL A 311 ? 0.41975 0.30641 0.23137 0.01437  0.02126  0.01299  311 VAL A N   
2317 C CA  . VAL A 311 ? 0.43633 0.31179 0.23337 0.01135  0.02432  0.01983  311 VAL A CA  
2318 C C   . VAL A 311 ? 0.47409 0.34985 0.26207 0.00670  0.03778  0.01971  311 VAL A C   
2319 O O   . VAL A 311 ? 0.40835 0.29718 0.21224 0.00453  0.04551  0.01594  311 VAL A O   
2320 C CB  . VAL A 311 ? 0.42255 0.29953 0.23444 0.00979  0.02240  0.02369  311 VAL A CB  
2321 C CG1 . VAL A 311 ? 0.46623 0.32878 0.26281 0.00612  0.02634  0.03086  311 VAL A CG1 
2322 C CG2 . VAL A 311 ? 0.41525 0.29340 0.23524 0.01490  0.00984  0.02356  311 VAL A CG2 
2323 N N   . VAL A 312 ? 0.47099 0.33347 0.23322 0.00552  0.04056  0.02365  312 VAL A N   
2324 C CA  . VAL A 312 ? 0.45984 0.32166 0.21105 0.00002  0.05454  0.02495  312 VAL A CA  
2325 C C   . VAL A 312 ? 0.58427 0.42908 0.31789 -0.00401 0.05572  0.03456  312 VAL A C   
2326 O O   . VAL A 312 ? 0.53697 0.36659 0.24463 -0.00193 0.05202  0.03888  312 VAL A O   
2327 C CB  . VAL A 312 ? 0.54993 0.41103 0.28306 0.00246  0.05870  0.02015  312 VAL A CB  
2328 C CG1 . VAL A 312 ? 0.48546 0.34788 0.20807 -0.00364 0.07468  0.02180  312 VAL A CG1 
2329 C CG2 . VAL A 312 ? 0.44449 0.31940 0.19498 0.00728  0.05656  0.01039  312 VAL A CG2 
2330 N N   . GLY A 313 ? 0.56287 0.40886 0.30994 -0.00951 0.05989  0.03797  313 GLY A N   
2331 C CA  . GLY A 313 ? 0.59924 0.42637 0.33142 -0.01302 0.05978  0.04715  313 GLY A CA  
2332 C C   . GLY A 313 ? 0.53519 0.35368 0.24694 -0.02053 0.07305  0.05220  313 GLY A C   
2333 O O   . GLY A 313 ? 0.56805 0.39997 0.28641 -0.02550 0.08508  0.04827  313 GLY A O   
2334 N N   . ARG A 314 ? 0.57326 0.36907 0.25973 -0.02113 0.07094  0.06142  314 ARG A N   
2335 C CA  . ARG A 314 ? 0.65770 0.44232 0.32078 -0.02875 0.08373  0.06790  314 ARG A CA  
2336 C C   . ARG A 314 ? 0.71684 0.50991 0.39652 -0.04035 0.09770  0.06812  314 ARG A C   
2337 O O   . ARG A 314 ? 0.73225 0.52971 0.40374 -0.04750 0.11185  0.06882  314 ARG A O   
2338 C CB  . ARG A 314 ? 0.61550 0.37171 0.24941 -0.02713 0.07777  0.07909  314 ARG A CB  
2339 C CG  . ARG A 314 ? 0.69388 0.43424 0.30226 -0.03648 0.09135  0.08825  314 ARG A CG  
2340 C CD  . ARG A 314 ? 0.63457 0.38300 0.22699 -0.03581 0.09805  0.08521  314 ARG A CD  
2341 N NE  . ARG A 314 ? 0.76501 0.50879 0.34689 -0.04443 0.10964  0.09137  314 ARG A NE  
2342 C CZ  . ARG A 314 ? 0.74235 0.49754 0.33794 -0.05547 0.12489  0.09066  314 ARG A CZ  
2343 N NH1 . ARG A 314 ? 0.69824 0.47106 0.31927 -0.05920 0.13070  0.08369  314 ARG A NH1 
2344 N NH2 . ARG A 314 ? 0.81823 0.56821 0.40246 -0.06300 0.13437  0.09707  314 ARG A NH2 
2345 N N   . ASP A 315 ? 0.63548 0.43243 0.33892 -0.04255 0.09419  0.06687  315 ASP A N   
2346 C CA  . ASP A 315 ? 0.65045 0.45608 0.37147 -0.05404 0.10569  0.06626  315 ASP A CA  
2347 C C   . ASP A 315 ? 0.71566 0.55194 0.46596 -0.05468 0.11053  0.05574  315 ASP A C   
2348 O O   . ASP A 315 ? 0.61613 0.46390 0.38488 -0.06376 0.11882  0.05383  315 ASP A O   
2349 C CB  . ASP A 315 ? 0.69617 0.48867 0.42603 -0.05648 0.09941  0.06980  315 ASP A CB  
2350 C CG  . ASP A 315 ? 0.78992 0.58933 0.53747 -0.04630 0.08486  0.06433  315 ASP A CG  
2351 O OD1 . ASP A 315 ? 0.65472 0.46902 0.40908 -0.03830 0.07953  0.05817  315 ASP A OD1 
2352 O OD2 . ASP A 315 ? 0.67825 0.46733 0.43242 -0.04657 0.07913  0.06620  315 ASP A OD2 
2353 N N   . GLY A 316 ? 0.55490 0.40436 0.30998 -0.04545 0.10540  0.04882  316 GLY A N   
2354 C CA  . GLY A 316 ? 0.50956 0.38595 0.29033 -0.04467 0.10963  0.03946  316 GLY A CA  
2355 C C   . GLY A 316 ? 0.48770 0.37524 0.29367 -0.03905 0.09875  0.03407  316 GLY A C   
2356 O O   . GLY A 316 ? 0.52744 0.43665 0.35590 -0.03844 0.10150  0.02706  316 GLY A O   
2357 N N   . THR A 317 ? 0.49818 0.37217 0.30087 -0.03456 0.08674  0.03724  317 THR A N   
2358 C CA  . THR A 317 ? 0.46846 0.35302 0.29224 -0.02843 0.07659  0.03228  317 THR A CA  
2359 C C   . THR A 317 ? 0.48049 0.36902 0.30074 -0.01899 0.06954  0.02824  317 THR A C   
2360 O O   . THR A 317 ? 0.48365 0.35792 0.28412 -0.01466 0.06349  0.03143  317 THR A O   
2361 C CB  . THR A 317 ? 0.54698 0.41710 0.37017 -0.02753 0.06769  0.03667  317 THR A CB  
2362 O OG1 . THR A 317 ? 0.54929 0.41571 0.37784 -0.03700 0.07429  0.03904  317 THR A OG1 
2363 C CG2 . THR A 317 ? 0.55975 0.44136 0.40273 -0.02079 0.05767  0.03171  317 THR A CG2 
2364 N N   . CYS A 318 ? 0.41312 0.32041 0.25195 -0.01598 0.07016  0.02118  318 CYS A N   
2365 C CA  . CYS A 318 ? 0.43353 0.34441 0.27063 -0.00809 0.06466  0.01647  318 CYS A CA  
2366 C C   . CYS A 318 ? 0.42936 0.35308 0.28961 -0.00377 0.05769  0.01213  318 CYS A C   
2367 O O   . CYS A 318 ? 0.37748 0.31396 0.25662 -0.00650 0.06075  0.01034  318 CYS A O   
2368 C CB  . CYS A 318 ? 0.42932 0.34822 0.26162 -0.00784 0.07445  0.01185  318 CYS A CB  
2369 S SG  . CYS A 318 ? 0.54533 0.45022 0.34751 -0.01318 0.08461  0.01700  318 CYS A SG  
2370 N N   . GLY A 319 ? 0.37042 0.29085 0.22857 0.00256  0.04830  0.01049  319 GLY A N   
2371 C CA  . GLY A 319 ? 0.33620 0.26756 0.21390 0.00657  0.04231  0.00692  319 GLY A CA  
2372 C C   . GLY A 319 ? 0.40851 0.33328 0.28020 0.01179  0.03253  0.00592  319 GLY A C   
2373 O O   . GLY A 319 ? 0.35109 0.26553 0.20443 0.01296  0.03103  0.00607  319 GLY A O   
2374 N N   . VAL A 320 ? 0.37382 0.30465 0.26041 0.01442  0.02569  0.00495  320 VAL A N   
2375 C CA  . VAL A 320 ? 0.34043 0.26620 0.22364 0.01794  0.01636  0.00407  320 VAL A CA  
2376 C C   . VAL A 320 ? 0.32407 0.25391 0.22028 0.01854  0.00937  0.00662  320 VAL A C   
2377 O O   . VAL A 320 ? 0.31543 0.25484 0.22677 0.01794  0.01130  0.00660  320 VAL A O   
2378 C CB  . VAL A 320 ? 0.33525 0.26382 0.22142 0.02102  0.01653  -0.00158 320 VAL A CB  
2379 C CG1 . VAL A 320 ? 0.27489 0.21602 0.18101 0.02230  0.01917  -0.00342 320 VAL A CG1 
2380 C CG2 . VAL A 320 ? 0.34063 0.26272 0.22257 0.02298  0.00683  -0.00292 320 VAL A CG2 
2381 N N   . VAL A 321 ? 0.30755 0.23101 0.19747 0.01991  0.00138  0.00869  321 VAL A N   
2382 C CA  . VAL A 321 ? 0.28526 0.21382 0.18740 0.02118  -0.00532 0.01051  321 VAL A CA  
2383 C C   . VAL A 321 ? 0.33630 0.26888 0.24551 0.02247  -0.01095 0.00773  321 VAL A C   
2384 O O   . VAL A 321 ? 0.31882 0.24520 0.21798 0.02301  -0.01477 0.00562  321 VAL A O   
2385 C CB  . VAL A 321 ? 0.38381 0.30481 0.27718 0.02264  -0.01116 0.01427  321 VAL A CB  
2386 C CG1 . VAL A 321 ? 0.39262 0.32122 0.30083 0.02426  -0.01536 0.01571  321 VAL A CG1 
2387 C CG2 . VAL A 321 ? 0.43502 0.34536 0.31376 0.02104  -0.00623 0.01754  321 VAL A CG2 
2388 N N   . CYS A 322 ? 0.33178 0.27383 0.25718 0.02256  -0.01179 0.00780  322 CYS A N   
2389 C CA  . CYS A 322 ? 0.33548 0.28021 0.26812 0.02263  -0.01523 0.00564  322 CYS A CA  
2390 C C   . CYS A 322 ? 0.31472 0.26549 0.25736 0.02234  -0.02172 0.00761  322 CYS A C   
2391 O O   . CYS A 322 ? 0.34965 0.30820 0.30215 0.02267  -0.02057 0.00989  322 CYS A O   
2392 C CB  . CYS A 322 ? 0.34498 0.29552 0.28743 0.02307  -0.01004 0.00457  322 CYS A CB  
2393 S SG  . CYS A 322 ? 0.35265 0.30076 0.28761 0.02391  -0.00156 0.00154  322 CYS A SG  
2394 N N   . GLU A 323 ? 0.32911 0.27749 0.26999 0.02146  -0.02830 0.00616  323 GLU A N   
2395 C CA  . GLU A 323 ? 0.28038 0.23731 0.23415 0.02013  -0.03342 0.00748  323 GLU A CA  
2396 C C   . GLU A 323 ? 0.39371 0.35271 0.35660 0.01811  -0.03106 0.00711  323 GLU A C   
2397 O O   . GLU A 323 ? 0.43052 0.38197 0.38920 0.01683  -0.03200 0.00418  323 GLU A O   
2398 C CB  . GLU A 323 ? 0.31385 0.26925 0.26411 0.01916  -0.04190 0.00582  323 GLU A CB  
2399 C CG  . GLU A 323 ? 0.33517 0.30285 0.29908 0.01887  -0.04678 0.00781  323 GLU A CG  
2400 C CD  . GLU A 323 ? 0.35339 0.32873 0.33199 0.01479  -0.04623 0.00827  323 GLU A CD  
2401 O OE1 . GLU A 323 ? 0.38546 0.35582 0.36353 0.01096  -0.04882 0.00577  323 GLU A OE1 
2402 O OE2 . GLU A 323 ? 0.36640 0.35170 0.35605 0.01521  -0.04306 0.01112  323 GLU A OE2 
2403 N N   A HIS A 324 ? 0.35889 0.32725 0.33322 0.01817  -0.02846 0.01014  324 HIS A N   
2404 N N   B HIS A 324 ? 0.36112 0.32861 0.33481 0.01826  -0.02787 0.00994  324 HIS A N   
2405 C CA  A HIS A 324 ? 0.38455 0.35528 0.36616 0.01761  -0.02489 0.01150  324 HIS A CA  
2406 C CA  B HIS A 324 ? 0.37336 0.33982 0.35184 0.01751  -0.02501 0.01025  324 HIS A CA  
2407 C C   A HIS A 324 ? 0.32217 0.29154 0.30968 0.01386  -0.02820 0.01196  324 HIS A C   
2408 C C   B HIS A 324 ? 0.32121 0.29107 0.30933 0.01380  -0.02811 0.01218  324 HIS A C   
2409 O O   A HIS A 324 ? 0.28103 0.24628 0.27026 0.01365  -0.02603 0.01270  324 HIS A O   
2410 O O   B HIS A 324 ? 0.29357 0.26326 0.28634 0.01340  -0.02560 0.01427  324 HIS A O   
2411 C CB  A HIS A 324 ? 0.32550 0.30707 0.31509 0.01888  -0.02192 0.01457  324 HIS A CB  
2412 C CB  B HIS A 324 ? 0.25965 0.23171 0.24166 0.02001  -0.01927 0.01196  324 HIS A CB  
2413 C CG  A HIS A 324 ? 0.28417 0.26855 0.27827 0.01971  -0.01796 0.01625  324 HIS A CG  
2414 C CG  B HIS A 324 ? 0.34522 0.32820 0.33556 0.02005  -0.01886 0.01499  324 HIS A CG  
2415 N ND1 A HIS A 324 ? 0.30536 0.28344 0.29915 0.01941  -0.01767 0.01622  324 HIS A ND1 
2416 N ND1 B HIS A 324 ? 0.24111 0.22861 0.23323 0.01990  -0.02182 0.01554  324 HIS A ND1 
2417 C CD2 A HIS A 324 ? 0.35492 0.34720 0.35312 0.02140  -0.01477 0.01783  324 HIS A CD2 
2418 C CD2 B HIS A 324 ? 0.36916 0.35953 0.36568 0.02098  -0.01587 0.01715  324 HIS A CD2 
2419 C CE1 A HIS A 324 ? 0.32411 0.30652 0.32169 0.02140  -0.01473 0.01838  324 HIS A CE1 
2420 C CE1 B HIS A 324 ? 0.34115 0.33817 0.34044 0.02073  -0.02004 0.01747  324 HIS A CE1 
2421 N NE2 A HIS A 324 ? 0.37634 0.36806 0.37655 0.02234  -0.01306 0.01918  324 HIS A NE2 
2422 N NE2 B HIS A 324 ? 0.27805 0.27683 0.27931 0.02109  -0.01647 0.01848  324 HIS A NE2 
2423 N N   . SER A 325 ? 0.29890 0.27136 0.28985 0.01079  -0.03364 0.01159  325 SER A N   
2424 C CA  . SER A 325 ? 0.26253 0.23684 0.26250 0.00554  -0.03603 0.01293  325 SER A CA  
2425 C C   . SER A 325 ? 0.33288 0.29322 0.32831 0.00334  -0.03645 0.01087  325 SER A C   
2426 O O   . SER A 325 ? 0.31139 0.27084 0.31358 -0.00015 -0.03546 0.01388  325 SER A O   
2427 C CB  . SER A 325 ? 0.26980 0.25218 0.27603 0.00223  -0.04236 0.01196  325 SER A CB  
2428 O OG  . SER A 325 ? 0.34974 0.32400 0.34713 0.00162  -0.04812 0.00735  325 SER A OG  
2429 N N   . PRO A 326 ? 0.28573 0.23420 0.26943 0.00539  -0.03739 0.00607  326 PRO A N   
2430 C CA  . PRO A 326 ? 0.27574 0.20980 0.25520 0.00422  -0.03768 0.00330  326 PRO A CA  
2431 C C   . PRO A 326 ? 0.31799 0.24578 0.29407 0.00958  -0.03188 0.00359  326 PRO A C   
2432 O O   . PRO A 326 ? 0.31945 0.23426 0.29253 0.00962  -0.03227 0.00138  326 PRO A O   
2433 C CB  . PRO A 326 ? 0.37982 0.30494 0.34715 0.00415  -0.04213 -0.00331 326 PRO A CB  
2434 C CG  . PRO A 326 ? 0.38072 0.31503 0.34483 0.00609  -0.04354 -0.00283 326 PRO A CG  
2435 C CD  . PRO A 326 ? 0.34600 0.29236 0.31860 0.00836  -0.03888 0.00263  326 PRO A CD  
2436 N N   . PHE A 327 ? 0.26595 0.20190 0.24248 0.01427  -0.02698 0.00555  327 PHE A N   
2437 C CA  . PHE A 327 ? 0.30815 0.24074 0.28327 0.01965  -0.02217 0.00520  327 PHE A CA  
2438 C C   . PHE A 327 ? 0.29780 0.24365 0.27814 0.02239  -0.01811 0.00864  327 PHE A C   
2439 O O   . PHE A 327 ? 0.27751 0.23191 0.25879 0.02111  -0.01823 0.00965  327 PHE A O   
2440 C CB  . PHE A 327 ? 0.31098 0.23498 0.27515 0.02338  -0.02031 -0.00115 327 PHE A CB  
2441 C CG  . PHE A 327 ? 0.29375 0.22151 0.25029 0.02288  -0.02015 -0.00321 327 PHE A CG  
2442 C CD1 . PHE A 327 ? 0.29689 0.23411 0.25404 0.02502  -0.01549 -0.00156 327 PHE A CD1 
2443 C CD2 . PHE A 327 ? 0.35169 0.27275 0.29983 0.01994  -0.02519 -0.00659 327 PHE A CD2 
2444 C CE1 . PHE A 327 ? 0.37320 0.31136 0.32208 0.02423  -0.01533 -0.00230 327 PHE A CE1 
2445 C CE2 . PHE A 327 ? 0.32719 0.25050 0.26657 0.02005  -0.02565 -0.00736 327 PHE A CE2 
2446 C CZ  . PHE A 327 ? 0.33370 0.26457 0.27308 0.02224  -0.02038 -0.00479 327 PHE A CZ  
2447 N N   . ASP A 328 ? 0.32780 0.27461 0.31110 0.02667  -0.01499 0.00992  328 ASP A N   
2448 C CA  . ASP A 328 ? 0.31347 0.27284 0.30155 0.02932  -0.01165 0.01203  328 ASP A CA  
2449 C C   . ASP A 328 ? 0.29994 0.26111 0.28497 0.03352  -0.00745 0.00774  328 ASP A C   
2450 O O   . ASP A 328 ? 0.28023 0.23323 0.25845 0.03480  -0.00651 0.00328  328 ASP A O   
2451 C CB  . ASP A 328 ? 0.24879 0.21108 0.24295 0.03101  -0.01182 0.01697  328 ASP A CB  
2452 C CG  . ASP A 328 ? 0.26724 0.22784 0.26417 0.02588  -0.01465 0.02150  328 ASP A CG  
2453 O OD1 . ASP A 328 ? 0.31030 0.27775 0.30920 0.02205  -0.01556 0.02204  328 ASP A OD1 
2454 O OD2 . ASP A 328 ? 0.28313 0.23525 0.28040 0.02566  -0.01581 0.02450  328 ASP A OD2 
2455 N N   . GLY A 329 ? 0.29918 0.27207 0.28945 0.03532  -0.00465 0.00872  329 GLY A N   
2456 C CA  . GLY A 329 ? 0.31833 0.29638 0.30720 0.03674  -0.00006 0.00494  329 GLY A CA  
2457 C C   . GLY A 329 ? 0.32290 0.30083 0.31323 0.04230  0.00295  0.00147  329 GLY A C   
2458 O O   . GLY A 329 ? 0.26199 0.24161 0.24924 0.04298  0.00747  -0.00259 329 GLY A O   
2459 N N   . ILE A 330 ? 0.24925 0.22527 0.24405 0.04670  0.00085  0.00317  330 ILE A N   
2460 C CA  . ILE A 330 ? 0.25288 0.22907 0.25019 0.05379  0.00320  -0.00036 330 ILE A CA  
2461 C C   . ILE A 330 ? 0.30390 0.26698 0.29223 0.05489  0.00467  -0.00548 330 ILE A C   
2462 O O   . ILE A 330 ? 0.27781 0.24412 0.26540 0.05867  0.00952  -0.01067 330 ILE A O   
2463 C CB  . ILE A 330 ? 0.27926 0.25288 0.28138 0.05904  -0.00045 0.00349  330 ILE A CB  
2464 C CG1 . ILE A 330 ? 0.34420 0.33152 0.35330 0.05845  -0.00216 0.00826  330 ILE A CG1 
2465 C CG2 . ILE A 330 ? 0.34148 0.31295 0.34588 0.06799  0.00121  -0.00053 330 ILE A CG2 
2466 C CD1 . ILE A 330 ? 0.42640 0.43123 0.44216 0.05858  0.00118  0.00517  330 ILE A CD1 
2467 N N   . VAL A 331 ? 0.25633 0.20514 0.23799 0.05158  0.00056  -0.00455 331 VAL A N   
2468 C CA  . VAL A 331 ? 0.28948 0.22460 0.26095 0.05202  0.00082  -0.01017 331 VAL A CA  
2469 C C   . VAL A 331 ? 0.30825 0.24714 0.27188 0.04878  0.00442  -0.01345 331 VAL A C   
2470 O O   . VAL A 331 ? 0.36371 0.29883 0.31990 0.05163  0.00839  -0.01924 331 VAL A O   
2471 C CB  . VAL A 331 ? 0.37891 0.29940 0.34629 0.04750  -0.00530 -0.00847 331 VAL A CB  
2472 C CG1 . VAL A 331 ? 0.36535 0.27407 0.32048 0.04536  -0.00625 -0.01463 331 VAL A CG1 
2473 C CG2 . VAL A 331 ? 0.38475 0.29490 0.35571 0.05174  -0.00765 -0.00663 331 VAL A CG2 
2474 N N   . LEU A 332 ? 0.25167 0.19742 0.21594 0.04319  0.00340  -0.00965 332 LEU A N   
2475 C CA  . LEU A 332 ? 0.29814 0.24522 0.25352 0.04008  0.00637  -0.01137 332 LEU A CA  
2476 C C   . LEU A 332 ? 0.34384 0.30033 0.30081 0.04282  0.01424  -0.01424 332 LEU A C   
2477 O O   . LEU A 332 ? 0.36458 0.31772 0.31130 0.04289  0.01860  -0.01808 332 LEU A O   
2478 C CB  . LEU A 332 ? 0.23741 0.18937 0.19444 0.03482  0.00349  -0.00644 332 LEU A CB  
2479 C CG  . LEU A 332 ? 0.31286 0.26421 0.26023 0.03149  0.00529  -0.00630 332 LEU A CG  
2480 C CD1 . LEU A 332 ? 0.36185 0.32279 0.31218 0.03132  0.01252  -0.00643 332 LEU A CD1 
2481 C CD2 . LEU A 332 ? 0.35073 0.29062 0.28315 0.03163  0.00478  -0.01031 332 LEU A CD2 
2482 N N   . VAL A 333 ? 0.28691 0.25611 0.25669 0.04501  0.01624  -0.01267 333 VAL A N   
2483 C CA  . VAL A 333 ? 0.27351 0.25489 0.24801 0.04683  0.02366  -0.01569 333 VAL A CA  
2484 C C   . VAL A 333 ? 0.31415 0.29305 0.28708 0.05374  0.02749  -0.02165 333 VAL A C   
2485 O O   . VAL A 333 ? 0.31323 0.29798 0.28364 0.05431  0.03492  -0.02565 333 VAL A O   
2486 C CB  . VAL A 333 ? 0.28807 0.28485 0.27754 0.04728  0.02325  -0.01305 333 VAL A CB  
2487 C CG1 . VAL A 333 ? 0.36194 0.37326 0.36102 0.05149  0.02945  -0.01723 333 VAL A CG1 
2488 C CG2 . VAL A 333 ? 0.35775 0.35825 0.34676 0.04008  0.02275  -0.00946 333 VAL A CG2 
2489 N N   . GLN A 334 ? 0.30412 0.27398 0.27836 0.05918  0.02305  -0.02244 334 GLN A N   
2490 C CA  . GLN A 334 ? 0.35094 0.31462 0.32143 0.06643  0.02620  -0.02899 334 GLN A CA  
2491 C C   . GLN A 334 ? 0.37573 0.32975 0.32966 0.06379  0.02947  -0.03354 334 GLN A C   
2492 O O   . GLN A 334 ? 0.33805 0.29568 0.28834 0.06754  0.03671  -0.03932 334 GLN A O   
2493 C CB  . GLN A 334 ? 0.40963 0.35881 0.38049 0.07127  0.01984  -0.02865 334 GLN A CB  
2494 C CG  . GLN A 334 ? 0.41891 0.37544 0.40344 0.07647  0.01704  -0.02473 334 GLN A CG  
2495 C CD  . GLN A 334 ? 0.65767 0.62860 0.65211 0.08493  0.02242  -0.02898 334 GLN A CD  
2496 O OE1 . GLN A 334 ? 0.62915 0.59377 0.62160 0.09288  0.02471  -0.03481 334 GLN A OE1 
2497 N NE2 . GLN A 334 ? 0.55963 0.55076 0.56552 0.08342  0.02439  -0.02675 334 GLN A NE2 
2498 N N   . CYS A 335 ? 0.34471 0.28681 0.28823 0.05784  0.02395  -0.03124 335 CYS A N   
2499 C CA  . CYS A 335 ? 0.39994 0.33270 0.32583 0.05500  0.02541  -0.03482 335 CYS A CA  
2500 C C   . CYS A 335 ? 0.34100 0.28444 0.26270 0.05201  0.03356  -0.03448 335 CYS A C   
2501 O O   . CYS A 335 ? 0.38591 0.32815 0.29717 0.05404  0.04020  -0.03968 335 CYS A O   
2502 C CB  . CYS A 335 ? 0.37464 0.29700 0.29352 0.04882  0.01683  -0.03133 335 CYS A CB  
2503 S SG  . CYS A 335 ? 0.46768 0.37958 0.36316 0.04526  0.01674  -0.03475 335 CYS A SG  
2504 N N   . THR A 336 ? 0.35559 0.30874 0.28452 0.04687  0.03360  -0.02849 336 THR A N   
2505 C CA  . THR A 336 ? 0.34478 0.30428 0.26766 0.04236  0.04094  -0.02736 336 THR A CA  
2506 C C   . THR A 336 ? 0.39029 0.36401 0.32109 0.04539  0.05105  -0.03134 336 THR A C   
2507 O O   . THR A 336 ? 0.42258 0.39823 0.34370 0.04314  0.05927  -0.03307 336 THR A O   
2508 C CB  . THR A 336 ? 0.33823 0.30273 0.26688 0.03621  0.03848  -0.02067 336 THR A CB  
2509 O OG1 . THR A 336 ? 0.45722 0.43426 0.40469 0.03767  0.03747  -0.01918 336 THR A OG1 
2510 C CG2 . THR A 336 ? 0.50985 0.46245 0.43083 0.03360  0.02931  -0.01711 336 THR A CG2 
2511 N N   . GLU A 337 ? 0.38386 0.36864 0.33227 0.05051  0.05080  -0.03263 337 GLU A N   
2512 C CA  . GLU A 337 ? 0.36353 0.36435 0.32148 0.05429  0.06008  -0.03726 337 GLU A CA  
2513 C C   . GLU A 337 ? 0.38926 0.38358 0.33634 0.06058  0.06518  -0.04460 337 GLU A C   
2514 O O   . GLU A 337 ? 0.39551 0.40030 0.34189 0.06113  0.07549  -0.04856 337 GLU A O   
2515 C CB  . GLU A 337 ? 0.37613 0.39064 0.35522 0.05960  0.05716  -0.03702 337 GLU A CB  
2516 C CG  . GLU A 337 ? 0.44640 0.46959 0.43488 0.05280  0.05396  -0.03107 337 GLU A CG  
2517 C CD  . GLU A 337 ? 0.70226 0.74345 0.71106 0.05686  0.05258  -0.03131 337 GLU A CD  
2518 O OE1 . GLU A 337 ? 0.65679 0.69600 0.67128 0.06527  0.04763  -0.03218 337 GLU A OE1 
2519 O OE2 . GLU A 337 ? 0.51954 0.57607 0.53792 0.05137  0.05614  -0.03056 337 GLU A OE2 
2520 N N   . HIS A 338 ? 0.44156 0.41879 0.38007 0.06510  0.05856  -0.04698 338 HIS A N   
2521 C CA  . HIS A 338 ? 0.40852 0.37698 0.33432 0.07110  0.06287  -0.05502 338 HIS A CA  
2522 C C   . HIS A 338 ? 0.43666 0.39956 0.34158 0.06533  0.06831  -0.05579 338 HIS A C   
2523 O O   . HIS A 338 ? 0.47945 0.44696 0.37719 0.06815  0.07806  -0.06151 338 HIS A O   
2524 C CB  . HIS A 338 ? 0.40493 0.35360 0.32507 0.07543  0.05356  -0.05732 338 HIS A CB  
2525 C CG  . HIS A 338 ? 0.49116 0.42869 0.39841 0.08245  0.05698  -0.06684 338 HIS A CG  
2526 N ND1 . HIS A 338 ? 0.68116 0.60778 0.56625 0.07941  0.05893  -0.07063 338 HIS A ND1 
2527 C CD2 . HIS A 338 ? 0.59956 0.53396 0.51193 0.09296  0.05828  -0.07366 338 HIS A CD2 
2528 C CE1 . HIS A 338 ? 0.46958 0.38745 0.34646 0.08736  0.06182  -0.08004 338 HIS A CE1 
2529 N NE2 . HIS A 338 ? 0.69325 0.61509 0.58681 0.09591  0.06155  -0.08214 338 HIS A NE2 
2530 N N   . LEU A 339 ? 0.41640 0.36948 0.31079 0.05773  0.06210  -0.04994 339 LEU A N   
2531 C CA  . LEU A 339 ? 0.44723 0.39437 0.32079 0.05215  0.06610  -0.04883 339 LEU A CA  
2532 C C   . LEU A 339 ? 0.42640 0.38920 0.30265 0.04886  0.07875  -0.04777 339 LEU A C   
2533 O O   . LEU A 339 ? 0.48222 0.44465 0.34385 0.04930  0.08770  -0.05162 339 LEU A O   
2534 C CB  . LEU A 339 ? 0.49220 0.43049 0.35987 0.04519  0.05697  -0.04127 339 LEU A CB  
2535 C CG  . LEU A 339 ? 0.53830 0.46170 0.40123 0.04601  0.04462  -0.04176 339 LEU A CG  
2536 C CD1 . LEU A 339 ? 0.45634 0.37520 0.31441 0.03955  0.03741  -0.03441 339 LEU A CD1 
2537 C CD2 . LEU A 339 ? 0.58402 0.49393 0.42767 0.04946  0.04410  -0.04940 339 LEU A CD2 
2538 N N   A LEU A 340 ? 0.44453 0.42132 0.33903 0.04490  0.07986  -0.04271 340 LEU A N   
2539 N N   B LEU A 340 ? 0.44473 0.42167 0.33941 0.04499  0.07992  -0.04280 340 LEU A N   
2540 C CA  A LEU A 340 ? 0.44676 0.43813 0.34491 0.03946  0.09145  -0.04116 340 LEU A CA  
2541 C CA  B LEU A 340 ? 0.44722 0.43854 0.34526 0.03944  0.09147  -0.04116 340 LEU A CA  
2542 C C   A LEU A 340 ? 0.49816 0.50527 0.40512 0.04547  0.10223  -0.04872 340 LEU A C   
2543 C C   B LEU A 340 ? 0.49779 0.50526 0.40517 0.04537  0.10228  -0.04864 340 LEU A C   
2544 O O   A LEU A 340 ? 0.47833 0.49200 0.37737 0.04232  0.11401  -0.05014 340 LEU A O   
2545 O O   B LEU A 340 ? 0.47800 0.49265 0.37825 0.04204  0.11414  -0.04992 340 LEU A O   
2546 C CB  A LEU A 340 ? 0.45672 0.45903 0.37342 0.03377  0.08894  -0.03526 340 LEU A CB  
2547 C CB  B LEU A 340 ? 0.45781 0.45955 0.37374 0.03349  0.08891  -0.03506 340 LEU A CB  
2548 C CG  A LEU A 340 ? 0.51232 0.50106 0.41942 0.02698  0.08132  -0.02766 340 LEU A CG  
2549 C CG  B LEU A 340 ? 0.51177 0.50233 0.41625 0.02471  0.08545  -0.02721 340 LEU A CG  
2550 C CD1 A LEU A 340 ? 0.55479 0.55470 0.48008 0.02209  0.07987  -0.02355 340 LEU A CD1 
2551 C CD1 B LEU A 340 ? 0.45154 0.42145 0.33694 0.02625  0.07604  -0.02567 340 LEU A CD1 
2552 C CD2 A LEU A 340 ? 0.48688 0.46516 0.37105 0.02110  0.08710  -0.02463 340 LEU A CD2 
2553 C CD2 B LEU A 340 ? 0.55458 0.55299 0.47754 0.02140  0.08015  -0.02310 340 LEU A CD2 
2554 N N   . LYS A 341 ? 0.48960 0.50308 0.41282 0.05446  0.09868  -0.05344 341 LYS A N   
2555 C CA  . LYS A 341 ? 0.47272 0.50235 0.40648 0.06210  0.10820  -0.06119 341 LYS A CA  
2556 C C   . LYS A 341 ? 0.52767 0.54753 0.44008 0.06633  0.11505  -0.06802 341 LYS A C   
2557 O O   . LYS A 341 ? 0.59803 0.63242 0.51243 0.06862  0.12759  -0.07328 341 LYS A O   
2558 C CB  . LYS A 341 ? 0.61448 0.64860 0.56724 0.07232  0.10112  -0.06424 341 LYS A CB  
2559 C CG  . LYS A 341 ? 0.55954 0.60939 0.52426 0.08315  0.10939  -0.07305 341 LYS A CG  
2560 C CD  . LYS A 341 ? 0.76747 0.82255 0.75259 0.09277  0.10114  -0.07380 341 LYS A CD  
2561 C CE  . LYS A 341 ? 0.78513 0.85158 0.78064 0.10628  0.10719  -0.08302 341 LYS A CE  
2562 N NZ  . LYS A 341 ? 0.73914 0.80980 0.75367 0.11606  0.09831  -0.08246 341 LYS A NZ  
2563 N N   . HIS A 342 ? 0.54806 0.54458 0.43992 0.06712  0.10727  -0.06851 342 HIS A N   
2564 C CA  . HIS A 342 ? 0.64634 0.63266 0.51675 0.07188  0.11269  -0.07627 342 HIS A CA  
2565 C C   . HIS A 342 ? 0.62261 0.60289 0.46844 0.06346  0.11894  -0.07294 342 HIS A C   
2566 O O   . HIS A 342 ? 0.64910 0.62295 0.47478 0.06664  0.12525  -0.07924 342 HIS A O   
2567 C CB  . HIS A 342 ? 0.87985 0.84419 0.74101 0.07794  0.10097  -0.08049 342 HIS A CB  
2568 C CG  . HIS A 342 ? 0.95238 0.91999 0.83309 0.08829  0.09748  -0.08527 342 HIS A CG  
2569 N ND1 . HIS A 342 ? 0.81760 0.79571 0.72205 0.08846  0.09219  -0.07978 342 HIS A ND1 
2570 C CD2 . HIS A 342 ? 0.94278 0.90380 0.82182 0.09943  0.09859  -0.09497 342 HIS A CD2 
2571 C CE1 . HIS A 342 ? 0.94431 0.92184 0.86040 0.09931  0.08982  -0.08503 342 HIS A CE1 
2572 N NE2 . HIS A 342 ? 1.13591 1.10257 1.03746 0.10628  0.09364  -0.09435 342 HIS A NE2 
2573 N N   . MET A 343 ? 0.53989 0.52152 0.38608 0.05325  0.11756  -0.06326 343 MET A N   
2574 C CA  . MET A 343 ? 0.73977 0.71955 0.56607 0.04514  0.12649  -0.05897 343 MET A CA  
2575 C C   . MET A 343 ? 0.77544 0.77714 0.61081 0.04408  0.14336  -0.06183 343 MET A C   
2576 O O   . MET A 343 ? 0.89426 0.89480 0.70966 0.04106  0.15425  -0.06239 343 MET A O   
2577 C CB  . MET A 343 ? 0.60030 0.57460 0.42631 0.03518  0.12044  -0.04788 343 MET A CB  
2578 C CG  . MET A 343 ? 0.59202 0.54572 0.40581 0.03524  0.10518  -0.04457 343 MET A CG  
2579 S SD  . MET A 343 ? 0.63944 0.58842 0.45634 0.02574  0.09819  -0.03256 343 MET A SD  
2580 C CE  . MET A 343 ? 0.62496 0.57055 0.41924 0.01742  0.11053  -0.02687 343 MET A CE  
2581 N N   . THR A 344 ? 0.92949 0.95221 0.79489 0.04648  0.14561  -0.06360 344 THR A N   
2582 C CA  . THR A 344 ? 1.14247 1.19047 1.02198 0.04582  0.16111  -0.06720 344 THR A CA  
2583 C C   . THR A 344 ? 1.02035 1.07168 0.89047 0.05563  0.17062  -0.07783 344 THR A C   
2584 O O   . THR A 344 ? 1.12829 1.19603 0.99823 0.05341  0.18618  -0.08045 344 THR A O   
2585 C CB  . THR A 344 ? 1.04724 1.11718 0.96186 0.04805  0.15853  -0.06779 344 THR A CB  
2586 O OG1 . THR A 344 ? 0.99954 1.06859 0.92432 0.06153  0.15143  -0.07495 344 THR A OG1 
2587 C CG2 . THR A 344 ? 0.72797 0.79235 0.65031 0.03982  0.14771  -0.05859 344 THR A CG2 
2588 N N   . GLN A 345 ? 0.97235 1.00834 0.83473 0.06616  0.16203  -0.08433 345 GLN A N   
2589 C CA  . GLN A 345 ? 0.94087 0.97666 0.79263 0.07659  0.16992  -0.09563 345 GLN A CA  
2590 C C   . GLN A 345 ? 1.08871 1.10187 0.90296 0.07420  0.17036  -0.09649 345 GLN A C   
2591 O O   . GLN A 345 ? 0.96659 0.97356 0.76390 0.06344  0.17236  -0.08822 345 GLN A O   
2592 C CB  . GLN A 345 ? 0.82861 0.85924 0.69348 0.09004  0.16051  -0.10321 345 GLN A CB  
2593 N N   . LEU A 356 ? 0.93946 0.70448 0.28709 0.04882  -0.02457 -0.08346 359 LEU A N   
2594 C CA  . LEU A 356 ? 1.02417 0.79123 0.39561 0.04742  -0.02412 -0.07360 359 LEU A CA  
2595 C C   . LEU A 356 ? 1.05340 0.81852 0.42462 0.04713  -0.03877 -0.06171 359 LEU A C   
2596 O O   . LEU A 356 ? 1.00659 0.76968 0.36485 0.04688  -0.03480 -0.04922 359 LEU A O   
2597 C CB  . LEU A 356 ? 1.14437 0.91534 0.51793 0.04616  -0.00366 -0.06594 359 LEU A CB  
2598 C CG  . LEU A 356 ? 1.11036 0.88547 0.51222 0.04503  0.00293  -0.06337 359 LEU A CG  
2599 C CD1 . LEU A 356 ? 1.15015 0.92587 0.56997 0.04678  -0.00110 -0.07733 359 LEU A CD1 
2600 C CD2 . LEU A 356 ? 1.10134 0.88261 0.50408 0.04331  0.02411  -0.05825 359 LEU A CD2 
2601 N N   . PRO A 357 ? 1.08874 0.85482 0.47561 0.04718  -0.05558 -0.06562 360 PRO A N   
2602 C CA  . PRO A 357 ? 0.90240 0.66896 0.29095 0.04793  -0.07065 -0.05596 360 PRO A CA  
2603 C C   . PRO A 357 ? 0.99086 0.75829 0.39558 0.04746  -0.06605 -0.04296 360 PRO A C   
2604 O O   . PRO A 357 ? 0.87768 0.64660 0.29725 0.04592  -0.05435 -0.04295 360 PRO A O   
2605 C CB  . PRO A 357 ? 1.21913 0.98939 0.62391 0.04725  -0.08819 -0.06612 360 PRO A CB  
2606 C CG  . PRO A 357 ? 1.21253 0.98154 0.62447 0.04580  -0.08144 -0.08057 360 PRO A CG  
2607 C CD  . PRO A 357 ? 1.18847 0.95603 0.59629 0.04632  -0.06048 -0.07793 360 PRO A CD  
2608 N N   . ALA A 358 ? 0.88506 0.65156 0.28692 0.04914  -0.07564 -0.03210 361 ALA A N   
2609 C CA  . ALA A 358 ? 0.85839 0.62396 0.27282 0.04894  -0.07111 -0.01932 361 ALA A CA  
2610 C C   . ALA A 358 ? 0.82373 0.59575 0.26848 0.04869  -0.07992 -0.02147 361 ALA A C   
2611 O O   . ALA A 358 ? 0.79941 0.57685 0.25400 0.04928  -0.09489 -0.02883 361 ALA A O   
2612 C CB  . ALA A 358 ? 0.88320 0.64404 0.28380 0.05167  -0.07791 -0.00685 361 ALA A CB  
2613 N N   . PRO A 359 ? 0.81880 0.59117 0.27921 0.04727  -0.07082 -0.01535 362 PRO A N   
2614 C CA  . PRO A 359 ? 0.70618 0.48507 0.19438 0.04729  -0.07954 -0.01597 362 PRO A CA  
2615 C C   . PRO A 359 ? 0.81171 0.59393 0.30565 0.05064  -0.09612 -0.00976 362 PRO A C   
2616 O O   . PRO A 359 ? 0.79501 0.57201 0.27429 0.05316  -0.09718 -0.00046 362 PRO A O   
2617 C CB  . PRO A 359 ? 0.75278 0.53018 0.25122 0.04535  -0.06502 -0.00860 362 PRO A CB  
2618 C CG  . PRO A 359 ? 0.76431 0.53724 0.24498 0.04315  -0.04713 -0.00946 362 PRO A CG  
2619 C CD  . PRO A 359 ? 0.81397 0.58225 0.26855 0.04486  -0.05155 -0.00881 362 PRO A CD  
2620 N N   . ARG A 360 ? 0.70611 0.49771 0.22259 0.05071  -0.10899 -0.01500 363 ARG A N   
2621 C CA  . ARG A 360 ? 0.76115 0.56003 0.28693 0.05415  -0.12565 -0.01146 363 ARG A CA  
2622 C C   . ARG A 360 ? 0.79748 0.60028 0.34467 0.05600  -0.12609 -0.00259 363 ARG A C   
2623 O O   . ARG A 360 ? 0.74039 0.54829 0.30800 0.05359  -0.12346 -0.00544 363 ARG A O   
2624 C CB  . ARG A 360 ? 0.77937 0.58882 0.31867 0.05232  -0.14002 -0.02318 363 ARG A CB  
2625 C CG  . ARG A 360 ? 0.92795 0.73368 0.44706 0.05066  -0.14173 -0.03306 363 ARG A CG  
2626 C CD  . ARG A 360 ? 0.98739 0.80113 0.52397 0.04647  -0.15154 -0.04594 363 ARG A CD  
2627 N NE  . ARG A 360 ? 0.95550 0.76447 0.49864 0.04272  -0.14063 -0.05302 363 ARG A NE  
2628 C CZ  . ARG A 360 ? 0.85798 0.67237 0.42411 0.03859  -0.14553 -0.06075 363 ARG A CZ  
2629 N NH1 . ARG A 360 ? 1.19445 1.02131 0.78236 0.03695  -0.16006 -0.06163 363 ARG A NH1 
2630 N NH2 . ARG A 360 ? 0.98113 0.78873 0.54923 0.03600  -0.13533 -0.06781 363 ARG A NH2 
2631 N N   . ARG A 361 ? 0.67401 0.47399 0.21632 0.06056  -0.12966 0.00784  364 ARG A N   
2632 C CA  . ARG A 361 ? 0.78221 0.58682 0.34610 0.06349  -0.13247 0.01523  364 ARG A CA  
2633 C C   . ARG A 361 ? 0.67771 0.49963 0.26808 0.06449  -0.14764 0.00890  364 ARG A C   
2634 O O   . ARG A 361 ? 0.65650 0.48564 0.24493 0.06570  -0.16007 0.00399  364 ARG A O   
2635 C CB  . ARG A 361 ? 0.76102 0.55742 0.31300 0.06883  -0.13395 0.02687  364 ARG A CB  
2636 C CG  . ARG A 361 ? 0.75957 0.55631 0.33065 0.07180  -0.13254 0.03505  364 ARG A CG  
2637 C CD  . ARG A 361 ? 0.76963 0.55952 0.33234 0.07834  -0.13801 0.04485  364 ARG A CD  
2638 N NE  . ARG A 361 ? 0.77738 0.54987 0.30998 0.07712  -0.12876 0.05163  364 ARG A NE  
2639 C CZ  . ARG A 361 ? 0.82574 0.58399 0.35098 0.07580  -0.11701 0.06093  364 ARG A CZ  
2640 N NH1 . ARG A 361 ? 0.71333 0.47142 0.25805 0.07611  -0.11331 0.06455  364 ARG A NH1 
2641 N NH2 . ARG A 361 ? 0.76047 0.50456 0.25836 0.07355  -0.10846 0.06647  364 ARG A NH2 
2642 N N   . LEU A 362 ? 0.60383 0.43351 0.21941 0.06341  -0.14643 0.00876  365 LEU A N   
2643 C CA  . LEU A 362 ? 0.63747 0.48550 0.28121 0.06432  -0.15980 0.00449  365 LEU A CA  
2644 C C   . LEU A 362 ? 0.72666 0.57974 0.37692 0.07169  -0.16800 0.01233  365 LEU A C   
2645 O O   . LEU A 362 ? 0.69141 0.53683 0.34115 0.07539  -0.16153 0.02146  365 LEU A O   
2646 C CB  . LEU A 362 ? 0.57132 0.42643 0.23948 0.06116  -0.15548 0.00261  365 LEU A CB  
2647 C CG  . LEU A 362 ? 0.61816 0.47177 0.28806 0.05359  -0.14750 -0.00635 365 LEU A CG  
2648 C CD1 . LEU A 362 ? 0.66285 0.52807 0.36736 0.04924  -0.13859 -0.00665 365 LEU A CD1 
2649 C CD2 . LEU A 362 ? 0.72177 0.58082 0.38920 0.05069  -0.16047 -0.01732 365 LEU A CD2 
2650 N N   . ARG A 363 ? 0.61886 0.48463 0.27571 0.07378  -0.18208 0.00842  366 ARG A N   
2651 C CA  . ARG A 363 ? 0.72868 0.60030 0.39179 0.08169  -0.19056 0.01511  366 ARG A CA  
2652 C C   . ARG A 363 ? 0.64295 0.53482 0.34200 0.08339  -0.19649 0.01373  366 ARG A C   
2653 O O   . ARG A 363 ? 0.64765 0.55238 0.36691 0.07762  -0.19801 0.00618  366 ARG A O   
2654 C CB  . ARG A 363 ? 0.68158 0.55667 0.33072 0.08391  -0.20256 0.01246  366 ARG A CB  
2655 C CG  . ARG A 363 ? 1.02159 0.87582 0.63442 0.08593  -0.19668 0.01867  366 ARG A CG  
2656 C CD  . ARG A 363 ? 1.15889 1.01362 0.75221 0.08408  -0.20434 0.01210  366 ARG A CD  
2657 N NE  . ARG A 363 ? 1.32802 1.20392 0.94269 0.08257  -0.21880 0.00305  366 ARG A NE  
2658 C CZ  . ARG A 363 ? 1.24664 1.12828 0.86307 0.07546  -0.22186 -0.00837 366 ARG A CZ  
2659 N NH1 . ARG A 363 ? 1.27669 1.14460 0.87379 0.07031  -0.21185 -0.01272 366 ARG A NH1 
2660 N NH2 . ARG A 363 ? 1.12436 1.02611 0.76292 0.07330  -0.23500 -0.01588 366 ARG A NH2 
2661 N N   . TRP A 364 ? 0.66598 0.56010 0.37286 0.09137  -0.19918 0.02116  367 TRP A N   
2662 C CA  . TRP A 364 ? 0.58639 0.50051 0.32696 0.09442  -0.20387 0.02039  367 TRP A CA  
2663 C C   . TRP A 364 ? 0.79586 0.71998 0.54209 0.10309  -0.21544 0.02339  367 TRP A C   
2664 O O   . TRP A 364 ? 0.64673 0.55607 0.37059 0.10885  -0.21625 0.03016  367 TRP A O   
2665 C CB  . TRP A 364 ? 0.60932 0.51618 0.35856 0.09646  -0.19272 0.02637  367 TRP A CB  
2666 C CG  . TRP A 364 ? 0.65657 0.55311 0.40001 0.08898  -0.18080 0.02473  367 TRP A CG  
2667 C CD1 . TRP A 364 ? 0.65157 0.52584 0.37122 0.08725  -0.16883 0.03003  367 TRP A CD1 
2668 C CD2 . TRP A 364 ? 0.65368 0.56232 0.41612 0.08207  -0.17956 0.01747  367 TRP A CD2 
2669 N NE1 . TRP A 364 ? 0.66157 0.53414 0.38430 0.08032  -0.16028 0.02627  367 TRP A NE1 
2670 C CE2 . TRP A 364 ? 0.60142 0.49384 0.34951 0.07731  -0.16704 0.01869  367 TRP A CE2 
2671 C CE3 . TRP A 364 ? 0.51331 0.44514 0.30387 0.07893  -0.18757 0.01022  367 TRP A CE3 
2672 C CZ2 . TRP A 364 ? 0.57458 0.47475 0.34043 0.06880  -0.15903 0.01273  367 TRP A CZ2 
2673 C CZ3 . TRP A 364 ? 0.57686 0.51354 0.38080 0.07082  -0.18207 0.00485  367 TRP A CZ3 
2674 C CH2 . TRP A 364 ? 0.55213 0.47351 0.34569 0.06544  -0.16605 0.00617  367 TRP A CH2 
2675 N N   . LYS A 365 ? 0.62197 0.57171 0.39884 0.10388  -0.22398 0.01855  368 LYS A N   
2676 C CA  . LYS A 365 ? 0.69584 0.65948 0.48444 0.11273  -0.23470 0.02089  368 LYS A CA  
2677 C C   . LYS A 365 ? 0.80043 0.77591 0.61749 0.11762  -0.23101 0.02311  368 LYS A C   
2678 O O   . LYS A 365 ? 0.76964 0.76687 0.61555 0.11331  -0.23166 0.01723  368 LYS A O   
2679 C CB  . LYS A 365 ? 0.68151 0.66756 0.48204 0.10931  -0.24803 0.01279  368 LYS A CB  
2680 C CG  . LYS A 365 ? 0.92549 0.89953 0.69609 0.10555  -0.25255 0.01012  368 LYS A CG  
2681 C CD  . LYS A 365 ? 0.97724 0.92477 0.71393 0.11220  -0.24828 0.01956  368 LYS A CD  
2682 C CE  . LYS A 365 ? 0.98832 0.92780 0.69632 0.11138  -0.25523 0.01803  368 LYS A CE  
2683 N NZ  . LYS A 365 ? 1.01877 0.94158 0.70313 0.12089  -0.25639 0.02837  368 LYS A NZ  
2684 N N   . CYS A 366 ? 0.68126 0.64171 0.48968 0.12620  -0.22664 0.03141  369 CYS A N   
2685 C CA  . CYS A 366 ? 0.87413 0.84168 0.70547 0.13187  -0.22205 0.03364  369 CYS A CA  
2686 C C   . CYS A 366 ? 0.82888 0.81266 0.67606 0.14217  -0.23231 0.03468  369 CYS A C   
2687 O O   . CYS A 366 ? 0.78058 0.76568 0.61691 0.14604  -0.24269 0.03561  369 CYS A O   
2688 C CB  . CYS A 366 ? 0.96633 0.90608 0.77940 0.13448  -0.21040 0.04139  369 CYS A CB  
2689 S SG  . CYS A 366 ? 0.99330 0.91447 0.78741 0.12295  -0.19779 0.04071  369 CYS A SG  
2690 N N   . SER A 367 ? 0.82801 0.82482 0.70115 0.14682  -0.22920 0.03426  370 SER A N   
2691 C CA  . SER A 367 ? 0.83831 0.85261 0.73087 0.15720  -0.23712 0.03465  370 SER A CA  
2692 C C   . SER A 367 ? 0.94676 0.94916 0.84303 0.16545  -0.22896 0.03940  370 SER A C   
2693 O O   . SER A 367 ? 0.79271 0.77642 0.67917 0.16179  -0.21767 0.04169  370 SER A O   
2694 C CB  . SER A 367 ? 0.87742 0.92841 0.80529 0.15312  -0.24225 0.02653  370 SER A CB  
2695 O OG  . SER A 367 ? 0.82357 0.88367 0.77082 0.14652  -0.23235 0.02287  370 SER A OG  
2696 N N   . PRO A 368 ? 0.91568 0.92717 0.82476 0.17693  -0.23464 0.04091  371 PRO A N   
2697 C CA  . PRO A 368 ? 0.78413 0.78707 0.70083 0.18461  -0.22677 0.04353  371 PRO A CA  
2698 C C   . PRO A 368 ? 0.58274 0.60000 0.52304 0.17885  -0.21694 0.03830  371 PRO A C   
2699 O O   . PRO A 368 ? 0.78786 0.78954 0.72530 0.18069  -0.20707 0.04039  371 PRO A O   
2700 C CB  . PRO A 368 ? 0.82988 0.84811 0.76182 0.19742  -0.23645 0.04377  371 PRO A CB  
2701 C CG  . PRO A 368 ? 0.83888 0.85762 0.75557 0.19821  -0.24884 0.04547  371 PRO A CG  
2702 C CD  . PRO A 368 ? 0.80299 0.82815 0.71534 0.18438  -0.24859 0.04104  371 PRO A CD  
2703 N N   . GLU A 369 ? 0.64711 0.69337 0.61045 0.17149  -0.21934 0.03155  372 GLU A N   
2704 C CA  . GLU A 369 ? 0.57627 0.63521 0.55964 0.16455  -0.20964 0.02705  372 GLU A CA  
2705 C C   . GLU A 369 ? 0.56565 0.59899 0.52777 0.15703  -0.19975 0.02942  372 GLU A C   
2706 O O   . GLU A 369 ? 0.61365 0.64199 0.58154 0.15672  -0.18966 0.02936  372 GLU A O   
2707 C CB  . GLU A 369 ? 0.66286 0.75313 0.66962 0.15534  -0.21407 0.02017  372 GLU A CB  
2708 C CG  . GLU A 369 ? 0.86732 0.99057 0.90407 0.15986  -0.22110 0.01636  372 GLU A CG  
2709 C CD  . GLU A 369 ? 0.93873 1.08905 0.99509 0.14761  -0.22486 0.00991  372 GLU A CD  
2710 O OE1 . GLU A 369 ? 0.72120 0.87164 0.76686 0.14294  -0.23431 0.00866  372 GLU A OE1 
2711 O OE2 . GLU A 369 ? 0.61296 0.78297 0.69406 0.14196  -0.21794 0.00602  372 GLU A OE2 
2712 N N   . ILE A 370 ? 0.60314 0.62103 0.54072 0.15077  -0.20240 0.03112  373 ILE A N   
2713 C CA  . ILE A 370 ? 0.56240 0.55974 0.48186 0.14239  -0.19310 0.03253  373 ILE A CA  
2714 C C   . ILE A 370 ? 0.58395 0.55224 0.48446 0.14736  -0.18493 0.03920  373 ILE A C   
2715 O O   . ILE A 370 ? 0.48769 0.44510 0.38541 0.14290  -0.17469 0.03976  373 ILE A O   
2716 C CB  . ILE A 370 ? 0.67235 0.66134 0.57005 0.13482  -0.19773 0.03194  373 ILE A CB  
2717 C CG1 . ILE A 370 ? 0.60056 0.61680 0.51858 0.12706  -0.20404 0.02405  373 ILE A CG1 
2718 C CG2 . ILE A 370 ? 0.57601 0.53934 0.44991 0.12797  -0.18752 0.03479  373 ILE A CG2 
2719 C CD1 . ILE A 370 ? 0.52750 0.55714 0.46717 0.11962  -0.19656 0.01950  373 ILE A CD1 
2720 N N   . GLN A 371 ? 0.55419 0.50932 0.44175 0.15639  -0.18953 0.04435  374 GLN A N   
2721 C CA  . GLN A 371 ? 0.65138 0.57823 0.52206 0.16072  -0.18217 0.05064  374 GLN A CA  
2722 C C   . GLN A 371 ? 0.54739 0.47998 0.43871 0.16410  -0.17474 0.04821  374 GLN A C   
2723 O O   . GLN A 371 ? 0.55828 0.47120 0.43999 0.16146  -0.16496 0.05060  374 GLN A O   
2724 C CB  . GLN A 371 ? 0.68074 0.59468 0.53676 0.17063  -0.18976 0.05635  374 GLN A CB  
2725 C CG  . GLN A 371 ? 0.83196 0.71089 0.65389 0.16865  -0.18476 0.06434  374 GLN A CG  
2726 C CD  . GLN A 371 ? 0.86769 0.73890 0.67071 0.15698  -0.18076 0.06442  374 GLN A CD  
2727 O OE1 . GLN A 371 ? 0.98464 0.87150 0.78958 0.15319  -0.18740 0.06037  374 GLN A OE1 
2728 N NE2 . GLN A 371 ? 0.93281 0.77994 0.71775 0.15104  -0.16971 0.06862  374 GLN A NE2 
2729 N N   . GLY A 372 ? 0.54896 0.50936 0.46905 0.16943  -0.17884 0.04306  375 GLY A N   
2730 C CA  . GLY A 372 ? 0.52509 0.49364 0.46543 0.17248  -0.17125 0.03972  375 GLY A CA  
2731 C C   . GLY A 372 ? 0.51266 0.48608 0.45959 0.16234  -0.16227 0.03640  375 GLY A C   
2732 O O   . GLY A 372 ? 0.45479 0.41893 0.40325 0.16262  -0.15320 0.03611  375 GLY A O   
2733 N N   . HIS A 373 ? 0.46097 0.44886 0.41199 0.15341  -0.16506 0.03351  376 HIS A N   
2734 C CA  . HIS A 373 ? 0.42672 0.41794 0.38237 0.14380  -0.15735 0.03081  376 HIS A CA  
2735 C C   . HIS A 373 ? 0.43497 0.39490 0.36369 0.13939  -0.14977 0.03563  376 HIS A C   
2736 O O   . HIS A 373 ? 0.43086 0.38701 0.36253 0.13547  -0.14101 0.03471  376 HIS A O   
2737 C CB  . HIS A 373 ? 0.46925 0.47944 0.43276 0.13504  -0.16293 0.02670  376 HIS A CB  
2738 C CG  . HIS A 373 ? 0.48034 0.52517 0.47628 0.13530  -0.16658 0.02094  376 HIS A CG  
2739 N ND1 . HIS A 373 ? 0.51008 0.57266 0.51534 0.13699  -0.17700 0.01899  376 HIS A ND1 
2740 C CD2 . HIS A 373 ? 0.48955 0.55538 0.51091 0.13350  -0.16062 0.01682  376 HIS A CD2 
2741 C CE1 . HIS A 373 ? 0.47931 0.57254 0.51517 0.13565  -0.17699 0.01404  376 HIS A CE1 
2742 N NE2 . HIS A 373 ? 0.56013 0.65587 0.60594 0.13354  -0.16677 0.01276  376 HIS A NE2 
2743 N N   . LEU A 374 ? 0.47613 0.41436 0.37851 0.13956  -0.15273 0.04085  377 LEU A N   
2744 C CA  . LEU A 374 ? 0.45827 0.36734 0.33457 0.13436  -0.14470 0.04590  377 LEU A CA  
2745 C C   . LEU A 374 ? 0.52895 0.42090 0.40334 0.13881  -0.13709 0.04865  377 LEU A C   
2746 O O   . LEU A 374 ? 0.50467 0.38510 0.37415 0.13327  -0.12786 0.04926  377 LEU A O   
2747 C CB  . LEU A 374 ? 0.46556 0.35714 0.31460 0.13380  -0.14920 0.05093  377 LEU A CB  
2748 C CG  . LEU A 374 ? 0.48351 0.38397 0.32624 0.12677  -0.15416 0.04808  377 LEU A CG  
2749 C CD1 . LEU A 374 ? 0.64170 0.52911 0.46062 0.12941  -0.16067 0.05245  377 LEU A CD1 
2750 C CD2 . LEU A 374 ? 0.45765 0.34901 0.29007 0.11657  -0.14520 0.04750  377 LEU A CD2 
2751 N N   . ALA A 375 ? 0.47751 0.36735 0.35587 0.14887  -0.14114 0.04996  378 ALA A N   
2752 C CA  . ALA A 375 ? 0.50813 0.38100 0.38526 0.15348  -0.13463 0.05149  378 ALA A CA  
2753 C C   . ALA A 375 ? 0.51551 0.40296 0.41434 0.15249  -0.12799 0.04554  378 ALA A C   
2754 O O   . ALA A 375 ? 0.47132 0.34226 0.36429 0.14978  -0.11943 0.04615  378 ALA A O   
2755 C CB  . ALA A 375 ? 0.54490 0.41595 0.42498 0.16552  -0.14128 0.05287  378 ALA A CB  
2756 N N   . SER A 376 ? 0.45397 0.37283 0.37804 0.15410  -0.13157 0.03966  379 SER A N   
2757 C CA  . SER A 376 ? 0.43698 0.37199 0.38165 0.15289  -0.12486 0.03404  379 SER A CA  
2758 C C   . SER A 376 ? 0.40596 0.33620 0.34458 0.14008  -0.11614 0.03387  379 SER A C   
2759 O O   . SER A 376 ? 0.46155 0.38997 0.40575 0.13566  -0.10578 0.03134  379 SER A O   
2760 C CB  . SER A 376 ? 0.47162 0.44270 0.44459 0.15527  -0.12951 0.02835  379 SER A CB  
2761 O OG  . SER A 376 ? 0.60396 0.59196 0.59578 0.15302  -0.12229 0.02327  379 SER A OG  
2762 N N   . SER A 377 ? 0.42599 0.35584 0.35443 0.13150  -0.11798 0.03555  380 SER A N   
2763 C CA  . SER A 377 ? 0.38990 0.31693 0.31458 0.11743  -0.10720 0.03464  380 SER A CA  
2764 C C   . SER A 377 ? 0.41164 0.31020 0.31620 0.11405  -0.09893 0.03876  380 SER A C   
2765 O O   . SER A 377 ? 0.40389 0.30193 0.31184 0.10542  -0.08846 0.03678  380 SER A O   
2766 C CB  . SER A 377 ? 0.40055 0.33232 0.31805 0.11001  -0.11112 0.03471  380 SER A CB  
2767 O OG  . SER A 377 ? 0.51875 0.47824 0.45797 0.11008  -0.11714 0.02997  380 SER A OG  
2768 N N   . ALA A 378 ? 0.39860 0.27331 0.28163 0.12016  -0.10368 0.04481  381 ALA A N   
2769 C CA  . ALA A 378 ? 0.45175 0.29833 0.31584 0.11622  -0.09566 0.04923  381 ALA A CA  
2770 C C   . ALA A 378 ? 0.44773 0.29196 0.32360 0.11825  -0.08923 0.04594  381 ALA A C   
2771 O O   . ALA A 378 ? 0.46924 0.30411 0.34188 0.10936  -0.07909 0.04534  381 ALA A O   
2772 C CB  . ALA A 378 ? 0.52894 0.34945 0.36762 0.12365  -0.10278 0.05716  381 ALA A CB  
2773 N N   . GLU A 379 ? 0.47060 0.32395 0.36028 0.13027  -0.09527 0.04323  382 GLU A N   
2774 C CA  . GLU A 379 ? 0.47737 0.33014 0.37864 0.13377  -0.08983 0.03871  382 GLU A CA  
2775 C C   . GLU A 379 ? 0.46503 0.34009 0.38474 0.12443  -0.08106 0.03225  382 GLU A C   
2776 O O   . GLU A 379 ? 0.45538 0.32265 0.37490 0.11903  -0.07253 0.02986  382 GLU A O   
2777 C CB  . GLU A 379 ? 0.47196 0.33334 0.38502 0.14992  -0.09864 0.03662  382 GLU A CB  
2778 C CG  . GLU A 379 ? 0.69439 0.54908 0.61463 0.15689  -0.09444 0.03211  382 GLU A CG  
2779 C CD  . GLU A 379 ? 0.95377 0.83675 0.89784 0.15379  -0.08785 0.02388  382 GLU A CD  
2780 O OE1 . GLU A 379 ? 0.90962 0.78553 0.85566 0.15323  -0.08077 0.01959  382 GLU A OE1 
2781 O OE2 . GLU A 379 ? 0.97847 0.88998 0.93831 0.15153  -0.08981 0.02177  382 GLU A OE2 
2782 N N   . LYS A 380 ? 0.40563 0.30795 0.34085 0.12208  -0.08335 0.02947  383 LYS A N   
2783 C CA  . LYS A 380 ? 0.32938 0.25122 0.28012 0.11326  -0.07532 0.02457  383 LYS A CA  
2784 C C   . LYS A 380 ? 0.42517 0.33532 0.36438 0.10060  -0.06708 0.02613  383 LYS A C   
2785 O O   . LYS A 380 ? 0.35584 0.27018 0.30153 0.09492  -0.05913 0.02277  383 LYS A O   
2786 C CB  . LYS A 380 ? 0.38897 0.33874 0.35621 0.11167  -0.07949 0.02243  383 LYS A CB  
2787 C CG  . LYS A 380 ? 0.45670 0.42517 0.44088 0.12298  -0.08647 0.01974  383 LYS A CG  
2788 C CD  . LYS A 380 ? 0.58813 0.56252 0.58417 0.12873  -0.08090 0.01512  383 LYS A CD  
2789 C CE  . LYS A 380 ? 0.66377 0.67040 0.68472 0.13322  -0.08277 0.01067  383 LYS A CE  
2790 N NZ  . LYS A 380 ? 0.51000 0.52853 0.53677 0.13863  -0.09403 0.01210  383 LYS A NZ  
2791 N N   . LEU A 381 ? 0.36242 0.25966 0.28480 0.09623  -0.06889 0.03086  384 LEU A N   
2792 C CA  . LEU A 381 ? 0.37351 0.26217 0.28659 0.08469  -0.06046 0.03185  384 LEU A CA  
2793 C C   . LEU A 381 ? 0.34827 0.21670 0.25262 0.08273  -0.05403 0.03262  384 LEU A C   
2794 O O   . LEU A 381 ? 0.40072 0.27046 0.30781 0.07413  -0.04584 0.03037  384 LEU A O   
2795 C CB  . LEU A 381 ? 0.37119 0.25046 0.26695 0.08112  -0.06315 0.03630  384 LEU A CB  
2796 C CG  . LEU A 381 ? 0.40667 0.27762 0.29211 0.07014  -0.05425 0.03736  384 LEU A CG  
2797 C CD1 . LEU A 381 ? 0.38386 0.27484 0.28584 0.06320  -0.04869 0.03233  384 LEU A CD1 
2798 C CD2 . LEU A 381 ? 0.40414 0.26486 0.26986 0.06845  -0.05728 0.04160  384 LEU A CD2 
2799 N N   . GLN A 382 ? 0.37080 0.22032 0.26520 0.09074  -0.05808 0.03554  385 GLN A N   
2800 C CA  . GLN A 382 ? 0.44202 0.26962 0.32758 0.08805  -0.05226 0.03612  385 GLN A CA  
2801 C C   . GLN A 382 ? 0.40709 0.24553 0.30891 0.08774  -0.04750 0.02893  385 GLN A C   
2802 O O   . GLN A 382 ? 0.40376 0.23263 0.30279 0.08022  -0.04053 0.02724  385 GLN A O   
2803 C CB  . GLN A 382 ? 0.49676 0.29913 0.36738 0.09749  -0.05811 0.04105  385 GLN A CB  
2804 C CG  . GLN A 382 ? 0.52080 0.29426 0.37709 0.09193  -0.05181 0.04345  385 GLN A CG  
2805 C CD  . GLN A 382 ? 0.74859 0.51293 0.59085 0.07876  -0.04492 0.04804  385 GLN A CD  
2806 O OE1 . GLN A 382 ? 0.66281 0.43493 0.49954 0.07664  -0.04660 0.05105  385 GLN A OE1 
2807 N NE2 . GLN A 382 ? 0.71231 0.46108 0.54939 0.06970  -0.03696 0.04792  385 GLN A NE2 
2808 N N   . ARG A 383 ? 0.39994 0.25909 0.31864 0.09548  -0.05105 0.02441  386 ARG A N   
2809 C CA  . ARG A 383 ? 0.39451 0.26646 0.32747 0.09480  -0.04594 0.01742  386 ARG A CA  
2810 C C   . ARG A 383 ? 0.33795 0.22209 0.27585 0.08270  -0.03888 0.01556  386 ARG A C   
2811 O O   . ARG A 383 ? 0.34116 0.22504 0.28221 0.07846  -0.03333 0.01126  386 ARG A O   
2812 C CB  . ARG A 383 ? 0.37354 0.26885 0.32398 0.10437  -0.04994 0.01347  386 ARG A CB  
2813 C CG  . ARG A 383 ? 0.43141 0.31849 0.38153 0.11860  -0.05635 0.01308  386 ARG A CG  
2814 C CD  . ARG A 383 ? 0.51870 0.43514 0.48897 0.12641  -0.05961 0.00926  386 ARG A CD  
2815 N NE  . ARG A 383 ? 0.60030 0.51346 0.57304 0.14152  -0.06666 0.00867  386 ARG A NE  
2816 C CZ  . ARG A 383 ? 0.80025 0.73823 0.79042 0.15012  -0.07103 0.00603  386 ARG A CZ  
2817 N NH1 . ARG A 383 ? 0.52179 0.48816 0.52731 0.14407  -0.06944 0.00462  386 ARG A NH1 
2818 N NH2 . ARG A 383 ? 0.86377 0.79799 0.85659 0.16513  -0.07705 0.00477  386 ARG A NH2 
2819 N N   . ILE A 384 ? 0.33027 0.22555 0.26912 0.07764  -0.03957 0.01824  387 ILE A N   
2820 C CA  . ILE A 384 ? 0.36241 0.26828 0.30564 0.06746  -0.03341 0.01678  387 ILE A CA  
2821 C C   . ILE A 384 ? 0.33067 0.21902 0.26198 0.05918  -0.02773 0.01821  387 ILE A C   
2822 O O   . ILE A 384 ? 0.34217 0.23566 0.27853 0.05272  -0.02205 0.01482  387 ILE A O   
2823 C CB  . ILE A 384 ? 0.38217 0.30107 0.32813 0.06490  -0.03598 0.01894  387 ILE A CB  
2824 C CG1 . ILE A 384 ? 0.38810 0.32907 0.35039 0.06989  -0.03958 0.01644  387 ILE A CG1 
2825 C CG2 . ILE A 384 ? 0.36448 0.28799 0.31054 0.05503  -0.02985 0.01851  387 ILE A CG2 
2826 C CD1 . ILE A 384 ? 0.37720 0.32971 0.34283 0.06691  -0.04293 0.01798  387 ILE A CD1 
2827 N N   . VAL A 385 ? 0.36007 0.22867 0.27544 0.05886  -0.02917 0.02342  388 VAL A N   
2828 C CA  . VAL A 385 ? 0.32368 0.17494 0.22737 0.05030  -0.02307 0.02546  388 VAL A CA  
2829 C C   . VAL A 385 ? 0.36873 0.21133 0.27522 0.04892  -0.01976 0.02133  388 VAL A C   
2830 O O   . VAL A 385 ? 0.37925 0.22366 0.28863 0.04002  -0.01365 0.01863  388 VAL A O   
2831 C CB  . VAL A 385 ? 0.40494 0.23394 0.28892 0.05170  -0.02556 0.03259  388 VAL A CB  
2832 C CG1 . VAL A 385 ? 0.45716 0.26684 0.32917 0.04227  -0.01832 0.03510  388 VAL A CG1 
2833 C CG2 . VAL A 385 ? 0.39072 0.22796 0.26984 0.05186  -0.02866 0.03574  388 VAL A CG2 
2834 N N   A LYS A 386 ? 0.34238 0.17517 0.24798 0.05805  -0.02417 0.02030  389 LYS A N   
2835 N N   B LYS A 386 ? 0.34201 0.17515 0.24787 0.05802  -0.02413 0.02020  389 LYS A N   
2836 C CA  A LYS A 386 ? 0.35244 0.17360 0.25878 0.05752  -0.02167 0.01557  389 LYS A CA  
2837 C CA  B LYS A 386 ? 0.35230 0.17342 0.25856 0.05708  -0.02144 0.01558  389 LYS A CA  
2838 C C   A LYS A 386 ? 0.35331 0.19568 0.27506 0.05523  -0.01864 0.00788  389 LYS A C   
2839 C C   B LYS A 386 ? 0.35351 0.19574 0.27534 0.05549  -0.01872 0.00775  389 LYS A C   
2840 O O   A LYS A 386 ? 0.36137 0.19794 0.28370 0.04951  -0.01479 0.00332  389 LYS A O   
2841 O O   B LYS A 386 ? 0.35775 0.19377 0.28026 0.05063  -0.01520 0.00294  389 LYS A O   
2842 C CB  A LYS A 386 ? 0.39720 0.20422 0.29988 0.06998  -0.02751 0.01542  389 LYS A CB  
2843 C CB  B LYS A 386 ? 0.40143 0.20604 0.30251 0.06891  -0.02708 0.01593  389 LYS A CB  
2844 C CG  A LYS A 386 ? 0.52739 0.31069 0.41287 0.07433  -0.03190 0.02357  389 LYS A CG  
2845 C CG  B LYS A 386 ? 0.53742 0.31459 0.41947 0.07035  -0.02970 0.02409  389 LYS A CG  
2846 C CD  A LYS A 386 ? 0.60671 0.37105 0.48790 0.08636  -0.03687 0.02262  389 LYS A CD  
2847 C CD  B LYS A 386 ? 0.60400 0.36794 0.48279 0.08474  -0.03678 0.02446  389 LYS A CD  
2848 C CE  A LYS A 386 ? 0.61273 0.37611 0.49001 0.09945  -0.04591 0.02764  389 LYS A CE  
2849 C CE  B LYS A 386 ? 0.58087 0.31486 0.43870 0.08736  -0.04017 0.03336  389 LYS A CE  
2850 N NZ  A LYS A 386 ? 0.42713 0.22256 0.32283 0.10683  -0.04993 0.02365  389 LYS A NZ  
2851 N NZ  B LYS A 386 ? 0.58165 0.30806 0.43895 0.10383  -0.04866 0.03364  389 LYS A NZ  
2852 N N   . ASN A 387 ? 0.31029 0.17659 0.24390 0.05952  -0.02061 0.00636  390 ASN A N   
2853 C CA  . ASN A 387 ? 0.32745 0.21337 0.27387 0.05905  -0.01820 -0.00011 390 ASN A CA  
2854 C C   . ASN A 387 ? 0.34774 0.24450 0.29783 0.04841  -0.01333 -0.00107 390 ASN A C   
2855 O O   . ASN A 387 ? 0.29478 0.20291 0.25202 0.04651  -0.01106 -0.00646 390 ASN A O   
2856 C CB  . ASN A 387 ? 0.31959 0.22726 0.27726 0.06642  -0.02135 -0.00038 390 ASN A CB  
2857 C CG  . ASN A 387 ? 0.33542 0.25913 0.30353 0.06928  -0.01922 -0.00692 390 ASN A CG  
2858 O OD1 . ASN A 387 ? 0.33190 0.24702 0.29756 0.06987  -0.01741 -0.01215 390 ASN A OD1 
2859 N ND2 . ASN A 387 ? 0.31415 0.26024 0.29300 0.07114  -0.01948 -0.00672 390 ASN A ND2 
2860 N N   . LEU A 388 ? 0.32625 0.22082 0.27149 0.04221  -0.01187 0.00376  391 LEU A N   
2861 C CA  . LEU A 388 ? 0.29114 0.19941 0.24207 0.03420  -0.00782 0.00274  391 LEU A CA  
2862 C C   . LEU A 388 ? 0.35450 0.25457 0.30352 0.02613  -0.00356 -0.00053 391 LEU A C   
2863 O O   . LEU A 388 ? 0.29445 0.17565 0.23383 0.02200  -0.00184 0.00186  391 LEU A O   
2864 C CB  . LEU A 388 ? 0.26666 0.17670 0.21363 0.03128  -0.00742 0.00797  391 LEU A CB  
2865 C CG  . LEU A 388 ? 0.29712 0.21839 0.24886 0.02360  -0.00284 0.00702  391 LEU A CG  
2866 C CD1 . LEU A 388 ? 0.24009 0.18246 0.20439 0.02536  -0.00347 0.00389  391 LEU A CD1 
2867 C CD2 . LEU A 388 ? 0.28084 0.19970 0.22574 0.02119  -0.00179 0.01159  391 LEU A CD2 
2868 N N   . ASP A 389 ? 0.28609 0.20021 0.24401 0.02369  -0.00213 -0.00598 392 ASP A N   
2869 C CA  . ASP A 389 ? 0.27208 0.18398 0.23127 0.01508  0.00120  -0.01015 392 ASP A CA  
2870 C C   . ASP A 389 ? 0.32286 0.25099 0.28848 0.00928  0.00396  -0.00900 392 ASP A C   
2871 O O   . ASP A 389 ? 0.27944 0.22580 0.25300 0.01163  0.00290  -0.01054 392 ASP A O   
2872 C CB  . ASP A 389 ? 0.26306 0.18042 0.22691 0.01741  -0.00020 -0.01767 392 ASP A CB  
2873 C CG  . ASP A 389 ? 0.34357 0.25948 0.30944 0.00827  0.00194  -0.02332 392 ASP A CG  
2874 O OD1 . ASP A 389 ? 0.33429 0.24461 0.29890 -0.00014 0.00511  -0.02107 392 ASP A OD1 
2875 O OD2 . ASP A 389 ? 0.29413 0.21489 0.26272 0.00930  0.00050  -0.03039 392 ASP A OD2 
2876 N N   . PHE A 390 ? 0.29909 0.22056 0.26097 0.00206  0.00781  -0.00615 393 PHE A N   
2877 C CA  . PHE A 390 ? 0.29000 0.22666 0.25783 -0.00165 0.01063  -0.00498 393 PHE A CA  
2878 C C   . PHE A 390 ? 0.35506 0.29337 0.32659 -0.01180 0.01552  -0.00747 393 PHE A C   
2879 O O   . PHE A 390 ? 0.28310 0.20523 0.24764 -0.01780 0.01864  -0.00615 393 PHE A O   
2880 C CB  . PHE A 390 ? 0.31159 0.24376 0.27227 0.00053  0.01123  0.00114  393 PHE A CB  
2881 C CG  . PHE A 390 ? 0.29654 0.24336 0.26286 -0.00169 0.01406  0.00162  393 PHE A CG  
2882 C CD1 . PHE A 390 ? 0.32485 0.28849 0.30019 0.00256  0.01157  0.00018  393 PHE A CD1 
2883 C CD2 . PHE A 390 ? 0.29249 0.23590 0.25487 -0.00789 0.01967  0.00345  393 PHE A CD2 
2884 C CE1 . PHE A 390 ? 0.29162 0.26705 0.27211 0.00170  0.01374  0.00032  393 PHE A CE1 
2885 C CE2 . PHE A 390 ? 0.29434 0.25166 0.26250 -0.00856 0.02242  0.00300  393 PHE A CE2 
2886 C CZ  . PHE A 390 ? 0.31073 0.28341 0.28809 -0.00337 0.01909  0.00128  393 PHE A CZ  
2887 N N   . ILE A 391 ? 0.24844 0.20652 0.23108 -0.01389 0.01636  -0.01051 394 ILE A N   
2888 C CA  . ILE A 391 ? 0.23858 0.20263 0.22783 -0.02347 0.02079  -0.01348 394 ILE A CA  
2889 C C   . ILE A 391 ? 0.31189 0.29580 0.31024 -0.02294 0.02270  -0.01323 394 ILE A C   
2890 O O   . ILE A 391 ? 0.21564 0.21229 0.21895 -0.01622 0.01900  -0.01364 394 ILE A O   
2891 C CB  . ILE A 391 ? 0.30191 0.27003 0.29782 -0.02749 0.01849  -0.02067 394 ILE A CB  
2892 C CG1 . ILE A 391 ? 0.46600 0.44312 0.47124 -0.03844 0.02278  -0.02412 394 ILE A CG1 
2893 C CG2 . ILE A 391 ? 0.36997 0.35518 0.37266 -0.02076 0.01337  -0.02400 394 ILE A CG2 
2894 C CD1 . ILE A 391 ? 0.57737 0.55170 0.58643 -0.04536 0.02092  -0.03136 394 ILE A CD1 
2895 N N   . VAL A 392 ? 0.27603 0.26182 0.27604 -0.02974 0.02889  -0.01233 395 VAL A N   
2896 C CA  . VAL A 392 ? 0.27777 0.28367 0.28854 -0.02957 0.03139  -0.01362 395 VAL A CA  
2897 C C   . VAL A 392 ? 0.30311 0.32336 0.32748 -0.03711 0.03235  -0.01968 395 VAL A C   
2898 O O   . VAL A 392 ? 0.26272 0.27604 0.28686 -0.04686 0.03675  -0.02076 395 VAL A O   
2899 C CB  . VAL A 392 ? 0.31261 0.31451 0.31746 -0.03174 0.03829  -0.00967 395 VAL A CB  
2900 C CG1 . VAL A 392 ? 0.32670 0.35055 0.34414 -0.03019 0.04090  -0.01217 395 VAL A CG1 
2901 C CG2 . VAL A 392 ? 0.31591 0.30291 0.30628 -0.02479 0.03619  -0.00426 395 VAL A CG2 
2902 N N   . TYR A 393 ? 0.22062 0.26026 0.25645 -0.03303 0.02788  -0.02351 396 TYR A N   
2903 C CA  . TYR A 393 ? 0.21815 0.27380 0.26766 -0.03939 0.02683  -0.03009 396 TYR A CA  
2904 C C   . TYR A 393 ? 0.24015 0.31975 0.30340 -0.03640 0.02764  -0.03155 396 TYR A C   
2905 O O   . TYR A 393 ? 0.20474 0.29146 0.26846 -0.02661 0.02363  -0.02983 396 TYR A O   
2906 C CB  . TYR A 393 ? 0.24732 0.30409 0.29664 -0.03647 0.01913  -0.03423 396 TYR A CB  
2907 C CG  . TYR A 393 ? 0.24654 0.32419 0.31046 -0.04086 0.01599  -0.04143 396 TYR A CG  
2908 C CD1 . TYR A 393 ? 0.34752 0.42785 0.41944 -0.05284 0.01932  -0.04602 396 TYR A CD1 
2909 C CD2 . TYR A 393 ? 0.29028 0.38527 0.35990 -0.03322 0.00951  -0.04333 396 TYR A CD2 
2910 C CE1 . TYR A 393 ? 0.35495 0.45685 0.44194 -0.05727 0.01563  -0.05330 396 TYR A CE1 
2911 C CE2 . TYR A 393 ? 0.23706 0.35221 0.31962 -0.03642 0.00551  -0.04989 396 TYR A CE2 
2912 C CZ  . TYR A 393 ? 0.24220 0.36183 0.33425 -0.04842 0.00828  -0.05529 396 TYR A CZ  
2913 O OH  . TYR A 393 ? 0.34066 0.48290 0.44731 -0.05188 0.00339  -0.06253 396 TYR A OH  
2914 N N   . LYS A 394 ? 0.22384 0.31541 0.29837 -0.04467 0.03303  -0.03454 397 LYS A N   
2915 C CA  . LYS A 394 ? 0.25568 0.37197 0.34556 -0.04183 0.03433  -0.03688 397 LYS A CA  
2916 C C   . LYS A 394 ? 0.24427 0.38131 0.34971 -0.04453 0.02840  -0.04392 397 LYS A C   
2917 O O   . LYS A 394 ? 0.22566 0.36654 0.33865 -0.05591 0.03033  -0.04849 397 LYS A O   
2918 C CB  . LYS A 394 ? 0.35319 0.47339 0.44739 -0.04894 0.04474  -0.03622 397 LYS A CB  
2919 C CG  . LYS A 394 ? 0.38341 0.52798 0.49210 -0.04270 0.04651  -0.03827 397 LYS A CG  
2920 C CD  . LYS A 394 ? 0.47488 0.62543 0.58790 -0.04926 0.05813  -0.03811 397 LYS A CD  
2921 C CE  . LYS A 394 ? 0.57295 0.74016 0.69392 -0.03876 0.06002  -0.03890 397 LYS A CE  
2922 N NZ  . LYS A 394 ? 0.64785 0.80042 0.75484 -0.02606 0.05437  -0.03460 397 LYS A NZ  
2923 N N   . PHE A 395 ? 0.18137 0.33075 0.29065 -0.03449 0.02079  -0.04471 398 PHE A N   
2924 C CA  . PHE A 395 ? 0.17907 0.35086 0.30295 -0.03553 0.01422  -0.05133 398 PHE A CA  
2925 C C   . PHE A 395 ? 0.17469 0.37178 0.31774 -0.03605 0.01779  -0.05416 398 PHE A C   
2926 O O   . PHE A 395 ? 0.22184 0.42441 0.36641 -0.02657 0.01929  -0.05098 398 PHE A O   
2927 C CB  . PHE A 395 ? 0.20735 0.38170 0.32578 -0.02396 0.00485  -0.05002 398 PHE A CB  
2928 C CG  . PHE A 395 ? 0.17986 0.37776 0.31109 -0.02286 -0.00322 -0.05615 398 PHE A CG  
2929 C CD1 . PHE A 395 ? 0.17660 0.37466 0.30706 -0.02969 -0.00840 -0.06225 398 PHE A CD1 
2930 C CD2 . PHE A 395 ? 0.16393 0.38330 0.30730 -0.01438 -0.00631 -0.05622 398 PHE A CD2 
2931 C CE1 . PHE A 395 ? 0.17714 0.39738 0.31826 -0.02857 -0.01685 -0.06833 398 PHE A CE1 
2932 C CE2 . PHE A 395 ? 0.16431 0.40606 0.31889 -0.01234 -0.01498 -0.06158 398 PHE A CE2 
2933 C CZ  . PHE A 395 ? 0.17828 0.42123 0.33165 -0.01975 -0.02049 -0.06774 398 PHE A CZ  
2934 N N   . ASP A 396 ? 0.27308 0.32266 0.31134 -0.02126 0.01791  0.01025  399 ASP A N   
2935 C CA  . ASP A 396 ? 0.37902 0.44141 0.42598 -0.02226 0.02179  0.00954  399 ASP A CA  
2936 C C   . ASP A 396 ? 0.30466 0.37185 0.36279 -0.02268 0.01929  0.00884  399 ASP A C   
2937 O O   . ASP A 396 ? 0.24978 0.32841 0.31711 -0.02397 0.02222  0.00854  399 ASP A O   
2938 C CB  . ASP A 396 ? 0.43773 0.50460 0.48280 -0.02770 0.02530  0.01349  399 ASP A CB  
2939 C CG  . ASP A 396 ? 0.45090 0.51215 0.49607 -0.03307 0.02182  0.01796  399 ASP A CG  
2940 O OD1 . ASP A 396 ? 0.73802 0.79355 0.78589 -0.03274 0.01703  0.01748  399 ASP A OD1 
2941 O OD2 . ASP A 396 ? 0.74655 0.80899 0.78874 -0.03798 0.02377  0.02209  399 ASP A OD2 
2942 N N   . ASN A 397 ? 0.20735 0.26671 0.26510 -0.02184 0.01396  0.00861  400 ASN A N   
2943 C CA  . ASN A 397 ? 0.25859 0.32240 0.32653 -0.02266 0.01089  0.00832  400 ASN A CA  
2944 C C   . ASN A 397 ? 0.32312 0.39381 0.39898 -0.01781 0.01127  0.00463  400 ASN A C   
2945 O O   . ASN A 397 ? 0.24370 0.32298 0.33099 -0.01828 0.01070  0.00420  400 ASN A O   
2946 C CB  . ASN A 397 ? 0.27413 0.32743 0.33813 -0.02374 0.00486  0.00916  400 ASN A CB  
2947 C CG  . ASN A 397 ? 0.39048 0.44777 0.46413 -0.02569 0.00085  0.00951  400 ASN A CG  
2948 O OD1 . ASN A 397 ? 0.28871 0.34476 0.36458 -0.02300 -0.00270 0.00777  400 ASN A OD1 
2949 N ND2 . ASN A 397 ? 0.28659 0.34855 0.36592 -0.03071 0.00105  0.01214  400 ASN A ND2 
2950 N N   . TYR A 398 ? 0.22867 0.29567 0.29951 -0.01317 0.01182  0.00199  401 TYR A N   
2951 C CA  . TYR A 398 ? 0.23763 0.30975 0.31580 -0.00834 0.01173  -0.00160 401 TYR A CA  
2952 C C   . TYR A 398 ? 0.20762 0.27470 0.27793 -0.00439 0.01315  -0.00393 401 TYR A C   
2953 O O   . TYR A 398 ? 0.21050 0.27019 0.27031 -0.00534 0.01359  -0.00260 401 TYR A O   
2954 C CB  . TYR A 398 ? 0.23019 0.29965 0.31378 -0.00732 0.00559  -0.00159 401 TYR A CB  
2955 C CG  . TYR A 398 ? 0.23064 0.28790 0.30429 -0.00714 0.00121  -0.00056 401 TYR A CG  
2956 C CD1 . TYR A 398 ? 0.18883 0.24092 0.25785 -0.00323 0.00031  -0.00231 401 TYR A CD1 
2957 C CD2 . TYR A 398 ? 0.17008 0.22143 0.23945 -0.01099 -0.00202 0.00191  401 TYR A CD2 
2958 C CE1 . TYR A 398 ? 0.20637 0.24881 0.26680 -0.00335 -0.00306 -0.00137 401 TYR A CE1 
2959 C CE2 . TYR A 398 ? 0.20309 0.24440 0.26345 -0.01069 -0.00539 0.00218  401 TYR A CE2 
2960 C CZ  . TYR A 398 ? 0.22808 0.26554 0.28409 -0.00694 -0.00561 0.00067  401 TYR A CZ  
2961 O OH  . TYR A 398 ? 0.20428 0.23320 0.25182 -0.00689 -0.00836 0.00096  401 TYR A OH  
2962 N N   . GLY A 399 ? 0.20113 0.27178 0.27732 0.00015  0.01318  -0.00747 402 GLY A N   
2963 C CA  . GLY A 399 ? 0.21906 0.28490 0.28916 0.00396  0.01375  -0.00998 402 GLY A CA  
2964 C C   . GLY A 399 ? 0.25254 0.31775 0.32937 0.00827  0.01018  -0.01252 402 GLY A C   
2965 O O   . GLY A 399 ? 0.19690 0.25976 0.27779 0.00788  0.00532  -0.01094 402 GLY A O   
2966 N N   . LYS A 400 ? 0.19322 0.26021 0.27117 0.01227  0.01217  -0.01644 403 LYS A N   
2967 C CA  . LYS A 400 ? 0.20457 0.26938 0.28865 0.01654  0.00822  -0.01882 403 LYS A CA  
2968 C C   . LYS A 400 ? 0.20993 0.28133 0.30783 0.01760  0.00561  -0.01931 403 LYS A C   
2969 O O   . LYS A 400 ? 0.23125 0.29835 0.33318 0.01914  -0.00010 -0.01851 403 LYS A O   
2970 C CB  . LYS A 400 ? 0.20666 0.27286 0.29035 0.02058  0.01111  -0.02367 403 LYS A CB  
2971 C CG  . LYS A 400 ? 0.27103 0.32885 0.34187 0.02007  0.01151  -0.02298 403 LYS A CG  
2972 C CD  . LYS A 400 ? 0.31212 0.37159 0.38078 0.02328  0.01478  -0.02791 403 LYS A CD  
2973 C CE  . LYS A 400 ? 0.53584 0.60135 0.61554 0.02778  0.01516  -0.03324 403 LYS A CE  
2974 N NZ  . LYS A 400 ? 0.40938 0.47881 0.48551 0.02994  0.02008  -0.03852 403 LYS A NZ  
2975 N N   . THR A 401 ? 0.23572 0.31800 0.34152 0.01680  0.00956  -0.02055 404 THR A N   
2976 C CA  . THR A 401 ? 0.19025 0.28009 0.31122 0.01845  0.00710  -0.02162 404 THR A CA  
2977 C C   . THR A 401 ? 0.23160 0.31645 0.35358 0.01569  0.00050  -0.01711 404 THR A C   
2978 O O   . THR A 401 ? 0.24031 0.32382 0.37009 0.01807  -0.00515 -0.01716 404 THR A O   
2979 C CB  . THR A 401 ? 0.27951 0.38293 0.40861 0.01709  0.01300  -0.02314 404 THR A CB  
2980 O OG1 . THR A 401 ? 0.32075 0.42883 0.44787 0.01985  0.01911  -0.02785 404 THR A OG1 
2981 C CG2 . THR A 401 ? 0.26605 0.37851 0.41285 0.01905  0.01033  -0.02445 404 THR A CG2 
2982 N N   . PHE A 402 ? 0.19911 0.28063 0.31291 0.01064  0.00069  -0.01322 405 PHE A N   
2983 C CA  . PHE A 402 ? 0.22697 0.30317 0.34000 0.00781  -0.00557 -0.00946 405 PHE A CA  
2984 C C   . PHE A 402 ? 0.26452 0.32987 0.37038 0.00943  -0.01063 -0.00849 405 PHE A C   
2985 O O   . PHE A 402 ? 0.20519 0.26804 0.31482 0.00945  -0.01680 -0.00680 405 PHE A O   
2986 C CB  . PHE A 402 ? 0.18535 0.25897 0.29017 0.00230  -0.00427 -0.00620 405 PHE A CB  
2987 C CG  . PHE A 402 ? 0.23515 0.30234 0.33711 -0.00065 -0.01056 -0.00307 405 PHE A CG  
2988 C CD1 . PHE A 402 ? 0.26646 0.33909 0.37840 -0.00268 -0.01411 -0.00178 405 PHE A CD1 
2989 C CD2 . PHE A 402 ? 0.24798 0.30414 0.33754 -0.00124 -0.01308 -0.00173 405 PHE A CD2 
2990 C CE1 . PHE A 402 ? 0.31753 0.38402 0.42592 -0.00553 -0.02029 0.00078  405 PHE A CE1 
2991 C CE2 . PHE A 402 ? 0.20037 0.25100 0.28635 -0.00392 -0.01857 0.00057  405 PHE A CE2 
2992 C CZ  . PHE A 402 ? 0.22507 0.28056 0.32001 -0.00614 -0.02235 0.00179  405 PHE A CZ  
2993 N N   . ILE A 403 ? 0.20692 0.26598 0.30237 0.01044  -0.00829 -0.00922 406 ILE A N   
2994 C CA  . ILE A 403 ? 0.19669 0.24598 0.28473 0.01115  -0.01248 -0.00782 406 ILE A CA  
2995 C C   . ILE A 403 ? 0.21337 0.26264 0.30999 0.01505  -0.01669 -0.00913 406 ILE A C   
2996 O O   . ILE A 403 ? 0.23899 0.28285 0.33478 0.01451  -0.02259 -0.00657 406 ILE A O   
2997 C CB  . ILE A 403 ? 0.15807 0.20186 0.23480 0.01144  -0.00891 -0.00849 406 ILE A CB  
2998 C CG1 . ILE A 403 ? 0.21072 0.25240 0.27859 0.00750  -0.00632 -0.00650 406 ILE A CG1 
2999 C CG2 . ILE A 403 ? 0.16063 0.19609 0.23210 0.01242  -0.01297 -0.00729 406 ILE A CG2 
3000 C CD1 . ILE A 403 ? 0.21855 0.25687 0.27705 0.00791  -0.00210 -0.00738 406 ILE A CD1 
3001 N N   . LYS A 404 ? 0.17953 0.23484 0.28469 0.01897  -0.01398 -0.01318 407 LYS A N   
3002 C CA  . LYS A 404 ? 0.19287 0.24773 0.30766 0.02318  -0.01845 -0.01487 407 LYS A CA  
3003 C C   . LYS A 404 ? 0.22973 0.28794 0.35536 0.02284  -0.02409 -0.01292 407 LYS A C   
3004 O O   . LYS A 404 ? 0.22005 0.27408 0.35040 0.02477  -0.03043 -0.01186 407 LYS A O   
3005 C CB  . LYS A 404 ? 0.22812 0.28925 0.35024 0.02779  -0.01404 -0.02064 407 LYS A CB  
3006 C CG  . LYS A 404 ? 0.23833 0.29400 0.35001 0.02885  -0.01070 -0.02267 407 LYS A CG  
3007 C CD  . LYS A 404 ? 0.37735 0.44013 0.49476 0.03287  -0.00560 -0.02892 407 LYS A CD  
3008 C CE  . LYS A 404 ? 0.44386 0.50036 0.55116 0.03397  -0.00363 -0.03098 407 LYS A CE  
3009 N NZ  . LYS A 404 ? 0.66656 0.73006 0.77531 0.03670  0.00247  -0.03697 407 LYS A NZ  
3010 N N   . LYS A 405 ? 0.19261 0.25817 0.32264 0.02019  -0.02242 -0.01214 408 LYS A N   
3011 C CA  . LYS A 405 ? 0.28532 0.35405 0.42533 0.01926  -0.02835 -0.00992 408 LYS A CA  
3012 C C   . LYS A 405 ? 0.28086 0.34019 0.41175 0.01572  -0.03494 -0.00498 408 LYS A C   
3013 O O   . LYS A 405 ? 0.20634 0.26656 0.34404 0.01486  -0.04132 -0.00267 408 LYS A O   
3014 C CB  . LYS A 405 ? 0.22643 0.30540 0.37297 0.01654  -0.02482 -0.01007 408 LYS A CB  
3015 C CG  . LYS A 405 ? 0.22204 0.31299 0.38090 0.02001  -0.01903 -0.01489 408 LYS A CG  
3016 C CD  . LYS A 405 ? 0.27346 0.37432 0.43673 0.01621  -0.01472 -0.01427 408 LYS A CD  
3017 C CE  . LYS A 405 ? 0.39583 0.51041 0.57277 0.01958  -0.00893 -0.01914 408 LYS A CE  
3018 N NZ  . LYS A 405 ? 0.37447 0.49874 0.55434 0.01485  -0.00417 -0.01775 408 LYS A NZ  
3019 N N   . GLN A 406 ? 0.23253 0.28341 0.34840 0.01364  -0.03357 -0.00345 409 GLN A N   
3020 C CA  . GLN A 406 ? 0.25261 0.29477 0.35836 0.01047  -0.03885 0.00063  409 GLN A CA  
3021 C C   . GLN A 406 ? 0.28042 0.31516 0.38282 0.01247  -0.04251 0.00171  409 GLN A C   
3022 O O   . GLN A 406 ? 0.30082 0.32823 0.39256 0.00963  -0.04560 0.00504  409 GLN A O   
3023 C CB  . GLN A 406 ? 0.25969 0.29786 0.35146 0.00662  -0.03491 0.00155  409 GLN A CB  
3024 C CG  . GLN A 406 ? 0.19600 0.24072 0.29035 0.00464  -0.03024 0.00037  409 GLN A CG  
3025 C CD  . GLN A 406 ? 0.23860 0.29009 0.34438 0.00324  -0.03380 0.00123  409 GLN A CD  
3026 O OE1 . GLN A 406 ? 0.24709 0.29559 0.35253 0.00132  -0.04024 0.00379  409 GLN A OE1 
3027 N NE2 . GLN A 406 ? 0.23936 0.30046 0.35526 0.00397  -0.02964 -0.00084 409 GLN A NE2 
3028 N N   . LYS A 407 ? 0.25693 0.29351 0.36839 0.01714  -0.04234 -0.00110 410 LYS A N   
3029 C CA  . LYS A 407 ? 0.21376 0.24294 0.32334 0.01911  -0.04602 -0.00021 410 LYS A CA  
3030 C C   . LYS A 407 ? 0.27217 0.29473 0.36695 0.01699  -0.04265 0.00076  410 LYS A C   
3031 O O   . LYS A 407 ? 0.29030 0.30560 0.37847 0.01548  -0.04648 0.00404  410 LYS A O   
3032 C CB  . LYS A 407 ? 0.30030 0.32492 0.41215 0.01789  -0.05505 0.00431  410 LYS A CB  
3033 C CG  . LYS A 407 ? 0.38812 0.41854 0.51630 0.02056  -0.05994 0.00366  410 LYS A CG  
3034 C CD  . LYS A 407 ? 0.48781 0.51179 0.61764 0.01983  -0.06978 0.00849  410 LYS A CD  
3035 C CE  . LYS A 407 ? 0.58337 0.60321 0.70090 0.01389  -0.07325 0.01371  410 LYS A CE  
3036 N NZ  . LYS A 407 ? 0.77936 0.80599 0.90107 0.01180  -0.07356 0.01362  410 LYS A NZ  
3037 N N   . CYS A 408 ? 0.24438 0.26982 0.33435 0.01674  -0.03556 -0.00187 411 CYS A N   
3038 C CA  . CYS A 408 ? 0.28018 0.30058 0.35769 0.01517  -0.03194 -0.00150 411 CYS A CA  
3039 C C   . CYS A 408 ? 0.32220 0.34476 0.40111 0.01834  -0.02676 -0.00576 411 CYS A C   
3040 O O   . CYS A 408 ? 0.25468 0.28421 0.34016 0.02019  -0.02317 -0.00905 411 CYS A O   
3041 C CB  . CYS A 408 ? 0.20290 0.22350 0.27116 0.01123  -0.02877 -0.00022 411 CYS A CB  
3042 S SG  . CYS A 408 ? 0.36596 0.38298 0.42927 0.00699  -0.03470 0.00423  411 CYS A SG  
3043 N N   . SER A 409 ? 0.23367 0.25063 0.30598 0.01858  -0.02633 -0.00560 412 SER A N   
3044 C CA  . SER A 409 ? 0.29870 0.31664 0.36861 0.02048  -0.02132 -0.00916 412 SER A CA  
3045 C C   . SER A 409 ? 0.26870 0.28960 0.33183 0.01819  -0.01589 -0.00932 412 SER A C   
3046 O O   . SER A 409 ? 0.26777 0.28568 0.32327 0.01494  -0.01606 -0.00638 412 SER A O   
3047 C CB  . SER A 409 ? 0.33448 0.34523 0.39851 0.02025  -0.02311 -0.00792 412 SER A CB  
3048 O OG  . SER A 409 ? 0.33646 0.34642 0.39298 0.01973  -0.01876 -0.00910 412 SER A OG  
3049 N N   . PRO A 410 ? 0.19525 0.22179 0.26062 0.01965  -0.01112 -0.01267 413 PRO A N   
3050 C CA  . PRO A 410 ? 0.23257 0.26069 0.29081 0.01707  -0.00659 -0.01205 413 PRO A CA  
3051 C C   . PRO A 410 ? 0.24768 0.26950 0.29543 0.01563  -0.00595 -0.01052 413 PRO A C   
3052 O O   . PRO A 410 ? 0.21422 0.23436 0.25596 0.01283  -0.00504 -0.00835 413 PRO A O   
3053 C CB  . PRO A 410 ? 0.25800 0.29279 0.31971 0.01907  -0.00187 -0.01590 413 PRO A CB  
3054 C CG  . PRO A 410 ? 0.30760 0.34718 0.38137 0.02212  -0.00378 -0.01837 413 PRO A CG  
3055 C CD  . PRO A 410 ? 0.29344 0.32594 0.36842 0.02337  -0.00972 -0.01701 413 PRO A CD  
3056 N N   . ASP A 411 ? 0.22099 0.23924 0.26710 0.01749  -0.00670 -0.01172 414 ASP A N   
3057 C CA  . ASP A 411 ? 0.22172 0.23506 0.25922 0.01614  -0.00606 -0.01031 414 ASP A CA  
3058 C C   . ASP A 411 ? 0.22392 0.23345 0.25742 0.01349  -0.00856 -0.00677 414 ASP A C   
3059 O O   . ASP A 411 ? 0.18138 0.18915 0.20838 0.01164  -0.00692 -0.00557 414 ASP A O   
3060 C CB  . ASP A 411 ? 0.25229 0.26241 0.28975 0.01816  -0.00729 -0.01188 414 ASP A CB  
3061 C CG  . ASP A 411 ? 0.35050 0.35729 0.38025 0.01690  -0.00599 -0.01086 414 ASP A CG  
3062 O OD1 . ASP A 411 ? 0.30267 0.31121 0.32862 0.01668  -0.00269 -0.01179 414 ASP A OD1 
3063 O OD2 . ASP A 411 ? 0.27656 0.27940 0.30427 0.01586  -0.00829 -0.00879 414 ASP A OD2 
3064 N N   . ALA A 412 ? 0.21348 0.22157 0.25067 0.01333  -0.01273 -0.00519 415 ALA A N   
3065 C CA  . ALA A 412 ? 0.26047 0.26509 0.29255 0.01050  -0.01509 -0.00186 415 ALA A CA  
3066 C C   . ALA A 412 ? 0.22412 0.23032 0.25372 0.00826  -0.01419 -0.00108 415 ALA A C   
3067 O O   . ALA A 412 ? 0.20961 0.21336 0.23223 0.00609  -0.01360 0.00016  415 ALA A O   
3068 C CB  . ALA A 412 ? 0.19699 0.19956 0.23322 0.01046  -0.02037 0.00021  415 ALA A CB  
3069 N N   . PHE A 413 ? 0.16858 0.17911 0.20439 0.00876  -0.01409 -0.00206 416 PHE A N   
3070 C CA  . PHE A 413 ? 0.16187 0.17386 0.19625 0.00631  -0.01359 -0.00133 416 PHE A CA  
3071 C C   . PHE A 413 ? 0.21782 0.22865 0.24570 0.00532  -0.00958 -0.00194 416 PHE A C   
3072 O O   . PHE A 413 ? 0.21387 0.22183 0.23606 0.00309  -0.00978 -0.00102 416 PHE A O   
3073 C CB  . PHE A 413 ? 0.21303 0.23116 0.25698 0.00716  -0.01378 -0.00239 416 PHE A CB  
3074 C CG  . PHE A 413 ? 0.22627 0.24653 0.27101 0.00435  -0.01417 -0.00140 416 PHE A CG  
3075 C CD1 . PHE A 413 ? 0.19148 0.21277 0.23319 0.00276  -0.01048 -0.00177 416 PHE A CD1 
3076 C CD2 . PHE A 413 ? 0.21606 0.23728 0.26534 0.00315  -0.01879 0.00009  416 PHE A CD2 
3077 C CE1 . PHE A 413 ? 0.19815 0.22111 0.24140 -0.00018 -0.01127 -0.00075 416 PHE A CE1 
3078 C CE2 . PHE A 413 ? 0.25325 0.27669 0.30417 0.00032  -0.01961 0.00087  416 PHE A CE2 
3079 C CZ  . PHE A 413 ? 0.18849 0.21267 0.23649 -0.00141 -0.01582 0.00040  416 PHE A CZ  
3080 N N   . ILE A 414 ? 0.20181 0.21429 0.23009 0.00705  -0.00627 -0.00363 417 ILE A N   
3081 C CA  . ILE A 414 ? 0.20180 0.21277 0.22424 0.00615  -0.00315 -0.00374 417 ILE A CA  
3082 C C   . ILE A 414 ? 0.21525 0.22114 0.23091 0.00585  -0.00348 -0.00310 417 ILE A C   
3083 O O   . ILE A 414 ? 0.20327 0.20661 0.21424 0.00447  -0.00265 -0.00272 417 ILE A O   
3084 C CB  . ILE A 414 ? 0.22594 0.24002 0.24963 0.00783  0.00005  -0.00546 417 ILE A CB  
3085 C CG1 . ILE A 414 ? 0.23839 0.25881 0.26835 0.00748  0.00150  -0.00613 417 ILE A CG1 
3086 C CG2 . ILE A 414 ? 0.22956 0.24087 0.24657 0.00705  0.00228  -0.00499 417 ILE A CG2 
3087 C CD1 . ILE A 414 ? 0.19496 0.21998 0.22745 0.00978  0.00448  -0.00878 417 ILE A CD1 
3088 N N   . GLN A 415 ? 0.19030 0.19478 0.20593 0.00709  -0.00475 -0.00306 418 GLN A N   
3089 C CA  . GLN A 415 ? 0.17735 0.17838 0.18746 0.00650  -0.00473 -0.00234 418 GLN A CA  
3090 C C   . GLN A 415 ? 0.20011 0.19929 0.20630 0.00422  -0.00597 -0.00130 418 GLN A C   
3091 O O   . GLN A 415 ? 0.19679 0.19395 0.19808 0.00362  -0.00458 -0.00169 418 GLN A O   
3092 C CB  . GLN A 415 ? 0.17878 0.17891 0.19032 0.00743  -0.00642 -0.00184 418 GLN A CB  
3093 C CG  . GLN A 415 ? 0.19400 0.19470 0.20718 0.00959  -0.00501 -0.00351 418 GLN A CG  
3094 C CD  . GLN A 415 ? 0.24736 0.24678 0.25609 0.00959  -0.00290 -0.00375 418 GLN A CD  
3095 O OE1 . GLN A 415 ? 0.23106 0.22909 0.23655 0.00841  -0.00278 -0.00274 418 GLN A OE1 
3096 N NE2 . GLN A 415 ? 0.19215 0.19238 0.20080 0.01093  -0.00128 -0.00520 418 GLN A NE2 
3097 N N   . VAL A 416 ? 0.17977 0.17960 0.18810 0.00308  -0.00883 -0.00024 419 VAL A N   
3098 C CA  . VAL A 416 ? 0.20031 0.19826 0.20394 0.00066  -0.01035 0.00046  419 VAL A CA  
3099 C C   . VAL A 416 ? 0.18106 0.17832 0.18302 -0.00024 -0.00887 -0.00079 419 VAL A C   
3100 O O   . VAL A 416 ? 0.19278 0.18731 0.18911 -0.00143 -0.00855 -0.00153 419 VAL A O   
3101 C CB  . VAL A 416 ? 0.23155 0.23026 0.23812 -0.00052 -0.01461 0.00221  419 VAL A CB  
3102 C CG1 . VAL A 416 ? 0.24735 0.24426 0.24870 -0.00329 -0.01659 0.00265  419 VAL A CG1 
3103 C CG2 . VAL A 416 ? 0.20865 0.20643 0.21557 -0.00016 -0.01665 0.00402  419 VAL A CG2 
3104 N N   . ALA A 417 ? 0.21172 0.21145 0.21860 0.00021  -0.00792 -0.00113 420 ALA A N   
3105 C CA  . ALA A 417 ? 0.21838 0.21704 0.22411 -0.00108 -0.00674 -0.00167 420 ALA A CA  
3106 C C   . ALA A 417 ? 0.16989 0.16517 0.17070 -0.00027 -0.00442 -0.00263 420 ALA A C   
3107 O O   . ALA A 417 ? 0.22957 0.22148 0.22711 -0.00141 -0.00456 -0.00335 420 ALA A O   
3108 C CB  . ALA A 417 ? 0.17688 0.17980 0.18866 -0.00098 -0.00544 -0.00140 420 ALA A CB  
3109 N N   . LEU A 418 ? 0.17034 0.16627 0.17116 0.00181  -0.00267 -0.00283 421 LEU A N   
3110 C CA  . LEU A 418 ? 0.21286 0.20600 0.21013 0.00279  -0.00096 -0.00363 421 LEU A CA  
3111 C C   . LEU A 418 ? 0.19985 0.19059 0.19278 0.00259  -0.00124 -0.00464 421 LEU A C   
3112 O O   . LEU A 418 ? 0.22109 0.20902 0.21148 0.00302  -0.00039 -0.00596 421 LEU A O   
3113 C CB  . LEU A 418 ? 0.20423 0.19889 0.20274 0.00484  0.00043  -0.00361 421 LEU A CB  
3114 C CG  . LEU A 418 ? 0.23600 0.23330 0.23738 0.00515  0.00144  -0.00325 421 LEU A CG  
3115 C CD1 . LEU A 418 ? 0.21103 0.20991 0.21347 0.00713  0.00201  -0.00381 421 LEU A CD1 
3116 C CD2 . LEU A 418 ? 0.21038 0.20562 0.20972 0.00440  0.00239  -0.00271 421 LEU A CD2 
3117 N N   . GLN A 419 ? 0.22176 0.21366 0.21379 0.00197  -0.00242 -0.00409 422 GLN A N   
3118 C CA  . GLN A 419 ? 0.19672 0.18721 0.18362 0.00118  -0.00225 -0.00508 422 GLN A CA  
3119 C C   . GLN A 419 ? 0.19477 0.18248 0.17845 -0.00039 -0.00332 -0.00655 422 GLN A C   
3120 O O   . GLN A 419 ? 0.21621 0.20175 0.19602 -0.00008 -0.00216 -0.00886 422 GLN A O   
3121 C CB  . GLN A 419 ? 0.18219 0.17435 0.16795 -0.00002 -0.00374 -0.00336 422 GLN A CB  
3122 C CG  . GLN A 419 ? 0.23505 0.22910 0.22381 0.00122  -0.00318 -0.00202 422 GLN A CG  
3123 C CD  . GLN A 419 ? 0.23934 0.23381 0.22657 0.00232  -0.00040 -0.00320 422 GLN A CD  
3124 O OE1 . GLN A 419 ? 0.24406 0.23856 0.22702 0.00153  0.00087  -0.00431 422 GLN A OE1 
3125 N NE2 . GLN A 419 ? 0.21481 0.20996 0.20565 0.00422  0.00054  -0.00328 422 GLN A NE2 
3126 N N   . LEU A 420 ? 0.17990 0.16779 0.16560 -0.00203 -0.00572 -0.00556 423 LEU A N   
3127 C CA  . LEU A 420 ? 0.20198 0.18683 0.18507 -0.00388 -0.00736 -0.00695 423 LEU A CA  
3128 C C   . LEU A 420 ? 0.22053 0.20215 0.20422 -0.00313 -0.00611 -0.00837 423 LEU A C   
3129 O O   . LEU A 420 ? 0.22784 0.20545 0.20786 -0.00355 -0.00655 -0.01079 423 LEU A O   
3130 C CB  . LEU A 420 ? 0.18509 0.17168 0.17197 -0.00593 -0.01049 -0.00519 423 LEU A CB  
3131 C CG  . LEU A 420 ? 0.23200 0.21555 0.21719 -0.00841 -0.01301 -0.00631 423 LEU A CG  
3132 C CD1 . LEU A 420 ? 0.24165 0.22189 0.21856 -0.00932 -0.01385 -0.00868 423 LEU A CD1 
3133 C CD2 . LEU A 420 ? 0.19029 0.17689 0.18088 -0.01049 -0.01642 -0.00424 423 LEU A CD2 
3134 N N   . ALA A 421 ? 0.20228 0.18523 0.19026 -0.00204 -0.00477 -0.00697 424 ALA A N   
3135 C CA  . ALA A 421 ? 0.19887 0.17828 0.18714 -0.00158 -0.00409 -0.00748 424 ALA A CA  
3136 C C   . ALA A 421 ? 0.27880 0.25534 0.26402 0.00064  -0.00274 -0.00989 424 ALA A C   
3137 O O   . ALA A 421 ? 0.24611 0.21784 0.22994 0.00081  -0.00340 -0.01177 424 ALA A O   
3138 C CB  . ALA A 421 ? 0.18054 0.16246 0.17262 -0.00098 -0.00273 -0.00525 424 ALA A CB  
3139 N N   . PHE A 422 ? 0.25160 0.23109 0.23667 0.00248  -0.00096 -0.00993 425 PHE A N   
3140 C CA  . PHE A 422 ? 0.25546 0.23372 0.23901 0.00470  0.00063  -0.01231 425 PHE A CA  
3141 C C   . PHE A 422 ? 0.23182 0.20820 0.21087 0.00418  0.00054  -0.01554 425 PHE A C   
3142 O O   . PHE A 422 ? 0.22280 0.19595 0.20102 0.00574  0.00104  -0.01860 425 PHE A O   
3143 C CB  . PHE A 422 ? 0.24831 0.23095 0.23312 0.00607  0.00237  -0.01139 425 PHE A CB  
3144 C CG  . PHE A 422 ? 0.18095 0.16359 0.16646 0.00854  0.00409  -0.01336 425 PHE A CG  
3145 C CD1 . PHE A 422 ? 0.26524 0.24856 0.24808 0.00900  0.00559  -0.01633 425 PHE A CD1 
3146 C CD2 . PHE A 422 ? 0.21037 0.19262 0.19924 0.01038  0.00415  -0.01245 425 PHE A CD2 
3147 C CE1 . PHE A 422 ? 0.27152 0.25573 0.25638 0.01158  0.00738  -0.01860 425 PHE A CE1 
3148 C CE2 . PHE A 422 ? 0.24972 0.23220 0.24054 0.01290  0.00524  -0.01435 425 PHE A CE2 
3149 C CZ  . PHE A 422 ? 0.25356 0.23728 0.24310 0.01366  0.00695  -0.01750 425 PHE A CZ  
3150 N N   . TYR A 423 ? 0.25070 0.22894 0.22664 0.00207  -0.00031 -0.01511 426 TYR A N   
3151 C CA  . TYR A 423 ? 0.22518 0.20196 0.19525 0.00119  -0.00037 -0.01831 426 TYR A CA  
3152 C C   . TYR A 423 ? 0.29768 0.26872 0.26648 0.00042  -0.00252 -0.02074 426 TYR A C   
3153 O O   . TYR A 423 ? 0.25851 0.22667 0.22374 0.00133  -0.00194 -0.02499 426 TYR A O   
3154 C CB  . TYR A 423 ? 0.22359 0.20310 0.19004 -0.00145 -0.00173 -0.01652 426 TYR A CB  
3155 C CG  . TYR A 423 ? 0.29158 0.27083 0.25039 -0.00247 -0.00104 -0.01965 426 TYR A CG  
3156 C CD1 . TYR A 423 ? 0.27912 0.26225 0.23529 -0.00183 0.00214  -0.02036 426 TYR A CD1 
3157 C CD2 . TYR A 423 ? 0.26643 0.24194 0.22048 -0.00434 -0.00349 -0.02200 426 TYR A CD2 
3158 C CE1 . TYR A 423 ? 0.34387 0.32778 0.29215 -0.00302 0.00347  -0.02345 426 TYR A CE1 
3159 C CE2 . TYR A 423 ? 0.36143 0.33683 0.30717 -0.00532 -0.00265 -0.02546 426 TYR A CE2 
3160 C CZ  . TYR A 423 ? 0.39320 0.37314 0.33592 -0.00464 0.00111  -0.02613 426 TYR A CZ  
3161 O OH  . TYR A 423 ? 0.47442 0.45527 0.40834 -0.00582 0.00262  -0.02966 426 TYR A OH  
3162 N N   . ARG A 424 ? 0.25187 0.22131 0.22375 -0.00137 -0.00505 -0.01838 427 ARG A N   
3163 C CA  . ARG A 424 ? 0.29377 0.25744 0.26442 -0.00283 -0.00767 -0.02046 427 ARG A CA  
3164 C C   . ARG A 424 ? 0.31409 0.27276 0.28690 -0.00061 -0.00724 -0.02234 427 ARG A C   
3165 O O   . ARG A 424 ? 0.30656 0.25935 0.27746 -0.00075 -0.00898 -0.02570 427 ARG A O   
3166 C CB  . ARG A 424 ? 0.29996 0.26414 0.27416 -0.00586 -0.01051 -0.01715 427 ARG A CB  
3167 C CG  . ARG A 424 ? 0.26752 0.23282 0.24794 -0.00562 -0.00981 -0.01373 427 ARG A CG  
3168 C CD  . ARG A 424 ? 0.31605 0.28506 0.30081 -0.00850 -0.01155 -0.01041 427 ARG A CD  
3169 N NE  . ARG A 424 ? 0.29440 0.26031 0.27860 -0.01163 -0.01507 -0.01117 427 ARG A NE  
3170 C CZ  . ARG A 424 ? 0.41204 0.38150 0.39886 -0.01413 -0.01735 -0.00946 427 ARG A CZ  
3171 N NH1 . ARG A 424 ? 0.26373 0.23966 0.25430 -0.01360 -0.01645 -0.00708 427 ARG A NH1 
3172 N NH2 . ARG A 424 ? 0.35015 0.31644 0.33638 -0.01712 -0.02100 -0.01035 427 ARG A NH2 
3173 N N   . LEU A 425 ? 0.25650 0.21695 0.23312 0.00154  -0.00539 -0.02044 428 LEU A N   
3174 C CA  . LEU A 425 ? 0.28091 0.23663 0.25999 0.00387  -0.00551 -0.02166 428 LEU A CA  
3175 C C   . LEU A 425 ? 0.31796 0.27392 0.29587 0.00740  -0.00325 -0.02606 428 LEU A C   
3176 O O   . LEU A 425 ? 0.29483 0.24535 0.27300 0.00921  -0.00415 -0.02981 428 LEU A O   
3177 C CB  . LEU A 425 ? 0.26981 0.22742 0.25317 0.00425  -0.00506 -0.01730 428 LEU A CB  
3178 C CG  . LEU A 425 ? 0.38554 0.33773 0.37166 0.00587  -0.00632 -0.01692 428 LEU A CG  
3179 C CD1 . LEU A 425 ? 0.36120 0.30583 0.34741 0.00383  -0.00970 -0.01728 428 LEU A CD1 
3180 C CD2 . LEU A 425 ? 0.30830 0.26352 0.29688 0.00563  -0.00575 -0.01228 428 LEU A CD2 
3181 N N   . HIS A 426 ? 0.28675 0.24911 0.26381 0.00835  -0.00036 -0.02591 429 HIS A N   
3182 C CA  . HIS A 426 ? 0.29097 0.25545 0.26852 0.01161  0.00240  -0.02949 429 HIS A CA  
3183 C C   . HIS A 426 ? 0.36160 0.32922 0.33346 0.01106  0.00454  -0.03308 429 HIS A C   
3184 O O   . HIS A 426 ? 0.33406 0.30384 0.30617 0.01366  0.00727  -0.03698 429 HIS A O   
3185 C CB  . HIS A 426 ? 0.27888 0.24860 0.26061 0.01307  0.00419  -0.02647 429 HIS A CB  
3186 C CG  . HIS A 426 ? 0.32626 0.29279 0.31253 0.01395  0.00226  -0.02363 429 HIS A CG  
3187 N ND1 . HIS A 426 ? 0.39117 0.35217 0.38030 0.01624  0.00070  -0.02546 429 HIS A ND1 
3188 C CD2 . HIS A 426 ? 0.24716 0.21493 0.23509 0.01266  0.00139  -0.01913 429 HIS A CD2 
3189 C CE1 . HIS A 426 ? 0.44718 0.40614 0.43899 0.01592  -0.00120 -0.02154 429 HIS A CE1 
3190 N NE2 . HIS A 426 ? 0.29412 0.25746 0.28492 0.01376  -0.00050 -0.01791 429 HIS A NE2 
3191 N N   . ARG A 427 ? 0.30365 0.27182 0.27044 0.00769  0.00329  -0.03193 430 ARG A N   
3192 C CA  . ARG A 427 ? 0.27747 0.24744 0.23692 0.00631  0.00445  -0.03512 430 ARG A CA  
3193 C C   . ARG A 427 ? 0.33294 0.31045 0.29093 0.00645  0.00818  -0.03436 430 ARG A C   
3194 O O   . ARG A 427 ? 0.32165 0.30172 0.27398 0.00615  0.01056  -0.03784 430 ARG A O   
3195 C CB  . ARG A 427 ? 0.38491 0.35015 0.34159 0.00811  0.00463  -0.04181 430 ARG A CB  
3196 C CG  . ARG A 427 ? 0.37212 0.32878 0.33171 0.00832  0.00070  -0.04268 430 ARG A CG  
3197 C CD  . ARG A 427 ? 0.53494 0.48954 0.49405 0.00429  -0.00318 -0.03823 430 ARG A CD  
3198 N NE  . ARG A 427 ? 0.65746 0.61188 0.60911 0.00123  -0.00473 -0.03986 430 ARG A NE  
3199 C CZ  . ARG A 427 ? 0.69822 0.65016 0.64909 -0.00225 -0.00872 -0.03764 430 ARG A CZ  
3200 N NH1 . ARG A 427 ? 0.53068 0.48089 0.48788 -0.00336 -0.01100 -0.03357 430 ARG A NH1 
3201 N NH2 . ARG A 427 ? 0.59685 0.54846 0.54036 -0.00489 -0.01050 -0.03951 430 ARG A NH2 
3202 N N   . ARG A 428 ? 0.31198 0.29319 0.27487 0.00667  0.00873  -0.02992 431 ARG A N   
3203 C CA  . ARG A 428 ? 0.27740 0.26534 0.23954 0.00580  0.01129  -0.02779 431 ARG A CA  
3204 C C   . ARG A 428 ? 0.25709 0.24618 0.22401 0.00510  0.00959  -0.02239 431 ARG A C   
3205 O O   . ARG A 428 ? 0.28805 0.27395 0.25933 0.00612  0.00773  -0.02113 431 ARG A O   
3206 C CB  . ARG A 428 ? 0.37175 0.36396 0.33704 0.00872  0.01533  -0.03079 431 ARG A CB  
3207 C CG  . ARG A 428 ? 0.34759 0.33848 0.32128 0.01200  0.01488  -0.03020 431 ARG A CG  
3208 C CD  . ARG A 428 ? 0.49827 0.49436 0.47661 0.01494  0.01848  -0.03291 431 ARG A CD  
3209 N NE  . ARG A 428 ? 0.50913 0.50359 0.49529 0.01779  0.01707  -0.03170 431 ARG A NE  
3210 C CZ  . ARG A 428 ? 0.72501 0.72457 0.71715 0.01933  0.01856  -0.03069 431 ARG A CZ  
3211 N NH1 . ARG A 428 ? 0.49970 0.50679 0.49182 0.01835  0.02197  -0.03087 431 ARG A NH1 
3212 N NH2 . ARG A 428 ? 0.52533 0.52252 0.52347 0.02147  0.01633  -0.02909 431 ARG A NH2 
3213 N N   . LEU A 429 ? 0.25673 0.25028 0.22260 0.00321  0.01020  -0.01928 432 LEU A N   
3214 C CA  . LEU A 429 ? 0.27137 0.26649 0.24264 0.00338  0.00923  -0.01524 432 LEU A CA  
3215 C C   . LEU A 429 ? 0.27809 0.27716 0.25373 0.00537  0.01203  -0.01572 432 LEU A C   
3216 O O   . LEU A 429 ? 0.23845 0.24060 0.21279 0.00600  0.01505  -0.01850 432 LEU A O   
3217 C CB  . LEU A 429 ? 0.28057 0.27734 0.24960 0.00028  0.00733  -0.01130 432 LEU A CB  
3218 C CG  . LEU A 429 ? 0.28091 0.27445 0.24734 -0.00167 0.00375  -0.01019 432 LEU A CG  
3219 C CD1 . LEU A 429 ? 0.30861 0.30345 0.27542 -0.00395 0.00103  -0.00578 432 LEU A CD1 
3220 C CD2 . LEU A 429 ? 0.25907 0.24929 0.22997 -0.00013 0.00224  -0.01069 432 LEU A CD2 
3221 N N   . VAL A 430 ? 0.26088 0.26030 0.24193 0.00635  0.01102  -0.01324 433 VAL A N   
3222 C CA  . VAL A 430 ? 0.24811 0.25109 0.23420 0.00813  0.01283  -0.01339 433 VAL A CA  
3223 C C   . VAL A 430 ? 0.27739 0.28212 0.26618 0.00685  0.01141  -0.00959 433 VAL A C   
3224 O O   . VAL A 430 ? 0.24224 0.24453 0.23041 0.00577  0.00890  -0.00746 433 VAL A O   
3225 C CB  . VAL A 430 ? 0.27166 0.27189 0.26208 0.01135  0.01232  -0.01505 433 VAL A CB  
3226 C CG1 . VAL A 430 ? 0.31425 0.31224 0.30324 0.01311  0.01348  -0.01932 433 VAL A CG1 
3227 C CG2 . VAL A 430 ? 0.22653 0.22256 0.21751 0.01114  0.00937  -0.01279 433 VAL A CG2 
3228 N N   . PRO A 431 ? 0.25097 0.25992 0.24358 0.00707  0.01277  -0.00894 434 PRO A N   
3229 C CA  . PRO A 431 ? 0.23744 0.24696 0.23336 0.00615  0.01080  -0.00579 434 PRO A CA  
3230 C C   . PRO A 431 ? 0.23587 0.24135 0.23369 0.00789  0.00832  -0.00556 434 PRO A C   
3231 O O   . PRO A 431 ? 0.21984 0.22397 0.21953 0.01024  0.00842  -0.00714 434 PRO A O   
3232 C CB  . PRO A 431 ? 0.21692 0.23144 0.21783 0.00671  0.01260  -0.00599 434 PRO A CB  
3233 C CG  . PRO A 431 ? 0.25546 0.27396 0.25412 0.00649  0.01636  -0.00850 434 PRO A CG  
3234 C CD  . PRO A 431 ? 0.24594 0.25967 0.24085 0.00823  0.01608  -0.01135 434 PRO A CD  
3235 N N   . THR A 432 ? 0.23888 0.24256 0.23627 0.00668  0.00603  -0.00355 435 THR A N   
3236 C CA  . THR A 432 ? 0.20099 0.20173 0.19945 0.00799  0.00424  -0.00362 435 THR A CA  
3237 C C   . THR A 432 ? 0.23247 0.23347 0.23414 0.00796  0.00240  -0.00229 435 THR A C   
3238 O O   . THR A 432 ? 0.21893 0.22081 0.22131 0.00622  0.00141  -0.00054 435 THR A O   
3239 C CB  . THR A 432 ? 0.20263 0.20129 0.19847 0.00700  0.00320  -0.00337 435 THR A CB  
3240 O OG1 . THR A 432 ? 0.23508 0.23289 0.22774 0.00690  0.00454  -0.00500 435 THR A OG1 
3241 C CG2 . THR A 432 ? 0.19068 0.18772 0.18822 0.00815  0.00203  -0.00355 435 THR A CG2 
3242 N N   . TYR A 433 ? 0.19730 0.19722 0.20051 0.00970  0.00171  -0.00310 436 TYR A N   
3243 C CA  . TYR A 433 ? 0.19982 0.19934 0.20553 0.01007  -0.00022 -0.00281 436 TYR A CA  
3244 C C   . TYR A 433 ? 0.23843 0.23633 0.24363 0.01078  -0.00109 -0.00352 436 TYR A C   
3245 O O   . TYR A 433 ? 0.23392 0.23131 0.23729 0.01145  -0.00006 -0.00429 436 TYR A O   
3246 C CB  . TYR A 433 ? 0.18987 0.18985 0.19707 0.01147  -0.00042 -0.00359 436 TYR A CB  
3247 C CG  . TYR A 433 ? 0.26518 0.26444 0.27434 0.01179  -0.00273 -0.00385 436 TYR A CG  
3248 C CD1 . TYR A 433 ? 0.27031 0.26789 0.27794 0.01296  -0.00351 -0.00524 436 TYR A CD1 
3249 C CD2 . TYR A 433 ? 0.23497 0.23542 0.24747 0.01068  -0.00407 -0.00291 436 TYR A CD2 
3250 C CE1 . TYR A 433 ? 0.27725 0.27388 0.28608 0.01344  -0.00566 -0.00632 436 TYR A CE1 
3251 C CE2 . TYR A 433 ? 0.22512 0.22413 0.23941 0.01088  -0.00671 -0.00353 436 TYR A CE2 
3252 C CZ  . TYR A 433 ? 0.27272 0.26959 0.28491 0.01245  -0.00755 -0.00553 436 TYR A CZ  
3253 O OH  . TYR A 433 ? 0.25810 0.25330 0.27157 0.01277  -0.01023 -0.00688 436 TYR A OH  
3254 N N   . GLU A 434 ? 0.23417 0.23144 0.24153 0.01058  -0.00303 -0.00330 437 GLU A N   
3255 C CA  . GLU A 434 ? 0.19161 0.18834 0.19995 0.01188  -0.00370 -0.00481 437 GLU A CA  
3256 C C   . GLU A 434 ? 0.25242 0.24801 0.26344 0.01266  -0.00590 -0.00580 437 GLU A C   
3257 O O   . GLU A 434 ? 0.20064 0.19508 0.21408 0.01160  -0.00803 -0.00446 437 GLU A O   
3258 C CB  . GLU A 434 ? 0.19519 0.19200 0.20465 0.01132  -0.00437 -0.00422 437 GLU A CB  
3259 C CG  . GLU A 434 ? 0.20328 0.20087 0.21514 0.01305  -0.00454 -0.00635 437 GLU A CG  
3260 C CD  . GLU A 434 ? 0.31113 0.30932 0.32640 0.01302  -0.00596 -0.00606 437 GLU A CD  
3261 O OE1 . GLU A 434 ? 0.23904 0.23629 0.25433 0.01141  -0.00758 -0.00382 437 GLU A OE1 
3262 O OE2 . GLU A 434 ? 0.27873 0.27883 0.29676 0.01461  -0.00543 -0.00818 437 GLU A OE2 
3263 N N   . SER A 435 ? 0.20978 0.20541 0.21998 0.01425  -0.00563 -0.00809 438 SER A N   
3264 C CA  . SER A 435 ? 0.23842 0.23253 0.25055 0.01526  -0.00786 -0.01003 438 SER A CA  
3265 C C   . SER A 435 ? 0.26324 0.25609 0.27942 0.01591  -0.00983 -0.01084 438 SER A C   
3266 O O   . SER A 435 ? 0.26804 0.26234 0.28515 0.01682  -0.00879 -0.01178 438 SER A O   
3267 C CB  . SER A 435 ? 0.26777 0.26260 0.27679 0.01680  -0.00676 -0.01280 438 SER A CB  
3268 O OG  . SER A 435 ? 0.45030 0.44571 0.45581 0.01626  -0.00567 -0.01165 438 SER A OG  
3269 N N   . ALA A 436 ? 0.19650 0.18662 0.21584 0.01543  -0.01305 -0.01045 439 ALA A N   
3270 C CA  . ALA A 436 ? 0.18944 0.17714 0.21352 0.01641  -0.01599 -0.01142 439 ALA A CA  
3271 C C   . ALA A 436 ? 0.31441 0.29911 0.34030 0.01767  -0.01865 -0.01440 439 ALA A C   
3272 O O   . ALA A 436 ? 0.28255 0.26556 0.30845 0.01598  -0.02042 -0.01297 439 ALA A O   
3273 C CB  . ALA A 436 ? 0.23698 0.22287 0.26329 0.01396  -0.01844 -0.00724 439 ALA A CB  
3274 N N   . SER A 437 ? 0.23290 0.21720 0.26071 0.02055  -0.01899 -0.01879 440 SER A N   
3275 C CA  . SER A 437 ? 0.22770 0.20874 0.25648 0.02197  -0.02159 -0.02261 440 SER A CA  
3276 C C   . SER A 437 ? 0.28606 0.26159 0.32062 0.02121  -0.02685 -0.02137 440 SER A C   
3277 O O   . SER A 437 ? 0.24265 0.21670 0.28193 0.02178  -0.02874 -0.02038 440 SER A O   
3278 C CB  . SER A 437 ? 0.28943 0.27222 0.31827 0.02547  -0.01990 -0.02843 440 SER A CB  
3279 O OG  . SER A 437 ? 0.25740 0.23597 0.28818 0.02717  -0.02325 -0.03275 440 SER A OG  
3280 N N   . ILE A 438 ? 0.24088 0.21313 0.27543 0.01980  -0.02972 -0.02127 441 ILE A N   
3281 C CA  . ILE A 438 ? 0.22998 0.19613 0.27013 0.01882  -0.03533 -0.02037 441 ILE A CA  
3282 C C   . ILE A 438 ? 0.21990 0.18191 0.26129 0.02138  -0.03821 -0.02652 441 ILE A C   
3283 O O   . ILE A 438 ? 0.21838 0.17503 0.26283 0.01991  -0.04301 -0.02620 441 ILE A O   
3284 C CB  . ILE A 438 ? 0.23274 0.19836 0.27314 0.01426  -0.03690 -0.01460 441 ILE A CB  
3285 C CG1 . ILE A 438 ? 0.21233 0.18148 0.24832 0.01330  -0.03450 -0.01494 441 ILE A CG1 
3286 C CG2 . ILE A 438 ? 0.25201 0.22044 0.29191 0.01186  -0.03502 -0.00904 441 ILE A CG2 
3287 C CD1 . ILE A 438 ? 0.21429 0.18344 0.25242 0.00905  -0.03651 -0.01032 441 ILE A CD1 
3288 N N   . ARG A 439 ? 0.25346 0.21791 0.29258 0.02510  -0.03537 -0.03231 442 ARG A N   
3289 C CA  . ARG A 439 ? 0.28219 0.24328 0.32166 0.02811  -0.03746 -0.03941 442 ARG A CA  
3290 C C   . ARG A 439 ? 0.29197 0.24661 0.33961 0.03009  -0.04264 -0.04168 442 ARG A C   
3291 O O   . ARG A 439 ? 0.31061 0.26122 0.35939 0.03267  -0.04521 -0.04798 442 ARG A O   
3292 C CB  . ARG A 439 ? 0.23936 0.20601 0.27428 0.03141  -0.03228 -0.04487 442 ARG A CB  
3293 C CG  . ARG A 439 ? 0.23209 0.20273 0.25807 0.02986  -0.02889 -0.04444 442 ARG A CG  
3294 C CD  . ARG A 439 ? 0.30614 0.28236 0.32726 0.03232  -0.02379 -0.04890 442 ARG A CD  
3295 N NE  . ARG A 439 ? 0.33661 0.31112 0.35802 0.03575  -0.02471 -0.05683 442 ARG A NE  
3296 C CZ  . ARG A 439 ? 0.32085 0.30028 0.34148 0.03876  -0.02057 -0.06194 442 ARG A CZ  
3297 N NH1 . ARG A 439 ? 0.30864 0.29476 0.32912 0.03856  -0.01566 -0.05955 442 ARG A NH1 
3298 N NH2 . ARG A 439 ? 0.33676 0.31471 0.35688 0.04193  -0.02129 -0.06989 442 ARG A NH2 
3299 N N   . ARG A 440 ? 0.24560 0.19877 0.29881 0.02906  -0.04461 -0.03694 443 ARG A N   
3300 C CA  . ARG A 440 ? 0.24518 0.19070 0.30664 0.03030  -0.05097 -0.03791 443 ARG A CA  
3301 C C   . ARG A 440 ? 0.24673 0.18496 0.30940 0.02762  -0.05662 -0.03705 443 ARG A C   
3302 O O   . ARG A 440 ? 0.26758 0.19819 0.33652 0.02922  -0.06239 -0.03985 443 ARG A O   
3303 C CB  . ARG A 440 ? 0.26081 0.20574 0.32686 0.02848  -0.05280 -0.03127 443 ARG A CB  
3304 C CG  . ARG A 440 ? 0.35266 0.30255 0.42141 0.03184  -0.04982 -0.03293 443 ARG A CG  
3305 C CD  . ARG A 440 ? 0.35146 0.30134 0.42230 0.02884  -0.05154 -0.02518 443 ARG A CD  
3306 N NE  . ARG A 440 ? 0.39315 0.34706 0.46823 0.03197  -0.05010 -0.02663 443 ARG A NE  
3307 C CZ  . ARG A 440 ? 0.44878 0.41077 0.52012 0.03281  -0.04393 -0.02784 443 ARG A CZ  
3308 N NH1 . ARG A 440 ? 0.39872 0.36505 0.46169 0.03092  -0.03882 -0.02756 443 ARG A NH1 
3309 N NH2 . ARG A 440 ? 0.46376 0.42947 0.54048 0.03551  -0.04324 -0.02920 443 ARG A NH2 
3310 N N   . PHE A 441 ? 0.26332 0.20365 0.32105 0.02354  -0.05544 -0.03313 444 PHE A N   
3311 C CA  . PHE A 441 ? 0.26182 0.19654 0.32155 0.01980  -0.06068 -0.03060 444 PHE A CA  
3312 C C   . PHE A 441 ? 0.28814 0.22342 0.34293 0.02028  -0.06022 -0.03549 444 PHE A C   
3313 O O   . PHE A 441 ? 0.28148 0.22282 0.32976 0.02200  -0.05502 -0.03822 444 PHE A O   
3314 C CB  . PHE A 441 ? 0.23173 0.16940 0.29103 0.01426  -0.05989 -0.02152 444 PHE A CB  
3315 C CG  . PHE A 441 ? 0.23179 0.16947 0.29397 0.01357  -0.06008 -0.01666 444 PHE A CG  
3316 C CD1 . PHE A 441 ? 0.25476 0.18464 0.32370 0.01302  -0.06651 -0.01487 444 PHE A CD1 
3317 C CD2 . PHE A 441 ? 0.25564 0.20041 0.31380 0.01349  -0.05452 -0.01406 444 PHE A CD2 
3318 C CE1 . PHE A 441 ? 0.30531 0.23478 0.37668 0.01245  -0.06747 -0.01033 444 PHE A CE1 
3319 C CE2 . PHE A 441 ? 0.26913 0.21360 0.32953 0.01286  -0.05531 -0.00992 444 PHE A CE2 
3320 C CZ  . PHE A 441 ? 0.29026 0.22721 0.35711 0.01230  -0.06187 -0.00794 444 PHE A CZ  
3321 N N   . GLN A 442 ? 0.28085 0.20941 0.33868 0.01844  -0.06619 -0.03630 445 GLN A N   
3322 C CA  . GLN A 442 ? 0.24240 0.17065 0.29571 0.01840  -0.06705 -0.04076 445 GLN A CA  
3323 C C   . GLN A 442 ? 0.30624 0.24272 0.35339 0.01612  -0.06218 -0.03725 445 GLN A C   
3324 O O   . GLN A 442 ? 0.28594 0.22587 0.33478 0.01225  -0.06108 -0.03007 445 GLN A O   
3325 C CB  . GLN A 442 ? 0.24695 0.16720 0.30558 0.01510  -0.07470 -0.03975 445 GLN A CB  
3326 C CG  . GLN A 442 ? 0.36522 0.27577 0.43003 0.01750  -0.08069 -0.04408 445 GLN A CG  
3327 C CD  . GLN A 442 ? 0.45835 0.36067 0.52773 0.01388  -0.08853 -0.04347 445 GLN A CD  
3328 O OE1 . GLN A 442 ? 0.37282 0.27694 0.43923 0.01109  -0.08927 -0.04319 445 GLN A OE1 
3329 N NE2 . GLN A 442 ? 0.36405 0.25709 0.44125 0.01369  -0.09492 -0.04294 445 GLN A NE2 
3330 N N   . GLU A 443 ? 0.27511 0.21466 0.31502 0.01853  -0.05942 -0.04250 446 GLU A N   
3331 C CA  . GLU A 443 ? 0.22617 0.17259 0.25992 0.01711  -0.05552 -0.04015 446 GLU A CA  
3332 C C   . GLU A 443 ? 0.23042 0.18353 0.26326 0.01668  -0.04973 -0.03497 446 GLU A C   
3333 O O   . GLU A 443 ? 0.23690 0.19524 0.26663 0.01501  -0.04702 -0.03165 446 GLU A O   
3334 C CB  . GLU A 443 ? 0.30633 0.25232 0.34223 0.01283  -0.05934 -0.03645 446 GLU A CB  
3335 C CG  . GLU A 443 ? 0.42929 0.36878 0.46564 0.01256  -0.06562 -0.04126 446 GLU A CG  
3336 C CD  . GLU A 443 ? 0.58032 0.52069 0.61974 0.00797  -0.06938 -0.03712 446 GLU A CD  
3337 O OE1 . GLU A 443 ? 0.54229 0.48902 0.58380 0.00525  -0.06667 -0.03072 446 GLU A OE1 
3338 O OE2 . GLU A 443 ? 0.56804 0.50288 0.60831 0.00714  -0.07520 -0.04063 446 GLU A OE2 
3339 N N   . GLY A 444 ? 0.25782 0.21064 0.29360 0.01828  -0.04816 -0.03443 447 GLY A N   
3340 C CA  . GLY A 444 ? 0.26179 0.21989 0.29739 0.01719  -0.04378 -0.02912 447 GLY A CA  
3341 C C   . GLY A 444 ? 0.26119 0.22561 0.28989 0.01858  -0.03813 -0.02998 447 GLY A C   
3342 O O   . GLY A 444 ? 0.25792 0.22313 0.28260 0.02162  -0.03627 -0.03523 447 GLY A O   
3343 N N   . ARG A 445 ? 0.23686 0.20585 0.26421 0.01629  -0.03536 -0.02492 448 ARG A N   
3344 C CA  . ARG A 445 ? 0.23454 0.20871 0.25605 0.01727  -0.03050 -0.02486 448 ARG A CA  
3345 C C   . ARG A 445 ? 0.21022 0.18717 0.23286 0.01713  -0.02713 -0.02167 448 ARG A C   
3346 O O   . ARG A 445 ? 0.22144 0.19814 0.24493 0.01926  -0.02608 -0.02388 448 ARG A O   
3347 C CB  . ARG A 445 ? 0.20545 0.18200 0.22473 0.01541  -0.03064 -0.02267 448 ARG A CB  
3348 C CG  . ARG A 445 ? 0.23728 0.21096 0.25433 0.01575  -0.03436 -0.02650 448 ARG A CG  
3349 C CD  . ARG A 445 ? 0.24150 0.21580 0.25091 0.01846  -0.03230 -0.03146 448 ARG A CD  
3350 N NE  . ARG A 445 ? 0.26743 0.24633 0.27190 0.01839  -0.02827 -0.02907 448 ARG A NE  
3351 C CZ  . ARG A 445 ? 0.32584 0.30609 0.32647 0.01747  -0.02905 -0.02782 448 ARG A CZ  
3352 N NH1 . ARG A 445 ? 0.28968 0.26774 0.29058 0.01646  -0.03357 -0.02879 448 ARG A NH1 
3353 N NH2 . ARG A 445 ? 0.25566 0.23919 0.25251 0.01749  -0.02577 -0.02539 448 ARG A NH2 
3354 N N   . VAL A 446 ? 0.18482 0.16475 0.20778 0.01483  -0.02540 -0.01689 449 VAL A N   
3355 C CA  . VAL A 446 ? 0.22488 0.20726 0.24786 0.01446  -0.02240 -0.01412 449 VAL A CA  
3356 C C   . VAL A 446 ? 0.30631 0.28943 0.33224 0.01124  -0.02304 -0.00921 449 VAL A C   
3357 O O   . VAL A 446 ? 0.26128 0.24481 0.28903 0.00928  -0.02453 -0.00763 449 VAL A O   
3358 C CB  . VAL A 446 ? 0.35016 0.33654 0.36816 0.01533  -0.01805 -0.01412 449 VAL A CB  
3359 C CG1 . VAL A 446 ? 0.27552 0.26233 0.28994 0.01790  -0.01655 -0.01833 449 VAL A CG1 
3360 C CG2 . VAL A 446 ? 0.38560 0.37386 0.40200 0.01423  -0.01765 -0.01261 449 VAL A CG2 
3361 N N   . ASP A 447 ? 0.22833 0.21204 0.25475 0.01048  -0.02194 -0.00679 450 ASP A N   
3362 C CA  . ASP A 447 ? 0.27256 0.25872 0.29920 0.00742  -0.02073 -0.00228 450 ASP A CA  
3363 C C   . ASP A 447 ? 0.23419 0.22338 0.25704 0.00815  -0.01681 -0.00198 450 ASP A C   
3364 O O   . ASP A 447 ? 0.27103 0.26052 0.29179 0.01058  -0.01528 -0.00470 450 ASP A O   
3365 C CB  . ASP A 447 ? 0.29433 0.27738 0.32445 0.00494  -0.02419 0.00091  450 ASP A CB  
3366 C CG  . ASP A 447 ? 0.33884 0.32479 0.36940 0.00079  -0.02346 0.00566  450 ASP A CG  
3367 O OD1 . ASP A 447 ? 0.24963 0.24046 0.27825 0.00031  -0.01982 0.00608  450 ASP A OD1 
3368 O OD2 . ASP A 447 ? 0.26772 0.25119 0.30081 -0.00207 -0.02656 0.00900  450 ASP A OD2 
3369 N N   . ASN A 448 ? 0.25256 0.24422 0.27431 0.00582  -0.01510 0.00120  451 ASN A N   
3370 C CA  . ASN A 448 ? 0.21323 0.20745 0.23120 0.00622  -0.01161 0.00125  451 ASN A CA  
3371 C C   . ASN A 448 ? 0.21796 0.21111 0.23504 0.00505  -0.01240 0.00315  451 ASN A C   
3372 O O   . ASN A 448 ? 0.20762 0.20007 0.22553 0.00236  -0.01420 0.00629  451 ASN A O   
3373 C CB  . ASN A 448 ? 0.20368 0.20181 0.22066 0.00473  -0.00890 0.00262  451 ASN A CB  
3374 C CG  . ASN A 448 ? 0.23908 0.23900 0.25231 0.00561  -0.00563 0.00175  451 ASN A CG  
3375 O OD1 . ASN A 448 ? 0.20521 0.20373 0.21666 0.00740  -0.00524 0.00006  451 ASN A OD1 
3376 N ND2 . ASN A 448 ? 0.23218 0.23540 0.24453 0.00438  -0.00319 0.00261  451 ASN A ND2 
3377 N N   . ILE A 449 ? 0.22661 0.21989 0.24194 0.00665  -0.01123 0.00164  452 ILE A N   
3378 C CA  . ILE A 449 ? 0.20933 0.20239 0.22321 0.00541  -0.01175 0.00343  452 ILE A CA  
3379 C C   . ILE A 449 ? 0.21026 0.20593 0.21949 0.00427  -0.00844 0.00388  452 ILE A C   
3380 O O   . ILE A 449 ? 0.22378 0.22055 0.23153 0.00589  -0.00599 0.00170  452 ILE A O   
3381 C CB  . ILE A 449 ? 0.23617 0.22854 0.25190 0.00769  -0.01249 0.00135  452 ILE A CB  
3382 C CG1 . ILE A 449 ? 0.16597 0.15573 0.18688 0.00928  -0.01583 0.00017  452 ILE A CG1 
3383 C CG2 . ILE A 449 ? 0.21582 0.20851 0.22999 0.00635  -0.01311 0.00312  452 ILE A CG2 
3384 C CD1 . ILE A 449 ? 0.22063 0.21148 0.24406 0.01235  -0.01515 -0.00340 452 ILE A CD1 
3385 N N   . ARG A 450 ? 0.19866 0.19519 0.20533 0.00138  -0.00842 0.00661  453 ARG A N   
3386 C CA  . ARG A 450 ? 0.18995 0.18908 0.19207 0.00049  -0.00508 0.00619  453 ARG A CA  
3387 C C   . ARG A 450 ? 0.25764 0.25577 0.25651 0.00021  -0.00550 0.00598  453 ARG A C   
3388 O O   . ARG A 450 ? 0.23358 0.23135 0.22954 -0.00229 -0.00696 0.00832  453 ARG A O   
3389 C CB  . ARG A 450 ? 0.19682 0.19850 0.19721 -0.00264 -0.00410 0.00871  453 ARG A CB  
3390 C CG  . ARG A 450 ? 0.25756 0.26163 0.26180 -0.00212 -0.00279 0.00817  453 ARG A CG  
3391 C CD  . ARG A 450 ? 0.25388 0.26201 0.25761 -0.00549 -0.00121 0.01071  453 ARG A CD  
3392 N NE  . ARG A 450 ? 0.24505 0.25608 0.25360 -0.00451 0.00001  0.00965  453 ARG A NE  
3393 C CZ  . ARG A 450 ? 0.25736 0.27225 0.26653 -0.00287 0.00346  0.00716  453 ARG A CZ  
3394 N NH1 . ARG A 450 ? 0.20027 0.21643 0.20522 -0.00208 0.00637  0.00517  453 ARG A NH1 
3395 N NH2 . ARG A 450 ? 0.23416 0.25141 0.24872 -0.00187 0.00356  0.00647  453 ARG A NH2 
3396 N N   . SER A 451 ? 0.20611 0.20379 0.20531 0.00243  -0.00447 0.00343  454 SER A N   
3397 C CA  . SER A 451 ? 0.20815 0.20493 0.20583 0.00213  -0.00546 0.00321  454 SER A CA  
3398 C C   . SER A 451 ? 0.17076 0.16795 0.16262 0.00031  -0.00413 0.00305  454 SER A C   
3399 O O   . SER A 451 ? 0.22587 0.22210 0.21602 -0.00064 -0.00573 0.00326  454 SER A O   
3400 C CB  . SER A 451 ? 0.24228 0.23896 0.24223 0.00446  -0.00450 0.00086  454 SER A CB  
3401 O OG  . SER A 451 ? 0.26338 0.26003 0.26776 0.00623  -0.00536 0.00028  454 SER A OG  
3402 N N   . ALA A 452 ? 0.20725 0.20609 0.19632 -0.00015 -0.00137 0.00233  455 ALA A N   
3403 C CA  . ALA A 452 ? 0.22004 0.21943 0.20310 -0.00167 0.00019  0.00131  455 ALA A CA  
3404 C C   . ALA A 452 ? 0.24551 0.24582 0.22450 -0.00511 -0.00117 0.00435  455 ALA A C   
3405 O O   . ALA A 452 ? 0.25046 0.25361 0.22643 -0.00674 0.00113  0.00478  455 ALA A O   
3406 C CB  . ALA A 452 ? 0.26502 0.26632 0.24756 -0.00022 0.00397  -0.00146 455 ALA A CB  
3407 N N   . THR A 453 ? 0.20802 0.20623 0.18717 -0.00636 -0.00509 0.00668  456 THR A N   
3408 C CA  . THR A 453 ? 0.26062 0.25877 0.23621 -0.00987 -0.00761 0.01059  456 THR A CA  
3409 C C   . THR A 453 ? 0.25252 0.25117 0.21927 -0.01250 -0.00701 0.01017  456 THR A C   
3410 O O   . THR A 453 ? 0.25405 0.25203 0.21852 -0.01137 -0.00579 0.00676  456 THR A O   
3411 C CB  . THR A 453 ? 0.21079 0.20614 0.19080 -0.00984 -0.01281 0.01318  456 THR A CB  
3412 O OG1 . THR A 453 ? 0.23669 0.23095 0.21640 -0.00908 -0.01419 0.01149  456 THR A OG1 
3413 C CG2 . THR A 453 ? 0.24086 0.23553 0.22928 -0.00688 -0.01339 0.01258  456 THR A CG2 
3414 N N   . PRO A 454 ? 0.25987 0.25939 0.22110 -0.01632 -0.00814 0.01368  457 PRO A N   
3415 C CA  . PRO A 454 ? 0.26242 0.26203 0.21402 -0.01924 -0.00843 0.01349  457 PRO A CA  
3416 C C   . PRO A 454 ? 0.29147 0.28759 0.24304 -0.01904 -0.01293 0.01336  457 PRO A C   
3417 O O   . PRO A 454 ? 0.27911 0.27467 0.22458 -0.01974 -0.01255 0.01069  457 PRO A O   
3418 C CB  . PRO A 454 ? 0.34082 0.34161 0.28751 -0.02382 -0.00996 0.01881  457 PRO A CB  
3419 C CG  . PRO A 454 ? 0.34548 0.34837 0.29870 -0.02306 -0.00791 0.02014  457 PRO A CG  
3420 C CD  . PRO A 454 ? 0.29270 0.29319 0.25559 -0.01858 -0.00908 0.01804  457 PRO A CD  
3421 N N   . GLU A 455 ? 0.25547 0.24940 0.21441 -0.01799 -0.01730 0.01585  458 GLU A N   
3422 C CA  . GLU A 455 ? 0.25599 0.24771 0.21694 -0.01766 -0.02166 0.01579  458 GLU A CA  
3423 C C   . GLU A 455 ? 0.25616 0.24799 0.22024 -0.01473 -0.01919 0.01106  458 GLU A C   
3424 O O   . GLU A 455 ? 0.23676 0.22746 0.19846 -0.01552 -0.02100 0.00969  458 GLU A O   
3425 C CB  . GLU A 455 ? 0.20823 0.19844 0.17785 -0.01665 -0.02645 0.01904  458 GLU A CB  
3426 C CG  . GLU A 455 ? 0.32421 0.31284 0.29059 -0.02020 -0.03071 0.02467  458 GLU A CG  
3427 C CD  . GLU A 455 ? 0.38184 0.37124 0.34866 -0.02094 -0.02838 0.02664  458 GLU A CD  
3428 O OE1 . GLU A 455 ? 0.27353 0.26481 0.24379 -0.01838 -0.02377 0.02354  458 GLU A OE1 
3429 O OE2 . GLU A 455 ? 0.40835 0.39635 0.37231 -0.02438 -0.03164 0.03169  458 GLU A OE2 
3430 N N   . ALA A 456 ? 0.23041 0.22332 0.19965 -0.01170 -0.01547 0.00883  459 ALA A N   
3431 C CA  . ALA A 456 ? 0.24121 0.23386 0.21262 -0.00941 -0.01314 0.00495  459 ALA A CA  
3432 C C   . ALA A 456 ? 0.23878 0.23080 0.20234 -0.01047 -0.01085 0.00189  459 ALA A C   
3433 O O   . ALA A 456 ? 0.25189 0.24218 0.21505 -0.01024 -0.01142 -0.00045 459 ALA A O   
3434 C CB  . ALA A 456 ? 0.22578 0.21950 0.20279 -0.00634 -0.00985 0.00355  459 ALA A CB  
3435 N N   . LEU A 457 ? 0.28134 0.27492 0.23885 -0.01172 -0.00823 0.00168  460 LEU A N   
3436 C CA  . LEU A 457 ? 0.27416 0.26749 0.22399 -0.01246 -0.00585 -0.00204 460 LEU A CA  
3437 C C   . LEU A 457 ? 0.26962 0.26073 0.21292 -0.01537 -0.00971 -0.00179 460 LEU A C   
3438 O O   . LEU A 457 ? 0.25173 0.24053 0.19208 -0.01517 -0.00976 -0.00549 460 LEU A O   
3439 C CB  . LEU A 457 ? 0.30247 0.29942 0.24754 -0.01344 -0.00187 -0.00226 460 LEU A CB  
3440 C CG  . LEU A 457 ? 0.34561 0.34296 0.28312 -0.01355 0.00133  -0.00726 460 LEU A CG  
3441 C CD1 . LEU A 457 ? 0.32638 0.32161 0.26873 -0.00966 0.00331  -0.01198 460 LEU A CD1 
3442 C CD2 . LEU A 457 ? 0.35650 0.35911 0.28927 -0.01494 0.00581  -0.00751 460 LEU A CD2 
3443 N N   . ALA A 458 ? 0.24855 0.23984 0.18955 -0.01826 -0.01358 0.00266  461 ALA A N   
3444 C CA  . ALA A 458 ? 0.25876 0.24792 0.19339 -0.02124 -0.01802 0.00322  461 ALA A CA  
3445 C C   . ALA A 458 ? 0.31542 0.30225 0.25622 -0.01993 -0.02101 0.00176  461 ALA A C   
3446 O O   . ALA A 458 ? 0.27136 0.25597 0.20729 -0.02134 -0.02282 -0.00072 461 ALA A O   
3447 C CB  . ALA A 458 ? 0.29874 0.28800 0.23155 -0.02437 -0.02274 0.00911  461 ALA A CB  
3448 N N   . PHE A 459 ? 0.24479 0.23234 0.19628 -0.01741 -0.02141 0.00307  462 PHE A N   
3449 C CA  . PHE A 459 ? 0.24058 0.22728 0.19896 -0.01648 -0.02371 0.00215  462 PHE A CA  
3450 C C   . PHE A 459 ? 0.29725 0.28216 0.25475 -0.01526 -0.02066 -0.00237 462 PHE A C   
3451 O O   . PHE A 459 ? 0.26253 0.24537 0.21927 -0.01658 -0.02313 -0.00389 462 PHE A O   
3452 C CB  . PHE A 459 ? 0.20409 0.19289 0.17352 -0.01401 -0.02397 0.00418  462 PHE A CB  
3453 C CG  . PHE A 459 ? 0.26075 0.25021 0.23796 -0.01288 -0.02461 0.00297  462 PHE A CG  
3454 C CD1 . PHE A 459 ? 0.27156 0.26089 0.25051 -0.01487 -0.02919 0.00367  462 PHE A CD1 
3455 C CD2 . PHE A 459 ? 0.22688 0.21745 0.20959 -0.01024 -0.02084 0.00145  462 PHE A CD2 
3456 C CE1 . PHE A 459 ? 0.30885 0.29979 0.29574 -0.01432 -0.02951 0.00288  462 PHE A CE1 
3457 C CE2 . PHE A 459 ? 0.26011 0.25202 0.24973 -0.00982 -0.02113 0.00087  462 PHE A CE2 
3458 C CZ  . PHE A 459 ? 0.24751 0.23986 0.23944 -0.01191 -0.02518 0.00157  462 PHE A CZ  
3459 N N   . VAL A 460 ? 0.25556 0.24089 0.21376 -0.01281 -0.01583 -0.00440 463 VAL A N   
3460 C CA  . VAL A 460 ? 0.22103 0.20388 0.17964 -0.01140 -0.01370 -0.00825 463 VAL A CA  
3461 C C   . VAL A 460 ? 0.26282 0.24275 0.21238 -0.01291 -0.01384 -0.01199 463 VAL A C   
3462 O O   . VAL A 460 ? 0.29094 0.26732 0.24057 -0.01291 -0.01467 -0.01485 463 VAL A O   
3463 C CB  . VAL A 460 ? 0.25207 0.23592 0.21406 -0.00825 -0.00919 -0.00936 463 VAL A CB  
3464 C CG1 . VAL A 460 ? 0.23986 0.22636 0.20962 -0.00688 -0.00923 -0.00622 463 VAL A CG1 
3465 C CG2 . VAL A 460 ? 0.23821 0.22371 0.19442 -0.00797 -0.00595 -0.01069 463 VAL A CG2 
3466 N N   . ARG A 461 ? 0.28812 0.26934 0.22952 -0.01439 -0.01301 -0.01221 464 ARG A N   
3467 C CA  . ARG A 461 ? 0.29816 0.27691 0.22998 -0.01590 -0.01307 -0.01640 464 ARG A CA  
3468 C C   . ARG A 461 ? 0.29450 0.27038 0.22379 -0.01893 -0.01877 -0.01587 464 ARG A C   
3469 O O   . ARG A 461 ? 0.30401 0.27591 0.22967 -0.01948 -0.01995 -0.02000 464 ARG A O   
3470 C CB  . ARG A 461 ? 0.28806 0.26994 0.21098 -0.01736 -0.01054 -0.01645 464 ARG A CB  
3471 C CG  . ARG A 461 ? 0.39571 0.38099 0.32067 -0.01464 -0.00465 -0.01796 464 ARG A CG  
3472 C CD  . ARG A 461 ? 0.47143 0.46102 0.38818 -0.01712 -0.00244 -0.01670 464 ARG A CD  
3473 N NE  . ARG A 461 ? 0.72570 0.71865 0.64128 -0.01499 0.00363  -0.02087 464 ARG A NE  
3474 C CZ  . ARG A 461 ? 0.72848 0.72690 0.63920 -0.01662 0.00726  -0.02003 464 ARG A CZ  
3475 N NH1 . ARG A 461 ? 0.56657 0.56699 0.47249 -0.02069 0.00519  -0.01456 464 ARG A NH1 
3476 N NH2 . ARG A 461 ? 0.70001 0.70217 0.61127 -0.01422 0.01294  -0.02456 464 ARG A NH2 
3477 N N   . ALA A 462 ? 0.28524 0.26287 0.21686 -0.02089 -0.02283 -0.01095 465 ALA A N   
3478 C CA  . ALA A 462 ? 0.26580 0.24133 0.19651 -0.02376 -0.02887 -0.01009 465 ALA A CA  
3479 C C   . ALA A 462 ? 0.26956 0.24282 0.20805 -0.02291 -0.03004 -0.01181 465 ALA A C   
3480 O O   . ALA A 462 ? 0.32452 0.29435 0.25990 -0.02501 -0.03347 -0.01411 465 ALA A O   
3481 C CB  . ALA A 462 ? 0.30784 0.28596 0.24271 -0.02521 -0.03325 -0.00429 465 ALA A CB  
3482 N N   . VAL A 463 ? 0.27901 0.25410 0.22734 -0.02022 -0.02745 -0.01059 466 VAL A N   
3483 C CA  . VAL A 463 ? 0.31748 0.29126 0.27362 -0.02001 -0.02842 -0.01113 466 VAL A CA  
3484 C C   . VAL A 463 ? 0.45003 0.41859 0.40214 -0.01956 -0.02686 -0.01598 466 VAL A C   
3485 O O   . VAL A 463 ? 0.43652 0.40180 0.39020 -0.02136 -0.02989 -0.01721 466 VAL A O   
3486 C CB  . VAL A 463 ? 0.32182 0.29927 0.28806 -0.01747 -0.02570 -0.00858 466 VAL A CB  
3487 C CG1 . VAL A 463 ? 0.32977 0.30594 0.30254 -0.01757 -0.02561 -0.00918 466 VAL A CG1 
3488 C CG2 . VAL A 463 ? 0.25968 0.24164 0.23174 -0.01783 -0.02834 -0.00445 466 VAL A CG2 
3489 N N   . THR A 464 ? 0.30645 0.27410 0.25401 -0.01717 -0.02244 -0.01887 467 THR A N   
3490 C CA  . THR A 464 ? 0.40222 0.36486 0.34834 -0.01568 -0.02077 -0.02355 467 THR A CA  
3491 C C   . THR A 464 ? 0.47025 0.42883 0.40613 -0.01686 -0.02184 -0.02876 467 THR A C   
3492 O O   . THR A 464 ? 0.50402 0.45701 0.43921 -0.01623 -0.02233 -0.03300 467 THR A O   
3493 C CB  . THR A 464 ? 0.43570 0.39977 0.38414 -0.01189 -0.01555 -0.02438 467 THR A CB  
3494 O OG1 . THR A 464 ? 0.48721 0.45507 0.43003 -0.01136 -0.01282 -0.02462 467 THR A OG1 
3495 C CG2 . THR A 464 ? 0.37411 0.34132 0.33191 -0.01069 -0.01459 -0.01999 467 THR A CG2 
3496 N N   . ASP A 465 ? 0.45635 0.41722 0.38393 -0.01866 -0.02243 -0.02865 468 ASP A N   
3497 C CA  . ASP A 465 ? 0.49628 0.45413 0.41248 -0.01969 -0.02256 -0.03418 468 ASP A CA  
3498 C C   . ASP A 465 ? 0.48633 0.44030 0.39946 -0.02347 -0.02899 -0.03451 468 ASP A C   
3499 O O   . ASP A 465 ? 0.48590 0.44188 0.39426 -0.02660 -0.03248 -0.03167 468 ASP A O   
3500 C CB  . ASP A 465 ? 0.51362 0.47642 0.42147 -0.02030 -0.01966 -0.03351 468 ASP A CB  
3501 C CG  . ASP A 465 ? 0.63805 0.59901 0.53287 -0.02156 -0.01902 -0.03940 468 ASP A CG  
3502 O OD1 . ASP A 465 ? 0.58523 0.54037 0.47746 -0.02148 -0.02092 -0.04483 468 ASP A OD1 
3503 O OD2 . ASP A 465 ? 0.48349 0.44892 0.37037 -0.02286 -0.01663 -0.03858 468 ASP A OD2 
3504 N N   . HIS A 466 ? 0.54100 0.48903 0.45729 -0.02342 -0.03117 -0.03768 469 HIS A N   
3505 C CA  . HIS A 466 ? 0.62851 0.57296 0.54410 -0.02729 -0.03781 -0.03752 469 HIS A CA  
3506 C C   . HIS A 466 ? 0.57100 0.51363 0.47297 -0.02994 -0.04042 -0.04114 469 HIS A C   
3507 O O   . HIS A 466 ? 0.58088 0.52369 0.48074 -0.03373 -0.04616 -0.03865 469 HIS A O   
3508 C CB  . HIS A 466 ? 0.72540 0.66313 0.64659 -0.02705 -0.03963 -0.04038 469 HIS A CB  
3509 C CG  . HIS A 466 ? 0.82398 0.76355 0.75774 -0.02555 -0.03791 -0.03604 469 HIS A CG  
3510 N ND1 . HIS A 466 ? 0.85713 0.79313 0.79485 -0.02250 -0.03484 -0.03813 469 HIS A ND1 
3511 C CD2 . HIS A 466 ? 0.81946 0.76437 0.76238 -0.02663 -0.03878 -0.02984 469 HIS A CD2 
3512 C CE1 . HIS A 466 ? 0.90373 0.84267 0.85141 -0.02222 -0.03393 -0.03307 469 HIS A CE1 
3513 N NE2 . HIS A 466 ? 0.89491 0.83955 0.84597 -0.02458 -0.03594 -0.02834 469 HIS A NE2 
3514 N N   . LYS A 467 ? 0.51377 0.45507 0.40637 -0.02805 -0.03632 -0.04709 470 LYS A N   
3515 C CA  . LYS A 467 ? 0.74486 0.68427 0.62305 -0.03070 -0.03842 -0.05145 470 LYS A CA  
3516 C C   . LYS A 467 ? 0.76424 0.70946 0.63595 -0.03375 -0.03974 -0.04607 470 LYS A C   
3517 O O   . LYS A 467 ? 0.65666 0.60028 0.51849 -0.03761 -0.04458 -0.04667 470 LYS A O   
3518 C CB  . LYS A 467 ? 0.62335 0.56122 0.49364 -0.02758 -0.03281 -0.05959 470 LYS A CB  
3519 C CG  . LYS A 467 ? 0.68296 0.62839 0.54866 -0.02596 -0.02606 -0.05873 470 LYS A CG  
3520 N N   . ALA A 468 ? 0.53755 0.48897 0.41482 -0.03231 -0.03620 -0.04053 471 ALA A N   
3521 C CA  . ALA A 468 ? 0.44068 0.39679 0.31361 -0.03527 -0.03831 -0.03444 471 ALA A CA  
3522 C C   . ALA A 468 ? 0.51429 0.46947 0.39227 -0.03848 -0.04632 -0.02948 471 ALA A C   
3523 O O   . ALA A 468 ? 0.47954 0.43615 0.35081 -0.04194 -0.05061 -0.02585 471 ALA A O   
3524 C CB  . ALA A 468 ? 0.47014 0.43210 0.34993 -0.03282 -0.03334 -0.02975 471 ALA A CB  
3525 N N   . ALA A 469 ? 0.43975 0.39296 0.32987 -0.03757 -0.04858 -0.02893 472 ALA A N   
3526 C CA  . ALA A 469 ? 0.41728 0.37012 0.31316 -0.04071 -0.05623 -0.02518 472 ALA A CA  
3527 C C   . ALA A 469 ? 0.35585 0.31409 0.25583 -0.04170 -0.05881 -0.01784 472 ALA A C   
3528 O O   . ALA A 469 ? 0.39632 0.35463 0.29384 -0.04515 -0.06566 -0.01493 472 ALA A O   
3529 C CB  . ALA A 469 ? 0.41339 0.36117 0.29819 -0.04459 -0.06206 -0.02904 472 ALA A CB  
3530 N N   . VAL A 470 ? 0.35821 0.32059 0.26480 -0.03862 -0.05384 -0.01488 473 VAL A N   
3531 C CA  . VAL A 470 ? 0.29561 0.26244 0.20801 -0.03893 -0.05633 -0.00817 473 VAL A CA  
3532 C C   . VAL A 470 ? 0.31585 0.28421 0.24151 -0.03952 -0.06177 -0.00518 473 VAL A C   
3533 O O   . VAL A 470 ? 0.32161 0.29040 0.25741 -0.03767 -0.05965 -0.00651 473 VAL A O   
3534 C CB  . VAL A 470 ? 0.31425 0.28457 0.23227 -0.03525 -0.04990 -0.00646 473 VAL A CB  
3535 C CG1 . VAL A 470 ? 0.33373 0.30778 0.25917 -0.03523 -0.05301 0.00006  473 VAL A CG1 
3536 C CG2 . VAL A 470 ? 0.33141 0.30147 0.23746 -0.03476 -0.04409 -0.00950 473 VAL A CG2 
3537 N N   . PRO A 471 ? 0.36305 0.33279 0.28982 -0.04205 -0.06869 -0.00089 474 PRO A N   
3538 C CA  . PRO A 471 ? 0.30316 0.27579 0.24442 -0.04232 -0.07368 0.00186  474 PRO A CA  
3539 C C   . PRO A 471 ? 0.33249 0.30995 0.28826 -0.03835 -0.06933 0.00388  474 PRO A C   
3540 O O   . PRO A 471 ? 0.28921 0.26817 0.24463 -0.03594 -0.06541 0.00547  474 PRO A O   
3541 C CB  . PRO A 471 ? 0.32822 0.30160 0.26714 -0.04511 -0.08157 0.00655  474 PRO A CB  
3542 C CG  . PRO A 471 ? 0.43082 0.40020 0.35056 -0.04777 -0.08159 0.00523  474 PRO A CG  
3543 C CD  . PRO A 471 ? 0.37770 0.34672 0.29256 -0.04494 -0.07241 0.00191  474 PRO A CD  
3544 N N   . ALA A 472 ? 0.28296 0.26314 0.25150 -0.03797 -0.07019 0.00381  475 ALA A N   
3545 C CA  . ALA A 472 ? 0.29442 0.27988 0.27656 -0.03445 -0.06615 0.00538  475 ALA A CA  
3546 C C   . ALA A 472 ? 0.24127 0.23031 0.22885 -0.03285 -0.06852 0.00961  475 ALA A C   
3547 O O   . ALA A 472 ? 0.31311 0.30460 0.30577 -0.02947 -0.06404 0.01032  475 ALA A O   
3548 C CB  . ALA A 472 ? 0.28207 0.27102 0.27694 -0.03527 -0.06750 0.00520  475 ALA A CB  
3549 N N   . SER A 473 ? 0.25988 0.24870 0.24629 -0.03530 -0.07611 0.01249  476 SER A N   
3550 C CA  . SER A 473 ? 0.32138 0.31262 0.31351 -0.03373 -0.07926 0.01677  476 SER A CA  
3551 C C   . SER A 473 ? 0.31596 0.30442 0.29831 -0.03260 -0.07534 0.01763  476 SER A C   
3552 O O   . SER A 473 ? 0.27823 0.26870 0.26751 -0.02972 -0.07409 0.01976  476 SER A O   
3553 C CB  . SER A 473 ? 0.35949 0.35010 0.35097 -0.03695 -0.08898 0.02010  476 SER A CB  
3554 O OG  . SER A 473 ? 0.31927 0.30430 0.29306 -0.04071 -0.09110 0.01971  476 SER A OG  
3555 N N   . GLU A 474 ? 0.30351 0.28762 0.27021 -0.03485 -0.07320 0.01565  477 GLU A N   
3556 C CA  . GLU A 474 ? 0.29638 0.27891 0.25409 -0.03417 -0.06873 0.01627  477 GLU A CA  
3557 C C   . GLU A 474 ? 0.31366 0.29774 0.27605 -0.03033 -0.06044 0.01348  477 GLU A C   
3558 O O   . GLU A 474 ? 0.31199 0.29677 0.27496 -0.02852 -0.05749 0.01514  477 GLU A O   
3559 C CB  . GLU A 474 ? 0.34711 0.32578 0.28707 -0.03772 -0.06853 0.01446  477 GLU A CB  
3560 C CG  . GLU A 474 ? 0.48971 0.46790 0.42007 -0.03751 -0.06307 0.01474  477 GLU A CG  
3561 C CD  . GLU A 474 ? 0.70933 0.68799 0.63997 -0.03845 -0.06656 0.02095  477 GLU A CD  
3562 O OE1 . GLU A 474 ? 0.66638 0.64405 0.59700 -0.04095 -0.07443 0.02501  477 GLU A OE1 
3563 O OE2 . GLU A 474 ? 0.65927 0.63896 0.59057 -0.03679 -0.06189 0.02195  477 GLU A OE2 
3564 N N   . LYS A 475 ? 0.28096 0.26517 0.24631 -0.02936 -0.05698 0.00948  478 LYS A N   
3565 C CA  . LYS A 475 ? 0.24695 0.23269 0.21763 -0.02582 -0.05005 0.00744  478 LYS A CA  
3566 C C   . LYS A 475 ? 0.24905 0.23896 0.23264 -0.02290 -0.05001 0.00998  478 LYS A C   
3567 O O   . LYS A 475 ? 0.27285 0.26376 0.25868 -0.02011 -0.04517 0.00955  478 LYS A O   
3568 C CB  . LYS A 475 ? 0.24514 0.23011 0.21840 -0.02574 -0.04779 0.00375  478 LYS A CB  
3569 C CG  . LYS A 475 ? 0.30116 0.28123 0.26224 -0.02757 -0.04666 -0.00016 478 LYS A CG  
3570 C CD  . LYS A 475 ? 0.27948 0.25788 0.24467 -0.02803 -0.04632 -0.00304 478 LYS A CD  
3571 C CE  . LYS A 475 ? 0.29873 0.27141 0.25268 -0.02932 -0.04554 -0.00770 478 LYS A CE  
3572 N NZ  . LYS A 475 ? 0.33060 0.30072 0.28962 -0.02966 -0.04529 -0.01012 478 LYS A NZ  
3573 N N   . LEU A 476 ? 0.26398 0.25659 0.25685 -0.02330 -0.05537 0.01214  479 LEU A N   
3574 C CA  . LEU A 476 ? 0.23958 0.23655 0.24564 -0.02005 -0.05531 0.01367  479 LEU A CA  
3575 C C   . LEU A 476 ? 0.25760 0.25302 0.26169 -0.01911 -0.05686 0.01670  479 LEU A C   
3576 O O   . LEU A 476 ? 0.24439 0.24127 0.25419 -0.01593 -0.05368 0.01652  479 LEU A O   
3577 C CB  . LEU A 476 ? 0.23066 0.23170 0.24833 -0.02056 -0.06071 0.01484  479 LEU A CB  
3578 C CG  . LEU A 476 ? 0.27081 0.27677 0.30299 -0.01702 -0.06190 0.01619  479 LEU A CG  
3579 C CD1 . LEU A 476 ? 0.21333 0.22285 0.25195 -0.01352 -0.05471 0.01351  479 LEU A CD1 
3580 C CD2 . LEU A 476 ? 0.30923 0.31988 0.35334 -0.01777 -0.06806 0.01742  479 LEU A CD2 
3581 N N   . LEU A 477 ? 0.26802 0.26018 0.26358 -0.02217 -0.06197 0.01963  480 LEU A N   
3582 C CA  . LEU A 477 ? 0.27882 0.26877 0.27090 -0.02219 -0.06339 0.02312  480 LEU A CA  
3583 C C   . LEU A 477 ? 0.27633 0.26528 0.26210 -0.02110 -0.05623 0.02142  480 LEU A C   
3584 O O   . LEU A 477 ? 0.29469 0.28347 0.28393 -0.01929 -0.05525 0.02303  480 LEU A O   
3585 C CB  . LEU A 477 ? 0.25127 0.23779 0.23230 -0.02665 -0.06945 0.02670  480 LEU A CB  
3586 C CG  . LEU A 477 ? 0.31271 0.29984 0.30001 -0.02796 -0.07803 0.02932  480 LEU A CG  
3587 C CD1 . LEU A 477 ? 0.42910 0.41220 0.40193 -0.03300 -0.08348 0.03280  480 LEU A CD1 
3588 C CD2 . LEU A 477 ? 0.36303 0.35185 0.36489 -0.02473 -0.08187 0.03209  480 LEU A CD2 
3589 N N   . LEU A 478 ? 0.26769 0.25576 0.24454 -0.02220 -0.05159 0.01807  481 LEU A N   
3590 C CA  . LEU A 478 ? 0.28354 0.27132 0.25555 -0.02095 -0.04490 0.01621  481 LEU A CA  
3591 C C   . LEU A 478 ? 0.23784 0.22804 0.22024 -0.01685 -0.04063 0.01415  481 LEU A C   
3592 O O   . LEU A 478 ? 0.27203 0.26239 0.25468 -0.01520 -0.03709 0.01418  481 LEU A O   
3593 C CB  . LEU A 478 ? 0.23416 0.22044 0.19534 -0.02260 -0.04136 0.01252  481 LEU A CB  
3594 C CG  . LEU A 478 ? 0.26692 0.25105 0.21506 -0.02679 -0.04431 0.01374  481 LEU A CG  
3595 C CD1 . LEU A 478 ? 0.31238 0.29501 0.25138 -0.02768 -0.04088 0.00873  481 LEU A CD1 
3596 C CD2 . LEU A 478 ? 0.29804 0.28228 0.23997 -0.02825 -0.04332 0.01712  481 LEU A CD2 
3597 N N   . LEU A 479 ? 0.28909 0.28146 0.27975 -0.01550 -0.04086 0.01237  482 LEU A N   
3598 C CA  . LEU A 479 ? 0.23530 0.23054 0.23526 -0.01198 -0.03694 0.01059  482 LEU A CA  
3599 C C   . LEU A 479 ? 0.28695 0.28332 0.29446 -0.00971 -0.03873 0.01264  482 LEU A C   
3600 O O   . LEU A 479 ? 0.27321 0.26993 0.28261 -0.00734 -0.03511 0.01168  482 LEU A O   
3601 C CB  . LEU A 479 ? 0.22068 0.21899 0.22847 -0.01174 -0.03735 0.00905  482 LEU A CB  
3602 C CG  . LEU A 479 ? 0.28971 0.29195 0.30647 -0.00880 -0.03311 0.00717  482 LEU A CG  
3603 C CD1 . LEU A 479 ? 0.27809 0.28319 0.30003 -0.01010 -0.03333 0.00614  482 LEU A CD1 
3604 C CD2 . LEU A 479 ? 0.36565 0.37113 0.39233 -0.00606 -0.03455 0.00805  482 LEU A CD2 
3605 N N   . LYS A 480 ? 0.24168 0.23830 0.25400 -0.01032 -0.04485 0.01535  483 LYS A N   
3606 C CA  . LYS A 480 ? 0.26286 0.25993 0.28376 -0.00775 -0.04724 0.01689  483 LYS A CA  
3607 C C   . LYS A 480 ? 0.26323 0.25643 0.27749 -0.00857 -0.04718 0.01926  483 LYS A C   
3608 O O   . LYS A 480 ? 0.24705 0.24001 0.26675 -0.00598 -0.04632 0.01903  483 LYS A O   
3609 C CB  . LYS A 480 ? 0.31548 0.31358 0.34424 -0.00800 -0.05448 0.01929  483 LYS A CB  
3610 C CG  . LYS A 480 ? 0.32473 0.32849 0.36423 -0.00644 -0.05407 0.01677  483 LYS A CG  
3611 C CD  . LYS A 480 ? 0.38230 0.39012 0.42927 -0.00261 -0.04787 0.01305  483 LYS A CD  
3612 C CE  . LYS A 480 ? 0.33762 0.35221 0.39527 -0.00161 -0.04686 0.01088  483 LYS A CE  
3613 N NZ  . LYS A 480 ? 0.30691 0.32445 0.37619 -0.00043 -0.05310 0.01229  483 LYS A NZ  
3614 N N   . ASP A 481 ? 0.24774 0.23818 0.25022 -0.01232 -0.04789 0.02134  484 ASP A N   
3615 C CA  . ASP A 481 ? 0.25851 0.24637 0.25465 -0.01368 -0.04698 0.02375  484 ASP A CA  
3616 C C   . ASP A 481 ? 0.30156 0.29057 0.29650 -0.01179 -0.03995 0.02058  484 ASP A C   
3617 O O   . ASP A 481 ? 0.27871 0.26664 0.27441 -0.01131 -0.03912 0.02186  484 ASP A O   
3618 C CB  . ASP A 481 ? 0.29259 0.27844 0.27568 -0.01845 -0.04863 0.02644  484 ASP A CB  
3619 C CG  . ASP A 481 ? 0.40337 0.38708 0.38106 -0.02082 -0.04925 0.03054  484 ASP A CG  
3620 O OD1 . ASP A 481 ? 0.45432 0.43625 0.43926 -0.01970 -0.05281 0.03335  484 ASP A OD1 
3621 O OD2 . ASP A 481 ? 0.40977 0.39367 0.37625 -0.02393 -0.04631 0.03093  484 ASP A OD2 
3622 N N   . ALA A 482 ? 0.22786 0.21869 0.22114 -0.01090 -0.03535 0.01670  485 ALA A N   
3623 C CA  . ALA A 482 ? 0.22592 0.21768 0.21902 -0.00886 -0.02945 0.01399  485 ALA A CA  
3624 C C   . ALA A 482 ? 0.21029 0.20334 0.21357 -0.00523 -0.02897 0.01283  485 ALA A C   
3625 O O   . ALA A 482 ? 0.21724 0.21000 0.22129 -0.00388 -0.02654 0.01233  485 ALA A O   
3626 C CB  . ALA A 482 ? 0.24835 0.24091 0.23765 -0.00874 -0.02541 0.01041  485 ALA A CB  
3627 N N   . ILE A 483 ? 0.23026 0.22518 0.24159 -0.00363 -0.03118 0.01206  486 ILE A N   
3628 C CA  . ILE A 483 ? 0.23266 0.22943 0.25354 -0.00001 -0.03050 0.01029  486 ILE A CA  
3629 C C   . ILE A 483 ? 0.21685 0.21092 0.24098 0.00065  -0.03420 0.01257  486 ILE A C   
3630 O O   . ILE A 483 ? 0.23702 0.23076 0.26458 0.00301  -0.03254 0.01102  486 ILE A O   
3631 C CB  . ILE A 483 ? 0.25932 0.25999 0.28868 0.00138  -0.03162 0.00879  486 ILE A CB  
3632 C CG1 . ILE A 483 ? 0.21908 0.22206 0.24583 0.00098  -0.02685 0.00628  486 ILE A CG1 
3633 C CG2 . ILE A 483 ? 0.26772 0.27073 0.30793 0.00527  -0.03201 0.00693  486 ILE A CG2 
3634 C CD1 . ILE A 483 ? 0.32228 0.32994 0.35687 0.00142  -0.02717 0.00508  486 ILE A CD1 
3635 N N   . ARG A 484 ? 0.21720 0.20877 0.23985 -0.00170 -0.03970 0.01647  487 ARG A N   
3636 C CA  . ARG A 484 ? 0.24925 0.23710 0.27423 -0.00185 -0.04400 0.01959  487 ARG A CA  
3637 C C   . ARG A 484 ? 0.20624 0.19220 0.22517 -0.00310 -0.04086 0.02028  487 ARG A C   
3638 O O   . ARG A 484 ? 0.25130 0.23540 0.27503 -0.00135 -0.04155 0.02003  487 ARG A O   
3639 C CB  . ARG A 484 ? 0.28342 0.26856 0.30546 -0.00519 -0.05056 0.02456  487 ARG A CB  
3640 C CG  . ARG A 484 ? 0.32508 0.30554 0.35045 -0.00561 -0.05618 0.02859  487 ARG A CG  
3641 C CD  . ARG A 484 ? 0.38082 0.35780 0.39818 -0.01063 -0.06156 0.03481  487 ARG A CD  
3642 N NE  . ARG A 484 ? 0.41876 0.39693 0.42291 -0.01452 -0.05696 0.03538  487 ARG A NE  
3643 C CZ  . ARG A 484 ? 0.45021 0.42818 0.44877 -0.01611 -0.05286 0.03589  487 ARG A CZ  
3644 N NH1 . ARG A 484 ? 0.31772 0.29355 0.32186 -0.01478 -0.05335 0.03655  487 ARG A NH1 
3645 N NH2 . ARG A 484 ? 0.35279 0.33295 0.34052 -0.01899 -0.04824 0.03538  487 ARG A NH2 
3646 N N   . ALA A 485 ? 0.23301 0.21958 0.24189 -0.00611 -0.03756 0.02092  488 ALA A N   
3647 C CA  . ALA A 485 ? 0.26520 0.25131 0.26915 -0.00744 -0.03422 0.02152  488 ALA A CA  
3648 C C   . ALA A 485 ? 0.26273 0.25036 0.27110 -0.00397 -0.02990 0.01745  488 ALA A C   
3649 O O   . ALA A 485 ? 0.25755 0.24402 0.26700 -0.00392 -0.02941 0.01802  488 ALA A O   
3650 C CB  . ALA A 485 ? 0.23541 0.22304 0.22864 -0.01067 -0.03087 0.02185  488 ALA A CB  
3651 N N   . GLN A 486 ? 0.18332 0.17350 0.19393 -0.00149 -0.02700 0.01363  489 GLN A N   
3652 C CA  . GLN A 486 ? 0.20379 0.19547 0.21764 0.00155  -0.02317 0.00998  489 GLN A CA  
3653 C C   . GLN A 486 ? 0.22219 0.21259 0.24404 0.00422  -0.02567 0.00911  489 GLN A C   
3654 O O   . GLN A 486 ? 0.23451 0.22413 0.25733 0.00537  -0.02432 0.00784  489 GLN A O   
3655 C CB  . GLN A 486 ? 0.19560 0.19015 0.21001 0.00292  -0.02024 0.00695  489 GLN A CB  
3656 C CG  . GLN A 486 ? 0.21735 0.21361 0.23431 0.00571  -0.01652 0.00355  489 GLN A CG  
3657 C CD  . GLN A 486 ? 0.24278 0.23848 0.25464 0.00525  -0.01331 0.00315  489 GLN A CD  
3658 O OE1 . GLN A 486 ? 0.30816 0.30349 0.31436 0.00317  -0.01225 0.00426  489 GLN A OE1 
3659 N NE2 . GLN A 486 ? 0.23893 0.23489 0.25297 0.00731  -0.01181 0.00123  489 GLN A NE2 
3660 N N   . THR A 487 ? 0.23987 0.23001 0.26799 0.00536  -0.02967 0.00949  490 THR A N   
3661 C CA  . THR A 487 ? 0.23228 0.22089 0.26898 0.00837  -0.03260 0.00810  490 THR A CA  
3662 C C   . THR A 487 ? 0.22621 0.20988 0.26236 0.00682  -0.03608 0.01117  490 THR A C   
3663 O O   . THR A 487 ? 0.19794 0.17971 0.23814 0.00889  -0.03651 0.00917  490 THR A O   
3664 C CB  . THR A 487 ? 0.28000 0.26958 0.32421 0.00977  -0.03675 0.00829  490 THR A CB  
3665 O OG1 . THR A 487 ? 0.27638 0.27116 0.32178 0.01072  -0.03339 0.00566  490 THR A OG1 
3666 C CG2 . THR A 487 ? 0.26836 0.25631 0.32272 0.01357  -0.04003 0.00609  490 THR A CG2 
3667 N N   . ALA A 488 ? 0.21977 0.20130 0.25063 0.00283  -0.03872 0.01613  491 ALA A N   
3668 C CA  . ALA A 488 ? 0.26747 0.24465 0.29724 0.00030  -0.04196 0.02004  491 ALA A CA  
3669 C C   . ALA A 488 ? 0.23366 0.21154 0.26044 -0.00016 -0.03777 0.01874  491 ALA A C   
3670 O O   . ALA A 488 ? 0.21202 0.18660 0.24243 0.00004  -0.04001 0.01917  491 ALA A O   
3671 C CB  . ALA A 488 ? 0.25573 0.23172 0.27839 -0.00462 -0.04455 0.02579  491 ALA A CB  
3672 N N   . TYR A 489 ? 0.22188 0.20372 0.24256 -0.00083 -0.03221 0.01718  492 TYR A N   
3673 C CA  . TYR A 489 ? 0.22850 0.21157 0.24734 -0.00099 -0.02850 0.01585  492 TYR A CA  
3674 C C   . TYR A 489 ? 0.22625 0.20876 0.25094 0.00299  -0.02806 0.01145  492 TYR A C   
3675 O O   . TYR A 489 ? 0.22664 0.20766 0.25284 0.00291  -0.02840 0.01114  492 TYR A O   
3676 C CB  . TYR A 489 ? 0.20728 0.19455 0.21963 -0.00172 -0.02299 0.01447  492 TYR A CB  
3677 C CG  . TYR A 489 ? 0.24414 0.23306 0.25380 -0.00358 -0.02019 0.01527  492 TYR A CG  
3678 C CD1 . TYR A 489 ? 0.21336 0.20216 0.22675 -0.00174 -0.01938 0.01309  492 TYR A CD1 
3679 C CD2 . TYR A 489 ? 0.26724 0.25834 0.27091 -0.00721 -0.01844 0.01802  492 TYR A CD2 
3680 C CE1 . TYR A 489 ? 0.20129 0.19225 0.21366 -0.00349 -0.01723 0.01395  492 TYR A CE1 
3681 C CE2 . TYR A 489 ? 0.23330 0.22718 0.23603 -0.00889 -0.01565 0.01867  492 TYR A CE2 
3682 C CZ  . TYR A 489 ? 0.27319 0.26701 0.28087 -0.00698 -0.01527 0.01677  492 TYR A CZ  
3683 O OH  . TYR A 489 ? 0.29331 0.29047 0.30129 -0.00855 -0.01283 0.01738  492 TYR A OH  
3684 N N   . THR A 490 ? 0.21550 0.19956 0.24333 0.00625  -0.02726 0.00794  493 THR A N   
3685 C CA  . THR A 490 ? 0.23018 0.21434 0.26273 0.01001  -0.02650 0.00333  493 THR A CA  
3686 C C   . THR A 490 ? 0.20836 0.18780 0.24698 0.01104  -0.03138 0.00328  493 THR A C   
3687 O O   . THR A 490 ? 0.22827 0.20619 0.26803 0.01216  -0.03125 0.00096  493 THR A O   
3688 C CB  . THR A 490 ? 0.22330 0.21086 0.25875 0.01272  -0.02492 0.00022  493 THR A CB  
3689 O OG1 . THR A 490 ? 0.24474 0.23568 0.27453 0.01145  -0.02079 0.00036  493 THR A OG1 
3690 C CG2 . THR A 490 ? 0.24034 0.22897 0.28015 0.01662  -0.02359 -0.00505 493 THR A CG2 
3691 N N   . VAL A 491 ? 0.23353 0.21006 0.27628 0.01066  -0.03632 0.00583  494 VAL A N   
3692 C CA  . VAL A 491 ? 0.21318 0.18396 0.26239 0.01161  -0.04192 0.00609  494 VAL A CA  
3693 C C   . VAL A 491 ? 0.26346 0.23094 0.30974 0.00809  -0.04315 0.00939  494 VAL A C   
3694 O O   . VAL A 491 ? 0.24804 0.21182 0.29809 0.00926  -0.04535 0.00741  494 VAL A O   
3695 C CB  . VAL A 491 ? 0.25886 0.22667 0.31282 0.01130  -0.04777 0.00938  494 VAL A CB  
3696 C CG1 . VAL A 491 ? 0.29962 0.26008 0.35980 0.01150  -0.05439 0.01077  494 VAL A CG1 
3697 C CG2 . VAL A 491 ? 0.27580 0.24736 0.33540 0.01527  -0.04711 0.00554  494 VAL A CG2 
3698 N N   . MET A 492 ? 0.21763 0.18673 0.25731 0.00359  -0.04174 0.01426  495 MET A N   
3699 C CA  . MET A 492 ? 0.26956 0.23741 0.30662 -0.00031 -0.04197 0.01769  495 MET A CA  
3700 C C   . MET A 492 ? 0.20856 0.17812 0.24578 0.00134  -0.03865 0.01360  495 MET A C   
3701 O O   . MET A 492 ? 0.24069 0.20695 0.28079 0.00037  -0.04122 0.01401  495 MET A O   
3702 C CB  . MET A 492 ? 0.25906 0.23069 0.28838 -0.00476 -0.03909 0.02213  495 MET A CB  
3703 C CG  . MET A 492 ? 0.27281 0.24451 0.29981 -0.00962 -0.03914 0.02659  495 MET A CG  
3704 S SD  . MET A 492 ? 0.34444 0.32107 0.36195 -0.01479 -0.03579 0.03142  495 MET A SD  
3705 C CE  . MET A 492 ? 0.25382 0.23689 0.26790 -0.01171 -0.02829 0.02580  495 MET A CE  
3706 N N   . ALA A 493 ? 0.19789 0.17221 0.23208 0.00362  -0.03345 0.00984  496 ALA A N   
3707 C CA  . ALA A 493 ? 0.24904 0.22505 0.28251 0.00481  -0.03066 0.00658  496 ALA A CA  
3708 C C   . ALA A 493 ? 0.23562 0.20807 0.27406 0.00826  -0.03325 0.00201  496 ALA A C   
3709 O O   . ALA A 493 ? 0.25930 0.22985 0.29893 0.00778  -0.03456 0.00111  496 ALA A O   
3710 C CB  . ALA A 493 ? 0.24830 0.22953 0.27712 0.00618  -0.02510 0.00425  496 ALA A CB  
3711 N N   . ILE A 494 ? 0.22956 0.20152 0.27114 0.01181  -0.03392 -0.00135 497 ILE A N   
3712 C CA  . ILE A 494 ? 0.20734 0.17684 0.25292 0.01549  -0.03543 -0.00687 497 ILE A CA  
3713 C C   . ILE A 494 ? 0.25135 0.21381 0.30260 0.01497  -0.04176 -0.00598 497 ILE A C   
3714 O O   . ILE A 494 ? 0.25200 0.21135 0.30596 0.01734  -0.04358 -0.01055 497 ILE A O   
3715 C CB  . ILE A 494 ? 0.25550 0.22767 0.30376 0.01962  -0.03378 -0.01130 497 ILE A CB  
3716 C CG1 . ILE A 494 ? 0.26824 0.23827 0.32220 0.01996  -0.03778 -0.00902 497 ILE A CG1 
3717 C CG2 . ILE A 494 ? 0.20292 0.18157 0.24554 0.01967  -0.02775 -0.01200 497 ILE A CG2 
3718 C CD1 . ILE A 494 ? 0.33499 0.30883 0.39344 0.02391  -0.03629 -0.01309 497 ILE A CD1 
3719 N N   . THR A 495 ? 0.22366 0.18305 0.27650 0.01177  -0.04554 -0.00022 498 THR A N   
3720 C CA  . THR A 495 ? 0.21341 0.16533 0.27146 0.01034  -0.05214 0.00184  498 THR A CA  
3721 C C   . THR A 495 ? 0.26699 0.21808 0.32257 0.00544  -0.05268 0.00603  498 THR A C   
3722 O O   . THR A 495 ? 0.26670 0.21177 0.32605 0.00281  -0.05822 0.00938  498 THR A O   
3723 C CB  . THR A 495 ? 0.30243 0.25075 0.36405 0.00925  -0.05698 0.00638  498 THR A CB  
3724 O OG1 . THR A 495 ? 0.28720 0.23900 0.34279 0.00464  -0.05503 0.01272  498 THR A OG1 
3725 C CG2 . THR A 495 ? 0.35136 0.30099 0.41768 0.01446  -0.05698 0.00183  498 THR A CG2 
3726 N N   . GLY A 496 ? 0.30083 0.25787 0.35100 0.00417  -0.04733 0.00588  499 GLY A N   
3727 C CA  . GLY A 496 ? 0.29539 0.25306 0.34463 -0.00008 -0.04745 0.00917  499 GLY A CA  
3728 C C   . GLY A 496 ? 0.31142 0.27085 0.35846 -0.00559 -0.04742 0.01660  499 GLY A C   
3729 O O   . GLY A 496 ? 0.28119 0.24058 0.32928 -0.00976 -0.04864 0.02019  499 GLY A O   
3730 N N   . MET A 497 ? 0.21394 0.17534 0.25777 -0.00601 -0.04602 0.01903  500 MET A N   
3731 C CA  . MET A 497 ? 0.23512 0.19780 0.27568 -0.01143 -0.04636 0.02604  500 MET A CA  
3732 C C   . MET A 497 ? 0.27333 0.24398 0.30705 -0.01274 -0.03971 0.02669  500 MET A C   
3733 O O   . MET A 497 ? 0.29967 0.27240 0.32924 -0.01705 -0.03908 0.03179  500 MET A O   
3734 C CB  . MET A 497 ? 0.23998 0.19781 0.28164 -0.01176 -0.05124 0.02917  500 MET A CB  
3735 C CG  . MET A 497 ? 0.34608 0.29499 0.39497 -0.01174 -0.05904 0.03037  500 MET A CG  
3736 S SD  . MET A 497 ? 0.40370 0.34961 0.45330 -0.01918 -0.06277 0.03799  500 MET A SD  
3737 C CE  . MET A 497 ? 0.31947 0.26236 0.37517 -0.01680 -0.06416 0.03255  500 MET A CE  
3738 N N   . ALA A 498 ? 0.19334 0.16829 0.22552 -0.00934 -0.03492 0.02171  501 ALA A N   
3739 C CA  . ALA A 498 ? 0.24419 0.22586 0.27069 -0.01019 -0.02908 0.02186  501 ALA A CA  
3740 C C   . ALA A 498 ? 0.28178 0.26783 0.30877 -0.01311 -0.02667 0.02339  501 ALA A C   
3741 O O   . ALA A 498 ? 0.29190 0.27565 0.32290 -0.01578 -0.03000 0.02592  501 ALA A O   
3742 C CB  . ALA A 498 ? 0.21289 0.19647 0.23779 -0.00546 -0.02574 0.01650  501 ALA A CB  
3743 N N   . ILE A 499 ? 0.18374 0.17614 0.20754 -0.01277 -0.02122 0.02197  502 ILE A N   
3744 C CA  . ILE A 499 ? 0.21991 0.21803 0.24438 -0.01631 -0.01856 0.02440  502 ILE A CA  
3745 C C   . ILE A 499 ? 0.22780 0.22973 0.25553 -0.01400 -0.01612 0.02089  502 ILE A C   
3746 O O   . ILE A 499 ? 0.23477 0.24103 0.26592 -0.01683 -0.01525 0.02283  502 ILE A O   
3747 C CB  . ILE A 499 ? 0.22305 0.22660 0.24157 -0.01894 -0.01427 0.02655  502 ILE A CB  
3748 C CG1 . ILE A 499 ? 0.24500 0.25091 0.25962 -0.01498 -0.01010 0.02200  502 ILE A CG1 
3749 C CG2 . ILE A 499 ? 0.27011 0.26998 0.28496 -0.02238 -0.01754 0.03126  502 ILE A CG2 
3750 C CD1 . ILE A 499 ? 0.22768 0.24002 0.23689 -0.01700 -0.00494 0.02249  502 ILE A CD1 
3751 N N   . ASP A 500 ? 0.20119 0.20244 0.22806 -0.00940 -0.01484 0.01623  503 ASP A N   
3752 C CA  . ASP A 500 ? 0.21353 0.21909 0.24263 -0.00764 -0.01237 0.01367  503 ASP A CA  
3753 C C   . ASP A 500 ? 0.25861 0.26307 0.29353 -0.00852 -0.01581 0.01384  503 ASP A C   
3754 O O   . ASP A 500 ? 0.25212 0.26180 0.29090 -0.01031 -0.01459 0.01492  503 ASP A O   
3755 C CB  . ASP A 500 ? 0.22191 0.22630 0.24825 -0.00307 -0.01085 0.00938  503 ASP A CB  
3756 C CG  . ASP A 500 ? 0.30385 0.31049 0.32532 -0.00239 -0.00703 0.00888  503 ASP A CG  
3757 O OD1 . ASP A 500 ? 0.24425 0.25008 0.26265 -0.00438 -0.00707 0.01103  503 ASP A OD1 
3758 O OD2 . ASP A 500 ? 0.28343 0.29205 0.30398 0.00009  -0.00450 0.00632  503 ASP A OD2 
3759 N N   . ASN A 501 ? 0.25180 0.24976 0.28794 -0.00731 -0.02026 0.01251  504 ASN A N   
3760 C CA  . ASN A 501 ? 0.24338 0.23939 0.28468 -0.00830 -0.02419 0.01225  504 ASN A CA  
3761 C C   . ASN A 501 ? 0.19947 0.19741 0.24500 -0.01365 -0.02562 0.01724  504 ASN A C   
3762 O O   . ASN A 501 ? 0.22852 0.22928 0.27904 -0.01548 -0.02667 0.01791  504 ASN A O   
3763 C CB  . ASN A 501 ? 0.18138 0.16955 0.22295 -0.00608 -0.02878 0.00947  504 ASN A CB  
3764 C CG  . ASN A 501 ? 0.25871 0.24605 0.29686 -0.00128 -0.02752 0.00418  504 ASN A CG  
3765 O OD1 . ASN A 501 ? 0.26952 0.26115 0.30602 -0.00000 -0.02450 0.00303  504 ASN A OD1 
3766 N ND2 . ASN A 501 ? 0.24785 0.22998 0.28512 0.00123  -0.02976 0.00118  504 ASN A ND2 
3767 N N   . HIS A 502 ? 0.22767 0.22413 0.27136 -0.01653 -0.02605 0.02113  505 HIS A N   
3768 C CA  . HIS A 502 ? 0.20706 0.20520 0.25392 -0.02242 -0.02747 0.02677  505 HIS A CA  
3769 C C   . HIS A 502 ? 0.19372 0.20202 0.24208 -0.02484 -0.02233 0.02834  505 HIS A C   
3770 O O   . HIS A 502 ? 0.23840 0.25003 0.29266 -0.02833 -0.02339 0.03069  505 HIS A O   
3771 C CB  . HIS A 502 ? 0.20429 0.19887 0.24733 -0.02491 -0.02885 0.03083  505 HIS A CB  
3772 C CG  . HIS A 502 ? 0.22328 0.21781 0.26875 -0.03151 -0.03140 0.03747  505 HIS A CG  
3773 N ND1 . HIS A 502 ? 0.22101 0.21363 0.26237 -0.03505 -0.03248 0.04253  505 HIS A ND1 
3774 C CD2 . HIS A 502 ? 0.22469 0.22055 0.27622 -0.03562 -0.03355 0.04032  505 HIS A CD2 
3775 C CE1 . HIS A 502 ? 0.21383 0.20661 0.25818 -0.04124 -0.03497 0.04848  505 HIS A CE1 
3776 N NE2 . HIS A 502 ? 0.24430 0.23920 0.29522 -0.04177 -0.03555 0.04724  505 HIS A NE2 
3777 N N   . LEU A 503 ? 0.20824 0.22181 0.25201 -0.02296 -0.01681 0.02678  506 LEU A N   
3778 C CA  . LEU A 503 ? 0.20626 0.22997 0.25214 -0.02434 -0.01153 0.02715  506 LEU A CA  
3779 C C   . LEU A 503 ? 0.21359 0.24028 0.26594 -0.02190 -0.01188 0.02404  506 LEU A C   
3780 O O   . LEU A 503 ? 0.20331 0.23756 0.26172 -0.02441 -0.01020 0.02554  506 LEU A O   
3781 C CB  . LEU A 503 ? 0.21387 0.24112 0.25340 -0.02199 -0.00615 0.02497  506 LEU A CB  
3782 C CG  . LEU A 503 ? 0.25479 0.28088 0.28736 -0.02523 -0.00538 0.02847  506 LEU A CG  
3783 C CD1 . LEU A 503 ? 0.20437 0.23246 0.23037 -0.02229 -0.00094 0.02526  506 LEU A CD1 
3784 C CD2 . LEU A 503 ? 0.23058 0.26322 0.26461 -0.03158 -0.00362 0.03368  506 LEU A CD2 
3785 N N   . LEU A 504 ? 0.18289 0.20428 0.23409 -0.01716 -0.01406 0.01982  507 LEU A N   
3786 C CA  . LEU A 504 ? 0.22526 0.24864 0.28165 -0.01497 -0.01531 0.01713  507 LEU A CA  
3787 C C   . LEU A 504 ? 0.20698 0.23051 0.27058 -0.01883 -0.01954 0.01964  507 LEU A C   
3788 O O   . LEU A 504 ? 0.21170 0.24208 0.28209 -0.01997 -0.01888 0.02006  507 LEU A O   
3789 C CB  . LEU A 504 ? 0.20387 0.22045 0.25627 -0.01016 -0.01762 0.01283  507 LEU A CB  
3790 C CG  . LEU A 504 ? 0.22480 0.24128 0.28125 -0.00845 -0.02071 0.01043  507 LEU A CG  
3791 C CD1 . LEU A 504 ? 0.19312 0.21739 0.25328 -0.00714 -0.01755 0.00976  507 LEU A CD1 
3792 C CD2 . LEU A 504 ? 0.27113 0.28068 0.32188 -0.00437 -0.02278 0.00648  507 LEU A CD2 
3793 N N   . ALA A 505 ? 0.18069 0.19664 0.24370 -0.02093 -0.02428 0.02134  508 ALA A N   
3794 C CA  . ALA A 505 ? 0.22553 0.24011 0.29537 -0.02501 -0.02914 0.02385  508 ALA A CA  
3795 C C   . ALA A 505 ? 0.25501 0.27783 0.32978 -0.03093 -0.02669 0.02927  508 ALA A C   
3796 O O   . ALA A 505 ? 0.20625 0.23336 0.28883 -0.03381 -0.02837 0.03072  508 ALA A O   
3797 C CB  . ALA A 505 ? 0.19055 0.19437 0.25881 -0.02571 -0.03492 0.02430  508 ALA A CB  
3798 N N   . LEU A 506 ? 0.23034 0.25570 0.30064 -0.03326 -0.02291 0.03250  509 LEU A N   
3799 C CA  . LEU A 506 ? 0.25129 0.28597 0.32539 -0.03913 -0.01958 0.03752  509 LEU A CA  
3800 C C   . LEU A 506 ? 0.18743 0.23364 0.26707 -0.03764 -0.01458 0.03524  509 LEU A C   
3801 O O   . LEU A 506 ? 0.22499 0.27903 0.31279 -0.04179 -0.01400 0.03801  509 LEU A O   
3802 C CB  . LEU A 506 ? 0.21279 0.24842 0.27919 -0.04149 -0.01603 0.04075  509 LEU A CB  
3803 C CG  . LEU A 506 ? 0.25222 0.27715 0.31394 -0.04357 -0.02126 0.04409  509 LEU A CG  
3804 C CD1 . LEU A 506 ? 0.25196 0.27860 0.30495 -0.04528 -0.01751 0.04674  509 LEU A CD1 
3805 C CD2 . LEU A 506 ? 0.24711 0.26890 0.31477 -0.04979 -0.02674 0.04962  509 LEU A CD2 
3806 N N   . ARG A 507 ? 0.18249 0.22985 0.25861 -0.03173 -0.01127 0.03025  510 ARG A N   
3807 C CA  . ARG A 507 ? 0.21243 0.26972 0.29430 -0.02931 -0.00711 0.02753  510 ARG A CA  
3808 C C   . ARG A 507 ? 0.23410 0.29253 0.32538 -0.02919 -0.01151 0.02675  510 ARG A C   
3809 O O   . ARG A 507 ? 0.19882 0.26744 0.29914 -0.03090 -0.00947 0.02759  510 ARG A O   
3810 C CB  . ARG A 507 ? 0.21167 0.26701 0.28769 -0.02286 -0.00443 0.02246  510 ARG A CB  
3811 C CG  . ARG A 507 ? 0.20278 0.26726 0.28494 -0.01961 -0.00064 0.01932  510 ARG A CG  
3812 C CD  . ARG A 507 ? 0.23208 0.29212 0.30809 -0.01353 0.00057  0.01477  510 ARG A CD  
3813 N NE  . ARG A 507 ? 0.22120 0.27418 0.29746 -0.01038 -0.00480 0.01269  510 ARG A NE  
3814 C CZ  . ARG A 507 ? 0.28593 0.33239 0.35590 -0.00602 -0.00563 0.00967  510 ARG A CZ  
3815 N NH1 . ARG A 507 ? 0.30915 0.35333 0.37171 -0.00448 -0.00237 0.00857  510 ARG A NH1 
3816 N NH2 . ARG A 507 ? 0.18115 0.22332 0.25199 -0.00356 -0.01003 0.00790  510 ARG A NH2 
3817 N N   . GLU A 508 ? 0.20734 0.25584 0.29672 -0.02697 -0.01755 0.02475  511 GLU A N   
3818 C CA  . GLU A 508 ? 0.21206 0.26114 0.30907 -0.02655 -0.02216 0.02346  511 GLU A CA  
3819 C C   . GLU A 508 ? 0.24297 0.29343 0.34766 -0.03293 -0.02591 0.02783  511 GLU A C   
3820 O O   . GLU A 508 ? 0.22069 0.27679 0.33472 -0.03426 -0.02795 0.02808  511 GLU A O   
3821 C CB  . GLU A 508 ? 0.24461 0.28316 0.33588 -0.02213 -0.02695 0.01937  511 GLU A CB  
3822 C CG  . GLU A 508 ? 0.24067 0.27913 0.32597 -0.01629 -0.02347 0.01549  511 GLU A CG  
3823 C CD  . GLU A 508 ? 0.27615 0.32426 0.36800 -0.01436 -0.02040 0.01444  511 GLU A CD  
3824 O OE1 . GLU A 508 ? 0.22844 0.28056 0.32872 -0.01514 -0.02352 0.01459  511 GLU A OE1 
3825 O OE2 . GLU A 508 ? 0.25723 0.30893 0.34632 -0.01188 -0.01514 0.01325  511 GLU A OE2 
3826 N N   . LEU A 509 ? 0.25847 0.30397 0.35997 -0.03717 -0.02721 0.03165  512 LEU A N   
3827 C CA  . LEU A 509 ? 0.25879 0.30618 0.36782 -0.04421 -0.03036 0.03687  512 LEU A CA  
3828 C C   . LEU A 509 ? 0.26511 0.32723 0.38118 -0.04831 -0.02432 0.04038  512 LEU A C   
3829 O O   . LEU A 509 ? 0.28877 0.35704 0.41509 -0.05271 -0.02617 0.04307  512 LEU A O   
3830 C CB  . LEU A 509 ? 0.27390 0.31166 0.37746 -0.04766 -0.03354 0.04052  512 LEU A CB  
3831 C CG  . LEU A 509 ? 0.26625 0.28983 0.36688 -0.04522 -0.04112 0.03760  512 LEU A CG  
3832 C CD1 . LEU A 509 ? 0.30103 0.31566 0.39569 -0.04695 -0.04316 0.04046  512 LEU A CD1 
3833 C CD2 . LEU A 509 ? 0.27396 0.29536 0.38353 -0.04881 -0.04792 0.03854  512 LEU A CD2 
3834 N N   . ALA A 510 ? 0.20674 0.27513 0.31773 -0.04693 -0.01700 0.04006  513 ALA A N   
3835 C CA  . ALA A 510 ? 0.22936 0.31301 0.34684 -0.04960 -0.01021 0.04179  513 ALA A CA  
3836 C C   . ALA A 510 ? 0.19125 0.28295 0.31944 -0.04642 -0.01014 0.03832  513 ALA A C   
3837 O O   . ALA A 510 ? 0.21530 0.31783 0.35469 -0.05051 -0.00907 0.04085  513 ALA A O   
3838 C CB  . ALA A 510 ? 0.18783 0.27542 0.29668 -0.04724 -0.00269 0.04024  513 ALA A CB  
3839 N N   . ARG A 511 ? 0.22524 0.31176 0.35049 -0.03934 -0.01171 0.03282  514 ARG A N   
3840 C CA  . ARG A 511 ? 0.25024 0.34364 0.38511 -0.03582 -0.01227 0.02962  514 ARG A CA  
3841 C C   . ARG A 511 ? 0.31241 0.40643 0.45762 -0.03960 -0.01885 0.03175  514 ARG A C   
3842 O O   . ARG A 511 ? 0.24910 0.35382 0.40627 -0.03981 -0.01829 0.03152  514 ARG A O   
3843 C CB  . ARG A 511 ? 0.17214 0.25779 0.30053 -0.02831 -0.01403 0.02425  514 ARG A CB  
3844 C CG  . ARG A 511 ? 0.28873 0.38252 0.42614 -0.02398 -0.01326 0.02105  514 ARG A CG  
3845 C CD  . ARG A 511 ? 0.27021 0.35534 0.40148 -0.01753 -0.01657 0.01677  514 ARG A CD  
3846 N NE  . ARG A 511 ? 0.26357 0.34093 0.38196 -0.01464 -0.01381 0.01502  514 ARG A NE  
3847 C CZ  . ARG A 511 ? 0.25371 0.33432 0.36905 -0.01121 -0.00808 0.01281  514 ARG A CZ  
3848 N NH1 . ARG A 511 ? 0.23355 0.32550 0.35762 -0.00997 -0.00364 0.01172  514 ARG A NH1 
3849 N NH2 . ARG A 511 ? 0.24762 0.31999 0.35138 -0.00887 -0.00689 0.01132  514 ARG A NH2 
3850 N N   . ALA A 512 ? 0.29401 0.37671 0.43545 -0.04250 -0.02540 0.03358  515 ALA A N   
3851 C CA  . ALA A 512 ? 0.32748 0.40970 0.47834 -0.04676 -0.03224 0.03565  515 ALA A CA  
3852 C C   . ALA A 512 ? 0.28232 0.37584 0.44347 -0.05438 -0.02983 0.04142  515 ALA A C   
3853 O O   . ALA A 512 ? 0.37659 0.47519 0.54936 -0.05768 -0.03374 0.04295  515 ALA A O   
3854 C CB  . ALA A 512 ? 0.30497 0.37165 0.44909 -0.04782 -0.03978 0.03561  515 ALA A CB  
3855 N N   . MET A 513 ? 0.25325 0.35089 0.41019 -0.05772 -0.02374 0.04494  516 MET A N   
3856 C CA  . MET A 513 ? 0.23522 0.34561 0.40142 -0.06527 -0.02014 0.05062  516 MET A CA  
3857 C C   . MET A 513 ? 0.40738 0.53509 0.58370 -0.06327 -0.01330 0.04856  516 MET A C   
3858 O O   . MET A 513 ? 0.32083 0.46022 0.51061 -0.06795 -0.01297 0.05140  516 MET A O   
3859 C CB  . MET A 513 ? 0.33165 0.44124 0.48886 -0.06982 -0.01573 0.05527  516 MET A CB  
3860 C CG  . MET A 513 ? 0.49929 0.59262 0.64769 -0.07222 -0.02226 0.05803  516 MET A CG  
3861 S SD  . MET A 513 ? 0.61010 0.70331 0.74740 -0.07718 -0.01706 0.06374  516 MET A SD  
3862 C CE  . MET A 513 ? 0.51513 0.63033 0.65862 -0.08048 -0.00609 0.06550  516 MET A CE  
3863 N N   . CYS A 514 ? 0.25268 0.38245 0.42352 -0.05635 -0.00789 0.04353  517 CYS A N   
3864 C CA  . CYS A 514 ? 0.24918 0.39503 0.42940 -0.05370 -0.00094 0.04088  517 CYS A CA  
3865 C C   . CYS A 514 ? 0.25195 0.39349 0.42595 -0.04454 0.00060  0.03428  517 CYS A C   
3866 O O   . CYS A 514 ? 0.21867 0.35064 0.37898 -0.04205 0.00180  0.03292  517 CYS A O   
3867 C CB  . CYS A 514 ? 0.27131 0.42927 0.45079 -0.05855 0.00810  0.04404  517 CYS A CB  
3868 S SG  . CYS A 514 ? 0.32192 0.50102 0.51361 -0.05503 0.01771  0.03982  517 CYS A SG  
3869 N N   . ALA A 515 ? 0.23619 0.38482 0.42062 -0.03974 0.00032  0.03049  518 ALA A N   
3870 C CA  . ALA A 515 ? 0.24697 0.39044 0.42572 -0.03130 0.00091  0.02473  518 ALA A CA  
3871 C C   . ALA A 515 ? 0.16870 0.31674 0.34068 -0.02878 0.00977  0.02228  518 ALA A C   
3872 O O   . ALA A 515 ? 0.18998 0.33055 0.35348 -0.02280 0.01017  0.01825  518 ALA A O   
3873 C CB  . ALA A 515 ? 0.25952 0.40979 0.45171 -0.02682 -0.00175 0.02166  518 ALA A CB  
3874 N N   . ALA A 516 ? 0.19154 0.35197 0.36707 -0.03337 0.01684  0.02451  519 ALA A N   
3875 C CA  . ALA A 516 ? 0.17302 0.33767 0.34061 -0.03179 0.02527  0.02214  519 ALA A CA  
3876 C C   . ALA A 516 ? 0.19815 0.35100 0.34943 -0.03512 0.02452  0.02524  519 ALA A C   
3877 O O   . ALA A 516 ? 0.19483 0.34896 0.34457 -0.04248 0.02457  0.03091  519 ALA A O   
3878 C CB  . ALA A 516 ? 0.20095 0.38441 0.37812 -0.03567 0.03348  0.02312  519 ALA A CB  
3879 N N   . LEU A 517 ? 0.21765 0.35913 0.35743 -0.02987 0.02349  0.02180  520 LEU A N   
3880 C CA  . LEU A 517 ? 0.23199 0.36191 0.35706 -0.03212 0.02217  0.02421  520 LEU A CA  
3881 C C   . LEU A 517 ? 0.25475 0.39222 0.37380 -0.03646 0.02955  0.02621  520 LEU A C   
3882 O O   . LEU A 517 ? 0.25219 0.40161 0.37495 -0.03492 0.03668  0.02309  520 LEU A O   
3883 C CB  . LEU A 517 ? 0.18848 0.30683 0.30396 -0.02538 0.02035  0.01965  520 LEU A CB  
3884 C CG  . LEU A 517 ? 0.29569 0.40343 0.41200 -0.02165 0.01266  0.01820  520 LEU A CG  
3885 C CD1 . LEU A 517 ? 0.24753 0.34549 0.35334 -0.01593 0.01243  0.01426  520 LEU A CD1 
3886 C CD2 . LEU A 517 ? 0.32363 0.42311 0.43812 -0.02637 0.00628  0.02261  520 LEU A CD2 
3887 N N   . PRO A 518 ? 0.22301 0.35364 0.33248 -0.04175 0.02787  0.03116  521 PRO A N   
3888 C CA  . PRO A 518 ? 0.30798 0.44508 0.40983 -0.04629 0.03440  0.03350  521 PRO A CA  
3889 C C   . PRO A 518 ? 0.23611 0.37067 0.32776 -0.04082 0.03857  0.02800  521 PRO A C   
3890 O O   . PRO A 518 ? 0.23500 0.36019 0.32378 -0.03452 0.03537  0.02378  521 PRO A O   
3891 C CB  . PRO A 518 ? 0.34146 0.46882 0.43584 -0.05271 0.02925  0.04046  521 PRO A CB  
3892 C CG  . PRO A 518 ? 0.33200 0.44499 0.42588 -0.04895 0.02095  0.03930  521 PRO A CG  
3893 C CD  . PRO A 518 ? 0.23941 0.35616 0.34485 -0.04384 0.01964  0.03477  521 PRO A CD  
3894 N N   . GLU A 519 ? 0.22016 0.36341 0.30610 -0.04364 0.04579  0.02811  522 GLU A N   
3895 C CA  . GLU A 519 ? 0.27954 0.42151 0.35601 -0.03888 0.05018  0.02243  522 GLU A CA  
3896 C C   . GLU A 519 ? 0.23701 0.36300 0.30152 -0.03686 0.04483  0.02260  522 GLU A C   
3897 O O   . GLU A 519 ? 0.26338 0.38472 0.32313 -0.03096 0.04562  0.01706  522 GLU A O   
3898 C CB  . GLU A 519 ? 0.26086 0.41365 0.33073 -0.04360 0.05812  0.02334  522 GLU A CB  
3899 C CG  . GLU A 519 ? 0.35154 0.52206 0.43305 -0.04441 0.06520  0.02137  522 GLU A CG  
3900 C CD  . GLU A 519 ? 0.82643 1.00746 0.90190 -0.05251 0.07141  0.02585  522 GLU A CD  
3901 O OE1 . GLU A 519 ? 0.64684 0.82755 0.70916 -0.05271 0.07561  0.02377  522 GLU A OE1 
3902 O OE2 . GLU A 519 ? 0.89186 1.08077 0.97501 -0.05910 0.07159  0.03182  522 GLU A OE2 
3903 N N   . MET A 520 ? 0.20394 0.32157 0.26428 -0.04173 0.03922  0.02888  523 MET A N   
3904 C CA  . MET A 520 ? 0.19853 0.30145 0.24941 -0.03979 0.03363  0.02921  523 MET A CA  
3905 C C   . MET A 520 ? 0.23142 0.32728 0.28484 -0.03192 0.03077  0.02341  523 MET A C   
3906 O O   . MET A 520 ? 0.23062 0.31947 0.27595 -0.02825 0.03040  0.02034  523 MET A O   
3907 C CB  . MET A 520 ? 0.26941 0.36467 0.32073 -0.04492 0.02682  0.03599  523 MET A CB  
3908 C CG  . MET A 520 ? 0.27789 0.35856 0.32288 -0.04194 0.02050  0.03556  523 MET A CG  
3909 S SD  . MET A 520 ? 0.28019 0.35614 0.31008 -0.04412 0.02151  0.03745  523 MET A SD  
3910 C CE  . MET A 520 ? 0.22852 0.29009 0.25535 -0.03770 0.01536  0.03392  523 MET A CE  
3911 N N   . PHE A 521 ? 0.24455 0.34236 0.30904 -0.02959 0.02853  0.02210  524 PHE A N   
3912 C CA  . PHE A 521 ? 0.17901 0.26992 0.24560 -0.02288 0.02514  0.01753  524 PHE A CA  
3913 C C   . PHE A 521 ? 0.20201 0.30006 0.27425 -0.01749 0.02942  0.01175  524 PHE A C   
3914 O O   . PHE A 521 ? 0.26097 0.35286 0.33323 -0.01196 0.02695  0.00807  524 PHE A O   
3915 C CB  . PHE A 521 ? 0.23952 0.32598 0.31342 -0.02354 0.01857  0.01971  524 PHE A CB  
3916 C CG  . PHE A 521 ? 0.22639 0.30411 0.29530 -0.02780 0.01359  0.02448  524 PHE A CG  
3917 C CD1 . PHE A 521 ? 0.19858 0.26555 0.25808 -0.02578 0.01096  0.02376  524 PHE A CD1 
3918 C CD2 . PHE A 521 ? 0.25343 0.33389 0.32740 -0.03397 0.01159  0.02977  524 PHE A CD2 
3919 C CE1 . PHE A 521 ? 0.23003 0.28886 0.28578 -0.02913 0.00616  0.02777  524 PHE A CE1 
3920 C CE2 . PHE A 521 ? 0.23686 0.30810 0.30662 -0.03767 0.00633  0.03412  524 PHE A CE2 
3921 C CZ  . PHE A 521 ? 0.21955 0.28003 0.28028 -0.03503 0.00366  0.03297  524 PHE A CZ  
3922 N N   . MET A 522 ? 0.19385 0.30479 0.27108 -0.01893 0.03573  0.01080  525 MET A N   
3923 C CA  . MET A 522 ? 0.24125 0.35878 0.32343 -0.01332 0.04021  0.00456  525 MET A CA  
3924 C C   . MET A 522 ? 0.32387 0.43946 0.39520 -0.01129 0.04453  0.00075  525 MET A C   
3925 O O   . MET A 522 ? 0.24354 0.35992 0.31693 -0.00552 0.04659  -0.00511 525 MET A O   
3926 C CB  . MET A 522 ? 0.19705 0.33047 0.29102 -0.01525 0.04535  0.00439  525 MET A CB  
3927 C CG  . MET A 522 ? 0.26817 0.40403 0.37375 -0.01763 0.04073  0.00815  525 MET A CG  
3928 S SD  . MET A 522 ? 0.34742 0.47556 0.46011 -0.01069 0.03381  0.00493  525 MET A SD  
3929 C CE  . MET A 522 ? 0.28881 0.42999 0.41384 -0.00495 0.03939  -0.00140 525 MET A CE  
3930 N N   . ASP A 523 ? 0.26059 0.37317 0.32067 -0.01603 0.04529  0.00411  526 ASP A N   
3931 C CA  . ASP A 523 ? 0.24256 0.35207 0.29064 -0.01516 0.04831  0.00128  526 ASP A CA  
3932 C C   . ASP A 523 ? 0.29651 0.39622 0.34204 -0.00863 0.04550  -0.00353 526 ASP A C   
3933 O O   . ASP A 523 ? 0.24092 0.33086 0.28618 -0.00724 0.03953  -0.00189 526 ASP A O   
3934 C CB  . ASP A 523 ? 0.29993 0.40340 0.33728 -0.02112 0.04576  0.00724  526 ASP A CB  
3935 C CG  . ASP A 523 ? 0.36961 0.47127 0.39385 -0.02197 0.04872  0.00557  526 ASP A CG  
3936 O OD1 . ASP A 523 ? 0.30866 0.41310 0.33106 -0.01796 0.05293  -0.00069 526 ASP A OD1 
3937 O OD2 . ASP A 523 ? 0.35237 0.44911 0.36819 -0.02679 0.04611  0.01070  526 ASP A OD2 
3938 N N   . GLU A 524 ? 0.22388 0.32603 0.26692 -0.00492 0.04986  -0.00951 527 GLU A N   
3939 C CA  . GLU A 524 ? 0.28989 0.38224 0.32999 0.00066  0.04708  -0.01371 527 GLU A CA  
3940 C C   . GLU A 524 ? 0.27663 0.35734 0.30574 -0.00116 0.04262  -0.01075 527 GLU A C   
3941 O O   . GLU A 524 ? 0.25592 0.32748 0.28448 0.00216  0.03830  -0.01164 527 GLU A O   
3942 C CB  . GLU A 524 ? 0.36710 0.46347 0.40559 0.00435  0.05237  -0.02071 527 GLU A CB  
3943 C CG  . GLU A 524 ? 0.39094 0.47720 0.42759 0.01011  0.04937  -0.02523 527 GLU A CG  
3944 C CD  . GLU A 524 ? 0.47780 0.56025 0.52462 0.01446  0.04474  -0.02536 527 GLU A CD  
3945 O OE1 . GLU A 524 ? 0.42223 0.51172 0.47972 0.01464  0.04481  -0.02416 527 GLU A OE1 
3946 O OE2 . GLU A 524 ? 0.46747 0.53983 0.51145 0.01744  0.04074  -0.02642 527 GLU A OE2 
3947 N N   . THR A 525 ? 0.22154 0.30269 0.24217 -0.00653 0.04342  -0.00699 528 THR A N   
3948 C CA  . THR A 525 ? 0.27040 0.34106 0.28231 -0.00820 0.03864  -0.00389 528 THR A CA  
3949 C C   . THR A 525 ? 0.30018 0.36447 0.31727 -0.00780 0.03269  -0.00046 528 THR A C   
3950 O O   . THR A 525 ? 0.24279 0.29808 0.25679 -0.00578 0.02869  -0.00067 528 THR A O   
3951 C CB  . THR A 525 ? 0.25809 0.33058 0.26113 -0.01446 0.03966  0.00051  528 THR A CB  
3952 O OG1 . THR A 525 ? 0.30484 0.38278 0.30104 -0.01487 0.04519  -0.00325 528 THR A OG1 
3953 C CG2 . THR A 525 ? 0.31543 0.37729 0.31138 -0.01587 0.03397  0.00389  528 THR A CG2 
3954 N N   . TYR A 526 ? 0.22448 0.29361 0.24937 -0.00997 0.03208  0.00262  529 TYR A N   
3955 C CA  . TYR A 526 ? 0.23511 0.29798 0.26447 -0.00953 0.02628  0.00519  529 TYR A CA  
3956 C C   . TYR A 526 ? 0.24139 0.30076 0.27555 -0.00377 0.02443  0.00127  529 TYR A C   
3957 O O   . TYR A 526 ? 0.21697 0.26798 0.24929 -0.00213 0.02001  0.00164  529 TYR A O   
3958 C CB  . TYR A 526 ? 0.21005 0.27870 0.24683 -0.01352 0.02564  0.00925  529 TYR A CB  
3959 C CG  . TYR A 526 ? 0.22257 0.28468 0.26403 -0.01291 0.01947  0.01109  529 TYR A CG  
3960 C CD1 . TYR A 526 ? 0.24870 0.30211 0.28537 -0.01476 0.01477  0.01411  529 TYR A CD1 
3961 C CD2 . TYR A 526 ? 0.21437 0.27901 0.26504 -0.01030 0.01813  0.00943  529 TYR A CD2 
3962 C CE1 . TYR A 526 ? 0.21893 0.26642 0.25944 -0.01393 0.00938  0.01488  529 TYR A CE1 
3963 C CE2 . TYR A 526 ? 0.22642 0.28490 0.28011 -0.00980 0.01241  0.01057  529 TYR A CE2 
3964 C CZ  . TYR A 526 ? 0.21898 0.26896 0.26736 -0.01157 0.00830  0.01301  529 TYR A CZ  
3965 O OH  . TYR A 526 ? 0.22950 0.27345 0.28053 -0.01089 0.00285  0.01334  529 TYR A OH  
3966 N N   . LEU A 527 ? 0.21724 0.28300 0.25768 -0.00065 0.02763  -0.00246 530 LEU A N   
3967 C CA  . LEU A 527 ? 0.23962 0.30142 0.28440 0.00463  0.02520  -0.00559 530 LEU A CA  
3968 C C   . LEU A 527 ? 0.20419 0.25731 0.24093 0.00716  0.02408  -0.00777 530 LEU A C   
3969 O O   . LEU A 527 ? 0.25141 0.29733 0.28748 0.00920  0.02005  -0.00759 530 LEU A O   
3970 C CB  . LEU A 527 ? 0.19894 0.26904 0.25250 0.00784  0.02861  -0.00939 530 LEU A CB  
3971 C CG  . LEU A 527 ? 0.27858 0.35930 0.34176 0.00524  0.03035  -0.00747 530 LEU A CG  
3972 C CD1 . LEU A 527 ? 0.30814 0.39795 0.38121 0.00910  0.03403  -0.01195 530 LEU A CD1 
3973 C CD2 . LEU A 527 ? 0.25021 0.32741 0.31802 0.00416  0.02461  -0.00402 530 LEU A CD2 
3974 N N   A MET A 528 ? 0.22497 0.27876 0.25512 0.00665  0.02751  -0.00973 531 MET A N   
3975 N N   B MET A 528 ? 0.22409 0.27813 0.25437 0.00665  0.02763  -0.00978 531 MET A N   
3976 C CA  A MET A 528 ? 0.26182 0.30753 0.28518 0.00879  0.02613  -0.01181 531 MET A CA  
3977 C CA  B MET A 528 ? 0.26462 0.31080 0.28745 0.00844  0.02650  -0.01177 531 MET A CA  
3978 C C   A MET A 528 ? 0.26134 0.29988 0.27862 0.00640  0.02232  -0.00825 531 MET A C   
3979 C C   B MET A 528 ? 0.26211 0.30078 0.28009 0.00653  0.02217  -0.00819 531 MET A C   
3980 O O   A MET A 528 ? 0.27654 0.30819 0.29030 0.00819  0.02010  -0.00920 531 MET A O   
3981 O O   B MET A 528 ? 0.25080 0.28263 0.26681 0.00873  0.01949  -0.00900 531 MET A O   
3982 C CB  A MET A 528 ? 0.28958 0.33768 0.30741 0.00892  0.03043  -0.01544 531 MET A CB  
3983 C CB  B MET A 528 ? 0.26460 0.31336 0.28040 0.00718  0.03069  -0.01417 531 MET A CB  
3984 C CG  A MET A 528 ? 0.27267 0.31310 0.28591 0.01192  0.02909  -0.01875 531 MET A CG  
3985 C CG  B MET A 528 ? 0.29967 0.35396 0.31913 0.01059  0.03506  -0.01982 531 MET A CG  
3986 S SD  A MET A 528 ? 0.59649 0.63018 0.59862 0.00843  0.02686  -0.01621 531 MET A SD  
3987 S SD  B MET A 528 ? 0.38082 0.43908 0.39057 0.00846  0.04039  -0.02307 531 MET A SD  
3988 C CE  A MET A 528 ? 0.45147 0.49268 0.44790 0.00428  0.03136  -0.01589 531 MET A CE  
3989 C CE  B MET A 528 ? 0.41027 0.45652 0.40967 0.00809  0.03612  -0.02263 531 MET A CE  
3990 N N   . SER A 529 ? 0.21743 0.25755 0.23429 0.00242  0.02132  -0.00412 532 SER A N   
3991 C CA  . SER A 529 ? 0.23668 0.27013 0.24944 0.00066  0.01732  -0.00105 532 SER A CA  
3992 C C   . SER A 529 ? 0.23148 0.25998 0.24792 0.00303  0.01339  -0.00093 532 SER A C   
3993 O O   . SER A 529 ? 0.21505 0.23774 0.22828 0.00294  0.01052  0.00007  532 SER A O   
3994 C CB  . SER A 529 ? 0.23850 0.27439 0.25065 -0.00419 0.01673  0.00343  532 SER A CB  
3995 O OG  . SER A 529 ? 0.24017 0.27753 0.25947 -0.00492 0.01461  0.00546  532 SER A OG  
3996 N N   . ASN A 530 ? 0.19151 0.22251 0.21455 0.00516  0.01318  -0.00209 533 ASN A N   
3997 C CA  . ASN A 530 ? 0.19156 0.21853 0.21742 0.00684  0.00932  -0.00178 533 ASN A CA  
3998 C C   . ASN A 530 ? 0.23051 0.25492 0.25700 0.01079  0.00888  -0.00450 533 ASN A C   
3999 O O   . ASN A 530 ? 0.24654 0.26837 0.27501 0.01219  0.00587  -0.00433 533 ASN A O   
4000 C CB  . ASN A 530 ? 0.23739 0.26856 0.27028 0.00538  0.00797  -0.00005 533 ASN A CB  
4001 C CG  . ASN A 530 ? 0.29725 0.32811 0.32935 0.00125  0.00655  0.00341  533 ASN A CG  
4002 O OD1 . ASN A 530 ? 0.27652 0.30180 0.30382 0.00050  0.00454  0.00442  533 ASN A OD1 
4003 N ND2 . ASN A 530 ? 0.30747 0.34436 0.34486 -0.00156 0.00736  0.00541  533 ASN A ND2 
4004 N N   . ARG A 531 ? 0.22940 0.25407 0.25389 0.01240  0.01147  -0.00693 534 ARG A N   
4005 C CA  . ARG A 531 ? 0.17732 0.19809 0.20168 0.01577  0.01061  -0.00913 534 ARG A CA  
4006 C C   . ARG A 531 ? 0.25030 0.26492 0.26758 0.01527  0.00975  -0.00894 534 ARG A C   
4007 O O   . ARG A 531 ? 0.21499 0.22907 0.22829 0.01474  0.01171  -0.01023 534 ARG A O   
4008 C CB  . ARG A 531 ? 0.24655 0.27086 0.27389 0.01800  0.01362  -0.01238 534 ARG A CB  
4009 C CG  . ARG A 531 ? 0.23326 0.26475 0.26952 0.01894  0.01446  -0.01281 534 ARG A CG  
4010 C CD  . ARG A 531 ? 0.28458 0.32066 0.32422 0.02135  0.01820  -0.01680 534 ARG A CD  
4011 N NE  . ARG A 531 ? 0.44767 0.49258 0.49650 0.02161  0.01976  -0.01704 534 ARG A NE  
4012 C CZ  . ARG A 531 ? 0.38343 0.43658 0.43517 0.02132  0.02460  -0.01932 534 ARG A CZ  
4013 N NH1 . ARG A 531 ? 0.36022 0.41343 0.40532 0.02074  0.02822  -0.02175 534 ARG A NH1 
4014 N NH2 . ARG A 531 ? 0.37452 0.43650 0.43593 0.02137  0.02585  -0.01919 534 ARG A NH2 
4015 N N   . PHE A 532 ? 0.21722 0.22765 0.23302 0.01535  0.00687  -0.00755 535 PHE A N   
4016 C CA  . PHE A 532 ? 0.21820 0.22423 0.22852 0.01443  0.00619  -0.00705 535 PHE A CA  
4017 C C   . PHE A 532 ? 0.25041 0.25236 0.25879 0.01614  0.00586  -0.00830 535 PHE A C   
4018 O O   . PHE A 532 ? 0.24028 0.23932 0.24824 0.01696  0.00392  -0.00758 535 PHE A O   
4019 C CB  . PHE A 532 ? 0.21750 0.22203 0.22749 0.01356  0.00383  -0.00538 535 PHE A CB  
4020 C CG  . PHE A 532 ? 0.26196 0.26923 0.27397 0.01154  0.00349  -0.00391 535 PHE A CG  
4021 C CD1 . PHE A 532 ? 0.21772 0.22592 0.22758 0.00935  0.00453  -0.00293 535 PHE A CD1 
4022 C CD2 . PHE A 532 ? 0.26745 0.27601 0.28335 0.01148  0.00167  -0.00322 535 PHE A CD2 
4023 C CE1 . PHE A 532 ? 0.24222 0.25234 0.25380 0.00698  0.00378  -0.00086 535 PHE A CE1 
4024 C CE2 . PHE A 532 ? 0.28241 0.29281 0.30051 0.00920  0.00091  -0.00154 535 PHE A CE2 
4025 C CZ  . PHE A 532 ? 0.20395 0.21509 0.22003 0.00687  0.00198  -0.00014 535 PHE A CZ  
4026 N N   . VAL A 533 ? 0.20682 0.20832 0.21343 0.01631  0.00763  -0.01012 536 VAL A N   
4027 C CA  . VAL A 533 ? 0.21798 0.21490 0.22296 0.01756  0.00703  -0.01139 536 VAL A CA  
4028 C C   . VAL A 533 ? 0.25490 0.24814 0.25623 0.01608  0.00551  -0.00970 536 VAL A C   
4029 O O   . VAL A 533 ? 0.22596 0.21526 0.22652 0.01662  0.00420  -0.00942 536 VAL A O   
4030 C CB  . VAL A 533 ? 0.22772 0.22496 0.23111 0.01780  0.00919  -0.01432 536 VAL A CB  
4031 C CG1 . VAL A 533 ? 0.24672 0.23808 0.24843 0.01877  0.00799  -0.01581 536 VAL A CG1 
4032 C CG2 . VAL A 533 ? 0.25051 0.25261 0.25863 0.01969  0.01129  -0.01652 536 VAL A CG2 
4033 N N   . LEU A 534 ? 0.24929 0.24396 0.24898 0.01417  0.00549  -0.00837 537 LEU A N   
4034 C CA  . LEU A 534 ? 0.20313 0.19590 0.20103 0.01311  0.00429  -0.00698 537 LEU A CA  
4035 C C   . LEU A 534 ? 0.20880 0.20352 0.20816 0.01296  0.00346  -0.00580 537 LEU A C   
4036 O O   . LEU A 534 ? 0.21242 0.20925 0.21269 0.01210  0.00348  -0.00538 537 LEU A O   
4037 C CB  . LEU A 534 ? 0.22937 0.22161 0.22477 0.01130  0.00447  -0.00707 537 LEU A CB  
4038 C CG  . LEU A 534 ? 0.23723 0.22884 0.23217 0.01012  0.00351  -0.00590 537 LEU A CG  
4039 C CD1 . LEU A 534 ? 0.23035 0.21963 0.22497 0.01040  0.00317  -0.00544 537 LEU A CD1 
4040 C CD2 . LEU A 534 ? 0.29360 0.28493 0.28682 0.00832  0.00309  -0.00602 537 LEU A CD2 
4041 N N   . SER A 535 ? 0.20517 0.19889 0.20439 0.01361  0.00249  -0.00526 538 SER A N   
4042 C CA  . SER A 535 ? 0.18966 0.18473 0.18989 0.01380  0.00149  -0.00497 538 SER A CA  
4043 C C   . SER A 535 ? 0.19984 0.19453 0.19825 0.01336  0.00144  -0.00489 538 SER A C   
4044 O O   . SER A 535 ? 0.23540 0.22877 0.23165 0.01323  0.00164  -0.00439 538 SER A O   
4045 C CB  . SER A 535 ? 0.23096 0.22602 0.23241 0.01504  0.00031  -0.00490 538 SER A CB  
4046 O OG  . SER A 535 ? 0.29479 0.29068 0.29670 0.01505  -0.00102 -0.00506 538 SER A OG  
4047 N N   . THR A 536 ? 0.23469 0.23071 0.23436 0.01306  0.00116  -0.00532 539 THR A N   
4048 C CA  . THR A 536 ? 0.24109 0.23800 0.24045 0.01272  0.00172  -0.00572 539 THR A CA  
4049 C C   . THR A 536 ? 0.24060 0.23870 0.24146 0.01366  0.00097  -0.00716 539 THR A C   
4050 O O   . THR A 536 ? 0.22682 0.22440 0.22929 0.01413  -0.00050 -0.00754 539 THR A O   
4051 C CB  . THR A 536 ? 0.24209 0.23943 0.24272 0.01162  0.00185  -0.00529 539 THR A CB  
4052 O OG1 . THR A 536 ? 0.25351 0.25128 0.25656 0.01160  0.00050  -0.00523 539 THR A OG1 
4053 C CG2 . THR A 536 ? 0.25189 0.24756 0.25078 0.01076  0.00229  -0.00465 539 THR A CG2 
4054 N N   . SER A 537 ? 0.21331 0.21322 0.21405 0.01383  0.00203  -0.00819 540 SER A N   
4055 C CA  . SER A 537 ? 0.20677 0.20805 0.20963 0.01515  0.00155  -0.01050 540 SER A CA  
4056 C C   . SER A 537 ? 0.25949 0.26420 0.26330 0.01516  0.00355  -0.01157 540 SER A C   
4057 O O   . SER A 537 ? 0.22557 0.23139 0.22692 0.01382  0.00532  -0.01030 540 SER A O   
4058 C CB  . SER A 537 ? 0.23046 0.23093 0.23065 0.01606  0.00087  -0.01196 540 SER A CB  
4059 O OG  . SER A 537 ? 0.31978 0.32083 0.31523 0.01541  0.00232  -0.01133 540 SER A OG  
4060 N N   A GLN A 538 ? 0.21699 0.22344 0.22520 0.01658  0.00307  -0.01379 541 GLN A N   
4061 N N   B GLN A 538 ? 0.21790 0.22436 0.22594 0.01665  0.00311  -0.01393 541 GLN A N   
4062 C CA  A GLN A 538 ? 0.25477 0.26588 0.26521 0.01720  0.00529  -0.01582 541 GLN A CA  
4063 C CA  B GLN A 538 ? 0.25572 0.26687 0.26634 0.01724  0.00527  -0.01586 541 GLN A CA  
4064 C C   A GLN A 538 ? 0.28506 0.29740 0.29307 0.01877  0.00631  -0.01920 541 GLN A C   
4065 C C   B GLN A 538 ? 0.28317 0.29596 0.29186 0.01892  0.00642  -0.01945 541 GLN A C   
4066 O O   A GLN A 538 ? 0.24915 0.25893 0.25819 0.02042  0.00411  -0.02125 541 GLN A O   
4067 O O   B GLN A 538 ? 0.24387 0.25477 0.25470 0.02086  0.00440  -0.02197 541 GLN A O   
4068 C CB  A GLN A 538 ? 0.26443 0.27713 0.28230 0.01838  0.00392  -0.01683 541 GLN A CB  
4069 C CB  B GLN A 538 ? 0.26406 0.27637 0.28198 0.01825  0.00366  -0.01651 541 GLN A CB  
4070 C CG  A GLN A 538 ? 0.26169 0.28064 0.28340 0.01879  0.00662  -0.01861 541 GLN A CG  
4071 C CG  B GLN A 538 ? 0.28091 0.29923 0.30371 0.01932  0.00584  -0.01897 541 GLN A CG  
4072 C CD  A GLN A 538 ? 0.34369 0.36467 0.37414 0.02101  0.00488  -0.02071 541 GLN A CD  
4073 C CD  B GLN A 538 ? 0.35628 0.37532 0.38757 0.02099  0.00325  -0.01991 541 GLN A CD  
4074 O OE1 A GLN A 538 ? 0.36368 0.38150 0.39738 0.02093  0.00138  -0.01893 541 GLN A OE1 
4075 O OE1 B GLN A 538 ? 0.22760 0.24902 0.26293 0.01998  0.00289  -0.01830 541 GLN A OE1 
4076 N NE2 A GLN A 538 ? 0.28146 0.30790 0.31579 0.02301  0.00723  -0.02454 541 GLN A NE2 
4077 N NE2 B GLN A 538 ? 0.25553 0.27205 0.28976 0.02346  0.00085  -0.02239 541 GLN A NE2 
4078 N N   . VAL A 539 ? 0.26664 0.28263 0.27086 0.01791  0.00944  -0.01965 542 VAL A N   
4079 C CA  . VAL A 539 ? 0.25967 0.27792 0.26086 0.01928  0.01094  -0.02346 542 VAL A CA  
4080 C C   . VAL A 539 ? 0.27703 0.30253 0.28040 0.01921  0.01493  -0.02529 542 VAL A C   
4081 O O   . VAL A 539 ? 0.28599 0.31444 0.28483 0.01671  0.01771  -0.02320 542 VAL A O   
4082 C CB  . VAL A 539 ? 0.36599 0.38193 0.35845 0.01792  0.01082  -0.02220 542 VAL A CB  
4083 C CG1 . VAL A 539 ? 0.33523 0.35321 0.32395 0.01945  0.01191  -0.02690 542 VAL A CG1 
4084 C CG2 . VAL A 539 ? 0.36877 0.37870 0.36079 0.01784  0.00706  -0.02003 542 VAL A CG2 
4085 N N   . PRO A 540 ? 0.26989 0.29859 0.28078 0.02177  0.01517  -0.02894 543 PRO A N   
4086 C CA  . PRO A 540 ? 0.29629 0.33335 0.31101 0.02194  0.01929  -0.03107 543 PRO A CA  
4087 C C   . PRO A 540 ? 0.36453 0.40591 0.37351 0.02254  0.02292  -0.03511 543 PRO A C   
4088 O O   . PRO A 540 ? 0.34332 0.38145 0.34891 0.02456  0.02146  -0.03859 543 PRO A O   
4089 C CB  . PRO A 540 ? 0.41579 0.45398 0.44143 0.02518  0.01734  -0.03402 543 PRO A CB  
4090 C CG  . PRO A 540 ? 0.35779 0.38837 0.38303 0.02720  0.01288  -0.03526 543 PRO A CG  
4091 C CD  . PRO A 540 ? 0.34306 0.36785 0.36025 0.02445  0.01130  -0.03082 543 PRO A CD  
4092 N N   . THR A 541 ? 0.28572 0.33467 0.29328 0.02043  0.02765  -0.03461 544 THR A N   
4093 C CA  . THR A 541 ? 0.33702 0.39165 0.33866 0.02065  0.03191  -0.03863 544 THR A CA  
4094 C C   . THR A 541 ? 0.40672 0.47232 0.41585 0.02115  0.03690  -0.04143 544 THR A C   
4095 O O   . THR A 541 ? 0.37838 0.44687 0.39575 0.02023  0.03688  -0.03883 544 THR A O   
4096 C CB  . THR A 541 ? 0.43901 0.49269 0.42846 0.01641  0.03333  -0.03443 544 THR A CB  
4097 O OG1 . THR A 541 ? 0.48462 0.54194 0.47528 0.01248  0.03545  -0.02919 544 THR A OG1 
4098 C CG2 . THR A 541 ? 0.36543 0.40913 0.34912 0.01593  0.02830  -0.03133 544 THR A CG2 
4099 N N   . THR A 542 ? 0.39316 0.46535 0.39934 0.02254  0.04123  -0.04698 545 THR A N   
4100 C CA  . THR A 542 ? 0.52484 0.60923 0.53841 0.02325  0.04688  -0.05052 545 THR A CA  
4101 C C   . THR A 542 ? 0.46844 0.56080 0.47417 0.01828  0.05273  -0.04764 545 THR A C   
4102 O O   . THR A 542 ? 0.56825 0.67131 0.58092 0.01718  0.05744  -0.04807 545 THR A O   
4103 C CB  . THR A 542 ? 0.44817 0.53616 0.46542 0.02866  0.04851  -0.05985 545 THR A CB  
4104 O OG1 . THR A 542 ? 0.91591 1.00779 0.92128 0.02748  0.05291  -0.06299 545 THR A OG1 
4105 C CG2 . THR A 542 ? 0.63216 0.70910 0.65145 0.03258  0.04188  -0.06219 545 THR A CG2 
4106 N N   . THR A 543 ? 0.37023 0.45787 0.36210 0.01510  0.05231  -0.04454 546 THR A N   
4107 C CA  . THR A 543 ? 0.49972 0.59290 0.48240 0.00956  0.05672  -0.04032 546 THR A CA  
4108 C C   . THR A 543 ? 0.57628 0.66317 0.55725 0.00494  0.05340  -0.03131 546 THR A C   
4109 O O   . THR A 543 ? 0.50174 0.58214 0.48974 0.00618  0.04879  -0.02910 546 THR A O   
4110 C CB  . THR A 543 ? 0.61589 0.70739 0.58389 0.00893  0.05763  -0.04255 546 THR A CB  
4111 O OG1 . THR A 543 ? 0.67585 0.75506 0.63965 0.01079  0.05101  -0.04194 546 THR A OG1 
4112 C CG2 . THR A 543 ? 0.56262 0.66258 0.53173 0.01282  0.06241  -0.05197 546 THR A CG2 
4113 N N   . GLU A 544 ? 0.39063 0.47913 0.36179 -0.00052 0.05556  -0.02611 547 GLU A N   
4114 C CA  . GLU A 544 ? 0.50721 0.58898 0.47598 -0.00495 0.05216  -0.01779 547 GLU A CA  
4115 C C   . GLU A 544 ? 0.55135 0.62040 0.51267 -0.00424 0.04594  -0.01530 547 GLU A C   
4116 O O   . GLU A 544 ? 0.53300 0.59572 0.49148 -0.00755 0.04284  -0.00882 547 GLU A O   
4117 C CB  . GLU A 544 ? 0.74937 0.83716 0.71078 -0.01141 0.05629  -0.01261 547 GLU A CB  
4118 C CG  . GLU A 544 ? 0.90193 1.00464 0.86886 -0.01241 0.06376  -0.01583 547 GLU A CG  
4119 C CD  . GLU A 544 ? 0.95154 1.06150 0.90867 -0.01218 0.06895  -0.02068 547 GLU A CD  
4120 O OE1 . GLU A 544 ? 0.78741 0.90436 0.73686 -0.01774 0.07354  -0.01715 547 GLU A OE1 
4121 O OE2 . GLU A 544 ? 0.77608 0.88457 0.73280 -0.00672 0.06831  -0.02797 547 GLU A OE2 
4122 N N   . MET A 545 ? 0.34812 0.41329 0.30698 -0.00004 0.04381  -0.02031 548 MET A N   
4123 C CA  . MET A 545 ? 0.34563 0.39996 0.29816 0.00027  0.03807  -0.01773 548 MET A CA  
4124 C C   . MET A 545 ? 0.38858 0.43575 0.34952 0.00189  0.03346  -0.01550 548 MET A C   
4125 O O   . MET A 545 ? 0.31017 0.35983 0.28135 0.00389  0.03398  -0.01747 548 MET A O   
4126 C CB  . MET A 545 ? 0.45885 0.51131 0.40623 0.00369  0.03688  -0.02356 548 MET A CB  
4127 C CG  . MET A 545 ? 0.58587 0.63490 0.54191 0.00881  0.03403  -0.02852 548 MET A CG  
4128 S SD  . MET A 545 ? 0.55848 0.60357 0.50741 0.01192  0.03150  -0.03461 548 MET A SD  
4129 C CE  . MET A 545 ? 0.53495 0.58776 0.47137 0.00911  0.03686  -0.03642 548 MET A CE  
4130 N N   . PHE A 546 ? 0.31335 0.35182 0.26989 0.00096  0.02885  -0.01135 549 PHE A N   
4131 C CA  . PHE A 546 ? 0.27293 0.30492 0.23634 0.00242  0.02485  -0.00959 549 PHE A CA  
4132 C C   . PHE A 546 ? 0.29295 0.31677 0.25173 0.00338  0.02007  -0.00824 549 PHE A C   
4133 O O   . PHE A 546 ? 0.28197 0.30419 0.23198 0.00194  0.01916  -0.00686 549 PHE A O   
4134 C CB  . PHE A 546 ? 0.31649 0.34795 0.28341 -0.00074 0.02493  -0.00460 549 PHE A CB  
4135 C CG  . PHE A 546 ? 0.32523 0.35335 0.28452 -0.00487 0.02393  0.00114  549 PHE A CG  
4136 C CD1 . PHE A 546 ? 0.38335 0.40271 0.34056 -0.00477 0.01921  0.00433  549 PHE A CD1 
4137 C CD2 . PHE A 546 ? 0.34184 0.37574 0.29656 -0.00897 0.02759  0.00356  549 PHE A CD2 
4138 C CE1 . PHE A 546 ? 0.32395 0.33936 0.27495 -0.00832 0.01747  0.00977  549 PHE A CE1 
4139 C CE2 . PHE A 546 ? 0.34850 0.37842 0.29608 -0.01322 0.02595  0.00966  549 PHE A CE2 
4140 C CZ  . PHE A 546 ? 0.37033 0.39048 0.31625 -0.01270 0.02054  0.01275  549 PHE A CZ  
4141 N N   . CYS A 547 ? 0.26034 0.27956 0.22530 0.00575  0.01699  -0.00870 550 CYS A N   
4142 C CA  . CYS A 547 ? 0.25899 0.27194 0.22237 0.00731  0.01274  -0.00844 550 CYS A CA  
4143 C C   . CYS A 547 ? 0.31461 0.32243 0.28077 0.00658  0.01019  -0.00443 550 CYS A C   
4144 O O   . CYS A 547 ? 0.27629 0.28474 0.24762 0.00607  0.01113  -0.00352 550 CYS A O   
4145 C CB  . CYS A 547 ? 0.30632 0.31900 0.27500 0.01075  0.01158  -0.01300 550 CYS A CB  
4146 S SG  . CYS A 547 ? 0.39929 0.41745 0.36643 0.01252  0.01436  -0.01912 550 CYS A SG  
4147 N N   . CYS A 548 ? 0.25577 0.25863 0.21885 0.00670  0.00676  -0.00241 551 CYS A N   
4148 C CA  . CYS A 548 ? 0.28085 0.27902 0.24718 0.00664  0.00443  0.00049  551 CYS A CA  
4149 C C   . CYS A 548 ? 0.30726 0.30160 0.27367 0.00840  0.00068  0.00053  551 CYS A C   
4150 O O   . CYS A 548 ? 0.27392 0.26852 0.23649 0.00889  -0.00066 -0.00069 551 CYS A O   
4151 C CB  . CYS A 548 ? 0.29667 0.29294 0.25967 0.00361  0.00439  0.00489  551 CYS A CB  
4152 S SG  . CYS A 548 ? 0.32182 0.31707 0.27485 0.00134  0.00295  0.00779  551 CYS A SG  
4153 N N   . TYR A 549 ? 0.22813 0.21931 0.19927 0.00935  -0.00099 0.00161  552 TYR A N   
4154 C CA  . TYR A 549 ? 0.26714 0.25560 0.24009 0.01103  -0.00435 0.00185  552 TYR A CA  
4155 C C   . TYR A 549 ? 0.25595 0.24130 0.23329 0.01164  -0.00534 0.00332  552 TYR A C   
4156 O O   . TYR A 549 ? 0.27498 0.26005 0.25398 0.01088  -0.00355 0.00356  552 TYR A O   
4157 C CB  . TYR A 549 ? 0.24751 0.23793 0.22420 0.01288  -0.00467 -0.00132 552 TYR A CB  
4158 C CG  . TYR A 549 ? 0.23789 0.23042 0.21905 0.01326  -0.00219 -0.00317 552 TYR A CG  
4159 C CD1 . TYR A 549 ? 0.26746 0.25913 0.25325 0.01373  -0.00193 -0.00275 552 TYR A CD1 
4160 C CD2 . TYR A 549 ? 0.26786 0.26325 0.24851 0.01323  -0.00031 -0.00546 552 TYR A CD2 
4161 C CE1 . TYR A 549 ? 0.31979 0.31315 0.30881 0.01372  -0.00024 -0.00401 552 TYR A CE1 
4162 C CE2 . TYR A 549 ? 0.29175 0.28875 0.27688 0.01359  0.00118  -0.00672 552 TYR A CE2 
4163 C CZ  . TYR A 549 ? 0.30159 0.29739 0.29045 0.01362  0.00100  -0.00569 552 TYR A CZ  
4164 O OH  . TYR A 549 ? 0.34217 0.33934 0.33466 0.01366  0.00189  -0.00655 552 TYR A OH  
4165 N N   . GLY A 550 ? 0.26025 0.24348 0.23996 0.01319  -0.00838 0.00391  553 GLY A N   
4166 C CA  . GLY A 550 ? 0.22211 0.20268 0.20661 0.01442  -0.00930 0.00442  553 GLY A CA  
4167 C C   . GLY A 550 ? 0.21781 0.20094 0.20807 0.01593  -0.00746 0.00164  553 GLY A C   
4168 O O   . GLY A 550 ? 0.24594 0.23230 0.23687 0.01589  -0.00609 -0.00007 553 GLY A O   
4169 N N   . PRO A 551 ? 0.24070 0.22217 0.23499 0.01718  -0.00753 0.00117  554 PRO A N   
4170 C CA  . PRO A 551 ? 0.22242 0.20680 0.22152 0.01839  -0.00569 -0.00130 554 PRO A CA  
4171 C C   . PRO A 551 ? 0.26280 0.25020 0.26613 0.01982  -0.00696 -0.00198 554 PRO A C   
4172 O O   . PRO A 551 ? 0.27793 0.26445 0.28138 0.02043  -0.00987 -0.00076 554 PRO A O   
4173 C CB  . PRO A 551 ? 0.23523 0.21676 0.23677 0.01952  -0.00564 -0.00203 554 PRO A CB  
4174 C CG  . PRO A 551 ? 0.23601 0.21234 0.23406 0.01846  -0.00765 0.00048  554 PRO A CG  
4175 C CD  . PRO A 551 ? 0.23827 0.21492 0.23283 0.01754  -0.00951 0.00276  554 PRO A CD  
4176 N N   . VAL A 552 ? 0.21194 0.20303 0.21895 0.02008  -0.00501 -0.00368 555 VAL A N   
4177 C CA  . VAL A 552 ? 0.20429 0.19911 0.21639 0.02090  -0.00595 -0.00413 555 VAL A CA  
4178 C C   . VAL A 552 ? 0.27673 0.27412 0.29517 0.02273  -0.00497 -0.00554 555 VAL A C   
4179 O O   . VAL A 552 ? 0.22824 0.22959 0.25226 0.02340  -0.00574 -0.00577 555 VAL A O   
4180 C CB  . VAL A 552 ? 0.22613 0.22391 0.23822 0.01930  -0.00490 -0.00449 555 VAL A CB  
4181 C CG1 . VAL A 552 ? 0.24232 0.23797 0.24905 0.01817  -0.00593 -0.00400 555 VAL A CG1 
4182 C CG2 . VAL A 552 ? 0.25618 0.25557 0.26829 0.01834  -0.00174 -0.00533 555 VAL A CG2 
4183 N N   . VAL A 553 ? 0.23127 0.22696 0.24942 0.02352  -0.00324 -0.00682 556 VAL A N   
4184 C CA  . VAL A 553 ? 0.24920 0.24703 0.27334 0.02590  -0.00223 -0.00903 556 VAL A CA  
4185 C C   . VAL A 553 ? 0.21848 0.21041 0.24178 0.02751  -0.00377 -0.00939 556 VAL A C   
4186 O O   . VAL A 553 ? 0.25789 0.24502 0.27534 0.02595  -0.00440 -0.00799 556 VAL A O   
4187 C CB  . VAL A 553 ? 0.23390 0.23598 0.25844 0.02513  0.00190  -0.01120 556 VAL A CB  
4188 C CG1 . VAL A 553 ? 0.31992 0.32751 0.34610 0.02316  0.00285  -0.01015 556 VAL A CG1 
4189 C CG2 . VAL A 553 ? 0.23122 0.22947 0.24904 0.02350  0.00324  -0.01147 556 VAL A CG2 
4190 N N   . PRO A 554 ? 0.22333 0.21557 0.25309 0.03061  -0.00458 -0.01124 557 PRO A N   
4191 C CA  . PRO A 554 ? 0.24397 0.22933 0.27376 0.03230  -0.00717 -0.01130 557 PRO A CA  
4192 C C   . PRO A 554 ? 0.25082 0.23220 0.27601 0.03136  -0.00526 -0.01294 557 PRO A C   
4193 O O   . PRO A 554 ? 0.24094 0.21541 0.26334 0.03091  -0.00778 -0.01147 557 PRO A O   
4194 C CB  . PRO A 554 ? 0.30395 0.29181 0.34342 0.03637  -0.00797 -0.01394 557 PRO A CB  
4195 C CG  . PRO A 554 ? 0.35438 0.34998 0.39857 0.03623  -0.00737 -0.01348 557 PRO A CG  
4196 C CD  . PRO A 554 ? 0.23823 0.23716 0.27658 0.03272  -0.00381 -0.01301 557 PRO A CD  
4197 N N   . ASN A 555 ? 0.24241 0.22776 0.26633 0.03059  -0.00122 -0.01560 558 ASN A N   
4198 C CA  . ASN A 555 ? 0.20683 0.18852 0.22601 0.02945  0.00017  -0.01734 558 ASN A CA  
4199 C C   . ASN A 555 ? 0.24421 0.22621 0.25674 0.02567  0.00117  -0.01500 558 ASN A C   
4200 O O   . ASN A 555 ? 0.24626 0.22785 0.25511 0.02420  0.00293  -0.01648 558 ASN A O   
4201 C CB  . ASN A 555 ? 0.23421 0.21961 0.25554 0.03112  0.00369  -0.02227 558 ASN A CB  
4202 C CG  . ASN A 555 ? 0.34145 0.33510 0.36222 0.02943  0.00740  -0.02245 558 ASN A CG  
4203 O OD1 . ASN A 555 ? 0.28133 0.27868 0.30377 0.02845  0.00694  -0.01969 558 ASN A OD1 
4204 N ND2 . ASN A 555 ? 0.30829 0.30451 0.32634 0.02885  0.01080  -0.02565 558 ASN A ND2 
4205 N N   . GLY A 556 ? 0.21189 0.19452 0.22288 0.02416  -0.00020 -0.01157 559 GLY A N   
4206 C CA  . GLY A 556 ? 0.20541 0.18954 0.21184 0.02125  0.00091  -0.00998 559 GLY A CA  
4207 C C   . GLY A 556 ? 0.24088 0.22095 0.24328 0.01934  -0.00076 -0.00733 559 GLY A C   
4208 O O   . GLY A 556 ? 0.21079 0.18636 0.21302 0.01970  -0.00305 -0.00598 559 GLY A O   
4209 N N   . TYR A 557 ? 0.21067 0.19282 0.21021 0.01717  0.00037  -0.00641 560 TYR A N   
4210 C CA  . TYR A 557 ? 0.22500 0.20581 0.22132 0.01514  -0.00025 -0.00414 560 TYR A CA  
4211 C C   . TYR A 557 ? 0.22397 0.20842 0.21973 0.01475  0.00003  -0.00331 560 TYR A C   
4212 O O   . TYR A 557 ? 0.21378 0.20147 0.21117 0.01509  0.00089  -0.00435 560 TYR A O   
4213 C CB  . TYR A 557 ? 0.20520 0.18567 0.19968 0.01307  0.00079  -0.00443 560 TYR A CB  
4214 C CG  . TYR A 557 ? 0.21276 0.18885 0.20697 0.01286  0.00012  -0.00547 560 TYR A CG  
4215 C CD1 . TYR A 557 ? 0.25605 0.22764 0.24926 0.01164  -0.00158 -0.00362 560 TYR A CD1 
4216 C CD2 . TYR A 557 ? 0.23202 0.20825 0.22664 0.01366  0.00106  -0.00835 560 TYR A CD2 
4217 C CE1 . TYR A 557 ? 0.25182 0.21829 0.24513 0.01138  -0.00281 -0.00481 560 TYR A CE1 
4218 C CE2 . TYR A 557 ? 0.22210 0.19379 0.21612 0.01361  0.00024  -0.01008 560 TYR A CE2 
4219 C CZ  . TYR A 557 ? 0.21998 0.18641 0.21374 0.01259  -0.00194 -0.00840 560 TYR A CZ  
4220 O OH  . TYR A 557 ? 0.26236 0.22339 0.25585 0.01246  -0.00331 -0.01032 560 TYR A OH  
4221 N N   . GLY A 558 ? 0.21589 0.19971 0.20900 0.01375  -0.00071 -0.00150 561 GLY A N   
4222 C CA  . GLY A 558 ? 0.19588 0.18291 0.18761 0.01307  0.00001  -0.00150 561 GLY A CA  
4223 C C   . GLY A 558 ? 0.23811 0.22603 0.22828 0.01110  0.00143  -0.00097 561 GLY A C   
4224 O O   . GLY A 558 ? 0.23305 0.21870 0.22158 0.00966  0.00123  0.00064  561 GLY A O   
4225 N N   . ALA A 559 ? 0.21795 0.20915 0.20947 0.01097  0.00257  -0.00220 562 ALA A N   
4226 C CA  . ALA A 559 ? 0.23178 0.22495 0.22343 0.00934  0.00387  -0.00194 562 ALA A CA  
4227 C C   . ALA A 559 ? 0.26892 0.26601 0.26147 0.00991  0.00478  -0.00334 562 ALA A C   
4228 O O   . ALA A 559 ? 0.29498 0.29319 0.29030 0.01093  0.00435  -0.00472 562 ALA A O   
4229 C CB  . ALA A 559 ? 0.23677 0.22945 0.23054 0.00867  0.00383  -0.00234 562 ALA A CB  
4230 N N   . CYS A 560 ? 0.18583 0.18497 0.17602 0.00916  0.00598  -0.00306 563 CYS A N   
4231 C CA  . CYS A 560 ? 0.17391 0.17700 0.16482 0.01007  0.00716  -0.00530 563 CYS A CA  
4232 C C   . CYS A 560 ? 0.26819 0.27556 0.26103 0.00862  0.00942  -0.00526 563 CYS A C   
4233 O O   . CYS A 560 ? 0.31258 0.32017 0.30306 0.00634  0.01043  -0.00303 563 CYS A O   
4234 C CB  . CYS A 560 ? 0.23862 0.24162 0.22459 0.01040  0.00705  -0.00568 563 CYS A CB  
4235 S SG  . CYS A 560 ? 0.29066 0.29763 0.27726 0.01226  0.00812  -0.00988 563 CYS A SG  
4236 N N   . TYR A 561 ? 0.23411 0.24489 0.23199 0.00977  0.00991  -0.00744 564 TYR A N   
4237 C CA  . TYR A 561 ? 0.23863 0.25433 0.24010 0.00847  0.01188  -0.00741 564 TYR A CA  
4238 C C   . TYR A 561 ? 0.26757 0.28888 0.27226 0.01030  0.01375  -0.01085 564 TYR A C   
4239 O O   . TYR A 561 ? 0.20921 0.22954 0.21505 0.01287  0.01256  -0.01351 564 TYR A O   
4240 C CB  . TYR A 561 ? 0.21238 0.22733 0.21861 0.00780  0.01028  -0.00646 564 TYR A CB  
4241 C CG  . TYR A 561 ? 0.24062 0.25347 0.24964 0.00986  0.00785  -0.00773 564 TYR A CG  
4242 C CD1 . TYR A 561 ? 0.23915 0.24704 0.24527 0.01010  0.00602  -0.00683 564 TYR A CD1 
4243 C CD2 . TYR A 561 ? 0.25678 0.27283 0.27176 0.01149  0.00730  -0.00972 564 TYR A CD2 
4244 C CE1 . TYR A 561 ? 0.25277 0.25908 0.26104 0.01127  0.00392  -0.00737 564 TYR A CE1 
4245 C CE2 . TYR A 561 ? 0.22197 0.23537 0.23931 0.01287  0.00448  -0.01012 564 TYR A CE2 
4246 C CZ  . TYR A 561 ? 0.24519 0.25383 0.25871 0.01245  0.00294  -0.00871 564 TYR A CZ  
4247 O OH  . TYR A 561 ? 0.26965 0.27599 0.28504 0.01315  0.00030  -0.00851 564 TYR A OH  
4248 N N   . ASN A 562 ? 0.20951 0.23688 0.21602 0.00886  0.01672  -0.01091 565 ASN A N   
4249 C CA  . ASN A 562 ? 0.23528 0.26950 0.24499 0.01058  0.01950  -0.01471 565 ASN A CA  
4250 C C   . ASN A 562 ? 0.26745 0.30773 0.28565 0.00989  0.02062  -0.01472 565 ASN A C   
4251 O O   . ASN A 562 ? 0.24672 0.29137 0.26492 0.00681  0.02312  -0.01259 565 ASN A O   
4252 C CB  . ASN A 562 ? 0.23697 0.27414 0.23946 0.00904  0.02279  -0.01476 565 ASN A CB  
4253 C CG  . ASN A 562 ? 0.35573 0.40045 0.36026 0.01100  0.02633  -0.01960 565 ASN A CG  
4254 O OD1 . ASN A 562 ? 0.31437 0.36275 0.32728 0.01362  0.02646  -0.02292 565 ASN A OD1 
4255 N ND2 . ASN A 562 ? 0.47589 0.52301 0.47259 0.00970  0.02911  -0.02006 565 ASN A ND2 
4256 N N   . PRO A 563 ? 0.22550 0.26609 0.25134 0.01237  0.01837  -0.01663 566 PRO A N   
4257 C CA  . PRO A 563 ? 0.30023 0.34648 0.33517 0.01186  0.01849  -0.01647 566 PRO A CA  
4258 C C   . PRO A 563 ? 0.31474 0.37057 0.35563 0.01355  0.02239  -0.02041 566 PRO A C   
4259 O O   . PRO A 563 ? 0.28430 0.34095 0.32585 0.01700  0.02303  -0.02474 566 PRO A O   
4260 C CB  . PRO A 563 ? 0.28169 0.32348 0.32152 0.01400  0.01376  -0.01673 566 PRO A CB  
4261 C CG  . PRO A 563 ? 0.37107 0.40803 0.40716 0.01666  0.01252  -0.01890 566 PRO A CG  
4262 C CD  . PRO A 563 ? 0.30812 0.34328 0.33467 0.01536  0.01493  -0.01838 566 PRO A CD  
4263 N N   . GLN A 564 ? 0.23511 0.29833 0.28058 0.01104  0.02503  -0.01914 567 GLN A N   
4264 C CA  . GLN A 564 ? 0.24320 0.31754 0.29522 0.01213  0.02964  -0.02274 567 GLN A CA  
4265 C C   . GLN A 564 ? 0.26062 0.34044 0.32561 0.01252  0.02800  -0.02269 567 GLN A C   
4266 O O   . GLN A 564 ? 0.22176 0.29597 0.28811 0.01131  0.02339  -0.01950 567 GLN A O   
4267 C CB  . GLN A 564 ? 0.30207 0.38166 0.34773 0.00797  0.03475  -0.02067 567 GLN A CB  
4268 C CG  . GLN A 564 ? 0.29503 0.36945 0.32781 0.00766  0.03583  -0.02070 567 GLN A CG  
4269 C CD  . GLN A 564 ? 0.39850 0.47556 0.43109 0.01206  0.03767  -0.02698 567 GLN A CD  
4270 O OE1 . GLN A 564 ? 0.32547 0.41181 0.36578 0.01412  0.04099  -0.03127 567 GLN A OE1 
4271 N NE2 . GLN A 564 ? 0.42824 0.49725 0.45291 0.01374  0.03527  -0.02796 567 GLN A NE2 
4272 N N   . PRO A 565 ? 0.27443 0.36525 0.34927 0.01427  0.03140  -0.02636 568 PRO A N   
4273 C CA  . PRO A 565 ? 0.25079 0.34679 0.33929 0.01493  0.02892  -0.02623 568 PRO A CA  
4274 C C   . PRO A 565 ? 0.26454 0.36004 0.35364 0.00969  0.02709  -0.02054 568 PRO A C   
4275 O O   . PRO A 565 ? 0.24690 0.33969 0.34217 0.00987  0.02191  -0.01897 568 PRO A O   
4276 C CB  . PRO A 565 ? 0.31732 0.42708 0.41551 0.01714  0.03448  -0.03124 568 PRO A CB  
4277 C CG  . PRO A 565 ? 0.31109 0.41905 0.40186 0.02053  0.03729  -0.03613 568 PRO A CG  
4278 C CD  . PRO A 565 ? 0.35329 0.45169 0.42817 0.01690  0.03682  -0.03185 568 PRO A CD  
4279 N N   . GLU A 566 ? 0.20978 0.30704 0.29218 0.00483  0.03064  -0.01728 569 GLU A N   
4280 C CA  . GLU A 566 ? 0.23031 0.32797 0.31435 -0.00051 0.02923  -0.01227 569 GLU A CA  
4281 C C   . GLU A 566 ? 0.23804 0.32541 0.30928 -0.00439 0.02778  -0.00775 569 GLU A C   
4282 O O   . GLU A 566 ? 0.24881 0.33469 0.32050 -0.00884 0.02603  -0.00376 569 GLU A O   
4283 C CB  . GLU A 566 ? 0.22710 0.33835 0.31841 -0.00369 0.03470  -0.01193 569 GLU A CB  
4284 C CG  . GLU A 566 ? 0.26866 0.39209 0.37449 0.00035  0.03686  -0.01694 569 GLU A CG  
4285 C CD  . GLU A 566 ? 0.45547 0.57671 0.57183 0.00291  0.03037  -0.01731 569 GLU A CD  
4286 O OE1 . GLU A 566 ? 0.55101 0.66711 0.66702 -0.00065 0.02581  -0.01295 569 GLU A OE1 
4287 O OE2 . GLU A 566 ? 0.68089 0.80491 0.80541 0.00844  0.02942  -0.02198 569 GLU A OE2 
4288 N N   . THR A 567 ? 0.26647 0.34647 0.32709 -0.00270 0.02798  -0.00845 570 THR A N   
4289 C CA  . THR A 567 ? 0.22005 0.29049 0.26935 -0.00564 0.02654  -0.00464 570 THR A CA  
4290 C C   . THR A 567 ? 0.24564 0.30669 0.28828 -0.00200 0.02368  -0.00622 570 THR A C   
4291 O O   . THR A 567 ? 0.23805 0.30021 0.28339 0.00227  0.02355  -0.01007 570 THR A O   
4292 C CB  . THR A 567 ? 0.23521 0.30867 0.27724 -0.00880 0.03118  -0.00283 570 THR A CB  
4293 O OG1 . THR A 567 ? 0.25163 0.32843 0.29076 -0.00531 0.03441  -0.00696 570 THR A OG1 
4294 C CG2 . THR A 567 ? 0.32986 0.41354 0.37801 -0.01329 0.03470  -0.00066 570 THR A CG2 
4295 N N   . ILE A 568 ? 0.22237 0.27419 0.25690 -0.00370 0.02126  -0.00332 571 ILE A N   
4296 C CA  . ILE A 568 ? 0.19434 0.23820 0.22217 -0.00085 0.01924  -0.00441 571 ILE A CA  
4297 C C   . ILE A 568 ? 0.24008 0.27858 0.25850 -0.00316 0.01970  -0.00158 571 ILE A C   
4298 O O   . ILE A 568 ? 0.28917 0.32384 0.30589 -0.00635 0.01822  0.00170  571 ILE A O   
4299 C CB  . ILE A 568 ? 0.22971 0.26696 0.25865 0.00033  0.01460  -0.00416 571 ILE A CB  
4300 C CG1 . ILE A 568 ? 0.21450 0.25623 0.25307 0.00188  0.01288  -0.00582 571 ILE A CG1 
4301 C CG2 . ILE A 568 ? 0.21699 0.24774 0.24000 0.00307  0.01320  -0.00533 571 ILE A CG2 
4302 C CD1 . ILE A 568 ? 0.26447 0.30007 0.30300 0.00146  0.00813  -0.00446 571 ILE A CD1 
4303 N N   . LEU A 569 ? 0.24119 0.27872 0.25367 -0.00150 0.02108  -0.00289 572 LEU A N   
4304 C CA  . LEU A 569 ? 0.19982 0.23193 0.20353 -0.00336 0.02074  -0.00006 572 LEU A CA  
4305 C C   . LEU A 569 ? 0.22007 0.24359 0.22059 -0.00114 0.01711  -0.00023 572 LEU A C   
4306 O O   . LEU A 569 ? 0.31342 0.33632 0.31477 0.00217  0.01633  -0.00313 572 LEU A O   
4307 C CB  . LEU A 569 ? 0.23586 0.27195 0.23414 -0.00315 0.02394  -0.00124 572 LEU A CB  
4308 C CG  . LEU A 569 ? 0.32438 0.35594 0.31373 -0.00613 0.02345  0.00278  572 LEU A CG  
4309 C CD1 . LEU A 569 ? 0.36741 0.40197 0.35702 -0.01117 0.02510  0.00698  572 LEU A CD1 
4310 C CD2 . LEU A 569 ? 0.46138 0.49493 0.44387 -0.00519 0.02528  0.00110  572 LEU A CD2 
4311 N N   . PHE A 570 ? 0.28040 0.29751 0.27784 -0.00296 0.01489  0.00275  573 PHE A N   
4312 C CA  . PHE A 570 ? 0.24759 0.25740 0.24233 -0.00102 0.01195  0.00258  573 PHE A CA  
4313 C C   . PHE A 570 ? 0.25357 0.25913 0.24185 -0.00190 0.01123  0.00493  573 PHE A C   
4314 O O   . PHE A 570 ? 0.30065 0.30481 0.28683 -0.00505 0.01117  0.00817  573 PHE A O   
4315 C CB  . PHE A 570 ? 0.20580 0.21130 0.20291 -0.00182 0.00956  0.00331  573 PHE A CB  
4316 C CG  . PHE A 570 ? 0.26093 0.26941 0.26366 -0.00094 0.00911  0.00139  573 PHE A CG  
4317 C CD1 . PHE A 570 ? 0.24306 0.25628 0.25066 -0.00307 0.00982  0.00195  573 PHE A CD1 
4318 C CD2 . PHE A 570 ? 0.23477 0.24144 0.23814 0.00171  0.00764  -0.00055 573 PHE A CD2 
4319 C CE1 . PHE A 570 ? 0.24615 0.26193 0.25923 -0.00222 0.00864  0.00050  573 PHE A CE1 
4320 C CE2 . PHE A 570 ? 0.23716 0.24599 0.24520 0.00223  0.00652  -0.00168 573 PHE A CE2 
4321 C CZ  . PHE A 570 ? 0.17749 0.19066 0.19041 0.00042  0.00677  -0.00118 573 PHE A CZ  
4322 N N   . CYS A 571 ? 0.24387 0.24716 0.22936 0.00063  0.01019  0.00364  574 CYS A N   
4323 C CA  . CYS A 571 ? 0.23942 0.23778 0.21970 0.00032  0.00831  0.00588  574 CYS A CA  
4324 C C   . CYS A 571 ? 0.24670 0.23960 0.22882 0.00248  0.00559  0.00522  574 CYS A C   
4325 O O   . CYS A 571 ? 0.24593 0.23944 0.22986 0.00506  0.00524  0.00272  574 CYS A O   
4326 C CB  . CYS A 571 ? 0.27153 0.27188 0.24739 0.00138  0.00884  0.00486  574 CYS A CB  
4327 S SG  . CYS A 571 ? 0.31235 0.31981 0.28459 -0.00130 0.01273  0.00526  574 CYS A SG  
4328 N N   . ILE A 572 ? 0.22598 0.21369 0.20790 0.00135  0.00370  0.00733  575 ILE A N   
4329 C CA  . ILE A 572 ? 0.20685 0.19014 0.19115 0.00343  0.00174  0.00601  575 ILE A CA  
4330 C C   . ILE A 572 ? 0.21332 0.19147 0.19575 0.00429  -0.00092 0.00766  575 ILE A C   
4331 O O   . ILE A 572 ? 0.24334 0.21814 0.22341 0.00215  -0.00232 0.01082  575 ILE A O   
4332 C CB  . ILE A 572 ? 0.25994 0.24115 0.24665 0.00206  0.00141  0.00583  575 ILE A CB  
4333 C CG1 . ILE A 572 ? 0.26368 0.25031 0.25307 0.00159  0.00336  0.00418  575 ILE A CG1 
4334 C CG2 . ILE A 572 ? 0.24729 0.22389 0.23554 0.00438  -0.00032 0.00388  575 ILE A CG2 
4335 C CD1 . ILE A 572 ? 0.32111 0.30714 0.31243 -0.00096 0.00301  0.00485  575 ILE A CD1 
4336 N N   . SER A 573 ? 0.18793 0.16559 0.17198 0.00725  -0.00191 0.00581  576 SER A N   
4337 C CA  . SER A 573 ? 0.19006 0.16340 0.17415 0.00872  -0.00484 0.00695  576 SER A CA  
4338 C C   . SER A 573 ? 0.23489 0.20604 0.22355 0.01129  -0.00554 0.00444  576 SER A C   
4339 O O   . SER A 573 ? 0.24546 0.21945 0.23624 0.01211  -0.00361 0.00175  576 SER A O   
4340 C CB  . SER A 573 ? 0.20342 0.17905 0.18599 0.00996  -0.00564 0.00696  576 SER A CB  
4341 O OG  . SER A 573 ? 0.21453 0.19418 0.19993 0.01170  -0.00410 0.00392  576 SER A OG  
4342 N N   . SER A 574 ? 0.22053 0.18666 0.21063 0.01251  -0.00841 0.00534  577 SER A N   
4343 C CA  . SER A 574 ? 0.24249 0.20708 0.23753 0.01561  -0.00902 0.00240  577 SER A CA  
4344 C C   . SER A 574 ? 0.26667 0.22650 0.26353 0.01720  -0.01298 0.00420  577 SER A C   
4345 O O   . SER A 574 ? 0.30887 0.26652 0.30218 0.01543  -0.01522 0.00801  577 SER A O   
4346 C CB  . SER A 574 ? 0.23078 0.19292 0.22661 0.01514  -0.00803 0.00027  577 SER A CB  
4347 O OG  . SER A 574 ? 0.27751 0.23358 0.27176 0.01307  -0.01032 0.00275  577 SER A OG  
4348 N N   . PHE A 575 ? 0.21454 0.17315 0.21697 0.02056  -0.01391 0.00147  578 PHE A N   
4349 C CA  . PHE A 575 ? 0.20585 0.15993 0.21182 0.02277  -0.01826 0.00284  578 PHE A CA  
4350 C C   . PHE A 575 ? 0.25842 0.20524 0.26708 0.02384  -0.02039 0.00177  578 PHE A C   
4351 O O   . PHE A 575 ? 0.25554 0.20286 0.26693 0.02549  -0.01819 -0.00265 578 PHE A O   
4352 C CB  . PHE A 575 ? 0.23928 0.19805 0.25158 0.02639  -0.01822 0.00029  578 PHE A CB  
4353 C CG  . PHE A 575 ? 0.24556 0.21002 0.25593 0.02543  -0.01755 0.00159  578 PHE A CG  
4354 C CD1 . PHE A 575 ? 0.26057 0.22325 0.26630 0.02359  -0.02054 0.00566  578 PHE A CD1 
4355 C CD2 . PHE A 575 ? 0.22297 0.19426 0.23594 0.02621  -0.01424 -0.00127 578 PHE A CD2 
4356 C CE1 . PHE A 575 ? 0.28669 0.25418 0.29044 0.02287  -0.02026 0.00612  578 PHE A CE1 
4357 C CE2 . PHE A 575 ? 0.30797 0.28367 0.31973 0.02532  -0.01422 -0.00031 578 PHE A CE2 
4358 C CZ  . PHE A 575 ? 0.28365 0.25726 0.29085 0.02385  -0.01733 0.00305  578 PHE A CZ  
4359 N N   . HIS A 576 ? 0.22719 0.16695 0.23495 0.02290  -0.02505 0.00578  579 HIS A N   
4360 C CA  . HIS A 576 ? 0.29652 0.22774 0.30724 0.02382  -0.02823 0.00520  579 HIS A CA  
4361 C C   . HIS A 576 ? 0.24490 0.17560 0.26429 0.02934  -0.02904 0.00007  579 HIS A C   
4362 O O   . HIS A 576 ? 0.30664 0.23152 0.32903 0.03089  -0.03024 -0.00287 579 HIS A O   
4363 C CB  . HIS A 576 ? 0.27717 0.20075 0.28563 0.02165  -0.03387 0.01137  579 HIS A CB  
4364 C CG  . HIS A 576 ? 0.29678 0.21937 0.29731 0.01580  -0.03313 0.01618  579 HIS A CG  
4365 N ND1 . HIS A 576 ? 0.30579 0.22592 0.30480 0.01311  -0.03163 0.01554  579 HIS A ND1 
4366 C CD2 . HIS A 576 ? 0.27453 0.19865 0.26846 0.01203  -0.03370 0.02161  579 HIS A CD2 
4367 C CE1 . HIS A 576 ? 0.42755 0.34846 0.42031 0.00793  -0.03104 0.02049  579 HIS A CE1 
4368 N NE2 . HIS A 576 ? 0.29349 0.21675 0.28272 0.00721  -0.03211 0.02416  579 HIS A NE2 
4369 N N   A SER A 577 ? 0.28580 0.22262 0.30965 0.03231  -0.02845 -0.00134 580 SER A N   
4370 N N   B SER A 577 ? 0.28539 0.22250 0.30919 0.03230  -0.02824 -0.00146 580 SER A N   
4371 C CA  A SER A 577 ? 0.28762 0.22558 0.32083 0.03767  -0.02864 -0.00649 580 SER A CA  
4372 C CA  B SER A 577 ? 0.28857 0.22708 0.32186 0.03770  -0.02855 -0.00642 580 SER A CA  
4373 C C   A SER A 577 ? 0.30158 0.24301 0.33542 0.03878  -0.02343 -0.01272 580 SER A C   
4374 C C   B SER A 577 ? 0.30537 0.24869 0.34003 0.03916  -0.02303 -0.01285 580 SER A C   
4375 O O   A SER A 577 ? 0.28716 0.22604 0.32671 0.04247  -0.02373 -0.01758 580 SER A O   
4376 O O   B SER A 577 ? 0.28694 0.23088 0.32894 0.04354  -0.02261 -0.01794 580 SER A O   
4377 C CB  A SER A 577 ? 0.28233 0.22767 0.32045 0.03987  -0.02872 -0.00633 580 SER A CB  
4378 C CB  B SER A 577 ? 0.28374 0.22865 0.32176 0.03975  -0.02946 -0.00555 580 SER A CB  
4379 O OG  A SER A 577 ? 0.25603 0.20810 0.28832 0.03670  -0.02513 -0.00487 580 SER A OG  
4380 O OG  B SER A 577 ? 0.25661 0.20328 0.30538 0.04510  -0.03029 -0.00990 580 SER A OG  
4381 N N   . CYS A 578 ? 0.29584 0.24290 0.32371 0.03567  -0.01888 -0.01279 581 CYS A N   
4382 C CA  . CYS A 578 ? 0.31796 0.26900 0.34507 0.03608  -0.01408 -0.01801 581 CYS A CA  
4383 C C   . CYS A 578 ? 0.33184 0.27553 0.35477 0.03417  -0.01489 -0.01896 581 CYS A C   
4384 O O   . CYS A 578 ? 0.29062 0.23222 0.30748 0.02994  -0.01530 -0.01517 581 CYS A O   
4385 C CB  . CYS A 578 ? 0.31855 0.27771 0.34123 0.03331  -0.00995 -0.01695 581 CYS A CB  
4386 S SG  . CYS A 578 ? 0.31815 0.28121 0.33767 0.03259  -0.00482 -0.02201 581 CYS A SG  
4387 N N   . ALA A 579 ? 0.32113 0.26112 0.34775 0.03730  -0.01517 -0.02431 582 ALA A N   
4388 C CA  . ALA A 579 ? 0.23224 0.16439 0.25549 0.03567  -0.01662 -0.02589 582 ALA A CA  
4389 C C   . ALA A 579 ? 0.27662 0.21241 0.29269 0.03190  -0.01292 -0.02661 582 ALA A C   
4390 O O   . ALA A 579 ? 0.35068 0.28068 0.36282 0.02883  -0.01463 -0.02568 582 ALA A O   
4391 C CB  . ALA A 579 ? 0.32478 0.25298 0.35365 0.04046  -0.01728 -0.03287 582 ALA A CB  
4392 N N   . ALA A 580 ? 0.28931 0.23436 0.30396 0.03184  -0.00836 -0.02799 583 ALA A N   
4393 C CA  . ALA A 580 ? 0.32641 0.27435 0.33448 0.02834  -0.00561 -0.02844 583 ALA A CA  
4394 C C   . ALA A 580 ? 0.38444 0.33243 0.38840 0.02387  -0.00661 -0.02240 583 ALA A C   
4395 O O   . ALA A 580 ? 0.36676 0.31242 0.36664 0.02066  -0.00704 -0.02180 583 ALA A O   
4396 C CB  . ALA A 580 ? 0.32246 0.27977 0.33009 0.02921  -0.00087 -0.03115 583 ALA A CB  
4397 N N   . THR A 581 ? 0.32764 0.27827 0.33285 0.02360  -0.00716 -0.01814 584 THR A N   
4398 C CA  . THR A 581 ? 0.24371 0.19620 0.24500 0.01973  -0.00704 -0.01345 584 THR A CA  
4399 C C   . THR A 581 ? 0.27837 0.22408 0.27864 0.01737  -0.01054 -0.00958 584 THR A C   
4400 O O   . THR A 581 ? 0.28128 0.22090 0.28425 0.01895  -0.01376 -0.00914 584 THR A O   
4401 C CB  . THR A 581 ? 0.29479 0.25333 0.29687 0.02016  -0.00593 -0.01102 584 THR A CB  
4402 O OG1 . THR A 581 ? 0.24123 0.19688 0.24670 0.02228  -0.00878 -0.00948 584 THR A OG1 
4403 C CG2 . THR A 581 ? 0.26576 0.23132 0.26912 0.02173  -0.00254 -0.01410 584 THR A CG2 
4404 N N   . SER A 582 ? 0.26192 0.20911 0.25869 0.01344  -0.00997 -0.00650 585 SER A N   
4405 C CA  . SER A 582 ? 0.25142 0.19404 0.24676 0.01014  -0.01254 -0.00194 585 SER A CA  
4406 C C   . SER A 582 ? 0.25015 0.19896 0.24269 0.00686  -0.01023 0.00100  585 SER A C   
4407 O O   . SER A 582 ? 0.25433 0.20672 0.24620 0.00560  -0.00830 -0.00056 585 SER A O   
4408 C CB  . SER A 582 ? 0.32822 0.26375 0.32376 0.00848  -0.01490 -0.00299 585 SER A CB  
4409 O OG  . SER A 582 ? 0.28708 0.22044 0.28100 0.00397  -0.01645 0.00191  585 SER A OG  
4410 N N   . SER A 583 ? 0.26333 0.21351 0.25423 0.00552  -0.01058 0.00507  586 SER A N   
4411 C CA  . SER A 583 ? 0.27287 0.22968 0.26160 0.00297  -0.00790 0.00689  586 SER A CA  
4412 C C   . SER A 583 ? 0.27726 0.23364 0.26572 -0.00111 -0.00785 0.00857  586 SER A C   
4413 O O   . SER A 583 ? 0.27443 0.23653 0.26333 -0.00238 -0.00550 0.00782  586 SER A O   
4414 C CB  . SER A 583 ? 0.27259 0.23122 0.25869 0.00250  -0.00807 0.01021  586 SER A CB  
4415 O OG  . SER A 583 ? 0.24446 0.20478 0.23168 0.00618  -0.00806 0.00818  586 SER A OG  
4416 N N   . SER A 584 ? 0.25727 0.20673 0.24580 -0.00324 -0.01084 0.01089  587 SER A N   
4417 C CA  . SER A 584 ? 0.36161 0.31016 0.35072 -0.00759 -0.01135 0.01269  587 SER A CA  
4418 C C   . SER A 584 ? 0.32723 0.27654 0.31819 -0.00711 -0.01088 0.00856  587 SER A C   
4419 O O   . SER A 584 ? 0.29491 0.24885 0.28691 -0.00988 -0.00961 0.00905  587 SER A O   
4420 C CB  . SER A 584 ? 0.27174 0.21093 0.26101 -0.00971 -0.01558 0.01568  587 SER A CB  
4421 O OG  . SER A 584 ? 0.60623 0.54548 0.59284 -0.01195 -0.01611 0.02092  587 SER A OG  
4422 N N   . LYS A 585 ? 0.26487 0.20951 0.25637 -0.00383 -0.01221 0.00447  588 LYS A N   
4423 C CA  . LYS A 585 ? 0.27154 0.21653 0.26330 -0.00357 -0.01197 0.00040  588 LYS A CA  
4424 C C   . LYS A 585 ? 0.30324 0.25675 0.29458 -0.00277 -0.00875 -0.00084 588 LYS A C   
4425 O O   . LYS A 585 ? 0.25490 0.21089 0.24645 -0.00454 -0.00861 -0.00182 588 LYS A O   
4426 C CB  . LYS A 585 ? 0.29148 0.23067 0.28332 0.00005  -0.01334 -0.00428 588 LYS A CB  
4427 C CG  . LYS A 585 ? 0.43139 0.36058 0.42441 -0.00070 -0.01745 -0.00417 588 LYS A CG  
4428 C CD  . LYS A 585 ? 0.46710 0.39146 0.46079 0.00360  -0.01829 -0.01010 588 LYS A CD  
4429 C CE  . LYS A 585 ? 0.60441 0.51768 0.59994 0.00319  -0.02300 -0.01064 588 LYS A CE  
4430 N NZ  . LYS A 585 ? 0.75715 0.66571 0.75388 0.00780  -0.02371 -0.01746 588 LYS A NZ  
4431 N N   . PHE A 586 ? 0.22872 0.18638 0.21974 -0.00017 -0.00670 -0.00074 589 PHE A N   
4432 C CA  . PHE A 586 ? 0.27218 0.23707 0.26324 0.00046  -0.00422 -0.00167 589 PHE A CA  
4433 C C   . PHE A 586 ? 0.25234 0.22236 0.24466 -0.00250 -0.00325 0.00098  589 PHE A C   
4434 O O   . PHE A 586 ? 0.26265 0.23671 0.25615 -0.00317 -0.00269 0.00005  589 PHE A O   
4435 C CB  . PHE A 586 ? 0.25196 0.21966 0.24288 0.00354  -0.00272 -0.00210 589 PHE A CB  
4436 C CG  . PHE A 586 ? 0.24918 0.22288 0.24038 0.00436  -0.00082 -0.00328 589 PHE A CG  
4437 C CD1 . PHE A 586 ? 0.29491 0.26904 0.28544 0.00534  -0.00048 -0.00602 589 PHE A CD1 
4438 C CD2 . PHE A 586 ? 0.23489 0.21353 0.22680 0.00401  0.00047  -0.00168 589 PHE A CD2 
4439 C CE1 . PHE A 586 ? 0.27969 0.25856 0.27038 0.00560  0.00064  -0.00634 589 PHE A CE1 
4440 C CE2 . PHE A 586 ? 0.24503 0.22814 0.23784 0.00484  0.00150  -0.00269 589 PHE A CE2 
4441 C CZ  . PHE A 586 ? 0.23764 0.22056 0.22990 0.00547  0.00135  -0.00463 589 PHE A CZ  
4442 N N   . ALA A 587 ? 0.23144 0.20170 0.22374 -0.00444 -0.00312 0.00433  590 ALA A N   
4443 C CA  . ALA A 587 ? 0.24843 0.22478 0.24259 -0.00727 -0.00156 0.00644  590 ALA A CA  
4444 C C   . ALA A 587 ? 0.28212 0.25810 0.27886 -0.01031 -0.00300 0.00649  590 ALA A C   
4445 O O   . ALA A 587 ? 0.23286 0.21497 0.23275 -0.01144 -0.00198 0.00640  590 ALA A O   
4446 C CB  . ALA A 587 ? 0.34006 0.31678 0.33264 -0.00936 -0.00093 0.01022  590 ALA A CB  
4447 N N   . LYS A 588 ? 0.26721 0.23588 0.26320 -0.01156 -0.00579 0.00643  591 LYS A N   
4448 C CA  . LYS A 588 ? 0.32129 0.28877 0.31944 -0.01454 -0.00785 0.00606  591 LYS A CA  
4449 C C   . LYS A 588 ? 0.28123 0.25074 0.27928 -0.01284 -0.00809 0.00251  591 LYS A C   
4450 O O   . LYS A 588 ? 0.22876 0.20167 0.22956 -0.01505 -0.00896 0.00262  591 LYS A O   
4451 C CB  . LYS A 588 ? 0.30483 0.26273 0.30185 -0.01586 -0.01129 0.00605  591 LYS A CB  
4452 C CG  . LYS A 588 ? 0.43866 0.39470 0.43794 -0.01964 -0.01401 0.00598  591 LYS A CG  
4453 C CD  . LYS A 588 ? 0.52847 0.49207 0.53210 -0.02384 -0.01269 0.00995  591 LYS A CD  
4454 C CE  . LYS A 588 ? 0.77460 0.73506 0.78126 -0.02867 -0.01607 0.01131  591 LYS A CE  
4455 N NZ  . LYS A 588 ? 0.72374 0.67988 0.72929 -0.02794 -0.01916 0.00703  591 LYS A NZ  
4456 N N   . ALA A 589 ? 0.24253 0.21022 0.23756 -0.00922 -0.00753 -0.00038 592 ALA A N   
4457 C CA  . ALA A 589 ? 0.27137 0.24120 0.26522 -0.00806 -0.00765 -0.00313 592 ALA A CA  
4458 C C   . ALA A 589 ? 0.22808 0.20579 0.22471 -0.00786 -0.00605 -0.00192 592 ALA A C   
4459 O O   . ALA A 589 ? 0.21207 0.19219 0.20951 -0.00863 -0.00727 -0.00261 592 ALA A O   
4460 C CB  . ALA A 589 ? 0.28939 0.25643 0.27963 -0.00459 -0.00686 -0.00619 592 ALA A CB  
4461 N N   . VAL A 590 ? 0.20689 0.18831 0.20489 -0.00668 -0.00370 -0.00032 593 VAL A N   
4462 C CA  . VAL A 590 ? 0.21248 0.20108 0.21397 -0.00623 -0.00225 0.00034  593 VAL A CA  
4463 C C   . VAL A 590 ? 0.24441 0.23712 0.25083 -0.00925 -0.00300 0.00176  593 VAL A C   
4464 O O   . VAL A 590 ? 0.21950 0.21643 0.22940 -0.00918 -0.00380 0.00130  593 VAL A O   
4465 C CB  . VAL A 590 ? 0.23254 0.22373 0.23382 -0.00463 0.00032  0.00126  593 VAL A CB  
4466 C CG1 . VAL A 590 ? 0.23615 0.23489 0.24185 -0.00433 0.00196  0.00145  593 VAL A CG1 
4467 C CG2 . VAL A 590 ? 0.23440 0.22296 0.23234 -0.00148 0.00068  -0.00029 593 VAL A CG2 
4468 N N   . GLU A 591 ? 0.25241 0.24415 0.25983 -0.01210 -0.00300 0.00380  594 GLU A N   
4469 C CA  . GLU A 591 ? 0.25016 0.24630 0.26312 -0.01556 -0.00370 0.00539  594 GLU A CA  
4470 C C   . GLU A 591 ? 0.22407 0.21829 0.23806 -0.01681 -0.00730 0.00408  594 GLU A C   
4471 O O   . GLU A 591 ? 0.23233 0.23222 0.25178 -0.01772 -0.00820 0.00429  594 GLU A O   
4472 C CB  . GLU A 591 ? 0.21650 0.21033 0.22938 -0.01912 -0.00364 0.00828  594 GLU A CB  
4473 C CG  . GLU A 591 ? 0.27572 0.27477 0.29509 -0.02341 -0.00419 0.01036  594 GLU A CG  
4474 C CD  . GLU A 591 ? 0.44940 0.44478 0.46819 -0.02769 -0.00484 0.01376  594 GLU A CD  
4475 O OE1 . GLU A 591 ? 0.63892 0.63635 0.65614 -0.02838 -0.00207 0.01617  594 GLU A OE1 
4476 O OE2 . GLU A 591 ? 0.62518 0.61505 0.64454 -0.03047 -0.00845 0.01405  594 GLU A OE2 
4477 N N   . GLU A 592 ? 0.25232 0.23862 0.26125 -0.01688 -0.00963 0.00253  595 GLU A N   
4478 C CA  . GLU A 592 ? 0.25337 0.23759 0.26189 -0.01838 -0.01324 0.00100  595 GLU A CA  
4479 C C   . GLU A 592 ? 0.24816 0.23600 0.25643 -0.01626 -0.01362 -0.00023 595 GLU A C   
4480 O O   . GLU A 592 ? 0.24640 0.23620 0.25701 -0.01790 -0.01656 -0.00021 595 GLU A O   
4481 C CB  . GLU A 592 ? 0.28062 0.25562 0.28300 -0.01831 -0.01521 -0.00138 595 GLU A CB  
4482 C CG  . GLU A 592 ? 0.34687 0.31682 0.35025 -0.02101 -0.01632 0.00016  595 GLU A CG  
4483 C CD  . GLU A 592 ? 0.69296 0.65303 0.69095 -0.02004 -0.01837 -0.00295 595 GLU A CD  
4484 O OE1 . GLU A 592 ? 0.56980 0.52803 0.56309 -0.01673 -0.01755 -0.00626 595 GLU A OE1 
4485 O OE2 . GLU A 592 ? 0.77265 0.72691 0.77154 -0.02265 -0.02078 -0.00215 595 GLU A OE2 
4486 N N   . SER A 593 ? 0.23596 0.22437 0.24149 -0.01287 -0.01120 -0.00102 596 SER A N   
4487 C CA  . SER A 593 ? 0.21385 0.20500 0.21903 -0.01116 -0.01182 -0.00159 596 SER A CA  
4488 C C   . SER A 593 ? 0.20721 0.20566 0.22017 -0.01117 -0.01194 -0.00005 596 SER A C   
4489 O O   . SER A 593 ? 0.21133 0.21173 0.22640 -0.01157 -0.01478 0.00018  596 SER A O   
4490 C CB  . SER A 593 ? 0.23831 0.22837 0.23958 -0.00795 -0.00925 -0.00251 596 SER A CB  
4491 O OG  . SER A 593 ? 0.25725 0.24142 0.25236 -0.00761 -0.00923 -0.00447 596 SER A OG  
4492 N N   . LEU A 594 ? 0.18317 0.18589 0.20052 -0.01068 -0.00900 0.00090  597 LEU A N   
4493 C CA  . LEU A 594 ? 0.20122 0.21175 0.22696 -0.01034 -0.00862 0.00157  597 LEU A CA  
4494 C C   . LEU A 594 ? 0.20379 0.21726 0.23544 -0.01353 -0.01146 0.00259  597 LEU A C   
4495 O O   . LEU A 594 ? 0.20957 0.22835 0.24811 -0.01304 -0.01319 0.00273  597 LEU A O   
4496 C CB  . LEU A 594 ? 0.19420 0.20916 0.22235 -0.00950 -0.00434 0.00192  597 LEU A CB  
4497 C CG  . LEU A 594 ? 0.21137 0.22452 0.23500 -0.00616 -0.00204 0.00079  597 LEU A CG  
4498 C CD1 . LEU A 594 ? 0.22583 0.24198 0.24941 -0.00623 0.00178  0.00131  597 LEU A CD1 
4499 C CD2 . LEU A 594 ? 0.23413 0.24992 0.26101 -0.00326 -0.00294 -0.00043 597 LEU A CD2 
4500 N N   . ILE A 595 ? 0.24855 0.25851 0.27834 -0.01680 -0.01243 0.00333  598 ILE A N   
4501 C CA  . ILE A 595 ? 0.21712 0.22944 0.25261 -0.02030 -0.01580 0.00433  598 ILE A CA  
4502 C C   . ILE A 595 ? 0.25157 0.26063 0.28438 -0.02045 -0.02063 0.00338  598 ILE A C   
4503 O O   . ILE A 595 ? 0.24523 0.25882 0.28465 -0.02154 -0.02380 0.00410  598 ILE A O   
4504 C CB  . ILE A 595 ? 0.24520 0.25350 0.27922 -0.02413 -0.01617 0.00547  598 ILE A CB  
4505 C CG1 . ILE A 595 ? 0.23162 0.24427 0.26853 -0.02482 -0.01166 0.00735  598 ILE A CG1 
4506 C CG2 . ILE A 595 ? 0.30680 0.31658 0.34629 -0.02813 -0.02045 0.00635  598 ILE A CG2 
4507 C CD1 . ILE A 595 ? 0.35268 0.37662 0.39988 -0.02550 -0.00964 0.00848  598 ILE A CD1 
4508 N N   . ASP A 596 ? 0.25671 0.25828 0.27985 -0.01949 -0.02135 0.00178  599 ASP A N   
4509 C CA  . ASP A 596 ? 0.25392 0.25258 0.27265 -0.01992 -0.02558 0.00095  599 ASP A CA  
4510 C C   . ASP A 596 ? 0.23464 0.23833 0.25778 -0.01793 -0.02681 0.00198  599 ASP A C   
4511 O O   . ASP A 596 ? 0.21661 0.22140 0.24178 -0.01935 -0.03149 0.00277  599 ASP A O   
4512 C CB  . ASP A 596 ? 0.20694 0.19843 0.21469 -0.01866 -0.02467 -0.00124 599 ASP A CB  
4513 C CG  . ASP A 596 ? 0.42458 0.40948 0.42756 -0.02062 -0.02534 -0.00301 599 ASP A CG  
4514 O OD1 . ASP A 596 ? 0.35726 0.34247 0.36483 -0.02366 -0.02750 -0.00214 599 ASP A OD1 
4515 O OD2 . ASP A 596 ? 0.36720 0.34673 0.36251 -0.01909 -0.02384 -0.00538 599 ASP A OD2 
4516 N N   . MET A 597 ? 0.19142 0.19756 0.21592 -0.01464 -0.02323 0.00198  600 MET A N   
4517 C CA  . MET A 597 ? 0.20546 0.21516 0.23430 -0.01241 -0.02467 0.00276  600 MET A CA  
4518 C C   . MET A 597 ? 0.18168 0.19884 0.22262 -0.01261 -0.02626 0.00368  600 MET A C   
4519 O O   . MET A 597 ? 0.21329 0.23236 0.25869 -0.01221 -0.03044 0.00464  600 MET A O   
4520 C CB  . MET A 597 ? 0.21623 0.22614 0.24374 -0.00898 -0.02060 0.00209  600 MET A CB  
4521 C CG  . MET A 597 ? 0.19012 0.19375 0.20700 -0.00859 -0.01965 0.00136  600 MET A CG  
4522 S SD  . MET A 597 ? 0.27964 0.28326 0.29507 -0.00516 -0.01493 0.00054  600 MET A SD  
4523 C CE  . MET A 597 ? 0.21835 0.22514 0.23989 -0.00302 -0.01716 0.00150  600 MET A CE  
4524 N N   . ARG A 598 ? 0.20913 0.23085 0.25582 -0.01343 -0.02315 0.00358  601 ARG A N   
4525 C CA  . ARG A 598 ? 0.20769 0.23781 0.26679 -0.01414 -0.02424 0.00425  601 ARG A CA  
4526 C C   . ARG A 598 ? 0.22700 0.25643 0.28821 -0.01729 -0.03039 0.00542  601 ARG A C   
4527 O O   . ARG A 598 ? 0.22890 0.26308 0.29872 -0.01662 -0.03411 0.00611  601 ARG A O   
4528 C CB  . ARG A 598 ? 0.19166 0.22640 0.25457 -0.01577 -0.01961 0.00442  601 ARG A CB  
4529 C CG  . ARG A 598 ? 0.22569 0.27057 0.30211 -0.01706 -0.01994 0.00508  601 ARG A CG  
4530 C CD  . ARG A 598 ? 0.28446 0.33215 0.36226 -0.02081 -0.01648 0.00631  601 ARG A CD  
4531 N NE  . ARG A 598 ? 0.26145 0.30200 0.33375 -0.02506 -0.02015 0.00755  601 ARG A NE  
4532 C CZ  . ARG A 598 ? 0.34866 0.38904 0.42129 -0.02921 -0.01898 0.00917  601 ARG A CZ  
4533 N NH1 . ARG A 598 ? 0.31276 0.35993 0.38980 -0.03011 -0.01383 0.01026  601 ARG A NH1 
4534 N NH2 . ARG A 598 ? 0.26850 0.30142 0.33646 -0.03273 -0.02319 0.00970  601 ARG A NH2 
4535 N N   . ASP A 599 ? 0.25093 0.27411 0.30447 -0.02066 -0.03202 0.00547  602 ASP A N   
4536 C CA  . ASP A 599 ? 0.24925 0.27126 0.30388 -0.02405 -0.03830 0.00626  602 ASP A CA  
4537 C C   . ASP A 599 ? 0.29511 0.31445 0.34600 -0.02297 -0.04328 0.00673  602 ASP A C   
4538 O O   . ASP A 599 ? 0.25023 0.27231 0.30704 -0.02440 -0.04890 0.00803  602 ASP A O   
4539 C CB  . ASP A 599 ? 0.26839 0.28286 0.31429 -0.02755 -0.03924 0.00542  602 ASP A CB  
4540 C CG  . ASP A 599 ? 0.29527 0.31155 0.34511 -0.02956 -0.03554 0.00588  602 ASP A CG  
4541 O OD1 . ASP A 599 ? 0.30028 0.32535 0.36077 -0.02936 -0.03298 0.00713  602 ASP A OD1 
4542 O OD2 . ASP A 599 ? 0.27432 0.28331 0.31668 -0.03138 -0.03520 0.00500  602 ASP A OD2 
4543 N N   . LEU A 600 ? 0.23542 0.24949 0.27655 -0.02082 -0.04165 0.00606  603 LEU A N   
4544 C CA  . LEU A 600 ? 0.23750 0.24911 0.27450 -0.02025 -0.04616 0.00726  603 LEU A CA  
4545 C C   . LEU A 600 ? 0.25530 0.27316 0.30419 -0.01774 -0.04834 0.00883  603 LEU A C   
4546 O O   . LEU A 600 ? 0.22257 0.24033 0.27328 -0.01851 -0.05461 0.01074  603 LEU A O   
4547 C CB  . LEU A 600 ? 0.22661 0.23260 0.25202 -0.01861 -0.04308 0.00648  603 LEU A CB  
4548 C CG  . LEU A 600 ? 0.26813 0.26733 0.28082 -0.02091 -0.04259 0.00462  603 LEU A CG  
4549 C CD1 . LEU A 600 ? 0.23258 0.22827 0.23667 -0.01876 -0.03769 0.00330  603 LEU A CD1 
4550 C CD2 . LEU A 600 ? 0.24621 0.24210 0.25209 -0.02409 -0.04895 0.00531  603 LEU A CD2 
4551 N N   . CYS A 601 ? 0.23184 0.25485 0.28865 -0.01456 -0.04355 0.00791  604 CYS A N   
4552 C CA  . CYS A 601 ? 0.32898 0.35812 0.39827 -0.01153 -0.04534 0.00844  604 CYS A CA  
4553 C C   . CYS A 601 ? 0.31003 0.34691 0.39272 -0.01275 -0.04821 0.00890  604 CYS A C   
4554 O O   . CYS A 601 ? 0.39663 0.43917 0.49133 -0.01013 -0.05054 0.00910  604 CYS A O   
4555 C CB  . CYS A 601 ? 0.25064 0.28289 0.32350 -0.00757 -0.03907 0.00647  604 CYS A CB  
4556 S SG  . CYS A 601 ? 0.32146 0.34596 0.38175 -0.00569 -0.03642 0.00614  604 CYS A SG  
4557 N N   . SER A 602 ? 0.27831 0.31577 0.36024 -0.01662 -0.04826 0.00897  605 SER A N   
4558 C CA  . SER A 602 ? 0.26332 0.30868 0.35843 -0.01853 -0.05099 0.00966  605 SER A CA  
4559 C C   . SER A 602 ? 0.40258 0.44438 0.49508 -0.02231 -0.05904 0.01144  605 SER A C   
4560 O O   . SER A 602 ? 0.46411 0.51038 0.56420 -0.02546 -0.06144 0.01202  605 SER A O   
4561 C CB  . SER A 602 ? 0.25563 0.30530 0.35375 -0.02086 -0.04550 0.00890  605 SER A CB  
4562 O OG  . SER A 602 ? 0.33333 0.38625 0.43242 -0.01781 -0.03811 0.00734  605 SER A OG  
4563 N N   . LEU A 603 ? 0.36536 0.39903 0.44617 -0.02260 -0.06304 0.01232  606 LEU A N   
4564 C CA  . LEU A 603 ? 0.37947 0.40960 0.45643 -0.02617 -0.07118 0.01400  606 LEU A CA  
4565 C C   . LEU A 603 ? 0.46094 0.49728 0.55188 -0.02488 -0.07760 0.01612  606 LEU A C   
4566 O O   . LEU A 603 ? 0.51116 0.55213 0.61110 -0.02737 -0.08208 0.01691  606 LEU A O   
4567 C CB  . LEU A 603 ? 0.42011 0.44055 0.47973 -0.02698 -0.07308 0.01443  606 LEU A CB  
4568 C CG  . LEU A 603 ? 0.38636 0.39984 0.43133 -0.02850 -0.06832 0.01204  606 LEU A CG  
4569 C CD1 . LEU A 603 ? 0.55384 0.56000 0.58366 -0.02902 -0.07017 0.01254  606 LEU A CD1 
4570 C CD2 . LEU A 603 ? 0.40544 0.41741 0.44905 -0.03274 -0.07020 0.01076  606 LEU A CD2 
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