data_8X3Y
# 
_entry.id   8X3Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8X3Y         pdb_00008x3y 10.2210/pdb8x3y/pdb 
WWPDB D_1300042448 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_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                        8X3Y 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mma@bjmu.edu.cn 
_pdbx_contact_author.name_first         Ming 
_pdbx_contact_author.name_last          Ma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8311-3892 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yu, J.H.' 1 ? 
'Liu, T.'  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                     'ThDP-dependent HKA synthase' 
_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 'Yu, J.H.' 1 ? 
primary 'Liu, T.'  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 BbmA                       62385.676 2   ? ? ? ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE" 427.201   2   ? ? ? ? 
3 non-polymer nat 'THIAMINE DIPHOSPHATE'     425.314   2   ? ? ? ? 
4 non-polymer nat 'MAGNESIUM ION'            24.305    2   ? ? ? ? 
5 water       nat water                      18.015    325 ? ? ? ? 
# 
_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       
;MGSSKTVTAVELLVRQMEAEGVSYVFGIPGGPLMPLYEAIFSRKKIQPILTKHEEGAAFMAEGYARVSGKLGVCCATTGP
GATNALTGIACAYSDSTPVLLLTAQVGTAAFGKGALQESTVHGVDLVSIFSPITKLSVMIPTAEKMGEMTRRALRTAQSG
RPGPIHLNIPADIAKHPVPLEVFPPMNYRGGKPAPTIMDVVRVAELIFHAKRPAILAGHGIECAKAWEELLDFAELTGIP
VATTPKGKSSFPENHALSLGVFGFAGHQKATDYLLSGDVDVLIVIGSSLGDWQTNSWDPRLTPSVALIQIDIDPMEIGKN
YPVDVGINADASETLKALILCIRSSGKMLKKPALPLETKEQTAFQEIDHGTEGNGIHPAMVVEAMQNRLPADTILFVDNG
SCINWGVHCYLAQTPGAFQIGLGLAAMGHAVAAAIGGKLAAPDRPVVALVGDAAFAMNGMEIHTAAEYKIPVTWIVLNNG
GHGLVHLGEQHQFDSKFDISSFRKSIDFCKMAESLGVKSYRAETVEDFDAALKGALAMNTPCLIDVQVDIDVLPPGMKQR
FDMLNKSYAGERYTAPIGHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSKTVTAVELLVRQMEAEGVSYVFGIPGGPLMPLYEAIFSRKKIQPILTKHEEGAAFMAEGYARVSGKLGVCCATTGP
GATNALTGIACAYSDSTPVLLLTAQVGTAAFGKGALQESTVHGVDLVSIFSPITKLSVMIPTAEKMGEMTRRALRTAQSG
RPGPIHLNIPADIAKHPVPLEVFPPMNYRGGKPAPTIMDVVRVAELIFHAKRPAILAGHGIECAKAWEELLDFAELTGIP
VATTPKGKSSFPENHALSLGVFGFAGHQKATDYLLSGDVDVLIVIGSSLGDWQTNSWDPRLTPSVALIQIDIDPMEIGKN
YPVDVGINADASETLKALILCIRSSGKMLKKPALPLETKEQTAFQEIDHGTEGNGIHPAMVVEAMQNRLPADTILFVDNG
SCINWGVHCYLAQTPGAFQIGLGLAAMGHAVAAAIGGKLAAPDRPVVALVGDAAFAMNGMEIHTAAEYKIPVTWIVLNNG
GHGLVHLGEQHQFDSKFDISSFRKSIDFCKMAESLGVKSYRAETVEDFDAALKGALAMNTPCLIDVQVDIDVLPPGMKQR
FDMLNKSYAGERYTAPIGHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE" ADP 
3 'THIAMINE DIPHOSPHATE'     TPP 
4 'MAGNESIUM ION'            MG  
5 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   LYS n 
1 6   THR n 
1 7   VAL n 
1 8   THR n 
1 9   ALA n 
1 10  VAL n 
1 11  GLU n 
1 12  LEU n 
1 13  LEU n 
1 14  VAL n 
1 15  ARG n 
1 16  GLN n 
1 17  MET n 
1 18  GLU n 
1 19  ALA n 
1 20  GLU n 
1 21  GLY n 
1 22  VAL n 
1 23  SER n 
1 24  TYR n 
1 25  VAL n 
1 26  PHE n 
1 27  GLY n 
1 28  ILE n 
1 29  PRO n 
1 30  GLY n 
1 31  GLY n 
1 32  PRO n 
1 33  LEU n 
1 34  MET n 
1 35  PRO n 
1 36  LEU n 
1 37  TYR n 
1 38  GLU n 
1 39  ALA n 
1 40  ILE n 
1 41  PHE n 
1 42  SER n 
1 43  ARG n 
1 44  LYS n 
1 45  LYS n 
1 46  ILE n 
1 47  GLN n 
1 48  PRO n 
1 49  ILE n 
1 50  LEU n 
1 51  THR n 
1 52  LYS n 
1 53  HIS n 
1 54  GLU n 
1 55  GLU n 
1 56  GLY n 
1 57  ALA n 
1 58  ALA n 
1 59  PHE n 
1 60  MET n 
1 61  ALA n 
1 62  GLU n 
1 63  GLY n 
1 64  TYR n 
1 65  ALA n 
1 66  ARG n 
1 67  VAL n 
1 68  SER n 
1 69  GLY n 
1 70  LYS n 
1 71  LEU n 
1 72  GLY n 
1 73  VAL n 
1 74  CYS n 
1 75  CYS n 
1 76  ALA n 
1 77  THR n 
1 78  THR n 
1 79  GLY n 
1 80  PRO n 
1 81  GLY n 
1 82  ALA n 
1 83  THR n 
1 84  ASN n 
1 85  ALA n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  ILE n 
1 90  ALA n 
1 91  CYS n 
1 92  ALA n 
1 93  TYR n 
1 94  SER n 
1 95  ASP n 
1 96  SER n 
1 97  THR n 
1 98  PRO n 
1 99  VAL n 
1 100 LEU n 
1 101 LEU n 
1 102 LEU n 
1 103 THR n 
1 104 ALA n 
1 105 GLN n 
1 106 VAL n 
1 107 GLY n 
1 108 THR n 
1 109 ALA n 
1 110 ALA n 
1 111 PHE n 
1 112 GLY n 
1 113 LYS n 
1 114 GLY n 
1 115 ALA n 
1 116 LEU n 
1 117 GLN n 
1 118 GLU n 
1 119 SER n 
1 120 THR n 
1 121 VAL n 
1 122 HIS n 
1 123 GLY n 
1 124 VAL n 
1 125 ASP n 
1 126 LEU n 
1 127 VAL n 
1 128 SER n 
1 129 ILE n 
1 130 PHE n 
1 131 SER n 
1 132 PRO n 
1 133 ILE n 
1 134 THR n 
1 135 LYS n 
1 136 LEU n 
1 137 SER n 
1 138 VAL n 
1 139 MET n 
1 140 ILE n 
1 141 PRO n 
1 142 THR n 
1 143 ALA n 
1 144 GLU n 
1 145 LYS n 
1 146 MET n 
1 147 GLY n 
1 148 GLU n 
1 149 MET n 
1 150 THR n 
1 151 ARG n 
1 152 ARG n 
1 153 ALA n 
1 154 LEU n 
1 155 ARG n 
1 156 THR n 
1 157 ALA n 
1 158 GLN n 
1 159 SER n 
1 160 GLY n 
1 161 ARG n 
1 162 PRO n 
1 163 GLY n 
1 164 PRO n 
1 165 ILE n 
1 166 HIS n 
1 167 LEU n 
1 168 ASN n 
1 169 ILE n 
1 170 PRO n 
1 171 ALA n 
1 172 ASP n 
1 173 ILE n 
1 174 ALA n 
1 175 LYS n 
1 176 HIS n 
1 177 PRO n 
1 178 VAL n 
1 179 PRO n 
1 180 LEU n 
1 181 GLU n 
1 182 VAL n 
1 183 PHE n 
1 184 PRO n 
1 185 PRO n 
1 186 MET n 
1 187 ASN n 
1 188 TYR n 
1 189 ARG n 
1 190 GLY n 
1 191 GLY n 
1 192 LYS n 
1 193 PRO n 
1 194 ALA n 
1 195 PRO n 
1 196 THR n 
1 197 ILE n 
1 198 MET n 
1 199 ASP n 
1 200 VAL n 
1 201 VAL n 
1 202 ARG n 
1 203 VAL n 
1 204 ALA n 
1 205 GLU n 
1 206 LEU n 
1 207 ILE n 
1 208 PHE n 
1 209 HIS n 
1 210 ALA n 
1 211 LYS n 
1 212 ARG n 
1 213 PRO n 
1 214 ALA n 
1 215 ILE n 
1 216 LEU n 
1 217 ALA n 
1 218 GLY n 
1 219 HIS n 
1 220 GLY n 
1 221 ILE n 
1 222 GLU n 
1 223 CYS n 
1 224 ALA n 
1 225 LYS n 
1 226 ALA n 
1 227 TRP n 
1 228 GLU n 
1 229 GLU n 
1 230 LEU n 
1 231 LEU n 
1 232 ASP n 
1 233 PHE n 
1 234 ALA n 
1 235 GLU n 
1 236 LEU n 
1 237 THR n 
1 238 GLY n 
1 239 ILE n 
1 240 PRO n 
1 241 VAL n 
1 242 ALA n 
1 243 THR n 
1 244 THR n 
1 245 PRO n 
1 246 LYS n 
1 247 GLY n 
1 248 LYS n 
1 249 SER n 
1 250 SER n 
1 251 PHE n 
1 252 PRO n 
1 253 GLU n 
1 254 ASN n 
1 255 HIS n 
1 256 ALA n 
1 257 LEU n 
1 258 SER n 
1 259 LEU n 
1 260 GLY n 
1 261 VAL n 
1 262 PHE n 
1 263 GLY n 
1 264 PHE n 
1 265 ALA n 
1 266 GLY n 
1 267 HIS n 
1 268 GLN n 
1 269 LYS n 
1 270 ALA n 
1 271 THR n 
1 272 ASP n 
1 273 TYR n 
1 274 LEU n 
1 275 LEU n 
1 276 SER n 
1 277 GLY n 
1 278 ASP n 
1 279 VAL n 
1 280 ASP n 
1 281 VAL n 
1 282 LEU n 
1 283 ILE n 
1 284 VAL n 
1 285 ILE n 
1 286 GLY n 
1 287 SER n 
1 288 SER n 
1 289 LEU n 
1 290 GLY n 
1 291 ASP n 
1 292 TRP n 
1 293 GLN n 
1 294 THR n 
1 295 ASN n 
1 296 SER n 
1 297 TRP n 
1 298 ASP n 
1 299 PRO n 
1 300 ARG n 
1 301 LEU n 
1 302 THR n 
1 303 PRO n 
1 304 SER n 
1 305 VAL n 
1 306 ALA n 
1 307 LEU n 
1 308 ILE n 
1 309 GLN n 
1 310 ILE n 
1 311 ASP n 
1 312 ILE n 
1 313 ASP n 
1 314 PRO n 
1 315 MET n 
1 316 GLU n 
1 317 ILE n 
1 318 GLY n 
1 319 LYS n 
1 320 ASN n 
1 321 TYR n 
1 322 PRO n 
1 323 VAL n 
1 324 ASP n 
1 325 VAL n 
1 326 GLY n 
1 327 ILE n 
1 328 ASN n 
1 329 ALA n 
1 330 ASP n 
1 331 ALA n 
1 332 SER n 
1 333 GLU n 
1 334 THR n 
1 335 LEU n 
1 336 LYS n 
1 337 ALA n 
1 338 LEU n 
1 339 ILE n 
1 340 LEU n 
1 341 CYS n 
1 342 ILE n 
1 343 ARG n 
1 344 SER n 
1 345 SER n 
1 346 GLY n 
1 347 LYS n 
1 348 MET n 
1 349 LEU n 
1 350 LYS n 
1 351 LYS n 
1 352 PRO n 
1 353 ALA n 
1 354 LEU n 
1 355 PRO n 
1 356 LEU n 
1 357 GLU n 
1 358 THR n 
1 359 LYS n 
1 360 GLU n 
1 361 GLN n 
1 362 THR n 
1 363 ALA n 
1 364 PHE n 
1 365 GLN n 
1 366 GLU n 
1 367 ILE n 
1 368 ASP n 
1 369 HIS n 
1 370 GLY n 
1 371 THR n 
1 372 GLU n 
1 373 GLY n 
1 374 ASN n 
1 375 GLY n 
1 376 ILE n 
1 377 HIS n 
1 378 PRO n 
1 379 ALA n 
1 380 MET n 
1 381 VAL n 
1 382 VAL n 
1 383 GLU n 
1 384 ALA n 
1 385 MET n 
1 386 GLN n 
1 387 ASN n 
1 388 ARG n 
1 389 LEU n 
1 390 PRO n 
1 391 ALA n 
1 392 ASP n 
1 393 THR n 
1 394 ILE n 
1 395 LEU n 
1 396 PHE n 
1 397 VAL n 
1 398 ASP n 
1 399 ASN n 
1 400 GLY n 
1 401 SER n 
1 402 CYS n 
1 403 ILE n 
1 404 ASN n 
1 405 TRP n 
1 406 GLY n 
1 407 VAL n 
1 408 HIS n 
1 409 CYS n 
1 410 TYR n 
1 411 LEU n 
1 412 ALA n 
1 413 GLN n 
1 414 THR n 
1 415 PRO n 
1 416 GLY n 
1 417 ALA n 
1 418 PHE n 
1 419 GLN n 
1 420 ILE n 
1 421 GLY n 
1 422 LEU n 
1 423 GLY n 
1 424 LEU n 
1 425 ALA n 
1 426 ALA n 
1 427 MET n 
1 428 GLY n 
1 429 HIS n 
1 430 ALA n 
1 431 VAL n 
1 432 ALA n 
1 433 ALA n 
1 434 ALA n 
1 435 ILE n 
1 436 GLY n 
1 437 GLY n 
1 438 LYS n 
1 439 LEU n 
1 440 ALA n 
1 441 ALA n 
1 442 PRO n 
1 443 ASP n 
1 444 ARG n 
1 445 PRO n 
1 446 VAL n 
1 447 VAL n 
1 448 ALA n 
1 449 LEU n 
1 450 VAL n 
1 451 GLY n 
1 452 ASP n 
1 453 ALA n 
1 454 ALA n 
1 455 PHE n 
1 456 ALA n 
1 457 MET n 
1 458 ASN n 
1 459 GLY n 
1 460 MET n 
1 461 GLU n 
1 462 ILE n 
1 463 HIS n 
1 464 THR n 
1 465 ALA n 
1 466 ALA n 
1 467 GLU n 
1 468 TYR n 
1 469 LYS n 
1 470 ILE n 
1 471 PRO n 
1 472 VAL n 
1 473 THR n 
1 474 TRP n 
1 475 ILE n 
1 476 VAL n 
1 477 LEU n 
1 478 ASN n 
1 479 ASN n 
1 480 GLY n 
1 481 GLY n 
1 482 HIS n 
1 483 GLY n 
1 484 LEU n 
1 485 VAL n 
1 486 HIS n 
1 487 LEU n 
1 488 GLY n 
1 489 GLU n 
1 490 GLN n 
1 491 HIS n 
1 492 GLN n 
1 493 PHE n 
1 494 ASP n 
1 495 SER n 
1 496 LYS n 
1 497 PHE n 
1 498 ASP n 
1 499 ILE n 
1 500 SER n 
1 501 SER n 
1 502 PHE n 
1 503 ARG n 
1 504 LYS n 
1 505 SER n 
1 506 ILE n 
1 507 ASP n 
1 508 PHE n 
1 509 CYS n 
1 510 LYS n 
1 511 MET n 
1 512 ALA n 
1 513 GLU n 
1 514 SER n 
1 515 LEU n 
1 516 GLY n 
1 517 VAL n 
1 518 LYS n 
1 519 SER n 
1 520 TYR n 
1 521 ARG n 
1 522 ALA n 
1 523 GLU n 
1 524 THR n 
1 525 VAL n 
1 526 GLU n 
1 527 ASP n 
1 528 PHE n 
1 529 ASP n 
1 530 ALA n 
1 531 ALA n 
1 532 LEU n 
1 533 LYS n 
1 534 GLY n 
1 535 ALA n 
1 536 LEU n 
1 537 ALA n 
1 538 MET n 
1 539 ASN n 
1 540 THR n 
1 541 PRO n 
1 542 CYS n 
1 543 LEU n 
1 544 ILE n 
1 545 ASP n 
1 546 VAL n 
1 547 GLN n 
1 548 VAL n 
1 549 ASP n 
1 550 ILE n 
1 551 ASP n 
1 552 VAL n 
1 553 LEU n 
1 554 PRO n 
1 555 PRO n 
1 556 GLY n 
1 557 MET n 
1 558 LYS n 
1 559 GLN n 
1 560 ARG n 
1 561 PHE n 
1 562 ASP n 
1 563 MET n 
1 564 LEU n 
1 565 ASN n 
1 566 LYS n 
1 567 SER n 
1 568 TYR n 
1 569 ALA n 
1 570 GLY n 
1 571 GLU n 
1 572 ARG n 
1 573 TYR n 
1 574 THR n 
1 575 ALA n 
1 576 PRO n 
1 577 ILE n 
1 578 GLY n 
1 579 HIS n 
1 580 HIS n 
1 581 HIS n 
1 582 HIS n 
1 583 HIS n 
1 584 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   584 
_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      Brevibacillus 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     55080 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2'    427.201 
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 
MG  non-polymer         . 'MAGNESIUM ION'            ? 'Mg 2'                 24.305  
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 
TPP non-polymer         . 'THIAMINE DIPHOSPHATE'     ? 'C12 H19 N4 O7 P2 S 1' 425.314 
TRP 'L-peptide linking' y TRYPTOPHAN                 ? 'C11 H12 N2 O2'        204.225 
TYR 'L-peptide linking' y TYROSINE                   ? 'C9 H11 N O3'          181.189 
VAL 'L-peptide linking' y VALINE                     ? 'C5 H11 N O2'          117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -3  ?   ?   ?   A . n 
A 1 2   GLY 2   -2  ?   ?   ?   A . n 
A 1 3   SER 3   -1  -1  SER SER A . n 
A 1 4   SER 4   0   0   SER SER A . n 
A 1 5   LYS 5   1   1   LYS LYS A . n 
A 1 6   THR 6   2   2   THR THR A . n 
A 1 7   VAL 7   3   3   VAL VAL A . n 
A 1 8   THR 8   4   4   THR THR A . n 
A 1 9   ALA 9   5   5   ALA ALA A . n 
A 1 10  VAL 10  6   6   VAL VAL A . n 
A 1 11  GLU 11  7   7   GLU GLU A . n 
A 1 12  LEU 12  8   8   LEU LEU A . n 
A 1 13  LEU 13  9   9   LEU LEU A . n 
A 1 14  VAL 14  10  10  VAL VAL A . n 
A 1 15  ARG 15  11  11  ARG ARG A . n 
A 1 16  GLN 16  12  12  GLN GLN A . n 
A 1 17  MET 17  13  13  MET MET A . n 
A 1 18  GLU 18  14  14  GLU GLU A . n 
A 1 19  ALA 19  15  15  ALA ALA A . n 
A 1 20  GLU 20  16  16  GLU GLU A . n 
A 1 21  GLY 21  17  17  GLY GLY A . n 
A 1 22  VAL 22  18  18  VAL VAL A . n 
A 1 23  SER 23  19  19  SER SER A . n 
A 1 24  TYR 24  20  20  TYR TYR A . n 
A 1 25  VAL 25  21  21  VAL VAL A . n 
A 1 26  PHE 26  22  22  PHE PHE A . n 
A 1 27  GLY 27  23  23  GLY GLY A . n 
A 1 28  ILE 28  24  24  ILE ILE A . n 
A 1 29  PRO 29  25  25  PRO PRO A . n 
A 1 30  GLY 30  26  26  GLY GLY A . n 
A 1 31  GLY 31  27  27  GLY GLY A . n 
A 1 32  PRO 32  28  28  PRO PRO A . n 
A 1 33  LEU 33  29  29  LEU LEU A . n 
A 1 34  MET 34  30  30  MET MET A . n 
A 1 35  PRO 35  31  31  PRO PRO A . n 
A 1 36  LEU 36  32  32  LEU LEU A . n 
A 1 37  TYR 37  33  33  TYR TYR A . n 
A 1 38  GLU 38  34  34  GLU GLU A . n 
A 1 39  ALA 39  35  35  ALA ALA A . n 
A 1 40  ILE 40  36  36  ILE ILE A . n 
A 1 41  PHE 41  37  37  PHE PHE A . n 
A 1 42  SER 42  38  38  SER SER A . n 
A 1 43  ARG 43  39  39  ARG ARG A . n 
A 1 44  LYS 44  40  40  LYS LYS A . n 
A 1 45  LYS 45  41  41  LYS LYS A . n 
A 1 46  ILE 46  42  42  ILE ILE A . n 
A 1 47  GLN 47  43  43  GLN GLN A . n 
A 1 48  PRO 48  44  44  PRO PRO A . n 
A 1 49  ILE 49  45  45  ILE ILE A . n 
A 1 50  LEU 50  46  46  LEU LEU A . n 
A 1 51  THR 51  47  47  THR THR A . n 
A 1 52  LYS 52  48  48  LYS LYS A . n 
A 1 53  HIS 53  49  49  HIS HIS A . n 
A 1 54  GLU 54  50  50  GLU GLU A . n 
A 1 55  GLU 55  51  51  GLU GLU A . n 
A 1 56  GLY 56  52  52  GLY GLY A . n 
A 1 57  ALA 57  53  53  ALA ALA A . n 
A 1 58  ALA 58  54  54  ALA ALA A . n 
A 1 59  PHE 59  55  55  PHE PHE A . n 
A 1 60  MET 60  56  56  MET MET A . n 
A 1 61  ALA 61  57  57  ALA ALA A . n 
A 1 62  GLU 62  58  58  GLU GLU A . n 
A 1 63  GLY 63  59  59  GLY GLY A . n 
A 1 64  TYR 64  60  60  TYR TYR A . n 
A 1 65  ALA 65  61  61  ALA ALA A . n 
A 1 66  ARG 66  62  62  ARG ARG A . n 
A 1 67  VAL 67  63  63  VAL VAL A . n 
A 1 68  SER 68  64  64  SER SER A . n 
A 1 69  GLY 69  65  65  GLY GLY A . n 
A 1 70  LYS 70  66  66  LYS LYS A . n 
A 1 71  LEU 71  67  67  LEU LEU A . n 
A 1 72  GLY 72  68  68  GLY GLY A . n 
A 1 73  VAL 73  69  69  VAL VAL A . n 
A 1 74  CYS 74  70  70  CYS CYS A . n 
A 1 75  CYS 75  71  71  CYS CYS A . n 
A 1 76  ALA 76  72  72  ALA ALA A . n 
A 1 77  THR 77  73  73  THR THR A . n 
A 1 78  THR 78  74  74  THR THR A . n 
A 1 79  GLY 79  75  75  GLY GLY A . n 
A 1 80  PRO 80  76  76  PRO PRO A . n 
A 1 81  GLY 81  77  77  GLY GLY A . n 
A 1 82  ALA 82  78  78  ALA ALA A . n 
A 1 83  THR 83  79  79  THR THR A . n 
A 1 84  ASN 84  80  80  ASN ASN A . n 
A 1 85  ALA 85  81  81  ALA ALA A . n 
A 1 86  LEU 86  82  82  LEU LEU A . n 
A 1 87  THR 87  83  83  THR THR A . n 
A 1 88  GLY 88  84  84  GLY GLY A . n 
A 1 89  ILE 89  85  85  ILE ILE A . n 
A 1 90  ALA 90  86  86  ALA ALA A . n 
A 1 91  CYS 91  87  87  CYS CYS A . n 
A 1 92  ALA 92  88  88  ALA ALA A . n 
A 1 93  TYR 93  89  89  TYR TYR A . n 
A 1 94  SER 94  90  90  SER SER A . n 
A 1 95  ASP 95  91  91  ASP ASP A . n 
A 1 96  SER 96  92  92  SER SER A . n 
A 1 97  THR 97  93  93  THR THR A . n 
A 1 98  PRO 98  94  94  PRO PRO A . n 
A 1 99  VAL 99  95  95  VAL VAL A . n 
A 1 100 LEU 100 96  96  LEU LEU A . n 
A 1 101 LEU 101 97  97  LEU LEU A . n 
A 1 102 LEU 102 98  98  LEU LEU A . n 
A 1 103 THR 103 99  99  THR THR A . n 
A 1 104 ALA 104 100 100 ALA ALA A . n 
A 1 105 GLN 105 101 101 GLN GLN A . n 
A 1 106 VAL 106 102 102 VAL VAL A . n 
A 1 107 GLY 107 103 103 GLY GLY A . n 
A 1 108 THR 108 104 104 THR THR A . n 
A 1 109 ALA 109 105 105 ALA ALA A . n 
A 1 110 ALA 110 106 106 ALA ALA A . n 
A 1 111 PHE 111 107 107 PHE PHE A . n 
A 1 112 GLY 112 108 108 GLY GLY A . n 
A 1 113 LYS 113 109 109 LYS LYS A . n 
A 1 114 GLY 114 110 110 GLY GLY A . n 
A 1 115 ALA 115 111 111 ALA ALA A . n 
A 1 116 LEU 116 112 112 LEU LEU A . n 
A 1 117 GLN 117 113 113 GLN GLN A . n 
A 1 118 GLU 118 114 114 GLU GLU A . n 
A 1 119 SER 119 115 115 SER SER A . n 
A 1 120 THR 120 116 116 THR THR A . n 
A 1 121 VAL 121 117 117 VAL VAL A . n 
A 1 122 HIS 122 118 118 HIS HIS A . n 
A 1 123 GLY 123 119 119 GLY GLY A . n 
A 1 124 VAL 124 120 120 VAL VAL A . n 
A 1 125 ASP 125 121 121 ASP ASP A . n 
A 1 126 LEU 126 122 122 LEU LEU A . n 
A 1 127 VAL 127 123 123 VAL VAL A . n 
A 1 128 SER 128 124 124 SER SER A . n 
A 1 129 ILE 129 125 125 ILE ILE A . n 
A 1 130 PHE 130 126 126 PHE PHE A . n 
A 1 131 SER 131 127 127 SER SER A . n 
A 1 132 PRO 132 128 128 PRO PRO A . n 
A 1 133 ILE 133 129 129 ILE ILE A . n 
A 1 134 THR 134 130 130 THR THR A . n 
A 1 135 LYS 135 131 131 LYS LYS A . n 
A 1 136 LEU 136 132 132 LEU LEU A . n 
A 1 137 SER 137 133 133 SER SER A . n 
A 1 138 VAL 138 134 134 VAL VAL A . n 
A 1 139 MET 139 135 135 MET MET A . n 
A 1 140 ILE 140 136 136 ILE ILE A . n 
A 1 141 PRO 141 137 137 PRO PRO A . n 
A 1 142 THR 142 138 138 THR THR A . n 
A 1 143 ALA 143 139 139 ALA ALA A . n 
A 1 144 GLU 144 140 140 GLU GLU A . n 
A 1 145 LYS 145 141 141 LYS LYS A . n 
A 1 146 MET 146 142 142 MET MET A . n 
A 1 147 GLY 147 143 143 GLY GLY A . n 
A 1 148 GLU 148 144 144 GLU GLU A . n 
A 1 149 MET 149 145 145 MET MET A . n 
A 1 150 THR 150 146 146 THR THR A . n 
A 1 151 ARG 151 147 147 ARG ARG A . n 
A 1 152 ARG 152 148 148 ARG ARG A . n 
A 1 153 ALA 153 149 149 ALA ALA A . n 
A 1 154 LEU 154 150 150 LEU LEU A . n 
A 1 155 ARG 155 151 151 ARG ARG A . n 
A 1 156 THR 156 152 152 THR THR A . n 
A 1 157 ALA 157 153 153 ALA ALA A . n 
A 1 158 GLN 158 154 154 GLN GLN A . n 
A 1 159 SER 159 155 155 SER SER A . n 
A 1 160 GLY 160 156 156 GLY GLY A . n 
A 1 161 ARG 161 157 157 ARG ARG A . n 
A 1 162 PRO 162 158 158 PRO PRO A . n 
A 1 163 GLY 163 159 159 GLY GLY A . n 
A 1 164 PRO 164 160 160 PRO PRO A . n 
A 1 165 ILE 165 161 161 ILE ILE A . n 
A 1 166 HIS 166 162 162 HIS HIS A . n 
A 1 167 LEU 167 163 163 LEU LEU A . n 
A 1 168 ASN 168 164 164 ASN ASN A . n 
A 1 169 ILE 169 165 165 ILE ILE A . n 
A 1 170 PRO 170 166 166 PRO PRO A . n 
A 1 171 ALA 171 167 167 ALA ALA A . n 
A 1 172 ASP 172 168 168 ASP ASP A . n 
A 1 173 ILE 173 169 169 ILE ILE A . n 
A 1 174 ALA 174 170 170 ALA ALA A . n 
A 1 175 LYS 175 171 171 LYS LYS A . n 
A 1 176 HIS 176 172 172 HIS HIS A . n 
A 1 177 PRO 177 173 173 PRO PRO A . n 
A 1 178 VAL 178 174 174 VAL VAL A . n 
A 1 179 PRO 179 175 175 PRO PRO A . n 
A 1 180 LEU 180 176 176 LEU LEU A . n 
A 1 181 GLU 181 177 177 GLU GLU A . n 
A 1 182 VAL 182 178 178 VAL VAL A . n 
A 1 183 PHE 183 179 179 PHE PHE A . n 
A 1 184 PRO 184 180 180 PRO PRO A . n 
A 1 185 PRO 185 181 181 PRO PRO A . n 
A 1 186 MET 186 182 182 MET MET A . n 
A 1 187 ASN 187 183 183 ASN ASN A . n 
A 1 188 TYR 188 184 184 TYR TYR A . n 
A 1 189 ARG 189 185 185 ARG ARG A . n 
A 1 190 GLY 190 186 186 GLY GLY A . n 
A 1 191 GLY 191 187 187 GLY GLY A . n 
A 1 192 LYS 192 188 188 LYS LYS A . n 
A 1 193 PRO 193 189 189 PRO PRO A . n 
A 1 194 ALA 194 190 190 ALA ALA A . n 
A 1 195 PRO 195 191 191 PRO PRO A . n 
A 1 196 THR 196 192 192 THR THR A . n 
A 1 197 ILE 197 193 193 ILE ILE A . n 
A 1 198 MET 198 194 194 MET MET A . n 
A 1 199 ASP 199 195 195 ASP ASP A . n 
A 1 200 VAL 200 196 196 VAL VAL A . n 
A 1 201 VAL 201 197 197 VAL VAL A . n 
A 1 202 ARG 202 198 198 ARG ARG A . n 
A 1 203 VAL 203 199 199 VAL VAL A . n 
A 1 204 ALA 204 200 200 ALA ALA A . n 
A 1 205 GLU 205 201 201 GLU GLU A . n 
A 1 206 LEU 206 202 202 LEU LEU A . n 
A 1 207 ILE 207 203 203 ILE ILE A . n 
A 1 208 PHE 208 204 204 PHE PHE A . n 
A 1 209 HIS 209 205 205 HIS HIS A . n 
A 1 210 ALA 210 206 206 ALA ALA A . n 
A 1 211 LYS 211 207 207 LYS LYS A . n 
A 1 212 ARG 212 208 208 ARG ARG A . n 
A 1 213 PRO 213 209 209 PRO PRO A . n 
A 1 214 ALA 214 210 210 ALA ALA A . n 
A 1 215 ILE 215 211 211 ILE ILE A . n 
A 1 216 LEU 216 212 212 LEU LEU A . n 
A 1 217 ALA 217 213 213 ALA ALA A . n 
A 1 218 GLY 218 214 214 GLY GLY A . n 
A 1 219 HIS 219 215 215 HIS HIS A . n 
A 1 220 GLY 220 216 216 GLY GLY A . n 
A 1 221 ILE 221 217 217 ILE ILE A . n 
A 1 222 GLU 222 218 218 GLU GLU A . n 
A 1 223 CYS 223 219 219 CYS CYS A . n 
A 1 224 ALA 224 220 220 ALA ALA A . n 
A 1 225 LYS 225 221 221 LYS LYS A . n 
A 1 226 ALA 226 222 222 ALA ALA A . n 
A 1 227 TRP 227 223 223 TRP TRP A . n 
A 1 228 GLU 228 224 224 GLU GLU A . n 
A 1 229 GLU 229 225 225 GLU GLU A . n 
A 1 230 LEU 230 226 226 LEU LEU A . n 
A 1 231 LEU 231 227 227 LEU LEU A . n 
A 1 232 ASP 232 228 228 ASP ASP A . n 
A 1 233 PHE 233 229 229 PHE PHE A . n 
A 1 234 ALA 234 230 230 ALA ALA A . n 
A 1 235 GLU 235 231 231 GLU GLU A . n 
A 1 236 LEU 236 232 232 LEU LEU A . n 
A 1 237 THR 237 233 233 THR THR A . n 
A 1 238 GLY 238 234 234 GLY GLY A . n 
A 1 239 ILE 239 235 235 ILE ILE A . n 
A 1 240 PRO 240 236 236 PRO PRO A . n 
A 1 241 VAL 241 237 237 VAL VAL A . n 
A 1 242 ALA 242 238 238 ALA ALA A . n 
A 1 243 THR 243 239 239 THR THR A . n 
A 1 244 THR 244 240 240 THR THR A . n 
A 1 245 PRO 245 241 241 PRO PRO A . n 
A 1 246 LYS 246 242 242 LYS LYS A . n 
A 1 247 GLY 247 243 243 GLY GLY A . n 
A 1 248 LYS 248 244 244 LYS LYS A . n 
A 1 249 SER 249 245 245 SER SER A . n 
A 1 250 SER 250 246 246 SER SER A . n 
A 1 251 PHE 251 247 247 PHE PHE A . n 
A 1 252 PRO 252 248 248 PRO PRO A . n 
A 1 253 GLU 253 249 249 GLU GLU A . n 
A 1 254 ASN 254 250 250 ASN ASN A . n 
A 1 255 HIS 255 251 251 HIS HIS A . n 
A 1 256 ALA 256 252 252 ALA ALA A . n 
A 1 257 LEU 257 253 253 LEU LEU A . n 
A 1 258 SER 258 254 254 SER SER A . n 
A 1 259 LEU 259 255 255 LEU LEU A . n 
A 1 260 GLY 260 256 256 GLY GLY A . n 
A 1 261 VAL 261 257 257 VAL VAL A . n 
A 1 262 PHE 262 258 258 PHE PHE A . n 
A 1 263 GLY 263 259 259 GLY GLY A . n 
A 1 264 PHE 264 260 260 PHE PHE A . n 
A 1 265 ALA 265 261 261 ALA ALA A . n 
A 1 266 GLY 266 262 262 GLY GLY A . n 
A 1 267 HIS 267 263 263 HIS HIS A . n 
A 1 268 GLN 268 264 264 GLN GLN A . n 
A 1 269 LYS 269 265 265 LYS LYS A . n 
A 1 270 ALA 270 266 266 ALA ALA A . n 
A 1 271 THR 271 267 267 THR THR A . n 
A 1 272 ASP 272 268 268 ASP ASP A . n 
A 1 273 TYR 273 269 269 TYR TYR A . n 
A 1 274 LEU 274 270 270 LEU LEU A . n 
A 1 275 LEU 275 271 271 LEU LEU A . n 
A 1 276 SER 276 272 272 SER SER A . n 
A 1 277 GLY 277 273 273 GLY GLY A . n 
A 1 278 ASP 278 274 274 ASP ASP A . n 
A 1 279 VAL 279 275 275 VAL VAL A . n 
A 1 280 ASP 280 276 276 ASP ASP A . n 
A 1 281 VAL 281 277 277 VAL VAL A . n 
A 1 282 LEU 282 278 278 LEU LEU A . n 
A 1 283 ILE 283 279 279 ILE ILE A . n 
A 1 284 VAL 284 280 280 VAL VAL A . n 
A 1 285 ILE 285 281 281 ILE ILE A . n 
A 1 286 GLY 286 282 282 GLY GLY A . n 
A 1 287 SER 287 283 283 SER SER A . n 
A 1 288 SER 288 284 284 SER SER A . n 
A 1 289 LEU 289 285 285 LEU LEU A . n 
A 1 290 GLY 290 286 286 GLY GLY A . n 
A 1 291 ASP 291 287 287 ASP ASP A . n 
A 1 292 TRP 292 288 288 TRP TRP A . n 
A 1 293 GLN 293 289 289 GLN GLN A . n 
A 1 294 THR 294 290 290 THR THR A . n 
A 1 295 ASN 295 291 291 ASN ASN A . n 
A 1 296 SER 296 292 292 SER SER A . n 
A 1 297 TRP 297 293 293 TRP TRP A . n 
A 1 298 ASP 298 294 294 ASP ASP A . n 
A 1 299 PRO 299 295 295 PRO PRO A . n 
A 1 300 ARG 300 296 296 ARG ARG A . n 
A 1 301 LEU 301 297 297 LEU LEU A . n 
A 1 302 THR 302 298 298 THR THR A . n 
A 1 303 PRO 303 299 299 PRO PRO A . n 
A 1 304 SER 304 300 300 SER SER A . n 
A 1 305 VAL 305 301 301 VAL VAL A . n 
A 1 306 ALA 306 302 302 ALA ALA A . n 
A 1 307 LEU 307 303 303 LEU LEU A . n 
A 1 308 ILE 308 304 304 ILE ILE A . n 
A 1 309 GLN 309 305 305 GLN GLN A . n 
A 1 310 ILE 310 306 306 ILE ILE A . n 
A 1 311 ASP 311 307 307 ASP ASP A . n 
A 1 312 ILE 312 308 308 ILE ILE A . n 
A 1 313 ASP 313 309 309 ASP ASP A . n 
A 1 314 PRO 314 310 310 PRO PRO A . n 
A 1 315 MET 315 311 311 MET MET A . n 
A 1 316 GLU 316 312 312 GLU GLU A . n 
A 1 317 ILE 317 313 313 ILE ILE A . n 
A 1 318 GLY 318 314 314 GLY GLY A . n 
A 1 319 LYS 319 315 315 LYS LYS A . n 
A 1 320 ASN 320 316 316 ASN ASN A . n 
A 1 321 TYR 321 317 317 TYR TYR A . n 
A 1 322 PRO 322 318 318 PRO PRO A . n 
A 1 323 VAL 323 319 319 VAL VAL A . n 
A 1 324 ASP 324 320 320 ASP ASP A . n 
A 1 325 VAL 325 321 321 VAL VAL A . n 
A 1 326 GLY 326 322 322 GLY GLY A . n 
A 1 327 ILE 327 323 323 ILE ILE A . n 
A 1 328 ASN 328 324 324 ASN ASN A . n 
A 1 329 ALA 329 325 325 ALA ALA A . n 
A 1 330 ASP 330 326 326 ASP ASP A . n 
A 1 331 ALA 331 327 327 ALA ALA A . n 
A 1 332 SER 332 328 328 SER SER A . n 
A 1 333 GLU 333 329 329 GLU GLU A . n 
A 1 334 THR 334 330 330 THR THR A . n 
A 1 335 LEU 335 331 331 LEU LEU A . n 
A 1 336 LYS 336 332 332 LYS LYS A . n 
A 1 337 ALA 337 333 333 ALA ALA A . n 
A 1 338 LEU 338 334 334 LEU LEU A . n 
A 1 339 ILE 339 335 335 ILE ILE A . n 
A 1 340 LEU 340 336 336 LEU LEU A . n 
A 1 341 CYS 341 337 337 CYS CYS A . n 
A 1 342 ILE 342 338 338 ILE ILE A . n 
A 1 343 ARG 343 339 339 ARG ARG A . n 
A 1 344 SER 344 340 340 SER SER A . n 
A 1 345 SER 345 341 341 SER SER A . n 
A 1 346 GLY 346 342 342 GLY GLY A . n 
A 1 347 LYS 347 343 343 LYS LYS A . n 
A 1 348 MET 348 344 ?   ?   ?   A . n 
A 1 349 LEU 349 345 ?   ?   ?   A . n 
A 1 350 LYS 350 346 ?   ?   ?   A . n 
A 1 351 LYS 351 347 ?   ?   ?   A . n 
A 1 352 PRO 352 348 ?   ?   ?   A . n 
A 1 353 ALA 353 349 ?   ?   ?   A . n 
A 1 354 LEU 354 350 ?   ?   ?   A . n 
A 1 355 PRO 355 351 ?   ?   ?   A . n 
A 1 356 LEU 356 352 ?   ?   ?   A . n 
A 1 357 GLU 357 353 ?   ?   ?   A . n 
A 1 358 THR 358 354 ?   ?   ?   A . n 
A 1 359 LYS 359 355 ?   ?   ?   A . n 
A 1 360 GLU 360 356 ?   ?   ?   A . n 
A 1 361 GLN 361 357 ?   ?   ?   A . n 
A 1 362 THR 362 358 ?   ?   ?   A . n 
A 1 363 ALA 363 359 ?   ?   ?   A . n 
A 1 364 PHE 364 360 ?   ?   ?   A . n 
A 1 365 GLN 365 361 ?   ?   ?   A . n 
A 1 366 GLU 366 362 ?   ?   ?   A . n 
A 1 367 ILE 367 363 ?   ?   ?   A . n 
A 1 368 ASP 368 364 ?   ?   ?   A . n 
A 1 369 HIS 369 365 ?   ?   ?   A . n 
A 1 370 GLY 370 366 ?   ?   ?   A . n 
A 1 371 THR 371 367 ?   ?   ?   A . n 
A 1 372 GLU 372 368 ?   ?   ?   A . n 
A 1 373 GLY 373 369 ?   ?   ?   A . n 
A 1 374 ASN 374 370 ?   ?   ?   A . n 
A 1 375 GLY 375 371 371 GLY GLY A . n 
A 1 376 ILE 376 372 372 ILE ILE A . n 
A 1 377 HIS 377 373 373 HIS HIS A . n 
A 1 378 PRO 378 374 374 PRO PRO A . n 
A 1 379 ALA 379 375 375 ALA ALA A . n 
A 1 380 MET 380 376 376 MET MET A . n 
A 1 381 VAL 381 377 377 VAL VAL A . n 
A 1 382 VAL 382 378 378 VAL VAL A . n 
A 1 383 GLU 383 379 379 GLU GLU A . n 
A 1 384 ALA 384 380 380 ALA ALA A . n 
A 1 385 MET 385 381 381 MET MET A . n 
A 1 386 GLN 386 382 382 GLN GLN A . n 
A 1 387 ASN 387 383 383 ASN ASN A . n 
A 1 388 ARG 388 384 384 ARG ARG A . n 
A 1 389 LEU 389 385 385 LEU LEU A . n 
A 1 390 PRO 390 386 386 PRO PRO A . n 
A 1 391 ALA 391 387 387 ALA ALA A . n 
A 1 392 ASP 392 388 388 ASP ASP A . n 
A 1 393 THR 393 389 389 THR THR A . n 
A 1 394 ILE 394 390 390 ILE ILE A . n 
A 1 395 LEU 395 391 391 LEU LEU A . n 
A 1 396 PHE 396 392 392 PHE PHE A . n 
A 1 397 VAL 397 393 393 VAL VAL A . n 
A 1 398 ASP 398 394 394 ASP ASP A . n 
A 1 399 ASN 399 395 395 ASN ASN A . n 
A 1 400 GLY 400 396 396 GLY GLY A . n 
A 1 401 SER 401 397 397 SER SER A . n 
A 1 402 CYS 402 398 398 CYS CYS A . n 
A 1 403 ILE 403 399 399 ILE ILE A . n 
A 1 404 ASN 404 400 400 ASN ASN A . n 
A 1 405 TRP 405 401 401 TRP TRP A . n 
A 1 406 GLY 406 402 402 GLY GLY A . n 
A 1 407 VAL 407 403 403 VAL VAL A . n 
A 1 408 HIS 408 404 404 HIS HIS A . n 
A 1 409 CYS 409 405 405 CYS CYS A . n 
A 1 410 TYR 410 406 406 TYR TYR A . n 
A 1 411 LEU 411 407 407 LEU LEU A . n 
A 1 412 ALA 412 408 408 ALA ALA A . n 
A 1 413 GLN 413 409 409 GLN GLN A . n 
A 1 414 THR 414 410 410 THR THR A . n 
A 1 415 PRO 415 411 411 PRO PRO A . n 
A 1 416 GLY 416 412 412 GLY GLY A . n 
A 1 417 ALA 417 413 413 ALA ALA A . n 
A 1 418 PHE 418 414 414 PHE PHE A . n 
A 1 419 GLN 419 415 415 GLN GLN A . n 
A 1 420 ILE 420 416 416 ILE ILE A . n 
A 1 421 GLY 421 417 417 GLY GLY A . n 
A 1 422 LEU 422 418 418 LEU LEU A . n 
A 1 423 GLY 423 419 419 GLY GLY A . n 
A 1 424 LEU 424 420 420 LEU LEU A . n 
A 1 425 ALA 425 421 421 ALA ALA A . n 
A 1 426 ALA 426 422 422 ALA ALA A . n 
A 1 427 MET 427 423 423 MET MET A . n 
A 1 428 GLY 428 424 424 GLY GLY A . n 
A 1 429 HIS 429 425 425 HIS HIS A . n 
A 1 430 ALA 430 426 426 ALA ALA A . n 
A 1 431 VAL 431 427 427 VAL VAL A . n 
A 1 432 ALA 432 428 428 ALA ALA A . n 
A 1 433 ALA 433 429 429 ALA ALA A . n 
A 1 434 ALA 434 430 430 ALA ALA A . n 
A 1 435 ILE 435 431 431 ILE ILE A . n 
A 1 436 GLY 436 432 432 GLY GLY A . n 
A 1 437 GLY 437 433 433 GLY GLY A . n 
A 1 438 LYS 438 434 434 LYS LYS A . n 
A 1 439 LEU 439 435 435 LEU LEU A . n 
A 1 440 ALA 440 436 436 ALA ALA A . n 
A 1 441 ALA 441 437 437 ALA ALA A . n 
A 1 442 PRO 442 438 438 PRO PRO A . n 
A 1 443 ASP 443 439 439 ASP ASP A . n 
A 1 444 ARG 444 440 440 ARG ARG A . n 
A 1 445 PRO 445 441 441 PRO PRO A . n 
A 1 446 VAL 446 442 442 VAL VAL A . n 
A 1 447 VAL 447 443 443 VAL VAL A . n 
A 1 448 ALA 448 444 444 ALA ALA A . n 
A 1 449 LEU 449 445 445 LEU LEU A . n 
A 1 450 VAL 450 446 446 VAL VAL A . n 
A 1 451 GLY 451 447 447 GLY GLY A . n 
A 1 452 ASP 452 448 448 ASP ASP A . n 
A 1 453 ALA 453 449 449 ALA ALA A . n 
A 1 454 ALA 454 450 450 ALA ALA A . n 
A 1 455 PHE 455 451 451 PHE PHE A . n 
A 1 456 ALA 456 452 452 ALA ALA A . n 
A 1 457 MET 457 453 453 MET MET A . n 
A 1 458 ASN 458 454 454 ASN ASN A . n 
A 1 459 GLY 459 455 455 GLY GLY A . n 
A 1 460 MET 460 456 456 MET MET A . n 
A 1 461 GLU 461 457 457 GLU GLU A . n 
A 1 462 ILE 462 458 458 ILE ILE A . n 
A 1 463 HIS 463 459 459 HIS HIS A . n 
A 1 464 THR 464 460 460 THR THR A . n 
A 1 465 ALA 465 461 461 ALA ALA A . n 
A 1 466 ALA 466 462 462 ALA ALA A . n 
A 1 467 GLU 467 463 463 GLU GLU A . n 
A 1 468 TYR 468 464 464 TYR TYR A . n 
A 1 469 LYS 469 465 465 LYS LYS A . n 
A 1 470 ILE 470 466 466 ILE ILE A . n 
A 1 471 PRO 471 467 467 PRO PRO A . n 
A 1 472 VAL 472 468 468 VAL VAL A . n 
A 1 473 THR 473 469 469 THR THR A . n 
A 1 474 TRP 474 470 470 TRP TRP A . n 
A 1 475 ILE 475 471 471 ILE ILE A . n 
A 1 476 VAL 476 472 472 VAL VAL A . n 
A 1 477 LEU 477 473 473 LEU LEU A . n 
A 1 478 ASN 478 474 474 ASN ASN A . n 
A 1 479 ASN 479 475 475 ASN ASN A . n 
A 1 480 GLY 480 476 476 GLY GLY A . n 
A 1 481 GLY 481 477 477 GLY GLY A . n 
A 1 482 HIS 482 478 478 HIS HIS A . n 
A 1 483 GLY 483 479 479 GLY GLY A . n 
A 1 484 LEU 484 480 480 LEU LEU A . n 
A 1 485 VAL 485 481 481 VAL VAL A . n 
A 1 486 HIS 486 482 482 HIS HIS A . n 
A 1 487 LEU 487 483 483 LEU LEU A . n 
A 1 488 GLY 488 484 484 GLY GLY A . n 
A 1 489 GLU 489 485 485 GLU GLU A . n 
A 1 490 GLN 490 486 486 GLN GLN A . n 
A 1 491 HIS 491 487 487 HIS HIS A . n 
A 1 492 GLN 492 488 488 GLN GLN A . n 
A 1 493 PHE 493 489 489 PHE PHE A . n 
A 1 494 ASP 494 490 490 ASP ASP A . n 
A 1 495 SER 495 491 491 SER SER A . n 
A 1 496 LYS 496 492 492 LYS LYS A . n 
A 1 497 PHE 497 493 493 PHE PHE A . n 
A 1 498 ASP 498 494 494 ASP ASP A . n 
A 1 499 ILE 499 495 495 ILE ILE A . n 
A 1 500 SER 500 496 496 SER SER A . n 
A 1 501 SER 501 497 497 SER SER A . n 
A 1 502 PHE 502 498 498 PHE PHE A . n 
A 1 503 ARG 503 499 499 ARG ARG A . n 
A 1 504 LYS 504 500 500 LYS LYS A . n 
A 1 505 SER 505 501 501 SER SER A . n 
A 1 506 ILE 506 502 502 ILE ILE A . n 
A 1 507 ASP 507 503 503 ASP ASP A . n 
A 1 508 PHE 508 504 504 PHE PHE A . n 
A 1 509 CYS 509 505 505 CYS CYS A . n 
A 1 510 LYS 510 506 506 LYS LYS A . n 
A 1 511 MET 511 507 507 MET MET A . n 
A 1 512 ALA 512 508 508 ALA ALA A . n 
A 1 513 GLU 513 509 509 GLU GLU A . n 
A 1 514 SER 514 510 510 SER SER A . n 
A 1 515 LEU 515 511 511 LEU LEU A . n 
A 1 516 GLY 516 512 512 GLY GLY A . n 
A 1 517 VAL 517 513 513 VAL VAL A . n 
A 1 518 LYS 518 514 514 LYS LYS A . n 
A 1 519 SER 519 515 515 SER SER A . n 
A 1 520 TYR 520 516 516 TYR TYR A . n 
A 1 521 ARG 521 517 517 ARG ARG A . n 
A 1 522 ALA 522 518 518 ALA ALA A . n 
A 1 523 GLU 523 519 519 GLU GLU A . n 
A 1 524 THR 524 520 520 THR THR A . n 
A 1 525 VAL 525 521 521 VAL VAL A . n 
A 1 526 GLU 526 522 522 GLU GLU A . n 
A 1 527 ASP 527 523 523 ASP ASP A . n 
A 1 528 PHE 528 524 524 PHE PHE A . n 
A 1 529 ASP 529 525 525 ASP ASP A . n 
A 1 530 ALA 530 526 526 ALA ALA A . n 
A 1 531 ALA 531 527 527 ALA ALA A . n 
A 1 532 LEU 532 528 528 LEU LEU A . n 
A 1 533 LYS 533 529 529 LYS LYS A . n 
A 1 534 GLY 534 530 530 GLY GLY A . n 
A 1 535 ALA 535 531 531 ALA ALA A . n 
A 1 536 LEU 536 532 532 LEU LEU A . n 
A 1 537 ALA 537 533 533 ALA ALA A . n 
A 1 538 MET 538 534 534 MET MET A . n 
A 1 539 ASN 539 535 535 ASN ASN A . n 
A 1 540 THR 540 536 536 THR THR A . n 
A 1 541 PRO 541 537 537 PRO PRO A . n 
A 1 542 CYS 542 538 538 CYS CYS A . n 
A 1 543 LEU 543 539 539 LEU LEU A . n 
A 1 544 ILE 544 540 540 ILE ILE A . n 
A 1 545 ASP 545 541 541 ASP ASP A . n 
A 1 546 VAL 546 542 542 VAL VAL A . n 
A 1 547 GLN 547 543 543 GLN GLN A . n 
A 1 548 VAL 548 544 544 VAL VAL A . n 
A 1 549 ASP 549 545 545 ASP ASP A . n 
A 1 550 ILE 550 546 546 ILE ILE A . n 
A 1 551 ASP 551 547 547 ASP ASP A . n 
A 1 552 VAL 552 548 548 VAL VAL A . n 
A 1 553 LEU 553 549 549 LEU LEU A . n 
A 1 554 PRO 554 550 550 PRO PRO A . n 
A 1 555 PRO 555 551 551 PRO PRO A . n 
A 1 556 GLY 556 552 552 GLY GLY A . n 
A 1 557 MET 557 553 553 MET MET A . n 
A 1 558 LYS 558 554 554 LYS LYS A . n 
A 1 559 GLN 559 555 555 GLN GLN A . n 
A 1 560 ARG 560 556 556 ARG ARG A . n 
A 1 561 PHE 561 557 557 PHE PHE A . n 
A 1 562 ASP 562 558 558 ASP ASP A . n 
A 1 563 MET 563 559 ?   ?   ?   A . n 
A 1 564 LEU 564 560 ?   ?   ?   A . n 
A 1 565 ASN 565 561 ?   ?   ?   A . n 
A 1 566 LYS 566 562 ?   ?   ?   A . n 
A 1 567 SER 567 563 ?   ?   ?   A . n 
A 1 568 TYR 568 564 ?   ?   ?   A . n 
A 1 569 ALA 569 565 ?   ?   ?   A . n 
A 1 570 GLY 570 566 ?   ?   ?   A . n 
A 1 571 GLU 571 567 ?   ?   ?   A . n 
A 1 572 ARG 572 568 ?   ?   ?   A . n 
A 1 573 TYR 573 569 ?   ?   ?   A . n 
A 1 574 THR 574 570 ?   ?   ?   A . n 
A 1 575 ALA 575 571 ?   ?   ?   A . n 
A 1 576 PRO 576 572 ?   ?   ?   A . n 
A 1 577 ILE 577 573 ?   ?   ?   A . n 
A 1 578 GLY 578 574 ?   ?   ?   A . n 
A 1 579 HIS 579 575 ?   ?   ?   A . n 
A 1 580 HIS 580 576 ?   ?   ?   A . n 
A 1 581 HIS 581 577 ?   ?   ?   A . n 
A 1 582 HIS 582 578 ?   ?   ?   A . n 
A 1 583 HIS 583 579 ?   ?   ?   A . n 
A 1 584 HIS 584 580 ?   ?   ?   A . n 
B 1 1   MET 1   -3  ?   ?   ?   B . n 
B 1 2   GLY 2   -2  ?   ?   ?   B . n 
B 1 3   SER 3   -1  -1  SER SER B . n 
B 1 4   SER 4   0   0   SER SER B . n 
B 1 5   LYS 5   1   1   LYS LYS B . n 
B 1 6   THR 6   2   2   THR THR B . n 
B 1 7   VAL 7   3   3   VAL VAL B . n 
B 1 8   THR 8   4   4   THR THR B . n 
B 1 9   ALA 9   5   5   ALA ALA B . n 
B 1 10  VAL 10  6   6   VAL VAL B . n 
B 1 11  GLU 11  7   7   GLU GLU B . n 
B 1 12  LEU 12  8   8   LEU LEU B . n 
B 1 13  LEU 13  9   9   LEU LEU B . n 
B 1 14  VAL 14  10  10  VAL VAL B . n 
B 1 15  ARG 15  11  11  ARG ARG B . n 
B 1 16  GLN 16  12  12  GLN GLN B . n 
B 1 17  MET 17  13  13  MET MET B . n 
B 1 18  GLU 18  14  14  GLU GLU B . n 
B 1 19  ALA 19  15  15  ALA ALA B . n 
B 1 20  GLU 20  16  16  GLU GLU B . n 
B 1 21  GLY 21  17  17  GLY GLY B . n 
B 1 22  VAL 22  18  18  VAL VAL B . n 
B 1 23  SER 23  19  19  SER SER B . n 
B 1 24  TYR 24  20  20  TYR TYR B . n 
B 1 25  VAL 25  21  21  VAL VAL B . n 
B 1 26  PHE 26  22  22  PHE PHE B . n 
B 1 27  GLY 27  23  23  GLY GLY B . n 
B 1 28  ILE 28  24  24  ILE ILE B . n 
B 1 29  PRO 29  25  25  PRO PRO B . n 
B 1 30  GLY 30  26  26  GLY GLY B . n 
B 1 31  GLY 31  27  27  GLY GLY B . n 
B 1 32  PRO 32  28  28  PRO PRO B . n 
B 1 33  LEU 33  29  29  LEU LEU B . n 
B 1 34  MET 34  30  30  MET MET B . n 
B 1 35  PRO 35  31  31  PRO PRO B . n 
B 1 36  LEU 36  32  32  LEU LEU B . n 
B 1 37  TYR 37  33  33  TYR TYR B . n 
B 1 38  GLU 38  34  34  GLU GLU B . n 
B 1 39  ALA 39  35  35  ALA ALA B . n 
B 1 40  ILE 40  36  36  ILE ILE B . n 
B 1 41  PHE 41  37  37  PHE PHE B . n 
B 1 42  SER 42  38  38  SER SER B . n 
B 1 43  ARG 43  39  39  ARG ARG B . n 
B 1 44  LYS 44  40  40  LYS LYS B . n 
B 1 45  LYS 45  41  41  LYS LYS B . n 
B 1 46  ILE 46  42  42  ILE ILE B . n 
B 1 47  GLN 47  43  43  GLN GLN B . n 
B 1 48  PRO 48  44  44  PRO PRO B . n 
B 1 49  ILE 49  45  45  ILE ILE B . n 
B 1 50  LEU 50  46  46  LEU LEU B . n 
B 1 51  THR 51  47  47  THR THR B . n 
B 1 52  LYS 52  48  48  LYS LYS B . n 
B 1 53  HIS 53  49  49  HIS HIS B . n 
B 1 54  GLU 54  50  50  GLU GLU B . n 
B 1 55  GLU 55  51  51  GLU GLU B . n 
B 1 56  GLY 56  52  52  GLY GLY B . n 
B 1 57  ALA 57  53  53  ALA ALA B . n 
B 1 58  ALA 58  54  54  ALA ALA B . n 
B 1 59  PHE 59  55  55  PHE PHE B . n 
B 1 60  MET 60  56  56  MET MET B . n 
B 1 61  ALA 61  57  57  ALA ALA B . n 
B 1 62  GLU 62  58  58  GLU GLU B . n 
B 1 63  GLY 63  59  59  GLY GLY B . n 
B 1 64  TYR 64  60  60  TYR TYR B . n 
B 1 65  ALA 65  61  61  ALA ALA B . n 
B 1 66  ARG 66  62  62  ARG ARG B . n 
B 1 67  VAL 67  63  63  VAL VAL B . n 
B 1 68  SER 68  64  64  SER SER B . n 
B 1 69  GLY 69  65  65  GLY GLY B . n 
B 1 70  LYS 70  66  66  LYS LYS B . n 
B 1 71  LEU 71  67  67  LEU LEU B . n 
B 1 72  GLY 72  68  68  GLY GLY B . n 
B 1 73  VAL 73  69  69  VAL VAL B . n 
B 1 74  CYS 74  70  70  CYS CYS B . n 
B 1 75  CYS 75  71  71  CYS CYS B . n 
B 1 76  ALA 76  72  72  ALA ALA B . n 
B 1 77  THR 77  73  73  THR THR B . n 
B 1 78  THR 78  74  74  THR THR B . n 
B 1 79  GLY 79  75  75  GLY GLY B . n 
B 1 80  PRO 80  76  76  PRO PRO B . n 
B 1 81  GLY 81  77  77  GLY GLY B . n 
B 1 82  ALA 82  78  78  ALA ALA B . n 
B 1 83  THR 83  79  79  THR THR B . n 
B 1 84  ASN 84  80  80  ASN ASN B . n 
B 1 85  ALA 85  81  81  ALA ALA B . n 
B 1 86  LEU 86  82  82  LEU LEU B . n 
B 1 87  THR 87  83  83  THR THR B . n 
B 1 88  GLY 88  84  84  GLY GLY B . n 
B 1 89  ILE 89  85  85  ILE ILE B . n 
B 1 90  ALA 90  86  86  ALA ALA B . n 
B 1 91  CYS 91  87  87  CYS CYS B . n 
B 1 92  ALA 92  88  88  ALA ALA B . n 
B 1 93  TYR 93  89  89  TYR TYR B . n 
B 1 94  SER 94  90  90  SER SER B . n 
B 1 95  ASP 95  91  91  ASP ASP B . n 
B 1 96  SER 96  92  92  SER SER B . n 
B 1 97  THR 97  93  93  THR THR B . n 
B 1 98  PRO 98  94  94  PRO PRO B . n 
B 1 99  VAL 99  95  95  VAL VAL B . n 
B 1 100 LEU 100 96  96  LEU LEU B . n 
B 1 101 LEU 101 97  97  LEU LEU B . n 
B 1 102 LEU 102 98  98  LEU LEU B . n 
B 1 103 THR 103 99  99  THR THR B . n 
B 1 104 ALA 104 100 100 ALA ALA B . n 
B 1 105 GLN 105 101 101 GLN GLN B . n 
B 1 106 VAL 106 102 102 VAL VAL B . n 
B 1 107 GLY 107 103 103 GLY GLY B . n 
B 1 108 THR 108 104 104 THR THR B . n 
B 1 109 ALA 109 105 105 ALA ALA B . n 
B 1 110 ALA 110 106 106 ALA ALA B . n 
B 1 111 PHE 111 107 107 PHE PHE B . n 
B 1 112 GLY 112 108 108 GLY GLY B . n 
B 1 113 LYS 113 109 109 LYS LYS B . n 
B 1 114 GLY 114 110 110 GLY GLY B . n 
B 1 115 ALA 115 111 111 ALA ALA B . n 
B 1 116 LEU 116 112 112 LEU LEU B . n 
B 1 117 GLN 117 113 113 GLN GLN B . n 
B 1 118 GLU 118 114 114 GLU GLU B . n 
B 1 119 SER 119 115 115 SER SER B . n 
B 1 120 THR 120 116 116 THR THR B . n 
B 1 121 VAL 121 117 117 VAL VAL B . n 
B 1 122 HIS 122 118 118 HIS HIS B . n 
B 1 123 GLY 123 119 119 GLY GLY B . n 
B 1 124 VAL 124 120 120 VAL VAL B . n 
B 1 125 ASP 125 121 121 ASP ASP B . n 
B 1 126 LEU 126 122 122 LEU LEU B . n 
B 1 127 VAL 127 123 123 VAL VAL B . n 
B 1 128 SER 128 124 124 SER SER B . n 
B 1 129 ILE 129 125 125 ILE ILE B . n 
B 1 130 PHE 130 126 126 PHE PHE B . n 
B 1 131 SER 131 127 127 SER SER B . n 
B 1 132 PRO 132 128 128 PRO PRO B . n 
B 1 133 ILE 133 129 129 ILE ILE B . n 
B 1 134 THR 134 130 130 THR THR B . n 
B 1 135 LYS 135 131 131 LYS LYS B . n 
B 1 136 LEU 136 132 132 LEU LEU B . n 
B 1 137 SER 137 133 133 SER SER B . n 
B 1 138 VAL 138 134 134 VAL VAL B . n 
B 1 139 MET 139 135 135 MET MET B . n 
B 1 140 ILE 140 136 136 ILE ILE B . n 
B 1 141 PRO 141 137 137 PRO PRO B . n 
B 1 142 THR 142 138 138 THR THR B . n 
B 1 143 ALA 143 139 139 ALA ALA B . n 
B 1 144 GLU 144 140 140 GLU GLU B . n 
B 1 145 LYS 145 141 141 LYS LYS B . n 
B 1 146 MET 146 142 142 MET MET B . n 
B 1 147 GLY 147 143 143 GLY GLY B . n 
B 1 148 GLU 148 144 144 GLU GLU B . n 
B 1 149 MET 149 145 145 MET MET B . n 
B 1 150 THR 150 146 146 THR THR B . n 
B 1 151 ARG 151 147 147 ARG ARG B . n 
B 1 152 ARG 152 148 148 ARG ARG B . n 
B 1 153 ALA 153 149 149 ALA ALA B . n 
B 1 154 LEU 154 150 150 LEU LEU B . n 
B 1 155 ARG 155 151 151 ARG ARG B . n 
B 1 156 THR 156 152 152 THR THR B . n 
B 1 157 ALA 157 153 153 ALA ALA B . n 
B 1 158 GLN 158 154 154 GLN GLN B . n 
B 1 159 SER 159 155 155 SER SER B . n 
B 1 160 GLY 160 156 156 GLY GLY B . n 
B 1 161 ARG 161 157 157 ARG ARG B . n 
B 1 162 PRO 162 158 158 PRO PRO B . n 
B 1 163 GLY 163 159 159 GLY GLY B . n 
B 1 164 PRO 164 160 160 PRO PRO B . n 
B 1 165 ILE 165 161 161 ILE ILE B . n 
B 1 166 HIS 166 162 162 HIS HIS B . n 
B 1 167 LEU 167 163 163 LEU LEU B . n 
B 1 168 ASN 168 164 164 ASN ASN B . n 
B 1 169 ILE 169 165 165 ILE ILE B . n 
B 1 170 PRO 170 166 166 PRO PRO B . n 
B 1 171 ALA 171 167 167 ALA ALA B . n 
B 1 172 ASP 172 168 168 ASP ASP B . n 
B 1 173 ILE 173 169 169 ILE ILE B . n 
B 1 174 ALA 174 170 170 ALA ALA B . n 
B 1 175 LYS 175 171 171 LYS LYS B . n 
B 1 176 HIS 176 172 172 HIS HIS B . n 
B 1 177 PRO 177 173 173 PRO PRO B . n 
B 1 178 VAL 178 174 174 VAL VAL B . n 
B 1 179 PRO 179 175 175 PRO PRO B . n 
B 1 180 LEU 180 176 176 LEU LEU B . n 
B 1 181 GLU 181 177 177 GLU GLU B . n 
B 1 182 VAL 182 178 178 VAL VAL B . n 
B 1 183 PHE 183 179 179 PHE PHE B . n 
B 1 184 PRO 184 180 180 PRO PRO B . n 
B 1 185 PRO 185 181 181 PRO PRO B . n 
B 1 186 MET 186 182 182 MET MET B . n 
B 1 187 ASN 187 183 183 ASN ASN B . n 
B 1 188 TYR 188 184 184 TYR TYR B . n 
B 1 189 ARG 189 185 185 ARG ARG B . n 
B 1 190 GLY 190 186 186 GLY GLY B . n 
B 1 191 GLY 191 187 187 GLY GLY B . n 
B 1 192 LYS 192 188 188 LYS LYS B . n 
B 1 193 PRO 193 189 189 PRO PRO B . n 
B 1 194 ALA 194 190 190 ALA ALA B . n 
B 1 195 PRO 195 191 191 PRO PRO B . n 
B 1 196 THR 196 192 192 THR THR B . n 
B 1 197 ILE 197 193 193 ILE ILE B . n 
B 1 198 MET 198 194 194 MET MET B . n 
B 1 199 ASP 199 195 195 ASP ASP B . n 
B 1 200 VAL 200 196 196 VAL VAL B . n 
B 1 201 VAL 201 197 197 VAL VAL B . n 
B 1 202 ARG 202 198 198 ARG ARG B . n 
B 1 203 VAL 203 199 199 VAL VAL B . n 
B 1 204 ALA 204 200 200 ALA ALA B . n 
B 1 205 GLU 205 201 201 GLU GLU B . n 
B 1 206 LEU 206 202 202 LEU LEU B . n 
B 1 207 ILE 207 203 203 ILE ILE B . n 
B 1 208 PHE 208 204 204 PHE PHE B . n 
B 1 209 HIS 209 205 205 HIS HIS B . n 
B 1 210 ALA 210 206 206 ALA ALA B . n 
B 1 211 LYS 211 207 207 LYS LYS B . n 
B 1 212 ARG 212 208 208 ARG ARG B . n 
B 1 213 PRO 213 209 209 PRO PRO B . n 
B 1 214 ALA 214 210 210 ALA ALA B . n 
B 1 215 ILE 215 211 211 ILE ILE B . n 
B 1 216 LEU 216 212 212 LEU LEU B . n 
B 1 217 ALA 217 213 213 ALA ALA B . n 
B 1 218 GLY 218 214 214 GLY GLY B . n 
B 1 219 HIS 219 215 215 HIS HIS B . n 
B 1 220 GLY 220 216 216 GLY GLY B . n 
B 1 221 ILE 221 217 217 ILE ILE B . n 
B 1 222 GLU 222 218 218 GLU GLU B . n 
B 1 223 CYS 223 219 219 CYS CYS B . n 
B 1 224 ALA 224 220 220 ALA ALA B . n 
B 1 225 LYS 225 221 221 LYS LYS B . n 
B 1 226 ALA 226 222 222 ALA ALA B . n 
B 1 227 TRP 227 223 223 TRP TRP B . n 
B 1 228 GLU 228 224 224 GLU GLU B . n 
B 1 229 GLU 229 225 225 GLU GLU B . n 
B 1 230 LEU 230 226 226 LEU LEU B . n 
B 1 231 LEU 231 227 227 LEU LEU B . n 
B 1 232 ASP 232 228 228 ASP ASP B . n 
B 1 233 PHE 233 229 229 PHE PHE B . n 
B 1 234 ALA 234 230 230 ALA ALA B . n 
B 1 235 GLU 235 231 231 GLU GLU B . n 
B 1 236 LEU 236 232 232 LEU LEU B . n 
B 1 237 THR 237 233 233 THR THR B . n 
B 1 238 GLY 238 234 234 GLY GLY B . n 
B 1 239 ILE 239 235 235 ILE ILE B . n 
B 1 240 PRO 240 236 236 PRO PRO B . n 
B 1 241 VAL 241 237 237 VAL VAL B . n 
B 1 242 ALA 242 238 238 ALA ALA B . n 
B 1 243 THR 243 239 239 THR THR B . n 
B 1 244 THR 244 240 240 THR THR B . n 
B 1 245 PRO 245 241 241 PRO PRO B . n 
B 1 246 LYS 246 242 242 LYS LYS B . n 
B 1 247 GLY 247 243 243 GLY GLY B . n 
B 1 248 LYS 248 244 244 LYS LYS B . n 
B 1 249 SER 249 245 245 SER SER B . n 
B 1 250 SER 250 246 246 SER SER B . n 
B 1 251 PHE 251 247 247 PHE PHE B . n 
B 1 252 PRO 252 248 248 PRO PRO B . n 
B 1 253 GLU 253 249 249 GLU GLU B . n 
B 1 254 ASN 254 250 250 ASN ASN B . n 
B 1 255 HIS 255 251 251 HIS HIS B . n 
B 1 256 ALA 256 252 252 ALA ALA B . n 
B 1 257 LEU 257 253 253 LEU LEU B . n 
B 1 258 SER 258 254 254 SER SER B . n 
B 1 259 LEU 259 255 255 LEU LEU B . n 
B 1 260 GLY 260 256 256 GLY GLY B . n 
B 1 261 VAL 261 257 257 VAL VAL B . n 
B 1 262 PHE 262 258 258 PHE PHE B . n 
B 1 263 GLY 263 259 259 GLY GLY B . n 
B 1 264 PHE 264 260 260 PHE PHE B . n 
B 1 265 ALA 265 261 261 ALA ALA B . n 
B 1 266 GLY 266 262 262 GLY GLY B . n 
B 1 267 HIS 267 263 263 HIS HIS B . n 
B 1 268 GLN 268 264 264 GLN GLN B . n 
B 1 269 LYS 269 265 265 LYS LYS B . n 
B 1 270 ALA 270 266 266 ALA ALA B . n 
B 1 271 THR 271 267 267 THR THR B . n 
B 1 272 ASP 272 268 268 ASP ASP B . n 
B 1 273 TYR 273 269 269 TYR TYR B . n 
B 1 274 LEU 274 270 270 LEU LEU B . n 
B 1 275 LEU 275 271 271 LEU LEU B . n 
B 1 276 SER 276 272 272 SER SER B . n 
B 1 277 GLY 277 273 273 GLY GLY B . n 
B 1 278 ASP 278 274 274 ASP ASP B . n 
B 1 279 VAL 279 275 275 VAL VAL B . n 
B 1 280 ASP 280 276 276 ASP ASP B . n 
B 1 281 VAL 281 277 277 VAL VAL B . n 
B 1 282 LEU 282 278 278 LEU LEU B . n 
B 1 283 ILE 283 279 279 ILE ILE B . n 
B 1 284 VAL 284 280 280 VAL VAL B . n 
B 1 285 ILE 285 281 281 ILE ILE B . n 
B 1 286 GLY 286 282 282 GLY GLY B . n 
B 1 287 SER 287 283 283 SER SER B . n 
B 1 288 SER 288 284 284 SER SER B . n 
B 1 289 LEU 289 285 285 LEU LEU B . n 
B 1 290 GLY 290 286 286 GLY GLY B . n 
B 1 291 ASP 291 287 287 ASP ASP B . n 
B 1 292 TRP 292 288 288 TRP TRP B . n 
B 1 293 GLN 293 289 289 GLN GLN B . n 
B 1 294 THR 294 290 290 THR THR B . n 
B 1 295 ASN 295 291 291 ASN ASN B . n 
B 1 296 SER 296 292 292 SER SER B . n 
B 1 297 TRP 297 293 293 TRP TRP B . n 
B 1 298 ASP 298 294 294 ASP ASP B . n 
B 1 299 PRO 299 295 295 PRO PRO B . n 
B 1 300 ARG 300 296 296 ARG ARG B . n 
B 1 301 LEU 301 297 297 LEU LEU B . n 
B 1 302 THR 302 298 298 THR THR B . n 
B 1 303 PRO 303 299 299 PRO PRO B . n 
B 1 304 SER 304 300 300 SER SER B . n 
B 1 305 VAL 305 301 301 VAL VAL B . n 
B 1 306 ALA 306 302 302 ALA ALA B . n 
B 1 307 LEU 307 303 303 LEU LEU B . n 
B 1 308 ILE 308 304 304 ILE ILE B . n 
B 1 309 GLN 309 305 305 GLN GLN B . n 
B 1 310 ILE 310 306 306 ILE ILE B . n 
B 1 311 ASP 311 307 307 ASP ASP B . n 
B 1 312 ILE 312 308 308 ILE ILE B . n 
B 1 313 ASP 313 309 309 ASP ASP B . n 
B 1 314 PRO 314 310 310 PRO PRO B . n 
B 1 315 MET 315 311 311 MET MET B . n 
B 1 316 GLU 316 312 312 GLU GLU B . n 
B 1 317 ILE 317 313 313 ILE ILE B . n 
B 1 318 GLY 318 314 314 GLY GLY B . n 
B 1 319 LYS 319 315 315 LYS LYS B . n 
B 1 320 ASN 320 316 316 ASN ASN B . n 
B 1 321 TYR 321 317 317 TYR TYR B . n 
B 1 322 PRO 322 318 318 PRO PRO B . n 
B 1 323 VAL 323 319 319 VAL VAL B . n 
B 1 324 ASP 324 320 320 ASP ASP B . n 
B 1 325 VAL 325 321 321 VAL VAL B . n 
B 1 326 GLY 326 322 322 GLY GLY B . n 
B 1 327 ILE 327 323 323 ILE ILE B . n 
B 1 328 ASN 328 324 324 ASN ASN B . n 
B 1 329 ALA 329 325 325 ALA ALA B . n 
B 1 330 ASP 330 326 326 ASP ASP B . n 
B 1 331 ALA 331 327 327 ALA ALA B . n 
B 1 332 SER 332 328 328 SER SER B . n 
B 1 333 GLU 333 329 329 GLU GLU B . n 
B 1 334 THR 334 330 330 THR THR B . n 
B 1 335 LEU 335 331 331 LEU LEU B . n 
B 1 336 LYS 336 332 332 LYS LYS B . n 
B 1 337 ALA 337 333 333 ALA ALA B . n 
B 1 338 LEU 338 334 334 LEU LEU B . n 
B 1 339 ILE 339 335 335 ILE ILE B . n 
B 1 340 LEU 340 336 336 LEU LEU B . n 
B 1 341 CYS 341 337 337 CYS CYS B . n 
B 1 342 ILE 342 338 338 ILE ILE B . n 
B 1 343 ARG 343 339 339 ARG ARG B . n 
B 1 344 SER 344 340 340 SER SER B . n 
B 1 345 SER 345 341 341 SER SER B . n 
B 1 346 GLY 346 342 342 GLY GLY B . n 
B 1 347 LYS 347 343 343 LYS LYS B . n 
B 1 348 MET 348 344 ?   ?   ?   B . n 
B 1 349 LEU 349 345 ?   ?   ?   B . n 
B 1 350 LYS 350 346 ?   ?   ?   B . n 
B 1 351 LYS 351 347 ?   ?   ?   B . n 
B 1 352 PRO 352 348 ?   ?   ?   B . n 
B 1 353 ALA 353 349 ?   ?   ?   B . n 
B 1 354 LEU 354 350 ?   ?   ?   B . n 
B 1 355 PRO 355 351 ?   ?   ?   B . n 
B 1 356 LEU 356 352 ?   ?   ?   B . n 
B 1 357 GLU 357 353 ?   ?   ?   B . n 
B 1 358 THR 358 354 ?   ?   ?   B . n 
B 1 359 LYS 359 355 ?   ?   ?   B . n 
B 1 360 GLU 360 356 ?   ?   ?   B . n 
B 1 361 GLN 361 357 ?   ?   ?   B . n 
B 1 362 THR 362 358 ?   ?   ?   B . n 
B 1 363 ALA 363 359 ?   ?   ?   B . n 
B 1 364 PHE 364 360 ?   ?   ?   B . n 
B 1 365 GLN 365 361 ?   ?   ?   B . n 
B 1 366 GLU 366 362 ?   ?   ?   B . n 
B 1 367 ILE 367 363 ?   ?   ?   B . n 
B 1 368 ASP 368 364 ?   ?   ?   B . n 
B 1 369 HIS 369 365 ?   ?   ?   B . n 
B 1 370 GLY 370 366 ?   ?   ?   B . n 
B 1 371 THR 371 367 ?   ?   ?   B . n 
B 1 372 GLU 372 368 ?   ?   ?   B . n 
B 1 373 GLY 373 369 ?   ?   ?   B . n 
B 1 374 ASN 374 370 ?   ?   ?   B . n 
B 1 375 GLY 375 371 371 GLY GLY B . n 
B 1 376 ILE 376 372 372 ILE ILE B . n 
B 1 377 HIS 377 373 373 HIS HIS B . n 
B 1 378 PRO 378 374 374 PRO PRO B . n 
B 1 379 ALA 379 375 375 ALA ALA B . n 
B 1 380 MET 380 376 376 MET MET B . n 
B 1 381 VAL 381 377 377 VAL VAL B . n 
B 1 382 VAL 382 378 378 VAL VAL B . n 
B 1 383 GLU 383 379 379 GLU GLU B . n 
B 1 384 ALA 384 380 380 ALA ALA B . n 
B 1 385 MET 385 381 381 MET MET B . n 
B 1 386 GLN 386 382 382 GLN GLN B . n 
B 1 387 ASN 387 383 383 ASN ASN B . n 
B 1 388 ARG 388 384 384 ARG ARG B . n 
B 1 389 LEU 389 385 385 LEU LEU B . n 
B 1 390 PRO 390 386 386 PRO PRO B . n 
B 1 391 ALA 391 387 387 ALA ALA B . n 
B 1 392 ASP 392 388 388 ASP ASP B . n 
B 1 393 THR 393 389 389 THR THR B . n 
B 1 394 ILE 394 390 390 ILE ILE B . n 
B 1 395 LEU 395 391 391 LEU LEU B . n 
B 1 396 PHE 396 392 392 PHE PHE B . n 
B 1 397 VAL 397 393 393 VAL VAL B . n 
B 1 398 ASP 398 394 394 ASP ASP B . n 
B 1 399 ASN 399 395 395 ASN ASN B . n 
B 1 400 GLY 400 396 396 GLY GLY B . n 
B 1 401 SER 401 397 397 SER SER B . n 
B 1 402 CYS 402 398 398 CYS CYS B . n 
B 1 403 ILE 403 399 399 ILE ILE B . n 
B 1 404 ASN 404 400 400 ASN ASN B . n 
B 1 405 TRP 405 401 401 TRP TRP B . n 
B 1 406 GLY 406 402 402 GLY GLY B . n 
B 1 407 VAL 407 403 403 VAL VAL B . n 
B 1 408 HIS 408 404 404 HIS HIS B . n 
B 1 409 CYS 409 405 405 CYS CYS B . n 
B 1 410 TYR 410 406 406 TYR TYR B . n 
B 1 411 LEU 411 407 407 LEU LEU B . n 
B 1 412 ALA 412 408 408 ALA ALA B . n 
B 1 413 GLN 413 409 409 GLN GLN B . n 
B 1 414 THR 414 410 410 THR THR B . n 
B 1 415 PRO 415 411 411 PRO PRO B . n 
B 1 416 GLY 416 412 412 GLY GLY B . n 
B 1 417 ALA 417 413 413 ALA ALA B . n 
B 1 418 PHE 418 414 414 PHE PHE B . n 
B 1 419 GLN 419 415 415 GLN GLN B . n 
B 1 420 ILE 420 416 416 ILE ILE B . n 
B 1 421 GLY 421 417 417 GLY GLY B . n 
B 1 422 LEU 422 418 418 LEU LEU B . n 
B 1 423 GLY 423 419 419 GLY GLY B . n 
B 1 424 LEU 424 420 420 LEU LEU B . n 
B 1 425 ALA 425 421 421 ALA ALA B . n 
B 1 426 ALA 426 422 422 ALA ALA B . n 
B 1 427 MET 427 423 423 MET MET B . n 
B 1 428 GLY 428 424 424 GLY GLY B . n 
B 1 429 HIS 429 425 425 HIS HIS B . n 
B 1 430 ALA 430 426 426 ALA ALA B . n 
B 1 431 VAL 431 427 427 VAL VAL B . n 
B 1 432 ALA 432 428 428 ALA ALA B . n 
B 1 433 ALA 433 429 429 ALA ALA B . n 
B 1 434 ALA 434 430 430 ALA ALA B . n 
B 1 435 ILE 435 431 431 ILE ILE B . n 
B 1 436 GLY 436 432 432 GLY GLY B . n 
B 1 437 GLY 437 433 433 GLY GLY B . n 
B 1 438 LYS 438 434 434 LYS LYS B . n 
B 1 439 LEU 439 435 435 LEU LEU B . n 
B 1 440 ALA 440 436 436 ALA ALA B . n 
B 1 441 ALA 441 437 437 ALA ALA B . n 
B 1 442 PRO 442 438 438 PRO PRO B . n 
B 1 443 ASP 443 439 439 ASP ASP B . n 
B 1 444 ARG 444 440 440 ARG ARG B . n 
B 1 445 PRO 445 441 441 PRO PRO B . n 
B 1 446 VAL 446 442 442 VAL VAL B . n 
B 1 447 VAL 447 443 443 VAL VAL B . n 
B 1 448 ALA 448 444 444 ALA ALA B . n 
B 1 449 LEU 449 445 445 LEU LEU B . n 
B 1 450 VAL 450 446 446 VAL VAL B . n 
B 1 451 GLY 451 447 447 GLY GLY B . n 
B 1 452 ASP 452 448 448 ASP ASP B . n 
B 1 453 ALA 453 449 449 ALA ALA B . n 
B 1 454 ALA 454 450 450 ALA ALA B . n 
B 1 455 PHE 455 451 451 PHE PHE B . n 
B 1 456 ALA 456 452 452 ALA ALA B . n 
B 1 457 MET 457 453 453 MET MET B . n 
B 1 458 ASN 458 454 454 ASN ASN B . n 
B 1 459 GLY 459 455 455 GLY GLY B . n 
B 1 460 MET 460 456 456 MET MET B . n 
B 1 461 GLU 461 457 457 GLU GLU B . n 
B 1 462 ILE 462 458 458 ILE ILE B . n 
B 1 463 HIS 463 459 459 HIS HIS B . n 
B 1 464 THR 464 460 460 THR THR B . n 
B 1 465 ALA 465 461 461 ALA ALA B . n 
B 1 466 ALA 466 462 462 ALA ALA B . n 
B 1 467 GLU 467 463 463 GLU GLU B . n 
B 1 468 TYR 468 464 464 TYR TYR B . n 
B 1 469 LYS 469 465 465 LYS LYS B . n 
B 1 470 ILE 470 466 466 ILE ILE B . n 
B 1 471 PRO 471 467 467 PRO PRO B . n 
B 1 472 VAL 472 468 468 VAL VAL B . n 
B 1 473 THR 473 469 469 THR THR B . n 
B 1 474 TRP 474 470 470 TRP TRP B . n 
B 1 475 ILE 475 471 471 ILE ILE B . n 
B 1 476 VAL 476 472 472 VAL VAL B . n 
B 1 477 LEU 477 473 473 LEU LEU B . n 
B 1 478 ASN 478 474 474 ASN ASN B . n 
B 1 479 ASN 479 475 475 ASN ASN B . n 
B 1 480 GLY 480 476 476 GLY GLY B . n 
B 1 481 GLY 481 477 477 GLY GLY B . n 
B 1 482 HIS 482 478 478 HIS HIS B . n 
B 1 483 GLY 483 479 479 GLY GLY B . n 
B 1 484 LEU 484 480 480 LEU LEU B . n 
B 1 485 VAL 485 481 481 VAL VAL B . n 
B 1 486 HIS 486 482 482 HIS HIS B . n 
B 1 487 LEU 487 483 483 LEU LEU B . n 
B 1 488 GLY 488 484 484 GLY GLY B . n 
B 1 489 GLU 489 485 485 GLU GLU B . n 
B 1 490 GLN 490 486 486 GLN GLN B . n 
B 1 491 HIS 491 487 487 HIS HIS B . n 
B 1 492 GLN 492 488 488 GLN GLN B . n 
B 1 493 PHE 493 489 489 PHE PHE B . n 
B 1 494 ASP 494 490 490 ASP ASP B . n 
B 1 495 SER 495 491 491 SER SER B . n 
B 1 496 LYS 496 492 492 LYS LYS B . n 
B 1 497 PHE 497 493 493 PHE PHE B . n 
B 1 498 ASP 498 494 494 ASP ASP B . n 
B 1 499 ILE 499 495 495 ILE ILE B . n 
B 1 500 SER 500 496 496 SER SER B . n 
B 1 501 SER 501 497 497 SER SER B . n 
B 1 502 PHE 502 498 498 PHE PHE B . n 
B 1 503 ARG 503 499 499 ARG ARG B . n 
B 1 504 LYS 504 500 500 LYS LYS B . n 
B 1 505 SER 505 501 501 SER SER B . n 
B 1 506 ILE 506 502 502 ILE ILE B . n 
B 1 507 ASP 507 503 503 ASP ASP B . n 
B 1 508 PHE 508 504 504 PHE PHE B . n 
B 1 509 CYS 509 505 505 CYS CYS B . n 
B 1 510 LYS 510 506 506 LYS LYS B . n 
B 1 511 MET 511 507 507 MET MET B . n 
B 1 512 ALA 512 508 508 ALA ALA B . n 
B 1 513 GLU 513 509 509 GLU GLU B . n 
B 1 514 SER 514 510 510 SER SER B . n 
B 1 515 LEU 515 511 511 LEU LEU B . n 
B 1 516 GLY 516 512 512 GLY GLY B . n 
B 1 517 VAL 517 513 513 VAL VAL B . n 
B 1 518 LYS 518 514 514 LYS LYS B . n 
B 1 519 SER 519 515 515 SER SER B . n 
B 1 520 TYR 520 516 516 TYR TYR B . n 
B 1 521 ARG 521 517 517 ARG ARG B . n 
B 1 522 ALA 522 518 518 ALA ALA B . n 
B 1 523 GLU 523 519 519 GLU GLU B . n 
B 1 524 THR 524 520 520 THR THR B . n 
B 1 525 VAL 525 521 521 VAL VAL B . n 
B 1 526 GLU 526 522 522 GLU GLU B . n 
B 1 527 ASP 527 523 523 ASP ASP B . n 
B 1 528 PHE 528 524 524 PHE PHE B . n 
B 1 529 ASP 529 525 525 ASP ASP B . n 
B 1 530 ALA 530 526 526 ALA ALA B . n 
B 1 531 ALA 531 527 527 ALA ALA B . n 
B 1 532 LEU 532 528 528 LEU LEU B . n 
B 1 533 LYS 533 529 529 LYS LYS B . n 
B 1 534 GLY 534 530 530 GLY GLY B . n 
B 1 535 ALA 535 531 531 ALA ALA B . n 
B 1 536 LEU 536 532 532 LEU LEU B . n 
B 1 537 ALA 537 533 533 ALA ALA B . n 
B 1 538 MET 538 534 534 MET MET B . n 
B 1 539 ASN 539 535 535 ASN ASN B . n 
B 1 540 THR 540 536 536 THR THR B . n 
B 1 541 PRO 541 537 537 PRO PRO B . n 
B 1 542 CYS 542 538 538 CYS CYS B . n 
B 1 543 LEU 543 539 539 LEU LEU B . n 
B 1 544 ILE 544 540 540 ILE ILE B . n 
B 1 545 ASP 545 541 541 ASP ASP B . n 
B 1 546 VAL 546 542 542 VAL VAL B . n 
B 1 547 GLN 547 543 543 GLN GLN B . n 
B 1 548 VAL 548 544 544 VAL VAL B . n 
B 1 549 ASP 549 545 545 ASP ASP B . n 
B 1 550 ILE 550 546 546 ILE ILE B . n 
B 1 551 ASP 551 547 547 ASP ASP B . n 
B 1 552 VAL 552 548 548 VAL VAL B . n 
B 1 553 LEU 553 549 549 LEU LEU B . n 
B 1 554 PRO 554 550 550 PRO PRO B . n 
B 1 555 PRO 555 551 551 PRO PRO B . n 
B 1 556 GLY 556 552 552 GLY GLY B . n 
B 1 557 MET 557 553 553 MET MET B . n 
B 1 558 LYS 558 554 554 LYS LYS B . n 
B 1 559 GLN 559 555 555 GLN GLN B . n 
B 1 560 ARG 560 556 556 ARG ARG B . n 
B 1 561 PHE 561 557 557 PHE PHE B . n 
B 1 562 ASP 562 558 558 ASP ASP B . n 
B 1 563 MET 563 559 ?   ?   ?   B . n 
B 1 564 LEU 564 560 ?   ?   ?   B . n 
B 1 565 ASN 565 561 ?   ?   ?   B . n 
B 1 566 LYS 566 562 ?   ?   ?   B . n 
B 1 567 SER 567 563 ?   ?   ?   B . n 
B 1 568 TYR 568 564 ?   ?   ?   B . n 
B 1 569 ALA 569 565 ?   ?   ?   B . n 
B 1 570 GLY 570 566 ?   ?   ?   B . n 
B 1 571 GLU 571 567 ?   ?   ?   B . n 
B 1 572 ARG 572 568 ?   ?   ?   B . n 
B 1 573 TYR 573 569 ?   ?   ?   B . n 
B 1 574 THR 574 570 ?   ?   ?   B . n 
B 1 575 ALA 575 571 ?   ?   ?   B . n 
B 1 576 PRO 576 572 ?   ?   ?   B . n 
B 1 577 ILE 577 573 ?   ?   ?   B . n 
B 1 578 GLY 578 574 ?   ?   ?   B . n 
B 1 579 HIS 579 575 ?   ?   ?   B . n 
B 1 580 HIS 580 576 ?   ?   ?   B . n 
B 1 581 HIS 581 577 ?   ?   ?   B . n 
B 1 582 HIS 582 578 ?   ?   ?   B . n 
B 1 583 HIS 583 579 ?   ?   ?   B . n 
B 1 584 HIS 584 580 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 TPP ? ? TPP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ADP 1   601 601 ADP ADP A . 
D 3 TPP 1   602 701 TPP TPP A . 
E 4 MG  1   603 1   MG  MG  A . 
F 2 ADP 1   601 601 ADP ADP B . 
G 3 TPP 1   602 701 TPP TPP B . 
H 4 MG  1   603 2   MG  MG  B . 
I 5 HOH 1   701 151 HOH HOH A . 
I 5 HOH 2   702 108 HOH HOH A . 
I 5 HOH 3   703 16  HOH HOH A . 
I 5 HOH 4   704 59  HOH HOH A . 
I 5 HOH 5   705 256 HOH HOH A . 
I 5 HOH 6   706 76  HOH HOH A . 
I 5 HOH 7   707 33  HOH HOH A . 
I 5 HOH 8   708 1   HOH HOH A . 
I 5 HOH 9   709 89  HOH HOH A . 
I 5 HOH 10  710 279 HOH HOH A . 
I 5 HOH 11  711 154 HOH HOH A . 
I 5 HOH 12  712 244 HOH HOH A . 
I 5 HOH 13  713 6   HOH HOH A . 
I 5 HOH 14  714 288 HOH HOH A . 
I 5 HOH 15  715 248 HOH HOH A . 
I 5 HOH 16  716 51  HOH HOH A . 
I 5 HOH 17  717 130 HOH HOH A . 
I 5 HOH 18  718 219 HOH HOH A . 
I 5 HOH 19  719 131 HOH HOH A . 
I 5 HOH 20  720 28  HOH HOH A . 
I 5 HOH 21  721 53  HOH HOH A . 
I 5 HOH 22  722 140 HOH HOH A . 
I 5 HOH 23  723 109 HOH HOH A . 
I 5 HOH 24  724 74  HOH HOH A . 
I 5 HOH 25  725 234 HOH HOH A . 
I 5 HOH 26  726 63  HOH HOH A . 
I 5 HOH 27  727 105 HOH HOH A . 
I 5 HOH 28  728 90  HOH HOH A . 
I 5 HOH 29  729 40  HOH HOH A . 
I 5 HOH 30  730 192 HOH HOH A . 
I 5 HOH 31  731 213 HOH HOH A . 
I 5 HOH 32  732 18  HOH HOH A . 
I 5 HOH 33  733 15  HOH HOH A . 
I 5 HOH 34  734 10  HOH HOH A . 
I 5 HOH 35  735 2   HOH HOH A . 
I 5 HOH 36  736 42  HOH HOH A . 
I 5 HOH 37  737 46  HOH HOH A . 
I 5 HOH 38  738 65  HOH HOH A . 
I 5 HOH 39  739 61  HOH HOH A . 
I 5 HOH 40  740 148 HOH HOH A . 
I 5 HOH 41  741 120 HOH HOH A . 
I 5 HOH 42  742 57  HOH HOH A . 
I 5 HOH 43  743 110 HOH HOH A . 
I 5 HOH 44  744 45  HOH HOH A . 
I 5 HOH 45  745 162 HOH HOH A . 
I 5 HOH 46  746 7   HOH HOH A . 
I 5 HOH 47  747 143 HOH HOH A . 
I 5 HOH 48  748 47  HOH HOH A . 
I 5 HOH 49  749 128 HOH HOH A . 
I 5 HOH 50  750 136 HOH HOH A . 
I 5 HOH 51  751 14  HOH HOH A . 
I 5 HOH 52  752 44  HOH HOH A . 
I 5 HOH 53  753 141 HOH HOH A . 
I 5 HOH 54  754 78  HOH HOH A . 
I 5 HOH 55  755 275 HOH HOH A . 
I 5 HOH 56  756 39  HOH HOH A . 
I 5 HOH 57  757 26  HOH HOH A . 
I 5 HOH 58  758 139 HOH HOH A . 
I 5 HOH 59  759 19  HOH HOH A . 
I 5 HOH 60  760 49  HOH HOH A . 
I 5 HOH 61  761 37  HOH HOH A . 
I 5 HOH 62  762 341 HOH HOH A . 
I 5 HOH 63  763 43  HOH HOH A . 
I 5 HOH 64  764 68  HOH HOH A . 
I 5 HOH 65  765 270 HOH HOH A . 
I 5 HOH 66  766 237 HOH HOH A . 
I 5 HOH 67  767 331 HOH HOH A . 
I 5 HOH 68  768 111 HOH HOH A . 
I 5 HOH 69  769 156 HOH HOH A . 
I 5 HOH 70  770 144 HOH HOH A . 
I 5 HOH 71  771 176 HOH HOH A . 
I 5 HOH 72  772 116 HOH HOH A . 
I 5 HOH 73  773 328 HOH HOH A . 
I 5 HOH 74  774 265 HOH HOH A . 
I 5 HOH 75  775 138 HOH HOH A . 
I 5 HOH 76  776 107 HOH HOH A . 
I 5 HOH 77  777 224 HOH HOH A . 
I 5 HOH 78  778 112 HOH HOH A . 
I 5 HOH 79  779 35  HOH HOH A . 
I 5 HOH 80  780 168 HOH HOH A . 
I 5 HOH 81  781 27  HOH HOH A . 
I 5 HOH 82  782 197 HOH HOH A . 
I 5 HOH 83  783 122 HOH HOH A . 
I 5 HOH 84  784 231 HOH HOH A . 
I 5 HOH 85  785 232 HOH HOH A . 
I 5 HOH 86  786 260 HOH HOH A . 
I 5 HOH 87  787 185 HOH HOH A . 
I 5 HOH 88  788 121 HOH HOH A . 
I 5 HOH 89  789 311 HOH HOH A . 
I 5 HOH 90  790 285 HOH HOH A . 
I 5 HOH 91  791 241 HOH HOH A . 
I 5 HOH 92  792 199 HOH HOH A . 
I 5 HOH 93  793 73  HOH HOH A . 
I 5 HOH 94  794 315 HOH HOH A . 
I 5 HOH 95  795 102 HOH HOH A . 
I 5 HOH 96  796 358 HOH HOH A . 
I 5 HOH 97  797 261 HOH HOH A . 
I 5 HOH 98  798 235 HOH HOH A . 
I 5 HOH 99  799 272 HOH HOH A . 
I 5 HOH 100 800 133 HOH HOH A . 
I 5 HOH 101 801 370 HOH HOH A . 
I 5 HOH 102 802 352 HOH HOH A . 
I 5 HOH 103 803 135 HOH HOH A . 
I 5 HOH 104 804 127 HOH HOH A . 
I 5 HOH 105 805 50  HOH HOH A . 
I 5 HOH 106 806 309 HOH HOH A . 
I 5 HOH 107 807 246 HOH HOH A . 
I 5 HOH 108 808 268 HOH HOH A . 
I 5 HOH 109 809 79  HOH HOH A . 
I 5 HOH 110 810 69  HOH HOH A . 
I 5 HOH 111 811 55  HOH HOH A . 
I 5 HOH 112 812 178 HOH HOH A . 
I 5 HOH 113 813 292 HOH HOH A . 
I 5 HOH 114 814 305 HOH HOH A . 
I 5 HOH 115 815 324 HOH HOH A . 
I 5 HOH 116 816 338 HOH HOH A . 
I 5 HOH 117 817 123 HOH HOH A . 
I 5 HOH 118 818 353 HOH HOH A . 
I 5 HOH 119 819 137 HOH HOH A . 
I 5 HOH 120 820 304 HOH HOH A . 
I 5 HOH 121 821 188 HOH HOH A . 
I 5 HOH 122 822 252 HOH HOH A . 
I 5 HOH 123 823 180 HOH HOH A . 
I 5 HOH 124 824 326 HOH HOH A . 
I 5 HOH 125 825 277 HOH HOH A . 
I 5 HOH 126 826 263 HOH HOH A . 
I 5 HOH 127 827 247 HOH HOH A . 
I 5 HOH 128 828 147 HOH HOH A . 
I 5 HOH 129 829 355 HOH HOH A . 
I 5 HOH 130 830 290 HOH HOH A . 
I 5 HOH 131 831 157 HOH HOH A . 
I 5 HOH 132 832 82  HOH HOH A . 
I 5 HOH 133 833 333 HOH HOH A . 
I 5 HOH 134 834 236 HOH HOH A . 
I 5 HOH 135 835 316 HOH HOH A . 
I 5 HOH 136 836 330 HOH HOH A . 
I 5 HOH 137 837 323 HOH HOH A . 
I 5 HOH 138 838 314 HOH HOH A . 
I 5 HOH 139 839 259 HOH HOH A . 
I 5 HOH 140 840 296 HOH HOH A . 
I 5 HOH 141 841 170 HOH HOH A . 
I 5 HOH 142 842 266 HOH HOH A . 
I 5 HOH 143 843 211 HOH HOH A . 
I 5 HOH 144 844 85  HOH HOH A . 
I 5 HOH 145 845 225 HOH HOH A . 
I 5 HOH 146 846 193 HOH HOH A . 
I 5 HOH 147 847 145 HOH HOH A . 
I 5 HOH 148 848 339 HOH HOH A . 
I 5 HOH 149 849 322 HOH HOH A . 
I 5 HOH 150 850 230 HOH HOH A . 
I 5 HOH 151 851 337 HOH HOH A . 
I 5 HOH 152 852 220 HOH HOH A . 
I 5 HOH 153 853 209 HOH HOH A . 
I 5 HOH 154 854 327 HOH HOH A . 
I 5 HOH 155 855 365 HOH HOH A . 
I 5 HOH 156 856 357 HOH HOH A . 
I 5 HOH 157 857 200 HOH HOH A . 
I 5 HOH 158 858 98  HOH HOH A . 
I 5 HOH 159 859 374 HOH HOH A . 
I 5 HOH 160 860 369 HOH HOH A . 
I 5 HOH 161 861 226 HOH HOH A . 
I 5 HOH 162 862 297 HOH HOH A . 
I 5 HOH 163 863 372 HOH HOH A . 
I 5 HOH 164 864 189 HOH HOH A . 
I 5 HOH 165 865 354 HOH HOH A . 
J 5 HOH 1   701 203 HOH HOH B . 
J 5 HOH 2   702 184 HOH HOH B . 
J 5 HOH 3   703 218 HOH HOH B . 
J 5 HOH 4   704 119 HOH HOH B . 
J 5 HOH 5   705 240 HOH HOH B . 
J 5 HOH 6   706 215 HOH HOH B . 
J 5 HOH 7   707 92  HOH HOH B . 
J 5 HOH 8   708 95  HOH HOH B . 
J 5 HOH 9   709 4   HOH HOH B . 
J 5 HOH 10  710 3   HOH HOH B . 
J 5 HOH 11  711 87  HOH HOH B . 
J 5 HOH 12  712 24  HOH HOH B . 
J 5 HOH 13  713 36  HOH HOH B . 
J 5 HOH 14  714 340 HOH HOH B . 
J 5 HOH 15  715 310 HOH HOH B . 
J 5 HOH 16  716 312 HOH HOH B . 
J 5 HOH 17  717 72  HOH HOH B . 
J 5 HOH 18  718 182 HOH HOH B . 
J 5 HOH 19  719 204 HOH HOH B . 
J 5 HOH 20  720 238 HOH HOH B . 
J 5 HOH 21  721 56  HOH HOH B . 
J 5 HOH 22  722 264 HOH HOH B . 
J 5 HOH 23  723 153 HOH HOH B . 
J 5 HOH 24  724 187 HOH HOH B . 
J 5 HOH 25  725 132 HOH HOH B . 
J 5 HOH 26  726 71  HOH HOH B . 
J 5 HOH 27  727 9   HOH HOH B . 
J 5 HOH 28  728 175 HOH HOH B . 
J 5 HOH 29  729 242 HOH HOH B . 
J 5 HOH 30  730 91  HOH HOH B . 
J 5 HOH 31  731 183 HOH HOH B . 
J 5 HOH 32  732 80  HOH HOH B . 
J 5 HOH 33  733 8   HOH HOH B . 
J 5 HOH 34  734 81  HOH HOH B . 
J 5 HOH 35  735 348 HOH HOH B . 
J 5 HOH 36  736 307 HOH HOH B . 
J 5 HOH 37  737 84  HOH HOH B . 
J 5 HOH 38  738 191 HOH HOH B . 
J 5 HOH 39  739 186 HOH HOH B . 
J 5 HOH 40  740 12  HOH HOH B . 
J 5 HOH 41  741 163 HOH HOH B . 
J 5 HOH 42  742 31  HOH HOH B . 
J 5 HOH 43  743 52  HOH HOH B . 
J 5 HOH 44  744 25  HOH HOH B . 
J 5 HOH 45  745 62  HOH HOH B . 
J 5 HOH 46  746 160 HOH HOH B . 
J 5 HOH 47  747 23  HOH HOH B . 
J 5 HOH 48  748 21  HOH HOH B . 
J 5 HOH 49  749 41  HOH HOH B . 
J 5 HOH 50  750 17  HOH HOH B . 
J 5 HOH 51  751 117 HOH HOH B . 
J 5 HOH 52  752 54  HOH HOH B . 
J 5 HOH 53  753 227 HOH HOH B . 
J 5 HOH 54  754 13  HOH HOH B . 
J 5 HOH 55  755 86  HOH HOH B . 
J 5 HOH 56  756 276 HOH HOH B . 
J 5 HOH 57  757 152 HOH HOH B . 
J 5 HOH 58  758 58  HOH HOH B . 
J 5 HOH 59  759 167 HOH HOH B . 
J 5 HOH 60  760 83  HOH HOH B . 
J 5 HOH 61  761 20  HOH HOH B . 
J 5 HOH 62  762 118 HOH HOH B . 
J 5 HOH 63  763 216 HOH HOH B . 
J 5 HOH 64  764 60  HOH HOH B . 
J 5 HOH 65  765 174 HOH HOH B . 
J 5 HOH 66  766 38  HOH HOH B . 
J 5 HOH 67  767 171 HOH HOH B . 
J 5 HOH 68  768 190 HOH HOH B . 
J 5 HOH 69  769 319 HOH HOH B . 
J 5 HOH 70  770 67  HOH HOH B . 
J 5 HOH 71  771 223 HOH HOH B . 
J 5 HOH 72  772 142 HOH HOH B . 
J 5 HOH 73  773 30  HOH HOH B . 
J 5 HOH 74  774 289 HOH HOH B . 
J 5 HOH 75  775 155 HOH HOH B . 
J 5 HOH 76  776 254 HOH HOH B . 
J 5 HOH 77  777 99  HOH HOH B . 
J 5 HOH 78  778 267 HOH HOH B . 
J 5 HOH 79  779 214 HOH HOH B . 
J 5 HOH 80  780 93  HOH HOH B . 
J 5 HOH 81  781 320 HOH HOH B . 
J 5 HOH 82  782 366 HOH HOH B . 
J 5 HOH 83  783 66  HOH HOH B . 
J 5 HOH 84  784 321 HOH HOH B . 
J 5 HOH 85  785 332 HOH HOH B . 
J 5 HOH 86  786 100 HOH HOH B . 
J 5 HOH 87  787 278 HOH HOH B . 
J 5 HOH 88  788 103 HOH HOH B . 
J 5 HOH 89  789 94  HOH HOH B . 
J 5 HOH 90  790 221 HOH HOH B . 
J 5 HOH 91  791 299 HOH HOH B . 
J 5 HOH 92  792 88  HOH HOH B . 
J 5 HOH 93  793 287 HOH HOH B . 
J 5 HOH 94  794 363 HOH HOH B . 
J 5 HOH 95  795 306 HOH HOH B . 
J 5 HOH 96  796 129 HOH HOH B . 
J 5 HOH 97  797 280 HOH HOH B . 
J 5 HOH 98  798 70  HOH HOH B . 
J 5 HOH 99  799 217 HOH HOH B . 
J 5 HOH 100 800 164 HOH HOH B . 
J 5 HOH 101 801 335 HOH HOH B . 
J 5 HOH 102 802 165 HOH HOH B . 
J 5 HOH 103 803 177 HOH HOH B . 
J 5 HOH 104 804 318 HOH HOH B . 
J 5 HOH 105 805 255 HOH HOH B . 
J 5 HOH 106 806 344 HOH HOH B . 
J 5 HOH 107 807 262 HOH HOH B . 
J 5 HOH 108 808 96  HOH HOH B . 
J 5 HOH 109 809 308 HOH HOH B . 
J 5 HOH 110 810 114 HOH HOH B . 
J 5 HOH 111 811 113 HOH HOH B . 
J 5 HOH 112 812 245 HOH HOH B . 
J 5 HOH 113 813 346 HOH HOH B . 
J 5 HOH 114 814 77  HOH HOH B . 
J 5 HOH 115 815 34  HOH HOH B . 
J 5 HOH 116 816 202 HOH HOH B . 
J 5 HOH 117 817 243 HOH HOH B . 
J 5 HOH 118 818 284 HOH HOH B . 
J 5 HOH 119 819 149 HOH HOH B . 
J 5 HOH 120 820 274 HOH HOH B . 
J 5 HOH 121 821 134 HOH HOH B . 
J 5 HOH 122 822 207 HOH HOH B . 
J 5 HOH 123 823 294 HOH HOH B . 
J 5 HOH 124 824 229 HOH HOH B . 
J 5 HOH 125 825 367 HOH HOH B . 
J 5 HOH 126 826 125 HOH HOH B . 
J 5 HOH 127 827 195 HOH HOH B . 
J 5 HOH 128 828 124 HOH HOH B . 
J 5 HOH 129 829 201 HOH HOH B . 
J 5 HOH 130 830 345 HOH HOH B . 
J 5 HOH 131 831 356 HOH HOH B . 
J 5 HOH 132 832 359 HOH HOH B . 
J 5 HOH 133 833 295 HOH HOH B . 
J 5 HOH 134 834 181 HOH HOH B . 
J 5 HOH 135 835 373 HOH HOH B . 
J 5 HOH 136 836 210 HOH HOH B . 
J 5 HOH 137 837 158 HOH HOH B . 
J 5 HOH 138 838 368 HOH HOH B . 
J 5 HOH 139 839 249 HOH HOH B . 
J 5 HOH 140 840 250 HOH HOH B . 
J 5 HOH 141 841 169 HOH HOH B . 
J 5 HOH 142 842 334 HOH HOH B . 
J 5 HOH 143 843 302 HOH HOH B . 
J 5 HOH 144 844 269 HOH HOH B . 
J 5 HOH 145 845 349 HOH HOH B . 
J 5 HOH 146 846 293 HOH HOH B . 
J 5 HOH 147 847 196 HOH HOH B . 
J 5 HOH 148 848 273 HOH HOH B . 
J 5 HOH 149 849 283 HOH HOH B . 
J 5 HOH 150 850 257 HOH HOH B . 
J 5 HOH 151 851 281 HOH HOH B . 
J 5 HOH 152 852 228 HOH HOH B . 
J 5 HOH 153 853 325 HOH HOH B . 
J 5 HOH 154 854 271 HOH HOH B . 
J 5 HOH 155 855 360 HOH HOH B . 
J 5 HOH 156 856 361 HOH HOH B . 
J 5 HOH 157 857 371 HOH HOH B . 
J 5 HOH 158 858 198 HOH HOH B . 
J 5 HOH 159 859 166 HOH HOH B . 
J 5 HOH 160 860 291 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.17.1-3660 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_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                     8X3Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     96.383 
_cell.length_a_esd                 ? 
_cell.length_b                     108.873 
_cell.length_b_esd                 ? 
_cell.length_c                     110.757 
_cell.length_c_esd                 ? 
_cell.volume                       1162229.284 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8X3Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (z,x,y)' 
_symmetry.space_group_name_H-M             'P 2 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                   8X3Y 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.18 
_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    '15% polyethylene glycol 1500 and 0.1 M bicine, pH 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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         2022-09-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_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                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             1.00 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8X3Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               72.17 
_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                                     63888 
_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                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.086 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.15 
_reflns_shell.d_res_low                                     2.20 
_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                             4455 
_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                               0.499 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8X3Y 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.15 
_refine.ls_d_res_low                             44.19 
_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                     63888 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1846 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1561 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AlphaFold 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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                       2.15 
_refine_hist.d_res_low                        44.19 
_refine_hist.number_atoms_solvent             325 
_refine_hist.number_atoms_total               8371 
_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        7938 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         108 
_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' ? 0.0119  ? 8224  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0997  ? 11198 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0797  ? 1282  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0068  ? 1434  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 22.6773 ? 2966  ? f_dihedral_angle_d ? ? 
# 
_struct.entry_id                     8X3Y 
_struct.title                        'ThDP-dependent HKA synthase' 
_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        8X3Y 
_struct_keywords.text            'ThDP-dependent HKA synthase, BIOSYNTHETIC PROTEIN' 
_struct_keywords.pdbx_keywords   'BIOSYNTHETIC PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8X3Y 
_struct_ref.pdbx_db_accession          8X3Y 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8X3Y A 1 ? 584 ? 8X3Y -3 ? 580 ? -3 580 
2 1 8X3Y B 1 ? 584 ? 8X3Y -3 ? 580 ? -3 580 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10080 ? 
1 MORE         -104  ? 
1 'SSA (A^2)'  33700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   '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 ALA A 9   ? GLU A 20  ? ALA A 5   GLU A 16  1 ? 12 
HELX_P HELX_P2  AA2 LEU A 33  ? LYS A 44  ? LEU A 29  LYS A 40  1 ? 12 
HELX_P HELX_P3  AA3 HIS A 53  ? GLY A 69  ? HIS A 49  GLY A 65  1 ? 17 
HELX_P HELX_P4  AA4 GLY A 79  ? SER A 96  ? GLY A 75  SER A 92  1 ? 18 
HELX_P HELX_P5  AA5 GLY A 107 ? PHE A 111 ? GLY A 103 PHE A 107 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 125 ? SER A 131 ? ASP A 121 SER A 127 1 ? 7  
HELX_P HELX_P7  AA7 PRO A 132 ? THR A 134 ? PRO A 128 THR A 130 5 ? 3  
HELX_P HELX_P8  AA8 THR A 142 ? GLU A 144 ? THR A 138 GLU A 140 5 ? 3  
HELX_P HELX_P9  AA9 LYS A 145 ? SER A 159 ? LYS A 141 SER A 155 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 172 ? LYS A 175 ? ASP A 168 LYS A 171 5 ? 4  
HELX_P HELX_P11 AB2 PRO A 184 ? ARG A 189 ? PRO A 180 ARG A 185 1 ? 6  
HELX_P HELX_P12 AB3 THR A 196 ? ALA A 210 ? THR A 192 ALA A 206 1 ? 15 
HELX_P HELX_P13 AB4 HIS A 219 ? ALA A 224 ? HIS A 215 ALA A 220 1 ? 6  
HELX_P HELX_P14 AB5 ALA A 226 ? GLY A 238 ? ALA A 222 GLY A 234 1 ? 13 
HELX_P HELX_P15 AB6 HIS A 267 ? SER A 276 ? HIS A 263 SER A 272 1 ? 10 
HELX_P HELX_P16 AB7 ASP A 298 ? THR A 302 ? ASP A 294 THR A 298 5 ? 5  
HELX_P HELX_P17 AB8 ASP A 313 ? ILE A 317 ? ASP A 309 ILE A 313 5 ? 5  
HELX_P HELX_P18 AB9 ASP A 330 ? GLY A 346 ? ASP A 326 GLY A 342 1 ? 17 
HELX_P HELX_P19 AC1 HIS A 377 ? ASN A 387 ? HIS A 373 ASN A 383 1 ? 11 
HELX_P HELX_P20 AC2 GLY A 400 ? TYR A 410 ? GLY A 396 TYR A 406 1 ? 11 
HELX_P HELX_P21 AC3 GLY A 428 ? ALA A 441 ? GLY A 424 ALA A 437 1 ? 14 
HELX_P HELX_P22 AC4 ASP A 452 ? GLY A 459 ? ASP A 448 GLY A 455 1 ? 8  
HELX_P HELX_P23 AC5 GLU A 461 ? TYR A 468 ? GLU A 457 TYR A 464 1 ? 8  
HELX_P HELX_P24 AC6 HIS A 482 ? PHE A 493 ? HIS A 478 PHE A 489 1 ? 12 
HELX_P HELX_P25 AC7 ASP A 507 ? LEU A 515 ? ASP A 503 LEU A 511 1 ? 9  
HELX_P HELX_P26 AC8 THR A 524 ? MET A 538 ? THR A 520 MET A 534 1 ? 15 
HELX_P HELX_P27 AC9 GLY A 556 ? ASP A 562 ? GLY A 552 ASP A 558 1 ? 7  
HELX_P HELX_P28 AD1 ALA B 9   ? GLU B 20  ? ALA B 5   GLU B 16  1 ? 12 
HELX_P HELX_P29 AD2 LEU B 33  ? LYS B 44  ? LEU B 29  LYS B 40  1 ? 12 
HELX_P HELX_P30 AD3 HIS B 53  ? GLY B 69  ? HIS B 49  GLY B 65  1 ? 17 
HELX_P HELX_P31 AD4 GLY B 79  ? ALA B 85  ? GLY B 75  ALA B 81  1 ? 7  
HELX_P HELX_P32 AD5 ALA B 85  ? SER B 96  ? ALA B 81  SER B 92  1 ? 12 
HELX_P HELX_P33 AD6 GLY B 107 ? PHE B 111 ? GLY B 103 PHE B 107 5 ? 5  
HELX_P HELX_P34 AD7 ASP B 125 ? SER B 131 ? ASP B 121 SER B 127 1 ? 7  
HELX_P HELX_P35 AD8 PRO B 132 ? THR B 134 ? PRO B 128 THR B 130 5 ? 3  
HELX_P HELX_P36 AD9 THR B 142 ? GLU B 144 ? THR B 138 GLU B 140 5 ? 3  
HELX_P HELX_P37 AE1 LYS B 145 ? SER B 159 ? LYS B 141 SER B 155 1 ? 15 
HELX_P HELX_P38 AE2 ALA B 171 ? LYS B 175 ? ALA B 167 LYS B 171 1 ? 5  
HELX_P HELX_P39 AE3 PRO B 184 ? ARG B 189 ? PRO B 180 ARG B 185 1 ? 6  
HELX_P HELX_P40 AE4 THR B 196 ? ALA B 210 ? THR B 192 ALA B 206 1 ? 15 
HELX_P HELX_P41 AE5 HIS B 219 ? ALA B 224 ? HIS B 215 ALA B 220 1 ? 6  
HELX_P HELX_P42 AE6 ALA B 226 ? GLY B 238 ? ALA B 222 GLY B 234 1 ? 13 
HELX_P HELX_P43 AE7 HIS B 267 ? SER B 276 ? HIS B 263 SER B 272 1 ? 10 
HELX_P HELX_P44 AE8 ASP B 291 ? ASN B 295 ? ASP B 287 ASN B 291 5 ? 5  
HELX_P HELX_P45 AE9 ASP B 298 ? THR B 302 ? ASP B 294 THR B 298 5 ? 5  
HELX_P HELX_P46 AF1 ASP B 313 ? ILE B 317 ? ASP B 309 ILE B 313 5 ? 5  
HELX_P HELX_P47 AF2 ASP B 330 ? GLY B 346 ? ASP B 326 GLY B 342 1 ? 17 
HELX_P HELX_P48 AF3 HIS B 377 ? LEU B 389 ? HIS B 373 LEU B 385 1 ? 13 
HELX_P HELX_P49 AF4 GLY B 400 ? TYR B 410 ? GLY B 396 TYR B 406 1 ? 11 
HELX_P HELX_P50 AF5 GLY B 428 ? ALA B 441 ? GLY B 424 ALA B 437 1 ? 14 
HELX_P HELX_P51 AF6 ASP B 452 ? GLY B 459 ? ASP B 448 GLY B 455 1 ? 8  
HELX_P HELX_P52 AF7 GLU B 461 ? LYS B 469 ? GLU B 457 LYS B 465 1 ? 9  
HELX_P HELX_P53 AF8 HIS B 482 ? PHE B 493 ? HIS B 478 PHE B 489 1 ? 12 
HELX_P HELX_P54 AF9 ASP B 507 ? LEU B 515 ? ASP B 503 LEU B 511 1 ? 9  
HELX_P HELX_P55 AG1 THR B 524 ? MET B 538 ? THR B 520 MET B 534 1 ? 15 
HELX_P HELX_P56 AG2 GLY B 556 ? ASP B 562 ? GLY B 552 ASP B 558 1 ? 7  
# 
_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 ASP 452 OD1 ? ? ? 1_555 E MG . MG ? ? A ASP 448 A MG 603 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc2  metalc ? ? A ASN 479 OD1 ? ? ? 1_555 E MG . MG ? ? A ASN 475 A MG 603 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc3  metalc ? ? A GLY 481 O   ? ? ? 1_555 E MG . MG ? ? A GLY 477 A MG 603 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc4  metalc ? ? D TPP .   O1A ? ? ? 1_555 E MG . MG ? ? A TPP 602 A MG 603 1_555 ? ? ? ? ? ? ? 1.931 ? ? 
metalc5  metalc ? ? D TPP .   O1B ? ? ? 1_555 E MG . MG ? ? A TPP 602 A MG 603 1_555 ? ? ? ? ? ? ? 2.139 ? ? 
metalc6  metalc ? ? B ASP 452 OD1 ? ? ? 1_555 H MG . MG ? ? B ASP 448 B MG 603 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
metalc7  metalc ? ? B ASN 479 OD1 ? ? ? 1_555 H MG . MG ? ? B ASN 475 B MG 603 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc8  metalc ? ? B GLY 481 O   ? ? ? 1_555 H MG . MG ? ? B GLY 477 B MG 603 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc9  metalc ? ? G TPP .   O1A ? ? ? 1_555 H MG . MG ? ? B TPP 602 B MG 603 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
metalc10 metalc ? ? G TPP .   O1B ? ? ? 1_555 H MG . MG ? ? B TPP 602 B MG 603 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
# 
_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  OD1 ? A ASP 452 ? A ASP 448 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 OD1 ? A ASN 479 ? A ASN 475 ? 1_555 79.4  ? 
2  OD1 ? A ASP 452 ? A ASP 448 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O   ? A GLY 481 ? A GLY 477 ? 1_555 93.8  ? 
3  OD1 ? A ASN 479 ? A ASN 475 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O   ? A GLY 481 ? A GLY 477 ? 1_555 85.3  ? 
4  OD1 ? A ASP 452 ? A ASP 448 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1A ? D TPP .   ? A TPP 602 ? 1_555 85.1  ? 
5  OD1 ? A ASN 479 ? A ASN 475 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1A ? D TPP .   ? A TPP 602 ? 1_555 164.5 ? 
6  O   ? A GLY 481 ? A GLY 477 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1A ? D TPP .   ? A TPP 602 ? 1_555 96.0  ? 
7  OD1 ? A ASP 452 ? A ASP 448 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1B ? D TPP .   ? A TPP 602 ? 1_555 165.3 ? 
8  OD1 ? A ASN 479 ? A ASN 475 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1B ? D TPP .   ? A TPP 602 ? 1_555 96.2  ? 
9  O   ? A GLY 481 ? A GLY 477 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1B ? D TPP .   ? A TPP 602 ? 1_555 99.8  ? 
10 O1A ? D TPP .   ? A TPP 602 ? 1_555 MG ? E MG . ? A MG 603 ? 1_555 O1B ? D TPP .   ? A TPP 602 ? 1_555 98.8  ? 
11 OD1 ? B ASP 452 ? B ASP 448 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 OD1 ? B ASN 479 ? B ASN 475 ? 1_555 83.8  ? 
12 OD1 ? B ASP 452 ? B ASP 448 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O   ? B GLY 481 ? B GLY 477 ? 1_555 101.6 ? 
13 OD1 ? B ASN 479 ? B ASN 475 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O   ? B GLY 481 ? B GLY 477 ? 1_555 88.4  ? 
14 OD1 ? B ASP 452 ? B ASP 448 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1A ? G TPP .   ? B TPP 602 ? 1_555 84.2  ? 
15 OD1 ? B ASN 479 ? B ASN 475 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1A ? G TPP .   ? B TPP 602 ? 1_555 168.0 ? 
16 O   ? B GLY 481 ? B GLY 477 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1A ? G TPP .   ? B TPP 602 ? 1_555 93.0  ? 
17 OD1 ? B ASP 452 ? B ASP 448 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1B ? G TPP .   ? B TPP 602 ? 1_555 160.6 ? 
18 OD1 ? B ASN 479 ? B ASN 475 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1B ? G TPP .   ? B TPP 602 ? 1_555 94.9  ? 
19 O   ? B GLY 481 ? B GLY 477 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1B ? G TPP .   ? B TPP 602 ? 1_555 97.7  ? 
20 O1A ? G TPP .   ? B TPP 602 ? 1_555 MG ? H MG . ? B MG 603 ? 1_555 O1B ? G TPP .   ? B TPP 602 ? 1_555 96.8  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 6 ? 
AA7 ? 6 ? 
AA8 ? 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 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 6   ? THR A 8   ? THR A 2   THR A 4   
AA1 2 PRO A 177 ? PRO A 179 ? PRO A 173 PRO A 175 
AA2 1 GLN A 47  ? LEU A 50  ? GLN A 43  LEU A 46  
AA2 2 TYR A 24  ? GLY A 27  ? TYR A 20  GLY A 23  
AA2 3 GLY A 72  ? ALA A 76  ? GLY A 68  ALA A 72  
AA2 4 VAL A 99  ? GLN A 105 ? VAL A 95  GLN A 101 
AA2 5 ILE A 165 ? PRO A 170 ? ILE A 161 PRO A 166 
AA2 6 LEU A 136 ? MET A 139 ? LEU A 132 MET A 135 
AA3 1 SER A 258 ? VAL A 261 ? SER A 254 VAL A 257 
AA3 2 VAL A 241 ? THR A 243 ? VAL A 237 THR A 239 
AA3 3 ALA A 214 ? ALA A 217 ? ALA A 210 ALA A 213 
AA3 4 VAL A 281 ? ILE A 285 ? VAL A 277 ILE A 281 
AA3 5 ALA A 306 ? ASP A 311 ? ALA A 302 ASP A 307 
AA3 6 VAL A 325 ? ASN A 328 ? VAL A 321 ASN A 324 
AA4 1 PHE A 418 ? ILE A 420 ? PHE A 414 ILE A 416 
AA4 2 ILE A 394 ? VAL A 397 ? ILE A 390 VAL A 393 
AA4 3 VAL A 446 ? GLY A 451 ? VAL A 442 GLY A 447 
AA4 4 THR A 473 ? ASN A 478 ? THR A 469 ASN A 474 
AA4 5 CYS A 542 ? GLN A 547 ? CYS A 538 GLN A 543 
AA4 6 LYS A 518 ? ALA A 522 ? LYS A 514 ALA A 518 
AA5 1 THR B 6   ? THR B 8   ? THR B 2   THR B 4   
AA5 2 PRO B 177 ? PRO B 179 ? PRO B 173 PRO B 175 
AA6 1 GLN B 47  ? LEU B 50  ? GLN B 43  LEU B 46  
AA6 2 TYR B 24  ? GLY B 27  ? TYR B 20  GLY B 23  
AA6 3 GLY B 72  ? ALA B 76  ? GLY B 68  ALA B 72  
AA6 4 VAL B 99  ? GLN B 105 ? VAL B 95  GLN B 101 
AA6 5 ILE B 165 ? PRO B 170 ? ILE B 161 PRO B 166 
AA6 6 LEU B 136 ? MET B 139 ? LEU B 132 MET B 135 
AA7 1 SER B 258 ? VAL B 261 ? SER B 254 VAL B 257 
AA7 2 VAL B 241 ? THR B 243 ? VAL B 237 THR B 239 
AA7 3 ALA B 214 ? ALA B 217 ? ALA B 210 ALA B 213 
AA7 4 VAL B 281 ? ILE B 285 ? VAL B 277 ILE B 281 
AA7 5 ALA B 306 ? ASP B 311 ? ALA B 302 ASP B 307 
AA7 6 VAL B 325 ? ASN B 328 ? VAL B 321 ASN B 324 
AA8 1 PHE B 418 ? ILE B 420 ? PHE B 414 ILE B 416 
AA8 2 ILE B 394 ? VAL B 397 ? ILE B 390 VAL B 393 
AA8 3 VAL B 446 ? GLY B 451 ? VAL B 442 GLY B 447 
AA8 4 THR B 473 ? ASN B 478 ? THR B 469 ASN B 474 
AA8 5 CYS B 542 ? GLN B 547 ? CYS B 538 GLN B 543 
AA8 6 LYS B 518 ? ALA B 522 ? LYS B 514 ALA B 518 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 7   ? N VAL A 3   O VAL A 178 ? O VAL A 174 
AA2 1 2 O ILE A 49  ? O ILE A 45  N VAL A 25  ? N VAL A 21  
AA2 2 3 N PHE A 26  ? N PHE A 22  O CYS A 75  ? O CYS A 71  
AA2 3 4 N GLY A 72  ? N GLY A 68  O LEU A 100 ? O LEU A 96  
AA2 4 5 N LEU A 101 ? N LEU A 97  O ILE A 165 ? O ILE A 161 
AA2 5 6 O HIS A 166 ? O HIS A 162 N LEU A 136 ? N LEU A 132 
AA3 1 2 O LEU A 259 ? O LEU A 255 N VAL A 241 ? N VAL A 237 
AA3 2 3 O ALA A 242 ? O ALA A 238 N ILE A 215 ? N ILE A 211 
AA3 3 4 N LEU A 216 ? N LEU A 212 O ILE A 283 ? O ILE A 279 
AA3 4 5 N VAL A 284 ? N VAL A 280 O ILE A 308 ? O ILE A 304 
AA3 5 6 N GLN A 309 ? N GLN A 305 O ILE A 327 ? O ILE A 323 
AA4 1 2 O GLN A 419 ? O GLN A 415 N LEU A 395 ? N LEU A 391 
AA4 2 3 N PHE A 396 ? N PHE A 392 O VAL A 447 ? O VAL A 443 
AA4 3 4 N ALA A 448 ? N ALA A 444 O ILE A 475 ? O ILE A 471 
AA4 4 5 N TRP A 474 ? N TRP A 470 O ILE A 544 ? O ILE A 540 
AA4 5 6 O ASP A 545 ? O ASP A 541 N TYR A 520 ? N TYR A 516 
AA5 1 2 N VAL B 7   ? N VAL B 3   O VAL B 178 ? O VAL B 174 
AA6 1 2 O ILE B 49  ? O ILE B 45  N VAL B 25  ? N VAL B 21  
AA6 2 3 N PHE B 26  ? N PHE B 22  O CYS B 75  ? O CYS B 71  
AA6 3 4 N GLY B 72  ? N GLY B 68  O LEU B 100 ? O LEU B 96  
AA6 4 5 N LEU B 101 ? N LEU B 97  O ILE B 165 ? O ILE B 161 
AA6 5 6 O HIS B 166 ? O HIS B 162 N LEU B 136 ? N LEU B 132 
AA7 1 2 O LEU B 259 ? O LEU B 255 N VAL B 241 ? N VAL B 237 
AA7 2 3 O ALA B 242 ? O ALA B 238 N ILE B 215 ? N ILE B 211 
AA7 3 4 N ALA B 214 ? N ALA B 210 O ILE B 283 ? O ILE B 279 
AA7 4 5 N VAL B 284 ? N VAL B 280 O ILE B 308 ? O ILE B 304 
AA7 5 6 N GLN B 309 ? N GLN B 305 O ILE B 327 ? O ILE B 323 
AA8 1 2 O GLN B 419 ? O GLN B 415 N LEU B 395 ? N LEU B 391 
AA8 2 3 N PHE B 396 ? N PHE B 392 O VAL B 447 ? O VAL B 443 
AA8 3 4 N ALA B 448 ? N ALA B 444 O ILE B 475 ? O ILE B 471 
AA8 4 5 N TRP B 474 ? N TRP B 470 O ILE B 544 ? O ILE B 540 
AA8 5 6 O ASP B 545 ? O ASP B 541 N ALA B 522 ? N ALA B 518 
# 
_pdbx_entry_details.entry_id                   8X3Y 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 41  ? ? -131.86 -60.29 
2 1 SER A 245 ? ? 89.07   9.45   
3 1 ALA A 261 ? ? 58.59   19.82  
4 1 ARG A 384 ? ? -133.73 -33.57 
5 1 LYS B 41  ? ? -133.51 -62.88 
6 1 SER B 245 ? ? 90.40   7.51   
7 1 VAL B 301 ? ? -120.52 -56.25 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x+1/2,y+1/2,-z 
4 -x,-y,z         
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -3  ? A MET 1   
2   1 Y 1 A GLY -2  ? A GLY 2   
3   1 Y 1 A MET 344 ? A MET 348 
4   1 Y 1 A LEU 345 ? A LEU 349 
5   1 Y 1 A LYS 346 ? A LYS 350 
6   1 Y 1 A LYS 347 ? A LYS 351 
7   1 Y 1 A PRO 348 ? A PRO 352 
8   1 Y 1 A ALA 349 ? A ALA 353 
9   1 Y 1 A LEU 350 ? A LEU 354 
10  1 Y 1 A PRO 351 ? A PRO 355 
11  1 Y 1 A LEU 352 ? A LEU 356 
12  1 Y 1 A GLU 353 ? A GLU 357 
13  1 Y 1 A THR 354 ? A THR 358 
14  1 Y 1 A LYS 355 ? A LYS 359 
15  1 Y 1 A GLU 356 ? A GLU 360 
16  1 Y 1 A GLN 357 ? A GLN 361 
17  1 Y 1 A THR 358 ? A THR 362 
18  1 Y 1 A ALA 359 ? A ALA 363 
19  1 Y 1 A PHE 360 ? A PHE 364 
20  1 Y 1 A GLN 361 ? A GLN 365 
21  1 Y 1 A GLU 362 ? A GLU 366 
22  1 Y 1 A ILE 363 ? A ILE 367 
23  1 Y 1 A ASP 364 ? A ASP 368 
24  1 Y 1 A HIS 365 ? A HIS 369 
25  1 Y 1 A GLY 366 ? A GLY 370 
26  1 Y 1 A THR 367 ? A THR 371 
27  1 Y 1 A GLU 368 ? A GLU 372 
28  1 Y 1 A GLY 369 ? A GLY 373 
29  1 Y 1 A ASN 370 ? A ASN 374 
30  1 Y 1 A MET 559 ? A MET 563 
31  1 Y 1 A LEU 560 ? A LEU 564 
32  1 Y 1 A ASN 561 ? A ASN 565 
33  1 Y 1 A LYS 562 ? A LYS 566 
34  1 Y 1 A SER 563 ? A SER 567 
35  1 Y 1 A TYR 564 ? A TYR 568 
36  1 Y 1 A ALA 565 ? A ALA 569 
37  1 Y 1 A GLY 566 ? A GLY 570 
38  1 Y 1 A GLU 567 ? A GLU 571 
39  1 Y 1 A ARG 568 ? A ARG 572 
40  1 Y 1 A TYR 569 ? A TYR 573 
41  1 Y 1 A THR 570 ? A THR 574 
42  1 Y 1 A ALA 571 ? A ALA 575 
43  1 Y 1 A PRO 572 ? A PRO 576 
44  1 Y 1 A ILE 573 ? A ILE 577 
45  1 Y 1 A GLY 574 ? A GLY 578 
46  1 Y 1 A HIS 575 ? A HIS 579 
47  1 Y 1 A HIS 576 ? A HIS 580 
48  1 Y 1 A HIS 577 ? A HIS 581 
49  1 Y 1 A HIS 578 ? A HIS 582 
50  1 Y 1 A HIS 579 ? A HIS 583 
51  1 Y 1 A HIS 580 ? A HIS 584 
52  1 Y 1 B MET -3  ? B MET 1   
53  1 Y 1 B GLY -2  ? B GLY 2   
54  1 Y 1 B MET 344 ? B MET 348 
55  1 Y 1 B LEU 345 ? B LEU 349 
56  1 Y 1 B LYS 346 ? B LYS 350 
57  1 Y 1 B LYS 347 ? B LYS 351 
58  1 Y 1 B PRO 348 ? B PRO 352 
59  1 Y 1 B ALA 349 ? B ALA 353 
60  1 Y 1 B LEU 350 ? B LEU 354 
61  1 Y 1 B PRO 351 ? B PRO 355 
62  1 Y 1 B LEU 352 ? B LEU 356 
63  1 Y 1 B GLU 353 ? B GLU 357 
64  1 Y 1 B THR 354 ? B THR 358 
65  1 Y 1 B LYS 355 ? B LYS 359 
66  1 Y 1 B GLU 356 ? B GLU 360 
67  1 Y 1 B GLN 357 ? B GLN 361 
68  1 Y 1 B THR 358 ? B THR 362 
69  1 Y 1 B ALA 359 ? B ALA 363 
70  1 Y 1 B PHE 360 ? B PHE 364 
71  1 Y 1 B GLN 361 ? B GLN 365 
72  1 Y 1 B GLU 362 ? B GLU 366 
73  1 Y 1 B ILE 363 ? B ILE 367 
74  1 Y 1 B ASP 364 ? B ASP 368 
75  1 Y 1 B HIS 365 ? B HIS 369 
76  1 Y 1 B GLY 366 ? B GLY 370 
77  1 Y 1 B THR 367 ? B THR 371 
78  1 Y 1 B GLU 368 ? B GLU 372 
79  1 Y 1 B GLY 369 ? B GLY 373 
80  1 Y 1 B ASN 370 ? B ASN 374 
81  1 Y 1 B MET 559 ? B MET 563 
82  1 Y 1 B LEU 560 ? B LEU 564 
83  1 Y 1 B ASN 561 ? B ASN 565 
84  1 Y 1 B LYS 562 ? B LYS 566 
85  1 Y 1 B SER 563 ? B SER 567 
86  1 Y 1 B TYR 564 ? B TYR 568 
87  1 Y 1 B ALA 565 ? B ALA 569 
88  1 Y 1 B GLY 566 ? B GLY 570 
89  1 Y 1 B GLU 567 ? B GLU 571 
90  1 Y 1 B ARG 568 ? B ARG 572 
91  1 Y 1 B TYR 569 ? B TYR 573 
92  1 Y 1 B THR 570 ? B THR 574 
93  1 Y 1 B ALA 571 ? B ALA 575 
94  1 Y 1 B PRO 572 ? B PRO 576 
95  1 Y 1 B ILE 573 ? B ILE 577 
96  1 Y 1 B GLY 574 ? B GLY 578 
97  1 Y 1 B HIS 575 ? B HIS 579 
98  1 Y 1 B HIS 576 ? B HIS 580 
99  1 Y 1 B HIS 577 ? B HIS 581 
100 1 Y 1 B HIS 578 ? B HIS 582 
101 1 Y 1 B HIS 579 ? B HIS 583 
102 1 Y 1 B HIS 580 ? B HIS 584 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CYS N      N  N N 116 
CYS CA     C  N R 117 
CYS C      C  N N 118 
CYS O      O  N N 119 
CYS CB     C  N N 120 
CYS SG     S  N N 121 
CYS OXT    O  N N 122 
CYS H      H  N N 123 
CYS H2     H  N N 124 
CYS HA     H  N N 125 
CYS HB2    H  N N 126 
CYS HB3    H  N N 127 
CYS HG     H  N N 128 
CYS HXT    H  N N 129 
GLN N      N  N N 130 
GLN CA     C  N S 131 
GLN C      C  N N 132 
GLN O      O  N N 133 
GLN CB     C  N N 134 
GLN CG     C  N N 135 
GLN CD     C  N N 136 
GLN OE1    O  N N 137 
GLN NE2    N  N N 138 
GLN OXT    O  N N 139 
GLN H      H  N N 140 
GLN H2     H  N N 141 
GLN HA     H  N N 142 
GLN HB2    H  N N 143 
GLN HB3    H  N N 144 
GLN HG2    H  N N 145 
GLN HG3    H  N N 146 
GLN HE21   H  N N 147 
GLN HE22   H  N N 148 
GLN HXT    H  N N 149 
GLU N      N  N N 150 
GLU CA     C  N S 151 
GLU C      C  N N 152 
GLU O      O  N N 153 
GLU CB     C  N N 154 
GLU CG     C  N N 155 
GLU CD     C  N N 156 
GLU OE1    O  N N 157 
GLU OE2    O  N N 158 
GLU OXT    O  N N 159 
GLU H      H  N N 160 
GLU H2     H  N N 161 
GLU HA     H  N N 162 
GLU HB2    H  N N 163 
GLU HB3    H  N N 164 
GLU HG2    H  N N 165 
GLU HG3    H  N N 166 
GLU HE2    H  N N 167 
GLU HXT    H  N N 168 
GLY N      N  N N 169 
GLY CA     C  N N 170 
GLY C      C  N N 171 
GLY O      O  N N 172 
GLY OXT    O  N N 173 
GLY H      H  N N 174 
GLY H2     H  N N 175 
GLY HA2    H  N N 176 
GLY HA3    H  N N 177 
GLY HXT    H  N N 178 
HIS N      N  N N 179 
HIS CA     C  N S 180 
HIS C      C  N N 181 
HIS O      O  N N 182 
HIS CB     C  N N 183 
HIS CG     C  Y N 184 
HIS ND1    N  Y N 185 
HIS CD2    C  Y N 186 
HIS CE1    C  Y N 187 
HIS NE2    N  Y N 188 
HIS OXT    O  N N 189 
HIS H      H  N N 190 
HIS H2     H  N N 191 
HIS HA     H  N N 192 
HIS HB2    H  N N 193 
HIS HB3    H  N N 194 
HIS HD1    H  N N 195 
HIS HD2    H  N N 196 
HIS HE1    H  N N 197 
HIS HE2    H  N N 198 
HIS HXT    H  N N 199 
HOH O      O  N N 200 
HOH H1     H  N N 201 
HOH H2     H  N N 202 
ILE N      N  N N 203 
ILE CA     C  N S 204 
ILE C      C  N N 205 
ILE O      O  N N 206 
ILE CB     C  N S 207 
ILE CG1    C  N N 208 
ILE CG2    C  N N 209 
ILE CD1    C  N N 210 
ILE OXT    O  N N 211 
ILE H      H  N N 212 
ILE H2     H  N N 213 
ILE HA     H  N N 214 
ILE HB     H  N N 215 
ILE HG12   H  N N 216 
ILE HG13   H  N N 217 
ILE HG21   H  N N 218 
ILE HG22   H  N N 219 
ILE HG23   H  N N 220 
ILE HD11   H  N N 221 
ILE HD12   H  N N 222 
ILE HD13   H  N N 223 
ILE HXT    H  N N 224 
LEU N      N  N N 225 
LEU CA     C  N S 226 
LEU C      C  N N 227 
LEU O      O  N N 228 
LEU CB     C  N N 229 
LEU CG     C  N N 230 
LEU CD1    C  N N 231 
LEU CD2    C  N N 232 
LEU OXT    O  N N 233 
LEU H      H  N N 234 
LEU H2     H  N N 235 
LEU HA     H  N N 236 
LEU HB2    H  N N 237 
LEU HB3    H  N N 238 
LEU HG     H  N N 239 
LEU HD11   H  N N 240 
LEU HD12   H  N N 241 
LEU HD13   H  N N 242 
LEU HD21   H  N N 243 
LEU HD22   H  N N 244 
LEU HD23   H  N N 245 
LEU HXT    H  N N 246 
LYS N      N  N N 247 
LYS CA     C  N S 248 
LYS C      C  N N 249 
LYS O      O  N N 250 
LYS CB     C  N N 251 
LYS CG     C  N N 252 
LYS CD     C  N N 253 
LYS CE     C  N N 254 
LYS NZ     N  N N 255 
LYS OXT    O  N N 256 
LYS H      H  N N 257 
LYS H2     H  N N 258 
LYS HA     H  N N 259 
LYS HB2    H  N N 260 
LYS HB3    H  N N 261 
LYS HG2    H  N N 262 
LYS HG3    H  N N 263 
LYS HD2    H  N N 264 
LYS HD3    H  N N 265 
LYS HE2    H  N N 266 
LYS HE3    H  N N 267 
LYS HZ1    H  N N 268 
LYS HZ2    H  N N 269 
LYS HZ3    H  N N 270 
LYS HXT    H  N N 271 
MET N      N  N N 272 
MET CA     C  N S 273 
MET C      C  N N 274 
MET O      O  N N 275 
MET CB     C  N N 276 
MET CG     C  N N 277 
MET SD     S  N N 278 
MET CE     C  N N 279 
MET OXT    O  N N 280 
MET H      H  N N 281 
MET H2     H  N N 282 
MET HA     H  N N 283 
MET HB2    H  N N 284 
MET HB3    H  N N 285 
MET HG2    H  N N 286 
MET HG3    H  N N 287 
MET HE1    H  N N 288 
MET HE2    H  N N 289 
MET HE3    H  N N 290 
MET HXT    H  N N 291 
MG  MG     MG N N 292 
PHE N      N  N N 293 
PHE CA     C  N S 294 
PHE C      C  N N 295 
PHE O      O  N N 296 
PHE CB     C  N N 297 
PHE CG     C  Y N 298 
PHE CD1    C  Y N 299 
PHE CD2    C  Y N 300 
PHE CE1    C  Y N 301 
PHE CE2    C  Y N 302 
PHE CZ     C  Y N 303 
PHE OXT    O  N N 304 
PHE H      H  N N 305 
PHE H2     H  N N 306 
PHE HA     H  N N 307 
PHE HB2    H  N N 308 
PHE HB3    H  N N 309 
PHE HD1    H  N N 310 
PHE HD2    H  N N 311 
PHE HE1    H  N N 312 
PHE HE2    H  N N 313 
PHE HZ     H  N N 314 
PHE HXT    H  N N 315 
PRO N      N  N N 316 
PRO CA     C  N S 317 
PRO C      C  N N 318 
PRO O      O  N N 319 
PRO CB     C  N N 320 
PRO CG     C  N N 321 
PRO CD     C  N N 322 
PRO OXT    O  N N 323 
PRO H      H  N N 324 
PRO HA     H  N N 325 
PRO HB2    H  N N 326 
PRO HB3    H  N N 327 
PRO HG2    H  N N 328 
PRO HG3    H  N N 329 
PRO HD2    H  N N 330 
PRO HD3    H  N N 331 
PRO HXT    H  N N 332 
SER N      N  N N 333 
SER CA     C  N S 334 
SER C      C  N N 335 
SER O      O  N N 336 
SER CB     C  N N 337 
SER OG     O  N N 338 
SER OXT    O  N N 339 
SER H      H  N N 340 
SER H2     H  N N 341 
SER HA     H  N N 342 
SER HB2    H  N N 343 
SER HB3    H  N N 344 
SER HG     H  N N 345 
SER HXT    H  N N 346 
THR N      N  N N 347 
THR CA     C  N S 348 
THR C      C  N N 349 
THR O      O  N N 350 
THR CB     C  N R 351 
THR OG1    O  N N 352 
THR CG2    C  N N 353 
THR OXT    O  N N 354 
THR H      H  N N 355 
THR H2     H  N N 356 
THR HA     H  N N 357 
THR HB     H  N N 358 
THR HG1    H  N N 359 
THR HG21   H  N N 360 
THR HG22   H  N N 361 
THR HG23   H  N N 362 
THR HXT    H  N N 363 
TPP "N1'"  N  Y N 364 
TPP "C2'"  C  Y N 365 
TPP CM2    C  N N 366 
TPP "N3'"  N  Y N 367 
TPP "C4'"  C  Y N 368 
TPP "N4'"  N  N N 369 
TPP "C5'"  C  Y N 370 
TPP "C6'"  C  Y N 371 
TPP "C7'"  C  N N 372 
TPP N3     N  Y N 373 
TPP C2     C  Y N 374 
TPP S1     S  Y N 375 
TPP C5     C  Y N 376 
TPP C4     C  Y N 377 
TPP CM4    C  N N 378 
TPP C6     C  N N 379 
TPP C7     C  N N 380 
TPP O7     O  N N 381 
TPP PA     P  N S 382 
TPP O1A    O  N N 383 
TPP O2A    O  N N 384 
TPP O3A    O  N N 385 
TPP PB     P  N N 386 
TPP O1B    O  N N 387 
TPP O2B    O  N N 388 
TPP O3B    O  N N 389 
TPP HM21   H  N N 390 
TPP HM22   H  N N 391 
TPP HM23   H  N N 392 
TPP HN41   H  N N 393 
TPP HN42   H  N N 394 
TPP "H6'"  H  N N 395 
TPP "H7'1" H  N N 396 
TPP "H7'2" H  N N 397 
TPP H2     H  N N 398 
TPP HM41   H  N N 399 
TPP HM42   H  N N 400 
TPP HM43   H  N N 401 
TPP H61    H  N N 402 
TPP H62    H  N N 403 
TPP H71    H  N N 404 
TPP H72    H  N N 405 
TPP HOA2   H  N N 406 
TPP HOB2   H  N N 407 
TPP HOB3   H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TYR N      N  N N 436 
TYR CA     C  N S 437 
TYR C      C  N N 438 
TYR O      O  N N 439 
TYR CB     C  N N 440 
TYR CG     C  Y N 441 
TYR CD1    C  Y N 442 
TYR CD2    C  Y N 443 
TYR CE1    C  Y N 444 
TYR CE2    C  Y N 445 
TYR CZ     C  Y N 446 
TYR OH     O  N N 447 
TYR OXT    O  N N 448 
TYR H      H  N N 449 
TYR H2     H  N N 450 
TYR HA     H  N N 451 
TYR HB2    H  N N 452 
TYR HB3    H  N N 453 
TYR HD1    H  N N 454 
TYR HD2    H  N N 455 
TYR HE1    H  N N 456 
TYR HE2    H  N N 457 
TYR HH     H  N N 458 
TYR HXT    H  N N 459 
VAL N      N  N N 460 
VAL CA     C  N S 461 
VAL C      C  N N 462 
VAL O      O  N N 463 
VAL CB     C  N N 464 
VAL CG1    C  N N 465 
VAL CG2    C  N N 466 
VAL OXT    O  N N 467 
VAL H      H  N N 468 
VAL H2     H  N N 469 
VAL HA     H  N N 470 
VAL HB     H  N N 471 
VAL HG11   H  N N 472 
VAL HG12   H  N N 473 
VAL HG13   H  N N 474 
VAL HG21   H  N N 475 
VAL HG22   H  N N 476 
VAL HG23   H  N N 477 
VAL HXT    H  N N 478 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
GLN N     CA     sing N N 127 
GLN N     H      sing N N 128 
GLN N     H2     sing N N 129 
GLN CA    C      sing N N 130 
GLN CA    CB     sing N N 131 
GLN CA    HA     sing N N 132 
GLN C     O      doub N N 133 
GLN C     OXT    sing N N 134 
GLN CB    CG     sing N N 135 
GLN CB    HB2    sing N N 136 
GLN CB    HB3    sing N N 137 
GLN CG    CD     sing N N 138 
GLN CG    HG2    sing N N 139 
GLN CG    HG3    sing N N 140 
GLN CD    OE1    doub N N 141 
GLN CD    NE2    sing N N 142 
GLN NE2   HE21   sing N N 143 
GLN NE2   HE22   sing N N 144 
GLN OXT   HXT    sing N N 145 
GLU N     CA     sing N N 146 
GLU N     H      sing N N 147 
GLU N     H2     sing N N 148 
GLU CA    C      sing N N 149 
GLU CA    CB     sing N N 150 
GLU CA    HA     sing N N 151 
GLU C     O      doub N N 152 
GLU C     OXT    sing N N 153 
GLU CB    CG     sing N N 154 
GLU CB    HB2    sing N N 155 
GLU CB    HB3    sing N N 156 
GLU CG    CD     sing N N 157 
GLU CG    HG2    sing N N 158 
GLU CG    HG3    sing N N 159 
GLU CD    OE1    doub N N 160 
GLU CD    OE2    sing N N 161 
GLU OE2   HE2    sing N N 162 
GLU OXT   HXT    sing N N 163 
GLY N     CA     sing N N 164 
GLY N     H      sing N N 165 
GLY N     H2     sing N N 166 
GLY CA    C      sing N N 167 
GLY CA    HA2    sing N N 168 
GLY CA    HA3    sing N N 169 
GLY C     O      doub N N 170 
GLY C     OXT    sing N N 171 
GLY OXT   HXT    sing N N 172 
HIS N     CA     sing N N 173 
HIS N     H      sing N N 174 
HIS N     H2     sing N N 175 
HIS CA    C      sing N N 176 
HIS CA    CB     sing N N 177 
HIS CA    HA     sing N N 178 
HIS C     O      doub N N 179 
HIS C     OXT    sing N N 180 
HIS CB    CG     sing N N 181 
HIS CB    HB2    sing N N 182 
HIS CB    HB3    sing N N 183 
HIS CG    ND1    sing Y N 184 
HIS CG    CD2    doub Y N 185 
HIS ND1   CE1    doub Y N 186 
HIS ND1   HD1    sing N N 187 
HIS CD2   NE2    sing Y N 188 
HIS CD2   HD2    sing N N 189 
HIS CE1   NE2    sing Y N 190 
HIS CE1   HE1    sing N N 191 
HIS NE2   HE2    sing N N 192 
HIS OXT   HXT    sing N N 193 
HOH O     H1     sing N N 194 
HOH O     H2     sing N N 195 
ILE N     CA     sing N N 196 
ILE N     H      sing N N 197 
ILE N     H2     sing N N 198 
ILE CA    C      sing N N 199 
ILE CA    CB     sing N N 200 
ILE CA    HA     sing N N 201 
ILE C     O      doub N N 202 
ILE C     OXT    sing N N 203 
ILE CB    CG1    sing N N 204 
ILE CB    CG2    sing N N 205 
ILE CB    HB     sing N N 206 
ILE CG1   CD1    sing N N 207 
ILE CG1   HG12   sing N N 208 
ILE CG1   HG13   sing N N 209 
ILE CG2   HG21   sing N N 210 
ILE CG2   HG22   sing N N 211 
ILE CG2   HG23   sing N N 212 
ILE CD1   HD11   sing N N 213 
ILE CD1   HD12   sing N N 214 
ILE CD1   HD13   sing N N 215 
ILE OXT   HXT    sing N N 216 
LEU N     CA     sing N N 217 
LEU N     H      sing N N 218 
LEU N     H2     sing N N 219 
LEU CA    C      sing N N 220 
LEU CA    CB     sing N N 221 
LEU CA    HA     sing N N 222 
LEU C     O      doub N N 223 
LEU C     OXT    sing N N 224 
LEU CB    CG     sing N N 225 
LEU CB    HB2    sing N N 226 
LEU CB    HB3    sing N N 227 
LEU CG    CD1    sing N N 228 
LEU CG    CD2    sing N N 229 
LEU CG    HG     sing N N 230 
LEU CD1   HD11   sing N N 231 
LEU CD1   HD12   sing N N 232 
LEU CD1   HD13   sing N N 233 
LEU CD2   HD21   sing N N 234 
LEU CD2   HD22   sing N N 235 
LEU CD2   HD23   sing N N 236 
LEU OXT   HXT    sing N N 237 
LYS N     CA     sing N N 238 
LYS N     H      sing N N 239 
LYS N     H2     sing N N 240 
LYS CA    C      sing N N 241 
LYS CA    CB     sing N N 242 
LYS CA    HA     sing N N 243 
LYS C     O      doub N N 244 
LYS C     OXT    sing N N 245 
LYS CB    CG     sing N N 246 
LYS CB    HB2    sing N N 247 
LYS CB    HB3    sing N N 248 
LYS CG    CD     sing N N 249 
LYS CG    HG2    sing N N 250 
LYS CG    HG3    sing N N 251 
LYS CD    CE     sing N N 252 
LYS CD    HD2    sing N N 253 
LYS CD    HD3    sing N N 254 
LYS CE    NZ     sing N N 255 
LYS CE    HE2    sing N N 256 
LYS CE    HE3    sing N N 257 
LYS NZ    HZ1    sing N N 258 
LYS NZ    HZ2    sing N N 259 
LYS NZ    HZ3    sing N N 260 
LYS OXT   HXT    sing N N 261 
MET N     CA     sing N N 262 
MET N     H      sing N N 263 
MET N     H2     sing N N 264 
MET CA    C      sing N N 265 
MET CA    CB     sing N N 266 
MET CA    HA     sing N N 267 
MET C     O      doub N N 268 
MET C     OXT    sing N N 269 
MET CB    CG     sing N N 270 
MET CB    HB2    sing N N 271 
MET CB    HB3    sing N N 272 
MET CG    SD     sing N N 273 
MET CG    HG2    sing N N 274 
MET CG    HG3    sing N N 275 
MET SD    CE     sing N N 276 
MET CE    HE1    sing N N 277 
MET CE    HE2    sing N N 278 
MET CE    HE3    sing N N 279 
MET OXT   HXT    sing N N 280 
PHE N     CA     sing N N 281 
PHE N     H      sing N N 282 
PHE N     H2     sing N N 283 
PHE CA    C      sing N N 284 
PHE CA    CB     sing N N 285 
PHE CA    HA     sing N N 286 
PHE C     O      doub N N 287 
PHE C     OXT    sing N N 288 
PHE CB    CG     sing N N 289 
PHE CB    HB2    sing N N 290 
PHE CB    HB3    sing N N 291 
PHE CG    CD1    doub Y N 292 
PHE CG    CD2    sing Y N 293 
PHE CD1   CE1    sing Y N 294 
PHE CD1   HD1    sing N N 295 
PHE CD2   CE2    doub Y N 296 
PHE CD2   HD2    sing N N 297 
PHE CE1   CZ     doub Y N 298 
PHE CE1   HE1    sing N N 299 
PHE CE2   CZ     sing Y N 300 
PHE CE2   HE2    sing N N 301 
PHE CZ    HZ     sing N N 302 
PHE OXT   HXT    sing N N 303 
PRO N     CA     sing N N 304 
PRO N     CD     sing N N 305 
PRO N     H      sing N N 306 
PRO CA    C      sing N N 307 
PRO CA    CB     sing N N 308 
PRO CA    HA     sing N N 309 
PRO C     O      doub N N 310 
PRO C     OXT    sing N N 311 
PRO CB    CG     sing N N 312 
PRO CB    HB2    sing N N 313 
PRO CB    HB3    sing N N 314 
PRO CG    CD     sing N N 315 
PRO CG    HG2    sing N N 316 
PRO CG    HG3    sing N N 317 
PRO CD    HD2    sing N N 318 
PRO CD    HD3    sing N N 319 
PRO OXT   HXT    sing N N 320 
SER N     CA     sing N N 321 
SER N     H      sing N N 322 
SER N     H2     sing N N 323 
SER CA    C      sing N N 324 
SER CA    CB     sing N N 325 
SER CA    HA     sing N N 326 
SER C     O      doub N N 327 
SER C     OXT    sing N N 328 
SER CB    OG     sing N N 329 
SER CB    HB2    sing N N 330 
SER CB    HB3    sing N N 331 
SER OG    HG     sing N N 332 
SER OXT   HXT    sing N N 333 
THR N     CA     sing N N 334 
THR N     H      sing N N 335 
THR N     H2     sing N N 336 
THR CA    C      sing N N 337 
THR CA    CB     sing N N 338 
THR CA    HA     sing N N 339 
THR C     O      doub N N 340 
THR C     OXT    sing N N 341 
THR CB    OG1    sing N N 342 
THR CB    CG2    sing N N 343 
THR CB    HB     sing N N 344 
THR OG1   HG1    sing N N 345 
THR CG2   HG21   sing N N 346 
THR CG2   HG22   sing N N 347 
THR CG2   HG23   sing N N 348 
THR OXT   HXT    sing N N 349 
TPP "N1'" "C2'"  doub Y N 350 
TPP "N1'" "C6'"  sing Y N 351 
TPP "C2'" CM2    sing N N 352 
TPP "C2'" "N3'"  sing Y N 353 
TPP CM2   HM21   sing N N 354 
TPP CM2   HM22   sing N N 355 
TPP CM2   HM23   sing N N 356 
TPP "N3'" "C4'"  doub Y N 357 
TPP "C4'" "N4'"  sing N N 358 
TPP "C4'" "C5'"  sing Y N 359 
TPP "N4'" HN41   sing N N 360 
TPP "N4'" HN42   sing N N 361 
TPP "C5'" "C6'"  doub Y N 362 
TPP "C5'" "C7'"  sing N N 363 
TPP "C6'" "H6'"  sing N N 364 
TPP "C7'" N3     sing N N 365 
TPP "C7'" "H7'1" sing N N 366 
TPP "C7'" "H7'2" sing N N 367 
TPP N3    C2     doub Y N 368 
TPP N3    C4     sing Y N 369 
TPP C2    S1     sing Y N 370 
TPP C2    H2     sing N N 371 
TPP S1    C5     sing Y N 372 
TPP C5    C4     doub Y N 373 
TPP C5    C6     sing N N 374 
TPP C4    CM4    sing N N 375 
TPP CM4   HM41   sing N N 376 
TPP CM4   HM42   sing N N 377 
TPP CM4   HM43   sing N N 378 
TPP C6    C7     sing N N 379 
TPP C6    H61    sing N N 380 
TPP C6    H62    sing N N 381 
TPP C7    O7     sing N N 382 
TPP C7    H71    sing N N 383 
TPP C7    H72    sing N N 384 
TPP O7    PA     sing N N 385 
TPP PA    O1A    doub N N 386 
TPP PA    O2A    sing N N 387 
TPP PA    O3A    sing N N 388 
TPP O2A   HOA2   sing N N 389 
TPP O3A   PB     sing N N 390 
TPP PB    O1B    doub N N 391 
TPP PB    O2B    sing N N 392 
TPP PB    O3B    sing N N 393 
TPP O2B   HOB2   sing N N 394 
TPP O3B   HOB3   sing N N 395 
TRP N     CA     sing N N 396 
TRP N     H      sing N N 397 
TRP N     H2     sing N N 398 
TRP CA    C      sing N N 399 
TRP CA    CB     sing N N 400 
TRP CA    HA     sing N N 401 
TRP C     O      doub N N 402 
TRP C     OXT    sing N N 403 
TRP CB    CG     sing N N 404 
TRP CB    HB2    sing N N 405 
TRP CB    HB3    sing N N 406 
TRP CG    CD1    doub Y N 407 
TRP CG    CD2    sing Y N 408 
TRP CD1   NE1    sing Y N 409 
TRP CD1   HD1    sing N N 410 
TRP CD2   CE2    doub Y N 411 
TRP CD2   CE3    sing Y N 412 
TRP NE1   CE2    sing Y N 413 
TRP NE1   HE1    sing N N 414 
TRP CE2   CZ2    sing Y N 415 
TRP CE3   CZ3    doub Y N 416 
TRP CE3   HE3    sing N N 417 
TRP CZ2   CH2    doub Y N 418 
TRP CZ2   HZ2    sing N N 419 
TRP CZ3   CH2    sing Y N 420 
TRP CZ3   HZ3    sing N N 421 
TRP CH2   HH2    sing N N 422 
TRP OXT   HXT    sing N N 423 
TYR N     CA     sing N N 424 
TYR N     H      sing N N 425 
TYR N     H2     sing N N 426 
TYR CA    C      sing N N 427 
TYR CA    CB     sing N N 428 
TYR CA    HA     sing N N 429 
TYR C     O      doub N N 430 
TYR C     OXT    sing N N 431 
TYR CB    CG     sing N N 432 
TYR CB    HB2    sing N N 433 
TYR CB    HB3    sing N N 434 
TYR CG    CD1    doub Y N 435 
TYR CG    CD2    sing Y N 436 
TYR CD1   CE1    sing Y N 437 
TYR CD1   HD1    sing N N 438 
TYR CD2   CE2    doub Y N 439 
TYR CD2   HD2    sing N N 440 
TYR CE1   CZ     doub Y N 441 
TYR CE1   HE1    sing N N 442 
TYR CE2   CZ     sing Y N 443 
TYR CE2   HE2    sing N N 444 
TYR CZ    OH     sing N N 445 
TYR OH    HH     sing N N 446 
TYR OXT   HXT    sing N N 447 
VAL N     CA     sing N N 448 
VAL N     H      sing N N 449 
VAL N     H2     sing N N 450 
VAL CA    C      sing N N 451 
VAL CA    CB     sing N N 452 
VAL CA    HA     sing N N 453 
VAL C     O      doub N N 454 
VAL C     OXT    sing N N 455 
VAL CB    CG1    sing N N 456 
VAL CB    CG2    sing N N 457 
VAL CB    HB     sing N N 458 
VAL CG1   HG11   sing N N 459 
VAL CG1   HG12   sing N N 460 
VAL CG1   HG13   sing N N 461 
VAL CG2   HG21   sing N N 462 
VAL CG2   HG22   sing N N 463 
VAL CG2   HG23   sing N N 464 
VAL OXT   HXT    sing N N 465 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.crystal_system   orthorhombic 
_space_group.name_H-M_alt     'P 21 21 2' 
_space_group.IT_number        18 
_space_group.name_Hall        'P 2 2ab' 
_space_group.id               1 
# 
_atom_sites.entry_id                    8X3Y 
_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]   0.010375 
_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]   0.009185 
_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]   0.009029 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
H  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N      . SER A 1 3   ? -39.58700 29.03300  24.89000  1.000 70.29264 ? -1  SER A N      1 
ATOM   2    C  CA     . SER A 1 3   ? -38.82800 28.64200  26.07200  1.000 63.33128 ? -1  SER A CA     1 
ATOM   3    C  C      . SER A 1 3   ? -39.54200 27.54500  26.87600  1.000 61.22576 ? -1  SER A C      1 
ATOM   4    O  O      . SER A 1 3   ? -39.64600 27.64500  28.09800  1.000 62.11797 ? -1  SER A O      1 
ATOM   5    C  CB     . SER A 1 3   ? -38.57800 29.86100  26.96100  1.000 62.27326 ? -1  SER A CB     1 
ATOM   6    O  OG     . SER A 1 3   ? -39.77900 30.30700  27.58200  1.000 73.75095 ? -1  SER A OG     1 
ATOM   7    N  N      . SER A 1 4   ? -40.01800 26.52100  26.17800  1.000 53.24586 ? 0   SER A N      1 
ATOM   8    C  CA     . SER A 1 4   ? -40.69500 25.42200  26.83000  1.000 52.28258 ? 0   SER A CA     1 
ATOM   9    C  C      . SER A 1 4   ? -39.75400 24.35600  27.32900  1.000 53.21954 ? 0   SER A C      1 
ATOM   10   O  O      . SER A 1 4   ? -38.59700 24.34900  27.01400  1.000 55.34874 ? 0   SER A O      1 
ATOM   11   C  CB     . SER A 1 4   ? -41.76300 24.81600  25.96300  1.000 48.23736 ? 0   SER A CB     1 
ATOM   12   O  OG     . SER A 1 4   ? -41.27200 24.64000  24.68600  1.000 63.35233 ? 0   SER A OG     1 
ATOM   13   N  N      . LYS A 1 5   ? -40.29000 23.48600  28.15200  1.000 44.52902 ? 1   LYS A N      1 
ATOM   14   C  CA     . LYS A 1 5   ? -39.56700 22.41900  28.77900  1.000 48.08734 ? 1   LYS A CA     1 
ATOM   15   C  C      . LYS A 1 5   ? -38.67000 21.60300  27.84900  1.000 36.53859 ? 1   LYS A C      1 
ATOM   16   O  O      . LYS A 1 5   ? -39.06500 21.25900  26.78700  1.000 38.35986 ? 1   LYS A O      1 
ATOM   17   C  CB     . LYS A 1 5   ? -40.55600 21.50700  29.45300  1.000 47.56623 ? 1   LYS A CB     1 
ATOM   18   C  CG     . LYS A 1 5   ? -39.92100 20.32100  30.09100  1.000 53.01688 ? 1   LYS A CG     1 
ATOM   19   C  CD     . LYS A 1 5   ? -40.79200 19.74700  31.16200  1.000 64.16822 ? 1   LYS A CD     1 
ATOM   20   C  CE     . LYS A 1 5   ? -39.90700 19.25300  32.26200  1.000 66.82380 ? 1   LYS A CE     1 
ATOM   21   N  NZ     . LYS A 1 5   ? -39.26200 18.00400  31.84200  1.000 64.17612 ? 1   LYS A NZ     1 
ATOM   22   N  N      . THR A 1 6   ? -37.45300 21.34200  28.26200  1.000 33.06186 ? 2   THR A N      1 
ATOM   23   C  CA     . THR A 1 6   ? -36.57100 20.51500  27.47400  1.000 40.74962 ? 2   THR A CA     1 
ATOM   24   C  C      . THR A 1 6   ? -36.19100 19.26900  28.22900  1.000 39.38367 ? 2   THR A C      1 
ATOM   25   O  O      . THR A 1 6   ? -36.25600 19.25900  29.42600  1.000 39.45999 ? 2   THR A O      1 
ATOM   26   C  CB     . THR A 1 6   ? -35.26300 21.20900  27.09300  1.000 42.26823 ? 2   THR A CB     1 
ATOM   27   O  OG1    . THR A 1 6   ? -34.50200 21.47000  28.25600  1.000 44.57377 ? 2   THR A OG1    1 
ATOM   28   C  CG2    . THR A 1 6   ? -35.50300 22.44100  26.37200  1.000 38.25985 ? 2   THR A CG2    1 
ATOM   29   N  N      . VAL A 1 7   ? -35.88700 18.20300  27.50500  1.000 33.79879 ? 3   VAL A N      1 
ATOM   30   C  CA     . VAL A 1 7   ? -35.34800 16.98500  28.07900  1.000 35.02262 ? 3   VAL A CA     1 
ATOM   31   C  C      . VAL A 1 7   ? -34.10000 16.62800  27.27500  1.000 36.44911 ? 3   VAL A C      1 
ATOM   32   O  O      . VAL A 1 7   ? -33.82400 17.21900  26.22800  1.000 41.27337 ? 3   VAL A O      1 
ATOM   33   C  CB     . VAL A 1 7   ? -36.36700 15.82600  28.05900  1.000 33.54086 ? 3   VAL A CB     1 
ATOM   34   C  CG1    . VAL A 1 7   ? -37.54400 16.12400  28.96700  1.000 31.73802 ? 3   VAL A CG1    1 
ATOM   35   C  CG2    . VAL A 1 7   ? -36.84100 15.55500  26.62500  1.000 30.66420 ? 3   VAL A CG2    1 
ATOM   36   N  N      . THR A 1 8   ? -33.34700 15.64400  27.76100  1.000 31.09057 ? 4   THR A N      1 
ATOM   37   C  CA     . THR A 1 8   ? -32.23500 15.15800  26.95100  1.000 31.62748 ? 4   THR A CA     1 
ATOM   38   C  C      . THR A 1 8   ? -32.76800 14.43500  25.72400  1.000 31.72486 ? 4   THR A C      1 
ATOM   39   O  O      . THR A 1 8   ? -33.87100 13.87500  25.73300  1.000 30.54314 ? 4   THR A O      1 
ATOM   40   C  CB     . THR A 1 8   ? -31.32200 14.20300  27.73300  1.000 31.74328 ? 4   THR A CB     1 
ATOM   41   O  OG1    . THR A 1 8   ? -32.05300 13.02900  28.10300  1.000 35.82272 ? 4   THR A OG1    1 
ATOM   42   C  CG2    . THR A 1 8   ? -30.74800 14.86400  28.98300  1.000 26.84269 ? 4   THR A CG2    1 
ATOM   43   N  N      . ALA A 1 9   ? -31.96600 14.44900  24.65700  1.000 35.56216 ? 5   ALA A N      1 
ATOM   44   C  CA     . ALA A 1 9   ? -32.35500 13.75500  23.43700  1.000 28.69028 ? 5   ALA A CA     1 
ATOM   45   C  C      . ALA A 1 9   ? -32.68600 12.29700  23.71700  1.000 34.53835 ? 5   ALA A C      1 
ATOM   46   O  O      . ALA A 1 9   ? -33.66000 11.75200  23.17600  1.000 30.90107 ? 5   ALA A O      1 
ATOM   47   C  CB     . ALA A 1 9   ? -31.24500 13.85200  22.39800  1.000 23.49492 ? 5   ALA A CB     1 
ATOM   48   N  N      . VAL A 1 10  ? -31.89400 11.64600  24.57300  1.000 28.42709 ? 6   VAL A N      1 
ATOM   49   C  CA     . VAL A 1 10  ? -32.12900 10.22700  24.80800  1.000 30.21152 ? 6   VAL A CA     1 
ATOM   50   C  C      . VAL A 1 10  ? -33.40100 10.02400  25.63300  1.000 29.30351 ? 6   VAL A C      1 
ATOM   51   O  O      . VAL A 1 10  ? -34.15700 9.07400   25.39100  1.000 35.43583 ? 6   VAL A O      1 
ATOM   52   C  CB     . VAL A 1 10  ? -30.87200 9.59900   25.45400  1.000 35.64901 ? 6   VAL A CB     1 
ATOM   53   C  CG1    . VAL A 1 10  ? -30.62800 10.13300  26.88300  1.000 26.86638 ? 6   VAL A CG1    1 
ATOM   54   C  CG2    . VAL A 1 10  ? -30.95200 8.08600   25.44500  1.000 44.97118 ? 6   VAL A CG2    1 
ATOM   55   N  N      . GLU A 1 11  ? -33.71700 10.95300  26.54200  1.000 26.40580 ? 7   GLU A N      1 
ATOM   56   C  CA     . GLU A 1 11  ? -34.99200 10.85400  27.24700  1.000 35.20685 ? 7   GLU A CA     1 
ATOM   57   C  C      . GLU A 1 11  ? -36.16300 11.07000  26.29500  1.000 34.57257 ? 7   GLU A C      1 
ATOM   58   O  O      . GLU A 1 11  ? -37.20200 10.40800  26.42600  1.000 31.37481 ? 7   GLU A O      1 
ATOM   59   C  CB     . GLU A 1 11  ? -35.07700 11.84600  28.40600  1.000 29.89043 ? 7   GLU A CB     1 
ATOM   60   C  CG     . GLU A 1 11  ? -36.41700 11.69800  29.13300  1.000 40.99965 ? 7   GLU A CG     1 
ATOM   61   C  CD     . GLU A 1 11  ? -36.56000 12.56500  30.37800  1.000 42.81040 ? 7   GLU A CD     1 
ATOM   62   O  OE1    . GLU A 1 11  ? -37.70600 12.97600  30.66400  1.000 36.75177 ? 7   GLU A OE1    1 
ATOM   63   O  OE2    . GLU A 1 11  ? -35.54400 12.83100  31.06100  1.000 43.82631 ? 7   GLU A OE2    1 
ATOM   64   N  N      . LEU A 1 12  ? -36.02500 12.00000  25.34400  1.000 26.61898 ? 8   LEU A N      1 
ATOM   65   C  CA     . LEU A 1 12  ? -37.08900 12.16600  24.36400  1.000 33.69615 ? 8   LEU A CA     1 
ATOM   66   C  C      . LEU A 1 12  ? -37.34900 10.85300  23.64700  1.000 29.63776 ? 8   LEU A C      1 
ATOM   67   O  O      . LEU A 1 12  ? -38.50300 10.43200  23.48600  1.000 25.62676 ? 8   LEU A O      1 
ATOM   68   C  CB     . LEU A 1 12  ? -36.75100 13.27700  23.36600  1.000 33.78037 ? 8   LEU A CB     1 
ATOM   69   C  CG     . LEU A 1 12  ? -37.91500 13.52000  22.39200  1.000 34.25411 ? 8   LEU A CG     1 
ATOM   70   C  CD1    . LEU A 1 12  ? -39.01600 14.34500  23.05800  1.000 33.63824 ? 8   LEU A CD1    1 
ATOM   71   C  CD2    . LEU A 1 12  ? -37.46500 14.17600  21.09800  1.000 32.01436 ? 8   LEU A CD2    1 
ATOM   72   N  N      . LEU A 1 13  ? -36.27300 10.17900  23.22800  1.000 28.03494 ? 9   LEU A N      1 
ATOM   73   C  CA     . LEU A 1 13  ? -36.40200 8.88400   22.56700  1.000 28.46394 ? 9   LEU A CA     1 
ATOM   74   C  C      . LEU A 1 13  ? -37.14100 7.87300   23.45100  1.000 31.29586 ? 9   LEU A C      1 
ATOM   75   O  O      . LEU A 1 13  ? -38.01800 7.14500   22.97700  1.000 31.32481 ? 9   LEU A O      1 
ATOM   76   C  CB     . LEU A 1 13  ? -35.01300 8.38300   22.16900  1.000 25.96364 ? 9   LEU A CB     1 
ATOM   77   C  CG     . LEU A 1 13  ? -34.81900 6.89700   21.88000  1.000 30.66420 ? 9   LEU A CG     1 
ATOM   78   C  CD1    . LEU A 1 13  ? -35.59800 6.44000   20.63400  1.000 29.18245 ? 9   LEU A CD1    1 
ATOM   79   C  CD2    . LEU A 1 13  ? -33.31700 6.58900   21.72400  1.000 26.24788 ? 9   LEU A CD2    1 
ATOM   80   N  N      . VAL A 1 14  ? -36.80000 7.81400   24.74100  1.000 28.17180 ? 10  VAL A N      1 
ATOM   81   C  CA     . VAL A 1 14  ? -37.47500 6.89800   25.65700  1.000 24.50031 ? 10  VAL A CA     1 
ATOM   82   C  C      . VAL A 1 14  ? -38.95400 7.24500   25.76900  1.000 26.34526 ? 10  VAL A C      1 
ATOM   83   O  O      . VAL A 1 14  ? -39.81700 6.36200   25.74900  1.000 30.91686 ? 10  VAL A O      1 
ATOM   84   C  CB     . VAL A 1 14  ? -36.78200 6.92000   27.03200  1.000 33.69351 ? 10  VAL A CB     1 
ATOM   85   C  CG1    . VAL A 1 14  ? -37.65000 6.21400   28.08400  1.000 38.58884 ? 10  VAL A CG1    1 
ATOM   86   C  CG2    . VAL A 1 14  ? -35.38900 6.27900   26.92900  1.000 35.57532 ? 10  VAL A CG2    1 
ATOM   87   N  N      . ARG A 1 15  ? -39.27100 8.53400   25.90300  1.000 23.95287 ? 11  ARG A N      1 
ATOM   88   C  CA     . ARG A 1 15  ? -40.67200 8.92100   26.02200  1.000 33.56718 ? 11  ARG A CA     1 
ATOM   89   C  C      . ARG A 1 15  ? -41.45000 8.60100   24.74800  1.000 32.02489 ? 11  ARG A C      1 
ATOM   90   O  O      . ARG A 1 15  ? -42.61600 8.19900   24.81200  1.000 29.37984 ? 11  ARG A O      1 
ATOM   91   C  CB     . ARG A 1 15  ? -40.78700 10.40600  26.35400  1.000 33.63035 ? 11  ARG A CB     1 
ATOM   92   C  CG     . ARG A 1 15  ? -40.25400 10.81400  27.72900  1.000 33.72510 ? 11  ARG A CG     1 
ATOM   93   C  CD     . ARG A 1 15  ? -40.20900 12.32300  27.78200  1.000 39.19154 ? 11  ARG A CD     1 
ATOM   94   N  NE     . ARG A 1 15  ? -39.96100 12.85400  29.11200  1.000 49.17695 ? 11  ARG A NE     1 
ATOM   95   C  CZ     . ARG A 1 15  ? -40.89700 13.37700  29.89300  1.000 46.14237 ? 11  ARG A CZ     1 
ATOM   96   N  NH1    . ARG A 1 15  ? -42.16400 13.42400  29.48900  1.000 41.52603 ? 11  ARG A NH1    1 
ATOM   97   N  NH2    . ARG A 1 15  ? -40.55900 13.85100  31.08100  1.000 42.26559 ? 11  ARG A NH2    1 
ATOM   98   N  N      . GLN A 1 16  ? -40.83000 8.78300   23.57900  1.000 30.47207 ? 12  GLN A N      1 
ATOM   99   C  CA     . GLN A 1 16  ? -41.53000 8.47200   22.33700  1.000 23.56862 ? 12  GLN A CA     1 
ATOM   100  C  C      . GLN A 1 16  ? -41.74000 6.96800   22.18700  1.000 30.32995 ? 12  GLN A C      1 
ATOM   101  O  O      . GLN A 1 16  ? -42.76200 6.54000   21.64700  1.000 30.84580 ? 12  GLN A O      1 
ATOM   102  C  CB     . GLN A 1 16  ? -40.76500 9.06100   21.13700  1.000 25.29514 ? 12  GLN A CB     1 
ATOM   103  C  CG     . GLN A 1 16  ? -41.49900 8.93700   19.78300  1.000 24.87140 ? 12  GLN A CG     1 
ATOM   104  C  CD     . GLN A 1 16  ? -42.82800 9.70700   19.72100  1.000 29.31667 ? 12  GLN A CD     1 
ATOM   105  O  OE1    . GLN A 1 16  ? -42.85100 10.92800  19.56100  1.000 31.26954 ? 12  GLN A OE1    1 
ATOM   106  N  NE2    . GLN A 1 16  ? -43.93600 8.98500   19.83100  1.000 28.47973 ? 12  GLN A NE2    1 
ATOM   107  N  N      . MET A 1 17  ? -40.80800 6.14500   22.68500  1.000 27.69806 ? 13  MET A N      1 
ATOM   108  C  CA     . MET A 1 17  ? -41.06500 4.70900   22.71000  1.000 25.09248 ? 13  MET A CA     1 
ATOM   109  C  C      . MET A 1 17  ? -42.18700 4.35700   23.68300  1.000 31.12215 ? 13  MET A C      1 
ATOM   110  O  O      . MET A 1 17  ? -42.95600 3.42400   23.43400  1.000 34.63573 ? 13  MET A O      1 
ATOM   111  C  CB     . MET A 1 17  ? -39.78500 3.94600   23.04800  1.000 21.70260 ? 13  MET A CB     1 
ATOM   112  C  CG     . MET A 1 17  ? -38.78000 3.98000   21.90800  1.000 27.58752 ? 13  MET A CG     1 
ATOM   113  S  SD     . MET A 1 17  ? -37.44600 2.80200   22.16700  1.000 37.24131 ? 13  MET A SD     1 
ATOM   114  C  CE     . MET A 1 17  ? -36.86000 3.27400   23.79200  1.000 32.02489 ? 13  MET A CE     1 
ATOM   115  N  N      . GLU A 1 18  ? -42.28500 5.07200   24.80700  1.000 22.97644 ? 14  GLU A N      1 
ATOM   116  C  CA     . GLU A 1 18  ? -43.41700 4.86500   25.71100  1.000 25.32146 ? 14  GLU A CA     1 
ATOM   117  C  C      . GLU A 1 18  ? -44.74400 5.04100   24.97700  1.000 31.04056 ? 14  GLU A C      1 
ATOM   118  O  O      . GLU A 1 18  ? -45.65500 4.21700   25.11700  1.000 31.66169 ? 14  GLU A O      1 
ATOM   119  C  CB     . GLU A 1 18  ? -43.33900 5.83400   26.89800  1.000 24.45293 ? 14  GLU A CB     1 
ATOM   120  C  CG     . GLU A 1 18  ? -42.26900 5.50700   27.93000  1.000 31.34586 ? 14  GLU A CG     1 
ATOM   121  C  CD     . GLU A 1 18  ? -42.00900 6.65100   28.93400  1.000 42.40508 ? 14  GLU A CD     1 
ATOM   122  O  OE1    . GLU A 1 18  ? -40.92800 6.64300   29.56900  1.000 46.40820 ? 14  GLU A OE1    1 
ATOM   123  O  OE2    . GLU A 1 18  ? -42.87100 7.55100   29.08300  1.000 44.26583 ? 14  GLU A OE2    1 
ATOM   124  N  N      . ALA A 1 19  ? -44.86700 6.10300   24.17500  1.000 31.43535 ? 15  ALA A N      1 
ATOM   125  C  CA     . ALA A 1 19  ? -46.12300 6.35300   23.47300  1.000 32.34072 ? 15  ALA A CA     1 
ATOM   126  C  C      . ALA A 1 19  ? -46.48600 5.22000   22.52600  1.000 29.30351 ? 15  ALA A C      1 
ATOM   127  O  O      . ALA A 1 19  ? -47.66800 5.04100   22.22100  1.000 35.50426 ? 15  ALA A O      1 
ATOM   128  C  CB     . ALA A 1 19  ? -46.04700 7.67500   22.71100  1.000 36.42279 ? 15  ALA A CB     1 
ATOM   129  N  N      . GLU A 1 20  ? -45.50800 4.44500   22.06600  1.000 25.86100 ? 16  GLU A N      1 
ATOM   130  C  CA     . GLU A 1 20  ? -45.78900 3.29000   21.22100  1.000 27.37697 ? 16  GLU A CA     1 
ATOM   131  C  C      . GLU A 1 20  ? -46.10800 2.03500   22.02300  1.000 34.12514 ? 16  GLU A C      1 
ATOM   132  O  O      . GLU A 1 20  ? -46.27900 0.96100   21.42600  1.000 40.55223 ? 16  GLU A O      1 
ATOM   133  C  CB     . GLU A 1 20  ? -44.60200 3.02000   20.28700  1.000 35.37266 ? 16  GLU A CB     1 
ATOM   134  C  CG     . GLU A 1 20  ? -44.47000 4.02700   19.15500  1.000 40.89701 ? 16  GLU A CG     1 
ATOM   135  C  CD     . GLU A 1 20  ? -45.16700 3.57800   17.87900  1.000 39.01784 ? 16  GLU A CD     1 
ATOM   136  O  OE1    . GLU A 1 20  ? -45.20000 4.37100   16.91300  1.000 39.66265 ? 16  GLU A OE1    1 
ATOM   137  O  OE2    . GLU A 1 20  ? -45.68900 2.44000   17.84400  1.000 40.55749 ? 16  GLU A OE2    1 
ATOM   138  N  N      . GLY A 1 21  ? -46.17700 2.14000   23.34900  1.000 32.58022 ? 17  GLY A N      1 
ATOM   139  C  CA     . GLY A 1 21  ? -46.46300 0.99200   24.18300  1.000 32.50127 ? 17  GLY A CA     1 
ATOM   140  C  C      . GLY A 1 21  ? -45.29100 0.06000   24.40000  1.000 38.38355 ? 17  GLY A C      1 
ATOM   141  O  O      . GLY A 1 21  ? -45.49300 -1.06800  24.86100  1.000 36.46227 ? 17  GLY A O      1 
ATOM   142  N  N      . VAL A 1 22  ? -44.06100 0.50700   24.11900  1.000 28.70344 ? 18  VAL A N      1 
ATOM   143  C  CA     . VAL A 1 22  ? -42.89400 -0.32500  24.40300  1.000 31.65906 ? 18  VAL A CA     1 
ATOM   144  C  C      . VAL A 1 22  ? -42.78900 -0.55000  25.90800  1.000 33.20398 ? 18  VAL A C      1 
ATOM   145  O  O      . VAL A 1 22  ? -42.86500 0.39800   26.69700  1.000 29.65882 ? 18  VAL A O      1 
ATOM   146  C  CB     . VAL A 1 22  ? -41.62400 0.33000   23.83700  1.000 32.92237 ? 18  VAL A CB     1 
ATOM   147  C  CG1    . VAL A 1 22  ? -40.37200 -0.41700  24.30300  1.000 32.67760 ? 18  VAL A CG1    1 
ATOM   148  C  CG2    . VAL A 1 22  ? -41.68600 0.39600   22.30800  1.000 30.84054 ? 18  VAL A CG2    1 
ATOM   149  N  N      . SER A 1 23  ? -42.60700 -1.81400  26.32000  1.000 28.60869 ? 19  SER A N      1 
ATOM   150  C  CA     . SER A 1 23  ? -42.50900 -2.13000  27.74600  1.000 30.44839 ? 19  SER A CA     1 
ATOM   151  C  C      . SER A 1 23  ? -41.16100 -2.68800  28.18000  1.000 33.27767 ? 19  SER A C      1 
ATOM   152  O  O      . SER A 1 23  ? -40.89300 -2.73100  29.38600  1.000 31.08004 ? 19  SER A O      1 
ATOM   153  C  CB     . SER A 1 23  ? -43.57600 -3.15900  28.15300  1.000 26.42422 ? 19  SER A CB     1 
ATOM   154  O  OG     . SER A 1 23  ? -44.87000 -2.79600  27.71100  1.000 38.28354 ? 19  SER A OG     1 
ATOM   155  N  N      . TYR A 1 24  ? -40.30700 -3.10300  27.24700  1.000 32.36704 ? 20  TYR A N      1 
ATOM   156  C  CA     . TYR A 1 24  ? -39.01000 -3.67900  27.56200  1.000 30.59314 ? 20  TYR A CA     1 
ATOM   157  C  C      . TYR A 1 24  ? -38.00200 -3.22500  26.52200  1.000 28.19549 ? 20  TYR A C      1 
ATOM   158  O  O      . TYR A 1 24  ? -38.34700 -3.01200  25.35700  1.000 29.33510 ? 20  TYR A O      1 
ATOM   159  C  CB     . TYR A 1 24  ? -39.07300 -5.21000  27.57900  1.000 26.91375 ? 20  TYR A CB     1 
ATOM   160  C  CG     . TYR A 1 24  ? -39.98000 -5.75100  28.66200  1.000 23.76864 ? 20  TYR A CG     1 
ATOM   161  C  CD1    . TYR A 1 24  ? -39.52200 -5.87300  29.97200  1.000 29.23508 ? 20  TYR A CD1    1 
ATOM   162  C  CD2    . TYR A 1 24  ? -41.28200 -6.12800  28.38500  1.000 24.82666 ? 20  TYR A CD2    1 
ATOM   163  C  CE1    . TYR A 1 24  ? -40.34000 -6.35900  30.97500  1.000 28.55869 ? 20  TYR A CE1    1 
ATOM   164  C  CE2    . TYR A 1 24  ? -42.11300 -6.60900  29.39000  1.000 26.35053 ? 20  TYR A CE2    1 
ATOM   165  C  CZ     . TYR A 1 24  ? -41.62800 -6.73000  30.67900  1.000 27.24274 ? 20  TYR A CZ     1 
ATOM   166  O  OH     . TYR A 1 24  ? -42.43100 -7.21500  31.68000  1.000 28.88504 ? 20  TYR A OH     1 
ATOM   167  N  N      . VAL A 1 25  ? -36.75200 -3.08500  26.95100  1.000 27.40592 ? 21  VAL A N      1 
ATOM   168  C  CA     . VAL A 1 25  ? -35.62700 -2.88500  26.04500  1.000 26.32158 ? 21  VAL A CA     1 
ATOM   169  C  C      . VAL A 1 25  ? -34.60800 -3.97100  26.36500  1.000 22.59481 ? 21  VAL A C      1 
ATOM   170  O  O      . VAL A 1 25  ? -34.10100 -4.03800  27.49500  1.000 28.65080 ? 21  VAL A O      1 
ATOM   171  C  CB     . VAL A 1 25  ? -35.00600 -1.48400  26.18500  1.000 29.14034 ? 21  VAL A CB     1 
ATOM   172  C  CG1    . VAL A 1 25  ? -33.72700 -1.38000  25.35300  1.000 25.84520 ? 21  VAL A CG1    1 
ATOM   173  C  CG2    . VAL A 1 25  ? -36.01000 -0.42200  25.76400  1.000 31.04846 ? 21  VAL A CG2    1 
ATOM   174  N  N      . PHE A 1 26  ? -34.35200 -4.84600  25.39900  1.000 25.69255 ? 22  PHE A N      1 
ATOM   175  C  CA     . PHE A 1 26  ? -33.41800 -5.95100  25.57200  1.000 26.99534 ? 22  PHE A CA     1 
ATOM   176  C  C      . PHE A 1 26  ? -32.04300 -5.54900  25.06100  1.000 30.61157 ? 22  PHE A C      1 
ATOM   177  O  O      . PHE A 1 26  ? -31.92500 -4.99400  23.96700  1.000 23.68179 ? 22  PHE A O      1 
ATOM   178  C  CB     . PHE A 1 26  ? -33.91500 -7.18900  24.82900  1.000 26.02944 ? 22  PHE A CB     1 
ATOM   179  C  CG     . PHE A 1 26  ? -35.33200 -7.59400  25.19600  1.000 25.47148 ? 22  PHE A CG     1 
ATOM   180  C  CD1    . PHE A 1 26  ? -35.56700 -8.47900  26.24700  1.000 24.54505 ? 22  PHE A CD1    1 
ATOM   181  C  CD2    . PHE A 1 26  ? -36.41300 -7.09200  24.48300  1.000 22.96854 ? 22  PHE A CD2    1 
ATOM   182  C  CE1    . PHE A 1 26  ? -36.86300 -8.86100  26.58300  1.000 28.63764 ? 22  PHE A CE1    1 
ATOM   183  C  CE2    . PHE A 1 26  ? -37.72600 -7.46400  24.81400  1.000 30.17467 ? 22  PHE A CE2    1 
ATOM   184  C  CZ     . PHE A 1 26  ? -37.95200 -8.34300  25.86800  1.000 27.19010 ? 22  PHE A CZ     1 
ATOM   185  N  N      . GLY A 1 27  ? -31.00300 -5.83500  25.83500  1.000 24.94246 ? 23  GLY A N      1 
ATOM   186  C  CA     . GLY A 1 27  ? -29.68300 -5.48200  25.36100  1.000 28.77977 ? 23  GLY A CA     1 
ATOM   187  C  C      . GLY A 1 27  ? -28.62600 -5.64800  26.43300  1.000 27.00850 ? 23  GLY A C      1 
ATOM   188  O  O      . GLY A 1 27  ? -28.86700 -6.20800  27.50600  1.000 26.75847 ? 23  GLY A O      1 
ATOM   189  N  N      . ILE A 1 28  ? -27.44800 -5.13200  26.10600  1.000 22.70535 ? 24  ILE A N      1 
ATOM   190  C  CA     . ILE A 1 28  ? -26.28100 -5.19900  26.98200  1.000 25.67150 ? 24  ILE A CA     1 
ATOM   191  C  C      . ILE A 1 28  ? -25.65500 -3.81000  27.01100  1.000 22.52639 ? 24  ILE A C      1 
ATOM   192  O  O      . ILE A 1 28  ? -25.46300 -3.19500  25.95600  1.000 30.76421 ? 24  ILE A O      1 
ATOM   193  C  CB     . ILE A 1 28  ? -25.28900 -6.26900  26.48900  1.000 21.76314 ? 24  ILE A CB     1 
ATOM   194  C  CG1    . ILE A 1 28  ? -25.91900 -7.65700  26.66600  1.000 22.85274 ? 24  ILE A CG1    1 
ATOM   195  C  CG2    . ILE A 1 28  ? -23.93700 -6.15000  27.23300  1.000 21.11832 ? 24  ILE A CG2    1 
ATOM   196  C  CD1    . ILE A 1 28  ? -25.05700 -8.82600  26.15700  1.000 27.17694 ? 24  ILE A CD1    1 
ATOM   197  N  N      . PRO A 1 29  ? -25.33400 -3.27600  28.17600  1.000 25.52674 ? 25  PRO A N      1 
ATOM   198  C  CA     . PRO A 1 29  ? -24.80200 -1.91000  28.24400  1.000 33.36189 ? 25  PRO A CA     1 
ATOM   199  C  C      . PRO A 1 29  ? -23.36700 -1.82100  27.73400  1.000 31.32744 ? 25  PRO A C      1 
ATOM   200  O  O      . PRO A 1 29  ? -22.68800 -2.81200  27.46700  1.000 32.15122 ? 25  PRO A O      1 
ATOM   201  C  CB     . PRO A 1 29  ? -24.87400 -1.58100  29.73900  1.000 32.68287 ? 25  PRO A CB     1 
ATOM   202  C  CG     . PRO A 1 29  ? -24.76300 -2.94300  30.41200  1.000 33.52507 ? 25  PRO A CG     1 
ATOM   203  C  CD     . PRO A 1 29  ? -25.57800 -3.84600  29.51300  1.000 31.05109 ? 25  PRO A CD     1 
ATOM   204  N  N      . GLY A 1 30  ? -22.92200 -0.57800  27.60100  1.000 30.08255 ? 26  GLY A N      1 
ATOM   205  C  CA     . GLY A 1 30  ? -21.55700 -0.25100  27.24800  1.000 29.37457 ? 26  GLY A CA     1 
ATOM   206  C  C      . GLY A 1 30  ? -21.37000 1.23600   27.43500  1.000 34.05935 ? 26  GLY A C      1 
ATOM   207  O  O      . GLY A 1 30  ? -22.34400 1.99000   27.52000  1.000 36.11486 ? 26  GLY A O      1 
ATOM   208  N  N      . GLY A 1 31  ? -20.10500 1.65000   27.51700  1.000 30.61683 ? 27  GLY A N      1 
ATOM   209  C  CA     . GLY A 1 31  ? -19.77800 3.02300   27.82500  1.000 28.41130 ? 27  GLY A CA     1 
ATOM   210  C  C      . GLY A 1 31  ? -20.48100 4.18500   27.14400  1.000 30.17993 ? 27  GLY A C      1 
ATOM   211  O  O      . GLY A 1 31  ? -20.94100 5.12700   27.79200  1.000 31.75907 ? 27  GLY A O      1 
ATOM   212  N  N      . PRO A 1 32  ? -20.60800 4.11500   25.81500  1.000 30.01676 ? 28  PRO A N      1 
ATOM   213  C  CA     . PRO A 1 32  ? -21.36800 5.14100   25.08300  1.000 28.26128 ? 28  PRO A CA     1 
ATOM   214  C  C      . PRO A 1 32  ? -22.87200 4.94400   25.12200  1.000 33.75405 ? 28  PRO A C      1 
ATOM   215  O  O      . PRO A 1 32  ? -23.60000 5.87400   24.76200  1.000 39.12311 ? 28  PRO A O      1 
ATOM   216  C  CB     . PRO A 1 32  ? -20.84800 5.02000   23.64000  1.000 28.12179 ? 28  PRO A CB     1 
ATOM   217  C  CG     . PRO A 1 32  ? -19.82900 3.91200   23.64600  1.000 31.04320 ? 28  PRO A CG     1 
ATOM   218  C  CD     . PRO A 1 32  ? -19.93900 3.16100   24.92100  1.000 34.84892 ? 28  PRO A CD     1 
ATOM   219  N  N      . LEU A 1 33  ? -23.35700 3.77600   25.53300  1.000 33.15398 ? 29  LEU A N      1 
ATOM   220  C  CA     . LEU A 1 33  ? -24.78400 3.48900   25.64400  1.000 31.92225 ? 29  LEU A CA     1 
ATOM   221  C  C      . LEU A 1 33  ? -25.37400 3.88600   27.00100  1.000 36.38594 ? 29  LEU A C      1 
ATOM   222  O  O      . LEU A 1 33  ? -26.60000 3.91400   27.14800  1.000 32.60128 ? 29  LEU A O      1 
ATOM   223  C  CB     . LEU A 1 33  ? -25.00700 1.98700   25.38700  1.000 31.15110 ? 29  LEU A CB     1 
ATOM   224  C  CG     . LEU A 1 33  ? -26.37700 1.42400   25.03300  1.000 30.94318 ? 29  LEU A CG     1 
ATOM   225  C  CD1    . LEU A 1 33  ? -26.94200 2.11500   23.78500  1.000 24.95826 ? 29  LEU A CD1    1 
ATOM   226  C  CD2    . LEU A 1 33  ? -26.26100 -0.09400  24.83000  1.000 27.04008 ? 29  LEU A CD2    1 
ATOM   227  N  N      . MET A 1 34  ? -24.53800 4.20800   27.98900  1.000 31.03530 ? 30  MET A N      1 
ATOM   228  C  CA     . MET A 1 34  ? -25.03800 4.42700   29.34700  1.000 29.89569 ? 30  MET A CA     1 
ATOM   229  C  C      . MET A 1 34  ? -26.06800 5.55400   29.47100  1.000 36.61228 ? 30  MET A C      1 
ATOM   230  O  O      . MET A 1 34  ? -26.99300 5.41900   30.29500  1.000 30.73790 ? 30  MET A O      1 
ATOM   231  C  CB     . MET A 1 34  ? -23.84900 4.66700   30.28700  1.000 27.89545 ? 30  MET A CB     1 
ATOM   232  C  CG     . MET A 1 34  ? -22.91900 3.46300   30.39500  1.000 32.15912 ? 30  MET A CG     1 
ATOM   233  S  SD     . MET A 1 34  ? -23.85000 1.92800   30.70500  1.000 44.50270 ? 30  MET A SD     1 
ATOM   234  C  CE     . MET A 1 34  ? -24.20400 2.18400   32.44800  1.000 35.38319 ? 30  MET A CE     1 
ATOM   235  N  N      . PRO A 1 35  ? -25.97700 6.66900   28.74200  1.000 37.83085 ? 31  PRO A N      1 
ATOM   236  C  CA     . PRO A 1 35  ? -27.04200 7.68200   28.86400  1.000 30.59841 ? 31  PRO A CA     1 
ATOM   237  C  C      . PRO A 1 35  ? -28.42700 7.13100   28.53100  1.000 31.48272 ? 31  PRO A C      1 
ATOM   238  O  O      . PRO A 1 35  ? -29.42200 7.59800   29.09900  1.000 28.98769 ? 31  PRO A O      1 
ATOM   239  C  CB     . PRO A 1 35  ? -26.59900 8.77800   27.88200  1.000 34.66995 ? 31  PRO A CB     1 
ATOM   240  C  CG     . PRO A 1 35  ? -25.09800 8.63200   27.82100  1.000 34.51203 ? 31  PRO A CG     1 
ATOM   241  C  CD     . PRO A 1 35  ? -24.87800 7.12800   27.87100  1.000 35.10947 ? 31  PRO A CD     1 
ATOM   242  N  N      . LEU A 1 36  ? -28.52800 6.16100   27.61700  1.000 29.90885 ? 32  LEU A N      1 
ATOM   243  C  CA     . LEU A 1 36  ? -29.81900 5.53000   27.36600  1.000 29.53512 ? 32  LEU A CA     1 
ATOM   244  C  C      . LEU A 1 36  ? -30.32600 4.82900   28.61900  1.000 32.31177 ? 32  LEU A C      1 
ATOM   245  O  O      . LEU A 1 36  ? -31.48400 5.00600   29.01700  1.000 34.96998 ? 32  LEU A O      1 
ATOM   246  C  CB     . LEU A 1 36  ? -29.71700 4.53200   26.20700  1.000 30.99319 ? 32  LEU A CB     1 
ATOM   247  C  CG     . LEU A 1 36  ? -30.96700 3.67700   25.96300  1.000 30.73790 ? 32  LEU A CG     1 
ATOM   248  C  CD1    . LEU A 1 36  ? -32.15900 4.54900   25.52700  1.000 25.15038 ? 32  LEU A CD1    1 
ATOM   249  C  CD2    . LEU A 1 36  ? -30.71600 2.54500   24.96500  1.000 33.64351 ? 32  LEU A CD2    1 
ATOM   250  N  N      . TYR A 1 37  ? -29.46200 4.05200   29.28000  1.000 28.30339 ? 33  TYR A N      1 
ATOM   251  C  CA     . TYR A 1 37  ? -29.91000 3.35800   30.48200  1.000 32.43020 ? 33  TYR A CA     1 
ATOM   252  C  C      . TYR A 1 37  ? -30.26500 4.35100   31.57300  1.000 31.80908 ? 33  TYR A C      1 
ATOM   253  O  O      . TYR A 1 37  ? -31.26600 4.17600   32.27900  1.000 29.69303 ? 33  TYR A O      1 
ATOM   254  C  CB     . TYR A 1 37  ? -28.84100 2.38300   30.96300  1.000 27.78491 ? 33  TYR A CB     1 
ATOM   255  C  CG     . TYR A 1 37  ? -28.84900 1.14000   30.14500  1.000 25.99522 ? 33  TYR A CG     1 
ATOM   256  C  CD1    . TYR A 1 37  ? -29.81800 0.17100   30.34100  1.000 30.79317 ? 33  TYR A CD1    1 
ATOM   257  C  CD2    . TYR A 1 37  ? -27.92200 0.95200   29.12200  1.000 31.69064 ? 33  TYR A CD2    1 
ATOM   258  C  CE1    . TYR A 1 37  ? -29.84100 -0.98500  29.56800  1.000 35.40951 ? 33  TYR A CE1    1 
ATOM   259  C  CE2    . TYR A 1 37  ? -27.95000 -0.18600  28.33900  1.000 26.19261 ? 33  TYR A CE2    1 
ATOM   260  C  CZ     . TYR A 1 37  ? -28.90600 -1.15500  28.57300  1.000 31.22743 ? 33  TYR A CZ     1 
ATOM   261  O  OH     . TYR A 1 37  ? -28.93300 -2.29700  27.80400  1.000 35.90957 ? 33  TYR A OH     1 
ATOM   262  N  N      . GLU A 1 38  ? -29.47700 5.42100   31.70000  1.000 28.20075 ? 34  GLU A N      1 
ATOM   263  C  CA     . GLU A 1 38  ? -29.81600 6.46400   32.66300  1.000 30.87739 ? 34  GLU A CA     1 
ATOM   264  C  C      . GLU A 1 38  ? -31.22200 7.00100   32.42300  1.000 26.85585 ? 34  GLU A C      1 
ATOM   265  O  O      . GLU A 1 38  ? -32.00400 7.16400   33.36600  1.000 33.02238 ? 34  GLU A O      1 
ATOM   266  C  CB     . GLU A 1 38  ? -28.79100 7.59700   32.58800  1.000 28.97979 ? 34  GLU A CB     1 
ATOM   267  C  CG     . GLU A 1 38  ? -29.11000 8.77700   33.49100  1.000 38.93625 ? 34  GLU A CG     1 
ATOM   268  C  CD     . GLU A 1 38  ? -27.99900 9.81100   33.47900  1.000 49.55857 ? 34  GLU A CD     1 
ATOM   269  O  OE1    . GLU A 1 38  ? -27.68800 10.34600  34.55600  1.000 53.94068 ? 34  GLU A OE1    1 
ATOM   270  O  OE2    . GLU A 1 38  ? -27.42800 10.07700  32.39600  1.000 51.35879 ? 34  GLU A OE2    1 
ATOM   271  N  N      . ALA A 1 39  ? -31.56200 7.29300   31.16000  1.000 32.40915 ? 35  ALA A N      1 
ATOM   272  C  CA     . ALA A 1 39  ? -32.89700 7.80300   30.84900  1.000 31.66959 ? 35  ALA A CA     1 
ATOM   273  C  C      . ALA A 1 39  ? -33.97000 6.76200   31.15100  1.000 30.84054 ? 35  ALA A C      1 
ATOM   274  O  O      . ALA A 1 39  ? -35.02700 7.09000   31.69900  1.000 31.86435 ? 35  ALA A O      1 
ATOM   275  C  CB     . ALA A 1 39  ? -32.96800 8.23700   29.38300  1.000 30.10361 ? 35  ALA A CB     1 
ATOM   276  N  N      . ILE A 1 40  ? -33.71200 5.49700   30.81100  1.000 32.82762 ? 36  ILE A N      1 
ATOM   277  C  CA     . ILE A 1 40  ? -34.69500 4.45000   31.07300  1.000 35.04894 ? 36  ILE A CA     1 
ATOM   278  C  C      . ILE A 1 40  ? -34.96200 4.34700   32.56500  1.000 33.16187 ? 36  ILE A C      1 
ATOM   279  O  O      . ILE A 1 40  ? -36.11400 4.31300   33.00900  1.000 34.62784 ? 36  ILE A O      1 
ATOM   280  C  CB     . ILE A 1 40  ? -34.22300 3.10700   30.49500  1.000 34.38307 ? 36  ILE A CB     1 
ATOM   281  C  CG1    . ILE A 1 40  ? -34.48800 3.05900   28.99300  1.000 35.42530 ? 36  ILE A CG1    1 
ATOM   282  C  CG2    . ILE A 1 40  ? -34.95500 1.96400   31.17500  1.000 33.63561 ? 36  ILE A CG2    1 
ATOM   283  C  CD1    . ILE A 1 40  ? -33.84700 1.85900   28.30500  1.000 30.66683 ? 36  ILE A CD1    1 
ATOM   284  N  N      . PHE A 1 41  ? -33.89500 4.32600   33.36600  1.000 33.97776 ? 37  PHE A N      1 
ATOM   285  C  CA     . PHE A 1 41  ? -34.06500 4.16700   34.80300  1.000 34.13830 ? 37  PHE A CA     1 
ATOM   286  C  C      . PHE A 1 41  ? -34.71100 5.39100   35.43200  1.000 37.76769 ? 37  PHE A C      1 
ATOM   287  O  O      . PHE A 1 41  ? -35.34900 5.27200   36.48200  1.000 37.54134 ? 37  PHE A O      1 
ATOM   288  C  CB     . PHE A 1 41  ? -32.71300 3.86400   35.46300  1.000 30.47207 ? 37  PHE A CB     1 
ATOM   289  C  CG     . PHE A 1 41  ? -32.32800 2.40200   35.39200  1.000 33.17240 ? 37  PHE A CG     1 
ATOM   290  C  CD1    . PHE A 1 41  ? -32.98300 1.46300   36.17500  1.000 38.97836 ? 37  PHE A CD1    1 
ATOM   291  C  CD2    . PHE A 1 41  ? -31.33800 1.96700   34.52200  1.000 31.13268 ? 37  PHE A CD2    1 
ATOM   292  C  CE1    . PHE A 1 41  ? -32.64800 0.11600   36.11000  1.000 40.55223 ? 37  PHE A CE1    1 
ATOM   293  C  CE2    . PHE A 1 41  ? -30.99300 0.61500   34.44600  1.000 32.10385 ? 37  PHE A CE2    1 
ATOM   294  C  CZ     . PHE A 1 41  ? -31.64900 -0.30900  35.24500  1.000 38.20195 ? 37  PHE A CZ     1 
ATOM   295  N  N      . SER A 1 42  ? -34.57800 6.56700   34.81200  1.000 38.70727 ? 38  SER A N      1 
ATOM   296  C  CA     . SER A 1 42  ? -35.19300 7.75800   35.40000  1.000 42.03662 ? 38  SER A CA     1 
ATOM   297  C  C      . SER A 1 42  ? -36.69800 7.82200   35.13400  1.000 40.30220 ? 38  SER A C      1 
ATOM   298  O  O      . SER A 1 42  ? -37.43300 8.44800   35.90600  1.000 41.38391 ? 38  SER A O      1 
ATOM   299  C  CB     . SER A 1 42  ? -34.51200 9.01800   34.87400  1.000 39.11258 ? 38  SER A CB     1 
ATOM   300  O  OG     . SER A 1 42  ? -35.03700 9.36800   33.60300  1.000 48.21894 ? 38  SER A OG     1 
ATOM   301  N  N      . ARG A 1 43  ? -37.18200 7.16500   34.07500  1.000 34.01197 ? 39  ARG A N      1 
ATOM   302  C  CA     . ARG A 1 43  ? -38.59900 7.19700   33.71500  1.000 36.11222 ? 39  ARG A CA     1 
ATOM   303  C  C      . ARG A 1 43  ? -39.40700 6.09500   34.37000  1.000 42.23401 ? 39  ARG A C      1 
ATOM   304  O  O      . ARG A 1 43  ? -40.62500 6.23300   34.49700  1.000 53.71433 ? 39  ARG A O      1 
ATOM   305  C  CB     . ARG A 1 43  ? -38.77400 7.05400   32.19500  1.000 35.54900 ? 39  ARG A CB     1 
ATOM   306  C  CG     . ARG A 1 43  ? -38.22700 8.19400   31.36100  1.000 35.13579 ? 39  ARG A CG     1 
ATOM   307  C  CD     . ARG A 1 43  ? -39.07700 9.43100   31.49900  1.000 40.35221 ? 39  ARG A CD     1 
ATOM   308  N  NE     . ARG A 1 43  ? -40.45400 9.16600   31.09200  1.000 38.01245 ? 39  ARG A NE     1 
ATOM   309  C  CZ     . ARG A 1 43  ? -41.48000 9.92200   31.46300  1.000 41.88660 ? 39  ARG A CZ     1 
ATOM   310  N  NH1    . ARG A 1 43  ? -41.25900 10.97600  32.23100  1.000 37.51239 ? 39  ARG A NH1    1 
ATOM   311  N  NH2    . ARG A 1 43  ? -42.71600 9.62800   31.06900  1.000 40.58645 ? 39  ARG A NH2    1 
ATOM   312  N  N      . LYS A 1 44  ? -38.77100 4.98800   34.72900  1.000 40.53381 ? 40  LYS A N      1 
ATOM   313  C  CA     . LYS A 1 44  ? -39.42000 3.88900   35.44000  1.000 48.09524 ? 40  LYS A CA     1 
ATOM   314  C  C      . LYS A 1 44  ? -40.74900 3.47200   34.79000  1.000 43.33677 ? 40  LYS A C      1 
ATOM   315  O  O      . LYS A 1 44  ? -41.76000 3.26400   35.46100  1.000 45.43703 ? 40  LYS A O      1 
ATOM   316  C  CB     . LYS A 1 44  ? -39.61200 4.25400   36.92000  1.000 51.38774 ? 40  LYS A CB     1 
ATOM   317  C  CG     . LYS A 1 44  ? -38.38700 3.93200   37.79500  1.000 56.66206 ? 40  LYS A CG     1 
ATOM   318  C  CD     . LYS A 1 44  ? -38.27300 4.81900   39.03400  1.000 62.34695 ? 40  LYS A CD     1 
ATOM   319  C  CE     . LYS A 1 44  ? -37.44900 6.07500   38.75100  1.000 70.15578 ? 40  LYS A CE     1 
ATOM   320  N  NZ     . LYS A 1 44  ? -36.08100 6.04900   39.35600  1.000 71.74808 ? 40  LYS A NZ     1 
ATOM   321  N  N      . LYS A 1 45  ? -40.72900 3.28600   33.47100  1.000 40.48117 ? 41  LYS A N      1 
ATOM   322  C  CA     . LYS A 1 45  ? -41.89300 2.67700   32.83900  1.000 40.24693 ? 41  LYS A CA     1 
ATOM   323  C  C      . LYS A 1 45  ? -41.38400 1.56600   31.91800  1.000 45.93445 ? 41  LYS A C      1 
ATOM   324  O  O      . LYS A 1 45  ? -41.71600 0.39600   32.12300  1.000 50.44026 ? 41  LYS A O      1 
ATOM   325  C  CB     . LYS A 1 45  ? -42.75200 3.72800   32.11100  1.000 43.17360 ? 41  LYS A CB     1 
ATOM   326  C  CG     . LYS A 1 45  ? -42.96500 5.03800   32.92700  1.000 52.77738 ? 41  LYS A CG     1 
ATOM   327  C  CD     . LYS A 1 45  ? -43.63500 6.18500   32.14800  1.000 59.14130 ? 41  LYS A CD     1 
ATOM   328  C  CE     . LYS A 1 45  ? -44.53800 7.04500   33.07900  1.000 65.72893 ? 41  LYS A CE     1 
ATOM   329  N  NZ     . LYS A 1 45  ? -45.85000 6.50400   33.57300  1.000 69.18724 ? 41  LYS A NZ     1 
ATOM   330  N  N      . ILE A 1 46  ? -40.55700 1.89200   30.92100  1.000 38.01772 ? 42  ILE A N      1 
ATOM   331  C  CA     . ILE A 1 46  ? -39.88200 0.84000   30.16200  1.000 34.40412 ? 42  ILE A CA     1 
ATOM   332  C  C      . ILE A 1 46  ? -38.85700 0.15800   31.06000  1.000 27.37960 ? 42  ILE A C      1 
ATOM   333  O  O      . ILE A 1 46  ? -38.08700 0.82600   31.76000  1.000 32.77235 ? 42  ILE A O      1 
ATOM   334  C  CB     . ILE A 1 46  ? -39.21400 1.40500   28.89700  1.000 34.51730 ? 42  ILE A CB     1 
ATOM   335  C  CG1    . ILE A 1 46  ? -40.28500 1.88200   27.90000  1.000 35.76745 ? 42  ILE A CG1    1 
ATOM   336  C  CG2    . ILE A 1 46  ? -38.31100 0.34100   28.26900  1.000 29.95359 ? 42  ILE A CG2    1 
ATOM   337  C  CD1    . ILE A 1 46  ? -39.76500 2.74300   26.75800  1.000 35.99905 ? 42  ILE A CD1    1 
ATOM   338  N  N      . GLN A 1 47  ? -38.84100 -1.19700  31.05200  1.000 27.34012 ? 43  GLN A N      1 
ATOM   339  C  CA     . GLN A 1 47  ? -37.89400 -1.91800  31.91100  1.000 34.22779 ? 43  GLN A CA     1 
ATOM   340  C  C      . GLN A 1 47  ? -36.72800 -2.47500  31.10600  1.000 29.00348 ? 43  GLN A C      1 
ATOM   341  O  O      . GLN A 1 47  ? -36.94700 -3.14100  30.08500  1.000 25.84784 ? 43  GLN A O      1 
ATOM   342  C  CB     . GLN A 1 47  ? -38.58100 -3.05300  32.66200  1.000 39.13101 ? 43  GLN A CB     1 
ATOM   343  C  CG     . GLN A 1 47  ? -37.82700 -3.43300  33.93700  1.000 58.83074 ? 43  GLN A CG     1 
ATOM   344  C  CD     . GLN A 1 47  ? -37.95400 -4.90200  34.29800  1.000 70.08998 ? 43  GLN A CD     1 
ATOM   345  O  OE1    . GLN A 1 47  ? -38.98400 -5.53400  34.05100  1.000 74.41419 ? 43  GLN A OE1    1 
ATOM   346  N  NE2    . GLN A 1 47  ? -36.90000 -5.45500  34.88700  1.000 72.55607 ? 43  GLN A NE2    1 
ATOM   347  N  N      . PRO A 1 48  ? -35.48300 -2.25700  31.51000  1.000 30.34838 ? 44  PRO A N      1 
ATOM   348  C  CA     . PRO A 1 48  ? -34.37100 -2.87700  30.78200  1.000 28.59553 ? 44  PRO A CA     1 
ATOM   349  C  C      . PRO A 1 48  ? -34.22900 -4.34800  31.13800  1.000 28.97979 ? 44  PRO A C      1 
ATOM   350  O  O      . PRO A 1 48  ? -34.37600 -4.75100  32.29400  1.000 29.59302 ? 44  PRO A O      1 
ATOM   351  C  CB     . PRO A 1 48  ? -33.15100 -2.07100  31.24500  1.000 26.47423 ? 44  PRO A CB     1 
ATOM   352  C  CG     . PRO A 1 48  ? -33.49700 -1.63900  32.63700  1.000 23.98182 ? 44  PRO A CG     1 
ATOM   353  C  CD     . PRO A 1 48  ? -35.02800 -1.49400  32.68600  1.000 27.77175 ? 44  PRO A CD     1 
ATOM   354  N  N      . ILE A 1 49  ? -33.94000 -5.16400  30.13300  1.000 25.55833 ? 45  ILE A N      1 
ATOM   355  C  CA     . ILE A 1 49  ? -33.66300 -6.57400  30.35700  1.000 30.23257 ? 45  ILE A CA     1 
ATOM   356  C  C      . ILE A 1 49  ? -32.22800 -6.81300  29.91600  1.000 27.66121 ? 45  ILE A C      1 
ATOM   357  O  O      . ILE A 1 49  ? -31.90400 -6.66800  28.73100  1.000 29.38247 ? 45  ILE A O      1 
ATOM   358  C  CB     . ILE A 1 49  ? -34.63700 -7.49800  29.61400  1.000 28.86399 ? 45  ILE A CB     1 
ATOM   359  C  CG1    . ILE A 1 49  ? -36.07700 -7.28000  30.09300  1.000 21.64470 ? 45  ILE A CG1    1 
ATOM   360  C  CG2    . ILE A 1 49  ? -34.19800 -8.96400  29.75800  1.000 27.42434 ? 45  ILE A CG2    1 
ATOM   361  C  CD1    . ILE A 1 49  ? -36.37800 -7.78400  31.54500  1.000 21.99737 ? 45  ILE A CD1    1 
ATOM   362  N  N      . LEU A 1 50  ? -31.36400 -7.14600  30.87100  1.000 27.16642 ? 46  LEU A N      1 
ATOM   363  C  CA     . LEU A 1 50  ? -29.97800 -7.50000  30.58000  1.000 22.50270 ? 46  LEU A CA     1 
ATOM   364  C  C      . LEU A 1 50  ? -29.91900 -8.93100  30.05500  1.000 27.32433 ? 46  LEU A C      1 
ATOM   365  O  O      . LEU A 1 50  ? -30.34200 -9.86000  30.74800  1.000 28.55079 ? 46  LEU A O      1 
ATOM   366  C  CB     . LEU A 1 50  ? -29.12800 -7.36800  31.84400  1.000 23.38965 ? 46  LEU A CB     1 
ATOM   367  C  CG     . LEU A 1 50  ? -27.65300 -7.74300  31.69200  1.000 24.94773 ? 46  LEU A CG     1 
ATOM   368  C  CD1    . LEU A 1 50  ? -26.98200 -6.80900  30.68800  1.000 20.83408 ? 46  LEU A CD1    1 
ATOM   369  C  CD2    . LEU A 1 50  ? -26.92500 -7.71400  33.05500  1.000 25.48200 ? 46  LEU A CD2    1 
ATOM   370  N  N      . THR A 1 51  ? -29.37600 -9.11800  28.84500  1.000 23.70021 ? 47  THR A N      1 
ATOM   371  C  CA     . THR A 1 51  ? -29.21700 -10.44100 28.25800  1.000 25.29514 ? 47  THR A CA     1 
ATOM   372  C  C      . THR A 1 51  ? -27.75200 -10.90100 28.32000  1.000 26.26894 ? 47  THR A C      1 
ATOM   373  O  O      . THR A 1 51  ? -26.84900 -10.17500 28.75200  1.000 22.93696 ? 47  THR A O      1 
ATOM   374  C  CB     . THR A 1 51  ? -29.72300 -10.44300 26.81000  1.000 27.67174 ? 47  THR A CB     1 
ATOM   375  O  OG1    . THR A 1 51  ? -28.86100 -9.62900  25.99700  1.000 26.61109 ? 47  THR A OG1    1 
ATOM   376  C  CG2    . THR A 1 51  ? -31.16100 -9.90800  26.75300  1.000 23.28437 ? 47  THR A CG2    1 
ATOM   377  N  N      . LYS A 1 52  ? -27.52300 -12.14700 27.89400  1.000 22.77642 ? 48  LYS A N      1 
ATOM   378  C  CA     . LYS A 1 52  ? -26.19000 -12.72500 27.89500  1.000 27.07693 ? 48  LYS A CA     1 
ATOM   379  C  C      . LYS A 1 52  ? -25.41800 -12.42800 26.62100  1.000 30.52998 ? 48  LYS A C      1 
ATOM   380  O  O      . LYS A 1 52  ? -24.18300 -12.40300 26.65100  1.000 31.57221 ? 48  LYS A O      1 
ATOM   381  C  CB     . LYS A 1 52  ? -26.28300 -14.24800 28.08600  1.000 27.04008 ? 48  LYS A CB     1 
ATOM   382  C  CG     . LYS A 1 52  ? -26.88100 -14.64900 29.41900  1.000 24.81350 ? 48  LYS A CG     1 
ATOM   383  C  CD     . LYS A 1 52  ? -25.99100 -14.12800 30.55800  1.000 24.56084 ? 48  LYS A CD     1 
ATOM   384  C  CE     . LYS A 1 52  ? -26.76200 -13.30100 31.58600  1.000 32.46705 ? 48  LYS A CE     1 
ATOM   385  N  NZ     . LYS A 1 52  ? -28.12000 -13.81100 31.90000  1.000 44.30794 ? 48  LYS A NZ     1 
ATOM   386  N  N      . HIS A 1 53  ? -26.11300 -12.16600 25.51900  1.000 28.39288 ? 49  HIS A N      1 
ATOM   387  C  CA     . HIS A 1 53  ? -25.49900 -11.91500 24.22700  1.000 25.01089 ? 49  HIS A CA     1 
ATOM   388  C  C      . HIS A 1 53  ? -26.46100 -10.99600 23.48500  1.000 23.65547 ? 49  HIS A C      1 
ATOM   389  O  O      . HIS A 1 53  ? -27.67000 -11.15800 23.60100  1.000 25.58991 ? 49  HIS A O      1 
ATOM   390  C  CB     . HIS A 1 53  ? -25.26900 -13.25300 23.48200  1.000 23.26858 ? 49  HIS A CB     1 
ATOM   391  C  CG     . HIS A 1 53  ? -24.40100 -13.17100 22.26100  1.000 21.58680 ? 49  HIS A CG     1 
ATOM   392  N  ND1    . HIS A 1 53  ? -24.78700 -12.52000 21.10500  1.000 24.20027 ? 49  HIS A ND1    1 
ATOM   393  C  CD2    . HIS A 1 53  ? -23.18500 -13.72100 21.99300  1.000 26.45317 ? 49  HIS A CD2    1 
ATOM   394  C  CE1    . HIS A 1 53  ? -23.84300 -12.66200 20.18600  1.000 21.46836 ? 49  HIS A CE1    1 
ATOM   395  N  NE2    . HIS A 1 53  ? -22.85900 -13.38100 20.70000  1.000 22.46322 ? 49  HIS A NE2    1 
ATOM   396  N  N      . GLU A 1 54  ? -25.93300 -10.01700 22.75200  1.000 21.08411 ? 50  GLU A N      1 
ATOM   397  C  CA     . GLU A 1 54  ? -26.81400 -9.09500  22.04400  1.000 17.43104 ? 50  GLU A CA     1 
ATOM   398  C  C      . GLU A 1 54  ? -27.63800 -9.81400  20.98500  1.000 21.55258 ? 50  GLU A C      1 
ATOM   399  O  O      . GLU A 1 54  ? -28.71800 -9.33900  20.61000  1.000 21.60522 ? 50  GLU A O      1 
ATOM   400  C  CB     . GLU A 1 54  ? -26.00600 -7.96500  21.40100  1.000 18.66540 ? 50  GLU A CB     1 
ATOM   401  C  CG     . GLU A 1 54  ? -25.44800 -6.96500  22.40800  1.000 22.65272 ? 50  GLU A CG     1 
ATOM   402  C  CD     . GLU A 1 54  ? -24.05600 -7.36500  22.91400  1.000 31.87751 ? 50  GLU A CD     1 
ATOM   403  O  OE1    . GLU A 1 54  ? -23.38900 -6.51400  23.55500  1.000 28.21391 ? 50  GLU A OE1    1 
ATOM   404  O  OE2    . GLU A 1 54  ? -23.63600 -8.52700  22.67200  1.000 28.63238 ? 50  GLU A OE2    1 
ATOM   405  N  N      . GLU A 1 55  ? -27.13900 -10.93400 20.45900  1.000 16.65989 ? 51  GLU A N      1 
ATOM   406  C  CA     . GLU A 1 55  ? -27.97200 -11.72800 19.56400  1.000 24.53189 ? 51  GLU A CA     1 
ATOM   407  C  C      . GLU A 1 55  ? -29.23200 -12.19900 20.28800  1.000 23.73706 ? 51  GLU A C      1 
ATOM   408  O  O      . GLU A 1 55  ? -30.34700 -12.10300 19.75500  1.000 20.53141 ? 51  GLU A O      1 
ATOM   409  C  CB     . GLU A 1 55  ? -27.18400 -12.91500 19.00300  1.000 24.09499 ? 51  GLU A CB     1 
ATOM   410  C  CG     . GLU A 1 55  ? -27.95500 -13.64300 17.90900  1.000 29.41668 ? 51  GLU A CG     1 
ATOM   411  C  CD     . GLU A 1 55  ? -27.36900 -15.00100 17.54600  1.000 31.41429 ? 51  GLU A CD     1 
ATOM   412  O  OE1    . GLU A 1 55  ? -27.76500 -15.55400 16.49000  1.000 32.95132 ? 51  GLU A OE1    1 
ATOM   413  O  OE2    . GLU A 1 55  ? -26.52500 -15.51200 18.30500  1.000 30.05887 ? 51  GLU A OE2    1 
ATOM   414  N  N      . GLY A 1 56  ? -29.07200 -12.68900 21.52100  1.000 22.12107 ? 52  GLY A N      1 
ATOM   415  C  CA     . GLY A 1 56  ? -30.23000 -13.09200 22.30300  1.000 22.76589 ? 52  GLY A CA     1 
ATOM   416  C  C      . GLY A 1 56  ? -31.15600 -11.93100 22.59300  1.000 25.48990 ? 52  GLY A C      1 
ATOM   417  O  O      . GLY A 1 56  ? -32.37800 -12.10300 22.66500  1.000 25.16881 ? 52  GLY A O      1 
ATOM   418  N  N      . ALA A 1 57  ? -30.58900 -10.73000 22.78300  1.000 22.88432 ? 53  ALA A N      1 
ATOM   419  C  CA     . ALA A 1 57  ? -31.43800 -9.55700  22.97400  1.000 23.58704 ? 53  ALA A CA     1 
ATOM   420  C  C      . ALA A 1 57  ? -32.28200 -9.28100  21.73300  1.000 26.19788 ? 53  ALA A C      1 
ATOM   421  O  O      . ALA A 1 57  ? -33.49000 -9.03400  21.84300  1.000 23.87392 ? 53  ALA A O      1 
ATOM   422  C  CB     . ALA A 1 57  ? -30.60100 -8.32900  23.33900  1.000 24.28975 ? 53  ALA A CB     1 
ATOM   423  N  N      . ALA A 1 58  ? -31.67500 -9.36400  20.53700  1.000 21.83946 ? 54  ALA A N      1 
ATOM   424  C  CA     . ALA A 1 58  ? -32.44000 -9.11800  19.31900  1.000 19.19704 ? 54  ALA A CA     1 
ATOM   425  C  C      . ALA A 1 58  ? -33.50700 -10.18900 19.13000  1.000 25.94522 ? 54  ALA A C      1 
ATOM   426  O  O      . ALA A 1 58  ? -34.66200 -9.88100  18.78300  1.000 25.21618 ? 54  ALA A O      1 
ATOM   427  C  CB     . ALA A 1 58  ? -31.51000 -9.06700  18.10000  1.000 19.57077 ? 54  ALA A CB     1 
ATOM   428  N  N      . PHE A 1 59  ? -33.15000 -11.45100 19.37300  1.000 21.09990 ? 55  PHE A N      1 
ATOM   429  C  CA     . PHE A 1 59  ? -34.14500 -12.51800 19.31100  1.000 20.13399 ? 55  PHE A CA     1 
ATOM   430  C  C      . PHE A 1 59  ? -35.29600 -12.24400 20.27300  1.000 22.62903 ? 55  PHE A C      1 
ATOM   431  O  O      . PHE A 1 59  ? -36.47000 -12.41100 19.91900  1.000 23.38438 ? 55  PHE A O      1 
ATOM   432  C  CB     . PHE A 1 59  ? -33.49500 -13.86400 19.64100  1.000 18.55749 ? 55  PHE A CB     1 
ATOM   433  C  CG     . PHE A 1 59  ? -32.69100 -14.45200 18.51500  1.000 24.41609 ? 55  PHE A CG     1 
ATOM   434  C  CD1    . PHE A 1 59  ? -33.06200 -14.25100 17.19200  1.000 26.63740 ? 55  PHE A CD1    1 
ATOM   435  C  CD2    . PHE A 1 59  ? -31.56700 -15.22200 18.78200  1.000 23.71337 ? 55  PHE A CD2    1 
ATOM   436  C  CE1    . PHE A 1 59  ? -32.32400 -14.80800 16.14400  1.000 28.36130 ? 55  PHE A CE1    1 
ATOM   437  C  CE2    . PHE A 1 59  ? -30.81800 -15.79400 17.73800  1.000 25.02932 ? 55  PHE A CE2    1 
ATOM   438  C  CZ     . PHE A 1 59  ? -31.19900 -15.57900 16.41900  1.000 27.32696 ? 55  PHE A CZ     1 
ATOM   439  N  N      . MET A 1 60  ? -34.98100 -11.80000 21.49000  1.000 17.55474 ? 56  MET A N      1 
ATOM   440  C  CA     . MET A 1 60  ? -36.03500 -11.54600 22.47400  1.000 20.80249 ? 56  MET A CA     1 
ATOM   441  C  C      . MET A 1 60  ? -36.93400 -10.41300 22.03200  1.000 22.09475 ? 56  MET A C      1 
ATOM   442  O  O      . MET A 1 60  ? -38.16200 -10.48400 22.19200  1.000 23.36859 ? 56  MET A O      1 
ATOM   443  C  CB     . MET A 1 60  ? -35.42700 -11.20800 23.82900  1.000 21.54206 ? 56  MET A CB     1 
ATOM   444  C  CG     . MET A 1 60  ? -34.86200 -12.42200 24.53200  1.000 32.31966 ? 56  MET A CG     1 
ATOM   445  S  SD     . MET A 1 60  ? -34.21300 -11.96000 26.13000  1.000 37.06497 ? 56  MET A SD     1 
ATOM   446  C  CE     . MET A 1 60  ? -32.85900 -13.12400 26.25400  1.000 41.36812 ? 56  MET A CE     1 
ATOM   447  N  N      . ALA A 1 61  ? -36.34000 -9.32800  21.52700  1.000 23.84233 ? 57  ALA A N      1 
ATOM   448  C  CA     . ALA A 1 61  ? -37.15700 -8.24700  20.98500  1.000 24.46872 ? 57  ALA A CA     1 
ATOM   449  C  C      . ALA A 1 61  ? -38.06100 -8.77300  19.87500  1.000 24.45556 ? 57  ALA A C      1 
ATOM   450  O  O      . ALA A 1 61  ? -39.22000 -8.35500  19.74600  1.000 23.15541 ? 57  ALA A O      1 
ATOM   451  C  CB     . ALA A 1 61  ? -36.26000 -7.12100  20.46800  1.000 22.92117 ? 57  ALA A CB     1 
ATOM   452  N  N      . GLU A 1 62  ? -37.53600 -9.68800  19.05600  1.000 25.23460 ? 58  GLU A N      1 
ATOM   453  C  CA     . GLU A 1 62  ? -38.31900 -10.26000 17.96500  1.000 20.92356 ? 58  GLU A CA     1 
ATOM   454  C  C      . GLU A 1 62  ? -39.46900 -11.10900 18.49800  1.000 23.91339 ? 58  GLU A C      1 
ATOM   455  O  O      . GLU A 1 62  ? -40.60000 -11.02200 17.99300  1.000 24.68191 ? 58  GLU A O      1 
ATOM   456  C  CB     . GLU A 1 62  ? -37.40000 -11.07200 17.04700  1.000 25.28198 ? 58  GLU A CB     1 
ATOM   457  C  CG     . GLU A 1 62  ? -37.89800 -11.21200 15.60400  1.000 30.72737 ? 58  GLU A CG     1 
ATOM   458  C  CD     . GLU A 1 62  ? -38.88900 -12.37800 15.43400  1.000 44.21056 ? 58  GLU A CD     1 
ATOM   459  O  OE1    . GLU A 1 62  ? -38.98500 -13.23400 16.34800  1.000 44.66325 ? 58  GLU A OE1    1 
ATOM   460  O  OE2    . GLU A 1 62  ? -39.56400 -12.43900 14.37600  1.000 43.12622 ? 58  GLU A OE2    1 
ATOM   461  N  N      . GLY A 1 63  ? -39.19900 -11.94500 19.50600  1.000 20.72617 ? 59  GLY A N      1 
ATOM   462  C  CA     . GLY A 1 63  ? -40.26000 -12.74700 20.09200  1.000 19.49971 ? 59  GLY A CA     1 
ATOM   463  C  C      . GLY A 1 63  ? -41.29400 -11.88700 20.78500  1.000 29.57197 ? 59  GLY A C      1 
ATOM   464  O  O      . GLY A 1 63  ? -42.50000 -12.11400 20.64200  1.000 28.25602 ? 59  GLY A O      1 
ATOM   465  N  N      . TYR A 1 64  ? -40.83100 -10.87300 21.53100  1.000 23.30279 ? 60  TYR A N      1 
ATOM   466  C  CA     . TYR A 1 64  ? -41.74800 -9.92100  22.15200  1.000 22.03948 ? 60  TYR A CA     1 
ATOM   467  C  C      . TYR A 1 64  ? -42.64100 -9.24700  21.11400  1.000 22.11318 ? 60  TYR A C      1 
ATOM   468  O  O      . TYR A 1 64  ? -43.85300 -9.09500  21.31700  1.000 26.24788 ? 60  TYR A O      1 
ATOM   469  C  CB     . TYR A 1 64  ? -40.97100 -8.85400  22.92600  1.000 24.06868 ? 60  TYR A CB     1 
ATOM   470  C  CG     . TYR A 1 64  ? -41.90700 -7.92200  23.65500  1.000 28.24549 ? 60  TYR A CG     1 
ATOM   471  C  CD1    . TYR A 1 64  ? -42.42500 -6.78500  23.03800  1.000 24.95562 ? 60  TYR A CD1    1 
ATOM   472  C  CD2    . TYR A 1 64  ? -42.30700 -8.20700  24.94900  1.000 30.84844 ? 60  TYR A CD2    1 
ATOM   473  C  CE1    . TYR A 1 64  ? -43.31000 -5.95200  23.71700  1.000 30.47207 ? 60  TYR A CE1    1 
ATOM   474  C  CE2    . TYR A 1 64  ? -43.17900 -7.38500  25.62600  1.000 35.61743 ? 60  TYR A CE2    1 
ATOM   475  C  CZ     . TYR A 1 64  ? -43.67800 -6.26400  25.01100  1.000 36.84915 ? 60  TYR A CZ     1 
ATOM   476  O  OH     . TYR A 1 64  ? -44.55000 -5.46600  25.71900  1.000 51.16403 ? 60  TYR A OH     1 
ATOM   477  N  N      . ALA A 1 65  ? -42.04800 -8.79100  20.01400  1.000 23.51598 ? 61  ALA A N      1 
ATOM   478  C  CA     . ALA A 1 65  ? -42.82400 -8.10700  18.98000  1.000 23.90287 ? 61  ALA A CA     1 
ATOM   479  C  C      . ALA A 1 65  ? -43.86200 -9.04100  18.35300  1.000 25.91100 ? 61  ALA A C      1 
ATOM   480  O  O      . ALA A 1 65  ? -45.02100 -8.65900  18.15700  1.000 25.80836 ? 61  ALA A O      1 
ATOM   481  C  CB     . ALA A 1 65  ? -41.87300 -7.52100  17.91800  1.000 20.25506 ? 61  ALA A CB     1 
ATOM   482  N  N      . ARG A 1 66  ? -43.46300 -10.26800 18.00300  1.000 25.04248 ? 62  ARG A N      1 
ATOM   483  C  CA     . ARG A 1 66  ? -44.41500 -11.16300 17.34600  1.000 31.31691 ? 62  ARG A CA     1 
ATOM   484  C  C      . ARG A 1 66  ? -45.58600 -11.51600 18.26800  1.000 29.15613 ? 62  ARG A C      1 
ATOM   485  O  O      . ARG A 1 66  ? -46.74200 -11.53300 17.83800  1.000 27.65595 ? 62  ARG A O      1 
ATOM   486  C  CB     . ARG A 1 66  ? -43.70900 -12.42800 16.86300  1.000 25.56096 ? 62  ARG A CB     1 
ATOM   487  C  CG     . ARG A 1 66  ? -42.93900 -12.23300 15.54700  1.000 26.03733 ? 62  ARG A CG     1 
ATOM   488  C  CD     . ARG A 1 66  ? -42.55700 -13.57300 14.93700  1.000 27.85597 ? 62  ARG A CD     1 
ATOM   489  N  NE     . ARG A 1 66  ? -43.74900 -14.36400 14.62800  1.000 25.96364 ? 62  ARG A NE     1 
ATOM   490  C  CZ     . ARG A 1 66  ? -43.72000 -15.54700 14.02200  1.000 32.50390 ? 62  ARG A CZ     1 
ATOM   491  N  NH1    . ARG A 1 66  ? -42.55300 -16.07500 13.66800  1.000 27.34012 ? 62  ARG A NH1    1 
ATOM   492  N  NH2    . ARG A 1 66  ? -44.85500 -16.20500 13.76900  1.000 32.29071 ? 62  ARG A NH2    1 
ATOM   493  N  N      . VAL A 1 67  ? -45.30900 -11.80100 19.53600  1.000 27.51909 ? 63  VAL A N      1 
ATOM   494  C  CA     . VAL A 1 67  ? -46.38800 -12.17800 20.44000  1.000 26.63477 ? 63  VAL A CA     1 
ATOM   495  C  C      . VAL A 1 67  ? -47.22400 -10.95500 20.81300  1.000 30.96424 ? 63  VAL A C      1 
ATOM   496  O  O      . VAL A 1 67  ? -48.45600 -11.03300 20.88300  1.000 28.79819 ? 63  VAL A O      1 
ATOM   497  C  CB     . VAL A 1 67  ? -45.83100 -12.89900 21.68500  1.000 24.91351 ? 63  VAL A CB     1 
ATOM   498  C  CG1    . VAL A 1 67  ? -46.93300 -13.03500 22.76700  1.000 22.65272 ? 63  VAL A CG1    1 
ATOM   499  C  CG2    . VAL A 1 67  ? -45.29400 -14.27800 21.30700  1.000 20.17610 ? 63  VAL A CG2    1 
ATOM   500  N  N      . SER A 1 68  ? -46.58000 -9.80500  21.05800  1.000 25.83204 ? 64  SER A N      1 
ATOM   501  C  CA     . SER A 1 68  ? -47.34600 -8.63800  21.50000  1.000 31.40640 ? 64  SER A CA     1 
ATOM   502  C  C      . SER A 1 68  ? -48.10900 -7.95800  20.37000  1.000 30.01412 ? 64  SER A C      1 
ATOM   503  O  O      . SER A 1 68  ? -49.10400 -7.28400  20.64100  1.000 29.13244 ? 64  SER A O      1 
ATOM   504  C  CB     . SER A 1 68  ? -46.44000 -7.59500  22.16900  1.000 31.15110 ? 64  SER A CB     1 
ATOM   505  O  OG     . SER A 1 68  ? -45.59300 -6.95200  21.21300  1.000 32.24071 ? 64  SER A OG     1 
ATOM   506  N  N      . GLY A 1 69  ? -47.67800 -8.11600  19.12300  1.000 30.42207 ? 65  GLY A N      1 
ATOM   507  C  CA     . GLY A 1 69  ? -48.21400 -7.28400  18.06800  1.000 26.79269 ? 65  GLY A CA     1 
ATOM   508  C  C      . GLY A 1 69  ? -47.73400 -5.85200  18.09900  1.000 32.65128 ? 65  GLY A C      1 
ATOM   509  O  O      . GLY A 1 69  ? -48.25900 -5.01500  17.35700  1.000 34.53835 ? 65  GLY A O      1 
ATOM   510  N  N      . LYS A 1 70  ? -46.73400 -5.54700  18.91800  1.000 26.74794 ? 66  LYS A N      1 
ATOM   511  C  CA     . LYS A 1 70  ? -46.19800 -4.20400  19.07700  1.000 27.04535 ? 66  LYS A CA     1 
ATOM   512  C  C      . LYS A 1 70  ? -44.73100 -4.17400  18.63800  1.000 27.00061 ? 66  LYS A C      1 
ATOM   513  O  O      . LYS A 1 70  ? -44.16100 -5.18500  18.22000  1.000 32.51179 ? 66  LYS A O      1 
ATOM   514  C  CB     . LYS A 1 70  ? -46.34300 -3.74100  20.53100  1.000 30.48523 ? 66  LYS A CB     1 
ATOM   515  C  CG     . LYS A 1 70  ? -47.78900 -3.67400  20.99900  1.000 37.86507 ? 66  LYS A CG     1 
ATOM   516  C  CD     . LYS A 1 70  ? -47.90600 -2.82000  22.24200  1.000 46.36082 ? 66  LYS A CD     1 
ATOM   517  C  CE     . LYS A 1 70  ? -47.33200 -3.55000  23.45100  1.000 55.40138 ? 66  LYS A CE     1 
ATOM   518  N  NZ     . LYS A 1 70  ? -47.77300 -2.95400  24.75500  1.000 65.06043 ? 66  LYS A NZ     1 
ATOM   519  N  N      . LEU A 1 71  ? -44.11300 -3.00700  18.77800  1.000 24.77139 ? 67  LEU A N      1 
ATOM   520  C  CA     . LEU A 1 71  ? -42.70700 -2.82900  18.43100  1.000 29.75357 ? 67  LEU A CA     1 
ATOM   521  C  C      . LEU A 1 71  ? -41.80900 -3.46100  19.49700  1.000 30.91423 ? 67  LEU A C      1 
ATOM   522  O  O      . LEU A 1 71  ? -42.01400 -3.25000  20.69100  1.000 32.01700 ? 67  LEU A O      1 
ATOM   523  C  CB     . LEU A 1 71  ? -42.39800 -1.33600  18.30100  1.000 27.29011 ? 67  LEU A CB     1 
ATOM   524  C  CG     . LEU A 1 71  ? -40.94100 -0.96800  18.00800  1.000 28.37445 ? 67  LEU A CG     1 
ATOM   525  C  CD1    . LEU A 1 71  ? -40.62600 -1.17000  16.51900  1.000 26.37685 ? 67  LEU A CD1    1 
ATOM   526  C  CD2    . LEU A 1 71  ? -40.67400 0.46900   18.42900  1.000 30.60630 ? 67  LEU A CD2    1 
ATOM   527  N  N      . GLY A 1 72  ? -40.82300 -4.24600  19.07100  1.000 25.85310 ? 68  GLY A N      1 
ATOM   528  C  CA     . GLY A 1 72  ? -39.79600 -4.74900  19.96300  1.000 25.38199 ? 68  GLY A CA     1 
ATOM   529  C  C      . GLY A 1 72  ? -38.55600 -3.87800  19.87600  1.000 29.00611 ? 68  GLY A C      1 
ATOM   530  O  O      . GLY A 1 72  ? -38.22800 -3.36100  18.81400  1.000 25.20565 ? 68  GLY A O      1 
ATOM   531  N  N      . VAL A 1 73  ? -37.85300 -3.72400  21.00100  1.000 18.59960 ? 69  VAL A N      1 
ATOM   532  C  CA     . VAL A 1 73  ? -36.71600 -2.81700  21.06800  1.000 19.97082 ? 69  VAL A CA     1 
ATOM   533  C  C      . VAL A 1 73  ? -35.55100 -3.50900  21.75700  1.000 25.63728 ? 69  VAL A C      1 
ATOM   534  O  O      . VAL A 1 73  ? -35.70200 -4.06500  22.85200  1.000 24.39766 ? 69  VAL A O      1 
ATOM   535  C  CB     . VAL A 1 73  ? -37.04800 -1.50800  21.80200  1.000 25.53201 ? 69  VAL A CB     1 
ATOM   536  C  CG1    . VAL A 1 73  ? -35.83900 -0.55800  21.73500  1.000 21.36835 ? 69  VAL A CG1    1 
ATOM   537  C  CG2    . VAL A 1 73  ? -38.31600 -0.86100  21.22800  1.000 24.92930 ? 69  VAL A CG2    1 
ATOM   538  N  N      . CYS A 1 74  ? -34.39800 -3.50200  21.09300  1.000 22.31583 ? 70  CYS A N      1 
ATOM   539  C  CA     . CYS A 1 74  ? -33.15100 -3.98500  21.66500  1.000 17.93110 ? 70  CYS A CA     1 
ATOM   540  C  C      . CYS A 1 74  ? -32.09800 -2.89100  21.52200  1.000 18.45748 ? 70  CYS A C      1 
ATOM   541  O  O      . CYS A 1 74  ? -32.20700 -2.01400  20.66300  1.000 22.13423 ? 70  CYS A O      1 
ATOM   542  C  CB     . CYS A 1 74  ? -32.71800 -5.30500  21.01200  1.000 21.26308 ? 70  CYS A CB     1 
ATOM   543  S  SG     . CYS A 1 74  ? -32.60900 -5.26900  19.22600  1.000 42.26296 ? 70  CYS A SG     1 
ATOM   544  N  N      . CYS A 1 75  ? -31.11600 -2.88800  22.40700  1.000 24.30555 ? 71  CYS A N      1 
ATOM   545  C  CA     . CYS A 1 75  ? -30.05700 -1.89500  22.31000  1.000 20.04451 ? 71  CYS A CA     1 
ATOM   546  C  C      . CYS A 1 75  ? -28.68700 -2.56900  22.42900  1.000 26.83216 ? 71  CYS A C      1 
ATOM   547  O  O      . CYS A 1 75  ? -28.53500 -3.59800  23.08800  1.000 25.72940 ? 71  CYS A O      1 
ATOM   548  C  CB     . CYS A 1 75  ? -30.24300 -0.78800  23.34100  1.000 21.19201 ? 71  CYS A CB     1 
ATOM   549  S  SG     . CYS A 1 75  ? -30.16300 -1.39900  25.00800  1.000 31.42745 ? 71  CYS A SG     1 
ATOM   550  N  N      . ALA A 1 76  ? -27.69200 -2.00400  21.75000  1.000 25.97943 ? 72  ALA A N      1 
ATOM   551  C  CA     . ALA A 1 76  ? -26.33000 -2.51600  21.86100  1.000 26.26104 ? 72  ALA A CA     1 
ATOM   552  C  C      . ALA A 1 76  ? -25.34300 -1.36000  21.82600  1.000 25.88731 ? 72  ALA A C      1 
ATOM   553  O  O      . ALA A 1 76  ? -25.64500 -0.27100  21.32600  1.000 29.57723 ? 72  ALA A O      1 
ATOM   554  C  CB     . ALA A 1 76  ? -26.01200 -3.52000  20.73200  1.000 21.46047 ? 72  ALA A CB     1 
ATOM   555  N  N      . THR A 1 77  ? -24.16000 -1.59800  22.39200  1.000 26.17682 ? 73  THR A N      1 
ATOM   556  C  CA     . THR A 1 77  ? -23.12000 -0.58000  22.40300  1.000 26.24262 ? 73  THR A CA     1 
ATOM   557  C  C      . THR A 1 77  ? -22.39400 -0.52700  21.05100  1.000 23.98709 ? 73  THR A C      1 
ATOM   558  O  O      . THR A 1 77  ? -22.70400 -1.26300  20.11300  1.000 23.73706 ? 73  THR A O      1 
ATOM   559  C  CB     . THR A 1 77  ? -22.14300 -0.82800  23.54900  1.000 25.74256 ? 73  THR A CB     1 
ATOM   560  O  OG1    . THR A 1 77  ? -21.27700 0.29700   23.66100  1.000 24.45820 ? 73  THR A OG1    1 
ATOM   561  C  CG2    . THR A 1 77  ? -21.31900 -2.08500  23.30300  1.000 24.27923 ? 73  THR A CG2    1 
ATOM   562  N  N      . THR A 1 78  ? -21.42100 0.37400   20.95100  1.000 23.23436 ? 74  THR A N      1 
ATOM   563  C  CA     . THR A 1 78  ? -20.59200 0.53600   19.75400  1.000 28.77713 ? 74  THR A CA     1 
ATOM   564  C  C      . THR A 1 78  ? -20.01200 -0.78100  19.26400  1.000 29.07980 ? 74  THR A C      1 
ATOM   565  O  O      . THR A 1 78  ? -19.89900 -1.74200  20.03000  1.000 28.18233 ? 74  THR A O      1 
ATOM   566  C  CB     . THR A 1 78  ? -19.42400 1.49000   20.03000  1.000 23.99498 ? 74  THR A CB     1 
ATOM   567  O  OG1    . THR A 1 78  ? -18.95800 1.29200   21.37800  1.000 26.37421 ? 74  THR A OG1    1 
ATOM   568  C  CG2    . THR A 1 78  ? -19.83800 2.94500   19.83200  1.000 26.75058 ? 74  THR A CG2    1 
ATOM   569  N  N      . GLY A 1 79  ? -19.65300 -0.83500  17.98600  1.000 28.50605 ? 75  GLY A N      1 
ATOM   570  C  CA     . GLY A 1 79  ? -18.82500 -1.89900  17.46800  1.000 22.17634 ? 75  GLY A CA     1 
ATOM   571  C  C      . GLY A 1 79  ? -19.40200 -3.28300  17.67100  1.000 26.24525 ? 75  GLY A C      1 
ATOM   572  O  O      . GLY A 1 79  ? -20.45300 -3.64300  17.12200  1.000 27.59541 ? 75  GLY A O      1 
ATOM   573  N  N      . PRO A 1 80  ? -18.71400 -4.09600  18.47900  1.000 21.80261 ? 76  PRO A N      1 
ATOM   574  C  CA     . PRO A 1 80  ? -19.07700 -5.51800  18.55500  1.000 24.24238 ? 76  PRO A CA     1 
ATOM   575  C  C      . PRO A 1 80  ? -20.37900 -5.75500  19.28200  1.000 24.55821 ? 76  PRO A C      1 
ATOM   576  O  O      . PRO A 1 80  ? -20.99300 -6.81400  19.08000  1.000 25.74782 ? 76  PRO A O      1 
ATOM   577  C  CB     . PRO A 1 80  ? -17.90600 -6.14200  19.32600  1.000 22.47901 ? 76  PRO A CB     1 
ATOM   578  C  CG     . PRO A 1 80  ? -17.52000 -5.03200  20.27700  1.000 23.28174 ? 76  PRO A CG     1 
ATOM   579  C  CD     . PRO A 1 80  ? -17.68400 -3.73600  19.47200  1.000 20.69722 ? 76  PRO A CD     1 
ATOM   580  N  N      . GLY A 1 81  ? -20.80600 -4.83400  20.15000  1.000 21.05779 ? 77  GLY A N      1 
ATOM   581  C  CA     . GLY A 1 81  ? -22.14700 -4.95200  20.69900  1.000 28.32971 ? 77  GLY A CA     1 
ATOM   582  C  C      . GLY A 1 81  ? -23.19100 -5.00700  19.59700  1.000 23.87918 ? 77  GLY A C      1 
ATOM   583  O  O      . GLY A 1 81  ? -24.01500 -5.92300  19.54000  1.000 24.08973 ? 77  GLY A O      1 
ATOM   584  N  N      . ALA A 1 82  ? -23.14200 -4.03600  18.68600  1.000 27.15852 ? 78  ALA A N      1 
ATOM   585  C  CA     . ALA A 1 82  ? -24.11600 -3.96000  17.60000  1.000 24.88719 ? 78  ALA A CA     1 
ATOM   586  C  C      . ALA A 1 82  ? -23.95500 -5.10900  16.61800  1.000 28.67975 ? 78  ALA A C      1 
ATOM   587  O  O      . ALA A 1 82  ? -24.95500 -5.66700  16.14900  1.000 28.30076 ? 78  ALA A O      1 
ATOM   588  C  CB     . ALA A 1 82  ? -23.97900 -2.62300  16.87000  1.000 20.66827 ? 78  ALA A CB     1 
ATOM   589  N  N      . THR A 1 83  ? -22.71200 -5.47400  16.27300  1.000 23.12909 ? 79  THR A N      1 
ATOM   590  C  CA     . THR A 1 83  ? -22.56100 -6.55300  15.30400  1.000 26.72162 ? 79  THR A CA     1 
ATOM   591  C  C      . THR A 1 83  ? -23.05700 -7.86500  15.88300  1.000 21.87368 ? 79  THR A C      1 
ATOM   592  O  O      . THR A 1 83  ? -23.53300 -8.72600  15.13400  1.000 21.41046 ? 79  THR A O      1 
ATOM   593  C  CB     . THR A 1 83  ? -21.10700 -6.70100  14.81700  1.000 29.13770 ? 79  THR A CB     1 
ATOM   594  O  OG1    . THR A 1 83  ? -20.22000 -6.90500  15.93000  1.000 25.50043 ? 79  THR A OG1    1 
ATOM   595  C  CG2    . THR A 1 83  ? -20.67200 -5.47400  14.02700  1.000 21.61838 ? 79  THR A CG2    1 
ATOM   596  N  N      . ASN A 1 84  ? -22.98600 -8.02000  17.20900  1.000 20.04977 ? 80  ASN A N      1 
ATOM   597  C  CA     . ASN A 1 84  ? -23.50000 -9.23400  17.83500  1.000 22.13950 ? 80  ASN A CA     1 
ATOM   598  C  C      . ASN A 1 84  ? -25.01000 -9.36500  17.65000  1.000 24.16342 ? 80  ASN A C      1 
ATOM   599  O  O      . ASN A 1 84  ? -25.53400 -10.48100 17.62700  1.000 22.32110 ? 80  ASN A O      1 
ATOM   600  C  CB     . ASN A 1 84  ? -23.14500 -9.24700  19.32900  1.000 22.73430 ? 80  ASN A CB     1 
ATOM   601  C  CG     . ASN A 1 84  ? -21.87000 -10.03900 19.63900  1.000 26.15314 ? 80  ASN A CG     1 
ATOM   602  O  OD1    . ASN A 1 84  ? -21.16300 -10.48600 18.74000  1.000 22.63692 ? 80  ASN A OD1    1 
ATOM   603  N  ND2    . ASN A 1 84  ? -21.58400 -10.21700 20.93700  1.000 28.65607 ? 80  ASN A ND2    1 
ATOM   604  N  N      . ALA A 1 85  ? -25.72200 -8.24700  17.48800  1.000 19.24968 ? 81  ALA A N      1 
ATOM   605  C  CA     . ALA A 1 85  ? -27.17100 -8.29800  17.31300  1.000 22.99749 ? 81  ALA A CA     1 
ATOM   606  C  C      . ALA A 1 85  ? -27.59200 -8.67400  15.89900  1.000 23.02118 ? 81  ALA A C      1 
ATOM   607  O  O      . ALA A 1 85  ? -28.76300 -8.99000  15.68200  1.000 23.66863 ? 81  ALA A O      1 
ATOM   608  C  CB     . ALA A 1 85  ? -27.79600 -6.94200  17.65800  1.000 16.77570 ? 81  ALA A CB     1 
ATOM   609  N  N      . LEU A 1 86  ? -26.67000 -8.67200  14.93800  1.000 22.23161 ? 82  LEU A N      1 
ATOM   610  C  CA     . LEU A 1 86  ? -27.07900 -8.62700  13.53800  1.000 19.79974 ? 82  LEU A CA     1 
ATOM   611  C  C      . LEU A 1 86  ? -27.97100 -9.80500  13.16800  1.000 17.61790 ? 82  LEU A C      1 
ATOM   612  O  O      . LEU A 1 86  ? -28.97900 -9.63700  12.48200  1.000 22.74483 ? 82  LEU A O      1 
ATOM   613  C  CB     . LEU A 1 86  ? -25.86200 -8.58300  12.61900  1.000 24.96878 ? 82  LEU A CB     1 
ATOM   614  C  CG     . LEU A 1 86  ? -26.45200 -8.23100  11.24200  1.000 34.86997 ? 82  LEU A CG     1 
ATOM   615  C  CD1    . LEU A 1 86  ? -25.77100 -7.01400  10.58700  1.000 28.12969 ? 82  LEU A CD1    1 
ATOM   616  C  CD2    . LEU A 1 86  ? -26.47800 -9.43300  10.31000  1.000 32.11438 ? 82  LEU A CD2    1 
ATOM   617  N  N      . THR A 1 87  ? -27.59500 -11.01900 13.56400  1.000 19.09703 ? 83  THR A N      1 
ATOM   618  C  CA     . THR A 1 87  ? -28.40000 -12.16400 13.14900  1.000 19.50234 ? 83  THR A CA     1 
ATOM   619  C  C      . THR A 1 87  ? -29.85300 -12.01600 13.59800  1.000 26.37948 ? 83  THR A C      1 
ATOM   620  O  O      . THR A 1 87  ? -30.78200 -12.31700 12.83700  1.000 24.33713 ? 83  THR A O      1 
ATOM   621  C  CB     . THR A 1 87  ? -27.80400 -13.46200 13.68100  1.000 16.10193 ? 83  THR A CB     1 
ATOM   622  O  OG1    . THR A 1 87  ? -26.50900 -13.67500 13.09900  1.000 17.79161 ? 83  THR A OG1    1 
ATOM   623  C  CG2    . THR A 1 87  ? -28.72000 -14.64300 13.32000  1.000 19.59709 ? 83  THR A CG2    1 
ATOM   624  N  N      . GLY A 1 88  ? -30.07900 -11.55800 14.82700  1.000 16.56251 ? 84  GLY A N      1 
ATOM   625  C  CA     . GLY A 1 88  ? -31.45200 -11.41300 15.27700  1.000 16.70200 ? 84  GLY A CA     1 
ATOM   626  C  C      . GLY A 1 88  ? -32.20600 -10.38800 14.45300  1.000 21.70260 ? 84  GLY A C      1 
ATOM   627  O  O      . GLY A 1 88  ? -33.35900 -10.60400 14.07700  1.000 24.43188 ? 84  GLY A O      1 
ATOM   628  N  N      . ILE A 1 89  ? -31.54400 -9.28200  14.11500  1.000 21.45520 ? 85  ILE A N      1 
ATOM   629  C  CA     . ILE A 1 89  ? -32.16700 -8.26800  13.27400  1.000 22.32373 ? 85  ILE A CA     1 
ATOM   630  C  C      . ILE A 1 89  ? -32.44700 -8.81900  11.88100  1.000 28.07179 ? 85  ILE A C      1 
ATOM   631  O  O      . ILE A 1 89  ? -33.48500 -8.51900  11.28600  1.000 23.21594 ? 85  ILE A O      1 
ATOM   632  C  CB     . ILE A 1 89  ? -31.28900 -7.01200  13.21800  1.000 22.33162 ? 85  ILE A CB     1 
ATOM   633  C  CG1    . ILE A 1 89  ? -31.07200 -6.45500  14.64000  1.000 17.92320 ? 85  ILE A CG1    1 
ATOM   634  C  CG2    . ILE A 1 89  ? -31.92000 -5.96500  12.29200  1.000 15.80979 ? 85  ILE A CG2    1 
ATOM   635  C  CD1    . ILE A 1 89  ? -32.33500 -6.18800  15.41000  1.000 21.96053 ? 85  ILE A CD1    1 
ATOM   636  N  N      . ALA A 1 90  ? -31.53600 -9.63400  11.34100  1.000 21.91052 ? 86  ALA A N      1 
ATOM   637  C  CA     . ALA A 1 90  ? -31.77000 -10.22800 10.03200  1.000 23.76338 ? 86  ALA A CA     1 
ATOM   638  C  C      . ALA A 1 90  ? -32.96900 -11.17000 10.06100  1.000 25.96627 ? 86  ALA A C      1 
ATOM   639  O  O      . ALA A 1 90  ? -33.69200 -11.28400 9.05700   1.000 22.93433 ? 86  ALA A O      1 
ATOM   640  C  CB     . ALA A 1 90  ? -30.51700 -10.97400 9.55400   1.000 21.61838 ? 86  ALA A CB     1 
ATOM   641  N  N      . CYS A 1 91  ? -33.24200 -11.81400 11.20100  1.000 24.00551 ? 87  CYS A N      1 
ATOM   642  C  CA     . CYS A 1 91  ? -34.41500 -12.68900 11.24600  1.000 27.02956 ? 87  CYS A CA     1 
ATOM   643  C  C      . CYS A 1 91  ? -35.70800 -11.88600 11.29800  1.000 27.70595 ? 87  CYS A C      1 
ATOM   644  O  O      . CYS A 1 91  ? -36.67000 -12.19900 10.58600  1.000 22.77115 ? 87  CYS A O      1 
ATOM   645  C  CB     . CYS A 1 91  ? -34.34900 -13.60300 12.47200  1.000 27.82702 ? 87  CYS A CB     1 
ATOM   646  S  SG     . CYS A 1 91  ? -33.02600 -14.81200 12.49100  1.000 30.70368 ? 87  CYS A SG     1 
ATOM   647  N  N      . ALA A 1 92  ? -35.69200 -10.78600 12.04400  1.000 22.66588 ? 88  ALA A N      1 
ATOM   648  C  CA     . ALA A 1 92  ? -36.82900 -9.87700  12.02800  1.000 19.64972 ? 88  ALA A CA     1 
ATOM   649  C  C      . ALA A 1 92  ? -37.08000 -9.37700  10.61800  1.000 24.03183 ? 88  ALA A C      1 
ATOM   650  O  O      . ALA A 1 92  ? -38.22700 -9.29700  10.16300  1.000 23.57651 ? 88  ALA A O      1 
ATOM   651  C  CB     . ALA A 1 92  ? -36.56100 -8.69900  12.96000  1.000 16.91519 ? 88  ALA A CB     1 
ATOM   652  N  N      . TYR A 1 93  ? -36.00400 -9.06600  9.90000   1.000 20.35507 ? 89  TYR A N      1 
ATOM   653  C  CA     . TYR A 1 93  ? -36.15300 -8.61300  8.53100   1.000 22.06317 ? 89  TYR A CA     1 
ATOM   654  C  C      . TYR A 1 93  ? -36.79700 -9.68900  7.67200   1.000 19.10755 ? 89  TYR A C      1 
ATOM   655  O  O      . TYR A 1 93  ? -37.70900 -9.40500  6.89100   1.000 23.09751 ? 89  TYR A O      1 
ATOM   656  C  CB     . TYR A 1 93  ? -34.78000 -8.22000  8.00200   1.000 26.84532 ? 89  TYR A CB     1 
ATOM   657  C  CG     . TYR A 1 93  ? -34.75400 -7.71800  6.59000   1.000 26.54266 ? 89  TYR A CG     1 
ATOM   658  C  CD1    . TYR A 1 93  ? -35.07900 -6.39300  6.29300   1.000 22.90011 ? 89  TYR A CD1    1 
ATOM   659  C  CD2    . TYR A 1 93  ? -34.35600 -8.55700  5.55100   1.000 21.69471 ? 89  TYR A CD2    1 
ATOM   660  C  CE1    . TYR A 1 93  ? -35.02400 -5.92500  4.98900   1.000 26.35316 ? 89  TYR A CE1    1 
ATOM   661  C  CE2    . TYR A 1 93  ? -34.30000 -8.10500  4.25200   1.000 27.42171 ? 89  TYR A CE2    1 
ATOM   662  C  CZ     . TYR A 1 93  ? -34.63700 -6.79400  3.97300   1.000 29.64829 ? 89  TYR A CZ     1 
ATOM   663  O  OH     . TYR A 1 93  ? -34.55900 -6.36000  2.67800   1.000 33.59613 ? 89  TYR A OH     1 
ATOM   664  N  N      . SER A 1 94  ? -36.36000 -10.94300 7.83700   1.000 20.69985 ? 90  SER A N      1 
ATOM   665  C  CA     . SER A 1 94  ? -36.86800 -12.02600 7.00200   1.000 21.07884 ? 90  SER A CA     1 
ATOM   666  C  C      . SER A 1 94  ? -38.28300 -12.42700 7.40400   1.000 23.89497 ? 90  SER A C      1 
ATOM   667  O  O      . SER A 1 94  ? -39.04000 -12.91500 6.56100   1.000 26.24525 ? 90  SER A O      1 
ATOM   668  C  CB     . SER A 1 94  ? -35.94900 -13.24500 7.09400   1.000 22.98433 ? 90  SER A CB     1 
ATOM   669  O  OG     . SER A 1 94  ? -34.62100 -12.90600 6.70200   1.000 35.03841 ? 90  SER A OG     1 
ATOM   670  N  N      . ASP A 1 95  ? -38.68100 -12.18900 8.65600   1.000 20.03135 ? 91  ASP A N      1 
ATOM   671  C  CA     . ASP A 1 95  ? -40.02100 -12.53500 9.11400   1.000 26.79005 ? 91  ASP A CA     1 
ATOM   672  C  C      . ASP A 1 95  ? -40.97000 -11.33600 9.16000   1.000 26.22156 ? 91  ASP A C      1 
ATOM   673  O  O      . ASP A 1 95  ? -42.11100 -11.48400 9.60900   1.000 29.02980 ? 91  ASP A O      1 
ATOM   674  C  CB     . ASP A 1 95  ? -39.94800 -13.20500 10.49500  1.000 21.92631 ? 91  ASP A CB     1 
ATOM   675  C  CG     . ASP A 1 95  ? -39.28600 -14.60900 10.44500  1.000 33.39874 ? 91  ASP A CG     1 
ATOM   676  O  OD1    . ASP A 1 95  ? -39.30900 -15.26200 9.37100   1.000 31.14321 ? 91  ASP A OD1    1 
ATOM   677  O  OD2    . ASP A 1 95  ? -38.74100 -15.06500 11.47900  1.000 36.06748 ? 91  ASP A OD2    1 
ATOM   678  N  N      . SER A 1 96  ? -40.53800 -10.16300 8.68400   1.000 22.37374 ? 92  SER A N      1 
ATOM   679  C  CA     . SER A 1 96  ? -41.36200 -8.94600  8.68300   1.000 22.06844 ? 92  SER A CA     1 
ATOM   680  C  C      . SER A 1 96  ? -41.85100 -8.58600  10.08900  1.000 25.56886 ? 92  SER A C      1 
ATOM   681  O  O      . SER A 1 96  ? -43.03100 -8.30600  10.31500  1.000 24.27396 ? 92  SER A O      1 
ATOM   682  C  CB     . SER A 1 96  ? -42.53100 -9.08300  7.71200   1.000 22.57113 ? 92  SER A CB     1 
ATOM   683  O  OG     . SER A 1 96  ? -42.05500 -9.46600  6.42900   1.000 30.83528 ? 92  SER A OG     1 
ATOM   684  N  N      . THR A 1 97  ? -40.91400 -8.57100  11.03800  1.000 27.95862 ? 93  THR A N      1 
ATOM   685  C  CA     . THR A 1 97  ? -41.18300 -8.21000  12.42100  1.000 21.59996 ? 93  THR A CA     1 
ATOM   686  C  C      . THR A 1 97  ? -40.64600 -6.82100  12.73400  1.000 23.72916 ? 93  THR A C      1 
ATOM   687  O  O      . THR A 1 97  ? -39.46900 -6.54600  12.46900  1.000 24.43977 ? 93  THR A O      1 
ATOM   688  C  CB     . THR A 1 97  ? -40.54700 -9.22800  13.36100  1.000 24.78192 ? 93  THR A CB     1 
ATOM   689  O  OG1    . THR A 1 97  ? -40.94600 -10.54800 12.97500  1.000 27.60857 ? 93  THR A OG1    1 
ATOM   690  C  CG2    . THR A 1 97  ? -40.95700 -8.95400  14.81100  1.000 25.39515 ? 93  THR A CG2    1 
ATOM   691  N  N      . PRO A 1 98  ? -41.45200 -5.93900  13.34000  1.000 25.23460 ? 94  PRO A N      1 
ATOM   692  C  CA     . PRO A 1 98  ? -40.95200 -4.59500  13.67500  1.000 22.98433 ? 94  PRO A CA     1 
ATOM   693  C  C      . PRO A 1 98  ? -40.07000 -4.60000  14.91400  1.000 27.97441 ? 94  PRO A C      1 
ATOM   694  O  O      . PRO A 1 98  ? -40.57200 -4.65500  16.04100  1.000 26.14261 ? 94  PRO A O      1 
ATOM   695  C  CB     . PRO A 1 98  ? -42.23600 -3.78200  13.89900  1.000 24.14763 ? 94  PRO A CB     1 
ATOM   696  C  CG     . PRO A 1 98  ? -43.25100 -4.78300  14.32200  1.000 24.09499 ? 94  PRO A CG     1 
ATOM   697  C  CD     . PRO A 1 98  ? -42.90900 -6.05500  13.54600  1.000 23.15541 ? 94  PRO A CD     1 
ATOM   698  N  N      . VAL A 1 99  ? -38.75200 -4.57400  14.71500  1.000 28.86662 ? 95  VAL A N      1 
ATOM   699  C  CA     . VAL A 1 99  ? -37.78500 -4.53200  15.80700  1.000 26.87427 ? 95  VAL A CA     1 
ATOM   700  C  C      . VAL A 1 99  ? -36.94200 -3.28900  15.62000  1.000 27.15589 ? 95  VAL A C      1 
ATOM   701  O  O      . VAL A 1 99  ? -36.44100 -3.03100  14.52000  1.000 24.21606 ? 95  VAL A O      1 
ATOM   702  C  CB     . VAL A 1 99  ? -36.90800 -5.79700  15.86000  1.000 23.90287 ? 95  VAL A CB     1 
ATOM   703  C  CG1    . VAL A 1 99  ? -35.78000 -5.64700  16.90500  1.000 20.81565 ? 95  VAL A CG1    1 
ATOM   704  C  CG2    . VAL A 1 99  ? -37.77500 -7.00500  16.20200  1.000 25.19513 ? 95  VAL A CG2    1 
ATOM   705  N  N      . LEU A 1 100 ? -36.83700 -2.49200  16.66800  1.000 25.61097 ? 96  LEU A N      1 
ATOM   706  C  CA     . LEU A 1 100 ? -35.97300 -1.32100  16.65900  1.000 23.82391 ? 96  LEU A CA     1 
ATOM   707  C  C      . LEU A 1 100 ? -34.68200 -1.67100  17.40300  1.000 28.35866 ? 96  LEU A C      1 
ATOM   708  O  O      . LEU A 1 100 ? -34.72700 -2.06800  18.58300  1.000 22.67640 ? 96  LEU A O      1 
ATOM   709  C  CB     . LEU A 1 100 ? -36.67800 -0.11800  17.28800  1.000 21.72103 ? 96  LEU A CB     1 
ATOM   710  C  CG     . LEU A 1 100 ? -35.82200 1.11200   17.60300  1.000 25.84257 ? 96  LEU A CG     1 
ATOM   711  C  CD1    . LEU A 1 100 ? -35.18400 1.72400   16.34300  1.000 27.26380 ? 96  LEU A CD1    1 
ATOM   712  C  CD2    . LEU A 1 100 ? -36.66400 2.15000   18.32400  1.000 23.60809 ? 96  LEU A CD2    1 
ATOM   713  N  N      . LEU A 1 101 ? -33.54500 -1.56300  16.70100  1.000 22.43690 ? 97  LEU A N      1 
ATOM   714  C  CA     . LEU A 1 101 ? -32.21800 -1.69400  17.30600  1.000 28.29550 ? 97  LEU A CA     1 
ATOM   715  C  C      . LEU A 1 101 ? -31.61700 -0.30200  17.49900  1.000 21.24202 ? 97  LEU A C      1 
ATOM   716  O  O      . LEU A 1 101 ? -31.38000 0.42200   16.52300  1.000 23.43439 ? 97  LEU A O      1 
ATOM   717  C  CB     . LEU A 1 101 ? -31.28800 -2.55700  16.44600  1.000 26.75584 ? 97  LEU A CB     1 
ATOM   718  C  CG     . LEU A 1 101 ? -29.81400 -2.62500  16.89800  1.000 26.12418 ? 97  LEU A CG     1 
ATOM   719  C  CD1    . LEU A 1 101 ? -29.68500 -3.27100  18.27600  1.000 23.49229 ? 97  LEU A CD1    1 
ATOM   720  C  CD2    . LEU A 1 101 ? -28.92300 -3.37200  15.88500  1.000 20.73406 ? 97  LEU A CD2    1 
ATOM   721  N  N      . LEU A 1 102 ? -31.38500 0.07100   18.75200  1.000 17.45472 ? 98  LEU A N      1 
ATOM   722  C  CA     . LEU A 1 102 ? -30.68400 1.30000   19.09500  1.000 20.71301 ? 98  LEU A CA     1 
ATOM   723  C  C      . LEU A 1 102 ? -29.21600 0.96100   19.34000  1.000 27.12957 ? 98  LEU A C      1 
ATOM   724  O  O      . LEU A 1 102 ? -28.90200 0.17000   20.23600  1.000 24.75560 ? 98  LEU A O      1 
ATOM   725  C  CB     . LEU A 1 102 ? -31.26900 1.94000   20.35400  1.000 25.10827 ? 98  LEU A CB     1 
ATOM   726  C  CG     . LEU A 1 102 ? -32.78700 2.08800   20.35800  1.000 30.55893 ? 98  LEU A CG     1 
ATOM   727  C  CD1    . LEU A 1 102 ? -33.26800 2.52900   21.74400  1.000 26.67688 ? 98  LEU A CD1    1 
ATOM   728  C  CD2    . LEU A 1 102 ? -33.20000 3.08900   19.27000  1.000 25.40041 ? 98  LEU A CD2    1 
ATOM   729  N  N      . THR A 1 103 ? -28.31500 1.57500   18.58500  1.000 24.97668 ? 99  THR A N      1 
ATOM   730  C  CA     . THR A 1 103 ? -26.89800 1.34700   18.83200  1.000 27.72964 ? 99  THR A CA     1 
ATOM   731  C  C      . THR A 1 103 ? -26.23000 2.64700   19.24100  1.000 25.33462 ? 99  THR A C      1 
ATOM   732  O  O      . THR A 1 103 ? -26.65100 3.73400   18.84300  1.000 22.44480 ? 99  THR A O      1 
ATOM   733  C  CB     . THR A 1 103 ? -26.16700 0.77100   17.61100  1.000 23.01855 ? 99  THR A CB     1 
ATOM   734  O  OG1    . THR A 1 103 ? -26.25800 1.68200   16.50400  1.000 25.25566 ? 99  THR A OG1    1 
ATOM   735  C  CG2    . THR A 1 103 ? -26.74900 -0.57800  17.21600  1.000 19.97608 ? 99  THR A CG2    1 
ATOM   736  N  N      . ALA A 1 104 ? -25.19900 2.52500   20.06200  1.000 21.88683 ? 100 ALA A N      1 
ATOM   737  C  CA     . ALA A 1 104 ? -24.42400 3.69900   20.41300  1.000 25.51622 ? 100 ALA A CA     1 
ATOM   738  C  C      . ALA A 1 104 ? -23.34600 3.96700   19.36200  1.000 26.80848 ? 100 ALA A C      1 
ATOM   739  O  O      . ALA A 1 104 ? -22.91600 3.08000   18.61600  1.000 23.80285 ? 100 ALA A O      1 
ATOM   740  C  CB     . ALA A 1 104 ? -23.78600 3.53300   21.79000  1.000 23.31859 ? 100 ALA A CB     1 
ATOM   741  N  N      . GLN A 1 105 ? -22.91000 5.21300   19.32600  1.000 25.49253 ? 101 GLN A N      1 
ATOM   742  C  CA     . GLN A 1 105 ? -21.83900 5.67300   18.46300  1.000 26.48212 ? 101 GLN A CA     1 
ATOM   743  C  C      . GLN A 1 105 ? -20.89700 6.50800   19.31900  1.000 30.09571 ? 101 GLN A C      1 
ATOM   744  O  O      . GLN A 1 105 ? -21.32200 7.10200   20.31500  1.000 26.99008 ? 101 GLN A O      1 
ATOM   745  C  CB     . GLN A 1 105 ? -22.40700 6.49800   17.30200  1.000 23.37649 ? 101 GLN A CB     1 
ATOM   746  C  CG     . GLN A 1 105 ? -21.36900 7.07600   16.36200  1.000 26.08997 ? 101 GLN A CG     1 
ATOM   747  C  CD     . GLN A 1 105 ? -20.61500 5.98600   15.64700  1.000 33.30399 ? 101 GLN A CD     1 
ATOM   748  O  OE1    . GLN A 1 105 ? -19.48200 5.67000   16.00200  1.000 30.04308 ? 101 GLN A OE1    1 
ATOM   749  N  NE2    . GLN A 1 105 ? -21.25700 5.37200   14.65300  1.000 33.69878 ? 101 GLN A NE2    1 
ATOM   750  N  N      . VAL A 1 106 ? -19.61300 6.54100   18.95400  1.000 25.36094 ? 102 VAL A N      1 
ATOM   751  C  CA     . VAL A 1 106 ? -18.66700 7.37000   19.70600  1.000 29.70093 ? 102 VAL A CA     1 
ATOM   752  C  C      . VAL A 1 106 ? -19.03900 8.83300   19.50700  1.000 28.94821 ? 102 VAL A C      1 
ATOM   753  O  O      . VAL A 1 106 ? -19.80300 9.16300   18.59500  1.000 31.70907 ? 102 VAL A O      1 
ATOM   754  C  CB     . VAL A 1 106 ? -17.21100 7.11300   19.27800  1.000 28.54026 ? 102 VAL A CB     1 
ATOM   755  C  CG1    . VAL A 1 106 ? -16.84400 5.65900   19.54000  1.000 25.61360 ? 102 VAL A CG1    1 
ATOM   756  C  CG2    . VAL A 1 106 ? -17.02700 7.45800   17.79300  1.000 24.94773 ? 102 VAL A CG2    1 
ATOM   757  N  N      . GLY A 1 107 ? -18.47900 9.71800   20.32800  1.000 34.73838 ? 103 GLY A N      1 
ATOM   758  C  CA     . GLY A 1 107 ? -18.72700 11.14200  20.15700  1.000 34.42518 ? 103 GLY A CA     1 
ATOM   759  C  C      . GLY A 1 107 ? -18.11800 11.65900  18.86300  1.000 35.42004 ? 103 GLY A C      1 
ATOM   760  O  O      . GLY A 1 107 ? -17.05500 11.20600  18.42400  1.000 31.27217 ? 103 GLY A O      1 
ATOM   761  N  N      . THR A 1 108 ? -18.81600 12.62300  18.24600  1.000 37.58872 ? 104 THR A N      1 
ATOM   762  C  CA     . THR A 1 108 ? -18.42100 13.14400  16.93300  1.000 40.31799 ? 104 THR A CA     1 
ATOM   763  C  C      . THR A 1 108 ? -16.98800 13.68200  16.92200  1.000 40.37063 ? 104 THR A C      1 
ATOM   764  O  O      . THR A 1 108 ? -16.30400 13.60400  15.89000  1.000 41.99714 ? 104 THR A O      1 
ATOM   765  C  CB     . THR A 1 108 ? -19.39700 14.23300  16.48200  1.000 40.28904 ? 104 THR A CB     1 
ATOM   766  O  OG1    . THR A 1 108 ? -19.23700 15.39100  17.31100  1.000 48.51108 ? 104 THR A OG1    1 
ATOM   767  C  CG2    . THR A 1 108 ? -20.82700 13.74900  16.60200  1.000 43.95790 ? 104 THR A CG2    1 
ATOM   768  N  N      . ALA A 1 109 ? -16.52400 14.25500  18.03800  1.000 41.43128 ? 105 ALA A N      1 
ATOM   769  C  CA     . ALA A 1 109 ? -15.18300 14.82900  18.09300  1.000 41.22863 ? 105 ALA A CA     1 
ATOM   770  C  C      . ALA A 1 109 ? -14.08400 13.79000  17.91600  1.000 39.70476 ? 105 ALA A C      1 
ATOM   771  O  O      . ALA A 1 109 ? -12.92400 14.16200  17.72900  1.000 34.47782 ? 105 ALA A O      1 
ATOM   772  C  CB     . ALA A 1 109 ? -14.97900 15.55600  19.42000  1.000 40.08902 ? 105 ALA A CB     1 
ATOM   773  N  N      . ALA A 1 110 ? -14.41300 12.50700  17.98600  1.000 33.91459 ? 106 ALA A N      1 
ATOM   774  C  CA     . ALA A 1 110 ? -13.42900 11.45400  17.81800  1.000 32.95921 ? 106 ALA A CA     1 
ATOM   775  C  C      . ALA A 1 110 ? -13.52200 10.77900  16.45400  1.000 32.67234 ? 106 ALA A C      1 
ATOM   776  O  O      . ALA A 1 110 ? -12.72200 9.88400   16.17000  1.000 33.37505 ? 106 ALA A O      1 
ATOM   777  C  CB     . ALA A 1 110 ? -13.59100 10.41200  18.93300  1.000 32.75130 ? 106 ALA A CB     1 
ATOM   778  N  N      . PHE A 1 111 ? -14.46300 11.19700  15.60100  1.000 25.66360 ? 107 PHE A N      1 
ATOM   779  C  CA     . PHE A 1 111 ? -14.63100 10.56600  14.29100  1.000 30.67210 ? 107 PHE A CA     1 
ATOM   780  C  C      . PHE A 1 111 ? -13.32700 10.60400  13.50500  1.000 29.38247 ? 107 PHE A C      1 
ATOM   781  O  O      . PHE A 1 111 ? -12.68400 11.65500  13.39200  1.000 25.43463 ? 107 PHE A O      1 
ATOM   782  C  CB     . PHE A 1 111 ? -15.73400 11.27000  13.48300  1.000 33.74615 ? 107 PHE A CB     1 
ATOM   783  C  CG     . PHE A 1 111 ? -17.13400 10.90200  13.89600  1.000 34.40412 ? 107 PHE A CG     1 
ATOM   784  C  CD1    . PHE A 1 111 ? -17.38500 10.27900  15.11400  1.000 37.16498 ? 107 PHE A CD1    1 
ATOM   785  C  CD2    . PHE A 1 111 ? -18.20200 11.18600  13.06200  1.000 37.81769 ? 107 PHE A CD2    1 
ATOM   786  C  CE1    . PHE A 1 111 ? -18.68800 9.94600   15.49300  1.000 37.73084 ? 107 PHE A CE1    1 
ATOM   787  C  CE2    . PHE A 1 111 ? -19.50200 10.85300  13.42300  1.000 39.21786 ? 107 PHE A CE2    1 
ATOM   788  C  CZ     . PHE A 1 111 ? -19.74800 10.23400  14.64200  1.000 39.98901 ? 107 PHE A CZ     1 
ATOM   789  N  N      . GLY A 1 112 ? -12.93700 9.44700   12.96300  1.000 28.08231 ? 108 GLY A N      1 
ATOM   790  C  CA     . GLY A 1 112 ? -11.76700 9.36200   12.11400  1.000 34.60941 ? 108 GLY A CA     1 
ATOM   791  C  C      . GLY A 1 112 ? -10.43500 9.39200   12.83200  1.000 35.96221 ? 108 GLY A C      1 
ATOM   792  O  O      . GLY A 1 112 ? -9.39600  9.40900   12.15800  1.000 35.21475 ? 108 GLY A O      1 
ATOM   793  N  N      . LYS A 1 113 ? -10.42300 9.40000   14.16700  1.000 30.99845 ? 109 LYS A N      1 
ATOM   794  C  CA     . LYS A 1 113 ? -9.17500  9.41300   14.92700  1.000 32.11964 ? 109 LYS A CA     1 
ATOM   795  C  C      . LYS A 1 113 ? -8.79500  8.04100   15.47300  1.000 33.49349 ? 109 LYS A C      1 
ATOM   796  O  O      . LYS A 1 113 ? -7.73400  7.90600   16.09300  1.000 34.98051 ? 109 LYS A O      1 
ATOM   797  C  CB     . LYS A 1 113 ? -9.25200  10.42800  16.08600  1.000 30.04571 ? 109 LYS A CB     1 
ATOM   798  C  CG     . LYS A 1 113 ? -9.56000  11.86600  15.65600  1.000 31.46956 ? 109 LYS A CG     1 
ATOM   799  C  CD     . LYS A 1 113 ? -9.48000  12.84800  16.83500  1.000 32.89079 ? 109 LYS A CD     1 
ATOM   800  C  CE     . LYS A 1 113 ? -8.04800  13.07500  17.29100  1.000 34.37517 ? 109 LYS A CE     1 
ATOM   801  N  NZ     . LYS A 1 113 ? -7.22100  13.57900  16.17400  1.000 36.74914 ? 109 LYS A NZ     1 
ATOM   802  N  N      . GLY A 1 114 ? -9.62900  7.02500   15.26600  1.000 27.62700 ? 110 GLY A N      1 
ATOM   803  C  CA     . GLY A 1 114 ? -9.35000  5.72500   15.84200  1.000 26.93481 ? 110 GLY A CA     1 
ATOM   804  C  C      . GLY A 1 114 ? -9.94600  5.64000   17.23400  1.000 33.81984 ? 110 GLY A C      1 
ATOM   805  O  O      . GLY A 1 114 ? -9.27400  5.27100   18.20400  1.000 31.17742 ? 110 GLY A O      1 
ATOM   806  N  N      . ALA A 1 115 ? -11.21500 6.01200   17.34500  1.000 31.23006 ? 111 ALA A N      1 
ATOM   807  C  CA     . ALA A 1 115 ? -11.87100 5.96900   18.63800  1.000 31.13268 ? 111 ALA A CA     1 
ATOM   808  C  C      . ALA A 1 115 ? -12.07800 4.52300   19.06700  1.000 27.11115 ? 111 ALA A C      1 
ATOM   809  O  O      . ALA A 1 115 ? -12.08200 3.59300   18.25500  1.000 24.36345 ? 111 ALA A O      1 
ATOM   810  C  CB     . ALA A 1 115 ? -13.20500 6.71400   18.59200  1.000 31.77486 ? 111 ALA A CB     1 
ATOM   811  N  N      . LEU A 1 116 ? -12.23200 4.34000   20.36700  1.000 30.25889 ? 112 LEU A N      1 
ATOM   812  C  CA     . LEU A 1 116 ? -12.57400 3.03800   20.91300  1.000 28.63501 ? 112 LEU A CA     1 
ATOM   813  C  C      . LEU A 1 116 ? -13.83800 2.49200   20.23700  1.000 29.42458 ? 112 LEU A C      1 
ATOM   814  O  O      . LEU A 1 116 ? -14.88800 3.13900   20.25100  1.000 27.25327 ? 112 LEU A O      1 
ATOM   815  C  CB     . LEU A 1 116 ? -12.77800 3.19100   22.42100  1.000 40.52328 ? 112 LEU A CB     1 
ATOM   816  C  CG     . LEU A 1 116 ? -13.31200 1.98900   23.19500  1.000 49.41645 ? 112 LEU A CG     1 
ATOM   817  C  CD1    . LEU A 1 116 ? -12.48600 0.73900   22.86600  1.000 49.53225 ? 112 LEU A CD1    1 
ATOM   818  C  CD2    . LEU A 1 116 ? -13.33100 2.27000   24.69700  1.000 47.77415 ? 112 LEU A CD2    1 
ATOM   819  N  N      . GLN A 1 117 ? -13.72900 1.31400   19.61600  1.000 24.63453 ? 113 GLN A N      1 
ATOM   820  C  CA     . GLN A 1 117 ? -14.86300 0.69000   18.92900  1.000 25.66360 ? 113 GLN A CA     1 
ATOM   821  C  C      . GLN A 1 117 ? -15.51700 1.67400   17.95800  1.000 31.61958 ? 113 GLN A C      1 
ATOM   822  O  O      . GLN A 1 117 ? -16.74800 1.73000   17.83000  1.000 25.00037 ? 113 GLN A O      1 
ATOM   823  C  CB     . GLN A 1 117 ? -15.89800 0.13900   19.93100  1.000 20.91567 ? 113 GLN A CB     1 
ATOM   824  C  CG     . GLN A 1 117 ? -15.39600 -1.03000  20.77300  1.000 23.15541 ? 113 GLN A CG     1 
ATOM   825  C  CD     . GLN A 1 117 ? -16.37600 -1.44500  21.87700  1.000 28.76398 ? 113 GLN A CD     1 
ATOM   826  O  OE1    . GLN A 1 117 ? -17.27600 -0.69000  22.25800  1.000 29.45880 ? 113 GLN A OE1    1 
ATOM   827  N  NE2    . GLN A 1 117 ? -16.20400 -2.66200  22.38200  1.000 24.07131 ? 113 GLN A NE2    1 
ATOM   828  N  N      . GLU A 1 118 ? -14.68800 2.48400   17.28800  1.000 23.58967 ? 114 GLU A N      1 
ATOM   829  C  CA     . GLU A 1 118 ? -15.23200 3.47000   16.36300  1.000 25.62676 ? 114 GLU A CA     1 
ATOM   830  C  C      . GLU A 1 118 ? -16.15800 2.79000   15.35600  1.000 26.75321 ? 114 GLU A C      1 
ATOM   831  O  O      . GLU A 1 118 ? -15.78600 1.80900   14.70100  1.000 27.74806 ? 114 GLU A O      1 
ATOM   832  C  CB     . GLU A 1 118 ? -14.11000 4.22400   15.64100  1.000 28.08231 ? 114 GLU A CB     1 
ATOM   833  C  CG     . GLU A 1 118 ? -14.68000 5.28300   14.71000  1.000 28.73502 ? 114 GLU A CG     1 
ATOM   834  C  CD     . GLU A 1 118 ? -13.69300 6.35400   14.27900  1.000 30.26679 ? 114 GLU A CD     1 
ATOM   835  O  OE1    . GLU A 1 118 ? -14.00700 7.07900   13.30900  1.000 29.30088 ? 114 GLU A OE1    1 
ATOM   836  O  OE2    . GLU A 1 118 ? -12.61200 6.47700   14.89300  1.000 35.55953 ? 114 GLU A OE2    1 
ATOM   837  N  N      . SER A 1 119 ? -17.37800 3.31100   15.23700  1.000 26.39001 ? 115 SER A N      1 
ATOM   838  C  CA     . SER A 1 119 ? -18.43500 2.63200   14.50000  1.000 31.27480 ? 115 SER A CA     1 
ATOM   839  C  C      . SER A 1 119 ? -18.92300 3.47000   13.32700  1.000 30.70631 ? 115 SER A C      1 
ATOM   840  O  O      . SER A 1 119 ? -20.06800 3.33900   12.88900  1.000 26.28210 ? 115 SER A O      1 
ATOM   841  C  CB     . SER A 1 119 ? -19.58600 2.28800   15.44400  1.000 32.30651 ? 115 SER A CB     1 
ATOM   842  O  OG     . SER A 1 119 ? -19.16300 1.34300   16.41900  1.000 31.06951 ? 115 SER A OG     1 
ATOM   843  N  N      . THR A 1 120 ? -18.02400 4.27300   12.77400  1.000 30.67736 ? 116 THR A N      1 
ATOM   844  C  CA     . THR A 1 120 ? -18.26100 5.15500   11.64500  1.000 30.26942 ? 116 THR A CA     1 
ATOM   845  C  C      . THR A 1 120 ? -17.74200 4.49800   10.36700  1.000 31.71959 ? 116 THR A C      1 
ATOM   846  O  O      . THR A 1 120 ? -17.20700 3.38400   10.37600  1.000 27.60594 ? 116 THR A O      1 
ATOM   847  C  CB     . THR A 1 120 ? -17.52100 6.47400   11.85100  1.000 28.56921 ? 116 THR A CB     1 
ATOM   848  O  OG1    . THR A 1 120 ? -16.12500 6.18500   11.87800  1.000 26.59003 ? 116 THR A OG1    1 
ATOM   849  C  CG2    . THR A 1 120 ? -17.90100 7.14000   13.16900  1.000 26.43738 ? 116 THR A CG2    1 
ATOM   850  N  N      . VAL A 1 121 ? -17.83900 5.23600   9.25800   1.000 29.56407 ? 117 VAL A N      1 
ATOM   851  C  CA     . VAL A 1 121 ? -17.22900 4.78100   8.01100   1.000 27.79807 ? 117 VAL A CA     1 
ATOM   852  C  C      . VAL A 1 121 ? -15.73500 4.51700   8.17900   1.000 27.29275 ? 117 VAL A C      1 
ATOM   853  O  O      . VAL A 1 121 ? -15.17100 3.67100   7.47500   1.000 32.33019 ? 117 VAL A O      1 
ATOM   854  C  CB     . VAL A 1 121 ? -17.48500 5.81400   6.89900   1.000 35.17264 ? 117 VAL A CB     1 
ATOM   855  C  CG1    . VAL A 1 121 ? -16.71200 7.09400   7.18700   1.000 29.72988 ? 117 VAL A CG1    1 
ATOM   856  C  CG2    . VAL A 1 121 ? -17.14300 5.22300   5.51900   1.000 29.87200 ? 117 VAL A CG2    1 
ATOM   857  N  N      . HIS A 1 122 ? -15.06600 5.21300   9.10600   1.000 25.43726 ? 118 HIS A N      1 
ATOM   858  C  CA     . HIS A 1 122 ? -13.62500 5.02400   9.31000   1.000 30.83791 ? 118 HIS A CA     1 
ATOM   859  C  C      . HIS A 1 122 ? -13.28400 3.83600   10.19500  1.000 32.03805 ? 118 HIS A C      1 
ATOM   860  O  O      . HIS A 1 122 ? -12.10100 3.47900   10.30100  1.000 30.15888 ? 118 HIS A O      1 
ATOM   861  C  CB     . HIS A 1 122 ? -12.98700 6.27400   9.93400   1.000 33.96460 ? 118 HIS A CB     1 
ATOM   862  C  CG     . HIS A 1 122 ? -13.46800 7.55600   9.33200   1.000 33.86722 ? 118 HIS A CG     1 
ATOM   863  N  ND1    . HIS A 1 122 ? -13.03000 8.01300   8.10500   1.000 31.32481 ? 118 HIS A ND1    1 
ATOM   864  C  CD2    . HIS A 1 122 ? -14.37100 8.46400   9.77600   1.000 29.95886 ? 118 HIS A CD2    1 
ATOM   865  C  CE1    . HIS A 1 122 ? -13.62800 9.16100   7.83100   1.000 35.99642 ? 118 HIS A CE1    1 
ATOM   866  N  NE2    . HIS A 1 122 ? -14.45200 9.45300   8.82600   1.000 34.16199 ? 118 HIS A NE2    1 
ATOM   867  N  N      . GLY A 1 123 ? -14.26600 3.24800   10.86800  1.000 28.21917 ? 119 GLY A N      1 
ATOM   868  C  CA     . GLY A 1 123 ? -13.99800 2.09400   11.70200  1.000 25.27671 ? 119 GLY A CA     1 
ATOM   869  C  C      . GLY A 1 123 ? -14.83400 0.92300   11.24900  1.000 27.52962 ? 119 GLY A C      1 
ATOM   870  O  O      . GLY A 1 123 ? -14.70500 0.45800   10.11000  1.000 27.49014 ? 119 GLY A O      1 
ATOM   871  N  N      . VAL A 1 124 ? -15.69600 0.44000   12.13500  1.000 23.98972 ? 120 VAL A N      1 
ATOM   872  C  CA     . VAL A 1 124 ? -16.65100 -0.61400  11.82200  1.000 27.32170 ? 120 VAL A CA     1 
ATOM   873  C  C      . VAL A 1 124 ? -17.97800 0.09500   11.54700  1.000 28.01389 ? 120 VAL A C      1 
ATOM   874  O  O      . VAL A 1 124 ? -18.64500 0.57700   12.47200  1.000 25.12143 ? 120 VAL A O      1 
ATOM   875  C  CB     . VAL A 1 124 ? -16.76000 -1.62600  12.96500  1.000 30.46681 ? 120 VAL A CB     1 
ATOM   876  C  CG1    . VAL A 1 124 ? -17.96900 -2.51600  12.77000  1.000 24.45820 ? 120 VAL A CG1    1 
ATOM   877  C  CG2    . VAL A 1 124 ? -15.46900 -2.45100  13.06900  1.000 28.41920 ? 120 VAL A CG2    1 
ATOM   878  N  N      . ASP A 1 125 ? -18.34000 0.21100   10.26800  1.000 22.31583 ? 121 ASP A N      1 
ATOM   879  C  CA     . ASP A 1 125 ? -19.41500 1.11200   9.82600   1.000 22.89748 ? 121 ASP A CA     1 
ATOM   880  C  C      . ASP A 1 125 ? -20.78200 0.46400   10.05700  1.000 27.15062 ? 121 ASP A C      1 
ATOM   881  O  O      . ASP A 1 125 ? -21.36800 -0.13200  9.15000   1.000 22.07633 ? 121 ASP A O      1 
ATOM   882  C  CB     . ASP A 1 125 ? -19.21800 1.45500   8.35700   1.000 22.98697 ? 121 ASP A CB     1 
ATOM   883  C  CG     . ASP A 1 125 ? -20.24800 2.44800   7.82500   1.000 30.26679 ? 121 ASP A CG     1 
ATOM   884  O  OD1    . ASP A 1 125 ? -21.23400 2.76200   8.53100   1.000 25.31883 ? 121 ASP A OD1    1 
ATOM   885  O  OD2    . ASP A 1 125 ? -20.04900 2.91900   6.68400   1.000 32.58812 ? 121 ASP A OD2    1 
ATOM   886  N  N      . LEU A 1 126 ? -21.32800 0.63200   11.27000  1.000 22.01053 ? 122 LEU A N      1 
ATOM   887  C  CA     . LEU A 1 126 ? -22.56700 -0.05500  11.64000  1.000 20.68932 ? 122 LEU A CA     1 
ATOM   888  C  C      . LEU A 1 126 ? -23.71600 0.32000   10.71700  1.000 25.22408 ? 122 LEU A C      1 
ATOM   889  O  O      . LEU A 1 126 ? -24.53800 -0.53400  10.35500  1.000 23.89497 ? 122 LEU A O      1 
ATOM   890  C  CB     . LEU A 1 126 ? -22.95300 0.26700   13.09100  1.000 25.45042 ? 122 LEU A CB     1 
ATOM   891  C  CG     . LEU A 1 126 ? -21.96700 -0.19200  14.17600  1.000 26.87164 ? 122 LEU A CG     1 
ATOM   892  C  CD1    . LEU A 1 126 ? -22.50900 0.11400   15.58000  1.000 23.66336 ? 122 LEU A CD1    1 
ATOM   893  C  CD2    . LEU A 1 126 ? -21.66100 -1.66500  14.02200  1.000 24.12921 ? 122 LEU A CD2    1 
ATOM   894  N  N      . VAL A 1 127 ? -23.81400 1.59900   10.35100  1.000 19.46549 ? 123 VAL A N      1 
ATOM   895  C  CA     . VAL A 1 127 ? -24.93600 2.03900   9.52400   1.000 27.21379 ? 123 VAL A CA     1 
ATOM   896  C  C      . VAL A 1 127 ? -24.96500 1.26600   8.20800   1.000 25.36620 ? 123 VAL A C      1 
ATOM   897  O  O      . VAL A 1 127 ? -26.02600 0.79800   7.78300   1.000 19.31547 ? 123 VAL A O      1 
ATOM   898  C  CB     . VAL A 1 127 ? -24.88000 3.56300   9.30400   1.000 28.71660 ? 123 VAL A CB     1 
ATOM   899  C  CG1    . VAL A 1 127 ? -25.85400 3.99800   8.19900   1.000 23.65284 ? 123 VAL A CG1    1 
ATOM   900  C  CG2    . VAL A 1 127 ? -25.21700 4.27900   10.60800  1.000 26.92428 ? 123 VAL A CG2    1 
ATOM   901  N  N      . SER A 1 128 ? -23.79700 1.06200   7.57200   1.000 20.01819 ? 124 SER A N      1 
ATOM   902  C  CA     . SER A 1 128 ? -23.75800 0.31500   6.31000   1.000 17.60211 ? 124 SER A CA     1 
ATOM   903  C  C      . SER A 1 128 ? -23.89800 -1.18700  6.50700   1.000 25.72414 ? 124 SER A C      1 
ATOM   904  O  O      . SER A 1 128 ? -24.46700 -1.86600  5.64600   1.000 26.37948 ? 124 SER A O      1 
ATOM   905  C  CB     . SER A 1 128 ? -22.44600 0.59500   5.56700   1.000 18.34957 ? 124 SER A CB     1 
ATOM   906  O  OG     . SER A 1 128 ? -22.22300 1.97900   5.57300   1.000 34.58836 ? 124 SER A OG     1 
ATOM   907  N  N      . ILE A 1 129 ? -23.41300 -1.70600  7.63300   1.000 23.28437 ? 125 ILE A N      1 
ATOM   908  C  CA     . ILE A 1 129 ? -23.55600 -3.13100  7.89600   1.000 18.98122 ? 125 ILE A CA     1 
ATOM   909  C  C      . ILE A 1 129 ? -25.02800 -3.51200  8.01900   1.000 19.83133 ? 125 ILE A C      1 
ATOM   910  O  O      . ILE A 1 129 ? -25.46400 -4.54500  7.49400   1.000 22.13686 ? 125 ILE A O      1 
ATOM   911  C  CB     . ILE A 1 129 ? -22.75900 -3.52300  9.15200   1.000 24.44240 ? 125 ILE A CB     1 
ATOM   912  C  CG1    . ILE A 1 129 ? -21.24600 -3.38500  8.89800   1.000 25.21881 ? 125 ILE A CG1    1 
ATOM   913  C  CG2    . ILE A 1 129 ? -23.13600 -4.93200  9.59000   1.000 16.59673 ? 125 ILE A CG2    1 
ATOM   914  C  CD1    . ILE A 1 129 ? -20.37400 -3.55600  10.16400  1.000 20.69985 ? 125 ILE A CD1    1 
ATOM   915  N  N      . PHE A 1 130 ? -25.82200 -2.68000  8.69400   1.000 17.77055 ? 126 PHE A N      1 
ATOM   916  C  CA     . PHE A 1 130 ? -27.22900 -3.01100  8.92900   1.000 19.52076 ? 126 PHE A CA     1 
ATOM   917  C  C      . PHE A 1 130 ? -28.14300 -2.60700  7.79000   1.000 22.09739 ? 126 PHE A C      1 
ATOM   918  O  O      . PHE A 1 130 ? -29.27800 -3.08700  7.71800   1.000 21.07358 ? 126 PHE A O      1 
ATOM   919  C  CB     . PHE A 1 130 ? -27.72800 -2.36300  10.22100  1.000 15.58608 ? 126 PHE A CB     1 
ATOM   920  C  CG     . PHE A 1 130 ? -27.41100 -3.18100  11.44200  1.000 23.92392 ? 126 PHE A CG     1 
ATOM   921  C  CD1    . PHE A 1 130 ? -26.18100 -3.04100  12.10300  1.000 18.36799 ? 126 PHE A CD1    1 
ATOM   922  C  CD2    . PHE A 1 130 ? -28.29300 -4.14900  11.87500  1.000 22.72904 ? 126 PHE A CD2    1 
ATOM   923  C  CE1    . PHE A 1 130 ? -25.86900 -3.82300  13.19500  1.000 22.96854 ? 126 PHE A CE1    1 
ATOM   924  C  CE2    . PHE A 1 130 ? -27.99800 -4.93700  12.97100  1.000 23.57651 ? 126 PHE A CE2    1 
ATOM   925  C  CZ     . PHE A 1 130 ? -26.77300 -4.77700  13.63900  1.000 25.64255 ? 126 PHE A CZ     1 
ATOM   926  N  N      . SER A 1 131 ? -27.66500 -1.76200  6.89300   1.000 19.99713 ? 127 SER A N      1 
ATOM   927  C  CA     . SER A 1 131 ? -28.49400 -1.28400  5.79100   1.000 20.03661 ? 127 SER A CA     1 
ATOM   928  C  C      . SER A 1 131 ? -29.16400 -2.41700  5.01800   1.000 21.73945 ? 127 SER A C      1 
ATOM   929  O  O      . SER A 1 131 ? -30.38200 -2.35200  4.80300   1.000 22.60797 ? 127 SER A O      1 
ATOM   930  C  CB     . SER A 1 131 ? -27.58000 -0.41200  4.91600   1.000 19.73131 ? 127 SER A CB     1 
ATOM   931  O  OG     . SER A 1 131 ? -28.32000 0.55900   4.22100   1.000 41.78922 ? 127 SER A OG     1 
ATOM   932  N  N      . PRO A 1 132 ? -28.48300 -3.49400  4.63300   1.000 26.43475 ? 128 PRO A N      1 
ATOM   933  C  CA     . PRO A 1 132 ? -29.16700 -4.52500  3.82700   1.000 23.14488 ? 128 PRO A CA     1 
ATOM   934  C  C      . PRO A 1 132 ? -30.25800 -5.27600  4.57100   1.000 24.93983 ? 128 PRO A C      1 
ATOM   935  O  O      . PRO A 1 132 ? -31.13300 -5.84800  3.91300   1.000 23.67915 ? 128 PRO A O      1 
ATOM   936  C  CB     . PRO A 1 132 ? -28.02600 -5.46600  3.40800   1.000 23.13435 ? 128 PRO A CB     1 
ATOM   937  C  CG     . PRO A 1 132 ? -26.76700 -4.57800  3.49500   1.000 21.16570 ? 128 PRO A CG     1 
ATOM   938  C  CD     . PRO A 1 132 ? -27.02900 -3.71600  4.69500   1.000 24.32923 ? 128 PRO A CD     1 
ATOM   939  N  N      . ILE A 1 133 ? -30.25800 -5.31200  5.90400   1.000 24.45293 ? 129 ILE A N      1 
ATOM   940  C  CA     . ILE A 1 133 ? -31.28000 -6.11300  6.58200   1.000 22.92643 ? 129 ILE A CA     1 
ATOM   941  C  C      . ILE A 1 133 ? -32.13800 -5.25800  7.50800   1.000 22.00527 ? 129 ILE A C      1 
ATOM   942  O  O      . ILE A 1 133 ? -32.63400 -5.74400  8.53300   1.000 23.69495 ? 129 ILE A O      1 
ATOM   943  C  CB     . ILE A 1 133 ? -30.66100 -7.31200  7.33700   1.000 24.97668 ? 129 ILE A CB     1 
ATOM   944  C  CG1    . ILE A 1 133 ? -29.36400 -6.93200  8.03600   1.000 23.34754 ? 129 ILE A CG1    1 
ATOM   945  C  CG2    . ILE A 1 133 ? -30.38200 -8.44600  6.37800   1.000 28.79819 ? 129 ILE A CG2    1 
ATOM   946  C  CD1    . ILE A 1 133 ? -29.55600 -6.11500  9.25100   1.000 22.39742 ? 129 ILE A CD1    1 
ATOM   947  N  N      . THR A 1 134 ? -32.30000 -3.98100  7.16700   1.000 22.76326 ? 130 THR A N      1 
ATOM   948  C  CA     . THR A 1 134 ? -33.24300 -3.11200  7.85000   1.000 23.16067 ? 130 THR A CA     1 
ATOM   949  C  C      . THR A 1 134 ? -34.05100 -2.34600  6.82100   1.000 27.92440 ? 130 THR A C      1 
ATOM   950  O  O      . THR A 1 134 ? -33.62000 -2.16500  5.68000   1.000 26.60845 ? 130 THR A O      1 
ATOM   951  C  CB     . THR A 1 134 ? -32.54900 -2.11400  8.81200   1.000 22.63429 ? 130 THR A CB     1 
ATOM   952  O  OG1    . THR A 1 134 ? -31.52500 -1.38700  8.11900   1.000 24.21606 ? 130 THR A OG1    1 
ATOM   953  C  CG2    . THR A 1 134 ? -31.96400 -2.85000  10.01600  1.000 17.66264 ? 130 THR A CG2    1 
ATOM   954  N  N      . LYS A 1 135 ? -35.23800 -1.89500  7.24100   1.000 27.73754 ? 131 LYS A N      1 
ATOM   955  C  CA     . LYS A 1 135 ? -35.98200 -0.96200  6.40800   1.000 28.86662 ? 131 LYS A CA     1 
ATOM   956  C  C      . LYS A 1 135 ? -35.33500 0.41600   6.44000   1.000 27.47698 ? 131 LYS A C      1 
ATOM   957  O  O      . LYS A 1 135 ? -35.47400 1.19500   5.49000   1.000 24.43451 ? 131 LYS A O      1 
ATOM   958  C  CB     . LYS A 1 135 ? -37.44700 -0.88300  6.85800   1.000 24.98721 ? 131 LYS A CB     1 
ATOM   959  C  CG     . LYS A 1 135 ? -38.22700 -2.18600  6.69500   1.000 21.27360 ? 131 LYS A CG     1 
ATOM   960  C  CD     . LYS A 1 135 ? -39.71100 -2.04600  7.07100   1.000 25.28198 ? 131 LYS A CD     1 
ATOM   961  C  CE     . LYS A 1 135 ? -40.49100 -1.23200  6.02100   1.000 20.95778 ? 131 LYS A CE     1 
ATOM   962  N  NZ     . LYS A 1 135 ? -41.94800 -1.23700  6.31500   1.000 20.08662 ? 131 LYS A NZ     1 
ATOM   963  N  N      . LEU A 1 136 ? -34.63700 0.73600   7.52400   1.000 23.08961 ? 132 LEU A N      1 
ATOM   964  C  CA     . LEU A 1 136 ? -33.95100 2.01600   7.66100   1.000 27.82702 ? 132 LEU A CA     1 
ATOM   965  C  C      . LEU A 1 136 ? -32.78100 1.84800   8.62400   1.000 26.36369 ? 132 LEU A C      1 
ATOM   966  O  O      . LEU A 1 136 ? -32.94700 1.25300   9.69200   1.000 19.50760 ? 132 LEU A O      1 
ATOM   967  C  CB     . LEU A 1 136 ? -34.91100 3.09500   8.16500   1.000 24.74507 ? 132 LEU A CB     1 
ATOM   968  C  CG     . LEU A 1 136 ? -34.28300 4.42400   8.55500   1.000 30.11677 ? 132 LEU A CG     1 
ATOM   969  C  CD1    . LEU A 1 136 ? -33.78200 5.21100   7.33000   1.000 30.30363 ? 132 LEU A CD1    1 
ATOM   970  C  CD2    . LEU A 1 136 ? -35.27500 5.24500   9.37000   1.000 24.85035 ? 132 LEU A CD2    1 
ATOM   971  N  N      . SER A 1 137 ? -31.61000 2.36500   8.24900   1.000 20.89987 ? 133 SER A N      1 
ATOM   972  C  CA     . SER A 1 137 ? -30.42700 2.32700   9.10300   1.000 25.98206 ? 133 SER A CA     1 
ATOM   973  C  C      . SER A 1 137 ? -29.78400 3.69700   8.97700   1.000 23.55019 ? 133 SER A C      1 
ATOM   974  O  O      . SER A 1 137 ? -29.41200 4.10000   7.87200   1.000 24.04499 ? 133 SER A O      1 
ATOM   975  C  CB     . SER A 1 137 ? -29.46200 1.19900   8.66100   1.000 22.51849 ? 133 SER A CB     1 
ATOM   976  O  OG     . SER A 1 137 ? -28.21600 1.20300   9.35900   1.000 21.96579 ? 133 SER A OG     1 
ATOM   977  N  N      . VAL A 1 138 ? -29.70100 4.44600   10.07600  1.000 24.95299 ? 134 VAL A N      1 
ATOM   978  C  CA     . VAL A 1 138 ? -29.30500 5.85000   9.99700   1.000 22.51849 ? 134 VAL A CA     1 
ATOM   979  C  C      . VAL A 1 138 ? -28.67300 6.27800   11.31400  1.000 27.11641 ? 134 VAL A C      1 
ATOM   980  O  O      . VAL A 1 138 ? -29.00500 5.75600   12.37900  1.000 25.76888 ? 134 VAL A O      1 
ATOM   981  C  CB     . VAL A 1 138 ? -30.52100 6.74200   9.64500   1.000 35.23580 ? 134 VAL A CB     1 
ATOM   982  C  CG1    . VAL A 1 138 ? -31.58700 6.63400   10.73200  1.000 28.97979 ? 134 VAL A CG1    1 
ATOM   983  C  CG2    . VAL A 1 138 ? -30.07700 8.19800   9.45300   1.000 39.08363 ? 134 VAL A CG2    1 
ATOM   984  N  N      . MET A 1 139 ? -27.74900 7.23000   11.23700  1.000 25.77677 ? 135 MET A N      1 
ATOM   985  C  CA     . MET A 1 139 ? -27.15200 7.84100   12.41700  1.000 28.74555 ? 135 MET A CA     1 
ATOM   986  C  C      . MET A 1 139 ? -27.83600 9.17600   12.68200  1.000 28.88504 ? 135 MET A C      1 
ATOM   987  O  O      . MET A 1 139 ? -27.93800 10.01200  11.77800  1.000 29.33510 ? 135 MET A O      1 
ATOM   988  C  CB     . MET A 1 139 ? -25.64300 8.04000   12.22900  1.000 20.18663 ? 135 MET A CB     1 
ATOM   989  C  CG     . MET A 1 139 ? -24.93600 8.67800   13.42500  1.000 30.65631 ? 135 MET A CG     1 
ATOM   990  S  SD     . MET A 1 139 ? -23.14400 8.82100   13.17200  1.000 34.97525 ? 135 MET A SD     1 
ATOM   991  C  CE     . MET A 1 139 ? -23.09200 10.34600  12.22200  1.000 35.43846 ? 135 MET A CE     1 
ATOM   992  N  N      . ILE A 1 140 ? -28.29900 9.37500   13.91500  1.000 29.60355 ? 136 ILE A N      1 
ATOM   993  C  CA     . ILE A 1 140 ? -28.93900 10.64200  14.28600  1.000 32.77761 ? 136 ILE A CA     1 
ATOM   994  C  C      . ILE A 1 140 ? -27.87300 11.71600  14.14700  1.000 29.32720 ? 136 ILE A C      1 
ATOM   995  O  O      . ILE A 1 140 ? -26.82600 11.62200  14.79700  1.000 28.99558 ? 136 ILE A O      1 
ATOM   996  C  CB     . ILE A 1 140 ? -29.51200 10.64100  15.71300  1.000 36.37015 ? 136 ILE A CB     1 
ATOM   997  C  CG1    . ILE A 1 140 ? -30.30000 9.36500   16.00000  1.000 35.20948 ? 136 ILE A CG1    1 
ATOM   998  C  CG2    . ILE A 1 140 ? -30.34700 11.90000  15.95000  1.000 34.93577 ? 136 ILE A CG2    1 
ATOM   999  C  CD1    . ILE A 1 140 ? -31.49100 9.22000   15.18200  1.000 36.09117 ? 136 ILE A CD1    1 
ATOM   1000 N  N      . PRO A 1 141 ? -28.07200 12.71900  13.29600  1.000 32.64865 ? 137 PRO A N      1 
ATOM   1001 C  CA     . PRO A 1 141 ? -26.99600 13.68600  13.03600  1.000 36.86495 ? 137 PRO A CA     1 
ATOM   1002 C  C      . PRO A 1 141 ? -26.87700 14.72800  14.13500  1.000 38.86519 ? 137 PRO A C      1 
ATOM   1003 O  O      . PRO A 1 141 ? -25.78700 15.23100  14.41000  1.000 36.96496 ? 137 PRO A O      1 
ATOM   1004 C  CB     . PRO A 1 141 ? -27.41200 14.31800  11.70500  1.000 31.64590 ? 137 PRO A CB     1 
ATOM   1005 C  CG     . PRO A 1 141 ? -28.91800 14.28000  11.75500  1.000 33.38032 ? 137 PRO A CG     1 
ATOM   1006 C  CD     . PRO A 1 141 ? -29.29600 13.02200  12.53400  1.000 30.59577 ? 137 PRO A CD     1 
ATOM   1007 N  N      . THR A 1 142 ? -28.00000 15.07700  14.75500  1.000 29.78778 ? 138 THR A N      1 
ATOM   1008 C  CA     . THR A 1 142 ? -27.98800 16.08700  15.80200  1.000 34.00145 ? 138 THR A CA     1 
ATOM   1009 C  C      . THR A 1 142 ? -29.06700 15.75900  16.81400  1.000 38.04667 ? 138 THR A C      1 
ATOM   1010 O  O      . THR A 1 142 ? -30.04500 15.06800  16.51000  1.000 34.74364 ? 138 THR A O      1 
ATOM   1011 C  CB     . THR A 1 142 ? -28.25300 17.48900  15.25600  1.000 37.37027 ? 138 THR A CB     1 
ATOM   1012 O  OG1    . THR A 1 142 ? -29.61600 17.54500  14.82500  1.000 42.82092 ? 138 THR A OG1    1 
ATOM   1013 C  CG2    . THR A 1 142 ? -27.34000 17.80600  14.09000  1.000 37.27289 ? 138 THR A CG2    1 
ATOM   1014 N  N      . ALA A 1 143 ? -28.89600 16.31000  18.01900  1.000 36.77283 ? 139 ALA A N      1 
ATOM   1015 C  CA     . ALA A 1 143 ? -29.90000 16.12300  19.05600  1.000 31.38271 ? 139 ALA A CA     1 
ATOM   1016 C  C      . ALA A 1 143 ? -31.25600 16.62100  18.57500  1.000 29.03506 ? 139 ALA A C      1 
ATOM   1017 O  O      . ALA A 1 143 ? -32.27600 15.96700  18.79500  1.000 30.85370 ? 139 ALA A O      1 
ATOM   1018 C  CB     . ALA A 1 143 ? -29.47800 16.85200  20.33500  1.000 28.32708 ? 139 ALA A CB     1 
ATOM   1019 N  N      . GLU A 1 144 ? -31.26000 17.73900  17.84600  1.000 28.94558 ? 140 GLU A N      1 
ATOM   1020 C  CA     . GLU A 1 144 ? -32.48500 18.36000  17.35600  1.000 36.39121 ? 140 GLU A CA     1 
ATOM   1021 C  C      . GLU A 1 144 ? -33.29100 17.42400  16.46300  1.000 37.24657 ? 140 GLU A C      1 
ATOM   1022 O  O      . GLU A 1 144 ? -34.52200 17.54600  16.39200  1.000 32.21702 ? 140 GLU A O      1 
ATOM   1023 C  CB     . GLU A 1 144 ? -32.12300 19.63900  16.59700  1.000 40.24430 ? 140 GLU A CB     1 
ATOM   1024 C  CG     . GLU A 1 144 ? -33.31800 20.46100  16.15200  1.000 60.69412 ? 140 GLU A CG     1 
ATOM   1025 C  CD     . GLU A 1 144 ? -33.82300 20.06700  14.77100  1.000 73.04823 ? 140 GLU A CD     1 
ATOM   1026 O  OE1    . GLU A 1 144 ? -32.98400 19.78600  13.88700  1.000 75.58275 ? 140 GLU A OE1    1 
ATOM   1027 O  OE2    . GLU A 1 144 ? -35.05900 20.03500  14.57500  1.000 77.28032 ? 140 GLU A OE2    1 
ATOM   1028 N  N      . LYS A 1 145 ? -32.63300 16.47500  15.79400  1.000 31.28007 ? 141 LYS A N      1 
ATOM   1029 C  CA     . LYS A 1 145 ? -33.33000 15.57300  14.88700  1.000 33.03291 ? 141 LYS A CA     1 
ATOM   1030 C  C      . LYS A 1 145 ? -33.78500 14.29100  15.56400  1.000 34.57257 ? 141 LYS A C      1 
ATOM   1031 O  O      . LYS A 1 145 ? -34.39400 13.44100  14.90200  1.000 30.18520 ? 141 LYS A O      1 
ATOM   1032 C  CB     . LYS A 1 145 ? -32.42200 15.20000  13.70200  1.000 33.75405 ? 141 LYS A CB     1 
ATOM   1033 C  CG     . LYS A 1 145 ? -31.95000 16.37800  12.87700  1.000 32.41968 ? 141 LYS A CG     1 
ATOM   1034 C  CD     . LYS A 1 145 ? -32.88400 16.58000  11.71100  1.000 40.16534 ? 141 LYS A CD     1 
ATOM   1035 C  CE     . LYS A 1 145 ? -33.54900 17.92600  11.79100  1.000 51.51670 ? 141 LYS A CE     1 
ATOM   1036 N  NZ     . LYS A 1 145 ? -34.33200 18.19700  10.56800  1.000 55.73037 ? 141 LYS A NZ     1 
ATOM   1037 N  N      . MET A 1 146 ? -33.54500 14.14900  16.86900  1.000 32.90131 ? 142 MET A N      1 
ATOM   1038 C  CA     . MET A 1 146 ? -33.88200 12.90300  17.55500  1.000 31.15900 ? 142 MET A CA     1 
ATOM   1039 C  C      . MET A 1 146 ? -35.37200 12.58500  17.43700  1.000 23.89497 ? 142 MET A C      1 
ATOM   1040 O  O      . MET A 1 146 ? -35.75100 11.45500  17.11100  1.000 28.21917 ? 142 MET A O      1 
ATOM   1041 C  CB     . MET A 1 146 ? -33.46300 12.97900  19.02500  1.000 29.79305 ? 142 MET A CB     1 
ATOM   1042 C  CG     . MET A 1 146 ? -33.86500 11.74900  19.83700  1.000 31.36165 ? 142 MET A CG     1 
ATOM   1043 S  SD     . MET A 1 146 ? -32.91400 10.27400  19.40000  1.000 40.39958 ? 142 MET A SD     1 
ATOM   1044 C  CE     . MET A 1 146 ? -31.34500 10.63800  20.20100  1.000 37.60451 ? 142 MET A CE     1 
ATOM   1045 N  N      . GLY A 1 147 ? -36.23400 13.56400  17.70700  1.000 22.86327 ? 143 GLY A N      1 
ATOM   1046 C  CA     . GLY A 1 147 ? -37.66800 13.30600  17.61800  1.000 29.09296 ? 143 GLY A CA     1 
ATOM   1047 C  C      . GLY A 1 147 ? -38.10400 12.86700  16.22800  1.000 29.21929 ? 143 GLY A C      1 
ATOM   1048 O  O      . GLY A 1 147 ? -38.76100 11.83300  16.06500  1.000 25.16091 ? 143 GLY A O      1 
ATOM   1049 N  N      . GLU A 1 148 ? -37.73400 13.64500  15.20400  1.000 28.34287 ? 144 GLU A N      1 
ATOM   1050 C  CA     . GLU A 1 148 ? -38.10400 13.30700  13.82600  1.000 31.37218 ? 144 GLU A CA     1 
ATOM   1051 C  C      . GLU A 1 148 ? -37.56700 11.93500  13.41700  1.000 27.51909 ? 144 GLU A C      1 
ATOM   1052 O  O      . GLU A 1 148 ? -38.28300 11.14200  12.79200  1.000 31.50378 ? 144 GLU A O      1 
ATOM   1053 C  CB     . GLU A 1 148 ? -37.58700 14.38500  12.86600  1.000 34.11462 ? 144 GLU A CB     1 
ATOM   1054 C  CG     . GLU A 1 148 ? -38.42100 15.65500  12.85900  1.000 45.75549 ? 144 GLU A CG     1 
ATOM   1055 C  CD     . GLU A 1 148 ? -37.83300 16.77900  11.99400  1.000 52.08256 ? 144 GLU A CD     1 
ATOM   1056 O  OE1    . GLU A 1 148 ? -36.68000 16.65900  11.53000  1.000 51.32984 ? 144 GLU A OE1    1 
ATOM   1057 O  OE2    . GLU A 1 148 ? -38.54400 17.79000  11.78000  1.000 55.14609 ? 144 GLU A OE2    1 
ATOM   1058 N  N      . MET A 1 149 ? -36.30300 11.64200  13.74600  1.000 30.11151 ? 145 MET A N      1 
ATOM   1059 C  CA     . MET A 1 149 ? -35.71300 10.36900  13.34400  1.000 25.24513 ? 145 MET A CA     1 
ATOM   1060 C  C      . MET A 1 149 ? -36.36000 9.21000   14.09200  1.000 27.85334 ? 145 MET A C      1 
ATOM   1061 O  O      . MET A 1 149 ? -36.57300 8.13300   13.52000  1.000 22.36847 ? 145 MET A O      1 
ATOM   1062 C  CB     . MET A 1 149 ? -34.19900 10.38400  13.58900  1.000 25.71624 ? 145 MET A CB     1 
ATOM   1063 C  CG     . MET A 1 149 ? -33.41000 11.29800  12.65400  1.000 36.57544 ? 145 MET A CG     1 
ATOM   1064 S  SD     . MET A 1 149 ? -33.57100 10.80100  10.91700  1.000 44.62904 ? 145 MET A SD     1 
ATOM   1065 C  CE     . MET A 1 149 ? -32.97700 12.29000  10.06600  1.000 41.60762 ? 145 MET A CE     1 
ATOM   1066 N  N      . THR A 1 150 ? -36.73400 9.41300   15.34000  1.000 24.35292 ? 146 THR A N      1 
ATOM   1067 C  CA     . THR A 1 150 ? -37.39400 8.39900   16.11200  1.000 24.37134 ? 146 THR A CA     1 
ATOM   1068 C  C      . THR A 1 150 ? -38.75700 8.08000   15.53800  1.000 26.12155 ? 146 THR A C      1 
ATOM   1069 O  O      . THR A 1 150 ? -39.08800 6.95400   15.36700  1.000 23.89760 ? 146 THR A O      1 
ATOM   1070 C  CB     . THR A 1 150 ? -37.48400 8.75800   17.58900  1.000 26.84006 ? 146 THR A CB     1 
ATOM   1071 O  OG1    . THR A 1 150 ? -36.19300 9.02600   18.07500  1.000 29.13507 ? 146 THR A OG1    1 
ATOM   1072 C  CG2    . THR A 1 150 ? -38.06400 7.66700   18.38300  1.000 22.12634 ? 146 THR A CG2    1 
ATOM   1073 N  N      . ARG A 1 151 ? -39.51100 9.10300   15.20000  1.000 24.12658 ? 147 ARG A N      1 
ATOM   1074 C  CA     . ARG A 1 151 ? -40.83200 8.93700   14.63200  1.000 23.43702 ? 147 ARG A CA     1 
ATOM   1075 C  C      . ARG A 1 151 ? -40.71800 8.31200   13.26300  1.000 26.34000 ? 147 ARG A C      1 
ATOM   1076 O  O      . ARG A 1 151 ? -41.47800 7.47800   12.92600  1.000 23.02645 ? 147 ARG A O      1 
ATOM   1077 C  CB     . ARG A 1 151 ? -41.62500 10.22500  14.64100  1.000 21.87894 ? 147 ARG A CB     1 
ATOM   1078 C  CG     . ARG A 1 151 ? -41.97900 10.67200  16.04400  1.000 25.72677 ? 147 ARG A CG     1 
ATOM   1079 C  CD     . ARG A 1 151 ? -42.86300 11.87300  16.05400  1.000 29.43774 ? 147 ARG A CD     1 
ATOM   1080 N  NE     . ARG A 1 151 ? -42.15000 13.10100  15.87600  1.000 39.52316 ? 147 ARG A NE     1 
ATOM   1081 C  CZ     . ARG A 1 151 ? -41.46500 13.68800  16.82600  1.000 42.69722 ? 147 ARG A CZ     1 
ATOM   1082 N  NH1    . ARG A 1 151 ? -41.35800 13.16300  18.02300  1.000 35.00420 ? 147 ARG A NH1    1 
ATOM   1083 N  NH2    . ARG A 1 151 ? -40.87100 14.78500  16.55800  1.000 47.80047 ? 147 ARG A NH2    1 
ATOM   1084 N  N      . ARG A 1 152 ? -39.73000 8.73800   12.50600  1.000 24.71612 ? 148 ARG A N      1 
ATOM   1085 C  CA     . ARG A 1 152 ? -39.45000 8.11600   11.22000  1.000 25.14512 ? 148 ARG A CA     1 
ATOM   1086 C  C      . ARG A 1 152 ? -39.18500 6.62400   11.38800  1.000 28.29550 ? 148 ARG A C      1 
ATOM   1087 O  O      . ARG A 1 152 ? -39.74100 5.79400   10.65700  1.000 27.57173 ? 148 ARG A O      1 
ATOM   1088 C  CB     . ARG A 1 152 ? -38.25300 8.80700   10.56900  1.000 22.38163 ? 148 ARG A CB     1 
ATOM   1089 C  CG     . ARG A 1 152 ? -37.80600 8.18200   9.26000   1.000 24.41345 ? 148 ARG A CG     1 
ATOM   1090 C  CD     . ARG A 1 152 ? -36.90000 9.16200   8.49400   1.000 29.66935 ? 148 ARG A CD     1 
ATOM   1091 N  NE     . ARG A 1 152 ? -37.05900 8.99800   7.05500   1.000 42.81566 ? 148 ARG A NE     1 
ATOM   1092 C  CZ     . ARG A 1 152 ? -37.31300 9.98500   6.21400   1.000 42.17348 ? 148 ARG A CZ     1 
ATOM   1093 N  NH1    . ARG A 1 152 ? -37.41700 11.22500  6.66300   1.000 32.38020 ? 148 ARG A NH1    1 
ATOM   1094 N  NH2    . ARG A 1 152 ? -37.45000 9.72500   4.92200   1.000 58.44648 ? 148 ARG A NH2    1 
ATOM   1095 N  N      . ALA A 1 153 ? -38.33600 6.25900   12.35300  1.000 26.07944 ? 149 ALA A N      1 
ATOM   1096 C  CA     . ALA A 1 153 ? -38.07300 4.84300   12.59600  1.000 25.10301 ? 149 ALA A CA     1 
ATOM   1097 C  C      . ALA A 1 153 ? -39.35400 4.09900   12.97200  1.000 25.47411 ? 149 ALA A C      1 
ATOM   1098 O  O      . ALA A 1 153 ? -39.64600 3.02200   12.43600  1.000 24.10552 ? 149 ALA A O      1 
ATOM   1099 C  CB     . ALA A 1 153 ? -37.01100 4.68900   13.69200  1.000 24.80034 ? 149 ALA A CB     1 
ATOM   1100 N  N      . LEU A 1 154 ? -40.13500 4.65500   13.90100  1.000 23.35806 ? 150 LEU A N      1 
ATOM   1101 C  CA     . LEU A 1 154 ? -41.33700 3.95300   14.34100  1.000 26.17945 ? 150 LEU A CA     1 
ATOM   1102 C  C      . LEU A 1 154 ? -42.34600 3.82600   13.19900  1.000 23.03697 ? 150 LEU A C      1 
ATOM   1103 O  O      . LEU A 1 154 ? -42.98900 2.78500   13.04200  1.000 23.75022 ? 150 LEU A O      1 
ATOM   1104 C  CB     . LEU A 1 154 ? -41.96200 4.67500   15.54000  1.000 25.87679 ? 150 LEU A CB     1 
ATOM   1105 C  CG     . LEU A 1 154 ? -41.08000 4.79000   16.79000  1.000 31.96173 ? 150 LEU A CG     1 
ATOM   1106 C  CD1    . LEU A 1 154 ? -41.74500 5.61300   17.88600  1.000 24.18974 ? 150 LEU A CD1    1 
ATOM   1107 C  CD2    . LEU A 1 154 ? -40.72100 3.43000   17.31300  1.000 34.64100 ? 150 LEU A CD2    1 
ATOM   1108 N  N      . ARG A 1 155 ? -42.49500 4.87900   12.39100  1.000 25.91627 ? 151 ARG A N      1 
ATOM   1109 C  CA     . ARG A 1 155 ? -43.36300 4.81000   11.21300  1.000 25.05827 ? 151 ARG A CA     1 
ATOM   1110 C  C      . ARG A 1 155 ? -42.88400 3.74900   10.23300  1.000 30.25363 ? 151 ARG A C      1 
ATOM   1111 O  O      . ARG A 1 155 ? -43.69900 3.01400   9.65400   1.000 22.71588 ? 151 ARG A O      1 
ATOM   1112 C  CB     . ARG A 1 155 ? -43.41200 6.17400   10.51900  1.000 23.43702 ? 151 ARG A CB     1 
ATOM   1113 C  CG     . ARG A 1 155 ? -44.02500 6.15200   9.11200   1.000 26.47159 ? 151 ARG A CG     1 
ATOM   1114 C  CD     . ARG A 1 155 ? -44.26600 7.57600   8.52900   1.000 21.12359 ? 151 ARG A CD     1 
ATOM   1115 N  NE     . ARG A 1 155 ? -43.03700 8.34900   8.36700   1.000 26.17156 ? 151 ARG A NE     1 
ATOM   1116 C  CZ     . ARG A 1 155 ? -42.63200 9.32700   9.17700   1.000 28.73502 ? 151 ARG A CZ     1 
ATOM   1117 N  NH1    . ARG A 1 155 ? -43.36100 9.66300   10.23400  1.000 26.00312 ? 151 ARG A NH1    1 
ATOM   1118 N  NH2    . ARG A 1 155 ? -41.48600 9.95900   8.93500   1.000 22.04475 ? 151 ARG A NH2    1 
ATOM   1119 N  N      . THR A 1 156 ? -41.56400 3.69800   9.98800   1.000 22.95275 ? 152 THR A N      1 
ATOM   1120 C  CA     . THR A 1 156 ? -41.03000 2.80600   8.96500   1.000 27.02429 ? 152 THR A CA     1 
ATOM   1121 C  C      . THR A 1 156 ? -41.16100 1.35300   9.39200   1.000 29.65356 ? 152 THR A C      1 
ATOM   1122 O  O      . THR A 1 156 ? -41.53500 0.50000   8.58100   1.000 24.26870 ? 152 THR A O      1 
ATOM   1123 C  CB     . THR A 1 156 ? -39.55800 3.15100   8.67700   1.000 27.95335 ? 152 THR A CB     1 
ATOM   1124 O  OG1    . THR A 1 156 ? -39.46800 4.52900   8.30600   1.000 25.56359 ? 152 THR A OG1    1 
ATOM   1125 C  CG2    . THR A 1 156 ? -39.02700 2.32600   7.54200   1.000 20.61826 ? 152 THR A CG2    1 
ATOM   1126 N  N      . ALA A 1 157 ? -40.90100 1.06600   10.67800  1.000 21.43678 ? 153 ALA A N      1 
ATOM   1127 C  CA     . ALA A 1 157 ? -40.94500 -0.30800  11.17100  1.000 24.97931 ? 153 ALA A CA     1 
ATOM   1128 C  C      . ALA A 1 157 ? -42.33600 -0.90400  11.05800  1.000 23.60020 ? 153 ALA A C      1 
ATOM   1129 O  O      . ALA A 1 157 ? -42.48600 -2.10900  10.83000  1.000 25.00826 ? 153 ALA A O      1 
ATOM   1130 C  CB     . ALA A 1 157 ? -40.48500 -0.36900  12.63000  1.000 17.91794 ? 153 ALA A CB     1 
ATOM   1131 N  N      . GLN A 1 158 ? -43.37000 -0.09700  11.27600  1.000 25.62149 ? 154 GLN A N      1 
ATOM   1132 C  CA     . GLN A 1 158 ? -44.70700 -0.64100  11.46400  1.000 22.92643 ? 154 GLN A CA     1 
ATOM   1133 C  C      . GLN A 1 158 ? -45.65400 -0.33200  10.31300  1.000 30.34838 ? 154 GLN A C      1 
ATOM   1134 O  O      . GLN A 1 158 ? -46.82400 -0.72100  10.37700  1.000 37.87823 ? 154 GLN A O      1 
ATOM   1135 C  CB     . GLN A 1 158 ? -45.28800 -0.13000  12.79000  1.000 21.47889 ? 154 GLN A CB     1 
ATOM   1136 C  CG     . GLN A 1 158 ? -44.42700 -0.50500  13.97500  1.000 28.54026 ? 154 GLN A CG     1 
ATOM   1137 C  CD     . GLN A 1 158 ? -44.84600 0.18100   15.25400  1.000 31.91698 ? 154 GLN A CD     1 
ATOM   1138 O  OE1    . GLN A 1 158 ? -45.53100 -0.41500  16.10000  1.000 28.09284 ? 154 GLN A OE1    1 
ATOM   1139 N  NE2    . GLN A 1 158 ? -44.43800 1.44200   15.41000  1.000 30.87212 ? 154 GLN A NE2    1 
ATOM   1140 N  N      . SER A 1 159 ? -45.17900 0.32000   9.25600   1.000 24.35029 ? 155 SER A N      1 
ATOM   1141 C  CA     . SER A 1 159 ? -45.98500 0.64600   8.08800   1.000 28.12706 ? 155 SER A CA     1 
ATOM   1142 C  C      . SER A 1 159 ? -45.62700 -0.28200  6.94300   1.000 29.49301 ? 155 SER A C      1 
ATOM   1143 O  O      . SER A 1 159 ? -44.55200 -0.88100  6.92500   1.000 26.51107 ? 155 SER A O      1 
ATOM   1144 C  CB     . SER A 1 159 ? -45.74000 2.09100   7.65000   1.000 29.05348 ? 155 SER A CB     1 
ATOM   1145 O  OG     . SER A 1 159 ? -46.11100 3.00500   8.66000   1.000 26.31105 ? 155 SER A OG     1 
ATOM   1146 N  N      . GLY A 1 160 ? -46.53400 -0.38900  5.97400   1.000 26.33474 ? 156 GLY A N      1 
ATOM   1147 C  CA     . GLY A 1 160 ? -46.31100 -1.33600  4.89300   1.000 25.65044 ? 156 GLY A CA     1 
ATOM   1148 C  C      . GLY A 1 160 ? -45.97800 -2.72800  5.40500   1.000 22.48427 ? 156 GLY A C      1 
ATOM   1149 O  O      . GLY A 1 160 ? -46.54100 -3.21500  6.39300   1.000 27.68490 ? 156 GLY A O      1 
ATOM   1150 N  N      . ARG A 1 161 ? -45.05000 -3.37800  4.73100   1.000 22.90275 ? 157 ARG A N      1 
ATOM   1151 C  CA     . ARG A 1 161 ? -44.54400 -4.64700  5.21900   1.000 23.66600 ? 157 ARG A CA     1 
ATOM   1152 C  C      . ARG A 1 161 ? -43.66600 -4.35900  6.42800   1.000 25.79257 ? 157 ARG A C      1 
ATOM   1153 O  O      . ARG A 1 161 ? -42.63200 -3.69800  6.28000   1.000 24.25291 ? 157 ARG A O      1 
ATOM   1154 C  CB     . ARG A 1 161 ? -43.75200 -5.35600  4.12800   1.000 26.63477 ? 157 ARG A CB     1 
ATOM   1155 C  CG     . ARG A 1 161 ? -43.39200 -6.79900  4.46700   1.000 28.53237 ? 157 ARG A CG     1 
ATOM   1156 C  CD     . ARG A 1 161 ? -42.46500 -7.36700  3.42100   1.000 23.10540 ? 157 ARG A CD     1 
ATOM   1157 N  NE     . ARG A 1 161 ? -42.11900 -8.75700  3.69200   1.000 21.79472 ? 157 ARG A NE     1 
ATOM   1158 C  CZ     . ARG A 1 161 ? -41.81500 -9.63400  2.74600   1.000 26.90323 ? 157 ARG A CZ     1 
ATOM   1159 N  NH1    . ARG A 1 161 ? -41.84600 -9.26700  1.46400   1.000 23.18436 ? 157 ARG A NH1    1 
ATOM   1160 N  NH2    . ARG A 1 161 ? -41.50200 -10.87900 3.07800   1.000 24.33713 ? 157 ARG A NH2    1 
ATOM   1161 N  N      . PRO A 1 162 ? -44.03800 -4.79400  7.62000   1.000 24.10815 ? 158 PRO A N      1 
ATOM   1162 C  CA     . PRO A 1 162 ? -43.27700 -4.40600  8.81700   1.000 23.99235 ? 158 PRO A CA     1 
ATOM   1163 C  C      . PRO A 1 162 ? -41.86500 -4.96100  8.77100   1.000 24.81087 ? 158 PRO A C      1 
ATOM   1164 O  O      . PRO A 1 162 ? -41.60500 -6.00900  8.17200   1.000 22.91854 ? 158 PRO A O      1 
ATOM   1165 C  CB     . PRO A 1 162 ? -44.07900 -5.02400  9.96900   1.000 24.30818 ? 158 PRO A CB     1 
ATOM   1166 C  CG     . PRO A 1 162 ? -45.42400 -5.28700  9.41000   1.000 26.05839 ? 158 PRO A CG     1 
ATOM   1167 C  CD     . PRO A 1 162 ? -45.20000 -5.62700  7.95000   1.000 24.77929 ? 158 PRO A CD     1 
ATOM   1168 N  N      . GLY A 1 163 ? -40.94700 -4.26500  9.43600   1.000 23.31069 ? 159 GLY A N      1 
ATOM   1169 C  CA     . GLY A 1 163 ? -39.57800 -4.72900  9.48400   1.000 21.57364 ? 159 GLY A CA     1 
ATOM   1170 C  C      . GLY A 1 163 ? -38.72400 -3.94700  10.45700  1.000 25.87152 ? 159 GLY A C      1 
ATOM   1171 O  O      . GLY A 1 163 ? -39.16200 -2.94300  11.02500  1.000 26.09523 ? 159 GLY A O      1 
ATOM   1172 N  N      . PRO A 1 164 ? -37.47500 -4.36900  10.63800  1.000 25.58728 ? 160 PRO A N      1 
ATOM   1173 C  CA     . PRO A 1 164 ? -36.61500 -3.75400  11.65600  1.000 24.04499 ? 160 PRO A CA     1 
ATOM   1174 C  C      . PRO A 1 164 ? -35.94700 -2.46500  11.18900  1.000 26.85322 ? 160 PRO A C      1 
ATOM   1175 O  O      . PRO A 1 164 ? -35.82800 -2.16200  10.00000  1.000 22.92117 ? 160 PRO A O      1 
ATOM   1176 C  CB     . PRO A 1 164 ? -35.55700 -4.83200  11.92500  1.000 22.65798 ? 160 PRO A CB     1 
ATOM   1177 C  CG     . PRO A 1 164 ? -35.44500 -5.58400  10.59800  1.000 20.73670 ? 160 PRO A CG     1 
ATOM   1178 C  CD     . PRO A 1 164 ? -36.85500 -5.55900  10.01400  1.000 19.58919 ? 160 PRO A CD     1 
ATOM   1179 N  N      . ILE A 1 165 ? -35.47800 -1.71700  12.18300  1.000 29.19034 ? 161 ILE A N      1 
ATOM   1180 C  CA     . ILE A 1 165 ? -34.85600 -0.41100  12.01400  1.000 23.74232 ? 161 ILE A CA     1 
ATOM   1181 C  C      . ILE A 1 165 ? -33.58100 -0.39800  12.83700  1.000 22.50270 ? 161 ILE A C      1 
ATOM   1182 O  O      . ILE A 1 165 ? -33.51900 -0.99700  13.91500  1.000 24.78455 ? 161 ILE A O      1 
ATOM   1183 C  CB     . ILE A 1 165 ? -35.77000 0.74400   12.48300  1.000 21.72892 ? 161 ILE A CB     1 
ATOM   1184 C  CG1    . ILE A 1 165 ? -37.17000 0.62500   11.89400  1.000 19.42865 ? 161 ILE A CG1    1 
ATOM   1185 C  CG2    . ILE A 1 165 ? -35.12400 2.07700   12.12400  1.000 19.75500 ? 161 ILE A CG2    1 
ATOM   1186 C  CD1    . ILE A 1 165 ? -37.20300 0.83200   10.39200  1.000 20.11820 ? 161 ILE A CD1    1 
ATOM   1187 N  N      . HIS A 1 166 ? -32.56300 0.29700   12.33100  1.000 23.72127 ? 162 HIS A N      1 
ATOM   1188 C  CA     . HIS A 1 166 ? -31.32200 0.54700   13.06500  1.000 20.15242 ? 162 HIS A CA     1 
ATOM   1189 C  C      . HIS A 1 166 ? -31.15700 2.05100   13.25600  1.000 20.21821 ? 162 HIS A C      1 
ATOM   1190 O  O      . HIS A 1 166 ? -31.03500 2.78800   12.27400  1.000 25.35830 ? 162 HIS A O      1 
ATOM   1191 C  CB     . HIS A 1 166 ? -30.11500 -0.04400  12.32000  1.000 21.81314 ? 162 HIS A CB     1 
ATOM   1192 C  CG     . HIS A 1 166 ? -28.79300 0.36400   12.89500  1.000 27.04798 ? 162 HIS A CG     1 
ATOM   1193 N  ND1    . HIS A 1 166 ? -27.78800 0.92400   12.13300  1.000 23.61862 ? 162 HIS A ND1    1 
ATOM   1194 C  CD2    . HIS A 1 166 ? -28.31900 0.30900   14.16500  1.000 26.89533 ? 162 HIS A CD2    1 
ATOM   1195 C  CE1    . HIS A 1 166 ? -26.74300 1.17700   12.90400  1.000 26.90059 ? 162 HIS A CE1    1 
ATOM   1196 N  NE2    . HIS A 1 166 ? -27.03600 0.80800   14.14000  1.000 27.94282 ? 162 HIS A NE2    1 
ATOM   1197 N  N      . LEU A 1 167 ? -31.17700 2.51100   14.51500  1.000 21.11832 ? 163 LEU A N      1 
ATOM   1198 C  CA     . LEU A 1 167 ? -30.89900 3.90500   14.86100  1.000 18.48906 ? 163 LEU A CA     1 
ATOM   1199 C  C      . LEU A 1 167 ? -29.58600 3.98000   15.63300  1.000 28.11127 ? 163 LEU A C      1 
ATOM   1200 O  O      . LEU A 1 167 ? -29.46500 3.40800   16.72400  1.000 26.05839 ? 163 LEU A O      1 
ATOM   1201 C  CB     . LEU A 1 167 ? -32.00800 4.51300   15.71600  1.000 27.27959 ? 163 LEU A CB     1 
ATOM   1202 C  CG     . LEU A 1 167 ? -33.24700 5.09900   15.05800  1.000 34.78049 ? 163 LEU A CG     1 
ATOM   1203 C  CD1    . LEU A 1 167 ? -34.07900 5.79700   16.12400  1.000 32.37757 ? 163 LEU A CD1    1 
ATOM   1204 C  CD2    . LEU A 1 167 ? -32.88200 6.05100   13.90900  1.000 30.64315 ? 163 LEU A CD2    1 
ATOM   1205 N  N      . ASN A 1 168 ? -28.62600 4.71300   15.08700  1.000 27.87966 ? 164 ASN A N      1 
ATOM   1206 C  CA     . ASN A 1 168 ? -27.29800 4.84900   15.66600  1.000 24.45293 ? 164 ASN A CA     1 
ATOM   1207 C  C      . ASN A 1 168 ? -27.16300 6.24000   16.27600  1.000 25.93732 ? 164 ASN A C      1 
ATOM   1208 O  O      . ASN A 1 168 ? -27.39900 7.24200   15.59700  1.000 28.11390 ? 164 ASN A O      1 
ATOM   1209 C  CB     . ASN A 1 168 ? -26.25300 4.61500   14.57500  1.000 23.48703 ? 164 ASN A CB     1 
ATOM   1210 C  CG     . ASN A 1 168 ? -24.85500 4.71700   15.08500  1.000 27.31117 ? 164 ASN A CG     1 
ATOM   1211 O  OD1    . ASN A 1 168 ? -24.09700 5.60900   14.67800  1.000 27.82702 ? 164 ASN A OD1    1 
ATOM   1212 N  ND2    . ASN A 1 168 ? -24.48600 3.79900   15.98400  1.000 29.45616 ? 164 ASN A ND2    1 
ATOM   1213 N  N      . ILE A 1 169 ? -26.73700 6.30500   17.53400  1.000 28.77187 ? 165 ILE A N      1 
ATOM   1214 C  CA     . ILE A 1 169 ? -26.83500 7.54200   18.31200  1.000 24.64769 ? 165 ILE A CA     1 
ATOM   1215 C  C      . ILE A 1 169 ? -25.47200 7.98900   18.83900  1.000 29.32983 ? 165 ILE A C      1 
ATOM   1216 O  O      . ILE A 1 169 ? -24.90700 7.33000   19.72200  1.000 27.80597 ? 165 ILE A O      1 
ATOM   1217 C  CB     . ILE A 1 169 ? -27.81000 7.36100   19.48400  1.000 31.22216 ? 165 ILE A CB     1 
ATOM   1218 C  CG1    . ILE A 1 169 ? -29.16100 6.83300   18.97400  1.000 36.50701 ? 165 ILE A CG1    1 
ATOM   1219 C  CG2    . ILE A 1 169 ? -27.95000 8.68000   20.25000  1.000 29.81936 ? 165 ILE A CG2    1 
ATOM   1220 C  CD1    . ILE A 1 169 ? -30.08600 6.29000   20.05800  1.000 33.24609 ? 165 ILE A CD1    1 
ATOM   1221 N  N      . PRO A 1 170 ? -24.90100 9.08700   18.34700  1.000 29.56933 ? 166 PRO A N      1 
ATOM   1222 C  CA     . PRO A 1 170 ? -23.61800 9.54200   18.89900  1.000 27.76912 ? 166 PRO A CA     1 
ATOM   1223 C  C      . PRO A 1 170 ? -23.74000 9.88900   20.37900  1.000 39.00731 ? 166 PRO A C      1 
ATOM   1224 O  O      . PRO A 1 170 ? -24.72800 10.48800  20.82600  1.000 31.60116 ? 166 PRO A O      1 
ATOM   1225 C  CB     . PRO A 1 170 ? -23.27700 10.76800  18.04500  1.000 28.96663 ? 166 PRO A CB     1 
ATOM   1226 C  CG     . PRO A 1 170 ? -24.05900 10.56700  16.78100  1.000 30.54314 ? 166 PRO A CG     1 
ATOM   1227 C  CD     . PRO A 1 170 ? -25.33100 9.91100   17.20700  1.000 26.35842 ? 166 PRO A CD     1 
ATOM   1228 N  N      . ALA A 1 171 ? -22.71300 9.50200   21.14400  1.000 30.56156 ? 167 ALA A N      1 
ATOM   1229 C  CA     . ALA A 1 171 ? -22.80100 9.61200   22.59400  1.000 34.50677 ? 167 ALA A CA     1 
ATOM   1230 C  C      . ALA A 1 171 ? -22.87700 11.06300  23.04900  1.000 30.75369 ? 167 ALA A C      1 
ATOM   1231 O  O      . ALA A 1 171 ? -23.52600 11.35400  24.05800  1.000 41.48919 ? 167 ALA A O      1 
ATOM   1232 C  CB     . ALA A 1 171 ? -21.60400 8.91700   23.24700  1.000 37.70189 ? 167 ALA A CB     1 
ATOM   1233 N  N      . ASP A 1 172 ? -22.28300 11.99400  22.30100  1.000 29.95359 ? 168 ASP A N      1 
ATOM   1234 C  CA     . ASP A 1 172 ? -22.33500 13.38900  22.74100  1.000 38.63621 ? 168 ASP A CA     1 
ATOM   1235 C  C      . ASP A 1 172 ? -23.70600 14.00300  22.48100  1.000 43.29993 ? 168 ASP A C      1 
ATOM   1236 O  O      . ASP A 1 172 ? -24.17200 14.82600  23.27300  1.000 53.60643 ? 168 ASP A O      1 
ATOM   1237 C  CB     . ASP A 1 172 ? -21.22100 14.21000  22.07200  1.000 36.23066 ? 168 ASP A CB     1 
ATOM   1238 C  CG     . ASP A 1 172 ? -21.22300 14.08700  20.55300  1.000 47.05038 ? 168 ASP A CG     1 
ATOM   1239 O  OD1    . ASP A 1 172 ? -21.76400 13.09700  20.02000  1.000 51.31931 ? 168 ASP A OD1    1 
ATOM   1240 O  OD2    . ASP A 1 172 ? -20.67000 14.98300  19.88400  1.000 55.91460 ? 168 ASP A OD2    1 
ATOM   1241 N  N      . ILE A 1 173 ? -24.36500 13.59500  21.39400  1.000 36.56754 ? 169 ILE A N      1 
ATOM   1242 C  CA     . ILE A 1 173 ? -25.73000 14.02600  21.09100  1.000 41.16020 ? 169 ILE A CA     1 
ATOM   1243 C  C      . ILE A 1 173 ? -26.71700 13.57500  22.16900  1.000 34.39886 ? 169 ILE A C      1 
ATOM   1244 O  O      . ILE A 1 173 ? -27.72100 14.25200  22.43500  1.000 31.89856 ? 169 ILE A O      1 
ATOM   1245 C  CB     . ILE A 1 173 ? -26.11900 13.47800  19.69600  1.000 41.15230 ? 169 ILE A CB     1 
ATOM   1246 C  CG1    . ILE A 1 173 ? -25.39600 14.25400  18.59700  1.000 43.28940 ? 169 ILE A CG1    1 
ATOM   1247 C  CG2    . ILE A 1 173 ? -27.61100 13.42600  19.50100  1.000 43.34730 ? 169 ILE A CG2    1 
ATOM   1248 C  CD1    . ILE A 1 173 ? -25.18300 15.69000  18.92900  1.000 55.78564 ? 169 ILE A CD1    1 
ATOM   1249 N  N      . ALA A 1 174 ? -26.43500 12.44800  22.82600  1.000 29.27456 ? 170 ALA A N      1 
ATOM   1250 C  CA     . ALA A 1 174 ? -27.45000 11.78100  23.63000  1.000 34.18831 ? 170 ALA A CA     1 
ATOM   1251 C  C      . ALA A 1 174 ? -27.99000 12.66700  24.74700  1.000 35.53584 ? 170 ALA A C      1 
ATOM   1252 O  O      . ALA A 1 174 ? -29.16500 12.55000  25.11100  1.000 36.60702 ? 170 ALA A O      1 
ATOM   1253 C  CB     . ALA A 1 174 ? -26.88500 10.48700  24.20700  1.000 34.73311 ? 170 ALA A CB     1 
ATOM   1254 N  N      . LYS A 1 175 ? -27.16300 13.53400  25.32900  1.000 34.29885 ? 171 LYS A N      1 
ATOM   1255 C  CA     . LYS A 1 175 ? -27.60500 14.32800  26.46900  1.000 40.99702 ? 171 LYS A CA     1 
ATOM   1256 C  C      . LYS A 1 175 ? -27.75500 15.81200  26.14800  1.000 40.32589 ? 171 LYS A C      1 
ATOM   1257 O  O      . LYS A 1 175 ? -27.89700 16.62300  27.06500  1.000 39.25207 ? 171 LYS A O      1 
ATOM   1258 C  CB     . LYS A 1 175 ? -26.65600 14.13700  27.65600  1.000 42.14716 ? 171 LYS A CB     1 
ATOM   1259 C  CG     . LYS A 1 175 ? -26.52700 12.67500  28.09900  1.000 49.84808 ? 171 LYS A CG     1 
ATOM   1260 C  CD     . LYS A 1 175 ? -25.89300 12.53600  29.48400  1.000 50.99032 ? 171 LYS A CD     1 
ATOM   1261 C  CE     . LYS A 1 175 ? -26.84900 13.00400  30.57600  1.000 47.74783 ? 171 LYS A CE     1 
ATOM   1262 N  NZ     . LYS A 1 175 ? -26.35300 12.67100  31.94600  1.000 49.12957 ? 171 LYS A NZ     1 
ATOM   1263 N  N      . HIS A 1 176 ? -27.79400 16.18500  24.87600  1.000 36.20960 ? 172 HIS A N      1 
ATOM   1264 C  CA     . HIS A 1 176 ? -28.11500 17.56400  24.56300  1.000 34.98577 ? 172 HIS A CA     1 
ATOM   1265 C  C      . HIS A 1 176 ? -29.60300 17.81200  24.80400  1.000 36.49122 ? 172 HIS A C      1 
ATOM   1266 O  O      . HIS A 1 176 ? -30.44000 16.92600  24.59100  1.000 34.86207 ? 172 HIS A O      1 
ATOM   1267 C  CB     . HIS A 1 176 ? -27.75900 17.89800  23.11800  1.000 41.90502 ? 172 HIS A CB     1 
ATOM   1268 C  CG     . HIS A 1 176 ? -26.28700 17.90700  22.84500  1.000 50.09285 ? 172 HIS A CG     1 
ATOM   1269 N  ND1    . HIS A 1 176 ? -25.76400 17.83800  21.57100  1.000 52.41944 ? 172 HIS A ND1    1 
ATOM   1270 C  CD2    . HIS A 1 176 ? -25.22600 17.97300  23.68400  1.000 53.22480 ? 172 HIS A CD2    1 
ATOM   1271 C  CE1    . HIS A 1 176 ? -24.44500 17.86100  21.63600  1.000 54.17755 ? 172 HIS A CE1    1 
ATOM   1272 N  NE2    . HIS A 1 176 ? -24.09300 17.94400  22.90700  1.000 53.28270 ? 172 HIS A NE2    1 
ATOM   1273 N  N      . PRO A 1 177 ? -29.96200 19.01100  25.24200  1.000 36.42279 ? 173 PRO A N      1 
ATOM   1274 C  CA     . PRO A 1 177 ? -31.37500 19.30400  25.49300  1.000 38.11246 ? 173 PRO A CA     1 
ATOM   1275 C  C      . PRO A 1 177 ? -32.12300 19.47400  24.18400  1.000 41.17073 ? 173 PRO A C      1 
ATOM   1276 O  O      . PRO A 1 177 ? -31.58900 20.01200  23.21000  1.000 45.32649 ? 173 PRO A O      1 
ATOM   1277 C  CB     . PRO A 1 177 ? -31.33600 20.62200  26.28200  1.000 39.95216 ? 173 PRO A CB     1 
ATOM   1278 C  CG     . PRO A 1 177 ? -29.87700 20.95700  26.48500  1.000 40.14692 ? 173 PRO A CG     1 
ATOM   1279 C  CD     . PRO A 1 177 ? -29.08700 20.16400  25.50800  1.000 38.22564 ? 173 PRO A CD     1 
ATOM   1280 N  N      . VAL A 1 178 ? -33.35500 18.97200  24.15700  1.000 38.91256 ? 174 VAL A N      1 
ATOM   1281 C  CA     . VAL A 1 178 ? -34.24400 19.13300  23.00700  1.000 35.96484 ? 174 VAL A CA     1 
ATOM   1282 C  C      . VAL A 1 178 ? -35.63100 19.47500  23.51100  1.000 37.89665 ? 174 VAL A C      1 
ATOM   1283 O  O      . VAL A 1 178 ? -36.00200 19.12500  24.63900  1.000 32.92763 ? 174 VAL A O      1 
ATOM   1284 C  CB     . VAL A 1 178 ? -34.31100 17.86300  22.13000  1.000 35.68323 ? 174 VAL A CB     1 
ATOM   1285 C  CG1    . VAL A 1 178 ? -32.91400 17.37100  21.74400  1.000 36.49648 ? 174 VAL A CG1    1 
ATOM   1286 C  CG2    . VAL A 1 178 ? -35.14000 16.76300  22.82000  1.000 28.72713 ? 174 VAL A CG2    1 
ATOM   1287 N  N      . PRO A 1 179 ? -36.44000 20.12300  22.67300  1.000 41.05755 ? 175 PRO A N      1 
ATOM   1288 C  CA     . PRO A 1 179 ? -37.82600 20.41000  23.06200  1.000 41.10756 ? 175 PRO A CA     1 
ATOM   1289 C  C      . PRO A 1 179 ? -38.59300 19.13100  23.36700  1.000 41.51024 ? 175 PRO A C      1 
ATOM   1290 O  O      . PRO A 1 179 ? -38.49000 18.13600  22.64600  1.000 34.93840 ? 175 PRO A O      1 
ATOM   1291 C  CB     . PRO A 1 179 ? -38.39500 21.12400  21.83000  1.000 42.34718 ? 175 PRO A CB     1 
ATOM   1292 C  CG     . PRO A 1 179 ? -37.17600 21.72400  21.15200  1.000 41.67079 ? 175 PRO A CG     1 
ATOM   1293 C  CD     . PRO A 1 179 ? -36.06600 20.75300  21.39400  1.000 42.70512 ? 175 PRO A CD     1 
ATOM   1294 N  N      . LEU A 1 180 ? -39.38800 19.16600  24.44000  1.000 39.30998 ? 176 LEU A N      1 
ATOM   1295 C  CA     . LEU A 1 180 ? -40.16200 17.98700  24.83200  1.000 41.47866 ? 176 LEU A CA     1 
ATOM   1296 C  C      . LEU A 1 180 ? -41.37700 17.88700  23.91700  1.000 44.12634 ? 176 LEU A C      1 
ATOM   1297 O  O      . LEU A 1 180 ? -42.39100 18.54200  24.14300  1.000 48.99008 ? 176 LEU A O      1 
ATOM   1298 C  CB     . LEU A 1 180 ? -40.56200 18.06100  26.30000  1.000 36.17013 ? 176 LEU A CB     1 
ATOM   1299 C  CG     . LEU A 1 180 ? -41.45400 16.92600  26.81600  1.000 35.25423 ? 176 LEU A CG     1 
ATOM   1300 C  CD1    . LEU A 1 180 ? -40.83700 15.57800  26.53000  1.000 39.09153 ? 176 LEU A CD1    1 
ATOM   1301 C  CD2    . LEU A 1 180 ? -41.70600 17.07900  28.32300  1.000 42.18927 ? 176 LEU A CD2    1 
ATOM   1302 N  N      . GLU A 1 181 ? -41.28200 17.07600  22.88500  1.000 44.51586 ? 177 GLU A N      1 
ATOM   1303 C  CA     . GLU A 1 181 ? -42.31300 16.91100  21.89400  1.000 39.32050 ? 177 GLU A CA     1 
ATOM   1304 C  C      . GLU A 1 181 ? -42.52800 15.46100  21.53600  1.000 32.90921 ? 177 GLU A C      1 
ATOM   1305 O  O      . GLU A 1 181 ? -41.80000 14.87400  20.79300  1.000 35.73323 ? 177 GLU A O      1 
ATOM   1306 C  CB     . GLU A 1 181 ? -41.94400 17.70700  20.67000  1.000 49.76386 ? 177 GLU A CB     1 
ATOM   1307 C  CG     . GLU A 1 181 ? -42.50700 19.10700  20.66100  1.000 64.33403 ? 177 GLU A CG     1 
ATOM   1308 C  CD     . GLU A 1 181 ? -43.99000 19.07700  20.39000  1.000 76.77499 ? 177 GLU A CD     1 
ATOM   1309 O  OE1    . GLU A 1 181 ? -44.49300 19.87100  19.59400  1.000 78.58574 ? 177 GLU A OE1    1 
ATOM   1310 O  OE2    . GLU A 1 181 ? -44.64300 18.19200  20.94900  1.000 81.68611 ? 177 GLU A OE2    1 
ATOM   1311 N  N      . VAL A 1 182 ? -43.57400 14.91400  22.09100  1.000 32.91974 ? 178 VAL A N      1 
ATOM   1312 C  CA     . VAL A 1 182 ? -43.94100 13.53500  21.96000  1.000 37.95718 ? 178 VAL A CA     1 
ATOM   1313 C  C      . VAL A 1 182 ? -45.30700 13.44700  21.31400  1.000 38.89414 ? 178 VAL A C      1 
ATOM   1314 O  O      . VAL A 1 182 ? -46.20100 14.16300  21.65100  1.000 36.84126 ? 178 VAL A O      1 
ATOM   1315 C  CB     . VAL A 1 182 ? -43.95100 12.88600  23.34500  1.000 35.53847 ? 178 VAL A CB     1 
ATOM   1316 C  CG1    . VAL A 1 182 ? -44.34600 11.44400  23.27600  1.000 33.88038 ? 178 VAL A CG1    1 
ATOM   1317 C  CG2    . VAL A 1 182 ? -42.62400 13.04300  24.02100  1.000 32.59075 ? 178 VAL A CG2    1 
ATOM   1318 N  N      . PHE A 1 183 ? -45.46500 12.52300  20.40200  1.000 34.99367 ? 179 PHE A N      1 
ATOM   1319 C  CA     . PHE A 1 183 ? -46.70900 12.42100  19.65500  1.000 34.57520 ? 179 PHE A CA     1 
ATOM   1320 C  C      . PHE A 1 183 ? -47.32000 11.03300  19.82500  1.000 26.08997 ? 179 PHE A C      1 
ATOM   1321 O  O      . PHE A 1 183 ? -46.59900 10.04100  19.91900  1.000 28.14285 ? 179 PHE A O      1 
ATOM   1322 C  CB     . PHE A 1 183 ? -46.49400 12.66500  18.15000  1.000 31.21427 ? 179 PHE A CB     1 
ATOM   1323 C  CG     . PHE A 1 183 ? -46.00500 14.04700  17.80400  1.000 35.10947 ? 179 PHE A CG     1 
ATOM   1324 C  CD1    . PHE A 1 183 ? -44.67200 14.38400  17.94800  1.000 34.29359 ? 179 PHE A CD1    1 
ATOM   1325 C  CD2    . PHE A 1 183 ? -46.88200 14.99900  17.30400  1.000 42.56563 ? 179 PHE A CD2    1 
ATOM   1326 C  CE1    . PHE A 1 183 ? -44.22200 15.65200  17.61900  1.000 35.51478 ? 179 PHE A CE1    1 
ATOM   1327 C  CE2    . PHE A 1 183 ? -46.43800 16.26600  16.96900  1.000 41.27600 ? 179 PHE A CE2    1 
ATOM   1328 C  CZ     . PHE A 1 183 ? -45.10600 16.59100  17.12700  1.000 38.28617 ? 179 PHE A CZ     1 
ATOM   1329 N  N      . PRO A 1 184 ? -48.65500 10.93300  19.81300  1.000 27.71122 ? 180 PRO A N      1 
ATOM   1330 C  CA     . PRO A 1 184 ? -49.25200 9.58800   19.70500  1.000 32.45389 ? 180 PRO A CA     1 
ATOM   1331 C  C      . PRO A 1 184 ? -48.96700 8.99600   18.38900  1.000 34.83839 ? 180 PRO A C      1 
ATOM   1332 O  O      . PRO A 1 184 ? -48.79700 9.69600   17.35400  1.000 33.59087 ? 180 PRO A O      1 
ATOM   1333 C  CB     . PRO A 1 184 ? -50.76600 9.89100   19.89200  1.000 33.44875 ? 180 PRO A CB     1 
ATOM   1334 C  CG     . PRO A 1 184 ? -50.92900 11.34000  19.55500  1.000 35.70691 ? 180 PRO A CG     1 
ATOM   1335 C  CD     . PRO A 1 184 ? -49.63600 12.01400  19.91500  1.000 34.64100 ? 180 PRO A CD     1 
ATOM   1336 N  N      . PRO A 1 185 ? -48.88000 7.65800   18.26900  1.000 33.68035 ? 181 PRO A N      1 
ATOM   1337 C  CA     . PRO A 1 185 ? -48.50200 7.02100   17.00300  1.000 33.90670 ? 181 PRO A CA     1 
ATOM   1338 C  C      . PRO A 1 185 ? -49.33600 7.43500   15.79400  1.000 38.83624 ? 181 PRO A C      1 
ATOM   1339 O  O      . PRO A 1 185 ? -48.77100 7.47600   14.68600  1.000 38.42040 ? 181 PRO A O      1 
ATOM   1340 C  CB     . PRO A 1 185 ? -48.67100 5.53000   17.30800  1.000 34.93840 ? 181 PRO A CB     1 
ATOM   1341 C  CG     . PRO A 1 185 ? -48.37500 5.43100   18.77700  1.000 40.56802 ? 181 PRO A CG     1 
ATOM   1342 C  CD     . PRO A 1 185 ? -48.96300 6.68500   19.38300  1.000 37.30974 ? 181 PRO A CD     1 
ATOM   1343 N  N      . MET A 1 186 ? -50.63700 7.74600   15.95300  1.000 30.71158 ? 182 MET A N      1 
ATOM   1344 C  CA     . MET A 1 186 ? -51.49000 8.02900   14.79600  1.000 38.85992 ? 182 MET A CA     1 
ATOM   1345 C  C      . MET A 1 186 ? -51.15000 9.34400   14.11100  1.000 36.34383 ? 182 MET A C      1 
ATOM   1346 O  O      . MET A 1 186 ? -51.53600 9.53800   12.95800  1.000 37.03602 ? 182 MET A O      1 
ATOM   1347 C  CB     . MET A 1 186 ? -52.98900 8.03600   15.18600  1.000 44.63430 ? 182 MET A CB     1 
ATOM   1348 C  CG     . MET A 1 186 ? -53.43200 9.02700   16.28200  1.000 59.57556 ? 182 MET A CG     1 
ATOM   1349 S  SD     . MET A 1 186 ? -55.07300 9.81200   16.04400  1.000 73.75621 ? 182 MET A SD     1 
ATOM   1350 C  CE     . MET A 1 186 ? -54.73300 10.78800  14.55900  1.000 66.88170 ? 182 MET A CE     1 
ATOM   1351 N  N      . ASN A 1 187 ? -50.41200 10.23800  14.77700  1.000 33.18556 ? 183 ASN A N      1 
ATOM   1352 C  CA     . ASN A 1 187 ? -50.02300 11.50700  14.17000  1.000 31.60379 ? 183 ASN A CA     1 
ATOM   1353 C  C      . ASN A 1 187 ? -48.85500 11.36400  13.19500  1.000 31.18795 ? 183 ASN A C      1 
ATOM   1354 O  O      . ASN A 1 187 ? -48.65900 12.24500  12.34600  1.000 32.35388 ? 183 ASN A O      1 
ATOM   1355 C  CB     . ASN A 1 187 ? -49.62400 12.52300  15.24300  1.000 35.62532 ? 183 ASN A CB     1 
ATOM   1356 C  CG     . ASN A 1 187 ? -50.81100 13.10400  15.98300  1.000 41.88397 ? 183 ASN A CG     1 
ATOM   1357 O  OD1    . ASN A 1 187 ? -51.95600 12.97300  15.54600  1.000 49.41382 ? 183 ASN A OD1    1 
ATOM   1358 N  ND2    . ASN A 1 187 ? -50.54400 13.75500  17.10400  1.000 45.69495 ? 183 ASN A ND2    1 
ATOM   1359 N  N      . TYR A 1 188 ? -48.04200 10.31800  13.31500  1.000 24.91615 ? 184 TYR A N      1 
ATOM   1360 C  CA     . TYR A 1 188 ? -46.84500 10.21800  12.48100  1.000 24.55031 ? 184 TYR A CA     1 
ATOM   1361 C  C      . TYR A 1 188 ? -46.75400 8.90800   11.70700  1.000 28.87451 ? 184 TYR A C      1 
ATOM   1362 O  O      . TYR A 1 188 ? -45.68100 8.59900   11.15700  1.000 29.41932 ? 184 TYR A O      1 
ATOM   1363 C  CB     . TYR A 1 188 ? -45.56700 10.42400  13.31300  1.000 24.01341 ? 184 TYR A CB     1 
ATOM   1364 C  CG     . TYR A 1 188 ? -45.40000 9.44600   14.45200  1.000 32.21965 ? 184 TYR A CG     1 
ATOM   1365 C  CD1    . TYR A 1 188 ? -44.81800 8.19600   14.25300  1.000 30.07203 ? 184 TYR A CD1    1 
ATOM   1366 C  CD2    . TYR A 1 188 ? -45.80900 9.78100   15.73900  1.000 35.41477 ? 184 TYR A CD2    1 
ATOM   1367 C  CE1    . TYR A 1 188 ? -44.66500 7.29300   15.31400  1.000 29.60618 ? 184 TYR A CE1    1 
ATOM   1368 C  CE2    . TYR A 1 188 ? -45.65600 8.90400   16.80200  1.000 31.92488 ? 184 TYR A CE2    1 
ATOM   1369 C  CZ     . TYR A 1 188 ? -45.09300 7.66600   16.59100  1.000 35.74902 ? 184 TYR A CZ     1 
ATOM   1370 O  OH     . TYR A 1 188 ? -44.96300 6.81800   17.66500  1.000 35.01209 ? 184 TYR A OH     1 
ATOM   1371 N  N      . ARG A 1 189 ? -47.82700 8.12300   11.65800  1.000 27.38223 ? 185 ARG A N      1 
ATOM   1372 C  CA     . ARG A 1 189 ? -47.90800 7.01900   10.71600  1.000 28.05600 ? 185 ARG A CA     1 
ATOM   1373 C  C      . ARG A 1 189 ? -49.37000 6.81600   10.35200  1.000 39.31524 ? 185 ARG A C      1 
ATOM   1374 O  O      . ARG A 1 189 ? -50.26500 7.12700   11.14300  1.000 41.54445 ? 185 ARG A O      1 
ATOM   1375 C  CB     . ARG A 1 189 ? -47.29500 5.71600   11.24600  1.000 32.05911 ? 185 ARG A CB     1 
ATOM   1376 C  CG     . ARG A 1 189 ? -47.71300 5.24200   12.63100  1.000 40.41800 ? 185 ARG A CG     1 
ATOM   1377 C  CD     . ARG A 1 189 ? -46.60800 4.27700   13.14500  1.000 42.41298 ? 185 ARG A CD     1 
ATOM   1378 N  NE     . ARG A 1 189 ? -46.86300 3.68400   14.45900  1.000 38.90466 ? 185 ARG A NE     1 
ATOM   1379 C  CZ     . ARG A 1 189 ? -47.70700 2.67700   14.67500  1.000 41.58393 ? 185 ARG A CZ     1 
ATOM   1380 N  NH1    . ARG A 1 189 ? -48.39700 2.14700   13.66600  1.000 31.68538 ? 185 ARG A NH1    1 
ATOM   1381 N  NH2    . ARG A 1 189 ? -47.86400 2.20500   15.90700  1.000 42.73144 ? 185 ARG A NH2    1 
ATOM   1382 N  N      . GLY A 1 190 ? -49.60300 6.32900   9.12900   1.000 37.50713 ? 186 GLY A N      1 
ATOM   1383 C  CA     . GLY A 1 190 ? -50.94500 6.22900   8.58900   1.000 34.15936 ? 186 GLY A CA     1 
ATOM   1384 C  C      . GLY A 1 190 ? -51.57500 4.86200   8.79500   1.000 31.97489 ? 186 GLY A C      1 
ATOM   1385 O  O      . GLY A 1 190 ? -51.00300 3.95500   9.40300   1.000 30.16414 ? 186 GLY A O      1 
ATOM   1386 N  N      . GLY A 1 191 ? -52.74700 4.66600   8.23300   1.000 30.13782 ? 187 GLY A N      1 
ATOM   1387 C  CA     . GLY A 1 191 ? -53.44300 3.41800   8.31300   1.000 30.78527 ? 187 GLY A CA     1 
ATOM   1388 C  C      . GLY A 1 191 ? -53.07800 2.37700   7.28500   1.000 34.64626 ? 187 GLY A C      1 
ATOM   1389 O  O      . GLY A 1 191 ? -52.16300 2.48400   6.56700   1.000 31.67748 ? 187 GLY A O      1 
ATOM   1390 N  N      . LYS A 1 192 ? -53.85900 1.34100   7.24400   1.000 33.49875 ? 188 LYS A N      1 
ATOM   1391 C  CA     . LYS A 1 192 ? -53.62300 0.25400   6.35600   1.000 34.49361 ? 188 LYS A CA     1 
ATOM   1392 C  C      . LYS A 1 192 ? -54.40400 0.39300   5.09500   1.000 25.72414 ? 188 LYS A C      1 
ATOM   1393 O  O      . LYS A 1 192 ? -55.43800 0.91000   5.09000   1.000 24.14500 ? 188 LYS A O      1 
ATOM   1394 C  CB     . LYS A 1 192 ? -54.03900 -1.01700  7.04700   1.000 45.17384 ? 188 LYS A CB     1 
ATOM   1395 C  CG     . LYS A 1 192 ? -53.57900 -1.10300  8.48400   1.000 57.65954 ? 188 LYS A CG     1 
ATOM   1396 C  CD     . LYS A 1 192 ? -52.30800 -1.92200  8.63600   1.000 64.96305 ? 188 LYS A CD     1 
ATOM   1397 C  CE     . LYS A 1 192 ? -51.38900 -1.68400  7.45500   1.000 66.51324 ? 188 LYS A CE     1 
ATOM   1398 N  NZ     . LYS A 1 192 ? -50.43000 -0.56300  7.60600   1.000 61.78109 ? 188 LYS A NZ     1 
ATOM   1399 N  N      . PRO A 1 193 ? -53.85600 -0.08400  4.00800   1.000 31.43798 ? 189 PRO A N      1 
ATOM   1400 C  CA     . PRO A 1 193 ? -54.52100 -0.04300  2.72100   1.000 28.14811 ? 189 PRO A CA     1 
ATOM   1401 C  C      . PRO A 1 193 ? -55.56800 -1.16100  2.58800   1.000 27.38223 ? 189 PRO A C      1 
ATOM   1402 O  O      . PRO A 1 193 ? -55.40600 -2.22000  3.11600   1.000 27.93756 ? 189 PRO A O      1 
ATOM   1403 C  CB     . PRO A 1 193 ? -53.37800 -0.21700  1.76200   1.000 26.02417 ? 189 PRO A CB     1 
ATOM   1404 C  CG     . PRO A 1 193 ? -52.38900 -0.98500  2.49000   1.000 32.64076 ? 189 PRO A CG     1 
ATOM   1405 C  CD     . PRO A 1 193 ? -52.53900 -0.69200  3.92500   1.000 30.61946 ? 189 PRO A CD     1 
ATOM   1406 N  N      . ALA A 1 194 ? -56.62900 -0.87700  1.87100   1.000 28.20601 ? 190 ALA A N      1 
ATOM   1407 C  CA     . ALA A 1 194 ? -57.73200 -1.80200  1.65400   1.000 25.49779 ? 190 ALA A CA     1 
ATOM   1408 C  C      . ALA A 1 194 ? -57.81900 -2.19800  0.18300   1.000 34.58836 ? 190 ALA A C      1 
ATOM   1409 O  O      . ALA A 1 194 ? -57.24300 -1.53700  -0.69000  1.000 29.76673 ? 190 ALA A O      1 
ATOM   1410 C  CB     . ALA A 1 194 ? -59.06800 -1.18500  2.09200   1.000 31.09057 ? 190 ALA A CB     1 
ATOM   1411 N  N      . PRO A 1 195 ? -58.54400 -3.26400  -0.13500  1.000 32.35388 ? 191 PRO A N      1 
ATOM   1412 C  CA     . PRO A 1 195 ? -58.73800 -3.61700  -1.54600  1.000 32.69603 ? 191 PRO A CA     1 
ATOM   1413 C  C      . PRO A 1 195 ? -59.70400 -2.64600  -2.20100  1.000 30.43786 ? 191 PRO A C      1 
ATOM   1414 O  O      . PRO A 1 195 ? -60.45800 -1.94900  -1.52700  1.000 31.45904 ? 191 PRO A O      1 
ATOM   1415 C  CB     . PRO A 1 195 ? -59.33500 -5.02400  -1.48000  1.000 33.42243 ? 191 PRO A CB     1 
ATOM   1416 C  CG     . PRO A 1 195 ? -60.12100 -5.00300  -0.19700  1.000 34.67521 ? 191 PRO A CG     1 
ATOM   1417 C  CD     . PRO A 1 195 ? -59.28700 -4.15800  0.76800   1.000 32.59338 ? 191 PRO A CD     1 
ATOM   1418 N  N      . THR A 1 196 ? -59.64400 -2.56400  -3.53000  1.000 32.71182 ? 192 THR A N      1 
ATOM   1419 C  CA     . THR A 1 196 ? -60.63300 -1.78200  -4.25600  1.000 37.93086 ? 192 THR A CA     1 
ATOM   1420 C  C      . THR A 1 196 ? -61.94200 -2.55700  -4.32300  1.000 35.30950 ? 192 THR A C      1 
ATOM   1421 O  O      . THR A 1 196 ? -61.95700 -3.79100  -4.30700  1.000 34.91471 ? 192 THR A O      1 
ATOM   1422 C  CB     . THR A 1 196 ? -60.16700 -1.46100  -5.68300  1.000 38.30459 ? 192 THR A CB     1 
ATOM   1423 O  OG1    . THR A 1 196 ? -60.16000 -2.66100  -6.46600  1.000 40.28904 ? 192 THR A OG1    1 
ATOM   1424 C  CG2    . THR A 1 196 ? -58.77300 -0.86000  -5.69600  1.000 37.36764 ? 192 THR A CG2    1 
ATOM   1425 N  N      . ILE A 1 197 ? -63.04800 -1.82300  -4.44600  1.000 37.64662 ? 193 ILE A N      1 
ATOM   1426 C  CA     . ILE A 1 197 ? -64.34600 -2.48300  -4.55700  1.000 41.75764 ? 193 ILE A CA     1 
ATOM   1427 C  C      . ILE A 1 197 ? -64.37900 -3.39300  -5.77500  1.000 37.72558 ? 193 ILE A C      1 
ATOM   1428 O  O      . ILE A 1 197 ? -64.99500 -4.46800  -5.75400  1.000 38.40197 ? 193 ILE A O      1 
ATOM   1429 C  CB     . ILE A 1 197 ? -65.48000 -1.44600  -4.59600  1.000 44.72115 ? 193 ILE A CB     1 
ATOM   1430 C  CG1    . ILE A 1 197 ? -65.58200 -0.74900  -3.24500  1.000 50.76398 ? 193 ILE A CG1    1 
ATOM   1431 C  CG2    . ILE A 1 197 ? -66.80600 -2.12100  -4.93000  1.000 44.03160 ? 193 ILE A CG2    1 
ATOM   1432 C  CD1    . ILE A 1 197 ? -65.97300 -1.69800  -2.11300  1.000 57.29898 ? 193 ILE A CD1    1 
ATOM   1433 N  N      . MET A 1 198 ? -63.70500 -2.99200  -6.84600  1.000 31.69327 ? 194 MET A N      1 
ATOM   1434 C  CA     . MET A 1 198 ? -63.68800 -3.81900  -8.04600  1.000 39.83899 ? 194 MET A CA     1 
ATOM   1435 C  C      . MET A 1 198 ? -63.05000 -5.18200  -7.77100  1.000 39.43894 ? 194 MET A C      1 
ATOM   1436 O  O      . MET A 1 198 ? -63.55800 -6.21600  -8.22500  1.000 38.44671 ? 194 MET A O      1 
ATOM   1437 C  CB     . MET A 1 198 ? -62.93200 -3.08900  -9.15300  1.000 42.74723 ? 194 MET A CB     1 
ATOM   1438 C  CG     . MET A 1 198 ? -63.04000 -3.73400  -10.50500 1.000 58.99128 ? 194 MET A CG     1 
ATOM   1439 S  SD     . MET A 1 198 ? -62.44100 -2.62500  -11.79600 1.000 72.80347 ? 194 MET A SD     1 
ATOM   1440 C  CE     . MET A 1 198 ? -61.18300 -3.63000  -12.56800 1.000 69.96102 ? 194 MET A CE     1 
ATOM   1441 N  N      . ASP A 1 199 ? -61.96100 -5.20900  -7.00000  1.000 35.88062 ? 195 ASP A N      1 
ATOM   1442 C  CA     . ASP A 1 199 ? -61.28300 -6.48000  -6.75900  1.000 34.75943 ? 195 ASP A CA     1 
ATOM   1443 C  C      . ASP A 1 199 ? -62.06700 -7.34300  -5.76900  1.000 37.09129 ? 195 ASP A C      1 
ATOM   1444 O  O      . ASP A 1 199 ? -62.10500 -8.57300  -5.90000  1.000 38.59673 ? 195 ASP A O      1 
ATOM   1445 C  CB     . ASP A 1 199 ? -59.86300 -6.22400  -6.25300  1.000 35.95957 ? 195 ASP A CB     1 
ATOM   1446 C  CG     . ASP A 1 199 ? -58.90400 -5.79500  -7.37900  1.000 46.46610 ? 195 ASP A CG     1 
ATOM   1447 O  OD1    . ASP A 1 199 ? -59.21700 -6.06000  -8.56300  1.000 47.25567 ? 195 ASP A OD1    1 
ATOM   1448 O  OD2    . ASP A 1 199 ? -57.84400 -5.19600  -7.07700  1.000 50.22971 ? 195 ASP A OD2    1 
ATOM   1449 N  N      . VAL A 1 200 ? -62.71200 -6.71500  -4.78200  1.000 34.60678 ? 196 VAL A N      1 
ATOM   1450 C  CA     . VAL A 1 200 ? -63.59000 -7.45700  -3.87600  1.000 33.32768 ? 196 VAL A CA     1 
ATOM   1451 C  C      . VAL A 1 200 ? -64.69500 -8.14200  -4.66800  1.000 32.43284 ? 196 VAL A C      1 
ATOM   1452 O  O      . VAL A 1 200 ? -64.95200 -9.34000  -4.51100  1.000 40.92859 ? 196 VAL A O      1 
ATOM   1453 C  CB     . VAL A 1 200 ? -64.17000 -6.51900  -2.80000  1.000 33.63561 ? 196 VAL A CB     1 
ATOM   1454 C  CG1    . VAL A 1 200 ? -65.20800 -7.24600  -1.94800  1.000 40.92070 ? 196 VAL A CG1    1 
ATOM   1455 C  CG2    . VAL A 1 200 ? -63.05300 -5.94600  -1.93000  1.000 33.80142 ? 196 VAL A CG2    1 
ATOM   1456 N  N      . VAL A 1 201 ? -65.36300 -7.39000  -5.53800  1.000 36.47543 ? 197 VAL A N      1 
ATOM   1457 C  CA     . VAL A 1 201 ? -66.46400 -7.95400  -6.31500  1.000 38.49409 ? 197 VAL A CA     1 
ATOM   1458 C  C      . VAL A 1 201 ? -65.96000 -9.08700  -7.19800  1.000 38.96520 ? 197 VAL A C      1 
ATOM   1459 O  O      . VAL A 1 201 ? -66.63000 -10.11300 -7.35900  1.000 39.41525 ? 197 VAL A O      1 
ATOM   1460 C  CB     . VAL A 1 201 ? -67.14700 -6.84900  -7.13700  1.000 42.32613 ? 197 VAL A CB     1 
ATOM   1461 C  CG1    . VAL A 1 201 ? -68.14400 -7.45600  -8.11800  1.000 41.21547 ? 197 VAL A CG1    1 
ATOM   1462 C  CG2    . VAL A 1 201 ? -67.81500 -5.86000  -6.20500  1.000 39.32314 ? 197 VAL A CG2    1 
ATOM   1463 N  N      . ARG A 1 202 ? -64.76200 -8.92300  -7.76700  1.000 39.18628 ? 198 ARG A N      1 
ATOM   1464 C  CA     . ARG A 1 202 ? -64.18500 -9.95900  -8.61600  1.000 42.38929 ? 198 ARG A CA     1 
ATOM   1465 C  C      . ARG A 1 202 ? -63.89100 -11.22900 -7.82900  1.000 38.73359 ? 198 ARG A C      1 
ATOM   1466 O  O      . ARG A 1 202 ? -64.20600 -12.33800 -8.28200  1.000 41.85502 ? 198 ARG A O      1 
ATOM   1467 C  CB     . ARG A 1 202 ? -62.90300 -9.43700  -9.26900  1.000 40.43643 ? 198 ARG A CB     1 
ATOM   1468 C  CG     . ARG A 1 202 ? -62.32900 -10.36400 -10.32300 1.000 46.93984 ? 198 ARG A CG     1 
ATOM   1469 C  CD     . ARG A 1 202 ? -63.38900 -10.77900 -11.33200 1.000 55.27242 ? 198 ARG A CD     1 
ATOM   1470 N  NE     . ARG A 1 202 ? -62.90800 -11.82700 -12.23200 1.000 61.76004 ? 198 ARG A NE     1 
ATOM   1471 C  CZ     . ARG A 1 202 ? -63.68500 -12.74800 -12.80000 1.000 70.97956 ? 198 ARG A CZ     1 
ATOM   1472 N  NH1    . ARG A 1 202 ? -65.00100 -12.76900 -12.57100 1.000 71.98495 ? 198 ARG A NH1    1 
ATOM   1473 N  NH2    . ARG A 1 202 ? -63.14000 -13.65300 -13.60500 1.000 70.97167 ? 198 ARG A NH2    1 
ATOM   1474 N  N      . VAL A 1 203 ? -63.31800 -11.09300 -6.63300  1.000 35.53321 ? 199 VAL A N      1 
ATOM   1475 C  CA     . VAL A 1 203 ? -63.02500 -12.28000 -5.84100  1.000 34.18831 ? 199 VAL A CA     1 
ATOM   1476 C  C      . VAL A 1 203 ? -64.32300 -12.95700 -5.42200  1.000 39.68107 ? 199 VAL A C      1 
ATOM   1477 O  O      . VAL A 1 203 ? -64.46200 -14.18300 -5.53200  1.000 40.39432 ? 199 VAL A O      1 
ATOM   1478 C  CB     . VAL A 1 203 ? -62.16100 -11.91800 -4.62400  1.000 34.56204 ? 199 VAL A CB     1 
ATOM   1479 C  CG1    . VAL A 1 203 ? -61.93300 -13.15800 -3.75100  1.000 31.47746 ? 199 VAL A CG1    1 
ATOM   1480 C  CG2    . VAL A 1 203 ? -60.83200 -11.32100 -5.05900  1.000 33.95144 ? 199 VAL A CG2    1 
ATOM   1481 N  N      . ALA A 1 204 ? -65.30400 -12.16500 -4.97000  1.000 34.52256 ? 200 ALA A N      1 
ATOM   1482 C  CA     . ALA A 1 204 ? -66.59700 -12.72500 -4.58000  1.000 39.63896 ? 200 ALA A CA     1 
ATOM   1483 C  C      . ALA A 1 204 ? -67.22400 -13.49900 -5.72900  1.000 41.35233 ? 200 ALA A C      1 
ATOM   1484 O  O      . ALA A 1 204 ? -67.78200 -14.58500 -5.53200  1.000 39.84951 ? 200 ALA A O      1 
ATOM   1485 C  CB     . ALA A 1 204 ? -67.53900 -11.61500 -4.11200  1.000 36.46490 ? 200 ALA A CB     1 
ATOM   1486 N  N      . GLU A 1 205 ? -67.15200 -12.95200 -6.93700  1.000 37.67557 ? 201 GLU A N      1 
ATOM   1487 C  CA     . GLU A 1 205 ? -67.70100 -13.65600 -8.09100  1.000 46.13185 ? 201 GLU A CA     1 
ATOM   1488 C  C      . GLU A 1 205 ? -66.91500 -14.93300 -8.39200  1.000 39.19417 ? 201 GLU A C      1 
ATOM   1489 O  O      . GLU A 1 205 ? -67.51000 -15.98400 -8.65700  1.000 38.41776 ? 201 GLU A O      1 
ATOM   1490 C  CB     . GLU A 1 205 ? -67.72200 -12.71300 -9.28900  1.000 53.29323 ? 201 GLU A CB     1 
ATOM   1491 C  CG     . GLU A 1 205 ? -68.11400 -13.33500 -10.59500 1.000 72.98507 ? 201 GLU A CG     1 
ATOM   1492 C  CD     . GLU A 1 205 ? -68.04900 -12.32800 -11.72000 1.000 86.64723 ? 201 GLU A CD     1 
ATOM   1493 O  OE1    . GLU A 1 205 ? -67.94100 -11.11800 -11.41900 1.000 89.20806 ? 201 GLU A OE1    1 
ATOM   1494 O  OE2    . GLU A 1 205 ? -68.09700 -12.74300 -12.89800 1.000 91.33200 ? 201 GLU A OE2    1 
ATOM   1495 N  N      . LEU A 1 206 ? -65.58100 -14.87800 -8.30900  1.000 39.87847 ? 202 LEU A N      1 
ATOM   1496 C  CA     . LEU A 1 206 ? -64.79000 -16.08500 -8.52400  1.000 36.49648 ? 202 LEU A CA     1 
ATOM   1497 C  C      . LEU A 1 206 ? -65.12800 -17.13900 -7.48100  1.000 38.94941 ? 202 LEU A C      1 
ATOM   1498 O  O      . LEU A 1 206 ? -65.19800 -18.33300 -7.79100  1.000 38.41513 ? 202 LEU A O      1 
ATOM   1499 C  CB     . LEU A 1 206 ? -63.29200 -15.76300 -8.47300  1.000 34.89892 ? 202 LEU A CB     1 
ATOM   1500 C  CG     . LEU A 1 206 ? -62.64600 -15.05800 -9.66700  1.000 40.59960 ? 202 LEU A CG     1 
ATOM   1501 C  CD1    . LEU A 1 206 ? -61.29000 -14.51300 -9.25900  1.000 33.74089 ? 202 LEU A CD1    1 
ATOM   1502 C  CD2    . LEU A 1 206 ? -62.53100 -15.99400 -10.86300 1.000 38.27827 ? 202 LEU A CD2    1 
ATOM   1503 N  N      . ILE A 1 207 ? -65.34300 -16.71800 -6.23700  1.000 42.16821 ? 203 ILE A N      1 
ATOM   1504 C  CA     . ILE A 1 207 ? -65.70400 -17.67500 -5.19700  1.000 43.62102 ? 203 ILE A CA     1 
ATOM   1505 C  C      . ILE A 1 207 ? -67.10200 -18.22800 -5.44300  1.000 39.17575 ? 203 ILE A C      1 
ATOM   1506 O  O      . ILE A 1 207 ? -67.32700 -19.44200 -5.37500  1.000 37.71505 ? 203 ILE A O      1 
ATOM   1507 C  CB     . ILE A 1 207 ? -65.60000 -17.01100 -3.81000  1.000 42.60248 ? 203 ILE A CB     1 
ATOM   1508 C  CG1    . ILE A 1 207 ? -64.13400 -16.73300 -3.45500  1.000 38.30722 ? 203 ILE A CG1    1 
ATOM   1509 C  CG2    . ILE A 1 207 ? -66.26100 -17.87400 -2.75300  1.000 41.27600 ? 203 ILE A CG2    1 
ATOM   1510 C  CD1    . ILE A 1 207 ? -63.98300 -15.89700 -2.20600  1.000 42.87883 ? 203 ILE A CD1    1 
ATOM   1511 N  N      . PHE A 1 208 ? -68.05100 -17.35500 -5.79100  1.000 39.09679 ? 204 PHE A N      1 
ATOM   1512 C  CA     . PHE A 1 208 ? -69.43200 -17.79700 -5.98400  1.000 49.96915 ? 204 PHE A CA     1 
ATOM   1513 C  C      . PHE A 1 208 ? -69.53200 -18.89800 -7.03100  1.000 47.14776 ? 204 PHE A C      1 
ATOM   1514 O  O      . PHE A 1 208 ? -70.44000 -19.73300 -6.97000  1.000 50.18760 ? 204 PHE A O      1 
ATOM   1515 C  CB     . PHE A 1 208 ? -70.33300 -16.61900 -6.37800  1.000 56.29622 ? 204 PHE A CB     1 
ATOM   1516 C  CG     . PHE A 1 208 ? -70.60600 -15.64600 -5.25000  1.000 66.67642 ? 204 PHE A CG     1 
ATOM   1517 C  CD1    . PHE A 1 208 ? -70.38200 -16.01000 -3.92900  1.000 67.41861 ? 204 PHE A CD1    1 
ATOM   1518 C  CD2    . PHE A 1 208 ? -71.08400 -14.36300 -5.51600  1.000 66.87118 ? 204 PHE A CD2    1 
ATOM   1519 C  CE1    . PHE A 1 208 ? -70.62600 -15.11900 -2.89400  1.000 67.54757 ? 204 PHE A CE1    1 
ATOM   1520 C  CE2    . PHE A 1 208 ? -71.33000 -13.46700 -4.48100  1.000 64.13664 ? 204 PHE A CE2    1 
ATOM   1521 C  CZ     . PHE A 1 208 ? -71.10000 -13.84900 -3.17000  1.000 62.29957 ? 204 PHE A CZ     1 
ATOM   1522 N  N      . HIS A 1 209 ? -68.64000 -18.89500 -8.01200  1.000 44.35269 ? 205 HIS A N      1 
ATOM   1523 C  CA     . HIS A 1 209 ? -68.70500 -19.82600 -9.12600  1.000 46.95826 ? 205 HIS A CA     1 
ATOM   1524 C  C      . HIS A 1 209 ? -67.71300 -20.97900 -9.01000  1.000 49.70859 ? 205 HIS A C      1 
ATOM   1525 O  O      . HIS A 1 209 ? -67.74100 -21.88200 -9.85300  1.000 50.26655 ? 205 HIS A O      1 
ATOM   1526 C  CB     . HIS A 1 209 ? -68.48300 -19.06300 -10.44000 1.000 47.27935 ? 205 HIS A CB     1 
ATOM   1527 C  CG     . HIS A 1 209 ? -69.63300 -18.18000 -10.83300 1.000 57.51742 ? 205 HIS A CG     1 
ATOM   1528 N  ND1    . HIS A 1 209 ? -70.93900 -18.62500 -10.86400 1.000 61.79951 ? 205 HIS A ND1    1 
ATOM   1529 C  CD2    . HIS A 1 209 ? -69.67100 -16.88400 -11.22600 1.000 60.05457 ? 205 HIS A CD2    1 
ATOM   1530 C  CE1    . HIS A 1 209 ? -71.73100 -17.64200 -11.25900 1.000 62.00743 ? 205 HIS A CE1    1 
ATOM   1531 N  NE2    . HIS A 1 209 ? -70.98600 -16.57600 -11.48900 1.000 59.42555 ? 205 HIS A NE2    1 
ATOM   1532 N  N      . ALA A 1 210 ? -66.85400 -20.98400 -7.98500  1.000 42.84987 ? 206 ALA A N      1 
ATOM   1533 C  CA     . ALA A 1 210 ? -65.79000 -21.97700 -7.88300  1.000 42.94462 ? 206 ALA A CA     1 
ATOM   1534 C  C      . ALA A 1 210 ? -66.33500 -23.32800 -7.44500  1.000 45.35544 ? 206 ALA A C      1 
ATOM   1535 O  O      . ALA A 1 210 ? -67.20800 -23.41300 -6.57900  1.000 45.30806 ? 206 ALA A O      1 
ATOM   1536 C  CB     . ALA A 1 210 ? -64.71900 -21.52200 -6.88800  1.000 36.88337 ? 206 ALA A CB     1 
ATOM   1537 N  N      . LYS A 1 211 ? -65.80500 -24.39300 -8.04100  1.000 46.18448 ? 207 LYS A N      1 
ATOM   1538 C  CA     . LYS A 1 211 ? -66.22500 -25.73200 -7.65200  1.000 45.59757 ? 207 LYS A CA     1 
ATOM   1539 C  C      . LYS A 1 211 ? -65.28800 -26.38400 -6.64000  1.000 46.67402 ? 207 LYS A C      1 
ATOM   1540 O  O      . LYS A 1 211 ? -65.73100 -27.24900 -5.87700  1.000 41.24179 ? 207 LYS A O      1 
ATOM   1541 C  CB     . LYS A 1 211 ? -66.34300 -26.64700 -8.87800  1.000 45.78444 ? 207 LYS A CB     1 
ATOM   1542 C  CG     . LYS A 1 211 ? -66.98300 -26.02100 -10.11500 1.000 48.64531 ? 207 LYS A CG     1 
ATOM   1543 C  CD     . LYS A 1 211 ? -68.21000 -25.19300 -9.79300  1.000 57.19633 ? 207 LYS A CD     1 
ATOM   1544 C  CE     . LYS A 1 211 ? -68.75900 -24.52100 -11.05500 1.000 60.79150 ? 207 LYS A CE     1 
ATOM   1545 N  NZ     . LYS A 1 211 ? -70.14000 -24.02200 -10.83600 1.000 66.26584 ? 207 LYS A NZ     1 
ATOM   1546 N  N      . ARG A 1 212 ? -64.01300 -25.98800 -6.58700  1.000 43.78420 ? 208 ARG A N      1 
ATOM   1547 C  CA     . ARG A 1 212 ? -63.06900 -26.52000 -5.60000  1.000 42.25770 ? 208 ARG A CA     1 
ATOM   1548 C  C      . ARG A 1 212 ? -62.08600 -25.42900 -5.17600  1.000 38.02035 ? 208 ARG A C      1 
ATOM   1549 O  O      . ARG A 1 212 ? -60.88600 -25.49100 -5.46700  1.000 34.27253 ? 208 ARG A O      1 
ATOM   1550 C  CB     . ARG A 1 212 ? -62.34400 -27.74500 -6.16600  1.000 46.76613 ? 208 ARG A CB     1 
ATOM   1551 C  CG     . ARG A 1 212 ? -61.85700 -28.73200 -5.11300  1.000 54.73288 ? 208 ARG A CG     1 
ATOM   1552 C  CD     . ARG A 1 212 ? -62.77800 -29.93900 -5.01000  1.000 67.32386 ? 208 ARG A CD     1 
ATOM   1553 N  NE     . ARG A 1 212 ? -62.53600 -30.72200 -3.79700  1.000 73.07192 ? 208 ARG A NE     1 
ATOM   1554 C  CZ     . ARG A 1 212 ? -63.48200 -31.06900 -2.92500  1.000 72.41921 ? 208 ARG A CZ     1 
ATOM   1555 N  NH1    . ARG A 1 212 ? -64.74400 -30.70700 -3.12900  1.000 71.29276 ? 208 ARG A NH1    1 
ATOM   1556 N  NH2    . ARG A 1 212 ? -63.17000 -31.78200 -1.84700  1.000 72.66924 ? 208 ARG A NH2    1 
ATOM   1557 N  N      . PRO A 1 213 ? -62.56400 -24.43100 -4.44100  1.000 34.57257 ? 209 PRO A N      1 
ATOM   1558 C  CA     . PRO A 1 213 ? -61.68200 -23.35900 -3.97600  1.000 34.17778 ? 209 PRO A CA     1 
ATOM   1559 C  C      . PRO A 1 213 ? -60.81500 -23.81500 -2.80600  1.000 34.12778 ? 209 PRO A C      1 
ATOM   1560 O  O      . PRO A 1 213 ? -61.08400 -24.82000 -2.15000  1.000 41.58393 ? 209 PRO A O      1 
ATOM   1561 C  CB     . PRO A 1 213 ? -62.66800 -22.26900 -3.53900  1.000 36.68598 ? 209 PRO A CB     1 
ATOM   1562 C  CG     . PRO A 1 213 ? -63.86800 -23.05400 -3.04400  1.000 38.02824 ? 209 PRO A CG     1 
ATOM   1563 C  CD     . PRO A 1 213 ? -63.95300 -24.26900 -3.95600  1.000 39.17575 ? 209 PRO A CD     1 
ATOM   1564 N  N      . ALA A 1 214 ? -59.74200 -23.06600 -2.56700  1.000 35.14369 ? 210 ALA A N      1 
ATOM   1565 C  CA     . ALA A 1 214 ? -58.87600 -23.30300 -1.41900  1.000 32.27492 ? 210 ALA A CA     1 
ATOM   1566 C  C      . ALA A 1 214 ? -58.22900 -21.98800 -1.02800  1.000 32.43284 ? 210 ALA A C      1 
ATOM   1567 O  O      . ALA A 1 214 ? -58.05700 -21.09600 -1.86300  1.000 36.42016 ? 210 ALA A O      1 
ATOM   1568 C  CB     . ALA A 1 214 ? -57.78800 -24.34400 -1.70100  1.000 29.22982 ? 210 ALA A CB     1 
ATOM   1569 N  N      . ILE A 1 215 ? -57.88100 -21.87500 0.25000   1.000 32.54864 ? 211 ILE A N      1 
ATOM   1570 C  CA     . ILE A 1 215 ? -57.12200 -20.74700 0.77400   1.000 27.51646 ? 211 ILE A CA     1 
ATOM   1571 C  C      . ILE A 1 215 ? -55.78000 -21.26600 1.26900   1.000 33.34084 ? 211 ILE A C      1 
ATOM   1572 O  O      . ILE A 1 215 ? -55.72700 -22.28500 1.96700   1.000 30.46681 ? 211 ILE A O      1 
ATOM   1573 C  CB     . ILE A 1 215 ? -57.87100 -20.03700 1.91400   1.000 30.29837 ? 211 ILE A CB     1 
ATOM   1574 C  CG1    . ILE A 1 215 ? -59.13400 -19.33900 1.38400   1.000 30.15098 ? 211 ILE A CG1    1 
ATOM   1575 C  CG2    . ILE A 1 215 ? -56.93300 -19.06100 2.67500   1.000 24.37134 ? 211 ILE A CG2    1 
ATOM   1576 C  CD1    . ILE A 1 215 ? -60.14400 -19.08700 2.47700   1.000 29.83779 ? 211 ILE A CD1    1 
ATOM   1577 N  N      . LEU A 1 216 ? -54.70000 -20.57500 0.89600   1.000 32.45915 ? 212 LEU A N      1 
ATOM   1578 C  CA     . LEU A 1 216 ? -53.36900 -20.79100 1.46800   1.000 28.34287 ? 212 LEU A CA     1 
ATOM   1579 C  C      . LEU A 1 216 ? -53.00800 -19.53300 2.24900   1.000 25.67150 ? 212 LEU A C      1 
ATOM   1580 O  O      . LEU A 1 216 ? -52.82400 -18.46300 1.66000   1.000 24.63980 ? 212 LEU A O      1 
ATOM   1581 C  CB     . LEU A 1 216 ? -52.33400 -21.10000 0.38700   1.000 23.26068 ? 212 LEU A CB     1 
ATOM   1582 C  CG     . LEU A 1 216 ? -50.91000 -21.34000 0.92600   1.000 34.76206 ? 212 LEU A CG     1 
ATOM   1583 C  CD1    . LEU A 1 216 ? -50.86300 -22.47100 1.97700   1.000 31.05899 ? 212 LEU A CD1    1 
ATOM   1584 C  CD2    . LEU A 1 216 ? -49.93700 -21.61300 -0.19600  1.000 30.89055 ? 212 LEU A CD2    1 
ATOM   1585 N  N      . ALA A 1 217 ? -52.97800 -19.64800 3.57300   1.000 23.87392 ? 213 ALA A N      1 
ATOM   1586 C  CA     . ALA A 1 217 ? -52.76100 -18.51800 4.46400   1.000 25.41621 ? 213 ALA A CA     1 
ATOM   1587 C  C      . ALA A 1 217 ? -51.35000 -18.58400 5.02800   1.000 22.54481 ? 213 ALA A C      1 
ATOM   1588 O  O      . ALA A 1 217 ? -50.93300 -19.62200 5.54400   1.000 22.33426 ? 213 ALA A O      1 
ATOM   1589 C  CB     . ALA A 1 217 ? -53.78100 -18.51500 5.60300   1.000 31.50641 ? 213 ALA A CB     1 
ATOM   1590 N  N      . GLY A 1 218 ? -50.62000 -17.47800 4.93200   1.000 23.69758 ? 214 GLY A N      1 
ATOM   1591 C  CA     . GLY A 1 218 ? -49.26600 -17.40900 5.41400   1.000 25.43989 ? 214 GLY A CA     1 
ATOM   1592 C  C      . GLY A 1 218 ? -49.13000 -16.54100 6.65000   1.000 33.74089 ? 214 GLY A C      1 
ATOM   1593 O  O      . GLY A 1 218 ? -50.11000 -16.08700 7.25200   1.000 29.76673 ? 214 GLY A O      1 
ATOM   1594 N  N      . HIS A 1 219 ? -47.86800 -16.29400 7.00300   1.000 26.96902 ? 215 HIS A N      1 
ATOM   1595 C  CA     . HIS A 1 219 ? -47.51000 -15.49900 8.16600   1.000 25.39252 ? 215 HIS A CA     1 
ATOM   1596 C  C      . HIS A 1 219 ? -48.08500 -14.08200 8.12400   1.000 23.72916 ? 215 HIS A C      1 
ATOM   1597 O  O      . HIS A 1 219 ? -48.21400 -13.45000 9.17500   1.000 26.95586 ? 215 HIS A O      1 
ATOM   1598 C  CB     . HIS A 1 219 ? -45.97500 -15.46800 8.26400   1.000 26.91639 ? 215 HIS A CB     1 
ATOM   1599 C  CG     . HIS A 1 219 ? -45.45300 -14.61600 9.37200   1.000 27.35591 ? 215 HIS A CG     1 
ATOM   1600 N  ND1    . HIS A 1 219 ? -45.75900 -14.85100 10.69700  1.000 25.80309 ? 215 HIS A ND1    1 
ATOM   1601 C  CD2    . HIS A 1 219 ? -44.63600 -13.53500 9.35600   1.000 27.33749 ? 215 HIS A CD2    1 
ATOM   1602 C  CE1    . HIS A 1 219 ? -45.16900 -13.93700 11.44900  1.000 27.05061 ? 215 HIS A CE1    1 
ATOM   1603 N  NE2    . HIS A 1 219 ? -44.48000 -13.12900 10.66100  1.000 29.20087 ? 215 HIS A NE2    1 
ATOM   1604 N  N      . GLY A 1 220 ? -48.42000 -13.55100 6.94400   1.000 22.65272 ? 216 GLY A N      1 
ATOM   1605 C  CA     . GLY A 1 220 ? -49.08600 -12.25800 6.90900   1.000 23.45544 ? 216 GLY A CA     1 
ATOM   1606 C  C      . GLY A 1 220 ? -50.37600 -12.21700 7.72400   1.000 29.24561 ? 216 GLY A C      1 
ATOM   1607 O  O      . GLY A 1 220 ? -50.76600 -11.16000 8.23600   1.000 23.03960 ? 216 GLY A O      1 
ATOM   1608 N  N      . ILE A 1 221 ? -51.04900 -13.36000 7.87300   1.000 25.79520 ? 217 ILE A N      1 
ATOM   1609 C  CA     . ILE A 1 221 ? -52.24500 -13.38100 8.71000   1.000 27.38749 ? 217 ILE A CA     1 
ATOM   1610 C  C      . ILE A 1 221 ? -51.90800 -12.87400 10.10600  1.000 30.62736 ? 217 ILE A C      1 
ATOM   1611 O  O      . ILE A 1 221 ? -52.64400 -12.06400 10.68100  1.000 30.83528 ? 217 ILE A O      1 
ATOM   1612 C  CB     . ILE A 1 221 ? -52.86600 -14.79300 8.75800   1.000 23.60283 ? 217 ILE A CB     1 
ATOM   1613 C  CG1    . ILE A 1 221 ? -53.51500 -15.14900 7.42000   1.000 25.67939 ? 217 ILE A CG1    1 
ATOM   1614 C  CG2    . ILE A 1 221 ? -53.84600 -14.90000 9.94000   1.000 25.49516 ? 217 ILE A CG2    1 
ATOM   1615 C  CD1    . ILE A 1 221 ? -54.66700 -14.23200 6.99200   1.000 24.05552 ? 217 ILE A CD1    1 
ATOM   1616 N  N      . GLU A 1 222 ? -50.77400 -13.31800 10.65900  1.000 32.68287 ? 218 GLU A N      1 
ATOM   1617 C  CA     . GLU A 1 222 ? -50.36400 -12.85000 11.98000  1.000 28.68502 ? 218 GLU A CA     1 
ATOM   1618 C  C      . GLU A 1 222 ? -49.98600 -11.37600 11.94700  1.000 29.70356 ? 218 GLU A C      1 
ATOM   1619 O  O      . GLU A 1 222 ? -50.39500 -10.60400 12.81900  1.000 24.11342 ? 218 GLU A O      1 
ATOM   1620 C  CB     . GLU A 1 222 ? -49.18900 -13.67100 12.51300  1.000 27.55067 ? 218 GLU A CB     1 
ATOM   1621 C  CG     . GLU A 1 222 ? -48.62000 -13.07700 13.79400  1.000 37.07287 ? 218 GLU A CG     1 
ATOM   1622 C  CD     . GLU A 1 222 ? -47.42400 -13.85600 14.36100  1.000 43.86842 ? 218 GLU A CD     1 
ATOM   1623 O  OE1    . GLU A 1 222 ? -46.30700 -13.29900 14.35700  1.000 41.77869 ? 218 GLU A OE1    1 
ATOM   1624 O  OE2    . GLU A 1 222 ? -47.60900 -15.00900 14.80900  1.000 44.50270 ? 218 GLU A OE2    1 
ATOM   1625 N  N      . CYS A 1 223 ? -49.21900 -10.95900 10.93400  1.000 28.40341 ? 219 CYS A N      1 
ATOM   1626 C  CA     . CYS A 1 223 ? -48.81400 -9.56200  10.87000  1.000 28.81661 ? 219 CYS A CA     1 
ATOM   1627 C  C      . CYS A 1 223 ? -50.03300 -8.65700  10.80200  1.000 29.64829 ? 219 CYS A C      1 
ATOM   1628 O  O      . CYS A 1 223 ? -50.05200 -7.58500  11.42200  1.000 29.30878 ? 219 CYS A O      1 
ATOM   1629 C  CB     . CYS A 1 223 ? -47.96500 -9.32300  9.61800   1.000 29.34562 ? 219 CYS A CB     1 
ATOM   1630 S  SG     . CYS A 1 223 ? -46.48100 -10.31300 9.46300   1.000 33.55665 ? 219 CYS A SG     1 
ATOM   1631 N  N      . ALA A 1 224 ? -51.09400 -9.11800  10.15300  1.000 23.42386 ? 220 ALA A N      1 
ATOM   1632 C  CA     . ALA A 1 224 ? -52.32500 -8.34500  10.04000  1.000 26.37685 ? 220 ALA A CA     1 
ATOM   1633 C  C      . ALA A 1 224 ? -53.28600 -8.57300  11.19900  1.000 29.69303 ? 220 ALA A C      1 
ATOM   1634 O  O      . ALA A 1 224 ? -54.31800 -7.89800  11.26800  1.000 36.11486 ? 220 ALA A O      1 
ATOM   1635 C  CB     . ALA A 1 224 ? -53.03400 -8.68400  8.72100   1.000 24.77139 ? 220 ALA A CB     1 
ATOM   1636 N  N      . LYS A 1 225 ? -52.96400 -9.47900  12.11700  1.000 28.43762 ? 221 LYS A N      1 
ATOM   1637 C  CA     . LYS A 1 225 ? -53.87600 -9.84400  13.19700  1.000 32.65392 ? 221 LYS A CA     1 
ATOM   1638 C  C      . LYS A 1 225 ? -55.25500 -10.17400 12.63800  1.000 32.62233 ? 221 LYS A C      1 
ATOM   1639 O  O      . LYS A 1 225 ? -56.28500 -9.70900  13.12800  1.000 36.72546 ? 221 LYS A O      1 
ATOM   1640 C  CB     . LYS A 1 225 ? -53.94800 -8.72400  14.24000  1.000 29.51670 ? 221 LYS A CB     1 
ATOM   1641 C  CG     . LYS A 1 225 ? -52.54900 -8.28900  14.73100  1.000 32.82762 ? 221 LYS A CG     1 
ATOM   1642 C  CD     . LYS A 1 225 ? -52.62800 -6.96700  15.48500  1.000 40.28115 ? 221 LYS A CD     1 
ATOM   1643 C  CE     . LYS A 1 225 ? -51.33400 -6.65500  16.23100  1.000 48.16367 ? 221 LYS A CE     1 
ATOM   1644 N  NZ     . LYS A 1 225 ? -50.34900 -5.89700  15.40000  1.000 49.67175 ? 221 LYS A NZ     1 
ATOM   1645 N  N      . ALA A 1 226 ? -55.27000 -11.01300 11.60400  1.000 33.02764 ? 222 ALA A N      1 
ATOM   1646 C  CA     . ALA A 1 226 ? -56.47600 -11.27100 10.82800  1.000 32.11701 ? 222 ALA A CA     1 
ATOM   1647 C  C      . ALA A 1 226 ? -57.09500 -12.63400 11.13400  1.000 31.71696 ? 222 ALA A C      1 
ATOM   1648 O  O      . ALA A 1 226 ? -57.90800 -13.12700 10.35100  1.000 29.42458 ? 222 ALA A O      1 
ATOM   1649 C  CB     . ALA A 1 226 ? -56.15100 -11.16200 9.33600   1.000 25.54254 ? 222 ALA A CB     1 
ATOM   1650 N  N      . TRP A 1 227 ? -56.75900 -13.24200 12.27600  1.000 30.11151 ? 223 TRP A N      1 
ATOM   1651 C  CA     . TRP A 1 227 ? -57.21400 -14.60700 12.53800  1.000 26.86112 ? 223 TRP A CA     1 
ATOM   1652 C  C      . TRP A 1 227 ? -58.73100 -14.70900 12.54200  1.000 30.94582 ? 223 TRP A C      1 
ATOM   1653 O  O      . TRP A 1 227 ? -59.30800 -15.63300 11.94600  1.000 32.86183 ? 223 TRP A O      1 
ATOM   1654 C  CB     . TRP A 1 227 ? -56.68200 -15.09900 13.87800  1.000 24.62664 ? 223 TRP A CB     1 
ATOM   1655 C  CG     . TRP A 1 227 ? -55.20600 -15.05600 14.01800  1.000 23.42123 ? 223 TRP A CG     1 
ATOM   1656 C  CD1    . TRP A 1 227 ? -54.31200 -15.97700 13.56100  1.000 31.73275 ? 223 TRP A CD1    1 
ATOM   1657 C  CD2    . TRP A 1 227 ? -54.44400 -14.05200 14.69600  1.000 29.32457 ? 223 TRP A CD2    1 
ATOM   1658 N  NE1    . TRP A 1 227 ? -53.03100 -15.60300 13.90900  1.000 30.95898 ? 223 TRP A NE1    1 
ATOM   1659 C  CE2    . TRP A 1 227 ? -53.08800 -14.42900 14.61300  1.000 28.00073 ? 223 TRP A CE2    1 
ATOM   1660 C  CE3    . TRP A 1 227 ? -54.77900 -12.87600 15.38200  1.000 31.05636 ? 223 TRP A CE3    1 
ATOM   1661 C  CZ2    . TRP A 1 227 ? -52.06000 -13.66900 15.18500  1.000 35.26739 ? 223 TRP A CZ2    1 
ATOM   1662 C  CZ3    . TRP A 1 227 ? -53.75500 -12.12100 15.95200  1.000 31.78539 ? 223 TRP A CZ3    1 
ATOM   1663 C  CH2    . TRP A 1 227 ? -52.41300 -12.52200 15.84600  1.000 30.60104 ? 223 TRP A CH2    1 
ATOM   1664 N  N      . GLU A 1 228 ? -59.40200 -13.80200 13.24600  1.000 30.97477 ? 224 GLU A N      1 
ATOM   1665 C  CA     . GLU A 1 228 ? -60.84500 -13.96700 13.36400  1.000 32.40915 ? 224 GLU A CA     1 
ATOM   1666 C  C      . GLU A 1 228 ? -61.54600 -13.67700 12.04600  1.000 30.54577 ? 224 GLU A C      1 
ATOM   1667 O  O      . GLU A 1 228 ? -62.50600 -14.36800 11.69800  1.000 32.30124 ? 224 GLU A O      1 
ATOM   1668 C  CB     . GLU A 1 228 ? -61.40200 -13.08200 14.47400  1.000 40.38116 ? 224 GLU A CB     1 
ATOM   1669 C  CG     . GLU A 1 228 ? -62.84200 -13.48400 14.83400  1.000 66.96329 ? 224 GLU A CG     1 
ATOM   1670 C  CD     . GLU A 1 228 ? -63.66400 -12.36200 15.45500  1.000 84.03639 ? 224 GLU A CD     1 
ATOM   1671 O  OE1    . GLU A 1 228 ? -64.90200 -12.52000 15.56600  1.000 94.83242 ? 224 GLU A OE1    1 
ATOM   1672 O  OE2    . GLU A 1 228 ? -63.07200 -11.33100 15.84200  1.000 90.54507 ? 224 GLU A OE2    1 
ATOM   1673 N  N      . GLU A 1 229 ? -61.03600 -12.72100 11.27100  1.000 29.75094 ? 225 GLU A N      1 
ATOM   1674 C  CA     . GLU A 1 229 ? -61.62200 -12.45400 9.96000   1.000 31.55905 ? 225 GLU A CA     1 
ATOM   1675 C  C      . GLU A 1 229 ? -61.38000 -13.62000 9.01100   1.000 29.78252 ? 225 GLU A C      1 
ATOM   1676 O  O      . GLU A 1 229 ? -62.24700 -13.95900 8.20200   1.000 27.00850 ? 225 GLU A O      1 
ATOM   1677 C  CB     . GLU A 1 229 ? -61.04900 -11.16200 9.37100   1.000 35.06736 ? 225 GLU A CB     1 
ATOM   1678 C  CG     . GLU A 1 229 ? -61.45100 -9.89900  10.11700  1.000 45.41071 ? 225 GLU A CG     1 
ATOM   1679 C  CD     . GLU A 1 229 ? -60.52700 -9.58300  11.28800  1.000 56.04093 ? 225 GLU A CD     1 
ATOM   1680 O  OE1    . GLU A 1 229 ? -59.66000 -10.42000 11.62600  1.000 57.09369 ? 225 GLU A OE1    1 
ATOM   1681 O  OE2    . GLU A 1 229 ? -60.67800 -8.49400  11.88100  1.000 63.86029 ? 225 GLU A OE2    1 
ATOM   1682 N  N      . LEU A 1 230 ? -60.19900 -14.23900 9.08300   1.000 30.28258 ? 226 LEU A N      1 
ATOM   1683 C  CA     . LEU A 1 230 ? -59.95200 -15.42200 8.26200   1.000 31.77486 ? 226 LEU A CA     1 
ATOM   1684 C  C      . LEU A 1 230 ? -60.91600 -16.55200 8.62500   1.000 35.68059 ? 226 LEU A C      1 
ATOM   1685 O  O      . LEU A 1 230 ? -61.47700 -17.21700 7.74200   1.000 31.03530 ? 226 LEU A O      1 
ATOM   1686 C  CB     . LEU A 1 230 ? -58.49500 -15.87700 8.42300   1.000 24.92404 ? 226 LEU A CB     1 
ATOM   1687 C  CG     . LEU A 1 230 ? -58.15200 -17.21400 7.74700   1.000 30.96424 ? 226 LEU A CG     1 
ATOM   1688 C  CD1    . LEU A 1 230 ? -58.39900 -17.13500 6.25400   1.000 34.11462 ? 226 LEU A CD1    1 
ATOM   1689 C  CD2    . LEU A 1 230 ? -56.72400 -17.66400 8.01900   1.000 23.15014 ? 226 LEU A CD2    1 
ATOM   1690 N  N      . LEU A 1 231 ? -61.11700 -16.78800 9.92300   1.000 31.47219 ? 227 LEU A N      1 
ATOM   1691 C  CA     . LEU A 1 231 ? -62.00200 -17.86500 10.35300  1.000 28.66923 ? 227 LEU A CA     1 
ATOM   1692 C  C      . LEU A 1 231 ? -63.43400 -17.60300 9.90000   1.000 34.16199 ? 227 LEU A C      1 
ATOM   1693 O  O      . LEU A 1 231 ? -64.11200 -18.49000 9.36100   1.000 33.99881 ? 227 LEU A O      1 
ATOM   1694 C  CB     . LEU A 1 231 ? -61.93200 -18.00700 11.87200  1.000 31.74854 ? 227 LEU A CB     1 
ATOM   1695 C  CG     . LEU A 1 231 ? -62.89400 -19.01600 12.51500  1.000 40.79963 ? 227 LEU A CG     1 
ATOM   1696 C  CD1    . LEU A 1 231 ? -62.60900 -20.44700 12.05000  1.000 39.93110 ? 227 LEU A CD1    1 
ATOM   1697 C  CD2    . LEU A 1 231 ? -62.81400 -18.91600 14.02700  1.000 42.26033 ? 227 LEU A CD2    1 
ATOM   1698 N  N      . ASP A 1 232 ? -63.89900 -16.37000 10.08700  1.000 28.43762 ? 228 ASP A N      1 
ATOM   1699 C  CA     . ASP A 1 232 ? -65.24800 -16.01100 9.67100   1.000 31.59589 ? 228 ASP A CA     1 
ATOM   1700 C  C      . ASP A 1 232 ? -65.38200 -16.08100 8.15700   1.000 36.63860 ? 228 ASP A C      1 
ATOM   1701 O  O      . ASP A 1 232 ? -66.40700 -16.53700 7.63600   1.000 35.81482 ? 228 ASP A O      1 
ATOM   1702 C  CB     . ASP A 1 232 ? -65.56800 -14.61000 10.19100  1.000 41.56814 ? 228 ASP A CB     1 
ATOM   1703 C  CG     . ASP A 1 232 ? -67.01400 -14.22000 9.98700   1.000 66.65799 ? 228 ASP A CG     1 
ATOM   1704 O  OD1    . ASP A 1 232 ? -67.89600 -15.11500 9.99400   1.000 72.32709 ? 228 ASP A OD1    1 
ATOM   1705 O  OD2    . ASP A 1 232 ? -67.26800 -13.00500 9.82800   1.000 73.98519 ? 228 ASP A OD2    1 
ATOM   1706 N  N      . PHE A 1 233 ? -64.34300 -15.66300 7.42700   1.000 33.31978 ? 229 PHE A N      1 
ATOM   1707 C  CA     . PHE A 1 233 ? -64.40800 -15.74300 5.97300   1.000 31.53273 ? 229 PHE A CA     1 
ATOM   1708 C  C      . PHE A 1 233 ? -64.48600 -17.19400 5.50500   1.000 34.22252 ? 229 PHE A C      1 
ATOM   1709 O  O      . PHE A 1 233 ? -65.30200 -17.53300 4.63800   1.000 31.88540 ? 229 PHE A O      1 
ATOM   1710 C  CB     . PHE A 1 233 ? -63.19500 -15.03500 5.35500   1.000 30.67736 ? 229 PHE A CB     1 
ATOM   1711 C  CG     . PHE A 1 233 ? -63.08200 -15.21900 3.87000   1.000 32.40915 ? 229 PHE A CG     1 
ATOM   1712 C  CD1    . PHE A 1 233 ? -63.96800 -14.60300 3.01400   1.000 33.00396 ? 229 PHE A CD1    1 
ATOM   1713 C  CD2    . PHE A 1 233 ? -62.08800 -16.00300 3.33800   1.000 36.70177 ? 229 PHE A CD2    1 
ATOM   1714 C  CE1    . PHE A 1 233 ? -63.87200 -14.78000 1.65500   1.000 36.02800 ? 229 PHE A CE1    1 
ATOM   1715 C  CE2    . PHE A 1 233 ? -61.97100 -16.17400 1.97900   1.000 42.61037 ? 229 PHE A CE2    1 
ATOM   1716 C  CZ     . PHE A 1 233 ? -62.86600 -15.56500 1.13500   1.000 36.47543 ? 229 PHE A CZ     1 
ATOM   1717 N  N      . ALA A 1 234 ? -63.65300 -18.06900 6.07400   1.000 35.20159 ? 230 ALA A N      1 
ATOM   1718 C  CA     . ALA A 1 234 ? -63.66200 -19.47000 5.65600   1.000 37.97824 ? 230 ALA A CA     1 
ATOM   1719 C  C      . ALA A 1 234 ? -64.98500 -20.15200 5.99500   1.000 36.76493 ? 230 ALA A C      1 
ATOM   1720 O  O      . ALA A 1 234 ? -65.50200 -20.94400 5.19800   1.000 34.99367 ? 230 ALA A O      1 
ATOM   1721 C  CB     . ALA A 1 234 ? -62.49500 -20.21200 6.30400   1.000 31.84329 ? 230 ALA A CB     1 
ATOM   1722 N  N      . GLU A 1 235 ? -65.55300 -19.84900 7.16800   1.000 35.72007 ? 231 GLU A N      1 
ATOM   1723 C  CA     . GLU A 1 235 ? -66.82000 -20.46400 7.55300   1.000 36.42542 ? 231 GLU A CA     1 
ATOM   1724 C  C      . GLU A 1 235 ? -67.96100 -19.93100 6.70100   1.000 41.89450 ? 231 GLU A C      1 
ATOM   1725 O  O      . GLU A 1 235 ? -68.87700 -20.67700 6.33600   1.000 37.72558 ? 231 GLU A O      1 
ATOM   1726 C  CB     . GLU A 1 235 ? -67.10500 -20.21400 9.03300   1.000 38.29407 ? 231 GLU A CB     1 
ATOM   1727 C  CG     . GLU A 1 235 ? -66.15700 -20.94100 9.98600   1.000 47.56623 ? 231 GLU A CG     1 
ATOM   1728 C  CD     . GLU A 1 235 ? -66.47300 -20.69500 11.45900  1.000 51.99834 ? 231 GLU A CD     1 
ATOM   1729 O  OE1    . GLU A 1 235 ? -66.09400 -21.54000 12.29800  1.000 53.96436 ? 231 GLU A OE1    1 
ATOM   1730 O  OE2    . GLU A 1 235 ? -67.09300 -19.66000 11.78200  1.000 54.99080 ? 231 GLU A OE2    1 
ATOM   1731 N  N      . LEU A 1 236 ? -67.93400 -18.63700 6.39100   1.000 42.46299 ? 232 LEU A N      1 
ATOM   1732 C  CA     . LEU A 1 236 ? -68.98100 -18.06000 5.56200   1.000 33.71457 ? 232 LEU A CA     1 
ATOM   1733 C  C      . LEU A 1 236 ? -69.01400 -18.71600 4.18600   1.000 37.74663 ? 232 LEU A C      1 
ATOM   1734 O  O      . LEU A 1 236 ? -70.08900 -18.96000 3.62800   1.000 38.48619 ? 232 LEU A O      1 
ATOM   1735 C  CB     . LEU A 1 236 ? -68.75000 -16.55300 5.44200   1.000 33.10397 ? 232 LEU A CB     1 
ATOM   1736 C  CG     . LEU A 1 236 ? -69.64400 -15.73600 4.51500   1.000 38.56778 ? 232 LEU A CG     1 
ATOM   1737 C  CD1    . LEU A 1 236 ? -71.08700 -15.67700 5.02500   1.000 40.73646 ? 232 LEU A CD1    1 
ATOM   1738 C  CD2    . LEU A 1 236 ? -69.05800 -14.34000 4.36500   1.000 40.53381 ? 232 LEU A CD2    1 
ATOM   1739 N  N      . THR A 1 237 ? -67.85200 -19.04100 3.63500   1.000 32.29071 ? 233 THR A N      1 
ATOM   1740 C  CA     . THR A 1 237 ? -67.76600 -19.54500 2.27200   1.000 36.54649 ? 233 THR A CA     1 
ATOM   1741 C  C      . THR A 1 237 ? -67.62700 -21.05900 2.18200   1.000 38.07299 ? 233 THR A C      1 
ATOM   1742 O  O      . THR A 1 237 ? -67.78900 -21.61000 1.09300   1.000 37.97561 ? 233 THR A O      1 
ATOM   1743 C  CB     . THR A 1 237 ? -66.58000 -18.90500 1.55800   1.000 40.90754 ? 233 THR A CB     1 
ATOM   1744 O  OG1    . THR A 1 237 ? -65.38000 -19.22300 2.28100   1.000 36.82810 ? 233 THR A OG1    1 
ATOM   1745 C  CG2    . THR A 1 237 ? -66.75800 -17.39400 1.50400   1.000 35.81745 ? 233 THR A CG2    1 
ATOM   1746 N  N      . GLY A 1 238 ? -67.31300 -21.74300 3.27700   1.000 39.64949 ? 234 GLY A N      1 
ATOM   1747 C  CA     . GLY A 1 238 ? -67.00200 -23.15300 3.17200   1.000 34.97788 ? 234 GLY A CA     1 
ATOM   1748 C  C      . GLY A 1 238 ? -65.68200 -23.46300 2.49300   1.000 37.94666 ? 234 GLY A C      1 
ATOM   1749 O  O      . GLY A 1 238 ? -65.46600 -24.59900 2.07300   1.000 40.61276 ? 234 GLY A O      1 
ATOM   1750 N  N      . ILE A 1 239 ? -64.79300 -22.49000 2.35800   1.000 29.67198 ? 235 ILE A N      1 
ATOM   1751 C  CA     . ILE A 1 239 ? -63.53500 -22.73400 1.65100   1.000 29.15086 ? 235 ILE A CA     1 
ATOM   1752 C  C      . ILE A 1 239 ? -62.52600 -23.33400 2.62700   1.000 34.08303 ? 235 ILE A C      1 
ATOM   1753 O  O      . ILE A 1 239 ? -62.25500 -22.72800 3.67800   1.000 33.58297 ? 235 ILE A O      1 
ATOM   1754 C  CB     . ILE A 1 239 ? -62.99300 -21.45400 1.03200   1.000 31.63537 ? 235 ILE A CB     1 
ATOM   1755 C  CG1    . ILE A 1 239 ? -63.94500 -20.92900 -0.04800  1.000 36.09380 ? 235 ILE A CG1    1 
ATOM   1756 C  CG2    . ILE A 1 239 ? -61.66200 -21.73600 0.40200   1.000 29.21403 ? 235 ILE A CG2    1 
ATOM   1757 C  CD1    . ILE A 1 239 ? -63.53800 -19.56600 -0.57100  1.000 32.74603 ? 235 ILE A CD1    1 
ATOM   1758 N  N      . PRO A 1 240 ? -61.94100 -24.48200 2.30200   1.000 31.63274 ? 236 PRO A N      1 
ATOM   1759 C  CA     . PRO A 1 240 ? -60.91800 -25.07000 3.17000   1.000 33.45664 ? 236 PRO A CA     1 
ATOM   1760 C  C      . PRO A 1 240 ? -59.63200 -24.24800 3.16200   1.000 37.31237 ? 236 PRO A C      1 
ATOM   1761 O  O      . PRO A 1 240 ? -59.28500 -23.58900 2.17600   1.000 33.35926 ? 236 PRO A O      1 
ATOM   1762 C  CB     . PRO A 1 240 ? -60.69300 -26.46200 2.57000   1.000 36.71493 ? 236 PRO A CB     1 
ATOM   1763 C  CG     . PRO A 1 240 ? -61.29800 -26.41000 1.16200   1.000 38.55199 ? 236 PRO A CG     1 
ATOM   1764 C  CD     . PRO A 1 240 ? -62.34000 -25.35200 1.17500   1.000 30.70368 ? 236 PRO A CD     1 
ATOM   1765 N  N      . VAL A 1 241 ? -58.91200 -24.31200 4.28100   1.000 28.26918 ? 237 VAL A N      1 
ATOM   1766 C  CA     . VAL A 1 241 ? -57.78100 -23.42600 4.53500   1.000 29.43248 ? 237 VAL A CA     1 
ATOM   1767 C  C      . VAL A 1 241 ? -56.55500 -24.26500 4.84000   1.000 29.06664 ? 237 VAL A C      1 
ATOM   1768 O  O      . VAL A 1 241 ? -56.54700 -25.03700 5.80500   1.000 28.19812 ? 237 VAL A O      1 
ATOM   1769 C  CB     . VAL A 1 241 ? -58.05200 -22.45300 5.69300   1.000 32.00910 ? 237 VAL A CB     1 
ATOM   1770 C  CG1    . VAL A 1 241 ? -56.81100 -21.58400 5.93900   1.000 24.29239 ? 237 VAL A CG1    1 
ATOM   1771 C  CG2    . VAL A 1 241 ? -59.27600 -21.59600 5.39900   1.000 27.37170 ? 237 VAL A CG2    1 
ATOM   1772 N  N      . ALA A 1 242 ? -55.52900 -24.12300 4.02000   1.000 29.45880 ? 238 ALA A N      1 
ATOM   1773 C  CA     . ALA A 1 242 ? -54.19300 -24.56400 4.37700   1.000 29.46143 ? 238 ALA A CA     1 
ATOM   1774 C  C      . ALA A 1 242 ? -53.37900 -23.35100 4.80700   1.000 30.44839 ? 238 ALA A C      1 
ATOM   1775 O  O      . ALA A 1 242 ? -53.67700 -22.21600 4.43300   1.000 30.19573 ? 238 ALA A O      1 
ATOM   1776 C  CB     . ALA A 1 242 ? -53.51600 -25.26700 3.20200   1.000 26.72689 ? 238 ALA A CB     1 
ATOM   1777 N  N      . THR A 1 243 ? -52.36100 -23.59500 5.61800   1.000 26.40317 ? 239 THR A N      1 
ATOM   1778 C  CA     . THR A 1 243 ? -51.39300 -22.56900 5.97000   1.000 25.31619 ? 239 THR A CA     1 
ATOM   1779 C  C      . THR A 1 243 ? -50.02100 -22.97000 5.44900   1.000 27.04535 ? 239 THR A C      1 
ATOM   1780 O  O      . THR A 1 243 ? -49.75600 -24.14800 5.18700   1.000 25.21618 ? 239 THR A O      1 
ATOM   1781 C  CB     . THR A 1 243 ? -51.29800 -22.36000 7.48400   1.000 32.15386 ? 239 THR A CB     1 
ATOM   1782 O  OG1    . THR A 1 243 ? -50.57800 -23.46500 8.05900   1.000 30.61157 ? 239 THR A OG1    1 
ATOM   1783 C  CG2    . THR A 1 243 ? -52.68600 -22.25000 8.11100   1.000 22.44743 ? 239 THR A CG2    1 
ATOM   1784 N  N      . THR A 1 244 ? -49.14600 -21.97300 5.30500   1.000 27.60068 ? 240 THR A N      1 
ATOM   1785 C  CA     . THR A 1 244 ? -47.73600 -22.23400 5.09400   1.000 21.13938 ? 240 THR A CA     1 
ATOM   1786 C  C      . THR A 1 244 ? -47.15300 -22.77200 6.38900   1.000 26.96113 ? 240 THR A C      1 
ATOM   1787 O  O      . THR A 1 244 ? -47.77600 -22.69000 7.44400   1.000 25.90047 ? 240 THR A O      1 
ATOM   1788 C  CB     . THR A 1 244 ? -47.01000 -20.96400 4.68600   1.000 21.95000 ? 240 THR A CB     1 
ATOM   1789 O  OG1    . THR A 1 244 ? -47.06700 -20.03400 5.78100   1.000 26.00049 ? 240 THR A OG1    1 
ATOM   1790 C  CG2    . THR A 1 244 ? -47.65200 -20.35500 3.42600   1.000 20.85250 ? 240 THR A CG2    1 
ATOM   1791 N  N      . PRO A 1 245 ? -45.95600 -23.34000 6.34000   1.000 27.80070 ? 241 PRO A N      1 
ATOM   1792 C  CA     . PRO A 1 245 ? -45.32800 -23.78700 7.59000   1.000 26.61372 ? 241 PRO A CA     1 
ATOM   1793 C  C      . PRO A 1 245 ? -45.21900 -22.67000 8.61700   1.000 27.35854 ? 241 PRO A C      1 
ATOM   1794 O  O      . PRO A 1 245 ? -45.62100 -22.84600 9.77400   1.000 25.80046 ? 241 PRO A O      1 
ATOM   1795 C  CB     . PRO A 1 245 ? -43.96100 -24.29700 7.11400   1.000 21.88157 ? 241 PRO A CB     1 
ATOM   1796 C  CG     . PRO A 1 245 ? -44.23000 -24.76000 5.68700   1.000 26.05576 ? 241 PRO A CG     1 
ATOM   1797 C  CD     . PRO A 1 245 ? -45.19200 -23.74000 5.14300   1.000 26.68741 ? 241 PRO A CD     1 
ATOM   1798 N  N      . LYS A 1 246 ? -44.70000 -21.51400 8.21400   1.000 24.88719 ? 242 LYS A N      1 
ATOM   1799 C  CA     . LYS A 1 246 ? -44.56500 -20.40700 9.15200   1.000 29.47195 ? 242 LYS A CA     1 
ATOM   1800 C  C      . LYS A 1 246 ? -45.91900 -19.84400 9.54400   1.000 28.82451 ? 242 LYS A C      1 
ATOM   1801 O  O      . LYS A 1 246 ? -46.06300 -19.28700 10.64100  1.000 27.81912 ? 242 LYS A O      1 
ATOM   1802 C  CB     . LYS A 1 246 ? -43.69500 -19.30400 8.55800   1.000 25.00037 ? 242 LYS A CB     1 
ATOM   1803 C  CG     . LYS A 1 246 ? -43.32300 -18.24200 9.57400   1.000 24.93194 ? 242 LYS A CG     1 
ATOM   1804 C  CD     . LYS A 1 246 ? -42.07100 -17.44600 9.12800   1.000 30.47734 ? 242 LYS A CD     1 
ATOM   1805 C  CE     . LYS A 1 246 ? -42.40100 -16.36000 8.09300   1.000 29.73514 ? 242 LYS A CE     1 
ATOM   1806 N  NZ     . LYS A 1 246 ? -41.19100 -15.84800 7.31900   1.000 25.30303 ? 242 LYS A NZ     1 
ATOM   1807 N  N      . GLY A 1 247 ? -46.91300 -19.96400 8.66200   1.000 25.49779 ? 243 GLY A N      1 
ATOM   1808 C  CA     . GLY A 1 247 ? -48.25700 -19.52400 8.95100   1.000 23.84496 ? 243 GLY A CA     1 
ATOM   1809 C  C      . GLY A 1 247 ? -49.04800 -20.45100 9.83600   1.000 26.95850 ? 243 GLY A C      1 
ATOM   1810 O  O      . GLY A 1 247 ? -50.21000 -20.16400 10.13300  1.000 25.71098 ? 243 GLY A O      1 
ATOM   1811 N  N      . LYS A 1 248 ? -48.46400 -21.53900 10.27900  1.000 21.31045 ? 244 LYS A N      1 
ATOM   1812 C  CA     . LYS A 1 248 ? -49.12200 -22.43700 11.18900  1.000 24.94510 ? 244 LYS A CA     1 
ATOM   1813 C  C      . LYS A 1 248 ? -49.55200 -21.65400 12.44600  1.000 30.46418 ? 244 LYS A C      1 
ATOM   1814 O  O      . LYS A 1 248 ? -48.78400 -20.86200 12.98400  1.000 29.86411 ? 244 LYS A O      1 
ATOM   1815 C  CB     . LYS A 1 248 ? -48.25300 -23.63900 11.53200  1.000 22.91854 ? 244 LYS A CB     1 
ATOM   1816 C  CG     . LYS A 1 248 ? -48.89600 -24.69100 12.39200  1.000 22.36847 ? 244 LYS A CG     1 
ATOM   1817 C  CD     . LYS A 1 248 ? -47.88700 -25.69300 12.86500  1.000 24.38187 ? 244 LYS A CD     1 
ATOM   1818 C  CE     . LYS A 1 248 ? -48.47900 -26.88500 13.52100  1.000 24.98984 ? 244 LYS A CE     1 
ATOM   1819 N  NZ     . LYS A 1 248 ? -49.08200 -27.84300 12.60700  1.000 30.05360 ? 244 LYS A NZ     1 
ATOM   1820 N  N      . SER A 1 249 ? -50.79800 -21.91700 12.81100  1.000 30.15098 ? 245 SER A N      1 
ATOM   1821 C  CA     . SER A 1 249 ? -51.64000 -21.33100 13.86500  1.000 32.49600 ? 245 SER A CA     1 
ATOM   1822 C  C      . SER A 1 249 ? -52.42400 -20.11400 13.35300  1.000 36.32278 ? 245 SER A C      1 
ATOM   1823 O  O      . SER A 1 249 ? -53.01500 -19.42300 14.11600  1.000 31.92225 ? 245 SER A O      1 
ATOM   1824 C  CB     . SER A 1 249 ? -50.99400 -21.03900 15.22600  1.000 21.82630 ? 245 SER A CB     1 
ATOM   1825 O  OG     . SER A 1 249 ? -50.12200 -19.96500 15.12000  1.000 27.71648 ? 245 SER A OG     1 
ATOM   1826 N  N      . SER A 1 250 ? -52.41400 -19.86400 12.06400  1.000 27.39802 ? 246 SER A N      1 
ATOM   1827 C  CA     . SER A 1 250 ? -53.22100 -18.79200 11.56200  1.000 28.72713 ? 246 SER A CA     1 
ATOM   1828 C  C      . SER A 1 250 ? -54.65600 -19.25300 11.44100  1.000 29.51143 ? 246 SER A C      1 
ATOM   1829 O  O      . SER A 1 250 ? -55.50700 -18.46100 11.39300  1.000 34.19884 ? 246 SER A O      1 
ATOM   1830 C  CB     . SER A 1 250 ? -52.78200 -18.26700 10.22100  1.000 30.06676 ? 246 SER A CB     1 
ATOM   1831 O  OG     . SER A 1 250 ? -51.49600 -17.77000 10.26800  1.000 41.49445 ? 246 SER A OG     1 
ATOM   1832 N  N      . PHE A 1 251 ? -54.88400 -20.54600 11.39500  1.000 27.66911 ? 247 PHE A N      1 
ATOM   1833 C  CA     . PHE A 1 251 ? -56.20200 -21.11800 11.27700  1.000 27.24537 ? 247 PHE A CA     1 
ATOM   1834 C  C      . PHE A 1 251 ? -56.27000 -22.33100 12.19700  1.000 33.14345 ? 247 PHE A C      1 
ATOM   1835 O  O      . PHE A 1 251 ? -55.30200 -23.10100 12.27500  1.000 32.29071 ? 247 PHE A O      1 
ATOM   1836 C  CB     . PHE A 1 251 ? -56.49300 -21.52000 9.82700   1.000 25.27671 ? 247 PHE A CB     1 
ATOM   1837 C  CG     . PHE A 1 251 ? -57.91800 -21.89300 9.58500   1.000 29.25614 ? 247 PHE A CG     1 
ATOM   1838 C  CD1    . PHE A 1 251 ? -58.89500 -20.91300 9.47100   1.000 26.73742 ? 247 PHE A CD1    1 
ATOM   1839 C  CD2    . PHE A 1 251 ? -58.29000 -23.22700 9.48000   1.000 25.78467 ? 247 PHE A CD2    1 
ATOM   1840 C  CE1    . PHE A 1 251 ? -60.20900 -21.25100 9.24900   1.000 27.61121 ? 247 PHE A CE1    1 
ATOM   1841 C  CE2    . PHE A 1 251 ? -59.61100 -23.57300 9.26900   1.000 31.50378 ? 247 PHE A CE2    1 
ATOM   1842 C  CZ     . PHE A 1 251 ? -60.57000 -22.58900 9.15500   1.000 33.65930 ? 247 PHE A CZ     1 
ATOM   1843 N  N      . PRO A 1 252 ? -57.37600 -22.52300 12.91800  1.000 33.11976 ? 248 PRO A N      1 
ATOM   1844 C  CA     . PRO A 1 252 ? -57.42800 -23.61700 13.91300  1.000 30.33785 ? 248 PRO A CA     1 
ATOM   1845 C  C      . PRO A 1 252 ? -57.35000 -24.98000 13.23600  1.000 34.91734 ? 248 PRO A C      1 
ATOM   1846 O  O      . PRO A 1 252 ? -58.17900 -25.32200 12.39300  1.000 37.92297 ? 248 PRO A O      1 
ATOM   1847 C  CB     . PRO A 1 252 ? -58.77300 -23.40500 14.62700  1.000 30.75895 ? 248 PRO A CB     1 
ATOM   1848 C  CG     . PRO A 1 252 ? -59.51800 -22.36400 13.83900  1.000 37.98613 ? 248 PRO A CG     1 
ATOM   1849 C  CD     . PRO A 1 252 ? -58.52300 -21.60500 13.00400  1.000 34.93840 ? 248 PRO A CD     1 
ATOM   1850 N  N      . GLU A 1 253 ? -56.34800 -25.76900 13.62300  1.000 32.49337 ? 249 GLU A N      1 
ATOM   1851 C  CA     . GLU A 1 253 ? -56.07100 -27.00900 12.90600  1.000 33.08028 ? 249 GLU A CA     1 
ATOM   1852 C  C      . GLU A 1 253 ? -57.01400 -28.14800 13.26900  1.000 33.73299 ? 249 GLU A C      1 
ATOM   1853 O  O      . GLU A 1 253 ? -56.98400 -29.18200 12.59300  1.000 39.19154 ? 249 GLU A O      1 
ATOM   1854 C  CB     . GLU A 1 253 ? -54.60500 -27.41600 13.12400  1.000 37.73610 ? 249 GLU A CB     1 
ATOM   1855 C  CG     . GLU A 1 253 ? -53.65200 -26.59300 12.27000  1.000 30.90371 ? 249 GLU A CG     1 
ATOM   1856 C  CD     . GLU A 1 253 ? -52.19600 -27.05900 12.33700  1.000 43.92369 ? 249 GLU A CD     1 
ATOM   1857 O  OE1    . GLU A 1 253 ? -51.73900 -27.50500 13.41500  1.000 42.65511 ? 249 GLU A OE1    1 
ATOM   1858 O  OE2    . GLU A 1 253 ? -51.50000 -26.96700 11.30200  1.000 40.43643 ? 249 GLU A OE2    1 
ATOM   1859 N  N      . ASN A 1 254 ? -57.85100 -27.98600 14.29600  1.000 32.59601 ? 250 ASN A N      1 
ATOM   1860 C  CA     . ASN A 1 254 ? -58.91800 -28.92900 14.61100  1.000 35.83851 ? 250 ASN A CA     1 
ATOM   1861 C  C      . ASN A 1 254 ? -60.22800 -28.57500 13.91700  1.000 37.77032 ? 250 ASN A C      1 
ATOM   1862 O  O      . ASN A 1 254 ? -61.23100 -29.27300 14.10300  1.000 35.47794 ? 250 ASN A O      1 
ATOM   1863 C  CB     . ASN A 1 254 ? -59.13700 -28.99800 16.13400  1.000 35.80429 ? 250 ASN A CB     1 
ATOM   1864 C  CG     . ASN A 1 254 ? -59.40400 -27.63300 16.74600  1.000 42.96568 ? 250 ASN A CG     1 
ATOM   1865 O  OD1    . ASN A 1 254 ? -58.96300 -26.60500 16.22700  1.000 45.43703 ? 250 ASN A OD1    1 
ATOM   1866 N  ND2    . ASN A 1 254 ? -60.12400 -27.61600 17.85000  1.000 51.96413 ? 250 ASN A ND2    1 
ATOM   1867 N  N      . HIS A 1 255 ? -60.24200 -27.50200 13.13700  1.000 37.50450 ? 251 HIS A N      1 
ATOM   1868 C  CA     . HIS A 1 255 ? -61.45000 -27.05900 12.46400  1.000 36.08854 ? 251 HIS A CA     1 
ATOM   1869 C  C      . HIS A 1 255 ? -61.74700 -27.96000 11.27200  1.000 35.89641 ? 251 HIS A C      1 
ATOM   1870 O  O      . HIS A 1 255 ? -60.84000 -28.47900 10.61800  1.000 36.43858 ? 251 HIS A O      1 
ATOM   1871 C  CB     . HIS A 1 255 ? -61.27300 -25.60600 12.01500  1.000 41.48392 ? 251 HIS A CB     1 
ATOM   1872 C  CG     . HIS A 1 255 ? -62.54800 -24.91200 11.65500  1.000 39.72845 ? 251 HIS A CG     1 
ATOM   1873 N  ND1    . HIS A 1 255 ? -63.22300 -25.16100 10.47900  1.000 39.73371 ? 251 HIS A ND1    1 
ATOM   1874 C  CD2    . HIS A 1 255 ? -63.25100 -23.95100 12.29900  1.000 39.20733 ? 251 HIS A CD2    1 
ATOM   1875 C  CE1    . HIS A 1 255 ? -64.30400 -24.40200 10.42700  1.000 37.58872 ? 251 HIS A CE1    1 
ATOM   1876 N  NE2    . HIS A 1 255 ? -64.34000 -23.65300 11.51500  1.000 39.43631 ? 251 HIS A NE2    1 
ATOM   1877 N  N      . ALA A 1 256 ? -63.03800 -28.13800 10.98500  1.000 32.48811 ? 252 ALA A N      1 
ATOM   1878 C  CA     . ALA A 1 256 ? -63.42600 -29.01500 9.89100   1.000 36.88600 ? 252 ALA A CA     1 
ATOM   1879 C  C      . ALA A 1 256 ? -62.93700 -28.50000 8.54100   1.000 37.92034 ? 252 ALA A C      1 
ATOM   1880 O  O      . ALA A 1 256 ? -62.80200 -29.28700 7.60000   1.000 39.08100 ? 252 ALA A O      1 
ATOM   1881 C  CB     . ALA A 1 256 ? -64.94500 -29.19900 9.87900   1.000 34.19621 ? 252 ALA A CB     1 
ATOM   1882 N  N      . LEU A 1 257 ? -62.67400 -27.20600 8.41800   1.000 35.19369 ? 253 LEU A N      1 
ATOM   1883 C  CA     . LEU A 1 257 ? -62.20700 -26.65200 7.15500   1.000 33.95933 ? 253 LEU A CA     1 
ATOM   1884 C  C      . LEU A 1 257 ? -60.68400 -26.62600 7.03800   1.000 35.29107 ? 253 LEU A C      1 
ATOM   1885 O  O      . LEU A 1 257 ? -60.16600 -26.16600 6.01400   1.000 32.24334 ? 253 LEU A O      1 
ATOM   1886 C  CB     . LEU A 1 257 ? -62.75900 -25.23300 6.96400   1.000 33.13555 ? 253 LEU A CB     1 
ATOM   1887 C  CG     . LEU A 1 257 ? -64.25900 -25.07600 6.71100   1.000 39.51263 ? 253 LEU A CG     1 
ATOM   1888 C  CD1    . LEU A 1 257 ? -64.63900 -23.59100 6.71800   1.000 37.82296 ? 253 LEU A CD1    1 
ATOM   1889 C  CD2    . LEU A 1 257 ? -64.65900 -25.74600 5.40200   1.000 40.24430 ? 253 LEU A CD2    1 
ATOM   1890 N  N      . SER A 1 258 ? -59.95400 -27.15400 8.02300   1.000 32.45652 ? 254 SER A N      1 
ATOM   1891 C  CA     . SER A 1 258 ? -58.50100 -27.05800 8.01300   1.000 31.68801 ? 254 SER A CA     1 
ATOM   1892 C  C      . SER A 1 258 ? -57.88100 -28.16900 7.18300   1.000 32.57496 ? 254 SER A C      1 
ATOM   1893 O  O      . SER A 1 258 ? -58.14600 -29.35200 7.40800   1.000 34.85418 ? 254 SER A O      1 
ATOM   1894 C  CB     . SER A 1 258 ? -57.93400 -27.13400 9.42800   1.000 34.35149 ? 254 SER A CB     1 
ATOM   1895 O  OG     . SER A 1 258 ? -56.51400 -27.26900 9.36200   1.000 32.11174 ? 254 SER A OG     1 
ATOM   1896 N  N      . LEU A 1 259 ? -57.03000 -27.77800 6.24500   1.000 27.33749 ? 255 LEU A N      1 
ATOM   1897 C  CA     . LEU A 1 259 ? -56.22900 -28.70900 5.46900   1.000 34.04882 ? 255 LEU A CA     1 
ATOM   1898 C  C      . LEU A 1 259 ? -54.90100 -29.02600 6.13500   1.000 35.56216 ? 255 LEU A C      1 
ATOM   1899 O  O      . LEU A 1 259 ? -54.16900 -29.89300 5.64300   1.000 38.08088 ? 255 LEU A O      1 
ATOM   1900 C  CB     . LEU A 1 259 ? -55.96100 -28.13200 4.06800   1.000 31.60379 ? 255 LEU A CB     1 
ATOM   1901 C  CG     . LEU A 1 259 ? -57.20200 -27.93900 3.19600   1.000 30.51945 ? 255 LEU A CG     1 
ATOM   1902 C  CD1    . LEU A 1 259 ? -56.85100 -27.14700 1.93700   1.000 29.14034 ? 255 LEU A CD1    1 
ATOM   1903 C  CD2    . LEU A 1 259 ? -57.78200 -29.28500 2.84400   1.000 30.70368 ? 255 LEU A CD2    1 
ATOM   1904 N  N      . GLY A 1 260 ? -54.57800 -28.34200 7.23200   1.000 33.32768 ? 256 GLY A N      1 
ATOM   1905 C  CA     . GLY A 1 260 ? -53.26800 -28.46400 7.83600   1.000 29.35615 ? 256 GLY A CA     1 
ATOM   1906 C  C      . GLY A 1 260 ? -52.26800 -27.59500 7.09300   1.000 33.60140 ? 256 GLY A C      1 
ATOM   1907 O  O      . GLY A 1 260 ? -52.61700 -26.61300 6.42200   1.000 28.86925 ? 256 GLY A O      1 
ATOM   1908 N  N      . VAL A 1 261 ? -51.00800 -27.99800 7.18500   1.000 24.16869 ? 257 VAL A N      1 
ATOM   1909 C  CA     . VAL A 1 261 ? -49.89100 -27.24500 6.62400   1.000 23.55282 ? 257 VAL A CA     1 
ATOM   1910 C  C      . VAL A 1 261 ? -49.60000 -27.77200 5.22500   1.000 29.02980 ? 257 VAL A C      1 
ATOM   1911 O  O      . VAL A 1 261 ? -49.49700 -28.98900 5.01900   1.000 29.12981 ? 257 VAL A O      1 
ATOM   1912 C  CB     . VAL A 1 261 ? -48.64600 -27.37100 7.52500   1.000 26.77689 ? 257 VAL A CB     1 
ATOM   1913 C  CG1    . VAL A 1 261 ? -47.42300 -26.70900 6.88500   1.000 24.96878 ? 257 VAL A CG1    1 
ATOM   1914 C  CG2    . VAL A 1 261 ? -48.90800 -26.80900 8.92400   1.000 24.99510 ? 257 VAL A CG2    1 
ATOM   1915 N  N      . PHE A 1 262 ? -49.48100 -26.86500 4.25500   1.000 29.87727 ? 258 PHE A N      1 
ATOM   1916 C  CA     . PHE A 1 262 ? -48.96800 -27.20300 2.93200   1.000 27.14536 ? 258 PHE A CA     1 
ATOM   1917 C  C      . PHE A 1 262 ? -47.48400 -26.85300 2.82800   1.000 29.55354 ? 258 PHE A C      1 
ATOM   1918 O  O      . PHE A 1 262 ? -47.07100 -25.75900 3.21800   1.000 28.22444 ? 258 PHE A O      1 
ATOM   1919 C  CB     . PHE A 1 262 ? -49.72700 -26.47900 1.82500   1.000 31.83013 ? 258 PHE A CB     1 
ATOM   1920 C  CG     . PHE A 1 262 ? -49.12900 -26.71100 0.47100   1.000 35.33318 ? 258 PHE A CG     1 
ATOM   1921 C  CD1    . PHE A 1 262 ? -49.21900 -27.95200 -0.12800  1.000 35.85693 ? 258 PHE A CD1    1 
ATOM   1922 C  CD2    . PHE A 1 262 ? -48.40900 -25.71700 -0.16600  1.000 34.27516 ? 258 PHE A CD2    1 
ATOM   1923 C  CE1    . PHE A 1 262 ? -48.64100 -28.18200 -1.36700  1.000 39.83636 ? 258 PHE A CE1    1 
ATOM   1924 C  CE2    . PHE A 1 262 ? -47.82100 -25.94600 -1.39700  1.000 34.80680 ? 258 PHE A CE2    1 
ATOM   1925 C  CZ     . PHE A 1 262 ? -47.93900 -27.17600 -2.00000  1.000 31.78539 ? 258 PHE A CZ     1 
ATOM   1926 N  N      . GLY A 1 263 ? -46.69200 -27.76700 2.27500   1.000 27.93493 ? 259 GLY A N      1 
ATOM   1927 C  CA     . GLY A 1 263 ? -45.29200 -27.46300 2.04300   1.000 28.77450 ? 259 GLY A CA     1 
ATOM   1928 C  C      . GLY A 1 263 ? -44.34800 -28.27000 2.91700   1.000 29.44037 ? 259 GLY A C      1 
ATOM   1929 O  O      . GLY A 1 263 ? -44.63300 -29.42100 3.26400   1.000 34.35412 ? 259 GLY A O      1 
ATOM   1930 N  N      . PHE A 1 264 ? -43.23100 -27.67000 3.30100   1.000 25.79783 ? 260 PHE A N      1 
ATOM   1931 C  CA     . PHE A 1 264 ? -42.20900 -28.41600 4.02100   1.000 32.11438 ? 260 PHE A CA     1 
ATOM   1932 C  C      . PHE A 1 264 ? -42.77900 -28.99000 5.31600   1.000 28.92715 ? 260 PHE A C      1 
ATOM   1933 O  O      . PHE A 1 264 ? -43.40100 -28.27700 6.11000   1.000 27.90598 ? 260 PHE A O      1 
ATOM   1934 C  CB     . PHE A 1 264 ? -41.01100 -27.51400 4.32700   1.000 27.92966 ? 260 PHE A CB     1 
ATOM   1935 C  CG     . PHE A 1 264 ? -39.87100 -28.23500 4.97600   1.000 35.63059 ? 260 PHE A CG     1 
ATOM   1936 C  CD1    . PHE A 1 264 ? -39.05300 -29.07000 4.23300   1.000 38.38881 ? 260 PHE A CD1    1 
ATOM   1937 C  CD2    . PHE A 1 264 ? -39.62700 -28.09800 6.32900   1.000 33.41190 ? 260 PHE A CD2    1 
ATOM   1938 C  CE1    . PHE A 1 264 ? -37.99700 -29.74300 4.83000   1.000 43.13675 ? 260 PHE A CE1    1 
ATOM   1939 C  CE2    . PHE A 1 264 ? -38.58100 -28.76500 6.92900   1.000 35.72007 ? 260 PHE A CE2    1 
ATOM   1940 C  CZ     . PHE A 1 264 ? -37.76300 -29.58900 6.18100   1.000 40.16271 ? 260 PHE A CZ     1 
ATOM   1941 N  N      . ALA A 1 265 ? -42.58000 -30.29200 5.51000   1.000 28.39025 ? 261 ALA A N      1 
ATOM   1942 C  CA     . ALA A 1 265 ? -43.08900 -31.03500 6.66300   1.000 29.97465 ? 261 ALA A CA     1 
ATOM   1943 C  C      . ALA A 1 265 ? -44.60600 -30.96300 6.78300   1.000 32.11701 ? 261 ALA A C      1 
ATOM   1944 O  O      . ALA A 1 265 ? -45.15400 -31.20800 7.86400   1.000 35.37793 ? 261 ALA A O      1 
ATOM   1945 C  CB     . ALA A 1 265 ? -42.45200 -30.53900 7.96500   1.000 24.42135 ? 261 ALA A CB     1 
ATOM   1946 N  N      . GLY A 1 266 ? -45.30600 -30.63100 5.70200   1.000 32.28545 ? 262 GLY A N      1 
ATOM   1947 C  CA     . GLY A 1 266 ? -46.74000 -30.43500 5.76200   1.000 29.21666 ? 262 GLY A CA     1 
ATOM   1948 C  C      . GLY A 1 266 ? -47.49800 -31.75200 5.74600   1.000 34.19094 ? 262 GLY A C      1 
ATOM   1949 O  O      . GLY A 1 266 ? -46.92900 -32.84200 5.83800   1.000 36.87284 ? 262 GLY A O      1 
ATOM   1950 N  N      . HIS A 1 267 ? -48.81400 -31.63800 5.59300   1.000 29.27193 ? 263 HIS A N      1 
ATOM   1951 C  CA     . HIS A 1 267 ? -49.71600 -32.77300 5.74000   1.000 35.23580 ? 263 HIS A CA     1 
ATOM   1952 C  C      . HIS A 1 267 ? -50.24300 -33.23300 4.39200   1.000 37.38606 ? 263 HIS A C      1 
ATOM   1953 O  O      . HIS A 1 267 ? -50.50100 -32.41500 3.49400   1.000 36.40173 ? 263 HIS A O      1 
ATOM   1954 C  CB     . HIS A 1 267 ? -50.87600 -32.42100 6.67000   1.000 29.25614 ? 263 HIS A CB     1 
ATOM   1955 C  CG     . HIS A 1 267 ? -50.42000 -31.93700 8.00500   1.000 32.42757 ? 263 HIS A CG     1 
ATOM   1956 N  ND1    . HIS A 1 267 ? -50.38100 -30.60100 8.33900   1.000 36.15433 ? 263 HIS A ND1    1 
ATOM   1957 C  CD2    . HIS A 1 267 ? -49.95600 -32.60900 9.08500   1.000 32.48284 ? 263 HIS A CD2    1 
ATOM   1958 C  CE1    . HIS A 1 267 ? -49.93000 -30.47100 9.57400   1.000 33.66983 ? 263 HIS A CE1    1 
ATOM   1959 N  NE2    . HIS A 1 267 ? -49.66000 -31.67500 10.04700  1.000 31.53273 ? 263 HIS A NE2    1 
ATOM   1960 N  N      . GLN A 1 268 ? -50.38900 -34.55300 4.25900   1.000 37.43080 ? 264 GLN A N      1 
ATOM   1961 C  CA     . GLN A 1 268 ? -50.85600 -35.12500 3.00300   1.000 40.83648 ? 264 GLN A CA     1 
ATOM   1962 C  C      . GLN A 1 268 ? -52.21100 -34.55400 2.61100   1.000 38.39671 ? 264 GLN A C      1 
ATOM   1963 O  O      . GLN A 1 268 ? -52.46100 -34.27800 1.43100   1.000 45.22121 ? 264 GLN A O      1 
ATOM   1964 C  CB     . GLN A 1 268 ? -50.92400 -36.65300 3.11600   1.000 43.45521 ? 264 GLN A CB     1 
ATOM   1965 C  CG     . GLN A 1 268 ? -51.08400 -37.36600 1.77500   1.000 46.31345 ? 264 GLN A CG     1 
ATOM   1966 C  CD     . GLN A 1 268 ? -49.82400 -37.28300 0.92300   1.000 57.96484 ? 264 GLN A CD     1 
ATOM   1967 O  OE1    . GLN A 1 268 ? -49.83900 -36.73900 -0.18100  1.000 63.58657 ? 264 GLN A OE1    1 
ATOM   1968 N  NE2    . GLN A 1 268 ? -48.72300 -37.81600 1.44300   1.000 61.06522 ? 264 GLN A NE2    1 
ATOM   1969 N  N      . LYS A 1 269 ? -53.08400 -34.34500 3.59200   1.000 35.00157 ? 265 LYS A N      1 
ATOM   1970 C  CA     . LYS A 1 269 ? -54.38400 -33.73800 3.31900   1.000 33.84090 ? 265 LYS A CA     1 
ATOM   1971 C  C      . LYS A 1 269 ? -54.23100 -32.43500 2.53900   1.000 35.54637 ? 265 LYS A C      1 
ATOM   1972 O  O      . LYS A 1 269 ? -54.90900 -32.21400 1.53000   1.000 36.32014 ? 265 LYS A O      1 
ATOM   1973 C  CB     . LYS A 1 269 ? -55.10400 -33.49400 4.64100   1.000 38.21774 ? 265 LYS A CB     1 
ATOM   1974 C  CG     . LYS A 1 269 ? -56.50600 -32.94100 4.53500   1.000 38.97573 ? 265 LYS A CG     1 
ATOM   1975 C  CD     . LYS A 1 269 ? -57.12300 -32.89100 5.92000   1.000 42.82356 ? 265 LYS A CD     1 
ATOM   1976 C  CE     . LYS A 1 269 ? -58.59100 -32.53400 5.87200   1.000 51.47459 ? 265 LYS A CE     1 
ATOM   1977 N  NZ     . LYS A 1 269 ? -59.12500 -32.26300 7.23800   1.000 56.33833 ? 265 LYS A NZ     1 
ATOM   1978 N  N      . ALA A 1 270 ? -53.30200 -31.57400 2.96600   1.000 33.20135 ? 266 ALA A N      1 
ATOM   1979 C  CA     . ALA A 1 270 ? -53.10700 -30.32800 2.23700   1.000 35.13842 ? 266 ALA A CA     1 
ATOM   1980 C  C      . ALA A 1 270 ? -52.46200 -30.59400 0.88300   1.000 37.63346 ? 266 ALA A C      1 
ATOM   1981 O  O      . ALA A 1 270 ? -52.83400 -29.97000 -0.11700  1.000 37.88086 ? 266 ALA A O      1 
ATOM   1982 C  CB     . ALA A 1 270 ? -52.26900 -29.34800 3.05600   1.000 28.60606 ? 266 ALA A CB     1 
ATOM   1983 N  N      . THR A 1 271 ? -51.50900 -31.52900 0.82600   1.000 40.44169 ? 267 THR A N      1 
ATOM   1984 C  CA     . THR A 1 271 ? -50.85900 -31.86100 -0.44200  1.000 39.58106 ? 267 THR A CA     1 
ATOM   1985 C  C      . THR A 1 271 ? -51.86300 -32.39500 -1.45900  1.000 45.08962 ? 267 THR A C      1 
ATOM   1986 O  O      . THR A 1 271 ? -51.86900 -31.97900 -2.62600  1.000 46.66612 ? 267 THR A O      1 
ATOM   1987 C  CB     . THR A 1 271 ? -49.74300 -32.87900 -0.21300  1.000 41.08914 ? 267 THR A CB     1 
ATOM   1988 O  OG1    . THR A 1 271 ? -48.85600 -32.39300 0.80100   1.000 44.81064 ? 267 THR A OG1    1 
ATOM   1989 C  CG2    . THR A 1 271 ? -48.96100 -33.11100 -1.49600  1.000 48.66899 ? 267 THR A CG2    1 
ATOM   1990 N  N      . ASP A 1 272 ? -52.71300 -33.33500 -1.03800  1.000 41.18915 ? 268 ASP A N      1 
ATOM   1991 C  CA     . ASP A 1 272 ? -53.70600 -33.88700 -1.95100  1.000 45.35017 ? 268 ASP A CA     1 
ATOM   1992 C  C      . ASP A 1 272 ? -54.62600 -32.79800 -2.47000  1.000 47.41358 ? 268 ASP A C      1 
ATOM   1993 O  O      . ASP A 1 272 ? -54.94700 -32.75700 -3.66600  1.000 48.59793 ? 268 ASP A O      1 
ATOM   1994 C  CB     . ASP A 1 272 ? -54.54700 -34.96400 -1.25700  1.000 46.40030 ? 268 ASP A CB     1 
ATOM   1995 C  CG     . ASP A 1 272 ? -53.74600 -36.19800 -0.88700  1.000 54.48285 ? 268 ASP A CG     1 
ATOM   1996 O  OD1    . ASP A 1 272 ? -52.59700 -36.33600 -1.36500  1.000 53.46167 ? 268 ASP A OD1    1 
ATOM   1997 O  OD2    . ASP A 1 272 ? -54.27500 -37.03400 -0.11600  1.000 55.15398 ? 268 ASP A OD2    1 
ATOM   1998 N  N      . TYR A 1 273 ? -55.07400 -31.91300 -1.58200  1.000 43.34467 ? 269 TYR A N      1 
ATOM   1999 C  CA     . TYR A 1 273 ? -56.06900 -30.93300 -1.98900  1.000 44.33163 ? 269 TYR A CA     1 
ATOM   2000 C  C      . TYR A 1 273 ? -55.49900 -29.95400 -3.00900  1.000 44.34216 ? 269 TYR A C      1 
ATOM   2001 O  O      . TYR A 1 273 ? -56.12500 -29.68900 -4.04100  1.000 41.49708 ? 269 TYR A O      1 
ATOM   2002 C  CB     . TYR A 1 273 ? -56.60300 -30.19900 -0.76300  1.000 41.53919 ? 269 TYR A CB     1 
ATOM   2003 C  CG     . TYR A 1 273 ? -58.01400 -29.73200 -0.95000  1.000 39.72318 ? 269 TYR A CG     1 
ATOM   2004 C  CD1    . TYR A 1 273 ? -58.28200 -28.53100 -1.58700  1.000 38.75201 ? 269 TYR A CD1    1 
ATOM   2005 C  CD2    . TYR A 1 273 ? -59.08300 -30.50100 -0.50600  1.000 43.32625 ? 269 TYR A CD2    1 
ATOM   2006 C  CE1    . TYR A 1 273 ? -59.58100 -28.09900 -1.77100  1.000 41.87607 ? 269 TYR A CE1    1 
ATOM   2007 C  CE2    . TYR A 1 273 ? -60.38500 -30.08000 -0.69100  1.000 46.48978 ? 269 TYR A CE2    1 
ATOM   2008 C  CZ     . TYR A 1 273 ? -60.62600 -28.87600 -1.32300  1.000 51.30615 ? 269 TYR A CZ     1 
ATOM   2009 O  OH     . TYR A 1 273 ? -61.91800 -28.44900 -1.50500  1.000 65.32362 ? 269 TYR A OH     1 
ATOM   2010 N  N      . LEU A 1 274 ? -54.28800 -29.45000 -2.76000  1.000 41.87871 ? 270 LEU A N      1 
ATOM   2011 C  CA     . LEU A 1 274 ? -53.75900 -28.30800 -3.49300  1.000 38.76254 ? 270 LEU A CA     1 
ATOM   2012 C  C      . LEU A 1 274 ? -52.96500 -28.67300 -4.74200  1.000 41.85765 ? 270 LEU A C      1 
ATOM   2013 O  O      . LEU A 1 274 ? -52.85600 -27.83600 -5.64300  1.000 42.27086 ? 270 LEU A O      1 
ATOM   2014 C  CB     . LEU A 1 274 ? -52.87100 -27.46100 -2.57800  1.000 33.65140 ? 270 LEU A CB     1 
ATOM   2015 C  CG     . LEU A 1 274 ? -53.60100 -26.80300 -1.40800  1.000 36.52806 ? 270 LEU A CG     1 
ATOM   2016 C  CD1    . LEU A 1 274 ? -52.64000 -25.98300 -0.57100  1.000 39.79688 ? 270 LEU A CD1    1 
ATOM   2017 C  CD2    . LEU A 1 274 ? -54.72600 -25.92500 -1.91500  1.000 38.51251 ? 270 LEU A CD2    1 
ATOM   2018 N  N      . LEU A 1 275 ? -52.39900 -29.87400 -4.82200  1.000 39.02573 ? 271 LEU A N      1 
ATOM   2019 C  CA     . LEU A 1 275 ? -51.61600 -30.26200 -5.98700  1.000 43.29730 ? 271 LEU A CA     1 
ATOM   2020 C  C      . LEU A 1 275 ? -52.34900 -31.25300 -6.87800  1.000 47.79784 ? 271 LEU A C      1 
ATOM   2021 O  O      . LEU A 1 275 ? -51.78300 -31.71300 -7.86900  1.000 49.49278 ? 271 LEU A O      1 
ATOM   2022 C  CB     . LEU A 1 275 ? -50.26300 -30.84800 -5.55300  1.000 40.49433 ? 271 LEU A CB     1 
ATOM   2023 C  CG     . LEU A 1 275 ? -49.38200 -29.94400 -4.68900  1.000 37.01760 ? 271 LEU A CG     1 
ATOM   2024 C  CD1    . LEU A 1 275 ? -48.11700 -30.66800 -4.28600  1.000 40.83384 ? 271 LEU A CD1    1 
ATOM   2025 C  CD2    . LEU A 1 275 ? -49.04900 -28.61600 -5.39000  1.000 35.79640 ? 271 LEU A CD2    1 
ATOM   2026 N  N      . SER A 1 276 ? -53.60500 -31.57200 -6.55200  1.000 51.37984 ? 272 SER A N      1 
ATOM   2027 C  CA     . SER A 1 276 ? -54.38500 -32.54700 -7.30500  1.000 54.08543 ? 272 SER A CA     1 
ATOM   2028 C  C      . SER A 1 276 ? -54.72800 -32.08000 -8.71500  1.000 54.72235 ? 272 SER A C      1 
ATOM   2029 O  O      . SER A 1 276 ? -55.08300 -32.91400 -9.55700  1.000 54.92501 ? 272 SER A O      1 
ATOM   2030 C  CB     . SER A 1 276 ? -55.68000 -32.85400 -6.55500  1.000 54.63023 ? 272 SER A CB     1 
ATOM   2031 O  OG     . SER A 1 276 ? -56.68200 -31.88400 -6.84000  1.000 56.20148 ? 272 SER A OG     1 
ATOM   2032 N  N      . GLY A 1 277 ? -54.66800 -30.78100 -8.99000  1.000 54.40916 ? 273 GLY A N      1 
ATOM   2033 C  CA     . GLY A 1 277 ? -55.16700 -30.26400 -10.24600 1.000 52.35891 ? 273 GLY A CA     1 
ATOM   2034 C  C      . GLY A 1 277 ? -56.64100 -29.93500 -10.22900 1.000 53.04057 ? 273 GLY A C      1 
ATOM   2035 O  O      . GLY A 1 277 ? -57.18400 -29.49300 -11.25300 1.000 49.79018 ? 273 GLY A O      1 
ATOM   2036 N  N      . ASP A 1 278 ? -57.31700 -30.16700 -9.11000  1.000 48.22157 ? 274 ASP A N      1 
ATOM   2037 C  CA     . ASP A 1 278 ? -58.74800 -29.92500 -9.03100  1.000 54.98291 ? 274 ASP A CA     1 
ATOM   2038 C  C      . ASP A 1 278 ? -59.09700 -28.57300 -8.42900  1.000 45.55809 ? 274 ASP A C      1 
ATOM   2039 O  O      . ASP A 1 278 ? -60.25900 -28.15800 -8.52100  1.000 47.91101 ? 274 ASP A O      1 
ATOM   2040 C  CB     . ASP A 1 278 ? -59.42100 -31.04600 -8.24300  1.000 60.08089 ? 274 ASP A CB     1 
ATOM   2041 C  CG     . ASP A 1 278 ? -59.20600 -32.39100 -8.88900  1.000 68.10290 ? 274 ASP A CG     1 
ATOM   2042 O  OD1    . ASP A 1 278 ? -59.43800 -32.49900 -10.11700 1.000 72.05338 ? 274 ASP A OD1    1 
ATOM   2043 O  OD2    . ASP A 1 278 ? -58.77600 -33.32600 -8.18400  1.000 71.74544 ? 274 ASP A OD2    1 
ATOM   2044 N  N      . VAL A 1 279 ? -58.14100 -27.89200 -7.80100  1.000 41.68658 ? 275 VAL A N      1 
ATOM   2045 C  CA     . VAL A 1 279 ? -58.40600 -26.56300 -7.26400  1.000 37.79927 ? 275 VAL A CA     1 
ATOM   2046 C  C      . VAL A 1 279 ? -58.56500 -25.60300 -8.43500  1.000 37.13866 ? 275 VAL A C      1 
ATOM   2047 O  O      . VAL A 1 279 ? -57.68100 -25.49500 -9.29000  1.000 38.27827 ? 275 VAL A O      1 
ATOM   2048 C  CB     . VAL A 1 279 ? -57.28100 -26.10900 -6.32500  1.000 40.07059 ? 275 VAL A CB     1 
ATOM   2049 C  CG1    . VAL A 1 279 ? -57.44400 -24.64000 -6.01600  1.000 32.45126 ? 275 VAL A CG1    1 
ATOM   2050 C  CG2    . VAL A 1 279 ? -57.29500 -26.92200 -5.03100  1.000 41.66026 ? 275 VAL A CG2    1 
ATOM   2051 N  N      . ASP A 1 280 ? -59.71600 -24.93800 -8.51800  1.000 37.94929 ? 276 ASP A N      1 
ATOM   2052 C  CA     . ASP A 1 280 ? -59.91200 -23.98200 -9.60300  1.000 34.42518 ? 276 ASP A CA     1 
ATOM   2053 C  C      . ASP A 1 280 ? -59.60300 -22.54600 -9.19600  1.000 31.99594 ? 276 ASP A C      1 
ATOM   2054 O  O      . ASP A 1 280 ? -59.04400 -21.79100 -9.99900  1.000 38.75465 ? 276 ASP A O      1 
ATOM   2055 C  CB     . ASP A 1 280 ? -61.33500 -24.08500 -10.18400 1.000 34.02776 ? 276 ASP A CB     1 
ATOM   2056 C  CG     . ASP A 1 280 ? -62.43200 -24.16800 -9.12000  1.000 42.57089 ? 276 ASP A CG     1 
ATOM   2057 O  OD1    . ASP A 1 280 ? -62.12400 -24.20700 -7.90200  1.000 41.27074 ? 276 ASP A OD1    1 
ATOM   2058 O  OD2    . ASP A 1 280 ? -63.63000 -24.20700 -9.52500  1.000 45.68442 ? 276 ASP A OD2    1 
ATOM   2059 N  N      . VAL A 1 281 ? -59.92900 -22.15600 -7.96500  1.000 34.46729 ? 277 VAL A N      1 
ATOM   2060 C  CA     . VAL A 1 281 ? -59.68500 -20.81000 -7.44900  1.000 33.34610 ? 277 VAL A CA     1 
ATOM   2061 C  C      . VAL A 1 281 ? -58.87400 -20.93900 -6.16800  1.000 35.99642 ? 277 VAL A C      1 
ATOM   2062 O  O      . VAL A 1 281 ? -59.36300 -21.48500 -5.17200  1.000 36.10170 ? 277 VAL A O      1 
ATOM   2063 C  CB     . VAL A 1 281 ? -60.99500 -20.04800 -7.18700  1.000 36.91758 ? 277 VAL A CB     1 
ATOM   2064 C  CG1    . VAL A 1 281 ? -60.70300 -18.64700 -6.66000  1.000 33.67772 ? 277 VAL A CG1    1 
ATOM   2065 C  CG2    . VAL A 1 281 ? -61.84500 -19.98400 -8.46400  1.000 35.97010 ? 277 VAL A CG2    1 
ATOM   2066 N  N      . LEU A 1 282 ? -57.64300 -20.43200 -6.19100  1.000 37.90981 ? 278 LEU A N      1 
ATOM   2067 C  CA     . LEU A 1 282 ? -56.75600 -20.45800 -5.03900  1.000 31.75644 ? 278 LEU A CA     1 
ATOM   2068 C  C      . LEU A 1 282 ? -56.52800 -19.03700 -4.53700  1.000 32.64602 ? 278 LEU A C      1 
ATOM   2069 O  O      . LEU A 1 282 ? -56.11300 -18.15900 -5.30300  1.000 32.12227 ? 278 LEU A O      1 
ATOM   2070 C  CB     . LEU A 1 282 ? -55.41700 -21.12200 -5.38600  1.000 25.99522 ? 278 LEU A CB     1 
ATOM   2071 C  CG     . LEU A 1 282 ? -54.39100 -21.11300 -4.25100  1.000 25.18460 ? 278 LEU A CG     1 
ATOM   2072 C  CD1    . LEU A 1 282 ? -54.87500 -22.01400 -3.11200  1.000 25.27935 ? 278 LEU A CD1    1 
ATOM   2073 C  CD2    . LEU A 1 282 ? -53.00700 -21.53900 -4.74400  1.000 24.90562 ? 278 LEU A CD2    1 
ATOM   2074 N  N      . ILE A 1 283 ? -56.77500 -18.82200 -3.24900  1.000 34.28832 ? 279 ILE A N      1 
ATOM   2075 C  CA     . ILE A 1 283 ? -56.60200 -17.52400 -2.61100  1.000 29.49564 ? 279 ILE A CA     1 
ATOM   2076 C  C      . ILE A 1 283 ? -55.39100 -17.62900 -1.69700  1.000 29.37721 ? 279 ILE A C      1 
ATOM   2077 O  O      . ILE A 1 283 ? -55.42000 -18.35100 -0.69000  1.000 26.83480 ? 279 ILE A O      1 
ATOM   2078 C  CB     . ILE A 1 283 ? -57.85100 -17.09800 -1.82800  1.000 30.79053 ? 279 ILE A CB     1 
ATOM   2079 C  CG1    . ILE A 1 283 ? -59.07500 -17.08100 -2.74700  1.000 32.59865 ? 279 ILE A CG1    1 
ATOM   2080 C  CG2    . ILE A 1 283 ? -57.62400 -15.73400 -1.18300  1.000 25.74256 ? 279 ILE A CG2    1 
ATOM   2081 C  CD1    . ILE A 1 283 ? -60.39200 -16.87600 -2.02100  1.000 36.43068 ? 279 ILE A CD1    1 
ATOM   2082 N  N      . VAL A 1 284 ? -54.31800 -16.92300 -2.05600  1.000 24.96089 ? 280 VAL A N      1 
ATOM   2083 C  CA     . VAL A 1 284 ? -53.12000 -16.82400 -1.23400  1.000 27.75596 ? 280 VAL A CA     1 
ATOM   2084 C  C      . VAL A 1 284 ? -53.22100 -15.53600 -0.43100  1.000 25.46358 ? 280 VAL A C      1 
ATOM   2085 O  O      . VAL A 1 284 ? -53.36400 -14.45300 -1.00500  1.000 25.96627 ? 280 VAL A O      1 
ATOM   2086 C  CB     . VAL A 1 284 ? -51.84900 -16.84000 -2.10000  1.000 29.34826 ? 280 VAL A CB     1 
ATOM   2087 C  CG1    . VAL A 1 284 ? -50.58100 -16.73200 -1.22400  1.000 26.34526 ? 280 VAL A CG1    1 
ATOM   2088 C  CG2    . VAL A 1 284 ? -51.83900 -18.11400 -2.94200  1.000 28.17180 ? 280 VAL A CG2    1 
ATOM   2089 N  N      . ILE A 1 285 ? -53.16700 -15.64000 0.89300   1.000 25.73993 ? 281 ILE A N      1 
ATOM   2090 C  CA     . ILE A 1 285 ? -53.27400 -14.47300 1.76500   1.000 28.01125 ? 281 ILE A CA     1 
ATOM   2091 C  C      . ILE A 1 285 ? -51.99700 -14.38000 2.58700   1.000 25.82152 ? 281 ILE A C      1 
ATOM   2092 O  O      . ILE A 1 285 ? -51.73400 -15.24500 3.43500   1.000 24.25817 ? 281 ILE A O      1 
ATOM   2093 C  CB     . ILE A 1 285 ? -54.50300 -14.54300 2.68400   1.000 28.04020 ? 281 ILE A CB     1 
ATOM   2094 C  CG1    . ILE A 1 285 ? -55.72400 -15.03600 1.89800   1.000 37.88875 ? 281 ILE A CG1    1 
ATOM   2095 C  CG2    . ILE A 1 285 ? -54.74300 -13.18300 3.32500   1.000 28.28497 ? 281 ILE A CG2    1 
ATOM   2096 C  CD1    . ILE A 1 285 ? -57.04400 -15.03700 2.67500   1.000 34.56204 ? 281 ILE A CD1    1 
ATOM   2097 N  N      . GLY A 1 286 ? -51.21400 -13.32900 2.35200   1.000 24.11868 ? 282 GLY A N      1 
ATOM   2098 C  CA     . GLY A 1 286 ? -50.07100 -13.04800 3.20900   1.000 29.54302 ? 282 GLY A CA     1 
ATOM   2099 C  C      . GLY A 1 286 ? -49.00600 -14.12200 3.22800   1.000 26.90059 ? 282 GLY A C      1 
ATOM   2100 O  O      . GLY A 1 286 ? -48.47600 -14.44800 4.29900   1.000 26.59529 ? 282 GLY A O      1 
ATOM   2101 N  N      . SER A 1 287 ? -48.68100 -14.69000 2.07200   1.000 29.46406 ? 283 SER A N      1 
ATOM   2102 C  CA     . SER A 1 287 ? -47.52000 -15.56200 1.94500   1.000 24.15553 ? 283 SER A CA     1 
ATOM   2103 C  C      . SER A 1 287 ? -46.61400 -15.03200 0.84800   1.000 29.16402 ? 283 SER A C      1 
ATOM   2104 O  O      . SER A 1 287 ? -47.09000 -14.61700 -0.21100  1.000 27.17957 ? 283 SER A O      1 
ATOM   2105 C  CB     . SER A 1 287 ? -47.90600 -17.00100 1.62100   1.000 23.01855 ? 283 SER A CB     1 
ATOM   2106 O  OG     . SER A 1 287 ? -46.73300 -17.74500 1.32900   1.000 28.66133 ? 283 SER A OG     1 
ATOM   2107 N  N      . SER A 1 288 ? -45.30300 -15.06600 1.10100   1.000 23.60020 ? 284 SER A N      1 
ATOM   2108 C  CA     . SER A 1 288 ? -44.35400 -14.71300 0.05300   1.000 29.75094 ? 284 SER A CA     1 
ATOM   2109 C  C      . SER A 1 288 ? -44.15900 -15.81900 -0.98000  1.000 27.18747 ? 284 SER A C      1 
ATOM   2110 O  O      . SER A 1 288 ? -43.44800 -15.59600 -1.96500  1.000 26.77426 ? 284 SER A O      1 
ATOM   2111 C  CB     . SER A 1 288 ? -43.00100 -14.35400 0.66600   1.000 24.82929 ? 284 SER A CB     1 
ATOM   2112 O  OG     . SER A 1 288 ? -42.45300 -15.48200 1.32600   1.000 31.95646 ? 284 SER A OG     1 
ATOM   2113 N  N      . LEU A 1 289 ? -44.74500 -16.99800 -0.77700  1.000 20.20242 ? 285 LEU A N      1 
ATOM   2114 C  CA     . LEU A 1 289 ? -44.65600 -18.10200 -1.73500  1.000 21.39467 ? 285 LEU A CA     1 
ATOM   2115 C  C      . LEU A 1 289 ? -43.20200 -18.44400 -2.06200  1.000 27.18221 ? 285 LEU A C      1 
ATOM   2116 O  O      . LEU A 1 289 ? -42.81900 -18.62800 -3.22300  1.000 26.02154 ? 285 LEU A O      1 
ATOM   2117 C  CB     . LEU A 1 289 ? -45.45400 -17.78800 -3.00300  1.000 26.07418 ? 285 LEU A CB     1 
ATOM   2118 C  CG     . LEU A 1 289 ? -46.97500 -17.70700 -2.76000  1.000 24.42661 ? 285 LEU A CG     1 
ATOM   2119 C  CD1    . LEU A 1 289 ? -47.77400 -17.38300 -4.04300  1.000 26.18735 ? 285 LEU A CD1    1 
ATOM   2120 C  CD2    . LEU A 1 289 ? -47.47500 -19.01400 -2.18000  1.000 22.91591 ? 285 LEU A CD2    1 
ATOM   2121 N  N      . GLY A 1 290 ? -42.38100 -18.53300 -1.01200  1.000 24.60558 ? 286 GLY A N      1 
ATOM   2122 C  CA     . GLY A 1 290 ? -41.02200 -19.01900 -1.14700  1.000 20.34981 ? 286 GLY A CA     1 
ATOM   2123 C  C      . GLY A 1 290 ? -40.97700 -20.53600 -1.29400  1.000 25.67676 ? 286 GLY A C      1 
ATOM   2124 O  O      . GLY A 1 290 ? -41.98400 -21.20900 -1.51200  1.000 25.78467 ? 286 GLY A O      1 
ATOM   2125 N  N      . ASP A 1 291 ? -39.76600 -21.07300 -1.13200  1.000 26.92428 ? 287 ASP A N      1 
ATOM   2126 C  CA     . ASP A 1 291 ? -39.47100 -22.47800 -1.43300  1.000 28.34024 ? 287 ASP A CA     1 
ATOM   2127 C  C      . ASP A 1 291 ? -40.30000 -23.43600 -0.57800  1.000 24.57137 ? 287 ASP A C      1 
ATOM   2128 O  O      . ASP A 1 291 ? -41.01900 -24.30200 -1.09100  1.000 26.75584 ? 287 ASP A O      1 
ATOM   2129 C  CB     . ASP A 1 291 ? -37.97500 -22.71300 -1.21200  1.000 31.59589 ? 287 ASP A CB     1 
ATOM   2130 C  CG     . ASP A 1 291 ? -37.54100 -24.12400 -1.54500  1.000 39.71002 ? 287 ASP A CG     1 
ATOM   2131 O  OD1    . ASP A 1 291 ? -38.38500 -24.99200 -1.85900  1.000 37.24657 ? 287 ASP A OD1    1 
ATOM   2132 O  OD2    . ASP A 1 291 ? -36.32100 -24.36300 -1.49600  1.000 42.29718 ? 287 ASP A OD2    1 
ATOM   2133 N  N      . TRP A 1 292 ? -40.17800 -23.31900 0.73500   1.000 26.39001 ? 288 TRP A N      1 
ATOM   2134 C  CA     . TRP A 1 292 ? -40.86900 -24.24900 1.61900   1.000 24.65822 ? 288 TRP A CA     1 
ATOM   2135 C  C      . TRP A 1 292 ? -42.38000 -24.07600 1.55100   1.000 29.62987 ? 288 TRP A C      1 
ATOM   2136 O  O      . TRP A 1 292 ? -43.11800 -25.03600 1.80100   1.000 29.41668 ? 288 TRP A O      1 
ATOM   2137 C  CB     . TRP A 1 292 ? -40.36400 -24.05700 3.04300   1.000 29.27456 ? 288 TRP A CB     1 
ATOM   2138 C  CG     . TRP A 1 292 ? -39.08900 -24.77500 3.28300   1.000 35.12263 ? 288 TRP A CG     1 
ATOM   2139 C  CD1    . TRP A 1 292 ? -38.35900 -25.47000 2.36600   1.000 40.31273 ? 288 TRP A CD1    1 
ATOM   2140 C  CD2    . TRP A 1 292 ? -38.39800 -24.89900 4.52300   1.000 34.39886 ? 288 TRP A CD2    1 
ATOM   2141 N  NE1    . TRP A 1 292 ? -37.24800 -26.01000 2.95600   1.000 37.35974 ? 288 TRP A NE1    1 
ATOM   2142 C  CE2    . TRP A 1 292 ? -37.24900 -25.67700 4.28400   1.000 37.04128 ? 288 TRP A CE2    1 
ATOM   2143 C  CE3    . TRP A 1 292 ? -38.64300 -24.43400 5.82000   1.000 39.28366 ? 288 TRP A CE3    1 
ATOM   2144 C  CZ2    . TRP A 1 292 ? -36.33100 -25.99400 5.29500   1.000 41.78133 ? 288 TRP A CZ2    1 
ATOM   2145 C  CZ3    . TRP A 1 292 ? -37.73000 -24.74800 6.82500   1.000 44.47375 ? 288 TRP A CZ3    1 
ATOM   2146 C  CH2    . TRP A 1 292 ? -36.58900 -25.51900 6.55500   1.000 36.23856 ? 288 TRP A CH2    1 
ATOM   2147 N  N      . GLN A 1 293 ? -42.85400 -22.87400 1.21200   1.000 28.57711 ? 289 GLN A N      1 
ATOM   2148 C  CA     . GLN A 1 293 ? -44.28500 -22.61600 1.08000   1.000 28.00599 ? 289 GLN A CA     1 
ATOM   2149 C  C      . GLN A 1 293 ? -44.88600 -23.24300 -0.17000  1.000 28.62975 ? 289 GLN A C      1 
ATOM   2150 O  O      . GLN A 1 293 ? -46.10800 -23.36700 -0.25100  1.000 29.66408 ? 289 GLN A O      1 
ATOM   2151 C  CB     . GLN A 1 293 ? -44.55700 -21.10200 1.03500   1.000 22.34478 ? 289 GLN A CB     1 
ATOM   2152 C  CG     . GLN A 1 293 ? -44.01900 -20.30200 2.23700   1.000 24.95826 ? 289 GLN A CG     1 
ATOM   2153 C  CD     . GLN A 1 293 ? -42.62400 -19.74600 1.98700   1.000 31.84066 ? 289 GLN A CD     1 
ATOM   2154 O  OE1    . GLN A 1 293 ? -41.72000 -20.47300 1.59100   1.000 33.67509 ? 289 GLN A OE1    1 
ATOM   2155 N  NE2    . GLN A 1 293 ? -42.44600 -18.45000 2.22700   1.000 23.18699 ? 289 GLN A NE2    1 
ATOM   2156 N  N      . THR A 1 294 ? -44.07000 -23.67200 -1.13100  1.000 31.76697 ? 290 THR A N      1 
ATOM   2157 C  CA     . THR A 1 294 ? -44.59700 -24.05900 -2.43600  1.000 26.84006 ? 290 THR A CA     1 
ATOM   2158 C  C      . THR A 1 294 ? -44.05500 -25.39400 -2.92200  1.000 30.81948 ? 290 THR A C      1 
ATOM   2159 O  O      . THR A 1 294 ? -44.24500 -25.73200 -4.10300  1.000 28.67186 ? 290 THR A O      1 
ATOM   2160 C  CB     . THR A 1 294 ? -44.28200 -22.97200 -3.47400  1.000 28.15864 ? 290 THR A CB     1 
ATOM   2161 O  OG1    . THR A 1 294 ? -42.85100 -22.79500 -3.56300  1.000 28.05073 ? 290 THR A OG1    1 
ATOM   2162 C  CG2    . THR A 1 294 ? -44.92900 -21.66300 -3.05300  1.000 25.47674 ? 290 THR A CG2    1 
ATOM   2163 N  N      . ASN A 1 295 ? -43.40400 -26.15600 -2.04300  1.000 36.45963 ? 291 ASN A N      1 
ATOM   2164 C  CA     . ASN A 1 295 ? -42.64500 -27.34900 -2.41100  1.000 41.66289 ? 291 ASN A CA     1 
ATOM   2165 C  C      . ASN A 1 295 ? -41.73700 -27.08000 -3.61400  1.000 33.18819 ? 291 ASN A C      1 
ATOM   2166 O  O      . ASN A 1 295 ? -41.85700 -27.70000 -4.67500  1.000 34.66731 ? 291 ASN A O      1 
ATOM   2167 C  CB     . ASN A 1 295 ? -43.58900 -28.52600 -2.66000  1.000 49.23485 ? 291 ASN A CB     1 
ATOM   2168 C  CG     . ASN A 1 295 ? -42.84500 -29.83100 -2.88400  1.000 63.54972 ? 291 ASN A CG     1 
ATOM   2169 O  OD1    . ASN A 1 295 ? -42.00700 -30.23500 -2.08000  1.000 68.66086 ? 291 ASN A OD1    1 
ATOM   2170 N  ND2    . ASN A 1 295 ? -43.16400 -30.50800 -3.98700  1.000 67.32913 ? 291 ASN A ND2    1 
ATOM   2171 N  N      . SER A 1 296 ? -40.80100 -26.14900 -3.42200  1.000 29.00085 ? 292 SER A N      1 
ATOM   2172 C  CA     . SER A 1 296 ? -39.88100 -25.67300 -4.46200  1.000 38.50988 ? 292 SER A CA     1 
ATOM   2173 C  C      . SER A 1 296 ? -40.61600 -25.25100 -5.73600  1.000 37.62820 ? 292 SER A C      1 
ATOM   2174 O  O      . SER A 1 296 ? -40.28300 -25.67200 -6.84200  1.000 31.16689 ? 292 SER A O      1 
ATOM   2175 C  CB     . SER A 1 296 ? -38.82200 -26.73100 -4.79400  1.000 37.95718 ? 292 SER A CB     1 
ATOM   2176 O  OG     . SER A 1 296 ? -38.19000 -27.19700 -3.62000  1.000 42.37613 ? 292 SER A OG     1 
ATOM   2177 N  N      . TRP A 1 297 ? -41.57800 -24.34600 -5.56400  1.000 32.84341 ? 293 TRP A N      1 
ATOM   2178 C  CA     . TRP A 1 297 ? -42.28200 -23.71200 -6.68500  1.000 33.24346 ? 293 TRP A CA     1 
ATOM   2179 C  C      . TRP A 1 297 ? -42.88600 -24.75700 -7.61200  1.000 32.19597 ? 293 TRP A C      1 
ATOM   2180 O  O      . TRP A 1 297 ? -42.81700 -24.66600 -8.83900  1.000 32.45389 ? 293 TRP A O      1 
ATOM   2181 C  CB     . TRP A 1 297 ? -41.34700 -22.75200 -7.42200  1.000 32.48021 ? 293 TRP A CB     1 
ATOM   2182 C  CG     . TRP A 1 297 ? -40.71400 -21.83500 -6.41000  1.000 29.24824 ? 293 TRP A CG     1 
ATOM   2183 C  CD1    . TRP A 1 297 ? -41.32500 -20.80900 -5.75100  1.000 26.94797 ? 293 TRP A CD1    1 
ATOM   2184 C  CD2    . TRP A 1 297 ? -39.37700 -21.91100 -5.88300  1.000 25.53990 ? 293 TRP A CD2    1 
ATOM   2185 N  NE1    . TRP A 1 297 ? -40.45000 -20.22800 -4.86100  1.000 28.67449 ? 293 TRP A NE1    1 
ATOM   2186 C  CE2    . TRP A 1 297 ? -39.24900 -20.88600 -4.92300  1.000 27.55067 ? 293 TRP A CE2    1 
ATOM   2187 C  CE3    . TRP A 1 297 ? -38.27500 -22.73700 -6.14200  1.000 31.85908 ? 293 TRP A CE3    1 
ATOM   2188 C  CZ2    . TRP A 1 297 ? -38.05500 -20.65700 -4.21700  1.000 26.75584 ? 293 TRP A CZ2    1 
ATOM   2189 C  CZ3    . TRP A 1 297 ? -37.09600 -22.51500 -5.44300  1.000 28.78766 ? 293 TRP A CZ3    1 
ATOM   2190 C  CH2    . TRP A 1 297 ? -36.99600 -21.47900 -4.49300  1.000 27.96125 ? 293 TRP A CH2    1 
ATOM   2191 N  N      . ASP A 1 298 ? -43.53500 -25.73500 -6.99400  1.000 33.11186 ? 294 ASP A N      1 
ATOM   2192 C  CA     . ASP A 1 298 ? -44.22600 -26.78100 -7.71600  1.000 34.65679 ? 294 ASP A CA     1 
ATOM   2193 C  C      . ASP A 1 298 ? -45.26000 -26.16200 -8.65300  1.000 36.00695 ? 294 ASP A C      1 
ATOM   2194 O  O      . ASP A 1 298 ? -46.11000 -25.38200 -8.19800  1.000 38.23616 ? 294 ASP A O      1 
ATOM   2195 C  CB     . ASP A 1 298 ? -44.89000 -27.73500 -6.72700  1.000 35.31739 ? 294 ASP A CB     1 
ATOM   2196 C  CG     . ASP A 1 298 ? -45.32000 -29.04200 -7.37100  1.000 41.67079 ? 294 ASP A CG     1 
ATOM   2197 O  OD1    . ASP A 1 298 ? -45.72200 -29.01900 -8.55700  1.000 39.43368 ? 294 ASP A OD1    1 
ATOM   2198 O  OD2    . ASP A 1 298 ? -45.27000 -30.08400 -6.68200  1.000 43.34204 ? 294 ASP A OD2    1 
ATOM   2199 N  N      . PRO A 1 299 ? -45.20100 -26.44000 -9.95600  1.000 38.48356 ? 295 PRO A N      1 
ATOM   2200 C  CA     . PRO A 1 299 ? -46.20300 -25.87000 -10.86800 1.000 34.30938 ? 295 PRO A CA     1 
ATOM   2201 C  C      . PRO A 1 299 ? -47.60200 -26.38900 -10.61900 1.000 40.99176 ? 295 PRO A C      1 
ATOM   2202 O  O      . PRO A 1 299 ? -48.56900 -25.71600 -10.99600 1.000 43.76051 ? 295 PRO A O      1 
ATOM   2203 C  CB     . PRO A 1 299 ? -45.69400 -26.28500 -12.26000 1.000 34.41202 ? 295 PRO A CB     1 
ATOM   2204 C  CG     . PRO A 1 299 ? -44.82100 -27.48100 -12.00600 1.000 38.46777 ? 295 PRO A CG     1 
ATOM   2205 C  CD     . PRO A 1 299 ? -44.15400 -27.18700 -10.67700 1.000 39.38367 ? 295 PRO A CD     1 
ATOM   2206 N  N      . ARG A 1 300 ? -47.74600 -27.56600 -10.01100 1.000 36.40700 ? 296 ARG A N      1 
ATOM   2207 C  CA     . ARG A 1 300 ? -49.07400 -28.09300 -9.73500  1.000 33.26715 ? 296 ARG A CA     1 
ATOM   2208 C  C      . ARG A 1 300 ? -49.84100 -27.23700 -8.74300  1.000 37.53345 ? 296 ARG A C      1 
ATOM   2209 O  O      . ARG A 1 300 ? -51.05000 -27.40600 -8.61100  1.000 36.21750 ? 296 ARG A O      1 
ATOM   2210 C  CB     . ARG A 1 300 ? -48.97000 -29.52800 -9.23100  1.000 33.19082 ? 296 ARG A CB     1 
ATOM   2211 C  CG     . ARG A 1 300 ? -48.64200 -30.51400 -10.33300 1.000 38.14931 ? 296 ARG A CG     1 
ATOM   2212 C  CD     . ARG A 1 300 ? -48.38800 -31.87400 -9.75000  1.000 39.98374 ? 296 ARG A CD     1 
ATOM   2213 N  NE     . ARG A 1 300 ? -47.33200 -31.78300 -8.75400  1.000 50.45342 ? 296 ARG A NE     1 
ATOM   2214 C  CZ     . ARG A 1 300 ? -47.06200 -32.73400 -7.87300  1.000 48.69531 ? 296 ARG A CZ     1 
ATOM   2215 N  NH1    . ARG A 1 300 ? -47.78400 -33.85100 -7.87700  1.000 44.28689 ? 296 ARG A NH1    1 
ATOM   2216 N  NH2    . ARG A 1 300 ? -46.07900 -32.56600 -6.99100  1.000 38.30986 ? 296 ARG A NH2    1 
ATOM   2217 N  N      . LEU A 1 301 ? -49.16800 -26.34200 -8.01200  1.000 34.91998 ? 297 LEU A N      1 
ATOM   2218 C  CA     . LEU A 1 301 ? -49.91000 -25.42500 -7.15200  1.000 35.06473 ? 297 LEU A CA     1 
ATOM   2219 C  C      . LEU A 1 301 ? -50.79500 -24.47100 -7.96900  1.000 36.60965 ? 297 LEU A C      1 
ATOM   2220 O  O      . LEU A 1 301 ? -51.77900 -23.93600 -7.45000  1.000 37.70452 ? 297 LEU A O      1 
ATOM   2221 C  CB     . LEU A 1 301 ? -48.93100 -24.66400 -6.25100  1.000 29.47195 ? 297 LEU A CB     1 
ATOM   2222 C  CG     . LEU A 1 301 ? -49.49300 -23.79900 -5.12800  1.000 36.38068 ? 297 LEU A CG     1 
ATOM   2223 C  CD1    . LEU A 1 301 ? -50.34800 -24.62000 -4.16500  1.000 32.36704 ? 297 LEU A CD1    1 
ATOM   2224 C  CD2    . LEU A 1 301 ? -48.35700 -23.09800 -4.38800  1.000 35.30160 ? 297 LEU A CD2    1 
ATOM   2225 N  N      . THR A 1 302 ? -50.45400 -24.22700 -9.23100  1.000 38.27827 ? 298 THR A N      1 
ATOM   2226 C  CA     . THR A 1 302 ? -51.23100 -23.31300 -10.06700 1.000 35.09368 ? 298 THR A CA     1 
ATOM   2227 C  C      . THR A 1 302 ? -52.68800 -23.75900 -10.14700 1.000 36.73862 ? 298 THR A C      1 
ATOM   2228 O  O      . THR A 1 302 ? -52.95900 -24.91700 -10.49800 1.000 35.29634 ? 298 THR A O      1 
ATOM   2229 C  CB     . THR A 1 302 ? -50.62700 -23.24400 -11.46700 1.000 34.17515 ? 298 THR A CB     1 
ATOM   2230 O  OG1    . THR A 1 302 ? -49.25600 -22.84500 -11.36400 1.000 37.92034 ? 298 THR A OG1    1 
ATOM   2231 C  CG2    . THR A 1 302 ? -51.38300 -22.25100 -12.34800 1.000 36.80441 ? 298 THR A CG2    1 
ATOM   2232 N  N      . PRO A 1 303 ? -53.64300 -22.88800 -9.83600  1.000 41.80501 ? 299 PRO A N      1 
ATOM   2233 C  CA     . PRO A 1 303 ? -55.05700 -23.25500 -9.96200  1.000 41.16283 ? 299 PRO A CA     1 
ATOM   2234 C  C      . PRO A 1 303 ? -55.49200 -23.20600 -11.41600 1.000 43.96843 ? 299 PRO A C      1 
ATOM   2235 O  O      . PRO A 1 303 ? -54.85200 -22.57300 -12.25700 1.000 32.43810 ? 299 PRO A O      1 
ATOM   2236 C  CB     . PRO A 1 303 ? -55.77700 -22.18100 -9.14100  1.000 40.53118 ? 299 PRO A CB     1 
ATOM   2237 C  CG     . PRO A 1 303 ? -54.86800 -20.97900 -9.25700  1.000 38.82571 ? 299 PRO A CG     1 
ATOM   2238 C  CD     . PRO A 1 303 ? -53.45900 -21.51900 -9.31900  1.000 35.92799 ? 299 PRO A CD     1 
ATOM   2239 N  N      . SER A 1 304 ? -56.61400 -23.88500 -11.70600 1.000 41.17073 ? 300 SER A N      1 
ATOM   2240 C  CA     . SER A 1 304 ? -57.02200 -24.02100 -13.09800 1.000 41.37075 ? 300 SER A CA     1 
ATOM   2241 C  C      . SER A 1 304 ? -57.82500 -22.83100 -13.60100 1.000 43.19465 ? 300 SER A C      1 
ATOM   2242 O  O      . SER A 1 304 ? -57.93100 -22.65200 -14.81900 1.000 46.13974 ? 300 SER A O      1 
ATOM   2243 C  CB     . SER A 1 304 ? -57.82900 -25.30500 -13.31900 1.000 31.78539 ? 300 SER A CB     1 
ATOM   2244 O  OG     . SER A 1 304 ? -59.03600 -25.28100 -12.58600 1.000 33.61456 ? 300 SER A OG     1 
ATOM   2245 N  N      . VAL A 1 305 ? -58.36600 -21.99800 -12.71300 1.000 36.45963 ? 301 VAL A N      1 
ATOM   2246 C  CA     . VAL A 1 305 ? -59.19300 -20.87900 -13.15900 1.000 33.99881 ? 301 VAL A CA     1 
ATOM   2247 C  C      . VAL A 1 305 ? -58.57000 -19.55500 -12.72000 1.000 36.10433 ? 301 VAL A C      1 
ATOM   2248 O  O      . VAL A 1 305 ? -58.32700 -18.67400 -13.54700 1.000 40.35747 ? 301 VAL A O      1 
ATOM   2249 C  CB     . VAL A 1 305 ? -60.64500 -20.99800 -12.64700 1.000 37.00707 ? 301 VAL A CB     1 
ATOM   2250 C  CG1    . VAL A 1 305 ? -61.38700 -19.68600 -12.84800 1.000 34.82786 ? 301 VAL A CG1    1 
ATOM   2251 C  CG2    . VAL A 1 305 ? -61.39400 -22.13400 -13.36600 1.000 35.20685 ? 301 VAL A CG2    1 
ATOM   2252 N  N      . ALA A 1 306 ? -58.33100 -19.37700 -11.42400 1.000 34.58046 ? 302 ALA A N      1 
ATOM   2253 C  CA     . ALA A 1 306 ? -57.83800 -18.08300 -10.97100 1.000 33.66983 ? 302 ALA A CA     1 
ATOM   2254 C  C      . ALA A 1 306 ? -56.97700 -18.24200 -9.73000  1.000 32.00384 ? 302 ALA A C      1 
ATOM   2255 O  O      . ALA A 1 306 ? -57.35100 -18.96300 -8.80000  1.000 34.28043 ? 302 ALA A O      1 
ATOM   2256 C  CB     . ALA A 1 306 ? -58.99100 -17.11800 -10.69000 1.000 34.17252 ? 302 ALA A CB     1 
ATOM   2257 N  N      . LEU A 1 307 ? -55.82100 -17.57400 -9.73900  1.000 29.12718 ? 303 LEU A N      1 
ATOM   2258 C  CA     . LEU A 1 307 ? -54.99700 -17.35600 -8.55800  1.000 26.43212 ? 303 LEU A CA     1 
ATOM   2259 C  C      . LEU A 1 307 ? -55.21600 -15.92400 -8.07700  1.000 31.59589 ? 303 LEU A C      1 
ATOM   2260 O  O      . LEU A 1 307 ? -55.05500 -14.96800 -8.84900  1.000 32.38809 ? 303 LEU A O      1 
ATOM   2261 C  CB     . LEU A 1 307 ? -53.51900 -17.60700 -8.85600  1.000 27.31380 ? 303 LEU A CB     1 
ATOM   2262 C  CG     . LEU A 1 307 ? -52.56500 -17.29100 -7.69500  1.000 37.17288 ? 303 LEU A CG     1 
ATOM   2263 C  CD1    . LEU A 1 307 ? -52.84000 -18.19600 -6.50300  1.000 28.70344 ? 303 LEU A CD1    1 
ATOM   2264 C  CD2    . LEU A 1 307 ? -51.09700 -17.37000 -8.12100  1.000 37.96245 ? 303 LEU A CD2    1 
ATOM   2265 N  N      . ILE A 1 308 ? -55.64300 -15.79000 -6.82700  1.000 30.69315 ? 304 ILE A N      1 
ATOM   2266 C  CA     . ILE A 1 308 ? -55.85000 -14.51600 -6.15600  1.000 24.99510 ? 304 ILE A CA     1 
ATOM   2267 C  C      . ILE A 1 308 ? -54.76700 -14.39300 -5.09400  1.000 24.20290 ? 304 ILE A C      1 
ATOM   2268 O  O      . ILE A 1 308 ? -54.57300 -15.31900 -4.29800  1.000 28.34287 ? 304 ILE A O      1 
ATOM   2269 C  CB     . ILE A 1 308 ? -57.25300 -14.46100 -5.51700  1.000 25.42410 ? 304 ILE A CB     1 
ATOM   2270 C  CG1    . ILE A 1 308 ? -58.32900 -14.67000 -6.57700  1.000 27.35328 ? 304 ILE A CG1    1 
ATOM   2271 C  CG2    . ILE A 1 308 ? -57.47100 -13.16000 -4.74100  1.000 25.49516 ? 304 ILE A CG2    1 
ATOM   2272 C  CD1    . ILE A 1 308 ? -59.65700 -15.15000 -6.00400  1.000 30.16414 ? 304 ILE A CD1    1 
ATOM   2273 N  N      . GLN A 1 309 ? -54.04500 -13.27400 -5.07900  1.000 23.70547 ? 305 GLN A N      1 
ATOM   2274 C  CA     . GLN A 1 309 ? -53.01100 -13.08700 -4.06900  1.000 24.35292 ? 305 GLN A CA     1 
ATOM   2275 C  C      . GLN A 1 309 ? -53.20200 -11.75900 -3.35000  1.000 30.52208 ? 305 GLN A C      1 
ATOM   2276 O  O      . GLN A 1 309 ? -53.30800 -10.70200 -3.99000  1.000 28.62712 ? 305 GLN A O      1 
ATOM   2277 C  CB     . GLN A 1 309 ? -51.60900 -13.15400 -4.66100  1.000 26.37158 ? 305 GLN A CB     1 
ATOM   2278 C  CG     . GLN A 1 309 ? -50.54600 -13.04100 -3.56400  1.000 21.83946 ? 305 GLN A CG     1 
ATOM   2279 C  CD     . GLN A 1 309 ? -49.16400 -13.29700 -4.08900  1.000 34.04882 ? 305 GLN A CD     1 
ATOM   2280 O  OE1    . GLN A 1 309 ? -48.93600 -13.26900 -5.30700  1.000 32.06700 ? 305 GLN A OE1    1 
ATOM   2281 N  NE2    . GLN A 1 309 ? -48.22100 -13.54900 -3.18200  1.000 30.34048 ? 305 GLN A NE2    1 
ATOM   2282 N  N      . ILE A 1 310 ? -53.26400 -11.82100 -2.02300  1.000 26.86375 ? 306 ILE A N      1 
ATOM   2283 C  CA     . ILE A 1 310 ? -53.47800 -10.65200 -1.17800  1.000 25.85047 ? 306 ILE A CA     1 
ATOM   2284 C  C      . ILE A 1 310 ? -52.21200 -10.41300 -0.37500  1.000 26.94270 ? 306 ILE A C      1 
ATOM   2285 O  O      . ILE A 1 310 ? -51.76700 -11.28900 0.38100   1.000 25.80573 ? 306 ILE A O      1 
ATOM   2286 C  CB     . ILE A 1 310 ? -54.69200 -10.83500 -0.25800  1.000 30.90107 ? 306 ILE A CB     1 
ATOM   2287 C  CG1    . ILE A 1 310 ? -55.96400 -10.96600 -1.10100  1.000 31.85908 ? 306 ILE A CG1    1 
ATOM   2288 C  CG2    . ILE A 1 310 ? -54.79400 -9.67300  0.74900   1.000 24.87403 ? 306 ILE A CG2    1 
ATOM   2289 C  CD1    . ILE A 1 310 ? -56.98600 -11.91800 -0.49600  1.000 27.76912 ? 306 ILE A CD1    1 
ATOM   2290 N  N      . ASP A 1 311 ? -51.63100 -9.23300  -0.52300  1.000 24.39503 ? 307 ASP A N      1 
ATOM   2291 C  CA     . ASP A 1 311 ? -50.37400 -8.97000  0.16900   1.000 24.07657 ? 307 ASP A CA     1 
ATOM   2292 C  C      . ASP A 1 311 ? -50.20800 -7.47800  0.39700   1.000 23.82654 ? 307 ASP A C      1 
ATOM   2293 O  O      . ASP A 1 311 ? -50.53600 -6.67800  -0.48100  1.000 27.45329 ? 307 ASP A O      1 
ATOM   2294 C  CB     . ASP A 1 311 ? -49.19100 -9.50200  -0.63800  1.000 23.68968 ? 307 ASP A CB     1 
ATOM   2295 C  CG     . ASP A 1 311 ? -48.03100 -9.90700  0.24800   1.000 39.08627 ? 307 ASP A CG     1 
ATOM   2296 O  OD1    . ASP A 1 311 ? -47.30500 -9.01000  0.74200   1.000 28.73239 ? 307 ASP A OD1    1 
ATOM   2297 O  OD2    . ASP A 1 311 ? -47.88900 -11.12700 0.47400   1.000 34.82260 ? 307 ASP A OD2    1 
ATOM   2298 N  N      . ILE A 1 312 ? -49.70200 -7.10200  1.57300   1.000 22.56323 ? 308 ILE A N      1 
ATOM   2299 C  CA     . ILE A 1 312 ? -49.46500 -5.68500  1.81700   1.000 28.27707 ? 308 ILE A CA     1 
ATOM   2300 C  C      . ILE A 1 312 ? -48.24700 -5.17300  1.05000   1.000 27.01640 ? 308 ILE A C      1 
ATOM   2301 O  O      . ILE A 1 312 ? -48.07600 -3.95700  0.89000   1.000 24.77139 ? 308 ILE A O      1 
ATOM   2302 C  CB     . ILE A 1 312 ? -49.29000 -5.42100  3.32700   1.000 30.76948 ? 308 ILE A CB     1 
ATOM   2303 C  CG1    . ILE A 1 312 ? -49.57600 -3.94600  3.65400   1.000 24.57663 ? 308 ILE A CG1    1 
ATOM   2304 C  CG2    . ILE A 1 312 ? -47.88500 -5.84300  3.78700   1.000 24.99773 ? 308 ILE A CG2    1 
ATOM   2305 C  CD1    . ILE A 1 312 ? -50.04900 -3.75700  5.10700   1.000 23.43965 ? 308 ILE A CD1    1 
ATOM   2306 N  N      . ASP A 1 313 ? -47.38700 -6.07100  0.58600   1.000 27.20853 ? 309 ASP A N      1 
ATOM   2307 C  CA     . ASP A 1 313 ? -46.16500 -5.68800  -0.10500  1.000 27.00587 ? 309 ASP A CA     1 
ATOM   2308 C  C      . ASP A 1 313 ? -46.39200 -5.86800  -1.59800  1.000 26.91375 ? 309 ASP A C      1 
ATOM   2309 O  O      . ASP A 1 313 ? -46.47200 -7.01300  -2.06800  1.000 30.70895 ? 309 ASP A O      1 
ATOM   2310 C  CB     . ASP A 1 313 ? -44.98900 -6.54800  0.37000   1.000 18.85226 ? 309 ASP A CB     1 
ATOM   2311 C  CG     . ASP A 1 313 ? -43.68800 -6.25100  -0.37800  1.000 23.50545 ? 309 ASP A CG     1 
ATOM   2312 O  OD1    . ASP A 1 313 ? -43.69500 -5.44300  -1.33500  1.000 27.88229 ? 309 ASP A OD1    1 
ATOM   2313 O  OD2    . ASP A 1 313 ? -42.63600 -6.82600  -0.00400  1.000 27.11378 ? 309 ASP A OD2    1 
ATOM   2314 N  N      . PRO A 1 314 ? -46.48200 -4.79600  -2.38200  1.000 27.80070 ? 310 PRO A N      1 
ATOM   2315 C  CA     . PRO A 1 314 ? -46.80300 -4.96800  -3.80800  1.000 26.51897 ? 310 PRO A CA     1 
ATOM   2316 C  C      . PRO A 1 314 ? -45.73000 -5.71500  -4.57400  1.000 28.99558 ? 310 PRO A C      1 
ATOM   2317 O  O      . PRO A 1 314 ? -46.04000 -6.28800  -5.62700  1.000 29.93517 ? 310 PRO A O      1 
ATOM   2318 C  CB     . PRO A 1 314 ? -46.95300 -3.53100  -4.31300  1.000 28.35866 ? 310 PRO A CB     1 
ATOM   2319 C  CG     . PRO A 1 314 ? -46.10600 -2.71200  -3.37800  1.000 23.18173 ? 310 PRO A CG     1 
ATOM   2320 C  CD     . PRO A 1 314 ? -46.13200 -3.40800  -2.03800  1.000 23.66600 ? 310 PRO A CD     1 
ATOM   2321 N  N      . MET A 1 315 ? -44.48800 -5.74900  -4.06800  1.000 19.73131 ? 311 MET A N      1 
ATOM   2322 C  CA     . MET A 1 315 ? -43.40100 -6.43900  -4.76000  1.000 23.15278 ? 311 MET A CA     1 
ATOM   2323 C  C      . MET A 1 315 ? -43.49200 -7.95600  -4.66800  1.000 29.54038 ? 311 MET A C      1 
ATOM   2324 O  O      . MET A 1 315 ? -42.77100 -8.63900  -5.40200  1.000 33.49875 ? 311 MET A O      1 
ATOM   2325 C  CB     . MET A 1 315 ? -42.04400 -5.98900  -4.21100  1.000 22.82379 ? 311 MET A CB     1 
ATOM   2326 C  CG     . MET A 1 315 ? -41.80200 -4.48300  -4.28900  1.000 32.18281 ? 311 MET A CG     1 
ATOM   2327 S  SD     . MET A 1 315 ? -42.53600 -3.72700  -5.76400  1.000 42.72091 ? 311 MET A SD     1 
ATOM   2328 C  CE     . MET A 1 315 ? -42.45200 -1.99900  -5.28500  1.000 47.70835 ? 311 MET A CE     1 
ATOM   2329 N  N      . GLU A 1 316 ? -44.31800 -8.49800  -3.77000  1.000 28.33761 ? 312 GLU A N      1 
ATOM   2330 C  CA     . GLU A 1 316 ? -44.52000 -9.94100  -3.67600  1.000 29.15350 ? 312 GLU A CA     1 
ATOM   2331 C  C      . GLU A 1 316 ? -45.58500 -10.45800 -4.63100  1.000 31.24059 ? 312 GLU A C      1 
ATOM   2332 O  O      . GLU A 1 316 ? -45.65100 -11.67400 -4.86500  1.000 32.60128 ? 312 GLU A O      1 
ATOM   2333 C  CB     . GLU A 1 316 ? -44.92900 -10.34800 -2.25000  1.000 30.52471 ? 312 GLU A CB     1 
ATOM   2334 C  CG     . GLU A 1 316 ? -43.83100 -10.19600 -1.21100  1.000 33.63035 ? 312 GLU A CG     1 
ATOM   2335 C  CD     . GLU A 1 316 ? -42.65700 -11.14100 -1.43500  1.000 38.95730 ? 312 GLU A CD     1 
ATOM   2336 O  OE1    . GLU A 1 316 ? -41.58500 -10.91300 -0.84700  1.000 37.14919 ? 312 GLU A OE1    1 
ATOM   2337 O  OE2    . GLU A 1 316 ? -42.79900 -12.12200 -2.19300  1.000 39.97058 ? 312 GLU A OE2    1 
ATOM   2338 N  N      . ILE A 1 317 ? -46.43900 -9.58500  -5.16300  1.000 26.62951 ? 313 ILE A N      1 
ATOM   2339 C  CA     . ILE A 1 317 ? -47.61500 -10.03600 -5.89500  1.000 30.64841 ? 313 ILE A CA     1 
ATOM   2340 C  C      . ILE A 1 317 ? -47.20100 -10.49200 -7.28600  1.000 30.42470 ? 313 ILE A C      1 
ATOM   2341 O  O      . ILE A 1 317 ? -46.67300 -9.70400  -8.07500  1.000 31.12478 ? 313 ILE A O      1 
ATOM   2342 C  CB     . ILE A 1 317 ? -48.67600 -8.93400  -5.96500  1.000 34.04356 ? 313 ILE A CB     1 
ATOM   2343 C  CG1    . ILE A 1 317 ? -49.18800 -8.61100  -4.55300  1.000 33.69878 ? 313 ILE A CG1    1 
ATOM   2344 C  CG2    . ILE A 1 317 ? -49.81500 -9.36000  -6.89700  1.000 28.70081 ? 313 ILE A CG2    1 
ATOM   2345 C  CD1    . ILE A 1 317 ? -50.16900 -7.43400  -4.51400  1.000 32.07753 ? 313 ILE A CD1    1 
ATOM   2346 N  N      . GLY A 1 318 ? -47.46000 -11.76100 -7.59600  1.000 29.74304 ? 314 GLY A N      1 
ATOM   2347 C  CA     . GLY A 1 318 ? -47.09200 -12.31000 -8.88900  1.000 31.97225 ? 314 GLY A CA     1 
ATOM   2348 C  C      . GLY A 1 318 ? -45.62700 -12.63500 -9.04700  1.000 28.87715 ? 314 GLY A C      1 
ATOM   2349 O  O      . GLY A 1 318 ? -45.16000 -12.80400 -10.17700 1.000 31.96699 ? 314 GLY A O      1 
ATOM   2350 N  N      . LYS A 1 319 ? -44.88600 -12.71300 -7.97000  1.000 24.21869 ? 315 LYS A N      1 
ATOM   2351 C  CA     . LYS A 1 319 ? -43.48600 -13.01000 -8.02700  1.000 27.77701 ? 315 LYS A CA     1 
ATOM   2352 C  C      . LYS A 1 319 ? -43.11500 -14.34900 -8.64600  1.000 29.85095 ? 315 LYS A C      1 
ATOM   2353 O  O      . LYS A 1 319 ? -42.34300 -14.41900 -9.53700  1.000 32.62233 ? 315 LYS A O      1 
ATOM   2354 C  CB     . LYS A 1 319 ? -42.89300 -12.92600 -6.63000  1.000 25.57938 ? 315 LYS A CB     1 
ATOM   2355 C  CG     . LYS A 1 319 ? -41.40000 -13.04000 -6.58600  1.000 33.93828 ? 315 LYS A CG     1 
ATOM   2356 C  CD     . LYS A 1 319 ? -40.82600 -12.71700 -5.21800  1.000 31.95646 ? 315 LYS A CD     1 
ATOM   2357 C  CE     . LYS A 1 319 ? -40.70600 -13.96700 -4.41700  1.000 33.58824 ? 315 LYS A CE     1 
ATOM   2358 N  NZ     . LYS A 1 319 ? -40.81900 -13.69300 -2.99300  1.000 38.68359 ? 315 LYS A NZ     1 
ATOM   2359 N  N      . ASN A 1 320 ? -43.68800 -15.40500 -8.13900  1.000 32.30651 ? 316 ASN A N      1 
ATOM   2360 C  CA     . ASN A 1 320 ? -43.36400 -16.75600 -8.58700  1.000 31.31691 ? 316 ASN A CA     1 
ATOM   2361 C  C      . ASN A 1 320 ? -44.48200 -17.46400 -9.34200  1.000 36.12275 ? 316 ASN A C      1 
ATOM   2362 O  O      . ASN A 1 320 ? -44.19400 -18.41600 -10.07300 1.000 35.16737 ? 316 ASN A O      1 
ATOM   2363 C  CB     . ASN A 1 320 ? -42.98200 -17.62900 -7.38400  1.000 30.03781 ? 316 ASN A CB     1 
ATOM   2364 C  CG     . ASN A 1 320 ? -41.65900 -17.22500 -6.76900  1.000 30.54050 ? 316 ASN A CG     1 
ATOM   2365 O  OD1    . ASN A 1 320 ? -40.72200 -16.87400 -7.47500  1.000 25.94522 ? 316 ASN A OD1    1 
ATOM   2366 N  ND2    . ASN A 1 320 ? -41.58000 -17.27200 -5.44100  1.000 27.44803 ? 316 ASN A ND2    1 
ATOM   2367 N  N      . TYR A 1 321 ? -45.73600 -17.02800 -9.18600  1.000 23.50019 ? 317 TYR A N      1 
ATOM   2368 C  CA     . TYR A 1 321 ? -46.88500 -17.59400 -9.87900  1.000 26.76110 ? 317 TYR A CA     1 
ATOM   2369 C  C      . TYR A 1 321 ? -47.68800 -16.44300 -10.47400 1.000 32.96448 ? 317 TYR A C      1 
ATOM   2370 O  O      . TYR A 1 321 ? -47.91100 -15.43000 -9.79200  1.000 30.34574 ? 317 TYR A O      1 
ATOM   2371 C  CB     . TYR A 1 321 ? -47.77900 -18.41400 -8.93000  1.000 29.67987 ? 317 TYR A CB     1 
ATOM   2372 C  CG     . TYR A 1 321 ? -47.15600 -19.69500 -8.41900  1.000 34.34622 ? 317 TYR A CG     1 
ATOM   2373 C  CD1    . TYR A 1 321 ? -46.29800 -19.68000 -7.33200  1.000 34.07251 ? 317 TYR A CD1    1 
ATOM   2374 C  CD2    . TYR A 1 321 ? -47.44100 -20.91900 -9.01200  1.000 32.15386 ? 317 TYR A CD2    1 
ATOM   2375 C  CE1    . TYR A 1 321 ? -45.73000 -20.85100 -6.84700  1.000 33.46454 ? 317 TYR A CE1    1 
ATOM   2376 C  CE2    . TYR A 1 321 ? -46.87300 -22.09300 -8.53400  1.000 33.63035 ? 317 TYR A CE2    1 
ATOM   2377 C  CZ     . TYR A 1 321 ? -46.02200 -22.04600 -7.45100  1.000 28.54553 ? 317 TYR A CZ     1 
ATOM   2378 O  OH     . TYR A 1 321 ? -45.45700 -23.19400 -6.97400  1.000 33.71983 ? 317 TYR A OH     1 
ATOM   2379 N  N      . PRO A 1 322 ? -48.12000 -16.53500 -11.73200 1.000 32.10385 ? 318 PRO A N      1 
ATOM   2380 C  CA     . PRO A 1 322 ? -48.95100 -15.46000 -12.29500 1.000 31.12478 ? 318 PRO A CA     1 
ATOM   2381 C  C      . PRO A 1 322 ? -50.28300 -15.38600 -11.56300 1.000 30.65631 ? 318 PRO A C      1 
ATOM   2382 O  O      . PRO A 1 322 ? -50.90300 -16.40500 -11.26300 1.000 32.03542 ? 318 PRO A O      1 
ATOM   2383 C  CB     . PRO A 1 322 ? -49.13600 -15.87000 -13.76300 1.000 33.67509 ? 318 PRO A CB     1 
ATOM   2384 C  CG     . PRO A 1 322 ? -48.81600 -17.32400 -13.80600 1.000 41.34443 ? 318 PRO A CG     1 
ATOM   2385 C  CD     . PRO A 1 322 ? -47.76200 -17.54200 -12.74000 1.000 38.49146 ? 318 PRO A CD     1 
ATOM   2386 N  N      . VAL A 1 323 ? -50.71500 -14.16900 -11.26000 1.000 24.93194 ? 319 VAL A N      1 
ATOM   2387 C  CA     . VAL A 1 323 ? -51.96000 -13.97300 -10.54000 1.000 28.08231 ? 319 VAL A CA     1 
ATOM   2388 C  C      . VAL A 1 323 ? -53.00400 -13.44200 -11.50100 1.000 28.43499 ? 319 VAL A C      1 
ATOM   2389 O  O      . VAL A 1 323 ? -52.70100 -12.78800 -12.50300 1.000 37.68083 ? 319 VAL A O      1 
ATOM   2390 C  CB     . VAL A 1 323 ? -51.80500 -13.02700 -9.33100  1.000 32.89342 ? 319 VAL A CB     1 
ATOM   2391 C  CG1    . VAL A 1 323 ? -50.76800 -13.57500 -8.35800  1.000 27.98493 ? 319 VAL A CG1    1 
ATOM   2392 C  CG2    . VAL A 1 323 ? -51.44100 -11.63800 -9.79800  1.000 33.12502 ? 319 VAL A CG2    1 
ATOM   2393 N  N      . ASP A 1 324 ? -54.25100 -13.73400 -11.18100 1.000 30.14046 ? 320 ASP A N      1 
ATOM   2394 C  CA     . ASP A 1 324 ? -55.38600 -13.21000 -11.91100 1.000 31.32481 ? 320 ASP A CA     1 
ATOM   2395 C  C      . ASP A 1 324 ? -56.02100 -12.02800 -11.20500 1.000 37.17288 ? 320 ASP A C      1 
ATOM   2396 O  O      . ASP A 1 324 ? -56.49000 -11.09900 -11.87700 1.000 35.73323 ? 320 ASP A O      1 
ATOM   2397 C  CB     . ASP A 1 324 ? -56.40100 -14.33700 -12.14100 1.000 28.48499 ? 320 ASP A CB     1 
ATOM   2398 C  CG     . ASP A 1 324 ? -55.77600 -15.50500 -12.91300 1.000 43.36836 ? 320 ASP A CG     1 
ATOM   2399 O  OD1    . ASP A 1 324 ? -55.52900 -15.35100 -14.13000 1.000 46.84772 ? 320 ASP A OD1    1 
ATOM   2400 O  OD2    . ASP A 1 324 ? -55.47600 -16.55400 -12.29900 1.000 44.75273 ? 320 ASP A OD2    1 
ATOM   2401 N  N      . VAL A 1 325 ? -55.99600 -12.02900 -9.87000  1.000 31.10110 ? 321 VAL A N      1 
ATOM   2402 C  CA     . VAL A 1 325 ? -56.39600 -10.89100 -9.05600  1.000 35.64112 ? 321 VAL A CA     1 
ATOM   2403 C  C      . VAL A 1 325 ? -55.25300 -10.65100 -8.07500  1.000 33.05133 ? 321 VAL A C      1 
ATOM   2404 O  O      . VAL A 1 325 ? -55.02000 -11.46900 -7.17600  1.000 31.60642 ? 321 VAL A O      1 
ATOM   2405 C  CB     . VAL A 1 325 ? -57.72600 -11.12900 -8.31700  1.000 30.41417 ? 321 VAL A CB     1 
ATOM   2406 C  CG1    . VAL A 1 325 ? -58.24100 -9.84000  -7.69500  1.000 30.82475 ? 321 VAL A CG1    1 
ATOM   2407 C  CG2    . VAL A 1 325 ? -58.75800 -11.71300 -9.25600  1.000 32.46705 ? 321 VAL A CG2    1 
ATOM   2408 N  N      . GLY A 1 326 ? -54.52500 -9.55100  -8.26300  1.000 28.50079 ? 322 GLY A N      1 
ATOM   2409 C  CA     . GLY A 1 326 ? -53.43600 -9.19300  -7.38000  1.000 29.06927 ? 322 GLY A CA     1 
ATOM   2410 C  C      . GLY A 1 326 ? -53.82700 -8.01900  -6.50700  1.000 27.35065 ? 322 GLY A C      1 
ATOM   2411 O  O      . GLY A 1 326 ? -53.90500 -6.88800  -6.98500  1.000 33.67772 ? 322 GLY A O      1 
ATOM   2412 N  N      . ILE A 1 327 ? -54.09500 -8.28000  -5.23400  1.000 26.46633 ? 323 ILE A N      1 
ATOM   2413 C  CA     . ILE A 1 327 ? -54.66300 -7.29400  -4.32100  1.000 29.95886 ? 323 ILE A CA     1 
ATOM   2414 C  C      . ILE A 1 327 ? -53.54300 -6.80600  -3.41500  1.000 29.81147 ? 323 ILE A C      1 
ATOM   2415 O  O      . ILE A 1 327 ? -53.02000 -7.57100  -2.59700  1.000 32.36967 ? 323 ILE A O      1 
ATOM   2416 C  CB     . ILE A 1 327 ? -55.81400 -7.88100  -3.49100  1.000 29.79305 ? 323 ILE A CB     1 
ATOM   2417 C  CG1    . ILE A 1 327 ? -57.01900 -8.18400  -4.37600  1.000 32.65918 ? 323 ILE A CG1    1 
ATOM   2418 C  CG2    . ILE A 1 327 ? -56.16600 -6.94800  -2.33200  1.000 24.61085 ? 323 ILE A CG2    1 
ATOM   2419 C  CD1    . ILE A 1 327 ? -58.13600 -8.87000  -3.65400  1.000 31.79592 ? 323 ILE A CD1    1 
ATOM   2420 N  N      . ASN A 1 328 ? -53.19600 -5.52400  -3.53200  1.000 29.11928 ? 324 ASN A N      1 
ATOM   2421 C  CA     . ASN A 1 328 ? -52.20700 -4.90400  -2.64700  1.000 29.60355 ? 324 ASN A CA     1 
ATOM   2422 C  C      . ASN A 1 328 ? -52.96200 -4.28800  -1.47400  1.000 29.13244 ? 324 ASN A C      1 
ATOM   2423 O  O      . ASN A 1 328 ? -53.43300 -3.15200  -1.55500  1.000 35.28055 ? 324 ASN A O      1 
ATOM   2424 C  CB     . ASN A 1 328 ? -51.39400 -3.85000  -3.39300  1.000 26.54529 ? 324 ASN A CB     1 
ATOM   2425 C  CG     . ASN A 1 328 ? -50.41000 -3.13200  -2.48500  1.000 30.60367 ? 324 ASN A CG     1 
ATOM   2426 O  OD1    . ASN A 1 328 ? -49.91100 -3.71500  -1.52300  1.000 36.40700 ? 324 ASN A OD1    1 
ATOM   2427 N  ND2    . ASN A 1 328 ? -50.13500 -1.86400  -2.77800  1.000 30.00623 ? 324 ASN A ND2    1 
ATOM   2428 N  N      . ALA A 1 329 ? -53.06700 -5.01800  -0.37000  1.000 24.68191 ? 325 ALA A N      1 
ATOM   2429 C  CA     . ALA A 1 329 ? -53.83200 -4.52100  0.76500   1.000 25.95048 ? 325 ALA A CA     1 
ATOM   2430 C  C      . ALA A 1 329 ? -53.46800 -5.32100  2.00100   1.000 30.34311 ? 325 ALA A C      1 
ATOM   2431 O  O      . ALA A 1 329 ? -52.86400 -6.39400  1.92200   1.000 34.99367 ? 325 ALA A O      1 
ATOM   2432 C  CB     . ALA A 1 329 ? -55.35100 -4.59400  0.51500   1.000 22.93959 ? 325 ALA A CB     1 
ATOM   2433 N  N      . ASP A 1 330 ? -53.84800 -4.77400  3.14900   1.000 26.40053 ? 326 ASP A N      1 
ATOM   2434 C  CA     . ASP A 1 330 ? -53.74900 -5.49400  4.40500   1.000 26.72162 ? 326 ASP A CA     1 
ATOM   2435 C  C      . ASP A 1 330 ? -54.71500 -6.68400  4.40400   1.000 35.01209 ? 326 ASP A C      1 
ATOM   2436 O  O      . ASP A 1 330 ? -55.83800 -6.60100  3.88200   1.000 32.81709 ? 326 ASP A O      1 
ATOM   2437 C  CB     . ASP A 1 330 ? -54.05300 -4.53300  5.55500   1.000 26.82953 ? 326 ASP A CB     1 
ATOM   2438 C  CG     . ASP A 1 330 ? -54.24800 -5.23800  6.87600   1.000 29.36668 ? 326 ASP A CG     1 
ATOM   2439 O  OD1    . ASP A 1 330 ? -53.23700 -5.49100  7.55000   1.000 35.79640 ? 326 ASP A OD1    1 
ATOM   2440 O  OD2    . ASP A 1 330 ? -55.39200 -5.51400  7.26300   1.000 34.64100 ? 326 ASP A OD2    1 
ATOM   2441 N  N      . ALA A 1 331 ? -54.26900 -7.80400  4.98200   1.000 28.40604 ? 327 ALA A N      1 
ATOM   2442 C  CA     . ALA A 1 331 ? -55.08200 -9.02000  4.96400   1.000 27.97177 ? 327 ALA A CA     1 
ATOM   2443 C  C      . ALA A 1 331 ? -56.36800 -8.84700  5.76200   1.000 30.69052 ? 327 ALA A C      1 
ATOM   2444 O  O      . ALA A 1 331 ? -57.41900 -9.37300  5.38100   1.000 34.67521 ? 327 ALA A O      1 
ATOM   2445 C  CB     . ALA A 1 331 ? -54.29500 -10.21000 5.52100   1.000 21.60259 ? 327 ALA A CB     1 
ATOM   2446 N  N      . SER A 1 332 ? -56.30800 -8.13700  6.88700   1.000 31.83540 ? 328 SER A N      1 
ATOM   2447 C  CA     . SER A 1 332 ? -57.50900 -8.00400  7.70000   1.000 32.92237 ? 328 SER A CA     1 
ATOM   2448 C  C      . SER A 1 332 ? -58.53100 -7.10300  7.01300   1.000 30.37733 ? 328 SER A C      1 
ATOM   2449 O  O      . SER A 1 332 ? -59.72500 -7.40800  6.99800   1.000 31.15637 ? 328 SER A O      1 
ATOM   2450 C  CB     . SER A 1 332 ? -57.13100 -7.47900  9.08500   1.000 40.08375 ? 328 SER A CB     1 
ATOM   2451 O  OG     . SER A 1 332 ? -58.17500 -6.73400  9.67300   1.000 52.95898 ? 328 SER A OG     1 
ATOM   2452 N  N      . GLU A 1 333 ? -58.07100 -6.01400  6.39800   1.000 29.96675 ? 329 GLU A N      1 
ATOM   2453 C  CA     . GLU A 1 333 ? -58.98900 -5.13700  5.67600   1.000 32.32756 ? 329 GLU A CA     1 
ATOM   2454 C  C      . GLU A 1 333 ? -59.61700 -5.85400  4.49100   1.000 27.34538 ? 329 GLU A C      1 
ATOM   2455 O  O      . GLU A 1 333 ? -60.80300 -5.66300  4.19700   1.000 32.65655 ? 329 GLU A O      1 
ATOM   2456 C  CB     . GLU A 1 333 ? -58.25200 -3.88100  5.20400   1.000 36.87811 ? 329 GLU A CB     1 
ATOM   2457 C  CG     . GLU A 1 333 ? -57.86400 -2.91700  6.32300   1.000 45.28438 ? 329 GLU A CG     1 
ATOM   2458 C  CD     . GLU A 1 333 ? -59.06600 -2.48500  7.17000   1.000 56.69890 ? 329 GLU A CD     1 
ATOM   2459 O  OE1    . GLU A 1 333 ? -60.16100 -2.29400  6.60300   1.000 55.94355 ? 329 GLU A OE1    1 
ATOM   2460 O  OE2    . GLU A 1 333 ? -58.91100 -2.33800  8.40300   1.000 61.22050 ? 329 GLU A OE2    1 
ATOM   2461 N  N      . THR A 1 334 ? -58.83000 -6.67100  3.78700   1.000 29.93780 ? 330 THR A N      1 
ATOM   2462 C  CA     . THR A 1 334 ? -59.35400 -7.40400  2.63800   1.000 28.46657 ? 330 THR A CA     1 
ATOM   2463 C  C      . THR A 1 334 ? -60.39800 -8.42000  3.07500   1.000 29.70883 ? 330 THR A C      1 
ATOM   2464 O  O      . THR A 1 334 ? -61.48500 -8.50100  2.49100   1.000 26.08997 ? 330 THR A O      1 
ATOM   2465 C  CB     . THR A 1 334 ? -58.21800 -8.11000  1.88700   1.000 32.98290 ? 330 THR A CB     1 
ATOM   2466 O  OG1    . THR A 1 334 ? -57.25600 -7.15200  1.44500   1.000 32.48547 ? 330 THR A OG1    1 
ATOM   2467 C  CG2    . THR A 1 334 ? -58.76600 -8.89300  0.68300   1.000 24.38713 ? 330 THR A CG2    1 
ATOM   2468 N  N      . LEU A 1 335 ? -60.08600 -9.21200  4.10200   1.000 34.71995 ? 331 LEU A N      1 
ATOM   2469 C  CA     . LEU A 1 335 ? -61.04400 -10.22000 4.54300   1.000 31.61695 ? 331 LEU A CA     1 
ATOM   2470 C  C      . LEU A 1 335 ? -62.32500 -9.58000  5.07000   1.000 32.33282 ? 331 LEU A C      1 
ATOM   2471 O  O      . LEU A 1 335 ? -63.42800 -10.04300 4.75900   1.000 32.73550 ? 331 LEU A O      1 
ATOM   2472 C  CB     . LEU A 1 335 ? -60.39800 -11.13000 5.59400   1.000 29.45880 ? 331 LEU A CB     1 
ATOM   2473 C  CG     . LEU A 1 335 ? -59.40700 -12.15500 5.03600   1.000 28.37182 ? 331 LEU A CG     1 
ATOM   2474 C  CD1    . LEU A 1 335 ? -58.49400 -12.67600 6.14200   1.000 26.94797 ? 331 LEU A CD1    1 
ATOM   2475 C  CD2    . LEU A 1 335 ? -60.14100 -13.31300 4.35000   1.000 26.10313 ? 331 LEU A CD2    1 
ATOM   2476 N  N      . LYS A 1 336 ? -62.21000 -8.49900  5.84500   1.000 33.14608 ? 332 LYS A N      1 
ATOM   2477 C  CA     . LYS A 1 336 ? -63.42400 -7.82800  6.30200   1.000 31.11689 ? 332 LYS A CA     1 
ATOM   2478 C  C      . LYS A 1 336 ? -64.24900 -7.35600  5.11300   1.000 34.17778 ? 332 LYS A C      1 
ATOM   2479 O  O      . LYS A 1 336 ? -65.47700 -7.53000  5.08000   1.000 30.87739 ? 332 LYS A O      1 
ATOM   2480 C  CB     . LYS A 1 336 ? -63.07400 -6.65800  7.22500   1.000 34.55941 ? 332 LYS A CB     1 
ATOM   2481 C  CG     . LYS A 1 336 ? -62.33300 -7.08800  8.48800   1.000 42.87619 ? 332 LYS A CG     1 
ATOM   2482 C  CD     . LYS A 1 336 ? -62.28100 -5.98400  9.54400   1.000 50.65607 ? 332 LYS A CD     1 
ATOM   2483 C  CE     . LYS A 1 336 ? -61.10700 -5.03900  9.33700   1.000 60.44409 ? 332 LYS A CE     1 
ATOM   2484 N  NZ     . LYS A 1 336 ? -60.81600 -4.26200  10.57900  1.000 66.73432 ? 332 LYS A NZ     1 
ATOM   2485 N  N      . ALA A 1 337 ? -63.58500 -6.77900  4.10700   1.000 34.53046 ? 333 ALA A N      1 
ATOM   2486 C  CA     . ALA A 1 337 ? -64.30900 -6.31900  2.92700   1.000 33.99881 ? 333 ALA A CA     1 
ATOM   2487 C  C      . ALA A 1 337 ? -65.01100 -7.48000  2.23700   1.000 36.97285 ? 333 ALA A C      1 
ATOM   2488 O  O      . ALA A 1 337 ? -66.18400 -7.37100  1.85200   1.000 38.49935 ? 333 ALA A O      1 
ATOM   2489 C  CB     . ALA A 1 337 ? -63.35000 -5.61300  1.96300   1.000 31.18795 ? 333 ALA A CB     1 
ATOM   2490 N  N      . LEU A 1 338 ? -64.31600 -8.61200  2.09300   1.000 34.41202 ? 334 LEU A N      1 
ATOM   2491 C  CA     . LEU A 1 338 ? -64.92200 -9.77000  1.44400   1.000 33.75405 ? 334 LEU A CA     1 
ATOM   2492 C  C      . LEU A 1 338 ? -66.10000 -10.30100 2.24500   1.000 38.21248 ? 334 LEU A C      1 
ATOM   2493 O  O      . LEU A 1 338 ? -67.11700 -10.70300 1.66900   1.000 32.63286 ? 334 LEU A O      1 
ATOM   2494 C  CB     . LEU A 1 338 ? -63.88400 -10.86500 1.23400   1.000 35.09368 ? 334 LEU A CB     1 
ATOM   2495 C  CG     . LEU A 1 338 ? -62.85200 -10.57800 0.13800   1.000 38.83097 ? 334 LEU A CG     1 
ATOM   2496 C  CD1    . LEU A 1 338 ? -61.62500 -11.47500 0.29200   1.000 30.17204 ? 334 LEU A CD1    1 
ATOM   2497 C  CD2    . LEU A 1 338 ? -63.47300 -10.72900 -1.24400  1.000 46.00025 ? 334 LEU A CD2    1 
ATOM   2498 N  N      . ILE A 1 339 ? -65.98100 -10.32300 3.57700   1.000 38.32565 ? 335 ILE A N      1 
ATOM   2499 C  CA     . ILE A 1 339 ? -67.09900 -10.78500 4.39500   1.000 36.08591 ? 335 ILE A CA     1 
ATOM   2500 C  C      . ILE A 1 339 ? -68.29800 -9.86900  4.21400   1.000 39.37841 ? 335 ILE A C      1 
ATOM   2501 O  O      . ILE A 1 339 ? -69.43300 -10.32600 4.03500   1.000 38.13089 ? 335 ILE A O      1 
ATOM   2502 C  CB     . ILE A 1 339 ? -66.68000 -10.84900 5.87400   1.000 35.39898 ? 335 ILE A CB     1 
ATOM   2503 C  CG1    . ILE A 1 339 ? -65.63700 -11.94700 6.10000   1.000 31.94857 ? 335 ILE A CG1    1 
ATOM   2504 C  CG2    . ILE A 1 339 ? -67.90800 -11.05100 6.75800   1.000 32.55917 ? 335 ILE A CG2    1 
ATOM   2505 C  CD1    . ILE A 1 339 ? -64.89600 -11.83100 7.45100   1.000 27.91124 ? 335 ILE A CD1    1 
ATOM   2506 N  N      . LEU A 1 340 ? -68.05100 -8.56100  4.19000   1.000 42.36034 ? 336 LEU A N      1 
ATOM   2507 C  CA     . LEU A 1 340 ? -69.13400 -7.59800  4.06800   1.000 41.29969 ? 336 LEU A CA     1 
ATOM   2508 C  C      . LEU A 1 340 ? -69.86000 -7.76500  2.74500   1.000 42.01820 ? 336 LEU A C      1 
ATOM   2509 O  O      . LEU A 1 340 ? -71.09200 -7.70800  2.68600   1.000 47.60571 ? 336 LEU A O      1 
ATOM   2510 C  CB     . LEU A 1 340 ? -68.56500 -6.18800  4.16700   1.000 40.58645 ? 336 LEU A CB     1 
ATOM   2511 C  CG     . LEU A 1 340 ? -69.49300 -5.06800  4.61100   1.000 57.19107 ? 336 LEU A CG     1 
ATOM   2512 C  CD1    . LEU A 1 340 ? -69.57500 -5.06300  6.13100   1.000 62.94439 ? 336 LEU A CD1    1 
ATOM   2513 C  CD2    . LEU A 1 340 ? -68.99200 -3.73100  4.07200   1.000 58.94654 ? 336 LEU A CD2    1 
ATOM   2514 N  N      . CYS A 1 341 ? -69.10900 -8.01900  1.68100   1.000 40.63119 ? 337 CYS A N      1 
ATOM   2515 C  CA     . CYS A 1 341 ? -69.69000 -8.16300  0.35200   1.000 42.30770 ? 337 CYS A CA     1 
ATOM   2516 C  C      . CYS A 1 341 ? -70.47600 -9.46000  0.23500   1.000 46.40293 ? 337 CYS A C      1 
ATOM   2517 O  O      . CYS A 1 341 ? -71.62500 -9.46100  -0.22100  1.000 44.59745 ? 337 CYS A O      1 
ATOM   2518 C  CB     . CYS A 1 341 ? -68.56800 -8.10800  -0.68900  1.000 44.99750 ? 337 CYS A CB     1 
ATOM   2519 S  SG     . CYS A 1 341 ? -69.05800 -8.40600  -2.38900  1.000 52.09572 ? 337 CYS A SG     1 
ATOM   2520 N  N      . ILE A 1 342 ? -69.87700 -10.57500 0.66000   1.000 43.64207 ? 338 ILE A N      1 
ATOM   2521 C  CA     . ILE A 1 342 ? -70.53000 -11.86900 0.49900   1.000 44.98960 ? 338 ILE A CA     1 
ATOM   2522 C  C      . ILE A 1 342 ? -71.76400 -11.96500 1.39000   1.000 43.65523 ? 338 ILE A C      1 
ATOM   2523 O  O      . ILE A 1 342 ? -72.80000 -12.49800 0.97400   1.000 49.68754 ? 338 ILE A O      1 
ATOM   2524 C  CB     . ILE A 1 342 ? -69.52300 -13.00000 0.76700   1.000 46.60822 ? 338 ILE A CB     1 
ATOM   2525 C  CG1    . ILE A 1 342 ? -68.52600 -13.08400 -0.39000  1.000 55.94355 ? 338 ILE A CG1    1 
ATOM   2526 C  CG2    . ILE A 1 342 ? -70.22300 -14.33500 0.92400   1.000 44.58166 ? 338 ILE A CG2    1 
ATOM   2527 C  CD1    . ILE A 1 342 ? -67.27100 -13.86200 -0.05000  1.000 57.12001 ? 338 ILE A CD1    1 
ATOM   2528 N  N      . ARG A 1 343 ? -71.68700 -11.44000 2.61700   1.000 44.39216 ? 339 ARG A N      1 
ATOM   2529 C  CA     . ARG A 1 343 ? -72.83800 -11.48900 3.51400   1.000 42.48404 ? 339 ARG A CA     1 
ATOM   2530 C  C      . ARG A 1 343 ? -73.98400 -10.65300 2.96400   1.000 51.18245 ? 339 ARG A C      1 
ATOM   2531 O  O      . ARG A 1 343 ? -75.10300 -11.15000 2.78300   1.000 53.19585 ? 339 ARG A O      1 
ATOM   2532 C  CB     . ARG A 1 343 ? -72.46000 -11.01100 4.91600   1.000 41.94187 ? 339 ARG A CB     1 
ATOM   2533 C  CG     . ARG A 1 343 ? -71.90400 -12.10500 5.78300   1.000 53.63011 ? 339 ARG A CG     1 
ATOM   2534 C  CD     . ARG A 1 343 ? -72.26700 -11.96400 7.25100   1.000 58.52807 ? 339 ARG A CD     1 
ATOM   2535 N  NE     . ARG A 1 343 ? -71.80200 -13.13800 7.98700   1.000 64.55774 ? 339 ARG A NE     1 
ATOM   2536 C  CZ     . ARG A 1 343 ? -70.73100 -13.15300 8.77200   1.000 61.57054 ? 339 ARG A CZ     1 
ATOM   2537 N  NH1    . ARG A 1 343 ? -70.02000 -12.04800 8.94500   1.000 57.88062 ? 339 ARG A NH1    1 
ATOM   2538 N  NH2    . ARG A 1 343 ? -70.38000 -14.27000 9.39300   1.000 58.22803 ? 339 ARG A NH2    1 
ATOM   2539 N  N      . SER A 1 344 ? -73.73300 -9.36300  2.72400   1.000 55.74616 ? 340 SER A N      1 
ATOM   2540 C  CA     . SER A 1 344 ? -74.74800 -8.51500  2.09000   1.000 56.95946 ? 340 SER A CA     1 
ATOM   2541 C  C      . SER A 1 344 ? -75.34100 -9.18000  0.84900   1.000 54.40126 ? 340 SER A C      1 
ATOM   2542 O  O      . SER A 1 344 ? -76.52900 -9.01200  0.54800   1.000 59.19657 ? 340 SER A O      1 
ATOM   2543 C  CB     . SER A 1 344 ? -74.14800 -7.14400  1.75200   1.000 58.49912 ? 340 SER A CB     1 
ATOM   2544 O  OG     . SER A 1 344 ? -73.49300 -7.16300  0.49800   1.000 65.19992 ? 340 SER A OG     1 
ATOM   2545 N  N      . SER A 1 345 ? -74.61300 -9.94300  0.08100   1.000 54.70393 ? 341 SER A N      1 
ATOM   2546 C  CA     . SER A 1 345 ? -75.21000 -10.52400 -1.10400  1.000 55.86722 ? 341 SER A CA     1 
ATOM   2547 C  C      . SER A 1 345 ? -76.25500 -11.52500 -0.76300  1.000 65.74472 ? 341 SER A C      1 
ATOM   2548 O  O      . SER A 1 345 ? -77.13100 -11.81000 -1.53800  1.000 69.37674 ? 341 SER A O      1 
ATOM   2549 C  CB     . SER A 1 345 ? -74.19300 -11.27800 -1.86700  1.000 60.24670 ? 341 SER A CB     1 
ATOM   2550 O  OG     . SER A 1 345 ? -73.80800 -12.38700 -1.13900  1.000 64.24981 ? 341 SER A OG     1 
ATOM   2551 N  N      . GLY A 1 346 ? -76.05900 -12.18400 0.36000   1.000 65.00253 ? 342 GLY A N      1 
ATOM   2552 C  CA     . GLY A 1 346 ? -76.93400 -13.24000 0.78500   1.000 63.99715 ? 342 GLY A CA     1 
ATOM   2553 C  C      . GLY A 1 346 ? -76.75100 -14.56000 0.06000   1.000 66.18425 ? 342 GLY A C      1 
ATOM   2554 O  O      . GLY A 1 346 ? -77.50600 -15.45900 0.31600   1.000 63.66553 ? 342 GLY A O      1 
ATOM   2555 N  N      . LYS A 1 347 ? -75.75900 -14.72000 -0.80600  1.000 67.85287 ? 343 LYS A N      1 
ATOM   2556 C  CA     . LYS A 1 347 ? -75.65600 -15.99000 -1.51200  1.000 72.31130 ? 343 LYS A CA     1 
ATOM   2557 C  C      . LYS A 1 347 ? -74.74500 -17.03800 -0.87500  1.000 72.27972 ? 343 LYS A C      1 
ATOM   2558 O  O      . LYS A 1 347 ? -75.02200 -17.54500 0.19100   1.000 69.29515 ? 343 LYS A O      1 
ATOM   2559 C  CB     . LYS A 1 347 ? -75.31300 -15.80300 -2.99600  1.000 70.41107 ? 343 LYS A CB     1 
ATOM   2560 C  CG     . LYS A 1 347 ? -74.79600 -14.44600 -3.38500  1.000 73.24299 ? 343 LYS A CG     1 
ATOM   2561 C  CD     . LYS A 1 347 ? -75.48900 -13.86400 -4.59800  1.000 74.87213 ? 343 LYS A CD     1 
ATOM   2562 C  CE     . LYS A 1 347 ? -75.22400 -14.67500 -5.84900  1.000 79.86484 ? 343 LYS A CE     1 
ATOM   2563 N  NZ     . LYS A 1 347 ? -76.21500 -14.33600 -6.90700  1.000 85.82608 ? 343 LYS A NZ     1 
ATOM   2564 N  N      . GLY A 1 375 ? -33.48900 -43.73900 22.63900  1.000 45.36860 ? 371 GLY A N      1 
ATOM   2565 C  CA     . GLY A 1 375 ? -34.11300 -42.52100 23.12800  1.000 51.54829 ? 371 GLY A CA     1 
ATOM   2566 C  C      . GLY A 1 375 ? -35.62800 -42.52700 23.00300  1.000 55.54087 ? 371 GLY A C      1 
ATOM   2567 O  O      . GLY A 1 375 ? -36.23500 -43.58500 22.83900  1.000 59.29658 ? 371 GLY A O      1 
ATOM   2568 N  N      . ILE A 1 376 ? -36.25500 -41.35700 23.13500  1.000 49.07167 ? 372 ILE A N      1 
ATOM   2569 C  CA     . ILE A 1 376 ? -37.69400 -41.22500 22.92700  1.000 37.47028 ? 372 ILE A CA     1 
ATOM   2570 C  C      . ILE A 1 376 ? -37.93800 -40.86300 21.47000  1.000 33.48296 ? 372 ILE A C      1 
ATOM   2571 O  O      . ILE A 1 376 ? -37.27500 -39.97500 20.92700  1.000 34.11725 ? 372 ILE A O      1 
ATOM   2572 C  CB     . ILE A 1 376 ? -38.29800 -40.16100 23.85500  1.000 40.61013 ? 372 ILE A CB     1 
ATOM   2573 C  CG1    . ILE A 1 376 ? -37.80600 -40.33100 25.29300  1.000 38.64148 ? 372 ILE A CG1    1 
ATOM   2574 C  CG2    . ILE A 1 376 ? -39.82900 -40.21800 23.79500  1.000 40.93386 ? 372 ILE A CG2    1 
ATOM   2575 C  CD1    . ILE A 1 376 ? -38.47400 -39.37400 26.25100  1.000 33.14871 ? 372 ILE A CD1    1 
ATOM   2576 N  N      . HIS A 1 377 ? -38.90500 -41.51700 20.84100  1.000 32.50390 ? 373 HIS A N      1 
ATOM   2577 C  CA     . HIS A 1 377 ? -39.24900 -41.14700 19.47600  1.000 33.01975 ? 373 HIS A CA     1 
ATOM   2578 C  C      . HIS A 1 377 ? -39.84900 -39.74900 19.48800  1.000 34.53309 ? 373 HIS A C      1 
ATOM   2579 O  O      . HIS A 1 377 ? -40.80000 -39.50100 20.23600  1.000 39.94689 ? 373 HIS A O      1 
ATOM   2580 C  CB     . HIS A 1 377 ? -40.24700 -42.13100 18.86000  1.000 39.31261 ? 373 HIS A CB     1 
ATOM   2581 C  CG     . HIS A 1 377 ? -40.36900 -42.00400 17.37300  1.000 42.31823 ? 373 HIS A CG     1 
ATOM   2582 N  ND1    . HIS A 1 377 ? -41.05500 -40.97200 16.76700  1.000 41.24442 ? 373 HIS A ND1    1 
ATOM   2583 C  CD2    . HIS A 1 377 ? -39.86500 -42.76300 16.36900  1.000 42.64459 ? 373 HIS A CD2    1 
ATOM   2584 C  CE1    . HIS A 1 377 ? -40.98200 -41.11100 15.45500  1.000 41.24968 ? 373 HIS A CE1    1 
ATOM   2585 N  NE2    . HIS A 1 377 ? -40.26000 -42.18500 15.18700  1.000 43.32362 ? 373 HIS A NE2    1 
ATOM   2586 N  N      . PRO A 1 378 ? -39.34100 -38.82200 18.67300  1.000 32.45126 ? 374 PRO A N      1 
ATOM   2587 C  CA     . PRO A 1 378 ? -39.80400 -37.42900 18.77500  1.000 35.69112 ? 374 PRO A CA     1 
ATOM   2588 C  C      . PRO A 1 378 ? -41.29900 -37.26000 18.56900  1.000 39.43104 ? 374 PRO A C      1 
ATOM   2589 O  O      . PRO A 1 378 ? -41.89300 -36.36300 19.17800  1.000 37.59398 ? 374 PRO A O      1 
ATOM   2590 C  CB     . PRO A 1 378 ? -38.99600 -36.71700 17.68300  1.000 34.31990 ? 374 PRO A CB     1 
ATOM   2591 C  CG     . PRO A 1 378 ? -37.74500 -37.54900 17.55500  1.000 34.75943 ? 374 PRO A CG     1 
ATOM   2592 C  CD     . PRO A 1 378 ? -38.25000 -38.96900 17.70000  1.000 38.10983 ? 374 PRO A CD     1 
ATOM   2593 N  N      . ALA A 1 379 ? -41.94200 -38.11100 17.76400  1.000 40.76805 ? 375 ALA A N      1 
ATOM   2594 C  CA     . ALA A 1 379 ? -43.39200 -38.01700 17.63200  1.000 38.51251 ? 375 ALA A CA     1 
ATOM   2595 C  C      . ALA A 1 379 ? -44.08600 -38.30400 18.96000  1.000 37.71242 ? 375 ALA A C      1 
ATOM   2596 O  O      . ALA A 1 379 ? -45.16300 -37.75500 19.23000  1.000 34.57783 ? 375 ALA A O      1 
ATOM   2597 C  CB     . ALA A 1 379 ? -43.89700 -38.96900 16.54200  1.000 37.44396 ? 375 ALA A CB     1 
ATOM   2598 N  N      . MET A 1 380 ? -43.48300 -39.15100 19.80400  1.000 35.82272 ? 376 MET A N      1 
ATOM   2599 C  CA     . MET A 1 380 ? -44.04200 -39.40000 21.13100  1.000 37.20972 ? 376 MET A CA     1 
ATOM   2600 C  C      . MET A 1 380 ? -43.85300 -38.20200 22.04700  1.000 36.15960 ? 376 MET A C      1 
ATOM   2601 O  O      . MET A 1 380 ? -44.69800 -37.94800 22.91600  1.000 35.05683 ? 376 MET A O      1 
ATOM   2602 C  CB     . MET A 1 380 ? -43.40100 -40.63100 21.76400  1.000 34.86997 ? 376 MET A CB     1 
ATOM   2603 C  CG     . MET A 1 380 ? -43.78800 -41.94200 21.11700  1.000 53.50905 ? 376 MET A CG     1 
ATOM   2604 S  SD     . MET A 1 380 ? -45.53300 -42.35900 21.35200  1.000 73.26142 ? 376 MET A SD     1 
ATOM   2605 C  CE     . MET A 1 380 ? -46.04400 -41.17600 22.61000  1.000 68.58191 ? 376 MET A CE     1 
ATOM   2606 N  N      . VAL A 1 381 ? -42.75000 -37.47200 21.88000  1.000 30.04571 ? 377 VAL A N      1 
ATOM   2607 C  CA     . VAL A 1 381 ? -42.56200 -36.22900 22.62100  1.000 36.69124 ? 377 VAL A CA     1 
ATOM   2608 C  C      . VAL A 1 381 ? -43.68300 -35.25200 22.29400  1.000 37.00180 ? 377 VAL A C      1 
ATOM   2609 O  O      . VAL A 1 381 ? -44.31600 -34.67900 23.18800  1.000 35.28318 ? 377 VAL A O      1 
ATOM   2610 C  CB     . VAL A 1 381 ? -41.18300 -35.61400 22.30700  1.000 33.91722 ? 377 VAL A CB     1 
ATOM   2611 C  CG1    . VAL A 1 381 ? -41.05300 -34.24800 22.97600  1.000 30.71947 ? 377 VAL A CG1    1 
ATOM   2612 C  CG2    . VAL A 1 381 ? -40.05700 -36.54400 22.74800  1.000 37.20183 ? 377 VAL A CG2    1 
ATOM   2613 N  N      . VAL A 1 382 ? -43.93500 -35.04200 21.00100  1.000 38.08615 ? 378 VAL A N      1 
ATOM   2614 C  CA     . VAL A 1 382 ? -44.97000 -34.09900 20.58600  1.000 32.83025 ? 378 VAL A CA     1 
ATOM   2615 C  C      . VAL A 1 382 ? -46.34800 -34.57100 21.04200  1.000 30.72474 ? 378 VAL A C      1 
ATOM   2616 O  O      . VAL A 1 382 ? -47.17200 -33.76700 21.48400  1.000 31.35376 ? 378 VAL A O      1 
ATOM   2617 C  CB     . VAL A 1 382 ? -44.91200 -33.88300 19.06300  1.000 26.01891 ? 378 VAL A CB     1 
ATOM   2618 C  CG1    . VAL A 1 382 ? -46.00500 -32.91800 18.61600  1.000 27.34012 ? 378 VAL A CG1    1 
ATOM   2619 C  CG2    . VAL A 1 382 ? -43.53100 -33.34800 18.65600  1.000 27.10325 ? 378 VAL A CG2    1 
ATOM   2620 N  N      . GLU A 1 383 ? -46.62700 -35.87600 20.95500  1.000 30.21415 ? 379 GLU A N      1 
ATOM   2621 C  CA     . GLU A 1 383 ? -47.92700 -36.33700 21.44300  1.000 35.35161 ? 379 GLU A CA     1 
ATOM   2622 C  C      . GLU A 1 383 ? -48.07200 -36.05900 22.93700  1.000 39.39946 ? 379 GLU A C      1 
ATOM   2623 O  O      . GLU A 1 383 ? -49.15200 -35.67400 23.40600  1.000 33.80405 ? 379 GLU A O      1 
ATOM   2624 C  CB     . GLU A 1 383 ? -48.14500 -37.81800 21.16600  1.000 39.07311 ? 379 GLU A CB     1 
ATOM   2625 C  CG     . GLU A 1 383 ? -49.51300 -38.26700 21.68000  1.000 49.05851 ? 379 GLU A CG     1 
ATOM   2626 C  CD     . GLU A 1 383 ? -49.77200 -39.75200 21.52400  1.000 64.80251 ? 379 GLU A CD     1 
ATOM   2627 O  OE1    . GLU A 1 383 ? -48.80100 -40.53700 21.48000  1.000 70.24526 ? 379 GLU A OE1    1 
ATOM   2628 O  OE2    . GLU A 1 383 ? -50.96000 -40.13300 21.45000  1.000 73.76937 ? 379 GLU A OE2    1 
ATOM   2629 N  N      . ALA A 1 384 ? -47.00500 -36.28600 23.71100  1.000 33.85932 ? 380 ALA A N      1 
ATOM   2630 C  CA     . ALA A 1 384 ? -47.07600 -36.00100 25.14300  1.000 36.32541 ? 380 ALA A CA     1 
ATOM   2631 C  C      . ALA A 1 384 ? -47.29600 -34.51800 25.38100  1.000 32.89868 ? 380 ALA A C      1 
ATOM   2632 O  O      . ALA A 1 384 ? -48.13100 -34.12900 26.20300  1.000 31.81697 ? 380 ALA A O      1 
ATOM   2633 C  CB     . ALA A 1 384 ? -45.80000 -36.46200 25.83900  1.000 34.00934 ? 380 ALA A CB     1 
ATOM   2634 N  N      . MET A 1 385 ? -46.57900 -33.67400 24.63800  1.000 28.56132 ? 381 MET A N      1 
ATOM   2635 C  CA     . MET A 1 385 ? -46.86600 -32.24800 24.69000  1.000 35.67007 ? 381 MET A CA     1 
ATOM   2636 C  C      . MET A 1 385 ? -48.32700 -31.99500 24.34300  1.000 36.47279 ? 381 MET A C      1 
ATOM   2637 O  O      . MET A 1 385 ? -48.99500 -31.17200 24.96500  1.000 36.34910 ? 381 MET A O      1 
ATOM   2638 C  CB     . MET A 1 385 ? -45.98500 -31.48200 23.70800  1.000 28.19285 ? 381 MET A CB     1 
ATOM   2639 C  CG     . MET A 1 385 ? -44.51900 -31.50400 24.09200  1.000 34.86997 ? 381 MET A CG     1 
ATOM   2640 S  SD     . MET A 1 385 ? -43.48300 -30.94400 22.72200  1.000 36.60439 ? 381 MET A SD     1 
ATOM   2641 C  CE     . MET A 1 385 ? -44.05600 -29.25100 22.55100  1.000 37.37553 ? 381 MET A CE     1 
ATOM   2642 N  N      . GLN A 1 386 ? -48.81700 -32.61500 23.27900  1.000 37.40975 ? 382 GLN A N      1 
ATOM   2643 C  CA     . GLN A 1 386 ? -50.21100 -32.41000 22.95700  1.000 40.09165 ? 382 GLN A CA     1 
ATOM   2644 C  C      . GLN A 1 386 ? -51.08800 -32.86400 24.07900  1.000 45.77391 ? 382 GLN A C      1 
ATOM   2645 O  O      . GLN A 1 386 ? -52.21400 -32.38700 24.18500  1.000 54.08543 ? 382 GLN A O      1 
ATOM   2646 C  CB     . GLN A 1 386 ? -50.59300 -33.18500 21.71900  1.000 39.84951 ? 382 GLN A CB     1 
ATOM   2647 C  CG     . GLN A 1 386 ? -51.79100 -32.62900 20.92800  1.000 35.57005 ? 382 GLN A CG     1 
ATOM   2648 C  CD     . GLN A 1 386 ? -51.42900 -31.51700 19.90800  1.000 41.62868 ? 382 GLN A CD     1 
ATOM   2649 O  OE1    . GLN A 1 386 ? -50.73800 -31.76400 18.91200  1.000 38.29933 ? 382 GLN A OE1    1 
ATOM   2650 N  NE2    . GLN A 1 386 ? -51.94000 -30.29800 20.14500  1.000 44.70273 ? 382 GLN A NE2    1 
ATOM   2651 N  N      . ASN A 1 387 ? -50.64800 -33.89100 24.81300  1.000 47.75573 ? 383 ASN A N      1 
ATOM   2652 C  CA     . ASN A 1 387 ? -51.38400 -34.55600 25.88400  1.000 39.65739 ? 383 ASN A CA     1 
ATOM   2653 C  C      . ASN A 1 387 ? -51.29500 -33.80500 27.23200  1.000 50.55869 ? 383 ASN A C      1 
ATOM   2654 O  O      . ASN A 1 387 ? -51.78200 -34.28400 28.21700  1.000 61.48895 ? 383 ASN A O      1 
ATOM   2655 C  CB     . ASN A 1 387 ? -50.96600 -36.03200 26.10200  1.000 38.50725 ? 383 ASN A CB     1 
ATOM   2656 C  CG     . ASN A 1 387 ? -51.66000 -36.93500 25.06800  1.000 42.12084 ? 383 ASN A CG     1 
ATOM   2657 O  OD1    . ASN A 1 387 ? -52.57600 -36.49300 24.34900  1.000 49.16379 ? 383 ASN A OD1    1 
ATOM   2658 N  ND2    . ASN A 1 387 ? -51.23600 -38.19200 25.03100  1.000 51.32721 ? 383 ASN A ND2    1 
ATOM   2659 N  N      . ARG A 1 388 ? -50.54600 -32.71700 27.36300  1.000 35.80429 ? 384 ARG A N      1 
ATOM   2660 C  CA     . ARG A 1 388 ? -50.41700 -31.92500 28.65300  1.000 40.15745 ? 384 ARG A CA     1 
ATOM   2661 C  C      . ARG A 1 388 ? -50.54800 -30.41900 28.46000  1.000 44.68694 ? 384 ARG A C      1 
ATOM   2662 O  O      . ARG A 1 388 ? -51.03100 -29.76600 29.33200  1.000 43.45784 ? 384 ARG A O      1 
ATOM   2663 C  CB     . ARG A 1 388 ? -49.09600 -32.19200 29.33800  1.000 46.28976 ? 384 ARG A CB     1 
ATOM   2664 C  CG     . ARG A 1 388 ? -49.08100 -31.74400 30.88000  1.000 53.69854 ? 384 ARG A CG     1 
ATOM   2665 C  CD     . ARG A 1 388 ? -48.09100 -32.61000 31.70100  1.000 55.21715 ? 384 ARG A CD     1 
ATOM   2666 N  NE     . ARG A 1 388 ? -48.54000 -33.99600 31.77500  1.000 52.78001 ? 384 ARG A NE     1 
ATOM   2667 C  CZ     . ARG A 1 388 ? -49.55300 -34.38000 32.54200  1.000 59.08077 ? 384 ARG A CZ     1 
ATOM   2668 N  NH1    . ARG A 1 388 ? -50.18100 -33.47100 33.27600  1.000 57.79377 ? 384 ARG A NH1    1 
ATOM   2669 N  NH2    . ARG A 1 388 ? -49.93300 -35.65100 32.58900  1.000 66.03687 ? 384 ARG A NH2    1 
ATOM   2670 N  N      . LEU A 1 389 ? -50.08700 -29.84500 27.31300  1.000 37.00180 ? 385 LEU A N      1 
ATOM   2671 C  CA     . LEU A 1 389 ? -49.97900 -28.37700 27.24800  1.000 36.29119 ? 385 LEU A CA     1 
ATOM   2672 C  C      . LEU A 1 389 ? -51.35100 -27.72900 27.22500  1.000 38.66516 ? 385 LEU A C      1 
ATOM   2673 O  O      . LEU A 1 389 ? -52.21400 -28.15100 26.43300  1.000 33.21714 ? 385 LEU A O      1 
ATOM   2674 C  CB     . LEU A 1 389 ? -49.17600 -27.98900 26.03200  1.000 29.31404 ? 385 LEU A CB     1 
ATOM   2675 C  CG     . LEU A 1 389 ? -47.68200 -28.37900 26.04300  1.000 38.09930 ? 385 LEU A CG     1 
ATOM   2676 C  CD1    . LEU A 1 389 ? -46.95200 -28.13500 24.70100  1.000 43.09727 ? 385 LEU A CD1    1 
ATOM   2677 C  CD2    . LEU A 1 389 ? -46.95000 -27.69600 27.18600  1.000 36.46227 ? 385 LEU A CD2    1 
ATOM   2678 N  N      . PRO A 1 390 ? -51.58200 -26.69900 28.03000  1.000 34.88576 ? 386 PRO A N      1 
ATOM   2679 C  CA     . PRO A 1 390 ? -52.84800 -25.99400 27.96200  1.000 34.74364 ? 386 PRO A CA     1 
ATOM   2680 C  C      . PRO A 1 390 ? -53.08800 -25.42700 26.56900  1.000 39.34156 ? 386 PRO A C      1 
ATOM   2681 O  O      . PRO A 1 390 ? -52.17200 -25.24600 25.75800  1.000 37.31763 ? 386 PRO A O      1 
ATOM   2682 C  CB     . PRO A 1 390 ? -52.68900 -24.88900 29.01300  1.000 35.48057 ? 386 PRO A CB     1 
ATOM   2683 C  CG     . PRO A 1 390 ? -51.69700 -25.42200 29.98300  1.000 38.89677 ? 386 PRO A CG     1 
ATOM   2684 C  CD     . PRO A 1 390 ? -50.70600 -26.18500 29.10100  1.000 39.31261 ? 386 PRO A CD     1 
ATOM   2685 N  N      . ALA A 1 391 ? -54.36900 -25.16200 26.29100  1.000 42.34455 ? 387 ALA A N      1 
ATOM   2686 C  CA     . ALA A 1 391 ? -54.76400 -24.72700 24.95500  1.000 46.67928 ? 387 ALA A CA     1 
ATOM   2687 C  C      . ALA A 1 391 ? -54.17400 -23.36700 24.61300  1.000 42.37087 ? 387 ALA A C      1 
ATOM   2688 O  O      . ALA A 1 391 ? -53.86900 -23.09700 23.44500  1.000 45.06330 ? 387 ALA A O      1 
ATOM   2689 C  CB     . ALA A 1 391 ? -56.29500 -24.68700 24.84500  1.000 47.21356 ? 387 ALA A CB     1 
ATOM   2690 N  N      . ASP A 1 392 ? -53.98500 -22.50900 25.61000  1.000 43.69998 ? 388 ASP A N      1 
ATOM   2691 C  CA     . ASP A 1 392 ? -53.44400 -21.18200 25.37500  1.000 43.31572 ? 388 ASP A CA     1 
ATOM   2692 C  C      . ASP A 1 392 ? -51.91100 -21.16400 25.32900  1.000 38.23880 ? 388 ASP A C      1 
ATOM   2693 O  O      . ASP A 1 392 ? -51.32700 -20.08100 25.35300  1.000 32.16965 ? 388 ASP A O      1 
ATOM   2694 C  CB     . ASP A 1 392 ? -53.97100 -20.19700 26.43500  1.000 37.72821 ? 388 ASP A CB     1 
ATOM   2695 C  CG     . ASP A 1 392 ? -53.58600 -20.58400 27.85300  1.000 52.09835 ? 388 ASP A CG     1 
ATOM   2696 O  OD1    . ASP A 1 392 ? -53.28500 -21.77300 28.09500  1.000 53.76960 ? 388 ASP A OD1    1 
ATOM   2697 O  OD2    . ASP A 1 392 ? -53.59000 -19.69400 28.73400  1.000 58.38068 ? 388 ASP A OD2    1 
ATOM   2698 N  N      . THR A 1 393 ? -51.25000 -22.31900 25.24600  1.000 32.46705 ? 389 THR A N      1 
ATOM   2699 C  CA     . THR A 1 393 ? -49.79100 -22.32700 25.22000  1.000 29.62987 ? 389 THR A CA     1 
ATOM   2700 C  C      . THR A 1 393 ? -49.28100 -21.68600 23.93200  1.000 32.34862 ? 389 THR A C      1 
ATOM   2701 O  O      . THR A 1 393 ? -49.81700 -21.92700 22.84600  1.000 38.64411 ? 389 THR A O      1 
ATOM   2702 C  CB     . THR A 1 393 ? -49.23000 -23.75200 25.31700  1.000 30.16414 ? 389 THR A CB     1 
ATOM   2703 O  OG1    . THR A 1 393 ? -49.66100 -24.37700 26.53200  1.000 28.34814 ? 389 THR A OG1    1 
ATOM   2704 C  CG2    . THR A 1 393 ? -47.70300 -23.72800 25.28500  1.000 28.77450 ? 389 THR A CG2    1 
ATOM   2705 N  N      . ILE A 1 394 ? -48.25900 -20.83700 24.06200  1.000 28.60869 ? 390 ILE A N      1 
ATOM   2706 C  CA     . ILE A 1 394 ? -47.51200 -20.34200 22.90900  1.000 31.25112 ? 390 ILE A CA     1 
ATOM   2707 C  C      . ILE A 1 394 ? -46.28600 -21.23400 22.74200  1.000 31.00635 ? 390 ILE A C      1 
ATOM   2708 O  O      . ILE A 1 394 ? -45.43800 -21.30400 23.63600  1.000 29.51143 ? 390 ILE A O      1 
ATOM   2709 C  CB     . ILE A 1 394 ? -47.11000 -18.86700 23.07500  1.000 28.16390 ? 390 ILE A CB     1 
ATOM   2710 C  CG1    . ILE A 1 394 ? -48.34800 -17.98500 23.28500  1.000 30.14046 ? 390 ILE A CG1    1 
ATOM   2711 C  CG2    . ILE A 1 394 ? -46.29000 -18.38900 21.84000  1.000 21.92895 ? 390 ILE A CG2    1 
ATOM   2712 C  CD1    . ILE A 1 394 ? -48.03100 -16.59900 23.86500  1.000 32.71445 ? 390 ILE A CD1    1 
ATOM   2713 N  N      . LEU A 1 395 ? -46.20200 -21.93300 21.60700  1.000 26.16630 ? 391 LEU A N      1 
ATOM   2714 C  CA     . LEU A 1 395 ? -45.11800 -22.87400 21.33700  1.000 27.84281 ? 391 LEU A CA     1 
ATOM   2715 C  C      . LEU A 1 395 ? -44.11000 -22.22600 20.38900  1.000 27.55067 ? 391 LEU A C      1 
ATOM   2716 O  O      . LEU A 1 395 ? -44.42300 -21.94900 19.22500  1.000 30.33522 ? 391 LEU A O      1 
ATOM   2717 C  CB     . LEU A 1 395 ? -45.66800 -24.17300 20.74800  1.000 27.52172 ? 391 LEU A CB     1 
ATOM   2718 C  CG     . LEU A 1 395 ? -44.62100 -25.21200 20.32200  1.000 28.77977 ? 391 LEU A CG     1 
ATOM   2719 C  CD1    . LEU A 1 395 ? -43.84000 -25.75300 21.52200  1.000 30.02465 ? 391 LEU A CD1    1 
ATOM   2720 C  CD2    . LEU A 1 395 ? -45.28100 -26.35600 19.55900  1.000 30.67999 ? 391 LEU A CD2    1 
ATOM   2721 N  N      . PHE A 1 396 ? -42.89700 -21.99500 20.88800  1.000 24.16869 ? 392 PHE A N      1 
ATOM   2722 C  CA     . PHE A 1 396 ? -41.77500 -21.56300 20.06500  1.000 28.38761 ? 392 PHE A CA     1 
ATOM   2723 C  C      . PHE A 1 396 ? -41.04900 -22.80800 19.58300  1.000 30.45628 ? 392 PHE A C      1 
ATOM   2724 O  O      . PHE A 1 396 ? -40.79500 -23.72800 20.36700  1.000 25.97153 ? 392 PHE A O      1 
ATOM   2725 C  CB     . PHE A 1 396 ? -40.81300 -20.65500 20.84900  1.000 26.40580 ? 392 PHE A CB     1 
ATOM   2726 C  CG     . PHE A 1 396 ? -41.32100 -19.24700 21.02100  1.000 26.41896 ? 392 PHE A CG     1 
ATOM   2727 C  CD1    . PHE A 1 396 ? -42.37000 -18.97100 21.89200  1.000 20.06030 ? 392 PHE A CD1    1 
ATOM   2728 C  CD2    . PHE A 1 396 ? -40.77600 -18.21300 20.29100  1.000 24.52926 ? 392 PHE A CD2    1 
ATOM   2729 C  CE1    . PHE A 1 396 ? -42.85100 -17.67500 22.03800  1.000 20.48667 ? 392 PHE A CE1    1 
ATOM   2730 C  CE2    . PHE A 1 396 ? -41.24900 -16.93300 20.42700  1.000 26.36106 ? 392 PHE A CE2    1 
ATOM   2731 C  CZ     . PHE A 1 396 ? -42.29700 -16.65900 21.30600  1.000 21.74998 ? 392 PHE A CZ     1 
ATOM   2732 N  N      . VAL A 1 397 ? -40.74900 -22.85300 18.29100  1.000 28.26392 ? 393 VAL A N      1 
ATOM   2733 C  CA     . VAL A 1 397 ? -40.06700 -23.99100 17.69500  1.000 21.54206 ? 393 VAL A CA     1 
ATOM   2734 C  C      . VAL A 1 397 ? -38.80600 -23.44700 17.05200  1.000 22.86590 ? 393 VAL A C      1 
ATOM   2735 O  O      . VAL A 1 397 ? -38.86200 -22.46600 16.30400  1.000 25.22934 ? 393 VAL A O      1 
ATOM   2736 C  CB     . VAL A 1 397 ? -40.96100 -24.72300 16.67600  1.000 28.86662 ? 393 VAL A CB     1 
ATOM   2737 C  CG1    . VAL A 1 397 ? -40.17300 -25.83300 15.95800  1.000 30.30627 ? 393 VAL A CG1    1 
ATOM   2738 C  CG2    . VAL A 1 397 ? -42.19700 -25.31400 17.38900  1.000 24.52399 ? 393 VAL A CG2    1 
ATOM   2739 N  N      . ASP A 1 398 ? -37.68100 -24.07200 17.34500  1.000 22.39479 ? 394 ASP A N      1 
ATOM   2740 C  CA     . ASP A 1 398 ? -36.41200 -23.59300 16.82400  1.000 27.88755 ? 394 ASP A CA     1 
ATOM   2741 C  C      . ASP A 1 398 ? -36.19700 -24.17300 15.43300  1.000 31.18269 ? 394 ASP A C      1 
ATOM   2742 O  O      . ASP A 1 398 ? -37.13000 -24.64400 14.78100  1.000 35.37529 ? 394 ASP A O      1 
ATOM   2743 C  CB     . ASP A 1 398 ? -35.26200 -23.92700 17.77600  1.000 25.19776 ? 394 ASP A CB     1 
ATOM   2744 C  CG     . ASP A 1 398 ? -34.06500 -22.96200 17.61500  1.000 35.64375 ? 394 ASP A CG     1 
ATOM   2745 O  OD1    . ASP A 1 398 ? -33.24000 -23.16100 16.69300  1.000 34.34622 ? 394 ASP A OD1    1 
ATOM   2746 O  OD2    . ASP A 1 398 ? -33.96100 -21.99800 18.39900  1.000 37.65978 ? 394 ASP A OD2    1 
ATOM   2747 N  N      . ASN A 1 399 ? -34.97500 -24.07300 14.92900  1.000 30.58525 ? 395 ASN A N      1 
ATOM   2748 C  CA     . ASN A 1 399 ? -34.64600 -24.55500 13.59900  1.000 34.37781 ? 395 ASN A CA     1 
ATOM   2749 C  C      . ASN A 1 399 ? -33.64100 -25.69400 13.71100  1.000 44.44217 ? 395 ASN A C      1 
ATOM   2750 O  O      . ASN A 1 399 ? -32.66200 -25.60900 14.46100  1.000 61.69424 ? 395 ASN A O      1 
ATOM   2751 C  CB     . ASN A 1 399 ? -34.15300 -23.39100 12.75900  1.000 29.83252 ? 395 ASN A CB     1 
ATOM   2752 C  CG     . ASN A 1 399 ? -35.12700 -22.22300 12.79600  1.000 33.35663 ? 395 ASN A CG     1 
ATOM   2753 O  OD1    . ASN A 1 399 ? -36.21200 -22.28800 12.20300  1.000 36.23066 ? 395 ASN A OD1    1 
ATOM   2754 N  ND2    . ASN A 1 399 ? -34.77700 -21.17400 13.53200  1.000 32.51179 ? 395 ASN A ND2    1 
ATOM   2755 N  N      . GLY A 1 400 ? -33.88300 -26.73800 12.95700  1.000 35.13053 ? 396 GLY A N      1 
ATOM   2756 C  CA     . GLY A 1 400 ? -33.35900 -28.06700 13.16700  1.000 27.52698 ? 396 GLY A CA     1 
ATOM   2757 C  C      . GLY A 1 400 ? -34.47800 -29.05300 12.90000  1.000 31.98015 ? 396 GLY A C      1 
ATOM   2758 O  O      . GLY A 1 400 ? -35.53900 -28.68900 12.38700  1.000 28.66396 ? 396 GLY A O      1 
ATOM   2759 N  N      . SER A 1 401 ? -34.27700 -30.31500 13.27500  1.000 27.28222 ? 397 SER A N      1 
ATOM   2760 C  CA     . SER A 1 401 ? -35.34700 -31.28000 13.03300  1.000 26.63740 ? 397 SER A CA     1 
ATOM   2761 C  C      . SER A 1 401 ? -36.61400 -30.94400 13.81400  1.000 29.78252 ? 397 SER A C      1 
ATOM   2762 O  O      . SER A 1 401 ? -37.69100 -31.43400 13.45700  1.000 27.01377 ? 397 SER A O      1 
ATOM   2763 C  CB     . SER A 1 401 ? -34.89100 -32.69700 13.39800  1.000 25.43463 ? 397 SER A CB     1 
ATOM   2764 O  OG     . SER A 1 401 ? -34.73000 -32.81400 14.80300  1.000 26.30579 ? 397 SER A OG     1 
ATOM   2765 N  N      . CYS A 1 402 ? -36.50700 -30.15900 14.89600  1.000 23.53440 ? 398 CYS A N      1 
ATOM   2766 C  CA     . CYS A 1 402 ? -37.69500 -29.62800 15.57500  1.000 30.30100 ? 398 CYS A CA     1 
ATOM   2767 C  C      . CYS A 1 402 ? -38.69200 -29.01300 14.59300  1.000 29.11665 ? 398 CYS A C      1 
ATOM   2768 O  O      . CYS A 1 402 ? -39.90500 -29.06700 14.81600  1.000 31.01161 ? 398 CYS A O      1 
ATOM   2769 C  CB     . CYS A 1 402 ? -37.30300 -28.63900 16.68000  1.000 31.65116 ? 398 CYS A CB     1 
ATOM   2770 S  SG     . CYS A 1 402 ? -36.35200 -27.21300 16.15200  1.000 40.82068 ? 398 CYS A SG     1 
ATOM   2771 N  N      . ILE A 1 403 ? -38.20400 -28.34700 13.54400  1.000 29.07191 ? 399 ILE A N      1 
ATOM   2772 C  CA     . ILE A 1 403 ? -39.13000 -27.79900 12.55500  1.000 27.85071 ? 399 ILE A CA     1 
ATOM   2773 C  C      . ILE A 1 403 ? -40.07300 -28.89200 12.07900  1.000 30.64841 ? 399 ILE A C      1 
ATOM   2774 O  O      . ILE A 1 403 ? -41.30200 -28.75000 12.13300  1.000 31.29849 ? 399 ILE A O      1 
ATOM   2775 C  CB     . ILE A 1 403 ? -38.37400 -27.18900 11.36100  1.000 26.00575 ? 399 ILE A CB     1 
ATOM   2776 C  CG1    . ILE A 1 403 ? -37.51000 -26.00600 11.79400  1.000 21.61049 ? 399 ILE A CG1    1 
ATOM   2777 C  CG2    . ILE A 1 403 ? -39.39200 -26.79000 10.28500  1.000 25.97680 ? 399 ILE A CG2    1 
ATOM   2778 C  CD1    . ILE A 1 403 ? -36.47300 -25.58900 10.75100  1.000 26.47159 ? 399 ILE A CD1    1 
ATOM   2779 N  N      . ASN A 1 404 ? -39.49900 -30.00500 11.59600  1.000 25.03721 ? 400 ASN A N      1 
ATOM   2780 C  CA     . ASN A 1 404 ? -40.31500 -31.08300 11.04900  1.000 29.90622 ? 400 ASN A CA     1 
ATOM   2781 C  C      . ASN A 1 404 ? -41.27500 -31.62800 12.09700  1.000 30.48787 ? 400 ASN A C      1 
ATOM   2782 O  O      . ASN A 1 404 ? -42.46500 -31.81400 11.82300  1.000 28.62448 ? 400 ASN A O      1 
ATOM   2783 C  CB     . ASN A 1 404 ? -39.42300 -32.20000 10.50800  1.000 27.32959 ? 400 ASN A CB     1 
ATOM   2784 C  CG     . ASN A 1 404 ? -38.42200 -31.70600 9.47700   1.000 35.79640 ? 400 ASN A CG     1 
ATOM   2785 O  OD1    . ASN A 1 404 ? -37.45500 -31.01700 9.80800   1.000 32.47495 ? 400 ASN A OD1    1 
ATOM   2786 N  ND2    . ASN A 1 404 ? -38.64700 -32.06700 8.21700   1.000 37.79927 ? 400 ASN A ND2    1 
ATOM   2787 N  N      . TRP A 1 405 ? -40.77500 -31.90100 13.31000  1.000 29.01927 ? 401 TRP A N      1 
ATOM   2788 C  CA     . TRP A 1 405 ? -41.64700 -32.47700 14.33900  1.000 30.87212 ? 401 TRP A CA     1 
ATOM   2789 C  C      . TRP A 1 405 ? -42.73200 -31.49700 14.76200  1.000 26.56634 ? 401 TRP A C      1 
ATOM   2790 O  O      . TRP A 1 405 ? -43.89100 -31.88200 14.92500  1.000 31.97752 ? 401 TRP A O      1 
ATOM   2791 C  CB     . TRP A 1 405 ? -40.82400 -32.92300 15.55000  1.000 30.26679 ? 401 TRP A CB     1 
ATOM   2792 C  CG     . TRP A 1 405 ? -39.83900 -33.97300 15.18300  1.000 33.46454 ? 401 TRP A CG     1 
ATOM   2793 C  CD1    . TRP A 1 405 ? -38.48100 -33.85500 15.17400  1.000 32.60128 ? 401 TRP A CD1    1 
ATOM   2794 C  CD2    . TRP A 1 405 ? -40.13200 -35.29700 14.72100  1.000 33.53034 ? 401 TRP A CD2    1 
ATOM   2795 N  NE1    . TRP A 1 405 ? -37.91000 -35.02400 14.74700  1.000 24.80824 ? 401 TRP A NE1    1 
ATOM   2796 C  CE2    . TRP A 1 405 ? -38.90000 -35.92800 14.46400  1.000 31.05899 ? 401 TRP A CE2    1 
ATOM   2797 C  CE3    . TRP A 1 405 ? -41.31700 -36.01200 14.50700  1.000 32.16701 ? 401 TRP A CE3    1 
ATOM   2798 C  CZ2    . TRP A 1 405 ? -38.81600 -37.23800 14.00800  1.000 34.63573 ? 401 TRP A CZ2    1 
ATOM   2799 C  CZ3    . TRP A 1 405 ? -41.23200 -37.31600 14.04800  1.000 35.79377 ? 401 TRP A CZ3    1 
ATOM   2800 C  CH2    . TRP A 1 405 ? -39.98700 -37.91400 13.80100  1.000 35.53847 ? 401 TRP A CH2    1 
ATOM   2801 N  N      . GLY A 1 406 ? -42.38000 -30.22600 14.95500  1.000 26.34790 ? 402 GLY A N      1 
ATOM   2802 C  CA     . GLY A 1 406 ? -43.38900 -29.26600 15.37800  1.000 32.86973 ? 402 GLY A CA     1 
ATOM   2803 C  C      . GLY A 1 406 ? -44.40300 -28.97300 14.28400  1.000 34.48835 ? 402 GLY A C      1 
ATOM   2804 O  O      . GLY A 1 406 ? -45.61800 -29.03100 14.50700  1.000 28.79556 ? 402 GLY A O      1 
ATOM   2805 N  N      . VAL A 1 407 ? -43.92000 -28.67900 13.07700  1.000 28.61133 ? 403 VAL A N      1 
ATOM   2806 C  CA     . VAL A 1 407 ? -44.82700 -28.32600 11.98800  1.000 26.50581 ? 403 VAL A CA     1 
ATOM   2807 C  C      . VAL A 1 407 ? -45.77400 -29.48000 11.68800  1.000 34.01460 ? 403 VAL A C      1 
ATOM   2808 O  O      . VAL A 1 407 ? -46.98500 -29.28100 11.51700  1.000 31.97225 ? 403 VAL A O      1 
ATOM   2809 C  CB     . VAL A 1 407 ? -44.01800 -27.91500 10.74300  1.000 22.86590 ? 403 VAL A CB     1 
ATOM   2810 C  CG1    . VAL A 1 407 ? -44.91000 -27.82700 9.50600   1.000 22.17634 ? 403 VAL A CG1    1 
ATOM   2811 C  CG2    . VAL A 1 407 ? -43.30300 -26.58500 11.00900  1.000 21.34466 ? 403 VAL A CG2    1 
ATOM   2812 N  N      . HIS A 1 408 ? -45.24800 -30.70700 11.66400  1.000 32.71971 ? 404 HIS A N      1 
ATOM   2813 C  CA     . HIS A 1 408 ? -46.04800 -31.83800 11.22000  1.000 27.59015 ? 404 HIS A CA     1 
ATOM   2814 C  C      . HIS A 1 408 ? -46.92000 -32.39200 12.33500  1.000 28.25339 ? 404 HIS A C      1 
ATOM   2815 O  O      . HIS A 1 408 ? -48.09900 -32.70300 12.11600  1.000 29.97728 ? 404 HIS A O      1 
ATOM   2816 C  CB     . HIS A 1 408 ? -45.15400 -32.95300 10.66700  1.000 27.33749 ? 404 HIS A CB     1 
ATOM   2817 C  CG     . HIS A 1 408 ? -45.92200 -33.99600 9.91000   1.000 32.81183 ? 404 HIS A CG     1 
ATOM   2818 N  ND1    . HIS A 1 408 ? -46.40700 -33.77800 8.64000   1.000 33.04607 ? 404 HIS A ND1    1 
ATOM   2819 C  CD2    . HIS A 1 408 ? -46.34300 -35.23700 10.26400  1.000 30.88528 ? 404 HIS A CD2    1 
ATOM   2820 C  CE1    . HIS A 1 408 ? -47.07300 -34.84900 8.23200   1.000 30.78001 ? 404 HIS A CE1    1 
ATOM   2821 N  NE2    . HIS A 1 408 ? -47.04900 -35.74700 9.20000   1.000 28.06389 ? 404 HIS A NE2    1 
ATOM   2822 N  N      . CYS A 1 409 ? -46.35400 -32.57100 13.52400  1.000 26.12682 ? 405 CYS A N      1 
ATOM   2823 C  CA     . CYS A 1 409 ? -47.01500 -33.39000 14.53600  1.000 31.81434 ? 405 CYS A CA     1 
ATOM   2824 C  C      . CYS A 1 409 ? -47.81500 -32.60400 15.55800  1.000 32.22228 ? 405 CYS A C      1 
ATOM   2825 O  O      . CYS A 1 409 ? -48.65800 -33.19000 16.23500  1.000 36.84389 ? 405 CYS A O      1 
ATOM   2826 C  CB     . CYS A 1 409 ? -45.97700 -34.24300 15.26600  1.000 32.40915 ? 405 CYS A CB     1 
ATOM   2827 S  SG     . CYS A 1 409 ? -45.19700 -35.43300 14.14700  1.000 38.34670 ? 405 CYS A SG     1 
ATOM   2828 N  N      . TYR A 1 410 ? -47.54300 -31.32400 15.73700  1.000 32.63023 ? 406 TYR A N      1 
ATOM   2829 C  CA     . TYR A 1 410 ? -48.23800 -30.54300 16.75100  1.000 30.50629 ? 406 TYR A CA     1 
ATOM   2830 C  C      . TYR A 1 410 ? -49.49400 -29.93900 16.14900  1.000 30.15888 ? 406 TYR A C      1 
ATOM   2831 O  O      . TYR A 1 410 ? -49.44400 -29.32200 15.08200  1.000 33.95407 ? 406 TYR A O      1 
ATOM   2832 C  CB     . TYR A 1 410 ? -47.33700 -29.43700 17.28900  1.000 33.03028 ? 406 TYR A CB     1 
ATOM   2833 C  CG     . TYR A 1 410 ? -47.91500 -28.67400 18.44900  1.000 31.62484 ? 406 TYR A CG     1 
ATOM   2834 C  CD1    . TYR A 1 410 ? -47.99100 -29.24700 19.70800  1.000 34.03303 ? 406 TYR A CD1    1 
ATOM   2835 C  CD2    . TYR A 1 410 ? -48.36700 -27.37400 18.29000  1.000 35.78324 ? 406 TYR A CD2    1 
ATOM   2836 C  CE1    . TYR A 1 410 ? -48.50600 -28.55100 20.77700  1.000 40.78910 ? 406 TYR A CE1    1 
ATOM   2837 C  CE2    . TYR A 1 410 ? -48.88600 -26.66600 19.35500  1.000 38.70201 ? 406 TYR A CE2    1 
ATOM   2838 C  CZ     . TYR A 1 410 ? -48.95000 -27.25700 20.59500  1.000 41.92871 ? 406 TYR A CZ     1 
ATOM   2839 O  OH     . TYR A 1 410 ? -49.47000 -26.55700 21.65700  1.000 47.50570 ? 406 TYR A OH     1 
ATOM   2840 N  N      . LEU A 1 411 ? -50.61200 -30.09800 16.83500  1.000 34.59099 ? 407 LEU A N      1 
ATOM   2841 C  CA     . LEU A 1 411 ? -51.86600 -29.53300 16.36900  1.000 34.11725 ? 407 LEU A CA     1 
ATOM   2842 C  C      . LEU A 1 411 ? -52.03700 -28.16500 17.01500  1.000 35.76745 ? 407 LEU A C      1 
ATOM   2843 O  O      . LEU A 1 411 ? -52.10300 -28.05300 18.24600  1.000 38.61252 ? 407 LEU A O      1 
ATOM   2844 C  CB     . LEU A 1 411 ? -53.03400 -30.45400 16.70800  1.000 35.69112 ? 407 LEU A CB     1 
ATOM   2845 C  CG     . LEU A 1 411 ? -54.28900 -30.21000 15.86800  1.000 44.45796 ? 407 LEU A CG     1 
ATOM   2846 C  CD1    . LEU A 1 411 ? -55.13900 -31.46600 15.77400  1.000 45.01856 ? 407 LEU A CD1    1 
ATOM   2847 C  CD2    . LEU A 1 411 ? -55.09200 -29.05800 16.44800  1.000 49.67438 ? 407 LEU A CD2    1 
ATOM   2848 N  N      . ALA A 1 412 ? -52.06600 -27.11700 16.22000  1.000 29.84568 ? 408 ALA A N      1 
ATOM   2849 C  CA     . ALA A 1 412 ? -52.22800 -25.79000 16.75000  1.000 33.09871 ? 408 ALA A CA     1 
ATOM   2850 C  C      . ALA A 1 412 ? -53.65200 -25.31900 16.66200  1.000 37.63346 ? 408 ALA A C      1 
ATOM   2851 O  O      . ALA A 1 412 ? -54.20000 -25.20400 15.62400  1.000 45.07646 ? 408 ALA A O      1 
ATOM   2852 C  CB     . ALA A 1 412 ? -51.31000 -24.81900 16.06100  1.000 36.05432 ? 408 ALA A CB     1 
ATOM   2853 N  N      . GLN A 1 413 ? -54.22200 -25.00200 17.78000  1.000 31.06951 ? 409 GLN A N      1 
ATOM   2854 C  CA     . GLN A 1 413 ? -55.57900 -24.58100 17.81400  1.000 45.94235 ? 409 GLN A CA     1 
ATOM   2855 C  C      . GLN A 1 413 ? -55.79400 -23.13200 18.06300  1.000 42.83145 ? 409 GLN A C      1 
ATOM   2856 O  O      . GLN A 1 413 ? -56.78900 -22.62100 17.69400  1.000 50.00863 ? 409 GLN A O      1 
ATOM   2857 C  CB     . GLN A 1 413 ? -56.31300 -25.32900 18.92300  1.000 47.31094 ? 409 GLN A CB     1 
ATOM   2858 C  CG     . GLN A 1 413 ? -56.31600 -26.82600 18.76700  1.000 69.25830 ? 409 GLN A CG     1 
ATOM   2859 C  CD     . GLN A 1 413 ? -56.47600 -27.59600 20.08200  1.000 71.77703 ? 409 GLN A CD     1 
ATOM   2860 O  OE1    . GLN A 1 413 ? -57.16000 -27.15900 20.99800  1.000 73.79306 ? 409 GLN A OE1    1 
ATOM   2861 N  NE2    . GLN A 1 413 ? -55.83700 -28.74500 20.16500  1.000 72.16918 ? 409 GLN A NE2    1 
ATOM   2862 N  N      . THR A 1 414 ? -54.86600 -22.48300 18.71100  1.000 37.89139 ? 410 THR A N      1 
ATOM   2863 C  CA     . THR A 1 414 ? -55.02700 -21.10800 19.10300  1.000 33.27504 ? 410 THR A CA     1 
ATOM   2864 C  C      . THR A 1 414 ? -54.35900 -20.13000 18.18000  1.000 30.52208 ? 410 THR A C      1 
ATOM   2865 O  O      . THR A 1 414 ? -53.29400 -20.36400 17.75500  1.000 34.09356 ? 410 THR A O      1 
ATOM   2866 C  CB     . THR A 1 414 ? -54.56100 -20.96500 20.55800  1.000 41.66289 ? 410 THR A CB     1 
ATOM   2867 O  OG1    . THR A 1 414 ? -55.47000 -21.65900 21.37100  1.000 48.42423 ? 410 THR A OG1    1 
ATOM   2868 C  CG2    . THR A 1 414 ? -54.55800 -19.56400 21.01500  1.000 47.38726 ? 410 THR A CG2    1 
ATOM   2869 N  N      . PRO A 1 415 ? -55.02300 -19.02400 17.86600  1.000 35.78324 ? 411 PRO A N      1 
ATOM   2870 C  CA     . PRO A 1 415 ? -54.43900 -18.05200 16.93000  1.000 32.87763 ? 411 PRO A CA     1 
ATOM   2871 C  C      . PRO A 1 415 ? -53.07600 -17.54700 17.37700  1.000 33.99881 ? 411 PRO A C      1 
ATOM   2872 O  O      . PRO A 1 415 ? -52.91500 -17.01900 18.47900  1.000 38.04140 ? 411 PRO A O      1 
ATOM   2873 C  CB     . PRO A 1 415 ? -55.47100 -16.91700 16.90100  1.000 34.97525 ? 411 PRO A CB     1 
ATOM   2874 C  CG     . PRO A 1 415 ? -56.73600 -17.54100 17.27800  1.000 42.53405 ? 411 PRO A CG     1 
ATOM   2875 C  CD     . PRO A 1 415 ? -56.41600 -18.68700 18.21800  1.000 37.96771 ? 411 PRO A CD     1 
ATOM   2876 N  N      . GLY A 1 416 ? -52.09900 -17.66700 16.48000  1.000 37.05707 ? 412 GLY A N      1 
ATOM   2877 C  CA     . GLY A 1 416 ? -50.77600 -17.13900 16.74300  1.000 27.85597 ? 412 GLY A CA     1 
ATOM   2878 C  C      . GLY A 1 416 ? -49.96200 -17.90300 17.76100  1.000 31.02477 ? 412 GLY A C      1 
ATOM   2879 O  O      . GLY A 1 416 ? -48.86600 -17.45200 18.11700  1.000 36.54649 ? 412 GLY A O      1 
ATOM   2880 N  N      . ALA A 1 417 ? -50.43800 -19.05500 18.23300  1.000 27.70595 ? 413 ALA A N      1 
ATOM   2881 C  CA     . ALA A 1 417 ? -49.74300 -19.77400 19.29100  1.000 28.46920 ? 413 ALA A CA     1 
ATOM   2882 C  C      . ALA A 1 417 ? -48.62500 -20.69000 18.78300  1.000 30.21152 ? 413 ALA A C      1 
ATOM   2883 O  O      . ALA A 1 417 ? -48.04000 -21.42900 19.57800  1.000 38.43092 ? 413 ALA A O      1 
ATOM   2884 C  CB     . ALA A 1 417 ? -50.74000 -20.59300 20.11600  1.000 25.13196 ? 413 ALA A CB     1 
ATOM   2885 N  N      . PHE A 1 418 ? -48.32700 -20.68700 17.49500  1.000 25.43989 ? 414 PHE A N      1 
ATOM   2886 C  CA     . PHE A 1 418 ? -47.20500 -21.45200 16.95200  1.000 26.30842 ? 414 PHE A CA     1 
ATOM   2887 C  C      . PHE A 1 418 ? -46.23100 -20.42500 16.39700  1.000 29.11928 ? 414 PHE A C      1 
ATOM   2888 O  O      . PHE A 1 418 ? -46.58800 -19.65600 15.49900  1.000 27.37960 ? 414 PHE A O      1 
ATOM   2889 C  CB     . PHE A 1 418 ? -47.66000 -22.45000 15.88400  1.000 27.05061 ? 414 PHE A CB     1 
ATOM   2890 C  CG     . PHE A 1 418 ? -46.57700 -23.39100 15.41500  1.000 29.61408 ? 414 PHE A CG     1 
ATOM   2891 C  CD1    . PHE A 1 418 ? -45.73900 -23.03900 14.36300  1.000 27.51909 ? 414 PHE A CD1    1 
ATOM   2892 C  CD2    . PHE A 1 418 ? -46.41600 -24.63800 16.01000  1.000 31.59853 ? 414 PHE A CD2    1 
ATOM   2893 C  CE1    . PHE A 1 418 ? -44.75500 -23.91700 13.91600  1.000 27.60594 ? 414 PHE A CE1    1 
ATOM   2894 C  CE2    . PHE A 1 418 ? -45.43700 -25.51000 15.58000  1.000 26.50055 ? 414 PHE A CE2    1 
ATOM   2895 C  CZ     . PHE A 1 418 ? -44.60000 -25.14700 14.52500  1.000 27.76649 ? 414 PHE A CZ     1 
ATOM   2896 N  N      . GLN A 1 419 ? -45.04600 -20.33700 17.00300  1.000 26.92428 ? 415 GLN A N      1 
ATOM   2897 C  CA     . GLN A 1 419 ? -44.08000 -19.28400 16.71400  1.000 24.43714 ? 415 GLN A CA     1 
ATOM   2898 C  C      . GLN A 1 419 ? -42.80300 -19.92100 16.17000  1.000 28.65344 ? 415 GLN A C      1 
ATOM   2899 O  O      . GLN A 1 419 ? -42.01700 -20.48700 16.93100  1.000 24.51347 ? 415 GLN A O      1 
ATOM   2900 C  CB     . GLN A 1 419 ? -43.78800 -18.46700 17.97700  1.000 27.76649 ? 415 GLN A CB     1 
ATOM   2901 C  CG     . GLN A 1 419 ? -44.94000 -17.61400 18.45500  1.000 28.75082 ? 415 GLN A CG     1 
ATOM   2902 C  CD     . GLN A 1 419 ? -45.17000 -16.43600 17.52400  1.000 37.05971 ? 415 GLN A CD     1 
ATOM   2903 O  OE1    . GLN A 1 419 ? -44.22400 -15.76500 17.11600  1.000 36.36225 ? 415 GLN A OE1    1 
ATOM   2904 N  NE2    . GLN A 1 419 ? -46.42000 -16.20500 17.15600  1.000 31.37481 ? 415 GLN A NE2    1 
ATOM   2905 N  N      . ILE A 1 420 ? -42.60300 -19.81600 14.88100  1.000 25.45568 ? 416 ILE A N      1 
ATOM   2906 C  CA     . ILE A 1 420 ? -41.44700 -20.36000 14.21200  1.000 25.43726 ? 416 ILE A CA     1 
ATOM   2907 C  C      . ILE A 1 420 ? -40.86500 -19.31400 13.26300  1.000 25.12406 ? 416 ILE A C      1 
ATOM   2908 O  O      . ILE A 1 420 ? -41.56800 -18.67000 12.55600  1.000 23.66336 ? 416 ILE A O      1 
ATOM   2909 C  CB     . ILE A 1 420 ? -41.78300 -21.69800 13.52500  1.000 26.37421 ? 416 ILE A CB     1 
ATOM   2910 C  CG1    . ILE A 1 420 ? -40.55700 -22.52900 13.24700  1.000 25.55570 ? 416 ILE A CG1    1 
ATOM   2911 C  CG2    . ILE A 1 420 ? -42.57400 -21.51500 12.26700  1.000 25.56096 ? 416 ILE A CG2    1 
ATOM   2912 C  CD1    . ILE A 1 420 ? -40.89400 -23.92000 12.80400  1.000 27.70069 ? 416 ILE A CD1    1 
ATOM   2913 N  N      . GLY A 1 421 ? -39.56100 -19.16100 13.30900  1.000 26.74531 ? 417 GLY A N      1 
ATOM   2914 C  CA     . GLY A 1 421 ? -38.84600 -18.19000 12.52400  1.000 22.97381 ? 417 GLY A CA     1 
ATOM   2915 C  C      . GLY A 1 421 ? -38.25000 -18.78100 11.28300  1.000 32.11964 ? 417 GLY A C      1 
ATOM   2916 O  O      . GLY A 1 421 ? -37.08700 -18.89700 11.19700  1.000 32.28019 ? 417 GLY A O      1 
ATOM   2917 N  N      . LEU A 1 422 ? -39.07700 -19.13500 10.32600  1.000 28.10863 ? 418 LEU A N      1 
ATOM   2918 C  CA     . LEU A 1 422 ? -38.61600 -19.77200 9.12700   1.000 28.55079 ? 418 LEU A CA     1 
ATOM   2919 C  C      . LEU A 1 422 ? -38.12100 -18.87100 8.03100   1.000 26.06365 ? 418 LEU A C      1 
ATOM   2920 O  O      . LEU A 1 422 ? -37.60200 -19.35200 7.10400   1.000 29.89832 ? 418 LEU A O      1 
ATOM   2921 C  CB     . LEU A 1 422 ? -39.68700 -20.69200 8.57100   1.000 32.36177 ? 418 LEU A CB     1 
ATOM   2922 C  CG     . LEU A 1 422 ? -40.04000 -21.88300 9.42700   1.000 29.48775 ? 418 LEU A CG     1 
ATOM   2923 C  CD1    . LEU A 1 422 ? -41.02500 -22.74300 8.70200   1.000 25.53990 ? 418 LEU A CD1    1 
ATOM   2924 C  CD2    . LEU A 1 422 ? -38.79800 -22.62300 9.81800   1.000 21.91315 ? 418 LEU A CD2    1 
ATOM   2925 N  N      . GLY A 1 423 ? -38.32600 -17.57300 8.14200   1.000 25.40568 ? 419 GLY A N      1 
ATOM   2926 C  CA     . GLY A 1 423 ? -37.81000 -16.67600 7.12800   1.000 25.57675 ? 419 GLY A CA     1 
ATOM   2927 C  C      . GLY A 1 423 ? -36.31800 -16.84700 6.94200   1.000 30.70895 ? 419 GLY A C      1 
ATOM   2928 O  O      . GLY A 1 423 ? -35.82900 -17.01900 5.82500   1.000 33.87775 ? 419 GLY A O      1 
ATOM   2929 N  N      . LEU A 1 424 ? -35.57000 -16.77800 8.04000   1.000 27.16642 ? 420 LEU A N      1 
ATOM   2930 C  CA     . LEU A 1 424 ? -34.14400 -17.02800 8.00900   1.000 27.77438 ? 420 LEU A CA     1 
ATOM   2931 C  C      . LEU A 1 424 ? -33.76200 -18.35900 8.64500   1.000 27.86650 ? 420 LEU A C      1 
ATOM   2932 O  O      . LEU A 1 424 ? -32.66500 -18.86200 8.37500   1.000 22.50007 ? 420 LEU A O      1 
ATOM   2933 C  CB     . LEU A 1 424 ? -33.40300 -15.88400 8.71100   1.000 28.40341 ? 420 LEU A CB     1 
ATOM   2934 C  CG     . LEU A 1 424 ? -31.96800 -15.63700 8.25800   1.000 32.39599 ? 420 LEU A CG     1 
ATOM   2935 C  CD1    . LEU A 1 424 ? -31.89700 -15.50300 6.73600   1.000 28.66133 ? 420 LEU A CD1    1 
ATOM   2936 C  CD2    . LEU A 1 424 ? -31.44500 -14.38800 8.93500   1.000 34.18305 ? 420 LEU A CD2    1 
ATOM   2937 N  N      . ALA A 1 425 ? -34.63800 -18.94000 9.47200   1.000 22.34478 ? 421 ALA A N      1 
ATOM   2938 C  CA     . ALA A 1 425 ? -34.39600 -20.25200 10.07800  1.000 24.17658 ? 421 ALA A CA     1 
ATOM   2939 C  C      . ALA A 1 425 ? -33.03800 -20.29800 10.78500  1.000 27.59015 ? 421 ALA A C      1 
ATOM   2940 O  O      . ALA A 1 425 ? -32.20500 -21.17600 10.54500  1.000 29.83779 ? 421 ALA A O      1 
ATOM   2941 C  CB     . ALA A 1 425 ? -34.50100 -21.35800 9.03100   1.000 20.25243 ? 421 ALA A CB     1 
ATOM   2942 N  N      . ALA A 1 426 ? -32.81200 -19.32400 11.65900  1.000 21.26571 ? 422 ALA A N      1 
ATOM   2943 C  CA     . ALA A 1 426 ? -31.56100 -19.23600 12.40200  1.000 23.18699 ? 422 ALA A CA     1 
ATOM   2944 C  C      . ALA A 1 426 ? -31.61700 -20.14300 13.62500  1.000 26.49265 ? 422 ALA A C      1 
ATOM   2945 O  O      . ALA A 1 426 ? -32.51100 -20.00600 14.46100  1.000 25.37936 ? 422 ALA A O      1 
ATOM   2946 C  CB     . ALA A 1 426 ? -31.29300 -17.79500 12.83200  1.000 18.16270 ? 422 ALA A CB     1 
ATOM   2947 N  N      . MET A 1 427 ? -30.65000 -21.04000 13.75300  1.000 25.09248 ? 423 MET A N      1 
ATOM   2948 C  CA     . MET A 1 427 ? -30.57200 -21.84300 14.96400  1.000 29.53512 ? 423 MET A CA     1 
ATOM   2949 C  C      . MET A 1 427 ? -30.43000 -20.94600 16.18100  1.000 27.76649 ? 423 MET A C      1 
ATOM   2950 O  O      . MET A 1 427 ? -29.67000 -19.97500 16.16800  1.000 25.99259 ? 423 MET A O      1 
ATOM   2951 C  CB     . MET A 1 427 ? -29.38600 -22.79400 14.89000  1.000 30.74579 ? 423 MET A CB     1 
ATOM   2952 C  CG     . MET A 1 427 ? -29.59800 -23.95900 13.95500  1.000 33.94091 ? 423 MET A CG     1 
ATOM   2953 S  SD     . MET A 1 427 ? -28.00800 -24.74500 13.62100  1.000 36.62281 ? 423 MET A SD     1 
ATOM   2954 C  CE     . MET A 1 427 ? -27.50700 -25.18000 15.31300  1.000 29.23245 ? 423 MET A CE     1 
ATOM   2955 N  N      . GLY A 1 428 ? -31.16500 -21.27400 17.24300  1.000 29.04559 ? 424 GLY A N      1 
ATOM   2956 C  CA     . GLY A 1 428 ? -31.09200 -20.52500 18.47800  1.000 27.51909 ? 424 GLY A CA     1 
ATOM   2957 C  C      . GLY A 1 428 ? -32.11400 -19.42400 18.61100  1.000 30.97477 ? 424 GLY A C      1 
ATOM   2958 O  O      . GLY A 1 428 ? -32.30200 -18.91700 19.72500  1.000 26.18998 ? 424 GLY A O      1 
ATOM   2959 N  N      . HIS A 1 429 ? -32.77400 -19.04800 17.50800  1.000 23.38438 ? 425 HIS A N      1 
ATOM   2960 C  CA     . HIS A 1 429 ? -33.82600 -18.03500 17.51300  1.000 22.87906 ? 425 HIS A CA     1 
ATOM   2961 C  C      . HIS A 1 429 ? -34.88500 -18.33100 18.56900  1.000 29.68777 ? 425 HIS A C      1 
ATOM   2962 O  O      . HIS A 1 429 ? -35.17700 -17.49700 19.43800  1.000 25.73466 ? 425 HIS A O      1 
ATOM   2963 C  CB     . HIS A 1 429 ? -34.45900 -17.98600 16.11900  1.000 28.78503 ? 425 HIS A CB     1 
ATOM   2964 C  CG     . HIS A 1 429 ? -35.45700 -16.88900 15.93400  1.000 38.82308 ? 425 HIS A CG     1 
ATOM   2965 N  ND1    . HIS A 1 429 ? -35.95800 -16.54600 14.69500  1.000 40.42327 ? 425 HIS A ND1    1 
ATOM   2966 C  CD2    . HIS A 1 429 ? -36.05200 -16.05700 16.82300  1.000 39.99953 ? 425 HIS A CD2    1 
ATOM   2967 C  CE1    . HIS A 1 429 ? -36.81900 -15.55300 14.83100  1.000 39.20996 ? 425 HIS A CE1    1 
ATOM   2968 N  NE2    . HIS A 1 429 ? -36.90000 -15.24400 16.11300  1.000 36.13591 ? 425 HIS A NE2    1 
ATOM   2969 N  N      . ALA A 1 430 ? -35.48400 -19.52400 18.49800  1.000 26.22420 ? 426 ALA A N      1 
ATOM   2970 C  CA     . ALA A 1 430 ? -36.56600 -19.85700 19.42200  1.000 27.50593 ? 426 ALA A CA     1 
ATOM   2971 C  C      . ALA A 1 430 ? -36.05000 -19.95000 20.85100  1.000 24.23975 ? 426 ALA A C      1 
ATOM   2972 O  O      . ALA A 1 430 ? -36.74400 -19.55900 21.79500  1.000 26.35842 ? 426 ALA A O      1 
ATOM   2973 C  CB     . ALA A 1 430 ? -37.23400 -21.16600 19.00400  1.000 27.59805 ? 426 ALA A CB     1 
ATOM   2974 N  N      . VAL A 1 431 ? -34.82900 -20.45400 21.02300  1.000 25.74782 ? 427 VAL A N      1 
ATOM   2975 C  CA     . VAL A 1 431 ? -34.23600 -20.56500 22.35700  1.000 32.08806 ? 427 VAL A CA     1 
ATOM   2976 C  C      . VAL A 1 431 ? -34.37300 -19.24500 23.09800  1.000 30.62999 ? 427 VAL A C      1 
ATOM   2977 O  O      . VAL A 1 431 ? -34.75900 -19.20000 24.26900  1.000 35.50163 ? 427 VAL A O      1 
ATOM   2978 C  CB     . VAL A 1 431 ? -32.75800 -20.99000 22.25200  1.000 30.28521 ? 427 VAL A CB     1 
ATOM   2979 C  CG1    . VAL A 1 431 ? -32.06300 -20.86300 23.59500  1.000 26.86638 ? 427 VAL A CG1    1 
ATOM   2980 C  CG2    . VAL A 1 431 ? -32.63900 -22.40500 21.68000  1.000 28.45604 ? 427 VAL A CG2    1 
ATOM   2981 N  N      . ALA A 1 432 ? -34.05200 -18.14900 22.42000  1.000 31.53010 ? 428 ALA A N      1 
ATOM   2982 C  CA     . ALA A 1 432 ? -34.11400 -16.82400 23.02800  1.000 29.03769 ? 428 ALA A CA     1 
ATOM   2983 C  C      . ALA A 1 432 ? -35.45400 -16.13200 22.79900  1.000 27.71648 ? 428 ALA A C      1 
ATOM   2984 O  O      . ALA A 1 432 ? -35.98300 -15.48200 23.71200  1.000 30.73263 ? 428 ALA A O      1 
ATOM   2985 C  CB     . ALA A 1 432 ? -32.97700 -15.95500 22.47900  1.000 23.97656 ? 428 ALA A CB     1 
ATOM   2986 N  N      . ALA A 1 433 ? -36.03100 -16.25700 21.60400  1.000 22.25530 ? 429 ALA A N      1 
ATOM   2987 C  CA     . ALA A 1 433 ? -37.26700 -15.52100 21.34900  1.000 20.96567 ? 429 ALA A CA     1 
ATOM   2988 C  C      . ALA A 1 433 ? -38.34300 -15.87400 22.36800  1.000 22.89485 ? 429 ALA A C      1 
ATOM   2989 O  O      . ALA A 1 433 ? -39.14000 -15.00900 22.74600  1.000 24.40293 ? 429 ALA A O      1 
ATOM   2990 C  CB     . ALA A 1 433 ? -37.76100 -15.77300 19.91800  1.000 25.77677 ? 429 ALA A CB     1 
ATOM   2991 N  N      . ALA A 1 434 ? -38.35200 -17.12100 22.86600  1.000 22.68430 ? 430 ALA A N      1 
ATOM   2992 C  CA     . ALA A 1 434 ? -39.39100 -17.53500 23.81400  1.000 26.67951 ? 430 ALA A CA     1 
ATOM   2993 C  C      . ALA A 1 434 ? -39.41100 -16.66000 25.05700  1.000 26.91639 ? 430 ALA A C      1 
ATOM   2994 O  O      . ALA A 1 434 ? -40.46700 -16.47500 25.66900  1.000 25.40568 ? 430 ALA A O      1 
ATOM   2995 C  CB     . ALA A 1 434 ? -39.19300 -18.99500 24.22900  1.000 22.40269 ? 430 ALA A CB     1 
ATOM   2996 N  N      . ILE A 1 435 ? -38.26000 -16.12500 25.46100  1.000 26.09787 ? 431 ILE A N      1 
ATOM   2997 C  CA     . ILE A 1 435 ? -38.24500 -15.27000 26.64000  1.000 26.15577 ? 431 ILE A CA     1 
ATOM   2998 C  C      . ILE A 1 435 ? -38.98300 -13.96900 26.35800  1.000 31.36429 ? 431 ILE A C      1 
ATOM   2999 O  O      . ILE A 1 435 ? -39.77700 -13.49600 27.18400  1.000 28.06126 ? 431 ILE A O      1 
ATOM   3000 C  CB     . ILE A 1 435 ? -36.79500 -15.02900 27.10000  1.000 27.52962 ? 431 ILE A CB     1 
ATOM   3001 C  CG1    . ILE A 1 435 ? -36.17300 -16.35900 27.52800  1.000 22.11581 ? 431 ILE A CG1    1 
ATOM   3002 C  CG2    . ILE A 1 435 ? -36.75700 -14.00300 28.23400  1.000 26.84532 ? 431 ILE A CG2    1 
ATOM   3003 C  CD1    . ILE A 1 435 ? -34.65800 -16.30800 27.76900  1.000 21.73682 ? 431 ILE A CD1    1 
ATOM   3004 N  N      . GLY A 1 436 ? -38.74900 -13.36800 25.18800  1.000 26.05576 ? 432 GLY A N      1 
ATOM   3005 C  CA     . GLY A 1 436 ? -39.51900 -12.18400 24.83900  1.000 20.34454 ? 432 GLY A CA     1 
ATOM   3006 C  C      . GLY A 1 436 ? -41.00000 -12.48700 24.72000  1.000 22.87380 ? 432 GLY A C      1 
ATOM   3007 O  O      . GLY A 1 436 ? -41.84600 -11.69700 25.15000  1.000 26.36632 ? 432 GLY A O      1 
ATOM   3008 N  N      . GLY A 1 437 ? -41.33700 -13.65200 24.16300  1.000 22.20793 ? 433 GLY A N      1 
ATOM   3009 C  CA     . GLY A 1 437 ? -42.73800 -14.02400 24.07400  1.000 24.61611 ? 433 GLY A CA     1 
ATOM   3010 C  C      . GLY A 1 437 ? -43.40500 -14.09500 25.43700  1.000 30.54577 ? 433 GLY A C      1 
ATOM   3011 O  O      . GLY A 1 437 ? -44.53200 -13.61700 25.61300  1.000 27.79807 ? 433 GLY A O      1 
ATOM   3012 N  N      . LYS A 1 438 ? -42.71700 -14.67800 26.42500  1.000 21.15517 ? 434 LYS A N      1 
ATOM   3013 C  CA     . LYS A 1 438 ? -43.32100 -14.78700 27.75200  1.000 24.88193 ? 434 LYS A CA     1 
ATOM   3014 C  C      . LYS A 1 438 ? -43.53400 -13.41100 28.36400  1.000 27.20063 ? 434 LYS A C      1 
ATOM   3015 O  O      . LYS A 1 438 ? -44.56000 -13.16500 29.01100  1.000 28.84556 ? 434 LYS A O      1 
ATOM   3016 C  CB     . LYS A 1 438 ? -42.46800 -15.66500 28.66700  1.000 22.03159 ? 434 LYS A CB     1 
ATOM   3017 C  CG     . LYS A 1 438 ? -43.07700 -15.90400 30.07600  1.000 26.06892 ? 434 LYS A CG     1 
ATOM   3018 C  CD     . LYS A 1 438 ? -44.30100 -16.83100 30.01800  1.000 24.35292 ? 434 LYS A CD     1 
ATOM   3019 C  CE     . LYS A 1 438 ? -44.96400 -16.98500 31.38100  1.000 28.24023 ? 434 LYS A CE     1 
ATOM   3020 N  NZ     . LYS A 1 438 ? -45.80600 -18.20200 31.40300  1.000 31.70117 ? 434 LYS A NZ     1 
ATOM   3021 N  N      . LEU A 1 439 ? -42.58900 -12.48800 28.15100  1.000 27.36644 ? 435 LEU A N      1 
ATOM   3022 C  CA     . LEU A 1 439 ? -42.77000 -11.13900 28.67600  1.000 25.29777 ? 435 LEU A CA     1 
ATOM   3023 C  C      . LEU A 1 439 ? -43.94300 -10.43200 28.00500  1.000 31.85119 ? 435 LEU A C      1 
ATOM   3024 O  O      . LEU A 1 439 ? -44.60200 -9.58900  28.62800  1.000 27.16115 ? 435 LEU A O      1 
ATOM   3025 C  CB     . LEU A 1 439 ? -41.47900 -10.34000 28.49700  1.000 21.48942 ? 435 LEU A CB     1 
ATOM   3026 C  CG     . LEU A 1 439 ? -40.33900 -10.75300 29.44100  1.000 27.21116 ? 435 LEU A CG     1 
ATOM   3027 C  CD1    . LEU A 1 439 ? -39.09500 -9.98400  29.12100  1.000 25.40305 ? 435 LEU A CD1    1 
ATOM   3028 C  CD2    . LEU A 1 439 ? -40.72700 -10.55700 30.92000  1.000 22.42900 ? 435 LEU A CD2    1 
ATOM   3029 N  N      . ALA A 1 440 ? -44.23800 -10.79100 26.75500  1.000 24.19501 ? 436 ALA A N      1 
ATOM   3030 C  CA     . ALA A 1 440 ? -45.35200 -10.19900 26.03300  1.000 25.64518 ? 436 ALA A CA     1 
ATOM   3031 C  C      . ALA A 1 440 ? -46.68700 -10.79400 26.46900  1.000 35.72797 ? 436 ALA A C      1 
ATOM   3032 O  O      . ALA A 1 440 ? -47.71100 -10.10100 26.45300  1.000 32.56443 ? 436 ALA A O      1 
ATOM   3033 C  CB     . ALA A 1 440 ? -45.14600 -10.39700 24.52600  1.000 24.18185 ? 436 ALA A CB     1 
ATOM   3034 N  N      . ALA A 1 441 ? -46.68800 -12.04600 26.91600  1.000 30.49576 ? 437 ALA A N      1 
ATOM   3035 C  CA     . ALA A 1 441 ? -47.90900 -12.74300 27.31200  1.000 30.77474 ? 437 ALA A CA     1 
ATOM   3036 C  C      . ALA A 1 441 ? -47.66300 -13.44400 28.63900  1.000 29.34562 ? 437 ALA A C      1 
ATOM   3037 O  O      . ALA A 1 441 ? -47.63200 -14.67900 28.70900  1.000 33.40664 ? 437 ALA A O      1 
ATOM   3038 C  CB     . ALA A 1 441 ? -48.33300 -13.74100 26.23500  1.000 32.32756 ? 437 ALA A CB     1 
ATOM   3039 N  N      . PRO A 1 442 ? -47.48800 -12.68400 29.72400  1.000 33.62508 ? 438 PRO A N      1 
ATOM   3040 C  CA     . PRO A 1 442 ? -47.03600 -13.31100 30.98100  1.000 32.94079 ? 438 PRO A CA     1 
ATOM   3041 C  C      . PRO A 1 442 ? -48.05900 -14.23800 31.59600  1.000 33.13818 ? 438 PRO A C      1 
ATOM   3042 O  O      . PRO A 1 442 ? -47.68600 -15.11000 32.39000  1.000 37.64136 ? 438 PRO A O      1 
ATOM   3043 C  CB     . PRO A 1 442 ? -46.75100 -12.11000 31.89700  1.000 37.77821 ? 438 PRO A CB     1 
ATOM   3044 C  CG     . PRO A 1 442 ? -47.59500 -11.00600 31.34900  1.000 36.18592 ? 438 PRO A CG     1 
ATOM   3045 C  CD     . PRO A 1 442 ? -47.69100 -11.23200 29.85600  1.000 29.82200 ? 438 PRO A CD     1 
ATOM   3046 N  N      . ASP A 1 443 ? -49.32800 -14.08000 31.25600  1.000 26.41896 ? 439 ASP A N      1 
ATOM   3047 C  CA     . ASP A 1 443 ? -50.40100 -14.92700 31.76400  1.000 38.63621 ? 439 ASP A CA     1 
ATOM   3048 C  C      . ASP A 1 443 ? -50.54200 -16.23600 30.99600  1.000 38.80202 ? 439 ASP A C      1 
ATOM   3049 O  O      . ASP A 1 443 ? -51.45500 -17.00000 31.29500  1.000 40.74173 ? 439 ASP A O      1 
ATOM   3050 C  CB     . ASP A 1 443 ? -51.73200 -14.16900 31.73900  1.000 40.05217 ? 439 ASP A CB     1 
ATOM   3051 C  CG     . ASP A 1 443 ? -51.99700 -13.49300 30.39200  1.000 56.85155 ? 439 ASP A CG     1 
ATOM   3052 O  OD1    . ASP A 1 443 ? -51.02200 -13.21600 29.63200  1.000 46.36082 ? 439 ASP A OD1    1 
ATOM   3053 O  OD2    . ASP A 1 443 ? -53.18900 -13.23400 30.10100  1.000 62.97597 ? 439 ASP A OD2    1 
ATOM   3054 N  N      . ARG A 1 444 ? -49.73300 -16.47600 29.96700  1.000 40.53381 ? 440 ARG A N      1 
ATOM   3055 C  CA     . ARG A 1 444 ? -49.87300 -17.65900 29.13600  1.000 30.81159 ? 440 ARG A CA     1 
ATOM   3056 C  C      . ARG A 1 444 ? -48.65300 -18.56700 29.25000  1.000 35.15421 ? 440 ARG A C      1 
ATOM   3057 O  O      . ARG A 1 444 ? -47.52800 -18.08900 29.44000  1.000 35.06999 ? 440 ARG A O      1 
ATOM   3058 C  CB     . ARG A 1 444 ? -50.07600 -17.25600 27.67400  1.000 29.56670 ? 440 ARG A CB     1 
ATOM   3059 C  CG     . ARG A 1 444 ? -51.40300 -16.53400 27.47200  1.000 39.34682 ? 440 ARG A CG     1 
ATOM   3060 C  CD     . ARG A 1 444 ? -51.57000 -16.10000 26.05000  1.000 39.28103 ? 440 ARG A CD     1 
ATOM   3061 N  NE     . ARG A 1 444 ? -51.73000 -17.24700 25.17500  1.000 38.00982 ? 440 ARG A NE     1 
ATOM   3062 C  CZ     . ARG A 1 444 ? -51.89000 -17.14500 23.86600  1.000 36.52017 ? 440 ARG A CZ     1 
ATOM   3063 N  NH1    . ARG A 1 444 ? -51.92200 -15.94500 23.31100  1.000 41.39180 ? 440 ARG A NH1    1 
ATOM   3064 N  NH2    . ARG A 1 444 ? -52.01700 -18.23100 23.12000  1.000 37.49134 ? 440 ARG A NH2    1 
ATOM   3065 N  N      . PRO A 1 445 ? -48.84200 -19.88300 29.13700  1.000 33.69878 ? 441 PRO A N      1 
ATOM   3066 C  CA     . PRO A 1 445 ? -47.68900 -20.78700 29.14400  1.000 31.20901 ? 441 PRO A CA     1 
ATOM   3067 C  C      . PRO A 1 445 ? -46.89000 -20.59900 27.86900  1.000 31.06425 ? 441 PRO A C      1 
ATOM   3068 O  O      . PRO A 1 445 ? -47.45600 -20.44800 26.78000  1.000 28.59553 ? 441 PRO A O      1 
ATOM   3069 C  CB     . PRO A 1 445 ? -48.31900 -22.18700 29.19900  1.000 33.16713 ? 441 PRO A CB     1 
ATOM   3070 C  CG     . PRO A 1 445 ? -49.81000 -21.96100 29.37700  1.000 34.39360 ? 441 PRO A CG     1 
ATOM   3071 C  CD     . PRO A 1 445 ? -50.08800 -20.59700 28.83400  1.000 33.26715 ? 441 PRO A CD     1 
ATOM   3072 N  N      . VAL A 1 446 ? -45.56800 -20.58100 28.01400  1.000 27.15062 ? 442 VAL A N      1 
ATOM   3073 C  CA     . VAL A 1 446 ? -44.66200 -20.42600 26.87700  1.000 31.00635 ? 442 VAL A CA     1 
ATOM   3074 C  C      . VAL A 1 446 ? -43.65400 -21.56300 26.92900  1.000 29.56933 ? 442 VAL A C      1 
ATOM   3075 O  O      . VAL A 1 446 ? -42.98200 -21.75800 27.94800  1.000 26.45317 ? 442 VAL A O      1 
ATOM   3076 C  CB     . VAL A 1 446 ? -43.95700 -19.06000 26.85500  1.000 28.26655 ? 442 VAL A CB     1 
ATOM   3077 C  CG1    . VAL A 1 446 ? -42.91500 -19.02100 25.71300  1.000 26.42422 ? 442 VAL A CG1    1 
ATOM   3078 C  CG2    . VAL A 1 446 ? -44.99900 -17.94100 26.62800  1.000 21.78156 ? 442 VAL A CG2    1 
ATOM   3079 N  N      . VAL A 1 447 ? -43.57900 -22.32900 25.84300  1.000 30.62999 ? 443 VAL A N      1 
ATOM   3080 C  CA     . VAL A 1 447 ? -42.73900 -23.51500 25.74100  1.000 25.52148 ? 443 VAL A CA     1 
ATOM   3081 C  C      . VAL A 1 447 ? -41.94200 -23.41900 24.44800  1.000 28.83767 ? 443 VAL A C      1 
ATOM   3082 O  O      . VAL A 1 447 ? -42.44400 -22.93400 23.42500  1.000 26.44264 ? 443 VAL A O      1 
ATOM   3083 C  CB     . VAL A 1 447 ? -43.58700 -24.80500 25.78100  1.000 30.86423 ? 443 VAL A CB     1 
ATOM   3084 C  CG1    . VAL A 1 447 ? -42.71200 -26.05300 25.59900  1.000 29.57723 ? 443 VAL A CG1    1 
ATOM   3085 C  CG2    . VAL A 1 447 ? -44.37700 -24.87500 27.09400  1.000 24.71349 ? 443 VAL A CG2    1 
ATOM   3086 N  N      . ALA A 1 448 ? -40.68300 -23.83800 24.50400  1.000 24.58189 ? 444 ALA A N      1 
ATOM   3087 C  CA     . ALA A 1 448 ? -39.80600 -23.80800 23.34800  1.000 26.00312 ? 444 ALA A CA     1 
ATOM   3088 C  C      . ALA A 1 448 ? -39.31300 -25.21500 23.05600  1.000 28.23233 ? 444 ALA A C      1 
ATOM   3089 O  O      . ALA A 1 448 ? -38.79900 -25.89600 23.94700  1.000 33.33821 ? 444 ALA A O      1 
ATOM   3090 C  CB     . ALA A 1 448 ? -38.63000 -22.85900 23.58400  1.000 26.57161 ? 444 ALA A CB     1 
ATOM   3091 N  N      . LEU A 1 449 ? -39.45900 -25.64400 21.81500  1.000 26.18735 ? 445 LEU A N      1 
ATOM   3092 C  CA     . LEU A 1 449 ? -38.99000 -26.95000 21.37300  1.000 30.22994 ? 445 LEU A CA     1 
ATOM   3093 C  C      . LEU A 1 449 ? -37.75800 -26.70800 20.50200  1.000 29.84305 ? 445 LEU A C      1 
ATOM   3094 O  O      . LEU A 1 449 ? -37.86800 -26.12000 19.42400  1.000 26.46633 ? 445 LEU A O      1 
ATOM   3095 C  CB     . LEU A 1 449 ? -40.10300 -27.67300 20.61700  1.000 30.42470 ? 445 LEU A CB     1 
ATOM   3096 C  CG     . LEU A 1 449 ? -39.78900 -29.07000 20.09900  1.000 33.60403 ? 445 LEU A CG     1 
ATOM   3097 C  CD1    . LEU A 1 449 ? -39.64600 -30.02000 21.27500  1.000 24.16606 ? 445 LEU A CD1    1 
ATOM   3098 C  CD2    . LEU A 1 449 ? -40.89400 -29.51400 19.14900  1.000 31.64327 ? 445 LEU A CD2    1 
ATOM   3099 N  N      . VAL A 1 450 ? -36.59000 -27.16400 20.96600  1.000 21.32887 ? 446 VAL A N      1 
ATOM   3100 C  CA     . VAL A 1 450 ? -35.30700 -26.78100 20.39000  1.000 21.93421 ? 446 VAL A CA     1 
ATOM   3101 C  C      . VAL A 1 450 ? -34.36000 -27.97600 20.35700  1.000 26.12682 ? 446 VAL A C      1 
ATOM   3102 O  O      . VAL A 1 450 ? -34.45800 -28.90200 21.17200  1.000 24.82666 ? 446 VAL A O      1 
ATOM   3103 C  CB     . VAL A 1 450 ? -34.65800 -25.63500 21.20200  1.000 27.24537 ? 446 VAL A CB     1 
ATOM   3104 C  CG1    . VAL A 1 450 ? -35.66600 -24.50800 21.45300  1.000 27.69806 ? 446 VAL A CG1    1 
ATOM   3105 C  CG2    . VAL A 1 450 ? -34.15800 -26.17300 22.51500  1.000 29.79041 ? 446 VAL A CG2    1 
ATOM   3106 N  N      . GLY A 1 451 ? -33.42000 -27.93600 19.41300  1.000 23.77653 ? 447 GLY A N      1 
ATOM   3107 C  CA     . GLY A 1 451 ? -32.36500 -28.92800 19.34200  1.000 27.46382 ? 447 GLY A CA     1 
ATOM   3108 C  C      . GLY A 1 451 ? -31.17400 -28.59500 20.24200  1.000 31.11162 ? 447 GLY A C      1 
ATOM   3109 O  O      . GLY A 1 451 ? -31.00300 -27.47500 20.73800  1.000 28.04810 ? 447 GLY A O      1 
ATOM   3110 N  N      . ASP A 1 452 ? -30.31700 -29.59800 20.44500  1.000 27.70332 ? 448 ASP A N      1 
ATOM   3111 C  CA     . ASP A 1 452 ? -29.18200 -29.40700 21.34100  1.000 27.36907 ? 448 ASP A CA     1 
ATOM   3112 C  C      . ASP A 1 452 ? -28.12300 -28.48500 20.73100  1.000 31.94594 ? 448 ASP A C      1 
ATOM   3113 O  O      . ASP A 1 452 ? -27.54200 -27.64800 21.43700  1.000 23.83180 ? 448 ASP A O      1 
ATOM   3114 C  CB     . ASP A 1 452 ? -28.58500 -30.76100 21.73400  1.000 28.11916 ? 448 ASP A CB     1 
ATOM   3115 C  CG     . ASP A 1 452 ? -28.14400 -31.60300 20.52800  1.000 34.67521 ? 448 ASP A CG     1 
ATOM   3116 O  OD1    . ASP A 1 452 ? -28.91300 -31.74600 19.54600  1.000 27.70595 ? 448 ASP A OD1    1 
ATOM   3117 O  OD2    . ASP A 1 452 ? -27.02100 -32.15100 20.58900  1.000 32.67497 ? 448 ASP A OD2    1 
ATOM   3118 N  N      . ALA A 1 453 ? -27.86200 -28.59200 19.42600  1.000 26.96902 ? 449 ALA A N      1 
ATOM   3119 C  CA     . ALA A 1 453 ? -26.90400 -27.65600 18.82900  1.000 28.41130 ? 449 ALA A CA     1 
ATOM   3120 C  C      . ALA A 1 453 ? -27.43500 -26.22400 18.86600  1.000 27.35065 ? 449 ALA A C      1 
ATOM   3121 O  O      . ALA A 1 453 ? -26.68100 -25.28300 19.12700  1.000 25.49779 ? 449 ALA A O      1 
ATOM   3122 C  CB     . ALA A 1 453 ? -26.55600 -28.06500 17.39700  1.000 20.72880 ? 449 ALA A CB     1 
ATOM   3123 N  N      . ALA A 1 454 ? -28.72800 -26.02600 18.60400  1.000 27.27695 ? 450 ALA A N      1 
ATOM   3124 C  CA     . ALA A 1 454 ? -29.26400 -24.67300 18.70500  1.000 22.50533 ? 450 ALA A CA     1 
ATOM   3125 C  C      . ALA A 1 454 ? -29.18100 -24.16400 20.14000  1.000 30.60104 ? 450 ALA A C      1 
ATOM   3126 O  O      . ALA A 1 454 ? -28.88800 -22.98700 20.37800  1.000 29.40879 ? 450 ALA A O      1 
ATOM   3127 C  CB     . ALA A 1 454 ? -30.69900 -24.63800 18.20100  1.000 25.58728 ? 450 ALA A CB     1 
ATOM   3128 N  N      . PHE A 1 455 ? -29.40900 -25.04000 21.11800  1.000 27.44803 ? 451 PHE A N      1 
ATOM   3129 C  CA     . PHE A 1 455 ? -29.29200 -24.59400 22.49900  1.000 32.32756 ? 451 PHE A CA     1 
ATOM   3130 C  C      . PHE A 1 455 ? -27.84900 -24.26900 22.85900  1.000 35.94115 ? 451 PHE A C      1 
ATOM   3131 O  O      . PHE A 1 455 ? -27.61500 -23.37700 23.67800  1.000 28.79029 ? 451 PHE A O      1 
ATOM   3132 C  CB     . PHE A 1 455 ? -29.85400 -25.63900 23.46900  1.000 32.85131 ? 451 PHE A CB     1 
ATOM   3133 C  CG     . PHE A 1 455 ? -30.18600 -25.07900 24.82700  1.000 24.97668 ? 451 PHE A CG     1 
ATOM   3134 C  CD1    . PHE A 1 455 ? -31.44100 -24.54900 25.08200  1.000 32.64076 ? 451 PHE A CD1    1 
ATOM   3135 C  CD2    . PHE A 1 455 ? -29.23700 -25.06300 25.83500  1.000 31.74854 ? 451 PHE A CD2    1 
ATOM   3136 C  CE1    . PHE A 1 455 ? -31.74900 -24.01700 26.32500  1.000 27.86913 ? 451 PHE A CE1    1 
ATOM   3137 C  CE2    . PHE A 1 455 ? -29.53200 -24.53800 27.08600  1.000 30.02465 ? 451 PHE A CE2    1 
ATOM   3138 C  CZ     . PHE A 1 455 ? -30.78500 -24.01000 27.32800  1.000 32.22228 ? 451 PHE A CZ     1 
ATOM   3139 N  N      . ALA A 1 456 ? -26.87100 -24.96900 22.26700  1.000 30.19309 ? 452 ALA A N      1 
ATOM   3140 C  CA     . ALA A 1 456 ? -25.47600 -24.59100 22.49600  1.000 35.55163 ? 452 ALA A CA     1 
ATOM   3141 C  C      . ALA A 1 456 ? -25.14600 -23.20900 21.94200  1.000 35.76745 ? 452 ALA A C      1 
ATOM   3142 O  O      . ALA A 1 456 ? -24.23600 -22.55400 22.45600  1.000 35.31476 ? 452 ALA A O      1 
ATOM   3143 C  CB     . ALA A 1 456 ? -24.52800 -25.62800 21.88600  1.000 28.04810 ? 452 ALA A CB     1 
ATOM   3144 N  N      . MET A 1 457 ? -25.89400 -22.72600 20.94200  1.000 34.91471 ? 453 MET A N      1 
ATOM   3145 C  CA     . MET A 1 457 ? -25.61000 -21.41100 20.37200  1.000 29.27983 ? 453 MET A CA     1 
ATOM   3146 C  C      . MET A 1 457 ? -26.14700 -20.26200 21.22300  1.000 31.05636 ? 453 MET A C      1 
ATOM   3147 O  O      . MET A 1 457 ? -25.49800 -19.21600 21.31600  1.000 32.53285 ? 453 MET A O      1 
ATOM   3148 C  CB     . MET A 1 457 ? -26.19400 -21.28300 18.96600  1.000 30.24836 ? 453 MET A CB     1 
ATOM   3149 C  CG     . MET A 1 457 ? -25.38900 -21.86300 17.87300  1.000 40.30483 ? 453 MET A CG     1 
ATOM   3150 S  SD     . MET A 1 457 ? -26.29200 -21.48200 16.38700  1.000 41.04703 ? 453 MET A SD     1 
ATOM   3151 C  CE     . MET A 1 457 ? -24.90900 -21.28300 15.29300  1.000 53.23533 ? 453 MET A CE     1 
ATOM   3152 N  N      . ASN A 1 458 ? -27.36100 -20.39100 21.79200  1.000 23.20541 ? 454 ASN A N      1 
ATOM   3153 C  CA     . ASN A 1 458 ? -27.96400 -19.26900 22.50800  1.000 29.76409 ? 454 ASN A CA     1 
ATOM   3154 C  C      . ASN A 1 458 ? -28.59700 -19.67900 23.83500  1.000 32.55390 ? 454 ASN A C      1 
ATOM   3155 O  O      . ASN A 1 458 ? -29.33500 -18.87300 24.42900  1.000 32.60128 ? 454 ASN A O      1 
ATOM   3156 C  CB     . ASN A 1 458 ? -29.01900 -18.56300 21.66000  1.000 30.64578 ? 454 ASN A CB     1 
ATOM   3157 C  CG     . ASN A 1 458 ? -28.42400 -17.86000 20.45700  1.000 36.98601 ? 454 ASN A CG     1 
ATOM   3158 O  OD1    . ASN A 1 458 ? -28.43700 -18.39600 19.35300  1.000 32.71971 ? 454 ASN A OD1    1 
ATOM   3159 N  ND2    . ASN A 1 458 ? -27.90600 -16.65200 20.66400  1.000 34.06724 ? 454 ASN A ND2    1 
ATOM   3160 N  N      . GLY A 1 459 ? -28.36200 -20.90900 24.29600  1.000 26.99534 ? 455 GLY A N      1 
ATOM   3161 C  CA     . GLY A 1 459 ? -28.99100 -21.39800 25.51000  1.000 25.42147 ? 455 GLY A CA     1 
ATOM   3162 C  C      . GLY A 1 459 ? -28.52700 -20.70200 26.76600  1.000 29.54038 ? 455 GLY A C      1 
ATOM   3163 O  O      . GLY A 1 459 ? -29.20300 -20.80800 27.79600  1.000 28.54290 ? 455 GLY A O      1 
ATOM   3164 N  N      . MET A 1 460 ? -27.38000 -20.00600 26.72000  1.000 27.97967 ? 456 MET A N      1 
ATOM   3165 C  CA     . MET A 1 460 ? -26.95900 -19.23400 27.88500  1.000 26.71373 ? 456 MET A CA     1 
ATOM   3166 C  C      . MET A 1 460 ? -28.03300 -18.24300 28.30500  1.000 30.29311 ? 456 MET A C      1 
ATOM   3167 O  O      . MET A 1 460 ? -28.06400 -17.84300 29.47400  1.000 29.54038 ? 456 MET A O      1 
ATOM   3168 C  CB     . MET A 1 460 ? -25.65200 -18.47900 27.61200  1.000 27.09535 ? 456 MET A CB     1 
ATOM   3169 C  CG     . MET A 1 460 ? -24.42900 -19.37200 27.49000  1.000 38.39408 ? 456 MET A CG     1 
ATOM   3170 S  SD     . MET A 1 460 ? -23.99400 -20.27100 29.00900  1.000 45.91603 ? 456 MET A SD     1 
ATOM   3171 C  CE     . MET A 1 460 ? -23.83700 -18.92300 30.16700  1.000 44.55271 ? 456 MET A CE     1 
ATOM   3172 N  N      . GLU A 1 461 ? -28.93800 -17.86300 27.39300  1.000 25.50569 ? 457 GLU A N      1 
ATOM   3173 C  CA     . GLU A 1 461 ? -29.98900 -16.91300 27.74500  1.000 26.37158 ? 457 GLU A CA     1 
ATOM   3174 C  C      . GLU A 1 461 ? -30.95400 -17.45600 28.79400  1.000 28.25602 ? 457 GLU A C      1 
ATOM   3175 O  O      . GLU A 1 461 ? -31.72900 -16.67200 29.35800  1.000 29.47722 ? 457 GLU A O      1 
ATOM   3176 C  CB     . GLU A 1 461 ? -30.79300 -16.49200 26.50400  1.000 30.55366 ? 457 GLU A CB     1 
ATOM   3177 C  CG     . GLU A 1 461 ? -30.01200 -15.68200 25.45300  1.000 36.30698 ? 457 GLU A CG     1 
ATOM   3178 C  CD     . GLU A 1 461 ? -29.35200 -14.42500 26.02400  1.000 31.78013 ? 457 GLU A CD     1 
ATOM   3179 O  OE1    . GLU A 1 461 ? -28.44900 -13.87800 25.36200  1.000 33.04607 ? 457 GLU A OE1    1 
ATOM   3180 O  OE2    . GLU A 1 461 ? -29.74000 -13.98300 27.12800  1.000 33.78563 ? 457 GLU A OE2    1 
ATOM   3181 N  N      . ILE A 1 462 ? -30.95600 -18.76300 29.08100  1.000 24.44767 ? 458 ILE A N      1 
ATOM   3182 C  CA     . ILE A 1 462 ? -31.83700 -19.19700 30.15800  1.000 30.96424 ? 458 ILE A CA     1 
ATOM   3183 C  C      . ILE A 1 462 ? -31.41200 -18.58700 31.49400  1.000 31.29323 ? 458 ILE A C      1 
ATOM   3184 O  O      . ILE A 1 462 ? -32.22000 -18.52600 32.42900  1.000 30.73526 ? 458 ILE A O      1 
ATOM   3185 C  CB     . ILE A 1 462 ? -31.93200 -20.73400 30.25200  1.000 32.23808 ? 458 ILE A CB     1 
ATOM   3186 C  CG1    . ILE A 1 462 ? -30.59900 -21.35300 30.69100  1.000 28.97716 ? 458 ILE A CG1    1 
ATOM   3187 C  CG2    . ILE A 1 462 ? -32.49600 -21.32200 28.94000  1.000 25.05564 ? 458 ILE A CG2    1 
ATOM   3188 C  CD1    . ILE A 1 462 ? -30.74200 -22.81000 31.11800  1.000 26.48739 ? 458 ILE A CD1    1 
ATOM   3189 N  N      . HIS A 1 463 ? -30.15900 -18.13200 31.61200  1.000 26.67951 ? 459 HIS A N      1 
ATOM   3190 C  CA     . HIS A 1 463 ? -29.76000 -17.39500 32.80900  1.000 30.36943 ? 459 HIS A CA     1 
ATOM   3191 C  C      . HIS A 1 463 ? -30.49600 -16.06800 32.90200  1.000 26.17419 ? 459 HIS A C      1 
ATOM   3192 O  O      . HIS A 1 463 ? -30.84500 -15.62400 34.00000  1.000 29.42721 ? 459 HIS A O      1 
ATOM   3193 C  CB     . HIS A 1 463 ? -28.24400 -17.16800 32.82500  1.000 28.66659 ? 459 HIS A CB     1 
ATOM   3194 C  CG     . HIS A 1 463 ? -27.74900 -16.46400 34.05200  1.000 28.27181 ? 459 HIS A CG     1 
ATOM   3195 N  ND1    . HIS A 1 463 ? -27.28800 -15.16400 34.02700  1.000 26.23736 ? 459 HIS A ND1    1 
ATOM   3196 C  CD2    . HIS A 1 463 ? -27.63900 -16.88000 35.33900  1.000 27.99283 ? 459 HIS A CD2    1 
ATOM   3197 C  CE1    . HIS A 1 463 ? -26.90800 -14.81300 35.24600  1.000 32.93290 ? 459 HIS A CE1    1 
ATOM   3198 N  NE2    . HIS A 1 463 ? -27.11900 -15.83200 36.06000  1.000 26.15577 ? 459 HIS A NE2    1 
ATOM   3199 N  N      . THR A 1 464 ? -30.76200 -15.43900 31.75800  1.000 28.56658 ? 460 THR A N      1 
ATOM   3200 C  CA     . THR A 1 464 ? -31.58300 -14.23600 31.73900  1.000 26.09260 ? 460 THR A CA     1 
ATOM   3201 C  C      . THR A 1 464 ? -32.98800 -14.51800 32.26700  1.000 29.06138 ? 460 THR A C      1 
ATOM   3202 O  O      . THR A 1 464 ? -33.54700 -13.71600 33.02300  1.000 26.55845 ? 460 THR A O      1 
ATOM   3203 C  CB     . THR A 1 464 ? -31.65700 -13.69300 30.31600  1.000 26.43475 ? 460 THR A CB     1 
ATOM   3204 O  OG1    . THR A 1 464 ? -30.33600 -13.38100 29.86200  1.000 26.07681 ? 460 THR A OG1    1 
ATOM   3205 C  CG2    . THR A 1 464 ? -32.54400 -12.45100 30.26100  1.000 26.36632 ? 460 THR A CG2    1 
ATOM   3206 N  N      . ALA A 1 465 ? -33.57900 -15.64700 31.85500  1.000 27.77965 ? 461 ALA A N      1 
ATOM   3207 C  CA     . ALA A 1 465 ? -34.88300 -16.03900 32.37600  1.000 30.39312 ? 461 ALA A CA     1 
ATOM   3208 C  C      . ALA A 1 465 ? -34.82700 -16.29900 33.88200  1.000 29.42721 ? 461 ALA A C      1 
ATOM   3209 O  O      . ALA A 1 465 ? -35.76700 -15.96100 34.60600  1.000 29.99044 ? 461 ALA A O      1 
ATOM   3210 C  CB     . ALA A 1 465 ? -35.39700 -17.27300 31.63300  1.000 30.67736 ? 461 ALA A CB     1 
ATOM   3211 N  N      . ALA A 1 466 ? -33.74600 -16.92600 34.36700  1.000 27.09009 ? 462 ALA A N      1 
ATOM   3212 C  CA     . ALA A 1 466 ? -33.60100 -17.14400 35.80600  1.000 30.79580 ? 462 ALA A CA     1 
ATOM   3213 C  C      . ALA A 1 466 ? -33.44400 -15.82000 36.55200  1.000 33.13555 ? 462 ALA A C      1 
ATOM   3214 O  O      . ALA A 1 466 ? -34.09200 -15.60200 37.58400  1.000 30.26415 ? 462 ALA A O      1 
ATOM   3215 C  CB     . ALA A 1 466 ? -32.41000 -18.06000 36.08400  1.000 23.92129 ? 462 ALA A CB     1 
ATOM   3216 N  N      . GLU A 1 467 ? -32.61100 -14.91600 36.01700  1.000 28.26392 ? 463 GLU A N      1 
ATOM   3217 C  CA     . GLU A 1 467 ? -32.35500 -13.62800 36.65900  1.000 24.79771 ? 463 GLU A CA     1 
ATOM   3218 C  C      . GLU A 1 467 ? -33.64400 -12.84900 36.87900  1.000 33.70667 ? 463 GLU A C      1 
ATOM   3219 O  O      . GLU A 1 467 ? -33.85100 -12.27300 37.94900  1.000 30.41944 ? 463 GLU A O      1 
ATOM   3220 C  CB     . GLU A 1 467 ? -31.39200 -12.80000 35.80200  1.000 28.75871 ? 463 GLU A CB     1 
ATOM   3221 C  CG     . GLU A 1 467 ? -29.92100 -13.19000 35.91600  1.000 30.06939 ? 463 GLU A CG     1 
ATOM   3222 C  CD     . GLU A 1 467 ? -29.31000 -12.75800 37.24500  1.000 40.16534 ? 463 GLU A CD     1 
ATOM   3223 O  OE1    . GLU A 1 467 ? -29.07800 -11.53900 37.43900  1.000 37.43870 ? 463 GLU A OE1    1 
ATOM   3224 O  OE2    . GLU A 1 467 ? -29.07600 -13.64300 38.09600  1.000 37.38606 ? 463 GLU A OE2    1 
ATOM   3225 N  N      . TYR A 1 468 ? -34.52900 -12.82500 35.88300  1.000 30.74842 ? 464 TYR A N      1 
ATOM   3226 C  CA     . TYR A 1 468 ? -35.76800 -12.07300 35.97900  1.000 27.69806 ? 464 TYR A CA     1 
ATOM   3227 C  C      . TYR A 1 468 ? -36.96400 -12.94700 36.33400  1.000 29.46932 ? 464 TYR A C      1 
ATOM   3228 O  O      . TYR A 1 468 ? -38.10200 -12.46500 36.30800  1.000 30.95371 ? 464 TYR A O      1 
ATOM   3229 C  CB     . TYR A 1 468 ? -36.02900 -11.34700 34.65800  1.000 33.67772 ? 464 TYR A CB     1 
ATOM   3230 C  CG     . TYR A 1 468 ? -35.03000 -10.24500 34.38800  1.000 31.46167 ? 464 TYR A CG     1 
ATOM   3231 C  CD1    . TYR A 1 468 ? -35.22600 -8.96200  34.89100  1.000 28.18233 ? 464 TYR A CD1    1 
ATOM   3232 C  CD2    . TYR A 1 468 ? -33.87900 -10.49700 33.64700  1.000 28.72713 ? 464 TYR A CD2    1 
ATOM   3233 C  CE1    . TYR A 1 468 ? -34.30000 -7.95600  34.64600  1.000 23.53703 ? 464 TYR A CE1    1 
ATOM   3234 C  CE2    . TYR A 1 468 ? -32.96300 -9.50700  33.38900  1.000 27.30064 ? 464 TYR A CE2    1 
ATOM   3235 C  CZ     . TYR A 1 468 ? -33.17100 -8.24200  33.89600  1.000 25.17933 ? 464 TYR A CZ     1 
ATOM   3236 O  OH     . TYR A 1 468 ? -32.24800 -7.26400  33.63400  1.000 26.55055 ? 464 TYR A OH     1 
ATOM   3237 N  N      . LYS A 1 469 ? -36.74100 -14.22200 36.63200  1.000 29.00611 ? 465 LYS A N      1 
ATOM   3238 C  CA     . LYS A 1 469 ? -37.82400 -15.11900 37.02000  1.000 32.78288 ? 465 LYS A CA     1 
ATOM   3239 C  C      . LYS A 1 469 ? -38.91100 -15.16900 35.94500  1.000 32.79341 ? 465 LYS A C      1 
ATOM   3240 O  O      . LYS A 1 469 ? -40.09200 -14.93000 36.20200  1.000 29.19297 ? 465 LYS A O      1 
ATOM   3241 C  CB     . LYS A 1 469 ? -38.40700 -14.71900 38.37700  1.000 31.11689 ? 465 LYS A CB     1 
ATOM   3242 C  CG     . LYS A 1 469 ? -39.09100 -15.87000 39.10800  1.000 46.53453 ? 465 LYS A CG     1 
ATOM   3243 C  CD     . LYS A 1 469 ? -39.50600 -15.48800 40.53500  1.000 53.98279 ? 465 LYS A CD     1 
ATOM   3244 C  CE     . LYS A 1 469 ? -40.63200 -16.39700 41.05600  1.000 55.87512 ? 465 LYS A CE     1 
ATOM   3245 N  NZ     . LYS A 1 469 ? -40.30700 -17.06500 42.34700  1.000 57.80693 ? 465 LYS A NZ     1 
ATOM   3246 N  N      . ILE A 1 470 ? -38.49800 -15.45400 34.71500  1.000 32.35914 ? 466 ILE A N      1 
ATOM   3247 C  CA     . ILE A 1 470 ? -39.41000 -15.52300 33.57800  1.000 29.89832 ? 466 ILE A CA     1 
ATOM   3248 C  C      . ILE A 1 470 ? -39.72400 -17.00100 33.33300  1.000 31.95120 ? 466 ILE A C      1 
ATOM   3249 O  O      . ILE A 1 470 ? -38.81600 -17.75800 32.95300  1.000 29.22719 ? 466 ILE A O      1 
ATOM   3250 C  CB     . ILE A 1 470 ? -38.81100 -14.85300 32.33800  1.000 32.68550 ? 466 ILE A CB     1 
ATOM   3251 C  CG1    . ILE A 1 470 ? -38.44600 -13.39600 32.67100  1.000 26.43738 ? 466 ILE A CG1    1 
ATOM   3252 C  CG2    . ILE A 1 470 ? -39.79800 -14.92000 31.16600  1.000 31.33534 ? 466 ILE A CG2    1 
ATOM   3253 C  CD1    . ILE A 1 470 ? -37.61000 -12.68700 31.62500  1.000 27.76122 ? 466 ILE A CD1    1 
ATOM   3254 N  N      . PRO A 1 471 ? -40.95200 -17.46400 33.60500  1.000 30.07203 ? 467 PRO A N      1 
ATOM   3255 C  CA     . PRO A 1 471 ? -41.23200 -18.90700 33.48800  1.000 31.70380 ? 467 PRO A CA     1 
ATOM   3256 C  C      . PRO A 1 471 ? -41.44600 -19.35000 32.04800  1.000 29.37194 ? 467 PRO A C      1 
ATOM   3257 O  O      . PRO A 1 471 ? -42.53100 -19.20600 31.47900  1.000 32.10122 ? 467 PRO A O      1 
ATOM   3258 C  CB     . PRO A 1 471 ? -42.50600 -19.10900 34.33400  1.000 34.48308 ? 467 PRO A CB     1 
ATOM   3259 C  CG     . PRO A 1 471 ? -42.83100 -17.76700 34.95700  1.000 36.47806 ? 467 PRO A CG     1 
ATOM   3260 C  CD     . PRO A 1 471 ? -42.05600 -16.70800 34.22500  1.000 31.55905 ? 467 PRO A CD     1 
ATOM   3261 N  N      . VAL A 1 472 ? -40.39100 -19.88500 31.44800  1.000 26.81637 ? 468 VAL A N      1 
ATOM   3262 C  CA     . VAL A 1 472 ? -40.44000 -20.48600 30.12400  1.000 27.83492 ? 468 VAL A CA     1 
ATOM   3263 C  C      . VAL A 1 472 ? -39.93500 -21.91400 30.27500  1.000 30.61683 ? 468 VAL A C      1 
ATOM   3264 O  O      . VAL A 1 472 ? -39.02700 -22.17500 31.07000  1.000 26.82164 ? 468 VAL A O      1 
ATOM   3265 C  CB     . VAL A 1 472 ? -39.57500 -19.69100 29.10800  1.000 27.64805 ? 468 VAL A CB     1 
ATOM   3266 C  CG1    . VAL A 1 472 ? -39.32000 -20.52400 27.87800  1.000 22.60008 ? 468 VAL A CG1    1 
ATOM   3267 C  CG2    . VAL A 1 472 ? -40.23500 -18.37600 28.72800  1.000 25.11354 ? 468 VAL A CG2    1 
ATOM   3268 N  N      . THR A 1 473 ? -40.48200 -22.83600 29.48400  1.000 28.54290 ? 469 THR A N      1 
ATOM   3269 C  CA     . THR A 1 473 ? -40.02500 -24.22200 29.50800  1.000 25.70835 ? 469 THR A CA     1 
ATOM   3270 C  C      . THR A 1 473 ? -39.31400 -24.54500 28.20200  1.000 31.59326 ? 469 THR A C      1 
ATOM   3271 O  O      . THR A 1 473 ? -39.91600 -24.45800 27.12300  1.000 27.96651 ? 469 THR A O      1 
ATOM   3272 C  CB     . THR A 1 473 ? -41.17800 -25.19500 29.71800  1.000 30.16677 ? 469 THR A CB     1 
ATOM   3273 O  OG1    . THR A 1 473 ? -41.83400 -24.90900 30.95900  1.000 29.11402 ? 469 THR A OG1    1 
ATOM   3274 C  CG2    . THR A 1 473 ? -40.64000 -26.61600 29.74000  1.000 24.85298 ? 469 THR A CG2    1 
ATOM   3275 N  N      . TRP A 1 474 ? -38.03600 -24.90700 28.29900  1.000 22.68693 ? 470 TRP A N      1 
ATOM   3276 C  CA     . TRP A 1 474 ? -37.29100 -25.38300 27.14300  1.000 26.92165 ? 470 TRP A CA     1 
ATOM   3277 C  C      . TRP A 1 474 ? -37.31900 -26.90700 27.09700  1.000 30.79580 ? 470 TRP A C      1 
ATOM   3278 O  O      . TRP A 1 474 ? -36.96600 -27.57400 28.07200  1.000 27.86124 ? 470 TRP A O      1 
ATOM   3279 C  CB     . TRP A 1 474 ? -35.84200 -24.88300 27.17400  1.000 21.96316 ? 470 TRP A CB     1 
ATOM   3280 C  CG     . TRP A 1 474 ? -35.70900 -23.41800 26.90300  1.000 23.74495 ? 470 TRP A CG     1 
ATOM   3281 C  CD1    . TRP A 1 474 ? -35.50400 -22.82100 25.69000  1.000 27.13483 ? 470 TRP A CD1    1 
ATOM   3282 C  CD2    . TRP A 1 474 ? -35.79000 -22.35500 27.86300  1.000 25.43463 ? 470 TRP A CD2    1 
ATOM   3283 N  NE1    . TRP A 1 474 ? -35.44200 -21.45300 25.83700  1.000 25.53990 ? 470 TRP A NE1    1 
ATOM   3284 C  CE2    . TRP A 1 474 ? -35.60800 -21.14000 27.15900  1.000 28.47183 ? 470 TRP A CE2    1 
ATOM   3285 C  CE3    . TRP A 1 474 ? -35.97500 -22.31100 29.24600  1.000 25.93995 ? 470 TRP A CE3    1 
ATOM   3286 C  CZ2    . TRP A 1 474 ? -35.63000 -19.89800 27.78900  1.000 27.61384 ? 470 TRP A CZ2    1 
ATOM   3287 C  CZ3    . TRP A 1 474 ? -35.99100 -21.07100 29.87100  1.000 26.27947 ? 470 TRP A CZ3    1 
ATOM   3288 C  CH2    . TRP A 1 474 ? -35.81900 -19.88500 29.14000  1.000 21.51574 ? 470 TRP A CH2    1 
ATOM   3289 N  N      . ILE A 1 475 ? -37.71400 -27.45100 25.95200  1.000 27.85071 ? 471 ILE A N      1 
ATOM   3290 C  CA     . ILE A 1 475 ? -37.63500 -28.88100 25.68500  1.000 25.89784 ? 471 ILE A CA     1 
ATOM   3291 C  C      . ILE A 1 475 ? -36.51300 -29.07400 24.67200  1.000 29.71146 ? 471 ILE A C      1 
ATOM   3292 O  O      . ILE A 1 475 ? -36.64600 -28.69700 23.50100  1.000 31.84329 ? 471 ILE A O      1 
ATOM   3293 C  CB     . ILE A 1 475 ? -38.96200 -29.43800 25.16100  1.000 26.32947 ? 471 ILE A CB     1 
ATOM   3294 C  CG1    . ILE A 1 475 ? -40.07600 -29.26400 26.20100  1.000 23.35280 ? 471 ILE A CG1    1 
ATOM   3295 C  CG2    . ILE A 1 475 ? -38.80900 -30.89600 24.77600  1.000 23.37386 ? 471 ILE A CG2    1 
ATOM   3296 C  CD1    . ILE A 1 475 ? -41.48400 -29.35800 25.58200  1.000 26.88217 ? 471 ILE A CD1    1 
ATOM   3297 N  N      . VAL A 1 476 ? -35.39800 -29.63900 25.11300  1.000 25.12406 ? 472 VAL A N      1 
ATOM   3298 C  CA     . VAL A 1 476 ? -34.23100 -29.80700 24.25500  1.000 25.97943 ? 472 VAL A CA     1 
ATOM   3299 C  C      . VAL A 1 476 ? -34.25400 -31.22200 23.70900  1.000 28.04547 ? 472 VAL A C      1 
ATOM   3300 O  O      . VAL A 1 476 ? -34.19400 -32.19100 24.47300  1.000 27.72701 ? 472 VAL A O      1 
ATOM   3301 C  CB     . VAL A 1 476 ? -32.91400 -29.52100 25.00100  1.000 25.28198 ? 472 VAL A CB     1 
ATOM   3302 C  CG1    . VAL A 1 476 ? -31.72700 -29.59000 24.01300  1.000 22.90538 ? 472 VAL A CG1    1 
ATOM   3303 C  CG2    . VAL A 1 476 ? -32.95900 -28.15200 25.64300  1.000 27.02956 ? 472 VAL A CG2    1 
ATOM   3304 N  N      . LEU A 1 477 ? -34.37900 -31.33600 22.38700  1.000 26.10050 ? 473 LEU A N      1 
ATOM   3305 C  CA     . LEU A 1 477 ? -34.23500 -32.61600 21.70000  1.000 24.55031 ? 473 LEU A CA     1 
ATOM   3306 C  C      . LEU A 1 477 ? -32.74200 -32.90200 21.61400  1.000 30.56945 ? 473 LEU A C      1 
ATOM   3307 O  O      . LEU A 1 477 ? -32.05000 -32.38700 20.73300  1.000 30.72737 ? 473 LEU A O      1 
ATOM   3308 C  CB     . LEU A 1 477 ? -34.88100 -32.56700 20.32400  1.000 26.36369 ? 473 LEU A CB     1 
ATOM   3309 C  CG     . LEU A 1 477 ? -36.37400 -32.21800 20.32800  1.000 30.06413 ? 473 LEU A CG     1 
ATOM   3310 C  CD1    . LEU A 1 477 ? -36.90600 -32.21600 18.93700  1.000 28.93768 ? 473 LEU A CD1    1 
ATOM   3311 C  CD2    . LEU A 1 477 ? -37.14100 -33.21400 21.20500  1.000 29.57986 ? 473 LEU A CD2    1 
ATOM   3312 N  N      . ASN A 1 478 ? -32.22800 -33.68600 22.56700  1.000 27.15062 ? 474 ASN A N      1 
ATOM   3313 C  CA     . ASN A 1 478 ? -30.78700 -33.92500 22.68600  1.000 29.19561 ? 474 ASN A CA     1 
ATOM   3314 C  C      . ASN A 1 478 ? -30.42500 -35.18800 21.90800  1.000 33.03028 ? 474 ASN A C      1 
ATOM   3315 O  O      . ASN A 1 478 ? -30.49200 -36.29800 22.42800  1.000 28.13495 ? 474 ASN A O      1 
ATOM   3316 C  CB     . ASN A 1 478 ? -30.39000 -34.03000 24.15200  1.000 29.21403 ? 474 ASN A CB     1 
ATOM   3317 C  CG     . ASN A 1 478 ? -28.88700 -34.07500 24.35700  1.000 33.43559 ? 474 ASN A CG     1 
ATOM   3318 O  OD1    . ASN A 1 478 ? -28.09800 -34.14800 23.40000  1.000 30.12203 ? 474 ASN A OD1    1 
ATOM   3319 N  ND2    . ASN A 1 478 ? -28.48000 -34.05300 25.61800  1.000 25.63728 ? 474 ASN A ND2    1 
ATOM   3320 N  N      . ASN A 1 479 ? -30.04700 -35.02500 20.63700  1.000 31.36692 ? 475 ASN A N      1 
ATOM   3321 C  CA     . ASN A 1 479 ? -29.58900 -36.15400 19.83700  1.000 25.77941 ? 475 ASN A CA     1 
ATOM   3322 C  C      . ASN A 1 479 ? -28.07200 -36.17100 19.66000  1.000 31.99857 ? 475 ASN A C      1 
ATOM   3323 O  O      . ASN A 1 479 ? -27.56500 -36.83700 18.74900  1.000 31.44061 ? 475 ASN A O      1 
ATOM   3324 C  CB     . ASN A 1 479 ? -30.30200 -36.17900 18.47600  1.000 24.74507 ? 475 ASN A CB     1 
ATOM   3325 C  CG     . ASN A 1 479 ? -30.23600 -34.84300 17.73100  1.000 33.36716 ? 475 ASN A CG     1 
ATOM   3326 O  OD1    . ASN A 1 479 ? -29.43900 -33.94700 18.05700  1.000 29.30088 ? 475 ASN A OD1    1 
ATOM   3327 N  ND2    . ASN A 1 479 ? -31.10100 -34.70100 16.72800  1.000 27.40329 ? 475 ASN A ND2    1 
ATOM   3328 N  N      . GLY A 1 480 ? -27.34100 -35.45500 20.51100  1.000 33.19872 ? 476 GLY A N      1 
ATOM   3329 C  CA     . GLY A 1 480 ? -25.88700 -35.47400 20.45900  1.000 26.33474 ? 476 GLY A CA     1 
ATOM   3330 C  C      . GLY A 1 480 ? -25.29900 -34.94800 19.16600  1.000 31.34323 ? 476 GLY A C      1 
ATOM   3331 O  O      . GLY A 1 480 ? -24.32600 -35.51800 18.66200  1.000 25.73993 ? 476 GLY A O      1 
ATOM   3332 N  N      . GLY A 1 481 ? -25.86000 -33.86700 18.61500  1.000 32.70655 ? 477 GLY A N      1 
ATOM   3333 C  CA     . GLY A 1 481 ? -25.26100 -33.23700 17.45600  1.000 29.54828 ? 477 GLY A CA     1 
ATOM   3334 C  C      . GLY A 1 481 ? -26.30600 -32.67500 16.50400  1.000 28.55342 ? 477 GLY A C      1 
ATOM   3335 O  O      . GLY A 1 481 ? -27.42500 -32.37000 16.89600  1.000 24.61611 ? 477 GLY A O      1 
ATOM   3336 N  N      . HIS A 1 482 ? -25.89400 -32.51300 15.24300  1.000 28.04020 ? 478 HIS A N      1 
ATOM   3337 C  CA     . HIS A 1 482 ? -26.65700 -31.80600 14.21200  1.000 26.46107 ? 478 HIS A CA     1 
ATOM   3338 C  C      . HIS A 1 482 ? -27.45400 -32.83300 13.40800  1.000 34.52256 ? 478 HIS A C      1 
ATOM   3339 O  O      . HIS A 1 482 ? -26.97800 -33.37300 12.40400  1.000 29.05348 ? 478 HIS A O      1 
ATOM   3340 C  CB     . HIS A 1 482 ? -25.71600 -30.99600 13.32000  1.000 24.44504 ? 478 HIS A CB     1 
ATOM   3341 C  CG     . HIS A 1 482 ? -24.90600 -29.97300 14.05700  1.000 30.41944 ? 478 HIS A CG     1 
ATOM   3342 N  ND1    . HIS A 1 482 ? -25.08700 -28.61800 13.88200  1.000 31.27480 ? 478 HIS A ND1    1 
ATOM   3343 C  CD2    . HIS A 1 482 ? -23.92900 -30.10400 14.98600  1.000 31.00372 ? 478 HIS A CD2    1 
ATOM   3344 C  CE1    . HIS A 1 482 ? -24.24700 -27.95600 14.66100  1.000 34.27253 ? 478 HIS A CE1    1 
ATOM   3345 N  NE2    . HIS A 1 482 ? -23.53200 -28.83300 15.34100  1.000 31.36955 ? 478 HIS A NE2    1 
ATOM   3346 N  N      . GLY A 1 483 ? -28.67300 -33.12300 13.87000  1.000 29.31930 ? 479 GLY A N      1 
ATOM   3347 C  CA     . GLY A 1 483 ? -29.52100 -34.15700 13.29000  1.000 32.19860 ? 479 GLY A CA     1 
ATOM   3348 C  C      . GLY A 1 483 ? -29.76900 -34.04700 11.79700  1.000 29.23508 ? 479 GLY A C      1 
ATOM   3349 O  O      . GLY A 1 483 ? -29.51100 -34.99400 11.05100  1.000 34.28569 ? 479 GLY A O      1 
ATOM   3350 N  N      . LEU A 1 484 ? -30.28000 -32.89500 11.35200  1.000 25.82678 ? 480 LEU A N      1 
ATOM   3351 C  CA     . LEU A 1 484 ? -30.55200 -32.70700 9.92900   1.000 33.23293 ? 480 LEU A CA     1 
ATOM   3352 C  C      . LEU A 1 484 ? -29.28400 -32.84300 9.09400   1.000 34.04092 ? 480 LEU A C      1 
ATOM   3353 O  O      . LEU A 1 484 ? -29.32700 -33.34900 7.96600   1.000 36.07275 ? 480 LEU A O      1 
ATOM   3354 C  CB     . LEU A 1 484 ? -31.20600 -31.34400 9.69300   1.000 26.95586 ? 480 LEU A CB     1 
ATOM   3355 C  CG     . LEU A 1 484 ? -32.61700 -31.18700 10.26500  1.000 34.66205 ? 480 LEU A CG     1 
ATOM   3356 C  CD1    . LEU A 1 484 ? -33.22500 -29.84700 9.84300   1.000 34.11462 ? 480 LEU A CD1    1 
ATOM   3357 C  CD2    . LEU A 1 484 ? -33.50200 -32.34600 9.84000   1.000 34.37254 ? 480 LEU A CD2    1 
ATOM   3358 N  N      . VAL A 1 485 ? -28.14100 -32.39900 9.62600   1.000 34.05408 ? 481 VAL A N      1 
ATOM   3359 C  CA     . VAL A 1 485 ? -26.90000 -32.51800 8.86300   1.000 33.90407 ? 481 VAL A CA     1 
ATOM   3360 C  C      . VAL A 1 485 ? -26.46500 -33.98200 8.78500   1.000 34.93050 ? 481 VAL A C      1 
ATOM   3361 O  O      . VAL A 1 485 ? -26.07700 -34.47500 7.71600   1.000 30.51682 ? 481 VAL A O      1 
ATOM   3362 C  CB     . VAL A 1 485 ? -25.80100 -31.62800 9.48000   1.000 33.98039 ? 481 VAL A CB     1 
ATOM   3363 C  CG1    . VAL A 1 485 ? -24.51000 -31.77300 8.71300   1.000 33.90933 ? 481 VAL A CG1    1 
ATOM   3364 C  CG2    . VAL A 1 485 ? -26.23300 -30.15400 9.52200   1.000 31.64590 ? 481 VAL A CG2    1 
ATOM   3365 N  N      . HIS A 1 486 ? -26.56400 -34.70300 9.90600   1.000 34.23042 ? 482 HIS A N      1 
ATOM   3366 C  CA     . HIS A 1 486 ? -26.27500 -36.13500 9.94900   1.000 30.68789 ? 482 HIS A CA     1 
ATOM   3367 C  C      . HIS A 1 486 ? -27.12400 -36.91200 8.94400   1.000 37.19920 ? 482 HIS A C      1 
ATOM   3368 O  O      . HIS A 1 486 ? -26.63000 -37.81900 8.26100   1.000 34.59099 ? 482 HIS A O      1 
ATOM   3369 C  CB     . HIS A 1 486 ? -26.52300 -36.64500 11.37000  1.000 32.96711 ? 482 HIS A CB     1 
ATOM   3370 C  CG     . HIS A 1 486 ? -26.18100 -38.08800 11.57700  1.000 45.33701 ? 482 HIS A CG     1 
ATOM   3371 N  ND1    . HIS A 1 486 ? -24.91800 -38.51100 11.93200  1.000 50.59291 ? 482 HIS A ND1    1 
ATOM   3372 C  CD2    . HIS A 1 486 ? -26.94400 -39.20400 11.50300  1.000 47.61887 ? 482 HIS A CD2    1 
ATOM   3373 C  CE1    . HIS A 1 486 ? -24.91700 -39.82600 12.06400  1.000 50.32709 ? 482 HIS A CE1    1 
ATOM   3374 N  NE2    . HIS A 1 486 ? -26.13300 -40.27100 11.80600  1.000 51.14297 ? 482 HIS A NE2    1 
ATOM   3375 N  N      . LEU A 1 487 ? -28.42400 -36.60900 8.87600   1.000 34.45413 ? 483 LEU A N      1 
ATOM   3376 C  CA     . LEU A 1 487 ? -29.26300 -37.29900 7.90400   1.000 37.44923 ? 483 LEU A CA     1 
ATOM   3377 C  C      . LEU A 1 487 ? -28.86400 -36.93000 6.47500   1.000 33.04080 ? 483 LEU A C      1 
ATOM   3378 O  O      . LEU A 1 487 ? -28.84400 -37.79000 5.59100   1.000 38.89677 ? 483 LEU A O      1 
ATOM   3379 C  CB     . LEU A 1 487 ? -30.73100 -36.98100 8.16900   1.000 37.60977 ? 483 LEU A CB     1 
ATOM   3380 C  CG     . LEU A 1 487 ? -31.25900 -37.43500 9.53100   1.000 40.39695 ? 483 LEU A CG     1 
ATOM   3381 C  CD1    . LEU A 1 487 ? -32.55100 -36.69400 9.84200   1.000 39.26523 ? 483 LEU A CD1    1 
ATOM   3382 C  CD2    . LEU A 1 487 ? -31.47100 -38.94900 9.57200   1.000 40.17061 ? 483 LEU A CD2    1 
ATOM   3383 N  N      . GLY A 1 488 ? -28.50000 -35.66700 6.24200   1.000 34.90682 ? 484 GLY A N      1 
ATOM   3384 C  CA     . GLY A 1 488 ? -27.99200 -35.28200 4.93100   1.000 37.40975 ? 484 GLY A CA     1 
ATOM   3385 C  C      . GLY A 1 488 ? -26.72900 -36.03500 4.54600   1.000 42.32613 ? 484 GLY A C      1 
ATOM   3386 O  O      . GLY A 1 488 ? -26.56300 -36.44200 3.39100   1.000 37.93613 ? 484 GLY A O      1 
ATOM   3387 N  N      . GLU A 1 489 ? -25.82000 -36.23800 5.50800   1.000 38.55989 ? 485 GLU A N      1 
ATOM   3388 C  CA     . GLU A 1 489 ? -24.62400 -37.02900 5.22500   1.000 37.34132 ? 485 GLU A CA     1 
ATOM   3389 C  C      . GLU A 1 489 ? -24.99100 -38.44000 4.78800   1.000 38.59147 ? 485 GLU A C      1 
ATOM   3390 O  O      . GLU A 1 489 ? -24.37100 -38.99200 3.87100   1.000 43.08938 ? 485 GLU A O      1 
ATOM   3391 C  CB     . GLU A 1 489 ? -23.71600 -37.09700 6.45100   1.000 34.73574 ? 485 GLU A CB     1 
ATOM   3392 C  CG     . GLU A 1 489 ? -23.14300 -35.77200 6.90100   1.000 39.76793 ? 485 GLU A CG     1 
ATOM   3393 C  CD     . GLU A 1 489 ? -22.58200 -35.84600 8.31200   1.000 43.98948 ? 485 GLU A CD     1 
ATOM   3394 O  OE1    . GLU A 1 489 ? -21.90300 -34.88500 8.72300   1.000 48.25052 ? 485 GLU A OE1    1 
ATOM   3395 O  OE2    . GLU A 1 489 ? -22.81400 -36.86500 9.00300   1.000 50.14022 ? 485 GLU A OE2    1 
ATOM   3396 N  N      . GLN A 1 490 ? -25.98800 -39.04100 5.44600   1.000 36.09643 ? 486 GLN A N      1 
ATOM   3397 C  CA     . GLN A 1 490 ? -26.39200 -40.41200 5.13700   1.000 41.98924 ? 486 GLN A CA     1 
ATOM   3398 C  C      . GLN A 1 490 ? -27.13800 -40.49400 3.81100   1.000 43.34204 ? 486 GLN A C      1 
ATOM   3399 O  O      . GLN A 1 490 ? -26.90600 -41.40500 3.01000   1.000 45.40281 ? 486 GLN A O      1 
ATOM   3400 C  CB     . GLN A 1 490 ? -27.26800 -40.96300 6.25900   1.000 43.32098 ? 486 GLN A CB     1 
ATOM   3401 C  CG     . GLN A 1 490 ? -26.62000 -40.96800 7.62800   1.000 45.21595 ? 486 GLN A CG     1 
ATOM   3402 C  CD     . GLN A 1 490 ? -27.56500 -41.49500 8.69800   1.000 52.22468 ? 486 GLN A CD     1 
ATOM   3403 O  OE1    . GLN A 1 490 ? -28.75900 -41.17600 8.70200   1.000 51.22983 ? 486 GLN A OE1    1 
ATOM   3404 N  NE2    . GLN A 1 490 ? -27.04100 -42.32200 9.59700   1.000 52.33522 ? 486 GLN A NE2    1 
ATOM   3405 N  N      . HIS A 1 491 ? -28.06400 -39.56700 3.57200   1.000 43.47363 ? 487 HIS A N      1 
ATOM   3406 C  CA     . HIS A 1 491 ? -28.96400 -39.68300 2.43300   1.000 42.56037 ? 487 HIS A CA     1 
ATOM   3407 C  C      . HIS A 1 491 ? -28.45900 -38.98900 1.18000   1.000 47.27672 ? 487 HIS A C      1 
ATOM   3408 O  O      . HIS A 1 491 ? -28.98800 -39.24900 0.09100   1.000 44.54481 ? 487 HIS A O      1 
ATOM   3409 C  CB     . HIS A 1 491 ? -30.34400 -39.14500 2.80900   1.000 44.56587 ? 487 HIS A CB     1 
ATOM   3410 C  CG     . HIS A 1 491 ? -31.08700 -40.05000 3.73700   1.000 53.49062 ? 487 HIS A CG     1 
ATOM   3411 N  ND1    . HIS A 1 491 ? -30.94100 -39.99200 5.10600   1.000 54.79868 ? 487 HIS A ND1    1 
ATOM   3412 C  CD2    . HIS A 1 491 ? -31.94700 -41.06600 3.49200   1.000 56.36992 ? 487 HIS A CD2    1 
ATOM   3413 C  CE1    . HIS A 1 491 ? -31.69000 -40.92500 5.66700   1.000 57.65691 ? 487 HIS A CE1    1 
ATOM   3414 N  NE2    . HIS A 1 491 ? -32.31200 -41.59000 4.70900   1.000 59.25184 ? 487 HIS A NE2    1 
ATOM   3415 N  N      . GLN A 1 492 ? -27.48300 -38.08900 1.30200   1.000 36.27014 ? 488 GLN A N      1 
ATOM   3416 C  CA     . GLN A 1 492 ? -26.94000 -37.40500 0.14500   1.000 38.70201 ? 488 GLN A CA     1 
ATOM   3417 C  C      . GLN A 1 492 ? -25.44700 -37.59300 -0.04600  1.000 42.97357 ? 488 GLN A C      1 
ATOM   3418 O  O      . GLN A 1 492 ? -24.95000 -37.28600 -1.13300  1.000 46.14764 ? 488 GLN A O      1 
ATOM   3419 C  CB     . GLN A 1 492 ? -27.23800 -35.90100 0.22100   1.000 44.60008 ? 488 GLN A CB     1 
ATOM   3420 C  CG     . GLN A 1 492 ? -28.67100 -35.57200 0.59500   1.000 52.09046 ? 488 GLN A CG     1 
ATOM   3421 C  CD     . GLN A 1 492 ? -28.90200 -34.07800 0.65900   1.000 59.63347 ? 488 GLN A CD     1 
ATOM   3422 O  OE1    . GLN A 1 492 ? -29.02600 -33.50500 1.74000   1.000 62.27589 ? 488 GLN A OE1    1 
ATOM   3423 N  NE2    . GLN A 1 492 ? -28.96000 -33.43800 -0.50000  1.000 60.45725 ? 488 GLN A NE2    1 
ATOM   3424 N  N      . PHE A 1 493 ? -24.71500 -38.06900 0.96700   1.000 43.87631 ? 489 PHE A N      1 
ATOM   3425 C  CA     . PHE A 1 493 ? -23.27000 -38.22200 0.84700   1.000 41.77343 ? 489 PHE A CA     1 
ATOM   3426 C  C      . PHE A 1 493 ? -22.78200 -39.60100 1.27600   1.000 43.13149 ? 489 PHE A C      1 
ATOM   3427 O  O      . PHE A 1 493 ? -21.60300 -39.75300 1.60200   1.000 44.57903 ? 489 PHE A O      1 
ATOM   3428 C  CB     . PHE A 1 493 ? -22.55700 -37.11800 1.63500   1.000 38.54410 ? 489 PHE A CB     1 
ATOM   3429 C  CG     . PHE A 1 493 ? -22.74300 -35.74500 1.04100   1.000 38.73096 ? 489 PHE A CG     1 
ATOM   3430 C  CD1    . PHE A 1 493 ? -21.92400 -35.29900 0.02100   1.000 41.36549 ? 489 PHE A CD1    1 
ATOM   3431 C  CD2    . PHE A 1 493 ? -23.75100 -34.91300 1.48900   1.000 36.20434 ? 489 PHE A CD2    1 
ATOM   3432 C  CE1    . PHE A 1 493 ? -22.10100 -34.03900 -0.53300  1.000 38.80465 ? 489 PHE A CE1    1 
ATOM   3433 C  CE2    . PHE A 1 493 ? -23.92800 -33.64900 0.94400   1.000 36.17276 ? 489 PHE A CE2    1 
ATOM   3434 C  CZ     . PHE A 1 493 ? -23.10600 -33.21500 -0.07200  1.000 35.65164 ? 489 PHE A CZ     1 
ATOM   3435 N  N      . ASP A 1 494 ? -23.66800 -40.60500 1.27600   1.000 41.19704 ? 490 ASP A N      1 
ATOM   3436 C  CA     . ASP A 1 494 ? -23.30400 -42.01300 1.50000   1.000 47.23461 ? 490 ASP A CA     1 
ATOM   3437 C  C      . ASP A 1 494 ? -22.51000 -42.21100 2.78400   1.000 48.64794 ? 490 ASP A C      1 
ATOM   3438 O  O      . ASP A 1 494 ? -21.65400 -43.09300 2.86800   1.000 51.54829 ? 490 ASP A O      1 
ATOM   3439 C  CB     . ASP A 1 494 ? -22.50300 -42.57900 0.32500   1.000 56.00935 ? 490 ASP A CB     1 
ATOM   3440 C  CG     . ASP A 1 494 ? -23.21500 -42.43600 -0.99500  1.000 66.32374 ? 490 ASP A CG     1 
ATOM   3441 O  OD1    . ASP A 1 494 ? -24.29000 -43.05200 -1.16300  1.000 66.58430 ? 490 ASP A OD1    1 
ATOM   3442 O  OD2    . ASP A 1 494 ? -22.68800 -41.70900 -1.86900  1.000 70.59267 ? 490 ASP A OD2    1 
ATOM   3443 N  N      . SER A 1 495 ? -22.81400 -41.42000 3.81100   1.000 40.56539 ? 491 SER A N      1 
ATOM   3444 C  CA     . SER A 1 495 ? -22.12100 -41.55800 5.09100   1.000 42.96568 ? 491 SER A CA     1 
ATOM   3445 C  C      . SER A 1 495 ? -20.60200 -41.53500 4.91200   1.000 45.96604 ? 491 SER A C      1 
ATOM   3446 O  O      . SER A 1 495 ? -19.86200 -42.14700 5.68100   1.000 51.44827 ? 491 SER A O      1 
ATOM   3447 C  CB     . SER A 1 495 ? -22.54500 -42.84200 5.80500   1.000 48.10314 ? 491 SER A CB     1 
ATOM   3448 O  OG     . SER A 1 495 ? -23.93000 -42.83900 6.07700   1.000 53.37482 ? 491 SER A OG     1 
ATOM   3449 N  N      . LYS A 1 496 ? -20.12300 -40.81200 3.89600   1.000 47.22145 ? 492 LYS A N      1 
ATOM   3450 C  CA     . LYS A 1 496 ? -18.69000 -40.74000 3.62300   1.000 43.88947 ? 492 LYS A CA     1 
ATOM   3451 C  C      . LYS A 1 496 ? -17.92900 -39.94400 4.67600   1.000 40.71804 ? 492 LYS A C      1 
ATOM   3452 O  O      . LYS A 1 496 ? -16.70600 -40.07600 4.77000   1.000 47.13723 ? 492 LYS A O      1 
ATOM   3453 C  CB     . LYS A 1 496 ? -18.45400 -40.11100 2.25100   1.000 45.80023 ? 492 LYS A CB     1 
ATOM   3454 C  CG     . LYS A 1 496 ? -18.60600 -41.06900 1.08800   1.000 52.29838 ? 492 LYS A CG     1 
ATOM   3455 C  CD     . LYS A 1 496 ? -18.21700 -40.38700 -0.22100  1.000 55.98040 ? 492 LYS A CD     1 
ATOM   3456 C  CE     . LYS A 1 496 ? -19.25800 -39.35300 -0.62900  1.000 53.65117 ? 492 LYS A CE     1 
ATOM   3457 N  NZ     . LYS A 1 496 ? -18.67600 -38.27400 -1.46600  1.000 53.08268 ? 492 LYS A NZ     1 
ATOM   3458 N  N      . PHE A 1 497 ? -18.61400 -39.09300 5.43300   1.000 42.04715 ? 493 PHE A N      1 
ATOM   3459 C  CA     . PHE A 1 497 ? -17.97800 -38.26100 6.44000   1.000 37.71505 ? 493 PHE A CA     1 
ATOM   3460 C  C      . PHE A 1 497 ? -19.03300 -37.86900 7.46100   1.000 38.69148 ? 493 PHE A C      1 
ATOM   3461 O  O      . PHE A 1 497 ? -20.23300 -37.87500 7.17400   1.000 34.23305 ? 493 PHE A O      1 
ATOM   3462 C  CB     . PHE A 1 497 ? -17.33100 -37.01100 5.81700   1.000 36.64124 ? 493 PHE A CB     1 
ATOM   3463 C  CG     . PHE A 1 497 ? -18.30400 -36.13400 5.03900   1.000 43.73945 ? 493 PHE A CG     1 
ATOM   3464 C  CD1    . PHE A 1 497 ? -19.06000 -35.16000 5.68000   1.000 41.38391 ? 493 PHE A CD1    1 
ATOM   3465 C  CD2    . PHE A 1 497 ? -18.46700 -36.29600 3.66700   1.000 46.94247 ? 493 PHE A CD2    1 
ATOM   3466 C  CE1    . PHE A 1 497 ? -19.95300 -34.35600 4.96300   1.000 41.05492 ? 493 PHE A CE1    1 
ATOM   3467 C  CE2    . PHE A 1 497 ? -19.36000 -35.50500 2.94500   1.000 37.71505 ? 493 PHE A CE2    1 
ATOM   3468 C  CZ     . PHE A 1 497 ? -20.10000 -34.53200 3.59400   1.000 42.14189 ? 493 PHE A CZ     1 
ATOM   3469 N  N      . ASP A 1 498 ? -18.56400 -37.50600 8.65200   1.000 39.22576 ? 494 ASP A N      1 
ATOM   3470 C  CA     . ASP A 1 498 ? -19.42800 -37.07400 9.74400   1.000 41.44181 ? 494 ASP A CA     1 
ATOM   3471 C  C      . ASP A 1 498 ? -18.88100 -35.76900 10.30800  1.000 40.64171 ? 494 ASP A C      1 
ATOM   3472 O  O      . ASP A 1 498 ? -17.79300 -35.74300 10.88900  1.000 42.52615 ? 494 ASP A O      1 
ATOM   3473 C  CB     . ASP A 1 498 ? -19.51500 -38.14200 10.82900  1.000 41.23126 ? 494 ASP A CB     1 
ATOM   3474 C  CG     . ASP A 1 498 ? -20.44500 -37.74100 11.95800  1.000 47.77152 ? 494 ASP A CG     1 
ATOM   3475 O  OD1    . ASP A 1 498 ? -20.28200 -36.63400 12.51400  1.000 47.40305 ? 494 ASP A OD1    1 
ATOM   3476 O  OD2    . ASP A 1 498 ? -21.34300 -38.53900 12.29000  1.000 56.72785 ? 494 ASP A OD2    1 
ATOM   3477 N  N      . ILE A 1 499 ? -19.62900 -34.69200 10.13300  1.000 37.11761 ? 495 ILE A N      1 
ATOM   3478 C  CA     . ILE A 1 499 ? -19.31200 -33.40500 10.72900  1.000 36.63597 ? 495 ILE A CA     1 
ATOM   3479 C  C      . ILE A 1 499 ? -20.47400 -32.91700 11.59300  1.000 37.84927 ? 495 ILE A C      1 
ATOM   3480 O  O      . ILE A 1 499 ? -20.65600 -31.71600 11.79000  1.000 43.17623 ? 495 ILE A O      1 
ATOM   3481 C  CB     . ILE A 1 499 ? -18.91900 -32.38400 9.64200   1.000 37.74400 ? 495 ILE A CB     1 
ATOM   3482 C  CG1    . ILE A 1 499 ? -18.27900 -31.12500 10.25400  1.000 36.13854 ? 495 ILE A CG1    1 
ATOM   3483 C  CG2    . ILE A 1 499 ? -20.11400 -32.05500 8.76700   1.000 35.20948 ? 495 ILE A CG2    1 
ATOM   3484 C  CD1    . ILE A 1 499 ? -17.00600 -31.39100 11.02200  1.000 40.38642 ? 495 ILE A CD1    1 
ATOM   3485 N  N      . SER A 1 500 ? -21.28900 -33.85600 12.06200  1.000 41.09966 ? 496 SER A N      1 
ATOM   3486 C  CA     . SER A 1 500 ? -22.57100 -33.57900 12.69400  1.000 40.83121 ? 496 SER A CA     1 
ATOM   3487 C  C      . SER A 1 500 ? -22.70600 -34.13300 14.10400  1.000 36.71756 ? 496 SER A C      1 
ATOM   3488 O  O      . SER A 1 500 ? -23.43400 -33.54500 14.90600  1.000 36.55701 ? 496 SER A O      1 
ATOM   3489 C  CB     . SER A 1 500 ? -23.70500 -34.16000 11.84400  1.000 33.33294 ? 496 SER A CB     1 
ATOM   3490 O  OG     . SER A 1 500 ? -23.41000 -35.51400 11.54900  1.000 41.10493 ? 496 SER A OG     1 
ATOM   3491 N  N      . SER A 1 501 ? -22.03900 -35.24400 14.42300  1.000 33.10660 ? 497 SER A N      1 
ATOM   3492 C  CA     . SER A 1 501 ? -22.23200 -35.92600 15.70200  1.000 38.99941 ? 497 SER A CA     1 
ATOM   3493 C  C      . SER A 1 501 ? -21.22000 -35.41900 16.71200  1.000 38.47567 ? 497 SER A C      1 
ATOM   3494 O  O      . SER A 1 501 ? -20.03100 -35.32000 16.40700  1.000 44.65535 ? 497 SER A O      1 
ATOM   3495 C  CB     . SER A 1 501 ? -22.07200 -37.44000 15.56000  1.000 36.94654 ? 497 SER A CB     1 
ATOM   3496 O  OG     . SER A 1 501 ? -22.77900 -37.93000 14.44300  1.000 46.52663 ? 497 SER A OG     1 
ATOM   3497 N  N      . PHE A 1 502 ? -21.69100 -35.09500 17.90800  1.000 32.43020 ? 498 PHE A N      1 
ATOM   3498 C  CA     . PHE A 1 502 ? -20.75800 -34.80400 18.98700  1.000 34.45939 ? 498 PHE A CA     1 
ATOM   3499 C  C      . PHE A 1 502 ? -20.10900 -36.09500 19.47300  1.000 36.17802 ? 498 PHE A C      1 
ATOM   3500 O  O      . PHE A 1 502 ? -20.75300 -37.14200 19.55200  1.000 35.11474 ? 498 PHE A O      1 
ATOM   3501 C  CB     . PHE A 1 502 ? -21.47400 -34.12200 20.14500  1.000 34.39886 ? 498 PHE A CB     1 
ATOM   3502 C  CG     . PHE A 1 502 ? -22.05600 -32.78100 19.80000  1.000 30.68526 ? 498 PHE A CG     1 
ATOM   3503 C  CD1    . PHE A 1 502 ? -21.48000 -31.99700 18.81200  1.000 28.61922 ? 498 PHE A CD1    1 
ATOM   3504 C  CD2    . PHE A 1 502 ? -23.16300 -32.29800 20.47300  1.000 25.26356 ? 498 PHE A CD2    1 
ATOM   3505 C  CE1    . PHE A 1 502 ? -21.99600 -30.75600 18.49100  1.000 26.90849 ? 498 PHE A CE1    1 
ATOM   3506 C  CE2    . PHE A 1 502 ? -23.70100 -31.05100 20.15400  1.000 27.84281 ? 498 PHE A CE2    1 
ATOM   3507 C  CZ     . PHE A 1 502 ? -23.10800 -30.28000 19.15700  1.000 29.79305 ? 498 PHE A CZ     1 
ATOM   3508 N  N      . ARG A 1 503 ? -18.82400 -36.00600 19.81700  1.000 33.48559 ? 499 ARG A N      1 
ATOM   3509 C  CA     . ARG A 1 503 ? -18.18800 -37.11700 20.50800  1.000 38.86255 ? 499 ARG A CA     1 
ATOM   3510 C  C      . ARG A 1 503 ? -18.77800 -37.30000 21.89900  1.000 38.18353 ? 499 ARG A C      1 
ATOM   3511 O  O      . ARG A 1 503 ? -18.87400 -38.43700 22.37300  1.000 32.41178 ? 499 ARG A O      1 
ATOM   3512 C  CB     . ARG A 1 503 ? -16.67700 -36.95100 20.57200  1.000 40.49959 ? 499 ARG A CB     1 
ATOM   3513 C  CG     . ARG A 1 503 ? -15.95800 -38.22800 20.98700  1.000 54.95922 ? 499 ARG A CG     1 
ATOM   3514 C  CD     . ARG A 1 503 ? -14.50200 -38.17200 20.57200  1.000 61.13101 ? 499 ARG A CD     1 
ATOM   3515 N  NE     . ARG A 1 503 ? -13.87900 -36.98900 21.14500  1.000 58.63335 ? 499 ARG A NE     1 
ATOM   3516 C  CZ     . ARG A 1 503 ? -13.34100 -36.95300 22.35700  1.000 55.35137 ? 499 ARG A CZ     1 
ATOM   3517 N  NH1    . ARG A 1 503 ? -13.34800 -38.04500 23.11800  1.000 48.80585 ? 499 ARG A NH1    1 
ATOM   3518 N  NH2    . ARG A 1 503 ? -12.80800 -35.82700 22.80700  1.000 50.95348 ? 499 ARG A NH2    1 
ATOM   3519 N  N      . LYS A 1 504 ? -19.18600 -36.23200 22.59600  1.000 38.98099 ? 500 LYS A N      1 
ATOM   3520 C  CA     . LYS A 1 504 ? -19.78500 -36.53800 23.88200  1.000 39.95479 ? 500 LYS A CA     1 
ATOM   3521 C  C      . LYS A 1 504 ? -20.90100 -35.48000 23.97100  1.000 39.28892 ? 500 LYS A C      1 
ATOM   3522 O  O      . LYS A 1 504 ? -20.64000 -34.27500 23.84900  1.000 36.48859 ? 500 LYS A O      1 
ATOM   3523 C  CB     . LYS A 1 504 ? -18.70700 -36.49300 24.96300  1.000 50.64291 ? 500 LYS A CB     1 
ATOM   3524 C  CG     . LYS A 1 504 ? -19.08500 -36.96300 26.38700  1.000 62.66278 ? 500 LYS A CG     1 
ATOM   3525 C  CD     . LYS A 1 504 ? -18.35000 -36.47900 27.65900  1.000 67.87393 ? 500 LYS A CD     1 
ATOM   3526 C  CE     . LYS A 1 504 ? -19.43000 -35.74400 28.59300  1.000 66.84749 ? 500 LYS A CE     1 
ATOM   3527 N  NZ     . LYS A 1 504 ? -18.82200 -34.99900 29.79800  1.000 65.25519 ? 500 LYS A NZ     1 
ATOM   3528 N  N      . SER A 1 505 ? -22.16600 -35.92400 23.96900  1.000 31.84592 ? 501 SER A N      1 
ATOM   3529 C  CA     . SER A 1 505 ? -23.30000 -35.00600 24.10800  1.000 32.88026 ? 501 SER A CA     1 
ATOM   3530 C  C      . SER A 1 505 ? -23.19500 -34.12200 25.35500  1.000 30.04308 ? 501 SER A C      1 
ATOM   3531 O  O      . SER A 1 505 ? -22.58400 -34.47700 26.36600  1.000 38.05193 ? 501 SER A O      1 
ATOM   3532 C  CB     . SER A 1 505 ? -24.61100 -35.77400 24.11300  1.000 32.71445 ? 501 SER A CB     1 
ATOM   3533 O  OG     . SER A 1 505 ? -24.46700 -36.95900 24.84200  1.000 40.60487 ? 501 SER A OG     1 
ATOM   3534 N  N      . ILE A 1 506 ? -23.77400 -32.92800 25.23200  1.000 28.51131 ? 502 ILE A N      1 
ATOM   3535 C  CA     . ILE A 1 506 ? -23.83400 -31.95700 26.31600  1.000 28.09021 ? 502 ILE A CA     1 
ATOM   3536 C  C      . ILE A 1 506 ? -24.87900 -32.37000 27.34600  1.000 32.27229 ? 502 ILE A C      1 
ATOM   3537 O  O      . ILE A 1 506 ? -25.95900 -32.86600 26.99900  1.000 28.37972 ? 502 ILE A O      1 
ATOM   3538 C  CB     . ILE A 1 506 ? -24.15200 -30.57000 25.72700  1.000 35.63322 ? 502 ILE A CB     1 
ATOM   3539 C  CG1    . ILE A 1 506 ? -22.95200 -30.08300 24.88700  1.000 38.30196 ? 502 ILE A CG1    1 
ATOM   3540 C  CG2    . ILE A 1 506 ? -24.57600 -29.59900 26.83100  1.000 27.26643 ? 502 ILE A CG2    1 
ATOM   3541 C  CD1    . ILE A 1 506 ? -23.28400 -28.94800 23.90700  1.000 40.69962 ? 502 ILE A CD1    1 
ATOM   3542 N  N      . ASP A 1 507 ? -24.56200 -32.15900 28.62500  1.000 30.00886 ? 503 ASP A N      1 
ATOM   3543 C  CA     . ASP A 1 507 ? -25.48000 -32.45100 29.72500  1.000 31.23532 ? 503 ASP A CA     1 
ATOM   3544 C  C      . ASP A 1 507 ? -26.26200 -31.17900 30.04100  1.000 36.70966 ? 503 ASP A C      1 
ATOM   3545 O  O      . ASP A 1 507 ? -25.82600 -30.33400 30.82500  1.000 32.75393 ? 503 ASP A O      1 
ATOM   3546 C  CB     . ASP A 1 507 ? -24.71500 -32.95200 30.94200  1.000 33.25925 ? 503 ASP A CB     1 
ATOM   3547 C  CG     . ASP A 1 507 ? -25.64200 -33.37700 32.09000  1.000 40.17587 ? 503 ASP A CG     1 
ATOM   3548 O  OD1    . ASP A 1 507 ? -26.83500 -32.97700 32.11400  1.000 41.82344 ? 503 ASP A OD1    1 
ATOM   3549 O  OD2    . ASP A 1 507 ? -25.17500 -34.12100 32.97200  1.000 43.25255 ? 503 ASP A OD2    1 
ATOM   3550 N  N      . PHE A 1 508 ? -27.44800 -31.03400 29.42900  1.000 29.58249 ? 504 PHE A N      1 
ATOM   3551 C  CA     . PHE A 1 508 ? -28.18300 -29.78100 29.59100  1.000 30.91686 ? 504 PHE A CA     1 
ATOM   3552 C  C      . PHE A 1 508 ? -28.78400 -29.62200 30.98600  1.000 35.11737 ? 504 PHE A C      1 
ATOM   3553 O  O      . PHE A 1 508 ? -29.02500 -28.48200 31.40700  1.000 31.65116 ? 504 PHE A O      1 
ATOM   3554 C  CB     . PHE A 1 508 ? -29.25200 -29.65500 28.50200  1.000 27.93493 ? 504 PHE A CB     1 
ATOM   3555 C  CG     . PHE A 1 508 ? -28.66700 -29.49300 27.12400  1.000 31.10110 ? 504 PHE A CG     1 
ATOM   3556 C  CD1    . PHE A 1 508 ? -28.11600 -28.27600 26.72900  1.000 28.37972 ? 504 PHE A CD1    1 
ATOM   3557 C  CD2    . PHE A 1 508 ? -28.60200 -30.57700 26.24900  1.000 31.78802 ? 504 PHE A CD2    1 
ATOM   3558 C  CE1    . PHE A 1 508 ? -27.53500 -28.12800 25.46300  1.000 33.19082 ? 504 PHE A CE1    1 
ATOM   3559 C  CE2    . PHE A 1 508 ? -28.02900 -30.44400 24.99300  1.000 34.28832 ? 504 PHE A CE2    1 
ATOM   3560 C  CZ     . PHE A 1 508 ? -27.49700 -29.21400 24.59300  1.000 34.73574 ? 504 PHE A CZ     1 
ATOM   3561 N  N      . CYS A 1 509 ? -28.97500 -30.70800 31.73900  1.000 33.01448 ? 505 CYS A N      1 
ATOM   3562 C  CA     . CYS A 1 509 ? -29.45600 -30.55000 33.11200  1.000 33.45401 ? 505 CYS A CA     1 
ATOM   3563 C  C      . CYS A 1 509 ? -28.40200 -29.90100 33.98800  1.000 36.75704 ? 505 CYS A C      1 
ATOM   3564 O  O      . CYS A 1 509 ? -28.71000 -29.01700 34.79700  1.000 40.58118 ? 505 CYS A O      1 
ATOM   3565 C  CB     . CYS A 1 509 ? -29.81400 -31.90900 33.71100  1.000 42.28928 ? 505 CYS A CB     1 
ATOM   3566 S  SG     . CYS A 1 509 ? -31.36500 -32.57800 33.16600  1.000 48.74795 ? 505 CYS A SG     1 
ATOM   3567 N  N      . LYS A 1 510 ? -27.15000 -30.32300 33.81400  1.000 34.02250 ? 506 LYS A N      1 
ATOM   3568 C  CA     . LYS A 1 510 ? -26.03600 -29.70000 34.51200  1.000 33.22767 ? 506 LYS A CA     1 
ATOM   3569 C  C      . LYS A 1 510 ? -25.82100 -28.26100 34.05700  1.000 32.92763 ? 506 LYS A C      1 
ATOM   3570 O  O      . LYS A 1 510 ? -25.47800 -27.39000 34.86700  1.000 29.41668 ? 506 LYS A O      1 
ATOM   3571 C  CB     . LYS A 1 510 ? -24.78300 -30.53100 34.29800  1.000 37.16761 ? 506 LYS A CB     1 
ATOM   3572 C  CG     . LYS A 1 510 ? -24.82700 -31.88500 34.96700  1.000 48.16893 ? 506 LYS A CG     1 
ATOM   3573 C  CD     . LYS A 1 510 ? -23.42600 -32.32700 35.38300  1.000 53.50905 ? 506 LYS A CD     1 
ATOM   3574 C  CE     . LYS A 1 510 ? -23.47000 -33.39200 36.47300  1.000 58.75704 ? 506 LYS A CE     1 
ATOM   3575 N  NZ     . LYS A 1 510 ? -24.05700 -34.68200 36.00200  1.000 63.38128 ? 506 LYS A NZ     1 
ATOM   3576 N  N      . MET A 1 511 ? -25.98200 -27.98900 32.76400  1.000 30.11151 ? 507 MET A N      1 
ATOM   3577 C  CA     . MET A 1 511 ? -25.85400 -26.61100 32.31000  1.000 33.28031 ? 507 MET A CA     1 
ATOM   3578 C  C      . MET A 1 511 ? -26.94400 -25.73200 32.91600  1.000 30.32995 ? 507 MET A C      1 
ATOM   3579 O  O      . MET A 1 511 ? -26.66700 -24.62800 33.40400  1.000 26.57161 ? 507 MET A O      1 
ATOM   3580 C  CB     . MET A 1 511 ? -25.87700 -26.55000 30.78400  1.000 31.81171 ? 507 MET A CB     1 
ATOM   3581 C  CG     . MET A 1 511 ? -25.45000 -25.20800 30.22600  1.000 39.72845 ? 507 MET A CG     1 
ATOM   3582 S  SD     . MET A 1 511 ? -26.07500 -24.98900 28.54800  1.000 54.74341 ? 507 MET A SD     1 
ATOM   3583 C  CE     . MET A 1 511 ? -25.35100 -26.39300 27.71600  1.000 58.97286 ? 507 MET A CE     1 
ATOM   3584 N  N      . ALA A 1 512 ? -28.19400 -26.20900 32.89400  1.000 29.41932 ? 508 ALA A N      1 
ATOM   3585 C  CA     . ALA A 1 512 ? -29.28700 -25.46500 33.51700  1.000 30.50366 ? 508 ALA A CA     1 
ATOM   3586 C  C      . ALA A 1 512 ? -28.99500 -25.20500 34.98800  1.000 29.05612 ? 508 ALA A C      1 
ATOM   3587 O  O      . ALA A 1 512 ? -29.12700 -24.07400 35.47400  1.000 29.86411 ? 508 ALA A O      1 
ATOM   3588 C  CB     . ALA A 1 512 ? -30.60300 -26.22700 33.35800  1.000 32.24860 ? 508 ALA A CB     1 
ATOM   3589 N  N      . GLU A 1 513 ? -28.57400 -26.24200 35.70800  1.000 25.16354 ? 509 GLU A N      1 
ATOM   3590 C  CA     . GLU A 1 513 ? -28.21000 -26.06700 37.10700  1.000 31.90119 ? 509 GLU A CA     1 
ATOM   3591 C  C      . GLU A 1 513 ? -27.14100 -24.98100 37.26400  1.000 35.13842 ? 509 GLU A C      1 
ATOM   3592 O  O      . GLU A 1 513 ? -27.25500 -24.09400 38.11800  1.000 33.63561 ? 509 GLU A O      1 
ATOM   3593 C  CB     . GLU A 1 513 ? -27.73500 -27.40500 37.67600  1.000 32.45389 ? 509 GLU A CB     1 
ATOM   3594 C  CG     . GLU A 1 513 ? -27.32400 -27.35200 39.12900  1.000 44.33163 ? 509 GLU A CG     1 
ATOM   3595 C  CD     . GLU A 1 513 ? -26.74100 -28.66800 39.62700  1.000 56.08830 ? 509 GLU A CD     1 
ATOM   3596 O  OE1    . GLU A 1 513 ? -26.19800 -28.69200 40.75200  1.000 59.37554 ? 509 GLU A OE1    1 
ATOM   3597 O  OE2    . GLU A 1 513 ? -26.82800 -29.67800 38.89500  1.000 60.46778 ? 509 GLU A OE2    1 
ATOM   3598 N  N      . SER A 1 514 ? -26.09300 -25.03300 36.44200  1.000 28.02441 ? 510 SER A N      1 
ATOM   3599 C  CA     . SER A 1 514 ? -25.04400 -24.02200 36.52800  1.000 30.44312 ? 510 SER A CA     1 
ATOM   3600 C  C      . SER A 1 514 ? -25.61000 -22.62200 36.34900  1.000 33.22240 ? 510 SER A C      1 
ATOM   3601 O  O      . SER A 1 514 ? -25.03900 -21.65100 36.86100  1.000 32.96974 ? 510 SER A O      1 
ATOM   3602 C  CB     . SER A 1 514 ? -23.94800 -24.29900 35.49500  1.000 30.65631 ? 510 SER A CB     1 
ATOM   3603 O  OG     . SER A 1 514 ? -24.27000 -23.71400 34.25000  1.000 33.24872 ? 510 SER A OG     1 
ATOM   3604 N  N      . LEU A 1 515 ? -26.70600 -22.49000 35.60300  1.000 25.92679 ? 511 LEU A N      1 
ATOM   3605 C  CA     . LEU A 1 515 ? -27.30800 -21.19300 35.33200  1.000 27.80597 ? 511 LEU A CA     1 
ATOM   3606 C  C      . LEU A 1 515 ? -28.50200 -20.88400 36.23100  1.000 31.91435 ? 511 LEU A C      1 
ATOM   3607 O  O      . LEU A 1 515 ? -29.23600 -19.93000 35.94600  1.000 30.34048 ? 511 LEU A O      1 
ATOM   3608 C  CB     . LEU A 1 515 ? -27.71500 -21.10900 33.85700  1.000 25.76098 ? 511 LEU A CB     1 
ATOM   3609 C  CG     . LEU A 1 515 ? -26.53600 -21.24000 32.89500  1.000 34.12251 ? 511 LEU A CG     1 
ATOM   3610 C  CD1    . LEU A 1 515 ? -27.03000 -21.32500 31.44200  1.000 27.18747 ? 511 LEU A CD1    1 
ATOM   3611 C  CD2    . LEU A 1 515 ? -25.57700 -20.07100 33.09300  1.000 33.60140 ? 511 LEU A CD2    1 
ATOM   3612 N  N      . GLY A 1 516 ? -28.73100 -21.67900 37.27800  1.000 29.41405 ? 512 GLY A N      1 
ATOM   3613 C  CA     . GLY A 1 516 ? -29.78300 -21.39000 38.24000  1.000 28.77977 ? 512 GLY A CA     1 
ATOM   3614 C  C      . GLY A 1 516 ? -31.19600 -21.71100 37.78300  1.000 35.86483 ? 512 GLY A C      1 
ATOM   3615 O  O      . GLY A 1 516 ? -32.15800 -21.09800 38.27300  1.000 29.73778 ? 512 GLY A O      1 
ATOM   3616 N  N      . VAL A 1 517 ? -31.34400 -22.69000 36.89000  1.000 31.58800 ? 513 VAL A N      1 
ATOM   3617 C  CA     . VAL A 1 517 ? -32.60800 -23.06800 36.26500  1.000 31.35902 ? 513 VAL A CA     1 
ATOM   3618 C  C      . VAL A 1 517 ? -32.87500 -24.53000 36.60200  1.000 35.12526 ? 513 VAL A C      1 
ATOM   3619 O  O      . VAL A 1 517 ? -31.99900 -25.37800 36.39600  1.000 31.78539 ? 513 VAL A O      1 
ATOM   3620 C  CB     . VAL A 1 517 ? -32.54200 -22.87100 34.73900  1.000 29.99307 ? 513 VAL A CB     1 
ATOM   3621 C  CG1    . VAL A 1 517 ? -33.78100 -23.46300 34.04100  1.000 30.32995 ? 513 VAL A CG1    1 
ATOM   3622 C  CG2    . VAL A 1 517 ? -32.32700 -21.39400 34.39700  1.000 28.69818 ? 513 VAL A CG2    1 
ATOM   3623 N  N      . LYS A 1 518 ? -34.07500 -24.82300 37.11900  1.000 33.14345 ? 514 LYS A N      1 
ATOM   3624 C  CA     . LYS A 1 518 ? -34.46600 -26.20800 37.38300  1.000 32.43284 ? 514 LYS A CA     1 
ATOM   3625 C  C      . LYS A 1 518 ? -34.54500 -26.99100 36.07600  1.000 31.16163 ? 514 LYS A C      1 
ATOM   3626 O  O      . LYS A 1 518 ? -34.84500 -26.43200 35.02100  1.000 28.45868 ? 514 LYS A O      1 
ATOM   3627 C  CB     . LYS A 1 518 ? -35.82400 -26.26200 38.09100  1.000 38.37829 ? 514 LYS A CB     1 
ATOM   3628 C  CG     . LYS A 1 518 ? -35.83300 -25.60400 39.46400  1.000 49.93493 ? 514 LYS A CG     1 
ATOM   3629 C  CD     . LYS A 1 518 ? -37.18000 -24.98200 39.75600  1.000 57.20949 ? 514 LYS A CD     1 
ATOM   3630 C  CE     . LYS A 1 518 ? -37.09400 -23.92700 40.84200  1.000 62.86543 ? 514 LYS A CE     1 
ATOM   3631 N  NZ     . LYS A 1 518 ? -36.69400 -24.54300 42.12900  1.000 59.62557 ? 514 LYS A NZ     1 
ATOM   3632 N  N      . SER A 1 519 ? -34.24900 -28.29400 36.14100  1.000 27.48487 ? 515 SER A N      1 
ATOM   3633 C  CA     . SER A 1 519 ? -34.12600 -29.09500 34.92300  1.000 32.38283 ? 515 SER A CA     1 
ATOM   3634 C  C      . SER A 1 519 ? -34.55900 -30.53100 35.18900  1.000 36.38594 ? 515 SER A C      1 
ATOM   3635 O  O      . SER A 1 519 ? -34.58300 -30.98800 36.33100  1.000 34.56204 ? 515 SER A O      1 
ATOM   3636 C  CB     . SER A 1 519 ? -32.69100 -29.07700 34.38000  1.000 35.55163 ? 515 SER A CB     1 
ATOM   3637 O  OG     . SER A 1 519 ? -31.75900 -29.46100 35.38200  1.000 42.83671 ? 515 SER A OG     1 
ATOM   3638 N  N      . TYR A 1 520 ? -34.89900 -31.24300 34.11100  1.000 33.08555 ? 516 TYR A N      1 
ATOM   3639 C  CA     . TYR A 1 520 ? -35.23400 -32.66100 34.17200  1.000 33.24083 ? 516 TYR A CA     1 
ATOM   3640 C  C      . TYR A 1 520 ? -34.58500 -33.37600 32.99800  1.000 34.40676 ? 516 TYR A C      1 
ATOM   3641 O  O      . TYR A 1 520 ? -34.51300 -32.83200 31.89500  1.000 35.62532 ? 516 TYR A O      1 
ATOM   3642 C  CB     . TYR A 1 520 ? -36.74500 -32.91700 34.11000  1.000 33.91196 ? 516 TYR A CB     1 
ATOM   3643 C  CG     . TYR A 1 520 ? -37.58200 -32.30800 35.21600  1.000 42.31823 ? 516 TYR A CG     1 
ATOM   3644 C  CD1    . TYR A 1 520 ? -37.71400 -32.94500 36.44500  1.000 41.54709 ? 516 TYR A CD1    1 
ATOM   3645 C  CD2    . TYR A 1 520 ? -38.28500 -31.12200 35.01200  1.000 44.45533 ? 516 TYR A CD2    1 
ATOM   3646 C  CE1    . TYR A 1 520 ? -38.49400 -32.40300 37.44800  1.000 46.87667 ? 516 TYR A CE1    1 
ATOM   3647 C  CE2    . TYR A 1 520 ? -39.06900 -30.57400 36.00900  1.000 43.65523 ? 516 TYR A CE2    1 
ATOM   3648 C  CZ     . TYR A 1 520 ? -39.17200 -31.21800 37.22500  1.000 50.30603 ? 516 TYR A CZ     1 
ATOM   3649 O  OH     . TYR A 1 520 ? -39.95200 -30.67900 38.22500  1.000 51.46407 ? 516 TYR A OH     1 
ATOM   3650 N  N      . ARG A 1 521 ? -34.13300 -34.59500 33.22800  1.000 32.40652 ? 517 ARG A N      1 
ATOM   3651 C  CA     . ARG A 1 521 ? -33.65900 -35.46100 32.15900  1.000 36.57281 ? 517 ARG A CA     1 
ATOM   3652 C  C      . ARG A 1 521 ? -34.74000 -36.49400 31.86900  1.000 40.53907 ? 517 ARG A C      1 
ATOM   3653 O  O      . ARG A 1 521 ? -35.27600 -37.11200 32.79300  1.000 41.62604 ? 517 ARG A O      1 
ATOM   3654 C  CB     . ARG A 1 521 ? -32.34300 -36.14300 32.55700  1.000 37.73874 ? 517 ARG A CB     1 
ATOM   3655 C  CG     . ARG A 1 521 ? -31.87400 -37.25600 31.62100  1.000 42.91041 ? 517 ARG A CG     1 
ATOM   3656 C  CD     . ARG A 1 521 ? -31.23100 -36.71700 30.33400  1.000 49.25064 ? 517 ARG A CD     1 
ATOM   3657 N  NE     . ARG A 1 521 ? -30.58800 -37.78900 29.56600  1.000 58.19908 ? 517 ARG A NE     1 
ATOM   3658 C  CZ     . ARG A 1 521 ? -30.19600 -37.70300 28.29100  1.000 55.17504 ? 517 ARG A CZ     1 
ATOM   3659 N  NH1    . ARG A 1 521 ? -30.36600 -36.57900 27.59200  1.000 41.80501 ? 517 ARG A NH1    1 
ATOM   3660 N  NH2    . ARG A 1 521 ? -29.62600 -38.75600 27.71100  1.000 49.83229 ? 517 ARG A NH2    1 
ATOM   3661 N  N      . ALA A 1 522 ? -35.06200 -36.68400 30.59100  1.000 37.77032 ? 518 ALA A N      1 
ATOM   3662 C  CA     . ALA A 1 522 ? -36.12400 -37.61100 30.20800  1.000 37.84664 ? 518 ALA A CA     1 
ATOM   3663 C  C      . ALA A 1 522 ? -35.57400 -38.59300 29.18700  1.000 43.57628 ? 518 ALA A C      1 
ATOM   3664 O  O      . ALA A 1 522 ? -35.18100 -38.19300 28.08400  1.000 43.00516 ? 518 ALA A O      1 
ATOM   3665 C  CB     . ALA A 1 522 ? -37.34100 -36.87700 29.63600  1.000 33.82511 ? 518 ALA A CB     1 
ATOM   3666 N  N      . GLU A 1 523 ? -35.54300 -39.87200 29.55600  1.000 31.99068 ? 519 GLU A N      1 
ATOM   3667 C  CA     . GLU A 1 523 ? -35.14600 -40.92500 28.64000  1.000 37.81769 ? 519 GLU A CA     1 
ATOM   3668 C  C      . GLU A 1 523 ? -36.28700 -41.86000 28.27500  1.000 44.67641 ? 519 GLU A C      1 
ATOM   3669 O  O      . GLU A 1 523 ? -36.10700 -42.70800 27.39200  1.000 42.91830 ? 519 GLU A O      1 
ATOM   3670 C  CB     . GLU A 1 523 ? -33.99000 -41.72900 29.24100  1.000 40.29430 ? 519 GLU A CB     1 
ATOM   3671 C  CG     . GLU A 1 523 ? -32.83300 -40.83400 29.61900  1.000 49.01640 ? 519 GLU A CG     1 
ATOM   3672 C  CD     . GLU A 1 523 ? -31.65500 -41.59800 30.16300  1.000 63.83134 ? 519 GLU A CD     1 
ATOM   3673 O  OE1    . GLU A 1 523 ? -30.58200 -40.97800 30.34900  1.000 68.88457 ? 519 GLU A OE1    1 
ATOM   3674 O  OE2    . GLU A 1 523 ? -31.80200 -42.81500 30.40900  1.000 66.81327 ? 519 GLU A OE2    1 
ATOM   3675 N  N      . THR A 1 524 ? -37.45400 -41.71000 28.90800  1.000 42.98936 ? 520 THR A N      1 
ATOM   3676 C  CA     . THR A 1 524 ? -38.67300 -42.41700 28.54800  1.000 42.12084 ? 520 THR A CA     1 
ATOM   3677 C  C      . THR A 1 524 ? -39.81900 -41.42100 28.45200  1.000 45.14489 ? 520 THR A C      1 
ATOM   3678 O  O      . THR A 1 524 ? -39.78000 -40.33400 29.03800  1.000 40.06007 ? 520 THR A O      1 
ATOM   3679 C  CB     . THR A 1 524 ? -39.04800 -43.48200 29.58100  1.000 42.31297 ? 520 THR A CB     1 
ATOM   3680 O  OG1    . THR A 1 524 ? -39.48900 -42.81900 30.77000  1.000 39.49421 ? 520 THR A OG1    1 
ATOM   3681 C  CG2    . THR A 1 524 ? -37.85100 -44.36200 29.90400  1.000 41.58393 ? 520 THR A CG2    1 
ATOM   3682 N  N      . VAL A 1 525 ? -40.87200 -41.81500 27.73300  1.000 40.26009 ? 521 VAL A N      1 
ATOM   3683 C  CA     . VAL A 1 525 ? -42.00600 -40.91000 27.61200  1.000 42.22348 ? 521 VAL A CA     1 
ATOM   3684 C  C      . VAL A 1 525 ? -42.64000 -40.66700 28.97700  1.000 40.84174 ? 521 VAL A C      1 
ATOM   3685 O  O      . VAL A 1 525 ? -43.19900 -39.59100 29.22700  1.000 43.39468 ? 521 VAL A O      1 
ATOM   3686 C  CB     . VAL A 1 525 ? -43.03100 -41.44000 26.58800  1.000 40.93386 ? 521 VAL A CB     1 
ATOM   3687 C  CG1    . VAL A 1 525 ? -43.65900 -42.71600 27.08100  1.000 37.95455 ? 521 VAL A CG1    1 
ATOM   3688 C  CG2    . VAL A 1 525 ? -44.09800 -40.39400 26.33300  1.000 41.03124 ? 521 VAL A CG2    1 
ATOM   3689 N  N      . GLU A 1 526 ? -42.55000 -41.64600 29.88500  1.000 38.32038 ? 522 GLU A N      1 
ATOM   3690 C  CA     . GLU A 1 526 ? -43.09600 -41.46700 31.23000  1.000 42.06294 ? 522 GLU A CA     1 
ATOM   3691 C  C      . GLU A 1 526 ? -42.31700 -40.40700 31.99500  1.000 39.24944 ? 522 GLU A C      1 
ATOM   3692 O  O      . GLU A 1 526 ? -42.91100 -39.55800 32.67500  1.000 37.64399 ? 522 GLU A O      1 
ATOM   3693 C  CB     . GLU A 1 526 ? -43.07900 -42.79100 31.99500  1.000 42.70512 ? 522 GLU A CB     1 
ATOM   3694 C  CG     . GLU A 1 526 ? -43.97200 -43.86900 31.39100  1.000 53.71170 ? 522 GLU A CG     1 
ATOM   3695 C  CD     . GLU A 1 526 ? -43.28700 -44.63700 30.27000  1.000 61.73372 ? 522 GLU A CD     1 
ATOM   3696 O  OE1    . GLU A 1 526 ? -43.93100 -45.53600 29.69300  1.000 67.41335 ? 522 GLU A OE1    1 
ATOM   3697 O  OE2    . GLU A 1 526 ? -42.10900 -44.35100 29.96800  1.000 60.39408 ? 522 GLU A OE2    1 
ATOM   3698 N  N      . ASP A 1 527 ? -40.98600 -40.43400 31.88300  1.000 34.72258 ? 523 ASP A N      1 
ATOM   3699 C  CA     . ASP A 1 527 ? -40.17700 -39.37800 32.48000  1.000 39.42578 ? 523 ASP A CA     1 
ATOM   3700 C  C      . ASP A 1 527 ? -40.49300 -38.03200 31.84800  1.000 38.50725 ? 523 ASP A C      1 
ATOM   3701 O  O      . ASP A 1 527 ? -40.54200 -37.00800 32.53900  1.000 35.31213 ? 523 ASP A O      1 
ATOM   3702 C  CB     . ASP A 1 527 ? -38.68600 -39.67300 32.30500  1.000 44.45533 ? 523 ASP A CB     1 
ATOM   3703 C  CG     . ASP A 1 527 ? -38.23000 -40.89300 33.07100  1.000 61.44947 ? 523 ASP A CG     1 
ATOM   3704 O  OD1    . ASP A 1 527 ? -38.79500 -41.18300 34.15000  1.000 60.08615 ? 523 ASP A OD1    1 
ATOM   3705 O  OD2    . ASP A 1 527 ? -37.28600 -41.55600 32.58300  1.000 68.95564 ? 523 ASP A OD2    1 
ATOM   3706 N  N      . PHE A 1 528 ? -40.72000 -38.00600 30.53300  1.000 38.22827 ? 524 PHE A N      1 
ATOM   3707 C  CA     . PHE A 1 528 ? -40.98200 -36.72400 29.88200  1.000 33.19872 ? 524 PHE A CA     1 
ATOM   3708 C  C      . PHE A 1 528 ? -42.30400 -36.12600 30.34400  1.000 34.70153 ? 524 PHE A C      1 
ATOM   3709 O  O      . PHE A 1 528 ? -42.37900 -34.92800 30.64600  1.000 36.79652 ? 524 PHE A O      1 
ATOM   3710 C  CB     . PHE A 1 528 ? -40.97200 -36.87200 28.36600  1.000 33.40927 ? 524 PHE A CB     1 
ATOM   3711 C  CG     . PHE A 1 528 ? -41.36200 -35.61900 27.65500  1.000 33.62508 ? 524 PHE A CG     1 
ATOM   3712 C  CD1    . PHE A 1 528 ? -40.52800 -34.51200 27.68200  1.000 33.72773 ? 524 PHE A CD1    1 
ATOM   3713 C  CD2    . PHE A 1 528 ? -42.58700 -35.52200 27.00500  1.000 33.36979 ? 524 PHE A CD2    1 
ATOM   3714 C  CE1    . PHE A 1 528 ? -40.88500 -33.34000 27.03900  1.000 31.23269 ? 524 PHE A CE1    1 
ATOM   3715 C  CE2    . PHE A 1 528 ? -42.94800 -34.35200 26.36000  1.000 37.66241 ? 524 PHE A CE2    1 
ATOM   3716 C  CZ     . PHE A 1 528 ? -42.08900 -33.25700 26.37900  1.000 36.66755 ? 524 PHE A CZ     1 
ATOM   3717 N  N      . ASP A 1 529 ? -43.36400 -36.94400 30.39400  1.000 35.29634 ? 525 ASP A N      1 
ATOM   3718 C  CA     . ASP A 1 529 ? -44.66500 -36.46300 30.85500  1.000 36.13591 ? 525 ASP A CA     1 
ATOM   3719 C  C      . ASP A 1 529 ? -44.57100 -35.90000 32.26600  1.000 38.39934 ? 525 ASP A C      1 
ATOM   3720 O  O      . ASP A 1 529 ? -45.15800 -34.85200 32.56800  1.000 40.13639 ? 525 ASP A O      1 
ATOM   3721 C  CB     . ASP A 1 529 ? -45.69900 -37.59100 30.79200  1.000 45.67653 ? 525 ASP A CB     1 
ATOM   3722 C  CG     . ASP A 1 529 ? -47.12800 -37.08900 30.98300  1.000 63.20758 ? 525 ASP A CG     1 
ATOM   3723 O  OD1    . ASP A 1 529 ? -47.52100 -36.12300 30.28100  1.000 65.35784 ? 525 ASP A OD1    1 
ATOM   3724 O  OD2    . ASP A 1 529 ? -47.86000 -37.65900 31.83300  1.000 66.46323 ? 525 ASP A OD2    1 
ATOM   3725 N  N      . ALA A 1 530 ? -43.82900 -36.57700 33.14300  1.000 33.56718 ? 526 ALA A N      1 
ATOM   3726 C  CA     . ALA A 1 530 ? -43.64600 -36.06400 34.49500  1.000 36.02800 ? 526 ALA A CA     1 
ATOM   3727 C  C      . ALA A 1 530 ? -42.88400 -34.74400 34.47900  1.000 34.71469 ? 526 ALA A C      1 
ATOM   3728 O  O      . ALA A 1 530 ? -43.24900 -33.79300 35.18100  1.000 37.71505 ? 526 ALA A O      1 
ATOM   3729 C  CB     . ALA A 1 530 ? -42.92100 -37.10100 35.35400  1.000 33.90933 ? 526 ALA A CB     1 
ATOM   3730 N  N      . ALA A 1 531 ? -41.85600 -34.64700 33.67400  1.000 30.86423 ? 527 ALA A N      1 
ATOM   3731 C  CA     . ALA A 1 531 ? -41.10700 -33.41400 33.57400  1.000 31.85645 ? 527 ALA A CA     1 
ATOM   3732 C  C      . ALA A 1 531 ? -41.94800 -32.24200 33.08200  1.000 33.48033 ? 527 ALA A C      1 
ATOM   3733 O  O      . ALA A 1 531 ? -41.94800 -31.20900 33.66200  1.000 33.64088 ? 527 ALA A O      1 
ATOM   3734 C  CB     . ALA A 1 531 ? -39.88300 -33.60500 32.72300  1.000 31.02740 ? 527 ALA A CB     1 
ATOM   3735 N  N      . LEU A 1 532 ? -42.71900 -32.44600 32.04600  1.000 35.50952 ? 528 LEU A N      1 
ATOM   3736 C  CA     . LEU A 1 532 ? -43.53500 -31.37700 31.51600  1.000 36.18329 ? 528 LEU A CA     1 
ATOM   3737 C  C      . LEU A 1 532 ? -44.53400 -30.87700 32.54000  1.000 34.50677 ? 528 LEU A C      1 
ATOM   3738 O  O      . LEU A 1 532 ? -44.68900 -29.71400 32.74500  1.000 33.42506 ? 528 LEU A O      1 
ATOM   3739 C  CB     . LEU A 1 532 ? -44.18700 -31.77600 30.21800  1.000 33.79616 ? 528 LEU A CB     1 
ATOM   3740 C  CG     . LEU A 1 532 ? -44.86100 -30.65900 29.45800  1.000 36.57281 ? 528 LEU A CG     1 
ATOM   3741 C  CD1    . LEU A 1 532 ? -43.93600 -29.49900 29.28200  1.000 28.82977 ? 528 LEU A CD1    1 
ATOM   3742 C  CD2    . LEU A 1 532 ? -45.36600 -31.16100 28.14300  1.000 36.77546 ? 528 LEU A CD2    1 
ATOM   3743 N  N      . LYS A 1 533 ? -45.16300 -31.80600 33.21300  1.000 36.23329 ? 529 LYS A N      1 
ATOM   3744 C  CA     . LYS A 1 533 ? -46.09400 -31.49600 34.26300  1.000 41.84712 ? 529 LYS A CA     1 
ATOM   3745 C  C      . LYS A 1 533 ? -45.42700 -30.65600 35.33900  1.000 39.38893 ? 529 LYS A C      1 
ATOM   3746 O  O      . LYS A 1 533 ? -45.94300 -29.68300 35.75900  1.000 38.92309 ? 529 LYS A O      1 
ATOM   3747 C  CB     . LYS A 1 533 ? -46.66200 -32.77500 34.82600  1.000 31.93014 ? 529 LYS A CB     1 
ATOM   3748 C  CG     . LYS A 1 533 ? -47.50200 -32.57700 36.03500  1.000 43.94211 ? 529 LYS A CG     1 
ATOM   3749 C  CD     . LYS A 1 533 ? -48.00700 -33.91700 36.50100  1.000 59.34922 ? 529 LYS A CD     1 
ATOM   3750 C  CE     . LYS A 1 533 ? -49.45200 -34.07500 36.13300  1.000 70.03734 ? 529 LYS A CE     1 
ATOM   3751 N  NZ     . LYS A 1 533 ? -50.22600 -33.13200 36.98500  1.000 80.31752 ? 529 LYS A NZ     1 
ATOM   3752 N  N      . GLY A 1 534 ? -44.26500 -31.05500 35.77600  1.000 35.50163 ? 530 GLY A N      1 
ATOM   3753 C  CA     . GLY A 1 534 ? -43.56600 -30.29500 36.76900  1.000 37.37027 ? 530 GLY A CA     1 
ATOM   3754 C  C      . GLY A 1 534 ? -43.22000 -28.91400 36.26900  1.000 39.35735 ? 530 GLY A C      1 
ATOM   3755 O  O      . GLY A 1 534 ? -43.39300 -27.94400 36.95000  1.000 38.20195 ? 530 GLY A O      1 
ATOM   3756 N  N      . ALA A 1 535 ? -42.74000 -28.85200 35.04200  1.000 34.24095 ? 531 ALA A N      1 
ATOM   3757 C  CA     . ALA A 1 535 ? -42.35600 -27.60000 34.43700  1.000 34.64100 ? 531 ALA A CA     1 
ATOM   3758 C  C      . ALA A 1 535 ? -43.50600 -26.63200 34.32500  1.000 37.44133 ? 531 ALA A C      1 
ATOM   3759 O  O      . ALA A 1 535 ? -43.38100 -25.50100 34.64500  1.000 36.14644 ? 531 ALA A O      1 
ATOM   3760 C  CB     . ALA A 1 535 ? -41.72300 -27.82700 33.09200  1.000 34.31990 ? 531 ALA A CB     1 
ATOM   3761 N  N      . LEU A 1 536 ? -44.64800 -27.10800 33.92200  1.000 33.00133 ? 532 LEU A N      1 
ATOM   3762 C  CA     . LEU A 1 536 ? -45.79000 -26.21500 33.76900  1.000 36.44648 ? 532 LEU A CA     1 
ATOM   3763 C  C      . LEU A 1 536 ? -46.23600 -25.61800 35.10200  1.000 41.10230 ? 532 LEU A C      1 
ATOM   3764 O  O      . LEU A 1 536 ? -46.66100 -24.45800 35.15300  1.000 38.35723 ? 532 LEU A O      1 
ATOM   3765 C  CB     . LEU A 1 536 ? -46.94600 -26.96600 33.10400  1.000 36.70966 ? 532 LEU A CB     1 
ATOM   3766 C  CG     . LEU A 1 536 ? -46.65700 -27.26600 31.63500  1.000 42.36297 ? 532 LEU A CG     1 
ATOM   3767 C  CD1    . LEU A 1 536 ? -47.59100 -28.33800 31.10100  1.000 47.66098 ? 532 LEU A CD1    1 
ATOM   3768 C  CD2    . LEU A 1 536 ? -46.76800 -25.98700 30.81700  1.000 37.88612 ? 532 LEU A CD2    1 
ATOM   3769 N  N      . ALA A 1 537 ? -46.08900 -26.35200 36.18800  1.000 35.32529 ? 533 ALA A N      1 
ATOM   3770 C  CA     . ALA A 1 537 ? -46.48900 -25.84500 37.48400  1.000 38.88887 ? 533 ALA A CA     1 
ATOM   3771 C  C      . ALA A 1 537 ? -45.51500 -24.90200 38.15100  1.000 44.57640 ? 533 ALA A C      1 
ATOM   3772 O  O      . ALA A 1 537 ? -45.84800 -24.29900 39.11300  1.000 47.02143 ? 533 ALA A O      1 
ATOM   3773 C  CB     . ALA A 1 537 ? -46.85300 -26.96600 38.42400  1.000 32.34335 ? 533 ALA A CB     1 
ATOM   3774 N  N      . MET A 1 538 ? -44.31100 -24.78100 37.64300  1.000 39.98901 ? 534 MET A N      1 
ATOM   3775 C  CA     . MET A 1 538 ? -43.35100 -23.86700 38.21800  1.000 46.81088 ? 534 MET A CA     1 
ATOM   3776 C  C      . MET A 1 538 ? -43.62400 -22.42900 37.84600  1.000 47.34515 ? 534 MET A C      1 
ATOM   3777 O  O      . MET A 1 538 ? -44.23000 -22.14900 36.87600  1.000 63.90766 ? 534 MET A O      1 
ATOM   3778 C  CB     . MET A 1 538 ? -41.96400 -24.19900 37.71500  1.000 43.69734 ? 534 MET A CB     1 
ATOM   3779 C  CG     . MET A 1 538 ? -41.35100 -25.40900 38.34300  1.000 54.56181 ? 534 MET A CG     1 
ATOM   3780 S  SD     . MET A 1 538 ? -39.97700 -26.08900 37.45500  1.000 49.20327 ? 534 MET A SD     1 
ATOM   3781 C  CE     . MET A 1 538 ? -38.70400 -25.14800 38.15800  1.000 54.91711 ? 534 MET A CE     1 
ATOM   3782 N  N      . ASN A 1 539 ? -43.18300 -21.50500 38.64700  1.000 41.92345 ? 535 ASN A N      1 
ATOM   3783 C  CA     . ASN A 1 539 ? -43.31900 -20.11700 38.28600  1.000 54.33546 ? 535 ASN A CA     1 
ATOM   3784 C  C      . ASN A 1 539 ? -41.92300 -19.63600 38.10700  1.000 57.24897 ? 535 ASN A C      1 
ATOM   3785 O  O      . ASN A 1 539 ? -41.60400 -18.56000 38.48100  1.000 52.06940 ? 535 ASN A O      1 
ATOM   3786 C  CB     . ASN A 1 539 ? -44.02100 -19.31200 39.36200  1.000 66.78959 ? 535 ASN A CB     1 
ATOM   3787 C  CG     . ASN A 1 539 ? -43.30400 -19.32600 40.68200  1.000 74.58789 ? 535 ASN A CG     1 
ATOM   3788 O  OD1    . ASN A 1 539 ? -43.58100 -18.51100 41.52200  1.000 74.96425 ? 535 ASN A OD1    1 
ATOM   3789 N  ND2    . ASN A 1 539 ? -42.40400 -20.24900 40.87900  1.000 70.55056 ? 535 ASN A ND2    1 
ATOM   3790 N  N      . THR A 1 540 ? -41.07800 -20.49800 37.56800  1.000 51.83779 ? 536 THR A N      1 
ATOM   3791 C  CA     . THR A 1 540 ? -39.68900 -20.21300 37.35100  1.000 42.22875 ? 536 THR A CA     1 
ATOM   3792 C  C      . THR A 1 540 ? -39.35700 -20.97700 36.05800  1.000 38.87571 ? 536 THR A C      1 
ATOM   3793 O  O      . THR A 1 540 ? -39.99500 -21.92800 35.69300  1.000 35.92273 ? 536 THR A O      1 
ATOM   3794 C  CB     . THR A 1 540 ? -38.68700 -20.58300 38.46900  1.000 45.94761 ? 536 THR A CB     1 
ATOM   3795 O  OG1    . THR A 1 540 ? -38.65000 -21.97700 38.64300  1.000 47.50043 ? 536 THR A OG1    1 
ATOM   3796 C  CG2    . THR A 1 540 ? -38.97800 -19.90700 39.75100  1.000 43.03411 ? 536 THR A CG2    1 
ATOM   3797 N  N      . PRO A 1 541 ? -38.30100 -20.57700 35.38500  1.000 32.58812 ? 537 PRO A N      1 
ATOM   3798 C  CA     . PRO A 1 541 ? -37.95000 -21.29000 34.16700  1.000 31.22480 ? 537 PRO A CA     1 
ATOM   3799 C  C      . PRO A 1 541 ? -37.52600 -22.73200 34.40400  1.000 30.76421 ? 537 PRO A C      1 
ATOM   3800 O  O      . PRO A 1 541 ? -37.02500 -23.08300 35.42800  1.000 37.69399 ? 537 PRO A O      1 
ATOM   3801 C  CB     . PRO A 1 541 ? -36.82100 -20.47100 33.59400  1.000 31.36692 ? 537 PRO A CB     1 
ATOM   3802 C  CG     . PRO A 1 541 ? -36.31800 -19.66100 34.70100  1.000 36.34646 ? 537 PRO A CG     1 
ATOM   3803 C  CD     . PRO A 1 541 ? -37.35600 -19.53200 35.72900  1.000 32.32230 ? 537 PRO A CD     1 
ATOM   3804 N  N      . CYS A 1 542 ? -37.68400 -23.54500 33.39800  1.000 30.61157 ? 538 CYS A N      1 
ATOM   3805 C  CA     . CYS A 1 542 ? -37.38400 -24.96900 33.48400  1.000 28.74292 ? 538 CYS A CA     1 
ATOM   3806 C  C      . CYS A 1 542 ? -36.85300 -25.48800 32.15400  1.000 30.78790 ? 538 CYS A C      1 
ATOM   3807 O  O      . CYS A 1 542 ? -37.29300 -25.07300 31.08000  1.000 27.55067 ? 538 CYS A O      1 
ATOM   3808 C  CB     . CYS A 1 542 ? -38.62600 -25.78400 33.87500  1.000 30.73526 ? 538 CYS A CB     1 
ATOM   3809 S  SG     . CYS A 1 542 ? -38.29300 -27.52700 34.23200  1.000 38.15194 ? 538 CYS A SG     1 
ATOM   3810 N  N      . LEU A 1 543 ? -35.93900 -26.45100 32.23800  1.000 26.79005 ? 539 LEU A N      1 
ATOM   3811 C  CA     . LEU A 1 543 ? -35.37000 -27.07500 31.05300  1.000 28.98242 ? 539 LEU A CA     1 
ATOM   3812 C  C      . LEU A 1 543 ? -35.56800 -28.57800 31.15000  1.000 31.17742 ? 539 LEU A C      1 
ATOM   3813 O  O      . LEU A 1 543 ? -35.37100 -29.17100 32.21500  1.000 27.93230 ? 539 LEU A O      1 
ATOM   3814 C  CB     . LEU A 1 543 ? -33.88000 -26.74900 30.88500  1.000 27.35854 ? 539 LEU A CB     1 
ATOM   3815 C  CG     . LEU A 1 543 ? -33.22700 -27.33900 29.63100  1.000 29.49827 ? 539 LEU A CG     1 
ATOM   3816 C  CD1    . LEU A 1 543 ? -32.15900 -26.39400 29.09100  1.000 34.36991 ? 539 LEU A CD1    1 
ATOM   3817 C  CD2    . LEU A 1 543 ? -32.63500 -28.72900 29.89500  1.000 29.02980 ? 539 LEU A CD2    1 
ATOM   3818 N  N      . ILE A 1 544 ? -35.97900 -29.18800 30.04200  1.000 29.07454 ? 540 ILE A N      1 
ATOM   3819 C  CA     . ILE A 1 544 ? -36.17000 -30.63000 29.96500  1.000 29.09296 ? 540 ILE A CA     1 
ATOM   3820 C  C      . ILE A 1 544 ? -35.22800 -31.17500 28.89300  1.000 33.03028 ? 540 ILE A C      1 
ATOM   3821 O  O      . ILE A 1 544 ? -35.34000 -30.81500 27.71300  1.000 27.15852 ? 540 ILE A O      1 
ATOM   3822 C  CB     . ILE A 1 544 ? -37.63400 -30.98600 29.66400  1.000 32.23018 ? 540 ILE A CB     1 
ATOM   3823 C  CG1    . ILE A 1 544 ? -38.55900 -30.39400 30.74700  1.000 28.05336 ? 540 ILE A CG1    1 
ATOM   3824 C  CG2    . ILE A 1 544 ? -37.80700 -32.49200 29.55600  1.000 26.27947 ? 540 ILE A CG2    1 
ATOM   3825 C  CD1    . ILE A 1 544 ? -40.03900 -30.50800 30.42800  1.000 28.82714 ? 540 ILE A CD1    1 
ATOM   3826 N  N      . ASP A 1 545 ? -34.30900 -32.04100 29.30500  1.000 29.52986 ? 541 ASP A N      1 
ATOM   3827 C  CA     . ASP A 1 545 ? -33.28200 -32.61300 28.43400  1.000 31.59589 ? 541 ASP A CA     1 
ATOM   3828 C  C      . ASP A 1 545 ? -33.77500 -33.98800 27.96800  1.000 34.85418 ? 541 ASP A C      1 
ATOM   3829 O  O      . ASP A 1 545 ? -33.81900 -34.93800 28.75600  1.000 34.04619 ? 541 ASP A O      1 
ATOM   3830 C  CB     . ASP A 1 545 ? -31.96100 -32.70700 29.20400  1.000 35.42267 ? 541 ASP A CB     1 
ATOM   3831 C  CG     . ASP A 1 545 ? -30.78700 -33.21900 28.35400  1.000 41.57604 ? 541 ASP A CG     1 
ATOM   3832 O  OD1    . ASP A 1 545 ? -30.99700 -33.63700 27.20100  1.000 48.73742 ? 541 ASP A OD1    1 
ATOM   3833 O  OD2    . ASP A 1 545 ? -29.64100 -33.22000 28.86500  1.000 38.70464 ? 541 ASP A OD2    1 
ATOM   3834 N  N      . VAL A 1 546 ? -34.17700 -34.09100 26.70000  1.000 32.45389 ? 542 VAL A N      1 
ATOM   3835 C  CA     . VAL A 1 546 ? -34.84200 -35.29100 26.18000  1.000 30.26942 ? 542 VAL A CA     1 
ATOM   3836 C  C      . VAL A 1 546 ? -33.84500 -36.10500 25.35700  1.000 32.76972 ? 542 VAL A C      1 
ATOM   3837 O  O      . VAL A 1 546 ? -33.20600 -35.56900 24.43900  1.000 32.90658 ? 542 VAL A O      1 
ATOM   3838 C  CB     . VAL A 1 546 ? -36.07000 -34.91500 25.32900  1.000 33.81458 ? 542 VAL A CB     1 
ATOM   3839 C  CG1    . VAL A 1 546 ? -36.78900 -36.17100 24.82000  1.000 29.86411 ? 542 VAL A CG1    1 
ATOM   3840 C  CG2    . VAL A 1 546 ? -37.02800 -34.01300 26.11700  1.000 36.83073 ? 542 VAL A CG2    1 
ATOM   3841 N  N      . GLN A 1 547 ? -33.71000 -37.39800 25.67400  1.000 29.74041 ? 543 GLN A N      1 
ATOM   3842 C  CA     . GLN A 1 547 ? -32.84900 -38.26600 24.88100  1.000 34.56730 ? 543 GLN A CA     1 
ATOM   3843 C  C      . GLN A 1 547 ? -33.53400 -38.60900 23.56300  1.000 34.62520 ? 543 GLN A C      1 
ATOM   3844 O  O      . GLN A 1 547 ? -34.66300 -39.09800 23.55100  1.000 38.69148 ? 543 GLN A O      1 
ATOM   3845 C  CB     . GLN A 1 547 ? -32.49500 -39.55100 25.62700  1.000 41.77869 ? 543 GLN A CB     1 
ATOM   3846 C  CG     . GLN A 1 547 ? -31.42500 -40.38400 24.89900  1.000 46.02131 ? 543 GLN A CG     1 
ATOM   3847 C  CD     . GLN A 1 547 ? -31.23100 -41.78800 25.47600  1.000 50.73503 ? 543 GLN A CD     1 
ATOM   3848 O  OE1    . GLN A 1 547 ? -31.83800 -42.15500 26.48200  1.000 52.94845 ? 543 GLN A OE1    1 
ATOM   3849 N  NE2    . GLN A 1 547 ? -30.38000 -42.57800 24.82800  1.000 49.12168 ? 543 GLN A NE2    1 
ATOM   3850 N  N      . VAL A 1 548 ? -32.84600 -38.35800 22.45600  1.000 28.05336 ? 544 VAL A N      1 
ATOM   3851 C  CA     . VAL A 1 548 ? -33.40400 -38.58900 21.12800  1.000 34.80680 ? 544 VAL A CA     1 
ATOM   3852 C  C      . VAL A 1 548 ? -32.34500 -39.23700 20.24700  1.000 36.08854 ? 544 VAL A C      1 
ATOM   3853 O  O      . VAL A 1 548 ? -31.16700 -38.87200 20.30900  1.000 35.83061 ? 544 VAL A O      1 
ATOM   3854 C  CB     . VAL A 1 548 ? -33.90400 -37.27400 20.49700  1.000 37.15972 ? 544 VAL A CB     1 
ATOM   3855 C  CG1    . VAL A 1 548 ? -34.33300 -37.50600 19.05200  1.000 40.16534 ? 544 VAL A CG1    1 
ATOM   3856 C  CG2    . VAL A 1 548 ? -35.07200 -36.71000 21.31800  1.000 39.24418 ? 544 VAL A CG2    1 
ATOM   3857 N  N      . ASP A 1 549 ? -32.77400 -40.17400 19.40100  1.000 38.01772 ? 545 ASP A N      1 
ATOM   3858 C  CA     . ASP A 1 549 ? -31.86500 -40.86700 18.49200  1.000 36.11486 ? 545 ASP A CA     1 
ATOM   3859 C  C      . ASP A 1 549 ? -31.60800 -39.99600 17.25500  1.000 33.87248 ? 545 ASP A C      1 
ATOM   3860 O  O      . ASP A 1 549 ? -32.54400 -39.58500 16.56000  1.000 33.56192 ? 545 ASP A O      1 
ATOM   3861 C  CB     . ASP A 1 549 ? -32.44900 -42.23200 18.12400  1.000 41.87871 ? 545 ASP A CB     1 
ATOM   3862 C  CG     . ASP A 1 549 ? -31.54800 -43.04300 17.19700  1.000 53.38798 ? 545 ASP A CG     1 
ATOM   3863 O  OD1    . ASP A 1 549 ? -30.47800 -42.54500 16.78100  1.000 57.64112 ? 545 ASP A OD1    1 
ATOM   3864 O  OD2    . ASP A 1 549 ? -31.91500 -44.19800 16.88000  1.000 59.85454 ? 545 ASP A OD2    1 
ATOM   3865 N  N      . ILE A 1 550 ? -30.33100 -39.72200 16.97600  1.000 35.29897 ? 546 ILE A N      1 
ATOM   3866 C  CA     . ILE A 1 550 ? -29.98100 -38.83800 15.86700  1.000 33.25399 ? 546 ILE A CA     1 
ATOM   3867 C  C      . ILE A 1 550 ? -30.36700 -39.43400 14.51400  1.000 36.28067 ? 546 ILE A C      1 
ATOM   3868 O  O      . ILE A 1 550 ? -30.47500 -38.69700 13.52700  1.000 37.70189 ? 546 ILE A O      1 
ATOM   3869 C  CB     . ILE A 1 550 ? -28.47400 -38.52400 15.91800  1.000 30.72210 ? 546 ILE A CB     1 
ATOM   3870 C  CG1    . ILE A 1 550 ? -28.16500 -37.20300 15.19900  1.000 32.05648 ? 546 ILE A CG1    1 
ATOM   3871 C  CG2    . ILE A 1 550 ? -27.66400 -39.70300 15.36000  1.000 34.91208 ? 546 ILE A CG2    1 
ATOM   3872 C  CD1    . ILE A 1 550 ? -26.69600 -36.78700 15.28000  1.000 35.53321 ? 546 ILE A CD1    1 
ATOM   3873 N  N      . ASP A 1 551 ? -30.61900 -40.74600 14.45700  1.000 35.79640 ? 547 ASP A N      1 
ATOM   3874 C  CA     . ASP A 1 551 ? -30.89700 -41.45100 13.20900  1.000 39.10469 ? 547 ASP A CA     1 
ATOM   3875 C  C      . ASP A 1 551 ? -32.34800 -41.34900 12.75200  1.000 41.31548 ? 547 ASP A C      1 
ATOM   3876 O  O      . ASP A 1 551 ? -32.63100 -41.68800 11.59900  1.000 40.85227 ? 547 ASP A O      1 
ATOM   3877 C  CB     . ASP A 1 551 ? -30.56700 -42.93900 13.34800  1.000 34.80944 ? 547 ASP A CB     1 
ATOM   3878 C  CG     . ASP A 1 551 ? -29.09600 -43.22300 13.25400  1.000 56.68311 ? 547 ASP A CG     1 
ATOM   3879 O  OD1    . ASP A 1 551 ? -28.38700 -42.48500 12.53900  1.000 65.03675 ? 547 ASP A OD1    1 
ATOM   3880 O  OD2    . ASP A 1 551 ? -28.64900 -44.19200 13.90100  1.000 69.22672 ? 547 ASP A OD2    1 
ATOM   3881 N  N      . VAL A 1 552 ? -33.27700 -40.94700 13.62700  1.000 40.12060 ? 548 VAL A N      1 
ATOM   3882 C  CA     . VAL A 1 552 ? -34.69300 -40.96400 13.25700  1.000 39.25471 ? 548 VAL A CA     1 
ATOM   3883 C  C      . VAL A 1 552 ? -34.94100 -39.98100 12.12400  1.000 35.44899 ? 548 VAL A C      1 
ATOM   3884 O  O      . VAL A 1 552 ? -34.49100 -38.83100 12.16800  1.000 44.12898 ? 548 VAL A O      1 
ATOM   3885 C  CB     . VAL A 1 552 ? -35.58100 -40.63400 14.46300  1.000 44.47375 ? 548 VAL A CB     1 
ATOM   3886 C  CG1    . VAL A 1 552 ? -37.05200 -40.67500 14.04300  1.000 43.35520 ? 548 VAL A CG1    1 
ATOM   3887 C  CG2    . VAL A 1 552 ? -35.31700 -41.59700 15.62100  1.000 45.18173 ? 548 VAL A CG2    1 
ATOM   3888 N  N      . LEU A 1 553 ? -35.68400 -40.41100 11.11200  1.000 35.01999 ? 549 LEU A N      1 
ATOM   3889 C  CA     . LEU A 1 553 ? -35.92100 -39.53500 9.97300   1.000 40.50222 ? 549 LEU A CA     1 
ATOM   3890 C  C      . LEU A 1 553 ? -37.17300 -38.70800 10.22000  1.000 35.07789 ? 549 LEU A C      1 
ATOM   3891 O  O      . LEU A 1 553 ? -38.24700 -39.28200 10.40700  1.000 39.13364 ? 549 LEU A O      1 
ATOM   3892 C  CB     . LEU A 1 553 ? -36.06000 -40.33100 8.68800   1.000 44.62377 ? 549 LEU A CB     1 
ATOM   3893 C  CG     . LEU A 1 553 ? -36.12900 -39.38200 7.48800   1.000 56.48572 ? 549 LEU A CG     1 
ATOM   3894 C  CD1    . LEU A 1 553 ? -34.74800 -39.12200 6.88700   1.000 60.14669 ? 549 LEU A CD1    1 
ATOM   3895 C  CD2    . LEU A 1 553 ? -37.09000 -39.89400 6.42700   1.000 61.57317 ? 549 LEU A CD2    1 
ATOM   3896 N  N      . PRO A 1 554 ? -37.09000 -37.38200 10.23700  1.000 38.86519 ? 550 PRO A N      1 
ATOM   3897 C  CA     . PRO A 1 554 ? -38.26000 -36.57000 10.58300  1.000 39.68634 ? 550 PRO A CA     1 
ATOM   3898 C  C      . PRO A 1 554 ? -39.26300 -36.51600 9.44600   1.000 39.08627 ? 550 PRO A C      1 
ATOM   3899 O  O      . PRO A 1 554 ? -38.90800 -36.69000 8.27000   1.000 33.62508 ? 550 PRO A O      1 
ATOM   3900 C  CB     . PRO A 1 554 ? -37.66500 -35.17600 10.85100  1.000 38.39145 ? 550 PRO A CB     1 
ATOM   3901 C  CG     . PRO A 1 554 ? -36.19600 -35.39200 11.02800  1.000 38.12562 ? 550 PRO A CG     1 
ATOM   3902 C  CD     . PRO A 1 554 ? -35.86800 -36.56600 10.14700  1.000 39.71002 ? 550 PRO A CD     1 
ATOM   3903 N  N      . PRO A 1 555 ? -40.49900 -36.23000 9.73700   1.000 37.21499 ? 551 PRO A N      1 
ATOM   3904 C  CA     . PRO A 1 555 ? -41.51900 -36.11200 8.71200   1.000 37.81769 ? 551 PRO A CA     1 
ATOM   3905 C  C      . PRO A 1 555 ? -41.15300 -35.12500 7.63000   1.000 43.01832 ? 551 PRO A C      1 
ATOM   3906 O  O      . PRO A 1 555 ? -40.67300 -34.06000 7.92300   1.000 45.50019 ? 551 PRO A O      1 
ATOM   3907 C  CB     . PRO A 1 555 ? -42.73200 -35.61600 9.47600   1.000 38.99678 ? 551 PRO A CB     1 
ATOM   3908 C  CG     . PRO A 1 555 ? -42.31700 -35.49400 10.88000  1.000 39.54158 ? 551 PRO A CG     1 
ATOM   3909 C  CD     . PRO A 1 555 ? -41.06500 -36.23500 11.07000  1.000 40.51538 ? 551 PRO A CD     1 
ATOM   3910 N  N      . GLY A 1 556 ? -41.30600 -35.53600 6.38900   1.000 41.62604 ? 552 GLY A N      1 
ATOM   3911 C  CA     . GLY A 1 556 ? -41.00500 -34.68800 5.27500   1.000 45.41597 ? 552 GLY A CA     1 
ATOM   3912 C  C      . GLY A 1 556 ? -39.58400 -34.62500 4.79700   1.000 55.17504 ? 552 GLY A C      1 
ATOM   3913 O  O      . GLY A 1 556 ? -39.32500 -33.99800 3.80900   1.000 53.92752 ? 552 GLY A O      1 
ATOM   3914 N  N      . MET A 1 557 ? -38.67200 -35.29700 5.47500   1.000 57.64639 ? 553 MET A N      1 
ATOM   3915 C  CA     . MET A 1 557 ? -37.26900 -35.24000 5.11700   1.000 55.28031 ? 553 MET A CA     1 
ATOM   3916 C  C      . MET A 1 557 ? -36.95600 -36.07400 3.91200   1.000 53.34324 ? 553 MET A C      1 
ATOM   3917 O  O      . MET A 1 557 ? -36.23600 -35.67400 3.05700   1.000 55.42243 ? 553 MET A O      1 
ATOM   3918 C  CB     . MET A 1 557 ? -36.39100 -35.64000 6.26700   1.000 51.04823 ? 553 MET A CB     1 
ATOM   3919 C  CG     . MET A 1 557 ? -35.64600 -34.50400 6.91400   1.000 59.63347 ? 553 MET A CG     1 
ATOM   3920 S  SD     . MET A 1 557 ? -35.81800 -32.87500 6.19400   1.000 62.34695 ? 553 MET A SD     1 
ATOM   3921 C  CE     . MET A 1 557 ? -34.21700 -32.61000 5.52600   1.000 64.23402 ? 553 MET A CE     1 
ATOM   3922 N  N      . LYS A 1 558 ? -37.52300 -37.24300 3.85500   1.000 57.50426 ? 554 LYS A N      1 
ATOM   3923 C  CA     . LYS A 1 558 ? -37.34500 -38.09100 2.71200   1.000 66.90539 ? 554 LYS A CA     1 
ATOM   3924 C  C      . LYS A 1 558 ? -37.83600 -37.38200 1.43300   1.000 76.81184 ? 554 LYS A C      1 
ATOM   3925 O  O      . LYS A 1 558 ? -37.18800 -37.40600 0.41600   1.000 82.14406 ? 554 LYS A O      1 
ATOM   3926 C  CB     . LYS A 1 558 ? -38.11000 -39.38000 2.91700   1.000 63.79975 ? 554 LYS A CB     1 
ATOM   3927 C  CG     . LYS A 1 558 ? -37.84800 -40.38900 1.84000   1.000 70.87166 ? 554 LYS A CG     1 
ATOM   3928 C  CD     . LYS A 1 558 ? -36.37900 -40.42300 1.48100   1.000 72.66924 ? 554 LYS A CD     1 
ATOM   3929 C  CE     . LYS A 1 558 ? -36.01700 -41.70100 0.73700   1.000 74.20627 ? 554 LYS A CE     1 
ATOM   3930 N  NZ     . LYS A 1 558 ? -36.39100 -41.67800 -0.69500  1.000 75.08269 ? 554 LYS A NZ     1 
ATOM   3931 N  N      . GLN A 1 559 ? -38.98300 -36.74100 1.51100   1.000 71.78229 ? 555 GLN A N      1 
ATOM   3932 C  CA     . GLN A 1 559 ? -39.49300 -36.01900 0.36900   1.000 69.99523 ? 555 GLN A CA     1 
ATOM   3933 C  C      . GLN A 1 559 ? -38.50200 -34.92500 -0.01600  1.000 68.29766 ? 555 GLN A C      1 
ATOM   3934 O  O      . GLN A 1 559 ? -38.15600 -34.78200 -1.15900  1.000 71.16906 ? 555 GLN A O      1 
ATOM   3935 C  CB     . GLN A 1 559 ? -40.85000 -35.39700 0.67600   1.000 73.78779 ? 555 GLN A CB     1 
ATOM   3936 C  CG     . GLN A 1 559 ? -41.98900 -36.35900 0.98900   1.000 77.58825 ? 555 GLN A CG     1 
ATOM   3937 C  CD     . GLN A 1 559 ? -41.75700 -37.27300 2.17100   1.000 82.55463 ? 555 GLN A CD     1 
ATOM   3938 O  OE1    . GLN A 1 559 ? -41.52100 -36.84200 3.30400   1.000 87.28941 ? 555 GLN A OE1    1 
ATOM   3939 N  NE2    . GLN A 1 559 ? -41.84900 -38.55700 1.91600   1.000 79.72008 ? 555 GLN A NE2    1 
ATOM   3940 N  N      . ARG A 1 560 ? -37.99300 -34.17200 0.94700   1.000 64.24191 ? 556 ARG A N      1 
ATOM   3941 C  CA     . ARG A 1 560 ? -37.03300 -33.14000 0.60200   1.000 61.07048 ? 556 ARG A CA     1 
ATOM   3942 C  C      . ARG A 1 560 ? -35.74600 -33.72300 0.04600   1.000 64.13664 ? 556 ARG A C      1 
ATOM   3943 O  O      . ARG A 1 560 ? -35.14600 -33.12200 -0.79000  1.000 67.92130 ? 556 ARG A O      1 
ATOM   3944 C  CB     . ARG A 1 560 ? -36.79500 -32.13800 1.72900   1.000 58.42543 ? 556 ARG A CB     1 
ATOM   3945 C  CG     . ARG A 1 560 ? -37.45600 -30.78100 1.49400   1.000 58.41227 ? 556 ARG A CG     1 
ATOM   3946 C  CD     . ARG A 1 560 ? -36.66300 -29.96700 0.48900   1.000 61.66002 ? 556 ARG A CD     1 
ATOM   3947 N  NE     . ARG A 1 560 ? -37.18900 -28.64900 0.14800   1.000 66.61325 ? 556 ARG A NE     1 
ATOM   3948 C  CZ     . ARG A 1 560 ? -38.45800 -28.37900 -0.10400  1.000 72.02706 ? 556 ARG A CZ     1 
ATOM   3949 N  NH1    . ARG A 1 560 ? -39.37200 -29.32200 -0.05100  1.000 71.56911 ? 556 ARG A NH1    1 
ATOM   3950 N  NH2    . ARG A 1 560 ? -38.81400 -27.16100 -0.40600  1.000 74.24048 ? 556 ARG A NH2    1 
ATOM   3951 N  N      . PHE A 1 561 ? -35.36000 -34.90200 0.48200   1.000 67.49757 ? 557 PHE A N      1 
ATOM   3952 C  CA     . PHE A 1 561 ? -34.14100 -35.49800 -0.02700  1.000 71.66122 ? 557 PHE A CA     1 
ATOM   3953 C  C      . PHE A 1 561 ? -34.25800 -35.94200 -1.49100  1.000 77.32506 ? 557 PHE A C      1 
ATOM   3954 O  O      . PHE A 1 561 ? -33.34400 -35.78000 -2.26200  1.000 84.12324 ? 557 PHE A O      1 
ATOM   3955 C  CB     . PHE A 1 561 ? -33.67600 -36.65400 0.86900   1.000 64.90252 ? 557 PHE A CB     1 
ATOM   3956 C  CG     . PHE A 1 561 ? -32.99500 -36.22300 2.15000   1.000 59.00971 ? 557 PHE A CG     1 
ATOM   3957 C  CD1    . PHE A 1 561 ? -32.16300 -35.15100 2.18200   1.000 60.15195 ? 557 PHE A CD1    1 
ATOM   3958 C  CD2    . PHE A 1 561 ? -33.19000 -36.91600 3.30200   1.000 58.79916 ? 557 PHE A CD2    1 
ATOM   3959 C  CE1    . PHE A 1 561 ? -31.53900 -34.77500 3.32900   1.000 61.91795 ? 557 PHE A CE1    1 
ATOM   3960 C  CE2    . PHE A 1 561 ? -32.57600 -36.54400 4.46400   1.000 59.19394 ? 557 PHE A CE2    1 
ATOM   3961 C  CZ     . PHE A 1 561 ? -31.75000 -35.46500 4.47800   1.000 59.16236 ? 557 PHE A CZ     1 
ATOM   3962 N  N      . ASP A 1 562 ? -35.39300 -36.46900 -1.89300  1.000 30.00000 ? 558 ASP A N      1 
ATOM   3963 C  CA     . ASP A 1 562 ? -35.51500 -36.94500 -3.26500  1.000 30.00000 ? 558 ASP A CA     1 
ATOM   3964 C  C      . ASP A 1 562 ? -35.42500 -35.85400 -4.33400  1.000 30.00000 ? 558 ASP A C      1 
ATOM   3965 O  O      . ASP A 1 562 ? -36.37300 -35.13300 -4.57400  1.000 30.00000 ? 558 ASP A O      1 
ATOM   3966 C  CB     . ASP A 1 562 ? -36.76600 -37.80100 -3.43800  1.000 30.00000 ? 558 ASP A CB     1 
ATOM   3967 C  CG     . ASP A 1 562 ? -36.71600 -39.07700 -2.61900  1.000 30.00000 ? 558 ASP A CG     1 
ATOM   3968 O  OD1    . ASP A 1 562 ? -35.63100 -39.48300 -2.17600  1.000 30.00000 ? 558 ASP A OD1    1 
ATOM   3969 O  OD2    . ASP A 1 562 ? -37.76600 -39.68100 -2.40400  1.000 30.00000 ? 558 ASP A OD2    1 
ATOM   3970 N  N      . SER B 1 3   ? -8.36900  -29.93000 -22.68700 1.000 75.50379 ? -1  SER B N      1 
ATOM   3971 C  CA     . SER B 1 3   ? -9.08600  -31.11100 -22.25100 1.000 76.27757 ? -1  SER B CA     1 
ATOM   3972 C  C      . SER B 1 3   ? -8.36400  -31.66100 -21.04000 1.000 81.21500 ? -1  SER B C      1 
ATOM   3973 O  O      . SER B 1 3   ? -8.38700  -32.84100 -20.78200 1.000 91.77679 ? -1  SER B O      1 
ATOM   3974 C  CB     . SER B 1 3   ? -9.22800  -32.12500 -23.40900 1.000 74.85371 ? -1  SER B CB     1 
ATOM   3975 O  OG     . SER B 1 3   ? -9.78000  -33.36600 -23.01900 1.000 77.13030 ? -1  SER B OG     1 
ATOM   3976 N  N      . SER B 1 4   ? -7.78600  -30.76100 -20.25400 1.000 78.51994 ? 0   SER B N      1 
ATOM   3977 C  CA     . SER B 1 4   ? -7.03000  -31.03700 -19.02300 1.000 76.85922 ? 0   SER B CA     1 
ATOM   3978 C  C      . SER B 1 4   ? -7.81500  -31.51400 -17.76900 1.000 74.11152 ? 0   SER B C      1 
ATOM   3979 O  O      . SER B 1 4   ? -9.00900  -31.41000 -17.66600 1.000 74.40892 ? 0   SER B O      1 
ATOM   3980 C  CB     . SER B 1 4   ? -6.34800  -29.81400 -18.50500 1.000 72.53764 ? 0   SER B CB     1 
ATOM   3981 O  OG     . SER B 1 4   ? -7.14300  -28.64000 -18.54100 1.000 69.02670 ? 0   SER B OG     1 
ATOM   3982 N  N      . LYS B 1 5   ? -7.02900  -31.96900 -16.78800 1.000 72.22708 ? 1   LYS B N      1 
ATOM   3983 C  CA     . LYS B 1 5   ? -7.54400  -32.63400 -15.60400 1.000 67.12647 ? 1   LYS B CA     1 
ATOM   3984 C  C      . LYS B 1 5   ? -8.53800  -31.79600 -14.88100 1.000 59.43607 ? 1   LYS B C      1 
ATOM   3985 O  O      . LYS B 1 5   ? -8.20700  -30.68600 -14.57700 1.000 61.13101 ? 1   LYS B O      1 
ATOM   3986 C  CB     . LYS B 1 5   ? -6.42400  -33.02700 -14.64800 1.000 63.53130 ? 1   LYS B CB     1 
ATOM   3987 C  CG     . LYS B 1 5   ? -6.86600  -33.28300 -13.22100 1.000 60.32039 ? 1   LYS B CG     1 
ATOM   3988 C  CD     . LYS B 1 5   ? -6.08600  -34.34900 -12.47400 1.000 59.20184 ? 1   LYS B CD     1 
ATOM   3989 C  CE     . LYS B 1 5   ? -4.71200  -33.89800 -12.05700 1.000 58.84916 ? 1   LYS B CE     1 
ATOM   3990 N  NZ     . LYS B 1 5   ? -4.21200  -34.63300 -10.86500 1.000 55.32769 ? 1   LYS B NZ     1 
ATOM   3991 N  N      . THR B 1 6   ? -9.72100  -32.29500 -14.58700 1.000 54.84605 ? 2   THR B N      1 
ATOM   3992 C  CA     . THR B 1 6   ? -10.66800 -31.48800 -13.83600 1.000 47.28198 ? 2   THR B CA     1 
ATOM   3993 C  C      . THR B 1 6   ? -11.06200 -31.98000 -12.45700 1.000 43.25255 ? 2   THR B C      1 
ATOM   3994 O  O      . THR B 1 6   ? -11.15100 -33.14000 -12.19000 1.000 40.67593 ? 2   THR B O      1 
ATOM   3995 C  CB     . THR B 1 6   ? -11.98900 -31.28100 -14.55400 1.000 43.38152 ? 2   THR B CB     1 
ATOM   3996 O  OG1    . THR B 1 6   ? -12.79600 -32.43500 -14.38600 1.000 49.44277 ? 2   THR B OG1    1 
ATOM   3997 C  CG2    . THR B 1 6   ? -11.80800 -31.00600 -15.97800 1.000 44.39480 ? 2   THR B CG2    1 
ATOM   3998 N  N      . VAL B 1 7   ? -11.32900 -31.01600 -11.60600 1.000 44.67904 ? 3   VAL B N      1 
ATOM   3999 C  CA     . VAL B 1 7   ? -11.85300 -31.24900 -10.28900 1.000 41.84975 ? 3   VAL B CA     1 
ATOM   4000 C  C      . VAL B 1 7   ? -13.06600 -30.35600 -10.10600 1.000 41.82607 ? 3   VAL B C      1 
ATOM   4001 O  O      . VAL B 1 7   ? -13.35200 -29.50600 -10.91200 1.000 38.28880 ? 3   VAL B O      1 
ATOM   4002 C  CB     . VAL B 1 7   ? -10.84000 -30.93100 -9.19400  1.000 32.02752 ? 3   VAL B CB     1 
ATOM   4003 C  CG1    . VAL B 1 7   ? -9.67300  -31.85600 -9.25700  1.000 31.37481 ? 3   VAL B CG1    1 
ATOM   4004 C  CG2    . VAL B 1 7   ? -10.38800 -29.50900 -9.25900  1.000 32.98027 ? 3   VAL B CG2    1 
ATOM   4005 N  N      . THR B 1 8   ? -13.77300 -30.52000 -9.00000  1.000 36.88863 ? 4   THR B N      1 
ATOM   4006 C  CA     . THR B 1 8   ? -14.87300 -29.61600 -8.71000  1.000 36.81494 ? 4   THR B CA     1 
ATOM   4007 C  C      . THR B 1 8   ? -14.32300 -28.25600 -8.30400  1.000 34.07514 ? 4   THR B C      1 
ATOM   4008 O  O      . THR B 1 8   ? -13.18800 -28.13500 -7.83400  1.000 30.40101 ? 4   THR B O      1 
ATOM   4009 C  CB     . THR B 1 8   ? -15.77900 -30.17000 -7.61000  1.000 37.83085 ? 4   THR B CB     1 
ATOM   4010 O  OG1    . THR B 1 8   ? -15.02900 -30.31400 -6.40000  1.000 34.99367 ? 4   THR B OG1    1 
ATOM   4011 C  CG2    . THR B 1 8   ? -16.36100 -31.52800 -8.02800  1.000 34.20936 ? 4   THR B CG2    1 
ATOM   4012 N  N      . ALA B 1 9   ? -15.13100 -27.21600 -8.53100  1.000 33.68825 ? 5   ALA B N      1 
ATOM   4013 C  CA     . ALA B 1 9   ? -14.70700 -25.87200 -8.14700  1.000 31.76170 ? 5   ALA B CA     1 
ATOM   4014 C  C      . ALA B 1 9   ? -14.33000 -25.82000 -6.67300  1.000 35.13842 ? 5   ALA B C      1 
ATOM   4015 O  O      . ALA B 1 9   ? -13.33100 -25.19700 -6.29200  1.000 30.58788 ? 5   ALA B O      1 
ATOM   4016 C  CB     . ALA B 1 9   ? -15.81200 -24.86200 -8.45600  1.000 27.91651 ? 5   ALA B CB     1 
ATOM   4017 N  N      . VAL B 1 10  ? -15.11200 -26.48500 -5.82300  1.000 31.88540 ? 6   VAL B N      1 
ATOM   4018 C  CA     . VAL B 1 10  ? -14.83600 -26.39100 -4.39700  1.000 32.05121 ? 6   VAL B CA     1 
ATOM   4019 C  C      . VAL B 1 10  ? -13.58800 -27.18700 -4.03900  1.000 30.49313 ? 6   VAL B C      1 
ATOM   4020 O  O      . VAL B 1 10  ? -12.87000 -26.83200 -3.09500  1.000 36.25961 ? 6   VAL B O      1 
ATOM   4021 C  CB     . VAL B 1 10  ? -16.08100 -26.82200 -3.59100  1.000 37.75979 ? 6   VAL B CB     1 
ATOM   4022 C  CG1    . VAL B 1 10  ? -16.25700 -28.33400 -3.60600  1.000 33.84616 ? 6   VAL B CG1    1 
ATOM   4023 C  CG2    . VAL B 1 10  ? -16.00300 -26.29600 -2.17500  1.000 41.99188 ? 6   VAL B CG2    1 
ATOM   4024 N  N      . GLU B 1 11  ? -13.28000 -28.25600 -4.78300  1.000 28.84556 ? 7   GLU B N      1 
ATOM   4025 C  CA     . GLU B 1 11  ? -12.01400 -28.93900 -4.51700  1.000 30.93266 ? 7   GLU B CA     1 
ATOM   4026 C  C      . GLU B 1 11  ? -10.82900 -28.06400 -4.89100  1.000 32.59075 ? 7   GLU B C      1 
ATOM   4027 O  O      . GLU B 1 11  ? -9.82000  -28.03800 -4.17000  1.000 30.57209 ? 7   GLU B O      1 
ATOM   4028 C  CB     . GLU B 1 11  ? -11.92600 -30.27300 -5.25200  1.000 36.17276 ? 7   GLU B CB     1 
ATOM   4029 C  CG     . GLU B 1 11  ? -10.58300 -30.95900 -4.99400  1.000 43.72103 ? 7   GLU B CG     1 
ATOM   4030 C  CD     . GLU B 1 11  ? -10.48400 -32.36800 -5.58100  1.000 55.09345 ? 7   GLU B CD     1 
ATOM   4031 O  OE1    . GLU B 1 11  ? -9.36200  -32.78800 -5.94700  1.000 54.54601 ? 7   GLU B OE1    1 
ATOM   4032 O  OE2    . GLU B 1 11  ? -11.52100 -33.05900 -5.66800  1.000 56.36992 ? 7   GLU B OE2    1 
ATOM   4033 N  N      . LEU B 1 12  ? -10.93000 -27.33700 -6.01100  1.000 30.29047 ? 8   LEU B N      1 
ATOM   4034 C  CA     . LEU B 1 12  ? -9.86300  -26.41700 -6.38300  1.000 32.43284 ? 8   LEU B CA     1 
ATOM   4035 C  C      . LEU B 1 12  ? -9.61100  -25.42800 -5.25800  1.000 31.50378 ? 8   LEU B C      1 
ATOM   4036 O  O      . LEU B 1 12  ? -8.46700  -25.18900 -4.86400  1.000 29.90885 ? 8   LEU B O      1 
ATOM   4037 C  CB     . LEU B 1 12  ? -10.22600 -25.67500 -7.67300  1.000 32.78025 ? 8   LEU B CB     1 
ATOM   4038 C  CG     . LEU B 1 12  ? -9.12000  -24.76600 -8.20400  1.000 43.52364 ? 8   LEU B CG     1 
ATOM   4039 C  CD1    . LEU B 1 12  ? -8.00700  -25.61600 -8.80400  1.000 46.57137 ? 8   LEU B CD1    1 
ATOM   4040 C  CD2    . LEU B 1 12  ? -9.65400  -23.77100 -9.23000  1.000 43.68155 ? 8   LEU B CD2    1 
ATOM   4041 N  N      . LEU B 1 13  ? -10.68500 -24.86400 -4.71300  1.000 35.16474 ? 9   LEU B N      1 
ATOM   4042 C  CA     . LEU B 1 13  ? -10.55400 -23.93400 -3.60200  1.000 31.11952 ? 9   LEU B CA     1 
ATOM   4043 C  C      . LEU B 1 13  ? -9.81000  -24.57000 -2.43100  1.000 31.05109 ? 9   LEU B C      1 
ATOM   4044 O  O      . LEU B 1 13  ? -8.94300  -23.93500 -1.81900  1.000 32.02752 ? 9   LEU B O      1 
ATOM   4045 C  CB     . LEU B 1 13  ? -11.94800 -23.46600 -3.17900  1.000 28.13495 ? 9   LEU B CB     1 
ATOM   4046 C  CG     . LEU B 1 13  ? -12.08900 -22.82900 -1.79500  1.000 28.89557 ? 9   LEU B CG     1 
ATOM   4047 C  CD1    . LEU B 1 13  ? -11.35900 -21.53000 -1.77100  1.000 21.54469 ? 9   LEU B CD1    1 
ATOM   4048 C  CD2    . LEU B 1 13  ? -13.57200 -22.62900 -1.44800  1.000 31.22480 ? 9   LEU B CD2    1 
ATOM   4049 N  N      . VAL B 1 14  ? -10.14900 -25.81300 -2.08900  1.000 26.86901 ? 10  VAL B N      1 
ATOM   4050 C  CA     . VAL B 1 14  ? -9.49300  -26.48100 -0.96700  1.000 31.74591 ? 10  VAL B CA     1 
ATOM   4051 C  C      . VAL B 1 14  ? -8.00800  -26.66900 -1.25500  1.000 34.21200 ? 10  VAL B C      1 
ATOM   4052 O  O      . VAL B 1 14  ? -7.14500  -26.37000 -0.41900  1.000 30.45628 ? 10  VAL B O      1 
ATOM   4053 C  CB     . VAL B 1 14  ? -10.18500 -27.82600 -0.67000  1.000 24.84245 ? 10  VAL B CB     1 
ATOM   4054 C  CG1    . VAL B 1 14  ? -9.31200  -28.67700 0.24200   1.000 30.45628 ? 10  VAL B CG1    1 
ATOM   4055 C  CG2    . VAL B 1 14  ? -11.56000 -27.58600 -0.04900  1.000 24.14763 ? 10  VAL B CG2    1 
ATOM   4056 N  N      . ARG B 1 15  ? -7.69200  -27.14900 -2.45800  1.000 30.80106 ? 11  ARG B N      1 
ATOM   4057 C  CA     . ARG B 1 15  ? -6.30200  -27.38700 -2.82700  1.000 35.09895 ? 11  ARG B CA     1 
ATOM   4058 C  C      . ARG B 1 15  ? -5.49500  -26.09100 -2.86100  1.000 33.76721 ? 11  ARG B C      1 
ATOM   4059 O  O      . ARG B 1 15  ? -4.30500  -26.08800 -2.53200  1.000 33.00659 ? 11  ARG B O      1 
ATOM   4060 C  CB     . ARG B 1 15  ? -6.23900  -28.08300 -4.17900  1.000 34.56730 ? 11  ARG B CB     1 
ATOM   4061 C  CG     . ARG B 1 15  ? -6.64300  -29.55500 -4.17700  1.000 37.56240 ? 11  ARG B CG     1 
ATOM   4062 C  CD     . ARG B 1 15  ? -6.82100  -29.94700 -5.62200  1.000 42.50510 ? 11  ARG B CD     1 
ATOM   4063 N  NE     . ARG B 1 15  ? -7.07700  -31.36000 -5.84600  1.000 48.23210 ? 11  ARG B NE     1 
ATOM   4064 C  CZ     . ARG B 1 15  ? -6.18500  -32.21400 -6.33500  1.000 46.69770 ? 11  ARG B CZ     1 
ATOM   4065 N  NH1    . ARG B 1 15  ? -4.95800  -31.80600 -6.63600  1.000 41.47603 ? 11  ARG B NH1    1 
ATOM   4066 N  NH2    . ARG B 1 15  ? -6.52900  -33.47700 -6.52600  1.000 46.36082 ? 11  ARG B NH2    1 
ATOM   4067 N  N      . GLN B 1 16  ? -6.09100  -24.99500 -3.28900  1.000 28.79556 ? 12  GLN B N      1 
ATOM   4068 C  CA     . GLN B 1 16  ? -5.38800  -23.72700 -3.30600  1.000 29.81147 ? 12  GLN B CA     1 
ATOM   4069 C  C      . GLN B 1 16  ? -5.12200  -23.24800 -1.87900  1.000 31.26691 ? 12  GLN B C      1 
ATOM   4070 O  O      . GLN B 1 16  ? -4.13000  -22.66900 -1.63200  1.000 30.90897 ? 12  GLN B O      1 
ATOM   4071 C  CB     . GLN B 1 16  ? -6.07700  -22.69300 -4.16700  1.000 29.15876 ? 12  GLN B CB     1 
ATOM   4072 C  CG     . GLN B 1 16  ? -5.32500  -21.39700 -4.35300  1.000 25.03458 ? 12  GLN B CG     1 
ATOM   4073 C  CD     . GLN B 1 16  ? -4.08300  -21.53700 -5.18900  1.000 31.72749 ? 12  GLN B CD     1 
ATOM   4074 O  OE1    . GLN B 1 16  ? -4.14100  -21.63200 -6.36800  1.000 35.15421 ? 12  GLN B OE1    1 
ATOM   4075 N  NE2    . GLN B 1 16  ? -2.97400  -21.53200 -4.55400  1.000 33.11713 ? 12  GLN B NE2    1 
ATOM   4076 N  N      . MET B 1 17  ? -6.03900  -23.49700 -0.96400  1.000 28.37445 ? 13  MET B N      1 
ATOM   4077 C  CA     . MET B 1 17  ? -5.80000  -23.19800 0.44600   1.000 31.21953 ? 13  MET B CA     1 
ATOM   4078 C  C      . MET B 1 17  ? -4.70100  -24.08100 1.02100   1.000 29.91148 ? 13  MET B C      1 
ATOM   4079 O  O      . MET B 1 17  ? -3.93700  -23.64000 1.88700   1.000 32.34335 ? 13  MET B O      1 
ATOM   4080 C  CB     . MET B 1 17  ? -7.08600  -23.38500 1.25500   1.000 27.09799 ? 13  MET B CB     1 
ATOM   4081 C  CG     . MET B 1 17  ? -8.14200  -22.34100 0.97100   1.000 32.61444 ? 13  MET B CG     1 
ATOM   4082 S  SD     . MET B 1 17  ? -9.48800  -22.31900 2.16800   1.000 35.12263 ? 13  MET B SD     1 
ATOM   4083 C  CE     . MET B 1 17  ? -10.14200 -23.99700 2.11100   1.000 26.06628 ? 13  MET B CE     1 
ATOM   4084 N  N      . GLU B 1 18  ? -4.64000  -25.34700 0.58600   1.000 24.48978 ? 14  GLU B N      1 
ATOM   4085 C  CA     . GLU B 1 18  ? -3.53700  -26.21500 0.98500   1.000 34.45939 ? 14  GLU B CA     1 
ATOM   4086 C  C      . GLU B 1 18  ? -2.20200  -25.56800 0.64900   1.000 38.42829 ? 14  GLU B C      1 
ATOM   4087 O  O      . GLU B 1 18  ? -1.29800  -25.49800 1.49200   1.000 35.26739 ? 14  GLU B O      1 
ATOM   4088 C  CB     . GLU B 1 18  ? -3.64600  -27.56600 0.28300   1.000 32.38809 ? 14  GLU B CB     1 
ATOM   4089 C  CG     . GLU B 1 18  ? -4.72900  -28.48300 0.81300   1.000 41.59446 ? 14  GLU B CG     1 
ATOM   4090 C  CD     . GLU B 1 18  ? -4.91000  -29.72600 -0.05700  1.000 45.40544 ? 14  GLU B CD     1 
ATOM   4091 O  OE1    . GLU B 1 18  ? -5.98600  -30.36600 0.04000   1.000 42.42614 ? 14  GLU B OE1    1 
ATOM   4092 O  OE2    . GLU B 1 18  ? -3.98000  -30.05900 -0.83600  1.000 46.26344 ? 14  GLU B OE2    1 
ATOM   4093 N  N      . ALA B 1 19  ? -2.07900  -25.04700 -0.57400  1.000 37.14130 ? 15  ALA B N      1 
ATOM   4094 C  CA     . ALA B 1 19  ? -0.82800  -24.43400 -1.00000  1.000 35.13579 ? 15  ALA B CA     1 
ATOM   4095 C  C      . ALA B 1 19  ? -0.44400  -23.25100 -0.12500  1.000 37.70978 ? 15  ALA B C      1 
ATOM   4096 O  O      . ALA B 1 19  ? 0.73500   -22.88600 -0.08300  1.000 43.90000 ? 15  ALA B O      1 
ATOM   4097 C  CB     . ALA B 1 19  ? -0.92900  -24.00000 -2.46200  1.000 32.84604 ? 15  ALA B CB     1 
ATOM   4098 N  N      . GLU B 1 20  ? -1.40600  -22.62500 0.55500   1.000 36.01748 ? 16  GLU B N      1 
ATOM   4099 C  CA     . GLU B 1 20  ? -1.09700  -21.54400 1.48200   1.000 29.93517 ? 16  GLU B CA     1 
ATOM   4100 C  C      . GLU B 1 20  ? -0.75600  -22.04200 2.87700   1.000 35.18053 ? 16  GLU B C      1 
ATOM   4101 O  O      . GLU B 1 20  ? -0.53100  -21.22200 3.77500   1.000 39.61528 ? 16  GLU B O      1 
ATOM   4102 C  CB     . GLU B 1 20  ? -2.26500  -20.55500 1.56800   1.000 31.91698 ? 16  GLU B CB     1 
ATOM   4103 C  CG     . GLU B 1 20  ? -2.41300  -19.65400 0.34000   1.000 41.13388 ? 16  GLU B CG     1 
ATOM   4104 C  CD     . GLU B 1 20  ? -1.68100  -18.31800 0.47100   1.000 42.44193 ? 16  GLU B CD     1 
ATOM   4105 O  OE1    . GLU B 1 20  ? -1.61400  -17.57900 -0.53400  1.000 43.47363 ? 16  GLU B OE1    1 
ATOM   4106 O  OE2    . GLU B 1 20  ? -1.18100  -18.00600 1.57600   1.000 47.07407 ? 16  GLU B OE2    1 
ATOM   4107 N  N      . GLY B 1 21  ? -0.71200  -23.35600 3.08900   1.000 37.69399 ? 17  GLY B N      1 
ATOM   4108 C  CA     . GLY B 1 21  ? -0.42100  -23.86600 4.41400   1.000 35.30160 ? 17  GLY B CA     1 
ATOM   4109 C  C      . GLY B 1 21  ? -1.59200  -23.81100 5.36500   1.000 37.96771 ? 17  GLY B C      1 
ATOM   4110 O  O      . GLY B 1 21  ? -1.39300  -23.87000 6.58100   1.000 35.00157 ? 17  GLY B O      1 
ATOM   4111 N  N      . VAL B 1 22  ? -2.81300  -23.67500 4.84900   1.000 33.20924 ? 18  VAL B N      1 
ATOM   4112 C  CA     . VAL B 1 22  ? -3.99700  -23.73700 5.69900   1.000 33.21451 ? 18  VAL B CA     1 
ATOM   4113 C  C      . VAL B 1 22  ? -4.12100  -25.13800 6.27600   1.000 32.40652 ? 18  VAL B C      1 
ATOM   4114 O  O      . VAL B 1 22  ? -4.06600  -26.13500 5.54200   1.000 34.08830 ? 18  VAL B O      1 
ATOM   4115 C  CB     . VAL B 1 22  ? -5.25600  -23.35400 4.90900   1.000 30.89055 ? 18  VAL B CB     1 
ATOM   4116 C  CG1    . VAL B 1 22  ? -6.50300  -23.64000 5.74300   1.000 31.20111 ? 18  VAL B CG1    1 
ATOM   4117 C  CG2    . VAL B 1 22  ? -5.18900  -21.87900 4.49500   1.000 33.39348 ? 18  VAL B CG2    1 
ATOM   4118 N  N      . SER B 1 23  ? -4.31500  -25.22800 7.58900   1.000 29.63776 ? 19  SER B N      1 
ATOM   4119 C  CA     . SER B 1 23  ? -4.40900  -26.53000 8.23500   1.000 33.10923 ? 19  SER B CA     1 
ATOM   4120 C  C      . SER B 1 23  ? -5.75600  -26.82000 8.87100   1.000 30.50892 ? 19  SER B C      1 
ATOM   4121 O  O      . SER B 1 23  ? -6.04700  -27.98900 9.13700   1.000 30.35364 ? 19  SER B O      1 
ATOM   4122 C  CB     . SER B 1 23  ? -3.33600  -26.65900 9.32800   1.000 38.10457 ? 19  SER B CB     1 
ATOM   4123 O  OG     . SER B 1 23  ? -2.04300  -26.73200 8.76400   1.000 53.40377 ? 19  SER B OG     1 
ATOM   4124 N  N      . TYR B 1 24  ? -6.60200  -25.81300 9.05600   1.000 29.91148 ? 20  TYR B N      1 
ATOM   4125 C  CA     . TYR B 1 24  ? -7.89100  -25.98200 9.69900   1.000 28.88504 ? 20  TYR B CA     1 
ATOM   4126 C  C      . TYR B 1 24  ? -8.91200  -25.07200 9.04300   1.000 30.25626 ? 20  TYR B C      1 
ATOM   4127 O  O      . TYR B 1 24  ? -8.59200  -23.96800 8.59200   1.000 27.04535 ? 20  TYR B O      1 
ATOM   4128 C  CB     . TYR B 1 24  ? -7.81700  -25.64300 11.19100  1.000 25.52674 ? 20  TYR B CB     1 
ATOM   4129 C  CG     . TYR B 1 24  ? -6.91400  -26.55200 11.98600  1.000 25.12670 ? 20  TYR B CG     1 
ATOM   4130 C  CD1    . TYR B 1 24  ? -7.37500  -27.77700 12.46300  1.000 24.90562 ? 20  TYR B CD1    1 
ATOM   4131 C  CD2    . TYR B 1 24  ? -5.61000  -26.18200 12.27200  1.000 29.10612 ? 20  TYR B CD2    1 
ATOM   4132 C  CE1    . TYR B 1 24  ? -6.54800  -28.61600 13.20400  1.000 26.50318 ? 20  TYR B CE1    1 
ATOM   4133 C  CE2    . TYR B 1 24  ? -4.76700  -27.01700 13.00500  1.000 28.25602 ? 20  TYR B CE2    1 
ATOM   4134 C  CZ     . TYR B 1 24  ? -5.24100  -28.22100 13.46500  1.000 32.17228 ? 20  TYR B CZ     1 
ATOM   4135 O  OH     . TYR B 1 24  ? -4.39600  -29.03000 14.19100  1.000 41.79975 ? 20  TYR B OH     1 
ATOM   4136 N  N      . VAL B 1 25  ? -10.15400 -25.53200 9.02300   1.000 25.61097 ? 21  VAL B N      1 
ATOM   4137 C  CA     . VAL B 1 25  ? -11.28900 -24.68900 8.66300   1.000 28.62975 ? 21  VAL B CA     1 
ATOM   4138 C  C      . VAL B 1 25  ? -12.28600 -24.75900 9.80800   1.000 27.14799 ? 21  VAL B C      1 
ATOM   4139 O  O      . VAL B 1 25  ? -12.83600 -25.83300 10.09000  1.000 27.87703 ? 21  VAL B O      1 
ATOM   4140 C  CB     . VAL B 1 25  ? -11.94300 -25.12300 7.34100   1.000 30.80896 ? 21  VAL B CB     1 
ATOM   4141 C  CG1    . VAL B 1 25  ? -13.16700 -24.26100 7.07100   1.000 27.40329 ? 21  VAL B CG1    1 
ATOM   4142 C  CG2    . VAL B 1 25  ? -10.94400 -25.01400 6.20000   1.000 31.25112 ? 21  VAL B CG2    1 
ATOM   4143 N  N      . PHE B 1 26  ? -12.52200 -23.61600 10.45800  1.000 28.89557 ? 22  PHE B N      1 
ATOM   4144 C  CA     . PHE B 1 26  ? -13.44200 -23.52600 11.58500  1.000 26.32947 ? 22  PHE B CA     1 
ATOM   4145 C  C      . PHE B 1 26  ? -14.82700 -23.14500 11.08000  1.000 24.76086 ? 22  PHE B C      1 
ATOM   4146 O  O      . PHE B 1 26  ? -14.96600 -22.21400 10.28200  1.000 25.48990 ? 22  PHE B O      1 
ATOM   4147 C  CB     . PHE B 1 26  ? -12.95500 -22.47800 12.58900  1.000 25.35830 ? 22  PHE B CB     1 
ATOM   4148 C  CG     . PHE B 1 26  ? -11.55000 -22.70200 13.07700  1.000 26.61372 ? 22  PHE B CG     1 
ATOM   4149 C  CD1    . PHE B 1 26  ? -11.31700 -23.48700 14.19500  1.000 27.70069 ? 22  PHE B CD1    1 
ATOM   4150 C  CD2    . PHE B 1 26  ? -10.46700 -22.13000 12.41800  1.000 26.47423 ? 22  PHE B CD2    1 
ATOM   4151 C  CE1    . PHE B 1 26  ? -10.02600 -23.71300 14.65800  1.000 25.54254 ? 22  PHE B CE1    1 
ATOM   4152 C  CE2    . PHE B 1 26  ? -9.16200  -22.34200 12.87000  1.000 29.45880 ? 22  PHE B CE2    1 
ATOM   4153 C  CZ     . PHE B 1 26  ? -8.93900  -23.14100 13.99000  1.000 27.69806 ? 22  PHE B CZ     1 
ATOM   4154 N  N      . GLY B 1 27  ? -15.85700 -23.84100 11.54300  1.000 24.45556 ? 23  GLY B N      1 
ATOM   4155 C  CA     . GLY B 1 27  ? -17.18300 -23.45800 11.10300  1.000 23.32122 ? 23  GLY B CA     1 
ATOM   4156 C  C      . GLY B 1 27  ? -18.24400 -24.44900 11.52500  1.000 30.20362 ? 23  GLY B C      1 
ATOM   4157 O  O      . GLY B 1 27  ? -18.01800 -25.32800 12.36300  1.000 27.94019 ? 23  GLY B O      1 
ATOM   4158 N  N      . ILE B 1 28  ? -19.42700 -24.24600 10.94500  1.000 25.00300 ? 24  ILE B N      1 
ATOM   4159 C  CA     . ILE B 1 28  ? -20.59900 -25.07400 11.17900  1.000 25.31356 ? 24  ILE B CA     1 
ATOM   4160 C  C      . ILE B 1 28  ? -21.26800 -25.37900 9.84400   1.000 25.31883 ? 24  ILE B C      1 
ATOM   4161 O  O      . ILE B 1 28  ? -21.49700 -24.46800 9.03900   1.000 26.84796 ? 24  ILE B O      1 
ATOM   4162 C  CB     . ILE B 1 28  ? -21.57900 -24.38600 12.13400  1.000 23.87918 ? 24  ILE B CB     1 
ATOM   4163 C  CG1    . ILE B 1 28  ? -20.91800 -24.23500 13.50900  1.000 27.27695 ? 24  ILE B CG1    1 
ATOM   4164 C  CG2    . ILE B 1 28  ? -22.92700 -25.16500 12.14800  1.000 23.93182 ? 24  ILE B CG2    1 
ATOM   4165 C  CD1    . ILE B 1 28  ? -21.74600 -23.45200 14.51200  1.000 32.08016 ? 24  ILE B CD1    1 
ATOM   4166 N  N      . PRO B 1 29  ? -21.62000 -26.62800 9.58600   1.000 24.30818 ? 25  PRO B N      1 
ATOM   4167 C  CA     . PRO B 1 29  ? -22.16900 -26.99400 8.27800   1.000 31.75907 ? 25  PRO B CA     1 
ATOM   4168 C  C      . PRO B 1 29  ? -23.61000 -26.53800 8.09500   1.000 36.61228 ? 25  PRO B C      1 
ATOM   4169 O  O      . PRO B 1 29  ? -24.28700 -26.05100 9.00500   1.000 33.24083 ? 25  PRO B O      1 
ATOM   4170 C  CB     . PRO B 1 29  ? -22.06600 -28.52300 8.27400   1.000 30.13256 ? 25  PRO B CB     1 
ATOM   4171 C  CG     . PRO B 1 29  ? -22.12400 -28.88100 9.70800   1.000 27.92703 ? 25  PRO B CG     1 
ATOM   4172 C  CD     . PRO B 1 29  ? -21.34000 -27.81300 10.41400  1.000 27.24800 ? 25  PRO B CD     1 
ATOM   4173 N  N      . GLY B 1 30  ? -24.04900 -26.68300 6.84900   1.000 36.35699 ? 26  GLY B N      1 
ATOM   4174 C  CA     . GLY B 1 30  ? -25.41900 -26.43600 6.43700   1.000 26.99271 ? 26  GLY B CA     1 
ATOM   4175 C  C      . GLY B 1 30  ? -25.57500 -26.92400 5.01200   1.000 32.47231 ? 26  GLY B C      1 
ATOM   4176 O  O      . GLY B 1 30  ? -24.58400 -27.11100 4.29600   1.000 36.40700 ? 26  GLY B O      1 
ATOM   4177 N  N      . GLY B 1 31  ? -26.83300 -27.11200 4.60200   1.000 27.61910 ? 27  GLY B N      1 
ATOM   4178 C  CA     . GLY B 1 31  ? -27.14400 -27.70400 3.32000   1.000 29.66935 ? 27  GLY B CA     1 
ATOM   4179 C  C      . GLY B 1 31  ? -26.37800 -27.29500 2.07100   1.000 27.05061 ? 27  GLY B C      1 
ATOM   4180 O  O      . GLY B 1 31  ? -25.93200 -28.14000 1.29300   1.000 31.05636 ? 27  GLY B O      1 
ATOM   4181 N  N      . PRO B 1 32  ? -26.19800 -25.98700 1.86100   1.000 31.14058 ? 28  PRO B N      1 
ATOM   4182 C  CA     . PRO B 1 32  ? -25.53700 -25.52400 0.62400   1.000 25.49516 ? 28  PRO B CA     1 
ATOM   4183 C  C      . PRO B 1 32  ? -24.03400 -25.53600 0.85300   1.000 31.86171 ? 28  PRO B C      1 
ATOM   4184 O  O      . PRO B 1 32  ? -23.27900 -25.40500 -0.11800  1.000 27.03482 ? 28  PRO B O      1 
ATOM   4185 C  CB     . PRO B 1 32  ? -26.03700 -24.08400 0.39600   1.000 30.66683 ? 28  PRO B CB     1 
ATOM   4186 C  CG     . PRO B 1 32  ? -27.06000 -23.80300 1.47000   1.000 34.51993 ? 28  PRO B CG     1 
ATOM   4187 C  CD     . PRO B 1 32  ? -27.01500 -24.89400 2.48500   1.000 33.27767 ? 28  PRO B CD     1 
ATOM   4188 N  N      . LEU B 1 33  ? -23.58000 -25.68000 2.09400   1.000 28.19022 ? 29  LEU B N      1 
ATOM   4189 C  CA     . LEU B 1 33  ? -22.16400 -25.72800 2.42400   1.000 31.05109 ? 29  LEU B CA     1 
ATOM   4190 C  C      . LEU B 1 33  ? -21.59300 -27.13600 2.33900   1.000 26.17156 ? 29  LEU B C      1 
ATOM   4191 O  O      . LEU B 1 33  ? -20.37000 -27.29600 2.30400   1.000 32.03542 ? 29  LEU B O      1 
ATOM   4192 C  CB     . LEU B 1 33  ? -21.96000 -25.17900 3.84300   1.000 37.26763 ? 29  LEU B CB     1 
ATOM   4193 C  CG     . LEU B 1 33  ? -20.58500 -24.68200 4.25600   1.000 31.40377 ? 29  LEU B CG     1 
ATOM   4194 C  CD1    . LEU B 1 33  ? -20.16400 -23.59500 3.28800   1.000 31.95383 ? 29  LEU B CD1    1 
ATOM   4195 C  CD2    . LEU B 1 33  ? -20.63400 -24.17500 5.69900   1.000 32.79077 ? 29  LEU B CD2    1 
ATOM   4196 N  N      . MET B 1 34  ? -22.44200 -28.15400 2.25500   1.000 30.34048 ? 30  MET B N      1 
ATOM   4197 C  CA     . MET B 1 34  ? -21.95200 -29.52700 2.33700   1.000 29.74304 ? 30  MET B CA     1 
ATOM   4198 C  C      . MET B 1 34  ? -20.90700 -29.86000 1.27800   1.000 30.60104 ? 30  MET B C      1 
ATOM   4199 O  O      . MET B 1 34  ? -19.99800 -30.65500 1.57700   1.000 30.23257 ? 30  MET B O      1 
ATOM   4200 C  CB     . MET B 1 34  ? -23.13400 -30.50400 2.25000   1.000 28.61659 ? 30  MET B CB     1 
ATOM   4201 C  CG     . MET B 1 34  ? -24.12300 -30.40800 3.43600   1.000 31.40113 ? 30  MET B CG     1 
ATOM   4202 S  SD     . MET B 1 34  ? -23.22900 -30.28400 5.01900   1.000 41.60762 ? 30  MET B SD     1 
ATOM   4203 C  CE     . MET B 1 34  ? -22.55800 -31.94600 5.14000   1.000 36.68598 ? 30  MET B CE     1 
ATOM   4204 N  N      . PRO B 1 35  ? -20.97200 -29.34600 0.05100   1.000 33.33031 ? 31  PRO B N      1 
ATOM   4205 C  CA     . PRO B 1 35  ? -19.90400 -29.68300 -0.90400  1.000 32.11964 ? 31  PRO B CA     1 
ATOM   4206 C  C      . PRO B 1 35  ? -18.52000 -29.28400 -0.41600  1.000 29.45880 ? 31  PRO B C      1 
ATOM   4207 O  O      . PRO B 1 35  ? -17.55000 -30.00500 -0.68200  1.000 32.88026 ? 31  PRO B O      1 
ATOM   4208 C  CB     . PRO B 1 35  ? -20.31500 -28.92000 -2.17200  1.000 37.03602 ? 31  PRO B CB     1 
ATOM   4209 C  CG     . PRO B 1 35  ? -21.82500 -28.81700 -2.06700  1.000 34.69363 ? 31  PRO B CG     1 
ATOM   4210 C  CD     . PRO B 1 35  ? -22.06100 -28.57300 -0.58200  1.000 34.01724 ? 31  PRO B CD     1 
ATOM   4211 N  N      . LEU B 1 36  ? -18.39000 -28.17100 0.31200   1.000 29.06664 ? 32  LEU B N      1 
ATOM   4212 C  CA     . LEU B 1 36  ? -17.08100 -27.81200 0.85000   1.000 23.49229 ? 32  LEU B CA     1 
ATOM   4213 C  C      . LEU B 1 36  ? -16.59300 -28.88000 1.81400   1.000 28.89031 ? 32  LEU B C      1 
ATOM   4214 O  O      . LEU B 1 36  ? -15.42900 -29.29300 1.76600   1.000 30.30100 ? 32  LEU B O      1 
ATOM   4215 C  CB     . LEU B 1 36  ? -17.13000 -26.44900 1.54300   1.000 25.79520 ? 32  LEU B CB     1 
ATOM   4216 C  CG     . LEU B 1 36  ? -15.83500 -26.07200 2.28700   1.000 30.01149 ? 32  LEU B CG     1 
ATOM   4217 C  CD1    . LEU B 1 36  ? -14.70400 -25.82500 1.29100   1.000 27.34275 ? 32  LEU B CD1    1 
ATOM   4218 C  CD2    . LEU B 1 36  ? -16.00800 -24.85600 3.22200   1.000 29.38773 ? 32  LEU B CD2    1 
ATOM   4219 N  N      . TYR B 1 37  ? -17.47400 -29.34700 2.69700   1.000 30.95634 ? 33  TYR B N      1 
ATOM   4220 C  CA     . TYR B 1 37  ? -17.06600 -30.37600 3.64200   1.000 32.04858 ? 33  TYR B CA     1 
ATOM   4221 C  C      . TYR B 1 37  ? -16.72300 -31.67100 2.92100   1.000 30.77737 ? 33  TYR B C      1 
ATOM   4222 O  O      . TYR B 1 37  ? -15.73900 -32.33800 3.26600   1.000 30.19836 ? 33  TYR B O      1 
ATOM   4223 C  CB     . TYR B 1 37  ? -18.16500 -30.58100 4.69100   1.000 29.84305 ? 33  TYR B CB     1 
ATOM   4224 C  CG     . TYR B 1 37  ? -18.11900 -29.49800 5.74400   1.000 32.56969 ? 33  TYR B CG     1 
ATOM   4225 C  CD1    . TYR B 1 37  ? -17.12300 -29.50000 6.72400   1.000 30.39312 ? 33  TYR B CD1    1 
ATOM   4226 C  CD2    . TYR B 1 37  ? -19.03200 -28.45100 5.73700   1.000 30.10098 ? 33  TYR B CD2    1 
ATOM   4227 C  CE1    . TYR B 1 37  ? -17.05500 -28.50600 7.68200   1.000 28.50079 ? 33  TYR B CE1    1 
ATOM   4228 C  CE2    . TYR B 1 37  ? -18.97000 -27.44000 6.69300   1.000 35.57005 ? 33  TYR B CE2    1 
ATOM   4229 C  CZ     . TYR B 1 37  ? -17.97500 -27.47700 7.66400   1.000 39.49684 ? 33  TYR B CZ     1 
ATOM   4230 O  OH     . TYR B 1 37  ? -17.89500 -26.49000 8.62500   1.000 38.83097 ? 33  TYR B OH     1 
ATOM   4231 N  N      . GLU B 1 38  ? -17.50500 -32.02800 1.89400   1.000 33.34610 ? 34  GLU B N      1 
ATOM   4232 C  CA     . GLU B 1 38  ? -17.16800 -33.20000 1.09200   1.000 34.39623 ? 34  GLU B CA     1 
ATOM   4233 C  C      . GLU B 1 38  ? -15.76300 -33.08000 0.50100   1.000 30.67736 ? 34  GLU B C      1 
ATOM   4234 O  O      . GLU B 1 38  ? -14.97900 -34.03300 0.54200   1.000 30.66420 ? 34  GLU B O      1 
ATOM   4235 C  CB     . GLU B 1 38  ? -18.20700 -33.39600 -0.01500  1.000 37.22552 ? 34  GLU B CB     1 
ATOM   4236 C  CG     . GLU B 1 38  ? -17.91700 -34.61100 -0.91200  1.000 40.96544 ? 34  GLU B CG     1 
ATOM   4237 C  CD     . GLU B 1 38  ? -18.97600 -34.81600 -1.99000  1.000 46.56874 ? 34  GLU B CD     1 
ATOM   4238 O  OE1    . GLU B 1 38  ? -19.42600 -35.96800 -2.16900  1.000 46.31608 ? 34  GLU B OE1    1 
ATOM   4239 O  OE2    . GLU B 1 38  ? -19.35900 -33.82600 -2.66100  1.000 45.04487 ? 34  GLU B OE2    1 
ATOM   4240 N  N      . ALA B 1 39  ? -15.42100 -31.91300 -0.04900  1.000 31.43535 ? 35  ALA B N      1 
ATOM   4241 C  CA     . ALA B 1 39  ? -14.08000 -31.73700 -0.60100  1.000 30.02992 ? 35  ALA B CA     1 
ATOM   4242 C  C      . ALA B 1 39  ? -13.01400 -31.81200 0.48900   1.000 36.95969 ? 35  ALA B C      1 
ATOM   4243 O  O      . ALA B 1 39  ? -11.95100 -32.40800 0.28600   1.000 35.59111 ? 35  ALA B O      1 
ATOM   4244 C  CB     . ALA B 1 39  ? -13.98000 -30.41000 -1.34600  1.000 26.59003 ? 35  ALA B CB     1 
ATOM   4245 N  N      . ILE B 1 40  ? -13.26700 -31.20700 1.65200   1.000 33.12766 ? 36  ILE B N      1 
ATOM   4246 C  CA     . ILE B 1 40  ? -12.27000 -31.24400 2.72100   1.000 34.18831 ? 36  ILE B CA     1 
ATOM   4247 C  C      . ILE B 1 40  ? -12.00400 -32.68400 3.15200   1.000 34.39097 ? 36  ILE B C      1 
ATOM   4248 O  O      . ILE B 1 40  ? -10.85000 -33.12100 3.25200   1.000 36.46753 ? 36  ILE B O      1 
ATOM   4249 C  CB     . ILE B 1 40  ? -12.72000 -30.37900 3.91100   1.000 31.19321 ? 36  ILE B CB     1 
ATOM   4250 C  CG1    . ILE B 1 40  ? -12.60900 -28.90500 3.55000   1.000 31.45114 ? 36  ILE B CG1    1 
ATOM   4251 C  CG2    . ILE B 1 40  ? -11.87100 -30.70100 5.14500   1.000 34.28832 ? 36  ILE B CG2    1 
ATOM   4252 C  CD1    . ILE B 1 40  ? -13.15900 -27.98900 4.60000   1.000 34.59889 ? 36  ILE B CD1    1 
ATOM   4253 N  N      . PHE B 1 41  ? -13.06900 -33.45400 3.38800   1.000 34.51203 ? 37  PHE B N      1 
ATOM   4254 C  CA     . PHE B 1 41  ? -12.89400 -34.82200 3.86000   1.000 37.31237 ? 37  PHE B CA     1 
ATOM   4255 C  C      . PHE B 1 41  ? -12.30200 -35.71300 2.78600   1.000 39.51790 ? 37  PHE B C      1 
ATOM   4256 O  O      . PHE B 1 41  ? -11.66900 -36.72400 3.11600   1.000 39.94163 ? 37  PHE B O      1 
ATOM   4257 C  CB     . PHE B 1 41  ? -14.22200 -35.38600 4.34000   1.000 35.98063 ? 37  PHE B CB     1 
ATOM   4258 C  CG     . PHE B 1 41  ? -14.58300 -34.96200 5.73000   1.000 40.14429 ? 37  PHE B CG     1 
ATOM   4259 C  CD1    . PHE B 1 41  ? -13.91500 -35.48800 6.82800   1.000 43.42626 ? 37  PHE B CD1    1 
ATOM   4260 C  CD2    . PHE B 1 41  ? -15.57300 -34.02200 5.94100   1.000 38.09404 ? 37  PHE B CD2    1 
ATOM   4261 C  CE1    . PHE B 1 41  ? -14.24200 -35.09500 8.11000   1.000 43.97633 ? 37  PHE B CE1    1 
ATOM   4262 C  CE2    . PHE B 1 41  ? -15.90200 -33.61500 7.22500   1.000 40.50749 ? 37  PHE B CE2    1 
ATOM   4263 C  CZ     . PHE B 1 41  ? -15.23600 -34.15300 8.31100   1.000 41.76027 ? 37  PHE B CZ     1 
ATOM   4264 N  N      . SER B 1 42  ? -12.47300 -35.36900 1.51500   1.000 38.84676 ? 38  SER B N      1 
ATOM   4265 C  CA     . SER B 1 42  ? -11.87900 -36.19000 0.47600   1.000 39.39683 ? 38  SER B CA     1 
ATOM   4266 C  C      . SER B 1 42  ? -10.37500 -35.95200 0.33900   1.000 40.03638 ? 38  SER B C      1 
ATOM   4267 O  O      . SER B 1 42  ? -9.66400  -36.83800 -0.12000  1.000 40.87332 ? 38  SER B O      1 
ATOM   4268 C  CB     . SER B 1 42  ? -12.57300 -35.91200 -0.86000  1.000 44.57903 ? 38  SER B CB     1 
ATOM   4269 O  OG     . SER B 1 42  ? -11.91700 -34.85000 -1.52900  1.000 54.57760 ? 38  SER B OG     1 
ATOM   4270 N  N      . ARG B 1 43  ? -9.88300  -34.79600 0.78400   1.000 44.27110 ? 39  ARG B N      1 
ATOM   4271 C  CA     . ARG B 1 43  ? -8.46200  -34.48000 0.63900   1.000 41.64183 ? 39  ARG B CA     1 
ATOM   4272 C  C      . ARG B 1 43  ? -7.63500  -34.92300 1.83400   1.000 45.90814 ? 39  ARG B C      1 
ATOM   4273 O  O      . ARG B 1 43  ? -6.44700  -35.22400 1.68100   1.000 49.90598 ? 39  ARG B O      1 
ATOM   4274 C  CB     . ARG B 1 43  ? -8.26500  -32.97100 0.43000   1.000 38.44408 ? 39  ARG B CB     1 
ATOM   4275 C  CG     . ARG B 1 43  ? -8.71700  -32.46600 -0.94000  1.000 40.04691 ? 39  ARG B CG     1 
ATOM   4276 C  CD     . ARG B 1 43  ? -7.78700  -32.96100 -2.03200  1.000 39.56264 ? 39  ARG B CD     1 
ATOM   4277 N  NE     . ARG B 1 43  ? -6.43100  -32.44200 -1.86000  1.000 44.32637 ? 39  ARG B NE     1 
ATOM   4278 C  CZ     . ARG B 1 43  ? -5.37100  -32.88900 -2.53400  1.000 45.63179 ? 39  ARG B CZ     1 
ATOM   4279 N  NH1    . ARG B 1 43  ? -5.51600  -33.86000 -3.42400  1.000 45.28438 ? 39  ARG B NH1    1 
ATOM   4280 N  NH2    . ARG B 1 43  ? -4.17100  -32.36500 -2.31900  1.000 39.90478 ? 39  ARG B NH2    1 
ATOM   4281 N  N      . LYS B 1 44  ? -8.24100  -35.01800 3.01100   1.000 43.03937 ? 40  LYS B N      1 
ATOM   4282 C  CA     . LYS B 1 44  ? -7.54900  -35.50800 4.19500   1.000 47.49254 ? 40  LYS B CA     1 
ATOM   4283 C  C      . LYS B 1 44  ? -6.23000  -34.77100 4.43000   1.000 46.51610 ? 40  LYS B C      1 
ATOM   4284 O  O      . LYS B 1 44  ? -5.18400  -35.37600 4.65700   1.000 49.27696 ? 40  LYS B O      1 
ATOM   4285 C  CB     . LYS B 1 44  ? -7.30900  -37.01600 4.08500   1.000 53.73539 ? 40  LYS B CB     1 
ATOM   4286 C  CG     . LYS B 1 44  ? -8.57900  -37.85900 4.09500   1.000 58.16487 ? 40  LYS B CG     1 
ATOM   4287 C  CD     . LYS B 1 44  ? -8.56600  -38.89600 2.98600   1.000 63.77080 ? 40  LYS B CD     1 
ATOM   4288 C  CE     . LYS B 1 44  ? -9.97800  -39.34300 2.62100   1.000 68.14238 ? 40  LYS B CE     1 
ATOM   4289 N  NZ     . LYS B 1 44  ? -10.06700 -39.78300 1.18900   1.000 71.21907 ? 40  LYS B NZ     1 
ATOM   4290 N  N      . LYS B 1 45  ? -6.29000  -33.43900 4.38700   1.000 47.92417 ? 41  LYS B N      1 
ATOM   4291 C  CA     . LYS B 1 45  ? -5.15000  -32.62900 4.80800   1.000 42.36824 ? 41  LYS B CA     1 
ATOM   4292 C  C      . LYS B 1 45  ? -5.61200  -31.49900 5.72700   1.000 45.00013 ? 41  LYS B C      1 
ATOM   4293 O  O      . LYS B 1 45  ? -5.23400  -31.45100 6.90400   1.000 47.42411 ? 41  LYS B O      1 
ATOM   4294 C  CB     . LYS B 1 45  ? -4.40500  -32.08500 3.59400   1.000 36.80704 ? 41  LYS B CB     1 
ATOM   4295 C  CG     . LYS B 1 45  ? -3.89800  -33.20500 2.67700   1.000 43.32098 ? 41  LYS B CG     1 
ATOM   4296 C  CD     . LYS B 1 45  ? -3.20000  -32.68500 1.43100   1.000 49.34802 ? 41  LYS B CD     1 
ATOM   4297 C  CE     . LYS B 1 45  ? -2.77000  -33.85100 0.53200   1.000 58.71493 ? 41  LYS B CE     1 
ATOM   4298 N  NZ     . LYS B 1 45  ? -1.45600  -34.45500 0.94600   1.000 60.24407 ? 41  LYS B NZ     1 
ATOM   4299 N  N      . ILE B 1 46  ? -6.44200  -30.59500 5.20700   1.000 31.94067 ? 42  ILE B N      1 
ATOM   4300 C  CA     . ILE B 1 46  ? -7.07200  -29.58800 6.05000   1.000 33.79089 ? 42  ILE B CA     1 
ATOM   4301 C  C      . ILE B 1 46  ? -8.07600  -30.27500 6.96400   1.000 32.49074 ? 42  ILE B C      1 
ATOM   4302 O  O      . ILE B 1 46  ? -8.82900  -31.15700 6.53200   1.000 36.45700 ? 42  ILE B O      1 
ATOM   4303 C  CB     . ILE B 1 46  ? -7.74400  -28.50900 5.18800   1.000 33.04080 ? 42  ILE B CB     1 
ATOM   4304 C  CG1    . ILE B 1 46  ? -6.69000  -27.72200 4.40800   1.000 35.02262 ? 42  ILE B CG1    1 
ATOM   4305 C  CG2    . ILE B 1 46  ? -8.63400  -27.59300 6.05000   1.000 34.29095 ? 42  ILE B CG2    1 
ATOM   4306 C  CD1    . ILE B 1 46  ? -7.26400  -26.75400 3.38500   1.000 29.60881 ? 42  ILE B CD1    1 
ATOM   4307 N  N      . GLN B 1 47  ? -8.06500  -29.90300 8.24500   1.000 29.05875 ? 43  GLN B N      1 
ATOM   4308 C  CA     . GLN B 1 47  ? -8.96300  -30.52300 9.21400   1.000 28.44815 ? 43  GLN B CA     1 
ATOM   4309 C  C      . GLN B 1 47  ? -10.12800 -29.59800 9.51500   1.000 30.72210 ? 43  GLN B C      1 
ATOM   4310 O  O      . GLN B 1 47  ? -9.90600  -28.44800 9.92400   1.000 31.14058 ? 43  GLN B O      1 
ATOM   4311 C  CB     . GLN B 1 47  ? -8.20900  -30.84200 10.49300  1.000 29.49038 ? 43  GLN B CB     1 
ATOM   4312 C  CG     . GLN B 1 47  ? -9.05000  -31.49800 11.56400  1.000 50.19286 ? 43  GLN B CG     1 
ATOM   4313 C  CD     . GLN B 1 47  ? -8.38000  -32.72500 12.14700  1.000 63.35233 ? 43  GLN B CD     1 
ATOM   4314 O  OE1    . GLN B 1 47  ? -7.22300  -33.03300 11.83400  1.000 60.91257 ? 43  GLN B OE1    1 
ATOM   4315 N  NE2    . GLN B 1 47  ? -9.10200  -33.42700 13.01600  1.000 64.65249 ? 43  GLN B NE2    1 
ATOM   4316 N  N      . PRO B 1 48  ? -11.36600 -30.04100 9.35500   1.000 28.66659 ? 44  PRO B N      1 
ATOM   4317 C  CA     . PRO B 1 48  ? -12.49800 -29.20700 9.76900   1.000 27.38486 ? 44  PRO B CA     1 
ATOM   4318 C  C      . PRO B 1 48  ? -12.66400 -29.25200 11.27900  1.000 33.45664 ? 44  PRO B C      1 
ATOM   4319 O  O      . PRO B 1 48  ? -12.45400 -30.28900 11.91400  1.000 29.17981 ? 44  PRO B O      1 
ATOM   4320 C  CB     . PRO B 1 48  ? -13.69500 -29.84700 9.05700   1.000 26.46370 ? 44  PRO B CB     1 
ATOM   4321 C  CG     . PRO B 1 48  ? -13.30000 -31.27900 8.86800   1.000 25.56096 ? 44  PRO B CG     1 
ATOM   4322 C  CD     . PRO B 1 48  ? -11.78600 -31.31400 8.74200   1.000 27.90598 ? 44  PRO B CD     1 
ATOM   4323 N  N      . ILE B 1 49  ? -12.99900 -28.09600 11.85500  1.000 31.64327 ? 45  ILE B N      1 
ATOM   4324 C  CA     . ILE B 1 49  ? -13.28400 -27.96300 13.28200  1.000 31.89067 ? 45  ILE B CA     1 
ATOM   4325 C  C      . ILE B 1 49  ? -14.72700 -27.49600 13.41700  1.000 30.29311 ? 45  ILE B C      1 
ATOM   4326 O  O      . ILE B 1 49  ? -15.06200 -26.37300 13.01400  1.000 29.30351 ? 45  ILE B O      1 
ATOM   4327 C  CB     . ILE B 1 49  ? -12.32200 -26.99100 13.98600  1.000 28.95610 ? 45  ILE B CB     1 
ATOM   4328 C  CG1    . ILE B 1 49  ? -10.87900 -27.46700 13.84900  1.000 25.34251 ? 45  ILE B CG1    1 
ATOM   4329 C  CG2    . ILE B 1 49  ? -12.70200 -26.81600 15.46400  1.000 24.34766 ? 45  ILE B CG2    1 
ATOM   4330 C  CD1    . ILE B 1 49  ? -10.58900 -28.80800 14.53900  1.000 24.04762 ? 45  ILE B CD1    1 
ATOM   4331 N  N      . LEU B 1 50  ? -15.58000 -28.35400 13.97800  1.000 29.36405 ? 46  LEU B N      1 
ATOM   4332 C  CA     . LEU B 1 50  ? -16.96700 -28.00400 14.25700  1.000 22.98697 ? 46  LEU B CA     1 
ATOM   4333 C  C      . LEU B 1 50  ? -17.03100 -27.14800 15.51700  1.000 27.34275 ? 46  LEU B C      1 
ATOM   4334 O  O      . LEU B 1 50  ? -16.60800 -27.58500 16.59100  1.000 29.06664 ? 46  LEU B O      1 
ATOM   4335 C  CB     . LEU B 1 50  ? -17.80300 -29.27100 14.43800  1.000 25.04511 ? 46  LEU B CB     1 
ATOM   4336 C  CG     . LEU B 1 50  ? -19.28400 -29.08700 14.82100  1.000 30.10887 ? 46  LEU B CG     1 
ATOM   4337 C  CD1    . LEU B 1 50  ? -20.03100 -28.32200 13.74100  1.000 25.45042 ? 46  LEU B CD1    1 
ATOM   4338 C  CD2    . LEU B 1 50  ? -19.96000 -30.42000 15.06300  1.000 24.52662 ? 46  LEU B CD2    1 
ATOM   4339 N  N      . THR B 1 51  ? -17.56800 -25.93900 15.40200  1.000 23.96603 ? 47  THR B N      1 
ATOM   4340 C  CA     . THR B 1 51  ? -17.73000 -25.09200 16.57400  1.000 23.60020 ? 47  THR B CA     1 
ATOM   4341 C  C      . THR B 1 51  ? -19.20000 -25.05200 16.99700  1.000 29.46932 ? 47  THR B C      1 
ATOM   4342 O  O      . THR B 1 51  ? -20.08500 -25.62300 16.34900  1.000 25.70045 ? 47  THR B O      1 
ATOM   4343 C  CB     . THR B 1 51  ? -17.19000 -23.68100 16.31700  1.000 28.86399 ? 47  THR B CB     1 
ATOM   4344 O  OG1    . THR B 1 51  ? -18.02800 -22.98800 15.37800  1.000 27.76649 ? 47  THR B OG1    1 
ATOM   4345 C  CG2    . THR B 1 51  ? -15.74700 -23.75200 15.79100  1.000 23.83180 ? 47  THR B CG2    1 
ATOM   4346 N  N      . LYS B 1 52  ? -19.45200 -24.38500 18.12600  1.000 27.70595 ? 48  LYS B N      1 
ATOM   4347 C  CA     . LYS B 1 52  ? -20.81200 -24.29300 18.63500  1.000 25.24776 ? 48  LYS B CA     1 
ATOM   4348 C  C      . LYS B 1 52  ? -21.55800 -23.10100 18.06100  1.000 27.89808 ? 48  LYS B C      1 
ATOM   4349 O  O      . LYS B 1 52  ? -22.79600 -23.13500 17.99300  1.000 22.65008 ? 48  LYS B O      1 
ATOM   4350 C  CB     . LYS B 1 52  ? -20.79700 -24.22300 20.16800  1.000 27.87703 ? 48  LYS B CB     1 
ATOM   4351 C  CG     . LYS B 1 52  ? -20.11300 -25.45100 20.84000  1.000 26.44264 ? 48  LYS B CG     1 
ATOM   4352 C  CD     . LYS B 1 52  ? -20.86800 -26.72500 20.47800  1.000 22.12634 ? 48  LYS B CD     1 
ATOM   4353 C  CE     . LYS B 1 52  ? -19.97200 -27.73500 19.75300  1.000 30.44049 ? 48  LYS B CE     1 
ATOM   4354 N  NZ     . LYS B 1 52  ? -18.75600 -28.09900 20.54800  1.000 34.72522 ? 48  LYS B NZ     1 
ATOM   4355 N  N      . HIS B 1 53  ? -20.83200 -22.08100 17.59400  1.000 25.31619 ? 49  HIS B N      1 
ATOM   4356 C  CA     . HIS B 1 53  ? -21.41100 -20.84900 17.07300  1.000 22.43953 ? 49  HIS B CA     1 
ATOM   4357 C  C      . HIS B 1 53  ? -20.47000 -20.33500 16.00200  1.000 23.65810 ? 49  HIS B C      1 
ATOM   4358 O  O      . HIS B 1 53  ? -19.25100 -20.39900 16.17100  1.000 23.49755 ? 49  HIS B O      1 
ATOM   4359 C  CB     . HIS B 1 53  ? -21.58200 -19.80300 18.19300  1.000 23.14488 ? 49  HIS B CB     1 
ATOM   4360 C  CG     . HIS B 1 53  ? -22.46400 -18.64300 17.83600  1.000 27.12167 ? 49  HIS B CG     1 
ATOM   4361 N  ND1    . HIS B 1 53  ? -22.13500 -17.72000 16.86100  1.000 31.45904 ? 49  HIS B ND1    1 
ATOM   4362 C  CD2    . HIS B 1 53  ? -23.64700 -18.23300 18.35700  1.000 30.34838 ? 49  HIS B CD2    1 
ATOM   4363 C  CE1    . HIS B 1 53  ? -23.08600 -16.80100 16.79000  1.000 30.67736 ? 49  HIS B CE1    1 
ATOM   4364 N  NE2    . HIS B 1 53  ? -24.01500 -17.09100 17.68600  1.000 28.76398 ? 49  HIS B NE2    1 
ATOM   4365 N  N      . GLU B 1 54  ? -21.02100 -19.82000 14.90000  1.000 22.95012 ? 50  GLU B N      1 
ATOM   4366 C  CA     . GLU B 1 54  ? -20.13200 -19.36200 13.83800  1.000 19.97871 ? 50  GLU B CA     1 
ATOM   4367 C  C      . GLU B 1 54  ? -19.27900 -18.19500 14.30700  1.000 21.23149 ? 50  GLU B C      1 
ATOM   4368 O  O      . GLU B 1 54  ? -18.14500 -18.02600 13.83800  1.000 23.31859 ? 50  GLU B O      1 
ATOM   4369 C  CB     . GLU B 1 54  ? -20.92600 -18.97500 12.59200  1.000 22.68167 ? 50  GLU B CB     1 
ATOM   4370 C  CG     . GLU B 1 54  ? -21.48900 -20.16500 11.85300  1.000 20.99989 ? 50  GLU B CG     1 
ATOM   4371 C  CD     . GLU B 1 54  ? -22.88700 -20.55600 12.36500  1.000 29.43248 ? 50  GLU B CD     1 
ATOM   4372 O  OE1    . GLU B 1 54  ? -23.56400 -21.36100 11.67800  1.000 28.42446 ? 50  GLU B OE1    1 
ATOM   4373 O  OE2    . GLU B 1 54  ? -23.28900 -20.06900 13.45500  1.000 28.62185 ? 50  GLU B OE2    1 
ATOM   4374 N  N      . GLU B 1 55  ? -19.77800 -17.40800 15.26500  1.000 23.40281 ? 51  GLU B N      1 
ATOM   4375 C  CA     . GLU B 1 55  ? -18.94200 -16.35100 15.82400  1.000 21.66312 ? 51  GLU B CA     1 
ATOM   4376 C  C      . GLU B 1 55  ? -17.68100 -16.92900 16.44300  1.000 24.24238 ? 51  GLU B C      1 
ATOM   4377 O  O      . GLU B 1 55  ? -16.58500 -16.37900 16.27700  1.000 21.47100 ? 51  GLU B O      1 
ATOM   4378 C  CB     . GLU B 1 55  ? -19.71200 -15.55000 16.86400  1.000 20.28927 ? 51  GLU B CB     1 
ATOM   4379 C  CG     . GLU B 1 55  ? -18.93500 -14.31500 17.32500  1.000 28.89031 ? 51  GLU B CG     1 
ATOM   4380 C  CD     . GLU B 1 55  ? -19.53300 -13.64600 18.55700  1.000 36.28856 ? 51  GLU B CD     1 
ATOM   4381 O  OE1    . GLU B 1 55  ? -19.10500 -12.51200 18.88500  1.000 36.23066 ? 51  GLU B OE1    1 
ATOM   4382 O  OE2    . GLU B 1 55  ? -20.42900 -14.24300 19.18500  1.000 36.77020 ? 51  GLU B OE2    1 
ATOM   4383 N  N      . GLY B 1 56  ? -17.82800 -18.01900 17.19800  1.000 25.79520 ? 52  GLY B N      1 
ATOM   4384 C  CA     . GLY B 1 56  ? -16.67200 -18.67600 17.77000  1.000 21.91579 ? 52  GLY B CA     1 
ATOM   4385 C  C      . GLY B 1 56  ? -15.77000 -19.22700 16.69500  1.000 28.10600 ? 52  GLY B C      1 
ATOM   4386 O  O      . GLY B 1 56  ? -14.54600 -19.22000 16.84900  1.000 27.42434 ? 52  GLY B O      1 
ATOM   4387 N  N      . ALA B 1 57  ? -16.35400 -19.70100 15.58200  1.000 21.61838 ? 53  ALA B N      1 
ATOM   4388 C  CA     . ALA B 1 57  ? -15.51700 -20.17400 14.47800  1.000 25.03721 ? 53  ALA B CA     1 
ATOM   4389 C  C      . ALA B 1 57  ? -14.65100 -19.04100 13.93600  1.000 21.59469 ? 53  ALA B C      1 
ATOM   4390 O  O      . ALA B 1 57  ? -13.46000 -19.23100 13.67800  1.000 25.13459 ? 53  ALA B O      1 
ATOM   4391 C  CB     . ALA B 1 57  ? -16.37600 -20.78200 13.37000  1.000 21.68155 ? 53  ALA B CB     1 
ATOM   4392 N  N      . ALA B 1 58  ? -15.23200 -17.84300 13.78900  1.000 26.80058 ? 54  ALA B N      1 
ATOM   4393 C  CA     . ALA B 1 58  ? -14.47700 -16.69000 13.30400  1.000 24.26344 ? 54  ALA B CA     1 
ATOM   4394 C  C      . ALA B 1 58  ? -13.41600 -16.23700 14.31200  1.000 23.95024 ? 54  ALA B C      1 
ATOM   4395 O  O      . ALA B 1 58  ? -12.28800 -15.89000 13.92400  1.000 21.84736 ? 54  ALA B O      1 
ATOM   4396 C  CB     . ALA B 1 58  ? -15.44000 -15.54800 12.98400  1.000 22.06054 ? 54  ALA B CB     1 
ATOM   4397 N  N      . PHE B 1 59  ? -13.76300 -16.18800 15.60800  1.000 22.46322 ? 55  PHE B N      1 
ATOM   4398 C  CA     . PHE B 1 59  ? -12.74100 -15.88800 16.62200  1.000 23.92918 ? 55  PHE B CA     1 
ATOM   4399 C  C      . PHE B 1 59  ? -11.60200 -16.89900 16.56000  1.000 22.51849 ? 55  PHE B C      1 
ATOM   4400 O  O      . PHE B 1 59  ? -10.42700 -16.54100 16.69800  1.000 25.04248 ? 55  PHE B O      1 
ATOM   4401 C  CB     . PHE B 1 59  ? -13.34100 -15.90400 18.03400  1.000 19.06018 ? 55  PHE B CB     1 
ATOM   4402 C  CG     . PHE B 1 59  ? -14.19500 -14.71300 18.36700  1.000 24.97668 ? 55  PHE B CG     1 
ATOM   4403 C  CD1    . PHE B 1 59  ? -13.86900 -13.45100 17.90900  1.000 30.26415 ? 55  PHE B CD1    1 
ATOM   4404 C  CD2    . PHE B 1 59  ? -15.33600 -14.86600 19.14800  1.000 24.26344 ? 55  PHE B CD2    1 
ATOM   4405 C  CE1    . PHE B 1 59  ? -14.67600 -12.34000 18.22300  1.000 31.31954 ? 55  PHE B CE1    1 
ATOM   4406 C  CE2    . PHE B 1 59  ? -16.14500 -13.77500 19.47700  1.000 26.00312 ? 55  PHE B CE2    1 
ATOM   4407 C  CZ     . PHE B 1 59  ? -15.81600 -12.50100 19.00700  1.000 26.55055 ? 55  PHE B CZ     1 
ATOM   4408 N  N      . MET B 1 60  ? -11.93400 -18.18100 16.39100  1.000 20.10241 ? 56  MET B N      1 
ATOM   4409 C  CA     . MET B 1 60  ? -10.88900 -19.20500 16.38100  1.000 22.76589 ? 56  MET B CA     1 
ATOM   4410 C  C      . MET B 1 60  ? -9.96200  -19.02500 15.19400  1.000 23.23700 ? 56  MET B C      1 
ATOM   4411 O  O      . MET B 1 60  ? -8.74000  -19.12900 15.32900  1.000 23.80812 ? 56  MET B O      1 
ATOM   4412 C  CB     . MET B 1 60  ? -11.51200 -20.60100 16.33100  1.000 24.75034 ? 56  MET B CB     1 
ATOM   4413 C  CG     . MET B 1 60  ? -12.07000 -21.05000 17.65800  1.000 29.03243 ? 56  MET B CG     1 
ATOM   4414 S  SD     . MET B 1 60  ? -12.72000 -22.72100 17.65900  1.000 36.10959 ? 56  MET B SD     1 
ATOM   4415 C  CE     . MET B 1 60  ? -13.96200 -22.48400 18.92700  1.000 34.91208 ? 56  MET B CE     1 
ATOM   4416 N  N      . ALA B 1 61  ? -10.53300 -18.79300 14.01600  1.000 23.78180 ? 57  ALA B N      1 
ATOM   4417 C  CA     . ALA B 1 61  ? -9.71500  -18.53500 12.84400  1.000 21.01568 ? 57  ALA B CA     1 
ATOM   4418 C  C      . ALA B 1 61  ? -8.83000  -17.32400 13.07900  1.000 22.21056 ? 57  ALA B C      1 
ATOM   4419 O  O      . ALA B 1 61  ? -7.65800  -17.31800 12.69000  1.000 29.26140 ? 57  ALA B O      1 
ATOM   4420 C  CB     . ALA B 1 61  ? -10.62000 -18.32000 11.62200  1.000 19.20230 ? 57  ALA B CB     1 
ATOM   4421 N  N      . GLU B 1 62  ? -9.37500  -16.29900 13.74300  1.000 22.48427 ? 58  GLU B N      1 
ATOM   4422 C  CA     . GLU B 1 62  ? -8.60800  -15.08800 14.02900  1.000 24.60295 ? 58  GLU B CA     1 
ATOM   4423 C  C      . GLU B 1 62  ? -7.44200  -15.39900 14.96300  1.000 24.85298 ? 58  GLU B C      1 
ATOM   4424 O  O      . GLU B 1 62  ? -6.30600  -14.95600 14.73800  1.000 31.94330 ? 58  GLU B O      1 
ATOM   4425 C  CB     . GLU B 1 62  ? -9.53300  -14.02000 14.63700  1.000 24.98457 ? 58  GLU B CB     1 
ATOM   4426 C  CG     . GLU B 1 62  ? -9.03300  -12.56200 14.50100  1.000 31.90646 ? 58  GLU B CG     1 
ATOM   4427 C  CD     . GLU B 1 62  ? -8.03300  -12.15900 15.61000  1.000 43.88684 ? 58  GLU B CD     1 
ATOM   4428 O  OE1    . GLU B 1 62  ? -7.95000  -12.87100 16.64900  1.000 39.69686 ? 58  GLU B OE1    1 
ATOM   4429 O  OE2    . GLU B 1 62  ? -7.33000  -11.13300 15.43400  1.000 38.12299 ? 58  GLU B OE2    1 
ATOM   4430 N  N      . GLY B 1 63  ? -7.70800  -16.17100 16.01500  1.000 26.70320 ? 59  GLY B N      1 
ATOM   4431 C  CA     . GLY B 1 63  ? -6.64400  -16.56600 16.92200  1.000 24.62664 ? 59  GLY B CA     1 
ATOM   4432 C  C      . GLY B 1 63  ? -5.63200  -17.47400 16.25600  1.000 24.33713 ? 59  GLY B C      1 
ATOM   4433 O  O      . GLY B 1 63  ? -4.41700  -17.32000 16.45400  1.000 26.01891 ? 59  GLY B O      1 
ATOM   4434 N  N      . TYR B 1 64  ? -6.11000  -18.44000 15.46100  1.000 26.80058 ? 60  TYR B N      1 
ATOM   4435 C  CA     . TYR B 1 64  ? -5.18100  -19.28700 14.71600  1.000 25.01879 ? 60  TYR B CA     1 
ATOM   4436 C  C      . TYR B 1 64  ? -4.27900  -18.43500 13.82600  1.000 27.38486 ? 60  TYR B C      1 
ATOM   4437 O  O      . TYR B 1 64  ? -3.05500  -18.61600 13.81400  1.000 26.82953 ? 60  TYR B O      1 
ATOM   4438 C  CB     . TYR B 1 64  ? -5.93400  -20.32600 13.88600  1.000 20.77881 ? 60  TYR B CB     1 
ATOM   4439 C  CG     . TYR B 1 64  ? -4.99600  -21.20600 13.08200  1.000 26.18998 ? 60  TYR B CG     1 
ATOM   4440 C  CD1    . TYR B 1 64  ? -4.56300  -20.82200 11.81700  1.000 29.55881 ? 60  TYR B CD1    1 
ATOM   4441 C  CD2    . TYR B 1 64  ? -4.52400  -22.40600 13.59800  1.000 27.50067 ? 60  TYR B CD2    1 
ATOM   4442 C  CE1    . TYR B 1 64  ? -3.68700  -21.61700 11.08300  1.000 30.64052 ? 60  TYR B CE1    1 
ATOM   4443 C  CE2    . TYR B 1 64  ? -3.65500  -23.20800 12.87300  1.000 32.86710 ? 60  TYR B CE2    1 
ATOM   4444 C  CZ     . TYR B 1 64  ? -3.23900  -22.80700 11.61300  1.000 40.13376 ? 60  TYR B CZ     1 
ATOM   4445 O  OH     . TYR B 1 64  ? -2.37500  -23.60700 10.88300  1.000 51.15350 ? 60  TYR B OH     1 
ATOM   4446 N  N      . ALA B 1 65  ? -4.86700  -17.46700 13.10400  1.000 22.26320 ? 61  ALA B N      1 
ATOM   4447 C  CA     . ALA B 1 65  ? -4.07600  -16.62600 12.20400  1.000 27.82702 ? 61  ALA B CA     1 
ATOM   4448 C  C      . ALA B 1 65  ? -3.02800  -15.81700 12.96400  1.000 29.86937 ? 61  ALA B C      1 
ATOM   4449 O  O      . ALA B 1 65  ? -1.85600  -15.76100 12.56100  1.000 30.95898 ? 61  ALA B O      1 
ATOM   4450 C  CB     . ALA B 1 65  ? -4.99200  -15.68900 11.40500  1.000 19.80764 ? 61  ALA B CB     1 
ATOM   4451 N  N      . ARG B 1 66  ? -3.42900  -15.16200 14.05700  1.000 23.11067 ? 62  ARG B N      1 
ATOM   4452 C  CA     . ARG B 1 66  ? -2.48200  -14.29800 14.75300  1.000 24.45293 ? 62  ARG B CA     1 
ATOM   4453 C  C      . ARG B 1 66  ? -1.30700  -15.10100 15.30200  1.000 29.29299 ? 62  ARG B C      1 
ATOM   4454 O  O      . ARG B 1 66  ? -0.15500  -14.68000 15.18500  1.000 32.08806 ? 62  ARG B O      1 
ATOM   4455 C  CB     . ARG B 1 66  ? -3.17500  -13.52800 15.88100  1.000 28.08495 ? 62  ARG B CB     1 
ATOM   4456 C  CG     . ARG B 1 66  ? -3.92900  -12.28200 15.40800  1.000 37.86243 ? 62  ARG B CG     1 
ATOM   4457 C  CD     . ARG B 1 66  ? -4.33300  -11.38300 16.57200  1.000 37.08866 ? 62  ARG B CD     1 
ATOM   4458 N  NE     . ARG B 1 66  ? -3.16100  -10.90800 17.29100  1.000 29.31404 ? 62  ARG B NE     1 
ATOM   4459 C  CZ     . ARG B 1 66  ? -3.20600  -10.06700 18.31900  1.000 33.67509 ? 62  ARG B CZ     1 
ATOM   4460 N  NH1    . ARG B 1 66  ? -4.36900  -9.60800  18.75000  1.000 26.74531 ? 62  ARG B NH1    1 
ATOM   4461 N  NH2    . ARG B 1 66  ? -2.08100  -9.68400  18.91700  1.000 34.13567 ? 62  ARG B NH2    1 
ATOM   4462 N  N      . VAL B 1 67  ? -1.57400  -16.26600 15.89000  1.000 29.18508 ? 63  VAL B N      1 
ATOM   4463 C  CA     . VAL B 1 67  ? -0.48800  -17.05300 16.46000  1.000 27.29011 ? 63  VAL B CA     1 
ATOM   4464 C  C      . VAL B 1 67  ? 0.33700   -17.71500 15.36200  1.000 28.17180 ? 63  VAL B C      1 
ATOM   4465 O  O      . VAL B 1 67  ? 1.56300   -17.77000 15.44600  1.000 28.18496 ? 63  VAL B O      1 
ATOM   4466 C  CB     . VAL B 1 67  ? -1.04200  -18.08800 17.45400  1.000 27.06904 ? 63  VAL B CB     1 
ATOM   4467 C  CG1    . VAL B 1 67  ? 0.05200   -19.05300 17.89500  1.000 27.48751 ? 63  VAL B CG1    1 
ATOM   4468 C  CG2    . VAL B 1 67  ? -1.66200  -17.38100 18.66300  1.000 27.80597 ? 63  VAL B CG2    1 
ATOM   4469 N  N      . SER B 1 68  ? -0.30900  -18.24800 14.32500  1.000 25.95311 ? 64  SER B N      1 
ATOM   4470 C  CA     . SER B 1 68  ? 0.44400   -18.97100 13.30200  1.000 30.93002 ? 64  SER B CA     1 
ATOM   4471 C  C      . SER B 1 68  ? 1.19200   -18.04800 12.34800  1.000 33.22767 ? 64  SER B C      1 
ATOM   4472 O  O      . SER B 1 68  ? 2.10900   -18.50600 11.65600  1.000 32.60391 ? 64  SER B O      1 
ATOM   4473 C  CB     . SER B 1 68  ? -0.48000  -19.86900 12.48200  1.000 33.41453 ? 64  SER B CB     1 
ATOM   4474 O  OG     . SER B 1 68  ? -1.32800  -19.07400 11.65900  1.000 35.47004 ? 64  SER B OG     1 
ATOM   4475 N  N      . GLY B 1 69  ? 0.77600   -16.78800 12.24000  1.000 29.27456 ? 65  GLY B N      1 
ATOM   4476 C  CA     . GLY B 1 69  ? 1.28700   -15.93900 11.18900  1.000 32.20123 ? 65  GLY B CA     1 
ATOM   4477 C  C      . GLY B 1 69  ? 0.78600   -16.30600 9.81800   1.000 35.53584 ? 65  GLY B C      1 
ATOM   4478 O  O      . GLY B 1 69  ? 1.31000   -15.79500 8.82400   1.000 40.72857 ? 65  GLY B O      1 
ATOM   4479 N  N      . LYS B 1 70  ? -0.21800  -17.17400 9.73200   1.000 31.38271 ? 66  LYS B N      1 
ATOM   4480 C  CA     . LYS B 1 70  ? -0.73600  -17.66700 8.47100   1.000 28.74292 ? 66  LYS B CA     1 
ATOM   4481 C  C      . LYS B 1 70  ? -2.18700  -17.23000 8.31300   1.000 31.82487 ? 66  LYS B C      1 
ATOM   4482 O  O      . LYS B 1 70  ? -2.75600  -16.54900 9.16700   1.000 32.54074 ? 66  LYS B O      1 
ATOM   4483 C  CB     . LYS B 1 70  ? -0.60100  -19.19200 8.39500   1.000 30.07466 ? 66  LYS B CB     1 
ATOM   4484 C  CG     . LYS B 1 70  ? 0.84400   -19.67600 8.57300   1.000 39.72318 ? 66  LYS B CG     1 
ATOM   4485 C  CD     . LYS B 1 70  ? 1.03100   -21.10500 8.10600   1.000 45.22648 ? 66  LYS B CD     1 
ATOM   4486 C  CE     . LYS B 1 70  ? 0.02900   -22.04300 8.78300   1.000 55.17240 ? 66  LYS B CE     1 
ATOM   4487 N  NZ     . LYS B 1 70  ? 0.49900   -23.46000 8.76700   1.000 63.09178 ? 66  LYS B NZ     1 
ATOM   4488 N  N      . LEU B 1 71  ? -2.78500  -17.64500 7.20700   1.000 28.00599 ? 67  LEU B N      1 
ATOM   4489 C  CA     . LEU B 1 71  ? -4.17500  -17.32100 6.93600   1.000 28.95347 ? 67  LEU B CA     1 
ATOM   4490 C  C      . LEU B 1 71  ? -5.08200  -18.18500 7.80700   1.000 27.34802 ? 67  LEU B C      1 
ATOM   4491 O  O      . LEU B 1 71  ? -4.88800  -19.40000 7.90000   1.000 30.24047 ? 67  LEU B O      1 
ATOM   4492 C  CB     . LEU B 1 71  ? -4.47500  -17.54000 5.45400   1.000 28.56132 ? 67  LEU B CB     1 
ATOM   4493 C  CG     . LEU B 1 71  ? -5.92300  -17.32600 5.02400   1.000 32.24334 ? 67  LEU B CG     1 
ATOM   4494 C  CD1    . LEU B 1 71  ? -6.21800  -15.84000 4.94800   1.000 27.79017 ? 67  LEU B CD1    1 
ATOM   4495 C  CD2    . LEU B 1 71  ? -6.17500  -18.00200 3.68400   1.000 32.46179 ? 67  LEU B CD2    1 
ATOM   4496 N  N      . GLY B 1 72  ? -6.06600  -17.55800 8.45800   1.000 29.24298 ? 68  GLY B N      1 
ATOM   4497 C  CA     . GLY B 1 72  ? -7.10300  -18.30900 9.14800   1.000 29.16665 ? 68  GLY B CA     1 
ATOM   4498 C  C      . GLY B 1 72  ? -8.32500  -18.45400 8.25600   1.000 28.28760 ? 68  GLY B C      1 
ATOM   4499 O  O      . GLY B 1 72  ? -8.63200  -17.58200 7.45100   1.000 27.42171 ? 68  GLY B O      1 
ATOM   4500 N  N      . VAL B 1 73  ? -9.03100  -19.57400 8.37300   1.000 24.61611 ? 69  VAL B N      1 
ATOM   4501 C  CA     . VAL B 1 73  ? -10.17000 -19.82700 7.49700   1.000 25.20039 ? 69  VAL B CA     1 
ATOM   4502 C  C      . VAL B 1 73  ? -11.35500 -20.32800 8.31200   1.000 25.86889 ? 69  VAL B C      1 
ATOM   4503 O  O      . VAL B 1 73  ? -11.21500 -21.26300 9.10800   1.000 21.95000 ? 69  VAL B O      1 
ATOM   4504 C  CB     . VAL B 1 73  ? -9.82600  -20.84600 6.39900   1.000 25.00563 ? 69  VAL B CB     1 
ATOM   4505 C  CG1    . VAL B 1 73  ? -11.05800 -21.06700 5.50400   1.000 20.69459 ? 69  VAL B CG1    1 
ATOM   4506 C  CG2    . VAL B 1 73  ? -8.62500  -20.37200 5.59400   1.000 21.57364 ? 69  VAL B CG2    1 
ATOM   4507 N  N      . CYS B 1 74  ? -12.50900 -19.69600 8.13500   1.000 28.46657 ? 70  CYS B N      1 
ATOM   4508 C  CA     . CYS B 1 74  ? -13.74600 -20.20900 8.71600   1.000 20.39981 ? 70  CYS B CA     1 
ATOM   4509 C  C      . CYS B 1 74  ? -14.81600 -20.33100 7.62500   1.000 24.47662 ? 70  CYS B C      1 
ATOM   4510 O  O      . CYS B 1 74  ? -14.71100 -19.72200 6.56300   1.000 24.16079 ? 70  CYS B O      1 
ATOM   4511 C  CB     . CYS B 1 74  ? -14.24300 -19.33400 9.86300   1.000 22.27899 ? 70  CYS B CB     1 
ATOM   4512 S  SG     . CYS B 1 74  ? -14.26500 -17.60300 9.47100   1.000 31.15637 ? 70  CYS B SG     1 
ATOM   4513 N  N      . CYS B 1 75  ? -15.79200 -21.20700 7.84200   1.000 22.95275 ? 71  CYS B N      1 
ATOM   4514 C  CA     . CYS B 1 75  ? -16.89300 -21.33500 6.88700   1.000 24.40029 ? 71  CYS B CA     1 
ATOM   4515 C  C      . CYS B 1 75  ? -18.24100 -21.30000 7.61600   1.000 25.91890 ? 71  CYS B C      1 
ATOM   4516 O  O      . CYS B 1 75  ? -18.37000 -21.72800 8.76400   1.000 26.82953 ? 71  CYS B O      1 
ATOM   4517 C  CB     . CYS B 1 75  ? -16.79000 -22.61800 6.05500   1.000 25.04774 ? 71  CYS B CB     1 
ATOM   4518 S  SG     . CYS B 1 75  ? -16.78500 -24.06300 7.09900   1.000 29.57197 ? 71  CYS B SG     1 
ATOM   4519 N  N      . ALA B 1 76  ? -19.22800 -20.74000 6.92700   1.000 22.39479 ? 72  ALA B N      1 
ATOM   4520 C  CA     . ALA B 1 76  ? -20.59200 -20.66900 7.42900   1.000 23.37122 ? 72  ALA B CA     1 
ATOM   4521 C  C      . ALA B 1 76  ? -21.58000 -20.85800 6.28600   1.000 29.78778 ? 72  ALA B C      1 
ATOM   4522 O  O      . ALA B 1 76  ? -21.28100 -20.58000 5.11600   1.000 31.19058 ? 72  ALA B O      1 
ATOM   4523 C  CB     . ALA B 1 76  ? -20.84000 -19.31900 8.09700   1.000 20.25769 ? 72  ALA B CB     1 
ATOM   4524 N  N      . THR B 1 77  ? -22.76900 -21.32500 6.63400   1.000 29.12981 ? 73  THR B N      1 
ATOM   4525 C  CA     . THR B 1 77  ? -23.80400 -21.55700 5.64000   1.000 19.93397 ? 73  THR B CA     1 
ATOM   4526 C  C      . THR B 1 77  ? -24.51200 -20.24800 5.28200   1.000 25.91100 ? 73  THR B C      1 
ATOM   4527 O  O      . THR B 1 77  ? -24.21300 -19.17100 5.81300   1.000 23.64757 ? 73  THR B O      1 
ATOM   4528 C  CB     . THR B 1 77  ? -24.78200 -22.61800 6.13900   1.000 24.89772 ? 73  THR B CB     1 
ATOM   4529 O  OG1    . THR B 1 77  ? -25.56100 -23.07300 5.03700   1.000 29.79041 ? 73  THR B OG1    1 
ATOM   4530 C  CG2    . THR B 1 77  ? -25.73200 -22.05900 7.22600   1.000 25.18460 ? 73  THR B CG2    1 
ATOM   4531 N  N      . THR B 1 78  ? -25.47000 -20.34400 4.36000   1.000 21.12622 ? 74  THR B N      1 
ATOM   4532 C  CA     . THR B 1 78  ? -26.28300 -19.20900 3.94600   1.000 26.05576 ? 74  THR B CA     1 
ATOM   4533 C  C      . THR B 1 78  ? -26.88300 -18.50300 5.15100   1.000 25.38462 ? 74  THR B C      1 
ATOM   4534 O  O      . THR B 1 78  ? -27.01600 -19.10300 6.22400   1.000 24.75560 ? 74  THR B O      1 
ATOM   4535 C  CB     . THR B 1 78  ? -27.42700 -19.67500 3.04400   1.000 26.00049 ? 74  THR B CB     1 
ATOM   4536 O  OG1    . THR B 1 78  ? -27.93600 -20.90400 3.57800   1.000 32.46968 ? 74  THR B OG1    1 
ATOM   4537 C  CG2    . THR B 1 78  ? -26.94900 -19.92600 1.63200   1.000 26.77689 ? 74  THR B CG2    1 
ATOM   4538 N  N      . GLY B 1 79  ? -27.26200 -17.24000 4.97100   1.000 20.94725 ? 75  GLY B N      1 
ATOM   4539 C  CA     . GLY B 1 79  ? -28.10600 -16.53300 5.90700   1.000 20.10504 ? 75  GLY B CA     1 
ATOM   4540 C  C      . GLY B 1 79  ? -27.54600 -16.40200 7.30800   1.000 22.57902 ? 75  GLY B C      1 
ATOM   4541 O  O      . GLY B 1 79  ? -26.53500 -15.73200 7.54100   1.000 22.08686 ? 75  GLY B O      1 
ATOM   4542 N  N      . PRO B 1 80  ? -28.22200 -17.02300 8.27800   1.000 21.95790 ? 76  PRO B N      1 
ATOM   4543 C  CA     . PRO B 1 80  ? -27.86300 -16.78500 9.68600   1.000 24.10026 ? 76  PRO B CA     1 
ATOM   4544 C  C      . PRO B 1 80  ? -26.55800 -17.44100 10.08600  1.000 26.39790 ? 76  PRO B C      1 
ATOM   4545 O  O      . PRO B 1 80  ? -25.94300 -17.00900 11.07100  1.000 28.07179 ? 76  PRO B O      1 
ATOM   4546 C  CB     . PRO B 1 80  ? -29.04900 -17.38900 10.45600  1.000 20.18926 ? 76  PRO B CB     1 
ATOM   4547 C  CG     . PRO B 1 80  ? -29.45400 -18.56900 9.56800   1.000 26.93218 ? 76  PRO B CG     1 
ATOM   4548 C  CD     . PRO B 1 80  ? -29.23900 -18.07800 8.13100   1.000 21.64733 ? 76  PRO B CD     1 
ATOM   4549 N  N      . GLY B 1 81  ? -26.13200 -18.49200 9.38200   1.000 23.30806 ? 77  GLY B N      1 
ATOM   4550 C  CA     . GLY B 1 81  ? -24.78900 -19.00200 9.59500   1.000 23.96603 ? 77  GLY B CA     1 
ATOM   4551 C  C      . GLY B 1 81  ? -23.73900 -17.93500 9.35100   1.000 24.92141 ? 77  GLY B C      1 
ATOM   4552 O  O      . GLY B 1 81  ? -22.91900 -17.63600 10.22100  1.000 24.76613 ? 77  GLY B O      1 
ATOM   4553 N  N      . ALA B 1 82  ? -23.78800 -17.30600 8.17500   1.000 22.85800 ? 78  ALA B N      1 
ATOM   4554 C  CA     . ALA B 1 82  ? -22.81200 -16.27500 7.84700   1.000 26.86638 ? 78  ALA B CA     1 
ATOM   4555 C  C      . ALA B 1 82  ? -22.98100 -15.04600 8.73000   1.000 26.37685 ? 78  ALA B C      1 
ATOM   4556 O  O      . ALA B 1 82  ? -21.98900 -14.47600 9.20300   1.000 25.17407 ? 78  ALA B O      1 
ATOM   4557 C  CB     . ALA B 1 82  ? -22.93000 -15.89500 6.37000   1.000 23.17383 ? 78  ALA B CB     1 
ATOM   4558 N  N      . THR B 1 83  ? -24.22200 -14.62600 8.99600   1.000 22.47638 ? 79  THR B N      1 
ATOM   4559 C  CA     . THR B 1 83  ? -24.36100 -13.43300 9.82500   1.000 23.65020 ? 79  THR B CA     1 
ATOM   4560 C  C      . THR B 1 83  ? -23.85500 -13.68100 11.24300  1.000 22.30794 ? 79  THR B C      1 
ATOM   4561 O  O      . THR B 1 83  ? -23.33700 -12.75400 11.87100  1.000 20.82618 ? 79  THR B O      1 
ATOM   4562 C  CB     . THR B 1 83  ? -25.81600 -12.92600 9.86500   1.000 28.29813 ? 79  THR B CB     1 
ATOM   4563 O  OG1    . THR B 1 83  ? -26.66700 -13.90800 10.45900  1.000 23.94761 ? 79  THR B OG1    1 
ATOM   4564 C  CG2    . THR B 1 83  ? -26.33100 -12.54100 8.46800   1.000 27.93230 ? 79  THR B CG2    1 
ATOM   4565 N  N      . ASN B 1 84  ? -23.94100 -14.92400 11.74600  1.000 20.23927 ? 80  ASN B N      1 
ATOM   4566 C  CA     . ASN B 1 84  ? -23.40200 -15.23300 13.07300  1.000 18.63118 ? 80  ASN B CA     1 
ATOM   4567 C  C      . ASN B 1 84  ? -21.88600 -15.02700 13.14900  1.000 26.80058 ? 80  ASN B C      1 
ATOM   4568 O  O      . ASN B 1 84  ? -21.33900 -14.87200 14.24700  1.000 24.19237 ? 80  ASN B O      1 
ATOM   4569 C  CB     . ASN B 1 84  ? -23.74600 -16.68700 13.45600  1.000 18.79436 ? 80  ASN B CB     1 
ATOM   4570 C  CG     . ASN B 1 84  ? -25.03200 -16.79300 14.26700  1.000 25.10038 ? 80  ASN B CG     1 
ATOM   4571 O  OD1    . ASN B 1 84  ? -25.68600 -15.78700 14.53400  1.000 25.40568 ? 80  ASN B OD1    1 
ATOM   4572 N  ND2    . ASN B 1 84  ? -25.40500 -18.01200 14.64600  1.000 26.38474 ? 80  ASN B ND2    1 
ATOM   4573 N  N      . ALA B 1 85  ? -21.18400 -15.08400 12.01600  1.000 25.04511 ? 81  ALA B N      1 
ATOM   4574 C  CA     . ALA B 1 85  ? -19.73700 -14.92100 12.01700  1.000 21.47363 ? 81  ALA B CA     1 
ATOM   4575 C  C      . ALA B 1 85  ? -19.29700 -13.46900 12.08800  1.000 28.98505 ? 81  ALA B C      1 
ATOM   4576 O  O      . ALA B 1 85  ? -18.10900 -13.22200 12.31400  1.000 27.62173 ? 81  ALA B O      1 
ATOM   4577 C  CB     . ALA B 1 85  ? -19.14200 -15.54800 10.75200  1.000 18.04953 ? 81  ALA B CB     1 
ATOM   4578 N  N      . LEU B 1 86  ? -20.21200 -12.51200 11.89400  1.000 23.13698 ? 82  LEU B N      1 
ATOM   4579 C  CA     . LEU B 1 86  ? -19.80400 -11.15300 11.54100  1.000 27.02429 ? 82  LEU B CA     1 
ATOM   4580 C  C      . LEU B 1 86  ? -18.89500 -10.51600 12.59300  1.000 24.43714 ? 82  LEU B C      1 
ATOM   4581 O  O      . LEU B 1 86  ? -17.87500 -9.89300  12.25700  1.000 19.72868 ? 82  LEU B O      1 
ATOM   4582 C  CB     . LEU B 1 86  ? -21.03000 -10.28100 11.29900  1.000 28.54290 ? 82  LEU B CB     1 
ATOM   4583 C  CG     . LEU B 1 86  ? -20.51900 -8.95400  10.73600  1.000 35.72534 ? 82  LEU B CG     1 
ATOM   4584 C  CD1    . LEU B 1 86  ? -21.15800 -8.60700  9.39400   1.000 33.29083 ? 82  LEU B CD1    1 
ATOM   4585 C  CD2    . LEU B 1 86  ? -20.71500 -7.84900  11.75700  1.000 41.09440 ? 82  LEU B CD2    1 
ATOM   4586 N  N      . THR B 1 87  ? -19.26600 -10.61100 13.86700  1.000 19.52603 ? 83  THR B N      1 
ATOM   4587 C  CA     . THR B 1 87  ? -18.45800 -9.96200  14.89200  1.000 21.24992 ? 83  THR B CA     1 
ATOM   4588 C  C      . THR B 1 87  ? -17.01200 -10.43400 14.81600  1.000 21.08148 ? 83  THR B C      1 
ATOM   4589 O  O      . THR B 1 87  ? -16.08100 -9.62600  14.91900  1.000 23.83180 ? 83  THR B O      1 
ATOM   4590 C  CB     . THR B 1 87  ? -19.04200 -10.22300 16.28400  1.000 23.55019 ? 83  THR B CB     1 
ATOM   4591 O  OG1    . THR B 1 87  ? -20.35300 -9.64300  16.36400  1.000 24.25554 ? 83  THR B OG1    1 
ATOM   4592 C  CG2    . THR B 1 87  ? -18.13600 -9.61800  17.39400  1.000 19.45760 ? 83  THR B CG2    1 
ATOM   4593 N  N      . GLY B 1 88  ? -16.80400 -11.73700 14.60800  1.000 24.62664 ? 84  GLY B N      1 
ATOM   4594 C  CA     . GLY B 1 88  ? -15.44900 -12.24700 14.51100  1.000 17.11258 ? 84  GLY B CA     1 
ATOM   4595 C  C      . GLY B 1 88  ? -14.71200 -11.69800 13.30500  1.000 23.04750 ? 84  GLY B C      1 
ATOM   4596 O  O      . GLY B 1 88  ? -13.53200 -11.35600 13.38700  1.000 23.65020 ? 84  GLY B O      1 
ATOM   4597 N  N      . ILE B 1 89  ? -15.39400 -11.60300 12.16600  1.000 24.42398 ? 85  ILE B N      1 
ATOM   4598 C  CA     . ILE B 1 89  ? -14.76700 -10.98200 11.01100  1.000 23.64494 ? 85  ILE B CA     1 
ATOM   4599 C  C      . ILE B 1 89  ? -14.49300 -9.51000  11.29400  1.000 25.17933 ? 85  ILE B C      1 
ATOM   4600 O  O      . ILE B 1 89  ? -13.43200 -8.98100  10.93700  1.000 23.43439 ? 85  ILE B O      1 
ATOM   4601 C  CB     . ILE B 1 89  ? -15.64400 -11.17300 9.76900   1.000 24.50557 ? 85  ILE B CB     1 
ATOM   4602 C  CG1    . ILE B 1 89  ? -15.93600 -12.66400 9.58500   1.000 21.50521 ? 85  ILE B CG1    1 
ATOM   4603 C  CG2    . ILE B 1 89  ? -14.97600 -10.54200 8.54500   1.000 23.53177 ? 85  ILE B CG2    1 
ATOM   4604 C  CD1    . ILE B 1 89  ? -14.71500 -13.50600 9.65100   1.000 22.39216 ? 85  ILE B CD1    1 
ATOM   4605 N  N      . ALA B 1 90  ? -15.41200 -8.83800  11.98900  1.000 23.97393 ? 86  ALA B N      1 
ATOM   4606 C  CA     . ALA B 1 90  ? -15.18100 -7.43200  12.30300  1.000 20.51035 ? 86  ALA B CA     1 
ATOM   4607 C  C      . ALA B 1 90  ? -13.97400 -7.26000  13.21700  1.000 25.41357 ? 86  ALA B C      1 
ATOM   4608 O  O      . ALA B 1 90  ? -13.25600 -6.25700  13.10900  1.000 20.94988 ? 86  ALA B O      1 
ATOM   4609 C  CB     . ALA B 1 90  ? -16.42500 -6.81400  12.93400  1.000 21.20781 ? 86  ALA B CB     1 
ATOM   4610 N  N      . CYS B 1 91  ? -13.69800 -8.24400  14.08400  1.000 22.20529 ? 87  CYS B N      1 
ATOM   4611 C  CA     . CYS B 1 91  ? -12.51300 -8.13100  14.92800  1.000 24.89509 ? 87  CYS B CA     1 
ATOM   4612 C  C      . CYS B 1 91  ? -11.24200 -8.36900  14.13400  1.000 26.51371 ? 87  CYS B C      1 
ATOM   4613 O  O      . CYS B 1 91  ? -10.24700 -7.65600  14.31500  1.000 23.74495 ? 87  CYS B O      1 
ATOM   4614 C  CB     . CYS B 1 91  ? -12.57700 -9.14600  16.06900  1.000 22.28688 ? 87  CYS B CB     1 
ATOM   4615 S  SG     . CYS B 1 91  ? -13.84200 -8.78700  17.27400  1.000 31.89856 ? 87  CYS B SG     1 
ATOM   4616 N  N      . ALA B 1 92  ? -11.27700 -9.32400  13.20700  1.000 24.23448 ? 88  ALA B N      1 
ATOM   4617 C  CA     . ALA B 1 92  ? -10.13200 -9.51300  12.32900  1.000 19.54445 ? 88  ALA B CA     1 
ATOM   4618 C  C      . ALA B 1 92  ? -9.86600  -8.24900  11.52700  1.000 20.38929 ? 88  ALA B C      1 
ATOM   4619 O  O      . ALA B 1 92  ? -8.71200  -7.83300  11.36500  1.000 25.50832 ? 88  ALA B O      1 
ATOM   4620 C  CB     . ALA B 1 92  ? -10.36500 -10.70900 11.40800  1.000 19.78132 ? 88  ALA B CB     1 
ATOM   4621 N  N      . TYR B 1 93  ? -10.93100 -7.60200  11.06400  1.000 20.24190 ? 89  TYR B N      1 
ATOM   4622 C  CA     . TYR B 1 93  ? -10.79400 -6.36600  10.31000  1.000 18.51011 ? 89  TYR B CA     1 
ATOM   4623 C  C      . TYR B 1 93  ? -10.14500 -5.29100  11.15300  1.000 21.17096 ? 89  TYR B C      1 
ATOM   4624 O  O      . TYR B 1 93  ? -9.21700  -4.60800  10.70000  1.000 25.15565 ? 89  TYR B O      1 
ATOM   4625 C  CB     . TYR B 1 93  ? -12.17100 -5.91700  9.83100   1.000 20.77618 ? 89  TYR B CB     1 
ATOM   4626 C  CG     . TYR B 1 93  ? -12.18100 -4.65000  9.01500   1.000 23.65284 ? 89  TYR B CG     1 
ATOM   4627 C  CD1    . TYR B 1 93  ? -11.80300 -4.65800  7.67900   1.000 22.90275 ? 89  TYR B CD1    1 
ATOM   4628 C  CD2    . TYR B 1 93  ? -12.59400 -3.45400  9.57800   1.000 26.56634 ? 89  TYR B CD2    1 
ATOM   4629 C  CE1    . TYR B 1 93  ? -11.82300 -3.50300  6.93200   1.000 26.56898 ? 89  TYR B CE1    1 
ATOM   4630 C  CE2    . TYR B 1 93  ? -12.62700 -2.30100  8.84300   1.000 26.09260 ? 89  TYR B CE2    1 
ATOM   4631 C  CZ     . TYR B 1 93  ? -12.23800 -2.32900  7.52400   1.000 28.03231 ? 89  TYR B CZ     1 
ATOM   4632 O  OH     . TYR B 1 93  ? -12.27200 -1.17000  6.80500   1.000 31.85382 ? 89  TYR B OH     1 
ATOM   4633 N  N      . SER B 1 94  ? -10.57000 -5.16100  12.40900  1.000 22.60271 ? 90  SER B N      1 
ATOM   4634 C  CA     . SER B 1 94  ? -10.03300 -4.08900  13.23600  1.000 22.29215 ? 90  SER B CA     1 
ATOM   4635 C  C      . SER B 1 94  ? -8.61900  -4.39600  13.75200  1.000 25.58465 ? 90  SER B C      1 
ATOM   4636 O  O      . SER B 1 94  ? -7.86700  -3.47100  14.07600  1.000 24.85824 ? 90  SER B O      1 
ATOM   4637 C  CB     . SER B 1 94  ? -11.02300 -3.80000  14.37600  1.000 35.94905 ? 90  SER B CB     1 
ATOM   4638 O  OG     . SER B 1 94  ? -10.73100 -4.62500  15.49700  1.000 53.51957 ? 90  SER B OG     1 
ATOM   4639 N  N      . ASP B 1 95  ? -8.21300  -5.66600  13.79000  1.000 20.53404 ? 91  ASP B N      1 
ATOM   4640 C  CA     . ASP B 1 95  ? -6.86300  -6.00800  14.22900  1.000 26.28473 ? 91  ASP B CA     1 
ATOM   4641 C  C      . ASP B 1 95  ? -5.92800  -6.34100  13.06200  1.000 28.65080 ? 91  ASP B C      1 
ATOM   4642 O  O      . ASP B 1 95  ? -4.80400  -6.79200  13.29000  1.000 28.84293 ? 91  ASP B O      1 
ATOM   4643 C  CB     . ASP B 1 95  ? -6.90700  -7.16600  15.22800  1.000 25.33462 ? 91  ASP B CB     1 
ATOM   4644 C  CG     . ASP B 1 95  ? -7.58400  -6.76900  16.55500  1.000 36.44911 ? 91  ASP B CG     1 
ATOM   4645 O  OD1    . ASP B 1 95  ? -7.52300  -5.56000  16.89700  1.000 31.23006 ? 91  ASP B OD1    1 
ATOM   4646 O  OD2    . ASP B 1 95  ? -8.17100  -7.63900  17.25000  1.000 28.46394 ? 91  ASP B OD2    1 
ATOM   4647 N  N      . SER B 1 96  ? -6.37200  -6.14300  11.81600  1.000 22.35005 ? 92  SER B N      1 
ATOM   4648 C  CA     . SER B 1 96  ? -5.53700  -6.40600  10.64300  1.000 26.35579 ? 92  SER B CA     1 
ATOM   4649 C  C      . SER B 1 96  ? -5.04800  -7.85700  10.61100  1.000 24.43451 ? 92  SER B C      1 
ATOM   4650 O  O      . SER B 1 96  ? -3.86800  -8.12900  10.42300  1.000 25.24250 ? 92  SER B O      1 
ATOM   4651 C  CB     . SER B 1 96  ? -4.34900  -5.44100  10.59800  1.000 26.76374 ? 92  SER B CB     1 
ATOM   4652 O  OG     . SER B 1 96  ? -4.81600  -4.10300  10.67700  1.000 30.14835 ? 92  SER B OG     1 
ATOM   4653 N  N      . THR B 1 97  ? -5.97300  -8.78800  10.82700  1.000 22.37110 ? 93  THR B N      1 
ATOM   4654 C  CA     . THR B 1 97  ? -5.69400  -10.21800 10.79400  1.000 23.38438 ? 93  THR B CA     1 
ATOM   4655 C  C      . THR B 1 97  ? -6.24700  -10.81900 9.51900   1.000 22.87643 ? 93  THR B C      1 
ATOM   4656 O  O      . THR B 1 97  ? -7.42100  -10.59100 9.19800   1.000 26.19261 ? 93  THR B O      1 
ATOM   4657 C  CB     . THR B 1 97  ? -6.33000  -10.93000 11.98800  1.000 25.47411 ? 93  THR B CB     1 
ATOM   4658 O  OG1    . THR B 1 97  ? -6.04300  -10.22500 13.19300  1.000 26.23999 ? 93  THR B OG1    1 
ATOM   4659 C  CG2    . THR B 1 97  ? -5.81500  -12.35300 12.08300  1.000 28.70081 ? 93  THR B CG2    1 
ATOM   4660 N  N      . PRO B 1 98  ? -5.46500  -11.62000 8.80600   1.000 24.48978 ? 94  PRO B N      1 
ATOM   4661 C  CA     . PRO B 1 98  ? -5.97100  -12.26400 7.58700   1.000 22.47901 ? 94  PRO B CA     1 
ATOM   4662 C  C      . PRO B 1 98  ? -6.84800  -13.46800 7.88800   1.000 27.17957 ? 94  PRO B C      1 
ATOM   4663 O  O      . PRO B 1 98  ? -6.34600  -14.55200 8.20500   1.000 26.03207 ? 94  PRO B O      1 
ATOM   4664 C  CB     . PRO B 1 98  ? -4.68800  -12.67300 6.85100   1.000 25.45568 ? 94  PRO B CB     1 
ATOM   4665 C  CG     . PRO B 1 98  ? -3.67200  -12.89200 7.98600   1.000 22.54218 ? 94  PRO B CG     1 
ATOM   4666 C  CD     . PRO B 1 98  ? -4.02200  -11.85000 9.02100   1.000 24.33450 ? 94  PRO B CD     1 
ATOM   4667 N  N      . VAL B 1 99  ? -8.16500  -13.27300 7.82000   1.000 25.55043 ? 95  VAL B N      1 
ATOM   4668 C  CA     . VAL B 1 99  ? -9.14500  -14.33600 8.00900   1.000 22.99749 ? 95  VAL B CA     1 
ATOM   4669 C  C      . VAL B 1 99  ? -9.99100  -14.42700 6.74500   1.000 30.80369 ? 95  VAL B C      1 
ATOM   4670 O  O      . VAL B 1 99  ? -10.54100 -13.42200 6.27600   1.000 26.73478 ? 95  VAL B O      1 
ATOM   4671 C  CB     . VAL B 1 99  ? -10.04000 -14.08800 9.23900   1.000 22.61587 ? 95  VAL B CB     1 
ATOM   4672 C  CG1    . VAL B 1 99  ? -11.13300 -15.16300 9.32600   1.000 19.96292 ? 95  VAL B CG1    1 
ATOM   4673 C  CG2    . VAL B 1 99  ? -9.20100  -14.10200 10.50300  1.000 25.80309 ? 95  VAL B CG2    1 
ATOM   4674 N  N      . LEU B 1 100 ? -10.09300 -15.62300 6.20100   1.000 26.35579 ? 96  LEU B N      1 
ATOM   4675 C  CA     . LEU B 1 100 ? -10.96000 -15.88100 5.06300   1.000 19.90765 ? 96  LEU B CA     1 
ATOM   4676 C  C      . LEU B 1 100 ? -12.24600 -16.50900 5.57800   1.000 24.45293 ? 96  LEU B C      1 
ATOM   4677 O  O      . LEU B 1 100 ? -12.21700 -17.58100 6.19500   1.000 23.41070 ? 96  LEU B O      1 
ATOM   4678 C  CB     . LEU B 1 100 ? -10.27000 -16.80300 4.06600   1.000 19.28126 ? 96  LEU B CB     1 
ATOM   4679 C  CG     . LEU B 1 100 ? -11.11800 -17.37400 2.92700   1.000 25.49779 ? 96  LEU B CG     1 
ATOM   4680 C  CD1    . LEU B 1 100 ? -11.69500 -16.24600 2.10100   1.000 23.90287 ? 96  LEU B CD1    1 
ATOM   4681 C  CD2    . LEU B 1 100 ? -10.25500 -18.29300 2.06000   1.000 25.05827 ? 96  LEU B CD2    1 
ATOM   4682 N  N      . LEU B 1 101 ? -13.36800 -15.84400 5.33700   1.000 17.83372 ? 97  LEU B N      1 
ATOM   4683 C  CA     . LEU B 1 101 ? -14.67800 -16.42100 5.61700   1.000 23.73706 ? 97  LEU B CA     1 
ATOM   4684 C  C      . LEU B 1 101 ? -15.29500 -16.93100 4.31300   1.000 25.23197 ? 97  LEU B C      1 
ATOM   4685 O  O      . LEU B 1 101 ? -15.58200 -16.14600 3.39900   1.000 27.70595 ? 97  LEU B O      1 
ATOM   4686 C  CB     . LEU B 1 101 ? -15.59000 -15.39400 6.28100   1.000 21.11569 ? 97  LEU B CB     1 
ATOM   4687 C  CG     . LEU B 1 101 ? -17.05300 -15.82300 6.33100   1.000 27.60331 ? 97  LEU B CG     1 
ATOM   4688 C  CD1    . LEU B 1 101 ? -17.18700 -17.04400 7.23700   1.000 25.19513 ? 97  LEU B CD1    1 
ATOM   4689 C  CD2    . LEU B 1 101 ? -17.93000 -14.67800 6.83000   1.000 24.11605 ? 97  LEU B CD2    1 
ATOM   4690 N  N      . LEU B 1 102 ? -15.50600 -18.23600 4.24000   1.000 20.12347 ? 98  LEU B N      1 
ATOM   4691 C  CA     . LEU B 1 102 ? -16.19000 -18.87500 3.12200   1.000 22.77642 ? 98  LEU B CA     1 
ATOM   4692 C  C      . LEU B 1 102 ? -17.65300 -19.06200 3.49200   1.000 26.39264 ? 98  LEU B C      1 
ATOM   4693 O  O      . LEU B 1 102 ? -17.95100 -19.73000 4.48800   1.000 30.67210 ? 98  LEU B O      1 
ATOM   4694 C  CB     . LEU B 1 102 ? -15.56100 -20.23500 2.81500   1.000 22.56586 ? 98  LEU B CB     1 
ATOM   4695 C  CG     . LEU B 1 102 ? -14.06600 -20.21600 2.52100   1.000 26.48739 ? 98  LEU B CG     1 
ATOM   4696 C  CD1    . LEU B 1 102 ? -13.53300 -21.63700 2.44700   1.000 26.90849 ? 98  LEU B CD1    1 
ATOM   4697 C  CD2    . LEU B 1 102 ? -13.85100 -19.48600 1.21000   1.000 26.12682 ? 98  LEU B CD2    1 
ATOM   4698 N  N      . THR B 1 103 ? -18.56500 -18.49200 2.70400   1.000 23.61336 ? 99  THR B N      1 
ATOM   4699 C  CA     . THR B 1 103 ? -19.99200 -18.67500 2.95800   1.000 23.46597 ? 99  THR B CA     1 
ATOM   4700 C  C      . THR B 1 103 ? -20.67800 -19.33300 1.77200   1.000 24.83456 ? 99  THR B C      1 
ATOM   4701 O  O      . THR B 1 103 ? -20.30300 -19.12600 0.61100   1.000 24.85298 ? 99  THR B O      1 
ATOM   4702 C  CB     . THR B 1 103 ? -20.72100 -17.35200 3.27300   1.000 24.02130 ? 99  THR B CB     1 
ATOM   4703 O  OG1    . THR B 1 103 ? -20.68800 -16.46900 2.13600   1.000 24.47136 ? 99  THR B OG1    1 
ATOM   4704 C  CG2    . THR B 1 103 ? -20.10300 -16.67000 4.47300   1.000 19.02070 ? 99  THR B CG2    1 
ATOM   4705 N  N      . ALA B 1 104 ? -21.72600 -20.08600 2.07500   1.000 22.50270 ? 100 ALA B N      1 
ATOM   4706 C  CA     . ALA B 1 104 ? -22.51900 -20.70700 1.03100   1.000 26.07681 ? 100 ALA B CA     1 
ATOM   4707 C  C      . ALA B 1 104 ? -23.56900 -19.74200 0.49400   1.000 28.72450 ? 100 ALA B C      1 
ATOM   4708 O  O      . ALA B 1 104 ? -23.96300 -18.76000 1.13900   1.000 26.90586 ? 100 ALA B O      1 
ATOM   4709 C  CB     . ALA B 1 104 ? -23.20600 -21.97500 1.54800   1.000 18.99175 ? 100 ALA B CB     1 
ATOM   4710 N  N      . GLN B 1 105 ? -24.00600 -20.02500 -0.72400  1.000 26.59793 ? 101 GLN B N      1 
ATOM   4711 C  CA     . GLN B 1 105 ? -25.07200 -19.28700 -1.37100  1.000 24.10552 ? 101 GLN B CA     1 
ATOM   4712 C  C      . GLN B 1 105 ? -26.02200 -20.30300 -1.97900  1.000 25.71887 ? 101 GLN B C      1 
ATOM   4713 O  O      . GLN B 1 105 ? -25.61000 -21.41600 -2.32100  1.000 26.42159 ? 101 GLN B O      1 
ATOM   4714 C  CB     . GLN B 1 105 ? -24.52400 -18.33000 -2.43900  1.000 29.12718 ? 101 GLN B CB     1 
ATOM   4715 C  CG     . GLN B 1 105 ? -25.58700 -17.51500 -3.14300  1.000 31.37745 ? 101 GLN B CG     1 
ATOM   4716 C  CD     . GLN B 1 105 ? -26.31100 -16.58100 -2.19900  1.000 36.18329 ? 101 GLN B CD     1 
ATOM   4717 O  OE1    . GLN B 1 105 ? -27.41500 -16.88100 -1.73800  1.000 33.45138 ? 101 GLN B OE1    1 
ATOM   4718 N  NE2    . GLN B 1 105 ? -25.68300 -15.44600 -1.88900  1.000 29.70093 ? 101 GLN B NE2    1 
ATOM   4719 N  N      . VAL B 1 106 ? -27.30000 -19.93100 -2.08700  1.000 24.24238 ? 102 VAL B N      1 
ATOM   4720 C  CA     . VAL B 1 106 ? -28.27700 -20.82900 -2.69800  1.000 25.62939 ? 102 VAL B CA     1 
ATOM   4721 C  C      . VAL B 1 106 ? -27.91100 -21.01200 -4.16700  1.000 25.90311 ? 102 VAL B C      1 
ATOM   4722 O  O      . VAL B 1 106 ? -27.06200 -20.28900 -4.70300  1.000 27.17694 ? 102 VAL B O      1 
ATOM   4723 C  CB     . VAL B 1 106 ? -29.73200 -20.32300 -2.54300  1.000 25.82415 ? 102 VAL B CB     1 
ATOM   4724 C  CG1    . VAL B 1 106 ? -30.09000 -20.15900 -1.06400  1.000 25.23987 ? 102 VAL B CG1    1 
ATOM   4725 C  CG2    . VAL B 1 106 ? -29.93900 -19.00500 -3.28800  1.000 26.17945 ? 102 VAL B CG2    1 
ATOM   4726 N  N      . GLY B 1 107 ? -28.54400 -21.98400 -4.82000  1.000 30.54840 ? 103 GLY B N      1 
ATOM   4727 C  CA     . GLY B 1 107 ? -28.31200 -22.19000 -6.23600  1.000 35.28581 ? 103 GLY B CA     1 
ATOM   4728 C  C      . GLY B 1 107 ? -28.83700 -21.04000 -7.07400  1.000 34.01724 ? 103 GLY B C      1 
ATOM   4729 O  O      . GLY B 1 107 ? -29.86800 -20.43200 -6.77500  1.000 33.67509 ? 103 GLY B O      1 
ATOM   4730 N  N      . THR B 1 108 ? -28.11200 -20.74800 -8.15400  1.000 30.67999 ? 104 THR B N      1 
ATOM   4731 C  CA     . THR B 1 108 ? -28.45400 -19.60400 -8.99300  1.000 32.34598 ? 104 THR B CA     1 
ATOM   4732 C  C      . THR B 1 108 ? -29.88900 -19.68000 -9.48800  1.000 34.88313 ? 104 THR B C      1 
ATOM   4733 O  O      . THR B 1 108 ? -30.56200 -18.64800 -9.61300  1.000 45.52388 ? 104 THR B O      1 
ATOM   4734 C  CB     . THR B 1 108 ? -27.48400 -19.49800 -10.17500 1.000 39.56001 ? 104 THR B CB     1 
ATOM   4735 O  OG1    . THR B 1 108 ? -27.45800 -20.73100 -10.90600 1.000 46.61348 ? 104 THR B OG1    1 
ATOM   4736 C  CG2    . THR B 1 108 ? -26.08600 -19.19600 -9.66200  1.000 37.32026 ? 104 THR B CG2    1 
ATOM   4737 N  N      . ALA B 1 109 ? -30.38400 -20.88500 -9.77500  1.000 36.48332 ? 105 ALA B N      1 
ATOM   4738 C  CA     . ALA B 1 109 ? -31.74000 -21.00100 -10.30700 1.000 35.73323 ? 105 ALA B CA     1 
ATOM   4739 C  C      . ALA B 1 109 ? -32.80800 -20.54000 -9.32100  1.000 36.12275 ? 105 ALA B C      1 
ATOM   4740 O  O      . ALA B 1 109 ? -33.96200 -20.34100 -9.72500  1.000 34.98841 ? 105 ALA B O      1 
ATOM   4741 C  CB     . ALA B 1 109 ? -32.01700 -22.44800 -10.72200 1.000 33.76721 ? 105 ALA B CB     1 
ATOM   4742 N  N      . ALA B 1 110 ? -32.46200 -20.33800 -8.05600  1.000 32.82762 ? 106 ALA B N      1 
ATOM   4743 C  CA     . ALA B 1 110 ? -33.44100 -19.92600 -7.06100  1.000 35.70428 ? 106 ALA B CA     1 
ATOM   4744 C  C      . ALA B 1 110 ? -33.35400 -18.44900 -6.72000  1.000 29.06664 ? 106 ALA B C      1 
ATOM   4745 O  O      . ALA B 1 110 ? -34.13800 -17.97900 -5.88700  1.000 28.68502 ? 106 ALA B O      1 
ATOM   4746 C  CB     . ALA B 1 110 ? -33.28400 -20.75500 -5.78200  1.000 33.86722 ? 106 ALA B CB     1 
ATOM   4747 N  N      . PHE B 1 111 ? -32.43000 -17.71300 -7.34100  1.000 28.15338 ? 107 PHE B N      1 
ATOM   4748 C  CA     . PHE B 1 111 ? -32.26200 -16.29700 -7.04000  1.000 33.08291 ? 107 PHE B CA     1 
ATOM   4749 C  C      . PHE B 1 111 ? -33.57100 -15.54300 -7.25400  1.000 30.62736 ? 107 PHE B C      1 
ATOM   4750 O  O      . PHE B 1 111 ? -34.20700 -15.66300 -8.30700  1.000 32.20386 ? 107 PHE B O      1 
ATOM   4751 C  CB     . PHE B 1 111 ? -31.16500 -15.68600 -7.92600  1.000 30.73790 ? 107 PHE B CB     1 
ATOM   4752 C  CG     . PHE B 1 111 ? -29.74600 -15.99800 -7.48300  1.000 33.19345 ? 107 PHE B CG     1 
ATOM   4753 C  CD1    . PHE B 1 111 ? -29.47400 -17.03000 -6.59600  1.000 32.68287 ? 107 PHE B CD1    1 
ATOM   4754 C  CD2    . PHE B 1 111 ? -28.67700 -15.25700 -7.97800  1.000 40.69962 ? 107 PHE B CD2    1 
ATOM   4755 C  CE1    . PHE B 1 111 ? -28.16900 -17.31600 -6.20400  1.000 32.69603 ? 107 PHE B CE1    1 
ATOM   4756 C  CE2    . PHE B 1 111 ? -27.36700 -15.53600 -7.58900  1.000 41.32074 ? 107 PHE B CE2    1 
ATOM   4757 C  CZ     . PHE B 1 111 ? -27.11500 -16.57000 -6.70000  1.000 33.75142 ? 107 PHE B CZ     1 
ATOM   4758 N  N      . GLY B 1 112 ? -33.96400 -14.75000 -6.25900  1.000 27.16115 ? 108 GLY B N      1 
ATOM   4759 C  CA     . GLY B 1 112 ? -35.11700 -13.89400 -6.41100  1.000 28.38235 ? 108 GLY B CA     1 
ATOM   4760 C  C      . GLY B 1 112 ? -36.45300 -14.59300 -6.30500  1.000 29.51933 ? 108 GLY B C      1 
ATOM   4761 O  O      . GLY B 1 112 ? -37.48400 -13.94900 -6.52500  1.000 28.19549 ? 108 GLY B O      1 
ATOM   4762 N  N      . LYS B 1 113 ? -36.47000 -15.88800 -5.99000  1.000 26.07418 ? 109 LYS B N      1 
ATOM   4763 C  CA     . LYS B 1 113 ? -37.70400 -16.64300 -5.81600  1.000 23.39228 ? 109 LYS B CA     1 
ATOM   4764 C  C      . LYS B 1 113 ? -38.07100 -16.87000 -4.35200  1.000 27.18747 ? 109 LYS B C      1 
ATOM   4765 O  O      . LYS B 1 113 ? -39.14900 -17.41900 -4.07500  1.000 30.46944 ? 109 LYS B O      1 
ATOM   4766 C  CB     . LYS B 1 113 ? -37.59900 -18.00400 -6.52500  1.000 29.54565 ? 109 LYS B CB     1 
ATOM   4767 C  CG     . LYS B 1 113 ? -37.19600 -17.93400 -7.99800  1.000 29.50354 ? 109 LYS B CG     1 
ATOM   4768 C  CD     . LYS B 1 113 ? -37.35100 -19.28800 -8.68200  1.000 32.44863 ? 109 LYS B CD     1 
ATOM   4769 C  CE     . LYS B 1 113 ? -38.82500 -19.71500 -8.81000  1.000 33.05396 ? 109 LYS B CE     1 
ATOM   4770 N  NZ     . LYS B 1 113 ? -39.62800 -18.67400 -9.50900  1.000 41.27863 ? 109 LYS B NZ     1 
ATOM   4771 N  N      . GLY B 1 114 ? -37.22800 -16.45700 -3.41200  1.000 25.72414 ? 110 GLY B N      1 
ATOM   4772 C  CA     . GLY B 1 114 ? -37.50900 -16.72600 -2.01100  1.000 22.26320 ? 110 GLY B CA     1 
ATOM   4773 C  C      . GLY B 1 114 ? -36.91400 -18.06000 -1.59600  1.000 29.10612 ? 110 GLY B C      1 
ATOM   4774 O  O      . GLY B 1 114 ? -37.58300 -18.91900 -1.00500  1.000 24.28975 ? 110 GLY B O      1 
ATOM   4775 N  N      . ALA B 1 115 ? -35.64000 -18.24300 -1.92000  1.000 24.77929 ? 111 ALA B N      1 
ATOM   4776 C  CA     . ALA B 1 115 ? -34.96800 -19.48600 -1.58200  1.000 27.96914 ? 111 ALA B CA     1 
ATOM   4777 C  C      . ALA B 1 115 ? -34.77200 -19.57900 -0.06900  1.000 25.55833 ? 111 ALA B C      1 
ATOM   4778 O  O      . ALA B 1 115 ? -34.79000 -18.57800 0.65900   1.000 23.12646 ? 111 ALA B O      1 
ATOM   4779 C  CB     . ALA B 1 115 ? -33.62700 -19.58200 -2.31800  1.000 22.66851 ? 111 ALA B CB     1 
ATOM   4780 N  N      . LEU B 1 116 ? -34.62300 -20.80300 0.41300   1.000 24.22659 ? 112 LEU B N      1 
ATOM   4781 C  CA     . LEU B 1 116 ? -34.31500 -20.99800 1.82200   1.000 27.70332 ? 112 LEU B CA     1 
ATOM   4782 C  C      . LEU B 1 116 ? -33.05100 -20.22400 2.19400   1.000 27.01377 ? 112 LEU B C      1 
ATOM   4783 O  O      . LEU B 1 116 ? -31.99200 -20.40900 1.58300   1.000 28.11916 ? 112 LEU B O      1 
ATOM   4784 C  CB     . LEU B 1 116 ? -34.15700 -22.49200 2.11000   1.000 34.91208 ? 112 LEU B CB     1 
ATOM   4785 C  CG     . LEU B 1 116 ? -33.78800 -22.88300 3.54400   1.000 43.80525 ? 112 LEU B CG     1 
ATOM   4786 C  CD1    . LEU B 1 116 ? -34.77800 -22.29200 4.57300   1.000 38.75728 ? 112 LEU B CD1    1 
ATOM   4787 C  CD2    . LEU B 1 116 ? -33.70400 -24.40200 3.65700   1.000 45.72127 ? 112 LEU B CD2    1 
ATOM   4788 N  N      . GLN B 1 117 ? -33.17500 -19.32100 3.17100   1.000 24.18448 ? 113 GLN B N      1 
ATOM   4789 C  CA     . GLN B 1 117 ? -32.03800 -18.53100 3.63200   1.000 27.05324 ? 113 GLN B CA     1 
ATOM   4790 C  C      . GLN B 1 117 ? -31.36300 -17.81500 2.46400   1.000 31.40640 ? 113 GLN B C      1 
ATOM   4791 O  O      . GLN B 1 117 ? -30.13600 -17.70800 2.39900   1.000 25.33198 ? 113 GLN B O      1 
ATOM   4792 C  CB     . GLN B 1 117 ? -31.03400 -19.42300 4.37400   1.000 26.45054 ? 113 GLN B CB     1 
ATOM   4793 C  CG     . GLN B 1 117 ? -31.62200 -20.07600 5.62800   1.000 28.09284 ? 113 GLN B CG     1 
ATOM   4794 C  CD     . GLN B 1 117 ? -30.63000 -20.97000 6.35300   1.000 29.60618 ? 113 GLN B CD     1 
ATOM   4795 O  OE1    . GLN B 1 117 ? -29.68600 -21.49600 5.75200   1.000 32.64339 ? 113 GLN B OE1    1 
ATOM   4796 N  NE2    . GLN B 1 117 ? -30.83400 -21.14300 7.64900   1.000 20.58931 ? 113 GLN B NE2    1 
ATOM   4797 N  N      . GLU B 1 118 ? -32.17500 -17.33400 1.52000   1.000 24.24764 ? 114 GLU B N      1 
ATOM   4798 C  CA     . GLU B 1 118 ? -31.63600 -16.67400 0.34000   1.000 29.25877 ? 114 GLU B CA     1 
ATOM   4799 C  C      . GLU B 1 118 ? -30.68800 -15.55100 0.75300   1.000 24.25817 ? 114 GLU B C      1 
ATOM   4800 O  O      . GLU B 1 118 ? -31.04100 -14.67700 1.55300   1.000 26.36106 ? 114 GLU B O      1 
ATOM   4801 C  CB     . GLU B 1 118 ? -32.76800 -16.14000 -0.55300  1.000 26.59529 ? 114 GLU B CB     1 
ATOM   4802 C  CG     . GLU B 1 118 ? -32.21700 -15.58100 -1.85300  1.000 28.52184 ? 114 GLU B CG     1 
ATOM   4803 C  CD     . GLU B 1 118 ? -33.25100 -15.36500 -2.95600  1.000 29.11139 ? 114 GLU B CD     1 
ATOM   4804 O  OE1    . GLU B 1 118 ? -32.90700 -14.61900 -3.90000  1.000 30.24047 ? 114 GLU B OE1    1 
ATOM   4805 O  OE2    . GLU B 1 118 ? -34.37600 -15.91900 -2.89300  1.000 29.97991 ? 114 GLU B OE2    1 
ATOM   4806 N  N      . SER B 1 119 ? -29.47400 -15.57400 0.20100   1.000 23.58177 ? 115 SER B N      1 
ATOM   4807 C  CA     . SER B 1 119 ? -28.40100 -14.71200 0.69100   1.000 26.81901 ? 115 SER B CA     1 
ATOM   4808 C  C      . SER B 1 119 ? -27.94500 -13.73100 -0.37400  1.000 31.18532 ? 115 SER B C      1 
ATOM   4809 O  O      . SER B 1 119 ? -26.78500 -13.30400 -0.38000  1.000 25.22934 ? 115 SER B O      1 
ATOM   4810 C  CB     . SER B 1 119 ? -27.22200 -15.55400 1.16200   1.000 26.05049 ? 115 SER B CB     1 
ATOM   4811 O  OG     . SER B 1 119 ? -27.58000 -16.38900 2.24900   1.000 26.60845 ? 115 SER B OG     1 
ATOM   4812 N  N      . THR B 1 120 ? -28.86900 -13.33800 -1.24300  1.000 26.51107 ? 116 THR B N      1 
ATOM   4813 C  CA     . THR B 1 120 ? -28.64600 -12.41400 -2.33800  1.000 25.36357 ? 116 THR B CA     1 
ATOM   4814 C  C      . THR B 1 120 ? -29.18000 -11.03300 -1.96400  1.000 27.32433 ? 116 THR B C      1 
ATOM   4815 O  O      . THR B 1 120 ? -29.71200 -10.80700 -0.87300  1.000 29.21403 ? 116 THR B O      1 
ATOM   4816 C  CB     . THR B 1 120 ? -29.35900 -12.91200 -3.60000  1.000 28.38235 ? 116 THR B CB     1 
ATOM   4817 O  OG1    . THR B 1 120 ? -30.77300 -12.86600 -3.37100  1.000 24.25817 ? 116 THR B OG1    1 
ATOM   4818 C  CG2    . THR B 1 120 ? -28.96300 -14.35100 -3.93000  1.000 31.41166 ? 116 THR B CG2    1 
ATOM   4819 N  N      . VAL B 1 121 ? -29.08600 -10.11200 -2.92200  1.000 21.99737 ? 117 VAL B N      1 
ATOM   4820 C  CA     . VAL B 1 121 ? -29.72100 -8.81100  -2.78300  1.000 22.07107 ? 117 VAL B CA     1 
ATOM   4821 C  C      . VAL B 1 121 ? -31.21900 -8.95300  -2.54300  1.000 27.71385 ? 117 VAL B C      1 
ATOM   4822 O  O      . VAL B 1 121 ? -31.84200 -8.06600  -1.94600  1.000 27.60331 ? 117 VAL B O      1 
ATOM   4823 C  CB     . VAL B 1 121 ? -29.44100 -7.94700  -4.02900  1.000 38.18353 ? 117 VAL B CB     1 
ATOM   4824 C  CG1    . VAL B 1 121 ? -30.22100 -8.48500  -5.22300  1.000 36.52806 ? 117 VAL B CG1    1 
ATOM   4825 C  CG2    . VAL B 1 121 ? -29.79600 -6.47100  -3.74800  1.000 40.57329 ? 117 VAL B CG2    1 
ATOM   4826 N  N      . HIS B 1 122 ? -31.83300 -10.04500 -3.01800  1.000 26.66109 ? 118 HIS B N      1 
ATOM   4827 C  CA     . HIS B 1 122 ? -33.27000 -10.23800 -2.81200  1.000 26.38211 ? 118 HIS B CA     1 
ATOM   4828 C  C      . HIS B 1 122 ? -33.60900 -10.82000 -1.45100  1.000 30.91423 ? 118 HIS B C      1 
ATOM   4829 O  O      . HIS B 1 122 ? -34.78600 -10.84500 -1.09300  1.000 27.62963 ? 118 HIS B O      1 
ATOM   4830 C  CB     . HIS B 1 122 ? -33.85800 -11.16900 -3.87500  1.000 29.34299 ? 118 HIS B CB     1 
ATOM   4831 C  CG     . HIS B 1 122 ? -33.36600 -10.88300 -5.25600  1.000 29.98781 ? 118 HIS B CG     1 
ATOM   4832 N  ND1    . HIS B 1 122 ? -33.83300 -9.82200  -6.00300  1.000 32.69866 ? 118 HIS B ND1    1 
ATOM   4833 C  CD2    . HIS B 1 122 ? -32.43000 -11.50200 -6.01500  1.000 27.61384 ? 118 HIS B CD2    1 
ATOM   4834 C  CE1    . HIS B 1 122 ? -33.20600 -9.80300  -7.16800  1.000 34.16725 ? 118 HIS B CE1    1 
ATOM   4835 N  NE2    . HIS B 1 122 ? -32.35300 -10.81300 -7.20300  1.000 30.33785 ? 118 HIS B NE2    1 
ATOM   4836 N  N      . GLY B 1 123 ? -32.62600 -11.32100 -0.71000  1.000 28.10600 ? 119 GLY B N      1 
ATOM   4837 C  CA     . GLY B 1 123 ? -32.87500 -11.85600 0.61000   1.000 26.65583 ? 119 GLY B CA     1 
ATOM   4838 C  C      . GLY B 1 123 ? -32.03600 -11.11900 1.62800   1.000 28.84556 ? 119 GLY B C      1 
ATOM   4839 O  O      . GLY B 1 123 ? -32.18000 -9.90100  1.79700   1.000 28.34287 ? 119 GLY B O      1 
ATOM   4840 N  N      . VAL B 1 124 ? -31.15300 -11.85200 2.30500   1.000 28.50605 ? 120 VAL B N      1 
ATOM   4841 C  CA     . VAL B 1 124 ? -30.21200 -11.30300 3.27200   1.000 25.05037 ? 120 VAL B CA     1 
ATOM   4842 C  C      . VAL B 1 124 ? -28.87000 -11.17500 2.54900   1.000 25.55043 ? 120 VAL B C      1 
ATOM   4843 O  O      . VAL B 1 124 ? -28.16000 -12.16600 2.35100   1.000 24.26080 ? 120 VAL B O      1 
ATOM   4844 C  CB     . VAL B 1 124 ? -30.12300 -12.19000 4.51900   1.000 28.07179 ? 120 VAL B CB     1 
ATOM   4845 C  CG1    . VAL B 1 124 ? -28.91700 -11.81400 5.38200   1.000 31.20901 ? 120 VAL B CG1    1 
ATOM   4846 C  CG2    . VAL B 1 124 ? -31.41800 -12.08500 5.33700   1.000 27.19537 ? 120 VAL B CG2    1 
ATOM   4847 N  N      . ASP B 1 125 ? -28.51000 -9.95100  2.15500   1.000 20.81565 ? 121 ASP B N      1 
ATOM   4848 C  CA     . ASP B 1 125 ? -27.41800 -9.72800  1.19700   1.000 21.33414 ? 121 ASP B CA     1 
ATOM   4849 C  C      . ASP B 1 125 ? -26.06100 -9.81200  1.90500   1.000 20.50509 ? 121 ASP B C      1 
ATOM   4850 O  O      . ASP B 1 125 ? -25.48400 -8.80400  2.31900   1.000 24.24238 ? 121 ASP B O      1 
ATOM   4851 C  CB     . ASP B 1 125 ? -27.60900 -8.38200  0.51000   1.000 19.67078 ? 121 ASP B CB     1 
ATOM   4852 C  CG     . ASP B 1 125 ? -26.58800 -8.11100  -0.59600  1.000 28.32445 ? 121 ASP B CG     1 
ATOM   4853 O  OD1    . ASP B 1 125 ? -25.58300 -8.85900  -0.77400  1.000 26.61372 ? 121 ASP B OD1    1 
ATOM   4854 O  OD2    . ASP B 1 125 ? -26.80100 -7.09200  -1.28300  1.000 29.85621 ? 121 ASP B OD2    1 
ATOM   4855 N  N      . LEU B 1 126 ? -25.53400 -11.04000 2.00100   1.000 19.09176 ? 122 LEU B N      1 
ATOM   4856 C  CA     . LEU B 1 126 ? -24.29200 -11.27800 2.73400   1.000 22.30267 ? 122 LEU B CA     1 
ATOM   4857 C  C      . LEU B 1 126 ? -23.14500 -10.47900 2.14800   1.000 23.44492 ? 122 LEU B C      1 
ATOM   4858 O  O      . LEU B 1 126 ? -22.31600 -9.94200  2.88400   1.000 23.92392 ? 122 LEU B O      1 
ATOM   4859 C  CB     . LEU B 1 126 ? -23.92100 -12.76400 2.70100   1.000 25.07669 ? 122 LEU B CB     1 
ATOM   4860 C  CG     . LEU B 1 126 ? -24.84000 -13.75500 3.38900   1.000 21.75524 ? 122 LEU B CG     1 
ATOM   4861 C  CD1    . LEU B 1 126 ? -24.22100 -15.16900 3.33700   1.000 18.34430 ? 122 LEU B CD1    1 
ATOM   4862 C  CD2    . LEU B 1 126 ? -25.05600 -13.28200 4.79700   1.000 22.40532 ? 122 LEU B CD2    1 
ATOM   4863 N  N      . VAL B 1 127 ? -23.05500 -10.42200 0.81900   1.000 20.38139 ? 123 VAL B N      1 
ATOM   4864 C  CA     . VAL B 1 127 ? -21.92600 -9.72300  0.21800   1.000 22.31320 ? 123 VAL B CA     1 
ATOM   4865 C  C      . VAL B 1 127 ? -21.92700 -8.26400  0.65600   1.000 24.38187 ? 123 VAL B C      1 
ATOM   4866 O  O      . VAL B 1 127 ? -20.88000 -7.70300  0.99900   1.000 26.05312 ? 123 VAL B O      1 
ATOM   4867 C  CB     . VAL B 1 127 ? -21.93700 -9.85400  -1.32300  1.000 21.22886 ? 123 VAL B CB     1 
ATOM   4868 C  CG1    . VAL B 1 127 ? -20.96700 -8.83100  -1.92600  1.000 20.62879 ? 123 VAL B CG1    1 
ATOM   4869 C  CG2    . VAL B 1 127 ? -21.53100 -11.25800 -1.74100  1.000 25.93995 ? 123 VAL B CG2    1 
ATOM   4870 N  N      . SER B 1 128 ? -23.10300 -7.63400  0.67800   1.000 18.14691 ? 124 SER B N      1 
ATOM   4871 C  CA     . SER B 1 128 ? -23.16800 -6.23200  1.08100   1.000 22.83168 ? 124 SER B CA     1 
ATOM   4872 C  C      . SER B 1 128 ? -23.01200 -6.07100  2.58900   1.000 23.05013 ? 124 SER B C      1 
ATOM   4873 O  O      . SER B 1 128 ? -22.43500 -5.08100  3.05200   1.000 22.86064 ? 124 SER B O      1 
ATOM   4874 C  CB     . SER B 1 128 ? -24.49400 -5.61800  0.64500   1.000 23.80285 ? 124 SER B CB     1 
ATOM   4875 O  OG     . SER B 1 128 ? -24.60400 -5.60100  -0.77000  1.000 33.24609 ? 124 SER B OG     1 
ATOM   4876 N  N      . ILE B 1 129 ? -23.50200 -7.03400  3.37400   1.000 18.85752 ? 125 ILE B N      1 
ATOM   4877 C  CA     . ILE B 1 129 ? -23.37200 -6.93500  4.82500   1.000 17.13100 ? 125 ILE B CA     1 
ATOM   4878 C  C      . ILE B 1 129 ? -21.90500 -6.97200  5.23100   1.000 21.43941 ? 125 ILE B C      1 
ATOM   4879 O  O      . ILE B 1 129 ? -21.46400 -6.19700  6.08700   1.000 22.68693 ? 125 ILE B O      1 
ATOM   4880 C  CB     . ILE B 1 129 ? -24.17800 -8.05900  5.51000   1.000 23.68705 ? 125 ILE B CB     1 
ATOM   4881 C  CG1    . ILE B 1 129 ? -25.68900 -7.80100  5.35900   1.000 25.25829 ? 125 ILE B CG1    1 
ATOM   4882 C  CG2    . ILE B 1 129 ? -23.78000 -8.16800  6.99700   1.000 22.37637 ? 125 ILE B CG2    1 
ATOM   4883 C  CD1    . ILE B 1 129 ? -26.58200 -8.97900  5.82200   1.000 19.37074 ? 125 ILE B CD1    1 
ATOM   4884 N  N      . PHE B 1 130 ? -21.11400 -7.85400  4.60500   1.000 21.21307 ? 126 PHE B N      1 
ATOM   4885 C  CA     . PHE B 1 130 ? -19.71600 -8.00400  5.00600   1.000 19.88396 ? 126 PHE B CA     1 
ATOM   4886 C  C      . PHE B 1 130 ? -18.80600 -6.99300  4.34500   1.000 24.74770 ? 126 PHE B C      1 
ATOM   4887 O  O      . PHE B 1 130 ? -17.65800 -6.84500  4.78000   1.000 24.47399 ? 126 PHE B O      1 
ATOM   4888 C  CB     . PHE B 1 130 ? -19.21100 -9.41900  4.68900   1.000 16.59146 ? 126 PHE B CB     1 
ATOM   4889 C  CG     . PHE B 1 130 ? -19.54500 -10.42600 5.75700   1.000 27.74280 ? 126 PHE B CG     1 
ATOM   4890 C  CD1    . PHE B 1 130 ? -20.76600 -11.08400 5.74500   1.000 24.09499 ? 126 PHE B CD1    1 
ATOM   4891 C  CD2    . PHE B 1 130 ? -18.64900 -10.68700 6.79800   1.000 24.35029 ? 126 PHE B CD2    1 
ATOM   4892 C  CE1    . PHE B 1 130 ? -21.08800 -12.00100 6.73700   1.000 23.11856 ? 126 PHE B CE1    1 
ATOM   4893 C  CE2    . PHE B 1 130 ? -18.96500 -11.60700 7.78500   1.000 22.33162 ? 126 PHE B CE2    1 
ATOM   4894 C  CZ     . PHE B 1 130 ? -20.19000 -12.25700 7.75700   1.000 26.48212 ? 126 PHE B CZ     1 
ATOM   4895 N  N      . SER B 1 131 ? -19.28200 -6.30900  3.30900   1.000 21.62365 ? 127 SER B N      1 
ATOM   4896 C  CA     . SER B 1 131 ? -18.44600 -5.35500  2.58800   1.000 21.67365 ? 127 SER B CA     1 
ATOM   4897 C  C      . SER B 1 131 ? -17.76500 -4.33000  3.49300   1.000 21.44204 ? 127 SER B C      1 
ATOM   4898 O  O      . SER B 1 131 ? -16.58500 -4.03900  3.26100   1.000 23.30016 ? 127 SER B O      1 
ATOM   4899 C  CB     . SER B 1 131 ? -19.27000 -4.67200  1.49100   1.000 28.78240 ? 127 SER B CB     1 
ATOM   4900 O  OG     . SER B 1 131 ? -18.56100 -3.55700  0.99500   1.000 47.25303 ? 127 SER B OG     1 
ATOM   4901 N  N      . PRO B 1 132 ? -18.42300 -3.72900  4.49200   1.000 25.15565 ? 128 PRO B N      1 
ATOM   4902 C  CA     . PRO B 1 132 ? -17.73500 -2.70200  5.30100   1.000 25.76362 ? 128 PRO B CA     1 
ATOM   4903 C  C      . PRO B 1 132 ? -16.63800 -3.24000  6.19700   1.000 26.22420 ? 128 PRO B C      1 
ATOM   4904 O  O      . PRO B 1 132 ? -15.78400 -2.45300  6.62000   1.000 23.57914 ? 128 PRO B O      1 
ATOM   4905 C  CB     . PRO B 1 132 ? -18.87300 -2.07900  6.13100   1.000 23.42912 ? 128 PRO B CB     1 
ATOM   4906 C  CG     . PRO B 1 132 ? -20.11500 -2.43100  5.36900   1.000 25.11880 ? 128 PRO B CG     1 
ATOM   4907 C  CD     . PRO B 1 132 ? -19.85700 -3.79600  4.80200   1.000 26.12945 ? 128 PRO B CD     1 
ATOM   4908 N  N      . ILE B 1 133 ? -16.63500 -4.52800  6.53900   1.000 26.03733 ? 129 ILE B N      1 
ATOM   4909 C  CA     . ILE B 1 133 ? -15.61100 -5.01400  7.46300   1.000 25.13196 ? 129 ILE B CA     1 
ATOM   4910 C  C      . ILE B 1 133 ? -14.75300 -6.10500  6.83200   1.000 25.12406 ? 129 ILE B C      1 
ATOM   4911 O  O      . ILE B 1 133 ? -14.15500 -6.92400  7.53300   1.000 23.89234 ? 129 ILE B O      1 
ATOM   4912 C  CB     . ILE B 1 133 ? -16.25300 -5.50000  8.77500   1.000 25.67939 ? 129 ILE B CB     1 
ATOM   4913 C  CG1    . ILE B 1 133 ? -17.53700 -6.27800  8.50600   1.000 20.36560 ? 129 ILE B CG1    1 
ATOM   4914 C  CG2    . ILE B 1 133 ? -16.59100 -4.30500  9.66100   1.000 26.39264 ? 129 ILE B CG2    1 
ATOM   4915 C  CD1    . ILE B 1 133 ? -17.33700 -7.68800  8.13900   1.000 25.27408 ? 129 ILE B CD1    1 
ATOM   4916 N  N      . THR B 1 134 ? -14.62800 -6.09100  5.51200   1.000 24.88456 ? 130 THR B N      1 
ATOM   4917 C  CA     . THR B 1 134 ? -13.66700 -6.94600  4.83700   1.000 24.05025 ? 130 THR B CA     1 
ATOM   4918 C  C      . THR B 1 134 ? -12.88000 -6.10300  3.85800   1.000 21.99211 ? 130 THR B C      1 
ATOM   4919 O  O      . THR B 1 134 ? -13.33100 -5.03900  3.43500   1.000 22.92906 ? 130 THR B O      1 
ATOM   4920 C  CB     . THR B 1 134 ? -14.31300 -8.11000  4.07100   1.000 25.91100 ? 130 THR B CB     1 
ATOM   4921 O  OG1    . THR B 1 134 ? -15.31500 -7.61100  3.17900   1.000 23.00802 ? 130 THR B OG1    1 
ATOM   4922 C  CG2    . THR B 1 134 ? -14.89500 -9.14400  5.03700   1.000 21.16043 ? 130 THR B CG2    1 
ATOM   4923 N  N      . LYS B 1 135 ? -11.68400 -6.58700  3.51500   1.000 22.42111 ? 131 LYS B N      1 
ATOM   4924 C  CA     . LYS B 1 135 ? -10.95700 -5.97400  2.41100   1.000 17.48894 ? 131 LYS B CA     1 
ATOM   4925 C  C      . LYS B 1 135 ? -11.58900 -6.34000  1.07900   1.000 27.29538 ? 131 LYS B C      1 
ATOM   4926 O  O      . LYS B 1 135 ? -11.47000 -5.58400  0.10900   1.000 27.12957 ? 131 LYS B O      1 
ATOM   4927 C  CB     . LYS B 1 135 ? -9.47800  -6.39500  2.42100   1.000 17.87320 ? 131 LYS B CB     1 
ATOM   4928 C  CG     . LYS B 1 135 ? -8.71200  -6.06700  3.70900   1.000 22.40795 ? 131 LYS B CG     1 
ATOM   4929 C  CD     . LYS B 1 135 ? -7.23300  -6.47200  3.58100   1.000 24.87930 ? 131 LYS B CD     1 
ATOM   4930 C  CE     . LYS B 1 135 ? -6.47100  -5.50700  2.65600   1.000 22.70009 ? 131 LYS B CE     1 
ATOM   4931 N  NZ     . LYS B 1 135 ? -5.00500  -5.85000  2.60800   1.000 26.80321 ? 131 LYS B NZ     1 
ATOM   4932 N  N      . LEU B 1 136 ? -12.26800 -7.48400  1.01300   1.000 26.75847 ? 132 LEU B N      1 
ATOM   4933 C  CA     . LEU B 1 136 ? -12.92000 -7.92400  -0.21500  1.000 24.91088 ? 132 LEU B CA     1 
ATOM   4934 C  C      . LEU B 1 136 ? -14.11200 -8.78800  0.16000   1.000 25.08722 ? 132 LEU B C      1 
ATOM   4935 O  O      . LEU B 1 136 ? -13.97900 -9.69500  0.98500   1.000 22.89222 ? 132 LEU B O      1 
ATOM   4936 C  CB     . LEU B 1 136 ? -11.94300 -8.72100  -1.10300  1.000 21.39467 ? 132 LEU B CB     1 
ATOM   4937 C  CG     . LEU B 1 136 ? -12.57500 -9.40900  -2.31600  1.000 27.80070 ? 132 LEU B CG     1 
ATOM   4938 C  CD1    . LEU B 1 136 ? -13.04700 -8.37000  -3.34900  1.000 31.08004 ? 132 LEU B CD1    1 
ATOM   4939 C  CD2    . LEU B 1 136 ? -11.62300 -10.39700 -2.95500  1.000 29.66145 ? 132 LEU B CD2    1 
ATOM   4940 N  N      . SER B 1 137 ? -15.25900 -8.51200  -0.45100  1.000 22.79484 ? 133 SER B N      1 
ATOM   4941 C  CA     . SER B 1 137 ? -16.47300 -9.30000  -0.25100  1.000 24.77665 ? 133 SER B CA     1 
ATOM   4942 C  C      . SER B 1 137 ? -17.12300 -9.49900  -1.60600  1.000 25.92416 ? 133 SER B C      1 
ATOM   4943 O  O      . SER B 1 137 ? -17.55500 -8.52500  -2.23400  1.000 23.25016 ? 133 SER B O      1 
ATOM   4944 C  CB     . SER B 1 137 ? -17.45100 -8.60800  0.69900   1.000 21.88683 ? 133 SER B CB     1 
ATOM   4945 O  OG     . SER B 1 137 ? -18.62300 -9.38800  0.82700   1.000 23.42912 ? 133 SER B OG     1 
ATOM   4946 N  N      . VAL B 1 138 ? -17.21500 -10.75000 -2.05200  1.000 27.55857 ? 134 VAL B N      1 
ATOM   4947 C  CA     . VAL B 1 138 ? -17.61100 -11.01300 -3.42900  1.000 26.85585 ? 134 VAL B CA     1 
ATOM   4948 C  C      . VAL B 1 138 ? -18.24100 -12.39400 -3.50900  1.000 24.61611 ? 134 VAL B C      1 
ATOM   4949 O  O      . VAL B 1 138 ? -17.91500 -13.28400 -2.72300  1.000 25.38725 ? 134 VAL B O      1 
ATOM   4950 C  CB     . VAL B 1 138 ? -16.38800 -10.86800 -4.37300  1.000 28.80345 ? 134 VAL B CB     1 
ATOM   4951 C  CG1    . VAL B 1 138 ? -15.29300 -11.86700 -4.00300  1.000 18.56012 ? 134 VAL B CG1    1 
ATOM   4952 C  CG2    . VAL B 1 138 ? -16.81100 -11.03000 -5.84100  1.000 32.39599 ? 134 VAL B CG2    1 
ATOM   4953 N  N      . MET B 1 139 ? -19.18600 -12.55400 -4.44200  1.000 27.36381 ? 135 MET B N      1 
ATOM   4954 C  CA     . MET B 1 139 ? -19.77800 -13.84900 -4.77200  1.000 29.64829 ? 135 MET B CA     1 
ATOM   4955 C  C      . MET B 1 139 ? -19.09600 -14.41200 -6.01700  1.000 30.68789 ? 135 MET B C      1 
ATOM   4956 O  O      . MET B 1 139 ? -18.95500 -13.70400 -7.01900  1.000 29.46406 ? 135 MET B O      1 
ATOM   4957 C  CB     . MET B 1 139 ? -21.28400 -13.73100 -5.02900  1.000 23.79233 ? 135 MET B CB     1 
ATOM   4958 C  CG     . MET B 1 139 ? -21.96500 -15.05900 -5.36800  1.000 25.68466 ? 135 MET B CG     1 
ATOM   4959 S  SD     . MET B 1 139 ? -23.77100 -14.91500 -5.42600  1.000 33.47770 ? 135 MET B SD     1 
ATOM   4960 C  CE     . MET B 1 139 ? -23.95000 -14.43600 -7.14000  1.000 33.36453 ? 135 MET B CE     1 
ATOM   4961 N  N      . ILE B 1 140 ? -18.66500 -15.67100 -5.95200  1.000 24.98984 ? 136 ILE B N      1 
ATOM   4962 C  CA     . ILE B 1 140 ? -18.02400 -16.31600 -7.10200  1.000 32.13017 ? 136 ILE B CA     1 
ATOM   4963 C  C      . ILE B 1 140 ? -19.06000 -16.40600 -8.21500  1.000 32.22228 ? 136 ILE B C      1 
ATOM   4964 O  O      . ILE B 1 140 ? -20.09800 -17.04600 -8.02200  1.000 38.48093 ? 136 ILE B O      1 
ATOM   4965 C  CB     . ILE B 1 140 ? -17.47000 -17.70600 -6.74500  1.000 38.07299 ? 136 ILE B CB     1 
ATOM   4966 C  CG1    . ILE B 1 140 ? -16.75500 -17.67300 -5.39900  1.000 39.88373 ? 136 ILE B CG1    1 
ATOM   4967 C  CG2    . ILE B 1 140 ? -16.48200 -18.18100 -7.79500  1.000 32.52758 ? 136 ILE B CG2    1 
ATOM   4968 C  CD1    . ILE B 1 140 ? -15.42500 -17.03100 -5.47500  1.000 40.36537 ? 136 ILE B CD1    1 
ATOM   4969 N  N      . PRO B 1 141 ? -18.84300 -15.78200 -9.37500  1.000 35.30423 ? 137 PRO B N      1 
ATOM   4970 C  CA     . PRO B 1 141 ? -19.90000 -15.73900 -10.39800 1.000 36.98075 ? 137 PRO B CA     1 
ATOM   4971 C  C      . PRO B 1 141 ? -20.04600 -17.03200 -11.18700 1.000 39.29155 ? 137 PRO B C      1 
ATOM   4972 O  O      . PRO B 1 141 ? -21.14800 -17.37000 -11.62400 1.000 40.86016 ? 137 PRO B O      1 
ATOM   4973 C  CB     . PRO B 1 141 ? -19.44700 -14.59400 -11.31100 1.000 34.95945 ? 137 PRO B CB     1 
ATOM   4974 C  CG     . PRO B 1 141 ? -17.97000 -14.62900 -11.21900 1.000 34.03040 ? 137 PRO B CG     1 
ATOM   4975 C  CD     . PRO B 1 141 ? -17.64900 -15.02800 -9.78700  1.000 34.94893 ? 137 PRO B CD     1 
ATOM   4976 N  N      . THR B 1 142 ? -18.94400 -17.74300 -11.41000 1.000 37.49134 ? 138 THR B N      1 
ATOM   4977 C  CA     . THR B 1 142 ? -18.96600 -18.98500 -12.16900 1.000 38.59147 ? 138 THR B CA     1 
ATOM   4978 C  C      . THR B 1 142 ? -17.88400 -19.90200 -11.62800 1.000 34.93577 ? 138 THR B C      1 
ATOM   4979 O  O      . THR B 1 142 ? -16.90800 -19.45000 -11.02200 1.000 34.84628 ? 138 THR B O      1 
ATOM   4980 C  CB     . THR B 1 142 ? -18.72300 -18.75500 -13.66400 1.000 41.26811 ? 138 THR B CB     1 
ATOM   4981 O  OG1    . THR B 1 142 ? -17.40600 -18.24200 -13.82700 1.000 37.90454 ? 138 THR B OG1    1 
ATOM   4982 C  CG2    . THR B 1 142 ? -19.71800 -17.76700 -14.24200 1.000 36.89653 ? 138 THR B CG2    1 
ATOM   4983 N  N      . ALA B 1 143 ? -18.05100 -21.20200 -11.87000 1.000 35.98063 ? 139 ALA B N      1 
ATOM   4984 C  CA     . ALA B 1 143 ? -17.03600 -22.15000 -11.42300 1.000 38.28354 ? 139 ALA B CA     1 
ATOM   4985 C  C      . ALA B 1 143 ? -15.68200 -21.82300 -12.03900 1.000 35.38319 ? 139 ALA B C      1 
ATOM   4986 O  O      . ALA B 1 143 ? -14.64700 -21.91600 -11.37100 1.000 38.82308 ? 139 ALA B O      1 
ATOM   4987 C  CB     . ALA B 1 143 ? -17.46300 -23.58100 -11.76500 1.000 36.22803 ? 139 ALA B CB     1 
ATOM   4988 N  N      . GLU B 1 144 ? -15.68100 -21.40400 -13.30800 1.000 30.52208 ? 140 GLU B N      1 
ATOM   4989 C  CA     . GLU B 1 144 ? -14.44300 -21.08800 -14.01500 1.000 37.76769 ? 140 GLU B CA     1 
ATOM   4990 C  C      . GLU B 1 144 ? -13.64200 -19.99700 -13.30900 1.000 34.98051 ? 140 GLU B C      1 
ATOM   4991 O  O      . GLU B 1 144 ? -12.41700 -19.94100 -13.45100 1.000 35.13579 ? 140 GLU B O      1 
ATOM   4992 C  CB     . GLU B 1 144 ? -14.77000 -20.66200 -15.45000 1.000 47.52412 ? 140 GLU B CB     1 
ATOM   4993 C  CG     . GLU B 1 144 ? -13.56100 -20.50800 -16.35900 1.000 65.65524 ? 140 GLU B CG     1 
ATOM   4994 C  CD     . GLU B 1 144 ? -13.05200 -19.07300 -16.43700 1.000 77.35664 ? 140 GLU B CD     1 
ATOM   4995 O  OE1    . GLU B 1 144 ? -13.88000 -18.15600 -16.62200 1.000 81.84402 ? 140 GLU B OE1    1 
ATOM   4996 O  OE2    . GLU B 1 144 ? -11.82200 -18.86300 -16.32700 1.000 82.53621 ? 140 GLU B OE2    1 
ATOM   4997 N  N      . LYS B 1 145 ? -14.30100 -19.12800 -12.54400 1.000 36.35173 ? 141 LYS B N      1 
ATOM   4998 C  CA     . LYS B 1 145 ? -13.59900 -18.04200 -11.86900 1.000 32.59865 ? 141 LYS B CA     1 
ATOM   4999 C  C      . LYS B 1 145 ? -13.17700 -18.39800 -10.44800 1.000 28.46657 ? 141 LYS B C      1 
ATOM   5000 O  O      . LYS B 1 145 ? -12.59600 -17.54900 -9.76200  1.000 29.06138 ? 141 LYS B O      1 
ATOM   5001 C  CB     . LYS B 1 145 ? -14.47300 -16.77500 -11.84200 1.000 35.52794 ? 141 LYS B CB     1 
ATOM   5002 C  CG     . LYS B 1 145 ? -14.65600 -16.09600 -13.20300 1.000 39.04942 ? 141 LYS B CG     1 
ATOM   5003 C  CD     . LYS B 1 145 ? -13.54400 -15.08100 -13.42900 1.000 41.63920 ? 141 LYS B CD     1 
ATOM   5004 C  CE     . LYS B 1 145 ? -13.37600 -14.70600 -14.88800 1.000 46.60559 ? 141 LYS B CE     1 
ATOM   5005 N  NZ     . LYS B 1 145 ? -12.26400 -15.44100 -15.56200 1.000 58.23593 ? 141 LYS B NZ     1 
ATOM   5006 N  N      . MET B 1 146 ? -13.42800 -19.63100 -9.99800  1.000 31.36165 ? 142 MET B N      1 
ATOM   5007 C  CA     . MET B 1 146 ? -13.09500 -20.01500 -8.62300  1.000 31.22480 ? 142 MET B CA     1 
ATOM   5008 C  C      . MET B 1 146 ? -11.60100 -19.83700 -8.33000  1.000 28.10074 ? 142 MET B C      1 
ATOM   5009 O  O      . MET B 1 146 ? -11.21600 -19.28000 -7.29500  1.000 31.16163 ? 142 MET B O      1 
ATOM   5010 C  CB     . MET B 1 146 ? -13.51200 -21.46600 -8.37500  1.000 27.30854 ? 142 MET B CB     1 
ATOM   5011 C  CG     . MET B 1 146 ? -13.13000 -21.98300 -6.99700  1.000 33.21451 ? 142 MET B CG     1 
ATOM   5012 S  SD     . MET B 1 146 ? -14.14000 -21.24500 -5.67100  1.000 39.25471 ? 142 MET B SD     1 
ATOM   5013 C  CE     . MET B 1 146 ? -15.63000 -22.22700 -5.79800  1.000 39.22049 ? 142 MET B CE     1 
ATOM   5014 N  N      . GLY B 1 147 ? -10.74200 -20.32300 -9.22200  1.000 26.72426 ? 143 GLY B N      1 
ATOM   5015 C  CA     . GLY B 1 147 ? -9.30900  -20.20700 -8.98200  1.000 26.14261 ? 143 GLY B CA     1 
ATOM   5016 C  C      . GLY B 1 147 ? -8.86300  -18.76500 -8.87100  1.000 30.89318 ? 143 GLY B C      1 
ATOM   5017 O  O      . GLY B 1 147 ? -8.19500  -18.37800 -7.90700  1.000 37.66504 ? 143 GLY B O      1 
ATOM   5018 N  N      . GLU B 1 148 ? -9.23300  -17.94500 -9.86000  1.000 29.10875 ? 144 GLU B N      1 
ATOM   5019 C  CA     . GLU B 1 148 ? -8.84900  -16.53300 -9.86500  1.000 30.76948 ? 144 GLU B CA     1 
ATOM   5020 C  C      . GLU B 1 148 ? -9.35700  -15.80500 -8.62400  1.000 30.13256 ? 144 GLU B C      1 
ATOM   5021 O  O      . GLU B 1 148 ? -8.61600  -15.03500 -7.99400  1.000 31.79592 ? 144 GLU B O      1 
ATOM   5022 C  CB     . GLU B 1 148 ? -9.39100  -15.86200 -11.12600 1.000 31.70380 ? 144 GLU B CB     1 
ATOM   5023 C  CG     . GLU B 1 148 ? -8.61700  -16.22100 -12.37300 1.000 44.44217 ? 144 GLU B CG     1 
ATOM   5024 C  CD     . GLU B 1 148 ? -9.19100  -15.59700 -13.63700 1.000 52.73527 ? 144 GLU B CD     1 
ATOM   5025 O  OE1    . GLU B 1 148 ? -10.21800 -14.90000 -13.54600 1.000 55.86722 ? 144 GLU B OE1    1 
ATOM   5026 O  OE2    . GLU B 1 148 ? -8.61100  -15.80500 -14.72500 1.000 62.61277 ? 144 GLU B OE2    1 
ATOM   5027 N  N      . MET B 1 149 ? -10.61800 -16.03900 -8.25500  1.000 24.81877 ? 145 MET B N      1 
ATOM   5028 C  CA     . MET B 1 149 ? -11.18600 -15.36000 -7.09600  1.000 27.93756 ? 145 MET B CA     1 
ATOM   5029 C  C      . MET B 1 149 ? -10.54600 -15.83300 -5.80000  1.000 26.02154 ? 145 MET B C      1 
ATOM   5030 O  O      . MET B 1 149 ? -10.41700 -15.04600 -4.85600  1.000 26.27947 ? 145 MET B O      1 
ATOM   5031 C  CB     . MET B 1 149 ? -12.69700 -15.58800 -7.05000  1.000 33.75142 ? 145 MET B CB     1 
ATOM   5032 C  CG     . MET B 1 149 ? -13.45800 -14.93200 -8.18100  1.000 41.77343 ? 145 MET B CG     1 
ATOM   5033 S  SD     . MET B 1 149 ? -13.39300 -13.14100 -8.04600  1.000 49.71912 ? 145 MET B SD     1 
ATOM   5034 C  CE     . MET B 1 149 ? -13.98500 -12.66900 -9.68200  1.000 52.31417 ? 145 MET B CE     1 
ATOM   5035 N  N      . THR B 1 150 ? -10.17900 -17.12000 -5.72500  1.000 25.15565 ? 146 THR B N      1 
ATOM   5036 C  CA     . THR B 1 150 ? -9.51400  -17.64000 -4.53300  1.000 28.51131 ? 146 THR B CA     1 
ATOM   5037 C  C      . THR B 1 150 ? -8.12900  -17.02500 -4.37100  1.000 26.94534 ? 146 THR B C      1 
ATOM   5038 O  O      . THR B 1 150 ? -7.77800  -16.50700 -3.30300  1.000 24.21869 ? 146 THR B O      1 
ATOM   5039 C  CB     . THR B 1 150 ? -9.42700  -19.16700 -4.60800  1.000 29.70356 ? 146 THR B CB     1 
ATOM   5040 O  OG1    . THR B 1 150 ? -10.75200 -19.72600 -4.57600  1.000 29.42984 ? 146 THR B OG1    1 
ATOM   5041 C  CG2    . THR B 1 150 ? -8.62400  -19.71300 -3.42600  1.000 30.86159 ? 146 THR B CG2    1 
ATOM   5042 N  N      . ARG B 1 151 ? -7.37200  -16.98400 -5.44000  1.000 22.61324 ? 147 ARG B N      1 
ATOM   5043 C  CA     . ARG B 1 151 ? -6.06900  -16.37200 -5.41300  1.000 27.18221 ? 147 ARG B CA     1 
ATOM   5044 C  C      . ARG B 1 151 ? -6.14400  -14.88500 -5.09100  1.000 27.06114 ? 147 ARG B C      1 
ATOM   5045 O  O      . ARG B 1 151 ? -5.34400  -14.38900 -4.40200  1.000 28.67712 ? 147 ARG B O      1 
ATOM   5046 C  CB     . ARG B 1 151 ? -5.32900  -16.63900 -6.70500  1.000 23.46860 ? 147 ARG B CB     1 
ATOM   5047 C  CG     . ARG B 1 151 ? -4.86700  -18.06500 -6.83400  1.000 24.53715 ? 147 ARG B CG     1 
ATOM   5048 C  CD     . ARG B 1 151 ? -3.98000  -18.20700 -8.01500  1.000 29.85884 ? 147 ARG B CD     1 
ATOM   5049 N  NE     . ARG B 1 151 ? -4.71400  -18.24500 -9.23200  1.000 37.06497 ? 147 ARG B NE     1 
ATOM   5050 C  CZ     . ARG B 1 151 ? -5.41400  -19.28200 -9.61200  1.000 47.19776 ? 147 ARG B CZ     1 
ATOM   5051 N  NH1    . ARG B 1 151 ? -5.48400  -20.36200 -8.87000  1.000 42.03136 ? 147 ARG B NH1    1 
ATOM   5052 N  NH2    . ARG B 1 151 ? -6.06000  -19.22600 -10.71700 1.000 53.94331 ? 147 ARG B NH2    1 
ATOM   5053 N  N      . ARG B 1 152 ? -7.15100  -14.22200 -5.61000  1.000 26.76374 ? 148 ARG B N      1 
ATOM   5054 C  CA     . ARG B 1 152 ? -7.41600  -12.84600 -5.33500  1.000 23.68968 ? 148 ARG B CA     1 
ATOM   5055 C  C      . ARG B 1 152 ? -7.68800  -12.66800 -3.84000  1.000 30.14046 ? 148 ARG B C      1 
ATOM   5056 O  O      . ARG B 1 152 ? -7.11500  -11.84000 -3.22700  1.000 26.37421 ? 148 ARG B O      1 
ATOM   5057 C  CB     . ARG B 1 152 ? -8.58400  -12.40300 -6.14400  1.000 25.71887 ? 148 ARG B CB     1 
ATOM   5058 C  CG     . ARG B 1 152 ? -9.01300  -11.00400 -5.90200  1.000 28.26918 ? 148 ARG B CG     1 
ATOM   5059 C  CD     . ARG B 1 152 ? -9.87800  -10.55200 -7.03200  1.000 40.01269 ? 148 ARG B CD     1 
ATOM   5060 N  NE     . ARG B 1 152 ? -9.78600  -9.14500  -7.15600  1.000 48.13998 ? 148 ARG B NE     1 
ATOM   5061 C  CZ     . ARG B 1 152 ? -9.56700  -8.49500  -8.25900  1.000 45.45019 ? 148 ARG B CZ     1 
ATOM   5062 N  NH1    . ARG B 1 152 ? -9.46400  -9.10600  -9.38100  1.000 41.59972 ? 148 ARG B NH1    1 
ATOM   5063 N  NH2    . ARG B 1 152 ? -9.46600  -7.21400  -8.20400  1.000 56.06462 ? 148 ARG B NH2    1 
ATOM   5064 N  N      . ALA B 1 153 ? -8.56300  -13.48500 -3.28600  1.000 27.48224 ? 149 ALA B N      1 
ATOM   5065 C  CA     . ALA B 1 153 ? -8.82800  -13.40800 -1.85500  1.000 25.33725 ? 149 ALA B CA     1 
ATOM   5066 C  C      . ALA B 1 153 ? -7.54600  -13.59700 -1.05300  1.000 28.18759 ? 149 ALA B C      1 
ATOM   5067 O  O      . ALA B 1 153 ? -7.28200  -12.85000 -0.10300  1.000 26.18735 ? 149 ALA B O      1 
ATOM   5068 C  CB     . ALA B 1 153 ? -9.86600  -14.45600 -1.45400  1.000 20.22085 ? 149 ALA B CB     1 
ATOM   5069 N  N      . LEU B 1 154 ? -6.74100  -14.60800 -1.41000  1.000 24.45030 ? 150 LEU B N      1 
ATOM   5070 C  CA     . LEU B 1 154 ? -5.52300  -14.88100 -0.64200  1.000 26.40053 ? 150 LEU B CA     1 
ATOM   5071 C  C      . LEU B 1 154 ? -4.51100  -13.75100 -0.78000  1.000 33.85406 ? 150 LEU B C      1 
ATOM   5072 O  O      . LEU B 1 154 ? -3.87500  -13.35300 0.20600   1.000 28.17443 ? 150 LEU B O      1 
ATOM   5073 C  CB     . LEU B 1 154 ? -4.90000  -16.20400 -1.08600  1.000 29.74567 ? 150 LEU B CB     1 
ATOM   5074 C  CG     . LEU B 1 154 ? -5.84800  -17.40000 -0.95100  1.000 32.34072 ? 150 LEU B CG     1 
ATOM   5075 C  CD1    . LEU B 1 154 ? -5.23800  -18.68600 -1.52300  1.000 23.51071 ? 150 LEU B CD1    1 
ATOM   5076 C  CD2    . LEU B 1 154 ? -6.22900  -17.57000 0.49400   1.000 36.07275 ? 150 LEU B CD2    1 
ATOM   5077 N  N      . ARG B 1 155 ? -4.35800  -13.21100 -1.99300  1.000 30.97740 ? 151 ARG B N      1 
ATOM   5078 C  CA     . ARG B 1 155 ? -3.48000  -12.06200 -2.18200  1.000 25.88731 ? 151 ARG B CA     1 
ATOM   5079 C  C      . ARG B 1 155 ? -3.95900  -10.88300 -1.35200  1.000 29.08507 ? 151 ARG B C      1 
ATOM   5080 O  O      . ARG B 1 155 ? -3.16900  -10.22700 -0.66100  1.000 26.61635 ? 151 ARG B O      1 
ATOM   5081 C  CB     . ARG B 1 155 ? -3.43800  -11.68700 -3.66900  1.000 23.38438 ? 151 ARG B CB     1 
ATOM   5082 C  CG     . ARG B 1 155 ? -2.76200  -10.35700 -3.98900  1.000 26.33210 ? 151 ARG B CG     1 
ATOM   5083 C  CD     . ARG B 1 155 ? -2.58700  -10.15500 -5.51500  1.000 23.65810 ? 151 ARG B CD     1 
ATOM   5084 N  NE     . ARG B 1 155 ? -3.85800  -10.13200 -6.23800  1.000 29.95359 ? 151 ARG B NE     1 
ATOM   5085 C  CZ     . ARG B 1 155 ? -4.32300  -11.12500 -7.00100  1.000 32.74077 ? 151 ARG B CZ     1 
ATOM   5086 N  NH1    . ARG B 1 155 ? -3.61900  -12.24400 -7.14700  1.000 27.80597 ? 151 ARG B NH1    1 
ATOM   5087 N  NH2    . ARG B 1 155 ? -5.50400  -11.00300 -7.60500  1.000 22.76326 ? 151 ARG B NH2    1 
ATOM   5088 N  N      . THR B 1 156 ? -5.26800  -10.61600 -1.38700  1.000 25.50569 ? 152 THR B N      1 
ATOM   5089 C  CA     . THR B 1 156 ? -5.79100  -9.42400  -0.73200  1.000 26.41633 ? 152 THR B CA     1 
ATOM   5090 C  C      . THR B 1 156 ? -5.68300  -9.53300  0.78700   1.000 28.75345 ? 152 THR B C      1 
ATOM   5091 O  O      . THR B 1 156 ? -5.35000  -8.54600  1.45800   1.000 23.46597 ? 152 THR B O      1 
ATOM   5092 C  CB     . THR B 1 156 ? -7.23800  -9.18100  -1.16700  1.000 28.65607 ? 152 THR B CB     1 
ATOM   5093 O  OG1    . THR B 1 156 ? -7.30400  -9.10800  -2.60000  1.000 28.96137 ? 152 THR B OG1    1 
ATOM   5094 C  CG2    . THR B 1 156 ? -7.77100  -7.89400  -0.56700  1.000 24.38187 ? 152 THR B CG2    1 
ATOM   5095 N  N      . ALA B 1 157 ? -5.92500  -10.72800 1.34500   1.000 25.22671 ? 153 ALA B N      1 
ATOM   5096 C  CA     . ALA B 1 157 ? -5.90300  -10.88500 2.80100   1.000 32.04332 ? 153 ALA B CA     1 
ATOM   5097 C  C      . ALA B 1 157 ? -4.52500  -10.58700 3.38300   1.000 28.94294 ? 153 ALA B C      1 
ATOM   5098 O  O      . ALA B 1 157 ? -4.41300  -9.99000  4.46200   1.000 26.16630 ? 153 ALA B O      1 
ATOM   5099 C  CB     . ALA B 1 157 ? -6.32500  -12.30500 3.19800   1.000 21.07095 ? 153 ALA B CB     1 
ATOM   5100 N  N      . GLN B 1 158 ? -3.46200  -10.98800 2.68400   1.000 27.09535 ? 154 GLN B N      1 
ATOM   5101 C  CA     . GLN B 1 158 ? -2.12200  -11.00200 3.26300   1.000 31.27480 ? 154 GLN B CA     1 
ATOM   5102 C  C      . GLN B 1 158 ? -1.16900  -9.96500  2.67900   1.000 32.05648 ? 154 GLN B C      1 
ATOM   5103 O  O      . GLN B 1 158 ? -0.01600  -9.91700  3.09800   1.000 35.15948 ? 154 GLN B O      1 
ATOM   5104 C  CB     . GLN B 1 158 ? -1.51500  -12.40400 3.12800   1.000 32.83025 ? 154 GLN B CB     1 
ATOM   5105 C  CG     . GLN B 1 158 ? -2.40400  -13.45100 3.76800   1.000 31.46430 ? 154 GLN B CG     1 
ATOM   5106 C  CD     . GLN B 1 158 ? -2.02600  -14.85900 3.38500   1.000 34.80680 ? 154 GLN B CD     1 
ATOM   5107 O  OE1    . GLN B 1 158 ? -1.45400  -15.58600 4.18900   1.000 40.59960 ? 154 GLN B OE1    1 
ATOM   5108 N  NE2    . GLN B 1 158 ? -2.35600  -15.26100 2.15800   1.000 36.71493 ? 154 GLN B NE2    1 
ATOM   5109 N  N      . SER B 1 159 ? -1.62300  -9.11400  1.77200   1.000 26.79005 ? 155 SER B N      1 
ATOM   5110 C  CA     . SER B 1 159 ? -0.80200  -8.05500  1.20800   1.000 29.85358 ? 155 SER B CA     1 
ATOM   5111 C  C      . SER B 1 159 ? -1.18800  -6.72400  1.84200   1.000 28.27971 ? 155 SER B C      1 
ATOM   5112 O  O      . SER B 1 159 ? -2.25700  -6.59300  2.43600   1.000 26.15050 ? 155 SER B O      1 
ATOM   5113 C  CB     . SER B 1 159 ? -1.00100  -7.97800  -0.30600  1.000 27.22958 ? 155 SER B CB     1 
ATOM   5114 O  OG     . SER B 1 159 ? -0.62500  -9.19800  -0.92700  1.000 33.09871 ? 155 SER B OG     1 
ATOM   5115 N  N      . GLY B 1 160 ? -0.30200  -5.73900  1.72300   1.000 26.16893 ? 156 GLY B N      1 
ATOM   5116 C  CA     . GLY B 1 160 ? -0.56500  -4.46500  2.38200   1.000 26.37158 ? 156 GLY B CA     1 
ATOM   5117 C  C      . GLY B 1 160 ? -0.89900  -4.66300  3.84800   1.000 28.27707 ? 156 GLY B C      1 
ATOM   5118 O  O      . GLY B 1 160 ? -0.34500  -5.53100  4.53000   1.000 29.62460 ? 156 GLY B O      1 
ATOM   5119 N  N      . ARG B 1 161 ? -1.83800  -3.87300  4.33800   1.000 26.34526 ? 157 ARG B N      1 
ATOM   5120 C  CA     . ARG B 1 161 ? -2.35000  -4.08300  5.68600   1.000 26.66636 ? 157 ARG B CA     1 
ATOM   5121 C  C      . ARG B 1 161 ? -3.23400  -5.32700  5.69000   1.000 27.99809 ? 157 ARG B C      1 
ATOM   5122 O  O      . ARG B 1 161 ? -4.28900  -5.32500  5.04400   1.000 27.56383 ? 157 ARG B O      1 
ATOM   5123 C  CB     . ARG B 1 161 ? -3.13800  -2.86200  6.15400   1.000 24.32923 ? 157 ARG B CB     1 
ATOM   5124 C  CG     . ARG B 1 161 ? -3.64900  -2.96200  7.60000   1.000 28.09021 ? 157 ARG B CG     1 
ATOM   5125 C  CD     . ARG B 1 161 ? -4.41800  -1.71000  7.95500   1.000 30.50892 ? 157 ARG B CD     1 
ATOM   5126 N  NE     . ARG B 1 161 ? -4.76700  -1.62400  9.37000   1.000 25.68992 ? 157 ARG B NE     1 
ATOM   5127 C  CZ     . ARG B 1 161 ? -5.06300  -0.48000  9.98300   1.000 30.38785 ? 157 ARG B CZ     1 
ATOM   5128 N  NH1    . ARG B 1 161 ? -5.03200  0.66300   9.29500   1.000 29.19034 ? 157 ARG B NH1    1 
ATOM   5129 N  NH2    . ARG B 1 161 ? -5.39500  -0.47000  11.27500  1.000 22.29215 ? 157 ARG B NH2    1 
ATOM   5130 N  N      . PRO B 1 162 ? -2.85800  -6.39500  6.38900   1.000 25.86626 ? 158 PRO B N      1 
ATOM   5131 C  CA     . PRO B 1 162 ? -3.64000  -7.63800  6.30800   1.000 20.91567 ? 158 PRO B CA     1 
ATOM   5132 C  C      . PRO B 1 162 ? -5.04800  -7.41400  6.82800   1.000 24.34239 ? 158 PRO B C      1 
ATOM   5133 O  O      . PRO B 1 162 ? -5.28900  -6.54200  7.66300   1.000 26.36106 ? 158 PRO B O      1 
ATOM   5134 C  CB     . PRO B 1 162 ? -2.85900  -8.61300  7.20500   1.000 22.51059 ? 158 PRO B CB     1 
ATOM   5135 C  CG     . PRO B 1 162 ? -1.45000  -8.04600  7.25700   1.000 28.89031 ? 158 PRO B CG     1 
ATOM   5136 C  CD     . PRO B 1 162 ? -1.66100  -6.54300  7.23300   1.000 24.68191 ? 158 PRO B CD     1 
ATOM   5137 N  N      . GLY B 1 163 ? -5.98300  -8.22100  6.33500   1.000 22.71062 ? 159 GLY B N      1 
ATOM   5138 C  CA     . GLY B 1 163 ? -7.35500  -8.14100  6.78300   1.000 23.04750 ? 159 GLY B CA     1 
ATOM   5139 C  C      . GLY B 1 163 ? -8.18800  -9.29100  6.26100   1.000 27.04272 ? 159 GLY B C      1 
ATOM   5140 O  O      . GLY B 1 163 ? -7.70900  -10.12200 5.48400   1.000 25.35567 ? 159 GLY B O      1 
ATOM   5141 N  N      . PRO B 1 164 ? -9.45100  -9.35900  6.68500   1.000 27.33222 ? 160 PRO B N      1 
ATOM   5142 C  CA     . PRO B 1 164 ? -10.30700 -10.49800 6.32300   1.000 24.93194 ? 160 PRO B CA     1 
ATOM   5143 C  C      . PRO B 1 164 ? -10.96100 -10.36800 4.95100   1.000 25.87415 ? 160 PRO B C      1 
ATOM   5144 O  O      . PRO B 1 164 ? -11.09600 -9.28200  4.38100   1.000 22.34215 ? 160 PRO B O      1 
ATOM   5145 C  CB     . PRO B 1 164 ? -11.37500 -10.49300 7.42500   1.000 23.76074 ? 160 PRO B CB     1 
ATOM   5146 C  CG     . PRO B 1 164 ? -11.43100 -9.05800  7.89700   1.000 20.03398 ? 160 PRO B CG     1 
ATOM   5147 C  CD     . PRO B 1 164 ? -10.02000 -8.55700  7.78700   1.000 24.47399 ? 160 PRO B CD     1 
ATOM   5148 N  N      . ILE B 1 165 ? -11.41400 -11.51700 4.44700   1.000 24.13710 ? 161 ILE B N      1 
ATOM   5149 C  CA     . ILE B 1 165 ? -12.04100 -11.62800 3.13100   1.000 28.49026 ? 161 ILE B CA     1 
ATOM   5150 C  C      . ILE B 1 165 ? -13.32000 -12.43500 3.26900   1.000 25.48200 ? 161 ILE B C      1 
ATOM   5151 O  O      . ILE B 1 165 ? -13.35600 -13.41600 4.01800   1.000 25.66887 ? 161 ILE B O      1 
ATOM   5152 C  CB     . ILE B 1 165 ? -11.13100 -12.33200 2.10300   1.000 32.44073 ? 161 ILE B CB     1 
ATOM   5153 C  CG1    . ILE B 1 165 ? -9.73300  -11.70700 2.07700   1.000 23.22121 ? 161 ILE B CG1    1 
ATOM   5154 C  CG2    . ILE B 1 165 ? -11.83400 -12.37200 0.73000   1.000 25.56622 ? 161 ILE B CG2    1 
ATOM   5155 C  CD1    . ILE B 1 165 ? -9.70200  -10.28200 1.59300   1.000 19.84185 ? 161 ILE B CD1    1 
ATOM   5156 N  N      . HIS B 1 166 ? -14.34700 -12.07300 2.50200   1.000 22.88169 ? 162 HIS B N      1 
ATOM   5157 C  CA     . HIS B 1 166 ? -15.58000 -12.85800 2.43600   1.000 19.21020 ? 162 HIS B CA     1 
ATOM   5158 C  C      . HIS B 1 166 ? -15.77900 -13.36700 1.01200   1.000 19.89186 ? 162 HIS B C      1 
ATOM   5159 O  O      . HIS B 1 166 ? -15.94700 -12.56700 0.08800   1.000 25.81099 ? 162 HIS B O      1 
ATOM   5160 C  CB     . HIS B 1 166 ? -16.78000 -12.02500 2.90300   1.000 19.06544 ? 162 HIS B CB     1 
ATOM   5161 C  CG     . HIS B 1 166 ? -18.11300 -12.64400 2.60800   1.000 21.27360 ? 162 HIS B CG     1 
ATOM   5162 N  ND1    . HIS B 1 166 ? -19.12000 -11.95700 1.96400   1.000 23.75811 ? 162 HIS B ND1    1 
ATOM   5163 C  CD2    . HIS B 1 166 ? -18.61000 -13.87700 2.87700   1.000 22.83168 ? 162 HIS B CD2    1 
ATOM   5164 C  CE1    . HIS B 1 166 ? -20.18400 -12.73700 1.85700   1.000 28.64817 ? 162 HIS B CE1    1 
ATOM   5165 N  NE2    . HIS B 1 166 ? -19.89900 -13.91000 2.39900   1.000 23.58967 ? 162 HIS B NE2    1 
ATOM   5166 N  N      . LEU B 1 167 ? -15.74700 -14.68900 0.83700   1.000 21.96842 ? 163 LEU B N      1 
ATOM   5167 C  CA     . LEU B 1 167 ? -16.03700 -15.34900 -0.43600  1.000 23.10540 ? 163 LEU B CA     1 
ATOM   5168 C  C      . LEU B 1 167 ? -17.34800 -16.11600 -0.31300  1.000 28.62448 ? 163 LEU B C      1 
ATOM   5169 O  O      . LEU B 1 167 ? -17.47900 -17.01200 0.53700   1.000 25.51095 ? 163 LEU B O      1 
ATOM   5170 C  CB     . LEU B 1 167 ? -14.91900 -16.30700 -0.83200  1.000 25.85047 ? 163 LEU B CB     1 
ATOM   5171 C  CG     . LEU B 1 167 ? -13.73500 -15.79200 -1.63900  1.000 32.84078 ? 163 LEU B CG     1 
ATOM   5172 C  CD1    . LEU B 1 167 ? -12.86400 -16.97600 -2.05400  1.000 29.13244 ? 163 LEU B CD1    1 
ATOM   5173 C  CD2    . LEU B 1 167 ? -14.16500 -14.99300 -2.86100  1.000 31.92488 ? 163 LEU B CD2    1 
ATOM   5174 N  N      . ASN B 1 168 ? -18.31300 -15.76300 -1.15700  1.000 23.60020 ? 164 ASN B N      1 
ATOM   5175 C  CA     . ASN B 1 168 ? -19.64700 -16.34400 -1.14600  1.000 22.47375 ? 164 ASN B CA     1 
ATOM   5176 C  C      . ASN B 1 168 ? -19.77500 -17.27100 -2.35000  1.000 24.53715 ? 164 ASN B C      1 
ATOM   5177 O  O      . ASN B 1 168 ? -19.41300 -16.88800 -3.46800  1.000 29.72988 ? 164 ASN B O      1 
ATOM   5178 C  CB     . ASN B 1 168 ? -20.69500 -15.22300 -1.17100  1.000 25.43989 ? 164 ASN B CB     1 
ATOM   5179 C  CG     . ASN B 1 168 ? -22.11000 -15.73200 -1.13800  1.000 28.82977 ? 164 ASN B CG     1 
ATOM   5180 O  OD1    . ASN B 1 168 ? -22.90500 -15.45500 -2.04900  1.000 32.20649 ? 164 ASN B OD1    1 
ATOM   5181 N  ND2    . ASN B 1 168 ? -22.44700 -16.47000 -0.09100  1.000 26.71110 ? 164 ASN B ND2    1 
ATOM   5182 N  N      . ILE B 1 169 ? -20.24100 -18.49900 -2.12200  1.000 27.04008 ? 165 ILE B N      1 
ATOM   5183 C  CA     . ILE B 1 169 ? -20.16400 -19.53900 -3.15400  1.000 31.05636 ? 165 ILE B CA     1 
ATOM   5184 C  C      . ILE B 1 169 ? -21.52800 -20.15600 -3.45300  1.000 30.23784 ? 165 ILE B C      1 
ATOM   5185 O  O      . ILE B 1 169 ? -22.07300 -20.89100 -2.61700  1.000 30.00886 ? 165 ILE B O      1 
ATOM   5186 C  CB     . ILE B 1 169 ? -19.17000 -20.64100 -2.75200  1.000 31.39324 ? 165 ILE B CB     1 
ATOM   5187 C  CG1    . ILE B 1 169 ? -17.81700 -20.03500 -2.38600  1.000 32.14070 ? 165 ILE B CG1    1 
ATOM   5188 C  CG2    . ILE B 1 169 ? -19.02200 -21.65400 -3.88500  1.000 25.31356 ? 165 ILE B CG2    1 
ATOM   5189 C  CD1    . ILE B 1 169 ? -16.87500 -21.02000 -1.73100  1.000 33.29347 ? 165 ILE B CD1    1 
ATOM   5190 N  N      . PRO B 1 170 ? -22.10600 -19.91600 -4.62700  1.000 32.38809 ? 166 PRO B N      1 
ATOM   5191 C  CA     . PRO B 1 170 ? -23.38800 -20.55800 -4.95900  1.000 32.51706 ? 166 PRO B CA     1 
ATOM   5192 C  C      . PRO B 1 170 ? -23.25200 -22.07700 -4.97500  1.000 34.29095 ? 166 PRO B C      1 
ATOM   5193 O  O      . PRO B 1 170 ? -22.27500 -22.63400 -5.48300  1.000 33.50139 ? 166 PRO B O      1 
ATOM   5194 C  CB     . PRO B 1 170 ? -23.71500 -19.99500 -6.34900  1.000 32.55390 ? 166 PRO B CB     1 
ATOM   5195 C  CG     . PRO B 1 170 ? -22.98500 -18.65800 -6.37900  1.000 30.84580 ? 166 PRO B CG     1 
ATOM   5196 C  CD     . PRO B 1 170 ? -21.69000 -18.93700 -5.64700  1.000 31.78013 ? 166 PRO B CD     1 
ATOM   5197 N  N      . ALA B 1 171 ? -24.24200 -22.75300 -4.39700  1.000 32.60917 ? 167 ALA B N      1 
ATOM   5198 C  CA     . ALA B 1 171 ? -24.07700 -24.18000 -4.15700  1.000 32.85920 ? 167 ALA B CA     1 
ATOM   5199 C  C      . ALA B 1 171 ? -24.01600 -24.96300 -5.45900  1.000 33.45138 ? 167 ALA B C      1 
ATOM   5200 O  O      . ALA B 1 171 ? -23.37000 -26.01000 -5.51800  1.000 38.55989 ? 167 ALA B O      1 
ATOM   5201 C  CB     . ALA B 1 171 ? -25.20500 -24.69100 -3.26300  1.000 35.98589 ? 167 ALA B CB     1 
ATOM   5202 N  N      . ASP B 1 172 ? -24.65500 -24.47000 -6.51800  1.000 30.71158 ? 168 ASP B N      1 
ATOM   5203 C  CA     . ASP B 1 172 ? -24.59900 -25.18100 -7.78900  1.000 35.40688 ? 168 ASP B CA     1 
ATOM   5204 C  C      . ASP B 1 172 ? -23.25200 -24.98600 -8.48500  1.000 40.41800 ? 168 ASP B C      1 
ATOM   5205 O  O      . ASP B 1 172 ? -22.75800 -25.91200 -9.13800  1.000 43.01832 ? 168 ASP B O      1 
ATOM   5206 C  CB     . ASP B 1 172 ? -25.75700 -24.74100 -8.69100  1.000 36.22013 ? 168 ASP B CB     1 
ATOM   5207 C  CG     . ASP B 1 172 ? -25.77900 -23.24500 -8.93700  1.000 42.39456 ? 168 ASP B CG     1 
ATOM   5208 O  OD1    . ASP B 1 172 ? -25.29700 -22.47800 -8.07600  1.000 45.32649 ? 168 ASP B OD1    1 
ATOM   5209 O  OD2    . ASP B 1 172 ? -26.27600 -22.83100 -10.00200 1.000 47.28198 ? 168 ASP B OD2    1 
ATOM   5210 N  N      . ILE B 1 173 ? -22.63000 -23.81200 -8.33700  1.000 37.78085 ? 169 ILE B N      1 
ATOM   5211 C  CA     . ILE B 1 173 ? -21.28500 -23.59100 -8.87400  1.000 38.97309 ? 169 ILE B CA     1 
ATOM   5212 C  C      . ILE B 1 173 ? -20.27600 -24.53600 -8.23400  1.000 37.66504 ? 169 ILE B C      1 
ATOM   5213 O  O      . ILE B 1 173 ? -19.26700 -24.90400 -8.85600  1.000 30.94318 ? 169 ILE B O      1 
ATOM   5214 C  CB     . ILE B 1 173 ? -20.86300 -22.11800 -8.65700  1.000 40.78910 ? 169 ILE B CB     1 
ATOM   5215 C  CG1    . ILE B 1 173 ? -21.63500 -21.18400 -9.58800  1.000 44.75537 ? 169 ILE B CG1    1 
ATOM   5216 C  CG2    . ILE B 1 173 ? -19.36300 -21.93700 -8.81400  1.000 45.57389 ? 169 ILE B CG2    1 
ATOM   5217 C  CD1    . ILE B 1 173 ? -21.96100 -21.79900 -10.91000 1.000 47.73204 ? 169 ILE B CD1    1 
ATOM   5218 N  N      . ALA B 1 174 ? -20.52400 -24.93200 -6.98400  1.000 29.86411 ? 170 ALA B N      1 
ATOM   5219 C  CA     . ALA B 1 174 ? -19.48300 -25.54200 -6.16500  1.000 30.24047 ? 170 ALA B CA     1 
ATOM   5220 C  C      . ALA B 1 174 ? -18.97900 -26.84800 -6.75600  1.000 32.99343 ? 170 ALA B C      1 
ATOM   5221 O  O      . ALA B 1 174 ? -17.77900 -27.14800 -6.68500  1.000 32.19597 ? 170 ALA B O      1 
ATOM   5222 C  CB     . ALA B 1 174 ? -19.99800 -25.76200 -4.74800  1.000 29.73514 ? 170 ALA B CB     1 
ATOM   5223 N  N      . LYS B 1 175 ? -19.86300 -27.63000 -7.36700  1.000 35.09631 ? 171 LYS B N      1 
ATOM   5224 C  CA     . LYS B 1 175 ? -19.45600 -28.93300 -7.86600  1.000 39.15469 ? 171 LYS B CA     1 
ATOM   5225 C  C      . LYS B 1 175 ? -19.35900 -28.96400 -9.38700  1.000 38.73359 ? 171 LYS B C      1 
ATOM   5226 O  O      . LYS B 1 175 ? -19.29100 -30.04700 -9.98100  1.000 38.18353 ? 171 LYS B O      1 
ATOM   5227 C  CB     . LYS B 1 175 ? -20.39700 -30.01700 -7.33800  1.000 41.82870 ? 171 LYS B CB     1 
ATOM   5228 C  CG     . LYS B 1 175 ? -20.12500 -30.34900 -5.86600  1.000 51.01928 ? 171 LYS B CG     1 
ATOM   5229 C  CD     . LYS B 1 175 ? -20.94500 -31.52100 -5.34700  1.000 45.65021 ? 171 LYS B CD     1 
ATOM   5230 C  CE     . LYS B 1 175 ? -20.29600 -32.85000 -5.70200  1.000 48.82954 ? 171 LYS B CE     1 
ATOM   5231 N  NZ     . LYS B 1 175 ? -20.85600 -33.96400 -4.87800  1.000 54.30914 ? 171 LYS B NZ     1 
ATOM   5232 N  N      . HIS B 1 176 ? -19.28900 -27.80100 -10.03000 1.000 38.77044 ? 172 HIS B N      1 
ATOM   5233 C  CA     . HIS B 1 176 ? -18.99100 -27.79100 -11.45200 1.000 36.77283 ? 172 HIS B CA     1 
ATOM   5234 C  C      . HIS B 1 176 ? -17.51900 -28.12700 -11.67100 1.000 34.75417 ? 172 HIS B C      1 
ATOM   5235 O  O      . HIS B 1 176 ? -16.66200 -27.77000 -10.86000 1.000 34.85681 ? 172 HIS B O      1 
ATOM   5236 C  CB     . HIS B 1 176 ? -19.29500 -26.43200 -12.07500 1.000 41.55498 ? 172 HIS B CB     1 
ATOM   5237 C  CG     . HIS B 1 176 ? -20.75400 -26.12600 -12.18000 1.000 48.31369 ? 172 HIS B CG     1 
ATOM   5238 N  ND1    . HIS B 1 176 ? -21.23000 -24.86500 -12.46900 1.000 48.60320 ? 172 HIS B ND1    1 
ATOM   5239 C  CD2    . HIS B 1 176 ? -21.84300 -26.91600 -12.02800 1.000 46.60822 ? 172 HIS B CD2    1 
ATOM   5240 C  CE1    . HIS B 1 176 ? -22.55100 -24.89100 -12.49100 1.000 43.73419 ? 172 HIS B CE1    1 
ATOM   5241 N  NE2    . HIS B 1 176 ? -22.94600 -26.12300 -12.22800 1.000 46.26344 ? 172 HIS B NE2    1 
ATOM   5242 N  N      . PRO B 1 177 ? -17.20400 -28.82300 -12.76000 1.000 43.10517 ? 173 PRO B N      1 
ATOM   5243 C  CA     . PRO B 1 177 ? -15.80700 -29.15500 -13.04900 1.000 40.25746 ? 173 PRO B CA     1 
ATOM   5244 C  C      . PRO B 1 177 ? -15.05000 -27.94100 -13.56300 1.000 41.66815 ? 173 PRO B C      1 
ATOM   5245 O  O      . PRO B 1 177 ? -15.57400 -27.12800 -14.32800 1.000 47.10038 ? 173 PRO B O      1 
ATOM   5246 C  CB     . PRO B 1 177 ? -15.90500 -30.24000 -14.13200 1.000 39.05995 ? 173 PRO B CB     1 
ATOM   5247 C  CG     . PRO B 1 177 ? -17.35600 -30.50000 -14.34600 1.000 45.75812 ? 173 PRO B CG     1 
ATOM   5248 C  CD     . PRO B 1 177 ? -18.13000 -29.36100 -13.76800 1.000 42.61037 ? 173 PRO B CD     1 
ATOM   5249 N  N      . VAL B 1 178 ? -13.80600 -27.82200 -13.11800 1.000 39.60212 ? 174 VAL B N      1 
ATOM   5250 C  CA     . VAL B 1 178 ? -12.89500 -26.77500 -13.57700 1.000 37.70715 ? 174 VAL B CA     1 
ATOM   5251 C  C      . VAL B 1 178 ? -11.52700 -27.39600 -13.79900 1.000 37.81506 ? 174 VAL B C      1 
ATOM   5252 O  O      . VAL B 1 178 ? -11.21200 -28.45400 -13.24400 1.000 41.76290 ? 174 VAL B O      1 
ATOM   5253 C  CB     . VAL B 1 178 ? -12.78000 -25.62200 -12.56500 1.000 33.38821 ? 174 VAL B CB     1 
ATOM   5254 C  CG1    . VAL B 1 178 ? -14.17100 -25.06100 -12.21000 1.000 33.03028 ? 174 VAL B CG1    1 
ATOM   5255 C  CG2    . VAL B 1 178 ? -12.03000 -26.10900 -11.32700 1.000 31.64590 ? 174 VAL B CG2    1 
ATOM   5256 N  N      . PRO B 1 179 ? -10.69800 -26.75900 -14.62600 1.000 46.34503 ? 175 PRO B N      1 
ATOM   5257 C  CA     . PRO B 1 179 ? -9.31300  -27.22700 -14.76800 1.000 43.32362 ? 175 PRO B CA     1 
ATOM   5258 C  C      . PRO B 1 179 ? -8.57400  -27.12600 -13.43700 1.000 39.20733 ? 175 PRO B C      1 
ATOM   5259 O  O      . PRO B 1 179 ? -8.72200  -26.15300 -12.69500 1.000 38.46514 ? 175 PRO B O      1 
ATOM   5260 C  CB     . PRO B 1 179 ? -8.72300  -26.28100 -15.82400 1.000 45.64495 ? 175 PRO B CB     1 
ATOM   5261 C  CG     . PRO B 1 179 ? -9.91900  -25.63500 -16.49600 1.000 43.63155 ? 175 PRO B CG     1 
ATOM   5262 C  CD     . PRO B 1 179 ? -10.94500 -25.53400 -15.40400 1.000 43.22624 ? 175 PRO B CD     1 
ATOM   5263 N  N      . LEU B 1 180 ? -7.77500  -28.14300 -13.13500 1.000 37.32553 ? 176 LEU B N      1 
ATOM   5264 C  CA     . LEU B 1 180 ? -7.00900  -28.18200 -11.89000 1.000 41.45760 ? 176 LEU B CA     1 
ATOM   5265 C  C      . LEU B 1 180 ? -5.81100  -27.25000 -12.03600 1.000 41.61815 ? 176 LEU B C      1 
ATOM   5266 O  O      . LEU B 1 180 ? -4.77600  -27.62000 -12.59400 1.000 41.06019 ? 176 LEU B O      1 
ATOM   5267 C  CB     . LEU B 1 180 ? -6.57500  -29.60700 -11.57000 1.000 42.81566 ? 176 LEU B CB     1 
ATOM   5268 C  CG     . LEU B 1 180 ? -5.63300  -29.80300 -10.38000 1.000 45.40808 ? 176 LEU B CG     1 
ATOM   5269 C  CD1    . LEU B 1 180 ? -6.22400  -29.23500 -9.10200  1.000 34.72258 ? 176 LEU B CD1    1 
ATOM   5270 C  CD2    . LEU B 1 180 ? -5.30800  -31.28100 -10.21400 1.000 47.41095 ? 176 LEU B CD2    1 
ATOM   5271 N  N      . GLU B 1 181 ? -5.94600  -26.03500 -11.51800 1.000 40.73910 ? 177 GLU B N      1 
ATOM   5272 C  CA     . GLU B 1 181 ? -4.94700  -24.98300 -11.69100 1.000 44.45796 ? 177 GLU B CA     1 
ATOM   5273 C  C      . GLU B 1 181 ? -4.65600  -24.39100 -10.31600 1.000 42.64722 ? 177 GLU B C      1 
ATOM   5274 O  O      . GLU B 1 181 ? -5.35600  -23.48200 -9.87000  1.000 39.86794 ? 177 GLU B O      1 
ATOM   5275 C  CB     . GLU B 1 181 ? -5.45500  -23.92000 -12.66100 1.000 49.18748 ? 177 GLU B CB     1 
ATOM   5276 C  CG     . GLU B 1 181 ? -4.38000  -23.28500 -13.52200 1.000 64.30508 ? 177 GLU B CG     1 
ATOM   5277 C  CD     . GLU B 1 181 ? -3.95900  -24.19200 -14.65500 1.000 73.24562 ? 177 GLU B CD     1 
ATOM   5278 O  OE1    . GLU B 1 181 ? -2.76800  -24.15600 -15.04900 1.000 73.67199 ? 177 GLU B OE1    1 
ATOM   5279 O  OE2    . GLU B 1 181 ? -4.82800  -24.94500 -15.14600 1.000 75.11953 ? 177 GLU B OE2    1 
ATOM   5280 N  N      . VAL B 1 182 ? -3.61200  -24.89900 -9.66300  1.000 41.61025 ? 178 VAL B N      1 
ATOM   5281 C  CA     . VAL B 1 182 ? -3.20700  -24.47300 -8.32700  1.000 43.47627 ? 178 VAL B CA     1 
ATOM   5282 C  C      . VAL B 1 182 ? -1.78900  -23.92600 -8.42200  1.000 40.03112 ? 178 VAL B C      1 
ATOM   5283 O  O      . VAL B 1 182 ? -0.92400  -24.55800 -9.03500  1.000 37.57029 ? 178 VAL B O      1 
ATOM   5284 C  CB     . VAL B 1 182 ? -3.28000  -25.63100 -7.31400  1.000 45.55020 ? 178 VAL B CB     1 
ATOM   5285 C  CG1    . VAL B 1 182 ? -2.75500  -25.18100 -5.95000  1.000 39.85478 ? 178 VAL B CG1    1 
ATOM   5286 C  CG2    . VAL B 1 182 ? -4.70800  -26.14800 -7.19600  1.000 43.71840 ? 178 VAL B CG2    1 
ATOM   5287 N  N      . PHE B 1 183 ? -1.54700  -22.77100 -7.79300  1.000 39.67844 ? 179 PHE B N      1 
ATOM   5288 C  CA     . PHE B 1 183 ? -0.28900  -22.04200 -7.88700  1.000 41.31548 ? 179 PHE B CA     1 
ATOM   5289 C  C      . PHE B 1 183 ? 0.35100   -21.92500 -6.51100  1.000 36.77809 ? 179 PHE B C      1 
ATOM   5290 O  O      . PHE B 1 183 ? -0.35300  -21.88700 -5.50400  1.000 35.87535 ? 179 PHE B O      1 
ATOM   5291 C  CB     . PHE B 1 183 ? -0.48200  -20.62100 -8.45000  1.000 35.65427 ? 179 PHE B CB     1 
ATOM   5292 C  CG     . PHE B 1 183 ? -0.95700  -20.58000 -9.87500  1.000 36.33067 ? 179 PHE B CG     1 
ATOM   5293 C  CD1    . PHE B 1 183 ? -2.29200  -20.78300 -10.18000 1.000 37.69926 ? 179 PHE B CD1    1 
ATOM   5294 C  CD2    . PHE B 1 183 ? -0.07300  -20.33000 -10.90700 1.000 44.43164 ? 179 PHE B CD2    1 
ATOM   5295 C  CE1    . PHE B 1 183 ? -2.73100  -20.74900 -11.48500 1.000 39.77319 ? 179 PHE B CE1    1 
ATOM   5296 C  CE2    . PHE B 1 183 ? -0.50700  -20.29100 -12.22200 1.000 43.96317 ? 179 PHE B CE2    1 
ATOM   5297 C  CZ     . PHE B 1 183 ? -1.83300  -20.49700 -12.51200 1.000 39.10732 ? 179 PHE B CZ     1 
ATOM   5298 N  N      . PRO B 1 184 ? 1.68800   -21.89100 -6.43600  1.000 39.25471 ? 180 PRO B N      1 
ATOM   5299 C  CA     . PRO B 1 184 ? 2.32200   -21.54800 -5.16000  1.000 36.02537 ? 180 PRO B CA     1 
ATOM   5300 C  C      . PRO B 1 184 ? 2.04700   -20.10800 -4.80800  1.000 36.50964 ? 180 PRO B C      1 
ATOM   5301 O  O      . PRO B 1 184 ? 1.82600   -19.26000 -5.69400  1.000 33.14871 ? 180 PRO B O      1 
ATOM   5302 C  CB     . PRO B 1 184 ? 3.82200   -21.79100 -5.44200  1.000 39.77056 ? 180 PRO B CB     1 
ATOM   5303 C  CG     . PRO B 1 184 ? 3.97200   -21.68900 -6.90200  1.000 40.25746 ? 180 PRO B CG     1 
ATOM   5304 C  CD     . PRO B 1 184 ? 2.66200   -22.12400 -7.51400  1.000 40.10744 ? 180 PRO B CD     1 
ATOM   5305 N  N      . PRO B 1 185 ? 2.00800   -19.76900 -3.51300  1.000 39.89689 ? 181 PRO B N      1 
ATOM   5306 C  CA     . PRO B 1 185 ? 1.66800   -18.39000 -3.11900  1.000 37.52029 ? 181 PRO B CA     1 
ATOM   5307 C  C      . PRO B 1 185 ? 2.52600   -17.32000 -3.77000  1.000 41.28390 ? 181 PRO B C      1 
ATOM   5308 O  O      . PRO B 1 185 ? 2.02700   -16.21300 -4.01500  1.000 43.95527 ? 181 PRO B O      1 
ATOM   5309 C  CB     . PRO B 1 185 ? 1.85800   -18.40700 -1.59800  1.000 38.83360 ? 181 PRO B CB     1 
ATOM   5310 C  CG     . PRO B 1 185 ? 1.60900   -19.83000 -1.21200  1.000 35.40951 ? 181 PRO B CG     1 
ATOM   5311 C  CD     . PRO B 1 185 ? 2.14600   -20.66700 -2.35100  1.000 37.59661 ? 181 PRO B CD     1 
ATOM   5312 N  N      . MET B 1 186 ? 3.80000   -17.60100 -4.06200  1.000 39.87320 ? 182 MET B N      1 
ATOM   5313 C  CA     . MET B 1 186 ? 4.67100   -16.54700 -4.56200  1.000 39.80214 ? 182 MET B CA     1 
ATOM   5314 C  C      . MET B 1 186 ? 4.28900   -16.10500 -5.96800  1.000 38.88887 ? 182 MET B C      1 
ATOM   5315 O  O      . MET B 1 186 ? 4.64500   -14.99300 -6.37100  1.000 40.04954 ? 182 MET B O      1 
ATOM   5316 C  CB     . MET B 1 186 ? 6.12200   -17.01200 -4.53800  1.000 44.88959 ? 182 MET B CB     1 
ATOM   5317 C  CG     . MET B 1 186 ? 6.39700   -18.21500 -5.43200  1.000 57.59638 ? 182 MET B CG     1 
ATOM   5318 S  SD     . MET B 1 186 ? 8.12900   -18.36100 -5.94800  1.000 66.71326 ? 182 MET B SD     1 
ATOM   5319 C  CE     . MET B 1 186 ? 8.34000   -16.84400 -6.88000  1.000 61.08364 ? 182 MET B CE     1 
ATOM   5320 N  N      . ASN B 1 187 ? 3.51800   -16.91600 -6.69600  1.000 38.14142 ? 183 ASN B N      1 
ATOM   5321 C  CA     . ASN B 1 187 ? 3.13000   -16.58200 -8.06100  1.000 34.57520 ? 183 ASN B CA     1 
ATOM   5322 C  C      . ASN B 1 187 ? 2.00900   -15.55000 -8.14400  1.000 35.06736 ? 183 ASN B C      1 
ATOM   5323 O  O      . ASN B 1 187 ? 1.92000   -14.84900 -9.15900  1.000 36.58860 ? 183 ASN B O      1 
ATOM   5324 C  CB     . ASN B 1 187 ? 2.67700   -17.84400 -8.81000  1.000 41.84186 ? 183 ASN B CB     1 
ATOM   5325 C  CG     . ASN B 1 187 ? 3.84000   -18.66700 -9.33800  1.000 48.20841 ? 183 ASN B CG     1 
ATOM   5326 O  OD1    . ASN B 1 187 ? 3.70200   -19.85900 -9.61200  1.000 51.33773 ? 183 ASN B OD1    1 
ATOM   5327 N  ND2    . ASN B 1 187 ? 4.99300   -18.03200 -9.48000  1.000 49.14010 ? 183 ASN B ND2    1 
ATOM   5328 N  N      . TYR B 1 188 ? 1.16500   -15.41900 -7.11700  1.000 27.21905 ? 184 TYR B N      1 
ATOM   5329 C  CA     . TYR B 1 188 ? -0.01700  -14.56600 -7.22500  1.000 31.81171 ? 184 TYR B CA     1 
ATOM   5330 C  C      . TYR B 1 188 ? -0.10100  -13.49300 -6.14300  1.000 32.88026 ? 184 TYR B C      1 
ATOM   5331 O  O      . TYR B 1 188 ? -1.17000  -12.87600 -5.97100  1.000 31.49325 ? 184 TYR B O      1 
ATOM   5332 C  CB     . TYR B 1 188 ? -1.29800  -15.41300 -7.19900  1.000 29.01401 ? 184 TYR B CB     1 
ATOM   5333 C  CG     . TYR B 1 188 ? -1.44400  -16.31200 -5.98100  1.000 29.97991 ? 184 TYR B CG     1 
ATOM   5334 C  CD1    . TYR B 1 188 ? -2.02000  -15.83300 -4.80000  1.000 29.03243 ? 184 TYR B CD1    1 
ATOM   5335 C  CD2    . TYR B 1 188 ? -1.03100  -17.64200 -6.01900  1.000 29.16929 ? 184 TYR B CD2    1 
ATOM   5336 C  CE1    . TYR B 1 188 ? -2.16800  -16.65200 -3.68500  1.000 26.95323 ? 184 TYR B CE1    1 
ATOM   5337 C  CE2    . TYR B 1 188 ? -1.17000  -18.47000 -4.91700  1.000 31.16953 ? 184 TYR B CE2    1 
ATOM   5338 C  CZ     . TYR B 1 188 ? -1.74000  -17.97100 -3.75000  1.000 35.61743 ? 184 TYR B CZ     1 
ATOM   5339 O  OH     . TYR B 1 188 ? -1.87500  -18.78400 -2.64100  1.000 36.43858 ? 184 TYR B OH     1 
ATOM   5340 N  N      . ARG B 1 189 ? 0.97400   -13.26100 -5.40000  1.000 24.45030 ? 185 ARG B N      1 
ATOM   5341 C  CA     . ARG B 1 189 ? 1.04900   -12.10200 -4.52000  1.000 39.86794 ? 185 ARG B CA     1 
ATOM   5342 C  C      . ARG B 1 189 ? 2.50300   -11.68800 -4.39300  1.000 42.02609 ? 185 ARG B C      1 
ATOM   5343 O  O      . ARG B 1 189 ? 3.40200   -12.52100 -4.49100  1.000 42.24191 ? 185 ARG B O      1 
ATOM   5344 C  CB     . ARG B 1 189 ? 0.43400   -12.35300 -3.12900  1.000 33.88301 ? 185 ARG B CB     1 
ATOM   5345 C  CG     . ARG B 1 189 ? 0.86100   -13.60800 -2.36500  1.000 38.56778 ? 185 ARG B CG     1 
ATOM   5346 C  CD     . ARG B 1 189 ? -0.20600  -13.89300 -1.27900  1.000 36.09117 ? 185 ARG B CD     1 
ATOM   5347 N  NE     . ARG B 1 189 ? 0.10900   -14.99700 -0.36300  1.000 47.50833 ? 185 ARG B NE     1 
ATOM   5348 C  CZ     . ARG B 1 189 ? 0.96600   -14.91700 0.66000   1.000 50.24813 ? 185 ARG B CZ     1 
ATOM   5349 N  NH1    . ARG B 1 189 ? 1.61500   -13.78200 0.91000   1.000 44.51850 ? 185 ARG B NH1    1 
ATOM   5350 N  NH2    . ARG B 1 189 ? 1.17500   -15.97800 1.43800   1.000 49.76913 ? 185 ARG B NH2    1 
ATOM   5351 N  N      . GLY B 1 190 ? 2.71700   -10.38900 -4.17800  1.000 39.90215 ? 186 GLY B N      1 
ATOM   5352 C  CA     . GLY B 1 190 ? 4.03900   -9.80100  -4.19800  1.000 30.96950 ? 186 GLY B CA     1 
ATOM   5353 C  C      . GLY B 1 190 ? 4.67000   -9.72100  -2.82200  1.000 32.73814 ? 186 GLY B C      1 
ATOM   5354 O  O      . GLY B 1 190 ? 4.14100   -10.21200 -1.82500  1.000 37.11498 ? 186 GLY B O      1 
ATOM   5355 N  N      . GLY B 1 191 ? 5.84400   -9.10600  -2.78300  1.000 33.65404 ? 187 GLY B N      1 
ATOM   5356 C  CA     . GLY B 1 191 ? 6.59900   -8.96000  -1.55600  1.000 37.78085 ? 187 GLY B CA     1 
ATOM   5357 C  C      . GLY B 1 191 ? 6.16000   -7.75500  -0.74800  1.000 38.39934 ? 187 GLY B C      1 
ATOM   5358 O  O      . GLY B 1 191 ? 5.11300   -7.14600  -0.97800  1.000 36.52543 ? 187 GLY B O      1 
ATOM   5359 N  N      . LYS B 1 192 ? 6.99700   -7.40300  0.21600   1.000 32.48811 ? 188 LYS B N      1 
ATOM   5360 C  CA     . LYS B 1 192 ? 6.67900   -6.34900  1.16700   1.000 40.30746 ? 188 LYS B CA     1 
ATOM   5361 C  C      . LYS B 1 192 ? 7.39900   -5.06000  0.80200   1.000 35.09631 ? 188 LYS B C      1 
ATOM   5362 O  O      . LYS B 1 192 ? 8.52400   -5.10000  0.29100   1.000 36.47543 ? 188 LYS B O      1 
ATOM   5363 C  CB     . LYS B 1 192 ? 7.07800   -6.76300  2.59000   1.000 44.01580 ? 188 LYS B CB     1 
ATOM   5364 C  CG     . LYS B 1 192 ? 6.55800   -8.14400  2.98400   1.000 53.13532 ? 188 LYS B CG     1 
ATOM   5365 C  CD     . LYS B 1 192 ? 6.41200   -8.30900  4.49400   1.000 58.00432 ? 188 LYS B CD     1 
ATOM   5366 C  CE     . LYS B 1 192 ? 5.09400   -9.01000  4.83700   1.000 62.97860 ? 188 LYS B CE     1 
ATOM   5367 N  NZ     . LYS B 1 192 ? 4.53500   -8.52500  6.12500   1.000 64.74197 ? 188 LYS B NZ     1 
ATOM   5368 N  N      . PRO B 1 193 ? 6.78900   -3.90300  1.04500   1.000 30.14046 ? 189 PRO B N      1 
ATOM   5369 C  CA     . PRO B 1 193 ? 7.47200   -2.64200  0.74800   1.000 30.63525 ? 189 PRO B CA     1 
ATOM   5370 C  C      . PRO B 1 193 ? 8.55400   -2.33100  1.77800   1.000 34.21726 ? 189 PRO B C      1 
ATOM   5371 O  O      . PRO B 1 193 ? 8.44700   -2.66200  2.95900   1.000 30.46681 ? 189 PRO B O      1 
ATOM   5372 C  CB     . PRO B 1 193 ? 6.34000   -1.60900  0.79400   1.000 26.75321 ? 189 PRO B CB     1 
ATOM   5373 C  CG     . PRO B 1 193 ? 5.32900   -2.22100  1.71100   1.000 28.55869 ? 189 PRO B CG     1 
ATOM   5374 C  CD     . PRO B 1 193 ? 5.39200   -3.69800  1.46200   1.000 29.20350 ? 189 PRO B CD     1 
ATOM   5375 N  N      . ALA B 1 194 ? 9.61100   -1.68900  1.30300   1.000 32.10385 ? 190 ALA B N      1 
ATOM   5376 C  CA     . ALA B 1 194 ? 10.75400  -1.28200  2.09800   1.000 28.46657 ? 190 ALA B CA     1 
ATOM   5377 C  C      . ALA B 1 194 ? 10.85100  0.23800   2.13300   1.000 33.19082 ? 190 ALA B C      1 
ATOM   5378 O  O      . ALA B 1 194 ? 10.24000  0.92900   1.30700   1.000 32.23018 ? 190 ALA B O      1 
ATOM   5379 C  CB     . ALA B 1 194 ? 12.05200  -1.86500  1.51600   1.000 30.90371 ? 190 ALA B CB     1 
ATOM   5380 N  N      . PRO B 1 195 ? 11.61300  0.79400   3.06700   1.000 31.87224 ? 191 PRO B N      1 
ATOM   5381 C  CA     . PRO B 1 195 ? 11.84800  2.23900   3.06700   1.000 33.01975 ? 191 PRO B CA     1 
ATOM   5382 C  C      . PRO B 1 195 ? 12.83000  2.62400   1.96800   1.000 32.35388 ? 191 PRO B C      1 
ATOM   5383 O  O      . PRO B 1 195 ? 13.60200  1.80200   1.48300   1.000 33.77247 ? 191 PRO B O      1 
ATOM   5384 C  CB     . PRO B 1 195 ? 12.46100  2.48600   4.44600   1.000 32.68023 ? 191 PRO B CB     1 
ATOM   5385 C  CG     . PRO B 1 195 ? 13.24600  1.22200   4.68500   1.000 35.01999 ? 191 PRO B CG     1 
ATOM   5386 C  CD     . PRO B 1 195 ? 12.37400  0.11200   4.12800   1.000 30.54314 ? 191 PRO B CD     1 
ATOM   5387 N  N      . THR B 1 196 ? 12.78800  3.90100   1.58200   1.000 31.11952 ? 192 THR B N      1 
ATOM   5388 C  CA     . THR B 1 196 ? 13.74800  4.44300   0.62900   1.000 33.95933 ? 192 THR B CA     1 
ATOM   5389 C  C      . THR B 1 196 ? 15.07900  4.70000   1.32300   1.000 37.90718 ? 192 THR B C      1 
ATOM   5390 O  O      . THR B 1 196 ? 15.14600  4.83700   2.54700   1.000 34.10146 ? 192 THR B O      1 
ATOM   5391 C  CB     . THR B 1 196 ? 13.26200  5.75500   0.00500   1.000 37.65188 ? 192 THR B CB     1 
ATOM   5392 O  OG1    . THR B 1 196 ? 13.21700  6.76600   1.01600   1.000 38.68095 ? 192 THR B OG1    1 
ATOM   5393 C  CG2    . THR B 1 196 ? 11.87000  5.60200   -0.62800  1.000 35.57005 ? 192 THR B CG2    1 
ATOM   5394 N  N      . ILE B 1 197 ? 16.14200  4.71100   0.55100   1.000 33.73299 ? 193 ILE B N      1 
ATOM   5395 C  CA     . ILE B 1 197 ? 17.46500  4.98200   1.06100   1.000 38.21774 ? 193 ILE B CA     1 
ATOM   5396 C  C      . ILE B 1 197 ? 17.47600  6.29700   1.79600   1.000 39.13364 ? 193 ILE B C      1 
ATOM   5397 O  O      . ILE B 1 197 ? 17.97500  6.39700   2.86600   1.000 41.19968 ? 193 ILE B O      1 
ATOM   5398 C  CB     . ILE B 1 197 ? 18.50500  5.03200   -0.05300  1.000 47.90838 ? 193 ILE B CB     1 
ATOM   5399 C  CG1    . ILE B 1 197 ? 18.82700  3.65600   -0.55000  1.000 55.10924 ? 193 ILE B CG1    1 
ATOM   5400 C  CG2    . ILE B 1 197 ? 19.80500  5.53900   0.49300   1.000 48.70321 ? 193 ILE B CG2    1 
ATOM   5401 C  CD1    . ILE B 1 197 ? 19.31600  2.77200   0.56000   1.000 57.10948 ? 193 ILE B CD1    1 
ATOM   5402 N  N      . MET B 1 198 ? 16.84400  7.29100   1.22200   1.000 37.02286 ? 194 MET B N      1 
ATOM   5403 C  CA     . MET B 1 198 ? 16.77900  8.57200   1.84600   1.000 44.37374 ? 194 MET B CA     1 
ATOM   5404 C  C      . MET B 1 198 ? 16.16500  8.55900   3.23600   1.000 40.59697 ? 194 MET B C      1 
ATOM   5405 O  O      . MET B 1 198 ? 16.67400  9.17300   4.11000   1.000 40.81016 ? 194 MET B O      1 
ATOM   5406 C  CB     . MET B 1 198 ? 16.04400  9.53100   0.95000   1.000 59.81770 ? 194 MET B CB     1 
ATOM   5407 C  CG     . MET B 1 198 ? 15.98200  10.97200  1.42200   1.000 73.12982 ? 194 MET B CG     1 
ATOM   5408 S  SD     . MET B 1 198 ? 15.43500  12.04600  0.06600   1.000 81.84139 ? 194 MET B SD     1 
ATOM   5409 C  CE     . MET B 1 198 ? 14.61800  13.38100  0.90700   1.000 77.85144 ? 194 MET B CE     1 
ATOM   5410 N  N      . ASP B 1 199 ? 15.07300  7.86000   3.43200   1.000 29.89306 ? 195 ASP B N      1 
ATOM   5411 C  CA     . ASP B 1 199 ? 14.46700  7.86600   4.72600   1.000 35.80429 ? 195 ASP B CA     1 
ATOM   5412 C  C      . ASP B 1 199 ? 15.31300  7.13600   5.75100   1.000 37.03076 ? 195 ASP B C      1 
ATOM   5413 O  O      . ASP B 1 199 ? 15.40800  7.58100   6.84800   1.000 39.91268 ? 195 ASP B O      1 
ATOM   5414 C  CB     . ASP B 1 199 ? 13.03900  7.35600   4.68300   1.000 37.18341 ? 195 ASP B CB     1 
ATOM   5415 C  CG     . ASP B 1 199 ? 12.09800  8.32500   3.99400   1.000 52.15362 ? 195 ASP B CG     1 
ATOM   5416 O  OD1    . ASP B 1 199 ? 12.40800  9.51500   3.90600   1.000 55.61983 ? 195 ASP B OD1    1 
ATOM   5417 O  OD2    . ASP B 1 199 ? 11.06500  7.89400   3.50800   1.000 52.63526 ? 195 ASP B OD2    1 
ATOM   5418 N  N      . VAL B 1 200 ? 15.88100  6.00700   5.37700   1.000 32.26703 ? 196 VAL B N      1 
ATOM   5419 C  CA     . VAL B 1 200 ? 16.77300  5.27100   6.26500   1.000 35.38582 ? 196 VAL B CA     1 
ATOM   5420 C  C      . VAL B 1 200 ? 17.88100  6.19100   6.75600   1.000 38.62832 ? 196 VAL B C      1 
ATOM   5421 O  O      . VAL B 1 200 ? 18.09700  6.34200   7.96400   1.000 42.40772 ? 196 VAL B O      1 
ATOM   5422 C  CB     . VAL B 1 200 ? 17.35000  4.03400   5.55200   1.000 38.92835 ? 196 VAL B CB     1 
ATOM   5423 C  CG1    . VAL B 1 200 ? 18.44800  3.40100   6.40500   1.000 40.27851 ? 196 VAL B CG1    1 
ATOM   5424 C  CG2    . VAL B 1 200 ? 16.24300  3.02200   5.21300   1.000 31.40377 ? 196 VAL B CG2    1 
ATOM   5425 N  N      . VAL B 1 201 ? 18.56600  6.86000   5.82100   1.000 36.35962 ? 197 VAL B N      1 
ATOM   5426 C  CA     . VAL B 1 201 ? 19.66000  7.74700   6.20100   1.000 40.41537 ? 197 VAL B CA     1 
ATOM   5427 C  C      . VAL B 1 201 ? 19.14500  8.88300   7.06900   1.000 39.09153 ? 197 VAL B C      1 
ATOM   5428 O  O      . VAL B 1 201 ? 19.80100  9.30000   8.02900   1.000 37.64662 ? 197 VAL B O      1 
ATOM   5429 C  CB     . VAL B 1 201 ? 20.38700  8.28400   4.95300   1.000 44.53955 ? 197 VAL B CB     1 
ATOM   5430 C  CG1    . VAL B 1 201 ? 21.50900  9.20100   5.37200   1.000 44.67641 ? 197 VAL B CG1    1 
ATOM   5431 C  CG2    . VAL B 1 201 ? 20.92100  7.14000   4.13100   1.000 50.07442 ? 197 VAL B CG2    1 
ATOM   5432 N  N      . ARG B 1 202 ? 17.97400  9.41900   6.75000   1.000 34.78049 ? 198 ARG B N      1 
ATOM   5433 C  CA     . ARG B 1 202 ? 17.46500  10.49200  7.59400   1.000 43.21571 ? 198 ARG B CA     1 
ATOM   5434 C  C      . ARG B 1 202 ? 17.12600  10.01000  8.99800   1.000 41.45234 ? 198 ARG B C      1 
ATOM   5435 O  O      . ARG B 1 202 ? 17.37300  10.72700  9.97600   1.000 38.15194 ? 198 ARG B O      1 
ATOM   5436 C  CB     . ARG B 1 202 ? 16.29600  11.22200  6.93200   1.000 48.07945 ? 198 ARG B CB     1 
ATOM   5437 C  CG     . ARG B 1 202 ? 15.74500  12.20200  7.92500   1.000 60.12300 ? 198 ARG B CG     1 
ATOM   5438 C  CD     . ARG B 1 202 ? 16.38600  13.53700  7.59900   1.000 72.75872 ? 198 ARG B CD     1 
ATOM   5439 N  NE     . ARG B 1 202 ? 15.94000  14.61600  8.46500   1.000 78.08831 ? 198 ARG B NE     1 
ATOM   5440 C  CZ     . ARG B 1 202 ? 16.63700  15.72800  8.65800   1.000 84.51540 ? 198 ARG B CZ     1 
ATOM   5441 N  NH1    . ARG B 1 202 ? 17.83800  15.86800  8.10100   1.000 87.88422 ? 198 ARG B NH1    1 
ATOM   5442 N  NH2    . ARG B 1 202 ? 16.15400  16.68400  9.43700   1.000 85.49709 ? 198 ARG B NH2    1 
ATOM   5443 N  N      . VAL B 1 203 ? 16.54200  8.81500   9.11900   1.000 39.28103 ? 199 VAL B N      1 
ATOM   5444 C  CA     . VAL B 1 203 ? 16.24300  8.29200   10.45100  1.000 35.04894 ? 199 VAL B CA     1 
ATOM   5445 C  C      . VAL B 1 203 ? 17.53400  8.01500   11.21800  1.000 37.77821 ? 199 VAL B C      1 
ATOM   5446 O  O      . VAL B 1 203 ? 17.64900  8.34200   12.40600  1.000 36.58597 ? 199 VAL B O      1 
ATOM   5447 C  CB     . VAL B 1 203 ? 15.35600  7.04100   10.35900  1.000 35.50952 ? 199 VAL B CB     1 
ATOM   5448 C  CG1    . VAL B 1 203 ? 15.24000  6.34900   11.72200  1.000 31.34586 ? 199 VAL B CG1    1 
ATOM   5449 C  CG2    . VAL B 1 203 ? 13.95100  7.41000   9.83000   1.000 33.64351 ? 199 VAL B CG2    1 
ATOM   5450 N  N      . ALA B 1 204 ? 18.50600  7.42500   10.56200  1.000 36.91495 ? 200 ALA B N      1 
ATOM   5451 C  CA     . ALA B 1 204 ? 19.78500  7.13300   11.18000  1.000 43.53680 ? 200 ALA B CA     1 
ATOM   5452 C  C      . ALA B 1 204 ? 20.42000  8.40000   11.74500  1.000 46.18185 ? 200 ALA B C      1 
ATOM   5453 O  O      . ALA B 1 204 ? 20.84600  8.44200   12.84400  1.000 45.00803 ? 200 ALA B O      1 
ATOM   5454 C  CB     . ALA B 1 204 ? 20.71300  6.44800   10.21000  1.000 42.47351 ? 200 ALA B CB     1 
ATOM   5455 N  N      . GLU B 1 205 ? 20.40500  9.44800   10.96800  1.000 44.40006 ? 201 GLU B N      1 
ATOM   5456 C  CA     . GLU B 1 205 ? 20.94500  10.68100  11.40300  1.000 43.07885 ? 201 GLU B CA     1 
ATOM   5457 C  C      . GLU B 1 205 ? 20.18400  11.26800  12.56400  1.000 43.59470 ? 201 GLU B C      1 
ATOM   5458 O  O      . GLU B 1 205 ? 20.76300  11.84000  13.42100  1.000 47.40305 ? 201 GLU B O      1 
ATOM   5459 C  CB     . GLU B 1 205 ? 20.97400  11.64100  10.24400  1.000 48.76637 ? 201 GLU B CB     1 
ATOM   5460 C  CG     . GLU B 1 205 ? 21.01100  13.08900  10.63300  1.000 70.58215 ? 201 GLU B CG     1 
ATOM   5461 C  CD     . GLU B 1 205 ? 20.99400  14.01300  9.43300   1.000 86.72882 ? 201 GLU B CD     1 
ATOM   5462 O  OE1    . GLU B 1 205 ? 19.95000  14.63600  9.18500   1.000 91.24778 ? 201 GLU B OE1    1 
ATOM   5463 O  OE2    . GLU B 1 205 ? 22.01500  14.09900  8.73800   1.000 87.18940 ? 201 GLU B OE2    1 
ATOM   5464 N  N      . LEU B 1 206 ? 18.87800  11.13600  12.58900  1.000 42.50510 ? 202 LEU B N      1 
ATOM   5465 C  CA     . LEU B 1 206 ? 18.11700  11.68800  13.67600  1.000 41.86028 ? 202 LEU B CA     1 
ATOM   5466 C  C      . LEU B 1 206 ? 18.40600  10.93700  14.94400  1.000 43.78157 ? 202 LEU B C      1 
ATOM   5467 O  O      . LEU B 1 206 ? 18.43000  11.49400  15.98400  1.000 44.09476 ? 202 LEU B O      1 
ATOM   5468 C  CB     . LEU B 1 206 ? 16.63000  11.70800  13.37400  1.000 34.54362 ? 202 LEU B CB     1 
ATOM   5469 C  CG     . LEU B 1 206 ? 16.04400  12.81800  12.52200  1.000 38.25459 ? 202 LEU B CG     1 
ATOM   5470 C  CD1    . LEU B 1 206 ? 14.71900  12.38600  11.96300  1.000 35.02788 ? 202 LEU B CD1    1 
ATOM   5471 C  CD2    . LEU B 1 206 ? 15.90700  14.10900  13.27100  1.000 36.94917 ? 202 LEU B CD2    1 
ATOM   5472 N  N      . ILE B 1 207 ? 18.57900  9.64800   14.85000  1.000 40.45222 ? 203 ILE B N      1 
ATOM   5473 C  CA     . ILE B 1 207 ? 18.93000  8.88300   16.04300  1.000 41.71816 ? 203 ILE B CA     1 
ATOM   5474 C  C      . ILE B 1 207 ? 20.32600  9.25200   16.51600  1.000 44.79748 ? 203 ILE B C      1 
ATOM   5475 O  O      . ILE B 1 207 ? 20.56100  9.40500   17.71700  1.000 51.47722 ? 203 ILE B O      1 
ATOM   5476 C  CB     . ILE B 1 207 ? 18.82300  7.37600   15.78200  1.000 42.05767 ? 203 ILE B CB     1 
ATOM   5477 C  CG1    . ILE B 1 207 ? 17.38200  6.97400   15.49900  1.000 40.63908 ? 203 ILE B CG1    1 
ATOM   5478 C  CG2    . ILE B 1 207 ? 19.34300  6.59000   16.97000  1.000 44.16845 ? 203 ILE B CG2    1 
ATOM   5479 C  CD1    . ILE B 1 207 ? 17.27000  5.57500   14.95900  1.000 36.38594 ? 203 ILE B CD1    1 
ATOM   5480 N  N      . PHE B 1 208 ? 21.27100  9.40000   15.57800  1.000 40.94701 ? 204 PHE B N      1 
ATOM   5481 C  CA     . PHE B 1 208 ? 22.64700  9.70600   15.95300  1.000 49.28222 ? 204 PHE B CA     1 
ATOM   5482 C  C      . PHE B 1 208 ? 22.73700  10.98600  16.77600  1.000 48.54529 ? 204 PHE B C      1 
ATOM   5483 O  O      . PHE B 1 208 ? 23.57400  11.08900  17.67700  1.000 47.85047 ? 204 PHE B O      1 
ATOM   5484 C  CB     . PHE B 1 208 ? 23.52700  9.84700   14.70300  1.000 57.06737 ? 204 PHE B CB     1 
ATOM   5485 C  CG     . PHE B 1 208 ? 23.78700  8.55300   13.96400  1.000 64.74724 ? 204 PHE B CG     1 
ATOM   5486 C  CD1    . PHE B 1 208 ? 23.63600  7.32900   14.59300  1.000 64.09453 ? 204 PHE B CD1    1 
ATOM   5487 C  CD2    . PHE B 1 208 ? 24.19700  8.57100   12.63200  1.000 67.63706 ? 204 PHE B CD2    1 
ATOM   5488 C  CE1    . PHE B 1 208 ? 23.88100  6.14900   13.91000  1.000 65.63155 ? 204 PHE B CE1    1 
ATOM   5489 C  CE2    . PHE B 1 208 ? 24.44100  7.39100   11.94100  1.000 63.16810 ? 204 PHE B CE2    1 
ATOM   5490 C  CZ     . PHE B 1 208 ? 24.28400  6.18100   12.58300  1.000 64.52089 ? 204 PHE B CZ     1 
ATOM   5491 N  N      . HIS B 1 209 ? 21.87600  11.95700  16.49900  1.000 50.25076 ? 205 HIS B N      1 
ATOM   5492 C  CA     . HIS B 1 209 ? 21.93600  13.25300  17.15000  1.000 44.38953 ? 205 HIS B CA     1 
ATOM   5493 C  C      . HIS B 1 209 ? 20.91800  13.38700  18.27400  1.000 44.37901 ? 205 HIS B C      1 
ATOM   5494 O  O      . HIS B 1 209 ? 20.91700  14.40200  18.97100  1.000 47.20566 ? 205 HIS B O      1 
ATOM   5495 C  CB     . HIS B 1 209 ? 21.73700  14.36600  16.10900  1.000 47.12144 ? 205 HIS B CB     1 
ATOM   5496 C  CG     . HIS B 1 209 ? 22.82000  14.42600  15.06700  1.000 56.89366 ? 205 HIS B CG     1 
ATOM   5497 N  ND1    . HIS B 1 209 ? 24.16300  14.43800  15.38600  1.000 61.76530 ? 205 HIS B ND1    1 
ATOM   5498 C  CD2    . HIS B 1 209 ? 22.75900  14.48100  13.71400  1.000 57.94905 ? 205 HIS B CD2    1 
ATOM   5499 C  CE1    . HIS B 1 209 ? 24.88100  14.49800  14.27700  1.000 61.22839 ? 205 HIS B CE1    1 
ATOM   5500 N  NE2    . HIS B 1 209 ? 24.05300  14.52400  13.24800  1.000 62.23641 ? 205 HIS B NE2    1 
ATOM   5501 N  N      . ALA B 1 210 ? 20.06500  12.38300  18.48100  1.000 41.70237 ? 206 ALA B N      1 
ATOM   5502 C  CA     . ALA B 1 210 ? 19.00700  12.47800  19.47500  1.000 42.72091 ? 206 ALA B CA     1 
ATOM   5503 C  C      . ALA B 1 210 ? 19.56800  12.29600  20.87800  1.000 50.85347 ? 206 ALA B C      1 
ATOM   5504 O  O      . ALA B 1 210 ? 20.42000  11.43400  21.11900  1.000 55.10398 ? 206 ALA B O      1 
ATOM   5505 C  CB     . ALA B 1 210 ? 17.92800  11.42500  19.21700  1.000 35.62269 ? 206 ALA B CB     1 
ATOM   5506 N  N      . LYS B 1 211 ? 19.07700  13.10300  21.81300  1.000 48.27421 ? 207 LYS B N      1 
ATOM   5507 C  CA     . LYS B 1 211 ? 19.51800  12.98500  23.19300  1.000 48.73742 ? 207 LYS B CA     1 
ATOM   5508 C  C      . LYS B 1 211 ? 18.57200  12.16200  24.06800  1.000 48.71110 ? 207 LYS B C      1 
ATOM   5509 O  O      . LYS B 1 211 ? 19.02100  11.60300  25.07400  1.000 47.38463 ? 207 LYS B O      1 
ATOM   5510 C  CB     . LYS B 1 211 ? 19.74700  14.38200  23.78800  1.000 53.30376 ? 207 LYS B CB     1 
ATOM   5511 C  CG     . LYS B 1 211 ? 20.91700  15.14700  23.13200  1.000 61.60475 ? 207 LYS B CG     1 
ATOM   5512 C  CD     . LYS B 1 211 ? 22.28600  14.63100  23.59100  1.000 67.37650 ? 207 LYS B CD     1 
ATOM   5513 C  CE     . LYS B 1 211 ? 23.39500  15.66900  23.39200  1.000 74.73528 ? 207 LYS B CE     1 
ATOM   5514 N  NZ     . LYS B 1 211 ? 24.60400  15.13100  22.69100  1.000 76.71446 ? 207 LYS B NZ     1 
ATOM   5515 N  N      . ARG B 1 212 ? 17.29300  12.04200  23.70700  1.000 42.72618 ? 208 ARG B N      1 
ATOM   5516 C  CA     . ARG B 1 212 ? 16.35800  11.16200  24.41200  1.000 41.08914 ? 208 ARG B CA     1 
ATOM   5517 C  C      . ARG B 1 212 ? 15.37700  10.56400  23.41900  1.000 39.62054 ? 208 ARG B C      1 
ATOM   5518 O  O      . ARG B 1 212 ? 14.18900  10.92000  23.38400  1.000 36.98865 ? 208 ARG B O      1 
ATOM   5519 C  CB     . ARG B 1 212 ? 15.62800  11.88900  25.54300  1.000 46.08710 ? 208 ARG B CB     1 
ATOM   5520 C  CG     . ARG B 1 212 ? 15.31800  10.94200  26.71600  1.000 54.39073 ? 208 ARG B CG     1 
ATOM   5521 C  CD     . ARG B 1 212 ? 14.92600  11.67500  27.99100  1.000 64.14980 ? 208 ARG B CD     1 
ATOM   5522 N  NE     . ARG B 1 212 ? 14.97700  10.81700  29.18100  1.000 72.67977 ? 208 ARG B NE     1 
ATOM   5523 C  CZ     . ARG B 1 212 ? 13.91000  10.49400  29.91100  1.000 77.81196 ? 208 ARG B CZ     1 
ATOM   5524 N  NH1    . ARG B 1 212 ? 12.70700  10.94600  29.56400  1.000 77.02766 ? 208 ARG B NH1    1 
ATOM   5525 N  NH2    . ARG B 1 212 ? 14.03800  9.71200   30.97800  1.000 79.59375 ? 208 ARG B NH2    1 
ATOM   5526 N  N      . PRO B 1 213 ? 15.83400  9.64300   22.58400  1.000 38.87308 ? 209 PRO B N      1 
ATOM   5527 C  CA     . PRO B 1 213 ? 14.93600  8.99200   21.63700  1.000 35.59637 ? 209 PRO B CA     1 
ATOM   5528 C  C      . PRO B 1 213 ? 14.06500  7.96200   22.33900  1.000 35.09105 ? 209 PRO B C      1 
ATOM   5529 O  O      . PRO B 1 213 ? 14.38100  7.47000   23.41900  1.000 34.05408 ? 209 PRO B O      1 
ATOM   5530 C  CB     . PRO B 1 213 ? 15.90200  8.31700   20.65900  1.000 36.36489 ? 209 PRO B CB     1 
ATOM   5531 C  CG     . PRO B 1 213 ? 17.09100  7.96500   21.53300  1.000 38.03877 ? 209 PRO B CG     1 
ATOM   5532 C  CD     . PRO B 1 213 ? 17.20900  9.10500   22.52500  1.000 37.51239 ? 209 PRO B CD     1 
ATOM   5533 N  N      . ALA B 1 214 ? 12.95900  7.61300   21.68400  1.000 37.57556 ? 210 ALA B N      1 
ATOM   5534 C  CA     . ALA B 1 214 ? 12.08500  6.57500   22.20700  1.000 36.05695 ? 210 ALA B CA     1 
ATOM   5535 C  C      . ALA B 1 214 ? 11.39000  5.89000   21.04500  1.000 33.82511 ? 210 ALA B C      1 
ATOM   5536 O  O      . ALA B 1 214 ? 11.16500  6.49400   19.99300  1.000 32.84078 ? 210 ALA B O      1 
ATOM   5537 C  CB     . ALA B 1 214 ? 11.04600  7.13300   23.18400  1.000 36.34646 ? 210 ALA B CB     1 
ATOM   5538 N  N      . ILE B 1 215 ? 11.05000  4.62300   21.25300  1.000 32.41704 ? 211 ILE B N      1 
ATOM   5539 C  CA     . ILE B 1 215 ? 10.28400  3.83100   20.30200  1.000 32.43547 ? 211 ILE B CA     1 
ATOM   5540 C  C      . ILE B 1 215 ? 8.94000   3.51100   20.93300  1.000 37.22815 ? 211 ILE B C      1 
ATOM   5541 O  O      . ILE B 1 215 ? 8.87900   3.10900   22.10500  1.000 32.19333 ? 211 ILE B O      1 
ATOM   5542 C  CB     . ILE B 1 215 ? 11.01600  2.53200   19.92100  1.000 32.33019 ? 211 ILE B CB     1 
ATOM   5543 C  CG1    . ILE B 1 215 ? 12.33300  2.83700   19.21500  1.000 28.39288 ? 211 ILE B CG1    1 
ATOM   5544 C  CG2    . ILE B 1 215 ? 10.10700  1.62200   19.06300  1.000 27.10851 ? 211 ILE B CG2    1 
ATOM   5545 C  CD1    . ILE B 1 215 ? 13.32500  1.69000   19.28300  1.000 36.95180 ? 211 ILE B CD1    1 
ATOM   5546 N  N      . LEU B 1 216 ? 7.86400   3.71200   20.16500  1.000 30.35627 ? 212 LEU B N      1 
ATOM   5547 C  CA     . LEU B 1 216 ? 6.53300   3.22500   20.51000  1.000 28.07968 ? 212 LEU B CA     1 
ATOM   5548 C  C      . LEU B 1 216 ? 6.16800   2.16800   19.47600  1.000 32.35125 ? 212 LEU B C      1 
ATOM   5549 O  O      . LEU B 1 216 ? 5.91700   2.49200   18.30900  1.000 27.71122 ? 212 LEU B O      1 
ATOM   5550 C  CB     . LEU B 1 216 ? 5.50100   4.34900   20.53100  1.000 29.39563 ? 212 LEU B CB     1 
ATOM   5551 C  CG     . LEU B 1 216 ? 4.08300   3.88200   20.90500  1.000 30.02202 ? 212 LEU B CG     1 
ATOM   5552 C  CD1    . LEU B 1 216 ? 4.04700   3.20300   22.29500  1.000 36.97285 ? 212 LEU B CD1    1 
ATOM   5553 C  CD2    . LEU B 1 216 ? 3.09600   5.04500   20.85700  1.000 27.62436 ? 212 LEU B CD2    1 
ATOM   5554 N  N      . ALA B 1 217 ? 6.15900   0.90800   19.89800  1.000 28.89294 ? 213 ALA B N      1 
ATOM   5555 C  CA     . ALA B 1 217 ? 5.92700   -0.21100  18.99300  1.000 31.00635 ? 213 ALA B CA     1 
ATOM   5556 C  C      . ALA B 1 217 ? 4.50400   -0.70500  19.19000  1.000 32.31703 ? 213 ALA B C      1 
ATOM   5557 O  O      . ALA B 1 217 ? 4.06300   -0.89600  20.33200  1.000 26.17945 ? 213 ALA B O      1 
ATOM   5558 C  CB     . ALA B 1 217 ? 6.91300   -1.35500  19.24100  1.000 24.92667 ? 213 ALA B CB     1 
ATOM   5559 N  N      . GLY B 1 218 ? 3.77900   -0.86900  18.08100  1.000 27.44803 ? 214 GLY B N      1 
ATOM   5560 C  CA     . GLY B 1 218 ? 2.41200   -1.32700  18.10700  1.000 25.19249 ? 214 GLY B CA     1 
ATOM   5561 C  C      . GLY B 1 218 ? 2.23900   -2.73600  17.56200  1.000 25.78204 ? 214 GLY B C      1 
ATOM   5562 O  O      . GLY B 1 218 ? 3.19500   -3.47500  17.31100  1.000 28.14548 ? 214 GLY B O      1 
ATOM   5563 N  N      . HIS B 1 219 ? 0.97200   -3.10100  17.38600  1.000 21.69471 ? 215 HIS B N      1 
ATOM   5564 C  CA     . HIS B 1 219 ? 0.59500   -4.41600  16.88900  1.000 28.97453 ? 215 HIS B CA     1 
ATOM   5565 C  C      . HIS B 1 219 ? 1.18900   -4.72300  15.50900  1.000 28.12179 ? 215 HIS B C      1 
ATOM   5566 O  O      . HIS B 1 219 ? 1.31500   -5.90100  15.15800  1.000 25.79520 ? 215 HIS B O      1 
ATOM   5567 C  CB     . HIS B 1 219 ? -0.94100  -4.49300  16.85200  1.000 26.78479 ? 215 HIS B CB     1 
ATOM   5568 C  CG     . HIS B 1 219 ? -1.47800  -5.75600  16.26000  1.000 27.76122 ? 215 HIS B CG     1 
ATOM   5569 N  ND1    . HIS B 1 219 ? -1.15300  -7.00300  16.75100  1.000 27.54278 ? 215 HIS B ND1    1 
ATOM   5570 C  CD2    . HIS B 1 219 ? -2.33500  -5.96500  15.23200  1.000 26.39001 ? 215 HIS B CD2    1 
ATOM   5571 C  CE1    . HIS B 1 219 ? -1.76900  -7.93000  16.03700  1.000 26.30315 ? 215 HIS B CE1    1 
ATOM   5572 N  NE2    . HIS B 1 219 ? -2.49700  -7.32600  15.11100  1.000 30.33522 ? 215 HIS B NE2    1 
ATOM   5573 N  N      . GLY B 1 220 ? 1.54300   -3.69500  14.71700  1.000 25.20039 ? 216 GLY B N      1 
ATOM   5574 C  CA     . GLY B 1 220 ? 2.20000   -3.94100  13.43600  1.000 28.75345 ? 216 GLY B CA     1 
ATOM   5575 C  C      . GLY B 1 220 ? 3.47100   -4.76600  13.55600  1.000 32.65655 ? 216 GLY B C      1 
ATOM   5576 O  O      . GLY B 1 220 ? 3.86000   -5.46700  12.61300  1.000 29.02716 ? 216 GLY B O      1 
ATOM   5577 N  N      . ILE B 1 221 ? 4.15100   -4.67900  14.70400  1.000 29.82463 ? 217 ILE B N      1 
ATOM   5578 C  CA     . ILE B 1 221 ? 5.32700   -5.51600  14.92300  1.000 30.34838 ? 217 ILE B CA     1 
ATOM   5579 C  C      . ILE B 1 221 ? 4.95600   -6.98300  14.78300  1.000 25.87152 ? 217 ILE B C      1 
ATOM   5580 O  O      . ILE B 1 221 ? 5.68600   -7.76500  14.16900  1.000 26.38474 ? 217 ILE B O      1 
ATOM   5581 C  CB     . ILE B 1 221 ? 5.96300   -5.22700  16.29200  1.000 28.31392 ? 217 ILE B CB     1 
ATOM   5582 C  CG1    . ILE B 1 221 ? 6.52400   -3.80300  16.32600  1.000 29.81936 ? 217 ILE B CG1    1 
ATOM   5583 C  CG2    . ILE B 1 221 ? 7.06400   -6.25700  16.58500  1.000 25.81099 ? 217 ILE B CG2    1 
ATOM   5584 C  CD1    . ILE B 1 221 ? 7.75400   -3.60700  15.47500  1.000 27.11641 ? 217 ILE B CD1    1 
ATOM   5585 N  N      . GLU B 1 222 ? 3.80800   -7.38400  15.34800  1.000 24.68717 ? 218 GLU B N      1 
ATOM   5586 C  CA     . GLU B 1 222 ? 3.39000   -8.77300  15.20500  1.000 29.14823 ? 218 GLU B CA     1 
ATOM   5587 C  C      . GLU B 1 222 ? 3.01800   -9.07900  13.75900  1.000 32.55917 ? 218 GLU B C      1 
ATOM   5588 O  O      . GLU B 1 222 ? 3.38500   -10.13900 13.23100  1.000 26.54002 ? 218 GLU B O      1 
ATOM   5589 C  CB     . GLU B 1 222 ? 2.22200   -9.10300  16.13400  1.000 28.36393 ? 218 GLU B CB     1 
ATOM   5590 C  CG     . GLU B 1 222 ? 1.72200   -10.52100 15.89800  1.000 39.68897 ? 218 GLU B CG     1 
ATOM   5591 C  CD     . GLU B 1 222 ? 0.51400   -10.89400 16.72900  1.000 45.77917 ? 218 GLU B CD     1 
ATOM   5592 O  OE1    . GLU B 1 222 ? -0.58100  -11.01400 16.14600  1.000 46.75824 ? 218 GLU B OE1    1 
ATOM   5593 O  OE2    . GLU B 1 222 ? 0.66700   -11.09900 17.95200  1.000 53.95910 ? 218 GLU B OE2    1 
ATOM   5594 N  N      . CYS B 1 223 ? 2.29100   -8.16500  13.09800  1.000 25.65308 ? 219 CYS B N      1 
ATOM   5595 C  CA     . CYS B 1 223 ? 1.88700   -8.44000  11.72700  1.000 29.12981 ? 219 CYS B CA     1 
ATOM   5596 C  C      . CYS B 1 223 ? 3.09700   -8.59900  10.82600  1.000 32.31177 ? 219 CYS B C      1 
ATOM   5597 O  O      . CYS B 1 223 ? 3.09800   -9.44100  9.93200   1.000 33.54876 ? 219 CYS B O      1 
ATOM   5598 C  CB     . CYS B 1 223 ? 1.03000   -7.28500  11.17900  1.000 30.38785 ? 219 CYS B CB     1 
ATOM   5599 S  SG     . CYS B 1 223 ? -0.52200  -6.93200  12.05000  1.000 33.41190 ? 219 CYS B SG     1 
ATOM   5600 N  N      . ALA B 1 224 ? 4.15700   -7.86400  11.11900  1.000 30.30100 ? 220 ALA B N      1 
ATOM   5601 C  CA     . ALA B 1 224 ? 5.37700   -7.92300  10.33300  1.000 30.38522 ? 220 ALA B CA     1 
ATOM   5602 C  C      . ALA B 1 224 ? 6.33900   -8.99500  10.80900  1.000 26.56371 ? 220 ALA B C      1 
ATOM   5603 O  O      . ALA B 1 224 ? 7.39000   -9.18100  10.18200  1.000 36.23066 ? 220 ALA B O      1 
ATOM   5604 C  CB     . ALA B 1 224 ? 6.08400   -6.55900  10.36500  1.000 33.81984 ? 220 ALA B CB     1 
ATOM   5605 N  N      . LYS B 1 225 ? 6.00000   -9.69800  11.88700  1.000 28.02968 ? 221 LYS B N      1 
ATOM   5606 C  CA     . LYS B 1 225 ? 6.88300   -10.67300 12.50600  1.000 30.42733 ? 221 LYS B CA     1 
ATOM   5607 C  C      . LYS B 1 225 ? 8.26700   -10.06400 12.74100  1.000 32.87499 ? 221 LYS B C      1 
ATOM   5608 O  O      . LYS B 1 225 ? 9.29400   -10.65100 12.40800  1.000 33.70141 ? 221 LYS B O      1 
ATOM   5609 C  CB     . LYS B 1 225 ? 6.97600   -11.94500 11.64700  1.000 30.59841 ? 221 LYS B CB     1 
ATOM   5610 C  CG     . LYS B 1 225 ? 5.63000   -12.64600 11.41800  1.000 35.03841 ? 221 LYS B CG     1 
ATOM   5611 C  CD     . LYS B 1 225 ? 5.71900   -13.67500 10.29000  1.000 40.21008 ? 221 LYS B CD     1 
ATOM   5612 C  CE     . LYS B 1 225 ? 4.41900   -14.47500 10.13100  1.000 51.57987 ? 221 LYS B CE     1 
ATOM   5613 N  NZ     . LYS B 1 225 ? 3.43700   -13.85000 9.18400   1.000 52.35891 ? 221 LYS B NZ     1 
ATOM   5614 N  N      . ALA B 1 226 ? 8.28700   -8.86000  13.32100  1.000 30.32732 ? 222 ALA B N      1 
ATOM   5615 C  CA     . ALA B 1 226 ? 9.50800   -8.07000  13.40100  1.000 27.32696 ? 222 ALA B CA     1 
ATOM   5616 C  C      . ALA B 1 226 ? 10.10900  -8.05500  14.80300  1.000 31.04056 ? 222 ALA B C      1 
ATOM   5617 O  O      . ALA B 1 226 ? 10.88000  -7.15100  15.13000  1.000 30.24836 ? 222 ALA B O      1 
ATOM   5618 C  CB     . ALA B 1 226 ? 9.24900   -6.64600  12.90700  1.000 26.46107 ? 222 ALA B CB     1 
ATOM   5619 N  N      . TRP B 1 227 ? 9.78600   -9.05000  15.63200  1.000 31.15637 ? 223 TRP B N      1 
ATOM   5620 C  CA     . TRP B 1 227 ? 10.25400  -9.05100  17.02000  1.000 33.60403 ? 223 TRP B CA     1 
ATOM   5621 C  C      . TRP B 1 227 ? 11.77200  -9.03200  17.10400  1.000 36.11749 ? 223 TRP B C      1 
ATOM   5622 O  O      . TRP B 1 227 ? 12.34800  -8.24700  17.86800  1.000 35.74902 ? 223 TRP B O      1 
ATOM   5623 C  CB     . TRP B 1 227 ? 9.72100   -10.27800 17.76500  1.000 33.69615 ? 223 TRP B CB     1 
ATOM   5624 C  CG     . TRP B 1 227 ? 8.24800   -10.36400 17.78800  1.000 32.09595 ? 223 TRP B CG     1 
ATOM   5625 C  CD1    . TRP B 1 227 ? 7.40400   -9.62700  18.55400  1.000 30.76421 ? 223 TRP B CD1    1 
ATOM   5626 C  CD2    . TRP B 1 227 ? 7.43000   -11.25200 17.02000  1.000 32.74077 ? 223 TRP B CD2    1 
ATOM   5627 N  NE1    . TRP B 1 227 ? 6.10300   -9.99200  18.31500  1.000 29.32983 ? 223 TRP B NE1    1 
ATOM   5628 C  CE2    . TRP B 1 227 ? 6.08900   -10.99000 17.37400  1.000 34.76996 ? 223 TRP B CE2    1 
ATOM   5629 C  CE3    . TRP B 1 227 ? 7.69900   -12.23900 16.06400  1.000 33.74615 ? 223 TRP B CE3    1 
ATOM   5630 C  CZ2    . TRP B 1 227 ? 5.01300   -11.68500 16.80900  1.000 34.93577 ? 223 TRP B CZ2    1 
ATOM   5631 C  CZ3    . TRP B 1 227 ? 6.62700   -12.92600 15.49700  1.000 32.01173 ? 223 TRP B CZ3    1 
ATOM   5632 C  CH2    . TRP B 1 227 ? 5.30300   -12.64500 15.87200  1.000 30.94845 ? 223 TRP B CH2    1 
ATOM   5633 N  N      . GLU B 1 228 ? 12.44500  -9.89800  16.33500  1.000 34.54888 ? 224 GLU B N      1 
ATOM   5634 C  CA     . GLU B 1 228 ? 13.90000  -10.00900 16.48400  1.000 32.52232 ? 224 GLU B CA     1 
ATOM   5635 C  C      . GLU B 1 228 ? 14.61200  -8.78300  15.92100  1.000 35.07526 ? 224 GLU B C      1 
ATOM   5636 O  O      . GLU B 1 228 ? 15.62100  -8.33400  16.48600  1.000 39.47579 ? 224 GLU B O      1 
ATOM   5637 C  CB     . GLU B 1 228 ? 14.41400  -11.28800 15.81400  1.000 43.81315 ? 224 GLU B CB     1 
ATOM   5638 C  CG     . GLU B 1 228 ? 15.95600  -11.41100 15.74700  1.000 66.23689 ? 224 GLU B CG     1 
ATOM   5639 C  CD     . GLU B 1 228 ? 16.43600  -12.83600 15.45700  1.000 79.43058 ? 224 GLU B CD     1 
ATOM   5640 O  OE1    . GLU B 1 228 ? 17.67200  -13.03300 15.35600  1.000 83.93638 ? 224 GLU B OE1    1 
ATOM   5641 O  OE2    . GLU B 1 228 ? 15.59600  -13.75300 15.33600  1.000 83.68635 ? 224 GLU B OE2    1 
ATOM   5642 N  N      . GLU B 1 229 ? 14.08400  -8.19200  14.84900  1.000 37.59924 ? 225 GLU B N      1 
ATOM   5643 C  CA     . GLU B 1 229 ? 14.67400  -6.96700  14.30700  1.000 42.36034 ? 225 GLU B CA     1 
ATOM   5644 C  C      . GLU B 1 229 ? 14.47100  -5.78300  15.25000  1.000 37.18077 ? 225 GLU B C      1 
ATOM   5645 O  O      . GLU B 1 229 ? 15.38600  -4.97300  15.44800  1.000 31.46430 ? 225 GLU B O      1 
ATOM   5646 C  CB     . GLU B 1 229 ? 14.06300  -6.66100  12.93600  1.000 42.56300 ? 225 GLU B CB     1 
ATOM   5647 C  CG     . GLU B 1 229 ? 14.42600  -7.66200  11.85300  1.000 50.78767 ? 225 GLU B CG     1 
ATOM   5648 C  CD     . GLU B 1 229 ? 13.46800  -8.84300  11.78100  1.000 59.27816 ? 225 GLU B CD     1 
ATOM   5649 O  OE1    . GLU B 1 229 ? 12.62500  -9.01100  12.69200  1.000 61.23366 ? 225 GLU B OE1    1 
ATOM   5650 O  OE2    . GLU B 1 229 ? 13.57300  -9.61600  10.80900  1.000 65.42890 ? 225 GLU B OE2    1 
ATOM   5651 N  N      . LEU B 1 230 ? 13.28800  -5.67700  15.86000  1.000 32.03016 ? 226 LEU B N      1 
ATOM   5652 C  CA     . LEU B 1 230 ? 13.06100  -4.61200  16.82900  1.000 31.81697 ? 226 LEU B CA     1 
ATOM   5653 C  C      . LEU B 1 230 ? 14.01900  -4.73500  18.00900  1.000 33.64877 ? 226 LEU B C      1 
ATOM   5654 O  O      . LEU B 1 230 ? 14.58700  -3.73700  18.46700  1.000 36.18065 ? 226 LEU B O      1 
ATOM   5655 C  CB     . LEU B 1 230 ? 11.60600  -4.63500  17.30100  1.000 27.76386 ? 226 LEU B CB     1 
ATOM   5656 C  CG     . LEU B 1 230 ? 11.23200  -3.59500  18.35900  1.000 35.55426 ? 226 LEU B CG     1 
ATOM   5657 C  CD1    . LEU B 1 230 ? 11.46500  -2.18000  17.83800  1.000 31.19058 ? 226 LEU B CD1    1 
ATOM   5658 C  CD2    . LEU B 1 230 ? 9.79300   -3.77500  18.85600  1.000 26.70847 ? 226 LEU B CD2    1 
ATOM   5659 N  N      . LEU B 1 231 ? 14.24500  -5.92700  18.49400  1.000 35.38582 ? 227 LEU B N      1 
ATOM   5660 C  CA     . LEU B 1 231 ? 15.13600  -6.11800  19.61100  1.000 33.06712 ? 227 LEU B CA     1 
ATOM   5661 C  C      . LEU B 1 231 ? 16.56400  -5.74800  19.24900  1.000 33.44612 ? 227 LEU B C      1 
ATOM   5662 O  O      . LEU B 1 231 ? 17.20400  -5.04800  19.95500  1.000 35.13579 ? 227 LEU B O      1 
ATOM   5663 C  CB     . LEU B 1 231 ? 15.04800  -7.54300  20.14200  1.000 37.99666 ? 227 LEU B CB     1 
ATOM   5664 C  CG     . LEU B 1 231 ? 15.99400  -7.99000  21.26300  1.000 44.28952 ? 227 LEU B CG     1 
ATOM   5665 C  CD1    . LEU B 1 231 ? 15.93700  -7.10800  22.47000  1.000 40.97070 ? 227 LEU B CD1    1 
ATOM   5666 C  CD2    . LEU B 1 231 ? 15.78300  -9.43700  21.63600  1.000 40.38379 ? 227 LEU B CD2    1 
ATOM   5667 N  N      . ASP B 1 232 ? 17.01400  -6.23000  18.09400  1.000 35.70691 ? 228 ASP B N      1 
ATOM   5668 C  CA     . ASP B 1 232 ? 18.35300  -5.93300  17.61100  1.000 41.38128 ? 228 ASP B CA     1 
ATOM   5669 C  C      . ASP B 1 232 ? 18.50900  -4.42500  17.46400  1.000 35.44372 ? 228 ASP B C      1 
ATOM   5670 O  O      . ASP B 1 232 ? 19.50500  -3.85000  17.90200  1.000 36.60439 ? 228 ASP B O      1 
ATOM   5671 C  CB     . ASP B 1 232 ? 18.60800  -6.62400  16.27100  1.000 53.98542 ? 228 ASP B CB     1 
ATOM   5672 C  CG     . ASP B 1 232 ? 20.08100  -6.69200  15.92100  1.000 79.64639 ? 228 ASP B CG     1 
ATOM   5673 O  OD1    . ASP B 1 232 ? 20.91800  -6.43700  16.81300  1.000 87.31047 ? 228 ASP B OD1    1 
ATOM   5674 O  OD2    . ASP B 1 232 ? 20.40300  -7.00100  14.75400  1.000 86.61302 ? 228 ASP B OD2    1 
ATOM   5675 N  N      . PHE B 1 233 ? 17.51900  -3.78600  16.84400  1.000 41.27600 ? 229 PHE B N      1 
ATOM   5676 C  CA     . PHE B 1 233 ? 17.55400  -2.35800  16.66700  1.000 39.98374 ? 229 PHE B CA     1 
ATOM   5677 C  C      . PHE B 1 233 ? 17.58600  -1.63200  17.98700  1.000 39.17575 ? 229 PHE B C      1 
ATOM   5678 O  O      . PHE B 1 233 ? 18.33200  -0.71900  18.15400  1.000 36.91758 ? 229 PHE B O      1 
ATOM   5679 C  CB     . PHE B 1 233 ? 16.36500  -1.88700  15.87300  1.000 36.03853 ? 229 PHE B CB     1 
ATOM   5680 C  CG     . PHE B 1 233 ? 16.32000  -0.42600  15.65100  1.000 36.78862 ? 229 PHE B CG     1 
ATOM   5681 C  CD1    . PHE B 1 233 ? 17.23200  0.18900   14.85900  1.000 37.03865 ? 229 PHE B CD1    1 
ATOM   5682 C  CD2    . PHE B 1 233 ? 15.35800  0.31700   16.21900  1.000 40.49959 ? 229 PHE B CD2    1 
ATOM   5683 C  CE1    . PHE B 1 233 ? 17.18300  1.52600   14.64600  1.000 40.75225 ? 229 PHE B CE1    1 
ATOM   5684 C  CE2    . PHE B 1 233 ? 15.30000  1.65300   16.01300  1.000 40.56276 ? 229 PHE B CE2    1 
ATOM   5685 C  CZ     . PHE B 1 233 ? 16.21600  2.26200   15.22500  1.000 39.93900 ? 229 PHE B CZ     1 
ATOM   5686 N  N      . ALA B 1 234 ? 16.76000  -2.02700  18.92300  1.000 40.02059 ? 230 ALA B N      1 
ATOM   5687 C  CA     . ALA B 1 234 ? 16.76200  -1.34300  20.21200  1.000 37.73610 ? 230 ALA B CA     1 
ATOM   5688 C  C      . ALA B 1 234 ? 18.10100  -1.49000  20.91900  1.000 41.16020 ? 230 ALA B C      1 
ATOM   5689 O  O      . ALA B 1 234 ? 18.58900  -0.53300  21.53100  1.000 40.24693 ? 230 ALA B O      1 
ATOM   5690 C  CB     . ALA B 1 234 ? 15.63100  -1.87500  21.09700  1.000 38.75465 ? 230 ALA B CB     1 
ATOM   5691 N  N      . GLU B 1 235 ? 18.72000  -2.67600  20.83600  1.000 39.15733 ? 231 GLU B N      1 
ATOM   5692 C  CA     . GLU B 1 235 ? 19.99900  -2.89700  21.51400  1.000 44.49481 ? 231 GLU B CA     1 
ATOM   5693 C  C      . GLU B 1 235 ? 21.14800  -2.16900  20.82000  1.000 49.17958 ? 231 GLU B C      1 
ATOM   5694 O  O      . GLU B 1 235 ? 22.07100  -1.67400  21.48700  1.000 41.93134 ? 231 GLU B O      1 
ATOM   5695 C  CB     . GLU B 1 235 ? 20.30100  -4.39300  21.59800  1.000 42.88146 ? 231 GLU B CB     1 
ATOM   5696 C  CG     . GLU B 1 235 ? 19.35900  -5.15900  22.50800  1.000 45.98446 ? 231 GLU B CG     1 
ATOM   5697 C  CD     . GLU B 1 235 ? 19.64700  -6.64600  22.53100  1.000 47.04775 ? 231 GLU B CD     1 
ATOM   5698 O  OE1    . GLU B 1 235 ? 19.17500  -7.33200  23.46100  1.000 51.19035 ? 231 GLU B OE1    1 
ATOM   5699 O  OE2    . GLU B 1 235 ? 20.34100  -7.13400  21.61700  1.000 52.46155 ? 231 GLU B OE2    1 
ATOM   5700 N  N      . LEU B 1 236 ? 21.13900  -2.14900  19.48100  1.000 45.52651 ? 232 LEU B N      1 
ATOM   5701 C  CA     . LEU B 1 236 ? 22.19700  -1.48500  18.72200  1.000 44.90802 ? 232 LEU B CA     1 
ATOM   5702 C  C      . LEU B 1 236 ? 22.24200  0.00800   19.01500  1.000 44.94749 ? 232 LEU B C      1 
ATOM   5703 O  O      . LEU B 1 236 ? 23.31600  0.61900   19.00600  1.000 43.57101 ? 232 LEU B O      1 
ATOM   5704 C  CB     . LEU B 1 236 ? 21.99500  -1.73100  17.22900  1.000 40.94965 ? 232 LEU B CB     1 
ATOM   5705 C  CG     . LEU B 1 236 ? 22.88200  -0.91600  16.28400  1.000 43.67103 ? 232 LEU B CG     1 
ATOM   5706 C  CD1    . LEU B 1 236 ? 24.33300  -1.37700  16.30700  1.000 35.55426 ? 232 LEU B CD1    1 
ATOM   5707 C  CD2    . LEU B 1 236 ? 22.31000  -0.97800  14.86700  1.000 39.52053 ? 232 LEU B CD2    1 
ATOM   5708 N  N      . THR B 1 237 ? 21.07900  0.62200   19.23400  1.000 42.94725 ? 233 THR B N      1 
ATOM   5709 C  CA     . THR B 1 237 ? 20.98700  2.06400   19.41800  1.000 39.64160 ? 233 THR B CA     1 
ATOM   5710 C  C      . THR B 1 237 ? 20.87000  2.49300   20.87100  1.000 37.38080 ? 233 THR B C      1 
ATOM   5711 O  O      . THR B 1 237 ? 21.07100  3.67500   21.16200  1.000 42.23927 ? 233 THR B O      1 
ATOM   5712 C  CB     . THR B 1 237 ? 19.76500  2.62100   18.67800  1.000 37.66504 ? 233 THR B CB     1 
ATOM   5713 O  OG1    . THR B 1 237 ? 18.57700  1.99300   19.18600  1.000 39.44157 ? 233 THR B OG1    1 
ATOM   5714 C  CG2    . THR B 1 237 ? 19.87500  2.36300   17.18600  1.000 36.09643 ? 233 THR B CG2    1 
ATOM   5715 N  N      . GLY B 1 238 ? 20.53600  1.58100   21.78200  1.000 42.95778 ? 234 GLY B N      1 
ATOM   5716 C  CA     . GLY B 1 238 ? 20.21300  1.99000   23.13600  1.000 39.48105 ? 234 GLY B CA     1 
ATOM   5717 C  C      . GLY B 1 238 ? 18.89000  2.71800   23.29500  1.000 42.88672 ? 234 GLY B C      1 
ATOM   5718 O  O      . GLY B 1 238 ? 18.68100  3.37700   24.31500  1.000 47.37147 ? 234 GLY B O      1 
ATOM   5719 N  N      . ILE B 1 239 ? 17.98800  2.62900   22.32400  1.000 38.86782 ? 235 ILE B N      1 
ATOM   5720 C  CA     . ILE B 1 239 ? 16.72400  3.37200   22.39800  1.000 35.77008 ? 235 ILE B CA     1 
ATOM   5721 C  C      . ILE B 1 239 ? 15.71600  2.57100   23.22100  1.000 34.31464 ? 235 ILE B C      1 
ATOM   5722 O  O      . ILE B 1 239 ? 15.49100  1.38600   22.93000  1.000 32.04068 ? 235 ILE B O      1 
ATOM   5723 C  CB     . ILE B 1 239 ? 16.18700  3.66500   21.00100  1.000 36.57807 ? 235 ILE B CB     1 
ATOM   5724 C  CG1    . ILE B 1 239 ? 17.14900  4.58500   20.24500  1.000 36.87021 ? 235 ILE B CG1    1 
ATOM   5725 C  CG2    . ILE B 1 239 ? 14.81100  4.31100   21.08200  1.000 35.58058 ? 235 ILE B CG2    1 
ATOM   5726 C  CD1    . ILE B 1 239 ? 16.83700  4.70500   18.77300  1.000 37.39396 ? 235 ILE B CD1    1 
ATOM   5727 N  N      . PRO B 1 240 ? 15.11800  3.15800   24.25500  1.000 34.36465 ? 236 PRO B N      1 
ATOM   5728 C  CA     . PRO B 1 240 ? 14.09300  2.43500   25.02100  1.000 38.49672 ? 236 PRO B CA     1 
ATOM   5729 C  C      . PRO B 1 240 ? 12.80100  2.26700   24.23200  1.000 41.40496 ? 236 PRO B C      1 
ATOM   5730 O  O      . PRO B 1 240 ? 12.46600  3.06300   23.34700  1.000 39.45473 ? 236 PRO B O      1 
ATOM   5731 C  CB     . PRO B 1 240 ? 13.88900  3.30200   26.26900  1.000 37.72821 ? 236 PRO B CB     1 
ATOM   5732 C  CG     . PRO B 1 240 ? 14.51200  4.63200   25.94500  1.000 41.06019 ? 236 PRO B CG     1 
ATOM   5733 C  CD     . PRO B 1 240 ? 15.53600  4.41900   24.89500  1.000 33.95933 ? 236 PRO B CD     1 
ATOM   5734 N  N      . VAL B 1 241 ? 12.07000  1.20500   24.56900  1.000 33.46717 ? 237 VAL B N      1 
ATOM   5735 C  CA     . VAL B 1 241 ? 10.93800  0.74300   23.77300  1.000 33.54876 ? 237 VAL B CA     1 
ATOM   5736 C  C      . VAL B 1 241 ? 9.71000   0.64100   24.66600  1.000 34.31201 ? 237 VAL B C      1 
ATOM   5737 O  O      . VAL B 1 241 ? 9.69500   -0.14300  25.62500  1.000 33.28557 ? 237 VAL B O      1 
ATOM   5738 C  CB     . VAL B 1 241 ? 11.24000  -0.61300  23.10700  1.000 28.68502 ? 237 VAL B CB     1 
ATOM   5739 C  CG1    . VAL B 1 241 ? 10.00000  -1.18100  22.42400  1.000 27.72964 ? 237 VAL B CG1    1 
ATOM   5740 C  CG2    . VAL B 1 241 ? 12.41100  -0.46400  22.12200  1.000 29.39037 ? 237 VAL B CG2    1 
ATOM   5741 N  N      . ALA B 1 242 ? 8.68400   1.42400   24.34900  1.000 32.57496 ? 238 ALA B N      1 
ATOM   5742 C  CA     . ALA B 1 242 ? 7.34300   1.21200   24.87300  1.000 29.82463 ? 238 ALA B CA     1 
ATOM   5743 C  C      . ALA B 1 242 ? 6.51000   0.49800   23.82200  1.000 30.08519 ? 238 ALA B C      1 
ATOM   5744 O  O      . ALA B 1 242 ? 6.80300   0.57100   22.62600  1.000 30.42996 ? 238 ALA B O      1 
ATOM   5745 C  CB     . ALA B 1 242 ? 6.66900   2.53400   25.24000  1.000 27.14536 ? 238 ALA B CB     1 
ATOM   5746 N  N      . THR B 1 243 ? 5.48300   -0.21800  24.27300  1.000 26.60582 ? 239 THR B N      1 
ATOM   5747 C  CA     . THR B 1 243 ? 4.49100   -0.74600  23.35200  1.000 33.81721 ? 239 THR B CA     1 
ATOM   5748 C  C      . THR B 1 243 ? 3.13700   -0.11300  23.63800  1.000 33.53560 ? 239 THR B C      1 
ATOM   5749 O  O      . THR B 1 243 ? 2.90200   0.45500   24.71200  1.000 28.79819 ? 239 THR B O      1 
ATOM   5750 C  CB     . THR B 1 243 ? 4.36100   -2.28000  23.41900  1.000 34.74890 ? 239 THR B CB     1 
ATOM   5751 O  OG1    . THR B 1 243 ? 3.72500   -2.66200  24.65000  1.000 34.69627 ? 239 THR B OG1    1 
ATOM   5752 C  CG2    . THR B 1 243 ? 5.73200   -2.95100  23.29000  1.000 25.32409 ? 239 THR B CG2    1 
ATOM   5753 N  N      . THR B 1 244 ? 2.26700   -0.18400  22.62800  1.000 23.80812 ? 240 THR B N      1 
ATOM   5754 C  CA     . THR B 1 244 ? 0.86300   0.08900   22.82200  1.000 23.32122 ? 240 THR B CA     1 
ATOM   5755 C  C      . THR B 1 244 ? 0.25400   -1.05400  23.62300  1.000 27.90071 ? 240 THR B C      1 
ATOM   5756 O  O      . THR B 1 244 ? 0.86700   -2.11300  23.76600  1.000 28.74029 ? 240 THR B O      1 
ATOM   5757 C  CB     . THR B 1 244 ? 0.12900   0.20500   21.49100  1.000 25.72414 ? 240 THR B CB     1 
ATOM   5758 O  OG1    . THR B 1 244 ? 0.15000   -1.07500  20.84000  1.000 24.50294 ? 240 THR B OG1    1 
ATOM   5759 C  CG2    . THR B 1 244 ? 0.76500   1.27000   20.59000  1.000 22.82116 ? 240 THR B CG2    1 
ATOM   5760 N  N      . PRO B 1 245 ? -0.95400  -0.86700  24.15800  1.000 25.18197 ? 241 PRO B N      1 
ATOM   5761 C  CA     . PRO B 1 245 ? -1.60500  -1.98400  24.85000  1.000 27.07693 ? 241 PRO B CA     1 
ATOM   5762 C  C      . PRO B 1 245 ? -1.72000  -3.23500  23.99100  1.000 31.20637 ? 241 PRO B C      1 
ATOM   5763 O  O      . PRO B 1 245 ? -1.32600  -4.32300  24.43200  1.000 26.09787 ? 241 PRO B O      1 
ATOM   5764 C  CB     . PRO B 1 245 ? -2.96400  -1.39000  25.22900  1.000 26.49791 ? 241 PRO B CB     1 
ATOM   5765 C  CG     . PRO B 1 245 ? -2.65500  0.05100   25.45000  1.000 30.14835 ? 241 PRO B CG     1 
ATOM   5766 C  CD     . PRO B 1 245 ? -1.68300  0.40000   24.36000  1.000 26.00049 ? 241 PRO B CD     1 
ATOM   5767 N  N      . LYS B 1 246 ? -2.23800  -3.11100  22.76700  1.000 25.47148 ? 242 LYS B N      1 
ATOM   5768 C  CA     . LYS B 1 246 ? -2.37600  -4.29100  21.92300  1.000 24.79771 ? 242 LYS B CA     1 
ATOM   5769 C  C      . LYS B 1 246 ? -1.01800  -4.80800  21.47200  1.000 28.74555 ? 242 LYS B C      1 
ATOM   5770 O  O      . LYS B 1 246 ? -0.85700  -6.01000  21.23100  1.000 30.63788 ? 242 LYS B O      1 
ATOM   5771 C  CB     . LYS B 1 246 ? -3.26500  -3.97600  20.71200  1.000 26.85585 ? 242 LYS B CB     1 
ATOM   5772 C  CG     . LYS B 1 246 ? -3.71700  -5.23000  19.95600  1.000 32.83025 ? 242 LYS B CG     1 
ATOM   5773 C  CD     . LYS B 1 246 ? -4.91600  -4.95500  19.05000  1.000 37.42291 ? 242 LYS B CD     1 
ATOM   5774 C  CE     . LYS B 1 246 ? -4.50200  -4.22300  17.77500  1.000 36.34910 ? 242 LYS B CE     1 
ATOM   5775 N  NZ     . LYS B 1 246 ? -5.66500  -3.57700  17.06300  1.000 36.50174 ? 242 LYS B NZ     1 
ATOM   5776 N  N      . GLY B 1 247 ? -0.03400  -3.92300  21.35400  1.000 25.68466 ? 243 GLY B N      1 
ATOM   5777 C  CA     . GLY B 1 247 ? 1.30200   -4.31700  20.98300  1.000 24.19237 ? 243 GLY B CA     1 
ATOM   5778 C  C      . GLY B 1 247 ? 2.10000   -4.95700  22.10100  1.000 24.01341 ? 243 GLY B C      1 
ATOM   5779 O  O      . GLY B 1 247 ? 3.25800   -5.30400  21.89100  1.000 30.97477 ? 243 GLY B O      1 
ATOM   5780 N  N      . LYS B 1 248 ? 1.52100   -5.14800  23.26900  1.000 28.17443 ? 244 LYS B N      1 
ATOM   5781 C  CA     . LYS B 1 248 ? 2.17800   -5.83500  24.36800  1.000 28.97979 ? 244 LYS B CA     1 
ATOM   5782 C  C      . LYS B 1 248 ? 2.63100   -7.21800  23.89300  1.000 31.34850 ? 244 LYS B C      1 
ATOM   5783 O  O      . LYS B 1 248 ? 1.88500   -7.93200  23.25000  1.000 30.17467 ? 244 LYS B O      1 
ATOM   5784 C  CB     . LYS B 1 248 ? 1.29500   -5.92600  25.60500  1.000 36.80968 ? 244 LYS B CB     1 
ATOM   5785 C  CG     . LYS B 1 248 ? 1.96600   -6.38900  26.88600  1.000 29.17981 ? 244 LYS B CG     1 
ATOM   5786 C  CD     . LYS B 1 248 ? 0.94400   -6.69000  27.94600  1.000 30.60893 ? 244 LYS B CD     1 
ATOM   5787 C  CE     . LYS B 1 248 ? 1.50000   -7.09700  29.29200  1.000 26.57950 ? 244 LYS B CE     1 
ATOM   5788 N  NZ     . LYS B 1 248 ? 2.33700   -6.09300  29.95900  1.000 31.48009 ? 244 LYS B NZ     1 
ATOM   5789 N  N      . SER B 1 249 ? 3.89000   -7.48400  24.22300  1.000 31.92751 ? 245 SER B N      1 
ATOM   5790 C  CA     . SER B 1 249 ? 4.76000   -8.62300  23.89000  1.000 33.33821 ? 245 SER B CA     1 
ATOM   5791 C  C      . SER B 1 249 ? 5.56400   -8.42200  22.62300  1.000 32.33282 ? 245 SER B C      1 
ATOM   5792 O  O      . SER B 1 249 ? 6.17300   -9.31900  22.16500  1.000 29.18508 ? 245 SER B O      1 
ATOM   5793 C  CB     . SER B 1 249 ? 4.15600   -10.02200 23.96300  1.000 30.04834 ? 245 SER B CB     1 
ATOM   5794 O  OG     . SER B 1 249 ? 3.30200   -10.23900 22.89500  1.000 35.79903 ? 245 SER B OG     1 
ATOM   5795 N  N      . SER B 1 250 ? 5.52700   -7.23700  22.05200  1.000 28.99558 ? 246 SER B N      1 
ATOM   5796 C  CA     . SER B 1 250 ? 6.32400   -6.96000  20.88300  1.000 30.67210 ? 246 SER B CA     1 
ATOM   5797 C  C      . SER B 1 250 ? 7.76600   -6.79700  21.28100  1.000 33.17503 ? 246 SER B C      1 
ATOM   5798 O  O      . SER B 1 250 ? 8.60000   -6.88600  20.47000  1.000 35.74376 ? 246 SER B O      1 
ATOM   5799 C  CB     . SER B 1 250 ? 5.94700   -5.68300  20.19700  1.000 28.55869 ? 246 SER B CB     1 
ATOM   5800 O  OG     . SER B 1 250 ? 4.63400   -5.70600  19.79400  1.000 47.56623 ? 246 SER B OG     1 
ATOM   5801 N  N      . PHE B 1 251 ? 8.01400   -6.53100  22.54800  1.000 33.48823 ? 247 PHE B N      1 
ATOM   5802 C  CA     . PHE B 1 251 ? 9.33900   -6.31700  23.09600  1.000 32.83288 ? 247 PHE B CA     1 
ATOM   5803 C  C      . PHE B 1 251 ? 9.38600   -6.93800  24.48900  1.000 36.98865 ? 247 PHE B C      1 
ATOM   5804 O  O      . PHE B 1 251 ? 8.41800   -6.79700  25.25600  1.000 33.25399 ? 247 PHE B O      1 
ATOM   5805 C  CB     . PHE B 1 251 ? 9.64500   -4.81100  23.16100  1.000 33.28294 ? 247 PHE B CB     1 
ATOM   5806 C  CG     . PHE B 1 251 ? 11.07000  -4.49300  23.49600  1.000 34.81733 ? 247 PHE B CG     1 
ATOM   5807 C  CD1    . PHE B 1 251 ? 12.03900  -4.48500  22.51000  1.000 31.07478 ? 247 PHE B CD1    1 
ATOM   5808 C  CD2    . PHE B 1 251 ? 11.44200  -4.20000  24.80000  1.000 32.42757 ? 247 PHE B CD2    1 
ATOM   5809 C  CE1    . PHE B 1 251 ? 13.35900  -4.19300  22.81500  1.000 30.88265 ? 247 PHE B CE1    1 
ATOM   5810 C  CE2    . PHE B 1 251 ? 12.76800  -3.91500  25.11200  1.000 38.47567 ? 247 PHE B CE2    1 
ATOM   5811 C  CZ     . PHE B 1 251 ? 13.72300  -3.91400  24.11900  1.000 32.70392 ? 247 PHE B CZ     1 
ATOM   5812 N  N      . PRO B 1 252 ? 10.47700  -7.61900  24.85500  1.000 38.15457 ? 248 PRO B N      1 
ATOM   5813 C  CA     . PRO B 1 252 ? 10.50300  -8.31500  26.15800  1.000 40.27325 ? 248 PRO B CA     1 
ATOM   5814 C  C      . PRO B 1 252 ? 10.41600  -7.31400  27.30000  1.000 39.36788 ? 248 PRO B C      1 
ATOM   5815 O  O      . PRO B 1 252 ? 11.22300  -6.38800  27.40300  1.000 38.02035 ? 248 PRO B O      1 
ATOM   5816 C  CB     . PRO B 1 252 ? 11.84800  -9.06000  26.15200  1.000 38.53357 ? 248 PRO B CB     1 
ATOM   5817 C  CG     . PRO B 1 252 ? 12.64100  -8.47100  25.05600  1.000 38.57831 ? 248 PRO B CG     1 
ATOM   5818 C  CD     . PRO B 1 252 ? 11.70800  -7.83100  24.07100  1.000 30.20625 ? 248 PRO B CD     1 
ATOM   5819 N  N      . GLU B 1 253 ? 9.40500   -7.48600  28.15200  1.000 36.63597 ? 249 GLU B N      1 
ATOM   5820 C  CA     . GLU B 1 253 ? 9.15500   -6.49200  29.18600  1.000 35.65691 ? 249 GLU B CA     1 
ATOM   5821 C  C      . GLU B 1 253 ? 10.12600  -6.59600  30.35800  1.000 39.50737 ? 249 GLU B C      1 
ATOM   5822 O  O      . GLU B 1 253 ? 10.15200  -5.69000  31.19900  1.000 40.20482 ? 249 GLU B O      1 
ATOM   5823 C  CB     . GLU B 1 253 ? 7.70700   -6.59900  29.66700  1.000 34.57783 ? 249 GLU B CB     1 
ATOM   5824 C  CG     . GLU B 1 253 ? 6.71300   -5.98500  28.67900  1.000 37.11498 ? 249 GLU B CG     1 
ATOM   5825 C  CD     . GLU B 1 253 ? 5.27500   -5.93100  29.21000  1.000 45.38439 ? 249 GLU B CD     1 
ATOM   5826 O  OE1    . GLU B 1 253 ? 4.90600   -6.77500  30.06600  1.000 49.06641 ? 249 GLU B OE1    1 
ATOM   5827 O  OE2    . GLU B 1 253 ? 4.50300   -5.04900  28.76700  1.000 44.00264 ? 249 GLU B OE2    1 
ATOM   5828 N  N      . ASN B 1 254 ? 10.94100  -7.65100  30.41200  1.000 34.95156 ? 250 ASN B N      1 
ATOM   5829 C  CA     . ASN B 1 254 ? 12.02400  -7.76800  31.37900  1.000 43.07095 ? 250 ASN B CA     1 
ATOM   5830 C  C      . ASN B 1 254 ? 13.33100  -7.19200  30.85800  1.000 44.93960 ? 250 ASN B C      1 
ATOM   5831 O  O      . ASN B 1 254 ? 14.32600  -7.18500  31.59000  1.000 43.37099 ? 250 ASN B O      1 
ATOM   5832 C  CB     . ASN B 1 254 ? 12.23600  -9.24000  31.77500  1.000 41.66552 ? 250 ASN B CB     1 
ATOM   5833 C  CG     . ASN B 1 254 ? 12.45500  -10.15000 30.57100  1.000 51.40880 ? 250 ASN B CG     1 
ATOM   5834 O  OD1    . ASN B 1 254 ? 11.99100  -9.86900  29.46500  1.000 55.57508 ? 250 ASN B OD1    1 
ATOM   5835 N  ND2    . ASN B 1 254 ? 13.15300  -11.25200 30.78700  1.000 59.85981 ? 250 ASN B ND2    1 
ATOM   5836 N  N      . HIS B 1 255 ? 13.35600  -6.68900  29.63100  1.000 42.27875 ? 251 HIS B N      1 
ATOM   5837 C  CA     . HIS B 1 255 ? 14.59000  -6.16200  29.07100  1.000 37.16235 ? 251 HIS B CA     1 
ATOM   5838 C  C      . HIS B 1 255 ? 14.90200  -4.79900  29.67900  1.000 36.87021 ? 251 HIS B C      1 
ATOM   5839 O  O      . HIS B 1 255 ? 14.00400  -4.03300  30.03500  1.000 40.79700 ? 251 HIS B O      1 
ATOM   5840 C  CB     . HIS B 1 255 ? 14.45800  -6.05900  27.55000  1.000 38.99941 ? 251 HIS B CB     1 
ATOM   5841 C  CG     . HIS B 1 255 ? 15.74700  -5.79700  26.84600  1.000 38.96520 ? 251 HIS B CG     1 
ATOM   5842 N  ND1    . HIS B 1 255 ? 16.37900  -4.57500  26.88800  1.000 40.50486 ? 251 HIS B ND1    1 
ATOM   5843 C  CD2    . HIS B 1 255 ? 16.52400  -6.59900  26.08000  1.000 41.19441 ? 251 HIS B CD2    1 
ATOM   5844 C  CE1    . HIS B 1 255 ? 17.49800  -4.63700  26.18800  1.000 44.77905 ? 251 HIS B CE1    1 
ATOM   5845 N  NE2    . HIS B 1 255 ? 17.60600  -5.85200  25.68100  1.000 43.52890 ? 251 HIS B NE2    1 
ATOM   5846 N  N      . ALA B 1 256 ? 16.19100  -4.49000  29.79100  1.000 35.69902 ? 252 ALA B N      1 
ATOM   5847 C  CA     . ALA B 1 256 ? 16.58400  -3.22700  30.40300  1.000 34.20936 ? 252 ALA B CA     1 
ATOM   5848 C  C      . ALA B 1 256 ? 16.08200  -2.01800  29.62100  1.000 38.41776 ? 252 ALA B C      1 
ATOM   5849 O  O      . ALA B 1 256 ? 15.94100  -0.93700  30.19900  1.000 43.83683 ? 252 ALA B O      1 
ATOM   5850 C  CB     . ALA B 1 256 ? 18.11700  -3.16200  30.53000  1.000 35.29634 ? 252 ALA B CB     1 
ATOM   5851 N  N      . LEU B 1 257 ? 15.81500  -2.16500  28.32800  1.000 37.27815 ? 253 LEU B N      1 
ATOM   5852 C  CA     . LEU B 1 257 ? 15.34600  -1.05700  27.50200  1.000 37.38080 ? 253 LEU B CA     1 
ATOM   5853 C  C      . LEU B 1 257 ? 13.83000  -0.96800  27.43200  1.000 37.37553 ? 253 LEU B C      1 
ATOM   5854 O  O      . LEU B 1 257 ? 13.30600  -0.11400  26.71000  1.000 34.38570 ? 253 LEU B O      1 
ATOM   5855 C  CB     . LEU B 1 257 ? 15.92000  -1.18000  26.08600  1.000 36.93601 ? 253 LEU B CB     1 
ATOM   5856 C  CG     . LEU B 1 257 ? 17.43900  -1.00600  25.97600  1.000 39.60738 ? 253 LEU B CG     1 
ATOM   5857 C  CD1    . LEU B 1 257 ? 17.89700  -1.32700  24.57100  1.000 41.65236 ? 253 LEU B CD1    1 
ATOM   5858 C  CD2    . LEU B 1 257 ? 17.86100  0.40700   26.37200  1.000 33.70141 ? 253 LEU B CD2    1 
ATOM   5859 N  N      . SER B 1 258 ? 13.10700  -1.81000  28.16400  1.000 38.28354 ? 254 SER B N      1 
ATOM   5860 C  CA     . SER B 1 258 ? 11.65900  -1.83000  28.04900  1.000 34.31464 ? 254 SER B CA     1 
ATOM   5861 C  C      . SER B 1 258 ? 11.05700  -0.78000  28.96400  1.000 34.61731 ? 254 SER B C      1 
ATOM   5862 O  O      . SER B 1 258 ? 11.38900  -0.72200  30.15600  1.000 38.77833 ? 254 SER B O      1 
ATOM   5863 C  CB     . SER B 1 258 ? 11.10200  -3.21300  28.39400  1.000 37.23341 ? 254 SER B CB     1 
ATOM   5864 O  OG     . SER B 1 258 ? 9.73000   -3.11400  28.74700  1.000 42.65248 ? 254 SER B OG     1 
ATOM   5865 N  N      . LEU B 1 259 ? 10.20300  0.07300   28.40100  1.000 32.15122 ? 255 LEU B N      1 
ATOM   5866 C  CA     . LEU B 1 259 ? 9.41200   1.04100   29.14700  1.000 38.80728 ? 255 LEU B CA     1 
ATOM   5867 C  C      . LEU B 1 259 ? 8.07700   0.47300   29.59400  1.000 37.54661 ? 255 LEU B C      1 
ATOM   5868 O  O      . LEU B 1 259 ? 7.34300   1.14300   30.32500  1.000 39.71529 ? 255 LEU B O      1 
ATOM   5869 C  CB     . LEU B 1 259 ? 9.15600   2.29800   28.29600  1.000 37.92034 ? 255 LEU B CB     1 
ATOM   5870 C  CG     . LEU B 1 259 ? 10.39800  3.07000   27.85500  1.000 37.50186 ? 255 LEU B CG     1 
ATOM   5871 C  CD1    . LEU B 1 259 ? 10.08900  4.05500   26.72200  1.000 32.70655 ? 255 LEU B CD1    1 
ATOM   5872 C  CD2    . LEU B 1 259 ? 11.02800  3.77800   29.04600  1.000 38.02561 ? 255 LEU B CD2    1 
ATOM   5873 N  N      . GLY B 1 260 ? 7.74200   -0.73400  29.16500  1.000 33.76194 ? 256 GLY B N      1 
ATOM   5874 C  CA     . GLY B 1 260 ? 6.42600   -1.25100  29.42400  1.000 29.86937 ? 256 GLY B CA     1 
ATOM   5875 C  C      . GLY B 1 260 ? 5.43700   -0.70300  28.40800  1.000 33.54086 ? 256 GLY B C      1 
ATOM   5876 O  O      . GLY B 1 260 ? 5.79100   -0.30000  27.29600  1.000 30.57998 ? 256 GLY B O      1 
ATOM   5877 N  N      . VAL B 1 261 ? 4.18200   -0.67200  28.81500  1.000 34.96998 ? 257 VAL B N      1 
ATOM   5878 C  CA     . VAL B 1 261 ? 3.08100   -0.29500  27.94100  1.000 26.07418 ? 257 VAL B CA     1 
ATOM   5879 C  C      . VAL B 1 261 ? 2.79100   1.17700   28.14700  1.000 28.84293 ? 257 VAL B C      1 
ATOM   5880 O  O      . VAL B 1 261 ? 2.63800   1.62500   29.29000  1.000 26.81111 ? 257 VAL B O      1 
ATOM   5881 C  CB     . VAL B 1 261 ? 1.83400   -1.14600  28.23300  1.000 31.30639 ? 257 VAL B CB     1 
ATOM   5882 C  CG1    . VAL B 1 261 ? 0.60500   -0.63300  27.43200  1.000 29.92990 ? 257 VAL B CG1    1 
ATOM   5883 C  CG2    . VAL B 1 261 ? 2.12200   -2.61900  27.93700  1.000 29.63513 ? 257 VAL B CG2    1 
ATOM   5884 N  N      . PHE B 1 262 ? 2.69000   1.92300   27.04800  1.000 30.85370 ? 258 PHE B N      1 
ATOM   5885 C  CA     . PHE B 1 262 ? 2.17000   3.28300   27.06200  1.000 33.70930 ? 258 PHE B CA     1 
ATOM   5886 C  C      . PHE B 1 262 ? 0.68800   3.29500   26.67800  1.000 32.34862 ? 258 PHE B C      1 
ATOM   5887 O  O      . PHE B 1 262 ? 0.28900   2.67600   25.68500  1.000 36.13591 ? 258 PHE B O      1 
ATOM   5888 C  CB     . PHE B 1 262 ? 2.95400   4.18600   26.11100  1.000 35.69902 ? 258 PHE B CB     1 
ATOM   5889 C  CG     . PHE B 1 262 ? 2.38100   5.56400   26.01300  1.000 38.20195 ? 258 PHE B CG     1 
ATOM   5890 C  CD1    . PHE B 1 262 ? 2.49400   6.44700   27.08100  1.000 31.14058 ? 258 PHE B CD1    1 
ATOM   5891 C  CD2    . PHE B 1 262 ? 1.66500   5.95300   24.88700  1.000 33.89091 ? 258 PHE B CD2    1 
ATOM   5892 C  CE1    . PHE B 1 262 ? 1.93700   7.71500   27.01200  1.000 37.90454 ? 258 PHE B CE1    1 
ATOM   5893 C  CE2    . PHE B 1 262 ? 1.10600   7.21800   24.80300  1.000 35.31739 ? 258 PHE B CE2    1 
ATOM   5894 C  CZ     . PHE B 1 262 ? 1.24000   8.10400   25.87300  1.000 38.72833 ? 258 PHE B CZ     1 
ATOM   5895 N  N      . GLY B 1 263 ? -0.12300  4.01400   27.45200  1.000 28.42446 ? 259 GLY B N      1 
ATOM   5896 C  CA     . GLY B 1 263 ? -1.53000  4.15700   27.13300  1.000 25.46095 ? 259 GLY B CA     1 
ATOM   5897 C  C      . GLY B 1 263 ? -2.44500  3.46300   28.12500  1.000 34.35149 ? 259 GLY B C      1 
ATOM   5898 O  O      . GLY B 1 263 ? -2.09500  3.28500   29.29600  1.000 38.64937 ? 259 GLY B O      1 
ATOM   5899 N  N      . PHE B 1 264 ? -3.58600  2.98600   27.65200  1.000 29.76146 ? 260 PHE B N      1 
ATOM   5900 C  CA     . PHE B 1 264 ? -4.59500  2.47600   28.56500  1.000 35.46741 ? 260 PHE B CA     1 
ATOM   5901 C  C      . PHE B 1 264 ? -4.03300  1.33800   29.41800  1.000 29.72462 ? 260 PHE B C      1 
ATOM   5902 O  O      . PHE B 1 264 ? -3.45900  0.38200   28.89700  1.000 29.85095 ? 260 PHE B O      1 
ATOM   5903 C  CB     . PHE B 1 264 ? -5.81600  2.00600   27.76700  1.000 35.95694 ? 260 PHE B CB     1 
ATOM   5904 C  CG     . PHE B 1 264 ? -6.96600  1.59200   28.62200  1.000 39.77319 ? 260 PHE B CG     1 
ATOM   5905 C  CD1    . PHE B 1 264 ? -7.69000  2.53400   29.33000  1.000 45.40018 ? 260 PHE B CD1    1 
ATOM   5906 C  CD2    . PHE B 1 264 ? -7.31200  0.25500   28.74000  1.000 41.37338 ? 260 PHE B CD2    1 
ATOM   5907 C  CE1    . PHE B 1 264 ? -8.75200  2.15400   30.12200  1.000 50.11390 ? 260 PHE B CE1    1 
ATOM   5908 C  CE2    . PHE B 1 264 ? -8.36800  -0.13100  29.53600  1.000 44.36321 ? 260 PHE B CE2    1 
ATOM   5909 C  CZ     . PHE B 1 264 ? -9.09100  0.82100   30.22800  1.000 47.14513 ? 260 PHE B CZ     1 
ATOM   5910 N  N      . ALA B 1 265 ? -4.21800  1.44000   30.73300  1.000 30.09308 ? 261 ALA B N      1 
ATOM   5911 C  CA     . ALA B 1 265 ? -3.72300  0.45800   31.70400  1.000 32.06963 ? 261 ALA B CA     1 
ATOM   5912 C  C      . ALA B 1 265 ? -2.20000  0.32600   31.69700  1.000 32.58812 ? 261 ALA B C      1 
ATOM   5913 O  O      . ALA B 1 265 ? -1.65100  -0.66800  32.19600  1.000 35.03841 ? 261 ALA B O      1 
ATOM   5914 C  CB     . ALA B 1 265 ? -4.36500  -0.91400  31.46000  1.000 27.08219 ? 261 ALA B CB     1 
ATOM   5915 N  N      . GLY B 1 266 ? -1.50800  1.33000   31.18100  1.000 33.07765 ? 262 GLY B N      1 
ATOM   5916 C  CA     . GLY B 1 266 ? -0.07900  1.26400   31.00000  1.000 27.44803 ? 262 GLY B CA     1 
ATOM   5917 C  C      . GLY B 1 266 ? 0.69900   1.54500   32.26900  1.000 37.29395 ? 262 GLY B C      1 
ATOM   5918 O  O      . GLY B 1 266 ? 0.16500   1.64200   33.37800  1.000 36.10959 ? 262 GLY B O      1 
ATOM   5919 N  N      . HIS B 1 267 ? 2.00400   1.70300   32.08100  1.000 33.15398 ? 263 HIS B N      1 
ATOM   5920 C  CA     . HIS B 1 267 ? 2.94400   1.80700   33.18100  1.000 35.05157 ? 263 HIS B CA     1 
ATOM   5921 C  C      . HIS B 1 267 ? 3.44200   3.23000   33.32300  1.000 35.98063 ? 263 HIS B C      1 
ATOM   5922 O  O      . HIS B 1 267 ? 3.66700   3.92600   32.32600  1.000 32.88552 ? 263 HIS B O      1 
ATOM   5923 C  CB     . HIS B 1 267 ? 4.10000   0.84000   32.96800  1.000 32.77761 ? 263 HIS B CB     1 
ATOM   5924 C  CG     . HIS B 1 267 ? 3.63500   -0.57100  32.85900  1.000 38.29407 ? 263 HIS B CG     1 
ATOM   5925 N  ND1    . HIS B 1 267 ? 3.46800   -1.20600  31.64800  1.000 34.42255 ? 263 HIS B ND1    1 
ATOM   5926 C  CD2    . HIS B 1 267 ? 3.20600   -1.43900  33.80800  1.000 34.40939 ? 263 HIS B CD2    1 
ATOM   5927 C  CE1    . HIS B 1 267 ? 2.99000   -2.42000  31.85900  1.000 38.06509 ? 263 HIS B CE1    1 
ATOM   5928 N  NE2    . HIS B 1 267 ? 2.82700   -2.58800  33.16100  1.000 35.64112 ? 263 HIS B NE2    1 
ATOM   5929 N  N      . GLN B 1 268 ? 3.59700   3.64900   34.58000  1.000 36.85442 ? 264 GLN B N      1 
ATOM   5930 C  CA     . GLN B 1 268 ? 4.10400   4.98500   34.86900  1.000 40.04427 ? 264 GLN B CA     1 
ATOM   5931 C  C      . GLN B 1 268 ? 5.45500   5.20200   34.20500  1.000 37.26499 ? 264 GLN B C      1 
ATOM   5932 O  O      . GLN B 1 268 ? 5.76600   6.30900   33.75200  1.000 43.57891 ? 264 GLN B O      1 
ATOM   5933 C  CB     . GLN B 1 268 ? 4.22200   5.18600   36.38200  1.000 42.94989 ? 264 GLN B CB     1 
ATOM   5934 C  CG     . GLN B 1 268 ? 4.17600   6.64400   36.81000  1.000 48.80848 ? 264 GLN B CG     1 
ATOM   5935 C  CD     . GLN B 1 268 ? 2.85000   7.29000   36.47500  1.000 56.96209 ? 264 GLN B CD     1 
ATOM   5936 O  OE1    . GLN B 1 268 ? 1.79200   6.75900   36.81100  1.000 63.32865 ? 264 GLN B OE1    1 
ATOM   5937 N  NE2    . GLN B 1 268 ? 2.89600   8.44000   35.81000  1.000 58.66756 ? 264 GLN B NE2    1 
ATOM   5938 N  N      . LYS B 1 269 ? 6.27800   4.15300   34.15700  1.000 38.80992 ? 265 LYS B N      1 
ATOM   5939 C  CA     . LYS B 1 269 ? 7.57200   4.23000   33.48000  1.000 39.93374 ? 265 LYS B CA     1 
ATOM   5940 C  C      . LYS B 1 269 ? 7.42300   4.72800   32.04500  1.000 40.79173 ? 265 LYS B C      1 
ATOM   5941 O  O      . LYS B 1 269 ? 8.18000   5.59300   31.59500  1.000 33.98829 ? 265 LYS B O      1 
ATOM   5942 C  CB     . LYS B 1 269 ? 8.23700   2.85600   33.50400  1.000 40.05217 ? 265 LYS B CB     1 
ATOM   5943 C  CG     . LYS B 1 269 ? 9.64100   2.81600   32.97400  1.000 44.00264 ? 265 LYS B CG     1 
ATOM   5944 C  CD     . LYS B 1 269 ? 10.22900  1.43700   33.22900  1.000 48.35580 ? 265 LYS B CD     1 
ATOM   5945 C  CE     . LYS B 1 269 ? 11.71600  1.38900   32.94500  1.000 51.41406 ? 265 LYS B CE     1 
ATOM   5946 N  NZ     . LYS B 1 269 ? 12.17700  -0.03200  32.88800  1.000 55.27242 ? 265 LYS B NZ     1 
ATOM   5947 N  N      . ALA B 1 270 ? 6.45100   4.18500   31.30100  1.000 34.00671 ? 266 ALA B N      1 
ATOM   5948 C  CA     . ALA B 1 270 ? 6.26200   4.65100   29.93100  1.000 36.98075 ? 266 ALA B CA     1 
ATOM   5949 C  C      . ALA B 1 270 ? 5.63500   6.03900   29.90300  1.000 37.74400 ? 266 ALA B C      1 
ATOM   5950 O  O      . ALA B 1 270 ? 6.05700   6.90100   29.12100  1.000 37.64662 ? 266 ALA B O      1 
ATOM   5951 C  CB     . ALA B 1 270 ? 5.39800   3.66100   29.13400  1.000 30.61420 ? 266 ALA B CB     1 
ATOM   5952 N  N      . THR B 1 271 ? 4.64800   6.28700   30.76700  1.000 40.15745 ? 267 THR B N      1 
ATOM   5953 C  CA     . THR B 1 271 ? 4.00100   7.59600   30.78400  1.000 43.18676 ? 267 THR B CA     1 
ATOM   5954 C  C      . THR B 1 271 ? 5.01800   8.69900   31.05600  1.000 43.94474 ? 267 THR B C      1 
ATOM   5955 O  O      . THR B 1 271 ? 5.06300   9.70500   30.33900  1.000 46.42399 ? 267 THR B O      1 
ATOM   5956 C  CB     . THR B 1 271 ? 2.88100   7.62200   31.83300  1.000 44.55008 ? 267 THR B CB     1 
ATOM   5957 O  OG1    . THR B 1 271 ? 1.96500   6.53900   31.60000  1.000 42.67617 ? 267 THR B OG1    1 
ATOM   5958 C  CG2    . THR B 1 271 ? 2.12800   8.93900   31.78400  1.000 42.36561 ? 267 THR B CG2    1 
ATOM   5959 N  N      . ASP B 1 272 ? 5.86700   8.51100   32.07600  1.000 39.44947 ? 268 ASP B N      1 
ATOM   5960 C  CA     . ASP B 1 272 ? 6.86900   9.52000   32.40200  1.000 46.02920 ? 268 ASP B CA     1 
ATOM   5961 C  C      . ASP B 1 272 ? 7.84000   9.74000   31.24500  1.000 52.16678 ? 268 ASP B C      1 
ATOM   5962 O  O      . ASP B 1 272 ? 8.22600   10.88100  30.95600  1.000 55.31979 ? 268 ASP B O      1 
ATOM   5963 C  CB     . ASP B 1 272 ? 7.64100   9.13100   33.66700  1.000 41.65499 ? 268 ASP B CB     1 
ATOM   5964 C  CG     . ASP B 1 272 ? 6.76000   9.06900   34.90800  1.000 45.14752 ? 268 ASP B CG     1 
ATOM   5965 O  OD1    . ASP B 1 272 ? 5.58400   9.49800   34.85000  1.000 42.66301 ? 268 ASP B OD1    1 
ATOM   5966 O  OD2    . ASP B 1 272 ? 7.26100   8.59400   35.95100  1.000 52.81423 ? 268 ASP B OD2    1 
ATOM   5967 N  N      . TYR B 1 273 ? 8.29300   8.66000   30.60400  1.000 40.23904 ? 269 TYR B N      1 
ATOM   5968 C  CA     . TYR B 1 273 ? 9.29300   8.82900   29.55600  1.000 41.02334 ? 269 TYR B CA     1 
ATOM   5969 C  C      . TYR B 1 273 ? 8.71400   9.57700   28.36100  1.000 42.62353 ? 269 TYR B C      1 
ATOM   5970 O  O      . TYR B 1 273 ? 9.35700   10.48500  27.82600  1.000 41.58920 ? 269 TYR B O      1 
ATOM   5971 C  CB     . TYR B 1 273 ? 9.85700   7.47700   29.13200  1.000 42.01556 ? 269 TYR B CB     1 
ATOM   5972 C  CG     . TYR B 1 273 ? 11.27000  7.55100   28.58800  1.000 47.89785 ? 269 TYR B CG     1 
ATOM   5973 C  CD1    . TYR B 1 273 ? 11.50600  7.81300   27.24000  1.000 47.08196 ? 269 TYR B CD1    1 
ATOM   5974 C  CD2    . TYR B 1 273 ? 12.37000  7.36000   29.42200  1.000 51.66935 ? 269 TYR B CD2    1 
ATOM   5975 C  CE1    . TYR B 1 273 ? 12.80100  7.88700   26.73800  1.000 47.89258 ? 269 TYR B CE1    1 
ATOM   5976 C  CE2    . TYR B 1 273 ? 13.67200  7.42700   28.92500  1.000 52.39312 ? 269 TYR B CE2    1 
ATOM   5977 C  CZ     . TYR B 1 273 ? 13.87700  7.69100   27.57700  1.000 55.27768 ? 269 TYR B CZ     1 
ATOM   5978 O  OH     . TYR B 1 273 ? 15.15600  7.76300   27.06000  1.000 63.68132 ? 269 TYR B OH     1 
ATOM   5979 N  N      . LEU B 1 274 ? 7.49100   9.22900   27.94300  1.000 41.36022 ? 270 LEU B N      1 
ATOM   5980 C  CA     . LEU B 1 274 ? 6.97100   9.68900   26.66200  1.000 37.69926 ? 270 LEU B CA     1 
ATOM   5981 C  C      . LEU B 1 274 ? 6.21800   11.01100  26.73600  1.000 44.34216 ? 270 LEU B C      1 
ATOM   5982 O  O      . LEU B 1 274 ? 6.12800   11.70800  25.71300  1.000 40.04427 ? 270 LEU B O      1 
ATOM   5983 C  CB     . LEU B 1 274 ? 6.03400   8.63300   26.05600  1.000 36.16486 ? 270 LEU B CB     1 
ATOM   5984 C  CG     . LEU B 1 274 ? 6.68300   7.30600   25.66500  1.000 39.91531 ? 270 LEU B CG     1 
ATOM   5985 C  CD1    . LEU B 1 274 ? 5.68800   6.39400   24.95300  1.000 41.21810 ? 270 LEU B CD1    1 
ATOM   5986 C  CD2    . LEU B 1 274 ? 7.91000   7.55200   24.80500  1.000 41.52866 ? 270 LEU B CD2    1 
ATOM   5987 N  N      . LEU B 1 275 ? 5.66300   11.37100  27.89500  1.000 43.98159 ? 271 LEU B N      1 
ATOM   5988 C  CA     . LEU B 1 275 ? 4.89100   12.60300  28.02000  1.000 47.71362 ? 271 LEU B CA     1 
ATOM   5989 C  C      . LEU B 1 275 ? 5.60300   13.67900  28.82700  1.000 54.42758 ? 271 LEU B C      1 
ATOM   5990 O  O      . LEU B 1 275 ? 5.02800   14.75500  29.03900  1.000 54.93027 ? 271 LEU B O      1 
ATOM   5991 C  CB     . LEU B 1 275 ? 3.51800   12.30800  28.64400  1.000 38.19668 ? 271 LEU B CB     1 
ATOM   5992 C  CG     . LEU B 1 275 ? 2.64800   11.27200  27.93500  1.000 41.27600 ? 271 LEU B CG     1 
ATOM   5993 C  CD1    . LEU B 1 275 ? 1.39700   11.03500  28.74200  1.000 42.63406 ? 271 LEU B CD1    1 
ATOM   5994 C  CD2    . LEU B 1 275 ? 2.28600   11.72800  26.51400  1.000 41.27337 ? 271 LEU B CD2    1 
ATOM   5995 N  N      . SER B 1 276 ? 6.83800   13.42200  29.27100  1.000 52.59315 ? 272 SER B N      1 
ATOM   5996 C  CA     . SER B 1 276 ? 7.58600   14.36400  30.09100  1.000 53.23007 ? 272 SER B CA     1 
ATOM   5997 C  C      . SER B 1 276 ? 7.99200   15.61300  29.32500  1.000 57.19107 ? 272 SER B C      1 
ATOM   5998 O  O      . SER B 1 276 ? 8.43300   16.58600  29.94800  1.000 58.05696 ? 272 SER B O      1 
ATOM   5999 C  CB     . SER B 1 276 ? 8.82400   13.68300  30.69200  1.000 52.59578 ? 272 SER B CB     1 
ATOM   6000 O  OG     . SER B 1 276 ? 9.71500   13.22600  29.68700  1.000 60.87046 ? 272 SER B OG     1 
ATOM   6001 N  N      . GLY B 1 277 ? 7.90700   15.59500  27.99800  1.000 48.59793 ? 273 GLY B N      1 
ATOM   6002 C  CA     . GLY B 1 277 ? 8.40600   16.68800  27.19600  1.000 48.44265 ? 273 GLY B CA     1 
ATOM   6003 C  C      . GLY B 1 277 ? 9.86300   16.58400  26.81200  1.000 46.21870 ? 273 GLY B C      1 
ATOM   6004 O  O      . GLY B 1 277 ? 10.37200  17.47100  26.11400  1.000 53.35640 ? 273 GLY B O      1 
ATOM   6005 N  N      . ASP B 1 278 ? 10.55900  15.54000  27.24700  1.000 42.54721 ? 274 ASP B N      1 
ATOM   6006 C  CA     . ASP B 1 278 ? 11.98100  15.44400  26.96200  1.000 50.30603 ? 274 ASP B CA     1 
ATOM   6007 C  C      . ASP B 1 278 ? 12.31500  14.59600  25.74100  1.000 49.87177 ? 274 ASP B C      1 
ATOM   6008 O  O      . ASP B 1 278 ? 13.43700  14.70300  25.23100  1.000 45.13173 ? 274 ASP B O      1 
ATOM   6009 C  CB     . ASP B 1 278 ? 12.71900  14.88800  28.18100  1.000 56.92788 ? 274 ASP B CB     1 
ATOM   6010 C  CG     . ASP B 1 278 ? 12.42300  15.68000  29.44400  1.000 68.68981 ? 274 ASP B CG     1 
ATOM   6011 O  OD1    . ASP B 1 278 ? 12.45300  16.93500  29.38500  1.000 70.56899 ? 274 ASP B OD1    1 
ATOM   6012 O  OD2    . ASP B 1 278 ? 12.14500  15.04900  30.49100  1.000 72.73767 ? 274 ASP B OD2    1 
ATOM   6013 N  N      . VAL B 1 279 ? 11.38500  13.78300  25.23900  1.000 44.71062 ? 275 VAL B N      1 
ATOM   6014 C  CA     . VAL B 1 279 ? 11.69600  12.96000  24.07500  1.000 40.64961 ? 275 VAL B CA     1 
ATOM   6015 C  C      . VAL B 1 279 ? 11.83900  13.87300  22.86800  1.000 35.33055 ? 275 VAL B C      1 
ATOM   6016 O  O      . VAL B 1 279 ? 10.90200  14.59100  22.49800  1.000 39.56790 ? 275 VAL B O      1 
ATOM   6017 C  CB     . VAL B 1 279 ? 10.61900  11.88900  23.84300  1.000 39.41262 ? 275 VAL B CB     1 
ATOM   6018 C  CG1    . VAL B 1 279 ? 10.78000  11.26700  22.45300  1.000 31.20637 ? 275 VAL B CG1    1 
ATOM   6019 C  CG2    . VAL B 1 279 ? 10.71300  10.81300  24.91800  1.000 39.93110 ? 275 VAL B CG2    1 
ATOM   6020 N  N      . ASP B 1 280 ? 13.00800  13.84300  22.23800  1.000 38.14142 ? 276 ASP B N      1 
ATOM   6021 C  CA     . ASP B 1 280 ? 13.20100  14.68100  21.06200  1.000 35.29634 ? 276 ASP B CA     1 
ATOM   6022 C  C      . ASP B 1 280 ? 12.87400  13.92100  19.78400  1.000 38.40197 ? 276 ASP B C      1 
ATOM   6023 O  O      . ASP B 1 280 ? 12.26600  14.48800  18.87100  1.000 40.79436 ? 276 ASP B O      1 
ATOM   6024 C  CB     . ASP B 1 280 ? 14.63100  15.25100  21.01400  1.000 37.14393 ? 276 ASP B CB     1 
ATOM   6025 C  CG     . ASP B 1 280 ? 15.72200  14.19300  21.19900  1.000 43.91579 ? 276 ASP B CG     1 
ATOM   6026 O  OD1    . ASP B 1 280 ? 15.39400  13.02100  21.47400  1.000 46.92931 ? 276 ASP B OD1    1 
ATOM   6027 O  OD2    . ASP B 1 280 ? 16.92700  14.54500  21.06900  1.000 46.91615 ? 276 ASP B OD2    1 
ATOM   6028 N  N      . VAL B 1 281 ? 13.20200  12.63400  19.71500  1.000 36.27540 ? 277 VAL B N      1 
ATOM   6029 C  CA     . VAL B 1 281 ? 12.91000  11.82500  18.53600  1.000 35.07789 ? 277 VAL B CA     1 
ATOM   6030 C  C      . VAL B 1 281 ? 12.07600  10.62500  18.96700  1.000 35.80166 ? 277 VAL B C      1 
ATOM   6031 O  O      . VAL B 1 281 ? 12.53600  9.77200   19.74200  1.000 31.73538 ? 277 VAL B O      1 
ATOM   6032 C  CB     . VAL B 1 281 ? 14.18500  11.39000  17.81100  1.000 37.02023 ? 277 VAL B CB     1 
ATOM   6033 C  CG1    . VAL B 1 281 ? 13.84000  10.45200  16.66300  1.000 37.96508 ? 277 VAL B CG1    1 
ATOM   6034 C  CG2    . VAL B 1 281 ? 14.93800  12.62400  17.31200  1.000 32.43547 ? 277 VAL B CG2    1 
ATOM   6035 N  N      . LEU B 1 282 ? 10.84100  10.56100  18.48100  1.000 34.15146 ? 278 LEU B N      1 
ATOM   6036 C  CA     . LEU B 1 282 ? 9.95100   9.45400   18.77800  1.000 33.29873 ? 278 LEU B CA     1 
ATOM   6037 C  C      . LEU B 1 282 ? 9.73100   8.65500   17.50600  1.000 35.80692 ? 278 LEU B C      1 
ATOM   6038 O  O      . LEU B 1 282 ? 9.39400   9.22600   16.46400  1.000 35.13579 ? 278 LEU B O      1 
ATOM   6039 C  CB     . LEU B 1 282 ? 8.60900   9.94300   19.33100  1.000 29.76409 ? 278 LEU B CB     1 
ATOM   6040 C  CG     . LEU B 1 282 ? 7.58600   8.84700   19.57800  1.000 29.20350 ? 278 LEU B CG     1 
ATOM   6041 C  CD1    . LEU B 1 282 ? 8.04700   7.95400   20.73500  1.000 34.85944 ? 278 LEU B CD1    1 
ATOM   6042 C  CD2    . LEU B 1 282 ? 6.24100   9.45200   19.90500  1.000 34.66205 ? 278 LEU B CD2    1 
ATOM   6043 N  N      . ILE B 1 283 ? 9.94100   7.34500   17.58400  1.000 32.01173 ? 279 ILE B N      1 
ATOM   6044 C  CA     . ILE B 1 283 ? 9.74900   6.46000   16.44200  1.000 33.70141 ? 279 ILE B CA     1 
ATOM   6045 C  C      . ILE B 1 283 ? 8.53300   5.57700   16.71300  1.000 31.44061 ? 279 ILE B C      1 
ATOM   6046 O  O      . ILE B 1 283 ? 8.56600   4.70400   17.58900  1.000 29.06927 ? 279 ILE B O      1 
ATOM   6047 C  CB     . ILE B 1 283 ? 11.00000  5.62500   16.16200  1.000 30.72210 ? 279 ILE B CB     1 
ATOM   6048 C  CG1    . ILE B 1 283 ? 12.19200  6.56300   15.95600  1.000 34.04092 ? 279 ILE B CG1    1 
ATOM   6049 C  CG2    . ILE B 1 283 ? 10.77300  4.74900   14.93800  1.000 27.03482 ? 279 ILE B CG2    1 
ATOM   6050 C  CD1    . ILE B 1 283 ? 13.51000  5.84900   15.97300  1.000 37.88349 ? 279 ILE B CD1    1 
ATOM   6051 N  N      . VAL B 1 284 ? 7.46800   5.78400   15.94900  1.000 29.93254 ? 280 VAL B N      1 
ATOM   6052 C  CA     . VAL B 1 284 ? 6.26300   4.97100   16.04400  1.000 28.54290 ? 280 VAL B CA     1 
ATOM   6053 C  C      . VAL B 1 284 ? 6.33700   3.89600   14.96900  1.000 30.02728 ? 280 VAL B C      1 
ATOM   6054 O  O      . VAL B 1 284 ? 6.41700   4.20400   13.77400  1.000 28.93242 ? 280 VAL B O      1 
ATOM   6055 C  CB     . VAL B 1 284 ? 4.99900   5.83000   15.88300  1.000 27.77701 ? 280 VAL B CB     1 
ATOM   6056 C  CG1    . VAL B 1 284 ? 3.74800   4.94900   15.84300  1.000 23.73706 ? 280 VAL B CG1    1 
ATOM   6057 C  CG2    . VAL B 1 284 ? 4.92400   6.87400   17.00400  1.000 27.20589 ? 280 VAL B CG2    1 
ATOM   6058 N  N      . ILE B 1 285 ? 6.30000   2.63400   15.38200  1.000 27.31643 ? 281 ILE B N      1 
ATOM   6059 C  CA     . ILE B 1 285 ? 6.38800   1.50700   14.46200  1.000 30.97740 ? 281 ILE B CA     1 
ATOM   6060 C  C      . ILE B 1 285 ? 5.12400   0.67500   14.58800  1.000 30.51155 ? 281 ILE B C      1 
ATOM   6061 O  O      . ILE B 1 285 ? 4.89300   0.03400   15.62500  1.000 27.14799 ? 281 ILE B O      1 
ATOM   6062 C  CB     . ILE B 1 285 ? 7.61400   0.63300   14.72300  1.000 27.29538 ? 281 ILE B CB     1 
ATOM   6063 C  CG1    . ILE B 1 285 ? 8.80900   1.49100   15.09700  1.000 29.70093 ? 281 ILE B CG1    1 
ATOM   6064 C  CG2    . ILE B 1 285 ? 7.86500   -0.27900  13.50700  1.000 30.20099 ? 281 ILE B CG2    1 
ATOM   6065 C  CD1    . ILE B 1 285 ? 10.07700  0.68100   15.32600  1.000 38.01772 ? 281 ILE B CD1    1 
ATOM   6066 N  N      . GLY B 1 286 ? 4.33300   0.64500   13.52300  1.000 26.88743 ? 282 GLY B N      1 
ATOM   6067 C  CA     . GLY B 1 286 ? 3.18500   -0.24900  13.47500  1.000 24.36082 ? 282 GLY B CA     1 
ATOM   6068 C  C      . GLY B 1 286 ? 2.12100   0.00800   14.51800  1.000 24.96615 ? 282 GLY B C      1 
ATOM   6069 O  O      . GLY B 1 286 ? 1.58600   -0.94700  15.10200  1.000 28.17969 ? 282 GLY B O      1 
ATOM   6070 N  N      . SER B 1 287 ? 1.79100   1.27900   14.76600  1.000 26.41896 ? 283 SER B N      1 
ATOM   6071 C  CA     . SER B 1 287 ? 0.62800   1.62400   15.57400  1.000 29.31667 ? 283 SER B CA     1 
ATOM   6072 C  C      . SER B 1 287 ? -0.27000  2.57400   14.79900  1.000 28.89557 ? 283 SER B C      1 
ATOM   6073 O  O      . SER B 1 287 ? 0.22100   3.50700   14.15800  1.000 22.48427 ? 283 SER B O      1 
ATOM   6074 C  CB     . SER B 1 287 ? 1.01500   2.27600   16.90400  1.000 34.33833 ? 283 SER B CB     1 
ATOM   6075 O  OG     . SER B 1 287 ? -0.13400  2.86400   17.50600  1.000 34.66731 ? 283 SER B OG     1 
ATOM   6076 N  N      . SER B 1 288 ? -1.59000  2.35600   14.88700  1.000 21.51311 ? 284 SER B N      1 
ATOM   6077 C  CA     . SER B 1 288 ? -2.53600  3.30500   14.31400  1.000 29.38773 ? 284 SER B CA     1 
ATOM   6078 C  C      . SER B 1 288 ? -2.71600  4.55100   15.17400  1.000 28.89294 ? 284 SER B C      1 
ATOM   6079 O  O      . SER B 1 288 ? -3.38400  5.49300   14.73600  1.000 21.62891 ? 284 SER B O      1 
ATOM   6080 C  CB     . SER B 1 288 ? -3.89800  2.63500   14.08800  1.000 29.08507 ? 284 SER B CB     1 
ATOM   6081 O  OG     . SER B 1 288 ? -4.48800  2.21100   15.30900  1.000 31.56431 ? 284 SER B OG     1 
ATOM   6082 N  N      . LEU B 1 289 ? -2.12800  4.59000   16.37300  1.000 22.73430 ? 285 LEU B N      1 
ATOM   6083 C  CA     . LEU B 1 289 ? -2.20000  5.77200   17.24500  1.000 22.68167 ? 285 LEU B CA     1 
ATOM   6084 C  C      . LEU B 1 289 ? -3.64900  6.19000   17.49900  1.000 27.15326 ? 285 LEU B C      1 
ATOM   6085 O  O      . LEU B 1 289 ? -4.00600  7.37000   17.42400  1.000 31.31428 ? 285 LEU B O      1 
ATOM   6086 C  CB     . LEU B 1 289 ? -1.37900  6.93600   16.67200  1.000 23.30279 ? 285 LEU B CB     1 
ATOM   6087 C  CG     . LEU B 1 289 ? 0.14300   6.70400   16.58300  1.000 26.27420 ? 285 LEU B CG     1 
ATOM   6088 C  CD1    . LEU B 1 289 ? 0.87000   7.86600   15.88900  1.000 23.30279 ? 285 LEU B CD1    1 
ATOM   6089 C  CD2    . LEU B 1 289 ? 0.75600   6.42200   17.96900  1.000 24.77929 ? 285 LEU B CD2    1 
ATOM   6090 N  N      . GLY B 1 290 ? -4.48800  5.20300   17.81100  1.000 24.98721 ? 286 GLY B N      1 
ATOM   6091 C  CA     . GLY B 1 290 ? -5.84100  5.45900   18.25300  1.000 21.72629 ? 286 GLY B CA     1 
ATOM   6092 C  C      . GLY B 1 290 ? -5.91400  5.90400   19.71000  1.000 29.77462 ? 286 GLY B C      1 
ATOM   6093 O  O      . GLY B 1 290 ? -4.91900  6.23200   20.35800  1.000 27.64016 ? 286 GLY B O      1 
ATOM   6094 N  N      . ASP B 1 291 ? -7.13700  5.87100   20.23300  1.000 27.44803 ? 287 ASP B N      1 
ATOM   6095 C  CA     . ASP B 1 291 ? -7.43500  6.46400   21.53700  1.000 27.17694 ? 287 ASP B CA     1 
ATOM   6096 C  C      . ASP B 1 291 ? -6.60300  5.82500   22.64500  1.000 29.37721 ? 287 ASP B C      1 
ATOM   6097 O  O      . ASP B 1 291 ? -5.89200  6.50800   23.39400  1.000 26.17682 ? 287 ASP B O      1 
ATOM   6098 C  CB     . ASP B 1 291 ? -8.93800  6.30600   21.82100  1.000 34.88576 ? 287 ASP B CB     1 
ATOM   6099 C  CG     . ASP B 1 291 ? -9.36400  6.92000   23.14500  1.000 40.37326 ? 287 ASP B CG     1 
ATOM   6100 O  OD1    . ASP B 1 291 ? -8.50100  7.42500   23.89200  1.000 41.86028 ? 287 ASP B OD1    1 
ATOM   6101 O  OD2    . ASP B 1 291 ? -10.57600 6.89500   23.43400  1.000 43.60523 ? 287 ASP B OD2    1 
ATOM   6102 N  N      . TRP B 1 292 ? -6.70700  4.51100   22.78700  1.000 29.37984 ? 288 TRP B N      1 
ATOM   6103 C  CA     . TRP B 1 292 ? -6.01700  3.85400   23.88400  1.000 34.60152 ? 288 TRP B CA     1 
ATOM   6104 C  C      . TRP B 1 292 ? -4.50300  3.89200   23.71200  1.000 35.03578 ? 288 TRP B C      1 
ATOM   6105 O  O      . TRP B 1 292 ? -3.78100  3.88400   24.71000  1.000 30.98529 ? 288 TRP B O      1 
ATOM   6106 C  CB     . TRP B 1 292 ? -6.52900  2.42400   24.02800  1.000 31.20901 ? 288 TRP B CB     1 
ATOM   6107 C  CG     . TRP B 1 292 ? -7.78100  2.36200   24.82300  1.000 36.31488 ? 288 TRP B CG     1 
ATOM   6108 C  CD1    . TRP B 1 292 ? -8.48200  3.42100   25.33100  1.000 39.51790 ? 288 TRP B CD1    1 
ATOM   6109 C  CD2    . TRP B 1 292 ? -8.49700  1.18500   25.21300  1.000 43.98685 ? 288 TRP B CD2    1 
ATOM   6110 N  NE1    . TRP B 1 292 ? -9.58100  2.97500   26.02100  1.000 36.35699 ? 288 TRP B NE1    1 
ATOM   6111 C  CE2    . TRP B 1 292 ? -9.62000  1.60800   25.96100  1.000 40.30483 ? 288 TRP B CE2    1 
ATOM   6112 C  CE3    . TRP B 1 292 ? -8.29600  -0.18700  25.00900  1.000 46.53453 ? 288 TRP B CE3    1 
ATOM   6113 C  CZ2    . TRP B 1 292 ? -10.54600 0.71000   26.50000  1.000 45.13436 ? 288 TRP B CZ2    1 
ATOM   6114 C  CZ3    . TRP B 1 292 ? -9.21300  -1.07900  25.54500  1.000 52.52735 ? 288 TRP B CZ3    1 
ATOM   6115 C  CH2    . TRP B 1 292 ? -10.32500 -0.62500  26.28600  1.000 49.32960 ? 288 TRP B CH2    1 
ATOM   6116 N  N      . GLN B 1 293 ? -4.01300  3.96100   22.47000  1.000 30.00623 ? 289 GLN B N      1 
ATOM   6117 C  CA     . GLN B 1 293 ? -2.58000  4.02200   22.19500  1.000 26.82690 ? 289 GLN B CA     1 
ATOM   6118 C  C      . GLN B 1 293 ? -1.96300  5.37500   22.52900  1.000 30.03255 ? 289 GLN B C      1 
ATOM   6119 O  O      . GLN B 1 293 ? -0.73400  5.48200   22.58800  1.000 32.69076 ? 289 GLN B O      1 
ATOM   6120 C  CB     . GLN B 1 293 ? -2.30700  3.70600   20.71600  1.000 22.24740 ? 289 GLN B CB     1 
ATOM   6121 C  CG     . GLN B 1 293 ? -2.85900  2.34800   20.23100  1.000 23.12909 ? 289 GLN B CG     1 
ATOM   6122 C  CD     . GLN B 1 293 ? -4.26700  2.48100   19.61400  1.000 32.53285 ? 289 GLN B CD     1 
ATOM   6123 O  OE1    . GLN B 1 293 ? -5.19600  2.97000   20.26000  1.000 33.07502 ? 289 GLN B OE1    1 
ATOM   6124 N  NE2    . GLN B 1 293 ? -4.41100  2.06200   18.36300  1.000 28.02968 ? 289 GLN B NE2    1 
ATOM   6125 N  N      . THR B 1 294 ? -2.76700  6.41000   22.75200  1.000 27.37960 ? 290 THR B N      1 
ATOM   6126 C  CA     . THR B 1 294 ? -2.23800  7.76100   22.86000  1.000 25.40568 ? 290 THR B CA     1 
ATOM   6127 C  C      . THR B 1 294 ? -2.78700  8.53100   24.04800  1.000 31.30112 ? 290 THR B C      1 
ATOM   6128 O  O      . THR B 1 294 ? -2.65000  9.75800   24.08400  1.000 32.57233 ? 290 THR B O      1 
ATOM   6129 C  CB     . THR B 1 294 ? -2.55300  8.54400   21.59100  1.000 33.41190 ? 290 THR B CB     1 
ATOM   6130 O  OG1    . THR B 1 294 ? -3.97600  8.53700   21.40500  1.000 32.01436 ? 290 THR B OG1    1 
ATOM   6131 C  CG2    . THR B 1 294 ? -1.87400  7.90000   20.39600  1.000 33.49875 ? 290 THR B CG2    1 
ATOM   6132 N  N      . ASN B 1 295 ? -3.44000  7.86700   24.99200  1.000 31.49588 ? 291 ASN B N      1 
ATOM   6133 C  CA     . ASN B 1 295 ? -4.13900  8.55600   26.07200  1.000 37.40975 ? 291 ASN B CA     1 
ATOM   6134 C  C      . ASN B 1 295 ? -5.06500  9.65100   25.52800  1.000 38.44671 ? 291 ASN B C      1 
ATOM   6135 O  O      . ASN B 1 295 ? -4.96600  10.83000  25.87400  1.000 38.29670 ? 291 ASN B O      1 
ATOM   6136 C  CB     . ASN B 1 295 ? -3.09700  9.13000   27.03400  1.000 41.93134 ? 291 ASN B CB     1 
ATOM   6137 C  CG     . ASN B 1 295 ? -3.66700  9.43800   28.38300  1.000 58.15171 ? 291 ASN B CG     1 
ATOM   6138 O  OD1    . ASN B 1 295 ? -4.46000  8.66800   28.92000  1.000 71.04536 ? 291 ASN B OD1    1 
ATOM   6139 N  ND2    . ASN B 1 295 ? -3.28200  10.58100  28.94000  1.000 48.87954 ? 291 ASN B ND2    1 
ATOM   6140 N  N      . SER B 1 296 ? -6.01200  9.22200   24.69500  1.000 35.03052 ? 292 SER B N      1 
ATOM   6141 C  CA     . SER B 1 296 ? -6.92700  10.11000  23.97200  1.000 38.83360 ? 292 SER B CA     1 
ATOM   6142 C  C      . SER B 1 296 ? -6.17600  11.23700  23.26800  1.000 32.33019 ? 292 SER B C      1 
ATOM   6143 O  O      . SER B 1 296 ? -6.46400  12.41700  23.44300  1.000 35.85956 ? 292 SER B O      1 
ATOM   6144 C  CB     . SER B 1 296 ? -8.01000  10.67700  24.89300  1.000 39.95479 ? 292 SER B CB     1 
ATOM   6145 O  OG     . SER B 1 296 ? -8.62300  9.63600   25.61200  1.000 46.15817 ? 292 SER B OG     1 
ATOM   6146 N  N      . TRP B 1 297 ? -5.21700  10.84500  22.43300  1.000 32.93026 ? 293 TRP B N      1 
ATOM   6147 C  CA     . TRP B 1 297 ? -4.51800  11.79400  21.57700  1.000 29.60881 ? 293 TRP B CA     1 
ATOM   6148 C  C      . TRP B 1 297 ? -3.92200  12.92600  22.41500  1.000 32.04858 ? 293 TRP B C      1 
ATOM   6149 O  O      . TRP B 1 297 ? -4.03700  14.10900  22.09700  1.000 29.07454 ? 293 TRP B O      1 
ATOM   6150 C  CB     . TRP B 1 297 ? -5.45500  12.31000  20.47800  1.000 27.62963 ? 293 TRP B CB     1 
ATOM   6151 C  CG     . TRP B 1 297 ? -6.13800  11.14500  19.79100  1.000 30.01939 ? 293 TRP B CG     1 
ATOM   6152 C  CD1    . TRP B 1 297 ? -5.57200  10.28300  18.88800  1.000 33.08291 ? 293 TRP B CD1    1 
ATOM   6153 C  CD2    . TRP B 1 297 ? -7.47600  10.67400  20.00900  1.000 27.59541 ? 293 TRP B CD2    1 
ATOM   6154 N  NE1    . TRP B 1 297 ? -6.48700  9.32100   18.51300  1.000 30.81685 ? 293 TRP B NE1    1 
ATOM   6155 C  CE2    . TRP B 1 297 ? -7.66200  9.54100   19.18200  1.000 33.01712 ? 293 TRP B CE2    1 
ATOM   6156 C  CE3    . TRP B 1 297 ? -8.54400  11.11000  20.80400  1.000 28.82714 ? 293 TRP B CE3    1 
ATOM   6157 C  CZ2    . TRP B 1 297 ? -8.87200  8.83500   19.13400  1.000 29.01927 ? 293 TRP B CZ2    1 
ATOM   6158 C  CZ3    . TRP B 1 297 ? -9.75200  10.40100  20.75100  1.000 31.08531 ? 293 TRP B CZ3    1 
ATOM   6159 C  CH2    . TRP B 1 297 ? -9.89800  9.27900   19.92300  1.000 32.41178 ? 293 TRP B CH2    1 
ATOM   6160 N  N      . ASP B 1 298 ? -3.27200  12.53800  23.50600  1.000 33.68299 ? 294 ASP B N      1 
ATOM   6161 C  CA     . ASP B 1 298 ? -2.56600  13.48200  24.36400  1.000 34.19884 ? 294 ASP B CA     1 
ATOM   6162 C  C      . ASP B 1 298 ? -1.53100  14.25200  23.54500  1.000 36.78336 ? 294 ASP B C      1 
ATOM   6163 O  O      . ASP B 1 298 ? -0.65400  13.63000  22.92900  1.000 37.80980 ? 294 ASP B O      1 
ATOM   6164 C  CB     . ASP B 1 298 ? -1.88000  12.71800  25.50100  1.000 33.79879 ? 294 ASP B CB     1 
ATOM   6165 C  CG     . ASP B 1 298 ? -1.46500  13.62200  26.65600  1.000 41.06282 ? 294 ASP B CG     1 
ATOM   6166 O  OD1    . ASP B 1 298 ? -1.14800  14.80600  26.41200  1.000 39.51526 ? 294 ASP B OD1    1 
ATOM   6167 O  OD2    . ASP B 1 298 ? -1.44300  13.14100  27.80900  1.000 40.21272 ? 294 ASP B OD2    1 
ATOM   6168 N  N      . PRO B 1 299 ? -1.59300  15.58400  23.50300  1.000 37.27815 ? 295 PRO B N      1 
ATOM   6169 C  CA     . PRO B 1 299 ? -0.58200  16.34400  22.74000  1.000 38.38881 ? 295 PRO B CA     1 
ATOM   6170 C  C      . PRO B 1 299 ? 0.82400   16.23100  23.29800  1.000 41.00755 ? 295 PRO B C      1 
ATOM   6171 O  O      . PRO B 1 299 ? 1.78800   16.45900  22.55900  1.000 42.51036 ? 295 PRO B O      1 
ATOM   6172 C  CB     . PRO B 1 299 ? -1.09400  17.79100  22.81800  1.000 38.54936 ? 295 PRO B CB     1 
ATOM   6173 C  CG     . PRO B 1 299 ? -1.97600  17.81900  24.01100  1.000 40.14429 ? 295 PRO B CG     1 
ATOM   6174 C  CD     . PRO B 1 299 ? -2.63800  16.46300  24.05300  1.000 38.64148 ? 295 PRO B CD     1 
ATOM   6175 N  N      . ARG B 1 300 ? 0.97600   15.90400  24.58000  1.000 40.81016 ? 296 ARG B N      1 
ATOM   6176 C  CA     . ARG B 1 300 ? 2.30700   15.76200  25.14900  1.000 38.52304 ? 296 ARG B CA     1 
ATOM   6177 C  C      . ARG B 1 300 ? 3.08500   14.62000  24.51500  1.000 38.83624 ? 296 ARG B C      1 
ATOM   6178 O  O      . ARG B 1 300 ? 4.30700   14.54800  24.68200  1.000 38.19142 ? 296 ARG B O      1 
ATOM   6179 C  CB     . ARG B 1 300 ? 2.20300   15.57300  26.65800  1.000 37.25973 ? 296 ARG B CB     1 
ATOM   6180 C  CG     . ARG B 1 300 ? 1.91700   16.87100  27.39900  1.000 35.61743 ? 296 ARG B CG     1 
ATOM   6181 C  CD     . ARG B 1 300 ? 1.59800   16.57400  28.84800  1.000 41.22073 ? 296 ARG B CD     1 
ATOM   6182 N  NE     . ARG B 1 300 ? 0.56300   15.54500  28.96200  1.000 46.01604 ? 296 ARG B NE     1 
ATOM   6183 C  CZ     . ARG B 1 300 ? 0.20300   14.97400  30.11100  1.000 49.42961 ? 296 ARG B CZ     1 
ATOM   6184 N  NH1    . ARG B 1 300 ? 0.79700   15.32800  31.24300  1.000 54.19860 ? 296 ARG B NH1    1 
ATOM   6185 N  NH2    . ARG B 1 300 ? -0.74500  14.04500  30.13200  1.000 37.14919 ? 296 ARG B NH2    1 
ATOM   6186 N  N      . LEU B 1 301 ? 2.41100   13.72700  23.78600  1.000 37.45449 ? 297 LEU B N      1 
ATOM   6187 C  CA     . LEU B 1 301 ? 3.13200   12.67700  23.07700  1.000 40.00480 ? 297 LEU B CA     1 
ATOM   6188 C  C      . LEU B 1 301 ? 4.06500   13.24100  22.00700  1.000 39.09942 ? 297 LEU B C      1 
ATOM   6189 O  O      . LEU B 1 301 ? 5.06000   12.59800  21.66500  1.000 40.11797 ? 297 LEU B O      1 
ATOM   6190 C  CB     . LEU B 1 301 ? 2.13100   11.70000  22.45900  1.000 38.56778 ? 297 LEU B CB     1 
ATOM   6191 C  CG     . LEU B 1 301 ? 2.65300   10.36700  21.92400  1.000 35.55426 ? 297 LEU B CG     1 
ATOM   6192 C  CD1    . LEU B 1 301 ? 3.42100   9.62900   23.00900  1.000 35.48057 ? 297 LEU B CD1    1 
ATOM   6193 C  CD2    . LEU B 1 301 ? 1.49300   9.51400   21.39300  1.000 34.34096 ? 297 LEU B CD2    1 
ATOM   6194 N  N      . THR B 1 302 ? 3.77200   14.42700  21.49000  1.000 42.49194 ? 298 THR B N      1 
ATOM   6195 C  CA     . THR B 1 302 ? 4.53600   15.03600  20.41000  1.000 38.27301 ? 298 THR B CA     1 
ATOM   6196 C  C      . THR B 1 302 ? 6.00700   15.16800  20.76600  1.000 37.19393 ? 298 THR B C      1 
ATOM   6197 O  O      . THR B 1 302 ? 6.33600   15.82100  21.76700  1.000 36.69387 ? 298 THR B O      1 
ATOM   6198 C  CB     . THR B 1 302 ? 3.94800   16.40900  20.08800  1.000 41.17073 ? 298 THR B CB     1 
ATOM   6199 O  OG1    . THR B 1 302 ? 2.55500   16.25600  19.76500  1.000 41.67079 ? 298 THR B OG1    1 
ATOM   6200 C  CG2    . THR B 1 302 ? 4.69900   17.07500  18.92600  1.000 37.37553 ? 298 THR B CG2    1 
ATOM   6201 N  N      . PRO B 1 303 ? 6.91600   14.62400  19.96400  1.000 38.60989 ? 299 PRO B N      1 
ATOM   6202 C  CA     . PRO B 1 303 ? 8.34600   14.78300  20.24800  1.000 37.52029 ? 299 PRO B CA     1 
ATOM   6203 C  C      . PRO B 1 303 ? 8.81400   16.17300  19.86100  1.000 40.44169 ? 299 PRO B C      1 
ATOM   6204 O  O      . PRO B 1 303 ? 8.17400   16.88400  19.08400  1.000 39.28103 ? 299 PRO B O      1 
ATOM   6205 C  CB     . PRO B 1 303 ? 9.01200   13.71700  19.37200  1.000 35.01736 ? 299 PRO B CB     1 
ATOM   6206 C  CG     . PRO B 1 303 ? 8.05200   13.57700  18.19500  1.000 35.47004 ? 299 PRO B CG     1 
ATOM   6207 C  CD     . PRO B 1 303 ? 6.66800   13.81100  18.75800  1.000 33.29873 ? 299 PRO B CD     1 
ATOM   6208 N  N      . SER B 1 304 ? 9.96000   16.55100  20.42600  1.000 39.55474 ? 300 SER B N      1 
ATOM   6209 C  CA     . SER B 1 304 ? 10.44200  17.91500  20.28200  1.000 40.34957 ? 300 SER B CA     1 
ATOM   6210 C  C      . SER B 1 304 ? 11.22400  18.15200  18.99600  1.000 43.74735 ? 300 SER B C      1 
ATOM   6211 O  O      . SER B 1 304 ? 11.37800  19.30800  18.59600  1.000 46.89510 ? 300 SER B O      1 
ATOM   6212 C  CB     . SER B 1 304 ? 11.31600  18.28000  21.48100  1.000 38.34144 ? 300 SER B CB     1 
ATOM   6213 O  OG     . SER B 1 304 ? 12.58800  17.67600  21.35800  1.000 45.72917 ? 300 SER B OG     1 
ATOM   6214 N  N      . VAL B 1 305 ? 11.70700  17.10900  18.32800  1.000 41.45760 ? 301 VAL B N      1 
ATOM   6215 C  CA     . VAL B 1 305 ? 12.51900  17.32500  17.13600  1.000 39.12048 ? 301 VAL B CA     1 
ATOM   6216 C  C      . VAL B 1 305 ? 11.86100  16.65900  15.94300  1.000 39.12838 ? 301 VAL B C      1 
ATOM   6217 O  O      . VAL B 1 305 ? 11.59900  17.30800  14.92900  1.000 49.82439 ? 301 VAL B O      1 
ATOM   6218 C  CB     . VAL B 1 305 ? 13.95900  16.80700  17.31300  1.000 41.31811 ? 301 VAL B CB     1 
ATOM   6219 C  CG1    . VAL B 1 305 ? 14.69600  16.85500  15.97900  1.000 34.68574 ? 301 VAL B CG1    1 
ATOM   6220 C  CG2    . VAL B 1 305 ? 14.69900  17.63800  18.35500  1.000 44.26320 ? 301 VAL B CG2    1 
ATOM   6221 N  N      . ALA B 1 306 ? 11.60600  15.35900  16.04400  1.000 37.56766 ? 302 ALA B N      1 
ATOM   6222 C  CA     . ALA B 1 306 ? 11.07100  14.61500  14.91300  1.000 35.67533 ? 302 ALA B CA     1 
ATOM   6223 C  C      . ALA B 1 306 ? 10.18200  13.49600  15.41500  1.000 40.12850 ? 302 ALA B C      1 
ATOM   6224 O  O      . ALA B 1 306 ? 10.57100  12.72800  16.30400  1.000 36.96233 ? 302 ALA B O      1 
ATOM   6225 C  CB     . ALA B 1 306 ? 12.18700  14.02600  14.04600  1.000 32.74866 ? 302 ALA B CB     1 
ATOM   6226 N  N      . LEU B 1 307 ? 9.00200   13.39200  14.81800  1.000 32.10911 ? 303 LEU B N      1 
ATOM   6227 C  CA     . LEU B 1 307 ? 8.17800   12.21300  14.94700  1.000 32.74603 ? 303 LEU B CA     1 
ATOM   6228 C  C      . LEU B 1 307 ? 8.38200   11.40100  13.67600  1.000 38.67043 ? 303 LEU B C      1 
ATOM   6229 O  O      . LEU B 1 307 ? 8.17000   11.90700  12.56600  1.000 33.33294 ? 303 LEU B O      1 
ATOM   6230 C  CB     . LEU B 1 307 ? 6.70700   12.58400  15.14200  1.000 34.55151 ? 303 LEU B CB     1 
ATOM   6231 C  CG     . LEU B 1 307 ? 5.74200   11.41800  14.98200  1.000 34.83576 ? 303 LEU B CG     1 
ATOM   6232 C  CD1    . LEU B 1 307 ? 6.03400   10.35500  16.02100  1.000 30.42996 ? 303 LEU B CD1    1 
ATOM   6233 C  CD2    . LEU B 1 307 ? 4.29500   11.88100  15.08000  1.000 38.82308 ? 303 LEU B CD2    1 
ATOM   6234 N  N      . ILE B 1 308 ? 8.83200   10.16400  13.83500  1.000 30.03781 ? 304 ILE B N      1 
ATOM   6235 C  CA     . ILE B 1 308 ? 9.00200   9.23300   12.72800  1.000 31.64064 ? 304 ILE B CA     1 
ATOM   6236 C  C      . ILE B 1 308 ? 7.91200   8.19200   12.86800  1.000 29.85358 ? 304 ILE B C      1 
ATOM   6237 O  O      . ILE B 1 308 ? 7.71700   7.63900   13.95800  1.000 34.58573 ? 304 ILE B O      1 
ATOM   6238 C  CB     . ILE B 1 308 ? 10.39000  8.56800   12.74700  1.000 33.08818 ? 304 ILE B CB     1 
ATOM   6239 C  CG1    . ILE B 1 308 ? 11.50400  9.61200   12.58900  1.000 31.69854 ? 304 ILE B CG1    1 
ATOM   6240 C  CG2    . ILE B 1 308 ? 10.46000  7.42400   11.71300  1.000 27.63226 ? 304 ILE B CG2    1 
ATOM   6241 C  CD1    . ILE B 1 308 ? 12.78600  9.22800   13.29600  1.000 33.03028 ? 304 ILE B CD1    1 
ATOM   6242 N  N      . GLN B 1 309 ? 7.16700   7.94800   11.79700  1.000 28.28760 ? 305 GLN B N      1 
ATOM   6243 C  CA     . GLN B 1 309 ? 6.12700   6.93200   11.85400  1.000 29.51407 ? 305 GLN B CA     1 
ATOM   6244 C  C      . GLN B 1 309 ? 6.32600   5.96800   10.70200  1.000 31.05109 ? 305 GLN B C      1 
ATOM   6245 O  O      . GLN B 1 309 ? 6.35400   6.38600   9.54000   1.000 28.30339 ? 305 GLN B O      1 
ATOM   6246 C  CB     . GLN B 1 309 ? 4.72200   7.54200   11.81400  1.000 31.40113 ? 305 GLN B CB     1 
ATOM   6247 C  CG     . GLN B 1 309 ? 3.62600   6.48200   11.87400  1.000 29.00611 ? 305 GLN B CG     1 
ATOM   6248 C  CD     . GLN B 1 309 ? 2.22700   7.06400   12.04900  1.000 36.74125 ? 305 GLN B CD     1 
ATOM   6249 O  OE1    . GLN B 1 309 ? 1.97500   8.22700   11.71500  1.000 32.35388 ? 305 GLN B OE1    1 
ATOM   6250 N  NE2    . GLN B 1 309 ? 1.30900   6.24800   12.57700  1.000 31.48535 ? 305 GLN B NE2    1 
ATOM   6251 N  N      . ILE B 1 310 ? 6.43500   4.68400   11.03300  1.000 29.90359 ? 306 ILE B N      1 
ATOM   6252 C  CA     . ILE B 1 310 ? 6.63500   3.60300   10.07400  1.000 31.68801 ? 306 ILE B CA     1 
ATOM   6253 C  C      . ILE B 1 310 ? 5.35100   2.79000   10.04500  1.000 34.69363 ? 306 ILE B C      1 
ATOM   6254 O  O      . ILE B 1 310 ? 4.92800   2.25000   11.07800  1.000 34.41992 ? 306 ILE B O      1 
ATOM   6255 C  CB     . ILE B 1 310 ? 7.82200   2.70700   10.46300  1.000 30.88791 ? 306 ILE B CB     1 
ATOM   6256 C  CG1    . ILE B 1 310 ? 9.14000   3.48600   10.44200  1.000 28.85346 ? 306 ILE B CG1    1 
ATOM   6257 C  CG2    . ILE B 1 310 ? 7.85400   1.45400   9.58000   1.000 26.96113 ? 306 ILE B CG2    1 
ATOM   6258 C  CD1    . ILE B 1 310 ? 10.19000  2.98200   11.44500  1.000 26.02680 ? 306 ILE B CD1    1 
ATOM   6259 N  N      . ASP B 1 311 ? 4.73900   2.68600   8.87000   1.000 33.31189 ? 307 ASP B N      1 
ATOM   6260 C  CA     . ASP B 1 311 ? 3.48900   1.95100   8.74800   1.000 29.60092 ? 307 ASP B CA     1 
ATOM   6261 C  C      . ASP B 1 311 ? 3.31400   1.40500   7.33800   1.000 24.70559 ? 307 ASP B C      1 
ATOM   6262 O  O      . ASP B 1 311 ? 3.59800   2.09800   6.35600   1.000 27.82439 ? 307 ASP B O      1 
ATOM   6263 C  CB     . ASP B 1 311 ? 2.29500   2.83100   9.10700   1.000 22.05528 ? 307 ASP B CB     1 
ATOM   6264 C  CG     . ASP B 1 311 ? 1.15700   2.02200   9.68900   1.000 36.34120 ? 307 ASP B CG     1 
ATOM   6265 O  OD1    . ASP B 1 311 ? 0.45600   1.34300   8.90600   1.000 26.56634 ? 307 ASP B OD1    1 
ATOM   6266 O  OD2    . ASP B 1 311 ? 1.00600   2.03900   10.93600  1.000 32.18807 ? 307 ASP B OD2    1 
ATOM   6267 N  N      . ILE B 1 312 ? 2.83200   0.16100   7.23900   1.000 25.33988 ? 308 ILE B N      1 
ATOM   6268 C  CA     . ILE B 1 312 ? 2.58700   -0.40000  5.91200   1.000 30.51418 ? 308 ILE B CA     1 
ATOM   6269 C  C      . ILE B 1 312 ? 1.35100   0.22200   5.25600   1.000 30.96424 ? 308 ILE B C      1 
ATOM   6270 O  O      . ILE B 1 312 ? 1.18100   0.13100   4.03200   1.000 37.25183 ? 308 ILE B O      1 
ATOM   6271 C  CB     . ILE B 1 312 ? 2.47400   -1.93600  5.99100   1.000 28.65344 ? 308 ILE B CB     1 
ATOM   6272 C  CG1    . ILE B 1 312 ? 2.84100   -2.57200  4.65200   1.000 23.22121 ? 308 ILE B CG1    1 
ATOM   6273 C  CG2    . ILE B 1 312 ? 1.06700   -2.38500  6.46500   1.000 25.29514 ? 308 ILE B CG2    1 
ATOM   6274 C  CD1    . ILE B 1 312 ? 2.96500   -4.08900  4.75500   1.000 26.35579 ? 308 ILE B CD1    1 
ATOM   6275 N  N      . ASP B 1 313 ? 0.49200   0.88000   6.03200   1.000 28.90873 ? 309 ASP B N      1 
ATOM   6276 C  CA     . ASP B 1 313 ? -0.72300  1.47400   5.49600   1.000 25.18197 ? 309 ASP B CA     1 
ATOM   6277 C  C      . ASP B 1 313 ? -0.48400  2.96900   5.33600   1.000 30.76685 ? 309 ASP B C      1 
ATOM   6278 O  O      . ASP B 1 313 ? -0.38100  3.67800   6.35000   1.000 31.98541 ? 309 ASP B O      1 
ATOM   6279 C  CB     . ASP B 1 313 ? -1.90900  1.20900   6.43600   1.000 24.41609 ? 309 ASP B CB     1 
ATOM   6280 C  CG     . ASP B 1 313 ? -3.24700  1.76800   5.90100   1.000 31.36429 ? 309 ASP B CG     1 
ATOM   6281 O  OD1    . ASP B 1 313 ? -3.22800  2.57200   4.93400   1.000 26.31368 ? 309 ASP B OD1    1 
ATOM   6282 O  OD2    . ASP B 1 313 ? -4.31700  1.39100   6.45300   1.000 30.42733 ? 309 ASP B OD2    1 
ATOM   6283 N  N      . PRO B 1 314 ? -0.38900  3.50300   4.10800   1.000 33.73036 ? 310 PRO B N      1 
ATOM   6284 C  CA     . PRO B 1 314 ? -0.05600  4.93000   3.96900   1.000 31.21164 ? 310 PRO B CA     1 
ATOM   6285 C  C      . PRO B 1 314 ? -1.12400  5.83900   4.53700   1.000 32.07490 ? 310 PRO B C      1 
ATOM   6286 O  O      . PRO B 1 314 ? -0.80400  6.98100   4.90900   1.000 27.34802 ? 310 PRO B O      1 
ATOM   6287 C  CB     . PRO B 1 314 ? 0.09300   5.11900   2.45300   1.000 30.88791 ? 310 PRO B CB     1 
ATOM   6288 C  CG     . PRO B 1 314 ? -0.72500  4.04200   1.85400   1.000 27.59805 ? 310 PRO B CG     1 
ATOM   6289 C  CD     . PRO B 1 314 ? -0.66800  2.86900   2.80700   1.000 28.27181 ? 310 PRO B CD     1 
ATOM   6290 N  N      . MET B 1 315 ? -2.36700  5.35300   4.65800   1.000 22.26846 ? 311 MET B N      1 
ATOM   6291 C  CA     . MET B 1 315 ? -3.45500  6.16700   5.18600   1.000 27.53488 ? 311 MET B CA     1 
ATOM   6292 C  C      . MET B 1 315 ? -3.35100  6.39100   6.69200   1.000 33.62772 ? 311 MET B C      1 
ATOM   6293 O  O      . MET B 1 315 ? -4.03100  7.28500   7.20500   1.000 33.00133 ? 311 MET B O      1 
ATOM   6294 C  CB     . MET B 1 315 ? -4.81300  5.52800   4.85200   1.000 27.22168 ? 311 MET B CB     1 
ATOM   6295 C  CG     . MET B 1 315 ? -5.00800  5.19900   3.37900   1.000 32.05648 ? 311 MET B CG     1 
ATOM   6296 S  SD     . MET B 1 315 ? -4.29000  6.43100   2.27900   1.000 40.13376 ? 311 MET B SD     1 
ATOM   6297 C  CE     . MET B 1 315 ? -4.26600  5.51200   0.73200   1.000 40.37063 ? 311 MET B CE     1 
ATOM   6298 N  N      . GLU B 1 316 ? -2.52500  5.62300   7.41000   1.000 29.06138 ? 312 GLU B N      1 
ATOM   6299 C  CA     . GLU B 1 316 ? -2.34100  5.83900   8.84300   1.000 28.52710 ? 312 GLU B CA     1 
ATOM   6300 C  C      . GLU B 1 316 ? -1.28200  6.89000   9.15400   1.000 28.71397 ? 312 GLU B C      1 
ATOM   6301 O  O      . GLU B 1 316 ? -1.23000  7.39300   10.28300  1.000 31.45377 ? 312 GLU B O      1 
ATOM   6302 C  CB     . GLU B 1 316 ? -1.95800  4.52000   9.53700   1.000 25.87152 ? 312 GLU B CB     1 
ATOM   6303 C  CG     . GLU B 1 316 ? -3.06400  3.46700   9.55300   1.000 30.52998 ? 312 GLU B CG     1 
ATOM   6304 C  CD     . GLU B 1 316 ? -4.22300  3.86800   10.44800  1.000 38.81781 ? 312 GLU B CD     1 
ATOM   6305 O  OE1    . GLU B 1 316 ? -5.26700  3.17500   10.45400  1.000 44.50007 ? 312 GLU B OE1    1 
ATOM   6306 O  OE2    . GLU B 1 316 ? -4.07800  4.89200   11.14600  1.000 43.43152 ? 312 GLU B OE2    1 
ATOM   6307 N  N      . ILE B 1 317 ? -0.42900  7.22100   8.19300   1.000 30.01149 ? 313 ILE B N      1 
ATOM   6308 C  CA     . ILE B 1 317 ? 0.74500   8.04600   8.45900   1.000 32.75919 ? 313 ILE B CA     1 
ATOM   6309 C  C      . ILE B 1 317 ? 0.32400   9.50200   8.62100   1.000 37.31500 ? 313 ILE B C      1 
ATOM   6310 O  O      . ILE B 1 317 ? -0.25100  10.10200  7.70700   1.000 35.88851 ? 313 ILE B O      1 
ATOM   6311 C  CB     . ILE B 1 317 ? 1.78600   7.88600   7.34300   1.000 32.43547 ? 313 ILE B CB     1 
ATOM   6312 C  CG1    . ILE B 1 317 ? 2.29400   6.44100   7.31400   1.000 28.13758 ? 313 ILE B CG1    1 
ATOM   6313 C  CG2    . ILE B 1 317 ? 2.94100   8.86400   7.55200   1.000 34.03566 ? 313 ILE B CG2    1 
ATOM   6314 C  CD1    . ILE B 1 317 ? 3.28600   6.15500   6.17400   1.000 30.83791 ? 313 ILE B CD1    1 
ATOM   6315 N  N      . GLY B 1 318 ? 0.60300   10.07300  9.79200   1.000 32.90395 ? 314 GLY B N      1 
ATOM   6316 C  CA     . GLY B 1 318 ? 0.22500   11.45000  10.05000  1.000 28.65344 ? 314 GLY B CA     1 
ATOM   6317 C  C      . GLY B 1 318 ? -1.24800  11.66400  10.31300  1.000 29.31667 ? 314 GLY B C      1 
ATOM   6318 O  O      . GLY B 1 318 ? -1.72300  12.79500  10.22500  1.000 32.56180 ? 314 GLY B O      1 
ATOM   6319 N  N      . LYS B 1 319 ? -1.99400  10.60700  10.63400  1.000 27.99546 ? 315 LYS B N      1 
ATOM   6320 C  CA     . LYS B 1 319 ? -3.43800  10.74400  10.80500  1.000 30.99582 ? 315 LYS B CA     1 
ATOM   6321 C  C      . LYS B 1 319 ? -3.76000  11.66100  11.97900  1.000 38.13878 ? 315 LYS B C      1 
ATOM   6322 O  O      . LYS B 1 319 ? -4.51100  12.63100  11.83400  1.000 40.33115 ? 315 LYS B O      1 
ATOM   6323 C  CB     . LYS B 1 319 ? -4.07400  9.36000   10.99600  1.000 30.34574 ? 315 LYS B CB     1 
ATOM   6324 C  CG     . LYS B 1 319 ? -5.60400  9.35200   11.09100  1.000 25.10564 ? 315 LYS B CG     1 
ATOM   6325 C  CD     . LYS B 1 319 ? -6.11100  7.90600   11.18900  1.000 28.92715 ? 315 LYS B CD     1 
ATOM   6326 C  CE     . LYS B 1 319 ? -5.87400  7.34000   12.58500  1.000 34.11725 ? 315 LYS B CE     1 
ATOM   6327 N  NZ     . LYS B 1 319 ? -6.08300  5.87300   12.65500  1.000 32.54601 ? 315 LYS B NZ     1 
ATOM   6328 N  N      . ASN B 1 320 ? -3.17700  11.38300  13.15400  1.000 34.69363 ? 316 ASN B N      1 
ATOM   6329 C  CA     . ASN B 1 320 ? -3.48700  12.11900  14.37400  1.000 30.02465 ? 316 ASN B CA     1 
ATOM   6330 C  C      . ASN B 1 320 ? -2.35500  13.00500  14.87600  1.000 34.05145 ? 316 ASN B C      1 
ATOM   6331 O  O      . ASN B 1 320 ? -2.61900  13.93800  15.63900  1.000 34.62784 ? 316 ASN B O      1 
ATOM   6332 C  CB     . ASN B 1 320 ? -3.87400  11.13900  15.49500  1.000 26.75058 ? 316 ASN B CB     1 
ATOM   6333 C  CG     . ASN B 1 320 ? -5.21000  10.48100  15.24200  1.000 26.94270 ? 316 ASN B CG     1 
ATOM   6334 O  OD1    . ASN B 1 320 ? -6.10400  11.10500  14.71000  1.000 31.78802 ? 316 ASN B OD1    1 
ATOM   6335 N  ND2    . ASN B 1 320 ? -5.34700  9.22000   15.61700  1.000 25.34514 ? 316 ASN B ND2    1 
ATOM   6336 N  N      . TYR B 1 321 ? -1.11400  12.74900  14.45900  1.000 34.13830 ? 317 TYR B N      1 
ATOM   6337 C  CA     . TYR B 1 321 ? 0.04300   13.54400  14.84500  1.000 30.84054 ? 317 TYR B CA     1 
ATOM   6338 C  C      . TYR B 1 321 ? 0.83300   13.89300  13.58900  1.000 34.50677 ? 317 TYR B C      1 
ATOM   6339 O  O      . TYR B 1 321 ? 1.05200   13.01500  12.73500  1.000 31.11426 ? 317 TYR B O      1 
ATOM   6340 C  CB     . TYR B 1 321 ? 0.93400   12.78000  15.82400  1.000 27.00324 ? 317 TYR B CB     1 
ATOM   6341 C  CG     . TYR B 1 321 ? 0.34000   12.58100  17.19000  1.000 26.54002 ? 317 TYR B CG     1 
ATOM   6342 C  CD1    . TYR B 1 321 ? -0.47900  11.48500  17.46200  1.000 33.41453 ? 317 TYR B CD1    1 
ATOM   6343 C  CD2    . TYR B 1 321 ? 0.59300   13.48200  18.21300  1.000 30.84580 ? 317 TYR B CD2    1 
ATOM   6344 C  CE1    . TYR B 1 321 ? -1.03300  11.29600  18.71300  1.000 31.55378 ? 317 TYR B CE1    1 
ATOM   6345 C  CE2    . TYR B 1 321 ? 0.05800   13.29000  19.47600  1.000 33.92249 ? 317 TYR B CE2    1 
ATOM   6346 C  CZ     . TYR B 1 321 ? -0.75900  12.19400  19.71400  1.000 30.41680 ? 317 TYR B CZ     1 
ATOM   6347 O  OH     . TYR B 1 321 ? -1.29300  12.00500  20.96300  1.000 32.97501 ? 317 TYR B OH     1 
ATOM   6348 N  N      . PRO B 1 322 ? 1.26900   15.14100  13.42300  1.000 35.11210 ? 318 PRO B N      1 
ATOM   6349 C  CA     . PRO B 1 322 ? 2.08500   15.47700  12.24600  1.000 41.07335 ? 318 PRO B CA     1 
ATOM   6350 C  C      . PRO B 1 322 ? 3.41800   14.75200  12.30100  1.000 34.18568 ? 318 PRO B C      1 
ATOM   6351 O  O      . PRO B 1 322 ? 4.07600   14.70900  13.34200  1.000 35.40424 ? 318 PRO B O      1 
ATOM   6352 C  CB     . PRO B 1 322 ? 2.27100   16.99800  12.35400  1.000 40.16534 ? 318 PRO B CB     1 
ATOM   6353 C  CG     . PRO B 1 322 ? 2.08500   17.30000  13.79900  1.000 33.79353 ? 318 PRO B CG     1 
ATOM   6354 C  CD     . PRO B 1 322 ? 1.07900   16.29400  14.31900  1.000 31.87487 ? 318 PRO B CD     1 
ATOM   6355 N  N      . VAL B 1 323 ? 3.82600   14.18500  11.16900  1.000 30.52208 ? 319 VAL B N      1 
ATOM   6356 C  CA     . VAL B 1 323 ? 5.07300   13.43300  11.11700  1.000 33.45138 ? 319 VAL B CA     1 
ATOM   6357 C  C      . VAL B 1 323 ? 6.12500   14.25500  10.40100  1.000 37.81506 ? 319 VAL B C      1 
ATOM   6358 O  O      . VAL B 1 323 ? 5.82500   15.08700  9.53700   1.000 35.83588 ? 319 VAL B O      1 
ATOM   6359 C  CB     . VAL B 1 323 ? 4.93300   12.07100  10.41200  1.000 36.78073 ? 319 VAL B CB     1 
ATOM   6360 C  CG1    . VAL B 1 323 ? 3.85000   11.25300  11.08100  1.000 42.94725 ? 319 VAL B CG1    1 
ATOM   6361 C  CG2    . VAL B 1 323 ? 4.63700   12.28700  8.93200   1.000 36.96496 ? 319 VAL B CG2    1 
ATOM   6362 N  N      . ASP B 1 324 ? 7.37600   13.98800  10.75800  1.000 40.07059 ? 320 ASP B N      1 
ATOM   6363 C  CA     . ASP B 1 324 ? 8.52900   14.56300  10.09200  1.000 38.10457 ? 320 ASP B CA     1 
ATOM   6364 C  C      . ASP B 1 324 ? 9.17500   13.59300  9.12500   1.000 38.46777 ? 320 ASP B C      1 
ATOM   6365 O  O      . ASP B 1 324 ? 9.67700   14.01800  8.07900   1.000 36.58860 ? 320 ASP B O      1 
ATOM   6366 C  CB     . ASP B 1 324 ? 9.53000   15.03300  11.14300  1.000 33.56981 ? 320 ASP B CB     1 
ATOM   6367 C  CG     . ASP B 1 324 ? 8.91900   16.06200  12.06800  1.000 43.06306 ? 320 ASP B CG     1 
ATOM   6368 O  OD1    . ASP B 1 324 ? 8.77200   17.22100  11.63600  1.000 47.63729 ? 320 ASP B OD1    1 
ATOM   6369 O  OD2    . ASP B 1 324 ? 8.53100   15.71200  13.20000  1.000 47.13986 ? 320 ASP B OD2    1 
ATOM   6370 N  N      . VAL B 1 325 ? 9.15400   12.30000  9.44300   1.000 33.74878 ? 321 VAL B N      1 
ATOM   6371 C  CA     . VAL B 1 325 ? 9.57000   11.25700  8.52200   1.000 31.74065 ? 321 VAL B CA     1 
ATOM   6372 C  C      . VAL B 1 325 ? 8.44100   10.23900  8.49500   1.000 33.10660 ? 321 VAL B C      1 
ATOM   6373 O  O      . VAL B 1 325 ? 8.21600   9.52500   9.47900   1.000 32.95658 ? 321 VAL B O      1 
ATOM   6374 C  CB     . VAL B 1 325 ? 10.90200  10.61700  8.92100   1.000 34.13830 ? 321 VAL B CB     1 
ATOM   6375 C  CG1    . VAL B 1 325 ? 11.35300  9.63200   7.85200   1.000 36.47279 ? 321 VAL B CG1    1 
ATOM   6376 C  CG2    . VAL B 1 325 ? 11.95800  11.70500  9.08800   1.000 31.81171 ? 321 VAL B CG2    1 
ATOM   6377 N  N      . GLY B 1 326 ? 7.71700   10.19000  7.38500   1.000 30.37996 ? 322 GLY B N      1 
ATOM   6378 C  CA     . GLY B 1 326 ? 6.62200   9.25600   7.23900   1.000 33.63824 ? 322 GLY B CA     1 
ATOM   6379 C  C      . GLY B 1 326 ? 6.99100   8.13600   6.29400   1.000 33.57508 ? 322 GLY B C      1 
ATOM   6380 O  O      . GLY B 1 326 ? 7.07600   8.34300   5.08200   1.000 30.57209 ? 322 GLY B O      1 
ATOM   6381 N  N      . ILE B 1 327 ? 7.22500   6.95100   6.84100   1.000 30.90897 ? 323 ILE B N      1 
ATOM   6382 C  CA     . ILE B 1 327 ? 7.78300   5.83200   6.09800   1.000 29.24298 ? 323 ILE B CA     1 
ATOM   6383 C  C      . ILE B 1 327 ? 6.67000   4.84400   5.81900   1.000 32.33809 ? 323 ILE B C      1 
ATOM   6384 O  O      . ILE B 1 327 ? 6.10800   4.24500   6.74700   1.000 25.59254 ? 323 ILE B O      1 
ATOM   6385 C  CB     . ILE B 1 327 ? 8.92700   5.16000   6.87600   1.000 30.57998 ? 323 ILE B CB     1 
ATOM   6386 C  CG1    . ILE B 1 327 ? 10.08300  6.14900   7.08300   1.000 29.60618 ? 323 ILE B CG1    1 
ATOM   6387 C  CG2    . ILE B 1 327 ? 9.38300   3.90400   6.16700   1.000 29.17718 ? 323 ILE B CG2    1 
ATOM   6388 C  CD1    . ILE B 1 327 ? 11.20800  5.58700   7.95400   1.000 29.19824 ? 323 ILE B CD1    1 
ATOM   6389 N  N      . ASN B 1 328 ? 6.35300   4.66800   4.54500   1.000 31.87224 ? 324 ASN B N      1 
ATOM   6390 C  CA     . ASN B 1 328 ? 5.35900   3.68300   4.13600   1.000 34.24358 ? 324 ASN B CA     1 
ATOM   6391 C  C      . ASN B 1 328 ? 6.10000   2.40300   3.76800   1.000 31.73802 ? 324 ASN B C      1 
ATOM   6392 O  O      . ASN B 1 328 ? 6.62500   2.27100   2.66000   1.000 32.79341 ? 324 ASN B O      1 
ATOM   6393 C  CB     . ASN B 1 328 ? 4.51800   4.21000   2.98500   1.000 30.00623 ? 324 ASN B CB     1 
ATOM   6394 C  CG     . ASN B 1 328 ? 3.50900   3.19800   2.52000   1.000 30.65631 ? 324 ASN B CG     1 
ATOM   6395 O  OD1    . ASN B 1 328 ? 3.00400   2.40500   3.31600   1.000 30.76421 ? 324 ASN B OD1    1 
ATOM   6396 N  ND2    . ASN B 1 328 ? 3.23300   3.19100   1.22500   1.000 27.72701 ? 324 ASN B ND2    1 
ATOM   6397 N  N      . ALA B 1 329 ? 6.18200   1.47300   4.71300   1.000 25.18197 ? 325 ALA B N      1 
ATOM   6398 C  CA     . ALA B 1 329 ? 6.95700   0.25800   4.49400   1.000 26.87164 ? 325 ALA B CA     1 
ATOM   6399 C  C      . ALA B 1 329 ? 6.60700   -0.75900  5.56900   1.000 30.78790 ? 325 ALA B C      1 
ATOM   6400 O  O      . ALA B 1 329 ? 6.05800   -0.42600  6.62300   1.000 31.14584 ? 325 ALA B O      1 
ATOM   6401 C  CB     . ALA B 1 329 ? 8.47300   0.53800   4.50600   1.000 25.59517 ? 325 ALA B CB     1 
ATOM   6402 N  N      . ASP B 1 330 ? 6.96400   -2.00200  5.29500   1.000 28.81398 ? 326 ASP B N      1 
ATOM   6403 C  CA     . ASP B 1 330 ? 6.84900   -3.06200  6.27800   1.000 28.59290 ? 326 ASP B CA     1 
ATOM   6404 C  C      . ASP B 1 330 ? 7.81100   -2.80500  7.44100   1.000 35.41477 ? 326 ASP B C      1 
ATOM   6405 O  O      . ASP B 1 330 ? 8.92700   -2.29600  7.24900   1.000 29.70619 ? 326 ASP B O      1 
ATOM   6406 C  CB     . ASP B 1 330 ? 7.13800   -4.39100  5.58400   1.000 32.64865 ? 326 ASP B CB     1 
ATOM   6407 C  CG     . ASP B 1 330 ? 7.29900   -5.53800  6.55000   1.000 37.81506 ? 326 ASP B CG     1 
ATOM   6408 O  OD1    . ASP B 1 330 ? 6.28500   -6.19300  6.84400   1.000 38.81781 ? 326 ASP B OD1    1 
ATOM   6409 O  OD2    . ASP B 1 330 ? 8.43800   -5.80800  6.98000   1.000 39.30471 ? 326 ASP B OD2    1 
ATOM   6410 N  N      . ALA B 1 331 ? 7.35700   -3.11800  8.66400   1.000 30.85370 ? 327 ALA B N      1 
ATOM   6411 C  CA     . ALA B 1 331 ? 8.15800   -2.82000  9.85600   1.000 31.04056 ? 327 ALA B CA     1 
ATOM   6412 C  C      . ALA B 1 331 ? 9.44700   -3.63200  9.89300   1.000 30.57472 ? 327 ALA B C      1 
ATOM   6413 O  O      . ALA B 1 331 ? 10.48800  -3.14600  10.35900  1.000 31.45904 ? 327 ALA B O      1 
ATOM   6414 C  CB     . ALA B 1 331 ? 7.35800   -3.08700  11.13200  1.000 25.42410 ? 327 ALA B CB     1 
ATOM   6415 N  N      . SER B 1 332 ? 9.39100   -4.88800  9.45400   1.000 32.52758 ? 328 SER B N      1 
ATOM   6416 C  CA     . SER B 1 332 ? 10.58300  -5.72400  9.49500   1.000 30.65368 ? 328 SER B CA     1 
ATOM   6417 C  C      . SER B 1 332 ? 11.60600  -5.26400  8.46200   1.000 35.84640 ? 328 SER B C      1 
ATOM   6418 O  O      . SER B 1 332 ? 12.80900  -5.19900  8.75200   1.000 33.00659 ? 328 SER B O      1 
ATOM   6419 C  CB     . SER B 1 332 ? 10.19800  -7.18200  9.25500   1.000 37.68347 ? 328 SER B CB     1 
ATOM   6420 O  OG     . SER B 1 332 ? 11.30400  -7.90900  8.75700   1.000 56.52520 ? 328 SER B OG     1 
ATOM   6421 N  N      . GLU B 1 333 ? 11.14700  -4.91400  7.25600   1.000 34.85944 ? 329 GLU B N      1 
ATOM   6422 C  CA     . GLU B 1 333 ? 12.07300  -4.43000  6.23400   1.000 34.23042 ? 329 GLU B CA     1 
ATOM   6423 C  C      . GLU B 1 333 ? 12.71400  -3.11500  6.65500   1.000 28.56132 ? 329 GLU B C      1 
ATOM   6424 O  O      . GLU B 1 333 ? 13.91700  -2.90900  6.46100   1.000 31.77223 ? 329 GLU B O      1 
ATOM   6425 C  CB     . GLU B 1 333 ? 11.34500  -4.27900  4.89700   1.000 33.01975 ? 329 GLU B CB     1 
ATOM   6426 C  CG     . GLU B 1 333 ? 10.91500  -5.62000  4.29000   1.000 45.87392 ? 329 GLU B CG     1 
ATOM   6427 C  CD     . GLU B 1 333 ? 12.08600  -6.60500  4.15100   1.000 53.77750 ? 329 GLU B CD     1 
ATOM   6428 O  OE1    . GLU B 1 333 ? 13.19600  -6.16500  3.80700   1.000 51.63514 ? 329 GLU B OE1    1 
ATOM   6429 O  OE2    . GLU B 1 333 ? 11.89300  -7.81700  4.39400   1.000 57.43057 ? 329 GLU B OE2    1 
ATOM   6430 N  N      . THR B 1 334 ? 11.93300  -2.23400  7.27900   1.000 31.74591 ? 330 THR B N      1 
ATOM   6431 C  CA     . THR B 1 334 ? 12.46800  -0.96100  7.74500   1.000 27.74806 ? 330 THR B CA     1 
ATOM   6432 C  C      . THR B 1 334 ? 13.52200  -1.16800  8.82500   1.000 28.66133 ? 330 THR B C      1 
ATOM   6433 O  O      . THR B 1 334 ? 14.60700  -0.57700  8.77400   1.000 32.21176 ? 330 THR B O      1 
ATOM   6434 C  CB     . THR B 1 334 ? 11.33100  -0.09100  8.28100   1.000 33.31189 ? 330 THR B CB     1 
ATOM   6435 O  OG1    . THR B 1 334 ? 10.34200  0.08100   7.26000   1.000 31.53536 ? 330 THR B OG1    1 
ATOM   6436 C  CG2    . THR B 1 334 ? 11.86200  1.27900   8.72900   1.000 28.81398 ? 330 THR B CG2    1 
ATOM   6437 N  N      . LEU B 1 335 ? 13.21800  -2.00200  9.82100   1.000 32.58812 ? 331 LEU B N      1 
ATOM   6438 C  CA     . LEU B 1 335 ? 14.17000  -2.21500  10.90700  1.000 33.20661 ? 331 LEU B CA     1 
ATOM   6439 C  C      . LEU B 1 335 ? 15.45400  -2.85100  10.39400  1.000 30.47997 ? 331 LEU B C      1 
ATOM   6440 O  O      . LEU B 1 335 ? 16.55000  -2.47600  10.82200  1.000 32.84604 ? 331 LEU B O      1 
ATOM   6441 C  CB     . LEU B 1 335 ? 13.53500  -3.06700  12.01300  1.000 33.65930 ? 331 LEU B CB     1 
ATOM   6442 C  CG     . LEU B 1 335 ? 12.49200  -2.32500  12.86900  1.000 33.97249 ? 331 LEU B CG     1 
ATOM   6443 C  CD1    . LEU B 1 335 ? 11.57000  -3.29900  13.60800  1.000 28.77977 ? 331 LEU B CD1    1 
ATOM   6444 C  CD2    . LEU B 1 335 ? 13.19100  -1.37900  13.85300  1.000 34.54888 ? 331 LEU B CD2    1 
ATOM   6445 N  N      . LYS B 1 336 ? 15.34200  -3.81200  9.47300   1.000 31.61432 ? 332 LYS B N      1 
ATOM   6446 C  CA     . LYS B 1 336 ? 16.54000  -4.41500  8.88900   1.000 31.00898 ? 332 LYS B CA     1 
ATOM   6447 C  C      . LYS B 1 336 ? 17.38900  -3.36900  8.18100   1.000 32.67497 ? 332 LYS B C      1 
ATOM   6448 O  O      . LYS B 1 336 ? 18.62300  -3.36200  8.30100   1.000 33.79089 ? 332 LYS B O      1 
ATOM   6449 C  CB     . LYS B 1 336 ? 16.15600  -5.52300  7.90700   1.000 37.47555 ? 332 LYS B CB     1 
ATOM   6450 C  CG     . LYS B 1 336 ? 15.46600  -6.72800  8.53600   1.000 51.38248 ? 332 LYS B CG     1 
ATOM   6451 C  CD     . LYS B 1 336 ? 15.58500  -7.96500  7.65100   1.000 63.23127 ? 332 LYS B CD     1 
ATOM   6452 C  CE     . LYS B 1 336 ? 14.25100  -8.34200  7.02300   1.000 70.55846 ? 332 LYS B CE     1 
ATOM   6453 N  NZ     . LYS B 1 336 ? 13.67400  -9.56400  7.65100   1.000 75.34588 ? 332 LYS B NZ     1 
ATOM   6454 N  N      . ALA B 1 337 ? 16.75100  -2.50300  7.39300   1.000 30.91423 ? 333 ALA B N      1 
ATOM   6455 C  CA     . ALA B 1 337 ? 17.50200  -1.46400  6.70000   1.000 31.81171 ? 333 ALA B CA     1 
ATOM   6456 C  C      . ALA B 1 337 ? 18.17400  -0.53500  7.69900   1.000 38.40724 ? 333 ALA B C      1 
ATOM   6457 O  O      . ALA B 1 337 ? 19.35500  -0.19100  7.55500   1.000 38.18089 ? 333 ALA B O      1 
ATOM   6458 C  CB     . ALA B 1 337 ? 16.57900  -0.68300  5.76100   1.000 35.30950 ? 333 ALA B CB     1 
ATOM   6459 N  N      . LEU B 1 338 ? 17.43900  -0.13800  8.73500   1.000 37.27815 ? 334 LEU B N      1 
ATOM   6460 C  CA     . LEU B 1 338 ? 18.01300  0.72800   9.75100   1.000 35.10421 ? 334 LEU B CA     1 
ATOM   6461 C  C      . LEU B 1 338 ? 19.17000  0.03500   10.45900  1.000 35.40688 ? 334 LEU B C      1 
ATOM   6462 O  O      . LEU B 1 338 ? 20.18500  0.66600   10.77000  1.000 37.38606 ? 334 LEU B O      1 
ATOM   6463 C  CB     . LEU B 1 338 ? 16.93500  1.13300   10.74700  1.000 37.61504 ? 334 LEU B CB     1 
ATOM   6464 C  CG     . LEU B 1 338 ? 15.92400  2.17900   10.29500  1.000 40.75752 ? 334 LEU B CG     1 
ATOM   6465 C  CD1    . LEU B 1 338 ? 14.79300  2.27700   11.30800  1.000 31.89330 ? 334 LEU B CD1    1 
ATOM   6466 C  CD2    . LEU B 1 338 ? 16.60200  3.53400   10.07900  1.000 47.11354 ? 334 LEU B CD2    1 
ATOM   6467 N  N      . ILE B 1 339 ? 19.03200  -1.26000  10.73600  1.000 36.50174 ? 335 ILE B N      1 
ATOM   6468 C  CA     . ILE B 1 339 ? 20.13800  -1.98800  11.34800  1.000 40.67330 ? 335 ILE B CA     1 
ATOM   6469 C  C      . ILE B 1 339 ? 21.32000  -2.04600  10.38700  1.000 39.40472 ? 335 ILE B C      1 
ATOM   6470 O  O      . ILE B 1 339 ? 22.47700  -1.86000  10.78800  1.000 42.69722 ? 335 ILE B O      1 
ATOM   6471 C  CB     . ILE B 1 339 ? 19.68800  -3.38400  11.80100  1.000 37.72821 ? 335 ILE B CB     1 
ATOM   6472 C  CG1    . ILE B 1 339 ? 18.68900  -3.25200  12.95400  1.000 36.70966 ? 335 ILE B CG1    1 
ATOM   6473 C  CG2    . ILE B 1 339 ? 20.90600  -4.19900  12.25700  1.000 44.14213 ? 335 ILE B CG2    1 
ATOM   6474 C  CD1    . ILE B 1 339 ? 17.89900  -4.51000  13.24300  1.000 36.95180 ? 335 ILE B CD1    1 
ATOM   6475 N  N      . LEU B 1 340 ? 21.05300  -2.27400  9.09600   1.000 36.45700 ? 336 LEU B N      1 
ATOM   6476 C  CA     . LEU B 1 340 ? 22.13600  -2.24600  8.10700   1.000 40.54433 ? 336 LEU B CA     1 
ATOM   6477 C  C      . LEU B 1 340 ? 22.83000  -0.91400  8.04700   1.000 43.69998 ? 336 LEU B C      1 
ATOM   6478 O  O      . LEU B 1 340 ? 24.06300  -0.85300  8.00800   1.000 46.25555 ? 336 LEU B O      1 
ATOM   6479 C  CB     . LEU B 1 340 ? 21.60500  -2.52100  6.69800   1.000 53.81172 ? 336 LEU B CB     1 
ATOM   6480 C  CG     . LEU B 1 340 ? 22.67000  -2.87600  5.65600   1.000 64.82093 ? 336 LEU B CG     1 
ATOM   6481 C  CD1    . LEU B 1 340 ? 23.74600  -3.81500  6.13500   1.000 71.86125 ? 336 LEU B CD1    1 
ATOM   6482 C  CD2    . LEU B 1 340 ? 22.03600  -3.31200  4.31700   1.000 61.11259 ? 336 LEU B CD2    1 
ATOM   6483 N  N      . CYS B 1 341 ? 22.06000  0.16000   8.09600   1.000 47.06354 ? 337 CYS B N      1 
ATOM   6484 C  CA     . CYS B 1 341 ? 22.67200  1.47000   7.94700   1.000 45.74496 ? 337 CYS B CA     1 
ATOM   6485 C  C      . CYS B 1 341 ? 23.51800  1.81100   9.16200   1.000 46.38714 ? 337 CYS B C      1 
ATOM   6486 O  O      . CYS B 1 341 ? 24.69000  2.17800   9.03400   1.000 47.31883 ? 337 CYS B O      1 
ATOM   6487 C  CB     . CYS B 1 341 ? 21.58100  2.51600   7.73200   1.000 43.50785 ? 337 CYS B CB     1 
ATOM   6488 S  SG     . CYS B 1 341 ? 22.17600  4.19400   7.56200   1.000 48.10314 ? 337 CYS B SG     1 
ATOM   6489 N  N      . ILE B 1 342 ? 22.96000  1.61600   10.35400  1.000 47.59518 ? 338 ILE B N      1 
ATOM   6490 C  CA     . ILE B 1 342 ? 23.64700  2.03900   11.56700  1.000 48.41896 ? 338 ILE B CA     1 
ATOM   6491 C  C      . ILE B 1 342 ? 24.89300  1.19800   11.82500  1.000 49.64279 ? 338 ILE B C      1 
ATOM   6492 O  O      . ILE B 1 342 ? 25.95000  1.72900   12.18700  1.000 50.20865 ? 338 ILE B O      1 
ATOM   6493 C  CB     . ILE B 1 342 ? 22.67400  2.00500   12.75600  1.000 45.15015 ? 338 ILE B CB     1 
ATOM   6494 C  CG1    . ILE B 1 342 ? 21.60600  3.07500   12.56300  1.000 47.96365 ? 338 ILE B CG1    1 
ATOM   6495 C  CG2    . ILE B 1 342 ? 23.42100  2.21200   14.06200  1.000 42.25243 ? 338 ILE B CG2    1 
ATOM   6496 C  CD1    . ILE B 1 342 ? 20.35400  2.84400   13.36500  1.000 44.18688 ? 338 ILE B CD1    1 
ATOM   6497 N  N      . ARG B 1 343 ? 24.81000  -0.11500  11.61200  1.000 46.49768 ? 339 ARG B N      1 
ATOM   6498 C  CA     . ARG B 1 343 ? 25.97200  -0.96600  11.86700  1.000 50.56922 ? 339 ARG B CA     1 
ATOM   6499 C  C      . ARG B 1 343 ? 27.12600  -0.63900  10.92900  1.000 57.35951 ? 339 ARG B C      1 
ATOM   6500 O  O      . ARG B 1 343 ? 28.24100  -0.34700  11.36600  1.000 53.30113 ? 339 ARG B O      1 
ATOM   6501 C  CB     . ARG B 1 343 ? 25.59500  -2.43800  11.72800  1.000 53.86172 ? 339 ARG B CB     1 
ATOM   6502 C  CG     . ARG B 1 343 ? 24.93000  -3.02400  12.93700  1.000 53.92752 ? 339 ARG B CG     1 
ATOM   6503 C  CD     . ARG B 1 343 ? 25.47700  -4.39400  13.26200  1.000 60.04931 ? 339 ARG B CD     1 
ATOM   6504 N  NE     . ARG B 1 343 ? 24.52900  -5.11200  14.09800  1.000 67.56863 ? 339 ARG B NE     1 
ATOM   6505 C  CZ     . ARG B 1 343 ? 23.66200  -6.00500  13.63700  1.000 67.69759 ? 339 ARG B CZ     1 
ATOM   6506 N  NH1    . ARG B 1 343 ? 23.63500  -6.30300  12.34200  1.000 69.47412 ? 339 ARG B NH1    1 
ATOM   6507 N  NH2    . ARG B 1 343 ? 22.82800  -6.60600  14.47000  1.000 62.02059 ? 339 ARG B NH2    1 
ATOM   6508 N  N      . SER B 1 344 ? 26.87300  -0.72800  9.62500   1.000 50.55080 ? 340 SER B N      1 
ATOM   6509 C  CA     . SER B 1 344 ? 27.87500  -0.40900  8.61100   1.000 54.76709 ? 340 SER B CA     1 
ATOM   6510 C  C      . SER B 1 344 ? 28.55500  0.94300   8.88100   1.000 49.66911 ? 340 SER B C      1 
ATOM   6511 O  O      . SER B 1 344 ? 29.76400  1.09300   8.63600   1.000 52.29574 ? 340 SER B O      1 
ATOM   6512 C  CB     . SER B 1 344 ? 27.20200  -0.47400  7.24600   1.000 58.38595 ? 340 SER B CB     1 
ATOM   6513 O  OG     . SER B 1 344 ? 27.74000  0.43100   6.30900   1.000 70.86639 ? 340 SER B OG     1 
ATOM   6514 N  N      . SER B 1 345 ? 27.80800  1.94700   9.35900   1.000 49.38750 ? 341 SER B N      1 
ATOM   6515 C  CA     . SER B 1 345 ? 28.38700  3.23500   9.75500   1.000 48.82427 ? 341 SER B CA     1 
ATOM   6516 C  C      . SER B 1 345 ? 29.51000  3.06900   10.76800  1.000 56.63574 ? 341 SER B C      1 
ATOM   6517 O  O      . SER B 1 345 ? 30.49500  3.81100   10.73400  1.000 63.43919 ? 341 SER B O      1 
ATOM   6518 C  CB     . SER B 1 345 ? 27.30600  4.15900   10.31400  1.000 54.83289 ? 341 SER B CB     1 
ATOM   6519 O  OG     . SER B 1 345 ? 27.17800  3.99600   11.71600  1.000 56.56994 ? 341 SER B OG     1 
ATOM   6520 N  N      . GLY B 1 346 ? 29.32800  2.18700   11.75400  1.000 60.35987 ? 342 GLY B N      1 
ATOM   6521 C  CA     . GLY B 1 346 ? 30.26900  2.06400   12.85400  1.000 58.05433 ? 342 GLY B CA     1 
ATOM   6522 C  C      . GLY B 1 346 ? 30.11100  3.06400   13.97700  1.000 61.39420 ? 342 GLY B C      1 
ATOM   6523 O  O      . GLY B 1 346 ? 30.93800  3.06800   14.89200  1.000 61.49948 ? 342 GLY B O      1 
ATOM   6524 N  N      . LYS B 1 347 ? 29.07700  3.90500   13.94900  1.000 69.65835 ? 343 LYS B N      1 
ATOM   6525 C  CA     . LYS B 1 347 ? 28.88300  4.93300   14.97300  1.000 71.53752 ? 343 LYS B CA     1 
ATOM   6526 C  C      . LYS B 1 347 ? 28.15300  4.39200   16.20500  1.000 68.68455 ? 343 LYS B C      1 
ATOM   6527 O  O      . LYS B 1 347 ? 28.77500  3.84800   17.12200  1.000 70.42423 ? 343 LYS B O      1 
ATOM   6528 C  CB     . LYS B 1 347 ? 28.11400  6.12200   14.38600  1.000 73.29037 ? 343 LYS B CB     1 
ATOM   6529 C  CG     . LYS B 1 347 ? 28.53300  7.47800   14.94700  1.000 79.03053 ? 343 LYS B CG     1 
ATOM   6530 C  CD     . LYS B 1 347 ? 30.01700  7.77700   14.67200  1.000 83.42053 ? 343 LYS B CD     1 
ATOM   6531 C  CE     . LYS B 1 347 ? 30.24200  8.32100   13.25800  1.000 83.14155 ? 343 LYS B CE     1 
ATOM   6532 N  NZ     . LYS B 1 347 ? 31.64500  8.13600   12.78800  1.000 80.18593 ? 343 LYS B NZ     1 
ATOM   6533 N  N      . GLY B 1 375 ? -13.33500 -12.01900 47.87300  1.000 50.09811 ? 371 GLY B N      1 
ATOM   6534 C  CA     . GLY B 1 375 ? -12.69500 -12.80800 46.83400  1.000 54.44337 ? 371 GLY B CA     1 
ATOM   6535 C  C      . GLY B 1 375 ? -11.19300 -12.59900 46.74300  1.000 57.73061 ? 371 GLY B C      1 
ATOM   6536 O  O      . GLY B 1 375 ? -10.59400 -12.01000 47.63700  1.000 60.98889 ? 371 GLY B O      1 
ATOM   6537 N  N      . ILE B 1 376 ? -10.57700 -13.06000 45.65300  1.000 50.64555 ? 372 ILE B N      1 
ATOM   6538 C  CA     . ILE B 1 376 ? -9.14700  -12.86200 45.43200  1.000 46.59243 ? 372 ILE B CA     1 
ATOM   6539 C  C      . ILE B 1 376 ? -8.94400  -11.53600 44.72100  1.000 39.95216 ? 372 ILE B C      1 
ATOM   6540 O  O      . ILE B 1 376 ? -9.66700  -11.20300 43.77400  1.000 42.83935 ? 372 ILE B O      1 
ATOM   6541 C  CB     . ILE B 1 376 ? -8.53300  -14.01000 44.60800  1.000 47.87679 ? 372 ILE B CB     1 
ATOM   6542 C  CG1    . ILE B 1 376 ? -8.90700  -15.37300 45.18200  1.000 49.52173 ? 372 ILE B CG1    1 
ATOM   6543 C  CG2    . ILE B 1 376 ? -7.01800  -13.86600 44.53700  1.000 45.14752 ? 372 ILE B CG2    1 
ATOM   6544 C  CD1    . ILE B 1 376 ? -8.33900  -16.51400 44.36600  1.000 48.35053 ? 372 ILE B CD1    1 
ATOM   6545 N  N      . HIS B 1 377 ? -7.96500  -10.77600 45.16800  1.000 39.47315 ? 373 HIS B N      1 
ATOM   6546 C  CA     . HIS B 1 377 ? -7.64700  -9.53600  44.48800  1.000 37.94402 ? 373 HIS B CA     1 
ATOM   6547 C  C      . HIS B 1 377 ? -7.07800  -9.85900  43.11300  1.000 38.29670 ? 373 HIS B C      1 
ATOM   6548 O  O      . HIS B 1 377 ? -6.16200  -10.68000 43.00000  1.000 38.50462 ? 373 HIS B O      1 
ATOM   6549 C  CB     . HIS B 1 377 ? -6.66500  -8.69600  45.29900  1.000 38.90203 ? 373 HIS B CB     1 
ATOM   6550 C  CG     . HIS B 1 377 ? -6.51900  -7.29600  44.79000  1.000 48.22683 ? 373 HIS B CG     1 
ATOM   6551 N  ND1    . HIS B 1 377 ? -5.86300  -6.99900  43.61500  1.000 46.97142 ? 373 HIS B ND1    1 
ATOM   6552 C  CD2    . HIS B 1 377 ? -6.95600  -6.11400  45.28700  1.000 49.37960 ? 373 HIS B CD2    1 
ATOM   6553 C  CE1    . HIS B 1 377 ? -5.89300  -5.69400  43.41400  1.000 46.83719 ? 373 HIS B CE1    1 
ATOM   6554 N  NE2    . HIS B 1 377 ? -6.54900  -5.13300  44.41400  1.000 48.37948 ? 373 HIS B NE2    1 
ATOM   6555 N  N      . PRO B 1 378 ? -7.60100  -9.26000  42.05000  1.000 38.62042 ? 374 PRO B N      1 
ATOM   6556 C  CA     . PRO B 1 378 ? -7.17200  -9.67200  40.71000  1.000 38.35723 ? 374 PRO B CA     1 
ATOM   6557 C  C      . PRO B 1 378 ? -5.68000  -9.54800  40.49800  1.000 43.41310 ? 374 PRO B C      1 
ATOM   6558 O  O      . PRO B 1 378 ? -5.10200  -10.32700 39.72700  1.000 36.39384 ? 374 PRO B O      1 
ATOM   6559 C  CB     . PRO B 1 378 ? -7.95700  -8.72600  39.79100  1.000 40.54697 ? 374 PRO B CB     1 
ATOM   6560 C  CG     . PRO B 1 378 ? -9.20000  -8.39300  40.59200  1.000 38.25985 ? 374 PRO B CG     1 
ATOM   6561 C  CD     . PRO B 1 378 ? -8.69700  -8.28000  42.01700  1.000 37.69663 ? 374 PRO B CD     1 
ATOM   6562 N  N      . ALA B 1 379 ? -5.03300  -8.65200  41.21000  1.000 42.63143 ? 375 ALA B N      1 
ATOM   6563 C  CA     . ALA B 1 379 ? -3.59600  -8.53700  41.08600  1.000 45.18173 ? 375 ALA B CA     1 
ATOM   6564 C  C      . ALA B 1 379 ? -2.87500  -9.76900  41.60700  1.000 47.28198 ? 375 ALA B C      1 
ATOM   6565 O  O      . ALA B 1 379 ? -1.85800  -10.13900 41.10800  1.000 39.03889 ? 375 ALA B O      1 
ATOM   6566 C  CB     . ALA B 1 379 ? -3.09100  -7.30300  41.76800  1.000 40.10481 ? 375 ALA B CB     1 
ATOM   6567 N  N      . MET B 1 380 ? -3.45300  -10.39700 42.62700  1.000 46.67402 ? 376 MET B N      1 
ATOM   6568 C  CA     . MET B 1 380 ? -2.88000  -11.60600 43.20200  1.000 44.70273 ? 376 MET B CA     1 
ATOM   6569 C  C      . MET B 1 380 ? -3.00200  -12.73000 42.18100  1.000 43.46311 ? 376 MET B C      1 
ATOM   6570 O  O      . MET B 1 380 ? -2.09500  -13.54700 42.02500  1.000 43.16833 ? 376 MET B O      1 
ATOM   6571 C  CB     . MET B 1 380 ? -3.60100  -11.98200 44.49700  1.000 48.87691 ? 376 MET B CB     1 
ATOM   6572 C  CG     . MET B 1 380 ? -3.28200  -11.07200 45.67100  1.000 71.90336 ? 376 MET B CG     1 
ATOM   6573 S  SD     . MET B 1 380 ? -3.37200  -11.92500 47.25700  1.000 91.00828 ? 376 MET B SD     1 
ATOM   6574 C  CE     . MET B 1 380 ? -5.07800  -11.61900 47.70900  1.000 83.30999 ? 376 MET B CE     1 
ATOM   6575 N  N      . VAL B 1 381 ? -4.13600  -12.75900 41.48700  1.000 36.05695 ? 377 VAL B N      1 
ATOM   6576 C  CA     . VAL B 1 381 ? -4.38300  -13.74500 40.47300  1.000 40.30220 ? 377 VAL B CA     1 
ATOM   6577 C  C      . VAL B 1 381 ? -3.32000  -13.65700 39.39700  1.000 39.48105 ? 377 VAL B C      1 
ATOM   6578 O  O      . VAL B 1 381 ? -2.74400  -14.64000 39.05100  1.000 36.64124 ? 377 VAL B O      1 
ATOM   6579 C  CB     . VAL B 1 381 ? -5.74500  -13.54700 39.81400  1.000 36.44121 ? 377 VAL B CB     1 
ATOM   6580 C  CG1    . VAL B 1 381 ? -5.91100  -14.47900 38.66800  1.000 32.81709 ? 377 VAL B CG1    1 
ATOM   6581 C  CG2    . VAL B 1 381 ? -6.85200  -13.69100 40.82000  1.000 39.58896 ? 377 VAL B CG2    1 
ATOM   6582 N  N      . VAL B 1 382 ? -3.07800  -12.45700 38.89600  1.000 33.88827 ? 378 VAL B N      1 
ATOM   6583 C  CA     . VAL B 1 382 ? -2.06600  -12.26300 37.86200  1.000 35.10947 ? 378 VAL B CA     1 
ATOM   6584 C  C      . VAL B 1 382 ? -0.68600  -12.61700 38.39500  1.000 37.28868 ? 378 VAL B C      1 
ATOM   6585 O  O      . VAL B 1 382 ? 0.12600   -13.24500 37.70200  1.000 40.29430 ? 378 VAL B O      1 
ATOM   6586 C  CB     . VAL B 1 382 ? -2.09600  -10.82200 37.32000  1.000 38.21511 ? 378 VAL B CB     1 
ATOM   6587 C  CG1    . VAL B 1 382 ? -0.97900  -10.62700 36.29700  1.000 35.66480 ? 378 VAL B CG1    1 
ATOM   6588 C  CG2    . VAL B 1 382 ? -3.44700  -10.50100 36.70600  1.000 37.07813 ? 378 VAL B CG2    1 
ATOM   6589 N  N      . GLU B 1 383 ? -0.39700  -12.23300 39.63600  1.000 37.21762 ? 379 GLU B N      1 
ATOM   6590 C  CA     . GLU B 1 383 ? 0.88600   -12.60100 40.21600  1.000 38.32302 ? 379 GLU B CA     1 
ATOM   6591 C  C      . GLU B 1 383 ? 1.03400   -14.11300 40.27700  1.000 44.43691 ? 379 GLU B C      1 
ATOM   6592 O  O      . GLU B 1 383 ? 2.07100   -14.66100 39.88700  1.000 42.64459 ? 379 GLU B O      1 
ATOM   6593 C  CB     . GLU B 1 383 ? 1.02700   -11.97600 41.60300  1.000 46.01868 ? 379 GLU B CB     1 
ATOM   6594 C  CG     . GLU B 1 383 ? 2.37000   -12.27100 42.26300  1.000 59.62820 ? 379 GLU B CG     1 
ATOM   6595 C  CD     . GLU B 1 383 ? 2.55300   -11.52200 43.57200  1.000 75.12480 ? 379 GLU B CD     1 
ATOM   6596 O  OE1    . GLU B 1 383 ? 2.16400   -12.06800 44.62500  1.000 79.90695 ? 379 GLU B OE1    1 
ATOM   6597 O  OE2    . GLU B 1 383 ? 3.08100   -10.38700 43.54600  1.000 79.62534 ? 379 GLU B OE2    1 
ATOM   6598 N  N      . ALA B 1 384 ? -0.01700  -14.80400 40.72800  1.000 43.78157 ? 380 ALA B N      1 
ATOM   6599 C  CA     . ALA B 1 384 ? 0.03400   -16.26200 40.79900  1.000 41.84449 ? 380 ALA B CA     1 
ATOM   6600 C  C      . ALA B 1 384 ? 0.21400   -16.87500 39.41400  1.000 39.74424 ? 380 ALA B C      1 
ATOM   6601 O  O      . ALA B 1 384 ? 0.98400   -17.82800 39.23600  1.000 37.56240 ? 380 ALA B O      1 
ATOM   6602 C  CB     . ALA B 1 384 ? -1.23000  -16.80200 41.46400  1.000 43.38678 ? 380 ALA B CB     1 
ATOM   6603 N  N      . MET B 1 385 ? -0.49100  -16.33900 38.41700  1.000 37.15445 ? 381 MET B N      1 
ATOM   6604 C  CA     . MET B 1 385 ? -0.27200  -16.77500 37.04200  1.000 39.49684 ? 381 MET B CA     1 
ATOM   6605 C  C      . MET B 1 385 ? 1.18000   -16.58400 36.63500  1.000 39.45736 ? 381 MET B C      1 
ATOM   6606 O  O      . MET B 1 385 ? 1.78700   -17.47000 36.02400  1.000 41.36549 ? 381 MET B O      1 
ATOM   6607 C  CB     . MET B 1 385 ? -1.18200  -16.00100 36.08900  1.000 36.45700 ? 381 MET B CB     1 
ATOM   6608 C  CG     . MET B 1 385 ? -2.64400  -16.33000 36.18900  1.000 34.51466 ? 381 MET B CG     1 
ATOM   6609 S  SD     . MET B 1 385 ? -3.57100  -15.14000 35.17600  1.000 39.53632 ? 381 MET B SD     1 
ATOM   6610 C  CE     . MET B 1 385 ? -2.76600  -15.35200 33.59100  1.000 37.36501 ? 381 MET B CE     1 
ATOM   6611 N  N      . GLN B 1 386 ? 1.74800   -15.41700 36.95100  1.000 42.38403 ? 382 GLN B N      1 
ATOM   6612 C  CA     . GLN B 1 386 ? 3.14300   -15.14900 36.60600  1.000 48.26895 ? 382 GLN B CA     1 
ATOM   6613 C  C      . GLN B 1 386 ? 4.07500   -16.18500 37.22100  1.000 48.82427 ? 382 GLN B C      1 
ATOM   6614 O  O      . GLN B 1 386 ? 5.07500   -16.57800 36.60600  1.000 50.60607 ? 382 GLN B O      1 
ATOM   6615 C  CB     . GLN B 1 386 ? 3.54200   -13.74600 37.07600  1.000 49.93493 ? 382 GLN B CB     1 
ATOM   6616 C  CG     . GLN B 1 386 ? 4.77000   -13.17300 36.39100  1.000 52.18784 ? 382 GLN B CG     1 
ATOM   6617 C  CD     . GLN B 1 386 ? 4.39700   -12.42100 35.13200  1.000 49.62700 ? 382 GLN B CD     1 
ATOM   6618 O  OE1    . GLN B 1 386 ? 3.75000   -11.37700 35.19400  1.000 48.01628 ? 382 GLN B OE1    1 
ATOM   6619 N  NE2    . GLN B 1 386 ? 4.77900   -12.96400 33.97700  1.000 44.65535 ? 382 GLN B NE2    1 
ATOM   6620 N  N      . ASN B 1 387 ? 3.77300   -16.63500 38.43300  1.000 44.73168 ? 383 ASN B N      1 
ATOM   6621 C  CA     . ASN B 1 387 ? 4.67200   -17.56300 39.09900  1.000 44.11055 ? 383 ASN B CA     1 
ATOM   6622 C  C      . ASN B 1 387 ? 4.54100   -18.97900 38.57300  1.000 44.95276 ? 383 ASN B C      1 
ATOM   6623 O  O      . ASN B 1 387 ? 5.47200   -19.76500 38.73200  1.000 47.41095 ? 383 ASN B O      1 
ATOM   6624 C  CB     . ASN B 1 387 ? 4.41600   -17.56100 40.60900  1.000 54.66971 ? 383 ASN B CB     1 
ATOM   6625 C  CG     . ASN B 1 387 ? 4.86100   -16.27800 41.27000  1.000 54.10649 ? 383 ASN B CG     1 
ATOM   6626 O  OD1    . ASN B 1 387 ? 5.55100   -15.46700 40.66500  1.000 56.71996 ? 383 ASN B OD1    1 
ATOM   6627 N  ND2    . ASN B 1 387 ? 4.44400   -16.07700 42.51200  1.000 56.68311 ? 383 ASN B ND2    1 
ATOM   6628 N  N      . ARG B 1 388 ? 3.46800   -19.29800 37.86000  1.000 40.67330 ? 384 ARG B N      1 
ATOM   6629 C  CA     . ARG B 1 388 ? 3.22500   -20.67300 37.45500  1.000 40.74962 ? 384 ARG B CA     1 
ATOM   6630 C  C      . ARG B 1 388 ? 3.25200   -20.88500 35.95000  1.000 38.82571 ? 384 ARG B C      1 
ATOM   6631 O  O      . ARG B 1 388 ? 3.54800   -21.99600 35.51100  1.000 44.18951 ? 384 ARG B O      1 
ATOM   6632 C  CB     . ARG B 1 388 ? 1.87100   -21.16100 37.99500  1.000 44.88959 ? 384 ARG B CB     1 
ATOM   6633 C  CG     . ARG B 1 388 ? 1.93700   -21.52100 39.45500  1.000 48.86112 ? 384 ARG B CG     1 
ATOM   6634 C  CD     . ARG B 1 388 ? 2.07500   -23.01200 39.62200  1.000 50.11127 ? 384 ARG B CD     1 
ATOM   6635 N  NE     . ARG B 1 388 ? 2.04600   -23.38000 41.02700  1.000 50.96401 ? 384 ARG B NE     1 
ATOM   6636 C  CZ     . ARG B 1 388 ? 2.85500   -24.27100 41.58300  1.000 46.45031 ? 384 ARG B CZ     1 
ATOM   6637 N  NH1    . ARG B 1 388 ? 3.75800   -24.89800 40.84700  1.000 48.20052 ? 384 ARG B NH1    1 
ATOM   6638 N  NH2    . ARG B 1 388 ? 2.74900   -24.54100 42.87300  1.000 48.25052 ? 384 ARG B NH2    1 
ATOM   6639 N  N      . LEU B 1 389 ? 2.93800   -19.87400 35.15500  1.000 36.23592 ? 385 LEU B N      1 
ATOM   6640 C  CA     . LEU B 1 389 ? 2.87600   -20.07700 33.71700  1.000 41.50761 ? 385 LEU B CA     1 
ATOM   6641 C  C      . LEU B 1 389 ? 4.28800   -20.23800 33.16700  1.000 43.20781 ? 385 LEU B C      1 
ATOM   6642 O  O      . LEU B 1 389 ? 5.15500   -19.40800 33.46300  1.000 46.85035 ? 385 LEU B O      1 
ATOM   6643 C  CB     . LEU B 1 389 ? 2.19000   -18.89600 33.04000  1.000 40.52591 ? 385 LEU B CB     1 
ATOM   6644 C  CG     . LEU B 1 389 ? 0.70700   -18.70200 33.35900  1.000 37.11234 ? 385 LEU B CG     1 
ATOM   6645 C  CD1    . LEU B 1 389 ? 0.12100   -17.59500 32.51800  1.000 32.25124 ? 385 LEU B CD1    1 
ATOM   6646 C  CD2    . LEU B 1 389 ? -0.03400  -19.99700 33.14000  1.000 36.26751 ? 385 LEU B CD2    1 
ATOM   6647 N  N      . PRO B 1 390 ? 4.55900   -21.26900 32.36400  1.000 40.28641 ? 386 PRO B N      1 
ATOM   6648 C  CA     . PRO B 1 390 ? 5.87600   -21.37500 31.73400  1.000 40.71541 ? 386 PRO B CA     1 
ATOM   6649 C  C      . PRO B 1 390 ? 6.14000   -20.15500 30.86000  1.000 49.83229 ? 386 PRO B C      1 
ATOM   6650 O  O      . PRO B 1 390 ? 5.22300   -19.44400 30.44200  1.000 51.78779 ? 386 PRO B O      1 
ATOM   6651 C  CB     . PRO B 1 390 ? 5.77800   -22.66200 30.90800  1.000 36.79915 ? 386 PRO B CB     1 
ATOM   6652 C  CG     . PRO B 1 390 ? 4.67200   -23.42400 31.53400  1.000 38.68359 ? 386 PRO B CG     1 
ATOM   6653 C  CD     . PRO B 1 390 ? 3.69100   -22.39700 32.00200  1.000 38.64411 ? 386 PRO B CD     1 
ATOM   6654 N  N      . ALA B 1 391 ? 7.42500   -19.91600 30.58300  1.000 53.53537 ? 387 ALA B N      1 
ATOM   6655 C  CA     . ALA B 1 391 ? 7.81400   -18.69100 29.88500  1.000 50.37972 ? 387 ALA B CA     1 
ATOM   6656 C  C      . ALA B 1 391 ? 7.25500   -18.62700 28.46700  1.000 46.27660 ? 387 ALA B C      1 
ATOM   6657 O  O      . ALA B 1 391 ? 6.96100   -17.53200 27.96700  1.000 44.29215 ? 387 ALA B O      1 
ATOM   6658 C  CB     . ALA B 1 391 ? 9.33700   -18.57000 29.85800  1.000 53.67486 ? 387 ALA B CB     1 
ATOM   6659 N  N      . ASP B 1 392 ? 7.08700   -19.77200 27.81000  1.000 44.43691 ? 388 ASP B N      1 
ATOM   6660 C  CA     . ASP B 1 392 ? 6.57700   -19.81300 26.44700  1.000 47.98733 ? 388 ASP B CA     1 
ATOM   6661 C  C      . ASP B 1 392 ? 5.03400   -19.79700 26.37800  1.000 45.13699 ? 388 ASP B C      1 
ATOM   6662 O  O      . ASP B 1 392 ? 4.47000   -20.10300 25.32000  1.000 41.29179 ? 388 ASP B O      1 
ATOM   6663 C  CB     . ASP B 1 392 ? 7.16100   -21.03100 25.71500  1.000 43.46837 ? 388 ASP B CB     1 
ATOM   6664 C  CG     . ASP B 1 392 ? 6.83300   -22.33900 26.39300  1.000 52.30890 ? 388 ASP B CG     1 
ATOM   6665 O  OD1    . ASP B 1 392 ? 6.46700   -22.32100 27.58700  1.000 58.14908 ? 388 ASP B OD1    1 
ATOM   6666 O  OD2    . ASP B 1 392 ? 6.94300   -23.39600 25.72900  1.000 59.32817 ? 388 ASP B OD2    1 
ATOM   6667 N  N      . THR B 1 393 ? 4.34500   -19.45900 27.47200  1.000 39.39683 ? 389 THR B N      1 
ATOM   6668 C  CA     . THR B 1 393 ? 2.88400   -19.46300 27.48200  1.000 33.27504 ? 389 THR B CA     1 
ATOM   6669 C  C      . THR B 1 393 ? 2.33000   -18.37900 26.56100  1.000 34.53572 ? 389 THR B C      1 
ATOM   6670 O  O      . THR B 1 393 ? 2.80600   -17.23900 26.56900  1.000 36.03327 ? 389 THR B O      1 
ATOM   6671 C  CB     . THR B 1 393 ? 2.35300   -19.24200 28.89600  1.000 31.45377 ? 389 THR B CB     1 
ATOM   6672 O  OG1    . THR B 1 393 ? 2.72300   -20.34900 29.72200  1.000 34.77259 ? 389 THR B OG1    1 
ATOM   6673 C  CG2    . THR B 1 393 ? 0.80700   -19.13500 28.88800  1.000 32.20649 ? 389 THR B CG2    1 
ATOM   6674 N  N      . ILE B 1 394 ? 1.32800   -18.73100 25.76300  1.000 30.11677 ? 390 ILE B N      1 
ATOM   6675 C  CA     . ILE B 1 394 ? 0.57300   -17.73300 25.00600  1.000 28.77977 ? 390 ILE B CA     1 
ATOM   6676 C  C      . ILE B 1 394 ? -0.66600  -17.37300 25.81900  1.000 31.33797 ? 390 ILE B C      1 
ATOM   6677 O  O      . ILE B 1 394 ? -1.50400  -18.23300 26.11500  1.000 28.74292 ? 390 ILE B O      1 
ATOM   6678 C  CB     . ILE B 1 394 ? 0.20600   -18.24200 23.60600  1.000 32.92500 ? 390 ILE B CB     1 
ATOM   6679 C  CG1    . ILE B 1 394 ? 1.46600   -18.68100 22.86300  1.000 30.10624 ? 390 ILE B CG1    1 
ATOM   6680 C  CG2    . ILE B 1 394 ? -0.54300  -17.15500 22.82800  1.000 34.98577 ? 390 ILE B CG2    1 
ATOM   6681 C  CD1    . ILE B 1 394 ? 1.18400   -19.39500 21.54100  1.000 30.99845 ? 390 ILE B CD1    1 
ATOM   6682 N  N      . LEU B 1 395 ? -0.74700  -16.11000 26.22400  1.000 27.80597 ? 391 LEU B N      1 
ATOM   6683 C  CA     . LEU B 1 395 ? -1.80500  -15.61400 27.08900  1.000 28.91399 ? 391 LEU B CA     1 
ATOM   6684 C  C      . LEU B 1 395 ? -2.80000  -14.81100 26.25600  1.000 30.02992 ? 391 LEU B C      1 
ATOM   6685 O  O      . LEU B 1 395 ? -2.45500  -13.76400 25.69100  1.000 33.03291 ? 391 LEU B O      1 
ATOM   6686 C  CB     . LEU B 1 395 ? -1.22100  -14.77100 28.22200  1.000 28.55606 ? 391 LEU B CB     1 
ATOM   6687 C  CG     . LEU B 1 395 ? -2.31300  -14.18500 29.12400  1.000 33.23293 ? 391 LEU B CG     1 
ATOM   6688 C  CD1    . LEU B 1 395 ? -3.10900  -15.30700 29.83400  1.000 29.75357 ? 391 LEU B CD1    1 
ATOM   6689 C  CD2    . LEU B 1 395 ? -1.75000  -13.15000 30.12600  1.000 26.31631 ? 391 LEU B CD2    1 
ATOM   6690 N  N      . PHE B 1 396 ? -4.02400  -15.32400 26.16300  1.000 23.37912 ? 392 PHE B N      1 
ATOM   6691 C  CA     . PHE B 1 396 ? -5.14500  -14.61800 25.56900  1.000 22.52639 ? 392 PHE B CA     1 
ATOM   6692 C  C      . PHE B 1 396 ? -5.89500  -13.88100 26.66600  1.000 26.96376 ? 392 PHE B C      1 
ATOM   6693 O  O      . PHE B 1 396 ? -6.16600  -14.44300 27.73600  1.000 30.17730 ? 392 PHE B O      1 
ATOM   6694 C  CB     . PHE B 1 396 ? -6.08100  -15.59700 24.85300  1.000 27.38223 ? 392 PHE B CB     1 
ATOM   6695 C  CG     . PHE B 1 396 ? -5.54200  -16.10000 23.53400  1.000 29.03506 ? 392 PHE B CG     1 
ATOM   6696 C  CD1    . PHE B 1 396 ? -4.55900  -17.07400 23.49400  1.000 24.68454 ? 392 PHE B CD1    1 
ATOM   6697 C  CD2    . PHE B 1 396 ? -6.01200  -15.57900 22.33600  1.000 27.38223 ? 392 PHE B CD2    1 
ATOM   6698 C  CE1    . PHE B 1 396 ? -4.05200  -17.53800 22.27400  1.000 25.29251 ? 392 PHE B CE1    1 
ATOM   6699 C  CE2    . PHE B 1 396 ? -5.51800  -16.03400 21.12200  1.000 31.90119 ? 392 PHE B CE2    1 
ATOM   6700 C  CZ     . PHE B 1 396 ? -4.53000  -17.02100 21.09600  1.000 27.66911 ? 392 PHE B CZ     1 
ATOM   6701 N  N      . VAL B 1 397 ? -6.21700  -12.62200 26.41400  1.000 23.85812 ? 393 VAL B N      1 
ATOM   6702 C  CA     . VAL B 1 397 ? -6.90300  -11.79400 27.39500  1.000 26.62424 ? 393 VAL B CA     1 
ATOM   6703 C  C      . VAL B 1 397 ? -8.17300  -11.27300 26.75200  1.000 31.06162 ? 393 VAL B C      1 
ATOM   6704 O  O      . VAL B 1 397 ? -8.14200  -10.77400 25.62000  1.000 28.31392 ? 393 VAL B O      1 
ATOM   6705 C  CB     . VAL B 1 397 ? -6.00800  -10.64100 27.88300  1.000 26.95586 ? 393 VAL B CB     1 
ATOM   6706 C  CG1    . VAL B 1 397 ? -6.80600  -9.69500  28.76500  1.000 30.47471 ? 393 VAL B CG1    1 
ATOM   6707 C  CG2    . VAL B 1 397 ? -4.79700  -11.20500 28.63300  1.000 26.39264 ? 393 VAL B CG2    1 
ATOM   6708 N  N      . ASP B 1 398 ? -9.28000  -11.37600 27.46800  1.000 29.18245 ? 394 ASP B N      1 
ATOM   6709 C  CA     . ASP B 1 398 ? -10.53800 -10.94000 26.89200  1.000 27.31643 ? 394 ASP B CA     1 
ATOM   6710 C  C      . ASP B 1 398 ? -10.70100 -9.43800  27.10400  1.000 31.04320 ? 394 ASP B C      1 
ATOM   6711 O  O      . ASP B 1 398 ? -9.74500  -8.70500  27.37000  1.000 31.38534 ? 394 ASP B O      1 
ATOM   6712 C  CB     . ASP B 1 398 ? -11.71400 -11.74100 27.46000  1.000 29.87990 ? 394 ASP B CB     1 
ATOM   6713 C  CG     . ASP B 1 398 ? -12.86800 -11.87600 26.44700  1.000 34.65942 ? 394 ASP B CG     1 
ATOM   6714 O  OD1    . ASP B 1 398 ? -13.68300 -10.94200 26.36500  1.000 33.22240 ? 394 ASP B OD1    1 
ATOM   6715 O  OD2    . ASP B 1 398 ? -12.94100 -12.88800 25.70800  1.000 34.52256 ? 394 ASP B OD2    1 
ATOM   6716 N  N      . ASN B 1 399 ? -11.91400 -8.95700  26.89600  1.000 31.59589 ? 395 ASN B N      1 
ATOM   6717 C  CA     . ASN B 1 399 ? -12.25400 -7.55700  27.03300  1.000 30.40891 ? 395 ASN B CA     1 
ATOM   6718 C  C      . ASN B 1 399 ? -13.23300 -7.44300  28.19200  1.000 41.65499 ? 395 ASN B C      1 
ATOM   6719 O  O      . ASN B 1 399 ? -14.14200 -8.26500  28.33900  1.000 62.73384 ? 395 ASN B O      1 
ATOM   6720 C  CB     . ASN B 1 399 ? -12.79900 -7.04300  25.70000  1.000 31.57221 ? 395 ASN B CB     1 
ATOM   6721 C  CG     . ASN B 1 399 ? -11.82000 -7.33000  24.53700  1.000 39.26787 ? 395 ASN B CG     1 
ATOM   6722 O  OD1    . ASN B 1 399 ? -10.76800 -6.69300  24.43000  1.000 40.27851 ? 395 ASN B OD1    1 
ATOM   6723 N  ND2    . ASN B 1 399 ? -12.14200 -8.32100  23.70400  1.000 31.53536 ? 395 ASN B ND2    1 
ATOM   6724 N  N      . GLY B 1 400 ? -13.01600 -6.47700  29.01900  1.000 34.50151 ? 396 GLY B N      1 
ATOM   6725 C  CA     . GLY B 1 400 ? -13.54600 -6.43000  30.35900  1.000 27.45856 ? 396 GLY B CA     1 
ATOM   6726 C  C      . GLY B 1 400 ? -12.43400 -5.94400  31.24000  1.000 31.12742 ? 396 GLY B C      1 
ATOM   6727 O  O      . GLY B 1 400 ? -11.39600 -5.50000  30.74900  1.000 31.35376 ? 396 GLY B O      1 
ATOM   6728 N  N      . SER B 1 401 ? -12.62500 -6.04000  32.55100  1.000 27.54804 ? 397 SER B N      1 
ATOM   6729 C  CA     . SER B 1 401 ? -11.53500 -5.60300  33.41200  1.000 34.73048 ? 397 SER B CA     1 
ATOM   6730 C  C      . SER B 1 401 ? -10.28200 -6.46000  33.24800  1.000 30.07466 ? 397 SER B C      1 
ATOM   6731 O  O      . SER B 1 401 ? -9.21300  -6.03700  33.66600  1.000 31.52220 ? 397 SER B O      1 
ATOM   6732 C  CB     . SER B 1 401 ? -11.95300 -5.60600  34.89000  1.000 29.72988 ? 397 SER B CB     1 
ATOM   6733 O  OG     . SER B 1 401 ? -12.05200 -6.93800  35.36300  1.000 35.29897 ? 397 SER B OG     1 
ATOM   6734 N  N      . CYS B 1 402 ? -10.40300 -7.68400  32.72200  1.000 27.16905 ? 398 CYS B N      1 
ATOM   6735 C  CA     . CYS B 1 402 ? -9.20600  -8.45300  32.37800  1.000 28.39288 ? 398 CYS B CA     1 
ATOM   6736 C  C      . CYS B 1 402 ? -8.20200  -7.61500  31.57300  1.000 28.41393 ? 398 CYS B C      1 
ATOM   6737 O  O      . CYS B 1 402 ? -6.98600  -7.86400  31.65100  1.000 26.52160 ? 398 CYS B O      1 
ATOM   6738 C  CB     . CYS B 1 402 ? -9.54300  -9.75200  31.67000  1.000 29.27983 ? 398 CYS B CB     1 
ATOM   6739 S  SG     . CYS B 1 402 ? -10.57500 -9.62400  30.23500  1.000 37.98350 ? 398 CYS B SG     1 
ATOM   6740 N  N      . ILE B 1 403 ? -8.67500  -6.73100  30.68300  1.000 26.32421 ? 399 ILE B N      1 
ATOM   6741 C  CA     . ILE B 1 403 ? -7.74200  -5.89300  29.91400  1.000 28.92452 ? 399 ILE B CA     1 
ATOM   6742 C  C      . ILE B 1 403 ? -6.79100  -5.17000  30.85700  1.000 30.53787 ? 399 ILE B C      1 
ATOM   6743 O  O      . ILE B 1 403 ? -5.56800  -5.25000  30.71800  1.000 33.62245 ? 399 ILE B O      1 
ATOM   6744 C  CB     . ILE B 1 403 ? -8.48200  -4.87100  29.03000  1.000 27.39013 ? 399 ILE B CB     1 
ATOM   6745 C  CG1    . ILE B 1 403 ? -9.33100  -5.56400  27.95300  1.000 28.95610 ? 399 ILE B CG1    1 
ATOM   6746 C  CG2    . ILE B 1 403 ? -7.44800  -3.91600  28.37000  1.000 27.01903 ? 399 ILE B CG2    1 
ATOM   6747 C  CD1    . ILE B 1 403 ? -10.38400 -4.65200  27.32200  1.000 29.75883 ? 399 ILE B CD1    1 
ATOM   6748 N  N      . ASN B 1 404 ? -7.34800  -4.42700  31.81600  1.000 29.82200 ? 400 ASN B N      1 
ATOM   6749 C  CA     . ASN B 1 404 ? -6.51300  -3.63800  32.71800  1.000 33.18819 ? 400 ASN B CA     1 
ATOM   6750 C  C      . ASN B 1 404 ? -5.57100  -4.53300  33.50300  1.000 31.49851 ? 400 ASN B C      1 
ATOM   6751 O  O      . ASN B 1 404 ? -4.36200  -4.28700  33.55100  1.000 29.99570 ? 400 ASN B O      1 
ATOM   6752 C  CB     . ASN B 1 404 ? -7.37800  -2.81700  33.67500  1.000 30.22731 ? 400 ASN B CB     1 
ATOM   6753 C  CG     . ASN B 1 404 ? -8.42100  -1.98400  32.95200  1.000 36.72019 ? 400 ASN B CG     1 
ATOM   6754 O  OD1    . ASN B 1 404 ? -9.37100  -2.51900  32.38400  1.000 34.42781 ? 400 ASN B OD1    1 
ATOM   6755 N  ND2    . ASN B 1 404 ? -8.25600  -0.66400  32.98600  1.000 32.88815 ? 400 ASN B ND2    1 
ATOM   6756 N  N      . TRP B 1 405 ? -6.10000  -5.60600  34.09400  1.000 32.96448 ? 401 TRP B N      1 
ATOM   6757 C  CA     . TRP B 1 405 ? -5.24900  -6.47200  34.90400  1.000 37.92034 ? 401 TRP B CA     1 
ATOM   6758 C  C      . TRP B 1 405 ? -4.17300  -7.12800  34.05200  1.000 34.91998 ? 401 TRP B C      1 
ATOM   6759 O  O      . TRP B 1 405 ? -3.01100  -7.21600  34.46600  1.000 34.96735 ? 401 TRP B O      1 
ATOM   6760 C  CB     . TRP B 1 405 ? -6.09100  -7.54400  35.60700  1.000 33.29083 ? 401 TRP B CB     1 
ATOM   6761 C  CG     . TRP B 1 405 ? -7.08700  -6.96600  36.52600  1.000 32.71182 ? 401 TRP B CG     1 
ATOM   6762 C  CD1    . TRP B 1 405 ? -8.45000  -7.03700  36.42500  1.000 33.12766 ? 401 TRP B CD1    1 
ATOM   6763 C  CD2    . TRP B 1 405 ? -6.80500  -6.19600  37.69400  1.000 38.52304 ? 401 TRP B CD2    1 
ATOM   6764 N  NE1    . TRP B 1 405 ? -9.03400  -6.35700  37.47200  1.000 40.85490 ? 401 TRP B NE1    1 
ATOM   6765 C  CE2    . TRP B 1 405 ? -8.04300  -5.83500  38.26500  1.000 37.78874 ? 401 TRP B CE2    1 
ATOM   6766 C  CE3    . TRP B 1 405 ? -5.62200  -5.78800  38.32100  1.000 42.89198 ? 401 TRP B CE3    1 
ATOM   6767 C  CZ2    . TRP B 1 405 ? -8.13100  -5.08100  39.42800  1.000 39.31261 ? 401 TRP B CZ2    1 
ATOM   6768 C  CZ3    . TRP B 1 405 ? -5.70900  -5.03900  39.47600  1.000 40.57855 ? 401 TRP B CZ3    1 
ATOM   6769 C  CH2    . TRP B 1 405 ? -6.95800  -4.68900  40.01600  1.000 43.20255 ? 401 TRP B CH2    1 
ATOM   6770 N  N      . GLY B 1 406 ? -4.54500  -7.60800  32.86300  1.000 28.86662 ? 402 GLY B N      1 
ATOM   6771 C  CA     . GLY B 1 406 ? -3.57100  -8.28800  32.01900  1.000 34.11198 ? 402 GLY B CA     1 
ATOM   6772 C  C      . GLY B 1 406 ? -2.52800  -7.34400  31.45000  1.000 32.23544 ? 402 GLY B C      1 
ATOM   6773 O  O      . GLY B 1 406 ? -1.32400  -7.60000  31.54100  1.000 31.16163 ? 402 GLY B O      1 
ATOM   6774 N  N      . VAL B 1 407 ? -2.97700  -6.23300  30.86500  1.000 29.33510 ? 403 VAL B N      1 
ATOM   6775 C  CA     . VAL B 1 407 ? -2.04000  -5.26900  30.28900  1.000 25.16091 ? 403 VAL B CA     1 
ATOM   6776 C  C      . VAL B 1 407 ? -1.12100  -4.70400  31.36500  1.000 29.35615 ? 403 VAL B C      1 
ATOM   6777 O  O      . VAL B 1 407 ? 0.08300   -4.54000  31.14200  1.000 33.47507 ? 403 VAL B O      1 
ATOM   6778 C  CB     . VAL B 1 407 ? -2.80200  -4.15000  29.55800  1.000 29.54828 ? 403 VAL B CB     1 
ATOM   6779 C  CG1    . VAL B 1 407 ? -1.90000  -2.93500  29.32700  1.000 28.21391 ? 403 VAL B CG1    1 
ATOM   6780 C  CG2    . VAL B 1 407 ? -3.41100  -4.66800  28.22900  1.000 31.81171 ? 403 VAL B CG2    1 
ATOM   6781 N  N      . HIS B 1 408 ? -1.66500  -4.40200  32.55300  1.000 31.96699 ? 404 HIS B N      1 
ATOM   6782 C  CA     . HIS B 1 408 ? -0.87300  -3.68000  33.54900  1.000 29.66935 ? 404 HIS B CA     1 
ATOM   6783 C  C      . HIS B 1 408 ? 0.02700   -4.61400  34.34900  1.000 31.90383 ? 404 HIS B C      1 
ATOM   6784 O  O      . HIS B 1 408 ? 1.20300   -4.31100  34.56300  1.000 29.24561 ? 404 HIS B O      1 
ATOM   6785 C  CB     . HIS B 1 408 ? -1.77300  -2.87500  34.50900  1.000 27.25590 ? 404 HIS B CB     1 
ATOM   6786 C  CG     . HIS B 1 408 ? -1.00800  -1.90100  35.36500  1.000 32.89605 ? 404 HIS B CG     1 
ATOM   6787 N  ND1    . HIS B 1 408 ? -0.62400  -0.65400  34.91500  1.000 34.21463 ? 404 HIS B ND1    1 
ATOM   6788 C  CD2    . HIS B 1 408 ? -0.52500  -2.00600  36.62800  1.000 34.34096 ? 404 HIS B CD2    1 
ATOM   6789 C  CE1    . HIS B 1 408 ? 0.06000   -0.03300  35.86300  1.000 36.23066 ? 404 HIS B CE1    1 
ATOM   6790 N  NE2    . HIS B 1 408 ? 0.13000   -0.83000  36.91400  1.000 30.31942 ? 404 HIS B NE2    1 
ATOM   6791 N  N      . CYS B 1 409 ? -0.51600  -5.74300  34.81700  1.000 33.95407 ? 405 CYS B N      1 
ATOM   6792 C  CA     . CYS B 1 409 ? 0.14800   -6.55700  35.83200  1.000 33.95933 ? 405 CYS B CA     1 
ATOM   6793 C  C      . CYS B 1 409 ? 0.92800   -7.72600  35.27100  1.000 31.63011 ? 405 CYS B C      1 
ATOM   6794 O  O      . CYS B 1 409 ? 1.77300   -8.27100  35.97700  1.000 34.98051 ? 405 CYS B O      1 
ATOM   6795 C  CB     . CYS B 1 409 ? -0.87500  -7.13000  36.81600  1.000 32.88552 ? 405 CYS B CB     1 
ATOM   6796 S  SG     . CYS B 1 409 ? -1.76300  -5.87700  37.69700  1.000 38.64411 ? 405 CYS B SG     1 
ATOM   6797 N  N      . TYR B 1 410 ? 0.62700   -8.17200  34.06400  1.000 36.39910 ? 406 TYR B N      1 
ATOM   6798 C  CA     . TYR B 1 410 ? 1.29700   -9.34100  33.52700  1.000 35.22001 ? 406 TYR B CA     1 
ATOM   6799 C  C      . TYR B 1 410 ? 2.56300   -8.91000  32.80500  1.000 34.56993 ? 406 TYR B C      1 
ATOM   6800 O  O      . TYR B 1 410 ? 2.53400   -7.98900  31.98400  1.000 39.37051 ? 406 TYR B O      1 
ATOM   6801 C  CB     . TYR B 1 410 ? 0.37500   -10.09700 32.58000  1.000 31.72222 ? 406 TYR B CB     1 
ATOM   6802 C  CG     . TYR B 1 410 ? 0.96600   -11.38300 32.05000  1.000 35.82535 ? 406 TYR B CG     1 
ATOM   6803 C  CD1    . TYR B 1 410 ? 1.06800   -12.50900 32.85800  1.000 41.63131 ? 406 TYR B CD1    1 
ATOM   6804 C  CD2    . TYR B 1 410 ? 1.41600   -11.47100 30.73300  1.000 35.94905 ? 406 TYR B CD2    1 
ATOM   6805 C  CE1    . TYR B 1 410 ? 1.60200   -13.69500 32.36700  1.000 43.34467 ? 406 TYR B CE1    1 
ATOM   6806 C  CE2    . TYR B 1 410 ? 1.94000   -12.64800 30.23400  1.000 37.98087 ? 406 TYR B CE2    1 
ATOM   6807 C  CZ     . TYR B 1 410 ? 2.03100   -13.75200 31.05100  1.000 40.31799 ? 406 TYR B CZ     1 
ATOM   6808 O  OH     . TYR B 1 410 ? 2.55500   -14.91200 30.54000  1.000 43.26571 ? 406 TYR B OH     1 
ATOM   6809 N  N      . LEU B 1 411 ? 3.67600   -9.56000  33.12500  1.000 34.10935 ? 407 LEU B N      1 
ATOM   6810 C  CA     . LEU B 1 411 ? 4.93200   -9.25400  32.46100  1.000 35.96747 ? 407 LEU B CA     1 
ATOM   6811 C  C      . LEU B 1 411 ? 5.11600   -10.21200 31.29000  1.000 36.36225 ? 407 LEU B C      1 
ATOM   6812 O  O      . LEU B 1 411 ? 5.25500   -11.42300 31.48500  1.000 35.05157 ? 407 LEU B O      1 
ATOM   6813 C  CB     . LEU B 1 411 ? 6.10400   -9.34500  33.43200  1.000 40.20745 ? 407 LEU B CB     1 
ATOM   6814 C  CG     . LEU B 1 411 ? 7.33700   -8.68100  32.82400  1.000 47.32936 ? 407 LEU B CG     1 
ATOM   6815 C  CD1    . LEU B 1 411 ? 8.10300   -7.86300  33.85100  1.000 46.75824 ? 407 LEU B CD1    1 
ATOM   6816 C  CD2    . LEU B 1 411 ? 8.21900   -9.74100  32.20700  1.000 48.14788 ? 407 LEU B CD2    1 
ATOM   6817 N  N      . ALA B 1 412 ? 5.11900   -9.66500  30.08100  1.000 32.45652 ? 408 ALA B N      1 
ATOM   6818 C  CA     . ALA B 1 412 ? 5.24000   -10.44700 28.85700  1.000 38.29143 ? 408 ALA B CA     1 
ATOM   6819 C  C      . ALA B 1 412 ? 6.69800   -10.43800 28.42000  1.000 39.11785 ? 408 ALA B C      1 
ATOM   6820 O  O      . ALA B 1 412 ? 7.25500   -9.37300  28.13000  1.000 41.47339 ? 408 ALA B O      1 
ATOM   6821 C  CB     . ALA B 1 412 ? 4.34700   -9.88300  27.75200  1.000 36.28067 ? 408 ALA B CB     1 
ATOM   6822 N  N      . GLN B 1 413 ? 7.31600   -11.62200 28.38200  1.000 38.49146 ? 409 GLN B N      1 
ATOM   6823 C  CA     . GLN B 1 413 ? 8.71400   -11.73200 28.00300  1.000 38.85992 ? 409 GLN B CA     1 
ATOM   6824 C  C      . GLN B 1 413 ? 8.89700   -12.36800 26.64000  1.000 38.93888 ? 409 GLN B C      1 
ATOM   6825 O  O      . GLN B 1 413 ? 9.92400   -12.14700 25.99700  1.000 49.88493 ? 409 GLN B O      1 
ATOM   6826 C  CB     . GLN B 1 413 ? 9.48200   -12.56700 29.02500  1.000 46.81614 ? 409 GLN B CB     1 
ATOM   6827 C  CG     . GLN B 1 413 ? 9.35500   -12.08000 30.46400  1.000 62.30221 ? 409 GLN B CG     1 
ATOM   6828 C  CD     . GLN B 1 413 ? 9.95800   -13.05900 31.46600  1.000 71.37961 ? 409 GLN B CD     1 
ATOM   6829 O  OE1    . GLN B 1 413 ? 10.74300  -13.93300 31.09300  1.000 75.91963 ? 409 GLN B OE1    1 
ATOM   6830 N  NE2    . GLN B 1 413 ? 9.59400   -12.91600 32.73900  1.000 73.00086 ? 409 GLN B NE2    1 
ATOM   6831 N  N      . THR B 1 414 ? 7.91400   -13.07800 26.15500  1.000 35.72534 ? 410 THR B N      1 
ATOM   6832 C  CA     . THR B 1 414 ? 8.14900   -13.83700 24.94300  1.000 40.29694 ? 410 THR B CA     1 
ATOM   6833 C  C      . THR B 1 414 ? 7.48500   -13.14700 23.76700  1.000 35.30686 ? 410 THR B C      1 
ATOM   6834 O  O      . THR B 1 414 ? 6.36900   -12.63000 23.90600  1.000 33.69615 ? 410 THR B O      1 
ATOM   6835 C  CB     . THR B 1 414 ? 7.57900   -15.25300 25.08400  1.000 45.61336 ? 410 THR B CB     1 
ATOM   6836 O  OG1    . THR B 1 414 ? 8.35500   -15.99900 26.03300  1.000 46.24502 ? 410 THR B OG1    1 
ATOM   6837 C  CG2    . THR B 1 414 ? 7.56500   -15.98100 23.73100  1.000 46.84246 ? 410 THR B CG2    1 
ATOM   6838 N  N      . PRO B 1 415 ? 8.16400   -13.13100 22.61800  1.000 35.25686 ? 411 PRO B N      1 
ATOM   6839 C  CA     . PRO B 1 415 ? 7.63400   -12.40900 21.45300  1.000 36.64650 ? 411 PRO B CA     1 
ATOM   6840 C  C      . PRO B 1 415 ? 6.24700   -12.89900 21.06900  1.000 35.49636 ? 411 PRO B C      1 
ATOM   6841 O  O      . PRO B 1 415 ? 6.02600   -14.09000 20.84800  1.000 37.49660 ? 411 PRO B O      1 
ATOM   6842 C  CB     . PRO B 1 415 ? 8.65700   -12.70900 20.34800  1.000 36.36225 ? 411 PRO B CB     1 
ATOM   6843 C  CG     . PRO B 1 415 ? 9.87800   -13.11700 21.04200  1.000 35.19369 ? 411 PRO B CG     1 
ATOM   6844 C  CD     . PRO B 1 415 ? 9.49900   -13.70000 22.36800  1.000 34.34886 ? 411 PRO B CD     1 
ATOM   6845 N  N      . GLY B 1 416 ? 5.30600   -11.96500 20.99100  1.000 38.14405 ? 412 GLY B N      1 
ATOM   6846 C  CA     . GLY B 1 416 ? 3.99300   -12.32500 20.49600  1.000 33.55139 ? 412 GLY B CA     1 
ATOM   6847 C  C      . GLY B 1 416 ? 3.15300   -13.18700 21.41200  1.000 38.75728 ? 412 GLY B C      1 
ATOM   6848 O  O      . GLY B 1 416 ? 2.11000   -13.68200 20.97500  1.000 40.68383 ? 412 GLY B O      1 
ATOM   6849 N  N      . ALA B 1 417 ? 3.58100   -13.41500 22.65200  1.000 34.17515 ? 413 ALA B N      1 
ATOM   6850 C  CA     . ALA B 1 417 ? 2.87400   -14.32300 23.54700  1.000 28.53500 ? 413 ALA B CA     1 
ATOM   6851 C  C      . ALA B 1 417 ? 1.73700   -13.65800 24.32500  1.000 33.98039 ? 413 ALA B C      1 
ATOM   6852 O  O      . ALA B 1 417 ? 1.11600   -14.31600 25.17200  1.000 40.98913 ? 413 ALA B O      1 
ATOM   6853 C  CB     . ALA B 1 417 ? 3.86900   -14.96900 24.53200  1.000 25.42410 ? 413 ALA B CB     1 
ATOM   6854 N  N      . PHE B 1 418 ? 1.43300   -12.39000 24.05900  1.000 29.66408 ? 414 PHE B N      1 
ATOM   6855 C  CA     . PHE B 1 418 ? 0.31100   -11.69700 24.68900  1.000 30.94318 ? 414 PHE B CA     1 
ATOM   6856 C  C      . PHE B 1 418 ? -0.70900  -11.36100 23.60400  1.000 31.74854 ? 414 PHE B C      1 
ATOM   6857 O  O      . PHE B 1 418 ? -0.43000  -10.54100 22.72000  1.000 28.32182 ? 414 PHE B O      1 
ATOM   6858 C  CB     . PHE B 1 418 ? 0.79900   -10.44800 25.41800  1.000 30.76948 ? 414 PHE B CB     1 
ATOM   6859 C  CG     . PHE B 1 418 ? -0.24300  -9.80800  26.30100  1.000 33.66719 ? 414 PHE B CG     1 
ATOM   6860 C  CD1    . PHE B 1 418 ? -1.12500  -8.87000  25.78200  1.000 30.82212 ? 414 PHE B CD1    1 
ATOM   6861 C  CD2    . PHE B 1 418 ? -0.33200  -10.13700 27.65800  1.000 30.14046 ? 414 PHE B CD2    1 
ATOM   6862 C  CE1    . PHE B 1 418 ? -2.08000  -8.26600  26.59100  1.000 31.84329 ? 414 PHE B CE1    1 
ATOM   6863 C  CE2    . PHE B 1 418 ? -1.28600  -9.53700  28.48000  1.000 28.12706 ? 414 PHE B CE2    1 
ATOM   6864 C  CZ     . PHE B 1 418 ? -2.16100  -8.60300  27.94400  1.000 31.20111 ? 414 PHE B CZ     1 
ATOM   6865 N  N      . GLN B 1 419 ? -1.89000  -11.99800 23.66600  1.000 27.51383 ? 415 GLN B N      1 
ATOM   6866 C  CA     . GLN B 1 419 ? -2.88000  -11.94500 22.58600  1.000 26.22156 ? 415 GLN B CA     1 
ATOM   6867 C  C      . GLN B 1 419 ? -4.15900  -11.28100 23.08800  1.000 29.94043 ? 415 GLN B C      1 
ATOM   6868 O  O      . GLN B 1 419 ? -4.95300  -11.90400 23.80100  1.000 30.33785 ? 415 GLN B O      1 
ATOM   6869 C  CB     . GLN B 1 419 ? -3.16100  -13.34900 22.05900  1.000 30.90897 ? 415 GLN B CB     1 
ATOM   6870 C  CG     . GLN B 1 419 ? -1.97600  -13.97200 21.36200  1.000 32.40652 ? 415 GLN B CG     1 
ATOM   6871 C  CD     . GLN B 1 419 ? -1.74700  -13.34600 20.00200  1.000 37.05181 ? 415 GLN B CD     1 
ATOM   6872 O  OE1    . GLN B 1 419 ? -2.71200  -13.07100 19.27500  1.000 35.41740 ? 415 GLN B OE1    1 
ATOM   6873 N  NE2    . GLN B 1 419 ? -0.48600  -13.10100 19.65400  1.000 29.80094 ? 415 GLN B NE2    1 
ATOM   6874 N  N      . ILE B 1 420 ? -4.33500  -10.03700 22.70100  1.000 22.67114 ? 416 ILE B N      1 
ATOM   6875 C  CA     . ILE B 1 420 ? -5.48500  -9.24400  23.06700  1.000 30.05624 ? 416 ILE B CA     1 
ATOM   6876 C  C      . ILE B 1 420 ? -6.05300  -8.54000  21.84200  1.000 23.10540 ? 416 ILE B C      1 
ATOM   6877 O  O      . ILE B 1 420 ? -5.34300  -7.97800  21.10300  1.000 25.51622 ? 416 ILE B O      1 
ATOM   6878 C  CB     . ILE B 1 420 ? -5.15500  -8.26500  24.21600  1.000 26.89007 ? 416 ILE B CB     1 
ATOM   6879 C  CG1    . ILE B 1 420 ? -6.41000  -7.74000  24.86600  1.000 32.46705 ? 416 ILE B CG1    1 
ATOM   6880 C  CG2    . ILE B 1 420 ? -4.28700  -7.14800  23.74600  1.000 21.46573 ? 416 ILE B CG2    1 
ATOM   6881 C  CD1    . ILE B 1 420 ? -6.17400  -6.94300  26.12200  1.000 28.16390 ? 416 ILE B CD1    1 
ATOM   6882 N  N      . GLY B 1 421 ? -7.35400  -8.59400  21.66400  1.000 25.08459 ? 417 GLY B N      1 
ATOM   6883 C  CA     . GLY B 1 421 ? -8.03400  -8.01700  20.51400  1.000 29.90359 ? 417 GLY B CA     1 
ATOM   6884 C  C      . GLY B 1 421 ? -8.68100  -6.69000  20.80600  1.000 30.81948 ? 417 GLY B C      1 
ATOM   6885 O  O      . GLY B 1 421 ? -9.86000  -6.58300  20.90600  1.000 26.19261 ? 417 GLY B O      1 
ATOM   6886 N  N      . LEU B 1 422 ? -7.84700  -5.68300  20.93200  1.000 29.40353 ? 418 LEU B N      1 
ATOM   6887 C  CA     . LEU B 1 422 ? -8.29700  -4.38000  21.28800  1.000 27.88229 ? 418 LEU B CA     1 
ATOM   6888 C  C      . LEU B 1 422 ? -8.80100  -3.53600  20.14600  1.000 30.60104 ? 418 LEU B C      1 
ATOM   6889 O  O      . LEU B 1 422 ? -9.35100  -2.54200  20.41900  1.000 32.89605 ? 418 LEU B O      1 
ATOM   6890 C  CB     . LEU B 1 422 ? -7.23300  -3.61400  22.04700  1.000 24.84508 ? 418 LEU B CB     1 
ATOM   6891 C  CG     . LEU B 1 422 ? -6.82200  -4.12900  23.40800  1.000 31.33270 ? 418 LEU B CG     1 
ATOM   6892 C  CD1    . LEU B 1 422 ? -5.70300  -3.35200  24.02800  1.000 26.57687 ? 418 LEU B CD1    1 
ATOM   6893 C  CD2    . LEU B 1 422 ? -7.97300  -4.32100  24.34300  1.000 28.01915 ? 418 LEU B CD2    1 
ATOM   6894 N  N      . GLY B 1 423 ? -8.55200  -3.92300  18.90400  1.000 27.31380 ? 419 GLY B N      1 
ATOM   6895 C  CA     . GLY B 1 423 ? -9.08100  -3.14400  17.79900  1.000 29.64566 ? 419 GLY B CA     1 
ATOM   6896 C  C      . GLY B 1 423 ? -10.57800 -2.94600  17.93600  1.000 27.89282 ? 419 GLY B C      1 
ATOM   6897 O  O      . GLY B 1 423 ? -11.07300 -1.82100  17.94400  1.000 33.36189 ? 419 GLY B O      1 
ATOM   6898 N  N      . LEU B 1 424 ? -11.31200 -4.04000  18.12400  1.000 25.04248 ? 420 LEU B N      1 
ATOM   6899 C  CA     . LEU B 1 424 ? -12.74400 -3.95300  18.36900  1.000 27.35854 ? 420 LEU B CA     1 
ATOM   6900 C  C      . LEU B 1 424 ? -13.12800 -4.25800  19.81600  1.000 25.86889 ? 420 LEU B C      1 
ATOM   6901 O  O      . LEU B 1 424 ? -14.24400 -3.91900  20.22700  1.000 25.51622 ? 420 LEU B O      1 
ATOM   6902 C  CB     . LEU B 1 424 ? -13.49600 -4.90200  17.42100  1.000 26.12155 ? 420 LEU B CB     1 
ATOM   6903 C  CG     . LEU B 1 424 ? -14.96700 -4.62100  17.14400  1.000 31.57484 ? 420 LEU B CG     1 
ATOM   6904 C  CD1    . LEU B 1 424 ? -15.14100 -3.18400  16.64900  1.000 26.62161 ? 420 LEU B CD1    1 
ATOM   6905 C  CD2    . LEU B 1 424 ? -15.52500 -5.63500  16.13900  1.000 23.45018 ? 420 LEU B CD2    1 
ATOM   6906 N  N      . ALA B 1 425 ? -12.24900 -4.90700  20.58100  1.000 25.13722 ? 421 ALA B N      1 
ATOM   6907 C  CA     . ALA B 1 425 ? -12.48300 -5.17100  22.00100  1.000 23.90023 ? 421 ALA B CA     1 
ATOM   6908 C  C      . ALA B 1 425 ? -13.83700 -5.84900  22.21500  1.000 30.47997 ? 421 ALA B C      1 
ATOM   6909 O  O      . ALA B 1 425 ? -14.68300 -5.40200  22.99600  1.000 26.60056 ? 421 ALA B O      1 
ATOM   6910 C  CB     . ALA B 1 425 ? -12.36500 -3.87500  22.80700  1.000 25.30567 ? 421 ALA B CB     1 
ATOM   6911 N  N      . ALA B 1 426 ? -14.05200 -6.93600  21.48300  1.000 30.85896 ? 422 ALA B N      1 
ATOM   6912 C  CA     . ALA B 1 426 ? -15.30000 -7.68200  21.56800  1.000 30.77737 ? 422 ALA B CA     1 
ATOM   6913 C  C      . ALA B 1 426 ? -15.25500 -8.64000  22.75800  1.000 31.05372 ? 422 ALA B C      1 
ATOM   6914 O  O      . ALA B 1 426 ? -14.33800 -9.45200  22.86500  1.000 24.88719 ? 422 ALA B O      1 
ATOM   6915 C  CB     . ALA B 1 426 ? -15.52900 -8.44200  20.26300  1.000 19.55234 ? 422 ALA B CB     1 
ATOM   6916 N  N      . MET B 1 427 ? -16.23900 -8.55400  23.65500  1.000 32.11438 ? 423 MET B N      1 
ATOM   6917 C  CA     . MET B 1 427 ? -16.33200 -9.54600  24.71800  1.000 29.61145 ? 423 MET B CA     1 
ATOM   6918 C  C      . MET B 1 427 ? -16.47900 -10.93200 24.11500  1.000 34.11462 ? 423 MET B C      1 
ATOM   6919 O  O      . MET B 1 427 ? -17.22500 -11.12500 23.14900  1.000 27.61384 ? 423 MET B O      1 
ATOM   6920 C  CB     . MET B 1 427 ? -17.52500 -9.26700  25.62600  1.000 26.75058 ? 423 MET B CB     1 
ATOM   6921 C  CG     . MET B 1 427 ? -17.33100 -8.14300  26.60000  1.000 30.59841 ? 423 MET B CG     1 
ATOM   6922 S  SD     . MET B 1 427 ? -18.93700 -7.76300  27.34100  1.000 38.35723 ? 423 MET B SD     1 
ATOM   6923 C  CE     . MET B 1 427 ? -19.42400 -9.36900  27.98600  1.000 36.72282 ? 423 MET B CE     1 
ATOM   6924 N  N      . GLY B 1 428 ? -15.75100 -11.89900 24.68300  1.000 30.29574 ? 424 GLY B N      1 
ATOM   6925 C  CA     . GLY B 1 428 ? -15.79400 -13.26700 24.22000  1.000 23.40281 ? 424 GLY B CA     1 
ATOM   6926 C  C      . GLY B 1 428 ? -14.75500 -13.61700 23.17400  1.000 31.08267 ? 424 GLY B C      1 
ATOM   6927 O  O      . GLY B 1 428 ? -14.53000 -14.81100 22.92800  1.000 31.48799 ? 424 GLY B O      1 
ATOM   6928 N  N      . HIS B 1 429 ? -14.10600 -12.61500 22.56700  1.000 27.41645 ? 425 HIS B N      1 
ATOM   6929 C  CA     . HIS B 1 429 ? -13.07600 -12.85900 21.55700  1.000 28.38761 ? 425 HIS B CA     1 
ATOM   6930 C  C      . HIS B 1 429 ? -12.03300 -13.84300 22.06600  1.000 28.19285 ? 425 HIS B C      1 
ATOM   6931 O  O      . HIS B 1 429 ? -11.76400 -14.86700 21.42900  1.000 31.50115 ? 425 HIS B O      1 
ATOM   6932 C  CB     . HIS B 1 429 ? -12.41900 -11.52200 21.16700  1.000 32.61970 ? 425 HIS B CB     1 
ATOM   6933 C  CG     . HIS B 1 429 ? -11.41400 -11.61300 20.05100  1.000 37.28342 ? 425 HIS B CG     1 
ATOM   6934 N  ND1    . HIS B 1 429 ? -10.91500 -10.49500 19.41200  1.000 40.99439 ? 425 HIS B ND1    1 
ATOM   6935 C  CD2    . HIS B 1 429 ? -10.80500 -12.67600 19.47100  1.000 40.00743 ? 425 HIS B CD2    1 
ATOM   6936 C  CE1    . HIS B 1 429 ? -10.04700 -10.86600 18.48600  1.000 39.35472 ? 425 HIS B CE1    1 
ATOM   6937 N  NE2    . HIS B 1 429 ? -9.96100  -12.18500 18.50100  1.000 36.85179 ? 425 HIS B NE2    1 
ATOM   6938 N  N      . ALA B 1 430 ? -11.42500 -13.54400 23.21800  1.000 24.91615 ? 426 ALA B N      1 
ATOM   6939 C  CA     . ALA B 1 430 ? -10.36400 -14.40800 23.73100  1.000 27.58752 ? 426 ALA B CA     1 
ATOM   6940 C  C      . ALA B 1 430 ? -10.90300 -15.77700 24.12500  1.000 31.42482 ? 426 ALA B C      1 
ATOM   6941 O  O      . ALA B 1 430 ? -10.20300 -16.78200 23.97100  1.000 28.87978 ? 426 ALA B O      1 
ATOM   6942 C  CB     . ALA B 1 430 ? -9.65500  -13.74600 24.91800  1.000 22.69219 ? 426 ALA B CB     1 
ATOM   6943 N  N      . VAL B 1 431 ? -12.14000 -15.83700 24.63200  1.000 31.20374 ? 427 VAL B N      1 
ATOM   6944 C  CA     . VAL B 1 431 ? -12.72800 -17.11800 25.03500  1.000 31.86171 ? 427 VAL B CA     1 
ATOM   6945 C  C      . VAL B 1 431 ? -12.57800 -18.14300 23.92000  1.000 25.87942 ? 427 VAL B C      1 
ATOM   6946 O  O      . VAL B 1 431 ? -12.13400 -19.26900 24.14300  1.000 29.96149 ? 427 VAL B O      1 
ATOM   6947 C  CB     . VAL B 1 431 ? -14.20800 -16.93200 25.42900  1.000 31.91698 ? 427 VAL B CB     1 
ATOM   6948 C  CG1    . VAL B 1 431 ? -14.84900 -18.26500 25.70100  1.000 22.46059 ? 427 VAL B CG1    1 
ATOM   6949 C  CG2    . VAL B 1 431 ? -14.33700 -16.01000 26.65200  1.000 34.40149 ? 427 VAL B CG2    1 
ATOM   6950 N  N      . ALA B 1 432 ? -12.92400 -17.75600 22.68900  1.000 24.77929 ? 428 ALA B N      1 
ATOM   6951 C  CA     . ALA B 1 432 ? -12.82900 -18.69400 21.57500  1.000 28.32971 ? 428 ALA B CA     1 
ATOM   6952 C  C      . ALA B 1 432 ? -11.47400 -18.62900 20.86700  1.000 23.77917 ? 428 ALA B C      1 
ATOM   6953 O  O      . ALA B 1 432 ? -10.94800 -19.66100 20.43500  1.000 28.57448 ? 428 ALA B O      1 
ATOM   6954 C  CB     . ALA B 1 432 ? -13.96700 -18.43600 20.57800  1.000 29.46932 ? 428 ALA B CB     1 
ATOM   6955 N  N      . ALA B 1 433 ? -10.89500 -17.43500 20.71800  1.000 23.69495 ? 429 ALA B N      1 
ATOM   6956 C  CA     . ALA B 1 433 ? -9.63900  -17.33000 19.97000  1.000 25.71624 ? 429 ALA B CA     1 
ATOM   6957 C  C      . ALA B 1 433 ? -8.54900  -18.22800 20.55000  1.000 27.25853 ? 429 ALA B C      1 
ATOM   6958 O  O      . ALA B 1 433 ? -7.69500  -18.72100 19.80400  1.000 26.19788 ? 429 ALA B O      1 
ATOM   6959 C  CB     . ALA B 1 433 ? -9.15500  -15.87600 19.93400  1.000 22.40795 ? 429 ALA B CB     1 
ATOM   6960 N  N      . ALA B 1 434 ? -8.55200  -18.44900 21.87000  1.000 26.18209 ? 430 ALA B N      1 
ATOM   6961 C  CA     . ALA B 1 434 ? -7.49500  -19.25300 22.48400  1.000 27.21379 ? 430 ALA B CA     1 
ATOM   6962 C  C      . ALA B 1 434 ? -7.45100  -20.66600 21.91600  1.000 22.47112 ? 430 ALA B C      1 
ATOM   6963 O  O      . ALA B 1 434 ? -6.37600  -21.26500 21.82700  1.000 23.84233 ? 430 ALA B O      1 
ATOM   6964 C  CB     . ALA B 1 434 ? -7.66900  -19.28800 23.99900  1.000 22.50007 ? 430 ALA B CB     1 
ATOM   6965 N  N      . ILE B 1 435 ? -8.59300  -21.20200 21.49300  1.000 26.25315 ? 431 ILE B N      1 
ATOM   6966 C  CA     . ILE B 1 435 ? -8.60800  -22.54400 20.91800  1.000 26.86638 ? 431 ILE B CA     1 
ATOM   6967 C  C      . ILE B 1 435 ? -7.87800  -22.56100 19.58200  1.000 23.44755 ? 431 ILE B C      1 
ATOM   6968 O  O      . ILE B 1 435 ? -7.13400  -23.49700 19.27900  1.000 23.92129 ? 431 ILE B O      1 
ATOM   6969 C  CB     . ILE B 1 435 ? -10.06400 -23.03300 20.76700  1.000 30.02202 ? 431 ILE B CB     1 
ATOM   6970 C  CG1    . ILE B 1 435 ? -10.77000 -23.02700 22.12100  1.000 30.76158 ? 431 ILE B CG1    1 
ATOM   6971 C  CG2    . ILE B 1 435 ? -10.11200 -24.40800 20.11200  1.000 32.25650 ? 431 ILE B CG2    1 
ATOM   6972 C  CD1    . ILE B 1 435 ? -12.30700 -23.23000 22.02500  1.000 27.79807 ? 431 ILE B CD1    1 
ATOM   6973 N  N      . GLY B 1 436 ? -8.11900  -21.54900 18.74400  1.000 23.50282 ? 432 GLY B N      1 
ATOM   6974 C  CA     . GLY B 1 436 ? -7.39100  -21.45100 17.49400  1.000 21.66049 ? 432 GLY B CA     1 
ATOM   6975 C  C      . GLY B 1 436 ? -5.91100  -21.24700 17.73200  1.000 28.02968 ? 432 GLY B C      1 
ATOM   6976 O  O      . GLY B 1 436 ? -5.07300  -21.82100 17.03400  1.000 27.49540 ? 432 GLY B O      1 
ATOM   6977 N  N      . GLY B 1 437 ? -5.57200  -20.45000 18.74400  1.000 24.74507 ? 433 GLY B N      1 
ATOM   6978 C  CA     . GLY B 1 437 ? -4.17700  -20.25300 19.07500  1.000 21.97369 ? 433 GLY B CA     1 
ATOM   6979 C  C      . GLY B 1 437 ? -3.48500  -21.54600 19.45200  1.000 28.12442 ? 433 GLY B C      1 
ATOM   6980 O  O      . GLY B 1 437 ? -2.36000  -21.81200 19.01000  1.000 29.01401 ? 433 GLY B O      1 
ATOM   6981 N  N      . LYS B 1 438 ? -4.14900  -22.37600 20.26500  1.000 24.60558 ? 434 LYS B N      1 
ATOM   6982 C  CA     . LYS B 1 438 ? -3.52800  -23.63400 20.67800  1.000 26.80585 ? 434 LYS B CA     1 
ATOM   6983 C  C      . LYS B 1 438 ? -3.32100  -24.55000 19.47900  1.000 27.17431 ? 434 LYS B C      1 
ATOM   6984 O  O      . LYS B 1 438 ? -2.31300  -25.26300 19.40200  1.000 27.90071 ? 434 LYS B O      1 
ATOM   6985 C  CB     . LYS B 1 438 ? -4.37100  -24.31700 21.75700  1.000 23.74495 ? 434 LYS B CB     1 
ATOM   6986 C  CG     . LYS B 1 438 ? -3.76400  -25.60000 22.33000  1.000 28.76398 ? 434 LYS B CG     1 
ATOM   6987 C  CD     . LYS B 1 438 ? -2.51400  -25.34700 23.19200  1.000 27.67963 ? 434 LYS B CD     1 
ATOM   6988 C  CE     . LYS B 1 438 ? -1.91900  -26.67200 23.68500  1.000 29.00085 ? 434 LYS B CE     1 
ATOM   6989 N  NZ     . LYS B 1 438 ? -1.01600  -26.51100 24.87300  1.000 37.54924 ? 434 LYS B NZ     1 
ATOM   6990 N  N      . LEU B 1 439 ? -4.26700  -24.54900 18.53300  1.000 29.05875 ? 435 LEU B N      1 
ATOM   6991 C  CA     . LEU B 1 439 ? -4.08600  -25.34300 17.31900  1.000 31.58537 ? 435 LEU B CA     1 
ATOM   6992 C  C      . LEU B 1 439 ? -2.92600  -24.81700 16.48800  1.000 23.76601 ? 435 LEU B C      1 
ATOM   6993 O  O      . LEU B 1 439 ? -2.27900  -25.58600 15.77000  1.000 29.42984 ? 435 LEU B O      1 
ATOM   6994 C  CB     . LEU B 1 439 ? -5.37400  -25.34900 16.48000  1.000 23.04487 ? 435 LEU B CB     1 
ATOM   6995 C  CG     . LEU B 1 439 ? -6.57900  -26.09300 17.07300  1.000 31.84066 ? 435 LEU B CG     1 
ATOM   6996 C  CD1    . LEU B 1 439 ? -7.79900  -25.90700 16.18900  1.000 22.40795 ? 435 LEU B CD1    1 
ATOM   6997 C  CD2    . LEU B 1 439 ? -6.26900  -27.57600 17.25900  1.000 31.67748 ? 435 LEU B CD2    1 
ATOM   6998 N  N      . ALA B 1 440 ? -2.64100  -23.51800 16.57300  1.000 29.65092 ? 436 ALA B N      1 
ATOM   6999 C  CA     . ALA B 1 440 ? -1.51700  -22.97000 15.82200  1.000 31.23532 ? 436 ALA B CA     1 
ATOM   7000 C  C      . ALA B 1 440 ? -0.19400  -23.26800 16.49900  1.000 29.48511 ? 436 ALA B C      1 
ATOM   7001 O  O      . ALA B 1 440 ? 0.81700   -23.43100 15.81900  1.000 31.56168 ? 436 ALA B O      1 
ATOM   7002 C  CB     . ALA B 1 440 ? -1.67600  -21.45800 15.65700  1.000 25.52411 ? 436 ALA B CB     1 
ATOM   7003 N  N      . ALA B 1 441 ? -0.19500  -23.40400 17.82000  1.000 33.36716 ? 437 ALA B N      1 
ATOM   7004 C  CA     . ALA B 1 441 ? 1.02100   -23.61000 18.60600  1.000 26.90059 ? 437 ALA B CA     1 
ATOM   7005 C  C      . ALA B 1 441 ? 0.78800   -24.75200 19.58700  1.000 31.25901 ? 437 ALA B C      1 
ATOM   7006 O  O      . ALA B 1 441 ? 0.74800   -24.55000 20.80600  1.000 33.18819 ? 437 ALA B O      1 
ATOM   7007 C  CB     . ALA B 1 441 ? 1.39900   -22.32100 19.33500  1.000 29.80357 ? 437 ALA B CB     1 
ATOM   7008 N  N      . PRO B 1 442 ? 0.63900   -25.97800 19.08300  1.000 33.55402 ? 438 PRO B N      1 
ATOM   7009 C  CA     . PRO B 1 442 ? 0.20600   -27.07900 19.95800  1.000 37.04655 ? 438 PRO B CA     1 
ATOM   7010 C  C      . PRO B 1 442 ? 1.23700   -27.45000 21.00700  1.000 32.74603 ? 438 PRO B C      1 
ATOM   7011 O  O      . PRO B 1 442 ? 0.88400   -28.04600 22.03100  1.000 39.55211 ? 438 PRO B O      1 
ATOM   7012 C  CB     . PRO B 1 442 ? -0.03900  -28.23100 18.97100  1.000 38.48356 ? 438 PRO B CB     1 
ATOM   7013 C  CG     . PRO B 1 442 ? 0.87500   -27.93600 17.81100  1.000 33.84616 ? 438 PRO B CG     1 
ATOM   7014 C  CD     . PRO B 1 442 ? 1.01700   -26.43600 17.73200  1.000 33.42506 ? 438 PRO B CD     1 
ATOM   7015 N  N      . ASP B 1 443 ? 2.48700   -27.09200 20.79000  1.000 35.90694 ? 439 ASP B N      1 
ATOM   7016 C  CA     . ASP B 1 443 ? 3.58800   -27.36200 21.70500  1.000 43.16044 ? 439 ASP B CA     1 
ATOM   7017 C  C      . ASP B 1 443 ? 3.68200   -26.35800 22.84800  1.000 39.71266 ? 439 ASP B C      1 
ATOM   7018 O  O      . ASP B 1 443 ? 4.51300   -26.54200 23.73800  1.000 43.53680 ? 439 ASP B O      1 
ATOM   7019 C  CB     . ASP B 1 443 ? 4.89500   -27.32500 20.91700  1.000 45.54493 ? 439 ASP B CB     1 
ATOM   7020 C  CG     . ASP B 1 443 ? 5.02400   -26.04100 20.09200  1.000 63.72343 ? 439 ASP B CG     1 
ATOM   7021 O  OD1    . ASP B 1 443 ? 4.01700   -25.62000 19.46300  1.000 64.07084 ? 439 ASP B OD1    1 
ATOM   7022 O  OD2    . ASP B 1 443 ? 6.12500   -25.44300 20.08900  1.000 71.42435 ? 439 ASP B OD2    1 
ATOM   7023 N  N      . ARG B 1 444 ? 2.88400   -25.30800 22.84100  1.000 38.17826 ? 440 ARG B N      1 
ATOM   7024 C  CA     . ARG B 1 444 ? 3.02400   -24.26500 23.83800  1.000 32.97501 ? 440 ARG B CA     1 
ATOM   7025 C  C      . ARG B 1 444 ? 1.78700   -24.19200 24.73800  1.000 37.88875 ? 440 ARG B C      1 
ATOM   7026 O  O      . ARG B 1 444 ? 0.67500   -24.50300 24.29900  1.000 35.53847 ? 440 ARG B O      1 
ATOM   7027 C  CB     . ARG B 1 444 ? 3.25500   -22.91700 23.14900  1.000 32.10911 ? 440 ARG B CB     1 
ATOM   7028 C  CG     . ARG B 1 444 ? 4.61100   -22.87500 22.43000  1.000 40.66014 ? 440 ARG B CG     1 
ATOM   7029 C  CD     . ARG B 1 444 ? 4.87000   -21.55600 21.72700  1.000 41.39970 ? 440 ARG B CD     1 
ATOM   7030 N  NE     . ARG B 1 444 ? 5.01800   -20.46400 22.67900  1.000 40.88648 ? 440 ARG B NE     1 
ATOM   7031 C  CZ     . ARG B 1 444 ? 5.15300   -19.19000 22.33600  1.000 42.74460 ? 440 ARG B CZ     1 
ATOM   7032 N  NH1    . ARG B 1 444 ? 5.16700   -18.84300 21.05700  1.000 49.27696 ? 440 ARG B NH1    1 
ATOM   7033 N  NH2    . ARG B 1 444 ? 5.26800   -18.26000 23.27100  1.000 45.91077 ? 440 ARG B NH2    1 
ATOM   7034 N  N      . PRO B 1 445 ? 1.95100   -23.81400 26.01000  1.000 35.53321 ? 441 PRO B N      1 
ATOM   7035 C  CA     . PRO B 1 445 ? 0.78000   -23.65700 26.88000  1.000 32.99080 ? 441 PRO B CA     1 
ATOM   7036 C  C      . PRO B 1 445 ? -0.03700  -22.45900 26.43700  1.000 32.80657 ? 441 PRO B C      1 
ATOM   7037 O  O      . PRO B 1 445 ? 0.50500   -21.41700 26.05800  1.000 33.48296 ? 441 PRO B O      1 
ATOM   7038 C  CB     . PRO B 1 445 ? 1.38000   -23.44400 28.27900  1.000 31.42745 ? 441 PRO B CB     1 
ATOM   7039 C  CG     . PRO B 1 445 ? 2.87800   -23.70200 28.13500  1.000 32.81709 ? 441 PRO B CG     1 
ATOM   7040 C  CD     . PRO B 1 445 ? 3.19400   -23.41700 26.69000  1.000 34.34359 ? 441 PRO B CD     1 
ATOM   7041 N  N      . VAL B 1 446 ? -1.35500  -22.61800 26.45500  1.000 27.62173 ? 442 VAL B N      1 
ATOM   7042 C  CA     . VAL B 1 446 ? -2.24500  -21.54200 26.05300  1.000 27.97441 ? 442 VAL B CA     1 
ATOM   7043 C  C      . VAL B 1 446 ? -3.23800  -21.31000 27.17300  1.000 29.47195 ? 442 VAL B C      1 
ATOM   7044 O  O      . VAL B 1 446 ? -3.91300  -22.24300 27.61800  1.000 29.37984 ? 442 VAL B O      1 
ATOM   7045 C  CB     . VAL B 1 446 ? -2.96400  -21.84700 24.72800  1.000 31.51957 ? 442 VAL B CB     1 
ATOM   7046 C  CG1    . VAL B 1 446 ? -4.10600  -20.83300 24.47800  1.000 32.24860 ? 442 VAL B CG1    1 
ATOM   7047 C  CG2    . VAL B 1 446 ? -1.96700  -21.83000 23.58800  1.000 30.86949 ? 442 VAL B CG2    1 
ATOM   7048 N  N      . VAL B 1 447 ? -3.30800  -20.07400 27.64200  1.000 35.11737 ? 443 VAL B N      1 
ATOM   7049 C  CA     . VAL B 1 447 ? -4.17200  -19.70100 28.74600  1.000 32.38020 ? 443 VAL B CA     1 
ATOM   7050 C  C      . VAL B 1 447 ? -4.96300  -18.47000 28.34200  1.000 31.75644 ? 443 VAL B C      1 
ATOM   7051 O  O      . VAL B 1 447 ? -4.43300  -17.56000 27.69500  1.000 28.44025 ? 443 VAL B O      1 
ATOM   7052 C  CB     . VAL B 1 447 ? -3.36100  -19.43900 30.02800  1.000 31.25638 ? 443 VAL B CB     1 
ATOM   7053 C  CG1    . VAL B 1 447 ? -4.27500  -18.86900 31.12000  1.000 26.78479 ? 443 VAL B CG1    1 
ATOM   7054 C  CG2    . VAL B 1 447 ? -2.69600  -20.73900 30.48300  1.000 25.98469 ? 443 VAL B CG2    1 
ATOM   7055 N  N      . ALA B 1 448 ? -6.23300  -18.44400 28.72500  1.000 26.93744 ? 444 ALA B N      1 
ATOM   7056 C  CA     . ALA B 1 448 ? -7.10200  -17.32000 28.43800  1.000 28.47447 ? 444 ALA B CA     1 
ATOM   7057 C  C      . ALA B 1 448 ? -7.58800  -16.74000 29.75300  1.000 30.47734 ? 444 ALA B C      1 
ATOM   7058 O  O      . ALA B 1 448 ? -8.06300  -17.47600 30.62400  1.000 35.11474 ? 444 ALA B O      1 
ATOM   7059 C  CB     . ALA B 1 448 ? -8.28200  -17.73800 27.58000  1.000 22.23951 ? 444 ALA B CB     1 
ATOM   7060 N  N      . LEU B 1 449 ? -7.43700  -15.44200 29.91100  1.000 25.03984 ? 445 LEU B N      1 
ATOM   7061 C  CA     . LEU B 1 449 ? -7.91400  -14.74700 31.09700  1.000 29.34299 ? 445 LEU B CA     1 
ATOM   7062 C  C      . LEU B 1 449 ? -9.13100  -13.94100 30.66500  1.000 30.82212 ? 445 LEU B C      1 
ATOM   7063 O  O      . LEU B 1 449 ? -9.01100  -13.03200 29.83500  1.000 26.43738 ? 445 LEU B O      1 
ATOM   7064 C  CB     . LEU B 1 449 ? -6.81700  -13.86500 31.69000  1.000 30.00360 ? 445 LEU B CB     1 
ATOM   7065 C  CG     . LEU B 1 449 ? -7.26800  -12.96300 32.83400  1.000 30.65894 ? 445 LEU B CG     1 
ATOM   7066 C  CD1    . LEU B 1 449 ? -7.52800  -13.79400 34.09200  1.000 29.28509 ? 445 LEU B CD1    1 
ATOM   7067 C  CD2    . LEU B 1 449 ? -6.21600  -11.88000 33.09100  1.000 27.89019 ? 445 LEU B CD2    1 
ATOM   7068 N  N      . VAL B 1 450 ? -10.30600 -14.29300 31.19800  1.000 24.82666 ? 446 VAL B N      1 
ATOM   7069 C  CA     . VAL B 1 450 ? -11.57100 -13.77400 30.68900  1.000 25.82941 ? 446 VAL B CA     1 
ATOM   7070 C  C      . VAL B 1 450 ? -12.53000 -13.51100 31.84200  1.000 26.80058 ? 446 VAL B C      1 
ATOM   7071 O  O      . VAL B 1 450 ? -12.42300 -14.11600 32.91300  1.000 29.74567 ? 446 VAL B O      1 
ATOM   7072 C  CB     . VAL B 1 450 ? -12.19700 -14.75400 29.67300  1.000 25.10038 ? 446 VAL B CB     1 
ATOM   7073 C  CG1    . VAL B 1 450 ? -11.14500 -15.18200 28.66100  1.000 28.74292 ? 446 VAL B CG1    1 
ATOM   7074 C  CG2    . VAL B 1 450 ? -12.73800 -15.97400 30.39500  1.000 27.27695 ? 446 VAL B CG2    1 
ATOM   7075 N  N      . GLY B 1 451 ? -13.46300 -12.58200 31.61300  1.000 24.67138 ? 447 GLY B N      1 
ATOM   7076 C  CA     . GLY B 1 451 ? -14.51600 -12.30100 32.56600  1.000 27.22695 ? 447 GLY B CA     1 
ATOM   7077 C  C      . GLY B 1 451 ? -15.71300 -13.24600 32.43500  1.000 32.21439 ? 447 GLY B C      1 
ATOM   7078 O  O      . GLY B 1 451 ? -15.87300 -13.96700 31.44500  1.000 30.19573 ? 447 GLY B O      1 
ATOM   7079 N  N      . ASP B 1 452 ? -16.56900 -13.22400 33.46800  1.000 25.25040 ? 448 ASP B N      1 
ATOM   7080 C  CA     . ASP B 1 452 ? -17.71600 -14.13000 33.49700  1.000 27.36381 ? 448 ASP B CA     1 
ATOM   7081 C  C      . ASP B 1 452 ? -18.78400 -13.72500 32.48800  1.000 31.35639 ? 448 ASP B C      1 
ATOM   7082 O  O      . ASP B 1 452 ? -19.35500 -14.58900 31.81700  1.000 28.10074 ? 448 ASP B O      1 
ATOM   7083 C  CB     . ASP B 1 452 ? -18.31500 -14.20400 34.90300  1.000 27.16905 ? 448 ASP B CB     1 
ATOM   7084 C  CG     . ASP B 1 452 ? -18.66800 -12.83500 35.47100  1.000 31.04846 ? 448 ASP B CG     1 
ATOM   7085 O  OD1    . ASP B 1 452 ? -17.87000 -11.88900 35.33000  1.000 31.49062 ? 448 ASP B OD1    1 
ATOM   7086 O  OD2    . ASP B 1 452 ? -19.75000 -12.70800 36.07600  1.000 32.10385 ? 448 ASP B OD2    1 
ATOM   7087 N  N      . ALA B 1 453 ? -19.05100 -12.42300 32.33100  1.000 27.99546 ? 449 ALA B N      1 
ATOM   7088 C  CA     . ALA B 1 453 ? -20.02300 -12.03300 31.31400  1.000 29.50091 ? 449 ALA B CA     1 
ATOM   7089 C  C      . ALA B 1 453 ? -19.51800 -12.38700 29.92200  1.000 33.77773 ? 449 ALA B C      1 
ATOM   7090 O  O      . ALA B 1 453 ? -20.28900 -12.85500 29.07500  1.000 33.90407 ? 449 ALA B O      1 
ATOM   7091 C  CB     . ALA B 1 453 ? -20.35600 -10.54400 31.41100  1.000 25.83468 ? 449 ALA B CB     1 
ATOM   7092 N  N      . ALA B 1 454 ? -18.22100 -12.18700 29.66500  1.000 30.25363 ? 450 ALA B N      1 
ATOM   7093 C  CA     . ALA B 1 454 ? -17.66900 -12.58600 28.37100  1.000 31.91962 ? 450 ALA B CA     1 
ATOM   7094 C  C      . ALA B 1 454 ? -17.74200 -14.09800 28.19200  1.000 29.69567 ? 450 ALA B C      1 
ATOM   7095 O  O      . ALA B 1 454 ? -17.96000 -14.59300 27.08000  1.000 30.40628 ? 450 ALA B O      1 
ATOM   7096 C  CB     . ALA B 1 454 ? -16.23100 -12.09400 28.21900  1.000 30.96424 ? 450 ALA B CB     1 
ATOM   7097 N  N      . PHE B 1 455 ? -17.55100 -14.85200 29.27000  1.000 27.30064 ? 451 PHE B N      1 
ATOM   7098 C  CA     . PHE B 1 455 ? -17.66000 -16.29800 29.15300  1.000 28.10337 ? 451 PHE B CA     1 
ATOM   7099 C  C      . PHE B 1 455 ? -19.09700 -16.73400 28.88500  1.000 31.84329 ? 451 PHE B C      1 
ATOM   7100 O  O      . PHE B 1 455 ? -19.31900 -17.73200 28.18900  1.000 28.56658 ? 451 PHE B O      1 
ATOM   7101 C  CB     . PHE B 1 455 ? -17.11700 -16.98800 30.40600  1.000 27.40329 ? 451 PHE B CB     1 
ATOM   7102 C  CG     . PHE B 1 455 ? -16.69500 -18.39600 30.15600  1.000 23.90813 ? 451 PHE B CG     1 
ATOM   7103 C  CD1    . PHE B 1 455 ? -15.42200 -18.67400 29.68200  1.000 22.69746 ? 451 PHE B CD1    1 
ATOM   7104 C  CD2    . PHE B 1 455 ? -17.59200 -19.44100 30.33700  1.000 31.76433 ? 451 PHE B CD2    1 
ATOM   7105 C  CE1    . PHE B 1 455 ? -15.03500 -19.97300 29.41000  1.000 27.48751 ? 451 PHE B CE1    1 
ATOM   7106 C  CE2    . PHE B 1 455 ? -17.22100 -20.75000 30.07700  1.000 31.84592 ? 451 PHE B CE2    1 
ATOM   7107 C  CZ     . PHE B 1 455 ? -15.93900 -21.02100 29.61700  1.000 31.59589 ? 451 PHE B CZ     1 
ATOM   7108 N  N      . ALA B 1 456 ? -20.08600 -16.01800 29.42300  1.000 33.80405 ? 452 ALA B N      1 
ATOM   7109 C  CA     . ALA B 1 456 ? -21.47100 -16.31900 29.06500  1.000 30.99845 ? 452 ALA B CA     1 
ATOM   7110 C  C      . ALA B 1 456 ? -21.75000 -16.03900 27.59300  1.000 32.90395 ? 452 ALA B C      1 
ATOM   7111 O  O      . ALA B 1 456 ? -22.67800 -16.61400 27.01700  1.000 32.98553 ? 452 ALA B O      1 
ATOM   7112 C  CB     . ALA B 1 456 ? -22.44200 -15.51600 29.93800  1.000 25.36883 ? 452 ALA B CB     1 
ATOM   7113 N  N      . MET B 1 457 ? -20.96300 -15.18500 26.96300  1.000 29.39826 ? 453 MET B N      1 
ATOM   7114 C  CA     . MET B 1 457 ? -21.24500 -14.89200 25.56600  1.000 31.83540 ? 453 MET B CA     1 
ATOM   7115 C  C      . MET B 1 457 ? -20.74400 -16.00000 24.64500  1.000 30.16941 ? 453 MET B C      1 
ATOM   7116 O  O      . MET B 1 457 ? -21.44000 -16.36900 23.70300  1.000 30.56945 ? 453 MET B O      1 
ATOM   7117 C  CB     . MET B 1 457 ? -20.60400 -13.56600 25.16800  1.000 37.46502 ? 453 MET B CB     1 
ATOM   7118 C  CG     . MET B 1 457 ? -21.11400 -12.35000 25.88700  1.000 41.67079 ? 453 MET B CG     1 
ATOM   7119 S  SD     . MET B 1 457 ? -20.70400 -10.94100 24.84400  1.000 41.01018 ? 453 MET B SD     1 
ATOM   7120 C  CE     . MET B 1 457 ? -21.08600 -11.70300 23.29500  1.000 52.66158 ? 453 MET B CE     1 
ATOM   7121 N  N      . ASN B 1 458 ? -19.54700 -16.54900 24.89800  1.000 33.12766 ? 454 ASN B N      1 
ATOM   7122 C  CA     . ASN B 1 458 ? -18.94400 -17.49900 23.96800  1.000 30.40891 ? 454 ASN B CA     1 
ATOM   7123 C  C      . ASN B 1 458 ? -18.33900 -18.72300 24.65600  1.000 28.85346 ? 454 ASN B C      1 
ATOM   7124 O  O      . ASN B 1 458 ? -17.66100 -19.52400 23.98900  1.000 29.52986 ? 454 ASN B O      1 
ATOM   7125 C  CB     . ASN B 1 458 ? -17.87700 -16.79400 23.13300  1.000 32.73814 ? 454 ASN B CB     1 
ATOM   7126 C  CG     . ASN B 1 458 ? -18.47700 -15.83700 22.11600  1.000 42.05504 ? 454 ASN B CG     1 
ATOM   7127 O  OD1    . ASN B 1 458 ? -18.46900 -14.61800 22.30800  1.000 38.70990 ? 454 ASN B OD1    1 
ATOM   7128 N  ND2    . ASN B 1 458 ? -19.02300 -16.39000 21.03200  1.000 38.92046 ? 454 ASN B ND2    1 
ATOM   7129 N  N      . GLY B 1 459 ? -18.58000 -18.90600 25.95400  1.000 30.45628 ? 455 GLY B N      1 
ATOM   7130 C  CA     . GLY B 1 459 ? -17.95800 -19.99400 26.69000  1.000 32.21176 ? 455 GLY B CA     1 
ATOM   7131 C  C      . GLY B 1 459 ? -18.40900 -21.37200 26.26500  1.000 27.18221 ? 455 GLY B C      1 
ATOM   7132 O  O      . GLY B 1 459 ? -17.74300 -22.36100 26.59800  1.000 26.57687 ? 455 GLY B O      1 
ATOM   7133 N  N      . MET B 1 460 ? -19.53100 -21.47200 25.55300  1.000 26.63477 ? 456 MET B N      1 
ATOM   7134 C  CA     . MET B 1 460 ? -19.94000 -22.78500 25.06400  1.000 29.40089 ? 456 MET B CA     1 
ATOM   7135 C  C      . MET B 1 460 ? -18.84900 -23.42500 24.22200  1.000 26.81637 ? 456 MET B C      1 
ATOM   7136 O  O      . MET B 1 460 ? -18.82600 -24.65400 24.09400  1.000 29.78778 ? 456 MET B O      1 
ATOM   7137 C  CB     . MET B 1 460 ? -21.23700 -22.69000 24.24200  1.000 32.35388 ? 456 MET B CB     1 
ATOM   7138 C  CG     . MET B 1 460 ? -22.44200 -22.22100 25.03300  1.000 41.54182 ? 456 MET B CG     1 
ATOM   7139 S  SD     . MET B 1 460 ? -22.85900 -23.37400 26.35700  1.000 44.81853 ? 456 MET B SD     1 
ATOM   7140 C  CE     . MET B 1 460 ? -23.33100 -24.79900 25.40700  1.000 34.45413 ? 456 MET B CE     1 
ATOM   7141 N  N      . GLU B 1 461 ? -17.92700 -22.62500 23.66800  1.000 24.66348 ? 457 GLU B N      1 
ATOM   7142 C  CA     . GLU B 1 461 ? -16.88500 -23.17700 22.80600  1.000 28.15601 ? 457 GLU B CA     1 
ATOM   7143 C  C      . GLU B 1 461 ? -15.91400 -24.08400 23.53700  1.000 29.92727 ? 457 GLU B C      1 
ATOM   7144 O  O      . GLU B 1 461 ? -15.15400 -24.79500 22.86700  1.000 28.26655 ? 457 GLU B O      1 
ATOM   7145 C  CB     . GLU B 1 461 ? -16.09100 -22.06500 22.12200  1.000 31.75644 ? 457 GLU B CB     1 
ATOM   7146 C  CG     . GLU B 1 461 ? -16.93600 -21.22600 21.16400  1.000 34.54362 ? 457 GLU B CG     1 
ATOM   7147 C  CD     . GLU B 1 461 ? -17.54500 -22.02500 20.00200  1.000 35.40161 ? 457 GLU B CD     1 
ATOM   7148 O  OE1    . GLU B 1 461 ? -18.41100 -21.44300 19.31700  1.000 32.85920 ? 457 GLU B OE1    1 
ATOM   7149 O  OE2    . GLU B 1 461 ? -17.16600 -23.20500 19.75100  1.000 31.03530 ? 457 GLU B OE2    1 
ATOM   7150 N  N      . ILE B 1 462 ? -15.88800 -24.07500 24.87400  1.000 28.47447 ? 458 ILE B N      1 
ATOM   7151 C  CA     . ILE B 1 462 ? -15.03200 -25.04500 25.54000  1.000 28.59290 ? 458 ILE B CA     1 
ATOM   7152 C  C      . ILE B 1 462 ? -15.50100 -26.45400 25.21400  1.000 25.60570 ? 458 ILE B C      1 
ATOM   7153 O  O      . ILE B 1 462 ? -14.72500 -27.41100 25.32400  1.000 27.95598 ? 458 ILE B O      1 
ATOM   7154 C  CB     . ILE B 1 462 ? -14.97100 -24.81300 27.06900  1.000 31.22743 ? 458 ILE B CB     1 
ATOM   7155 C  CG1    . ILE B 1 462 ? -16.34100 -25.06200 27.72200  1.000 30.26942 ? 458 ILE B CG1    1 
ATOM   7156 C  CG2    . ILE B 1 462 ? -14.43200 -23.41200 27.37400  1.000 22.06844 ? 458 ILE B CG2    1 
ATOM   7157 C  CD1    . ILE B 1 462 ? -16.28600 -25.09000 29.25100  1.000 36.61755 ? 458 ILE B CD1    1 
ATOM   7158 N  N      . HIS B 1 463 ? -16.75600 -26.61200 24.79700  1.000 26.10313 ? 459 HIS B N      1 
ATOM   7159 C  CA     . HIS B 1 463 ? -17.17600 -27.92800 24.32900  1.000 33.83300 ? 459 HIS B CA     1 
ATOM   7160 C  C      . HIS B 1 463 ? -16.41800 -28.31800 23.06700  1.000 27.44276 ? 459 HIS B C      1 
ATOM   7161 O  O      . HIS B 1 463 ? -16.04900 -29.48000 22.88700  1.000 28.08758 ? 459 HIS B O      1 
ATOM   7162 C  CB     . HIS B 1 463 ? -18.68100 -27.95900 24.07300  1.000 29.53775 ? 459 HIS B CB     1 
ATOM   7163 C  CG     . HIS B 1 463 ? -19.17700 -29.31700 23.70300  1.000 31.39061 ? 459 HIS B CG     1 
ATOM   7164 N  ND1    . HIS B 1 463 ? -19.57300 -29.64100 22.42400  1.000 27.98230 ? 459 HIS B ND1    1 
ATOM   7165 C  CD2    . HIS B 1 463 ? -19.28100 -30.45500 24.43200  1.000 31.86171 ? 459 HIS B CD2    1 
ATOM   7166 C  CE1    . HIS B 1 463 ? -19.93600 -30.91000 22.38900  1.000 30.37206 ? 459 HIS B CE1    1 
ATOM   7167 N  NE2    . HIS B 1 463 ? -19.75100 -31.43200 23.59000  1.000 29.47459 ? 459 HIS B NE2    1 
ATOM   7168 N  N      . THR B 1 464 ? -16.14700 -27.34500 22.20400  1.000 29.98254 ? 460 THR B N      1 
ATOM   7169 C  CA     . THR B 1 464 ? -15.32200 -27.59800 21.03100  1.000 33.95933 ? 460 THR B CA     1 
ATOM   7170 C  C      . THR B 1 464 ? -13.92500 -28.03900 21.43600  1.000 27.24537 ? 460 THR B C      1 
ATOM   7171 O  O      . THR B 1 464 ? -13.38500 -29.01000 20.88800  1.000 25.72414 ? 460 THR B O      1 
ATOM   7172 C  CB     . THR B 1 464 ? -15.26900 -26.33600 20.17400  1.000 29.94833 ? 460 THR B CB     1 
ATOM   7173 O  OG1    . THR B 1 464 ? -16.61100 -25.95500 19.83300  1.000 35.47267 ? 460 THR B OG1    1 
ATOM   7174 C  CG2    . THR B 1 464 ? -14.45000 -26.57000 18.90600  1.000 25.39252 ? 460 THR B CG2    1 
ATOM   7175 N  N      . ALA B 1 465 ? -13.34400 -27.37300 22.43000  1.000 27.66384 ? 461 ALA B N      1 
ATOM   7176 C  CA     . ALA B 1 465 ? -12.03600 -27.79800 22.91800  1.000 30.11151 ? 461 ALA B CA     1 
ATOM   7177 C  C      . ALA B 1 465 ? -12.09900 -29.21200 23.47900  1.000 32.06963 ? 461 ALA B C      1 
ATOM   7178 O  O      . ALA B 1 465 ? -11.17800 -30.01200 23.27400  1.000 29.17981 ? 461 ALA B O      1 
ATOM   7179 C  CB     . ALA B 1 465 ? -11.52700 -26.81900 23.97100  1.000 26.51371 ? 461 ALA B CB     1 
ATOM   7180 N  N      . ALA B 1 466 ? -13.18100 -29.54300 24.19400  1.000 36.67282 ? 462 ALA B N      1 
ATOM   7181 C  CA     . ALA B 1 466 ? -13.32600 -30.90100 24.71900  1.000 35.53847 ? 462 ALA B CA     1 
ATOM   7182 C  C      . ALA B 1 466 ? -13.45900 -31.91100 23.58700  1.000 32.21965 ? 462 ALA B C      1 
ATOM   7183 O  O      . ALA B 1 466 ? -12.80400 -32.96400 23.59400  1.000 28.85872 ? 462 ALA B O      1 
ATOM   7184 C  CB     . ALA B 1 466 ? -14.54800 -30.98300 25.64300  1.000 29.62987 ? 462 ALA B CB     1 
ATOM   7185 N  N      . GLU B 1 467 ? -14.28800 -31.59400 22.59400  1.000 26.64530 ? 463 GLU B N      1 
ATOM   7186 C  CA     . GLU B 1 467 ? -14.52000 -32.52100 21.49400  1.000 28.35340 ? 463 GLU B CA     1 
ATOM   7187 C  C      . GLU B 1 467 ? -13.21600 -32.88600 20.79600  1.000 27.88755 ? 463 GLU B C      1 
ATOM   7188 O  O      . GLU B 1 467 ? -12.97300 -34.05900 20.49600  1.000 28.91136 ? 463 GLU B O      1 
ATOM   7189 C  CB     . GLU B 1 467 ? -15.49900 -31.89500 20.50300  1.000 28.24549 ? 463 GLU B CB     1 
ATOM   7190 C  CG     . GLU B 1 467 ? -16.91900 -31.87300 20.98800  1.000 29.04296 ? 463 GLU B CG     1 
ATOM   7191 C  CD     . GLU B 1 467 ? -17.54000 -33.24000 20.91500  1.000 36.99654 ? 463 GLU B CD     1 
ATOM   7192 O  OE1    . GLU B 1 467 ? -17.79500 -33.84300 21.97900  1.000 44.45270 ? 463 GLU B OE1    1 
ATOM   7193 O  OE2    . GLU B 1 467 ? -17.75200 -33.71100 19.78000  1.000 37.29395 ? 463 GLU B OE2    1 
ATOM   7194 N  N      . TYR B 1 468 ? -12.34900 -31.90700 20.55500  1.000 25.82415 ? 464 TYR B N      1 
ATOM   7195 C  CA     . TYR B 1 468 ? -11.12200 -32.16900 19.81400  1.000 31.50378 ? 464 TYR B CA     1 
ATOM   7196 C  C      . TYR B 1 468 ? -9.90000  -32.34000 20.71600  1.000 34.81470 ? 464 TYR B C      1 
ATOM   7197 O  O      . TYR B 1 468 ? -8.78400  -32.47000 20.20000  1.000 30.43260 ? 464 TYR B O      1 
ATOM   7198 C  CB     . TYR B 1 468 ? -10.87200 -31.05400 18.79600  1.000 26.55845 ? 464 TYR B CB     1 
ATOM   7199 C  CG     . TYR B 1 468 ? -11.90800 -31.02900 17.70600  1.000 32.98027 ? 464 TYR B CG     1 
ATOM   7200 C  CD1    . TYR B 1 468 ? -11.75300 -31.78700 16.55200  1.000 32.28808 ? 464 TYR B CD1    1 
ATOM   7201 C  CD2    . TYR B 1 468 ? -13.05900 -30.26500 17.83500  1.000 26.16366 ? 464 TYR B CD2    1 
ATOM   7202 C  CE1    . TYR B 1 468 ? -12.72400 -31.77700 15.55300  1.000 30.06939 ? 464 TYR B CE1    1 
ATOM   7203 C  CE2    . TYR B 1 468 ? -14.01600 -30.24700 16.84400  1.000 29.75883 ? 464 TYR B CE2    1 
ATOM   7204 C  CZ     . TYR B 1 468 ? -13.85000 -31.01000 15.71100  1.000 23.26595 ? 464 TYR B CZ     1 
ATOM   7205 O  OH     . TYR B 1 468 ? -14.82000 -30.98400 14.73100  1.000 26.41896 ? 464 TYR B OH     1 
ATOM   7206 N  N      . LYS B 1 469 ? -10.07800 -32.38100 22.04200  1.000 33.47507 ? 465 LYS B N      1 
ATOM   7207 C  CA     . LYS B 1 469 ? -8.95600  -32.57700 22.97100  1.000 35.46478 ? 465 LYS B CA     1 
ATOM   7208 C  C      . LYS B 1 469 ? -7.89700  -31.48400 22.80400  1.000 31.79855 ? 465 LYS B C      1 
ATOM   7209 O  O      . LYS B 1 469 ? -6.70400  -31.76000 22.70400  1.000 35.80956 ? 465 LYS B O      1 
ATOM   7210 C  CB     . LYS B 1 469 ? -8.31900  -33.95800 22.77500  1.000 33.31452 ? 465 LYS B CB     1 
ATOM   7211 C  CG     . LYS B 1 469 ? -9.31200  -35.12000 22.63800  1.000 47.51096 ? 465 LYS B CG     1 
ATOM   7212 C  CD     . LYS B 1 469 ? -8.58400  -36.46800 22.64000  1.000 55.23557 ? 465 LYS B CD     1 
ATOM   7213 C  CE     . LYS B 1 469 ? -9.42500  -37.58800 22.03100  1.000 60.72044 ? 465 LYS B CE     1 
ATOM   7214 N  NZ     . LYS B 1 469 ? -8.59400  -38.78600 21.70000  1.000 68.42136 ? 465 LYS B NZ     1 
ATOM   7215 N  N      . ILE B 1 470 ? -8.33800  -30.22900 22.80000  1.000 28.37972 ? 466 ILE B N      1 
ATOM   7216 C  CA     . ILE B 1 470 ? -7.45000  -29.08000 22.61500  1.000 32.54864 ? 466 ILE B CA     1 
ATOM   7217 C  C      . ILE B 1 470 ? -7.14100  -28.51800 23.99800  1.000 32.88552 ? 466 ILE B C      1 
ATOM   7218 O  O      . ILE B 1 470 ? -8.04600  -27.95600 24.64100  1.000 33.61719 ? 466 ILE B O      1 
ATOM   7219 C  CB     . ILE B 1 470 ? -8.10200  -28.02200 21.70700  1.000 31.04846 ? 466 ILE B CB     1 
ATOM   7220 C  CG1    . ILE B 1 470 ? -8.38300  -28.59600 20.31000  1.000 30.15625 ? 466 ILE B CG1    1 
ATOM   7221 C  CG2    . ILE B 1 470 ? -7.23700  -26.77300 21.57700  1.000 28.09547 ? 466 ILE B CG2    1 
ATOM   7222 C  CD1    . ILE B 1 470 ? -9.34300  -27.72700 19.45100  1.000 31.66432 ? 466 ILE B CD1    1 
ATOM   7223 N  N      . PRO B 1 471 ? -5.91500  -28.67900 24.52500  1.000 34.11988 ? 467 PRO B N      1 
ATOM   7224 C  CA     . PRO B 1 471 ? -5.66200  -28.26400 25.91300  1.000 35.37793 ? 467 PRO B CA     1 
ATOM   7225 C  C      . PRO B 1 471 ? -5.45300  -26.76800 26.07900  1.000 33.97513 ? 467 PRO B C      1 
ATOM   7226 O  O      . PRO B 1 471 ? -4.35000  -26.24000 25.89300  1.000 37.87559 ? 467 PRO B O      1 
ATOM   7227 C  CB     . PRO B 1 471 ? -4.40400  -29.05600 26.31000  1.000 36.02537 ? 467 PRO B CB     1 
ATOM   7228 C  CG     . PRO B 1 471 ? -4.04500  -29.90300 25.13500  1.000 31.39324 ? 467 PRO B CG     1 
ATOM   7229 C  CD     . PRO B 1 471 ? -4.77400  -29.40600 23.94200  1.000 26.78479 ? 467 PRO B CD     1 
ATOM   7230 N  N      . VAL B 1 472 ? -6.52000  -26.08200 26.46900  1.000 36.94654 ? 468 VAL B N      1 
ATOM   7231 C  CA     . VAL B 1 472 ? -6.48000  -24.66300 26.79600  1.000 34.12514 ? 468 VAL B CA     1 
ATOM   7232 C  C      . VAL B 1 472 ? -6.96000  -24.51900 28.23000  1.000 33.71194 ? 468 VAL B C      1 
ATOM   7233 O  O      . VAL B 1 472 ? -7.76300  -25.32400 28.71300  1.000 25.74519 ? 468 VAL B O      1 
ATOM   7234 C  CB     . VAL B 1 472 ? -7.35400  -23.82100 25.83900  1.000 32.99869 ? 468 VAL B CB     1 
ATOM   7235 C  CG1    . VAL B 1 472 ? -7.54200  -22.40100 26.37500  1.000 27.12430 ? 468 VAL B CG1    1 
ATOM   7236 C  CG2    . VAL B 1 472 ? -6.75400  -23.79100 24.43900  1.000 26.85322 ? 468 VAL B CG2    1 
ATOM   7237 N  N      . THR B 1 473 ? -6.42600  -23.52800 28.93600  1.000 28.67975 ? 469 THR B N      1 
ATOM   7238 C  CA     . THR B 1 473 ? -6.89100  -23.22500 30.28100  1.000 30.74842 ? 469 THR B CA     1 
ATOM   7239 C  C      . THR B 1 473 ? -7.54900  -21.85000 30.29200  1.000 35.57005 ? 469 THR B C      1 
ATOM   7240 O  O      . THR B 1 473 ? -6.89500  -20.84300 29.98600  1.000 31.28270 ? 469 THR B O      1 
ATOM   7241 C  CB     . THR B 1 473 ? -5.74500  -23.29600 31.27900  1.000 34.27779 ? 469 THR B CB     1 
ATOM   7242 O  OG1    . THR B 1 473 ? -5.24200  -24.63400 31.28500  1.000 34.92787 ? 469 THR B OG1    1 
ATOM   7243 C  CG2    . THR B 1 473 ? -6.24200  -22.94300 32.68000  1.000 29.64303 ? 469 THR B CG2    1 
ATOM   7244 N  N      . TRP B 1 474 ? -8.84500  -21.82000 30.62000  1.000 24.40293 ? 470 TRP B N      1 
ATOM   7245 C  CA     . TRP B 1 474 ? -9.57700  -20.57900 30.83700  1.000 25.62939 ? 470 TRP B CA     1 
ATOM   7246 C  C      . TRP B 1 474 ? -9.57200  -20.23800 32.32300  1.000 29.74567 ? 470 TRP B C      1 
ATOM   7247 O  O      . TRP B 1 474 ? -9.91800  -21.07400 33.16100  1.000 31.68538 ? 470 TRP B O      1 
ATOM   7248 C  CB     . TRP B 1 474 ? -11.02500 -20.69200 30.33900  1.000 24.58453 ? 470 TRP B CB     1 
ATOM   7249 C  CG     . TRP B 1 474 ? -11.13900 -20.78200 28.85100  1.000 27.55594 ? 470 TRP B CG     1 
ATOM   7250 C  CD1    . TRP B 1 474 ? -11.30700 -19.74200 27.97200  1.000 27.00061 ? 470 TRP B CD1    1 
ATOM   7251 C  CD2    . TRP B 1 474 ? -11.10200 -21.97700 28.06100  1.000 25.08195 ? 470 TRP B CD2    1 
ATOM   7252 N  NE1    . TRP B 1 474 ? -11.37100 -20.22400 26.67900  1.000 30.75632 ? 470 TRP B NE1    1 
ATOM   7253 C  CE2    . TRP B 1 474 ? -11.24200 -21.59100 26.70900  1.000 29.36931 ? 470 TRP B CE2    1 
ATOM   7254 C  CE3    . TRP B 1 474 ? -10.96900 -23.33300 28.36500  1.000 28.71397 ? 470 TRP B CE3    1 
ATOM   7255 C  CZ2    . TRP B 1 474 ? -11.25000 -22.51400 25.66600  1.000 27.83228 ? 470 TRP B CZ2    1 
ATOM   7256 C  CZ3    . TRP B 1 474 ? -10.96200 -24.25500 27.31900  1.000 27.36118 ? 470 TRP B CZ3    1 
ATOM   7257 C  CH2    . TRP B 1 474 ? -11.10300 -23.83600 25.98700  1.000 29.44827 ? 470 TRP B CH2    1 
ATOM   7258 N  N      . ILE B 1 475 ? -9.19200  -19.01000 32.63600  1.000 28.36393 ? 471 ILE B N      1 
ATOM   7259 C  CA     . ILE B 1 475 ? -9.27700  -18.45500 33.97800  1.000 28.96663 ? 471 ILE B CA     1 
ATOM   7260 C  C      . ILE B 1 475 ? -10.37600 -17.40100 33.94600  1.000 34.82260 ? 471 ILE B C      1 
ATOM   7261 O  O      . ILE B 1 475 ? -10.21300 -16.34200 33.32300  1.000 30.62736 ? 471 ILE B O      1 
ATOM   7262 C  CB     . ILE B 1 475 ? -7.93700  -17.85900 34.42700  1.000 28.83240 ? 471 ILE B CB     1 
ATOM   7263 C  CG1    . ILE B 1 475 ? -6.84700  -18.92800 34.36500  1.000 27.13483 ? 471 ILE B CG1    1 
ATOM   7264 C  CG2    . ILE B 1 475 ? -8.05100  -17.24400 35.83200  1.000 31.54852 ? 471 ILE B CG2    1 
ATOM   7265 C  CD1    . ILE B 1 475 ? -5.45100  -18.33600 34.30400  1.000 30.58788 ? 471 ILE B CD1    1 
ATOM   7266 N  N      . VAL B 1 476 ? -11.50500 -17.69600 34.59500  1.000 32.67760 ? 472 VAL B N      1 
ATOM   7267 C  CA     . VAL B 1 476 ? -12.67000 -16.81900 34.58700  1.000 27.13220 ? 472 VAL B CA     1 
ATOM   7268 C  C      . VAL B 1 476 ? -12.65800 -15.96300 35.84700  1.000 33.68299 ? 472 VAL B C      1 
ATOM   7269 O  O      . VAL B 1 476 ? -12.74600 -16.48300 36.97200  1.000 25.30040 ? 472 VAL B O      1 
ATOM   7270 C  CB     . VAL B 1 476 ? -13.97400 -17.62200 34.49000  1.000 33.07239 ? 472 VAL B CB     1 
ATOM   7271 C  CG1    . VAL B 1 476 ? -15.14700 -16.66800 34.40300  1.000 34.68837 ? 472 VAL B CG1    1 
ATOM   7272 C  CG2    . VAL B 1 476 ? -13.93500 -18.56300 33.28200  1.000 28.38761 ? 472 VAL B CG2    1 
ATOM   7273 N  N      . LEU B 1 477 ? -12.54500 -14.65100 35.66400  1.000 28.50342 ? 473 LEU B N      1 
ATOM   7274 C  CA     . LEU B 1 477 ? -12.67800 -13.70800 36.76900  1.000 26.05576 ? 473 LEU B CA     1 
ATOM   7275 C  C      . LEU B 1 477 ? -14.16300 -13.58000 37.05500  1.000 30.56682 ? 473 LEU B C      1 
ATOM   7276 O  O      . LEU B 1 477 ? -14.87600 -12.77500 36.44700  1.000 32.04068 ? 473 LEU B O      1 
ATOM   7277 C  CB     . LEU B 1 477 ? -12.05000 -12.36700 36.41200  1.000 26.80848 ? 473 LEU B CB     1 
ATOM   7278 C  CG     . LEU B 1 477 ? -10.55200 -12.48100 36.12000  1.000 31.59063 ? 473 LEU B CG     1 
ATOM   7279 C  CD1    . LEU B 1 477 ? -9.98700  -11.14100 35.73900  1.000 29.62987 ? 473 LEU B CD1    1 
ATOM   7280 C  CD2    . LEU B 1 477 ? -9.84700  -13.05400 37.35300  1.000 26.59003 ? 473 LEU B CD2    1 
ATOM   7281 N  N      . ASN B 1 478 ? -14.64400 -14.38100 37.99400  1.000 31.64327 ? 474 ASN B N      1 
ATOM   7282 C  CA     . ASN B 1 478 ? -16.07700 -14.45500 38.24300  1.000 31.24322 ? 474 ASN B CA     1 
ATOM   7283 C  C      . ASN B 1 478 ? -16.43700 -13.43800 39.32100  1.000 35.20685 ? 474 ASN B C      1 
ATOM   7284 O  O      . ASN B 1 478 ? -16.42900 -13.72900 40.51900  1.000 32.70655 ? 474 ASN B O      1 
ATOM   7285 C  CB     . ASN B 1 478 ? -16.47200 -15.87200 38.63000  1.000 33.00133 ? 474 ASN B CB     1 
ATOM   7286 C  CG     . ASN B 1 478 ? -17.95800 -16.03400 38.73300  1.000 32.75919 ? 474 ASN B CG     1 
ATOM   7287 O  OD1    . ASN B 1 478 ? -18.69400 -15.06100 38.58100  1.000 31.19321 ? 474 ASN B OD1    1 
ATOM   7288 N  ND2    . ASN B 1 478 ? -18.41600 -17.25100 39.00800  1.000 29.90359 ? 474 ASN B ND2    1 
ATOM   7289 N  N      . ASN B 1 479 ? -16.77600 -12.22500 38.88600  1.000 35.74113 ? 475 ASN B N      1 
ATOM   7290 C  CA     . ASN B 1 479 ? -17.23500 -11.18100 39.79100  1.000 34.25937 ? 475 ASN B CA     1 
ATOM   7291 C  C      . ASN B 1 479 ? -18.74900 -10.98600 39.73900  1.000 29.44300 ? 475 ASN B C      1 
ATOM   7292 O  O      . ASN B 1 479 ? -19.24300 -9.94300  40.17100  1.000 32.70918 ? 475 ASN B O      1 
ATOM   7293 C  CB     . ASN B 1 479 ? -16.50900 -9.86000  39.50100  1.000 30.42470 ? 475 ASN B CB     1 
ATOM   7294 C  CG     . ASN B 1 479 ? -16.64300 -9.41100  38.06100  1.000 33.43822 ? 475 ASN B CG     1 
ATOM   7295 O  OD1    . ASN B 1 479 ? -17.44100 -9.95500  37.29700  1.000 34.61994 ? 475 ASN B OD1    1 
ATOM   7296 N  ND2    . ASN B 1 479 ? -15.85900 -8.40600  37.68000  1.000 32.87499 ? 475 ASN B ND2    1 
ATOM   7297 N  N      . GLY B 1 480 ? -19.48500 -11.96700 39.22100  1.000 33.81458 ? 476 GLY B N      1 
ATOM   7298 C  CA     . GLY B 1 480 ? -20.94500 -11.92400 39.19700  1.000 30.13782 ? 476 GLY B CA     1 
ATOM   7299 C  C      . GLY B 1 480 ? -21.55300 -10.78900 38.39500  1.000 31.36692 ? 476 GLY B C      1 
ATOM   7300 O  O      . GLY B 1 480 ? -22.57100 -10.22100 38.80700  1.000 34.30411 ? 476 GLY B O      1 
ATOM   7301 N  N      . GLY B 1 481 ? -20.98600 -10.46800 37.23900  1.000 28.11390 ? 477 GLY B N      1 
ATOM   7302 C  CA     . GLY B 1 481 ? -21.61800 -9.48300  36.38700  1.000 29.60092 ? 477 GLY B CA     1 
ATOM   7303 C  C      . GLY B 1 481 ? -20.59100 -8.65700  35.64100  1.000 28.17180 ? 477 GLY B C      1 
ATOM   7304 O  O      . GLY B 1 481 ? -19.46000 -9.09500  35.42700  1.000 28.20601 ? 477 GLY B O      1 
ATOM   7305 N  N      . HIS B 1 482 ? -21.01900 -7.46500  35.22000  1.000 29.33773 ? 478 HIS B N      1 
ATOM   7306 C  CA     . HIS B 1 482 ? -20.24900 -6.60800  34.31200  1.000 27.46382 ? 478 HIS B CA     1 
ATOM   7307 C  C      . HIS B 1 482 ? -19.46500 -5.59200  35.13700  1.000 31.93014 ? 478 HIS B C      1 
ATOM   7308 O  O      . HIS B 1 482 ? -19.92600 -4.47600  35.38700  1.000 29.71409 ? 478 HIS B O      1 
ATOM   7309 C  CB     . HIS B 1 482 ? -21.17400 -5.92500  33.31400  1.000 29.44564 ? 478 HIS B CB     1 
ATOM   7310 C  CG     . HIS B 1 482 ? -22.00000 -6.88100  32.51100  1.000 29.80357 ? 478 HIS B CG     1 
ATOM   7311 N  ND1    . HIS B 1 482 ? -21.85800 -7.02400  31.14600  1.000 29.10349 ? 478 HIS B ND1    1 
ATOM   7312 C  CD2    . HIS B 1 482 ? -22.96200 -7.75900  32.88200  1.000 27.86650 ? 478 HIS B CD2    1 
ATOM   7313 C  CE1    . HIS B 1 482 ? -22.70400 -7.94100  30.71000  1.000 27.58752 ? 478 HIS B CE1    1 
ATOM   7314 N  NE2    . HIS B 1 482 ? -23.38700 -8.40100  31.74100  1.000 31.71433 ? 478 HIS B NE2    1 
ATOM   7315 N  N      . GLY B 1 483 ? -18.25900 -5.98700  35.55400  1.000 32.36967 ? 479 GLY B N      1 
ATOM   7316 C  CA     . GLY B 1 483 ? -17.42700 -5.16600  36.41300  1.000 30.55366 ? 479 GLY B CA     1 
ATOM   7317 C  C      . GLY B 1 483 ? -17.17000 -3.76500  35.89100  1.000 33.49349 ? 479 GLY B C      1 
ATOM   7318 O  O      . GLY B 1 483 ? -17.41300 -2.77700  36.59500  1.000 29.25351 ? 479 GLY B O      1 
ATOM   7319 N  N      . LEU B 1 484 ? -16.65700 -3.65400  34.66400  1.000 26.92165 ? 480 LEU B N      1 
ATOM   7320 C  CA     . LEU B 1 484 ? -16.35700 -2.32700  34.13500  1.000 32.24597 ? 480 LEU B CA     1 
ATOM   7321 C  C      . LEU B 1 484 ? -17.60600 -1.46000  34.07600  1.000 34.20410 ? 480 LEU B C      1 
ATOM   7322 O  O      . LEU B 1 484 ? -17.54100 -0.25600  34.34300  1.000 34.18305 ? 480 LEU B O      1 
ATOM   7323 C  CB     . LEU B 1 484 ? -15.69900 -2.42500  32.75600  1.000 30.54050 ? 480 LEU B CB     1 
ATOM   7324 C  CG     . LEU B 1 484 ? -14.24500 -2.90300  32.74000  1.000 38.11510 ? 480 LEU B CG     1 
ATOM   7325 C  CD1    . LEU B 1 484 ? -13.62200 -2.74700  31.35300  1.000 39.20996 ? 480 LEU B CD1    1 
ATOM   7326 C  CD2    . LEU B 1 484 ? -13.40200 -2.17600  33.81300  1.000 32.67234 ? 480 LEU B CD2    1 
ATOM   7327 N  N      . VAL B 1 485 ? -18.75900 -2.05000  33.75200  1.000 31.16953 ? 481 VAL B N      1 
ATOM   7328 C  CA     . VAL B 1 485 ? -19.98400 -1.25400  33.72100  1.000 29.81673 ? 481 VAL B CA     1 
ATOM   7329 C  C      . VAL B 1 485 ? -20.39300 -0.87900  35.13600  1.000 35.79903 ? 481 VAL B C      1 
ATOM   7330 O  O      . VAL B 1 485 ? -20.78600 0.26800   35.40000  1.000 32.74866 ? 481 VAL B O      1 
ATOM   7331 C  CB     . VAL B 1 485 ? -21.11100 -2.00400  32.98600  1.000 31.24322 ? 481 VAL B CB     1 
ATOM   7332 C  CG1    . VAL B 1 485 ? -22.37300 -1.14900  32.93600  1.000 29.54828 ? 481 VAL B CG1    1 
ATOM   7333 C  CG2    . VAL B 1 485 ? -20.68200 -2.37800  31.56200  1.000 29.09559 ? 481 VAL B CG2    1 
ATOM   7334 N  N      . HIS B 1 486 ? -20.27100 -1.82800  36.07400  1.000 31.75118 ? 482 HIS B N      1 
ATOM   7335 C  CA     . HIS B 1 486 ? -20.56600 -1.54400  37.47700  1.000 36.45437 ? 482 HIS B CA     1 
ATOM   7336 C  C      . HIS B 1 486 ? -19.75300 -0.35900  37.98600  1.000 37.30974 ? 482 HIS B C      1 
ATOM   7337 O  O      . HIS B 1 486 ? -20.27600 0.52100   38.67800  1.000 34.29095 ? 482 HIS B O      1 
ATOM   7338 C  CB     . HIS B 1 486 ? -20.29600 -2.78800  38.32500  1.000 33.68299 ? 482 HIS B CB     1 
ATOM   7339 C  CG     . HIS B 1 486 ? -20.62900 -2.62200  39.77600  1.000 44.99487 ? 482 HIS B CG     1 
ATOM   7340 N  ND1    . HIS B 1 486 ? -21.92000 -2.70200  40.25800  1.000 48.13472 ? 482 HIS B ND1    1 
ATOM   7341 C  CD2    . HIS B 1 486 ? -19.83500 -2.40900  40.85700  1.000 45.69495 ? 482 HIS B CD2    1 
ATOM   7342 C  CE1    . HIS B 1 486 ? -21.90600 -2.54100  41.57100  1.000 46.31871 ? 482 HIS B CE1    1 
ATOM   7343 N  NE2    . HIS B 1 486 ? -20.65600 -2.36200  41.95900  1.000 46.76877 ? 482 HIS B NE2    1 
ATOM   7344 N  N      . LEU B 1 487 ? -18.46000 -0.32700  37.66600  1.000 37.09918 ? 483 LEU B N      1 
ATOM   7345 C  CA     . LEU B 1 487 ? -17.63900 0.79000   38.12200  1.000 38.29933 ? 483 LEU B CA     1 
ATOM   7346 C  C      . LEU B 1 487 ? -18.05500 2.08900   37.44700  1.000 39.34156 ? 483 LEU B C      1 
ATOM   7347 O  O      . LEU B 1 487 ? -18.02000 3.15500   38.06800  1.000 41.68921 ? 483 LEU B O      1 
ATOM   7348 C  CB     . LEU B 1 487 ? -16.16300 0.49400   37.87400  1.000 34.44624 ? 483 LEU B CB     1 
ATOM   7349 C  CG     . LEU B 1 487 ? -15.61300 -0.70700  38.65200  1.000 37.93086 ? 483 LEU B CG     1 
ATOM   7350 C  CD1    . LEU B 1 487 ? -14.34800 -1.24600  37.98800  1.000 36.25961 ? 483 LEU B CD1    1 
ATOM   7351 C  CD2    . LEU B 1 487 ? -15.36500 -0.33500  40.11400  1.000 37.40712 ? 483 LEU B CD2    1 
ATOM   7352 N  N      . GLY B 1 488 ? -18.44800 2.02200   36.17500  1.000 33.78826 ? 484 GLY B N      1 
ATOM   7353 C  CA     . GLY B 1 488 ? -18.95500 3.21100   35.50800  1.000 38.64148 ? 484 GLY B CA     1 
ATOM   7354 C  C      . GLY B 1 488 ? -20.20400 3.77700   36.16700  1.000 40.91017 ? 484 GLY B C      1 
ATOM   7355 O  O      . GLY B 1 488 ? -20.36300 4.99600   36.26800  1.000 42.61300 ? 484 GLY B O      1 
ATOM   7356 N  N      . GLU B 1 489 ? -21.12200 2.90200   36.60000  1.000 35.88588 ? 485 GLU B N      1 
ATOM   7357 C  CA     . GLU B 1 489 ? -22.31600 3.37200   37.30600  1.000 36.88074 ? 485 GLU B CA     1 
ATOM   7358 C  C      . GLU B 1 489 ? -21.94700 4.12200   38.58300  1.000 39.69423 ? 485 GLU B C      1 
ATOM   7359 O  O      . GLU B 1 489 ? -22.57300 5.13400   38.92200  1.000 39.55474 ? 485 GLU B O      1 
ATOM   7360 C  CB     . GLU B 1 489 ? -23.24200 2.19900   37.64100  1.000 31.52483 ? 485 GLU B CB     1 
ATOM   7361 C  CG     . GLU B 1 489 ? -23.86600 1.50100   36.44100  1.000 36.09907 ? 485 GLU B CG     1 
ATOM   7362 C  CD     . GLU B 1 489 ? -24.30000 0.07400   36.75700  1.000 47.90048 ? 485 GLU B CD     1 
ATOM   7363 O  OE1    . GLU B 1 489 ? -24.87600 -0.57900  35.86100  1.000 52.44313 ? 485 GLU B OE1    1 
ATOM   7364 O  OE2    . GLU B 1 489 ? -24.06900 -0.39300  37.89900  1.000 54.33809 ? 485 GLU B OE2    1 
ATOM   7365 N  N      . GLN B 1 490 ? -20.94500 3.62200   39.31800  1.000 37.57556 ? 486 GLN B N      1 
ATOM   7366 C  CA     . GLN B 1 490 ? -20.52900 4.26100   40.56800  1.000 43.41047 ? 486 GLN B CA     1 
ATOM   7367 C  C      . GLN B 1 490 ? -19.78200 5.56700   40.31500  1.000 43.49469 ? 486 GLN B C      1 
ATOM   7368 O  O      . GLN B 1 490 ? -20.00200 6.56500   41.01100  1.000 43.04463 ? 486 GLN B O      1 
ATOM   7369 C  CB     . GLN B 1 490 ? -19.63600 3.32000   41.37000  1.000 38.99152 ? 486 GLN B CB     1 
ATOM   7370 C  CG     . GLN B 1 490 ? -20.23700 1.98100   41.69200  1.000 49.88230 ? 486 GLN B CG     1 
ATOM   7371 C  CD     . GLN B 1 490 ? -19.25600 1.08700   42.42800  1.000 61.48369 ? 486 GLN B CD     1 
ATOM   7372 O  OE1    . GLN B 1 490 ? -18.06400 1.06300   42.11400  1.000 61.66529 ? 486 GLN B OE1    1 
ATOM   7373 N  NE2    . GLN B 1 490 ? -19.75000 0.35900   43.42700  1.000 65.97107 ? 486 GLN B NE2    1 
ATOM   7374 N  N      . HIS B 1 491 ? -18.86100 5.54300   39.39300  1.000 40.19692 ? 487 HIS B N      1 
ATOM   7375 C  CA     . HIS B 1 491 ? -18.01500 6.66400   39.14300  1.000 43.83947 ? 487 HIS B CA     1 
ATOM   7376 C  C      . HIS B 1 491 ? -18.51300 7.68800   38.18600  1.000 48.15841 ? 487 HIS B C      1 
ATOM   7377 O  O      . HIS B 1 491 ? -17.98300 8.75700   38.14400  1.000 51.50618 ? 487 HIS B O      1 
ATOM   7378 C  CB     . HIS B 1 491 ? -16.65300 6.18100   38.69800  1.000 41.21020 ? 487 HIS B CB     1 
ATOM   7379 C  CG     . HIS B 1 491 ? -15.81800 5.64600   39.81300  1.000 54.79078 ? 487 HIS B CG     1 
ATOM   7380 N  ND1    . HIS B 1 491 ? -15.95300 4.37000   40.30000  1.000 54.53022 ? 487 HIS B ND1    1 
ATOM   7381 C  CD2    . HIS B 1 491 ? -14.83500 6.22200   40.54000  1.000 54.93290 ? 487 HIS B CD2    1 
ATOM   7382 C  CE1    . HIS B 1 491 ? -15.08400 4.18100   41.26900  1.000 57.92537 ? 487 HIS B CE1    1 
ATOM   7383 N  NE2    . HIS B 1 491 ? -14.39600 5.29000   41.43400  1.000 55.63562 ? 487 HIS B NE2    1 
ATOM   7384 N  N      . GLN B 1 492 ? -19.51700 7.37400   37.40600  1.000 41.82870 ? 488 GLN B N      1 
ATOM   7385 C  CA     . GLN B 1 492 ? -19.99800 8.35600   36.48700  1.000 43.32625 ? 488 GLN B CA     1 
ATOM   7386 C  C      . GLN B 1 492 ? -21.44200 8.64600   36.65700  1.000 43.39731 ? 488 GLN B C      1 
ATOM   7387 O  O      . GLN B 1 492 ? -21.88300 9.67200   36.28400  1.000 51.13771 ? 488 GLN B O      1 
ATOM   7388 C  CB     . GLN B 1 492 ? -19.72800 7.94300   35.06500  1.000 41.27863 ? 488 GLN B CB     1 
ATOM   7389 C  CG     . GLN B 1 492 ? -18.28000 7.94100   34.70600  1.000 44.90538 ? 488 GLN B CG     1 
ATOM   7390 C  CD     . GLN B 1 492 ? -18.07200 7.70100   33.25100  1.000 57.61480 ? 488 GLN B CD     1 
ATOM   7391 O  OE1    . GLN B 1 492 ? -17.95200 6.59400   32.83600  1.000 59.92824 ? 488 GLN B OE1    1 
ATOM   7392 N  NE2    . GLN B 1 492 ? -18.06200 8.74500   32.47800  1.000 62.11271 ? 488 GLN B NE2    1 
ATOM   7393 N  N      . PHE B 1 493 ? -22.18100 7.73900   37.22700  1.000 40.93649 ? 489 PHE B N      1 
ATOM   7394 C  CA     . PHE B 1 493 ? -23.59200 7.95600   37.38700  1.000 42.21032 ? 489 PHE B CA     1 
ATOM   7395 C  C      . PHE B 1 493 ? -24.04200 7.90400   38.84800  1.000 44.84748 ? 489 PHE B C      1 
ATOM   7396 O  O      . PHE B 1 493 ? -25.17600 7.63800   39.12400  1.000 44.32374 ? 489 PHE B O      1 
ATOM   7397 C  CB     . PHE B 1 493 ? -24.40100 6.98300   36.51300  1.000 40.71804 ? 489 PHE B CB     1 
ATOM   7398 C  CG     . PHE B 1 493 ? -24.20000 7.16100   35.04300  1.000 42.54457 ? 489 PHE B CG     1 
ATOM   7399 C  CD1    . PHE B 1 493 ? -23.14800 6.58100   34.41100  1.000 38.53357 ? 489 PHE B CD1    1 
ATOM   7400 C  CD2    . PHE B 1 493 ? -25.05800 7.90600   34.31000  1.000 39.97058 ? 489 PHE B CD2    1 
ATOM   7401 C  CE1    . PHE B 1 493 ? -22.94400 6.75000   33.07700  1.000 39.15469 ? 489 PHE B CE1    1 
ATOM   7402 C  CE2    . PHE B 1 493 ? -24.87400 8.06200   32.97100  1.000 41.96293 ? 489 PHE B CE2    1 
ATOM   7403 C  CZ     . PHE B 1 493 ? -23.81400 7.48600   32.34800  1.000 40.34431 ? 489 PHE B CZ     1 
ATOM   7404 N  N      . ASP B 1 494 ? -23.11800 8.10600   39.77300  1.000 42.79197 ? 490 ASP B N      1 
ATOM   7405 C  CA     . ASP B 1 494 ? -23.40400 8.15600   41.19900  1.000 48.43475 ? 490 ASP B CA     1 
ATOM   7406 C  C      . ASP B 1 494 ? -24.23100 7.01900   41.77700  1.000 47.53991 ? 490 ASP B C      1 
ATOM   7407 O  O      . ASP B 1 494 ? -25.07300 7.24700   42.59500  1.000 42.97357 ? 490 ASP B O      1 
ATOM   7408 C  CB     . ASP B 1 494 ? -24.12200 9.48300   41.53000  1.000 59.73874 ? 490 ASP B CB     1 
ATOM   7409 C  CG     . ASP B 1 494 ? -23.19300 10.67100  41.55500  1.000 72.33499 ? 490 ASP B CG     1 
ATOM   7410 O  OD1    . ASP B 1 494 ? -22.38700 10.77700  42.48400  1.000 73.98782 ? 490 ASP B OD1    1 
ATOM   7411 O  OD2    . ASP B 1 494 ? -23.26800 11.52500  40.66400  1.000 76.83553 ? 490 ASP B OD2    1 
ATOM   7412 N  N      . SER B 1 495 ? -24.02300 5.80000   41.30400  1.000 46.44504 ? 491 SER B N      1 
ATOM   7413 C  CA     . SER B 1 495 ? -24.77000 4.62100   41.70600  1.000 46.63191 ? 491 SER B CA     1 
ATOM   7414 C  C      . SER B 1 495 ? -26.28900 4.71100   41.60300  1.000 46.05552 ? 491 SER B C      1 
ATOM   7415 O  O      . SER B 1 495 ? -26.97300 4.05400   42.32700  1.000 43.71314 ? 491 SER B O      1 
ATOM   7416 C  CB     . SER B 1 495 ? -24.36400 4.15700   43.09700  1.000 43.18413 ? 491 SER B CB     1 
ATOM   7417 O  OG     . SER B 1 495 ? -23.02400 4.41200   43.31000  1.000 43.48679 ? 491 SER B OG     1 
ATOM   7418 N  N      . LYS B 1 496 ? -26.79900 5.46400   40.64500  1.000 44.05265 ? 492 LYS B N      1 
ATOM   7419 C  CA     . LYS B 1 496 ? -28.20400 5.67100   40.47500  1.000 43.43416 ? 492 LYS B CA     1 
ATOM   7420 C  C      . LYS B 1 496 ? -28.96400 4.48900   39.96300  1.000 43.00252 ? 492 LYS B C      1 
ATOM   7421 O  O      . LYS B 1 496 ? -30.13800 4.45700   40.11800  1.000 41.86291 ? 492 LYS B O      1 
ATOM   7422 C  CB     . LYS B 1 496 ? -28.44300 6.79600   39.51300  1.000 44.92644 ? 492 LYS B CB     1 
ATOM   7423 C  CG     . LYS B 1 496 ? -28.53700 8.13600   40.15700  1.000 54.20913 ? 492 LYS B CG     1 
ATOM   7424 C  CD     . LYS B 1 496 ? -28.86000 9.18700   39.13100  1.000 55.38296 ? 492 LYS B CD     1 
ATOM   7425 C  CE     . LYS B 1 496 ? -27.93700 9.07300   37.95300  1.000 48.83217 ? 492 LYS B CE     1 
ATOM   7426 N  NZ     . LYS B 1 496 ? -28.05600 10.27200  37.13300  1.000 52.91424 ? 492 LYS B NZ     1 
ATOM   7427 N  N      . PHE B 1 497 ? -28.29100 3.55600   39.32400  1.000 39.28366 ? 493 PHE B N      1 
ATOM   7428 C  CA     . PHE B 1 497 ? -28.92700 2.37400   38.78700  1.000 39.52579 ? 493 PHE B CA     1 
ATOM   7429 C  C      . PHE B 1 497 ? -27.90800 1.27800   38.62400  1.000 41.78659 ? 493 PHE B C      1 
ATOM   7430 O  O      . PHE B 1 497 ? -26.74100 1.53300   38.57400  1.000 35.67007 ? 493 PHE B O      1 
ATOM   7431 C  CB     . PHE B 1 497 ? -29.58700 2.67600   37.45000  1.000 33.25925 ? 493 PHE B CB     1 
ATOM   7432 C  CG     . PHE B 1 497 ? -28.66600 3.25800   36.45500  1.000 32.58812 ? 493 PHE B CG     1 
ATOM   7433 C  CD1    . PHE B 1 497 ? -27.86300 2.46400   35.71100  1.000 32.05384 ? 493 PHE B CD1    1 
ATOM   7434 C  CD2    . PHE B 1 497 ? -28.59100 4.59500   36.29500  1.000 31.11162 ? 493 PHE B CD2    1 
ATOM   7435 C  CE1    . PHE B 1 497 ? -27.00600 2.99700   34.80000  1.000 36.09643 ? 493 PHE B CE1    1 
ATOM   7436 C  CE2    . PHE B 1 497 ? -27.74900 5.14700   35.38300  1.000 35.68849 ? 493 PHE B CE2    1 
ATOM   7437 C  CZ     . PHE B 1 497 ? -26.95400 4.34800   34.62400  1.000 34.05671 ? 493 PHE B CZ     1 
ATOM   7438 N  N      . ASP B 1 498 ? -28.38100 0.05900   38.56700  1.000 37.26499 ? 494 ASP B N      1 
ATOM   7439 C  CA     . ASP B 1 498 ? -27.52800 -1.07500  38.39200  1.000 37.90454 ? 494 ASP B CA     1 
ATOM   7440 C  C      . ASP B 1 498 ? -28.07700 -1.93800  37.29800  1.000 39.09679 ? 494 ASP B C      1 
ATOM   7441 O  O      . ASP B 1 498 ? -29.14300 -2.45900  37.40400  1.000 42.39192 ? 494 ASP B O      1 
ATOM   7442 C  CB     . ASP B 1 498 ? -27.39100 -1.91400  39.66400  1.000 39.67581 ? 494 ASP B CB     1 
ATOM   7443 C  CG     . ASP B 1 498 ? -26.50500 -3.15300  39.46300  1.000 51.61672 ? 494 ASP B CG     1 
ATOM   7444 O  OD1    . ASP B 1 498 ? -26.73200 -3.93000  38.54600  1.000 47.40568 ? 494 ASP B OD1    1 
ATOM   7445 O  OD2    . ASP B 1 498 ? -25.56500 -3.35200  40.21800  1.000 55.56719 ? 494 ASP B OD2    1 
ATOM   7446 N  N      . ILE B 1 499 ? -27.34000 -2.04000  36.22400  1.000 38.23353 ? 495 ILE B N      1 
ATOM   7447 C  CA     . ILE B 1 499 ? -27.70100 -2.91600  35.14300  1.000 38.29670 ? 495 ILE B CA     1 
ATOM   7448 C  C      . ILE B 1 499 ? -26.47900 -3.75200  34.84000  1.000 39.43894 ? 495 ILE B C      1 
ATOM   7449 O  O      . ILE B 1 499 ? -26.23700 -4.10000  33.71400  1.000 42.95778 ? 495 ILE B O      1 
ATOM   7450 C  CB     . ILE B 1 499 ? -28.10600 -2.11700  33.90100  1.000 36.15170 ? 495 ILE B CB     1 
ATOM   7451 C  CG1    . ILE B 1 499 ? -28.55400 -3.02700  32.78200  1.000 34.26200 ? 495 ILE B CG1    1 
ATOM   7452 C  CG2    . ILE B 1 499 ? -26.94200 -1.33100  33.38100  1.000 36.71756 ? 495 ILE B CG2    1 
ATOM   7453 C  CD1    . ILE B 1 499 ? -29.93400 -3.55400  32.88700  1.000 29.37984 ? 495 ILE B CD1    1 
ATOM   7454 N  N      . SER B 1 500 ? -25.70600 -4.06200  35.85500  1.000 37.76505 ? 496 SER B N      1 
ATOM   7455 C  CA     . SER B 1 500 ? -24.47600 -4.77700  35.70300  1.000 32.68287 ? 496 SER B CA     1 
ATOM   7456 C  C      . SER B 1 500 ? -24.26600 -5.97500  36.57300  1.000 36.04643 ? 496 SER B C      1 
ATOM   7457 O  O      . SER B 1 500 ? -23.51800 -6.81000  36.22500  1.000 41.13914 ? 496 SER B O      1 
ATOM   7458 C  CB     . SER B 1 500 ? -23.34100 -3.83200  35.94600  1.000 31.31428 ? 496 SER B CB     1 
ATOM   7459 O  OG     . SER B 1 500 ? -23.40400 -3.34800  37.23800  1.000 40.57329 ? 496 SER B OG     1 
ATOM   7460 N  N      . SER B 1 501 ? -24.90300 -6.03800  37.71400  1.000 31.46167 ? 497 SER B N      1 
ATOM   7461 C  CA     . SER B 1 501 ? -24.72200 -7.15300  38.59300  1.000 40.14166 ? 497 SER B CA     1 
ATOM   7462 C  C      . SER B 1 501 ? -25.74400 -8.23000  38.43600  1.000 36.60176 ? 497 SER B C      1 
ATOM   7463 O  O      . SER B 1 501 ? -26.88400 -7.96300  38.37200  1.000 40.18113 ? 497 SER B O      1 
ATOM   7464 C  CB     . SER B 1 501 ? -24.75200 -6.71500  40.04300  1.000 39.12574 ? 497 SER B CB     1 
ATOM   7465 O  OG     . SER B 1 501 ? -24.10800 -5.50800  40.22500  1.000 49.43224 ? 497 SER B OG     1 
ATOM   7466 N  N      . PHE B 1 502 ? -25.31200 -9.45500  38.37000  1.000 28.94821 ? 498 PHE B N      1 
ATOM   7467 C  CA     . PHE B 1 502 ? -26.23600 -10.53600 38.31200  1.000 33.48033 ? 498 PHE B CA     1 
ATOM   7468 C  C      . PHE B 1 502 ? -26.83800 -10.73500 39.70500  1.000 34.55151 ? 498 PHE B C      1 
ATOM   7469 O  O      . PHE B 1 502 ? -26.22400 -10.48300 40.68500  1.000 34.13304 ? 498 PHE B O      1 
ATOM   7470 C  CB     . PHE B 1 502 ? -25.55300 -11.82800 37.88900  1.000 28.37972 ? 498 PHE B CB     1 
ATOM   7471 C  CG     . PHE B 1 502 ? -24.94500 -11.79300 36.52800  1.000 31.70380 ? 498 PHE B CG     1 
ATOM   7472 C  CD1    . PHE B 1 502 ? -25.53100 -11.10100 35.50600  1.000 31.67485 ? 498 PHE B CD1    1 
ATOM   7473 C  CD2    . PHE B 1 502 ? -23.80400 -12.47800 36.27100  1.000 29.88253 ? 498 PHE B CD2    1 
ATOM   7474 C  CE1    . PHE B 1 502 ? -24.96600 -11.07700 34.25700  1.000 31.28007 ? 498 PHE B CE1    1 
ATOM   7475 C  CE2    . PHE B 1 502 ? -23.23800 -12.46800 35.03500  1.000 30.38522 ? 498 PHE B CE2    1 
ATOM   7476 C  CZ     . PHE B 1 502 ? -23.82400 -11.76400 34.02400  1.000 31.28270 ? 498 PHE B CZ     1 
ATOM   7477 N  N      . ARG B 1 503 ? -28.06100 -11.20400 39.75500  1.000 33.99355 ? 499 ARG B N      1 
ATOM   7478 C  CA     . ARG B 1 503 ? -28.70400 -11.51700 40.98500  1.000 37.08076 ? 499 ARG B CA     1 
ATOM   7479 C  C      . ARG B 1 503 ? -28.13000 -12.84100 41.46000  1.000 39.85478 ? 499 ARG B C      1 
ATOM   7480 O  O      . ARG B 1 503 ? -27.97100 -13.05200 42.62400  1.000 35.76481 ? 499 ARG B O      1 
ATOM   7481 C  CB     . ARG B 1 503 ? -30.22400 -11.43200 40.88200  1.000 45.27385 ? 499 ARG B CB     1 
ATOM   7482 C  CG     . ARG B 1 503 ? -30.98100 -12.68800 40.57800  1.000 60.27565 ? 499 ARG B CG     1 
ATOM   7483 C  CD     . ARG B 1 503 ? -32.46900 -12.62100 40.99200  1.000 65.36573 ? 499 ARG B CD     1 
ATOM   7484 N  NE     . ARG B 1 503 ? -33.18000 -13.85300 40.65500  1.000 74.13784 ? 499 ARG B NE     1 
ATOM   7485 C  CZ     . ARG B 1 503 ? -32.70400 -15.05700 40.92500  1.000 77.73827 ? 499 ARG B CZ     1 
ATOM   7486 N  NH1    . ARG B 1 503 ? -31.56000 -15.17400 41.55100  1.000 82.17038 ? 499 ARG B NH1    1 
ATOM   7487 N  NH2    . ARG B 1 503 ? -33.36000 -16.14800 40.60300  1.000 74.67474 ? 499 ARG B NH2    1 
ATOM   7488 N  N      . LYS B 1 504 ? -27.78100 -13.71000 40.54000  1.000 31.92225 ? 500 LYS B N      1 
ATOM   7489 C  CA     . LYS B 1 504 ? -27.14100 -14.92800 40.90800  1.000 32.01436 ? 500 LYS B CA     1 
ATOM   7490 C  C      . LYS B 1 504 ? -25.99200 -15.21900 39.96500  1.000 33.69878 ? 500 LYS B C      1 
ATOM   7491 O  O      . LYS B 1 504 ? -26.17200 -15.38600 38.80600  1.000 36.93338 ? 500 LYS B O      1 
ATOM   7492 C  CB     . LYS B 1 504 ? -28.08600 -16.09800 40.95900  1.000 32.27492 ? 500 LYS B CB     1 
ATOM   7493 C  CG     . LYS B 1 504 ? -27.39500 -17.34300 41.44400  1.000 51.45091 ? 500 LYS B CG     1 
ATOM   7494 C  CD     . LYS B 1 504 ? -27.95200 -18.63200 40.86200  1.000 63.29969 ? 500 LYS B CD     1 
ATOM   7495 C  CE     . LYS B 1 504 ? -26.90300 -19.57900 40.22000  1.000 67.10278 ? 500 LYS B CE     1 
ATOM   7496 N  NZ     . LYS B 1 504 ? -26.69600 -19.44000 38.74000  1.000 59.69926 ? 500 LYS B NZ     1 
ATOM   7497 N  N      . SER B 1 505 ? -24.80000 -15.31700 40.50700  1.000 32.70392 ? 501 SER B N      1 
ATOM   7498 C  CA     . SER B 1 505 ? -23.60200 -15.64800 39.78000  1.000 36.10959 ? 501 SER B CA     1 
ATOM   7499 C  C      . SER B 1 505 ? -23.68500 -16.96200 39.06600  1.000 31.42219 ? 501 SER B C      1 
ATOM   7500 O  O      . SER B 1 505 ? -24.27500 -17.86400 39.50900  1.000 34.21463 ? 501 SER B O      1 
ATOM   7501 C  CB     . SER B 1 505 ? -22.46100 -15.83800 40.75300  1.000 38.79939 ? 501 SER B CB     1 
ATOM   7502 O  OG     . SER B 1 505 ? -21.68500 -14.71800 40.84100  1.000 55.34085 ? 501 SER B OG     1 
ATOM   7503 N  N      . ILE B 1 506 ? -23.01200 -17.07800 37.96700  1.000 33.84090 ? 502 ILE B N      1 
ATOM   7504 C  CA     . ILE B 1 506 ? -22.97500 -18.31100 37.25300  1.000 30.14046 ? 502 ILE B CA     1 
ATOM   7505 C  C      . ILE B 1 506 ? -21.91800 -19.23600 37.83600  1.000 32.42494 ? 502 ILE B C      1 
ATOM   7506 O  O      . ILE B 1 506 ? -20.86400 -18.80400 38.16600  1.000 30.55103 ? 502 ILE B O      1 
ATOM   7507 C  CB     . ILE B 1 506 ? -22.68200 -18.03200 35.77500  1.000 34.29885 ? 502 ILE B CB     1 
ATOM   7508 C  CG1    . ILE B 1 506 ? -23.87100 -17.33200 35.14500  1.000 35.01209 ? 502 ILE B CG1    1 
ATOM   7509 C  CG2    . ILE B 1 506 ? -22.38400 -19.28000 35.00000  1.000 26.86375 ? 502 ILE B CG2    1 
ATOM   7510 C  CD1    . ILE B 1 506 ? -23.67400 -16.91000 33.73800  1.000 35.24107 ? 502 ILE B CD1    1 
ATOM   7511 N  N      . ASP B 1 507 ? -22.25000 -20.49900 37.98000  1.000 30.11940 ? 503 ASP B N      1 
ATOM   7512 C  CA     . ASP B 1 507 ? -21.35000 -21.51500 38.44100  1.000 25.96627 ? 503 ASP B CA     1 
ATOM   7513 C  C      . ASP B 1 507 ? -20.64800 -22.12900 37.26800  1.000 31.16953 ? 503 ASP B C      1 
ATOM   7514 O  O      . ASP B 1 507 ? -21.13800 -23.02300 36.65800  1.000 33.08818 ? 503 ASP B O      1 
ATOM   7515 C  CB     . ASP B 1 507 ? -22.12500 -22.58400 39.17300  1.000 28.97979 ? 503 ASP B CB     1 
ATOM   7516 C  CG     . ASP B 1 507 ? -21.23700 -23.62000 39.81400  1.000 34.41202 ? 503 ASP B CG     1 
ATOM   7517 O  OD1    . ASP B 1 507 ? -20.05700 -23.67700 39.57000  1.000 41.09440 ? 503 ASP B OD1    1 
ATOM   7518 O  OD2    . ASP B 1 507 ? -21.73500 -24.38300 40.58000  1.000 39.43368 ? 503 ASP B OD2    1 
ATOM   7519 N  N      . PHE B 1 508 ? -19.47200 -21.64000 36.97700  1.000 32.99606 ? 504 PHE B N      1 
ATOM   7520 C  CA     . PHE B 1 508 ? -18.72600 -22.11300 35.84600  1.000 31.19585 ? 504 PHE B CA     1 
ATOM   7521 C  C      . PHE B 1 508 ? -18.20400 -23.52400 35.97800  1.000 35.42004 ? 504 PHE B C      1 
ATOM   7522 O  O      . PHE B 1 508 ? -18.02500 -24.18300 35.01100  1.000 34.11988 ? 504 PHE B O      1 
ATOM   7523 C  CB     . PHE B 1 508 ? -17.68700 -21.09400 35.43300  1.000 28.82977 ? 504 PHE B CB     1 
ATOM   7524 C  CG     . PHE B 1 508 ? -18.27800 -19.78800 35.00000  1.000 30.18257 ? 504 PHE B CG     1 
ATOM   7525 C  CD1    . PHE B 1 508 ? -18.77700 -19.63400 33.73700  1.000 28.57711 ? 504 PHE B CD1    1 
ATOM   7526 C  CD2    . PHE B 1 508 ? -18.37100 -18.74400 35.86900  1.000 28.84556 ? 504 PHE B CD2    1 
ATOM   7527 C  CE1    . PHE B 1 508 ? -19.34000 -18.46800 33.35800  1.000 32.68550 ? 504 PHE B CE1    1 
ATOM   7528 C  CE2    . PHE B 1 508 ? -18.93400 -17.57500 35.49300  1.000 28.09811 ? 504 PHE B CE2    1 
ATOM   7529 C  CZ     . PHE B 1 508 ? -19.42000 -17.43700 34.22100  1.000 30.04834 ? 504 PHE B CZ     1 
ATOM   7530 N  N      . CYS B 1 509 ? -17.97700 -23.97700 37.19600  1.000 30.97740 ? 505 CYS B N      1 
ATOM   7531 C  CA     . CYS B 1 509 ? -17.53700 -25.32200 37.38300  1.000 35.31476 ? 505 CYS B CA     1 
ATOM   7532 C  C      . CYS B 1 509 ? -18.56700 -26.28900 36.87300  1.000 38.92835 ? 505 CYS B C      1 
ATOM   7533 O  O      . CYS B 1 509 ? -18.26100 -27.18000 36.16600  1.000 38.44671 ? 505 CYS B O      1 
ATOM   7534 C  CB     . CYS B 1 509 ? -17.23500 -25.60100 38.83400  1.000 38.95730 ? 505 CYS B CB     1 
ATOM   7535 S  SG     . CYS B 1 509 ? -15.76500 -24.79800 39.36000  1.000 44.40269 ? 505 CYS B SG     1 
ATOM   7536 N  N      . LYS B 1 510 ? -19.80300 -26.09200 37.26400  1.000 35.50426 ? 506 LYS B N      1 
ATOM   7537 C  CA     . LYS B 1 510 ? -20.85200 -26.92900 36.78500  1.000 36.13854 ? 506 LYS B CA     1 
ATOM   7538 C  C      . LYS B 1 510 ? -21.04100 -26.79200 35.27100  1.000 27.14273 ? 506 LYS B C      1 
ATOM   7539 O  O      . LYS B 1 510 ? -21.30300 -27.73100 34.62800  1.000 31.55115 ? 506 LYS B O      1 
ATOM   7540 C  CB     . LYS B 1 510 ? -22.14200 -26.61600 37.49500  1.000 42.45509 ? 506 LYS B CB     1 
ATOM   7541 C  CG     . LYS B 1 510 ? -22.18600 -27.09400 38.90200  1.000 56.51730 ? 506 LYS B CG     1 
ATOM   7542 C  CD     . LYS B 1 510 ? -23.04000 -28.34100 39.02000  1.000 65.56839 ? 506 LYS B CD     1 
ATOM   7543 C  CE     . LYS B 1 510 ? -22.33400 -29.37500 39.86800  1.000 67.14489 ? 506 LYS B CE     1 
ATOM   7544 N  NZ     . LYS B 1 510 ? -22.39800 -30.73900 39.32700  1.000 68.28713 ? 506 LYS B NZ     1 
ATOM   7545 N  N      . MET B 1 511 ? -20.91800 -25.58500 34.75200  1.000 30.81685 ? 507 MET B N      1 
ATOM   7546 C  CA     . MET B 1 511 ? -21.02700 -25.33900 33.33000  1.000 31.02740 ? 507 MET B CA     1 
ATOM   7547 C  C      . MET B 1 511 ? -19.93000 -26.09900 32.60600  1.000 32.30387 ? 507 MET B C      1 
ATOM   7548 O  O      . MET B 1 511 ? -20.18500 -26.72200 31.63900  1.000 30.91423 ? 507 MET B O      1 
ATOM   7549 C  CB     . MET B 1 511 ? -21.02400 -23.85700 32.99300  1.000 28.79556 ? 507 MET B CB     1 
ATOM   7550 C  CG     . MET B 1 511 ? -21.29100 -23.50200 31.53000  1.000 42.64722 ? 507 MET B CG     1 
ATOM   7551 S  SD     . MET B 1 511 ? -20.84600 -21.80800 31.14600  1.000 50.92453 ? 507 MET B SD     1 
ATOM   7552 C  CE     . MET B 1 511 ? -20.26700 -21.88700 29.47400  1.000 59.32027 ? 507 MET B CE     1 
ATOM   7553 N  N      . ALA B 1 512 ? -18.72100 -26.07500 33.11800  1.000 31.96436 ? 508 ALA B N      1 
ATOM   7554 C  CA     . ALA B 1 512 ? -17.65000 -26.81700 32.50300  1.000 30.58788 ? 508 ALA B CA     1 
ATOM   7555 C  C      . ALA B 1 512 ? -17.95000 -28.29900 32.51400  1.000 33.30399 ? 508 ALA B C      1 
ATOM   7556 O  O      . ALA B 1 512 ? -17.79600 -28.96000 31.55300  1.000 29.66408 ? 508 ALA B O      1 
ATOM   7557 C  CB     . ALA B 1 512 ? -16.34400 -26.54100 33.18200  1.000 27.90598 ? 508 ALA B CB     1 
ATOM   7558 N  N      . GLU B 1 513 ? -18.44000 -28.78600 33.63800  1.000 33.44348 ? 509 GLU B N      1 
ATOM   7559 C  CA     . GLU B 1 513 ? -18.79300 -30.17500 33.80700  1.000 37.24920 ? 509 GLU B CA     1 
ATOM   7560 C  C      . GLU B 1 513 ? -19.81700 -30.61900 32.79700  1.000 36.84126 ? 509 GLU B C      1 
ATOM   7561 O  O      . GLU B 1 513 ? -19.68000 -31.62700 32.19700  1.000 34.81996 ? 509 GLU B O      1 
ATOM   7562 C  CB     . GLU B 1 513 ? -19.30600 -30.42000 35.19800  1.000 34.44624 ? 509 GLU B CB     1 
ATOM   7563 C  CG     . GLU B 1 513 ? -19.61600 -31.85400 35.46600  1.000 45.23437 ? 509 GLU B CG     1 
ATOM   7564 C  CD     . GLU B 1 513 ? -20.20800 -32.09200 36.84200  1.000 52.80633 ? 509 GLU B CD     1 
ATOM   7565 O  OE1    . GLU B 1 513 ? -20.84100 -33.10800 37.01600  1.000 56.49888 ? 509 GLU B OE1    1 
ATOM   7566 O  OE2    . GLU B 1 513 ? -20.05500 -31.27400 37.74200  1.000 55.59614 ? 509 GLU B OE2    1 
ATOM   7567 N  N      . SER B 1 514 ? -20.81800 -29.79600 32.56200  1.000 31.53536 ? 510 SER B N      1 
ATOM   7568 C  CA     . SER B 1 514 ? -21.82900 -30.07000 31.58900  1.000 28.05073 ? 510 SER B CA     1 
ATOM   7569 C  C      . SER B 1 514 ? -21.30400 -30.16700 30.16000  1.000 30.59577 ? 510 SER B C      1 
ATOM   7570 O  O      . SER B 1 514 ? -21.87600 -30.84500 29.40000  1.000 30.52998 ? 510 SER B O      1 
ATOM   7571 C  CB     . SER B 1 514 ? -22.95100 -29.05700 31.69700  1.000 26.59266 ? 510 SER B CB     1 
ATOM   7572 O  OG     . SER B 1 514 ? -22.74200 -27.95900 30.88000  1.000 31.59326 ? 510 SER B OG     1 
ATOM   7573 N  N      . LEU B 1 515 ? -20.22600 -29.47200 29.83800  1.000 25.40831 ? 511 LEU B N      1 
ATOM   7574 C  CA     . LEU B 1 515 ? -19.60300 -29.48500 28.55500  1.000 31.50378 ? 511 LEU B CA     1 
ATOM   7575 C  C      . LEU B 1 515 ? -18.43500 -30.45500 28.45900  1.000 34.50677 ? 511 LEU B C      1 
ATOM   7576 O  O      . LEU B 1 515 ? -17.77300 -30.48600 27.49100  1.000 32.38809 ? 511 LEU B O      1 
ATOM   7577 C  CB     . LEU B 1 515 ? -19.17500 -28.07900 28.17900  1.000 29.70093 ? 511 LEU B CB     1 
ATOM   7578 C  CG     . LEU B 1 515 ? -20.26000 -27.01600 28.18400  1.000 32.14859 ? 511 LEU B CG     1 
ATOM   7579 C  CD1    . LEU B 1 515 ? -19.80200 -25.65300 27.75900  1.000 25.06880 ? 511 LEU B CD1    1 
ATOM   7580 C  CD2    . LEU B 1 515 ? -21.45500 -27.45900 27.40700  1.000 30.64578 ? 511 LEU B CD2    1 
ATOM   7581 N  N      . GLY B 1 516 ? -18.21100 -31.24800 29.49300  1.000 30.55893 ? 512 GLY B N      1 
ATOM   7582 C  CA     . GLY B 1 516 ? -17.15000 -32.22200 29.52100  1.000 30.40365 ? 512 GLY B CA     1 
ATOM   7583 C  C      . GLY B 1 516 ? -15.75500 -31.69100 29.70000  1.000 39.04942 ? 512 GLY B C      1 
ATOM   7584 O  O      . GLY B 1 516 ? -14.85700 -32.21300 29.14700  1.000 42.90778 ? 512 GLY B O      1 
ATOM   7585 N  N      . VAL B 1 517 ? -15.59800 -30.66200 30.49600  1.000 32.71182 ? 513 VAL B N      1 
ATOM   7586 C  CA     . VAL B 1 517 ? -14.33500 -30.04900 30.71500  1.000 30.10624 ? 513 VAL B CA     1 
ATOM   7587 C  C      . VAL B 1 517 ? -14.08300 -29.96900 32.19400  1.000 35.40951 ? 513 VAL B C      1 
ATOM   7588 O  O      . VAL B 1 517 ? -14.89000 -29.46700 32.90900  1.000 31.40377 ? 513 VAL B O      1 
ATOM   7589 C  CB     . VAL B 1 517 ? -14.32700 -28.62000 30.17700  1.000 32.76445 ? 513 VAL B CB     1 
ATOM   7590 C  CG1    . VAL B 1 517 ? -13.09300 -27.88500 30.61700  1.000 30.98793 ? 513 VAL B CG1    1 
ATOM   7591 C  CG2    . VAL B 1 517 ? -14.48200 -28.61000 28.67900  1.000 32.71182 ? 513 VAL B CG2    1 
ATOM   7592 N  N      . LYS B 1 518 ? -12.92100 -30.43800 32.61800  1.000 35.52268 ? 514 LYS B N      1 
ATOM   7593 C  CA     . LYS B 1 518 ? -12.52900 -30.41500 34.01200  1.000 33.39085 ? 514 LYS B CA     1 
ATOM   7594 C  C      . LYS B 1 518 ? -12.41600 -29.00400 34.53800  1.000 35.36740 ? 514 LYS B C      1 
ATOM   7595 O  O      . LYS B 1 518 ? -11.94700 -28.15100 33.85100  1.000 35.28055 ? 514 LYS B O      1 
ATOM   7596 C  CB     . LYS B 1 518 ? -11.21400 -31.14700 34.19600  1.000 41.35759 ? 514 LYS B CB     1 
ATOM   7597 C  CG     . LYS B 1 518 ? -10.74400 -31.24100 35.63800  1.000 44.89749 ? 514 LYS B CG     1 
ATOM   7598 C  CD     . LYS B 1 518 ? -9.68200  -32.27700 35.81700  1.000 51.87201 ? 514 LYS B CD     1 
ATOM   7599 C  CE     . LYS B 1 518 ? -9.17800  -32.30300 37.24200  1.000 59.24131 ? 514 LYS B CE     1 
ATOM   7600 N  NZ     . LYS B 1 518 ? -10.21800 -32.53500 38.26100  1.000 63.86292 ? 514 LYS B NZ     1 
ATOM   7601 N  N      . SER B 1 519 ? -12.83500 -28.78400 35.76400  1.000 31.53536 ? 515 SER B N      1 
ATOM   7602 C  CA     . SER B 1 519 ? -12.78700 -27.49200 36.37100  1.000 35.75429 ? 515 SER B CA     1 
ATOM   7603 C  C      . SER B 1 519 ? -12.40500 -27.41800 37.83600  1.000 37.92823 ? 515 SER B C      1 
ATOM   7604 O  O      . SER B 1 519 ? -12.47700 -28.36900 38.51900  1.000 34.21726 ? 515 SER B O      1 
ATOM   7605 C  CB     . SER B 1 519 ? -14.13200 -26.83500 36.22300  1.000 39.73371 ? 515 SER B CB     1 
ATOM   7606 O  OG     . SER B 1 519 ? -15.13100 -27.63500 36.75800  1.000 44.50797 ? 515 SER B OG     1 
ATOM   7607 N  N      . TYR B 1 520 ? -12.02500 -26.23700 38.27400  1.000 36.77020 ? 516 TYR B N      1 
ATOM   7608 C  CA     . TYR B 1 520 ? -11.66100 -25.95400 39.63100  1.000 35.03052 ? 516 TYR B CA     1 
ATOM   7609 C  C      . TYR B 1 520 ? -12.26800 -24.64400 40.05700  1.000 35.60953 ? 516 TYR B C      1 
ATOM   7610 O  O      . TYR B 1 520 ? -12.38000 -23.75500 39.29700  1.000 35.34371 ? 516 TYR B O      1 
ATOM   7611 C  CB     . TYR B 1 520 ? -10.15000 -25.81000 39.78900  1.000 41.79185 ? 516 TYR B CB     1 
ATOM   7612 C  CG     . TYR B 1 520 ? -9.26300  -26.97600 39.44700  1.000 39.15733 ? 516 TYR B CG     1 
ATOM   7613 C  CD1    . TYR B 1 520 ? -9.01100  -27.94700 40.35200  1.000 45.86076 ? 516 TYR B CD1    1 
ATOM   7614 C  CD2    . TYR B 1 520 ? -8.66000  -27.07800 38.23200  1.000 39.41525 ? 516 TYR B CD2    1 
ATOM   7615 C  CE1    . TYR B 1 520 ? -8.18800  -28.99200 40.05900  1.000 47.42937 ? 516 TYR B CE1    1 
ATOM   7616 C  CE2    . TYR B 1 520 ? -7.84700  -28.12000 37.93400  1.000 37.27552 ? 516 TYR B CE2    1 
ATOM   7617 C  CZ     . TYR B 1 520 ? -7.61800  -29.06700 38.87000  1.000 46.23186 ? 516 TYR B CZ     1 
ATOM   7618 O  OH     . TYR B 1 520 ? -6.83000  -30.10500 38.59300  1.000 53.01951 ? 516 TYR B OH     1 
ATOM   7619 N  N      . ARG B 1 521 ? -12.65400 -24.52500 41.29700  1.000 35.78587 ? 517 ARG B N      1 
ATOM   7620 C  CA     . ARG B 1 521 ? -13.16300 -23.29200 41.77700  1.000 37.26236 ? 517 ARG B CA     1 
ATOM   7621 C  C      . ARG B 1 521 ? -12.13800 -22.74800 42.73000  1.000 41.19704 ? 517 ARG B C      1 
ATOM   7622 O  O      . ARG B 1 521 ? -11.62400 -23.46100 43.54100  1.000 41.11019 ? 517 ARG B O      1 
ATOM   7623 C  CB     . ARG B 1 521 ? -14.50600 -23.46800 42.44200  1.000 37.05707 ? 517 ARG B CB     1 
ATOM   7624 C  CG     . ARG B 1 521 ? -14.94000 -22.32700 43.33800  1.000 41.81554 ? 517 ARG B CG     1 
ATOM   7625 C  CD     . ARG B 1 521 ? -15.50900 -21.12700 42.60200  1.000 47.26619 ? 517 ARG B CD     1 
ATOM   7626 N  NE     . ARG B 1 521 ? -16.15100 -20.20200 43.50800  1.000 55.55140 ? 517 ARG B NE     1 
ATOM   7627 C  CZ     . ARG B 1 521 ? -16.62100 -19.00600 43.18600  1.000 54.47232 ? 517 ARG B CZ     1 
ATOM   7628 N  NH1    . ARG B 1 521 ? -16.56300 -18.55800 41.94600  1.000 45.15015 ? 517 ARG B NH1    1 
ATOM   7629 N  NH2    . ARG B 1 521 ? -17.17200 -18.27000 44.11300  1.000 51.04559 ? 517 ARG B NH2    1 
ATOM   7630 N  N      . ALA B 1 522 ? -11.84300 -21.47700 42.62000  1.000 31.97752 ? 518 ALA B N      1 
ATOM   7631 C  CA     . ALA B 1 522 ? -10.86600 -20.86400 43.46300  1.000 42.24191 ? 518 ALA B CA     1 
ATOM   7632 C  C      . ALA B 1 522 ? -11.33000 -19.65300 44.23000  1.000 40.12850 ? 518 ALA B C      1 
ATOM   7633 O  O      . ALA B 1 522 ? -11.68200 -18.66800 43.66700  1.000 36.40173 ? 518 ALA B O      1 
ATOM   7634 C  CB     . ALA B 1 522 ? -9.61900  -20.54800 42.68200  1.000 42.14716 ? 518 ALA B CB     1 
ATOM   7635 N  N      . GLU B 1 523 ? -11.31800 -19.75100 45.54300  1.000 37.90718 ? 519 GLU B N      1 
ATOM   7636 C  CA     . GLU B 1 523 ? -11.73500 -18.65500 46.37200  1.000 39.48631 ? 519 GLU B CA     1 
ATOM   7637 C  C      . GLU B 1 523 ? -10.60500 -18.06300 47.20400  1.000 36.73072 ? 519 GLU B C      1 
ATOM   7638 O  O      . GLU B 1 523 ? -10.78800 -17.09900 47.86900  1.000 37.83612 ? 519 GLU B O      1 
ATOM   7639 C  CB     . GLU B 1 523 ? -12.93300 -19.04200 47.21000  1.000 46.32134 ? 519 GLU B CB     1 
ATOM   7640 C  CG     . GLU B 1 523 ? -14.08900 -19.54600 46.37800  1.000 56.68048 ? 519 GLU B CG     1 
ATOM   7641 C  CD     . GLU B 1 523 ? -15.21200 -20.13200 47.19200  1.000 66.95803 ? 519 GLU B CD     1 
ATOM   7642 O  OE1    . GLU B 1 523 ? -16.24200 -20.47500 46.60700  1.000 68.97143 ? 519 GLU B OE1    1 
ATOM   7643 O  OE2    . GLU B 1 523 ? -15.06400 -20.24600 48.40400  1.000 65.83947 ? 519 GLU B OE2    1 
ATOM   7644 N  N      . THR B 1 524 ? -9.43900  -18.67000 47.13000  1.000 38.90203 ? 520 THR B N      1 
ATOM   7645 C  CA     . THR B 1 524 ? -8.23600  -18.20100 47.80300  1.000 44.68430 ? 520 THR B CA     1 
ATOM   7646 C  C      . THR B 1 524 ? -7.07700  -18.33600 46.84700  1.000 47.51622 ? 520 THR B C      1 
ATOM   7647 O  O      . THR B 1 524 ? -7.11700  -19.13000 45.96400  1.000 40.06270 ? 520 THR B O      1 
ATOM   7648 C  CB     . THR B 1 524 ? -7.85800  -19.03600 49.04600  1.000 44.12898 ? 520 THR B CB     1 
ATOM   7649 O  OG1    . THR B 1 524 ? -7.48700  -20.34300 48.66000  1.000 46.23975 ? 520 THR B OG1    1 
ATOM   7650 C  CG2    . THR B 1 524 ? -8.98000  -19.12600 49.99700  1.000 46.17659 ? 520 THR B CG2    1 
ATOM   7651 N  N      . VAL B 1 525 ? -5.99900  -17.61600 47.09600  1.000 51.16666 ? 521 VAL B N      1 
ATOM   7652 C  CA     . VAL B 1 525 ? -4.81500  -17.69900 46.26100  1.000 49.11905 ? 521 VAL B CA     1 
ATOM   7653 C  C      . VAL B 1 525 ? -4.18200  -19.08000 46.23600  1.000 47.58202 ? 521 VAL B C      1 
ATOM   7654 O  O      . VAL B 1 525 ? -3.65900  -19.49200 45.24200  1.000 43.07885 ? 521 VAL B O      1 
ATOM   7655 C  CB     . VAL B 1 525 ? -3.75700  -16.63100 46.60300  1.000 48.56372 ? 521 VAL B CB     1 
ATOM   7656 C  CG1    . VAL B 1 525 ? -4.30700  -15.25000 46.45300  1.000 54.46179 ? 521 VAL B CG1    1 
ATOM   7657 C  CG2    . VAL B 1 525 ? -3.26800  -16.75900 48.00700  1.000 55.94092 ? 521 VAL B CG2    1 
ATOM   7658 N  N      . GLU B 1 526 ? -4.23500  -19.77900 47.35500  1.000 49.18748 ? 522 GLU B N      1 
ATOM   7659 C  CA     . GLU B 1 526 ? -3.70300  -21.09000 47.48900  1.000 43.33941 ? 522 GLU B CA     1 
ATOM   7660 C  C      . GLU B 1 526 ? -4.50400  -22.02500 46.67000  1.000 42.76829 ? 522 GLU B C      1 
ATOM   7661 O  O      . GLU B 1 526 ? -3.97400  -22.86400 46.02000  1.000 46.66875 ? 522 GLU B O      1 
ATOM   7662 C  CB     . GLU B 1 526 ? -3.73600  -21.49900 48.94200  1.000 49.42435 ? 522 GLU B CB     1 
ATOM   7663 C  CG     . GLU B 1 526 ? -2.61400  -20.89900 49.74200  1.000 63.18389 ? 522 GLU B CG     1 
ATOM   7664 C  CD     . GLU B 1 526 ? -2.84800  -19.44700 50.10800  1.000 78.07778 ? 522 GLU B CD     1 
ATOM   7665 O  OE1    . GLU B 1 526 ? -4.02500  -19.00700 50.17100  1.000 78.34360 ? 522 GLU B OE1    1 
ATOM   7666 O  OE2    . GLU B 1 526 ? -1.84600  -18.73700 50.33000  1.000 79.48585 ? 522 GLU B OE2    1 
ATOM   7667 N  N      . ASP B 1 527 ? -5.80600  -21.87600 46.69300  1.000 44.32374 ? 523 ASP B N      1 
ATOM   7668 C  CA     . ASP B 1 527 ? -6.65700  -22.70400 45.86700  1.000 42.48141 ? 523 ASP B CA     1 
ATOM   7669 C  C      . ASP B 1 527 ? -6.33500  -22.43300 44.41500  1.000 37.68083 ? 523 ASP B C      1 
ATOM   7670 O  O      . ASP B 1 527 ? -6.23200  -23.32100 43.65900  1.000 43.47363 ? 523 ASP B O      1 
ATOM   7671 C  CB     . ASP B 1 527 ? -8.11400  -22.36900 46.07500  1.000 49.70596 ? 523 ASP B CB     1 
ATOM   7672 C  CG     . ASP B 1 527 ? -8.70900  -22.99700 47.29600  1.000 66.34216 ? 523 ASP B CG     1 
ATOM   7673 O  OD1    . ASP B 1 527 ? -8.17300  -23.95200 47.83100  1.000 73.20878 ? 523 ASP B OD1    1 
ATOM   7674 O  OD2    . ASP B 1 527 ? -9.75600  -22.51900 47.72500  1.000 75.03268 ? 523 ASP B OD2    1 
ATOM   7675 N  N      . PHE B 1 528 ? -6.18900  -21.17800 44.04600  1.000 36.37541 ? 524 PHE B N      1 
ATOM   7676 C  CA     . PHE B 1 528 ? -5.89800  -20.80000 42.68500  1.000 39.27576 ? 524 PHE B CA     1 
ATOM   7677 C  C      . PHE B 1 528 ? -4.59200  -21.36000 42.17100  1.000 43.55259 ? 524 PHE B C      1 
ATOM   7678 O  O      . PHE B 1 528 ? -4.53100  -21.88300 41.08500  1.000 37.84664 ? 524 PHE B O      1 
ATOM   7679 C  CB     . PHE B 1 528 ? -5.96500  -19.29100 42.51200  1.000 39.63107 ? 524 PHE B CB     1 
ATOM   7680 C  CG     . PHE B 1 528 ? -5.65200  -18.83700 41.13300  1.000 35.89904 ? 524 PHE B CG     1 
ATOM   7681 C  CD1    . PHE B 1 528 ? -6.49100  -19.13300 40.09100  1.000 36.65703 ? 524 PHE B CD1    1 
ATOM   7682 C  CD2    . PHE B 1 528 ? -4.50500  -18.17600 40.87700  1.000 39.53106 ? 524 PHE B CD2    1 
ATOM   7683 C  CE1    . PHE B 1 528 ? -6.18600  -18.75100 38.83300  1.000 35.81482 ? 524 PHE B CE1    1 
ATOM   7684 C  CE2    . PHE B 1 528 ? -4.19400  -17.79000 39.61100  1.000 39.46263 ? 524 PHE B CE2    1 
ATOM   7685 C  CZ     . PHE B 1 528 ? -5.03400  -18.08400 38.58600  1.000 32.79867 ? 524 PHE B CZ     1 
ATOM   7686 N  N      . ASP B 1 529 ? -3.55200  -21.26400 42.98300  1.000 44.80537 ? 525 ASP B N      1 
ATOM   7687 C  CA     . ASP B 1 529 ? -2.24300  -21.79700 42.63500  1.000 42.85514 ? 525 ASP B CA     1 
ATOM   7688 C  C      . ASP B 1 529 ? -2.30500  -23.29300 42.38200  1.000 43.00252 ? 525 ASP B C      1 
ATOM   7689 O  O      . ASP B 1 529 ? -1.73600  -23.77900 41.46100  1.000 43.07885 ? 525 ASP B O      1 
ATOM   7690 C  CB     . ASP B 1 529 ? -1.19700  -21.46200 43.69500  1.000 45.61863 ? 525 ASP B CB     1 
ATOM   7691 C  CG     . ASP B 1 529 ? 0.16900   -21.97700 43.34000  1.000 48.32422 ? 525 ASP B CG     1 
ATOM   7692 O  OD1    . ASP B 1 529 ? 0.79500   -21.45700 42.43100  1.000 51.66409 ? 525 ASP B OD1    1 
ATOM   7693 O  OD2    . ASP B 1 529 ? 0.61300   -22.93300 43.95400  1.000 53.69328 ? 525 ASP B OD2    1 
ATOM   7694 N  N      . ALA B 1 530 ? -3.03800  -24.01600 43.19000  1.000 41.29706 ? 526 ALA B N      1 
ATOM   7695 C  CA     . ALA B 1 530 ? -3.17700  -25.43200 42.98700  1.000 46.06605 ? 526 ALA B CA     1 
ATOM   7696 C  C      . ALA B 1 530 ? -3.92600  -25.74600 41.70900  1.000 44.40006 ? 526 ALA B C      1 
ATOM   7697 O  O      . ALA B 1 530 ? -3.55400  -26.62400 40.96800  1.000 40.41800 ? 526 ALA B O      1 
ATOM   7698 C  CB     . ALA B 1 530 ? -3.88400  -26.04400 44.16200  1.000 44.07107 ? 526 ALA B CB     1 
ATOM   7699 N  N      . ALA B 1 531 ? -5.00100  -25.01000 41.49100  1.000 40.68383 ? 527 ALA B N      1 
ATOM   7700 C  CA     . ALA B 1 531 ? -5.81000  -25.15600 40.30300  1.000 39.31524 ? 527 ALA B CA     1 
ATOM   7701 C  C      . ALA B 1 531 ? -4.97600  -24.90800 39.06400  1.000 43.67892 ? 527 ALA B C      1 
ATOM   7702 O  O      . ALA B 1 531 ? -4.96900  -25.67700 38.15600  1.000 39.72845 ? 527 ALA B O      1 
ATOM   7703 C  CB     . ALA B 1 531 ? -6.96900  -24.20400 40.35100  1.000 36.28330 ? 527 ALA B CB     1 
ATOM   7704 N  N      . LEU B 1 532 ? -4.22800  -23.83500 39.06800  1.000 37.23078 ? 528 LEU B N      1 
ATOM   7705 C  CA     . LEU B 1 532 ? -3.41400  -23.53900 37.92800  1.000 40.64961 ? 528 LEU B CA     1 
ATOM   7706 C  C      . LEU B 1 532 ? -2.38600  -24.60600 37.68800  1.000 38.85992 ? 528 LEU B C      1 
ATOM   7707 O  O      . LEU B 1 532 ? -2.15700  -25.00300 36.59300  1.000 40.56276 ? 528 LEU B O      1 
ATOM   7708 C  CB     . LEU B 1 532 ? -2.77700  -22.17700 38.06800  1.000 41.67605 ? 528 LEU B CB     1 
ATOM   7709 C  CG     . LEU B 1 532 ? -1.92500  -21.63300 36.94300  1.000 45.16331 ? 528 LEU B CG     1 
ATOM   7710 C  CD1    . LEU B 1 532 ? -2.53900  -21.83300 35.57100  1.000 40.72330 ? 528 LEU B CD1    1 
ATOM   7711 C  CD2    . LEU B 1 532 ? -1.70500  -20.17700 37.21900  1.000 44.92118 ? 528 LEU B CD2    1 
ATOM   7712 N  N      . LYS B 1 533 ? -1.78700  -25.08000 38.75200  1.000 38.65200 ? 529 LYS B N      1 
ATOM   7713 C  CA     . LYS B 1 533 ? -0.80900  -26.11100 38.65200  1.000 39.66002 ? 529 LYS B CA     1 
ATOM   7714 C  C      . LYS B 1 533 ? -1.40800  -27.35500 38.05100  1.000 46.23712 ? 529 LYS B C      1 
ATOM   7715 O  O      . LYS B 1 533 ? -0.85400  -27.92700 37.16800  1.000 50.29287 ? 529 LYS B O      1 
ATOM   7716 C  CB     . LYS B 1 533 ? -0.18800  -26.38800 40.00600  1.000 40.31536 ? 529 LYS B CB     1 
ATOM   7717 C  CG     . LYS B 1 533 ? 0.58200   -27.68000 40.05800  1.000 45.05277 ? 529 LYS B CG     1 
ATOM   7718 C  CD     . LYS B 1 533 ? 1.12700   -27.89700 41.44600  1.000 57.92010 ? 529 LYS B CD     1 
ATOM   7719 C  CE     . LYS B 1 533 ? 0.49600   -29.11000 42.10100  1.000 67.22385 ? 529 LYS B CE     1 
ATOM   7720 N  NZ     . LYS B 1 533 ? -0.10800  -28.77100 43.40400  1.000 71.90599 ? 529 LYS B NZ     1 
ATOM   7721 N  N      . GLY B 1 534 ? -2.55600  -27.77100 38.53000  1.000 42.63143 ? 530 GLY B N      1 
ATOM   7722 C  CA     . GLY B 1 534 ? -3.19200  -28.92300 37.97400  1.000 38.68622 ? 530 GLY B CA     1 
ATOM   7723 C  C      . GLY B 1 534 ? -3.55500  -28.71700 36.52300  1.000 43.42626 ? 530 GLY B C      1 
ATOM   7724 O  O      . GLY B 1 534 ? -3.35400  -29.57500 35.71500  1.000 39.96795 ? 530 GLY B O      1 
ATOM   7725 N  N      . ALA B 1 535 ? -4.08700  -27.55500 36.20600  1.000 39.20996 ? 531 ALA B N      1 
ATOM   7726 C  CA     . ALA B 1 535 ? -4.45800  -27.25500 34.83900  1.000 43.57101 ? 531 ALA B CA     1 
ATOM   7727 C  C      . ALA B 1 535 ? -3.32200  -27.37100 33.85200  1.000 44.35532 ? 531 ALA B C      1 
ATOM   7728 O  O      . ALA B 1 535 ? -3.48500  -27.93200 32.82100  1.000 44.78958 ? 531 ALA B O      1 
ATOM   7729 C  CB     . ALA B 1 535 ? -5.08600  -25.88700 34.73600  1.000 32.36441 ? 531 ALA B CB     1 
ATOM   7730 N  N      . LEU B 1 536 ? -2.16400  -26.86000 34.19600  1.000 40.01532 ? 532 LEU B N      1 
ATOM   7731 C  CA     . LEU B 1 536 ? -1.03000  -26.88800 33.31300  1.000 39.52316 ? 532 LEU B CA     1 
ATOM   7732 C  C      . LEU B 1 536 ? -0.51400  -28.25500 32.95000  1.000 43.81315 ? 532 LEU B C      1 
ATOM   7733 O  O      . LEU B 1 536 ? -0.00300  -28.44200 31.88600  1.000 47.61887 ? 532 LEU B O      1 
ATOM   7734 C  CB     . LEU B 1 536 ? 0.07700   -26.01900 33.85500  1.000 34.42781 ? 532 LEU B CB     1 
ATOM   7735 C  CG     . LEU B 1 536 ? -0.16200  -24.53600 33.75200  1.000 40.52854 ? 532 LEU B CG     1 
ATOM   7736 C  CD1    . LEU B 1 536 ? 0.65300   -23.71600 34.70400  1.000 39.10732 ? 532 LEU B CD1    1 
ATOM   7737 C  CD2    . LEU B 1 536 ? -0.03000  -24.05400 32.32800  1.000 39.69423 ? 532 LEU B CD2    1 
ATOM   7738 N  N      . ALA B 1 537 ? -0.63500  -29.16500 33.89400  1.000 44.38953 ? 533 ALA B N      1 
ATOM   7739 C  CA     . ALA B 1 537 ? -0.20300  -30.53000 33.75100  1.000 43.61049 ? 533 ALA B CA     1 
ATOM   7740 C  C      . ALA B 1 537 ? -1.17200  -31.35000 32.96600  1.000 51.32194 ? 533 ALA B C      1 
ATOM   7741 O  O      . ALA B 1 537 ? -0.87200  -32.42100 32.51000  1.000 54.33546 ? 533 ALA B O      1 
ATOM   7742 C  CB     . ALA B 1 537 ? -0.01000  -31.13900 35.11400  1.000 42.03136 ? 533 ALA B CB     1 
ATOM   7743 N  N      . MET B 1 538 ? -2.38900  -30.89300 32.78200  1.000 45.57652 ? 534 MET B N      1 
ATOM   7744 C  CA     . MET B 1 538 ? -3.34200  -31.67600 32.02000  1.000 56.23832 ? 534 MET B CA     1 
ATOM   7745 C  C      . MET B 1 538 ? -3.07700  -31.70700 30.53700  1.000 62.12850 ? 534 MET B C      1 
ATOM   7746 O  O      . MET B 1 538 ? -2.38400  -30.90900 29.99400  1.000 77.39875 ? 534 MET B O      1 
ATOM   7747 C  CB     . MET B 1 538 ? -4.74100  -31.19000 32.25300  1.000 55.84354 ? 534 MET B CB     1 
ATOM   7748 C  CG     . MET B 1 538 ? -5.09900  -31.13800 33.70200  1.000 61.93111 ? 534 MET B CG     1 
ATOM   7749 S  SD     . MET B 1 538 ? -6.63400  -30.27800 33.84400  1.000 73.62462 ? 534 MET B SD     1 
ATOM   7750 C  CE     . MET B 1 538 ? -7.65800  -31.45300 33.01800  1.000 72.84558 ? 534 MET B CE     1 
ATOM   7751 N  N      . ASN B 1 539 ? -3.63600  -32.67900 29.88000  1.000 49.43751 ? 535 ASN B N      1 
ATOM   7752 C  CA     . ASN B 1 539 ? -3.46900  -32.77700 28.47100  1.000 51.75094 ? 535 ASN B CA     1 
ATOM   7753 C  C      . ASN B 1 539 ? -4.84300  -32.60400 27.86600  1.000 60.22301 ? 535 ASN B C      1 
ATOM   7754 O  O      . ASN B 1 539 ? -5.11800  -33.01300 26.76900  1.000 66.25531 ? 535 ASN B O      1 
ATOM   7755 C  CB     . ASN B 1 539 ? -2.80700  -34.08000 28.12200  1.000 69.56097 ? 535 ASN B CB     1 
ATOM   7756 C  CG     . ASN B 1 539 ? -1.49400  -34.28900 28.89200  1.000 87.39206 ? 535 ASN B CG     1 
ATOM   7757 O  OD1    . ASN B 1 539 ? -0.42500  -33.90700 28.41200  1.000 93.75071 ? 535 ASN B OD1    1 
ATOM   7758 N  ND2    . ASN B 1 539 ? -1.57500  -34.88500 30.09700  1.000 86.91832 ? 535 ASN B ND2    1 
ATOM   7759 N  N      . THR B 1 540 ? -5.73500  -32.05300 28.66100  1.000 49.39540 ? 536 THR B N      1 
ATOM   7760 C  CA     . THR B 1 540 ? -7.00900  -31.68700 28.13500  1.000 49.73491 ? 536 THR B CA     1 
ATOM   7761 C  C      . THR B 1 540 ? -7.36900  -30.28700 28.59600  1.000 42.82356 ? 536 THR B C      1 
ATOM   7762 O  O      . THR B 1 540 ? -6.68500  -29.70800 29.39400  1.000 40.21008 ? 536 THR B O      1 
ATOM   7763 C  CB     . THR B 1 540 ? -8.07100  -32.62300 28.68900  1.000 57.68586 ? 536 THR B CB     1 
ATOM   7764 O  OG1    . THR B 1 540 ? -7.88100  -32.74400 30.08400  1.000 58.89390 ? 536 THR B OG1    1 
ATOM   7765 C  CG2    . THR B 1 540 ? -7.95700  -33.96600 28.07200  1.000 65.05254 ? 536 THR B CG2    1 
ATOM   7766 N  N      . PRO B 1 541 ? -8.47500  -29.74800 28.09000  1.000 39.04416 ? 537 PRO B N      1 
ATOM   7767 C  CA     . PRO B 1 541 ? -8.85400  -28.41300 28.52300  1.000 38.18089 ? 537 PRO B CA     1 
ATOM   7768 C  C      . PRO B 1 541 ? -9.31500  -28.34800 29.94600  1.000 33.70667 ? 537 PRO B C      1 
ATOM   7769 O  O      . PRO B 1 541 ? -9.76600  -29.29600 30.49600  1.000 29.73251 ? 537 PRO B O      1 
ATOM   7770 C  CB     . PRO B 1 541 ? -9.96200  -28.03100 27.58200  1.000 33.31978 ? 537 PRO B CB     1 
ATOM   7771 C  CG     . PRO B 1 541 ? -10.44400 -29.28200 27.03300  1.000 36.27803 ? 537 PRO B CG     1 
ATOM   7772 C  CD     . PRO B 1 541 ? -9.35500  -30.25700 27.05200  1.000 39.64160 ? 537 PRO B CD     1 
ATOM   7773 N  N      . CYS B 1 542 ? -9.19500  -27.18100 30.51200  1.000 29.44564 ? 538 CYS B N      1 
ATOM   7774 C  CA     . CYS B 1 542 ? -9.54300  -26.95900 31.86200  1.000 31.74591 ? 538 CYS B CA     1 
ATOM   7775 C  C      . CYS B 1 542 ? -10.04500 -25.55500 32.11900  1.000 32.49074 ? 538 CYS B C      1 
ATOM   7776 O  O      . CYS B 1 542 ? -9.63800  -24.62000 31.48200  1.000 34.32780 ? 538 CYS B O      1 
ATOM   7777 C  CB     . CYS B 1 542 ? -8.31000  -27.25600 32.71600  1.000 38.38618 ? 538 CYS B CB     1 
ATOM   7778 S  SG     . CYS B 1 542 ? -8.52600  -27.18100 34.46800  1.000 44.05002 ? 538 CYS B SG     1 
ATOM   7779 N  N      . LEU B 1 543 ? -10.91000 -25.42800 33.09100  1.000 27.57962 ? 539 LEU B N      1 
ATOM   7780 C  CA     . LEU B 1 543 ? -11.45700 -24.15800 33.48500  1.000 29.29562 ? 539 LEU B CA     1 
ATOM   7781 C  C      . LEU B 1 543 ? -11.26900 -23.83000 34.96000  1.000 33.45138 ? 539 LEU B C      1 
ATOM   7782 O  O      . LEU B 1 543 ? -11.47600 -24.63300 35.78400  1.000 32.26439 ? 539 LEU B O      1 
ATOM   7783 C  CB     . LEU B 1 543 ? -12.93500 -24.09300 33.12100  1.000 25.32146 ? 539 LEU B CB     1 
ATOM   7784 C  CG     . LEU B 1 543 ? -13.65200 -22.79700 33.35100  1.000 30.94055 ? 539 LEU B CG     1 
ATOM   7785 C  CD1    . LEU B 1 543 ? -14.69500 -22.54700 32.30100  1.000 33.65140 ? 539 LEU B CD1    1 
ATOM   7786 C  CD2    . LEU B 1 543 ? -14.23100 -22.65500 34.72900  1.000 25.15565 ? 539 LEU B CD2    1 
ATOM   7787 N  N      . ILE B 1 544 ? -10.87400 -22.62200 35.26600  1.000 33.21451 ? 540 ILE B N      1 
ATOM   7788 C  CA     . ILE B 1 544 ? -10.70300 -22.18800 36.62700  1.000 33.54086 ? 540 ILE B CA     1 
ATOM   7789 C  C      . ILE B 1 544 ? -11.60500 -21.00600 36.90600  1.000 32.93290 ? 540 ILE B C      1 
ATOM   7790 O  O      . ILE B 1 544 ? -11.43200 -19.97500 36.35200  1.000 30.96687 ? 540 ILE B O      1 
ATOM   7791 C  CB     . ILE B 1 544 ? -9.23900  -21.86200 36.95800  1.000 32.41968 ? 540 ILE B CB     1 
ATOM   7792 C  CG1    . ILE B 1 544 ? -8.32600  -23.00400 36.60400  1.000 27.97441 ? 540 ILE B CG1    1 
ATOM   7793 C  CG2    . ILE B 1 544 ? -9.07100  -21.48700 38.39700  1.000 28.02968 ? 540 ILE B CG2    1 
ATOM   7794 C  CD1    . ILE B 1 544 ? -6.88700  -22.70200 36.85200  1.000 29.56144 ? 540 ILE B CD1    1 
ATOM   7795 N  N      . ASP B 1 545 ? -12.58200 -21.21800 37.76900  1.000 30.60367 ? 541 ASP B N      1 
ATOM   7796 C  CA     . ASP B 1 545 ? -13.58000 -20.26700 38.20000  1.000 28.00073 ? 541 ASP B CA     1 
ATOM   7797 C  C      . ASP B 1 545 ? -13.06900 -19.52800 39.41500  1.000 29.61671 ? 541 ASP B C      1 
ATOM   7798 O  O      . ASP B 1 545 ? -13.08400 -20.04200 40.48600  1.000 34.75154 ? 541 ASP B O      1 
ATOM   7799 C  CB     . ASP B 1 545 ? -14.85100 -21.04900 38.51400  1.000 33.13029 ? 541 ASP B CB     1 
ATOM   7800 C  CG     . ASP B 1 545 ? -16.07200 -20.18400 38.80900  1.000 50.29814 ? 541 ASP B CG     1 
ATOM   7801 O  OD1    . ASP B 1 545 ? -15.96400 -19.03600 39.18900  1.000 59.95719 ? 541 ASP B OD1    1 
ATOM   7802 O  OD2    . ASP B 1 545 ? -17.18500 -20.69500 38.70800  1.000 52.35365 ? 541 ASP B OD2    1 
ATOM   7803 N  N      . VAL B 1 546 ? -12.62200 -18.30700 39.24800  1.000 32.16965 ? 542 VAL B N      1 
ATOM   7804 C  CA     . VAL B 1 546 ? -12.06900 -17.53400 40.33300  1.000 33.40137 ? 542 VAL B CA     1 
ATOM   7805 C  C      . VAL B 1 546 ? -13.00500 -16.51600 40.95100  1.000 37.91507 ? 542 VAL B C      1 
ATOM   7806 O  O      . VAL B 1 546 ? -13.56900 -15.70900 40.26200  1.000 37.02023 ? 542 VAL B O      1 
ATOM   7807 C  CB     . VAL B 1 546 ? -10.82300 -16.77700 39.86900  1.000 35.49899 ? 542 VAL B CB     1 
ATOM   7808 C  CG1    . VAL B 1 546 ? -10.14800 -16.07200 41.01500  1.000 29.23772 ? 542 VAL B CG1    1 
ATOM   7809 C  CG2    . VAL B 1 546 ? -9.86700  -17.69300 39.17700  1.000 33.93302 ? 542 VAL B CG2    1 
ATOM   7810 N  N      . GLN B 1 547 ? -13.14100 -16.54700 42.26700  1.000 34.33833 ? 543 GLN B N      1 
ATOM   7811 C  CA     . GLN B 1 547 ? -13.96800 -15.60100 42.98800  1.000 36.33857 ? 543 GLN B CA     1 
ATOM   7812 C  C      . GLN B 1 547 ? -13.27900 -14.26300 43.04000  1.000 39.13364 ? 543 GLN B C      1 
ATOM   7813 O  O      . GLN B 1 547 ? -12.19500 -14.17300 43.48700  1.000 37.14656 ? 543 GLN B O      1 
ATOM   7814 C  CB     . GLN B 1 547 ? -14.27900 -16.07900 44.39100  1.000 34.03303 ? 543 GLN B CB     1 
ATOM   7815 C  CG     . GLN B 1 547 ? -15.32500 -15.26600 45.11000  1.000 42.26559 ? 543 GLN B CG     1 
ATOM   7816 C  CD     . GLN B 1 547 ? -15.49800 -15.59700 46.60100  1.000 55.05397 ? 543 GLN B CD     1 
ATOM   7817 O  OE1    . GLN B 1 547 ? -14.73500 -16.32000 47.19500  1.000 52.44576 ? 543 GLN B OE1    1 
ATOM   7818 N  NE2    . GLN B 1 547 ? -16.50800 -15.04100 47.18700  1.000 59.27290 ? 543 GLN B NE2    1 
ATOM   7819 N  N      . VAL B 1 548 ? -13.92100 -13.22900 42.52000  1.000 34.44887 ? 544 VAL B N      1 
ATOM   7820 C  CA     . VAL B 1 548 ? -13.38500 -11.88900 42.45900  1.000 33.99881 ? 544 VAL B CA     1 
ATOM   7821 C  C      . VAL B 1 548 ? -14.47100 -10.86000 42.82300  1.000 37.45186 ? 544 VAL B C      1 
ATOM   7822 O  O      . VAL B 1 548 ? -15.59900 -11.05000 42.51600  1.000 33.45138 ? 544 VAL B O      1 
ATOM   7823 C  CB     . VAL B 1 548 ? -12.79900 -11.61700 41.05800  1.000 40.24693 ? 544 VAL B CB     1 
ATOM   7824 C  CG1    . VAL B 1 548 ? -12.44600 -10.17800 40.83100  1.000 41.72606 ? 544 VAL B CG1    1 
ATOM   7825 C  CG2    . VAL B 1 548 ? -11.57100 -12.43300 40.77500  1.000 45.73969 ? 544 VAL B CG2    1 
ATOM   7826 N  N      . ASP B 1 549 ? -14.10200 -9.82100  43.55600  1.000 37.15182 ? 545 ASP B N      1 
ATOM   7827 C  CA     . ASP B 1 549 ? -14.93900 -8.72600  43.97400  1.000 43.23150 ? 545 ASP B CA     1 
ATOM   7828 C  C      . ASP B 1 549 ? -15.15900 -7.72300  42.83300  1.000 42.74460 ? 545 ASP B C      1 
ATOM   7829 O  O      . ASP B 1 549 ? -14.25300 -7.20200  42.27000  1.000 36.55965 ? 545 ASP B O      1 
ATOM   7830 C  CB     . ASP B 1 549 ? -14.23500 -8.06300  45.13700  1.000 47.62939 ? 545 ASP B CB     1 
ATOM   7831 C  CG     . ASP B 1 549 ? -15.04000 -7.00900  45.82200  1.000 57.58322 ? 545 ASP B CG     1 
ATOM   7832 O  OD1    . ASP B 1 549 ? -16.09300 -6.58700  45.36800  1.000 56.14621 ? 545 ASP B OD1    1 
ATOM   7833 O  OD2    . ASP B 1 549 ? -14.57300 -6.56900  46.88500  1.000 61.86268 ? 545 ASP B OD2    1 
ATOM   7834 N  N      . ILE B 1 550 ? -16.41000 -7.43800  42.55800  1.000 39.68897 ? 546 ILE B N      1 
ATOM   7835 C  CA     . ILE B 1 550 ? -16.81000 -6.54700  41.49300  1.000 40.06796 ? 546 ILE B CA     1 
ATOM   7836 C  C      . ILE B 1 550 ? -16.49700 -5.07600  41.71000  1.000 44.01054 ? 546 ILE B C      1 
ATOM   7837 O  O      . ILE B 1 550 ? -16.45100 -4.33500  40.77800  1.000 40.11797 ? 546 ILE B O      1 
ATOM   7838 C  CB     . ILE B 1 550 ? -18.30500 -6.72400  41.19300  1.000 36.95180 ? 546 ILE B CB     1 
ATOM   7839 C  CG1    . ILE B 1 550 ? -18.64000 -6.24400  39.79000  1.000 36.14381 ? 546 ILE B CG1    1 
ATOM   7840 C  CG2    . ILE B 1 550 ? -19.13900 -5.99500  42.20900  1.000 33.79353 ? 546 ILE B CG2    1 
ATOM   7841 C  CD1    . ILE B 1 550 ? -19.98800 -6.63900  39.29800  1.000 31.52746 ? 546 ILE B CD1    1 
ATOM   7842 N  N      . ASP B 1 551 ? -16.25800 -4.67900  42.94800  1.000 38.46777 ? 547 ASP B N      1 
ATOM   7843 C  CA     . ASP B 1 551 ? -15.96100 -3.32600  43.28000  1.000 42.93936 ? 547 ASP B CA     1 
ATOM   7844 C  C      . ASP B 1 551 ? -14.51600 -2.93000  43.13500  1.000 43.81578 ? 547 ASP B C      1 
ATOM   7845 O  O      . ASP B 1 551 ? -14.21600 -1.78800  43.22000  1.000 48.82954 ? 547 ASP B O      1 
ATOM   7846 C  CB     . ASP B 1 551 ? -16.35700 -3.04600  44.71700  1.000 50.60080 ? 547 ASP B CB     1 
ATOM   7847 C  CG     . ASP B 1 551 ? -17.81200 -2.89700  44.89300  1.000 59.17815 ? 547 ASP B CG     1 
ATOM   7848 O  OD1    . ASP B 1 551 ? -18.47600 -2.34300  44.03100  1.000 61.33104 ? 547 ASP B OD1    1 
ATOM   7849 O  OD2    . ASP B 1 551 ? -18.31400 -3.34900  45.90900  1.000 68.83983 ? 547 ASP B OD2    1 
ATOM   7850 N  N      . VAL B 1 552 ? -13.62500 -3.85700  42.90900  1.000 41.27074 ? 548 VAL B N      1 
ATOM   7851 C  CA     . VAL B 1 552 ? -12.22500 -3.51800  42.79800  1.000 42.46562 ? 548 VAL B CA     1 
ATOM   7852 C  C      . VAL B 1 552 ? -11.91200 -2.65400  41.60600  1.000 38.28091 ? 548 VAL B C      1 
ATOM   7853 O  O      . VAL B 1 552 ? -12.26900 -2.95200  40.52600  1.000 41.01018 ? 548 VAL B O      1 
ATOM   7854 C  CB     . VAL B 1 552 ? -11.34500 -4.76100  42.81600  1.000 43.51838 ? 548 VAL B CB     1 
ATOM   7855 C  CG1    . VAL B 1 552 ? -9.90400  -4.40100  42.65200  1.000 45.11067 ? 548 VAL B CG1    1 
ATOM   7856 C  CG2    . VAL B 1 552 ? -11.54000 -5.50900  44.10300  1.000 44.93433 ? 548 VAL B CG2    1 
ATOM   7857 N  N      . LEU B 1 553 ? -11.24100 -1.55800  41.84800  1.000 39.28366 ? 549 LEU B N      1 
ATOM   7858 C  CA     . LEU B 1 553 ? -10.88700 -0.61800  40.82800  1.000 42.10768 ? 549 LEU B CA     1 
ATOM   7859 C  C      . LEU B 1 553 ? -9.61100  -1.01200  40.11500  1.000 41.60236 ? 549 LEU B C      1 
ATOM   7860 O  O      . LEU B 1 553 ? -8.57100  -0.96800  40.66100  1.000 39.40472 ? 549 LEU B O      1 
ATOM   7861 C  CB     . LEU B 1 553 ? -10.78400 0.74100   41.47300  1.000 47.24514 ? 549 LEU B CB     1 
ATOM   7862 C  CG     . LEU B 1 553 ? -10.93200 1.97800   40.63500  1.000 54.09333 ? 549 LEU B CG     1 
ATOM   7863 C  CD1    . LEU B 1 553 ? -9.89100  1.84400   39.58900  1.000 64.36035 ? 549 LEU B CD1    1 
ATOM   7864 C  CD2    . LEU B 1 553 ? -12.26700 2.15900   39.96100  1.000 48.23999 ? 549 LEU B CD2    1 
ATOM   7865 N  N      . PRO B 1 554 ? -9.70700  -1.37500  38.84800  1.000 42.85514 ? 550 PRO B N      1 
ATOM   7866 C  CA     . PRO B 1 554 ? -8.58000  -1.85000  38.05100  1.000 40.58381 ? 550 PRO B CA     1 
ATOM   7867 C  C      . PRO B 1 554 ? -7.59300  -0.78800  37.65800  1.000 40.56013 ? 550 PRO B C      1 
ATOM   7868 O  O      . PRO B 1 554 ? -7.92400  0.32300   37.57400  1.000 47.03722 ? 550 PRO B O      1 
ATOM   7869 C  CB     . PRO B 1 554 ? -9.26500  -2.43700  36.82000  1.000 45.13962 ? 550 PRO B CB     1 
ATOM   7870 C  CG     . PRO B 1 554 ? -10.69600 -2.50800  37.15800  1.000 43.13412 ? 550 PRO B CG     1 
ATOM   7871 C  CD     . PRO B 1 554 ? -10.92800 -1.37000  38.06600  1.000 41.58130 ? 550 PRO B CD     1 
ATOM   7872 N  N      . PRO B 1 555 ? -6.37300  -1.15500  37.40900  1.000 41.36285 ? 551 PRO B N      1 
ATOM   7873 C  CA     . PRO B 1 555 ? -5.35500  -0.18300  37.05100  1.000 40.92859 ? 551 PRO B CA     1 
ATOM   7874 C  C      . PRO B 1 555 ? -5.69900  0.66700   35.86000  1.000 44.88170 ? 551 PRO B C      1 
ATOM   7875 O  O      . PRO B 1 555 ? -6.15900  0.16000   34.87100  1.000 44.26847 ? 551 PRO B O      1 
ATOM   7876 C  CB     . PRO B 1 555 ? -4.14000  -1.02600  36.74500  1.000 39.36261 ? 551 PRO B CB     1 
ATOM   7877 C  CG     . PRO B 1 555 ? -4.54800  -2.41800  36.86400  1.000 40.63645 ? 551 PRO B CG     1 
ATOM   7878 C  CD     . PRO B 1 555 ? -5.85800  -2.50700  37.51200  1.000 42.02609 ? 551 PRO B CD     1 
ATOM   7879 N  N      . GLY B 1 556 ? -5.50300  1.96100   35.99600  1.000 40.72594 ? 552 GLY B N      1 
ATOM   7880 C  CA     . GLY B 1 556 ? -5.76800  2.89100   34.94000  1.000 40.16534 ? 552 GLY B CA     1 
ATOM   7881 C  C      . GLY B 1 556 ? -7.18800  3.36200   34.77800  1.000 51.73252 ? 552 GLY B C      1 
ATOM   7882 O  O      . GLY B 1 556 ? -7.43900  4.25400   34.03200  1.000 60.54937 ? 552 GLY B O      1 
ATOM   7883 N  N      . MET B 1 557 ? -8.13000  2.78100   35.47300  1.000 52.66684 ? 553 MET B N      1 
ATOM   7884 C  CA     . MET B 1 557 ? -9.49800  3.19900   35.30000  1.000 56.42519 ? 553 MET B CA     1 
ATOM   7885 C  C      . MET B 1 557 ? -9.81700  4.52800   35.94100  1.000 59.19920 ? 553 MET B C      1 
ATOM   7886 O  O      . MET B 1 557 ? -10.65600 5.24100   35.48100  1.000 57.74113 ? 553 MET B O      1 
ATOM   7887 C  CB     . MET B 1 557 ? -10.46100 2.14500   35.78900  1.000 55.69878 ? 553 MET B CB     1 
ATOM   7888 C  CG     . MET B 1 557 ? -10.64000 1.00300   34.82300  1.000 60.30986 ? 553 MET B CG     1 
ATOM   7889 S  SD     . MET B 1 557 ? -11.03200 1.54500   33.17200  1.000 59.72821 ? 553 MET B SD     1 
ATOM   7890 C  CE     . MET B 1 557 ? -12.62300 2.22100   33.47800  1.000 54.56181 ? 553 MET B CE     1 
ATOM   7891 N  N      . LYS B 1 558 ? -9.14800  4.84600   37.02000  1.000 65.18676 ? 554 LYS B N      1 
ATOM   7892 C  CA     . LYS B 1 558 ? -9.37300  6.09000   37.69600  1.000 67.46335 ? 554 LYS B CA     1 
ATOM   7893 C  C      . LYS B 1 558 ? -9.01800  7.20700   36.75100  1.000 73.31669 ? 554 LYS B C      1 
ATOM   7894 O  O      . LYS B 1 558 ? -9.81300  8.08300   36.49600  1.000 76.73025 ? 554 LYS B O      1 
ATOM   7895 C  CB     . LYS B 1 558 ? -8.51100  6.17600   38.91800  1.000 63.95240 ? 554 LYS B CB     1 
ATOM   7896 C  CG     . LYS B 1 558 ? -8.73900  7.44100   39.70300  1.000 68.49242 ? 554 LYS B CG     1 
ATOM   7897 C  CD     . LYS B 1 558 ? -9.52000  7.18200   40.97700  1.000 70.04524 ? 554 LYS B CD     1 
ATOM   7898 C  CE     . LYS B 1 558 ? -10.23800 8.43000   41.46200  1.000 73.45091 ? 554 LYS B CE     1 
ATOM   7899 N  NZ     . LYS B 1 558 ? -9.49200  9.71500   41.30900  1.000 74.19574 ? 554 LYS B NZ     1 
ATOM   7900 N  N      . GLN B 1 559 ? -7.82200  7.16400   36.19700  1.000 69.33989 ? 555 GLN B N      1 
ATOM   7901 C  CA     . GLN B 1 559 ? -7.39900  8.18800   35.26100  1.000 68.92932 ? 555 GLN B CA     1 
ATOM   7902 C  C      . GLN B 1 559 ? -8.35600  8.27400   34.08400  1.000 68.30293 ? 555 GLN B C      1 
ATOM   7903 O  O      . GLN B 1 559 ? -8.62900  9.33500   33.56300  1.000 70.28737 ? 555 GLN B O      1 
ATOM   7904 C  CB     . GLN B 1 559 ? -5.99100  7.90100   34.73300  1.000 70.64005 ? 555 GLN B CB     1 
ATOM   7905 C  CG     . GLN B 1 559 ? -4.90200  7.78200   35.78500  1.000 77.17504 ? 555 GLN B CG     1 
ATOM   7906 C  CD     . GLN B 1 559 ? -5.00600  6.51900   36.62000  1.000 79.90169 ? 555 GLN B CD     1 
ATOM   7907 O  OE1    . GLN B 1 559 ? -5.99200  5.78100   36.55300  1.000 81.67821 ? 555 GLN B OE1    1 
ATOM   7908 N  NE2    . GLN B 1 559 ? -3.97700  6.26400   37.41200  1.000 75.58538 ? 555 GLN B NE2    1 
ATOM   7909 N  N      . ARG B 1 560 ? -8.87000  7.11300   33.68900  1.000 61.51527 ? 556 ARG B N      1 
ATOM   7910 C  CA     . ARG B 1 560 ? -9.81100  7.02000   32.58500  1.000 58.79389 ? 556 ARG B CA     1 
ATOM   7911 C  C      . ARG B 1 560 ? -11.15100 7.63100   32.97300  1.000 65.64208 ? 556 ARG B C      1 
ATOM   7912 O  O      . ARG B 1 560 ? -11.84800 8.19600   32.13000  1.000 64.67618 ? 556 ARG B O      1 
ATOM   7913 C  CB     . ARG B 1 560 ? -9.99900  5.56200   32.16200  1.000 55.24083 ? 556 ARG B CB     1 
ATOM   7914 C  CG     . ARG B 1 560 ? -10.33100 5.38100   30.69000  1.000 60.90730 ? 556 ARG B CG     1 
ATOM   7915 C  CD     . ARG B 1 560 ? -9.19500  5.86500   29.80400  1.000 63.20231 ? 556 ARG B CD     1 
ATOM   7916 N  NE     . ARG B 1 560 ? -9.66600  6.27600   28.48400  1.000 65.78420 ? 556 ARG B NE     1 
ATOM   7917 C  CZ     . ARG B 1 560 ? -8.86800  6.53300   27.45300  1.000 66.76590 ? 556 ARG B CZ     1 
ATOM   7918 N  NH1    . ARG B 1 560 ? -7.55300  6.42200   27.58600  1.000 67.82655 ? 556 ARG B NH1    1 
ATOM   7919 N  NH2    . ARG B 1 560 ? -9.38400  6.90000   26.28800  1.000 66.16056 ? 556 ARG B NH2    1 
ATOM   7920 N  N      . PHE B 1 561 ? -11.51200 7.52000   34.24900  1.000 69.40569 ? 557 PHE B N      1 
ATOM   7921 C  CA     . PHE B 1 561 ? -12.75900 8.07300   34.70100  1.000 70.44792 ? 557 PHE B CA     1 
ATOM   7922 C  C      . PHE B 1 561 ? -12.58300 9.55600   34.82000  1.000 71.37172 ? 557 PHE B C      1 
ATOM   7923 O  O      . PHE B 1 561 ? -13.49300 10.30600  34.58000  1.000 73.27721 ? 557 PHE B O      1 
ATOM   7924 C  CB     . PHE B 1 561 ? -13.19600 7.48400   36.03300  1.000 64.00504 ? 557 PHE B CB     1 
ATOM   7925 C  CG     . PHE B 1 561 ? -13.87700 6.15800   35.92400  1.000 59.93877 ? 557 PHE B CG     1 
ATOM   7926 C  CD1    . PHE B 1 561 ? -14.69400 5.87300   34.87100  1.000 55.32769 ? 557 PHE B CD1    1 
ATOM   7927 C  CD2    . PHE B 1 561 ? -13.68100 5.19600   36.87900  1.000 57.31477 ? 557 PHE B CD2    1 
ATOM   7928 C  CE1    . PHE B 1 561 ? -15.30400 4.66000   34.76900  1.000 52.90898 ? 557 PHE B CE1    1 
ATOM   7929 C  CE2    . PHE B 1 561 ? -14.28600 3.98300   36.77500  1.000 52.65368 ? 557 PHE B CE2    1 
ATOM   7930 C  CZ     . PHE B 1 561 ? -15.10400 3.71200   35.72300  1.000 50.13496 ? 557 PHE B CZ     1 
ATOM   7931 N  N      . ASP B 1 562 ? -11.38800 9.98000   35.15900  1.000 68.57401 ? 558 ASP B N      1 
ATOM   7932 C  CA     . ASP B 1 562 ? -11.16100 11.39200  35.31100  1.000 73.35880 ? 558 ASP B CA     1 
ATOM   7933 C  C      . ASP B 1 562 ? -10.53900 12.01700  34.05600  1.000 72.82189 ? 558 ASP B C      1 
ATOM   7934 O  O      . ASP B 1 562 ? -11.21000 12.25700  33.06000  1.000 70.89008 ? 558 ASP B O      1 
ATOM   7935 C  CB     . ASP B 1 562 ? -10.30100 11.65900  36.55200  1.000 74.71422 ? 558 ASP B CB     1 
ATOM   7936 C  CG     . ASP B 1 562 ? -10.95700 11.18900  37.85000  1.000 76.66972 ? 558 ASP B CG     1 
ATOM   7937 O  OD1    . ASP B 1 562 ? -12.18300 11.00300  37.89600  1.000 75.89857 ? 558 ASP B OD1    1 
ATOM   7938 O  OD2    . ASP B 1 562 ? -10.23700 10.99500  38.83100  1.000 75.51695 ? 558 ASP B OD2    1 
HETATM 7939 P  PB     . ADP C 2 .   ? -44.84600 -17.35400 4.72900   1.000 35.45688 ? 601 ADP A PB     1 
HETATM 7940 O  O1B    . ADP C 2 .   ? -46.13100 -17.60700 5.46300   1.000 22.81326 ? 601 ADP A O1B    1 
HETATM 7941 O  O2B    . ADP C 2 .   ? -43.75200 -18.34100 4.99900   1.000 26.81111 ? 601 ADP A O2B    1 
HETATM 7942 O  O3B    . ADP C 2 .   ? -44.95400 -17.11400 3.26600   1.000 28.05336 ? 601 ADP A O3B    1 
HETATM 7943 P  PA     . ADP C 2 .   ? -43.38400 -14.84800 4.83200   1.000 24.47925 ? 601 ADP A PA     1 
HETATM 7944 O  O1A    . ADP C 2 .   ? -42.95000 -13.99500 5.99900   1.000 24.78981 ? 601 ADP A O1A    1 
HETATM 7945 O  O2A    . ADP C 2 .   ? -42.38600 -15.46200 3.88700   1.000 23.05013 ? 601 ADP A O2A    1 
HETATM 7946 O  O3A    . ADP C 2 .   ? -44.37900 -15.98100 5.43700   1.000 29.20613 ? 601 ADP A O3A    1 
HETATM 7947 O  "O5'"  . ADP C 2 .   ? -44.33300 -13.93800 3.93900   1.000 26.37948 ? 601 ADP A "O5'"  1 
HETATM 7948 C  "C5'"  . ADP C 2 .   ? -45.18400 -13.04800 4.65100   1.000 28.05863 ? 601 ADP A "C5'"  1 
HETATM 7949 C  "C4'"  . ADP C 2 .   ? -45.90200 -12.24100 3.58800   1.000 29.68514 ? 601 ADP A "C4'"  1 
HETATM 7950 O  "O4'"  . ADP C 2 .   ? -47.03300 -11.60200 4.18600   1.000 25.86626 ? 601 ADP A "O4'"  1 
HETATM 7951 C  "C3'"  . ADP C 2 .   ? -45.06400 -11.16900 2.87400   1.000 25.05564 ? 601 ADP A "C3'"  1 
HETATM 7952 O  "O3'"  . ADP C 2 .   ? -45.28200 -11.43000 1.48700   1.000 28.03231 ? 601 ADP A "O3'"  1 
HETATM 7953 C  "C2'"  . ADP C 2 .   ? -45.63500 -9.84100  3.35300   1.000 18.58118 ? 601 ADP A "C2'"  1 
HETATM 7954 O  "O2'"  . ADP C 2 .   ? -45.62600 -8.87000  2.32000   1.000 28.40867 ? 601 ADP A "O2'"  1 
HETATM 7955 C  "C1'"  . ADP C 2 .   ? -47.07000 -10.23900 3.74300   1.000 22.36584 ? 601 ADP A "C1'"  1 
HETATM 7956 N  N9     . ADP C 2 .   ? -47.65900 -9.37700  4.79100   1.000 23.12909 ? 601 ADP A N9     1 
HETATM 7957 C  C8     . ADP C 2 .   ? -47.06100 -8.86800  5.89700   1.000 22.75273 ? 601 ADP A C8     1 
HETATM 7958 N  N7     . ADP C 2 .   ? -47.94900 -8.13100  6.60400   1.000 25.30830 ? 601 ADP A N7     1 
HETATM 7959 C  C5     . ADP C 2 .   ? -49.11600 -8.18300  5.95300   1.000 20.73933 ? 601 ADP A C5     1 
HETATM 7960 C  C6     . ADP C 2 .   ? -50.46300 -7.64200  6.15400   1.000 24.39503 ? 601 ADP A C6     1 
HETATM 7961 N  N6     . ADP C 2 .   ? -50.65300 -6.87200  7.23200   1.000 24.17921 ? 601 ADP A N6     1 
HETATM 7962 N  N1     . ADP C 2 .   ? -51.44600 -7.91800  5.26900   1.000 29.12454 ? 601 ADP A N1     1 
HETATM 7963 C  C2     . ADP C 2 .   ? -51.18900 -8.68900  4.20100   1.000 29.40089 ? 601 ADP A C2     1 
HETATM 7964 N  N3     . ADP C 2 .   ? -49.97900 -9.22600  3.95700   1.000 23.58177 ? 601 ADP A N3     1 
HETATM 7965 C  C4     . ADP C 2 .   ? -48.93000 -9.01800  4.77800   1.000 22.57113 ? 601 ADP A C4     1 
HETATM 7966 H  "H5'1" . ADP C 2 .   ? -44.60500 -12.39700 5.30900   1.000 33.67000 ? 601 ADP A "H5'1" 1 
HETATM 7967 H  "H5'2" . ADP C 2 .   ? -45.89600 -13.60100 5.26700   1.000 33.67000 ? 601 ADP A "H5'2" 1 
HETATM 7968 H  "H4'"  . ADP C 2 .   ? -46.17900 -12.96700 2.81100   1.000 35.62000 ? 601 ADP A "H4'"  1 
HETATM 7969 H  "H3'"  . ADP C 2 .   ? -43.98100 -11.16200 3.06400   1.000 30.07000 ? 601 ADP A "H3'"  1 
HETATM 7970 H  "HO3'" . ADP C 2 .   ? -46.21300 -11.64800 1.34300   1.000 33.64000 ? 601 ADP A "HO3'" 1 
HETATM 7971 H  "H2'"  . ADP C 2 .   ? -45.06400 -9.37400  4.16800   1.000 22.30000 ? 601 ADP A "H2'"  1 
HETATM 7972 H  "HO2'" . ADP C 2 .   ? -45.28400 -9.26800  1.50700   1.000 34.09000 ? 601 ADP A "HO2'" 1 
HETATM 7973 H  "H1'"  . ADP C 2 .   ? -47.70300 -10.10900 2.85400   1.000 26.84000 ? 601 ADP A "H1'"  1 
HETATM 7974 H  H8     . ADP C 2 .   ? -46.02500 -9.02700  6.17200   1.000 27.30000 ? 601 ADP A H8     1 
HETATM 7975 H  HN61   . ADP C 2 .   ? -51.54600 -6.48700  7.41600   1.000 29.02000 ? 601 ADP A HN61   1 
HETATM 7976 H  HN62   . ADP C 2 .   ? -49.88700 -6.70700  7.86500   1.000 29.02000 ? 601 ADP A HN62   1 
HETATM 7977 H  H2     . ADP C 2 .   ? -51.99300 -8.89000  3.50400   1.000 35.28000 ? 601 ADP A H2     1 
HETATM 7978 N  "N1'"  . TPP D 3 .   ? -26.07600 -22.12800 11.56100  1.000 26.18998 ? 602 TPP A "N1'"  1 
HETATM 7979 C  "C2'"  . TPP D 3 .   ? -27.17500 -21.41600 11.86500  1.000 29.81673 ? 602 TPP A "C2'"  1 
HETATM 7980 C  CM2    . TPP D 3 .   ? -26.99300 -20.20500 12.72100  1.000 28.49815 ? 602 TPP A CM2    1 
HETATM 7981 N  "N3'"  . TPP D 3 .   ? -28.41900 -21.69900 11.46500  1.000 30.40101 ? 602 TPP A "N3'"  1 
HETATM 7982 C  "C4'"  . TPP D 3 .   ? -28.59900 -22.78900 10.69400  1.000 30.86159 ? 602 TPP A "C4'"  1 
HETATM 7983 N  "N4'"  . TPP D 3 .   ? -29.84400 -23.04200 10.28800  1.000 28.75871 ? 602 TPP A "N4'"  1 
HETATM 7984 C  "C5'"  . TPP D 3 .   ? -27.50100 -23.62500 10.32900  1.000 29.75094 ? 602 TPP A "C5'"  1 
HETATM 7985 C  "C6'"  . TPP D 3 .   ? -26.27100 -23.20700 10.79200  1.000 27.26380 ? 602 TPP A "C6'"  1 
HETATM 7986 C  "C7'"  . TPP D 3 .   ? -27.64600 -24.86100 9.47000   1.000 28.49815 ? 602 TPP A "C7'"  1 
HETATM 7987 N  N3     . TPP D 3 .   ? -28.38100 -25.96200 10.14800  1.000 30.53524 ? 602 TPP A N3     1 
HETATM 7988 C  C2     . TPP D 3 .   ? -29.63400 -26.29500 9.87100   1.000 36.60965 ? 602 TPP A C2     1 
HETATM 7989 S  S1     . TPP D 3 .   ? -30.19100 -27.56700 10.82200  1.000 35.76481 ? 602 TPP A S1     1 
HETATM 7990 C  C5     . TPP D 3 .   ? -28.66400 -27.67500 11.61200  1.000 31.36165 ? 602 TPP A C5     1 
HETATM 7991 C  C4     . TPP D 3 .   ? -27.80200 -26.73700 11.15700  1.000 34.88313 ? 602 TPP A C4     1 
HETATM 7992 C  CM4    . TPP D 3 .   ? -26.39200 -26.50700 11.58700  1.000 35.60427 ? 602 TPP A CM4    1 
HETATM 7993 C  C6     . TPP D 3 .   ? -28.48700 -28.65300 12.73400  1.000 28.16917 ? 602 TPP A C6     1 
HETATM 7994 C  C7     . TPP D 3 .   ? -29.21300 -28.18600 13.97000  1.000 29.71409 ? 602 TPP A C7     1 
HETATM 7995 O  O7     . TPP D 3 .   ? -28.92800 -29.07600 15.07000  1.000 23.53703 ? 602 TPP A O7     1 
HETATM 7996 P  PA     . TPP D 3 .   ? -29.83000 -29.16400 16.34400  1.000 26.63477 ? 602 TPP A PA     1 
HETATM 7997 O  O1A    . TPP D 3 .   ? -29.23400 -30.05000 17.36800  1.000 24.88983 ? 602 TPP A O1A    1 
HETATM 7998 O  O2A    . TPP D 3 .   ? -30.18500 -27.73800 16.75500  1.000 24.50031 ? 602 TPP A O2A    1 
HETATM 7999 O  O3A    . TPP D 3 .   ? -31.07600 -29.89900 15.72700  1.000 27.47435 ? 602 TPP A O3A    1 
HETATM 8000 P  PB     . TPP D 3 .   ? -31.44500 -31.34800 15.19300  1.000 28.35077 ? 602 TPP A PB     1 
HETATM 8001 O  O1B    . TPP D 3 .   ? -30.36000 -32.29400 15.56200  1.000 30.78001 ? 602 TPP A O1B    1 
HETATM 8002 O  O2B    . TPP D 3 .   ? -31.56700 -31.20800 13.66800  1.000 34.59362 ? 602 TPP A O2B    1 
HETATM 8003 O  O3B    . TPP D 3 .   ? -32.79500 -31.65700 15.87500  1.000 30.19836 ? 602 TPP A O3B    1 
HETATM 8004 H  HM21   . TPP D 3 .   ? -27.80200 -19.67000 12.69900  1.000 34.20000 ? 602 TPP A HM21   1 
HETATM 8005 H  HM22   . TPP D 3 .   ? -26.24900 -19.68100 12.38400  1.000 34.20000 ? 602 TPP A HM22   1 
HETATM 8006 H  HM23   . TPP D 3 .   ? -26.81000 -20.47900 13.63300  1.000 34.20000 ? 602 TPP A HM23   1 
HETATM 8007 H  HN41   . TPP D 3 .   ? -30.48000 -22.51500 10.52700  1.000 34.51000 ? 602 TPP A HN41   1 
HETATM 8008 H  HN42   . TPP D 3 .   ? -30.00200 -23.70700 9.76700   1.000 34.51000 ? 602 TPP A HN42   1 
HETATM 8009 H  "H6'"  . TPP D 3 .   ? -25.52500 -23.70900 10.55400  1.000 32.72000 ? 602 TPP A "H6'"  1 
HETATM 8010 H  "H7'1" . TPP D 3 .   ? -28.12700 -24.62100 8.66200   1.000 34.20000 ? 602 TPP A "H7'1" 1 
HETATM 8011 H  "H7'2" . TPP D 3 .   ? -26.76000 -25.18000 9.23700   1.000 34.20000 ? 602 TPP A "H7'2" 1 
HETATM 8012 H  H2     . TPP D 3 .   ? -30.14800 -25.87200 9.22200   1.000 43.93000 ? 602 TPP A H2     1 
HETATM 8013 H  HM41   . TPP D 3 .   ? -25.79700 -26.64400 10.83300  1.000 42.72000 ? 602 TPP A HM41   1 
HETATM 8014 H  HM42   . TPP D 3 .   ? -26.16400 -27.13000 12.29500  1.000 42.72000 ? 602 TPP A HM42   1 
HETATM 8015 H  HM43   . TPP D 3 .   ? -26.29700 -25.59900 11.91300  1.000 42.72000 ? 602 TPP A HM43   1 
HETATM 8016 H  H61    . TPP D 3 .   ? -28.84100 -29.51500 12.46400  1.000 33.80000 ? 602 TPP A H61    1 
HETATM 8017 H  H62    . TPP D 3 .   ? -27.54200 -28.74000 12.93400  1.000 33.80000 ? 602 TPP A H62    1 
HETATM 8018 H  H71    . TPP D 3 .   ? -30.16800 -28.18100 13.80000  1.000 35.66000 ? 602 TPP A H71    1 
HETATM 8019 H  H72    . TPP D 3 .   ? -28.91900 -27.29000 14.19700  1.000 35.66000 ? 602 TPP A H72    1 
HETATM 8020 MG MG     . MG  E 4 .   ? -29.38900 -31.97300 17.44100  1.000 26.28999 ? 603 MG  A MG     1 
HETATM 8021 P  PB     . ADP F 2 .   ? -2.09700  -0.70700  17.95900  1.000 24.71349 ? 601 ADP B PB     1 
HETATM 8022 O  O1B    . ADP F 2 .   ? -0.76100  -1.24000  18.44400  1.000 40.07323 ? 601 ADP B O1B    1 
HETATM 8023 O  O2B    . ADP F 2 .   ? -3.21800  -0.91200  18.95200  1.000 30.86686 ? 601 ADP B O2B    1 
HETATM 8024 O  O3B    . ADP F 2 .   ? -2.08300  0.68100   17.33000  1.000 28.84030 ? 601 ADP B O3B    1 
HETATM 8025 P  PA     . ADP F 2 .   ? -3.46900  -1.36900  15.54000  1.000 27.22958 ? 601 ADP B PA     1 
HETATM 8026 O  O1A    . ADP F 2 .   ? -3.97400  -2.66400  14.97300  1.000 25.93469 ? 601 ADP B O1A    1 
HETATM 8027 O  O2A    . ADP F 2 .   ? -4.44200  -0.28500  15.91600  1.000 24.20553 ? 601 ADP B O2A    1 
HETATM 8028 O  O3A    . ADP F 2 .   ? -2.50300  -1.73600  16.77300  1.000 32.21439 ? 601 ADP B O3A    1 
HETATM 8029 O  "O5'"  . ADP F 2 .   ? -2.50100  -0.73200  14.45800  1.000 26.14787 ? 601 ADP B "O5'"  1 
HETATM 8030 C  "C5'"  . ADP F 2 .   ? -1.65600  -1.62000  13.75600  1.000 32.09332 ? 601 ADP B "C5'"  1 
HETATM 8031 C  "C4'"  . ADP F 2 .   ? -0.92800  -0.79500  12.71900  1.000 27.36118 ? 601 ADP B "C4'"  1 
HETATM 8032 O  "O4'"  . ADP F 2 .   ? 0.14600   -1.57000  12.19000  1.000 28.54816 ? 601 ADP B "O4'"  1 
HETATM 8033 C  "C3'"  . ADP F 2 .   ? -1.79200  -0.32900  11.52800  1.000 24.52926 ? 601 ADP B "C3'"  1 
HETATM 8034 O  "O3'"  . ADP F 2 .   ? -1.59800  1.08600   11.48800  1.000 31.98541 ? 601 ADP B "O3'"  1 
HETATM 8035 C  "C2'"  . ADP F 2 .   ? -1.29100  -1.10700  10.31400  1.000 25.45042 ? 601 ADP B "C2'"  1 
HETATM 8036 O  "O2'"  . ADP F 2 .   ? -1.30900  -0.31100  9.13600   1.000 33.81721 ? 601 ADP B "O2'"  1 
HETATM 8037 C  "C1'"  . ADP F 2 .   ? 0.13300   -1.44600  10.75700  1.000 26.49791 ? 601 ADP B "C1'"  1 
HETATM 8038 N  N9     . ADP F 2 .   ? 0.68300   -2.67200  10.14300  1.000 22.24214 ? 601 ADP B N9     1 
HETATM 8039 C  C8     . ADP F 2 .   ? 0.08200   -3.85300  9.88100   1.000 23.37649 ? 601 ADP B C8     1 
HETATM 8040 N  N7     . ADP F 2 .   ? 0.96800   -4.71400  9.30700   1.000 25.30567 ? 601 ADP B N7     1 
HETATM 8041 C  C5     . ADP F 2 .   ? 2.14900   -4.06200  9.23400   1.000 27.28485 ? 601 ADP B C5     1 
HETATM 8042 C  C6     . ADP F 2 .   ? 3.50000   -4.35000  8.75400   1.000 26.70847 ? 601 ADP B C6     1 
HETATM 8043 N  N6     . ADP F 2 .   ? 3.70700   -5.55900  8.23500   1.000 27.74543 ? 601 ADP B N6     1 
HETATM 8044 N  N1     . ADP F 2 .   ? 4.46900   -3.41600  8.85700   1.000 30.73000 ? 601 ADP B N1     1 
HETATM 8045 C  C2     . ADP F 2 .   ? 4.21100   -2.20500  9.37400   1.000 29.41932 ? 601 ADP B C2     1 
HETATM 8046 N  N3     . ADP F 2 .   ? 2.99500   -1.86400  9.83500   1.000 27.48487 ? 601 ADP B N3     1 
HETATM 8047 C  C4     . ADP F 2 .   ? 1.95700   -2.73400  9.80200   1.000 23.62652 ? 601 ADP B C4     1 
HETATM 8048 H  "H5'1" . ADP F 2 .   ? -2.24000  -2.41000  13.27800  1.000 38.51000 ? 601 ADP B "H5'1" 1 
HETATM 8049 H  "H5'2" . ADP F 2 .   ? -0.94600  -2.09400  14.43700  1.000 38.51000 ? 601 ADP B "H5'2" 1 
HETATM 8050 H  "H4'"  . ADP F 2 .   ? -0.59100  0.11000   13.24300  1.000 32.83000 ? 601 ADP B "H4'"  1 
HETATM 8051 H  "H3'"  . ADP F 2 .   ? -2.87400  -0.51200  11.58300  1.000 29.44000 ? 601 ADP B "H3'"  1 
HETATM 8052 H  "HO3'" . ADP F 2 .   ? -0.65400  1.28400   11.56300  1.000 38.38000 ? 601 ADP B "HO3'" 1 
HETATM 8053 H  "H2'"  . ADP F 2 .   ? -1.90100  -1.98100  10.04500  1.000 30.54000 ? 601 ADP B "H2'"  1 
HETATM 8054 H  "HO2'" . ADP F 2 .   ? -1.41300  0.61900   9.37700   1.000 40.58000 ? 601 ADP B "HO2'" 1 
HETATM 8055 H  "H1'"  . ADP F 2 .   ? 0.76800   -0.61900  10.40800  1.000 31.80000 ? 601 ADP B "H1'"  1 
HETATM 8056 H  H8     . ADP F 2 .   ? -0.95500  -4.08300  10.09600  1.000 28.05000 ? 601 ADP B H8     1 
HETATM 8057 H  HN61   . ADP F 2 .   ? 4.60600   -5.81800  7.90000   1.000 33.30000 ? 601 ADP B HN61   1 
HETATM 8058 H  HN62   . ADP F 2 .   ? 2.94000   -6.20500  8.20700   1.000 33.30000 ? 601 ADP B HN62   1 
HETATM 8059 H  H2     . ADP F 2 .   ? 5.01000   -1.47600  9.42100   1.000 35.30000 ? 601 ADP B H2     1 
HETATM 8060 N  "N1'"  . TPP G 3 .   ? -20.88100 -6.14400  24.21500  1.000 26.33737 ? 602 TPP B "N1'"  1 
HETATM 8061 C  "C2'"  . TPP G 3 .   ? -19.79400 -6.63200  23.58100  1.000 25.37673 ? 602 TPP B "C2'"  1 
HETATM 8062 C  CM2    . TPP G 3 .   ? -20.00500 -7.75100  22.61600  1.000 23.31595 ? 602 TPP B CM2    1 
HETATM 8063 N  "N3'"  . TPP G 3 .   ? -18.54200 -6.21100  23.75600  1.000 25.29514 ? 602 TPP B "N3'"  1 
HETATM 8064 C  "C4'"  . TPP G 3 .   ? -18.33400 -5.21100  24.63000  1.000 26.85322 ? 602 TPP B "C4'"  1 
HETATM 8065 N  "N4'"  . TPP G 3 .   ? -17.08100 -4.78700  24.77300  1.000 25.86626 ? 602 TPP B "N4'"  1 
HETATM 8066 C  "C5'"  . TPP G 3 .   ? -19.41300 -4.63500  25.36600  1.000 25.41357 ? 602 TPP B "C5'"  1 
HETATM 8067 C  "C6'"  . TPP G 3 .   ? -20.65700 -5.15200  25.08400  1.000 26.98745 ? 602 TPP B "C6'"  1 
HETATM 8068 C  "C7'"  . TPP G 3 .   ? -19.22600 -3.53100  26.37100  1.000 32.61444 ? 602 TPP B "C7'"  1 
HETATM 8069 N  N3     . TPP G 3 .   ? -18.49200 -3.97300  27.59100  1.000 39.53632 ? 602 TPP B N3     1 
HETATM 8070 C  C2     . TPP G 3 .   ? -17.22600 -3.66100  27.84600  1.000 40.11270 ? 602 TPP B C2     1 
HETATM 8071 S  S1     . TPP G 3 .   ? -16.67100 -4.30000  29.30100  1.000 35.30950 ? 602 TPP B S1     1 
HETATM 8072 C  C5     . TPP G 3 .   ? -18.20200 -5.03700  29.59800  1.000 36.78336 ? 602 TPP B C5     1 
HETATM 8073 C  C4     . TPP G 3 .   ? -19.08500 -4.77300  28.57300  1.000 40.47854 ? 602 TPP B C4     1 
HETATM 8074 C  CM4    . TPP G 3 .   ? -20.50300 -5.21800  28.44200  1.000 41.04703 ? 602 TPP B CM4    1 
HETATM 8075 C  C6     . TPP G 3 .   ? -18.38400 -5.89200  30.81900  1.000 32.50127 ? 602 TPP B C6     1 
HETATM 8076 C  C7     . TPP G 3 .   ? -17.60700 -7.18200  30.70000  1.000 30.30100 ? 602 TPP B C7     1 
HETATM 8077 O  O7     . TPP G 3 .   ? -17.92300 -8.05800  31.80400  1.000 25.80836 ? 602 TPP B O7     1 
HETATM 8078 P  PA     . TPP G 3 .   ? -17.06300 -9.31900  32.18000  1.000 28.86925 ? 602 TPP B PA     1 
HETATM 8079 O  O1A    . TPP G 3 .   ? -17.76000 -10.09800 33.22700  1.000 30.24573 ? 602 TPP B O1A    1 
HETATM 8080 O  O2A    . TPP G 3 .   ? -16.64500 -10.05000 30.88900  1.000 26.23472 ? 602 TPP B O2A    1 
HETATM 8081 O  O3A    . TPP G 3 .   ? -15.81500 -8.60600  32.79100  1.000 25.34514 ? 602 TPP B O3A    1 
HETATM 8082 P  PB     . TPP G 3 .   ? -15.44100 -7.78500  34.09800  1.000 28.12706 ? 602 TPP B PB     1 
HETATM 8083 O  O1B    . TPP G 3 .   ? -16.53400 -7.92500  35.10700  1.000 30.01149 ? 602 TPP B O1B    1 
HETATM 8084 O  O2B    . TPP G 3 .   ? -15.26100 -6.35900  33.63100  1.000 29.20877 ? 602 TPP B O2B    1 
HETATM 8085 O  O3B    . TPP G 3 .   ? -14.10500 -8.39700  34.54000  1.000 32.73814 ? 602 TPP B O3B    1 
HETATM 8086 H  HM21   . TPP G 3 .   ? -19.20900 -7.86300  22.07200  1.000 27.98000 ? 602 TPP B HM21   1 
HETATM 8087 H  HM22   . TPP G 3 .   ? -20.76100 -7.54600  22.04400  1.000 27.98000 ? 602 TPP B HM22   1 
HETATM 8088 H  HM23   . TPP G 3 .   ? -20.18200 -8.57000  23.10400  1.000 27.98000 ? 602 TPP B HM23   1 
HETATM 8089 H  HN41   . TPP G 3 .   ? -16.45200 -5.15900  24.32100  1.000 31.04000 ? 602 TPP B HN41   1 
HETATM 8090 H  HN42   . TPP G 3 .   ? -16.90900 -4.12400  25.29200  1.000 31.04000 ? 602 TPP B HN42   1 
HETATM 8091 H  "H6'"  . TPP G 3 .   ? -21.38900 -4.78800  25.52700  1.000 32.38000 ? 602 TPP B "H6'"  1 
HETATM 8092 H  "H7'1" . TPP G 3 .   ? -18.72500 -2.81300  25.95300  1.000 39.14000 ? 602 TPP B "H7'1" 1 
HETATM 8093 H  "H7'2" . TPP G 3 .   ? -20.10000 -3.20400  26.63800  1.000 39.14000 ? 602 TPP B "H7'2" 1 
HETATM 8094 H  H2     . TPP G 3 .   ? -16.70100 -3.14400  27.27900  1.000 48.14000 ? 602 TPP B H2     1 
HETATM 8095 H  HM41   . TPP G 3 .   ? -21.08200 -4.44200  28.38900  1.000 49.25000 ? 602 TPP B HM41   1 
HETATM 8096 H  HM42   . TPP G 3 .   ? -20.74700 -5.75200  29.21400  1.000 49.25000 ? 602 TPP B HM42   1 
HETATM 8097 H  HM43   . TPP G 3 .   ? -20.60200 -5.75000  27.63700  1.000 49.25000 ? 602 TPP B HM43   1 
HETATM 8098 H  H61    . TPP G 3 .   ? -18.07200 -5.40500  31.59800  1.000 39.00000 ? 602 TPP B H61    1 
HETATM 8099 H  H62    . TPP G 3 .   ? -19.32600 -6.09800  30.92400  1.000 39.00000 ? 602 TPP B H62    1 
HETATM 8100 H  H71    . TPP G 3 .   ? -16.65700 -6.98600  30.70800  1.000 36.36000 ? 602 TPP B H71    1 
HETATM 8101 H  H72    . TPP G 3 .   ? -17.84000 -7.62100  29.86600  1.000 36.36000 ? 602 TPP B H72    1 
HETATM 8102 MG MG     . MG  H 4 .   ? -17.55100 -9.81900  35.22100  1.000 33.31189 ? 603 MG  B MG     1 
HETATM 8103 O  O      . HOH I 5 .   ? -31.15400 -27.95700 36.87200  1.000 36.44000 ? 701 HOH A O      1 
HETATM 8104 O  O      . HOH I 5 .   ? -34.19200 14.57900  30.62600  1.000 43.93000 ? 702 HOH A O      1 
HETATM 8105 O  O      . HOH I 5 .   ? -27.59300 -17.92000 16.59200  1.000 28.29000 ? 703 HOH A O      1 
HETATM 8106 O  O      . HOH I 5 .   ? -39.67600 -14.75200 13.65900  1.000 36.21000 ? 704 HOH A O      1 
HETATM 8107 O  O      . HOH I 5 .   ? -29.00000 -34.15600 31.02900  1.000 52.15000 ? 705 HOH A O      1 
HETATM 8108 O  O      . HOH I 5 .   ? -38.31000 3.30900   32.08500  1.000 35.73000 ? 706 HOH A O      1 
HETATM 8109 O  O      . HOH I 5 .   ? -16.19100 -0.33200  8.24100   1.000 27.80000 ? 707 HOH A O      1 
HETATM 8110 O  O      . HOH I 5 .   ? -41.52200 -11.92200 5.87900   1.000 25.85000 ? 708 HOH A O      1 
HETATM 8111 O  O      . HOH I 5 .   ? -48.27600 -30.53700 2.41100   1.000 43.05000 ? 709 HOH A O      1 
HETATM 8112 O  O      . HOH I 5 .   ? -58.22500 -30.88700 -4.78600  1.000 52.09000 ? 710 HOH A O      1 
HETATM 8113 O  O      . HOH I 5 .   ? -39.77700 4.41500   29.98300  1.000 42.68000 ? 711 HOH A O      1 
HETATM 8114 O  O      . HOH I 5 .   ? -61.75800 -3.09300  4.78000   1.000 45.01000 ? 712 HOH A O      1 
HETATM 8115 O  O      . HOH I 5 .   ? -23.96800 -4.06200  23.96400  1.000 27.18000 ? 713 HOH A O      1 
HETATM 8116 O  O      . HOH I 5 .   ? -54.93500 3.33300   4.41600   1.000 42.86000 ? 714 HOH A O      1 
HETATM 8117 O  O      . HOH I 5 .   ? -45.15900 -39.78400 33.89500  1.000 47.44000 ? 715 HOH A O      1 
HETATM 8118 O  O      . HOH I 5 .   ? -35.79800 -22.61200 37.64400  1.000 34.93000 ? 716 HOH A O      1 
HETATM 8119 O  O      . HOH I 5 .   ? -45.29300 -15.63500 -6.11600  1.000 35.31000 ? 717 HOH A O      1 
HETATM 8120 O  O      . HOH I 5 .   ? -10.69600 12.73600  12.12600  1.000 37.36000 ? 718 HOH A O      1 
HETATM 8121 O  O      . HOH I 5 .   ? -34.54100 -20.28700 37.63900  1.000 33.21000 ? 719 HOH A O      1 
HETATM 8122 O  O      . HOH I 5 .   ? -32.91400 -26.75900 16.78100  1.000 28.03000 ? 720 HOH A O      1 
HETATM 8123 O  O      . HOH I 5 .   ? -58.31800 -18.03900 12.04200  1.000 32.92000 ? 721 HOH A O      1 
HETATM 8124 O  O      . HOH I 5 .   ? -48.50100 2.56700   11.09500  1.000 50.38000 ? 722 HOH A O      1 
HETATM 8125 O  O      . HOH I 5 .   ? -48.01300 -17.52500 14.23600  1.000 35.74000 ? 723 HOH A O      1 
HETATM 8126 O  O      . HOH I 5 .   ? -44.58800 -33.88800 5.28100   1.000 33.45000 ? 724 HOH A O      1 
HETATM 8127 O  O      . HOH I 5 .   ? -18.71000 1.56400   4.87400   1.000 44.79000 ? 725 HOH A O      1 
HETATM 8128 O  O      . HOH I 5 .   ? -41.32000 -23.41800 33.97400  1.000 27.76000 ? 726 HOH A O      1 
HETATM 8129 O  O      . HOH I 5 .   ? -49.22300 0.78800   5.69400   1.000 36.94000 ? 727 HOH A O      1 
HETATM 8130 O  O      . HOH I 5 .   ? -41.19000 -18.05400 5.57800   1.000 37.39000 ? 728 HOH A O      1 
HETATM 8131 O  O      . HOH I 5 .   ? -44.47200 -8.82800  31.15700  1.000 27.23000 ? 729 HOH A O      1 
HETATM 8132 O  O      . HOH I 5 .   ? -40.24100 -6.62400  -1.12100  1.000 40.24000 ? 730 HOH A O      1 
HETATM 8133 O  O      . HOH I 5 .   ? -36.32100 14.78000  9.69200   1.000 36.54000 ? 731 HOH A O      1 
HETATM 8134 O  O      . HOH I 5 .   ? -25.81500 -32.81100 22.85800  1.000 27.15000 ? 732 HOH A O      1 
HETATM 8135 O  O      . HOH I 5 .   ? -22.12800 -27.33300 17.02200  1.000 29.30000 ? 733 HOH A O      1 
HETATM 8136 O  O      . HOH I 5 .   ? -49.53300 -13.02900 -0.38900  1.000 27.08000 ? 734 HOH A O      1 
HETATM 8137 O  O      . HOH I 5 .   ? -31.35600 -31.90000 18.21300  1.000 23.46000 ? 735 HOH A O      1 
HETATM 8138 O  O      . HOH I 5 .   ? -39.07600 -4.67400  23.41100  1.000 30.49000 ? 736 HOH A O      1 
HETATM 8139 O  O      . HOH I 5 .   ? -45.12100 -14.03200 -3.73800  1.000 24.74000 ? 737 HOH A O      1 
HETATM 8140 O  O      . HOH I 5 .   ? -22.98900 -12.00800 29.00600  1.000 29.48000 ? 738 HOH A O      1 
HETATM 8141 O  O      . HOH I 5 .   ? -36.89200 16.10900  15.82200  1.000 38.66000 ? 739 HOH A O      1 
HETATM 8142 O  O      . HOH I 5 .   ? -48.26800 -2.61300  8.34800   1.000 36.93000 ? 740 HOH A O      1 
HETATM 8143 O  O      . HOH I 5 .   ? -55.69800 -29.77200 10.32000  1.000 43.84000 ? 741 HOH A O      1 
HETATM 8144 O  O      . HOH I 5 .   ? -31.37100 -4.05000  28.45400  1.000 30.64000 ? 742 HOH A O      1 
HETATM 8145 O  O      . HOH I 5 .   ? -28.20000 6.16700   6.65600   1.000 38.10000 ? 743 HOH A O      1 
HETATM 8146 O  O      . HOH I 5 .   ? -43.50700 -20.95700 5.57700   1.000 28.11000 ? 744 HOH A O      1 
HETATM 8147 O  O      . HOH I 5 .   ? -35.30100 -41.09900 19.31300  1.000 44.49000 ? 745 HOH A O      1 
HETATM 8148 O  O      . HOH I 5 .   ? -44.94500 -18.84100 13.22200  1.000 29.92000 ? 746 HOH A O      1 
HETATM 8149 O  O      . HOH I 5 .   ? -27.39900 -15.68600 23.66100  1.000 38.12000 ? 747 HOH A O      1 
HETATM 8150 O  O      . HOH I 5 .   ? -40.29200 -8.69200  -6.46200  1.000 33.94000 ? 748 HOH A O      1 
HETATM 8151 O  O      . HOH I 5 .   ? -42.15800 -20.17100 -10.30500 1.000 39.94000 ? 749 HOH A O      1 
HETATM 8152 O  O      . HOH I 5 .   ? -31.17400 7.42800   35.92000  1.000 41.57000 ? 750 HOH A O      1 
HETATM 8153 O  O      . HOH I 5 .   ? -43.50500 -10.95700 12.22200  1.000 27.03000 ? 751 HOH A O      1 
HETATM 8154 O  O      . HOH I 5 .   ? -52.40700 -25.21900 9.45600   1.000 31.20000 ? 752 HOH A O      1 
HETATM 8155 O  O      . HOH I 5 .   ? -29.17100 10.13500  29.99300  1.000 39.47000 ? 753 HOH A O      1 
HETATM 8156 O  O      . HOH I 5 .   ? -33.85500 -7.99200  0.64100   1.000 39.73000 ? 754 HOH A O      1 
HETATM 8157 O  O      . HOH I 5 .   ? -48.83800 -13.22600 17.55900  1.000 45.89000 ? 755 HOH A O      1 
HETATM 8158 O  O      . HOH I 5 .   ? -47.57300 -5.17300  -7.56500  1.000 27.77000 ? 756 HOH A O      1 
HETATM 8159 O  O      . HOH I 5 .   ? -34.31600 -29.51200 16.55100  1.000 29.56000 ? 757 HOH A O      1 
HETATM 8160 O  O      . HOH I 5 .   ? -47.96800 -15.32600 -7.07900  1.000 36.30000 ? 758 HOH A O      1 
HETATM 8161 O  O      . HOH I 5 .   ? -34.93300 -17.54600 12.38700  1.000 26.79000 ? 759 HOH A O      1 
HETATM 8162 O  O      . HOH I 5 .   ? -24.77200 -10.42500 30.49700  1.000 31.24000 ? 760 HOH A O      1 
HETATM 8163 O  O      . HOH I 5 .   ? -36.28500 -15.73700 10.50700  1.000 31.74000 ? 761 HOH A O      1 
HETATM 8164 O  O      . HOH I 5 .   ? -52.94100 -21.82100 30.79900  1.000 53.49000 ? 762 HOH A O      1 
HETATM 8165 O  O      . HOH I 5 .   ? -47.40300 -16.92800 11.35000  1.000 25.63000 ? 763 HOH A O      1 
HETATM 8166 O  O      . HOH I 5 .   ? -52.57900 -23.29700 11.25900  1.000 30.53000 ? 764 HOH A O      1 
HETATM 8167 O  O      . HOH I 5 .   ? -64.70100 -19.33000 -10.30200 1.000 37.77000 ? 765 HOH A O      1 
HETATM 8168 O  O      . HOH I 5 .   ? -55.14800 -25.16100 8.24200   1.000 36.10000 ? 766 HOH A O      1 
HETATM 8169 O  O      . HOH I 5 .   ? -11.96600 6.33700   6.20000   1.000 53.56000 ? 767 HOH A O      1 
HETATM 8170 O  O      . HOH I 5 .   ? -45.46900 -6.86200  16.10800  1.000 32.70000 ? 768 HOH A O      1 
HETATM 8171 O  O      . HOH I 5 .   ? -23.41900 -2.36600  3.13900   1.000 39.47000 ? 769 HOH A O      1 
HETATM 8172 O  O      . HOH I 5 .   ? -18.72900 -0.29600  24.57800  1.000 30.39000 ? 770 HOH A O      1 
HETATM 8173 O  O      . HOH I 5 .   ? -16.01500 -37.57900 -1.78200  1.000 48.96000 ? 771 HOH A O      1 
HETATM 8174 O  O      . HOH I 5 .   ? -49.70500 3.72100   6.19400   1.000 39.58000 ? 772 HOH A O      1 
HETATM 8175 O  O      . HOH I 5 .   ? -32.08500 -19.37800 40.48000  1.000 52.48000 ? 773 HOH A O      1 
HETATM 8176 O  O      . HOH I 5 .   ? -15.86700 1.41800   5.96500   1.000 42.97000 ? 774 HOH A O      1 
HETATM 8177 O  O      . HOH I 5 .   ? -58.35200 -11.44100 14.32600  1.000 35.71000 ? 775 HOH A O      1 
HETATM 8178 O  O      . HOH I 5 .   ? -54.16900 -5.17800  10.17600  1.000 42.99000 ? 776 HOH A O      1 
HETATM 8179 O  O      . HOH I 5 .   ? -31.14300 -42.53200 9.28800   1.000 44.92000 ? 777 HOH A O      1 
HETATM 8180 O  O      . HOH I 5 .   ? -37.32700 9.31600   2.14800   1.000 48.31000 ? 778 HOH A O      1 
HETATM 8181 O  O      . HOH I 5 .   ? -46.05200 -0.56600  18.85500  1.000 23.58000 ? 779 HOH A O      1 
HETATM 8182 O  O      . HOH I 5 .   ? -55.46500 -28.86900 -7.09200  1.000 49.49000 ? 780 HOH A O      1 
HETATM 8183 O  O      . HOH I 5 .   ? -29.51200 -11.26000 33.04200  1.000 28.61000 ? 781 HOH A O      1 
HETATM 8184 O  O      . HOH I 5 .   ? -45.40000 -8.16200  11.84300  1.000 40.40000 ? 782 HOH A O      1 
HETATM 8185 O  O      . HOH I 5 .   ? -37.63200 17.68200  19.99500  1.000 36.27000 ? 783 HOH A O      1 
HETATM 8186 O  O      . HOH I 5 .   ? -31.51600 11.81500  30.60100  1.000 40.84000 ? 784 HOH A O      1 
HETATM 8187 O  O      . HOH I 5 .   ? -30.57700 -16.01600 38.44400  1.000 42.50000 ? 785 HOH A O      1 
HETATM 8188 O  O      . HOH I 5 .   ? -28.23400 -40.91100 18.46000  1.000 52.10000 ? 786 HOH A O      1 
HETATM 8189 O  O      . HOH I 5 .   ? -37.85900 11.86100  3.10500   1.000 44.36000 ? 787 HOH A O      1 
HETATM 8190 O  O      . HOH I 5 .   ? -16.92000 3.26800   22.23300  1.000 37.31000 ? 788 HOH A O      1 
HETATM 8191 O  O      . HOH I 5 .   ? -39.50500 -7.38100  6.01500   1.000 45.63000 ? 789 HOH A O      1 
HETATM 8192 O  O      . HOH I 5 .   ? -42.26400 -38.32200 5.62000   1.000 60.68000 ? 790 HOH A O      1 
HETATM 8193 O  O      . HOH I 5 .   ? -52.83800 -24.11800 20.10600  1.000 48.30000 ? 791 HOH A O      1 
HETATM 8194 O  O      . HOH I 5 .   ? -50.74500 -17.01600 12.95600  1.000 38.36000 ? 792 HOH A O      1 
HETATM 8195 O  O      . HOH I 5 .   ? -42.77400 -1.15100  3.58300   1.000 35.02000 ? 793 HOH A O      1 
HETATM 8196 O  O      . HOH I 5 .   ? -17.94200 14.81900  20.71300  1.000 56.17000 ? 794 HOH A O      1 
HETATM 8197 O  O      . HOH I 5 .   ? -35.52800 16.04800  18.94400  1.000 36.27000 ? 795 HOH A O      1 
HETATM 8198 O  O      . HOH I 5 .   ? -51.93400 -27.23600 22.95400  1.000 55.99000 ? 796 HOH A O      1 
HETATM 8199 O  O      . HOH I 5 .   ? -37.16100 -37.19200 34.96800  1.000 55.95000 ? 797 HOH A O      1 
HETATM 8200 O  O      . HOH I 5 .   ? -57.30800 -33.62600 0.79100   1.000 47.24000 ? 798 HOH A O      1 
HETATM 8201 O  O      . HOH I 5 .   ? -46.61200 -3.04500  15.57200  1.000 44.24000 ? 799 HOH A O      1 
HETATM 8202 O  O      . HOH I 5 .   ? -45.32300 -14.10100 -12.75900 1.000 44.32000 ? 800 HOH A O      1 
HETATM 8203 O  O      . HOH I 5 .   ? -25.48200 6.59900   22.68300  1.000 46.81000 ? 801 HOH A O      1 
HETATM 8204 O  O      . HOH I 5 .   ? -61.087   -0.580    9.176     1.000 56.71000 ? 802 HOH A O      1 
HETATM 8205 O  O      . HOH I 5 .   ? -35.72900 -17.72700 38.70800  1.000 35.35000 ? 803 HOH A O      1 
HETATM 8206 O  O      . HOH I 5 .   ? -40.17200 -5.01300  5.44700   1.000 37.71000 ? 804 HOH A O      1 
HETATM 8207 O  O      . HOH I 5 .   ? -26.55100 7.92500   8.66800   1.000 29.76000 ? 805 HOH A O      1 
HETATM 8208 O  O      . HOH I 5 .   ? -33.24000 11.25000  31.94200  1.000 58.02000 ? 806 HOH A O      1 
HETATM 8209 O  O      . HOH I 5 .   ? -23.53200 -38.28100 19.23200  1.000 49.84000 ? 807 HOH A O      1 
HETATM 8210 O  O      . HOH I 5 .   ? -25.70700 -44.00900 3.64200   1.000 47.66000 ? 808 HOH A O      1 
HETATM 8211 O  O      . HOH I 5 .   ? -40.10900 11.96700  10.59200  1.000 30.41000 ? 809 HOH A O      1 
HETATM 8212 O  O      . HOH I 5 .   ? -42.55100 -12.33700 -11.62000 1.000 31.09000 ? 810 HOH A O      1 
HETATM 8213 O  O      . HOH I 5 .   ? -25.54600 -19.33500 24.49100  1.000 38.38000 ? 811 HOH A O      1 
HETATM 8214 O  O      . HOH I 5 .   ? -33.81700 -35.80500 35.92100  1.000 58.28000 ? 812 HOH A O      1 
HETATM 8215 O  O      . HOH I 5 .   ? -28.69100 -24.21000 40.72000  1.000 57.42000 ? 813 HOH A O      1 
HETATM 8216 O  O      . HOH I 5 .   ? -40.69800 -15.45500 17.34300  1.000 51.55000 ? 814 HOH A O      1 
HETATM 8217 O  O      . HOH I 5 .   ? -38.17400 6.16000   6.17300   1.000 56.16000 ? 815 HOH A O      1 
HETATM 8218 O  O      . HOH I 5 .   ? -44.00300 -2.35600  2.12400   1.000 61.62000 ? 816 HOH A O      1 
HETATM 8219 O  O      . HOH I 5 .   ? -50.99900 -38.12800 31.26600  1.000 40.45000 ? 817 HOH A O      1 
HETATM 8220 O  O      . HOH I 5 .   ? -48.82900 -28.86000 35.56700  1.000 50.93000 ? 818 HOH A O      1 
HETATM 8221 O  O      . HOH I 5 .   ? -32.00100 0.27000   4.97700   1.000 34.84000 ? 819 HOH A O      1 
HETATM 8222 O  O      . HOH I 5 .   ? -25.32100 -12.85100 15.78000  1.000 46.24000 ? 820 HOH A O      1 
HETATM 8223 O  O      . HOH I 5 .   ? -63.02100 -0.16600  -7.66700  1.000 42.01000 ? 821 HOH A O      1 
HETATM 8224 O  O      . HOH I 5 .   ? -59.52300 -21.38900 18.11500  1.000 48.61000 ? 822 HOH A O      1 
HETATM 8225 O  O      . HOH I 5 .   ? -17.02900 10.89700  9.53200   1.000 41.42000 ? 823 HOH A O      1 
HETATM 8226 O  O      . HOH I 5 .   ? -31.39300 -30.88100 38.05600  1.000 52.26000 ? 824 HOH A O      1 
HETATM 8227 O  O      . HOH I 5 .   ? -36.45200 -43.34700 10.76200  1.000 57.80000 ? 825 HOH A O      1 
HETATM 8228 O  O      . HOH I 5 .   ? -7.88800  12.05200  11.88100  1.000 43.83000 ? 826 HOH A O      1 
HETATM 8229 O  O      . HOH I 5 .   ? -48.19300 -7.41700  25.07100  1.000 42.12000 ? 827 HOH A O      1 
HETATM 8230 O  O      . HOH I 5 .   ? -52.72500 -35.23700 6.49400   1.000 44.24000 ? 828 HOH A O      1 
HETATM 8231 O  O      . HOH I 5 .   ? -41.67900 21.64100  25.14700  1.000 61.35000 ? 829 HOH A O      1 
HETATM 8232 O  O      . HOH I 5 .   ? -40.14600 -17.51500 15.83100  1.000 46.97000 ? 830 HOH A O      1 
HETATM 8233 O  O      . HOH I 5 .   ? -40.51000 -43.80500 22.11800  1.000 47.74000 ? 831 HOH A O      1 
HETATM 8234 O  O      . HOH I 5 .   ? -48.85800 -5.11900  9.01900   1.000 35.31000 ? 832 HOH A O      1 
HETATM 8235 O  O      . HOH I 5 .   ? -28.85500 20.85600  22.04800  1.000 56.46000 ? 833 HOH A O      1 
HETATM 8236 O  O      . HOH I 5 .   ? -25.49700 -42.77000 13.59400  1.000 55.69000 ? 834 HOH A O      1 
HETATM 8237 O  O      . HOH I 5 .   ? -21.41000 -38.95500 -2.74000  1.000 60.36000 ? 835 HOH A O      1 
HETATM 8238 O  O      . HOH I 5 .   ? -45.40800 -14.74300 34.46500  1.000 56.33000 ? 836 HOH A O      1 
HETATM 8239 O  O      . HOH I 5 .   ? -62.844   1.198     -3.760    1.000 50.05000 ? 837 HOH A O      1 
HETATM 8240 O  O      . HOH I 5 .   ? -46.97900 -17.95000 34.27700  1.000 59.61000 ? 838 HOH A O      1 
HETATM 8241 O  O      . HOH I 5 .   ? -65.24500 -27.00700 12.88200  1.000 50.64000 ? 839 HOH A O      1 
HETATM 8242 O  O      . HOH I 5 .   ? -50.44500 0.79900   10.41900  1.000 61.17000 ? 840 HOH A O      1 
HETATM 8243 O  O      . HOH I 5 .   ? -17.42400 0.07800   27.07200  1.000 48.24000 ? 841 HOH A O      1 
HETATM 8244 O  O      . HOH I 5 .   ? -44.04100 11.96300  27.43100  1.000 42.80000 ? 842 HOH A O      1 
HETATM 8245 O  O      . HOH I 5 .   ? -51.46300 -32.99600 -10.72900 1.000 56.09000 ? 843 HOH A O      1 
HETATM 8246 O  O      . HOH I 5 .   ? -31.39500 3.06500   5.18100   1.000 31.89000 ? 844 HOH A O      1 
HETATM 8247 O  O      . HOH I 5 .   ? -45.13500 -31.84300 1.28200   1.000 47.03000 ? 845 HOH A O      1 
HETATM 8248 O  O      . HOH I 5 .   ? -28.96700 19.90400  18.17200  1.000 39.05000 ? 846 HOH A O      1 
HETATM 8249 O  O      . HOH I 5 .   ? -50.04200 -36.31200 6.88600   1.000 46.04000 ? 847 HOH A O      1 
HETATM 8250 O  O      . HOH I 5 .   ? -46.83800 -7.33200  28.44100  1.000 64.44000 ? 848 HOH A O      1 
HETATM 8251 O  O      . HOH I 5 .   ? -32.70300 19.27600  29.70500  1.000 55.18000 ? 849 HOH A O      1 
HETATM 8252 O  O      . HOH I 5 .   ? -45.99300 -10.29900 13.28700  1.000 42.65000 ? 850 HOH A O      1 
HETATM 8253 O  O      . HOH I 5 .   ? -64.53500 -21.67600 -11.30300 1.000 55.84000 ? 851 HOH A O      1 
HETATM 8254 O  O      . HOH I 5 .   ? -47.79200 -22.02900 36.95300  1.000 50.18000 ? 852 HOH A O      1 
HETATM 8255 O  O      . HOH I 5 .   ? -44.73300 9.35800   27.15500  1.000 50.70000 ? 853 HOH A O      1 
HETATM 8256 O  O      . HOH I 5 .   ? -27.50500 -43.61700 17.58000  1.000 67.55000 ? 854 HOH A O      1 
HETATM 8257 O  O      . HOH I 5 .   ? -49.31000 -0.81200  14.77800  1.000 63.97000 ? 855 HOH A O      1 
HETATM 8258 O  O      . HOH I 5 .   ? -41.12600 -29.12500 -7.77000  1.000 59.07000 ? 856 HOH A O      1 
HETATM 8259 O  O      . HOH I 5 .   ? -40.51000 -20.60200 4.87200   1.000 39.31000 ? 857 HOH A O      1 
HETATM 8260 O  O      . HOH I 5 .   ? -27.55100 10.80300  8.38100   1.000 46.47000 ? 858 HOH A O      1 
HETATM 8261 O  O      . HOH I 5 .   ? -49.28000 -0.82200  17.49200  1.000 62.97000 ? 859 HOH A O      1 
HETATM 8262 O  O      . HOH I 5 .   ? -13.463   4.548     3.938     1.000 61.45000 ? 860 HOH A O      1 
HETATM 8263 O  O      . HOH I 5 .   ? -46.68700 -6.23700  13.60600  1.000 45.95000 ? 861 HOH A O      1 
HETATM 8264 O  O      . HOH I 5 .   ? -31.64400 11.78000  33.94800  1.000 54.66000 ? 862 HOH A O      1 
HETATM 8265 O  O      . HOH I 5 .   ? -58.60600 -18.54300 14.99000  1.000 55.92000 ? 863 HOH A O      1 
HETATM 8266 O  O      . HOH I 5 .   ? -50.701   -40.067   28.941    1.000 51.35000 ? 864 HOH A O      1 
HETATM 8267 O  O      . HOH I 5 .   ? -39.31400 -29.12000 -9.74600  1.000 58.65000 ? 865 HOH A O      1 
HETATM 8268 O  O      . HOH J 5 .   ? -11.31300 -9.72700  44.24700  1.000 48.71000 ? 701 HOH B O      1 
HETATM 8269 O  O      . HOH J 5 .   ? 10.64400  5.72900   2.91000   1.000 40.87000 ? 702 HOH B O      1 
HETATM 8270 O  O      . HOH J 5 .   ? 9.43800   9.54200   3.46200   1.000 48.24000 ? 703 HOH B O      1 
HETATM 8271 O  O      . HOH J 5 .   ? -2.60000  -28.29600 15.49600  1.000 30.69000 ? 704 HOH B O      1 
HETATM 8272 O  O      . HOH J 5 .   ? -21.47900 6.19000   43.45900  1.000 46.45000 ? 705 HOH B O      1 
HETATM 8273 O  O      . HOH J 5 .   ? -13.08100 -33.19200 -7.46700  1.000 47.50000 ? 706 HOH B O      1 
HETATM 8274 O  O      . HOH J 5 .   ? -8.73800  -31.97900 3.79800   1.000 43.50000 ? 707 HOH B O      1 
HETATM 8275 O  O      . HOH J 5 .   ? -5.64600  -27.81900 30.58400  1.000 38.83000 ? 708 HOH B O      1 
HETATM 8276 O  O      . HOH J 5 .   ? -22.99500 -22.14600 9.38500   1.000 24.62000 ? 709 HOH B O      1 
HETATM 8277 O  O      . HOH J 5 .   ? -5.35900  -2.93200  12.91300  1.000 25.81000 ? 710 HOH B O      1 
HETATM 8278 O  O      . HOH J 5 .   ? -7.02900  -9.84300  17.61400  1.000 34.67000 ? 711 HOH B O      1 
HETATM 8279 O  O      . HOH J 5 .   ? -5.70900  -1.38700  18.78700  1.000 28.30000 ? 712 HOH B O      1 
HETATM 8280 O  O      . HOH J 5 .   ? -13.89700 -10.22500 29.94700  1.000 31.89000 ? 713 HOH B O      1 
HETATM 8281 O  O      . HOH J 5 .   ? -26.63900 -30.54900 0.86200   1.000 52.84000 ? 714 HOH B O      1 
HETATM 8282 O  O      . HOH J 5 .   ? -30.53300 10.50200  36.55800  1.000 49.05000 ? 715 HOH B O      1 
HETATM 8283 O  O      . HOH J 5 .   ? -24.67400 -31.88100 39.00000  1.000 57.52000 ? 716 HOH B O      1 
HETATM 8284 O  O      . HOH J 5 .   ? -1.82000  6.87200   12.74300  1.000 29.24000 ? 717 HOH B O      1 
HETATM 8285 O  O      . HOH J 5 .   ? -7.09900  -30.32600 2.37100   1.000 42.41000 ? 718 HOH B O      1 
HETATM 8286 O  O      . HOH J 5 .   ? 7.30300   -8.59600  7.65600   1.000 40.22000 ? 719 HOH B O      1 
HETATM 8287 O  O      . HOH J 5 .   ? -9.17700  -9.63300  23.52900  1.000 36.05000 ? 720 HOH B O      1 
HETATM 8288 O  O      . HOH J 5 .   ? 2.49900   3.22600   12.70400  1.000 35.58000 ? 721 HOH B O      1 
HETATM 8289 O  O      . HOH J 5 .   ? -18.82900 -7.68600  -4.34600  1.000 48.72000 ? 722 HOH B O      1 
HETATM 8290 O  O      . HOH J 5 .   ? 1.47500   4.35400   30.26800  1.000 43.87000 ? 723 HOH B O      1 
HETATM 8291 O  O      . HOH J 5 .   ? 2.68900   -7.23600  -1.95500  1.000 45.27000 ? 724 HOH B O      1 
HETATM 8292 O  O      . HOH J 5 .   ? -28.30700 -5.11700  -0.45100  1.000 39.71000 ? 725 HOH B O      1 
HETATM 8293 O  O      . HOH J 5 .   ? -12.80500 6.99000   22.04500  1.000 35.02000 ? 726 HOH B O      1 
HETATM 8294 O  O      . HOH J 5 .   ? -11.92400 -8.16000  20.07500  1.000 24.22000 ? 727 HOH B O      1 
HETATM 8295 O  O      . HOH J 5 .   ? -6.71900  2.40700   6.08600   1.000 44.20000 ? 728 HOH B O      1 
HETATM 8296 O  O      . HOH J 5 .   ? -1.50400  9.41900   13.69600  1.000 36.30000 ? 729 HOH B O      1 
HETATM 8297 O  O      . HOH J 5 .   ? -11.02600 -31.61900 30.54400  1.000 36.32000 ? 730 HOH B O      1 
HETATM 8298 O  O      . HOH J 5 .   ? -3.96300  -16.24600 -10.79400 1.000 47.66000 ? 731 HOH B O      1 
HETATM 8299 O  O      . HOH J 5 .   ? 1.06700   10.28200  13.12800  1.000 33.49000 ? 732 HOH B O      1 
HETATM 8300 O  O      . HOH J 5 .   ? -15.62700 -10.45800 35.25100  1.000 26.12000 ? 733 HOH B O      1 
HETATM 8301 O  O      . HOH J 5 .   ? -30.51200 -7.86600  2.24300   1.000 29.96000 ? 734 HOH B O      1 
HETATM 8302 O  O      . HOH J 5 .   ? 31.053    6.767     10.573    1.000 51.18000 ? 735 HOH B O      1 
HETATM 8303 O  O      . HOH J 5 .   ? 4.32300   -16.14300 20.71200  1.000 50.79000 ? 736 HOH B O      1 
HETATM 8304 O  O      . HOH J 5 .   ? -10.16400 -19.26000 -12.18400 1.000 38.25000 ? 737 HOH B O      1 
HETATM 8305 O  O      . HOH J 5 .   ? 7.12800   11.37500  23.24900  1.000 40.88000 ? 738 HOH B O      1 
HETATM 8306 O  O      . HOH J 5 .   ? 8.00000   -5.29300  -2.33200  1.000 43.56000 ? 739 HOH B O      1 
HETATM 8307 O  O      . HOH J 5 .   ? -17.51900 -29.47200 18.27800  1.000 28.85000 ? 740 HOH B O      1 
HETATM 8308 O  O      . HOH J 5 .   ? 3.85900   -9.01700  19.47300  1.000 43.69000 ? 741 HOH B O      1 
HETATM 8309 O  O      . HOH J 5 .   ? -24.06100 -25.52800 18.09700  1.000 29.92000 ? 742 HOH B O      1 
HETATM 8310 O  O      . HOH J 5 .   ? -15.67500 -26.85100 10.13600  1.000 34.21000 ? 743 HOH B O      1 
HETATM 8311 O  O      . HOH J 5 .   ? -10.68100 -6.70400  17.69000  1.000 33.31000 ? 744 HOH B O      1 
HETATM 8312 O  O      . HOH J 5 .   ? 11.35200  -7.69500  20.33700  1.000 29.64000 ? 745 HOH B O      1 
HETATM 8313 O  O      . HOH J 5 .   ? 1.16200   -9.81800  20.30600  1.000 37.18000 ? 746 HOH B O      1 
HETATM 8314 O  O      . HOH J 5 .   ? -24.97500 -11.47400 -1.30200  1.000 27.98000 ? 747 HOH B O      1 
HETATM 8315 O  O      . HOH J 5 .   ? 0.68200   8.63400   3.31100   1.000 31.01000 ? 748 HOH B O      1 
HETATM 8316 O  O      . HOH J 5 .   ? -9.57400  -23.55000 -12.76600 1.000 33.02000 ? 749 HOH B O      1 
HETATM 8317 O  O      . HOH J 5 .   ? -1.98500  -8.56600  21.41900  1.000 29.40000 ? 750 HOH B O      1 
HETATM 8318 O  O      . HOH J 5 .   ? -0.91100  -18.19300 4.84500   1.000 33.69000 ? 751 HOH B O      1 
HETATM 8319 O  O      . HOH J 5 .   ? -28.10900 -23.74900 5.79800   1.000 28.23000 ? 752 HOH B O      1 
HETATM 8320 O  O      . HOH J 5 .   ? -15.96700 -32.32200 -4.77800  1.000 47.31000 ? 753 HOH B O      1 
HETATM 8321 O  O      . HOH J 5 .   ? -3.36900  -9.26800  13.37500  1.000 27.49000 ? 754 HOH B O      1 
HETATM 8322 O  O      . HOH J 5 .   ? -12.63900 -9.48900  32.48500  1.000 36.56000 ? 755 HOH B O      1 
HETATM 8323 O  O      . HOH J 5 .   ? -17.81200 -31.49700 -2.98200  1.000 48.64000 ? 756 HOH B O      1 
HETATM 8324 O  O      . HOH J 5 .   ? 2.13800   -7.58100  7.10200   1.000 38.18000 ? 757 HOH B O      1 
HETATM 8325 O  O      . HOH J 5 .   ? -7.86300  -21.68800 9.96000   1.000 28.25000 ? 758 HOH B O      1 
HETATM 8326 O  O      . HOH J 5 .   ? 2.12200   -5.80000  0.40900   1.000 35.34000 ? 759 HOH B O      1 
HETATM 8327 O  O      . HOH J 5 .   ? -12.95100 1.23500   7.98000   1.000 39.56000 ? 760 HOH B O      1 
HETATM 8328 O  O      . HOH J 5 .   ? -3.42500  -0.72100  21.70900  1.000 28.63000 ? 761 HOH B O      1 
HETATM 8329 O  O      . HOH J 5 .   ? 2.59100   -12.49500 11.99800  1.000 42.91000 ? 762 HOH B O      1 
HETATM 8330 O  O      . HOH J 5 .   ? -11.20800 0.12000   19.92400  1.000 39.55000 ? 763 HOH B O      1 
HETATM 8331 O  O      . HOH J 5 .   ? 5.81300   -5.74900  25.22800  1.000 37.12000 ? 764 HOH B O      1 
HETATM 8332 O  O      . HOH J 5 .   ? -1.66900  -14.20000 10.18200  1.000 33.77000 ? 765 HOH B O      1 
HETATM 8333 O  O      . HOH J 5 .   ? -21.18800 -14.79000 37.23500  1.000 29.43000 ? 766 HOH B O      1 
HETATM 8334 O  O      . HOH J 5 .   ? -29.96400 -22.27200 2.00700   1.000 38.61000 ? 767 HOH B O      1 
HETATM 8335 O  O      . HOH J 5 .   ? -7.47900  -4.12800  8.57500   1.000 40.62000 ? 768 HOH B O      1 
HETATM 8336 O  O      . HOH J 5 .   ? 0.97100   -10.00700 8.22200   1.000 60.48000 ? 769 HOH B O      1 
HETATM 8337 O  O      . HOH J 5 .   ? -6.61000  8.32600   7.01100   1.000 36.98000 ? 770 HOH B O      1 
HETATM 8338 O  O      . HOH J 5 .   ? -6.94800  3.48000   15.64400  1.000 46.45000 ? 771 HOH B O      1 
HETATM 8339 O  O      . HOH J 5 .   ? -29.09100 -18.15100 38.12600  1.000 40.86000 ? 772 HOH B O      1 
HETATM 8340 O  O      . HOH J 5 .   ? 5.52700   -3.54500  26.65400  1.000 30.45000 ? 773 HOH B O      1 
HETATM 8341 O  O      . HOH J 5 .   ? -16.97800 -17.21800 -16.39400 1.000 50.91000 ? 774 HOH B O      1 
HETATM 8342 O  O      . HOH J 5 .   ? -19.28000 -19.15700 20.68600  1.000 36.43000 ? 775 HOH B O      1 
HETATM 8343 O  O      . HOH J 5 .   ? 15.12600  -3.91300  4.14200   1.000 47.02000 ? 776 HOH B O      1 
HETATM 8344 O  O      . HOH J 5 .   ? 0.38000   -7.33400  19.08700  1.000 34.69000 ? 777 HOH B O      1 
HETATM 8345 O  O      . HOH J 5 .   ? 2.39500   -14.33300 16.32200  1.000 42.56000 ? 778 HOH B O      1 
HETATM 8346 O  O      . HOH J 5 .   ? -23.55400 -10.24500 41.55400  1.000 43.27000 ? 779 HOH B O      1 
HETATM 8347 O  O      . HOH J 5 .   ? 1.52400   -7.64900  4.39300   1.000 44.51000 ? 780 HOH B O      1 
HETATM 8348 O  O      . HOH J 5 .   ? -20.58900 9.37700   39.85300  1.000 62.04000 ? 781 HOH B O      1 
HETATM 8349 O  O      . HOH J 5 .   ? 5.09200   17.57700  28.68700  1.000 52.78000 ? 782 HOH B O      1 
HETATM 8350 O  O      . HOH J 5 .   ? -27.29400 -10.71000 -5.06000  1.000 35.07000 ? 783 HOH B O      1 
HETATM 8351 O  O      . HOH J 5 .   ? 1.46800   -11.20300 -0.32200  1.000 52.65000 ? 784 HOH B O      1 
HETATM 8352 O  O      . HOH J 5 .   ? 1.93600   -28.03800 36.51700  1.000 51.36000 ? 785 HOH B O      1 
HETATM 8353 O  O      . HOH J 5 .   ? -20.13800 -22.15700 -13.59800 1.000 36.73000 ? 786 HOH B O      1 
HETATM 8354 O  O      . HOH J 5 .   ? 6.37000   -12.88400 -5.45300  1.000 52.16000 ? 787 HOH B O      1 
HETATM 8355 O  O      . HOH J 5 .   ? -30.94000 -6.13800  -0.00200  1.000 41.01000 ? 788 HOH B O      1 
HETATM 8356 O  O      . HOH J 5 .   ? 5.41200   -19.72300 -2.95400  1.000 45.73000 ? 789 HOH B O      1 
HETATM 8357 O  O      . HOH J 5 .   ? -7.25000  2.09200   12.25500  1.000 49.57000 ? 790 HOH B O      1 
HETATM 8358 O  O      . HOH J 5 .   ? -7.97800  2.47100   20.86100  1.000 39.80000 ? 791 HOH B O      1 
HETATM 8359 O  O      . HOH J 5 .   ? 8.15000   -2.55600  26.39100  1.000 29.32000 ? 792 HOH B O      1 
HETATM 8360 O  O      . HOH J 5 .   ? -4.69400  -33.63900 23.61600  1.000 41.85000 ? 793 HOH B O      1 
HETATM 8361 O  O      . HOH J 5 .   ? -19.11500 -20.46000 40.86200  1.000 58.86000 ? 794 HOH B O      1 
HETATM 8362 O  O      . HOH J 5 .   ? -29.865   -11.705   -8.412    1.000 50.15000 ? 795 HOH B O      1 
HETATM 8363 O  O      . HOH J 5 .   ? -4.37500  -14.14300 -9.21600  1.000 37.57000 ? 796 HOH B O      1 
HETATM 8364 O  O      . HOH J 5 .   ? 15.91600  3.41500   -2.04500  1.000 49.50000 ? 797 HOH B O      1 
HETATM 8365 O  O      . HOH J 5 .   ? -11.70200 -22.04000 -11.37300 1.000 32.89000 ? 798 HOH B O      1 
HETATM 8366 O  O      . HOH J 5 .   ? -4.25600  -30.25900 9.55800   1.000 54.99000 ? 799 HOH B O      1 
HETATM 8367 O  O      . HOH J 5 .   ? -8.43500  -7.40600  -4.69700  1.000 42.75000 ? 800 HOH B O      1 
HETATM 8368 O  O      . HOH J 5 .   ? 3.15700   -21.21800 12.03100  1.000 47.91000 ? 801 HOH B O      1 
HETATM 8369 O  O      . HOH J 5 .   ? -12.12300 -32.14200 28.07300  1.000 36.44000 ? 802 HOH B O      1 
HETATM 8370 O  O      . HOH J 5 .   ? -18.02600 -22.05300 -14.97700 1.000 39.01000 ? 803 HOH B O      1 
HETATM 8371 O  O      . HOH J 5 .   ? -11.27500 -33.51500 26.07800  1.000 44.18000 ? 804 HOH B O      1 
HETATM 8372 O  O      . HOH J 5 .   ? -15.73600 -36.89000 0.88400   1.000 42.54000 ? 805 HOH B O      1 
HETATM 8373 O  O      . HOH J 5 .   ? -10.38100 -26.16500 43.62900  1.000 63.35000 ? 806 HOH B O      1 
HETATM 8374 O  O      . HOH J 5 .   ? -21.78300 -36.62300 -3.87400  1.000 53.00000 ? 807 HOH B O      1 
HETATM 8375 O  O      . HOH J 5 .   ? -6.79500  -13.03600 -9.38000  1.000 32.57000 ? 808 HOH B O      1 
HETATM 8376 O  O      . HOH J 5 .   ? -10.034   -12.037   -9.593    1.000 49.11000 ? 809 HOH B O      1 
HETATM 8377 O  O      . HOH J 5 .   ? -14.17700 -33.18700 12.80900  1.000 40.91000 ? 810 HOH B O      1 
HETATM 8378 O  O      . HOH J 5 .   ? -21.44500 -19.33000 24.70100  1.000 30.29000 ? 811 HOH B O      1 
HETATM 8379 O  O      . HOH J 5 .   ? -18.08100 -25.96900 -15.49000 1.000 52.55000 ? 812 HOH B O      1 
HETATM 8380 O  O      . HOH J 5 .   ? -3.60900  -35.33600 -5.21600  1.000 57.80000 ? 813 HOH B O      1 
HETATM 8381 O  O      . HOH J 5 .   ? -2.337    -27.497   -10.476   1.000 38.07000 ? 814 HOH B O      1 
HETATM 8382 O  O      . HOH J 5 .   ? -20.33500 -10.12200 -5.79500  1.000 32.50000 ? 815 HOH B O      1 
HETATM 8383 O  O      . HOH J 5 .   ? -6.20800  -13.04000 19.10000  1.000 47.26000 ? 816 HOH B O      1 
HETATM 8384 O  O      . HOH J 5 .   ? -29.35500 -26.47200 6.13400   1.000 44.36000 ? 817 HOH B O      1 
HETATM 8385 O  O      . HOH J 5 .   ? -0.15500  -14.04700 6.44200   1.000 48.73000 ? 818 HOH B O      1 
HETATM 8386 O  O      . HOH J 5 .   ? -31.22700 -0.11600  39.57300  1.000 37.41000 ? 819 HOH B O      1 
HETATM 8387 O  O      . HOH J 5 .   ? 8.64700   -3.08200  31.58700  1.000 47.84000 ? 820 HOH B O      1 
HETATM 8388 O  O      . HOH J 5 .   ? -15.16700 -5.06400  0.77100   1.000 39.61000 ? 821 HOH B O      1 
HETATM 8389 O  O      . HOH J 5 .   ? -6.89400  -4.32800  6.27400   1.000 40.59000 ? 822 HOH B O      1 
HETATM 8390 O  O      . HOH J 5 .   ? -29.30100 -23.74500 -9.49900  1.000 57.17000 ? 823 HOH B O      1 
HETATM 8391 O  O      . HOH J 5 .   ? 22.09100  -1.63100  24.56300  1.000 53.91000 ? 824 HOH B O      1 
HETATM 8392 O  O      . HOH J 5 .   ? 5.54900   17.12500  25.81500  1.000 55.40000 ? 825 HOH B O      1 
HETATM 8393 O  O      . HOH J 5 .   ? -15.51000 -5.83200  -1.94400  1.000 38.26000 ? 826 HOH B O      1 
HETATM 8394 O  O      . HOH J 5 .   ? -12.60500 -27.05700 43.07400  1.000 46.06000 ? 827 HOH B O      1 
HETATM 8395 O  O      . HOH J 5 .   ? 16.09100  -0.03300  1.33600   1.000 45.41000 ? 828 HOH B O      1 
HETATM 8396 O  O      . HOH J 5 .   ? -7.48000  1.71000   18.13100  1.000 45.13000 ? 829 HOH B O      1 
HETATM 8397 O  O      . HOH J 5 .   ? -4.99900  4.23600   31.85900  1.000 56.73000 ? 830 HOH B O      1 
HETATM 8398 O  O      . HOH J 5 .   ? -10.78700 -0.43100  44.71800  1.000 59.98000 ? 831 HOH B O      1 
HETATM 8399 O  O      . HOH J 5 .   ? 25.16500  -1.93300  21.19800  1.000 61.85000 ? 832 HOH B O      1 
HETATM 8400 O  O      . HOH J 5 .   ? -7.31100  -4.96600  -8.41300  1.000 51.52000 ? 833 HOH B O      1 
HETATM 8401 O  O      . HOH J 5 .   ? -24.87500 -7.88900  -3.65900  1.000 50.24000 ? 834 HOH B O      1 
HETATM 8402 O  O      . HOH J 5 .   ? -26.77800 -8.96500  43.36400  1.000 55.25000 ? 835 HOH B O      1 
HETATM 8403 O  O      . HOH J 5 .   ? 18.99600  6.47300   24.64000  1.000 51.40000 ? 836 HOH B O      1 
HETATM 8404 O  O      . HOH J 5 .   ? -34.86200 -7.20700  -4.60600  1.000 45.75000 ? 837 HOH B O      1 
HETATM 8405 O  O      . HOH J 5 .   ? -8.12700  -25.82900 43.95400  1.000 58.58000 ? 838 HOH B O      1 
HETATM 8406 O  O      . HOH J 5 .   ? -5.81400  14.24700  25.94200  1.000 54.44000 ? 839 HOH B O      1 
HETATM 8407 O  O      . HOH J 5 .   ? -1.07200  -25.99800 12.87300  1.000 48.97000 ? 840 HOH B O      1 
HETATM 8408 O  O      . HOH J 5 .   ? 5.87400   1.60500   36.00300  1.000 49.51000 ? 841 HOH B O      1 
HETATM 8409 O  O      . HOH J 5 .   ? -2.48000  -28.53500 -3.43000  1.000 65.53000 ? 842 HOH B O      1 
HETATM 8410 O  O      . HOH J 5 .   ? -38.942   -14.404   -9.323    1.000 45.33000 ? 843 HOH B O      1 
HETATM 8411 O  O      . HOH J 5 .   ? -2.99600  -29.63000 -5.33900  1.000 55.81000 ? 844 HOH B O      1 
HETATM 8412 O  O      . HOH J 5 .   ? -13.97600 -33.44400 -3.63200  1.000 56.24000 ? 845 HOH B O      1 
HETATM 8413 O  O      . HOH J 5 .   ? -31.87800 5.75900   42.51400  1.000 57.87000 ? 846 HOH B O      1 
HETATM 8414 O  O      . HOH J 5 .   ? 3.22900   1.47800   36.96600  1.000 45.32000 ? 847 HOH B O      1 
HETATM 8415 O  O      . HOH J 5 .   ? -18.35900 -5.28000  -1.99300  1.000 49.74000 ? 848 HOH B O      1 
HETATM 8416 O  O      . HOH J 5 .   ? 2.59100   -16.23200 18.85200  1.000 57.66000 ? 849 HOH B O      1 
HETATM 8417 O  O      . HOH J 5 .   ? -6.31400  -0.07400  21.19800  1.000 42.44000 ? 850 HOH B O      1 
HETATM 8418 O  O      . HOH J 5 .   ? -14.36700 -38.68600 2.43400   1.000 48.21000 ? 851 HOH B O      1 
HETATM 8419 O  O      . HOH J 5 .   ? 20.69200  6.83700   22.61000  1.000 50.77000 ? 852 HOH B O      1 
HETATM 8420 O  O      . HOH J 5 .   ? 4.846     18.457    23.693    1.000 61.04000 ? 853 HOH B O      1 
HETATM 8421 O  O      . HOH J 5 .   ? -2.74000  -30.19400 17.56300  1.000 49.84000 ? 854 HOH B O      1 
HETATM 8422 O  O      . HOH J 5 .   ? -0.13200  -11.70000 9.14900   1.000 54.84000 ? 855 HOH B O      1 
HETATM 8423 O  O      . HOH J 5 .   ? -12.58700 -35.12800 11.84400  1.000 68.20000 ? 856 HOH B O      1 
HETATM 8424 O  O      . HOH J 5 .   ? 24.35400  -4.83700  20.35200  1.000 63.66000 ? 857 HOH B O      1 
HETATM 8425 O  O      . HOH J 5 .   ? -24.54800 -12.04700 -4.00400  1.000 41.15000 ? 858 HOH B O      1 
HETATM 8426 O  O      . HOH J 5 .   ? -23.10000 -9.87500  -5.26000  1.000 39.76000 ? 859 HOH B O      1 
HETATM 8427 O  O      . HOH J 5 .   ? -23.375   -10.245   -8.189    1.000 47.86000 ? 860 HOH B 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 3   ? 0.93450 0.71390 1.02240 0.11340  0.02950  -0.14010 -1  SER A N     
2    C  CA    . SER A 3   ? 0.85310 0.63180 0.92140 0.10900  0.02960  -0.15120 -1  SER A CA    
3    C  C     . SER A 3   ? 0.82520 0.62010 0.88100 0.11120  0.03600  -0.15380 -1  SER A C     
4    O  O     . SER A 3   ? 0.84070 0.63410 0.88540 0.11320  0.04030  -0.16640 -1  SER A O     
5    C  CB    . SER A 3   ? 0.84570 0.60690 0.91350 0.11130  0.03070  -0.16610 -1  SER A CB    
6    O  OG    . SER A 3   ? 0.98950 0.75060 1.06210 0.12070  0.03890  -0.17400 -1  SER A OG    
7    N  N     . SER A 4   ? 0.71830 0.52880 0.77600 0.11080  0.03650  -0.14210 0   SER A N     
8    C  CA    . SER A 4   ? 0.70430 0.53080 0.75140 0.11240  0.04220  -0.14310 0   SER A CA    
9    C  C     . SER A 4   ? 0.72070 0.55280 0.74860 0.10440  0.03910  -0.14430 0   SER A C     
10   O  O     . SER A 4   ? 0.75110 0.57660 0.77530 0.09760  0.03230  -0.14260 0   SER A O     
11   C  CB    . SER A 4   ? 0.64490 0.48520 0.70270 0.11510  0.04400  -0.13020 0   SER A CB    
12   O  OG    . SER A 4   ? 0.83430 0.67430 0.89850 0.10980  0.03710  -0.11820 0   SER A OG    
13   N  N     . LYS A 5   ? 0.61010 0.45550 0.62630 0.10510  0.04400  -0.14640 1   LYS A N     
14   C  CA    . LYS A 5   ? 0.65910 0.51050 0.65750 0.09800  0.04120  -0.14710 1   LYS A CA    
15   C  C     . LYS A 5   ? 0.51110 0.36660 0.51060 0.09120  0.03460  -0.13490 1   LYS A C     
16   O  O     . LYS A 5   ? 0.52850 0.39060 0.53840 0.09200  0.03420  -0.12400 1   LYS A O     
17   C  CB    . LYS A 5   ? 0.65120 0.51780 0.63830 0.09960  0.04740  -0.14870 1   LYS A CB    
18   C  CG    . LYS A 5   ? 0.71270 0.59250 0.70920 0.10300  0.05090  -0.13840 1   LYS A CG    
19   C  CD    . LYS A 5   ? 0.85280 0.73740 0.84790 0.10970  0.05910  -0.14590 1   LYS A CD    
20   C  CE    . LYS A 5   ? 0.88530 0.75850 0.89520 0.11660  0.06130  -0.15080 1   LYS A CE    
21   N  NZ    . LYS A 5   ? 0.84750 0.72840 0.86250 0.12590  0.07130  -0.15600 1   LYS A NZ    
22   N  N     . THR A 6   ? 0.47200 0.32420 0.46000 0.08430  0.02960  -0.13720 2   THR A N     
23   C  CA    . THR A 6   ? 0.56850 0.42570 0.55410 0.07750  0.02380  -0.12730 2   THR A CA    
24   C  C     . THR A 6   ? 0.55280 0.42140 0.52220 0.07390  0.02470  -0.12780 2   THR A C     
25   O  O     . THR A 6   ? 0.55710 0.42700 0.51520 0.07510  0.02810  -0.13720 2   THR A O     
26   C  CB    . THR A 6   ? 0.59150 0.43600 0.57850 0.07220  0.01670  -0.12840 2   THR A CB    
27   O  OG1   . THR A 6   ? 0.62680 0.46640 0.60040 0.06950  0.01580  -0.13950 2   THR A OG1   
28   C  CG2   . THR A 6   ? 0.53960 0.37160 0.54250 0.07600  0.01620  -0.12900 2   THR A CG2   
29   N  N     . VAL A 7   ? 0.47930 0.35670 0.44820 0.06980  0.02200  -0.11740 3   VAL A N     
30   C  CA    . VAL A 7   ? 0.49630 0.38300 0.45140 0.06500  0.02100  -0.11580 3   VAL A CA    
31   C  C     . VAL A 7   ? 0.51480 0.39940 0.47070 0.05840  0.01390  -0.10870 3   VAL A C     
32   O  O     . VAL A 7   ? 0.57440 0.45240 0.54140 0.05770  0.01060  -0.10420 3   VAL A O     
33   C  CB    . VAL A 7   ? 0.47310 0.37440 0.42690 0.06710  0.02580  -0.10960 3   VAL A CB    
34   C  CG1   . VAL A 7   ? 0.44960 0.35450 0.40180 0.07340  0.03320  -0.11680 3   VAL A CG1   
35   C  CG2   . VAL A 7   ? 0.43100 0.33590 0.39820 0.06770  0.02480  -0.09850 3   VAL A CG2   
36   N  N     . THR A 8   ? 0.44870 0.33950 0.39310 0.05350  0.01170  -0.10740 4   THR A N     
37   C  CA    . THR A 8   ? 0.45500 0.34580 0.40090 0.04760  0.00570  -0.09980 4   THR A CA    
38   C  C     . THR A 8   ? 0.45100 0.34890 0.40550 0.04820  0.00640  -0.08890 4   THR A C     
39   O  O     . THR A 8   ? 0.43300 0.33910 0.38840 0.05160  0.01110  -0.08640 4   THR A O     
40   C  CB    . THR A 8   ? 0.45900 0.35550 0.39160 0.04260  0.00320  -0.10020 4   THR A CB    
41   O  OG1   . THR A 8   ? 0.50870 0.41710 0.43530 0.04390  0.00730  -0.09680 4   THR A OG1   
42   C  CG2   . THR A 8   ? 0.40230 0.29270 0.32490 0.04130  0.00190  -0.11100 4   THR A CG2   
43   N  N     . ALA A 9   ? 0.49850 0.39340 0.45930 0.04440  0.00170  -0.08230 5   ALA A N     
44   C  CA    . ALA A 9   ? 0.40690 0.30830 0.37490 0.04420  0.00180  -0.07220 5   ALA A CA    
45   C  C     . ALA A 9   ? 0.47950 0.39280 0.44000 0.04330  0.00420  -0.06840 5   ALA A C     
46   O  O     . ALA A 9   ? 0.42960 0.34990 0.39460 0.04540  0.00710  -0.06310 5   ALA A O     
47   C  CB    . ALA A 9   ? 0.34070 0.23830 0.31370 0.03950  -0.00360 -0.06630 5   ALA A CB    
48   N  N     . VAL A 10  ? 0.40490 0.32070 0.35450 0.03990  0.00270  -0.07070 6   VAL A N     
49   C  CA    . VAL A 10  ? 0.42610 0.35250 0.36930 0.03860  0.00440  -0.06630 6   VAL A CA    
50   C  C     . VAL A 10  ? 0.41370 0.34630 0.35340 0.04300  0.01040  -0.06950 6   VAL A C     
51   O  O     . VAL A 10  ? 0.48820 0.42960 0.42860 0.04370  0.01310  -0.06420 6   VAL A O     
52   C  CB    . VAL A 10  ? 0.49790 0.42530 0.43130 0.03380  0.00080  -0.06700 6   VAL A CB    
53   C  CG1   . VAL A 10  ? 0.39090 0.31540 0.31450 0.03410  0.00100  -0.07630 6   VAL A CG1   
54   C  CG2   . VAL A 10  ? 0.61410 0.55140 0.54320 0.03200  0.00170  -0.06060 6   VAL A CG2   
55   N  N     . GLU A 11  ? 0.37950 0.30760 0.31620 0.04610  0.01270  -0.07830 7   GLU A N     
56   C  CA    . GLU A 11  ? 0.48950 0.42390 0.42430 0.05080  0.01890  -0.08130 7   GLU A CA    
57   C  C     . GLU A 11  ? 0.47650 0.41320 0.42390 0.05500  0.02190  -0.07670 7   GLU A C     
58   O  O     . GLU A 11  ? 0.43270 0.37880 0.38060 0.05720  0.02630  -0.07390 7   GLU A O     
59   C  CB    . GLU A 11  ? 0.42600 0.35480 0.35490 0.05360  0.02120  -0.09250 7   GLU A CB    
60   C  CG    . GLU A 11  ? 0.56470 0.50140 0.49170 0.05870  0.02840  -0.09550 7   GLU A CG    
61   C  CD    . GLU A 11  ? 0.59160 0.52400 0.51100 0.06160  0.03150  -0.10730 7   GLU A CD    
62   O  OE1   . GLU A 11  ? 0.51280 0.44770 0.43590 0.06730  0.03760  -0.11080 7   GLU A OE1   
63   O  OE2   . GLU A 11  ? 0.60940 0.53640 0.51940 0.05820  0.02810  -0.11310 7   GLU A OE2   
64   N  N     . LEU A 12  ? 0.37490 0.30350 0.33300 0.05580  0.01950  -0.07540 8   LEU A N     
65   C  CA    . LEU A 12  ? 0.45940 0.39100 0.42990 0.05930  0.02150  -0.06980 8   LEU A CA    
66   C  C     . LEU A 12  ? 0.40450 0.34610 0.37550 0.05660  0.02120  -0.06050 8   LEU A C     
67   O  O     . LEU A 12  ? 0.34950 0.29940 0.32480 0.05930  0.02500  -0.05710 8   LEU A O     
68   C  CB    . LEU A 12  ? 0.46010 0.38170 0.44170 0.05970  0.01800  -0.06830 8   LEU A CB    
69   C  CG    . LEU A 12  ? 0.46050 0.38570 0.45530 0.06360  0.02000  -0.06230 8   LEU A CG    
70   C  CD1   . LEU A 12  ? 0.45140 0.37580 0.45090 0.07050  0.02530  -0.06850 8   LEU A CD1   
71   C  CD2   . LEU A 12  ? 0.43090 0.34960 0.43590 0.06200  0.01540  -0.05670 8   LEU A CD2   
72   N  N     . LEU A 13  ? 0.38570 0.32680 0.35270 0.05120  0.01680  -0.05650 9   LEU A N     
73   C  CA    . LEU A 13  ? 0.38840 0.33790 0.35520 0.04820  0.01630  -0.04840 9   LEU A CA    
74   C  C     . LEU A 13  ? 0.42330 0.38260 0.38320 0.04900  0.02050  -0.04850 9   LEU A C     
75   O  O     . LEU A 13  ? 0.41970 0.38690 0.38360 0.04930  0.02250  -0.04300 9   LEU A O     
76   C  CB    . LEU A 13  ? 0.35910 0.30570 0.32170 0.04270  0.01130  -0.04560 9   LEU A CB    
77   C  CG    . LEU A 13  ? 0.41750 0.37150 0.37610 0.03910  0.01070  -0.03950 9   LEU A CG    
78   C  CD1   . LEU A 13  ? 0.39430 0.35340 0.36110 0.03900  0.01120  -0.03220 9   LEU A CD1   
79   C  CD2   . LEU A 13  ? 0.36420 0.31440 0.31870 0.03440  0.00610  -0.03850 9   LEU A CD2   
80   N  N     . VAL A 14  ? 0.38720 0.34640 0.33680 0.04890  0.02180  -0.05460 10  VAL A N     
81   C  CA    . VAL A 14  ? 0.33980 0.30870 0.28240 0.04940  0.02590  -0.05450 10  VAL A CA    
82   C  C     . VAL A 14  ? 0.35930 0.33350 0.30820 0.05470  0.03150  -0.05530 10  VAL A C     
83   O  O     . VAL A 14  ? 0.41360 0.39750 0.36360 0.05490  0.03450  -0.05060 10  VAL A O     
84   C  CB    . VAL A 14  ? 0.46090 0.42850 0.39080 0.04830  0.02590  -0.06120 10  VAL A CB    
85   C  CG1   . VAL A 14  ? 0.52180 0.49960 0.44480 0.04980  0.03110  -0.06190 10  VAL A CG1   
86   C  CG2   . VAL A 14  ? 0.48740 0.45260 0.41170 0.04270  0.02040  -0.05850 10  VAL A CG2   
87   N  N     . ARG A 15  ? 0.32940 0.29750 0.28320 0.05910  0.03310  -0.06130 11  ARG A N     
88   C  CA    . ARG A 15  ? 0.44700 0.42040 0.40800 0.06480  0.03870  -0.06220 11  ARG A CA    
89   C  C     . ARG A 15  ? 0.42180 0.40020 0.39480 0.06510  0.03830  -0.05350 11  ARG A C     
90   O  O     . ARG A 15  ? 0.38370 0.37170 0.36090 0.06750  0.04250  -0.05070 11  ARG A O     
91   C  CB    . ARG A 15  ? 0.44950 0.41400 0.41430 0.06960  0.04030  -0.07050 11  ARG A CB    
92   C  CG    . ARG A 15  ? 0.45610 0.41650 0.40880 0.07000  0.04170  -0.08060 11  ARG A CG    
93   C  CD    . ARG A 15  ? 0.52730 0.47620 0.48560 0.07400  0.04190  -0.08830 11  ARG A CD    
94   N  NE    . ARG A 15  ? 0.65860 0.60370 0.60620 0.07540  0.04430  -0.09920 11  ARG A NE    
95   C  CZ    . ARG A 15  ? 0.61940 0.56670 0.56710 0.08110  0.05080  -0.10610 11  ARG A CZ    
96   N  NH1   . ARG A 15  ? 0.55510 0.50890 0.51380 0.08620  0.05550  -0.10260 11  ARG A NH1   
97   N  NH2   . ARG A 15  ? 0.57530 0.51870 0.51190 0.08170  0.05250  -0.11660 11  ARG A NH2   
98   N  N     . GLN A 16  ? 0.40210 0.37480 0.38090 0.06250  0.03320  -0.04900 12  GLN A N     
99   C  CA    . GLN A 16  ? 0.30950 0.28730 0.29870 0.06220  0.03230  -0.04070 12  GLN A CA    
100  C  C     . GLN A 16  ? 0.39330 0.38070 0.37840 0.05820  0.03240  -0.03450 12  GLN A C     
101  O  O     . GLN A 16  ? 0.39480 0.39030 0.38690 0.05900  0.03400  -0.02910 12  GLN A O     
102  C  CB    . GLN A 16  ? 0.33210 0.30160 0.32740 0.06010  0.02690  -0.03750 12  GLN A CB    
103  C  CG    . GLN A 16  ? 0.32140 0.29570 0.32790 0.06000  0.02560  -0.02910 12  GLN A CG    
104  C  CD    . GLN A 16  ? 0.37280 0.35050 0.39060 0.06610  0.02920  -0.02890 12  GLN A CD    
105  O  OE1   . GLN A 16  ? 0.39750 0.36800 0.42260 0.06960  0.02880  -0.03130 12  GLN A OE1   
106  N  NE2   . GLN A 16  ? 0.35770 0.34660 0.37780 0.06720  0.03260  -0.02560 12  GLN A NE2   
107  N  N     . MET A 17  ? 0.36370 0.35060 0.33810 0.05400  0.03070  -0.03510 13  MET A N     
108  C  CA    . MET A 17  ? 0.32910 0.32470 0.29960 0.05060  0.03130  -0.02980 13  MET A CA    
109  C  C     . MET A 17  ? 0.40290 0.40790 0.37170 0.05340  0.03710  -0.03090 13  MET A C     
110  O  O     . MET A 17  ? 0.44360 0.45740 0.41500 0.05200  0.03860  -0.02530 13  MET A O     
111  C  CB    . MET A 17  ? 0.29060 0.28310 0.25090 0.04590  0.02810  -0.02990 13  MET A CB    
112  C  CG    . MET A 17  ? 0.36640 0.35240 0.32940 0.04240  0.02280  -0.02680 13  MET A CG    
113  S  SD    . MET A 17  ? 0.49230 0.47720 0.44550 0.03700  0.01960  -0.02510 13  MET A SD    
114  C  CE    . MET A 17  ? 0.43060 0.41280 0.37340 0.03820  0.02060  -0.03290 13  MET A CE    
115  N  N     . GLU A 18  ? 0.30170 0.30530 0.26600 0.05700  0.04050  -0.03820 14  GLU A N     
116  C  CA    . GLU A 18  ? 0.32850 0.34170 0.29190 0.06030  0.04670  -0.03960 14  GLU A CA    
117  C  C     . GLU A 18  ? 0.39430 0.41420 0.37090 0.06350  0.04920  -0.03510 14  GLU A C     
118  O  O     . GLU A 18  ? 0.39800 0.42860 0.37640 0.06310  0.05230  -0.03070 14  GLU A O     
119  C  CB    . GLU A 18  ? 0.32070 0.33020 0.27820 0.06430  0.05010  -0.04920 14  GLU A CB    
120  C  CG    . GLU A 18  ? 0.41380 0.42050 0.35670 0.06110  0.04860  -0.05350 14  GLU A CG    
121  C  CD    . GLU A 18  ? 0.55790 0.55840 0.49490 0.06460  0.05070  -0.06410 14  GLU A CD    
122  O  OE1   . GLU A 18  ? 0.61380 0.60940 0.54010 0.06160  0.04780  -0.06810 14  GLU A OE1   
123  O  OE2   . GLU A 18  ? 0.57940 0.57990 0.52260 0.07020  0.05510  -0.06850 14  GLU A OE2   
124  N  N     . ALA A 19  ? 0.39800 0.41190 0.38450 0.06650  0.04770  -0.03570 15  ALA A N     
125  C  CA    . ALA A 19  ? 0.40280 0.42330 0.40270 0.06980  0.04980  -0.03120 15  ALA A CA    
126  C  C     . ALA A 19  ? 0.36060 0.38850 0.36430 0.06530  0.04730  -0.02200 15  ALA A C     
127  O  O     . ALA A 19  ? 0.43300 0.47030 0.44570 0.06700  0.04980  -0.01760 15  ALA A O     
128  C  CB    . ALA A 19  ? 0.45410 0.46590 0.46390 0.07320  0.04760  -0.03250 15  ALA A CB    
129  N  N     . GLU A 20  ? 0.32030 0.34460 0.31770 0.05950  0.04270  -0.01920 16  GLU A N     
130  C  CA    . GLU A 20  ? 0.33670 0.36720 0.33630 0.05480  0.04040  -0.01140 16  GLU A CA    
131  C  C     . GLU A 20  ? 0.42160 0.46040 0.41460 0.05220  0.04320  -0.00960 16  GLU A C     
132  O  O     . GLU A 20  ? 0.50120 0.54450 0.49510 0.04780  0.04130  -0.00370 16  GLU A O     
133  C  CB    . GLU A 20  ? 0.44160 0.46420 0.43820 0.05000  0.03450  -0.00930 16  GLU A CB    
134  C  CG    . GLU A 20  ? 0.51060 0.52750 0.51580 0.05120  0.03120  -0.00790 16  GLU A CG    
135  C  CD    . GLU A 20  ? 0.48210 0.50500 0.49540 0.04890  0.02900  -0.00040 16  GLU A CD    
136  O  OE1   . GLU A 20  ? 0.48870 0.50860 0.50970 0.04990  0.02640  0.00180  16  GLU A OE1   
137  O  OE2   . GLU A 20  ? 0.49930 0.53010 0.51160 0.04590  0.02980  0.00340  16  GLU A OE2   
138  N  N     . GLY A 21  ? 0.40360 0.44450 0.38980 0.05460  0.04750  -0.01460 17  GLY A N     
139  C  CA    . GLY A 21  ? 0.40210 0.45110 0.38170 0.05210  0.05020  -0.01250 17  GLY A CA    
140  C  C     . GLY A 21  ? 0.48160 0.52620 0.45060 0.04690  0.04680  -0.01160 17  GLY A C     
141  O  O     . GLY A 21  ? 0.45650 0.50750 0.42140 0.04380  0.04800  -0.00800 17  GLY A O     
142  N  N     . VAL A 22  ? 0.36380 0.39790 0.32890 0.04580  0.04250  -0.01470 18  VAL A N     
143  C  CA    . VAL A 22  ? 0.40570 0.43590 0.36130 0.04130  0.03940  -0.01400 18  VAL A CA    
144  C  C     . VAL A 22  ? 0.42750 0.46120 0.37290 0.04190  0.04260  -0.01740 18  VAL A C     
145  O  O     . VAL A 22  ? 0.38400 0.41650 0.32640 0.04570  0.04530  -0.02390 18  VAL A O     
146  C  CB    . VAL A 22  ? 0.42580 0.44490 0.38020 0.04040  0.03460  -0.01680 18  VAL A CB    
147  C  CG1   . VAL A 22  ? 0.42710 0.44260 0.37190 0.03650  0.03170  -0.01680 18  VAL A CG1   
148  C  CG2   . VAL A 22  ? 0.39730 0.41380 0.36070 0.03900  0.03130  -0.01240 18  VAL A CG2   
149  N  N     . SER A 23  ? 0.36970 0.40780 0.30950 0.03800  0.04240  -0.01310 19  SER A N     
150  C  CA    . SER A 23  ? 0.39490 0.43750 0.32450 0.03800  0.04520  -0.01510 19  SER A CA    
151  C  C     . SER A 23  ? 0.43550 0.47320 0.35570 0.03430  0.04120  -0.01500 19  SER A C     
152  O  O     . SER A 23  ? 0.41000 0.45030 0.32060 0.03440  0.04270  -0.01760 19  SER A O     
153  C  CB    . SER A 23  ? 0.33980 0.39380 0.27040 0.03680  0.04910  -0.00950 19  SER A CB    
154  O  OG    . SER A 23  ? 0.48460 0.54480 0.42520 0.03970  0.05260  -0.00830 19  SER A OG    
155  N  N     . TYR A 24  ? 0.42530 0.45660 0.34790 0.03120  0.03630  -0.01200 20  TYR A N     
156  C  CA    . TYR A 24  ? 0.40660 0.43370 0.32210 0.02790  0.03240  -0.01120 20  TYR A CA    
157  C  C     . TYR A 24  ? 0.37820 0.39580 0.29730 0.02700  0.02770  -0.01230 20  TYR A C     
158  O  O     . TYR A 24  ? 0.39050 0.40610 0.31800 0.02730  0.02700  -0.01070 20  TYR A O     
159  C  CB    . TYR A 24  ? 0.35870 0.39030 0.27360 0.02400  0.03200  -0.00380 20  TYR A CB    
160  C  CG    . TYR A 24  ? 0.31690 0.35840 0.22780 0.02430  0.03650  -0.00160 20  TYR A CG    
161  C  CD1   . TYR A 24  ? 0.38870 0.43300 0.28910 0.02390  0.03710  -0.00310 20  TYR A CD1   
162  C  CD2   . TYR A 24  ? 0.32570 0.37450 0.24310 0.02460  0.04010  0.00200  20  TYR A CD2   
163  C  CE1   . TYR A 24  ? 0.37830 0.43230 0.27450 0.02390  0.04150  -0.00080 20  TYR A CE1   
164  C  CE2   . TYR A 24  ? 0.34280 0.40150 0.25690 0.02470  0.04450  0.00430  20  TYR A CE2   
165  C  CZ    . TYR A 24  ? 0.35690 0.41810 0.26010 0.02430  0.04530  0.00300  20  TYR A CZ    
166  O  OH    . TYR A 24  ? 0.37550 0.44710 0.27490 0.02420  0.04980  0.00570  20  TYR A OH    
167  N  N     . VAL A 25  ? 0.37200 0.38450 0.28480 0.02570  0.02440  -0.01460 21  VAL A N     
168  C  CA    . VAL A 25  ? 0.35990 0.36450 0.27570 0.02400  0.01970  -0.01460 21  VAL A CA    
169  C  C     . VAL A 25  ? 0.31430 0.31880 0.22540 0.02050  0.01690  -0.01080 21  VAL A C     
170  O  O     . VAL A 25  ? 0.39320 0.39920 0.29620 0.02000  0.01630  -0.01240 21  VAL A O     
171  C  CB    . VAL A 25  ? 0.39820 0.39620 0.31280 0.02590  0.01810  -0.02130 21  VAL A CB    
172  C  CG1   . VAL A 25  ? 0.35800 0.34890 0.27510 0.02360  0.01320  -0.02050 21  VAL A CG1   
173  C  CG2   . VAL A 25  ? 0.42050 0.41780 0.34140 0.02970  0.02080  -0.02440 21  VAL A CG2   
174  N  N     . PHE A 26  ? 0.35230 0.35550 0.26840 0.01810  0.01510  -0.00580 22  PHE A N     
175  C  CA    . PHE A 26  ? 0.36980 0.37250 0.28340 0.01520  0.01260  -0.00170 22  PHE A CA    
176  C  C     . PHE A 26  ? 0.41750 0.41340 0.33220 0.01430  0.00840  -0.00330 22  PHE A C     
177  O  O     . PHE A 26  ? 0.32920 0.32090 0.24970 0.01460  0.00750  -0.00430 22  PHE A O     
178  C  CB    . PHE A 26  ? 0.35530 0.35980 0.27390 0.01320  0.01340  0.00420  22  PHE A CB    
179  C  CG    . PHE A 26  ? 0.34560 0.35730 0.26490 0.01360  0.01740  0.00630  22  PHE A CG    
180  C  CD1   . PHE A 26  ? 0.33360 0.35090 0.24810 0.01240  0.01890  0.00980  22  PHE A CD1   
181  C  CD2   . PHE A 26  ? 0.31140 0.32480 0.23650 0.01510  0.01960  0.00550  22  PHE A CD2   
182  C  CE1   . PHE A 26  ? 0.38270 0.40720 0.29820 0.01260  0.02270  0.01220  22  PHE A CE1   
183  C  CE2   . PHE A 26  ? 0.39970 0.42050 0.32630 0.01550  0.02330  0.00790  22  PHE A CE2   
184  C  CZ    . PHE A 26  ? 0.36160 0.38810 0.28340 0.01420  0.02500  0.01110  22  PHE A CZ    
185  N  N     . GLY A 27  ? 0.34760 0.34310 0.25700 0.01290  0.00590  -0.00290 23  GLY A N     
186  C  CA    . GLY A 27  ? 0.39730 0.38750 0.30870 0.01190  0.00200  -0.00390 23  GLY A CA    
187  C  C     . GLY A 27  ? 0.37670 0.36780 0.28170 0.01060  -0.00100 -0.00390 23  GLY A C     
188  O  O     . GLY A 27  ? 0.37390 0.37000 0.27280 0.01020  -0.00010 -0.00230 23  GLY A O     
189  N  N     . ILE A 28  ? 0.32300 0.30980 0.22990 0.00980  -0.00460 -0.00550 24  ILE A N     
190  C  CA    . ILE A 28  ? 0.36190 0.34940 0.26410 0.00820  -0.00830 -0.00540 24  ILE A CA    
191  C  C     . ILE A 28  ? 0.32370 0.30690 0.22530 0.00830  -0.01080 -0.01130 24  ILE A C     
192  O  O     . ILE A 28  ? 0.42750 0.40590 0.33550 0.00860  -0.01130 -0.01260 24  ILE A O     
193  C  CB    . ILE A 28  ? 0.31090 0.29810 0.21790 0.00650  -0.01060 0.00030  24  ILE A CB    
194  C  CG1   . ILE A 28  ? 0.32340 0.31450 0.23040 0.00630  -0.00830 0.00600  24  ILE A CG1   
195  C  CG2   . ILE A 28  ? 0.30340 0.29140 0.20760 0.00490  -0.01520 0.00050  24  ILE A CG2   
196  C  CD1   . ILE A 28  ? 0.37660 0.36680 0.28920 0.00510  -0.01000 0.01170  24  ILE A CD1   
197  N  N     . PRO A 29  ? 0.36380 0.34830 0.25780 0.00780  -0.01260 -0.01500 25  PRO A N     
198  C  CA    . PRO A 29  ? 0.46490 0.44440 0.35830 0.00760  -0.01500 -0.02130 25  PRO A CA    
199  C  C     . PRO A 29  ? 0.43840 0.41510 0.33680 0.00530  -0.01970 -0.01950 25  PRO A C     
200  O  O     . PRO A 29  ? 0.44700 0.42600 0.34860 0.00410  -0.02120 -0.01380 25  PRO A O     
201  C  CB    . PRO A 29  ? 0.45890 0.44160 0.34130 0.00720  -0.01550 -0.02550 25  PRO A CB    
202  C  CG    . PRO A 29  ? 0.46860 0.45830 0.34690 0.00600  -0.01570 -0.01910 25  PRO A CG    
203  C  CD    . PRO A 29  ? 0.43480 0.42540 0.31960 0.00730  -0.01200 -0.01400 25  PRO A CD    
204  N  N     . GLY A 30  ? 0.42400 0.39550 0.32350 0.00490  -0.02190 -0.02460 26  GLY A N     
205  C  CA    . GLY A 30  ? 0.41430 0.38340 0.31840 0.00240  -0.02660 -0.02390 26  GLY A CA    
206  C  C     . GLY A 30  ? 0.47590 0.43920 0.37900 0.00190  -0.02850 -0.03090 26  GLY A C     
207  O  O     . GLY A 30  ? 0.50350 0.46380 0.40490 0.00410  -0.02570 -0.03570 26  GLY A O     
208  N  N     . GLY A 31  ? 0.43210 0.39410 0.33710 -0.00100 -0.03340 -0.03130 27  GLY A N     
209  C  CA    . GLY A 31  ? 0.40650 0.36270 0.31030 -0.00220 -0.03610 -0.03790 27  GLY A CA    
210  C  C     . GLY A 31  ? 0.42980 0.37930 0.33760 0.00030  -0.03310 -0.04190 27  GLY A C     
211  O  O     . GLY A 31  ? 0.45240 0.39940 0.35490 0.00200  -0.03120 -0.04820 27  GLY A O     
212  N  N     . PRO A 32  ? 0.42530 0.37240 0.34280 0.00060  -0.03230 -0.03820 28  PRO A N     
213  C  CA    . PRO A 32  ? 0.40350 0.34420 0.32610 0.00270  -0.03010 -0.04100 28  PRO A CA    
214  C  C     . PRO A 32  ? 0.47330 0.41540 0.39380 0.00660  -0.02490 -0.04200 28  PRO A C     
215  O  O     . PRO A 32  ? 0.54180 0.47890 0.46580 0.00880  -0.02310 -0.04520 28  PRO A O     
216  C  CB    . PRO A 32  ? 0.39860 0.33860 0.33130 0.00170  -0.03070 -0.03520 28  PRO A CB    
217  C  CG    . PRO A 32  ? 0.43360 0.37940 0.36650 -0.00060 -0.03280 -0.02990 28  PRO A CG    
218  C  CD    . PRO A 32  ? 0.48320 0.43390 0.40700 -0.00050 -0.03280 -0.03090 28  PRO A CD    
219  N  N     . LEU A 33  ? 0.46510 0.41380 0.38080 0.00750  -0.02240 -0.03910 29  LEU A N     
220  C  CA    . LEU A 33  ? 0.44930 0.40060 0.36300 0.01080  -0.01740 -0.03950 29  LEU A CA    
221  C  C     . LEU A 33  ? 0.50860 0.46080 0.41310 0.01230  -0.01580 -0.04590 29  LEU A C     
222  O  O     . LEU A 33  ? 0.46040 0.41440 0.36390 0.01540  -0.01130 -0.04740 29  LEU A O     
223  C  CB    . LEU A 33  ? 0.43730 0.39530 0.35100 0.01060  -0.01560 -0.03270 29  LEU A CB    
224  C  CG    . LEU A 33  ? 0.43310 0.39450 0.34810 0.01320  -0.01080 -0.03040 29  LEU A CG    
225  C  CD1   . LEU A 33  ? 0.35570 0.31330 0.27930 0.01480  -0.00950 -0.03000 29  LEU A CD1   
226  C  CD2   . LEU A 33  ? 0.38180 0.34870 0.29690 0.01190  -0.01020 -0.02380 29  LEU A CD2   
227  N  N     . MET A 34  ? 0.44330 0.39480 0.34110 0.01000  -0.01920 -0.04980 30  MET A N     
228  C  CA    . MET A 34  ? 0.43170 0.38530 0.31890 0.01100  -0.01760 -0.05580 30  MET A CA    
229  C  C     . MET A 34  ? 0.51830 0.46700 0.40580 0.01460  -0.01400 -0.06290 30  MET A C     
230  O  O     . MET A 34  ? 0.44480 0.39760 0.32550 0.01700  -0.01000 -0.06590 30  MET A O     
231  C  CB    . MET A 34  ? 0.40880 0.36210 0.28900 0.00730  -0.02280 -0.05890 30  MET A CB    
232  C  CG    . MET A 34  ? 0.46100 0.42070 0.34020 0.00430  -0.02610 -0.05170 30  MET A CG    
233  S  SD    . MET A 34  ? 0.61550 0.58460 0.49080 0.00600  -0.02150 -0.04530 30  MET A SD    
234  C  CE    . MET A 34  ? 0.50360 0.47680 0.36400 0.00590  -0.02080 -0.05170 30  MET A CE    
235  N  N     . PRO A 35  ? 0.53390 0.47440 0.42910 0.01530  -0.01500 -0.06580 31  PRO A N     
236  C  CA    . PRO A 35  ? 0.44340 0.37930 0.33990 0.01940  -0.01120 -0.07210 31  PRO A CA    
237  C  C     . PRO A 35  ? 0.45180 0.39330 0.35110 0.02340  -0.00540 -0.06880 31  PRO A C     
238  O  O     . PRO A 35  ? 0.42100 0.36270 0.31770 0.02700  -0.00110 -0.07410 31  PRO A O     
239  C  CB    . PRO A 35  ? 0.49470 0.42120 0.40140 0.01900  -0.01390 -0.07290 31  PRO A CB    
240  C  CG    . PRO A 35  ? 0.49320 0.41860 0.39950 0.01400  -0.01990 -0.07070 31  PRO A CG    
241  C  CD    . PRO A 35  ? 0.49880 0.43360 0.40160 0.01250  -0.01980 -0.06360 31  PRO A CD    
242  N  N     . LEU A 36  ? 0.42860 0.37450 0.33330 0.02270  -0.00500 -0.06050 32  LEU A N     
243  C  CA    . LEU A 36  ? 0.42110 0.37310 0.32800 0.02570  0.00000  -0.05710 32  LEU A CA    
244  C  C     . LEU A 36  ? 0.45710 0.41680 0.35380 0.02630  0.00310  -0.05850 32  LEU A C     
245  O  O     . LEU A 36  ? 0.49010 0.45290 0.38570 0.02980  0.00790  -0.06110 32  LEU A O     
246  C  CB    . LEU A 36  ? 0.43630 0.39160 0.34970 0.02410  -0.00070 -0.04830 32  LEU A CB    
247  C  CG    . LEU A 36  ? 0.43010 0.39250 0.34530 0.02610  0.00380  -0.04400 32  LEU A CG    
248  C  CD1   . LEU A 36  ? 0.35760 0.31840 0.27960 0.03020  0.00730  -0.04610 32  LEU A CD1   
249  C  CD2   . LEU A 36  ? 0.46440 0.42980 0.38410 0.02370  0.00260  -0.03610 32  LEU A CD2   
250  N  N     . TYR A 37  ? 0.40770 0.37090 0.29680 0.02290  0.00020  -0.05660 33  TYR A N     
251  C  CA    . TYR A 37  ? 0.46070 0.43180 0.33970 0.02300  0.00290  -0.05700 33  TYR A CA    
252  C  C     . TYR A 37  ? 0.45590 0.42540 0.32730 0.02500  0.00490  -0.06640 33  TYR A C     
253  O  O     . TYR A 37  ? 0.42880 0.40420 0.29520 0.02750  0.00990  -0.06820 33  TYR A O     
254  C  CB    . TYR A 37  ? 0.40250 0.37750 0.27570 0.01890  -0.00110 -0.05260 33  TYR A CB    
255  C  CG    . TYR A 37  ? 0.37660 0.35540 0.25570 0.01780  -0.00110 -0.04350 33  TYR A CG    
256  C  CD1   . TYR A 37  ? 0.43540 0.42140 0.31320 0.01880  0.00290  -0.03920 33  TYR A CD1   
257  C  CD2   . TYR A 37  ? 0.44760 0.42250 0.33400 0.01570  -0.00490 -0.03950 33  TYR A CD2   
258  C  CE1   . TYR A 37  ? 0.49110 0.47970 0.37460 0.01750  0.00280  -0.03130 33  TYR A CE1   
259  C  CE2   . TYR A 37  ? 0.37520 0.35300 0.26700 0.01480  -0.00460 -0.03200 33  TYR A CE2   
260  C  CZ    . TYR A 37  ? 0.43740 0.42160 0.32750 0.01570  -0.00090 -0.02810 33  TYR A CZ    
261  O  OH    . TYR A 37  ? 0.49430 0.48050 0.38960 0.01460  -0.00070 -0.02110 33  TYR A OH    
262  N  N     . GLU A 38  ? 0.41320 0.37460 0.28370 0.02400  0.00140  -0.07270 34  GLU A N     
263  C  CA    . GLU A 38  ? 0.45040 0.40870 0.31410 0.02600  0.00340  -0.08280 34  GLU A CA    
264  C  C     . GLU A 38  ? 0.39780 0.35570 0.26690 0.03150  0.00970  -0.08560 34  GLU A C     
265  O  O     . GLU A 38  ? 0.47690 0.43880 0.33900 0.03410  0.01430  -0.09090 34  GLU A O     
266  C  CB    . GLU A 38  ? 0.42940 0.37740 0.29430 0.02400  -0.00170 -0.08870 34  GLU A CB    
267  C  CG    . GLU A 38  ? 0.55930 0.50210 0.41800 0.02610  0.00020  -0.10010 34  GLU A CG    
268  C  CD    . GLU A 38  ? 0.69700 0.62950 0.55650 0.02310  -0.00560 -0.10570 34  GLU A CD    
269  O  OE1   . GLU A 38  ? 0.75660 0.68710 0.60580 0.02180  -0.00670 -0.11420 34  GLU A OE1   
270  O  OE2   . GLU A 38  ? 0.71820 0.64500 0.58820 0.02170  -0.00900 -0.10160 34  GLU A OE2   
271  N  N     . ALA A 39  ? 0.46520 0.41910 0.34710 0.03330  0.01000  -0.08200 35  ALA A N     
272  C  CA    . ALA A 39  ? 0.45350 0.40750 0.34230 0.03860  0.01560  -0.08370 35  ALA A CA    
273  C  C     . ALA A 39  ? 0.43990 0.40540 0.32650 0.04030  0.02070  -0.07920 35  ALA A C     
274  O  O     . ALA A 39  ? 0.45210 0.42100 0.33760 0.04440  0.02630  -0.08340 35  ALA A O     
275  C  CB    . ALA A 39  ? 0.43090 0.37920 0.33370 0.03960  0.01400  -0.07940 35  ALA A CB    
276  N  N     . ILE A 40  ? 0.46310 0.43470 0.34950 0.03710  0.01910  -0.07070 36  ILE A N     
277  C  CA    . ILE A 40  ? 0.48820 0.47040 0.37310 0.03810  0.02360  -0.06570 36  ILE A CA    
278  C  C     . ILE A 40  ? 0.46650 0.45470 0.33880 0.03860  0.02680  -0.07060 36  ILE A C     
279  O  O     . ILE A 40  ? 0.48310 0.47780 0.35480 0.04190  0.03270  -0.07180 36  ILE A O     
280  C  CB    . ILE A 40  ? 0.47790 0.46410 0.36440 0.03410  0.02070  -0.05620 36  ILE A CB    
281  C  CG1   . ILE A 40  ? 0.48780 0.47130 0.38690 0.03450  0.01990  -0.05090 36  ILE A CG1   
282  C  CG2   . ILE A 40  ? 0.46660 0.46350 0.34790 0.03380  0.02440  -0.05180 36  ILE A CG2   
283  C  CD1   . ILE A 40  ? 0.42630 0.41150 0.32740 0.03060  0.01660  -0.04280 36  ILE A CD1   
284  N  N     . PHE A 41  ? 0.48070 0.46740 0.34290 0.03530  0.02300  -0.07340 37  PHE A N     
285  C  CA    . PHE A 41  ? 0.48500 0.47830 0.33380 0.03510  0.02560  -0.07760 37  PHE A CA    
286  C  C     . PHE A 41  ? 0.53300 0.52330 0.37870 0.03930  0.02990  -0.08830 37  PHE A C     
287  O  O     . PHE A 41  ? 0.53070 0.52830 0.36740 0.04080  0.03470  -0.09160 37  PHE A O     
288  C  CB    . PHE A 41  ? 0.44210 0.43470 0.28100 0.03010  0.01960  -0.07770 37  PHE A CB    
289  C  CG    . PHE A 41  ? 0.47430 0.47390 0.31220 0.02650  0.01740  -0.06740 37  PHE A CG    
290  C  CD1   . PHE A 41  ? 0.54650 0.55680 0.37770 0.02630  0.02110  -0.06340 37  PHE A CD1   
291  C  CD2   . PHE A 41  ? 0.44770 0.44320 0.29200 0.02350  0.01190  -0.06160 37  PHE A CD2   
292  C  CE1   . PHE A 41  ? 0.56450 0.58060 0.39570 0.02310  0.01900  -0.05380 37  PHE A CE1   
293  C  CE2   . PHE A 41  ? 0.45810 0.45940 0.30230 0.02060  0.01010  -0.05240 37  PHE A CE2   
294  C  CZ    . PHE A 41  ? 0.53420 0.54530 0.37200 0.02040  0.01350  -0.04850 37  PHE A CZ    
295  N  N     . SER A 42  ? 0.54590 0.52560 0.39920 0.04150  0.02870  -0.09360 38  SER A N     
296  C  CA    . SER A 42  ? 0.59000 0.56580 0.44140 0.04590  0.03300  -0.10430 38  SER A CA    
297  C  C     . SER A 42  ? 0.56360 0.54470 0.42300 0.05160  0.04030  -0.10330 38  SER A C     
298  O  O     . SER A 42  ? 0.57810 0.56070 0.43360 0.05560  0.04590  -0.11110 38  SER A O     
299  C  CB    . SER A 42  ? 0.55560 0.51760 0.41290 0.04610  0.02900  -0.11030 38  SER A CB    
300  O  OG    . SER A 42  ? 0.66720 0.62500 0.53990 0.04900  0.02970  -0.10620 38  SER A OG    
301  N  N     . ARG A 43  ? 0.47910 0.46370 0.34950 0.05180  0.04060  -0.09400 39  ARG A N     
302  C  CA    . ARG A 43  ? 0.50070 0.49110 0.38030 0.05680  0.04680  -0.09200 39  ARG A CA    
303  C  C     . ARG A 43  ? 0.57540 0.57960 0.44970 0.05670  0.05160  -0.08730 39  ARG A C     
304  O  O     . ARG A 43  ? 0.71720 0.72770 0.59600 0.06110  0.05800  -0.08800 39  ARG A O     
305  C  CB    . ARG A 43  ? 0.48950 0.47730 0.38390 0.05680  0.04440  -0.08400 39  ARG A CB    
306  C  CG    . ARG A 43  ? 0.48570 0.46080 0.38850 0.05770  0.04050  -0.08710 39  ARG A CG    
307  C  CD    . ARG A 43  ? 0.55110 0.52210 0.46000 0.06390  0.04510  -0.09450 39  ARG A CD    
308  N  NE    . ARG A 43  ? 0.51550 0.49500 0.43380 0.06800  0.05040  -0.08990 39  ARG A NE    
309  C  CZ    . ARG A 43  ? 0.56270 0.54350 0.48530 0.07410  0.05640  -0.09530 39  ARG A CZ    
310  N  NH1   . ARG A 43  ? 0.51140 0.48470 0.42920 0.07670  0.05790  -0.10610 39  ARG A NH1   
311  N  NH2   . ARG A 43  ? 0.54010 0.52980 0.47220 0.07750  0.06100  -0.09030 39  ARG A NH2   
312  N  N     . LYS A 44  ? 0.55490 0.56420 0.42100 0.05170  0.04870  -0.08180 40  LYS A N     
313  C  CA    . LYS A 44  ? 0.64840 0.67060 0.50840 0.05070  0.05270  -0.07680 40  LYS A CA    
314  C  C     . LYS A 44  ? 0.58180 0.61150 0.45330 0.05360  0.05750  -0.07070 40  LYS A C     
315  O  O     . LYS A 44  ? 0.60580 0.64540 0.47520 0.05600  0.06380  -0.07100 40  LYS A O     
316  C  CB    . LYS A 44  ? 0.69310 0.72000 0.53940 0.05220  0.05700  -0.08490 40  LYS A CB    
317  C  CG    . LYS A 44  ? 0.76500 0.79110 0.59680 0.04710  0.05220  -0.08640 40  LYS A CG    
318  C  CD    . LYS A 44  ? 0.84160 0.86680 0.66050 0.04860  0.05450  -0.09800 40  LYS A CD    
319  C  CE    . LYS A 44  ? 0.94470 0.95570 0.76520 0.04900  0.05020  -0.10670 40  LYS A CE    
320  N  NZ    . LYS A 44  ? 0.97000 0.97730 0.77880 0.04370  0.04360  -0.10910 40  LYS A NZ    
321  N  N     . LYS A 45  ? 0.54290 0.56880 0.42640 0.05280  0.05430  -0.06460 41  LYS A N     
322  C  CA    . LYS A 45  ? 0.53390 0.56780 0.42750 0.05410  0.05770  -0.05750 41  LYS A CA    
323  C  C     . LYS A 45  ? 0.60470 0.63830 0.50230 0.04910  0.05260  -0.04810 41  LYS A C     
324  O  O     . LYS A 45  ? 0.65960 0.70150 0.55540 0.04650  0.05370  -0.04140 41  LYS A O     
325  C  CB    . LYS A 45  ? 0.56770 0.59870 0.47400 0.05950  0.06040  -0.06030 41  LYS A CB    
326  C  CG    . LYS A 45  ? 0.69170 0.71900 0.59460 0.06460  0.06440  -0.07140 41  LYS A CG    
327  C  CD    . LYS A 45  ? 0.76950 0.79150 0.68610 0.07010  0.06620  -0.07430 41  LYS A CD    
328  C  CE    . LYS A 45  ? 0.85220 0.87740 0.76780 0.07650  0.07370  -0.08280 41  LYS A CE    
329  N  NZ    . LYS A 45  ? 0.89050 0.93030 0.80800 0.07920  0.08110  -0.08000 41  LYS A NZ    
330  N  N     . ILE A 46  ? 0.50600 0.52980 0.40870 0.04760  0.04720  -0.04750 42  ILE A N     
331  C  CA    . ILE A 46  ? 0.46000 0.48270 0.36450 0.04280  0.04230  -0.03980 42  ILE A CA    
332  C  C     . ILE A 46  ? 0.37480 0.39810 0.26740 0.03890  0.03970  -0.03940 42  ILE A C     
333  O  O     . ILE A 46  ? 0.44730 0.46590 0.33200 0.03900  0.03800  -0.04570 42  ILE A O     
334  C  CB    . ILE A 46  ? 0.46210 0.47490 0.37450 0.04220  0.03750  -0.03950 42  ILE A CB    
335  C  CG1   . ILE A 46  ? 0.47340 0.48720 0.39840 0.04540  0.03960  -0.03780 42  ILE A CG1   
336  C  CG2   . ILE A 46  ? 0.40490 0.41610 0.31710 0.03720  0.03260  -0.03300 42  ILE A CG2   
337  C  CD1   . ILE A 46  ? 0.47690 0.48120 0.40970 0.04580  0.03560  -0.03850 42  ILE A CD1   
338  N  N     . GLN A 47  ? 0.37280 0.40180 0.26420 0.03540  0.03890  -0.03160 43  GLN A N     
339  C  CA    . GLN A 47  ? 0.46310 0.49340 0.34400 0.03180  0.03620  -0.03000 43  GLN A CA    
340  C  C     . GLN A 47  ? 0.39820 0.42200 0.28180 0.02810  0.03020  -0.02570 43  GLN A C     
341  O  O     . GLN A 47  ? 0.35560 0.37910 0.24740 0.02680  0.02940  -0.02000 43  GLN A O     
342  C  CB    . GLN A 47  ? 0.52300 0.56400 0.39980 0.03030  0.03960  -0.02430 43  GLN A CB    
343  C  CG    . GLN A 47  ? 0.77580 0.81990 0.63960 0.02790  0.03830  -0.02470 43  GLN A CG    
344  C  CD    . GLN A 47  ? 0.91660 0.96820 0.77830 0.02440  0.03850  -0.01570 43  GLN A CD    
345  O  OE1   . GLN A 47  ? 0.96740 1.02530 0.83470 0.02450  0.04200  -0.01060 43  GLN A OE1   
346  N  NE2   . GLN A 47  ? 0.95050 1.00160 0.80470 0.02120  0.03440  -0.01320 43  GLN A NE2   
347  N  N     . PRO A 48  ? 0.41890 0.43800 0.29620 0.02620  0.02590  -0.02830 44  PRO A N     
348  C  CA    . PRO A 48  ? 0.39730 0.41150 0.27770 0.02300  0.02060  -0.02360 44  PRO A CA    
349  C  C     . PRO A 48  ? 0.40110 0.42110 0.27890 0.01990  0.02010  -0.01590 44  PRO A C     
350  O  O     . PRO A 48  ? 0.40950 0.43600 0.27890 0.01920  0.02160  -0.01510 44  PRO A O     
351  C  CB    . PRO A 48  ? 0.37430 0.38270 0.24890 0.02210  0.01650  -0.02920 44  PRO A CB    
352  C  CG    . PRO A 48  ? 0.34470 0.35780 0.20870 0.02330  0.01920  -0.03450 44  PRO A CG    
353  C  CD    . PRO A 48  ? 0.39000 0.40850 0.25670 0.02680  0.02570  -0.03540 44  PRO A CD    
354  N  N     . ILE A 49  ? 0.35620 0.37370 0.24120 0.01790  0.01790  -0.01020 45  ILE A N     
355  C  CA    . ILE A 49  ? 0.41460 0.43560 0.29850 0.01500  0.01680  -0.00280 45  ILE A CA    
356  C  C     . ILE A 49  ? 0.38350 0.39850 0.26900 0.01290  0.01150  -0.00130 45  ILE A C     
357  O  O     . ILE A 49  ? 0.40470 0.41400 0.29770 0.01290  0.00980  -0.00130 45  ILE A O     
358  C  CB    . ILE A 49  ? 0.39380 0.41770 0.28520 0.01430  0.01930  0.00300  45  ILE A CB    
359  C  CG1   . ILE A 49  ? 0.30010 0.33140 0.19090 0.01630  0.02470  0.00210  45  ILE A CG1   
360  C  CG2   . ILE A 49  ? 0.37500 0.40060 0.26640 0.01110  0.01750  0.01060  45  ILE A CG2   
361  C  CD1   . ILE A 49  ? 0.30480 0.34460 0.18640 0.01560  0.02710  0.00410  45  ILE A CD1   
362  N  N     . LEU A 50  ? 0.37900 0.39580 0.25740 0.01120  0.00880  -0.00000 46  LEU A N     
363  C  CA    . LEU A 50  ? 0.32070 0.33330 0.20100 0.00920  0.00380  0.00240  46  LEU A CA    
364  C  C     . LEU A 50  ? 0.37960 0.39280 0.26580 0.00750  0.00350  0.01030  46  LEU A C     
365  O  O     . LEU A 50  ? 0.39430 0.41300 0.27750 0.00640  0.00490  0.01530  46  LEU A O     
366  C  CB    . LEU A 50  ? 0.33410 0.34960 0.20500 0.00790  0.00090  0.00150  46  LEU A CB    
367  C  CG    . LEU A 50  ? 0.35410 0.36670 0.22710 0.00590  -0.00450 0.00440  46  LEU A CG    
368  C  CD1   . LEU A 50  ? 0.30250 0.30760 0.18150 0.00650  -0.00680 -0.00010 46  LEU A CD1   
369  C  CD2   . LEU A 50  ? 0.36260 0.37980 0.22580 0.00420  -0.00770 0.00450  46  LEU A CD2   
370  N  N     . THR A 51  ? 0.33300 0.34030 0.22720 0.00720  0.00170  0.01140  47  THR A N     
371  C  CA    . THR A 51  ? 0.35150 0.35790 0.25170 0.00560  0.00140  0.01780  47  THR A CA    
372  C  C     . THR A 51  ? 0.36420 0.36830 0.26560 0.00440  -0.00290 0.02060  47  THR A C     
373  O  O     . THR A 51  ? 0.32340 0.32670 0.22140 0.00440  -0.00590 0.01770  47  THR A O     
374  C  CB    . THR A 51  ? 0.38030 0.38250 0.28860 0.00600  0.00290  0.01710  47  THR A CB    
375  O  OG1   . THR A 51  ? 0.36760 0.36430 0.27920 0.00660  0.00060  0.01340  47  THR A OG1   
376  C  CG2   . THR A 51  ? 0.32380 0.32910 0.23180 0.00740  0.00680  0.01470  47  THR A CG2   
377  N  N     . LYS A 52  ? 0.31860 0.32140 0.22540 0.00330  -0.00330 0.02640  48  LYS A N     
378  C  CA    . LYS A 52  ? 0.37270 0.37360 0.28250 0.00260  -0.00690 0.02980  48  LYS A CA    
379  C  C     . LYS A 52  ? 0.41600 0.41100 0.33300 0.00310  -0.00810 0.02740  48  LYS A C     
380  O  O     . LYS A 52  ? 0.42890 0.42280 0.34790 0.00290  -0.01130 0.02820  48  LYS A O     
381  C  CB    . LYS A 52  ? 0.37080 0.37290 0.28370 0.00140  -0.00650 0.03730  48  LYS A CB    
382  C  CG    . LYS A 52  ? 0.34270 0.35150 0.24860 0.00050  -0.00570 0.04110  48  LYS A CG    
383  C  CD    . LYS A 52  ? 0.34060 0.35330 0.23930 0.00020  -0.00920 0.04060  48  LYS A CD    
384  C  CE    . LYS A 52  ? 0.44230 0.46070 0.33060 0.00040  -0.00750 0.03690  48  LYS A CE    
385  N  NZ    . LYS A 52  ? 0.59140 0.61420 0.47790 0.00010  -0.00320 0.03950  48  LYS A NZ    
386  N  N     . HIS A 53  ? 0.38870 0.38050 0.30960 0.00360  -0.00560 0.02480  49  HIS A N     
387  C  CA    . HIS A 53  ? 0.34540 0.33220 0.27270 0.00390  -0.00620 0.02280  49  HIS A CA    
388  C  C     . HIS A 53  ? 0.32850 0.31420 0.25610 0.00460  -0.00400 0.01840  49  HIS A C     
389  O  O     . HIS A 53  ? 0.35270 0.34070 0.27890 0.00460  -0.00130 0.01870  49  HIS A O     
390  C  CB    . HIS A 53  ? 0.32210 0.30620 0.25580 0.00320  -0.00550 0.02700  49  HIS A CB    
391  C  CG    . HIS A 53  ? 0.30020 0.27990 0.24010 0.00350  -0.00620 0.02550  49  HIS A CG    
392  N  ND1   . HIS A 53  ? 0.33340 0.31070 0.27540 0.00360  -0.00470 0.02190  49  HIS A ND1   
393  C  CD2   . HIS A 53  ? 0.36080 0.33870 0.30560 0.00370  -0.00780 0.02770  49  HIS A CD2   
394  C  CE1   . HIS A 53  ? 0.29810 0.27240 0.24520 0.00360  -0.00530 0.02160  49  HIS A CE1   
395  N  NE2   . HIS A 53  ? 0.30990 0.28450 0.25910 0.00390  -0.00700 0.02490  49  HIS A NE2   
396  N  N     . GLU A 54  ? 0.29620 0.27880 0.22610 0.00510  -0.00510 0.01470  50  GLU A N     
397  C  CA    . GLU A 54  ? 0.25000 0.23150 0.18080 0.00590  -0.00330 0.01110  50  GLU A CA    
398  C  C     . GLU A 54  ? 0.30100 0.28180 0.23610 0.00520  -0.00100 0.01290  50  GLU A C     
399  O  O     . GLU A 54  ? 0.30120 0.28300 0.23670 0.00570  0.00090  0.01140  50  GLU A O     
400  C  CB    . GLU A 54  ? 0.26600 0.24400 0.19920 0.00620  -0.00530 0.00780  50  GLU A CB    
401  C  CG    . GLU A 54  ? 0.31790 0.29620 0.24660 0.00660  -0.00760 0.00460  50  GLU A CG    
402  C  CD    . GLU A 54  ? 0.43460 0.41340 0.36320 0.00550  -0.01090 0.00670  50  GLU A CD    
403  O  OE1   . GLU A 54  ? 0.38920 0.36780 0.31500 0.00520  -0.01360 0.00400  50  GLU A OE1   
404  O  OE2   . GLU A 54  ? 0.39230 0.37160 0.32400 0.00490  -0.01090 0.01090  50  GLU A OE2   
405  N  N     . GLU A 55  ? 0.23850 0.21740 0.17710 0.00410  -0.00110 0.01600  51  GLU A N     
406  C  CA    . GLU A 55  ? 0.33740 0.31560 0.27910 0.00300  0.00100  0.01740  51  GLU A CA    
407  C  C     . GLU A 55  ? 0.32680 0.30890 0.26620 0.00260  0.00300  0.01940  51  GLU A C     
408  O  O     . GLU A 55  ? 0.28530 0.26880 0.22600 0.00220  0.00480  0.01890  51  GLU A O     
409  C  CB    . GLU A 55  ? 0.33160 0.30660 0.27730 0.00200  0.00070  0.01990  51  GLU A CB    
410  C  CG    . GLU A 55  ? 0.39850 0.37180 0.34740 0.00040  0.00260  0.02020  51  GLU A CG    
411  C  CD    . GLU A 55  ? 0.42380 0.39350 0.37630 -0.00050 0.00280  0.02250  51  GLU A CD    
412  O  OE1   . GLU A 55  ? 0.44330 0.41050 0.39820 -0.00190 0.00410  0.02180  51  GLU A OE1   
413  O  OE2   . GLU A 55  ? 0.40660 0.37590 0.35960 0.00020  0.00170  0.02500  51  GLU A OE2   
414  N  N     . GLY A 56  ? 0.30660 0.29130 0.24260 0.00260  0.00260  0.02200  52  GLY A N     
415  C  CA    . GLY A 56  ? 0.31410 0.30340 0.24750 0.00220  0.00470  0.02420  52  GLY A CA    
416  C  C     . GLY A 56  ? 0.34830 0.34130 0.27890 0.00370  0.00630  0.02080  52  GLY A C     
417  O  O     . GLY A 56  ? 0.34280 0.33960 0.27390 0.00340  0.00880  0.02180  52  GLY A O     
418  N  N     . ALA A 57  ? 0.31650 0.30830 0.24470 0.00530  0.00500  0.01660  53  ALA A N     
419  C  CA    . ALA A 57  ? 0.32520 0.31930 0.25170 0.00720  0.00660  0.01270  53  ALA A CA    
420  C  C     . ALA A 57  ? 0.35670 0.35000 0.28870 0.00730  0.00790  0.01200  53  ALA A C     
421  O  O     . ALA A 57  ? 0.32570 0.32300 0.25840 0.00810  0.01040  0.01180  53  ALA A O     
422  C  CB    . ALA A 57  ? 0.33590 0.32760 0.25940 0.00860  0.00460  0.00820  53  ALA A CB    
423  N  N     . ALA A 58  ? 0.30160 0.29040 0.23780 0.00630  0.00640  0.01200  54  ALA A N     
424  C  CA    . ALA A 58  ? 0.26660 0.25520 0.20760 0.00590  0.00720  0.01170  54  ALA A CA    
425  C  C     . ALA A 58  ? 0.35030 0.34220 0.29330 0.00410  0.00900  0.01510  54  ALA A C     
426  O  O     . ALA A 58  ? 0.33910 0.33440 0.28460 0.00440  0.01050  0.01520  54  ALA A O     
427  C  CB    . ALA A 58  ? 0.27190 0.25570 0.21600 0.00490  0.00530  0.01120  54  ALA A CB    
428  N  N     . PHE A 59  ? 0.28940 0.28040 0.23190 0.00230  0.00880  0.01820  55  PHE A N     
429  C  CA    . PHE A 59  ? 0.27560 0.26930 0.22010 0.00010  0.01040  0.02160  55  PHE A CA    
430  C  C     . PHE A 59  ? 0.30550 0.30600 0.24830 0.00110  0.01280  0.02250  55  PHE A C     
431  O  O     . PHE A 59  ? 0.31270 0.31710 0.25870 0.00020  0.01430  0.02380  55  PHE A O     
432  C  CB    . PHE A 59  ? 0.25650 0.24770 0.20090 -0.00170 0.00970  0.02500  55  PHE A CB    
433  C  CG    . PHE A 59  ? 0.33170 0.31680 0.27920 -0.00300 0.00840  0.02460  55  PHE A CG    
434  C  CD1   . PHE A 59  ? 0.35930 0.34300 0.30980 -0.00420 0.00840  0.02270  55  PHE A CD1   
435  C  CD2   . PHE A 59  ? 0.32400 0.30530 0.27170 -0.00320 0.00720  0.02620  55  PHE A CD2   
436  C  CE1   . PHE A 59  ? 0.38220 0.36060 0.33480 -0.00550 0.00760  0.02180  55  PHE A CE1   
437  C  CE2   . PHE A 59  ? 0.34140 0.31720 0.29240 -0.00410 0.00660  0.02540  55  PHE A CE2   
438  C  CZ    . PHE A 59  ? 0.37030 0.34470 0.32330 -0.00530 0.00700  0.02290  55  PHE A CZ    
439  N  N     . MET A 60  ? 0.24220 0.24480 0.18000 0.00300  0.01310  0.02160  56  MET A N     
440  C  CA    . MET A 60  ? 0.28180 0.29130 0.21730 0.00420  0.01600  0.02210  56  MET A CA    
441  C  C     . MET A 60  ? 0.29640 0.30840 0.23470 0.00640  0.01750  0.01890  56  MET A C     
442  O  O     . MET A 60  ? 0.30970 0.32790 0.25030 0.00650  0.02010  0.02050  56  MET A O     
443  C  CB    . MET A 60  ? 0.29300 0.30410 0.22140 0.00570  0.01590  0.02090  56  MET A CB    
444  C  CG    . MET A 60  ? 0.43020 0.44160 0.35620 0.00360  0.01490  0.02560  56  MET A CG    
445  S  SD    . MET A 60  ? 0.49240 0.50680 0.40910 0.00500  0.01440  0.02430  56  MET A SD    
446  C  CE    . MET A 60  ? 0.54820 0.55850 0.46510 0.00280  0.01090  0.02900  56  MET A CE    
447  N  N     . ALA A 61  ? 0.31980 0.32760 0.25850 0.00820  0.01590  0.01490  57  ALA A N     
448  C  CA    . ALA A 61  ? 0.32590 0.33520 0.26860 0.01040  0.01700  0.01250  57  ALA A CA    
449  C  C     . ALA A 61  ? 0.32290 0.33440 0.27190 0.00830  0.01720  0.01550  57  ALA A C     
450  O  O     . ALA A 61  ? 0.30340 0.32010 0.25630 0.00950  0.01920  0.01580  57  ALA A O     
451  C  CB    . ALA A 61  ? 0.30820 0.31150 0.25120 0.01190  0.01470  0.00850  57  ALA A CB    
452  N  N     . GLU A 62  ? 0.33360 0.34140 0.28380 0.00520  0.01530  0.01750  58  GLU A N     
453  C  CA    . GLU A 62  ? 0.27680 0.28610 0.23210 0.00260  0.01500  0.02000  58  GLU A CA    
454  C  C     . GLU A 62  ? 0.31200 0.32780 0.26880 0.00100  0.01720  0.02360  58  GLU A C     
455  O  O     . GLU A 62  ? 0.31840 0.33930 0.28010 0.00040  0.01800  0.02500  58  GLU A O     
456  C  CB    . GLU A 62  ? 0.33400 0.33720 0.28940 -0.00030 0.01270  0.02040  58  GLU A CB    
457  C  CG    . GLU A 62  ? 0.40160 0.40470 0.36120 -0.00270 0.01160  0.02100  58  GLU A CG    
458  C  CD    . GLU A 62  ? 0.57040 0.57690 0.53250 -0.00610 0.01230  0.02430  58  GLU A CD    
459  O  OE1   . GLU A 62  ? 0.57620 0.58380 0.53700 -0.00700 0.01350  0.02650  58  GLU A OE1   
460  O  OE2   . GLU A 62  ? 0.55490 0.56320 0.52050 -0.00830 0.01140  0.02490  58  GLU A OE2   
461  N  N     . GLY A 63  ? 0.27260 0.28900 0.22590 0.00020  0.01810  0.02560  59  GLY A N     
462  C  CA    . GLY A 63  ? 0.25440 0.27730 0.20920 -0.00160 0.02030  0.02960  59  GLY A CA    
463  C  C     . GLY A 63  ? 0.37910 0.40990 0.33460 0.00140  0.02340  0.02890  59  GLY A C     
464  O  O     . GLY A 63  ? 0.35860 0.39610 0.31890 0.00040  0.02510  0.03160  59  GLY A O     
465  N  N     . TYR A 64  ? 0.30130 0.33170 0.25240 0.00510  0.02420  0.02520  60  TYR A N     
466  C  CA    . TYR A 64  ? 0.28290 0.31990 0.23460 0.00860  0.02750  0.02330  60  TYR A CA    
467  C  C     . TYR A 64  ? 0.28050 0.31980 0.23990 0.00970  0.02760  0.02290  60  TYR A C     
468  O  O     . TYR A 64  ? 0.32870 0.37610 0.29250 0.01070  0.03050  0.02450  60  TYR A O     
469  C  CB    . TYR A 64  ? 0.31160 0.34560 0.25730 0.01230  0.02770  0.01810  60  TYR A CB    
470  C  CG    . TYR A 64  ? 0.36220 0.40270 0.30830 0.01620  0.03170  0.01550  60  TYR A CG    
471  C  CD1   . TYR A 64  ? 0.31870 0.35910 0.27040 0.01930  0.03220  0.01270  60  TYR A CD1   
472  C  CD2   . TYR A 64  ? 0.39460 0.44170 0.33580 0.01680  0.03510  0.01630  60  TYR A CD2   
473  C  CE1   . TYR A 64  ? 0.38620 0.43250 0.33910 0.02340  0.03620  0.01010  60  TYR A CE1   
474  C  CE2   . TYR A 64  ? 0.45280 0.50630 0.39420 0.02060  0.03930  0.01350  60  TYR A CE2   
475  C  CZ    . TYR A 64  ? 0.46660 0.51940 0.41410 0.02410  0.04000  0.01030  60  TYR A CZ    
476  O  OH    . TYR A 64  ? 0.64550 0.70460 0.59390 0.02830  0.04460  0.00730  60  TYR A OH    
477  N  N     . ALA A 65  ? 0.29970 0.33270 0.26110 0.00950  0.02450  0.02110  61  ALA A N     
478  C  CA    . ALA A 65  ? 0.30140 0.33670 0.27010 0.01030  0.02400  0.02130  61  ALA A CA    
479  C  C     . ALA A 65  ? 0.32310 0.36410 0.29730 0.00670  0.02400  0.02600  61  ALA A C     
480  O  O     . ALA A 65  ? 0.31730 0.36550 0.29780 0.00780  0.02540  0.02760  61  ALA A O     
481  C  CB    . ALA A 65  ? 0.25780 0.28520 0.22660 0.01020  0.02050  0.01910  61  ALA A CB    
482  N  N     . ARG A 66  ? 0.31370 0.35150 0.28630 0.00220  0.02220  0.02830  62  ARG A N     
483  C  CA    . ARG A 66  ? 0.38990 0.43230 0.36770 -0.00180 0.02170  0.03230  62  ARG A CA    
484  C  C     . ARG A 66  ? 0.35840 0.41040 0.33900 -0.00180 0.02510  0.03560  62  ARG A C     
485  O  O     . ARG A 66  ? 0.33470 0.39400 0.32210 -0.00290 0.02550  0.03830  62  ARG A O     
486  C  CB    . ARG A 66  ? 0.31990 0.35600 0.29530 -0.00650 0.01930  0.03350  62  ARG A CB    
487  C  CG    . ARG A 66  ? 0.32840 0.35750 0.30340 -0.00770 0.01600  0.03120  62  ARG A CG    
488  C  CD    . ARG A 66  ? 0.35340 0.37750 0.32750 -0.01260 0.01420  0.03230  62  ARG A CD    
489  N  NE    . ARG A 66  ? 0.32600 0.35560 0.30490 -0.01650 0.01420  0.03570  62  ARG A NE    
490  C  CZ    . ARG A 66  ? 0.40980 0.43590 0.38930 -0.02130 0.01260  0.03670  62  ARG A CZ    
491  N  NH1   . ARG A 66  ? 0.34870 0.36580 0.32430 -0.02220 0.01140  0.03440  62  ARG A NH1   
492  N  NH2   . ARG A 66  ? 0.40380 0.43520 0.38790 -0.02520 0.01230  0.03980  62  ARG A NH2   
493  N  N     . VAL A 67  ? 0.33900 0.39200 0.31460 -0.00070 0.02750  0.03580  63  VAL A N     
494  C  CA    . VAL A 67  ? 0.32380 0.38660 0.30160 -0.00090 0.03110  0.03930  63  VAL A CA    
495  C  C     . VAL A 67  ? 0.37510 0.44520 0.35620 0.00400  0.03440  0.03740  63  VAL A C     
496  O  O     . VAL A 67  ? 0.34230 0.42200 0.32990 0.00380  0.03670  0.04060  63  VAL A O     
497  C  CB    . VAL A 67  ? 0.30460 0.36660 0.27540 -0.00160 0.03260  0.04070  63  VAL A CB    
498  C  CG1   . VAL A 67  ? 0.27170 0.34510 0.24390 -0.00090 0.03720  0.04390  63  VAL A CG1   
499  C  CG2   . VAL A 67  ? 0.24670 0.30290 0.21700 -0.00670 0.02990  0.04390  63  VAL A CG2   
500  N  N     . SER A 68  ? 0.31270 0.37860 0.29020 0.00860  0.03470  0.03230  64  SER A N     
501  C  CA    . SER A 68  ? 0.38020 0.45220 0.36090 0.01380  0.03820  0.02990  64  SER A CA    
502  C  C     . SER A 68  ? 0.35850 0.43310 0.34880 0.01490  0.03700  0.03060  64  SER A C     
503  O  O     . SER A 68  ? 0.34280 0.42520 0.33890 0.01840  0.04020  0.03070  64  SER A O     
504  C  CB    . SER A 68  ? 0.38120 0.44720 0.35520 0.01820  0.03880  0.02380  64  SER A CB    
505  O  OG    . SER A 68  ? 0.39790 0.45480 0.37230 0.01860  0.03490  0.02100  64  SER A OG    
506  N  N     . GLY A 69  ? 0.36500 0.43380 0.35710 0.01200  0.03250  0.03130  65  GLY A N     
507  C  CA    . GLY A 69  ? 0.31590 0.38630 0.31580 0.01350  0.03080  0.03160  65  GLY A CA    
508  C  C     . GLY A 69  ? 0.39190 0.45730 0.39140 0.01880  0.03100  0.02700  65  GLY A C     
509  O  O     . GLY A 69  ? 0.41270 0.48000 0.41960 0.02090  0.03010  0.02760  65  GLY A O     
510  N  N     . LYS A 70  ? 0.32200 0.38080 0.31350 0.02070  0.03180  0.02260  66  LYS A N     
511  C  CA    . LYS A 70  ? 0.32790 0.38110 0.31860 0.02540  0.03190  0.01760  66  LYS A CA    
512  C  C     . LYS A 70  ? 0.33300 0.37530 0.31760 0.02350  0.02800  0.01530  66  LYS A C     
513  O  O     . LYS A 70  ? 0.40480 0.44440 0.38610 0.01910  0.02560  0.01740  66  LYS A O     
514  C  CB    . LYS A 70  ? 0.37200 0.42770 0.35860 0.02960  0.03650  0.01370  66  LYS A CB    
515  C  CG    . LYS A 70  ? 0.45950 0.52660 0.45260 0.03210  0.04110  0.01560  66  LYS A CG    
516  C  CD    . LYS A 70  ? 0.56780 0.63610 0.55760 0.03740  0.04570  0.01020  66  LYS A CD    
517  C  CE    . LYS A 70  ? 0.68600 0.75440 0.66460 0.03570  0.04740  0.00890  66  LYS A CE    
518  N  NZ    . LYS A 70  ? 0.80780 0.88120 0.78300 0.04030  0.05300  0.00450  66  LYS A NZ    
519  N  N     . LEU A 71  ? 0.30720 0.34340 0.29060 0.02700  0.02760  0.01090  67  LEU A N     
520  C  CA    . LEU A 71  ? 0.37510 0.40180 0.35360 0.02550  0.02410  0.00860  67  LEU A CA    
521  C  C     . LEU A 71  ? 0.39390 0.41780 0.36290 0.02430  0.02450  0.00650  67  LEU A C     
522  O  O     . LEU A 71  ? 0.40830 0.43470 0.37350 0.02670  0.02760  0.00390  67  LEU A O     
523  C  CB    . LEU A 71  ? 0.34490 0.36610 0.32590 0.02950  0.02340  0.00470  67  LEU A CB    
524  C  CG    . LEU A 71  ? 0.36320 0.37490 0.34000 0.02830  0.02000  0.00220  67  LEU A CG    
525  C  CD1   . LEU A 71  ? 0.33740 0.34700 0.31780 0.02500  0.01630  0.00600  67  LEU A CD1   
526  C  CD2   . LEU A 71  ? 0.39290 0.39930 0.37070 0.03250  0.02040  -0.00270 67  LEU A CD2   
527  N  N     . GLY A 72  ? 0.33260 0.35180 0.29790 0.02050  0.02160  0.00790  68  GLY A N     
528  C  CA    . GLY A 72  ? 0.33040 0.34630 0.28770 0.01940  0.02110  0.00630  68  GLY A CA    
529  C  C     . GLY A 72  ? 0.37990 0.38770 0.33450 0.02040  0.01850  0.00240  68  GLY A C     
530  O  O     . GLY A 72  ? 0.33170 0.33560 0.29040 0.02010  0.01620  0.00260  68  GLY A O     
531  N  N     . VAL A 73  ? 0.25100 0.25690 0.19880 0.02130  0.01880  -0.00070 69  VAL A N     
532  C  CA    . VAL A 73  ? 0.27150 0.27030 0.21700 0.02210  0.01630  -0.00470 69  VAL A CA    
533  C  C     . VAL A 73  ? 0.34630 0.34300 0.28480 0.01990  0.01450  -0.00470 69  VAL A C     
534  O  O     . VAL A 73  ? 0.33110 0.33180 0.26410 0.01980  0.01610  -0.00450 69  VAL A O     
535  C  CB    . VAL A 73  ? 0.34240 0.34040 0.28730 0.02610  0.01810  -0.01010 69  VAL A CB    
536  C  CG1   . VAL A 73  ? 0.29290 0.28270 0.23630 0.02630  0.01490  -0.01410 69  VAL A CG1   
537  C  CG2   . VAL A 73  ? 0.33110 0.33220 0.28390 0.02890  0.02030  -0.00960 69  VAL A CG2   
538  N  N     . CYS A 74  ? 0.30590 0.29700 0.24500 0.01810  0.01110  -0.00450 70  CYS A N     
539  C  CA    . CYS A 74  ? 0.25290 0.24160 0.18680 0.01630  0.00880  -0.00450 70  CYS A CA    
540  C  C     . CYS A 74  ? 0.26160 0.24420 0.19550 0.01670  0.00590  -0.00820 70  CYS A C     
541  O  O     . CYS A 74  ? 0.30750 0.28700 0.24650 0.01760  0.00530  -0.00930 70  CYS A O     
542  C  CB    . CYS A 74  ? 0.29460 0.28330 0.23000 0.01330  0.00770  0.00020  70  CYS A CB    
543  S  SG    . CYS A 74  ? 0.55930 0.54480 0.50170 0.01190  0.00630  0.00200  70  CYS A SG    
544  N  N     . CYS A 75  ? 0.33790 0.31920 0.26640 0.01600  0.00410  -0.00990 71  CYS A N     
545  C  CA    . CYS A 75  ? 0.28570 0.26140 0.21450 0.01580  0.00100  -0.01320 71  CYS A CA    
546  C  C     . CYS A 75  ? 0.37260 0.34730 0.29960 0.01320  -0.00220 -0.01110 71  CYS A C     
547  O  O     . CYS A 75  ? 0.35880 0.33690 0.28190 0.01220  -0.00200 -0.00850 71  CYS A O     
548  C  CB    . CYS A 75  ? 0.30210 0.27650 0.22660 0.01790  0.00150  -0.01910 71  CYS A CB    
549  S  SG    . CYS A 75  ? 0.43350 0.41280 0.34780 0.01750  0.00220  -0.02020 71  CYS A SG    
550  N  N     . ALA A 76  ? 0.36210 0.33230 0.29270 0.01220  -0.00500 -0.01160 72  ALA A N     
551  C  CA    . ALA A 76  ? 0.36600 0.33570 0.29610 0.01000  -0.00810 -0.00970 72  ALA A CA    
552  C  C     . ALA A 76  ? 0.36230 0.32760 0.29370 0.00930  -0.01130 -0.01290 72  ALA A C     
553  O  O     . ALA A 76  ? 0.40920 0.37080 0.34380 0.01030  -0.01120 -0.01550 72  ALA A O     
554  C  CB    . ALA A 76  ? 0.30340 0.27350 0.23850 0.00870  -0.00780 -0.00500 72  ALA A CB    
555  N  N     . THR A 77  ? 0.36650 0.33220 0.29590 0.00760  -0.01440 -0.01240 73  THR A N     
556  C  CA    . THR A 77  ? 0.36800 0.33000 0.29910 0.00630  -0.01790 -0.01500 73  THR A CA    
557  C  C     . THR A 77  ? 0.33740 0.29760 0.27640 0.00500  -0.01890 -0.01200 73  THR A C     
558  O  O     . THR A 77  ? 0.33270 0.29410 0.27510 0.00530  -0.01680 -0.00850 73  THR A O     
559  C  CB    . THR A 77  ? 0.36260 0.32680 0.28870 0.00460  -0.02120 -0.01540 73  THR A CB    
560  O  OG1   . THR A 77  ? 0.34720 0.30760 0.27450 0.00310  -0.02480 -0.01870 73  THR A OG1   
561  C  CG2   . THR A 77  ? 0.34200 0.30970 0.27080 0.00330  -0.02220 -0.00960 73  THR A CG2   
562  N  N     . THR A 78  ? 0.32800 0.28510 0.26970 0.00350  -0.02210 -0.01350 74  THR A N     
563  C  CA    . THR A 78  ? 0.39610 0.35210 0.34520 0.00200  -0.02320 -0.01070 74  THR A CA    
564  C  C     . THR A 78  ? 0.39780 0.35780 0.34930 0.00140  -0.02240 -0.00580 74  THR A C     
565  O  O     . THR A 78  ? 0.38660 0.34970 0.33450 0.00150  -0.02250 -0.00450 74  THR A O     
566  C  CB    . THR A 78  ? 0.33570 0.28920 0.28680 -0.00030 -0.02740 -0.01250 74  THR A CB    
567  O  OG1   . THR A 78  ? 0.36710 0.32260 0.31240 -0.00110 -0.02980 -0.01430 74  THR A OG1   
568  C  CG2   . THR A 78  ? 0.37190 0.31960 0.32490 -0.00000 -0.02790 -0.01630 74  THR A CG2   
569  N  N     . GLY A 79  ? 0.38860 0.34840 0.34610 0.00070  -0.02160 -0.00310 75  GLY A N     
570  C  CA    . GLY A 79  ? 0.30630 0.26910 0.26720 0.00000  -0.02120 0.00070  75  GLY A CA    
571  C  C     . GLY A 79  ? 0.35790 0.32320 0.31610 0.00130  -0.01870 0.00260  75  GLY A C     
572  O  O     . GLY A 79  ? 0.37540 0.34040 0.33270 0.00220  -0.01580 0.00280  75  GLY A O     
573  N  N     . PRO A 80  ? 0.30110 0.26900 0.25830 0.00110  -0.02000 0.00440  76  PRO A N     
574  C  CA    . PRO A 80  ? 0.33170 0.30150 0.28790 0.00210  -0.01780 0.00710  76  PRO A CA    
575  C  C     . PRO A 80  ? 0.33760 0.30770 0.28780 0.00310  -0.01620 0.00600  76  PRO A C     
576  O  O     . PRO A 80  ? 0.35250 0.32330 0.30250 0.00360  -0.01370 0.00810  76  PRO A O     
577  C  CB    . PRO A 80  ? 0.30800 0.28060 0.26550 0.00160  -0.02040 0.00970  76  PRO A CB    
578  C  CG    . PRO A 80  ? 0.31920 0.29190 0.27350 0.00060  -0.02410 0.00700  76  PRO A CG    
579  C  CD    . PRO A 80  ? 0.28690 0.25620 0.24330 0.00000  -0.02400 0.00400  76  PRO A CD    
580  N  N     . GLY A 81  ? 0.29510 0.26460 0.24040 0.00330  -0.01740 0.00270  77  GLY A N     
581  C  CA    . GLY A 81  ? 0.38860 0.35900 0.32880 0.00440  -0.01500 0.00150  77  GLY A CA    
582  C  C     . GLY A 81  ? 0.33180 0.30090 0.27460 0.00510  -0.01190 0.00160  77  GLY A C     
583  O  O     . GLY A 81  ? 0.33420 0.30500 0.27610 0.00550  -0.00950 0.00350  77  GLY A O     
584  N  N     . ALA A 82  ? 0.37300 0.33950 0.31940 0.00500  -0.01210 0.00010  78  ALA A N     
585  C  CA    . ALA A 82  ? 0.34360 0.30950 0.29250 0.00540  -0.00970 0.00050  78  ALA A CA    
586  C  C     . ALA A 82  ? 0.39030 0.35720 0.34220 0.00450  -0.00820 0.00370  78  ALA A C     
587  O  O     . ALA A 82  ? 0.38520 0.35310 0.33700 0.00460  -0.00600 0.00460  78  ALA A O     
588  C  CB    . ALA A 82  ? 0.28990 0.25300 0.24240 0.00530  -0.01080 -0.00110 78  ALA A CB    
589  N  N     . THR A 83  ? 0.31910 0.28580 0.27390 0.00360  -0.00940 0.00520  79  THR A N     
590  C  CA    . THR A 83  ? 0.36360 0.33060 0.32110 0.00290  -0.00750 0.00740  79  THR A CA    
591  C  C     . THR A 83  ? 0.30260 0.27060 0.25790 0.00320  -0.00610 0.00900  79  THR A C     
592  O  O     . THR A 83  ? 0.29640 0.26420 0.25290 0.00270  -0.00400 0.01000  79  THR A O     
593  C  CB    . THR A 83  ? 0.39270 0.35980 0.35460 0.00230  -0.00850 0.00860  79  THR A CB    
594  O  OG1   . THR A 83  ? 0.34640 0.31460 0.30790 0.00260  -0.01070 0.00940  79  THR A OG1   
595  C  CG2   . THR A 83  ? 0.29680 0.26310 0.26150 0.00150  -0.00950 0.00770  79  THR A CG2   
596  N  N     . ASN A 84  ? 0.28010 0.24950 0.23220 0.00380  -0.00730 0.00940  80  ASN A N     
597  C  CA    . ASN A 84  ? 0.30680 0.27740 0.25700 0.00390  -0.00610 0.01170  80  ASN A CA    
598  C  C     . ASN A 84  ? 0.33280 0.30420 0.28110 0.00390  -0.00380 0.01130  80  ASN A C     
599  O  O     . ASN A 84  ? 0.30930 0.28100 0.25780 0.00330  -0.00220 0.01340  80  ASN A O     
600  C  CB    . ASN A 84  ? 0.31490 0.28770 0.26120 0.00430  -0.00810 0.01240  80  ASN A CB    
601  C  CG    . ASN A 84  ? 0.35710 0.33040 0.30620 0.00420  -0.00990 0.01550  80  ASN A CG    
602  O  OD1   . ASN A 84  ? 0.31130 0.28310 0.26570 0.00410  -0.00940 0.01650  80  ASN A OD1   
603  N  ND2   . ASN A 84  ? 0.38910 0.36500 0.33470 0.00420  -0.01190 0.01710  80  ASN A ND2   
604  N  N     . ALA A 85  ? 0.27090 0.24240 0.21810 0.00440  -0.00350 0.00880  81  ALA A N     
605  C  CA    . ALA A 85  ? 0.31800 0.29130 0.26450 0.00450  -0.00130 0.00870  81  ALA A CA    
606  C  C     . ALA A 85  ? 0.31750 0.28990 0.26730 0.00330  -0.00010 0.00940  81  ALA A C     
607  O  O     . ALA A 85  ? 0.32510 0.29930 0.27490 0.00280  0.00150  0.01010  81  ALA A O     
608  C  CB    . ALA A 85  ? 0.23950 0.21340 0.18450 0.00600  -0.00140 0.00580  81  ALA A CB    
609  N  N     . LEU A 86  ? 0.30730 0.27750 0.25990 0.00250  -0.00070 0.00930  82  LEU A N     
610  C  CA    . LEU A 86  ? 0.27590 0.24580 0.23060 0.00130  0.00010  0.00920  82  LEU A CA    
611  C  C     . LEU A 86  ? 0.24800 0.21870 0.20270 -0.00020 0.00190  0.01050  82  LEU A C     
612  O  O     . LEU A 86  ? 0.31230 0.28450 0.26740 -0.00110 0.00250  0.01050  82  LEU A O     
613  C  CB    . LEU A 86  ? 0.34110 0.30930 0.29830 0.00060  -0.00030 0.00900  82  LEU A CB    
614  C  CG    . LEU A 86  ? 0.46590 0.43480 0.42420 -0.00080 0.00030  0.00890  82  LEU A CG    
615  C  CD1   . LEU A 86  ? 0.38000 0.34860 0.34020 -0.00080 -0.00090 0.00850  82  LEU A CD1   
616  C  CD2   . LEU A 86  ? 0.43110 0.39950 0.38960 -0.00250 0.00200  0.00910  82  LEU A CD2   
617  N  N     . THR A 87  ? 0.26720 0.23660 0.22180 -0.00060 0.00240  0.01180  83  THR A N     
618  C  CA    . THR A 87  ? 0.27230 0.24140 0.22730 -0.00240 0.00390  0.01280  83  THR A CA    
619  C  C     . THR A 87  ? 0.35860 0.33120 0.31250 -0.00270 0.00450  0.01360  83  THR A C     
620  O  O     . THR A 87  ? 0.33210 0.30580 0.28680 -0.00450 0.00520  0.01380  83  THR A O     
621  C  CB    . THR A 87  ? 0.22970 0.19650 0.18560 -0.00250 0.00430  0.01450  83  THR A CB    
622  O  OG1   . THR A 87  ? 0.25130 0.21530 0.20940 -0.00210 0.00420  0.01370  83  THR A OG1   
623  C  CG2   . THR A 87  ? 0.27410 0.23980 0.23070 -0.00470 0.00560  0.01540  83  THR A CG2   
624  N  N     . GLY A 88  ? 0.23420 0.20900 0.18610 -0.00100 0.00430  0.01400  84  GLY A N     
625  C  CA    . GLY A 88  ? 0.23480 0.21370 0.18610 -0.00100 0.00550  0.01480  84  GLY A CA    
626  C  C     . GLY A 88  ? 0.29690 0.27780 0.24990 -0.00070 0.00540  0.01350  84  GLY A C     
627  O  O     . GLY A 88  ? 0.32990 0.31390 0.28450 -0.00190 0.00630  0.01460  84  GLY A O     
628  N  N     . ILE A 89  ? 0.29420 0.27350 0.24750 0.00060  0.00420  0.01170  85  ILE A N     
629  C  CA    . ILE A 89  ? 0.30390 0.28470 0.25960 0.00090  0.00390  0.01110  85  ILE A CA    
630  C  C     . ILE A 89  ? 0.37610 0.35710 0.33340 -0.00180 0.00380  0.01200  85  ILE A C     
631  O  O     . ILE A 89  ? 0.31290 0.29710 0.27210 -0.00250 0.00380  0.01290  85  ILE A O     
632  C  CB    . ILE A 89  ? 0.30470 0.28300 0.26080 0.00260  0.00240  0.00930  85  ILE A CB    
633  C  CG1   . ILE A 89  ? 0.24980 0.22780 0.20340 0.00490  0.00230  0.00760  85  ILE A CG1   
634  C  CG2   . ILE A 89  ? 0.22060 0.20020 0.17990 0.00290  0.00190  0.00950  85  ILE A CG2   
635  C  CD1   . ILE A 89  ? 0.29980 0.28160 0.25300 0.00660  0.00400  0.00740  85  ILE A CD1   
636  N  N     . ALA A 90  ? 0.29940 0.27710 0.25600 -0.00340 0.00360  0.01180  86  ALA A N     
637  C  CA    . ALA A 90  ? 0.32270 0.30040 0.27980 -0.00630 0.00370  0.01190  86  ALA A CA    
638  C  C     . ALA A 90  ? 0.34970 0.32970 0.30720 -0.00830 0.00450  0.01320  86  ALA A C     
639  O  O     . ALA A 90  ? 0.31040 0.29250 0.26850 -0.01070 0.00410  0.01350  86  ALA A O     
640  C  CB    . ALA A 90  ? 0.29710 0.27080 0.25350 -0.00710 0.00410  0.01080  86  ALA A CB    
641  N  N     . CYS A 91  ? 0.32490 0.30520 0.28200 -0.00770 0.00540  0.01430  87  CYS A N     
642  C  CA    . CYS A 91  ? 0.36200 0.34490 0.32010 -0.01000 0.00610  0.01600  87  CYS A CA    
643  C  C     . CYS A 91  ? 0.36790 0.35680 0.32800 -0.00950 0.00610  0.01720  87  CYS A C     
644  O  O     . CYS A 91  ? 0.30380 0.29570 0.26570 -0.01210 0.00570  0.01820  87  CYS A O     
645  C  CB    . CYS A 91  ? 0.37260 0.35460 0.33010 -0.00980 0.00710  0.01760  87  CYS A CB    
646  S  SG    . CYS A 91  ? 0.41150 0.38670 0.36840 -0.01040 0.00720  0.01720  87  CYS A SG    
647  N  N     . ALA A 92  ? 0.30350 0.29410 0.26360 -0.00610 0.00630  0.01680  88  ALA A N     
648  C  CA    . ALA A 92  ? 0.26250 0.25860 0.22550 -0.00480 0.00650  0.01760  88  ALA A CA    
649  C  C     . ALA A 92  ? 0.31700 0.31400 0.28210 -0.00630 0.00490  0.01790  88  ALA A C     
650  O  O     . ALA A 92  ? 0.30840 0.31060 0.27680 -0.00740 0.00460  0.01970  88  ALA A O     
651  C  CB    . ALA A 92  ? 0.22810 0.22410 0.19050 -0.00080 0.00710  0.01610  88  ALA A CB    
652  N  N     . TYR A 93  ? 0.27230 0.26520 0.23590 -0.00660 0.00380  0.01640  89  TYR A N     
653  C  CA    . TYR A 93  ? 0.29310 0.28730 0.25790 -0.00830 0.00220  0.01710  89  TYR A CA    
654  C  C     . TYR A 93  ? 0.25510 0.25130 0.21960 -0.01250 0.00170  0.01790  89  TYR A C     
655  O  O     . TYR A 93  ? 0.30340 0.30420 0.27000 -0.01410 0.00050  0.01960  89  TYR A O     
656  C  CB    . TYR A 93  ? 0.35580 0.34550 0.31870 -0.00800 0.00150  0.01550  89  TYR A CB    
657  C  CG    . TYR A 93  ? 0.35130 0.34250 0.31470 -0.00990 -0.00000 0.01640  89  TYR A CG    
658  C  CD1   . TYR A 93  ? 0.30340 0.29680 0.26990 -0.00830 -0.00130 0.01810  89  TYR A CD1   
659  C  CD2   . TYR A 93  ? 0.29130 0.28130 0.25170 -0.01330 -0.00010 0.01560  89  TYR A CD2   
660  C  CE1   . TYR A 93  ? 0.34640 0.34170 0.31320 -0.01020 -0.00290 0.01970  89  TYR A CE1   
661  C  CE2   . TYR A 93  ? 0.36330 0.35540 0.32320 -0.01530 -0.00150 0.01650  89  TYR A CE2   
662  C  CZ    . TYR A 93  ? 0.38950 0.38450 0.35250 -0.01390 -0.00300 0.01890  89  TYR A CZ    
663  O  OH    . TYR A 93  ? 0.43890 0.43640 0.40120 -0.01610 -0.00440 0.02050  89  TYR A OH    
664  N  N     . SER A 94  ? 0.27730 0.26980 0.23940 -0.01440 0.00260  0.01670  90  SER A N     
665  C  CA    . SER A 94  ? 0.28220 0.27510 0.24360 -0.01880 0.00210  0.01670  90  SER A CA    
666  C  C     . SER A 94  ? 0.31510 0.31330 0.27950 -0.02020 0.00220  0.01910  90  SER A C     
667  O  O     . SER A 94  ? 0.34380 0.34460 0.30880 -0.02410 0.00090  0.01970  90  SER A O     
668  C  CB    . SER A 94  ? 0.30930 0.29590 0.26810 -0.02000 0.00320  0.01460  90  SER A CB    
669  O  OG    . SER A 94  ? 0.46400 0.44660 0.42070 -0.01860 0.00340  0.01250  90  SER A OG    
670  N  N     . ASP A 95  ? 0.26480 0.26520 0.23110 -0.01750 0.00350  0.02050  91  ASP A N     
671  C  CA    . ASP A 95  ? 0.34730 0.35360 0.31700 -0.01860 0.00400  0.02310  91  ASP A CA    
672  C  C     . ASP A 95  ? 0.33630 0.34970 0.31030 -0.01620 0.00380  0.02500  91  ASP A C     
673  O  O     . ASP A 95  ? 0.36850 0.38810 0.34640 -0.01650 0.00460  0.02750  91  ASP A O     
674  C  CB    . ASP A 95  ? 0.28620 0.29150 0.25540 -0.01750 0.00610  0.02390  91  ASP A CB    
675  C  CG    . ASP A 95  ? 0.43440 0.43330 0.40130 -0.02040 0.00620  0.02320  91  ASP A CG    
676  O  OD1   . ASP A 95  ? 0.40670 0.40340 0.37320 -0.02410 0.00490  0.02210  91  ASP A OD1   
677  O  OD2   . ASP A 95  ? 0.46960 0.46570 0.43510 -0.01900 0.00750  0.02360  91  ASP A OD2   
678  N  N     . SER A 96  ? 0.28770 0.30050 0.26190 -0.01380 0.00290  0.02420  92  SER A N     
679  C  CA    . SER A 96  ? 0.28030 0.29880 0.25940 -0.01100 0.00260  0.02600  92  SER A CA    
680  C  C     . SER A 96  ? 0.32300 0.34430 0.30420 -0.00710 0.00530  0.02630  92  SER A C     
681  O  O     . SER A 96  ? 0.30250 0.33090 0.28890 -0.00610 0.00600  0.02850  92  SER A O     
682  C  CB    . SER A 96  ? 0.28300 0.30840 0.26620 -0.01420 0.00070  0.02900  92  SER A CB    
683  O  OG    . SER A 96  ? 0.38960 0.41250 0.36950 -0.01810 -0.00160 0.02830  92  SER A OG    
684  N  N     . THR A 97  ? 0.35630 0.37250 0.33350 -0.00480 0.00670  0.02380  93  THR A N     
685  C  CA    . THR A 97  ? 0.27510 0.29330 0.25230 -0.00110 0.00930  0.02320  93  THR A CA    
686  C  C     . THR A 97  ? 0.30300 0.31840 0.28020 0.00320  0.00940  0.02070  93  THR A C     
687  O  O     . THR A 97  ? 0.31510 0.32430 0.28920 0.00330  0.00800  0.01870  93  THR A O     
688  C  CB    . THR A 97  ? 0.31810 0.33310 0.29040 -0.00210 0.01050  0.02260  93  THR A CB    
689  O  OG1   . THR A 97  ? 0.35340 0.36940 0.32620 -0.00650 0.01020  0.02480  93  THR A OG1   
690  C  CG2   . THR A 97  ? 0.32490 0.34350 0.29650 0.00110  0.01340  0.02230  93  THR A CG2   
691  N  N     . PRO A 98  ? 0.31940 0.33910 0.30030 0.00690  0.01120  0.02060  94  PRO A N     
692  C  CA    . PRO A 98  ? 0.29200 0.30810 0.27320 0.01110  0.01130  0.01770  94  PRO A CA    
693  C  C     . PRO A 98  ? 0.35870 0.37050 0.33370 0.01280  0.01260  0.01420  94  PRO A C     
694  O  O     . PRO A 98  ? 0.33480 0.35000 0.30850 0.01480  0.01530  0.01330  94  PRO A O     
695  C  CB    . PRO A 98  ? 0.30240 0.32480 0.29030 0.01450  0.01310  0.01860  94  PRO A CB    
696  C  CG    . PRO A 98  ? 0.29890 0.32870 0.28790 0.01290  0.01520  0.02120  94  PRO A CG    
697  C  CD    . PRO A 98  ? 0.28840 0.31670 0.27470 0.00740  0.01300  0.02330  94  PRO A CD    
698  N  N     . VAL A 99  ? 0.37360 0.37860 0.34460 0.01180  0.01060  0.01250  95  VAL A N     
699  C  CA    . VAL A 99  ? 0.35160 0.35260 0.31690 0.01300  0.01100  0.00950  95  VAL A CA    
700  C  C     . VAL A 99  ? 0.35690 0.35230 0.32260 0.01480  0.00930  0.00660  95  VAL A C     
701  O  O     . VAL A 99  ? 0.31990 0.31240 0.28780 0.01340  0.00700  0.00760  95  VAL A O     
702  C  CB    . VAL A 99  ? 0.31630 0.31480 0.27710 0.00970  0.01010  0.01050  95  VAL A CB    
703  C  CG1   . VAL A 99  ? 0.28030 0.27490 0.23570 0.01090  0.00970  0.00780  95  VAL A CG1   
704  C  CG2   . VAL A 99  ? 0.33100 0.33460 0.29170 0.00780  0.01190  0.01330  95  VAL A CG2   
705  N  N     . LEU A 100 ? 0.33850 0.33240 0.30220 0.01790  0.01040  0.00310  96  LEU A N     
706  C  CA    . LEU A 100 ? 0.31780 0.30570 0.28170 0.01940  0.00860  0.00000  96  LEU A CA    
707  C  C     . LEU A 100 ? 0.37870 0.36270 0.33610 0.01820  0.00730  -0.00210 96  LEU A C     
708  O  O     . LEU A 100 ? 0.30780 0.29370 0.26010 0.01880  0.00890  -0.00360 96  LEU A O     
709  C  CB    . LEU A 100 ? 0.29030 0.27830 0.25670 0.02370  0.01040  -0.00330 96  LEU A CB    
710  C  CG    . LEU A 100 ? 0.34500 0.32600 0.31090 0.02540  0.00880  -0.00760 96  LEU A CG    
711  C  CD1   . LEU A 100 ? 0.36300 0.33930 0.33360 0.02390  0.00570  -0.00560 96  LEU A CD1   
712  C  CD2   . LEU A 100 ? 0.31590 0.29710 0.28400 0.02980  0.01140  -0.01130 96  LEU A CD2   
713  N  N     . LEU A 101 ? 0.30510 0.28450 0.26290 0.01630  0.00460  -0.00170 97  LEU A N     
714  C  CA    . LEU A 101 ? 0.38200 0.35780 0.33530 0.01520  0.00280  -0.00350 97  LEU A CA    
715  C  C     . LEU A 101 ? 0.29410 0.26470 0.24830 0.01670  0.00110  -0.00710 97  LEU A C     
716  O  O     . LEU A 101 ? 0.32120 0.28900 0.28020 0.01630  -0.00040 -0.00620 97  LEU A O     
717  C  CB    . LEU A 101 ? 0.36280 0.33740 0.31640 0.01210  0.00120  -0.00070 97  LEU A CB    
718  C  CG    . LEU A 101 ? 0.35690 0.32810 0.30760 0.01110  -0.00100 -0.00180 97  LEU A CG    
719  C  CD1   . LEU A 101 ? 0.32480 0.29800 0.26980 0.01130  -0.00050 -0.00260 97  LEU A CD1   
720  C  CD2   . LEU A 101 ? 0.28830 0.25860 0.24090 0.00850  -0.00210 0.00090  97  LEU A CD2   
721  N  N     . LEU A 102 ? 0.24800 0.21760 0.19760 0.01800  0.00130  -0.01100 98  LEU A N     
722  C  CA    . LEU A 102 ? 0.29120 0.25510 0.24070 0.01880  -0.00070 -0.01510 98  LEU A CA    
723  C  C     . LEU A 102 ? 0.37420 0.33600 0.32060 0.01610  -0.00370 -0.01510 98  LEU A C     
724  O  O     . LEU A 102 ? 0.34520 0.30950 0.28590 0.01530  -0.00360 -0.01520 98  LEU A O     
725  C  CB    . LEU A 102 ? 0.34810 0.31210 0.29380 0.02160  0.00120  -0.02020 98  LEU A CB    
726  C  CG    . LEU A 102 ? 0.41490 0.38280 0.36340 0.02470  0.00490  -0.02020 98  LEU A CG    
727  C  CD1   . LEU A 102 ? 0.36710 0.33610 0.31040 0.02740  0.00740  -0.02560 98  LEU A CD1   
728  C  CD2   . LEU A 102 ? 0.34770 0.31250 0.30490 0.02620  0.00440  -0.01930 98  LEU A CD2   
729  N  N     . THR A 103 ? 0.34700 0.30470 0.29730 0.01470  -0.00640 -0.01460 99  THR A N     
730  C  CA    . THR A 103 ? 0.38300 0.33920 0.33140 0.01230  -0.00930 -0.01450 99  THR A CA    
731  C  C     . THR A 103 ? 0.35430 0.30510 0.30320 0.01220  -0.01190 -0.01860 99  THR A C     
732  O  O     . THR A 103 ? 0.31760 0.26450 0.27070 0.01350  -0.01190 -0.02020 99  THR A O     
733  C  CB    . THR A 103 ? 0.32180 0.27850 0.27430 0.01000  -0.01030 -0.01000 99  THR A CB    
734  O  OG1   . THR A 103 ? 0.34900 0.30300 0.30760 0.00990  -0.01090 -0.00900 99  THR A OG1   
735  C  CG2   . THR A 103 ? 0.28200 0.24320 0.23380 0.00970  -0.00790 -0.00650 99  THR A CG2   
736  N  N     . ALA A 104 ? 0.31210 0.26250 0.25700 0.01050  -0.01440 -0.02020 100 ALA A N     
737  C  CA    . ALA A 104 ? 0.35960 0.30470 0.30520 0.00960  -0.01750 -0.02400 100 ALA A CA    
738  C  C     . ALA A 104 ? 0.37450 0.31750 0.32660 0.00700  -0.02010 -0.02080 100 ALA A C     
739  O  O     . ALA A 104 ? 0.33450 0.28100 0.28890 0.00570  -0.01980 -0.01610 100 ALA A O     
740  C  CB    . ALA A 104 ? 0.33390 0.28000 0.27210 0.00850  -0.01950 -0.02720 100 ALA A CB    
741  N  N     . GLN A 105 ? 0.35860 0.29610 0.31390 0.00620  -0.02250 -0.02340 101 GLN A N     
742  C  CA    . GLN A 105 ? 0.36970 0.30510 0.33140 0.00350  -0.02530 -0.02070 101 GLN A CA    
743  C  C     . GLN A 105 ? 0.41720 0.34860 0.37770 0.00140  -0.02920 -0.02480 101 GLN A C     
744  O  O     . GLN A 105 ? 0.38050 0.30850 0.33650 0.00270  -0.02940 -0.03050 101 GLN A O     
745  C  CB    . GLN A 105 ? 0.32910 0.26130 0.29780 0.00440  -0.02440 -0.01870 101 GLN A CB    
746  C  CG    . GLN A 105 ? 0.36180 0.29210 0.33740 0.00140  -0.02700 -0.01540 101 GLN A CG    
747  C  CD    . GLN A 105 ? 0.45090 0.38710 0.42740 -0.00050 -0.02660 -0.01030 101 GLN A CD    
748  O  OE1   . GLN A 105 ? 0.40910 0.34710 0.38530 -0.00270 -0.02870 -0.01000 101 GLN A OE1   
749  N  NE2   . GLN A 105 ? 0.45430 0.39400 0.43210 0.00040  -0.02380 -0.00660 101 GLN A NE2   
750  N  N     . VAL A 106 ? 0.35570 0.28770 0.32020 -0.00180 -0.03230 -0.02210 102 VAL A N     
751  C  CA    . VAL A 106 ? 0.41200 0.34030 0.37620 -0.00450 -0.03660 -0.02580 102 VAL A CA    
752  C  C     . VAL A 106 ? 0.40390 0.32390 0.37210 -0.00410 -0.03750 -0.02920 102 VAL A C     
753  O  O     . VAL A 106 ? 0.43790 0.35610 0.41080 -0.00230 -0.03510 -0.02700 102 VAL A O     
754  C  CB    . VAL A 106 ? 0.39460 0.32610 0.36370 -0.00810 -0.03970 -0.02150 102 VAL A CB    
755  C  CG1   . VAL A 106 ? 0.35610 0.29520 0.32190 -0.00790 -0.03880 -0.01830 102 VAL A CG1   
756  C  CG2   . VAL A 106 ? 0.34640 0.27730 0.32420 -0.00890 -0.03890 -0.01650 102 VAL A CG2   
757  N  N     . GLY A 107 ? 0.47930 0.39430 0.44630 -0.00610 -0.04110 -0.03420 103 GLY A N     
758  C  CA    . GLY A 107 ? 0.47670 0.38280 0.44850 -0.00600 -0.04220 -0.03760 103 GLY A CA    
759  C  C     . GLY A 107 ? 0.48640 0.39090 0.46850 -0.00840 -0.04370 -0.03180 103 GLY A C     
760  O  O     . GLY A 107 ? 0.43130 0.34050 0.41640 -0.01150 -0.04550 -0.02720 103 GLY A O     
761  N  N     . THR A 108 ? 0.51400 0.41230 0.50190 -0.00680 -0.04270 -0.03180 104 THR A N     
762  C  CA    . THR A 108 ? 0.54570 0.44280 0.54340 -0.00870 -0.04360 -0.02550 104 THR A CA    
763  C  C     . THR A 108 ? 0.54540 0.44080 0.54770 -0.01390 -0.04830 -0.02440 104 THR A C     
764  O  O     . THR A 108 ? 0.56270 0.46160 0.57140 -0.01640 -0.04890 -0.01780 104 THR A O     
765  C  CB    . THR A 108 ? 0.54600 0.43560 0.54920 -0.00610 -0.04250 -0.02620 104 THR A CB    
766  O  OG1   . THR A 108 ? 0.65310 0.53310 0.65700 -0.00680 -0.04530 -0.03290 104 THR A OG1   
767  C  CG2   . THR A 108 ? 0.59310 0.48490 0.59220 -0.00110 -0.03810 -0.02750 104 THR A CG2   
768  N  N     . ALA A 109 ? 0.56150 0.45190 0.56080 -0.01570 -0.05170 -0.03090 105 ALA A N     
769  C  CA    . ALA A 109 ? 0.55790 0.44650 0.56210 -0.02100 -0.05670 -0.03020 105 ALA A CA    
770  C  C     . ALA A 109 ? 0.53530 0.43390 0.53940 -0.02380 -0.05770 -0.02510 105 ALA A C     
771  O  O     . ALA A 109 ? 0.46690 0.36620 0.47690 -0.02830 -0.06140 -0.02260 105 ALA A O     
772  C  CB    . ALA A 109 ? 0.54740 0.42890 0.54690 -0.02250 -0.06020 -0.03900 105 ALA A CB    
773  N  N     . ALA A 110 ? 0.46130 0.36770 0.45960 -0.02120 -0.05450 -0.02340 106 ALA A N     
774  C  CA    . ALA A 110 ? 0.44590 0.36160 0.44480 -0.02310 -0.05500 -0.01860 106 ALA A CA    
775  C  C     . ALA A 110 ? 0.43880 0.36030 0.44230 -0.02190 -0.05120 -0.01140 106 ALA A C     
776  O  O     . ALA A 110 ? 0.44470 0.37380 0.44960 -0.02300 -0.05090 -0.00720 106 ALA A O     
777  C  CB    . ALA A 110 ? 0.44490 0.36530 0.43420 -0.02140 -0.05440 -0.02170 106 ALA A CB    
778  N  N     . PHE A 111 ? 0.35030 0.26850 0.35630 -0.01980 -0.04850 -0.00980 107 PHE A N     
779  C  CA    . PHE A 111 ? 0.41080 0.33470 0.41990 -0.01900 -0.04500 -0.00340 107 PHE A CA    
780  C  C     . PHE A 111 ? 0.39050 0.31890 0.40700 -0.02280 -0.04650 0.00220  107 PHE A C     
781  O  O     . PHE A 111 ? 0.33970 0.26430 0.36240 -0.02610 -0.04970 0.00300  107 PHE A O     
782  C  CB    . PHE A 111 ? 0.45040 0.36960 0.46220 -0.01690 -0.04300 -0.00210 107 PHE A CB    
783  C  CG    . PHE A 111 ? 0.46120 0.37920 0.46680 -0.01250 -0.04000 -0.00560 107 PHE A CG    
784  C  CD1   . PHE A 111 ? 0.49850 0.41740 0.49620 -0.01080 -0.03960 -0.01070 107 PHE A CD1   
785  C  CD2   . PHE A 111 ? 0.50410 0.42080 0.51200 -0.01020 -0.03760 -0.00320 107 PHE A CD2   
786  C  CE1   . PHE A 111 ? 0.50760 0.42600 0.50000 -0.00680 -0.03660 -0.01360 107 PHE A CE1   
787  C  CE2   . PHE A 111 ? 0.52350 0.44000 0.52660 -0.00620 -0.03480 -0.00600 107 PHE A CE2   
788  C  CZ    . PHE A 111 ? 0.53550 0.45290 0.53100 -0.00450 -0.03410 -0.01130 107 PHE A CZ    
789  N  N     . GLY A 112 ? 0.37140 0.30810 0.38750 -0.02240 -0.04390 0.00610  108 GLY A N     
790  C  CA    . GLY A 112 ? 0.44980 0.39230 0.47290 -0.02550 -0.04420 0.01170  108 GLY A CA    
791  C  C     . GLY A 112 ? 0.46500 0.41020 0.49120 -0.02870 -0.04800 0.01150  108 GLY A C     
792  O  O     . GLY A 112 ? 0.45140 0.40190 0.48470 -0.03140 -0.04830 0.01630  108 GLY A O     
793  N  N     . LYS A 113 ? 0.40470 0.34710 0.42600 -0.02850 -0.05090 0.00620  109 LYS A N     
794  C  CA    . LYS A 113 ? 0.41700 0.36250 0.44090 -0.03180 -0.05520 0.00590  109 LYS A CA    
795  C  C     . LYS A 113 ? 0.43310 0.38620 0.45330 -0.03020 -0.05430 0.00650  109 LYS A C     
796  O  O     . LYS A 113 ? 0.44970 0.40700 0.47240 -0.03270 -0.05790 0.00710  109 LYS A O     
797  C  CB    . LYS A 113 ? 0.39430 0.33200 0.41530 -0.03370 -0.06000 -0.00030 109 LYS A CB    
798  C  CG    . LYS A 113 ? 0.41370 0.34250 0.43950 -0.03540 -0.06140 -0.00120 109 LYS A CG    
799  C  CD    . LYS A 113 ? 0.43520 0.35600 0.45850 -0.03770 -0.06640 -0.00810 109 LYS A CD    
800  C  CE    . LYS A 113 ? 0.45130 0.37540 0.47940 -0.04300 -0.07170 -0.00720 109 LYS A CE    
801  N  NZ    . LYS A 113 ? 0.47680 0.40320 0.51630 -0.04650 -0.07230 -0.00040 109 LYS A NZ    
802  N  N     . GLY A 114 ? 0.35990 0.31500 0.37480 -0.02620 -0.04990 0.00670  110 GLY A N     
803  C  CA    . GLY A 114 ? 0.35020 0.31140 0.36180 -0.02450 -0.04910 0.00730  110 GLY A CA    
804  C  C     . GLY A 114 ? 0.44150 0.39940 0.44410 -0.02330 -0.05110 0.00200  110 GLY A C     
805  O  O     . GLY A 114 ? 0.40740 0.36880 0.40840 -0.02450 -0.05430 0.00140  110 GLY A O     
806  N  N     . ALA A 115 ? 0.41260 0.36450 0.40950 -0.02110 -0.04920 -0.00180 111 ALA A N     
807  C  CA    . ALA A 115 ? 0.41530 0.36450 0.40310 -0.01990 -0.05040 -0.00710 111 ALA A CA    
808  C  C     . ALA A 115 ? 0.36410 0.31900 0.34700 -0.01740 -0.04820 -0.00560 111 ALA A C     
809  O  O     . ALA A 115 ? 0.32700 0.28600 0.31270 -0.01580 -0.04480 -0.00140 111 ALA A O     
810  C  CB    . ALA A 115 ? 0.42710 0.36900 0.41120 -0.01770 -0.04830 -0.01130 111 ALA A CB    
811  N  N     . LEU A 116 ? 0.40640 0.36150 0.38180 -0.01720 -0.05020 -0.00900 112 LEU A N     
812  C  CA    . LEU A 116 ? 0.38600 0.34590 0.35610 -0.01490 -0.04830 -0.00750 112 LEU A CA    
813  C  C     . LEU A 116 ? 0.39710 0.35570 0.36520 -0.01140 -0.04280 -0.00700 112 LEU A C     
814  O  O     . LEU A 116 ? 0.37240 0.32610 0.33700 -0.01010 -0.04120 -0.01060 112 LEU A O     
815  C  CB    . LEU A 116 ? 0.53980 0.49920 0.50070 -0.01550 -0.05110 -0.01210 112 LEU A CB    
816  C  CG    . LEU A 116 ? 0.65330 0.61710 0.60720 -0.01330 -0.04930 -0.01100 112 LEU A CG    
817  C  CD1   . LEU A 116 ? 0.65080 0.62120 0.61000 -0.01300 -0.04910 -0.00440 112 LEU A CD1   
818  C  CD2   . LEU A 116 ? 0.63550 0.59960 0.58010 -0.01460 -0.05270 -0.01530 112 LEU A CD2   
819  N  N     . GLN A 117 ? 0.33410 0.29710 0.30480 -0.01000 -0.04000 -0.00240 113 GLN A N     
820  C  CA    . GLN A 117 ? 0.34790 0.31020 0.31700 -0.00730 -0.03510 -0.00160 113 GLN A CA    
821  C  C     . GLN A 117 ? 0.42400 0.38170 0.39570 -0.00710 -0.03350 -0.00290 113 GLN A C     
822  O  O     . GLN A 117 ? 0.34210 0.29740 0.31040 -0.00510 -0.03080 -0.00460 113 GLN A O     
823  C  CB    . GLN A 117 ? 0.29050 0.25300 0.25120 -0.00530 -0.03380 -0.00380 113 GLN A CB    
824  C  CG    . GLN A 117 ? 0.31800 0.28550 0.27630 -0.00520 -0.03480 -0.00120 113 GLN A CG    
825  C  CD    . GLN A 117 ? 0.39180 0.35990 0.34120 -0.00380 -0.03380 -0.00310 113 GLN A CD    
826  O  OE1   . GLN A 117 ? 0.40330 0.36820 0.34780 -0.00310 -0.03310 -0.00750 113 GLN A OE1   
827  N  NE2   . GLN A 117 ? 0.33150 0.30380 0.27930 -0.00320 -0.03360 0.00040  113 GLN A NE2   
828  N  N     . GLU A 118 ? 0.32040 0.27720 0.29870 -0.00940 -0.03530 -0.00160 114 GLU A N     
829  C  CA    . GLU A 118 ? 0.34660 0.29910 0.32800 -0.00950 -0.03430 -0.00200 114 GLU A CA    
830  C  C     . GLU A 118 ? 0.36050 0.31440 0.34160 -0.00740 -0.02980 0.00030  114 GLU A C     
831  O  O     . GLU A 118 ? 0.37100 0.32920 0.35410 -0.00720 -0.02770 0.00360  114 GLU A O     
832  C  CB    . GLU A 118 ? 0.37500 0.32770 0.36430 -0.01250 -0.03650 0.00060  114 GLU A CB    
833  C  CG    . GLU A 118 ? 0.38360 0.33180 0.37640 -0.01280 -0.03570 0.00100  114 GLU A CG    
834  C  CD    . GLU A 118 ? 0.40100 0.34780 0.40120 -0.01620 -0.03870 0.00280  114 GLU A CD    
835  O  OE1   . GLU A 118 ? 0.38820 0.33260 0.39250 -0.01670 -0.03790 0.00490  114 GLU A OE1   
836  O  OE2   . GLU A 118 ? 0.46690 0.41510 0.46910 -0.01860 -0.04210 0.00250  114 GLU A OE2   
837  N  N     . SER A 119 ? 0.35790 0.30810 0.33670 -0.00570 -0.02830 -0.00180 115 SER A N     
838  C  CA    . SER A 119 ? 0.41970 0.37150 0.39710 -0.00380 -0.02450 -0.00020 115 SER A CA    
839  C  C     . SER A 119 ? 0.41180 0.36150 0.39340 -0.00410 -0.02360 0.00150  115 SER A C     
840  O  O     . SER A 119 ? 0.35620 0.30590 0.33650 -0.00240 -0.02130 0.00180  115 SER A O     
841  C  CB    . SER A 119 ? 0.43520 0.38620 0.40610 -0.00140 -0.02310 -0.00330 115 SER A CB    
842  O  OG    . SER A 119 ? 0.41990 0.37380 0.38680 -0.00130 -0.02360 -0.00370 115 SER A OG    
843  N  N     . THR A 120 ? 0.40990 0.35860 0.39710 -0.00640 -0.02560 0.00340  116 THR A N     
844  C  CA    . THR A 120 ? 0.40360 0.35080 0.39570 -0.00730 -0.02550 0.00610  116 THR A CA    
845  C  C     . THR A 120 ? 0.41930 0.37190 0.41400 -0.00870 -0.02340 0.01070  116 THR A C     
846  O  O     . THR A 120 ? 0.36630 0.32310 0.35950 -0.00870 -0.02200 0.01140  116 THR A O     
847  C  CB    . THR A 120 ? 0.38190 0.32470 0.37890 -0.00950 -0.02910 0.00560  116 THR A CB    
848  O  OG1   . THR A 120 ? 0.35480 0.30100 0.35450 -0.01200 -0.03060 0.00730  116 THR A OG1   
849  C  CG2   . THR A 120 ? 0.35780 0.29490 0.35180 -0.00830 -0.03110 -0.00000 116 THR A CG2   
850  N  N     . VAL A 121 ? 0.39070 0.34310 0.38950 -0.01000 -0.02330 0.01410  117 VAL A N     
851  C  CA    . VAL A 121 ? 0.36570 0.32360 0.36690 -0.01180 -0.02140 0.01840  117 VAL A CA    
852  C  C     . VAL A 121 ? 0.35720 0.31820 0.36160 -0.01370 -0.02230 0.01940  117 VAL A C     
853  O  O     . VAL A 121 ? 0.41910 0.38540 0.42390 -0.01420 -0.01980 0.02150  117 VAL A O     
854  C  CB    . VAL A 121 ? 0.45790 0.41520 0.46330 -0.01340 -0.02180 0.02240  117 VAL A CB    
855  C  CG1   . VAL A 121 ? 0.38830 0.34160 0.39970 -0.01540 -0.02530 0.02320  117 VAL A CG1   
856  C  CG2   . VAL A 121 ? 0.38850 0.35230 0.39420 -0.01500 -0.01910 0.02660  117 VAL A CG2   
857  N  N     . HIS A 122 ? 0.33390 0.29180 0.34080 -0.01470 -0.02570 0.01770  118 HIS A N     
858  C  CA    . HIS A 122 ? 0.39970 0.36130 0.41070 -0.01670 -0.02710 0.01900  118 HIS A CA    
859  C  C     . HIS A 122 ? 0.41510 0.37940 0.42280 -0.01520 -0.02660 0.01690  118 HIS A C     
860  O  O     . HIS A 122 ? 0.38860 0.35710 0.40020 -0.01640 -0.02730 0.01860  118 HIS A O     
861  C  CB    . HIS A 122 ? 0.43920 0.39660 0.45470 -0.01920 -0.03160 0.01820  118 HIS A CB    
862  C  CG    . HIS A 122 ? 0.43840 0.39110 0.45730 -0.02040 -0.03270 0.01970  118 HIS A CG    
863  N  ND1   . HIS A 122 ? 0.40340 0.35890 0.42790 -0.02280 -0.03190 0.02500  118 HIS A ND1   
864  C  CD2   . HIS A 122 ? 0.39170 0.33710 0.40950 -0.01940 -0.03430 0.01690  118 HIS A CD2   
865  C  CE1   . HIS A 122 ? 0.46360 0.41350 0.49060 -0.02330 -0.03340 0.02590  118 HIS A CE1   
866  N  NE2   . HIS A 122 ? 0.44370 0.38720 0.46710 -0.02110 -0.03480 0.02080  118 HIS A NE2   
867  N  N     . GLY A 123 ? 0.36960 0.33180 0.37080 -0.01260 -0.02570 0.01380  119 GLY A N     
868  C  CA    . GLY A 123 ? 0.33250 0.29720 0.33070 -0.01110 -0.02530 0.01260  119 GLY A CA    
869  C  C     . GLY A 123 ? 0.36180 0.32820 0.35600 -0.00890 -0.02130 0.01270  119 GLY A C     
870  O  O     . GLY A 123 ? 0.35970 0.32910 0.35570 -0.00910 -0.01840 0.01510  119 GLY A O     
871  N  N     . VAL A 124 ? 0.31950 0.28400 0.30800 -0.00700 -0.02110 0.01010  120 VAL A N     
872  C  CA    . VAL A 124 ? 0.36280 0.32810 0.34720 -0.00510 -0.01770 0.01000  120 VAL A CA    
873  C  C     . VAL A 124 ? 0.37340 0.33560 0.35540 -0.00450 -0.01720 0.00880  120 VAL A C     
874  O  O     . VAL A 124 ? 0.33880 0.29800 0.31770 -0.00350 -0.01840 0.00610  120 VAL A O     
875  C  CB    . VAL A 124 ? 0.40370 0.36970 0.38420 -0.00360 -0.01780 0.00880  120 VAL A CB    
876  C  CG1   . VAL A 124 ? 0.32910 0.29480 0.30540 -0.00210 -0.01480 0.00840  120 VAL A CG1   
877  C  CG2   . VAL A 124 ? 0.37530 0.34490 0.35960 -0.00390 -0.01810 0.01100  120 VAL A CG2   
878  N  N     . ASP A 125 ? 0.30040 0.26360 0.28390 -0.00510 -0.01530 0.01080  121 ASP A N     
879  C  CA    . ASP A 125 ? 0.30860 0.26940 0.29200 -0.00490 -0.01530 0.01080  121 ASP A CA    
880  C  C     . ASP A 125 ? 0.36400 0.32480 0.34280 -0.00300 -0.01340 0.00940  121 ASP A C     
881  O  O     . ASP A 125 ? 0.29930 0.26240 0.27710 -0.00320 -0.01130 0.01090  121 ASP A O     
882  C  CB    . ASP A 125 ? 0.30790 0.27090 0.29460 -0.00670 -0.01440 0.01430  121 ASP A CB    
883  C  CG    . ASP A 125 ? 0.40040 0.36140 0.38820 -0.00650 -0.01490 0.01540  121 ASP A CG    
884  O  OD1   . ASP A 125 ? 0.33930 0.29740 0.32530 -0.00460 -0.01540 0.01310  121 ASP A OD1   
885  O  OD2   . ASP A 125 ? 0.42820 0.39110 0.41890 -0.00830 -0.01480 0.01880  121 ASP A OD2   
886  N  N     . LEU A 126 ? 0.30060 0.25910 0.27660 -0.00130 -0.01430 0.00650  122 LEU A N     
887  C  CA    . LEU A 126 ? 0.28490 0.24430 0.25690 0.00040  -0.01240 0.00540  122 LEU A CA    
888  C  C     . LEU A 126 ? 0.34180 0.30170 0.31490 0.00070  -0.01120 0.00680  122 LEU A C     
889  O  O     . LEU A 126 ? 0.32480 0.28720 0.29590 0.00090  -0.00920 0.00750  122 LEU A O     
890  C  CB    . LEU A 126 ? 0.34700 0.30430 0.31570 0.00210  -0.01330 0.00200  122 LEU A CB    
891  C  CG    . LEU A 126 ? 0.36560 0.32330 0.33210 0.00180  -0.01480 0.00080  122 LEU A CG    
892  C  CD1   . LEU A 126 ? 0.32700 0.28330 0.28880 0.00330  -0.01540 -0.00270 122 LEU A CD1   
893  C  CD2   . LEU A 126 ? 0.33020 0.29110 0.29550 0.00150  -0.01320 0.00290  122 LEU A CD2   
894  N  N     . VAL A 127 ? 0.26840 0.22600 0.24520 0.00060  -0.01270 0.00740  123 VAL A N     
895  C  CA    . VAL A 127 ? 0.36560 0.32410 0.34430 0.00110  -0.01200 0.00930  123 VAL A CA    
896  C  C     . VAL A 127 ? 0.34100 0.30360 0.31920 -0.00080 -0.01060 0.01250  123 VAL A C     
897  O  O     . VAL A 127 ? 0.26390 0.22920 0.24080 -0.00060 -0.00930 0.01340  123 VAL A O     
898  C  CB    . VAL A 127 ? 0.38420 0.33900 0.36790 0.00130  -0.01410 0.01010  123 VAL A CB    
899  C  CG1   . VAL A 127 ? 0.31840 0.27510 0.30520 0.00130  -0.01380 0.01360  123 VAL A CG1   
900  C  CG2   . VAL A 127 ? 0.36310 0.31350 0.34640 0.00370  -0.01490 0.00590  123 VAL A CG2   
901  N  N     . SER A 128 ? 0.27260 0.23630 0.25170 -0.00290 -0.01070 0.01400  124 SER A N     
902  C  CA    . SER A 128 ? 0.24100 0.20880 0.21900 -0.00490 -0.00900 0.01630  124 SER A CA    
903  C  C     . SER A 128 ? 0.34470 0.31410 0.31860 -0.00470 -0.00680 0.01460  124 SER A C     
904  O  O     . SER A 128 ? 0.35280 0.32490 0.32460 -0.00580 -0.00530 0.01540  124 SER A O     
905  C  CB    . SER A 128 ? 0.24920 0.21820 0.22980 -0.00690 -0.00920 0.01830  124 SER A CB    
906  O  OG    . SER A 128 ? 0.45420 0.42080 0.43920 -0.00720 -0.01150 0.01990  124 SER A OG    
907  N  N     . ILE A 129 ? 0.31470 0.28250 0.28750 -0.00350 -0.00680 0.01230  125 ILE A N     
908  C  CA    . ILE A 129 ? 0.26100 0.22960 0.23060 -0.00320 -0.00490 0.01120  125 ILE A CA    
909  C  C     . ILE A 129 ? 0.27230 0.24170 0.23950 -0.00270 -0.00410 0.01080  125 ILE A C     
910  O  O     . ILE A 129 ? 0.30160 0.27260 0.26690 -0.00370 -0.00240 0.01090  125 ILE A O     
911  C  CB    . ILE A 129 ? 0.33070 0.29790 0.30010 -0.00200 -0.00560 0.00970  125 ILE A CB    
912  C  CG1   . ILE A 129 ? 0.33930 0.30700 0.31190 -0.00290 -0.00620 0.01060  125 ILE A CG1   
913  C  CG2   . ILE A 129 ? 0.23220 0.19970 0.19870 -0.00150 -0.00390 0.00910  125 ILE A CG2   
914  C  CD1   . ILE A 129 ? 0.28220 0.24900 0.25530 -0.00200 -0.00770 0.00970  125 ILE A CD1   
915  N  N     . PHE A 130 ? 0.24630 0.21480 0.21410 -0.00110 -0.00510 0.01030  126 PHE A N     
916  C  CA    . PHE A 130 ? 0.26850 0.23850 0.23470 -0.00030 -0.00420 0.01010  126 PHE A CA    
917  C  C     . PHE A 130 ? 0.29970 0.27230 0.26760 -0.00130 -0.00430 0.01230  126 PHE A C     
918  O  O     . PHE A 130 ? 0.28620 0.26120 0.25330 -0.00140 -0.00350 0.01280  126 PHE A O     
919  C  CB    . PHE A 130 ? 0.21910 0.18780 0.18530 0.00220  -0.00470 0.00830  126 PHE A CB    
920  C  CG    . PHE A 130 ? 0.32600 0.29410 0.28890 0.00290  -0.00420 0.00660  126 PHE A CG    
921  C  CD1   . PHE A 130 ? 0.25650 0.22250 0.21890 0.00310  -0.00550 0.00550  126 PHE A CD1   
922  C  CD2   . PHE A 130 ? 0.31090 0.28120 0.27150 0.00320  -0.00250 0.00680  126 PHE A CD2   
923  C  CE1   . PHE A 130 ? 0.31570 0.28190 0.27510 0.00360  -0.00530 0.00470  126 PHE A CE1   
924  C  CE2   . PHE A 130 ? 0.32270 0.29280 0.28030 0.00360  -0.00210 0.00610  126 PHE A CE2   
925  C  CZ    . PHE A 130 ? 0.34970 0.31790 0.30670 0.00390  -0.00360 0.00520  126 PHE A CZ    
926  N  N     . SER A 131 ? 0.27230 0.24490 0.24260 -0.00240 -0.00550 0.01410  127 SER A N     
927  C  CA    . SER A 131 ? 0.27120 0.24680 0.24330 -0.00350 -0.00610 0.01700  127 SER A CA    
928  C  C     . SER A 131 ? 0.29260 0.27180 0.26160 -0.00560 -0.00490 0.01760  127 SER A C     
929  O  O     . SER A 131 ? 0.30240 0.28440 0.27220 -0.00560 -0.00520 0.01890  127 SER A O     
930  C  CB    . SER A 131 ? 0.26670 0.24180 0.24120 -0.00490 -0.00730 0.01930  127 SER A CB    
931  O  OG    . SER A 131 ? 0.54440 0.52120 0.52220 -0.00500 -0.00870 0.02250  127 SER A OG    
932  N  N     . PRO A 132 ? 0.35310 0.33240 0.31890 -0.00740 -0.00350 0.01640  128 PRO A N     
933  C  CA    . PRO A 132 ? 0.31150 0.29360 0.27430 -0.00980 -0.00250 0.01640  128 PRO A CA    
934  C  C     . PRO A 132 ? 0.33430 0.31690 0.29640 -0.00920 -0.00200 0.01540  128 PRO A C     
935  O  O     . PRO A 132 ? 0.31780 0.30340 0.27850 -0.01140 -0.00200 0.01610  128 PRO A O     
936  C  CB    . PRO A 132 ? 0.31270 0.29350 0.27280 -0.01120 -0.00080 0.01450  128 PRO A CB    
937  C  CG    . PRO A 132 ? 0.28740 0.26670 0.25010 -0.01020 -0.00130 0.01520  128 PRO A CG    
938  C  CD    . PRO A 132 ? 0.32730 0.30440 0.29270 -0.00760 -0.00280 0.01520  128 PRO A CD    
939  N  N     . ILE A 133 ? 0.32870 0.30900 0.29140 -0.00670 -0.00160 0.01410  129 ILE A N     
940  C  CA    . ILE A 133 ? 0.30910 0.29080 0.27120 -0.00650 -0.00070 0.01370  129 ILE A CA    
941  C  C     . ILE A 133 ? 0.29620 0.27910 0.26080 -0.00380 -0.00110 0.01420  129 ILE A C     
942  O  O     . ILE A 133 ? 0.31770 0.30090 0.28170 -0.00260 0.00000  0.01340  129 ILE A O     
943  C  CB    . ILE A 133 ? 0.33680 0.31560 0.29660 -0.00650 0.00070  0.01190  129 ILE A CB    
944  C  CG1   . ILE A 133 ? 0.31720 0.29270 0.27720 -0.00460 0.00040  0.01080  129 ILE A CG1   
945  C  CG2   . ILE A 133 ? 0.38610 0.36430 0.34380 -0.00940 0.00160  0.01120  129 ILE A CG2   
946  C  CD1   . ILE A 133 ? 0.30510 0.28010 0.26580 -0.00200 -0.00020 0.01040  129 ILE A CD1   
947  N  N     . THR A 134 ? 0.30460 0.28800 0.27230 -0.00260 -0.00240 0.01550  130 THR A N     
948  C  CA    . THR A 134 ? 0.30800 0.29290 0.27910 0.00020  -0.00250 0.01580  130 THR A CA    
949  C  C     . THR A 134 ? 0.36590 0.35420 0.34090 -0.00030 -0.00390 0.01900  130 THR A C     
950  O  O     . THR A 134 ? 0.34910 0.33790 0.32400 -0.00250 -0.00510 0.02080  130 THR A O     
951  C  CB    . THR A 134 ? 0.30250 0.28310 0.27440 0.00310  -0.00280 0.01370  130 THR A CB    
952  O  OG1   . THR A 134 ? 0.32300 0.30090 0.29620 0.00230  -0.00440 0.01440  130 THR A OG1   
953  C  CG2   . THR A 134 ? 0.24150 0.22000 0.20960 0.00380  -0.00170 0.01100  130 THR A CG2   
954  N  N     . LYS A 135 ? 0.36120 0.35260 0.34010 0.00190  -0.00360 0.01990  131 LYS A N     
955  C  CA    . LYS A 135 ? 0.37270 0.36730 0.35680 0.00230  -0.00520 0.02340  131 LYS A CA    
956  C  C     . LYS A 135 ? 0.35540 0.34570 0.34290 0.00450  -0.00630 0.02350  131 LYS A C     
957  O  O     . LYS A 135 ? 0.31520 0.30670 0.30650 0.00400  -0.00820 0.02700  131 LYS A O     
958  C  CB    . LYS A 135 ? 0.32040 0.32010 0.30890 0.00430  -0.00430 0.02460  131 LYS A CB    
959  C  CG    . LYS A 135 ? 0.27230 0.27720 0.25880 0.00150  -0.00360 0.02540  131 LYS A CG    
960  C  CD    . LYS A 135 ? 0.31910 0.33030 0.31120 0.00340  -0.00280 0.02730  131 LYS A CD    
961  C  CE    . LYS A 135 ? 0.26060 0.27670 0.25900 0.00330  -0.00510 0.03180  131 LYS A CE    
962  N  NZ    . LYS A 135 ? 0.24510 0.26850 0.24960 0.00480  -0.00430 0.03410  131 LYS A NZ    
963  N  N     . LEU A 136 ? 0.30200 0.28710 0.28820 0.00680  -0.00550 0.01980  132 LEU A N     
964  C  CA    . LEU A 136 ? 0.36270 0.34260 0.35200 0.00850  -0.00670 0.01920  132 LEU A CA    
965  C  C     . LEU A 136 ? 0.34730 0.32210 0.33230 0.00880  -0.00630 0.01510  132 LEU A C     
966  O  O     . LEU A 136 ? 0.26150 0.23650 0.24320 0.01000  -0.00460 0.01220  132 LEU A O     
967  C  CB    . LEU A 136 ? 0.32170 0.30140 0.31710 0.01250  -0.00640 0.01910  132 LEU A CB    
968  C  CG    . LEU A 136 ? 0.39080 0.36380 0.38970 0.01480  -0.00750 0.01740  132 LEU A CG    
969  C  CD1   . LEU A 136 ? 0.39230 0.36390 0.39520 0.01290  -0.01020 0.02180  132 LEU A CD1   
970  C  CD2   . LEU A 136 ? 0.32270 0.29500 0.32650 0.01940  -0.00620 0.01550  132 LEU A CD2   
971  N  N     . SER A 137 ? 0.27920 0.25030 0.26460 0.00750  -0.00790 0.01540  133 SER A N     
972  C  CA    . SER A 137 ? 0.34610 0.31270 0.32840 0.00750  -0.00810 0.01200  133 SER A CA    
973  C  C     . SER A 137 ? 0.31540 0.27730 0.30210 0.00790  -0.01010 0.01220  133 SER A C     
974  O  O     . SER A 137 ? 0.32060 0.28290 0.31010 0.00590  -0.01150 0.01580  133 SER A O     
975  C  CB    . SER A 137 ? 0.30320 0.27110 0.28130 0.00440  -0.00780 0.01250  133 SER A CB    
976  O  OG    . SER A 137 ? 0.29790 0.26240 0.27430 0.00420  -0.00840 0.01010  133 SER A OG    
977  N  N     . VAL A 138 ? 0.33450 0.29180 0.32180 0.01030  -0.01040 0.00840  134 VAL A N     
978  C  CA    . VAL A 138 ? 0.30370 0.25560 0.29630 0.01090  -0.01240 0.00840  134 VAL A CA    
979  C  C     . VAL A 138 ? 0.36450 0.31100 0.35480 0.01210  -0.01300 0.00290  134 VAL A C     
980  O  O     . VAL A 138 ? 0.34870 0.29610 0.33430 0.01370  -0.01130 -0.00080 134 VAL A O     
981  C  CB    . VAL A 138 ? 0.46270 0.41460 0.46150 0.01360  -0.01230 0.01030  134 VAL A CB    
982  C  CG1   . VAL A 138 ? 0.38360 0.33630 0.38120 0.01730  -0.00990 0.00640  134 VAL A CG1   
983  C  CG2   . VAL A 138 ? 0.51140 0.45690 0.51670 0.01400  -0.01460 0.01090  134 VAL A CG2   
984  N  N     . MET A 139 ? 0.34820 0.28950 0.34170 0.01090  -0.01540 0.00260  135 MET A N     
985  C  CA    . MET A 139 ? 0.38820 0.32380 0.38020 0.01160  -0.01660 -0.00270 135 MET A CA    
986  C  C     . MET A 139 ? 0.39020 0.31990 0.38740 0.01450  -0.01690 -0.00490 135 MET A C     
987  O  O     . MET A 139 ? 0.39420 0.32190 0.39850 0.01430  -0.01820 -0.00120 135 MET A O     
988  C  CB    . MET A 139 ? 0.28040 0.21360 0.27300 0.00810  -0.01930 -0.00200 135 MET A CB    
989  C  CG    . MET A 139 ? 0.41550 0.34290 0.40640 0.00800  -0.02120 -0.00750 135 MET A CG    
990  S  SD    . MET A 139 ? 0.46990 0.39630 0.46270 0.00340  -0.02460 -0.00580 135 MET A SD    
991  C  CE    . MET A 139 ? 0.47450 0.39510 0.47690 0.00250  -0.02680 -0.00260 135 MET A CE    
992  N  N     . ILE A 140 ? 0.40110 0.32850 0.39520 0.01730  -0.01560 -0.01080 136 ILE A N     
993  C  CA    . ILE A 140 ? 0.44170 0.36290 0.44080 0.02060  -0.01540 -0.01410 136 ILE A CA    
994  C  C     . ILE A 140 ? 0.39920 0.31260 0.40250 0.01840  -0.01890 -0.01470 136 ILE A C     
995  O  O     . ILE A 140 ? 0.39720 0.30840 0.39610 0.01600  -0.02070 -0.01800 136 ILE A O     
996  C  CB    . ILE A 140 ? 0.48930 0.40950 0.48310 0.02390  -0.01300 -0.02130 136 ILE A CB    
997  C  CG1   . ILE A 140 ? 0.47360 0.40230 0.46190 0.02500  -0.00980 -0.02050 136 ILE A CG1   
998  C  CG2   . ILE A 140 ? 0.47100 0.38530 0.47110 0.02810  -0.01200 -0.02450 136 ILE A CG2   
999  C  CD1   . ILE A 140 ? 0.48140 0.41490 0.47500 0.02700  -0.00780 -0.01590 136 ILE A CD1   
1000 N  N     . PRO A 141 ? 0.43960 0.34920 0.45170 0.01880  -0.02030 -0.01120 137 PRO A N     
1001 C  CA    . PRO A 141 ? 0.49380 0.39630 0.51060 0.01590  -0.02380 -0.01060 137 PRO A CA    
1002 C  C     . PRO A 141 ? 0.52210 0.41510 0.53950 0.01750  -0.02480 -0.01810 137 PRO A C     
1003 O  O     . PRO A 141 ? 0.49970 0.38740 0.51740 0.01440  -0.02790 -0.02020 137 PRO A O     
1004 C  CB    . PRO A 141 ? 0.42460 0.32710 0.45070 0.01600  -0.02470 -0.00320 137 PRO A CB    
1005 C  CG    . PRO A 141 ? 0.44500 0.35020 0.47310 0.02070  -0.02170 -0.00330 137 PRO A CG    
1006 C  CD    . PRO A 141 ? 0.41070 0.32240 0.42940 0.02180  -0.01880 -0.00700 137 PRO A CD    
1007 N  N     . THR A 142 ? 0.40760 0.29860 0.42560 0.02230  -0.02210 -0.02250 138 THR A N     
1008 C  CA    . THR A 142 ? 0.46400 0.34560 0.48230 0.02430  -0.02250 -0.03060 138 THR A CA    
1009 C  C     . THR A 142 ? 0.51620 0.40030 0.52910 0.02900  -0.01830 -0.03660 138 THR A C     
1010 O  O     . THR A 142 ? 0.47180 0.36360 0.48470 0.03140  -0.01520 -0.03340 138 THR A O     
1011 C  CB    . THR A 142 ? 0.50580 0.37850 0.53560 0.02590  -0.02390 -0.02920 138 THR A CB    
1012 O  OG1   . THR A 142 ? 0.57190 0.44790 0.60720 0.03060  -0.02090 -0.02620 138 THR A OG1   
1013 C  CG2   . THR A 142 ? 0.50280 0.37450 0.53890 0.02130  -0.02770 -0.02150 138 THR A CG2   
1014 N  N     . ALA A 143 ? 0.50370 0.38120 0.51230 0.03010  -0.01820 -0.04560 139 ALA A N     
1015 C  CA    . ALA A 143 ? 0.43650 0.31610 0.43980 0.03470  -0.01380 -0.05200 139 ALA A CA    
1016 C  C     . ALA A 143 ? 0.40360 0.28350 0.41610 0.04010  -0.01060 -0.04990 139 ALA A C     
1017 O  O     . ALA A 143 ? 0.42480 0.31230 0.43520 0.04330  -0.00660 -0.04960 139 ALA A O     
1018 C  CB    . ALA A 143 ? 0.40230 0.27370 0.40030 0.03490  -0.01440 -0.06240 139 ALA A CB    
1019 N  N     . GLU A 144 ? 0.40140 0.27350 0.42490 0.04090  -0.01260 -0.04740 140 GLU A N     
1020 C  CA    . GLU A 144 ? 0.49240 0.36390 0.52640 0.04620  -0.01020 -0.04490 140 GLU A CA    
1021 C  C     . GLU A 144 ? 0.49860 0.38190 0.53470 0.04680  -0.00850 -0.03640 140 GLU A C     
1022 O  O     . GLU A 144 ? 0.43190 0.31860 0.47360 0.05170  -0.00520 -0.03540 140 GLU A O     
1023 C  CB    . GLU A 144 ? 0.54070 0.40200 0.58640 0.04560  -0.01360 -0.04190 140 GLU A CB    
1024 C  CG    . GLU A 144 ? 0.79630 0.65530 0.85450 0.05140  -0.01160 -0.03950 140 GLU A CG    
1025 C  CD    . GLU A 144 ? 0.94760 0.81520 1.01270 0.05090  -0.01240 -0.02780 140 GLU A CD    
1026 O  OE1   . GLU A 144 ? 0.97920 0.84870 1.04390 0.04560  -0.01600 -0.02110 140 GLU A OE1   
1027 O  OE2   . GLU A 144 ? 0.99750 0.87030 1.06850 0.05570  -0.00940 -0.02540 140 GLU A OE2   
1028 N  N     . LYS A 145 ? 0.42230 0.31210 0.45410 0.04190  -0.01060 -0.03040 141 LYS A N     
1029 C  CA    . LYS A 145 ? 0.44050 0.34090 0.47370 0.04170  -0.00950 -0.02260 141 LYS A CA    
1030 C  C     . LYS A 145 ? 0.46010 0.36960 0.48390 0.04210  -0.00610 -0.02470 141 LYS A C     
1031 O  O     . LYS A 145 ? 0.40150 0.31980 0.42560 0.04170  -0.00510 -0.01890 141 LYS A O     
1032 C  CB    . LYS A 145 ? 0.44870 0.35140 0.48240 0.03620  -0.01310 -0.01490 141 LYS A CB    
1033 C  CG    . LYS A 145 ? 0.43110 0.32630 0.47440 0.03500  -0.01660 -0.01090 141 LYS A CG    
1034 C  CD    . LYS A 145 ? 0.52460 0.42440 0.57710 0.03670  -0.01660 -0.00270 141 LYS A CD    
1035 C  CE    . LYS A 145 ? 0.66730 0.55930 0.73080 0.04140  -0.01650 -0.00360 141 LYS A CE    
1036 N  NZ    . LYS A 145 ? 0.71590 0.61240 0.78920 0.04240  -0.01740 0.00580  141 LYS A NZ    
1037 N  N     . MET A 146 ? 0.44240 0.34990 0.45780 0.04280  -0.00450 -0.03270 142 MET A N     
1038 C  CA    . MET A 146 ? 0.42050 0.33670 0.42670 0.04270  -0.00160 -0.03410 142 MET A CA    
1039 C  C     . MET A 146 ? 0.32460 0.24850 0.33480 0.04680  0.00240  -0.03180 142 MET A C     
1040 O  O     . MET A 146 ? 0.37730 0.31010 0.38480 0.04540  0.00340  -0.02730 142 MET A O     
1041 C  CB    . MET A 146 ? 0.40750 0.32020 0.40430 0.04310  -0.00060 -0.04320 142 MET A CB    
1042 C  CG    . MET A 146 ? 0.42750 0.34920 0.41490 0.04320  0.00260  -0.04440 142 MET A CG    
1043 S  SD    . MET A 146 ? 0.54210 0.47020 0.52270 0.03730  0.00000  -0.03850 142 MET A SD    
1044 C  CE    . MET A 146 ? 0.51150 0.43220 0.48510 0.03370  -0.00380 -0.04410 142 MET A CE    
1045 N  N     . GLY A 147 ? 0.31030 0.23080 0.32760 0.05200  0.00470  -0.03480 143 GLY A N     
1046 C  CA    . GLY A 147 ? 0.38480 0.31340 0.40720 0.05620  0.00860  -0.03240 143 GLY A CA    
1047 C  C     . GLY A 147 ? 0.38190 0.31720 0.41110 0.05450  0.00690  -0.02250 143 GLY A C     
1048 O  O     . GLY A 147 ? 0.32790 0.27300 0.35510 0.05380  0.00860  -0.01890 143 GLY A O     
1049 N  N     . GLU A 148 ? 0.36990 0.30000 0.40700 0.05340  0.00330  -0.01800 144 GLU A N     
1050 C  CA    . GLU A 148 ? 0.40420 0.34060 0.44720 0.05140  0.00120  -0.00850 144 GLU A CA    
1051 C  C     . GLU A 148 ? 0.35610 0.29920 0.39030 0.04590  0.00000  -0.00520 144 GLU A C     
1052 O  O     . GLU A 148 ? 0.40320 0.35530 0.43850 0.04500  0.00050  0.00010  144 GLU A O     
1053 C  CB    . GLU A 148 ? 0.43850 0.36770 0.49000 0.05050  -0.00280 -0.00420 144 GLU A CB    
1054 C  CG    . GLU A 148 ? 0.58340 0.50800 0.64710 0.05610  -0.00180 -0.00440 144 GLU A CG    
1055 C  CD    . GLU A 148 ? 0.66340 0.57970 0.73580 0.05500  -0.00600 -0.00000 144 GLU A CD    
1056 O  OE1   . GLU A 148 ? 0.65620 0.56970 0.72440 0.04980  -0.00930 0.00190  144 GLU A OE1   
1057 O  OE2   . GLU A 148 ? 0.69940 0.61240 0.78350 0.05950  -0.00570 0.00170  144 GLU A OE2   
1058 N  N     . MET A 149 ? 0.39310 0.33180 0.41920 0.04220  -0.00180 -0.00810 145 MET A N     
1059 C  CA    . MET A 149 ? 0.33210 0.27630 0.35080 0.03740  -0.00280 -0.00510 145 MET A CA    
1060 C  C     . MET A 149 ? 0.36480 0.31650 0.37700 0.03790  0.00050  -0.00700 145 MET A C     
1061 O  O     . MET A 149 ? 0.29380 0.25240 0.30370 0.03530  0.00050  -0.00270 145 MET A O     
1062 C  CB    . MET A 149 ? 0.34210 0.28020 0.35480 0.03370  -0.00530 -0.00780 145 MET A CB    
1063 C  CG    . MET A 149 ? 0.47960 0.41180 0.49830 0.03160  -0.00900 -0.00430 145 MET A CG    
1064 S  SD    . MET A 149 ? 0.57800 0.51720 0.60050 0.02830  -0.01080 0.00550  145 MET A SD    
1065 C  CE    . MET A 149 ? 0.53920 0.47070 0.57100 0.02750  -0.01450 0.00930  145 MET A CE    
1066 N  N     . THR A 150 ? 0.32190 0.27230 0.33110 0.04130  0.00350  -0.01340 146 THR A N     
1067 C  CA    . THR A 150 ? 0.32140 0.27960 0.32500 0.04190  0.00690  -0.01450 146 THR A CA    
1068 C  C     . THR A 150 ? 0.33850 0.30500 0.34900 0.04380  0.00880  -0.00950 146 THR A C     
1069 O  O     . THR A 150 ? 0.30880 0.28270 0.31650 0.04140  0.00940  -0.00600 146 THR A O     
1070 C  CB    . THR A 150 ? 0.35510 0.31070 0.35400 0.04530  0.01000  -0.02240 146 THR A CB    
1071 O  OG1   . THR A 150 ? 0.38880 0.33680 0.38140 0.04310  0.00760  -0.02690 146 THR A OG1   
1072 C  CG2   . THR A 150 ? 0.29480 0.25890 0.28700 0.04540  0.01350  -0.02320 146 THR A CG2   
1073 N  N     . ARG A 151 ? 0.31040 0.27570 0.33060 0.04790  0.00950  -0.00890 147 ARG A N     
1074 C  CA    . ARG A 151 ? 0.29610 0.27020 0.32420 0.04970  0.01090  -0.00350 147 ARG A CA    
1075 C  C     . ARG A 151 ? 0.33100 0.30920 0.36060 0.04510  0.00740  0.00410  147 ARG A C     
1076 O  O     . ARG A 151 ? 0.28590 0.27290 0.31610 0.04370  0.00810  0.00820  147 ARG A O     
1077 C  CB    . ARG A 151 ? 0.27350 0.24510 0.31270 0.05540  0.01210  -0.00410 147 ARG A CB    
1078 C  CG    . ARG A 151 ? 0.32410 0.29270 0.36070 0.06010  0.01650  -0.01260 147 ARG A CG    
1079 C  CD    . ARG A 151 ? 0.36820 0.33410 0.41620 0.06650  0.01860  -0.01410 147 ARG A CD    
1080 N  NE    . ARG A 151 ? 0.49620 0.45340 0.55210 0.06680  0.01480  -0.01190 147 ARG A NE    
1081 C  CZ    . ARG A 151 ? 0.54020 0.48590 0.59620 0.06840  0.01420  -0.01780 147 ARG A CZ    
1082 N  NH1   . ARG A 151 ? 0.44690 0.38850 0.49460 0.06970  0.01690  -0.02680 147 ARG A NH1   
1083 N  NH2   . ARG A 151 ? 0.60460 0.54280 0.66880 0.06840  0.01060  -0.01460 147 ARG A NH2   
1084 N  N     . ARG A 152 ? 0.31250 0.28450 0.34210 0.04230  0.00360  0.00590  148 ARG A N     
1085 C  CA    . ARG A 152 ? 0.31690 0.29260 0.34590 0.03750  0.00050  0.01220  148 ARG A CA    
1086 C  C     . ARG A 152 ? 0.35830 0.33870 0.37810 0.03360  0.00130  0.01190  148 ARG A C     
1087 O  O     . ARG A 152 ? 0.34670 0.33420 0.36670 0.03110  0.00080  0.01630  148 ARG A O     
1088 C  CB    . ARG A 152 ? 0.28430 0.25240 0.31370 0.03510  -0.00300 0.01340  148 ARG A CB    
1089 C  CG    . ARG A 152 ? 0.30950 0.28120 0.33690 0.03000  -0.00580 0.01930  148 ARG A CG    
1090 C  CD    . ARG A 152 ? 0.37690 0.34240 0.40800 0.02850  -0.00910 0.02190  148 ARG A CD    
1091 N  NE    . ARG A 152 ? 0.54080 0.51160 0.57440 0.02530  -0.01160 0.02920  148 ARG A NE    
1092 C  CZ    . ARG A 152 ? 0.53010 0.50030 0.57200 0.02590  -0.01390 0.03460  148 ARG A CZ    
1093 N  NH1   . ARG A 152 ? 0.40580 0.36930 0.45520 0.02990  -0.01400 0.03330  148 ARG A NH1   
1094 N  NH2   . ARG A 152 ? 0.73400 0.71010 0.77660 0.02250  -0.01610 0.04140  148 ARG A NH2   
1095 N  N     . ALA A 153 ? 0.33430 0.31060 0.34600 0.03290  0.00220  0.00660  149 ALA A N     
1096 C  CA    . ALA A 153 ? 0.32340 0.30350 0.32690 0.02960  0.00300  0.00650  149 ALA A CA    
1097 C  C     . ALA A 153 ? 0.32500 0.31350 0.32940 0.03070  0.00600  0.00750  149 ALA A C     
1098 O  O     . ALA A 153 ? 0.30640 0.30040 0.30910 0.02750  0.00560  0.01090  149 ALA A O     
1099 C  CB    . ALA A 153 ? 0.32390 0.29880 0.31960 0.02920  0.00340  0.00100  149 ALA A CB    
1100 N  N     . LEU A 154 ? 0.29690 0.28660 0.30400 0.03530  0.00900  0.00450  150 LEU A N     
1101 C  CA    . LEU A 154 ? 0.32930 0.32780 0.33760 0.03640  0.01220  0.00560  150 LEU A CA    
1102 C  C     . LEU A 154 ? 0.28450 0.29000 0.30080 0.03560  0.01100  0.01200  150 LEU A C     
1103 O  O     . LEU A 154 ? 0.29130 0.30420 0.30690 0.03320  0.01170  0.01490  150 LEU A O     
1104 C  CB    . LEU A 154 ? 0.32480 0.32350 0.33490 0.04190  0.01610  0.00080  150 LEU A CB    
1105 C  CG    . LEU A 154 ? 0.40680 0.39960 0.40800 0.04260  0.01740  -0.00590 150 LEU A CG    
1106 C  CD1   . LEU A 154 ? 0.30780 0.30060 0.31070 0.04810  0.02150  -0.01130 150 LEU A CD1   
1107 C  CD2   . LEU A 154 ? 0.44260 0.43880 0.43480 0.03900  0.01790  -0.00570 150 LEU A CD2   
1108 N  N     . ARG A 155 ? 0.31900 0.32250 0.34320 0.03730  0.00900  0.01450  151 ARG A N     
1109 C  CA    . ARG A 155 ? 0.30330 0.31380 0.33500 0.03600  0.00700  0.02120  151 ARG A CA    
1110 C  C     . ARG A 155 ? 0.37030 0.38270 0.39650 0.02980  0.00410  0.02460  151 ARG A C     
1111 O  O     . ARG A 155 ? 0.27150 0.29190 0.29970 0.02730  0.00350  0.02870  151 ARG A O     
1112 C  CB    . ARG A 155 ? 0.28100 0.28790 0.32160 0.03870  0.00480  0.02370  151 ARG A CB    
1113 C  CG    . ARG A 155 ? 0.31510 0.32850 0.36220 0.03630  0.00150  0.03140  151 ARG A CG    
1114 C  CD    . ARG A 155 ? 0.24470 0.25540 0.30250 0.03980  -0.00040 0.03480  151 ARG A CD    
1115 N  NE    . ARG A 155 ? 0.31280 0.31320 0.36840 0.03930  -0.00240 0.03300  151 ARG A NE    
1116 C  CZ    . ARG A 155 ? 0.34750 0.33930 0.40500 0.04330  -0.00100 0.02800  151 ARG A CZ    
1117 N  NH1   . ARG A 155 ? 0.31160 0.30380 0.37260 0.04860  0.00290  0.02380  151 ARG A NH1   
1118 N  NH2   . ARG A 155 ? 0.26630 0.24930 0.32200 0.04190  -0.00330 0.02710  151 ARG A NH2   
1119 N  N     . THR A 156 ? 0.28230 0.28760 0.30220 0.02710  0.00220  0.02290  152 THR A N     
1120 C  CA    . THR A 156 ? 0.33510 0.34150 0.35020 0.02150  -0.00040 0.02580  152 THR A CA    
1121 C  C     . THR A 156 ? 0.36930 0.37930 0.37810 0.01870  0.00130  0.02460  152 THR A C     
1122 O  O     . THR A 156 ? 0.29970 0.31470 0.30770 0.01490  0.00000  0.02780  152 THR A O     
1123 C  CB    . THR A 156 ? 0.35100 0.34940 0.36170 0.01980  -0.00230 0.02420  152 THR A CB    
1124 O  OG1   . THR A 156 ? 0.31970 0.31450 0.33710 0.02230  -0.00390 0.02560  152 THR A OG1   
1125 C  CG2   . THR A 156 ? 0.25900 0.25900 0.26540 0.01460  -0.00440 0.02690  152 THR A CG2   
1126 N  N     . ALA A 157 ? 0.26750 0.27520 0.27180 0.02050  0.00400  0.02010  153 ALA A N     
1127 C  CA    . ALA A 157 ? 0.31340 0.32380 0.31190 0.01790  0.00550  0.01940  153 ALA A CA    
1128 C  C     . ALA A 157 ? 0.29150 0.31090 0.29430 0.01720  0.00660  0.02270  153 ALA A C     
1129 O  O     . ALA A 157 ? 0.30940 0.33170 0.30910 0.01330  0.00640  0.02420  153 ALA A O     
1130 C  CB    . ALA A 157 ? 0.22680 0.23390 0.22010 0.02020  0.00800  0.01470  153 ALA A CB    
1131 N  N     . GLN A 158 ? 0.31310 0.33700 0.32340 0.02110  0.00800  0.02380  154 GLN A N     
1132 C  CA    . GLN A 158 ? 0.27430 0.30760 0.28920 0.02110  0.00980  0.02650  154 GLN A CA    
1133 C  C     . GLN A 158 ? 0.36330 0.40320 0.38660 0.02030  0.00740  0.03190  154 GLN A C     
1134 O  O     . GLN A 158 ? 0.45400 0.50270 0.48250 0.02010  0.00850  0.03480  154 GLN A O     
1135 C  CB    . GLN A 158 ? 0.25450 0.29000 0.27160 0.02640  0.01410  0.02360  154 GLN A CB    
1136 C  CG    . GLN A 158 ? 0.34870 0.37900 0.35670 0.02670  0.01620  0.01870  154 GLN A CG    
1137 C  CD    . GLN A 158 ? 0.39080 0.42220 0.39970 0.03200  0.02030  0.01480  154 GLN A CD    
1138 O  OE1   . GLN A 158 ? 0.34060 0.37830 0.34850 0.03260  0.02370  0.01480  154 GLN A OE1   
1139 N  NE2   . GLN A 158 ? 0.37910 0.40420 0.38970 0.03590  0.02020  0.01140  154 GLN A NE2   
1140 N  N     . SER A 159 ? 0.28790 0.32450 0.31280 0.01940  0.00400  0.03380  155 SER A N     
1141 C  CA    . SER A 159 ? 0.33110 0.37410 0.36350 0.01830  0.00110  0.03950  155 SER A CA    
1142 C  C     . SER A 159 ? 0.34990 0.39380 0.37690 0.01170  -0.00220 0.04170  155 SER A C     
1143 O  O     . SER A 159 ? 0.31700 0.35470 0.33560 0.00900  -0.00250 0.03880  155 SER A O     
1144 C  CB    . SER A 159 ? 0.34220 0.38130 0.38040 0.02170  -0.00050 0.04080  155 SER A CB    
1145 O  OG    . SER A 159 ? 0.30610 0.34380 0.34980 0.02800  0.00260  0.03810  155 SER A OG    
1146 N  N     . GLY A 160 ? 0.30550 0.35740 0.33770 0.00930  -0.00490 0.04690  156 GLY A N     
1147 C  CA    . GLY A 160 ? 0.29820 0.35160 0.32480 0.00270  -0.00790 0.04850  156 GLY A CA    
1148 C  C     . GLY A 160 ? 0.26140 0.31260 0.28030 -0.00070 -0.00620 0.04490  156 GLY A C     
1149 O  O     . GLY A 160 ? 0.32600 0.37980 0.34610 0.00060  -0.00330 0.04380  156 GLY A O     
1150 N  N     . ARG A 161 ? 0.27090 0.31740 0.28190 -0.00490 -0.00770 0.04330  157 ARG A N     
1151 C  CA    . ARG A 161 ? 0.28430 0.32680 0.28810 -0.00770 -0.00610 0.03970  157 ARG A CA    
1152 C  C     . ARG A 161 ? 0.31460 0.34990 0.31550 -0.00350 -0.00300 0.03560  157 ARG A C     
1153 O  O     . ARG A 161 ? 0.29800 0.32710 0.29640 -0.00210 -0.00350 0.03390  157 ARG A O     
1154 C  CB    . ARG A 161 ? 0.32540 0.36450 0.32210 -0.01280 -0.00820 0.03870  157 ARG A CB    
1155 C  CG    . ARG A 161 ? 0.35260 0.38820 0.34330 -0.01620 -0.00690 0.03550  157 ARG A CG    
1156 C  CD    . ARG A 161 ? 0.28770 0.31880 0.27140 -0.02030 -0.00840 0.03360  157 ARG A CD    
1157 N  NE    . ARG A 161 ? 0.27410 0.30110 0.25290 -0.02330 -0.00710 0.03050  157 ARG A NE    
1158 C  CZ    . ARG A 161 ? 0.34100 0.36630 0.31490 -0.02810 -0.00830 0.02890  157 ARG A CZ    
1159 N  NH1   . ARG A 161 ? 0.29350 0.32160 0.26580 -0.03070 -0.01090 0.03010  157 ARG A NH1   
1160 N  NH2   . ARG A 161 ? 0.31120 0.33180 0.28170 -0.03030 -0.00690 0.02610  157 ARG A NH2   
1161 N  N     . PRO A 162 ? 0.29280 0.32920 0.29400 -0.00180 -0.00010 0.03420  158 PRO A N     
1162 C  CA    . PRO A 162 ? 0.29430 0.32480 0.29250 0.00220  0.00250  0.03040  158 PRO A CA    
1163 C  C     . PRO A 162 ? 0.30990 0.33240 0.30040 0.00020  0.00210  0.02740  158 PRO A C     
1164 O  O     . PRO A 162 ? 0.28750 0.30910 0.27420 -0.00410 0.00110  0.02750  158 PRO A O     
1165 C  CB    . PRO A 162 ? 0.29640 0.33150 0.29570 0.00320  0.00560  0.03040  158 PRO A CB    
1166 C  CG    . PRO A 162 ? 0.31340 0.35760 0.31910 0.00120  0.00470  0.03450  158 PRO A CG    
1167 C  CD    . PRO A 162 ? 0.29790 0.34150 0.30210 -0.00360 0.00090  0.03620  158 PRO A CD    
1168 N  N     . GLY A 163 ? 0.29360 0.31030 0.28180 0.00350  0.00290  0.02450  159 GLY A N     
1169 C  CA    . GLY A 163 ? 0.27600 0.28580 0.25790 0.00200  0.00260  0.02190  159 GLY A CA    
1170 C  C     . GLY A 163 ? 0.33280 0.33730 0.31290 0.00560  0.00350  0.01870  159 GLY A C     
1171 O  O     . GLY A 163 ? 0.33420 0.33960 0.31770 0.00940  0.00440  0.01800  159 GLY A O     
1172 N  N     . PRO A 164 ? 0.33270 0.33180 0.30770 0.00460  0.00320  0.01670  160 PRO A N     
1173 C  CA    . PRO A 164 ? 0.31550 0.30990 0.28820 0.00740  0.00370  0.01360  160 PRO A CA    
1174 C  C     . PRO A 164 ? 0.35170 0.34210 0.32650 0.00880  0.00200  0.01280  160 PRO A C     
1175 O  O     . PRO A 164 ? 0.30110 0.29160 0.27820 0.00710  0.00020  0.01500  160 PRO A O     
1176 C  CB    . PRO A 164 ? 0.30080 0.29180 0.26830 0.00520  0.00370  0.01250  160 PRO A CB    
1177 C  CG    . PRO A 164 ? 0.27640 0.26770 0.24380 0.00150  0.00260  0.01440  160 PRO A CG    
1178 C  CD    . PRO A 164 ? 0.25860 0.25580 0.22990 0.00070  0.00260  0.01690  160 PRO A CD    
1179 N  N     . ILE A 165 ? 0.38280 0.36970 0.35660 0.01160  0.00240  0.00980  161 ILE A N     
1180 C  CA    . ILE A 165 ? 0.31450 0.29680 0.29080 0.01320  0.00080  0.00860  161 ILE A CA    
1181 C  C     . ILE A 165 ? 0.30200 0.27930 0.27370 0.01310  0.00030  0.00530  161 ILE A C     
1182 O  O     . ILE A 165 ? 0.33210 0.31010 0.29950 0.01370  0.00160  0.00340  161 ILE A O     
1183 C  CB    . ILE A 165 ? 0.28720 0.27010 0.26830 0.01710  0.00180  0.00750  161 ILE A CB    
1184 C  CG1   . ILE A 165 ? 0.25420 0.24360 0.24040 0.01750  0.00260  0.01090  161 ILE A CG1   
1185 C  CG2   . ILE A 165 ? 0.26290 0.24020 0.24750 0.01820  -0.00020 0.00680  161 ILE A CG2   
1186 C  CD1   . ILE A 165 ? 0.26130 0.25190 0.25120 0.01520  0.00020  0.01510  161 ILE A CD1   
1187 N  N     . HIS A 166 ? 0.31850 0.29140 0.29140 0.01240  -0.00180 0.00520  162 HIS A N     
1188 C  CA    . HIS A 166 ? 0.27580 0.24420 0.24570 0.01230  -0.00300 0.00230  162 HIS A CA    
1189 C  C     . HIS A 166 ? 0.27700 0.24080 0.25040 0.01430  -0.00420 0.00030  162 HIS A C     
1190 O  O     . HIS A 166 ? 0.34100 0.30330 0.31920 0.01370  -0.00570 0.00250  162 HIS A O     
1191 C  CB    . HIS A 166 ? 0.29760 0.26490 0.26630 0.00920  -0.00430 0.00400  162 HIS A CB    
1192 C  CG    . HIS A 166 ? 0.36570 0.32890 0.33310 0.00890  -0.00610 0.00180  162 HIS A CG    
1193 N  ND1   . HIS A 166 ? 0.32210 0.28300 0.29230 0.00720  -0.00800 0.00310  162 HIS A ND1   
1194 C  CD2   . HIS A 166 ? 0.36550 0.32720 0.32920 0.00970  -0.00630 -0.00120 162 HIS A CD2   
1195 C  CE1   . HIS A 166 ? 0.36510 0.32310 0.33390 0.00700  -0.00950 0.00080  162 HIS A CE1   
1196 N  NE2   . HIS A 166 ? 0.37960 0.33800 0.34410 0.00840  -0.00870 -0.00180 162 HIS A NE2   
1197 N  N     . LEU A 167 ? 0.29000 0.25150 0.26090 0.01650  -0.00370 -0.00400 163 LEU A N     
1198 C  CA    . LEU A 167 ? 0.25770 0.21350 0.23130 0.01830  -0.00490 -0.00720 163 LEU A CA    
1199 C  C     . LEU A 167 ? 0.38230 0.33420 0.35160 0.01680  -0.00690 -0.01030 163 LEU A C     
1200 O  O     . LEU A 167 ? 0.35780 0.31120 0.32110 0.01700  -0.00610 -0.01290 163 LEU A O     
1201 C  CB    . LEU A 167 ? 0.36870 0.32470 0.34310 0.02220  -0.00260 -0.01060 163 LEU A CB    
1202 C  CG    . LEU A 167 ? 0.46070 0.41860 0.44220 0.02470  -0.00140 -0.00830 163 LEU A CG    
1203 C  CD1   . LEU A 167 ? 0.43040 0.38740 0.41240 0.02900  0.00120  -0.01310 163 LEU A CD1   
1204 C  CD2   . LEU A 167 ? 0.40730 0.36130 0.39570 0.02390  -0.00400 -0.00530 163 LEU A CD2   
1205 N  N     . ASN A 168 ? 0.37970 0.32730 0.35230 0.01510  -0.00960 -0.00970 164 ASN A N     
1206 C  CA    . ASN A 168 ? 0.33830 0.28260 0.30820 0.01320  -0.01200 -0.01190 164 ASN A CA    
1207 C  C     . ASN A 168 ? 0.35860 0.29650 0.33040 0.01450  -0.01350 -0.01650 164 ASN A C     
1208 O  O     . ASN A 168 ? 0.38530 0.31950 0.36340 0.01520  -0.01430 -0.01540 164 ASN A O     
1209 C  CB    . ASN A 168 ? 0.32490 0.26970 0.29780 0.01000  -0.01390 -0.00770 164 ASN A CB    
1210 C  CG    . ASN A 168 ? 0.37450 0.31720 0.34600 0.00780  -0.01660 -0.00920 164 ASN A CG    
1211 O  OD1   . ASN A 168 ? 0.38080 0.31980 0.35670 0.00620  -0.01890 -0.00870 164 ASN A OD1   
1212 N  ND2   . ASN A 168 ? 0.40270 0.34790 0.36860 0.00740  -0.01640 -0.01060 164 ASN A ND2   
1213 N  N     . ILE A 169 ? 0.39700 0.33310 0.36310 0.01460  -0.01420 -0.02130 165 ILE A N     
1214 C  CA    . ILE A 169 ? 0.34680 0.27660 0.31310 0.01620  -0.01500 -0.02720 165 ILE A CA    
1215 C  C     . ILE A 169 ? 0.40810 0.33370 0.37260 0.01330  -0.01880 -0.02990 165 ILE A C     
1216 O  O     . ILE A 169 ? 0.39020 0.31840 0.34790 0.01190  -0.01960 -0.03160 165 ILE A O     
1217 C  CB    . ILE A 169 ? 0.43140 0.36320 0.39170 0.01940  -0.01190 -0.03190 165 ILE A CB    
1218 C  CG1   . ILE A 169 ? 0.49570 0.43290 0.45850 0.02200  -0.00820 -0.02860 165 ILE A CG1   
1219 C  CG2   . ILE A 169 ? 0.41590 0.34070 0.37640 0.02140  -0.01220 -0.03880 165 ILE A CG2   
1220 C  CD1   . ILE A 169 ? 0.45490 0.39680 0.41150 0.02440  -0.00460 -0.03150 165 ILE A CD1   
1221 N  N     . PRO A 170 ? 0.41120 0.33050 0.38180 0.01190  -0.02150 -0.03000 166 PRO A N     
1222 C  CA    . PRO A 170 ? 0.39010 0.30560 0.35940 0.00870  -0.02550 -0.03280 166 PRO A CA    
1223 C  C     . PRO A 170 ? 0.53580 0.44850 0.49780 0.00980  -0.02570 -0.04060 166 PRO A C     
1224 O  O     . PRO A 170 ? 0.44330 0.35280 0.40460 0.01320  -0.02340 -0.04510 166 PRO A O     
1225 C  CB    . PRO A 170 ? 0.40450 0.31330 0.38280 0.00750  -0.02780 -0.03130 166 PRO A CB    
1226 C  CG    . PRO A 170 ? 0.42160 0.33340 0.40550 0.00910  -0.02550 -0.02530 166 PRO A CG    
1227 C  CD    . PRO A 170 ? 0.36870 0.28470 0.34810 0.01280  -0.02150 -0.02670 166 PRO A CD    
1228 N  N     . ALA A 171 ? 0.43010 0.34450 0.38660 0.00680  -0.02850 -0.04220 167 ALA A N     
1229 C  CA    . ALA A 171 ? 0.48330 0.39700 0.43080 0.00730  -0.02870 -0.04920 167 ALA A CA    
1230 C  C     . ALA A 171 ? 0.43850 0.34280 0.38720 0.00780  -0.03010 -0.05630 167 ALA A C     
1231 O  O     . ALA A 171 ? 0.57710 0.47980 0.51950 0.01010  -0.02820 -0.06300 167 ALA A O     
1232 C  CB    . ALA A 171 ? 0.52410 0.44210 0.46630 0.00360  -0.03220 -0.04840 167 ALA A CB    
1233 N  N     . ASP A 172 ? 0.42770 0.32560 0.38480 0.00580  -0.03300 -0.05510 168 ASP A N     
1234 C  CA    . ASP A 172 ? 0.54040 0.42820 0.49940 0.00620  -0.03450 -0.06210 168 ASP A CA    
1235 C  C     . ASP A 172 ? 0.59940 0.48330 0.56250 0.01130  -0.03030 -0.06410 168 ASP A C     
1236 O  O     . ASP A 172 ? 0.73290 0.61030 0.69360 0.01350  -0.02940 -0.07190 168 ASP A O     
1237 C  CB    . ASP A 172 ? 0.50910 0.39110 0.47640 0.00190  -0.03930 -0.05980 168 ASP A CB    
1238 C  CG    . ASP A 172 ? 0.64220 0.52630 0.61920 0.00170  -0.03870 -0.05080 168 ASP A CG    
1239 O  OD1   . ASP A 172 ? 0.69400 0.58560 0.67030 0.00360  -0.03550 -0.04580 168 ASP A OD1   
1240 O  OD2   . ASP A 172 ? 0.75360 0.63190 0.73900 -0.00060 -0.04150 -0.04880 168 ASP A OD2   
1241 N  N     . ILE A 173 ? 0.51080 0.39870 0.47990 0.01340  -0.02780 -0.05710 169 ILE A N     
1242 C  CA    . ILE A 173 ? 0.56800 0.45420 0.54170 0.01840  -0.02370 -0.05760 169 ILE A CA    
1243 C  C     . ILE A 173 ? 0.48380 0.37400 0.44920 0.02220  -0.01940 -0.06300 169 ILE A C     
1244 O  O     . ILE A 173 ? 0.45260 0.33920 0.42020 0.02670  -0.01630 -0.06720 169 ILE A O     
1245 C  CB    . ILE A 173 ? 0.56380 0.45550 0.54430 0.01880  -0.02250 -0.04820 169 ILE A CB    
1246 C  CG1   . ILE A 173 ? 0.58930 0.47600 0.57950 0.01600  -0.02600 -0.04340 169 ILE A CG1   
1247 C  CG2   . ILE A 173 ? 0.58980 0.48420 0.57300 0.02390  -0.01800 -0.04750 169 ILE A CG2   
1248 C  CD1   . ILE A 173 ? 0.74980 0.62520 0.74460 0.01610  -0.02820 -0.04870 169 ILE A CD1   
1249 N  N     . ALA A 174 ? 0.41950 0.31730 0.37550 0.02070  -0.01910 -0.06270 170 ALA A N     
1250 C  CA    . ALA A 174 ? 0.48200 0.38610 0.43090 0.02400  -0.01450 -0.06520 170 ALA A CA    
1251 C  C     . ALA A 174 ? 0.50230 0.40110 0.44680 0.02700  -0.01250 -0.07490 170 ALA A C     
1252 O  O     . ALA A 174 ? 0.51520 0.41740 0.45830 0.03140  -0.00760 -0.07690 170 ALA A O     
1253 C  CB    . ALA A 174 ? 0.48930 0.40140 0.42900 0.02120  -0.01530 -0.06300 170 ALA A CB    
1254 N  N     . LYS A 175 ? 0.49000 0.38100 0.43220 0.02480  -0.01600 -0.08130 171 LYS A N     
1255 C  CA    . LYS A 175 ? 0.57840 0.46430 0.51500 0.02740  -0.01400 -0.09160 171 LYS A CA    
1256 C  C     . LYS A 175 ? 0.57100 0.44470 0.51650 0.02930  -0.01470 -0.09620 171 LYS A C     
1257 O  O     . LYS A 175 ? 0.56100 0.42810 0.50230 0.03080  -0.01390 -0.10580 171 LYS A O     
1258 C  CB    . LYS A 175 ? 0.59680 0.48330 0.52130 0.02340  -0.01720 -0.09710 171 LYS A CB    
1259 C  CG    . LYS A 175 ? 0.69330 0.59180 0.60890 0.02170  -0.01650 -0.09260 171 LYS A CG    
1260 C  CD    . LYS A 175 ? 0.71160 0.61180 0.61400 0.01880  -0.01870 -0.09900 171 LYS A CD    
1261 C  CE    . LYS A 175 ? 0.67350 0.57280 0.56790 0.02270  -0.01400 -0.10830 171 LYS A CE    
1262 N  NZ    . LYS A 175 ? 0.69450 0.59800 0.57420 0.01980  -0.01560 -0.11360 171 LYS A NZ    
1263 N  N     . HIS A 176 ? 0.51580 0.38640 0.47360 0.02950  -0.01580 -0.08960 172 HIS A N     
1264 C  CA    . HIS A 176 ? 0.50090 0.36020 0.46820 0.03210  -0.01590 -0.09310 172 HIS A CA    
1265 C  C     . HIS A 176 ? 0.51890 0.37910 0.48850 0.03910  -0.00970 -0.09630 172 HIS A C     
1266 O  O     . HIS A 176 ? 0.49520 0.36530 0.46410 0.04160  -0.00590 -0.09160 172 HIS A O     
1267 C  CB    . HIS A 176 ? 0.58530 0.44180 0.56510 0.03030  -0.01890 -0.08420 172 HIS A CB    
1268 C  CG    . HIS A 176 ? 0.68970 0.54410 0.66950 0.02380  -0.02480 -0.08150 172 HIS A CG    
1269 N  ND1   . HIS A 176 ? 0.71600 0.57140 0.70430 0.02100  -0.02740 -0.07230 172 HIS A ND1   
1270 C  CD2   . HIS A 176 ? 0.73270 0.58460 0.70500 0.01940  -0.02850 -0.08680 172 HIS A CD2   
1271 C  CE1   . HIS A 176 ? 0.73930 0.59320 0.72600 0.01540  -0.03220 -0.07180 172 HIS A CE1   
1272 N  NE2   . HIS A 176 ? 0.73180 0.58360 0.70910 0.01420  -0.03320 -0.08040 172 HIS A NE2   
1273 N  N     . PRO A 177 ? 0.52030 0.37030 0.49330 0.04230  -0.00850 -0.10440 173 PRO A N     
1274 C  CA    . PRO A 177 ? 0.54030 0.39120 0.51660 0.04950  -0.00220 -0.10780 173 PRO A CA    
1275 C  C     . PRO A 177 ? 0.57380 0.42600 0.56450 0.05250  -0.00120 -0.09870 173 PRO A C     
1276 O  O     . PRO A 177 ? 0.62530 0.47150 0.62540 0.05020  -0.00530 -0.09330 173 PRO A O     
1277 C  CB    . PRO A 177 ? 0.56790 0.40570 0.54440 0.05150  -0.00200 -0.11950 173 PRO A CB    
1278 C  CG    . PRO A 177 ? 0.57420 0.40470 0.54650 0.04470  -0.00860 -0.12210 173 PRO A CG    
1279 C  CD    . PRO A 177 ? 0.54690 0.38380 0.52170 0.03960  -0.01280 -0.11090 173 PRO A CD    
1280 N  N     . VAL A 178 ? 0.54180 0.40260 0.53410 0.05740  0.00410  -0.09650 174 VAL A N     
1281 C  CA    . VAL A 178 ? 0.49920 0.36240 0.50490 0.06090  0.00550  -0.08830 174 VAL A CA    
1282 C  C     . VAL A 178 ? 0.52180 0.38690 0.53120 0.06840  0.01190  -0.09280 174 VAL A C     
1283 O  O     . VAL A 178 ? 0.46070 0.33000 0.46040 0.07030  0.01600  -0.09990 174 VAL A O     
1284 C  CB    . VAL A 178 ? 0.49170 0.36710 0.49700 0.05810  0.00470  -0.07740 174 VAL A CB    
1285 C  CG1   . VAL A 178 ? 0.50380 0.37880 0.50410 0.05090  -0.00080 -0.07350 174 VAL A CG1   
1286 C  CG2   . VAL A 178 ? 0.40230 0.28980 0.39940 0.06010  0.00970  -0.07820 174 VAL A CG2   
1287 N  N     . PRO A 179 ? 0.55770 0.42080 0.58150 0.07270  0.01300  -0.08820 175 PRO A N     
1288 C  CA    . PRO A 179 ? 0.55540 0.42180 0.58470 0.08030  0.01930  -0.09140 175 PRO A CA    
1289 C  C     . PRO A 179 ? 0.55760 0.43940 0.58020 0.08110  0.02360  -0.08850 175 PRO A C     
1290 O  O     . PRO A 179 ? 0.47180 0.36240 0.49330 0.07740  0.02160  -0.07960 175 PRO A O     
1291 C  CB    . PRO A 179 ? 0.56620 0.42980 0.61300 0.08330  0.01810  -0.08340 175 PRO A CB    
1292 C  CG    . PRO A 179 ? 0.56010 0.41310 0.61010 0.07800  0.01140  -0.08070 175 PRO A CG    
1293 C  CD    . PRO A 179 ? 0.57650 0.43350 0.61260 0.07090  0.00830  -0.08040 175 PRO A CD    
1294 N  N     . LEU A 180 ? 0.53010 0.41510 0.54840 0.08600  0.02960  -0.09630 176 LEU A N     
1295 C  CA    . LEU A 180 ? 0.55470 0.45450 0.56680 0.08680  0.03410  -0.09380 176 LEU A CA    
1296 C  C     . LEU A 180 ? 0.58100 0.48870 0.60690 0.09090  0.03640  -0.08530 176 LEU A C     
1297 O  O     . LEU A 180 ? 0.63970 0.54750 0.67420 0.09760  0.04120  -0.08830 176 LEU A O     
1298 C  CB    . LEU A 180 ? 0.49020 0.39160 0.49250 0.09020  0.03990  -0.10480 176 LEU A CB    
1299 C  CG    . LEU A 180 ? 0.47540 0.39230 0.47180 0.09150  0.04530  -0.10250 176 LEU A CG    
1300 C  CD1   . LEU A 180 ? 0.52410 0.44910 0.51210 0.08460  0.04170  -0.09490 176 LEU A CD1   
1301 C  CD2   . LEU A 180 ? 0.56660 0.48460 0.55180 0.09440  0.05090  -0.11400 176 LEU A CD2   
1302 N  N     . GLU A 181 ? 0.58280 0.49720 0.61140 0.08680  0.03290  -0.07460 177 GLU A N     
1303 C  CA    . GLU A 181 ? 0.51010 0.43210 0.55180 0.08930  0.03360  -0.06530 177 GLU A CA    
1304 C  C     . GLU A 181 ? 0.42620 0.36170 0.46250 0.08540  0.03350  -0.05790 177 GLU A C     
1305 O  O     . GLU A 181 ? 0.46270 0.39890 0.49610 0.07950  0.02870  -0.05180 177 GLU A O     
1306 C  CB    . GLU A 181 ? 0.64110 0.55530 0.69440 0.08820  0.02830  -0.05900 177 GLU A CB    
1307 C  CG    . GLU A 181 ? 0.82380 0.73000 0.89060 0.09500  0.03020  -0.06190 177 GLU A CG    
1308 C  CD    . GLU A 181 ? 0.97430 0.89090 1.05190 0.10100  0.03490  -0.05780 177 GLU A CD    
1309 O  OE1   . GLU A 181 ? 0.99350 0.90630 1.08610 0.10560  0.03480  -0.05480 177 GLU A OE1   
1310 O  OE2   . GLU A 181 ? 1.03430 0.96320 1.10620 0.10100  0.03850  -0.05690 177 GLU A OE2   
1311 N  N     . VAL A 182 ? 0.42310 0.36930 0.45840 0.08860  0.03910  -0.05860 178 VAL A N     
1312 C  CA    . VAL A 182 ? 0.48430 0.44340 0.51450 0.08520  0.03980  -0.05250 178 VAL A CA    
1313 C  C     . VAL A 182 ? 0.48850 0.45770 0.53160 0.08900  0.04240  -0.04580 178 VAL A C     
1314 O  O     . VAL A 182 ? 0.45950 0.42950 0.51080 0.09560  0.04700  -0.04900 178 VAL A O     
1315 C  CB    . VAL A 182 ? 0.45660 0.42060 0.47310 0.08490  0.04400  -0.05900 178 VAL A CB    
1316 C  CG1   . VAL A 182 ? 0.43270 0.40980 0.44480 0.08130  0.04480  -0.05230 178 VAL A CG1   
1317 C  CG2   . VAL A 182 ? 0.42660 0.38100 0.43070 0.08100  0.04090  -0.06550 178 VAL A CG2   
1318 N  N     . PHE A 183 ? 0.43590 0.41270 0.48100 0.08480  0.03950  -0.03650 179 PHE A N     
1319 C  CA    . PHE A 183 ? 0.42310 0.40970 0.48090 0.08730  0.04070  -0.02910 179 PHE A CA    
1320 C  C     . PHE A 183 ? 0.31270 0.31280 0.36580 0.08450  0.04280  -0.02490 179 PHE A C     
1321 O  O     . PHE A 183 ? 0.34210 0.34300 0.38420 0.07880  0.04070  -0.02410 179 PHE A O     
1322 C  CB    . PHE A 183 ? 0.37840 0.36270 0.44490 0.08470  0.03480  -0.02060 179 PHE A CB    
1323 C  CG    . PHE A 183 ? 0.42950 0.40130 0.50320 0.08730  0.03230  -0.02260 179 PHE A CG    
1324 C  CD1   . PHE A 183 ? 0.42570 0.38580 0.49150 0.08400  0.02900  -0.02690 179 PHE A CD1   
1325 C  CD2   . PHE A 183 ? 0.51880 0.49060 0.60790 0.09280  0.03300  -0.01950 179 PHE A CD2   
1326 C  CE1   . PHE A 183 ? 0.44270 0.39100 0.51570 0.08590  0.02650  -0.02840 179 PHE A CE1   
1327 C  CE2   . PHE A 183 ? 0.50400 0.46380 0.60050 0.09500  0.03060  -0.02080 179 PHE A CE2   
1328 C  CZ    . PHE A 183 ? 0.47280 0.42070 0.56120 0.09140  0.02730  -0.02530 179 PHE A CZ    
1329 N  N     . PRO A 184 ? 0.32650 0.33740 0.38900 0.08840  0.04670  -0.02160 180 PRO A N     
1330 C  CA    . PRO A 184 ? 0.38300 0.40690 0.44320 0.08460  0.04740  -0.01580 180 PRO A CA    
1331 C  C     . PRO A 184 ? 0.41210 0.43740 0.47420 0.07880  0.04140  -0.00750 180 PRO A C     
1332 O  O     . PRO A 184 ? 0.39530 0.41570 0.46530 0.07900  0.03730  -0.00380 180 PRO A O     
1333 C  CB    . PRO A 184 ? 0.38780 0.42250 0.46060 0.09080  0.05270  -0.01400 180 PRO A CB    
1334 C  CG    . PRO A 184 ? 0.41500 0.44210 0.49960 0.09670  0.05250  -0.01570 180 PRO A CG    
1335 C  CD    . PRO A 184 ? 0.40950 0.42130 0.48540 0.09600  0.05040  -0.02310 180 PRO A CD    
1336 N  N     . PRO A 185 ? 0.39770 0.42940 0.45260 0.07310  0.04030  -0.00370 181 PRO A N     
1337 C  CA    . PRO A 185 ? 0.40040 0.43260 0.45530 0.06700  0.03450  0.00320  181 PRO A CA    
1338 C  C     . PRO A 185 ? 0.45660 0.49390 0.52510 0.06800  0.03200  0.01060  181 PRO A C     
1339 O  O     . PRO A 185 ? 0.45240 0.48590 0.52150 0.06430  0.02680  0.01470  181 PRO A O     
1340 C  CB    . PRO A 185 ? 0.41330 0.45360 0.46060 0.06220  0.03550  0.00540  181 PRO A CB    
1341 C  CG    . PRO A 185 ? 0.48830 0.52690 0.52620 0.06410  0.04000  -0.00180 181 PRO A CG    
1342 C  CD    . PRO A 185 ? 0.44510 0.48250 0.49000 0.07160  0.04420  -0.00660 181 PRO A CD    
1343 N  N     . MET A 186 ? 0.34700 0.39330 0.42660 0.07280  0.03550  0.01260  182 MET A N     
1344 C  CA    . MET A 186 ? 0.44350 0.49650 0.53650 0.07330  0.03270  0.02070  182 MET A CA    
1345 C  C     . MET A 186 ? 0.41190 0.45620 0.51280 0.07630  0.02970  0.02150  182 MET A C     
1346 O  O     . MET A 186 ? 0.41650 0.46450 0.52620 0.07510  0.02570  0.02900  182 MET A O     
1347 C  CB    . MET A 186 ? 0.50860 0.57450 0.61280 0.07790  0.03740  0.02300  182 MET A CB    
1348 C  CG    . MET A 186 ? 0.69670 0.76090 0.80600 0.08630  0.04370  0.01640  182 MET A CG    
1349 S  SD    . MET A 186 ? 0.86550 0.94100 0.99590 0.09390  0.04680  0.02140  182 MET A SD    
1350 C  CE    . MET A 186 ? 0.77760 0.84580 0.91780 0.09360  0.03960  0.02760  182 MET A CE    
1351 N  N     . ASN A 187 ? 0.37690 0.40940 0.47460 0.07970  0.03110  0.01430  183 ASN A N     
1352 C  CA    . ASN A 187 ? 0.35750 0.38040 0.46290 0.08240  0.02810  0.01500  183 ASN A CA    
1353 C  C     . ASN A 187 ? 0.35660 0.37260 0.45580 0.07600  0.02190  0.01820  183 ASN A C     
1354 O  O     . ASN A 187 ? 0.37050 0.38140 0.47740 0.07670  0.01830  0.02210  183 ASN A O     
1355 C  CB    . ASN A 187 ? 0.41240 0.42460 0.51660 0.08790  0.03180  0.00560  183 ASN A CB    
1356 C  CG    . ASN A 187 ? 0.48660 0.50390 0.60090 0.09580  0.03780  0.00290  183 ASN A CG    
1357 O  OD1   . ASN A 187 ? 0.57450 0.60300 0.70000 0.09790  0.03870  0.00920  183 ASN A OD1   
1358 N  ND2   . ASN A 187 ? 0.53870 0.54810 0.64940 0.10030  0.04210  -0.00670 183 ASN A ND2   
1359 N  N     . TYR A 188 ? 0.28190 0.29710 0.36770 0.07010  0.02070  0.01660  184 TYR A N     
1360 C  CA    . TYR A 188 ? 0.28160 0.28990 0.36130 0.06450  0.01550  0.01860  184 TYR A CA    
1361 C  C     . TYR A 188 ? 0.33600 0.35150 0.40960 0.05770  0.01280  0.02380  184 TYR A C     
1362 O  O     . TYR A 188 ? 0.34710 0.35740 0.41330 0.05280  0.00930  0.02440  184 TYR A O     
1363 C  CB    . TYR A 188 ? 0.28210 0.27900 0.35130 0.06380  0.01600  0.01070  184 TYR A CB    
1364 C  CG    . TYR A 188 ? 0.38900 0.38840 0.44680 0.06260  0.01940  0.00520  184 TYR A CG    
1365 C  CD1   . TYR A 188 ? 0.36420 0.36620 0.41220 0.05650  0.01770  0.00680  184 TYR A CD1   
1366 C  CD2   . TYR A 188 ? 0.42990 0.42890 0.48680 0.06760  0.02450  -0.00160 184 TYR A CD2   
1367 C  CE1   . TYR A 188 ? 0.36090 0.36510 0.39890 0.05540  0.02070  0.00250  184 TYR A CE1   
1368 C  CE2   . TYR A 188 ? 0.38830 0.39020 0.43450 0.06630  0.02760  -0.00610 184 TYR A CE2   
1369 C  CZ    . TYR A 188 ? 0.43890 0.44340 0.47600 0.06020  0.02550  -0.00360 184 TYR A CZ    
1370 O  OH    . TYR A 188 ? 0.43190 0.43930 0.45910 0.05900  0.02850  -0.00730 184 TYR A OH    
1371 N  N     . ARG A 189 ? 0.31230 0.33930 0.38880 0.05720  0.01430  0.02730  185 ARG A N     
1372 C  CA    . ARG A 189 ? 0.31970 0.35350 0.39280 0.05080  0.01100  0.03290  185 ARG A CA    
1373 C  C     . ARG A 189 ? 0.45460 0.50110 0.53810 0.05200  0.01160  0.03880  185 ARG A C     
1374 O  O     . ARG A 189 ? 0.47910 0.53020 0.56920 0.05720  0.01580  0.03720  185 ARG A O     
1375 C  CB    . ARG A 189 ? 0.37480 0.40830 0.43500 0.04620  0.01200  0.02950  185 ARG A CB    
1376 C  CG    . ARG A 189 ? 0.48080 0.51750 0.53740 0.04860  0.01730  0.02470  185 ARG A CG    
1377 C  CD    . ARG A 189 ? 0.51230 0.54400 0.55520 0.04430  0.01720  0.02080  185 ARG A CD    
1378 N  NE    . ARG A 189 ? 0.46860 0.50340 0.50620 0.04560  0.02180  0.01670  185 ARG A NE    
1379 C  CZ    . ARG A 189 ? 0.49930 0.54360 0.53710 0.04380  0.02370  0.01940  185 ARG A CZ    
1380 N  NH1   . ARG A 189 ? 0.36970 0.42120 0.41300 0.04060  0.02130  0.02570  185 ARG A NH1   
1381 N  NH2   . ARG A 189 ? 0.51470 0.56160 0.54730 0.04500  0.02790  0.01600  185 ARG A NH2   
1382 N  N     . GLY A 190 ? 0.42920 0.48160 0.51430 0.04710  0.00720  0.04560  186 GLY A N     
1383 C  CA    . GLY A 190 ? 0.37910 0.44380 0.47500 0.04750  0.00640  0.05220  186 GLY A CA    
1384 C  C     . GLY A 190 ? 0.34950 0.42370 0.44170 0.04350  0.00760  0.05320  186 GLY A C     
1385 O  O     . GLY A 190 ? 0.33120 0.40230 0.41260 0.04050  0.00930  0.04880  186 GLY A O     
1386 N  N     . GLY A 191 ? 0.31900 0.40500 0.42110 0.04300  0.00630  0.05960  187 GLY A N     
1387 C  CA    . GLY A 191 ? 0.32430 0.42030 0.42510 0.03890  0.00710  0.06150  187 GLY A CA    
1388 C  C     . GLY A 191 ? 0.37580 0.47230 0.46830 0.03050  0.00230  0.06400  187 GLY A C     
1389 O  O     . GLY A 191 ? 0.34340 0.43170 0.42850 0.02760  -0.00080 0.06300  187 GLY A O     
1390 N  N     . LYS A 192 ? 0.35750 0.46390 0.45140 0.02640  0.00180  0.06700  188 LYS A N     
1391 C  CA    . LYS A 192 ? 0.37260 0.47970 0.45830 0.01820  -0.00200 0.06830  188 LYS A CA    
1392 C  C     . LYS A 192 ? 0.25630 0.37230 0.34880 0.01460  -0.00740 0.07560  188 LYS A C     
1393 O  O     . LYS A 192 ? 0.22880 0.35460 0.33400 0.01770  -0.00750 0.08060  188 LYS A O     
1394 C  CB    . LYS A 192 ? 0.50740 0.61920 0.58980 0.01510  0.00070  0.06680  188 LYS A CB    
1395 C  CG    . LYS A 192 ? 0.67260 0.77470 0.74350 0.01520  0.00430  0.06010  188 LYS A CG    
1396 C  CD    . LYS A 192 ? 0.77260 0.86320 0.83250 0.01200  0.00150  0.05700  188 LYS A CD    
1397 C  CE    . LYS A 192 ? 0.79530 0.87710 0.85480 0.01740  0.00240  0.05400  188 LYS A CE    
1398 N  NZ    . LYS A 192 ? 0.74110 0.81400 0.79230 0.01420  -0.00090 0.05250  188 LYS A NZ    
1399 N  N     . PRO A 193 ? 0.33200 0.44560 0.41690 0.00830  -0.01210 0.07670  189 PRO A N     
1400 C  CA    . PRO A 193 ? 0.28540 0.40830 0.37580 0.00430  -0.01760 0.08370  189 PRO A CA    
1401 C  C     . PRO A 193 ? 0.27100 0.40510 0.36430 -0.00070 -0.01870 0.08650  189 PRO A C     
1402 O  O     . PRO A 193 ? 0.28070 0.41310 0.36770 -0.00380 -0.01650 0.08270  189 PRO A O     
1403 C  CB    . PRO A 193 ? 0.26480 0.38030 0.34370 -0.00090 -0.02140 0.08250  189 PRO A CB    
1404 C  CG    . PRO A 193 ? 0.35600 0.46110 0.42310 -0.00200 -0.01790 0.07490  189 PRO A CG    
1405 C  CD    . PRO A 193 ? 0.33000 0.43240 0.40100 0.00470  -0.01230 0.07150  189 PRO A CD    
1406 N  N     . ALA A 194 ? 0.27400 0.41990 0.37780 -0.00160 -0.02240 0.09370  190 ALA A N     
1407 C  CA    . ALA A 194 ? 0.23420 0.39210 0.34250 -0.00680 -0.02430 0.09740  190 ALA A CA    
1408 C  C     . ALA A 194 ? 0.34900 0.51160 0.45360 -0.01470 -0.03140 0.10140  190 ALA A C     
1409 O  O     . ALA A 194 ? 0.29010 0.44920 0.39170 -0.01490 -0.03470 0.10310  190 ALA A O     
1410 C  CB    . ALA A 194 ? 0.29520 0.46570 0.42040 -0.00160 -0.02280 0.10290  190 ALA A CB    
1411 N  N     . PRO A 195 ? 0.31800 0.48870 0.42260 -0.02150 -0.03390 0.10320  191 PRO A N     
1412 C  CA    . PRO A 195 ? 0.32160 0.49790 0.42280 -0.02930 -0.04100 0.10700  191 PRO A CA    
1413 C  C     . PRO A 195 ? 0.28430 0.47310 0.39910 -0.02720 -0.04500 0.11590  191 PRO A C     
1414 O  O     . PRO A 195 ? 0.29060 0.48580 0.41890 -0.02060 -0.04230 0.11930  191 PRO A O     
1415 C  CB    . PRO A 195 ? 0.32980 0.51120 0.42890 -0.03660 -0.04190 0.10590  191 PRO A CB    
1416 C  CG    . PRO A 195 ? 0.34030 0.52700 0.45020 -0.03140 -0.03670 0.10660  191 PRO A CG    
1417 C  CD    . PRO A 195 ? 0.31800 0.49400 0.42640 -0.02270 -0.03070 0.10220  191 PRO A CD    
1418 N  N     . THR A 196 ? 0.31310 0.50560 0.42420 -0.03260 -0.05140 0.11980  192 THR A N     
1419 C  CA    . THR A 196 ? 0.37040 0.57640 0.49440 -0.03190 -0.05630 0.12930  192 THR A CA    
1420 C  C     . THR A 196 ? 0.32970 0.55010 0.46180 -0.03680 -0.05900 0.13340  192 THR A C     
1421 O  O     . THR A 196 ? 0.32760 0.54720 0.45180 -0.04370 -0.05940 0.12940  192 THR A O     
1422 C  CB    . THR A 196 ? 0.37740 0.58380 0.49420 -0.03670 -0.06270 0.13270  192 THR A CB    
1423 O  OG1   . THR A 196 ? 0.40560 0.61410 0.51110 -0.04680 -0.06690 0.13060  192 THR A OG1   
1424 C  CG2   . THR A 196 ? 0.37360 0.56550 0.48070 -0.03330 -0.06030 0.12830  192 THR A CG2   
1425 N  N     . ILE A 197 ? 0.34930 0.58320 0.49790 -0.03340 -0.06110 0.14190  193 ILE A N     
1426 C  CA    . ILE A 197 ? 0.39310 0.64230 0.55120 -0.03820 -0.06410 0.14690  193 ILE A CA    
1427 C  C     . ILE A 197 ? 0.34410 0.59730 0.49200 -0.04960 -0.07150 0.14760  193 ILE A C     
1428 O  O     . ILE A 197 ? 0.35070 0.61000 0.49840 -0.05640 -0.07310 0.14700  193 ILE A O     
1429 C  CB    . ILE A 197 ? 0.41900 0.68270 0.59750 -0.03230 -0.06560 0.15670  193 ILE A CB    
1430 C  CG1   . ILE A 197 ? 0.49330 0.75360 0.68190 -0.02150 -0.05730 0.15460  193 ILE A CG1   
1431 C  CG2   . ILE A 197 ? 0.40120 0.68240 0.58940 -0.03850 -0.07010 0.16300  193 ILE A CG2   
1432 C  CD1   . ILE A 197 ? 0.57540 0.83700 0.76470 -0.02200 -0.05180 0.15000  193 ILE A CD1   
1433 N  N     . MET A 198 ? 0.27180 0.52150 0.41090 -0.05220 -0.07600 0.14870  194 MET A N     
1434 C  CA    . MET A 198 ? 0.37750 0.63070 0.50550 -0.06310 -0.08290 0.14870  194 MET A CA    
1435 C  C     . MET A 198 ? 0.38100 0.62350 0.49400 -0.06920 -0.08040 0.13880  194 MET A C     
1436 O  O     . MET A 198 ? 0.36770 0.61580 0.47730 -0.07790 -0.08440 0.13810  194 MET A O     
1437 C  CB    . MET A 198 ? 0.41810 0.66820 0.53790 -0.06400 -0.08690 0.15100  194 MET A CB    
1438 C  CG    . MET A 198 ? 0.62510 0.88160 0.73470 -0.07480 -0.09460 0.15240  194 MET A CG    
1439 S  SD    . MET A 198 ? 0.80140 1.05900 0.90580 -0.07490 -0.09980 0.15860  194 MET A SD    
1440 C  CE    . MET A 198 ? 0.77770 1.02350 0.85700 -0.08350 -0.10030 0.14860  194 MET A CE    
1441 N  N     . ASP A 199 ? 0.34380 0.57090 0.44860 -0.06450 -0.07400 0.13100  195 ASP A N     
1442 C  CA    . ASP A 199 ? 0.33780 0.55410 0.42880 -0.06980 -0.07170 0.12190  195 ASP A CA    
1443 C  C     . ASP A 199 ? 0.36370 0.58370 0.46190 -0.07080 -0.06870 0.12080  195 ASP A C     
1444 O  O     . ASP A 199 ? 0.38590 0.60370 0.47690 -0.07840 -0.07000 0.11660  195 ASP A O     
1445 C  CB    . ASP A 199 ? 0.36190 0.56160 0.44280 -0.06460 -0.06600 0.11480  195 ASP A CB    
1446 C  CG    . ASP A 199 ? 0.50050 0.69500 0.57000 -0.06680 -0.06920 0.11410  195 ASP A CG    
1447 O  OD1   . ASP A 199 ? 0.50950 0.71130 0.57470 -0.07410 -0.07550 0.11690  195 ASP A OD1   
1448 O  OD2   . ASP A 199 ? 0.55340 0.73700 0.61810 -0.06130 -0.06540 0.11080  195 ASP A OD2   
1449 N  N     . VAL A 200 ? 0.32560 0.55120 0.43810 -0.06320 -0.06460 0.12450  196 VAL A N     
1450 C  CA    . VAL A 200 ? 0.30460 0.53630 0.42540 -0.06410 -0.06190 0.12490  196 VAL A CA    
1451 C  C     . VAL A 200 ? 0.28700 0.53260 0.41270 -0.07310 -0.06870 0.13000  196 VAL A C     
1452 O  O     . VAL A 200 ? 0.39570 0.64110 0.51830 -0.07990 -0.06920 0.12720  196 VAL A O     
1453 C  CB    . VAL A 200 ? 0.30150 0.53890 0.43760 -0.05400 -0.05650 0.12870  196 VAL A CB    
1454 C  CG1   . VAL A 200 ? 0.38730 0.63410 0.53340 -0.05530 -0.05390 0.13050  196 VAL A CG1   
1455 C  CG2   . VAL A 200 ? 0.31050 0.53330 0.44050 -0.04580 -0.04970 0.12260  196 VAL A CG2   
1456 N  N     . VAL A 201 ? 0.33130 0.58930 0.46530 -0.07350 -0.07440 0.13790  197 VAL A N     
1457 C  CA    . VAL A 201 ? 0.35000 0.62280 0.48980 -0.08220 -0.08150 0.14350  197 VAL A CA    
1458 C  C     . VAL A 201 ? 0.36370 0.63000 0.48680 -0.09310 -0.08610 0.13770  197 VAL A C     
1459 O  O     . VAL A 201 ? 0.36720 0.63930 0.49110 -0.10130 -0.08940 0.13760  197 VAL A O     
1460 C  CB    . VAL A 201 ? 0.39020 0.67690 0.54110 -0.08010 -0.08710 0.15350  197 VAL A CB    
1461 C  CG1   . VAL A 201 ? 0.37010 0.67170 0.52420 -0.09040 -0.09570 0.15890  197 VAL A CG1   
1462 C  CG2   . VAL A 201 ? 0.34350 0.63760 0.51300 -0.06960 -0.08230 0.15910  197 VAL A CG2   
1463 N  N     . ARG A 202 ? 0.37560 0.62960 0.48370 -0.09320 -0.08620 0.13240  198 ARG A N     
1464 C  CA    . ARG A 202 ? 0.42420 0.67090 0.51550 -0.10290 -0.08980 0.12590  198 ARG A CA    
1465 C  C     . ARG A 202 ? 0.38330 0.61960 0.46880 -0.10590 -0.08550 0.11790  198 ARG A C     
1466 O  O     . ARG A 202 ? 0.42420 0.66140 0.50470 -0.11530 -0.08930 0.11530  198 ARG A O     
1467 C  CB    . ARG A 202 ? 0.40770 0.64350 0.48520 -0.10110 -0.08940 0.12200  198 ARG A CB    
1468 C  CG    . ARG A 202 ? 0.49780 0.72770 0.55800 -0.11070 -0.09340 0.11570  198 ARG A CG    
1469 C  CD    . ARG A 202 ? 0.59780 0.84220 0.66010 -0.12040 -0.10190 0.12050  198 ARG A CD    
1470 N  NE    . ARG A 202 ? 0.68760 0.92580 0.73320 -0.13020 -0.10530 0.11300  198 ARG A NE    
1471 C  CZ    . ARG A 202 ? 0.80240 1.04770 0.84680 -0.14030 -0.11110 0.11270  198 ARG A CZ    
1472 N  NH1   . ARG A 202 ? 0.80520 1.06510 0.86480 -0.14220 -0.11450 0.12010  198 ARG A NH1   
1473 N  NH2   . ARG A 202 ? 0.81020 1.04810 0.83830 -0.14860 -0.11350 0.10470  198 ARG A NH2   
1474 N  N     . VAL A 203 ? 0.34570 0.57220 0.43220 -0.09820 -0.07780 0.11430  199 VAL A N     
1475 C  CA    . VAL A 203 ? 0.33360 0.55030 0.41510 -0.10080 -0.07370 0.10770  199 VAL A CA    
1476 C  C     . VAL A 203 ? 0.39520 0.62370 0.48880 -0.10510 -0.07510 0.11200  199 VAL A C     
1477 O  O     . VAL A 203 ? 0.40680 0.63230 0.49570 -0.11330 -0.07690 0.10840  199 VAL A O     
1478 C  CB    . VAL A 203 ? 0.34260 0.54770 0.42290 -0.09140 -0.06550 0.10370  199 VAL A CB    
1479 C  CG1   . VAL A 203 ? 0.30780 0.50400 0.38420 -0.09410 -0.06150 0.09800  199 VAL A CG1   
1480 C  CG2   . VAL A 203 ? 0.34280 0.53610 0.41110 -0.08790 -0.06430 0.09920  199 VAL A CG2   
1481 N  N     . ALA A 204 ? 0.31990 0.56210 0.42970 -0.10000 -0.07450 0.12000  200 ALA A N     
1482 C  CA    . ALA A 204 ? 0.37590 0.63130 0.49890 -0.10380 -0.07570 0.12520  200 ALA A CA    
1483 C  C     . ALA A 204 ? 0.39580 0.65880 0.51660 -0.11570 -0.08430 0.12670  200 ALA A C     
1484 O  O     . ALA A 204 ? 0.37520 0.64060 0.49830 -0.12280 -0.08550 0.12600  200 ALA A O     
1485 C  CB    . ALA A 204 ? 0.32470 0.59490 0.46590 -0.09610 -0.07410 0.13390  200 ALA A CB    
1486 N  N     . GLU A 205 ? 0.34920 0.61650 0.46580 -0.11810 -0.09040 0.12890  201 GLU A N     
1487 C  CA    . GLU A 205 ? 0.45510 0.72970 0.56800 -0.12980 -0.09900 0.12990  201 GLU A CA    
1488 C  C     . GLU A 205 ? 0.37790 0.63740 0.47390 -0.13770 -0.09940 0.11970  201 GLU A C     
1489 O  O     . GLU A 205 ? 0.36700 0.62970 0.46300 -0.14730 -0.10350 0.11870  201 GLU A O     
1490 C  CB    . GLU A 205 ? 0.54380 0.82620 0.65490 -0.13010 -0.10520 0.13480  201 GLU A CB    
1491 C  CG    . GLU A 205 ? 0.79330 1.08240 0.89740 -0.14200 -0.11440 0.13500  201 GLU A CG    
1492 C  CD    . GLU A 205 ? 0.96460 1.26130 1.06630 -0.14160 -0.12000 0.14040  201 GLU A CD    
1493 O  OE1   . GLU A 205 ? 0.99350 1.29280 1.10320 -0.13180 -0.11710 0.14570  201 GLU A OE1   
1494 O  OE2   . GLU A 205 ? 1.02620 1.32610 1.11790 -0.15100 -0.12720 0.13930  201 GLU A OE2   
1495 N  N     . LEU A 206 ? 0.39660 0.63960 0.47900 -0.13380 -0.09500 0.11210  202 LEU A N     
1496 C  CA    . LEU A 206 ? 0.36380 0.59180 0.43110 -0.14030 -0.09450 0.10230  202 LEU A CA    
1497 C  C     . LEU A 206 ? 0.39440 0.61840 0.46710 -0.14230 -0.09090 0.10020  202 LEU A C     
1498 O  O     . LEU A 206 ? 0.39120 0.61030 0.45810 -0.15130 -0.09360 0.09540  202 LEU A O     
1499 C  CB    . LEU A 206 ? 0.35340 0.56520 0.40740 -0.13440 -0.08950 0.09530  202 LEU A CB    
1500 C  CG    . LEU A 206 ? 0.42930 0.64060 0.47270 -0.13470 -0.09290 0.09460  202 LEU A CG    
1501 C  CD1   . LEU A 206 ? 0.34970 0.54710 0.38520 -0.12640 -0.08650 0.08990  202 LEU A CD1   
1502 C  CD2   . LEU A 206 ? 0.40510 0.61400 0.43530 -0.14580 -0.09870 0.08900  202 LEU A CD2   
1503 N  N     . ILE A 207 ? 0.43080 0.65690 0.51450 -0.13410 -0.08480 0.10380  203 ILE A N     
1504 C  CA    . ILE A 207 ? 0.44810 0.67180 0.53750 -0.13590 -0.08110 0.10310  203 ILE A CA    
1505 C  C     . ILE A 207 ? 0.38290 0.62180 0.48380 -0.14430 -0.08670 0.10900  203 ILE A C     
1506 O  O     . ILE A 207 ? 0.36620 0.60120 0.46560 -0.15230 -0.08810 0.10610  203 ILE A O     
1507 C  CB    . ILE A 207 ? 0.43250 0.65600 0.53020 -0.12490 -0.07300 0.10560  203 ILE A CB    
1508 C  CG1   . ILE A 207 ? 0.38790 0.59430 0.47330 -0.11810 -0.06750 0.09860  203 ILE A CG1   
1509 C  CG2   . ILE A 207 ? 0.41180 0.63800 0.51850 -0.12700 -0.06990 0.10740  203 ILE A CG2   
1510 C  CD1   . ILE A 207 ? 0.44340 0.65000 0.53580 -0.10710 -0.06020 0.10070  203 ILE A CD1   
1511 N  N     . PHE A 208 ? 0.37210 0.62850 0.48490 -0.14280 -0.09030 0.11760  204 PHE A N     
1512 C  CA    . PHE A 208 ? 0.50010 0.77280 0.62570 -0.15030 -0.09570 0.12430  204 PHE A CA    
1513 C  C     . PHE A 208 ? 0.46840 0.73830 0.58470 -0.16340 -0.10320 0.11990  204 PHE A C     
1514 O  O     . PHE A 208 ? 0.50190 0.77920 0.62580 -0.17150 -0.10650 0.12240  204 PHE A O     
1515 C  CB    . PHE A 208 ? 0.56940 0.86120 0.70840 -0.14670 -0.09920 0.13410  204 PHE A CB    
1516 C  CG    . PHE A 208 ? 0.69430 0.99220 0.84690 -0.13480 -0.09210 0.13950  204 PHE A CG    
1517 C  CD1   . PHE A 208 ? 0.70530 0.99620 0.86010 -0.13000 -0.08400 0.13700  204 PHE A CD1   
1518 C  CD2   . PHE A 208 ? 0.68890 0.99970 0.85220 -0.12830 -0.09350 0.14710  204 PHE A CD2   
1519 C  CE1   . PHE A 208 ? 0.70120 0.99780 0.86750 -0.11930 -0.07720 0.14110  204 PHE A CE1   
1520 C  CE2   . PHE A 208 ? 0.64850 0.96420 0.82420 -0.11710 -0.08660 0.15120  204 PHE A CE2   
1521 C  CZ    . PHE A 208 ? 0.62720 0.93590 0.80400 -0.11270 -0.07840 0.14780  204 PHE A CZ    
1522 N  N     . HIS A 209 ? 0.44170 0.70170 0.54180 -0.16600 -0.10600 0.11350  205 HIS A N     
1523 C  CA    . HIS A 209 ? 0.47890 0.73650 0.56880 -0.17820 -0.11330 0.10860  205 HIS A CA    
1524 C  C     . HIS A 209 ? 0.52540 0.76240 0.60090 -0.18190 -0.11030 0.09740  205 HIS A C     
1525 O  O     . HIS A 209 ? 0.53670 0.76980 0.60340 -0.19230 -0.11570 0.09210  205 HIS A O     
1526 C  CB    . HIS A 209 ? 0.48410 0.74680 0.56550 -0.17950 -0.11920 0.10940  205 HIS A CB    
1527 C  CG    . HIS A 209 ? 0.60180 0.88620 0.69740 -0.17940 -0.12470 0.12070  205 HIS A CG    
1528 N  ND1   . HIS A 209 ? 0.64660 0.94620 0.75530 -0.18650 -0.13000 0.12700  205 HIS A ND1   
1529 C  CD2   . HIS A 209 ? 0.62960 0.92320 0.72900 -0.17290 -0.12600 0.12720  205 HIS A CD2   
1530 C  CE1   . HIS A 209 ? 0.63940 0.95710 0.75950 -0.18430 -0.13420 0.13690  205 HIS A CE1   
1531 N  NE2   . HIS A 209 ? 0.60970 0.92380 0.72440 -0.17600 -0.13200 0.13730  205 HIS A NE2   
1532 N  N     . ALA A 210 ? 0.44360 0.66760 0.51690 -0.17380 -0.10200 0.09380  206 ALA A N     
1533 C  CA    . ALA A 210 ? 0.45600 0.65990 0.51580 -0.17600 -0.09880 0.08340  206 ALA A CA    
1534 C  C     . ALA A 210 ? 0.48610 0.68670 0.55050 -0.18410 -0.09960 0.08190  206 ALA A C     
1535 O  O     . ALA A 210 ? 0.47760 0.68750 0.55640 -0.18340 -0.09810 0.08870  206 ALA A O     
1536 C  CB    . ALA A 210 ? 0.38410 0.57620 0.44110 -0.16480 -0.09010 0.08090  206 ALA A CB    
1537 N  N     . LYS A 211 ? 0.50510 0.69230 0.55740 -0.19180 -0.10180 0.07300  207 LYS A N     
1538 C  CA    . LYS A 211 ? 0.49830 0.67990 0.55430 -0.19980 -0.10250 0.07090  207 LYS A CA    
1539 C  C     . LYS A 211 ? 0.51900 0.68280 0.57160 -0.19510 -0.09500 0.06570  207 LYS A C     
1540 O  O     . LYS A 211 ? 0.44820 0.61000 0.50880 -0.19860 -0.09370 0.06740  207 LYS A O     
1541 C  CB    . LYS A 211 ? 0.50530 0.68270 0.55160 -0.21220 -0.10990 0.06400  207 LYS A CB    
1542 C  CG    . LYS A 211 ? 0.53700 0.72960 0.58170 -0.21730 -0.11790 0.06710  207 LYS A CG    
1543 C  CD    . LYS A 211 ? 0.63230 0.84670 0.69420 -0.21520 -0.12020 0.07960  207 LYS A CD    
1544 C  CE    . LYS A 211 ? 0.67350 0.90290 0.73340 -0.21970 -0.12840 0.08310  207 LYS A CE    
1545 N  NZ    . LYS A 211 ? 0.72940 0.98070 0.80770 -0.22060 -0.13220 0.09510  207 LYS A NZ    
1546 N  N     . ARG A 212 ? 0.49010 0.64160 0.53190 -0.18750 -0.09010 0.06010  208 ARG A N     
1547 C  CA    . ARG A 212 ? 0.47710 0.61240 0.51610 -0.18230 -0.08300 0.05590  208 ARG A CA    
1548 C  C     . ARG A 212 ? 0.42590 0.55800 0.46070 -0.17040 -0.07710 0.05580  208 ARG A C     
1549 O  O     . ARG A 212 ? 0.38700 0.50550 0.40970 -0.16760 -0.07460 0.04840  208 ARG A O     
1550 C  CB    . ARG A 212 ? 0.54400 0.66160 0.57130 -0.18910 -0.08410 0.04550  208 ARG A CB    
1551 C  CG    . ARG A 212 ? 0.64900 0.75230 0.67830 -0.18780 -0.07880 0.04310  208 ARG A CG    
1552 C  CD    . ARG A 212 ? 0.80590 0.90930 0.84280 -0.19820 -0.08260 0.04420  208 ARG A CD    
1553 N  NE    . ARG A 212 ? 0.88010 0.97370 0.92260 -0.19620 -0.07750 0.04540  208 ARG A NE    
1554 C  CZ    . ARG A 212 ? 0.86460 0.96640 0.92060 -0.19860 -0.07710 0.05320  208 ARG A CZ    
1555 N  NH1   . ARG A 212 ? 0.84100 0.96100 0.90680 -0.20290 -0.08160 0.06040  208 ARG A NH1   
1556 N  NH2   . ARG A 212 ? 0.86960 0.96200 0.92950 -0.19680 -0.07240 0.05430  208 ARG A NH2   
1557 N  N     . PRO A 213 ? 0.37480 0.51890 0.41990 -0.16310 -0.07450 0.06380  209 PRO A N     
1558 C  CA    . PRO A 213 ? 0.37190 0.51290 0.41380 -0.15190 -0.06910 0.06380  209 PRO A CA    
1559 C  C     . PRO A 213 ? 0.37630 0.50390 0.41650 -0.14650 -0.06210 0.06090  209 PRO A C     
1560 O  O     . PRO A 213 ? 0.47070 0.59410 0.51520 -0.15020 -0.06090 0.06110  209 PRO A O     
1561 C  CB    . PRO A 213 ? 0.39320 0.55220 0.44850 -0.14700 -0.06890 0.07350  209 PRO A CB    
1562 C  CG    . PRO A 213 ? 0.40330 0.57090 0.47070 -0.15320 -0.07050 0.07860  209 PRO A CG    
1563 C  CD    . PRO A 213 ? 0.42220 0.58330 0.48300 -0.16480 -0.07620 0.07310  209 PRO A CD    
1564 N  N     . ALA A 214 ? 0.39360 0.51430 0.42740 -0.13790 -0.05770 0.05830  210 ALA A N     
1565 C  CA    . ALA A 214 ? 0.36150 0.47100 0.39380 -0.13170 -0.05120 0.05630  210 ALA A CA    
1566 C  C     . ALA A 214 ? 0.36360 0.47420 0.39450 -0.12130 -0.04720 0.05750  210 ALA A C     
1567 O  O     . ALA A 214 ? 0.41400 0.52860 0.44120 -0.11960 -0.04950 0.05730  210 ALA A O     
1568 C  CB    . ALA A 214 ? 0.33260 0.42410 0.35390 -0.13460 -0.05030 0.04770  210 ALA A CB    
1569 N  N     . ILE A 215 ? 0.36510 0.47250 0.39910 -0.11470 -0.04150 0.05890  211 ILE A N     
1570 C  CA    . ILE A 215 ? 0.30260 0.40840 0.33450 -0.10490 -0.03720 0.05900  211 ILE A CA    
1571 C  C     . ILE A 215 ? 0.38460 0.47430 0.40790 -0.10200 -0.03320 0.05310  211 ILE A C     
1572 O  O     . ILE A 215 ? 0.34980 0.43350 0.37430 -0.10430 -0.03130 0.05260  211 ILE A O     
1573 C  CB    . ILE A 215 ? 0.33050 0.44730 0.37340 -0.09900 -0.03370 0.06570  211 ILE A CB    
1574 C  CG1   . ILE A 215 ? 0.31990 0.45340 0.37230 -0.10050 -0.03740 0.07190  211 ILE A CG1   
1575 C  CG2   . ILE A 215 ? 0.25810 0.37010 0.29780 -0.08900 -0.02860 0.06440  211 ILE A CG2   
1576 C  CD1   . ILE A 215 ? 0.30780 0.45320 0.37270 -0.09730 -0.03430 0.07850  211 ILE A CD1   
1577 N  N     . LEU A 216 ? 0.37820 0.46150 0.39360 -0.09720 -0.03210 0.04920  212 LEU A N     
1578 C  CA    . LEU A 216 ? 0.33280 0.40280 0.34130 -0.09270 -0.02780 0.04450  212 LEU A CA    
1579 C  C     . LEU A 216 ? 0.29730 0.37040 0.30770 -0.08350 -0.02420 0.04690  212 LEU A C     
1580 O  O     . LEU A 216 ? 0.28360 0.36020 0.29240 -0.08040 -0.02530 0.04710  212 LEU A O     
1581 C  CB    . LEU A 216 ? 0.27550 0.33510 0.27320 -0.09500 -0.02930 0.03750  212 LEU A CB    
1582 C  CG    . LEU A 216 ? 0.42770 0.47400 0.41910 -0.09030 -0.02510 0.03290  212 LEU A CG    
1583 C  CD1   . LEU A 216 ? 0.38210 0.42150 0.37650 -0.09130 -0.02250 0.03320  212 LEU A CD1   
1584 C  CD2   . LEU A 216 ? 0.38500 0.42230 0.36640 -0.09240 -0.02620 0.02600  212 LEU A CD2   
1585 N  N     . ALA A 217 ? 0.27360 0.34580 0.28770 -0.07950 -0.02000 0.04900  213 ALA A N     
1586 C  CA    . ALA A 217 ? 0.29130 0.36680 0.30760 -0.07120 -0.01630 0.05100  213 ALA A CA    
1587 C  C     . ALA A 217 ? 0.26150 0.32470 0.27040 -0.06680 -0.01300 0.04670  213 ALA A C     
1588 O  O     . ALA A 217 ? 0.26210 0.31760 0.26890 -0.06860 -0.01150 0.04520  213 ALA A O     
1589 C  CB    . ALA A 217 ? 0.36220 0.44720 0.38770 -0.06970 -0.01380 0.05660  213 ALA A CB    
1590 N  N     . GLY A 218 ? 0.27770 0.33940 0.28330 -0.06100 -0.01200 0.04510  214 GLY A N     
1591 C  CA    . GLY A 218 ? 0.30540 0.35660 0.30460 -0.05670 -0.00920 0.04130  214 GLY A CA    
1592 C  C     . GLY A 218 ? 0.40890 0.46260 0.41050 -0.04960 -0.00550 0.04310  214 GLY A C     
1593 O  O     . GLY A 218 ? 0.35320 0.41630 0.36150 -0.04770 -0.00430 0.04710  214 GLY A O     
1594 N  N     . HIS A 219 ? 0.32800 0.37300 0.32370 -0.04560 -0.00360 0.03970  215 HIS A N     
1595 C  CA    . HIS A 219 ? 0.30780 0.35320 0.30380 -0.03900 -0.00020 0.04020  215 HIS A CA    
1596 C  C     . HIS A 219 ? 0.28250 0.33600 0.28310 -0.03470 -0.00010 0.04210  215 HIS A C     
1597 O  O     . HIS A 219 ? 0.32170 0.37800 0.32450 -0.02970 0.00280  0.04300  215 HIS A O     
1598 C  CB    . HIS A 219 ? 0.33310 0.36770 0.32190 -0.03640 0.00070  0.03600  215 HIS A CB    
1599 C  CG    . HIS A 219 ? 0.33910 0.37320 0.32710 -0.03020 0.00350  0.03560  215 HIS A CG    
1600 N  ND1   . HIS A 219 ? 0.31810 0.35470 0.30760 -0.02820 0.00640  0.03760  215 HIS A ND1   
1601 C  CD2   . HIS A 219 ? 0.34070 0.37190 0.32610 -0.02570 0.00380  0.03350  215 HIS A CD2   
1602 C  CE1   . HIS A 219 ? 0.33500 0.37040 0.32240 -0.02280 0.00830  0.03620  215 HIS A CE1   
1603 N  NE2   . HIS A 219 ? 0.36420 0.39590 0.34940 -0.02120 0.00670  0.03360  215 HIS A NE2   
1604 N  N     . GLY A 220 ? 0.26720 0.32420 0.26930 -0.03630 -0.00330 0.04270  216 GLY A N     
1605 C  CA    . GLY A 220 ? 0.27270 0.33770 0.28080 -0.03220 -0.00340 0.04540  216 GLY A CA    
1606 C  C     . GLY A 220 ? 0.33980 0.41510 0.35630 -0.03100 -0.00140 0.04950  216 GLY A C     
1607 O  O     . GLY A 220 ? 0.25780 0.33830 0.27930 -0.02560 0.00050  0.05090  216 GLY A O     
1608 N  N     . ILE A 221 ? 0.29430 0.37280 0.31300 -0.03600 -0.00170 0.05150  217 ILE A N     
1609 C  CA    . ILE A 221 ? 0.30830 0.39720 0.33510 -0.03510 0.00060  0.05570  217 ILE A CA    
1610 C  C     . ILE A 221 ? 0.35000 0.43790 0.37580 -0.02860 0.00560  0.05460  217 ILE A C     
1611 O  O     . ILE A 221 ? 0.34780 0.44390 0.37990 -0.02420 0.00810  0.05670  217 ILE A O     
1612 C  CB    . ILE A 221 ? 0.25900 0.35010 0.28770 -0.04190 -0.00020 0.05790  217 ILE A CB    
1613 C  CG1   . ILE A 221 ? 0.28310 0.37820 0.31440 -0.04830 -0.00530 0.05940  217 ILE A CG1   
1614 C  CG2   . ILE A 221 ? 0.27750 0.37800 0.31320 -0.04030 0.00350  0.06200  217 ILE A CG2   
1615 C  CD1   . ILE A 221 ? 0.25510 0.36320 0.29570 -0.04700 -0.00680 0.06380  217 ILE A CD1   
1616 N  N     . GLU A 222 ? 0.38200 0.45990 0.39990 -0.02800 0.00700  0.05120  218 GLU A N     
1617 C  CA    . GLU A 222 ? 0.33260 0.40920 0.34810 -0.02230 0.01130  0.04990  218 GLU A CA    
1618 C  C     . GLU A 222 ? 0.34590 0.42140 0.36130 -0.01610 0.01190  0.04750  218 GLU A C     
1619 O  O     . GLU A 222 ? 0.27240 0.35290 0.29090 -0.01110 0.01520  0.04770  218 GLU A O     
1620 C  CB    . GLU A 222 ? 0.32440 0.39070 0.33170 -0.02330 0.01200  0.04730  218 GLU A CB    
1621 C  CG    . GLU A 222 ? 0.44680 0.51140 0.45040 -0.01760 0.01570  0.04540  218 GLU A CG    
1622 C  CD    . GLU A 222 ? 0.53850 0.59380 0.53450 -0.01840 0.01600  0.04350  218 GLU A CD    
1623 O  OE1   . GLU A 222 ? 0.51620 0.56420 0.50700 -0.01550 0.01560  0.03990  218 GLU A OE1   
1624 O  OE2   . GLU A 222 ? 0.54660 0.60190 0.54240 -0.02200 0.01660  0.04600  218 GLU A OE2   
1625 N  N     . CYS A 223 ? 0.33260 0.40180 0.34480 -0.01650 0.00880  0.04530  219 CYS A N     
1626 C  CA    . CYS A 223 ? 0.33830 0.40570 0.35090 -0.01100 0.00910  0.04330  219 CYS A CA    
1627 C  C     . CYS A 223 ? 0.34220 0.41990 0.36440 -0.00800 0.00970  0.04650  219 CYS A C     
1628 O  O     . CYS A 223 ? 0.33690 0.41530 0.36140 -0.00210 0.01210  0.04530  219 CYS A O     
1629 C  CB    . CYS A 223 ? 0.34840 0.40930 0.35730 -0.01290 0.00530  0.04170  219 CYS A CB    
1630 S  SG    . CYS A 223 ? 0.40900 0.45810 0.40790 -0.01610 0.00450  0.03780  219 CYS A SG    
1631 N  N     . ALA A 224 ? 0.25860 0.34450 0.28690 -0.01200 0.00770  0.05060  220 ALA A N     
1632 C  CA    . ALA A 224 ? 0.28880 0.38570 0.32770 -0.00940 0.00800  0.05450  220 ALA A CA    
1633 C  C     . ALA A 224 ? 0.32600 0.43180 0.37040 -0.00750 0.01240  0.05650  220 ALA A C     
1634 O  O     . ALA A 224 ? 0.40090 0.51640 0.45490 -0.00440 0.01360  0.05960  220 ALA A O     
1635 C  CB    . ALA A 224 ? 0.26490 0.36790 0.30840 -0.01490 0.00320  0.05840  220 ALA A CB    
1636 N  N     . LYS A 225 ? 0.31290 0.41580 0.35180 -0.00900 0.01490  0.05520  221 LYS A N     
1637 C  CA    . LYS A 225 ? 0.36180 0.47370 0.40520 -0.00810 0.01920  0.05780  221 LYS A CA    
1638 C  C     . LYS A 225 ? 0.35380 0.47800 0.40770 -0.01160 0.01760  0.06340  221 LYS A C     
1639 O  O     . LYS A 225 ? 0.39920 0.53430 0.46190 -0.00830 0.02060  0.06620  221 LYS A O     
1640 C  CB    . LYS A 225 ? 0.32080 0.43500 0.36570 -0.00020 0.02400  0.05560  221 LYS A CB    
1641 C  CG    . LYS A 225 ? 0.37020 0.47220 0.40490 0.00300  0.02480  0.04980  221 LYS A CG    
1642 C  CD    . LYS A 225 ? 0.46350 0.56670 0.50030 0.01070  0.02870  0.04690  221 LYS A CD    
1643 C  CE    . LYS A 225 ? 0.57030 0.66290 0.59680 0.01340  0.02990  0.04120  221 LYS A CE    
1644 N  NZ    . LYS A 225 ? 0.59360 0.67640 0.61730 0.01440  0.02630  0.03830  221 LYS A NZ    
1645 N  N     . ALA A 226 ? 0.35980 0.48230 0.41280 -0.01850 0.01290  0.06490  222 ALA A N     
1646 C  CA    . ALA A 226 ? 0.34150 0.47490 0.40390 -0.02280 0.00990  0.07000  222 ALA A CA    
1647 C  C     . ALA A 226 ? 0.33430 0.47220 0.39860 -0.02920 0.01000  0.07320  222 ALA A C     
1648 O  O     . ALA A 226 ? 0.30110 0.44570 0.37120 -0.03480 0.00640  0.07680  222 ALA A O     
1649 C  CB    . ALA A 226 ? 0.26020 0.38970 0.32060 -0.02650 0.00390  0.06960  222 ALA A CB    
1650 N  N     . TRP A 227 ? 0.31650 0.45130 0.37630 -0.02870 0.01400  0.07230  223 TRP A N     
1651 C  CA    . TRP A 227 ? 0.27410 0.41130 0.33520 -0.03540 0.01370  0.07540  223 TRP A CA    
1652 C  C     . TRP A 227 ? 0.31650 0.46930 0.39000 -0.03750 0.01410  0.08160  223 TRP A C     
1653 O  O     . TRP A 227 ? 0.33850 0.49440 0.41570 -0.04490 0.01050  0.08460  223 TRP A O     
1654 C  CB    . TRP A 227 ? 0.24910 0.38220 0.30440 -0.03360 0.01830  0.07450  223 TRP A CB    
1655 C  CG    . TRP A 227 ? 0.24240 0.36120 0.28630 -0.03150 0.01820  0.06910  223 TRP A CG    
1656 C  CD1   . TRP A 227 ? 0.35380 0.46110 0.39080 -0.03610 0.01530  0.06690  223 TRP A CD1   
1657 C  CD2   . TRP A 227 ? 0.32030 0.43490 0.35900 -0.02430 0.02130  0.06520  223 TRP A CD2   
1658 N  NE1   . TRP A 227 ? 0.35030 0.44740 0.37860 -0.03200 0.01640  0.06230  223 TRP A NE1   
1659 C  CE2   . TRP A 227 ? 0.31130 0.41250 0.34010 -0.02510 0.01980  0.06120  223 TRP A CE2   
1660 C  CE3   . TRP A 227 ? 0.33920 0.46000 0.38080 -0.01730 0.02520  0.06440  223 TRP A CE3   
1661 C  CZ2   . TRP A 227 ? 0.40790 0.50230 0.42980 -0.01950 0.02170  0.05690  223 TRP A CZ2   
1662 C  CZ3   . TRP A 227 ? 0.35350 0.46660 0.38760 -0.01180 0.02710  0.05950  223 TRP A CZ3   
1663 C  CH2   . TRP A 227 ? 0.34600 0.44630 0.37040 -0.01320 0.02510  0.05600  223 TRP A CH2   
1664 N  N     . GLU A 228 ? 0.31120 0.47420 0.39150 -0.03120 0.01840  0.08330  224 GLU A N     
1665 C  CA    . GLU A 228 ? 0.31990 0.49870 0.41280 -0.03310 0.01940  0.08960  224 GLU A CA    
1666 C  C     . GLU A 228 ? 0.29140 0.47680 0.39240 -0.03610 0.01380  0.09240  224 GLU A C     
1667 O  O     . GLU A 228 ? 0.30790 0.50260 0.41680 -0.04220 0.01150  0.09740  224 GLU A O     
1668 C  CB    . GLU A 228 ? 0.41570 0.60430 0.51430 -0.02520 0.02610  0.09060  224 GLU A CB    
1669 C  CG    . GLU A 228 ? 0.74250 0.94810 0.85370 -0.02750 0.02820  0.09740  224 GLU A CG    
1670 C  CD    . GLU A 228 ? 0.95130 1.16950 1.07220 -0.01940 0.03370  0.09890  224 GLU A CD    
1671 O  OE1   . GLU A 228 ? 1.07880 1.31240 1.21200 -0.02080 0.03510  0.10480  224 GLU A OE1   
1672 O  OE2   . GLU A 228 ? 1.03700 1.24980 1.15350 -0.01180 0.03660  0.09400  224 GLU A OE2   
1673 N  N     . GLU A 229 ? 0.28380 0.46410 0.38250 -0.03260 0.01130  0.08950  225 GLU A N     
1674 C  CA    . GLU A 229 ? 0.30260 0.48870 0.40780 -0.03580 0.00540  0.09250  225 GLU A CA    
1675 C  C     . GLU A 229 ? 0.28390 0.46420 0.38350 -0.04550 -0.00040 0.09200  225 GLU A C     
1676 O  O     . GLU A 229 ? 0.24350 0.43250 0.35020 -0.05120 -0.00490 0.09610  225 GLU A O     
1677 C  CB    . GLU A 229 ? 0.34920 0.53060 0.45260 -0.03000 0.00410  0.08990  225 GLU A CB    
1678 C  CG    . GLU A 229 ? 0.47550 0.66340 0.58650 -0.02060 0.00910  0.09050  225 GLU A CG    
1679 C  CD    . GLU A 229 ? 0.61610 0.79460 0.71860 -0.01460 0.01480  0.08500  225 GLU A CD    
1680 O  OE1   . GLU A 229 ? 0.63640 0.80480 0.72810 -0.01780 0.01510  0.08160  225 GLU A OE1   
1681 O  OE2   . GLU A 229 ? 0.71280 0.89400 0.81960 -0.00660 0.01900  0.08400  225 GLU A OE2   
1682 N  N     . LEU A 230 ? 0.29920 0.46490 0.38650 -0.04730 -0.00050 0.08690  226 LEU A N     
1683 C  CA    . LEU A 230 ? 0.32200 0.48120 0.40410 -0.05620 -0.00540 0.08570  226 LEU A CA    
1684 C  C     . LEU A 230 ? 0.36670 0.53350 0.45550 -0.06270 -0.00540 0.09020  226 LEU A C     
1685 O  O     . LEU A 230 ? 0.30580 0.47590 0.39750 -0.07040 -0.01050 0.09210  226 LEU A O     
1686 C  CB    . LEU A 230 ? 0.24530 0.38760 0.31410 -0.05600 -0.00450 0.07940  226 LEU A CB    
1687 C  CG    . LEU A 230 ? 0.32650 0.46040 0.38960 -0.06470 -0.00840 0.07730  226 LEU A CG    
1688 C  CD1   . LEU A 230 ? 0.36580 0.50160 0.42880 -0.06970 -0.01460 0.07700  226 LEU A CD1   
1689 C  CD2   . LEU A 230 ? 0.23670 0.35470 0.28820 -0.06360 -0.00690 0.07160  226 LEU A CD2   
1690 N  N     . LEU A 231 ? 0.31160 0.48150 0.40270 -0.06010 0.00010  0.09200  227 LEU A N     
1691 C  CA    . LEU A 231 ? 0.27140 0.44870 0.36920 -0.06630 0.00040  0.09690  227 LEU A CA    
1692 C  C     . LEU A 231 ? 0.33070 0.52510 0.44220 -0.06860 -0.00180 0.10310  227 LEU A C     
1693 O  O     . LEU A 231 ? 0.32560 0.52430 0.44190 -0.07700 -0.00590 0.10610  227 LEU A O     
1694 C  CB    . LEU A 231 ? 0.31010 0.48870 0.40750 -0.06210 0.00730  0.09810  227 LEU A CB    
1695 C  CG    . LEU A 231 ? 0.41900 0.60690 0.52430 -0.06760 0.00880  0.10420  227 LEU A CG    
1696 C  CD1   . LEU A 231 ? 0.41250 0.59080 0.51390 -0.07700 0.00450  0.10370  227 LEU A CD1   
1697 C  CD2   . LEU A 231 ? 0.43690 0.62770 0.54110 -0.06230 0.01610  0.10560  227 LEU A CD2   
1698 N  N     . ASP A 232 ? 0.25270 0.45670 0.37110 -0.06120 0.00080  0.10490  228 ASP A N     
1699 C  CA    . ASP A 232 ? 0.28220 0.50340 0.41490 -0.06240 -0.00120 0.11120  228 ASP A CA    
1700 C  C     . ASP A 232 ? 0.34610 0.56710 0.47890 -0.06850 -0.00920 0.11130  228 ASP A C     
1701 O  O     . ASP A 232 ? 0.32890 0.56100 0.47090 -0.07500 -0.01320 0.11640  228 ASP A O     
1702 C  CB    . ASP A 232 ? 0.40340 0.63300 0.54300 -0.05220 0.00360  0.11220  228 ASP A CB    
1703 C  CG    . ASP A 232 ? 0.70920 0.95800 0.86550 -0.05210 0.00290  0.11940  228 ASP A CG    
1704 O  OD1   . ASP A 232 ? 0.77540 1.03360 0.93910 -0.05900 0.00140  0.12440  228 ASP A OD1   
1705 O  OD2   . ASP A 232 ? 0.79800 1.05250 0.96060 -0.04500 0.00390  0.12020  228 ASP A OD2   
1706 N  N     . PHE A 233 ? 0.31160 0.52040 0.43400 -0.06700 -0.01180 0.10590  229 PHE A N     
1707 C  CA    . PHE A 233 ? 0.28960 0.49810 0.41040 -0.07300 -0.01940 0.10580  229 PHE A CA    
1708 C  C     . PHE A 233 ? 0.32630 0.53060 0.44340 -0.08380 -0.02360 0.10500  229 PHE A C     
1709 O  O     . PHE A 233 ? 0.29200 0.50470 0.41480 -0.09090 -0.02930 0.10840  229 PHE A O     
1710 C  CB    . PHE A 233 ? 0.28670 0.48270 0.39620 -0.06920 -0.02060 0.10010  229 PHE A CB    
1711 C  CG    . PHE A 233 ? 0.31080 0.50480 0.41580 -0.07580 -0.02800 0.09910  229 PHE A CG    
1712 C  CD1   . PHE A 233 ? 0.31110 0.51800 0.42490 -0.07700 -0.03270 0.10430  229 PHE A CD1   
1713 C  CD2   . PHE A 233 ? 0.37420 0.55410 0.46620 -0.08080 -0.03020 0.09310  229 PHE A CD2   
1714 C  CE1   . PHE A 233 ? 0.35150 0.55730 0.46010 -0.08350 -0.03960 0.10350  229 PHE A CE1   
1715 C  CE2   . PHE A 233 ? 0.45130 0.62960 0.53810 -0.08690 -0.03660 0.09160  229 PHE A CE2   
1716 C  CZ    . PHE A 233 ? 0.36660 0.55800 0.46130 -0.08850 -0.04140 0.09680  229 PHE A CZ    
1717 N  N     . ALA A 234 ? 0.34610 0.53730 0.45410 -0.08540 -0.02110 0.10070  230 ALA A N     
1718 C  CA    . ALA A 234 ? 0.38440 0.56960 0.48900 -0.09540 -0.02490 0.09940  230 ALA A CA    
1719 C  C     . ALA A 234 ? 0.36040 0.55900 0.47750 -0.10120 -0.02550 0.10620  230 ALA A C     
1720 O  O     . ALA A 234 ? 0.33660 0.53720 0.45580 -0.11040 -0.03120 0.10710  230 ALA A O     
1721 C  CB    . ALA A 234 ? 0.31580 0.48450 0.40960 -0.09480 -0.02150 0.09410  230 ALA A CB    
1722 N  N     . GLU A 235 ? 0.34110 0.54940 0.46670 -0.09620 -0.01980 0.11080  231 GLU A N     
1723 C  CA    . GLU A 235 ? 0.34110 0.56340 0.47950 -0.10140 -0.01980 0.11790  231 GLU A CA    
1724 C  C     . GLU A 235 ? 0.40110 0.63960 0.55110 -0.10370 -0.02450 0.12310  231 GLU A C     
1725 O  O     . GLU A 235 ? 0.34280 0.58980 0.50080 -0.11220 -0.02870 0.12730  231 GLU A O     
1726 C  CB    . GLU A 235 ? 0.36060 0.58990 0.50450 -0.09490 -0.01180 0.12140  231 GLU A CB    
1727 C  CG    . GLU A 235 ? 0.48580 0.70150 0.62000 -0.09420 -0.00750 0.11810  231 GLU A CG    
1728 C  CD    . GLU A 235 ? 0.53770 0.76150 0.67650 -0.08810 0.00040  0.12180  231 GLU A CD    
1729 O  OE1   . GLU A 235 ? 0.56610 0.78360 0.70070 -0.09000 0.00340  0.12210  231 GLU A OE1   
1730 O  OE2   . GLU A 235 ? 0.56870 0.80530 0.71540 -0.08150 0.00380  0.12450  231 GLU A OE2   
1731 N  N     . LEU A 236 ? 0.40610 0.64940 0.55790 -0.09630 -0.02420 0.12310  232 LEU A N     
1732 C  CA    . LEU A 236 ? 0.28620 0.54520 0.44960 -0.09780 -0.02900 0.12860  232 LEU A CA    
1733 C  C     . LEU A 236 ? 0.33980 0.59570 0.49870 -0.10810 -0.03780 0.12720  232 LEU A C     
1734 O  O     . LEU A 236 ? 0.34130 0.61060 0.51040 -0.11450 -0.04280 0.13260  232 LEU A O     
1735 C  CB    . LEU A 236 ? 0.27730 0.53870 0.44180 -0.08770 -0.02720 0.12830  232 LEU A CB    
1736 C  CG    . LEU A 236 ? 0.33790 0.61400 0.51350 -0.08760 -0.03220 0.13380  232 LEU A CG    
1737 C  CD1   . LEU A 236 ? 0.35240 0.64890 0.54650 -0.08740 -0.03050 0.14230  232 LEU A CD1   
1738 C  CD2   . LEU A 236 ? 0.36480 0.63730 0.53800 -0.07770 -0.03050 0.13180  232 LEU A CD2   
1739 N  N     . THR A 237 ? 0.28150 0.52020 0.42520 -0.11000 -0.03980 0.11970  233 THR A N     
1740 C  CA    . THR A 237 ? 0.33880 0.57360 0.47620 -0.11890 -0.04790 0.11710  233 THR A CA    
1741 C  C     . THR A 237 ? 0.36300 0.58850 0.49510 -0.12890 -0.05020 0.11380  233 THR A C     
1742 O  O     . THR A 237 ? 0.36330 0.58760 0.49200 -0.13760 -0.05710 0.11200  233 THR A O     
1743 C  CB    . THR A 237 ? 0.40260 0.62510 0.52660 -0.11500 -0.04890 0.11070  233 THR A CB    
1744 O  OG1   . THR A 237 ? 0.36010 0.56600 0.47320 -0.11110 -0.04360 0.10440  233 THR A OG1   
1745 C  CG2   . THR A 237 ? 0.33310 0.56470 0.46310 -0.10590 -0.04760 0.11430  233 THR A CG2   
1746 N  N     . GLY A 238 ? 0.38580 0.60400 0.51670 -0.12790 -0.04480 0.11290  234 GLY A N     
1747 C  CA    . GLY A 238 ? 0.33260 0.53880 0.45760 -0.13660 -0.04680 0.10910  234 GLY A CA    
1748 C  C     . GLY A 238 ? 0.38190 0.56910 0.49080 -0.13750 -0.04840 0.10000  234 GLY A C     
1749 O  O     . GLY A 238 ? 0.42070 0.59800 0.52440 -0.14570 -0.05150 0.09600  234 GLY A O     
1750 N  N     . ILE A 239 ? 0.28150 0.46330 0.38260 -0.12950 -0.04620 0.09640  235 ILE A N     
1751 C  CA    . ILE A 239 ? 0.28550 0.45040 0.37170 -0.13020 -0.04750 0.08790  235 ILE A CA    
1752 C  C     . ILE A 239 ? 0.35510 0.50510 0.43480 -0.12690 -0.04190 0.08390  235 ILE A C     
1753 O  O     . ILE A 239 ? 0.34780 0.49880 0.42940 -0.11860 -0.03610 0.08580  235 ILE A O     
1754 C  CB    . ILE A 239 ? 0.31850 0.48410 0.39940 -0.12370 -0.04800 0.08620  235 ILE A CB    
1755 C  CG1   . ILE A 239 ? 0.36830 0.54820 0.45490 -0.12770 -0.05440 0.09030  235 ILE A CG1   
1756 C  CG2   . ILE A 239 ? 0.29850 0.44720 0.36430 -0.12410 -0.04850 0.07760  235 ILE A CG2   
1757 C  CD1   . ILE A 239 ? 0.32600 0.50850 0.40970 -0.12070 -0.05470 0.09050  235 ILE A CD1   
1758 N  N     . PRO A 240 ? 0.33120 0.46730 0.40340 -0.13300 -0.04350 0.07840  236 PRO A N     
1759 C  CA    . PRO A 240 ? 0.36110 0.48260 0.42750 -0.12980 -0.03860 0.07490  236 PRO A CA    
1760 C  C     . PRO A 240 ? 0.41630 0.52880 0.47260 -0.12140 -0.03550 0.06990  236 PRO A C     
1761 O  O     . PRO A 240 ? 0.36830 0.48040 0.41880 -0.12040 -0.03810 0.06670  236 PRO A O     
1762 C  CB    . PRO A 240 ? 0.40800 0.51730 0.46970 -0.13900 -0.04210 0.07000  236 PRO A CB    
1763 C  CG    . PRO A 240 ? 0.42960 0.54490 0.49030 -0.14630 -0.04910 0.06850  236 PRO A CG    
1764 C  CD    . PRO A 240 ? 0.32060 0.45500 0.39100 -0.14370 -0.05020 0.07580  236 PRO A CD    
1765 N  N     . VAL A 241 ? 0.30480 0.41010 0.35920 -0.11550 -0.03000 0.06960  237 VAL A N     
1766 C  CA    . VAL A 241 ? 0.32410 0.42310 0.37110 -0.10670 -0.02640 0.06620  237 VAL A CA    
1767 C  C     . VAL A 241 ? 0.32780 0.41000 0.36660 -0.10640 -0.02420 0.06090  237 VAL A C     
1768 O  O     . VAL A 241 ? 0.31710 0.39570 0.35860 -0.10700 -0.02150 0.06310  237 VAL A O     
1769 C  CB    . VAL A 241 ? 0.35170 0.46000 0.40450 -0.09850 -0.02150 0.07110  237 VAL A CB    
1770 C  CG1   . VAL A 241 ? 0.25940 0.35960 0.30400 -0.09010 -0.01820 0.06700  237 VAL A CG1   
1771 C  CG2   . VAL A 241 ? 0.28410 0.40940 0.34650 -0.09810 -0.02330 0.07650  237 VAL A CG2   
1772 N  N     . ALA A 242 ? 0.33930 0.41150 0.36850 -0.10540 -0.02530 0.05440  238 ALA A N     
1773 C  CA    . ALA A 242 ? 0.34680 0.40410 0.36850 -0.10230 -0.02230 0.04960  238 ALA A CA    
1774 C  C     . ALA A 242 ? 0.36050 0.41790 0.37850 -0.09300 -0.01890 0.04890  238 ALA A C     
1775 O  O     . ALA A 242 ? 0.35410 0.42010 0.37310 -0.09000 -0.01980 0.05030  238 ALA A O     
1776 C  CB    . ALA A 242 ? 0.31870 0.36450 0.33230 -0.10720 -0.02530 0.04230  238 ALA A CB    
1777 N  N     . THR A 243 ? 0.31370 0.36160 0.32790 -0.08880 -0.01530 0.04720  239 THR A N     
1778 C  CA    . THR A 243 ? 0.30230 0.34780 0.31180 -0.08070 -0.01240 0.04550  239 THR A CA    
1779 C  C     . THR A 243 ? 0.33170 0.36330 0.33260 -0.08020 -0.01220 0.03900  239 THR A C     
1780 O  O     . THR A 243 ? 0.31210 0.33470 0.31130 -0.08490 -0.01310 0.03620  239 THR A O     
1781 C  CB    . THR A 243 ? 0.38730 0.43480 0.39960 -0.07520 -0.00800 0.04920  239 THR A CB    
1782 O  OG1   . THR A 243 ? 0.37220 0.40880 0.38210 -0.07640 -0.00640 0.04800  239 THR A OG1   
1783 C  CG2   . THR A 243 ? 0.25690 0.31770 0.27830 -0.07640 -0.00740 0.05570  239 THR A CG2   
1784 N  N     . THR A 244 ? 0.34090 0.37080 0.33700 -0.07440 -0.01100 0.03660  240 THR A N     
1785 C  CA    . THR A 244 ? 0.26550 0.28330 0.25440 -0.07230 -0.00980 0.03120  240 THR A CA    
1786 C  C     . THR A 244 ? 0.34090 0.35280 0.33070 -0.06920 -0.00640 0.03260  240 THR A C     
1787 O  O     . THR A 244 ? 0.32380 0.34180 0.31850 -0.06780 -0.00470 0.03750  240 THR A O     
1788 C  CB    . THR A 244 ? 0.27690 0.29570 0.26140 -0.06710 -0.00930 0.02930  240 THR A CB    
1789 O  OG1   . THR A 244 ? 0.32540 0.34950 0.31300 -0.06090 -0.00680 0.03290  240 THR A OG1   
1790 C  CG2   . THR A 244 ? 0.26070 0.28680 0.24480 -0.07010 -0.01290 0.02910  240 THR A CG2   
1791 N  N     . PRO A 245 ? 0.35690 0.35730 0.34210 -0.06810 -0.00520 0.02860  241 PRO A N     
1792 C  CA    . PRO A 245 ? 0.34330 0.33860 0.32930 -0.06480 -0.00230 0.03050  241 PRO A CA    
1793 C  C     . PRO A 245 ? 0.35040 0.35220 0.33690 -0.05840 -0.00000 0.03360  241 PRO A C     
1794 O  O     . PRO A 245 ? 0.32830 0.33380 0.31820 -0.05730 0.00180  0.03810  241 PRO A O     
1795 C  CB    . PRO A 245 ? 0.28910 0.27220 0.27010 -0.06380 -0.00180 0.02510  241 PRO A CB    
1796 C  CG    . PRO A 245 ? 0.34360 0.32400 0.32240 -0.06960 -0.00440 0.02050  241 PRO A CG    
1797 C  CD    . PRO A 245 ? 0.34750 0.33950 0.32700 -0.07050 -0.00650 0.02230  241 PRO A CD    
1798 N  N     . LYS A 246 ? 0.31970 0.32310 0.30280 -0.05430 -0.00000 0.03130  242 LYS A N     
1799 C  CA    . LYS A 246 ? 0.37600 0.38460 0.35920 -0.04820 0.00210  0.03340  242 LYS A CA    
1800 C  C     . LYS A 246 ? 0.36200 0.38250 0.35070 -0.04820 0.00220  0.03780  242 LYS A C     
1801 O  O     . LYS A 246 ? 0.34730 0.37240 0.33730 -0.04410 0.00470  0.04030  242 LYS A O     
1802 C  CB    . LYS A 246 ? 0.32130 0.32830 0.30030 -0.04430 0.00180  0.03000  242 LYS A CB    
1803 C  CG    . LYS A 246 ? 0.31970 0.32940 0.29820 -0.03810 0.00390  0.03110  242 LYS A CG    
1804 C  CD    . LYS A 246 ? 0.39310 0.39780 0.36710 -0.03460 0.00380  0.02740  242 LYS A CD    
1805 C  CE    . LYS A 246 ? 0.38210 0.39140 0.35630 -0.03430 0.00200  0.02660  242 LYS A CE    
1806 N  NZ    . LYS A 246 ? 0.32930 0.33310 0.29900 -0.03270 0.00140  0.02310  242 LYS A NZ    
1807 N  N     . GLY A 247 ? 0.31700 0.34280 0.30900 -0.05280 -0.00020 0.03860  243 GLY A N     
1808 C  CA    . GLY A 247 ? 0.28990 0.32770 0.28840 -0.05320 -0.00020 0.04320  243 GLY A CA    
1809 C  C     . GLY A 247 ? 0.32650 0.36780 0.33000 -0.05610 0.00110  0.04750  243 GLY A C     
1810 O  O     . GLY A 247 ? 0.30500 0.35720 0.31470 -0.05660 0.00150  0.05170  243 GLY A O     
1811 N  N     . LYS A 248 ? 0.25850 0.29120 0.26000 -0.05810 0.00180  0.04710  244 LYS A N     
1812 C  CA    . LYS A 248 ? 0.30190 0.33770 0.30820 -0.06090 0.00310  0.05210  244 LYS A CA    
1813 C  C     . LYS A 248 ? 0.36760 0.41340 0.37650 -0.05610 0.00660  0.05610  244 LYS A C     
1814 O  O     . LYS A 248 ? 0.36170 0.40650 0.36650 -0.05010 0.00870  0.05450  244 LYS A O     
1815 C  CB    . LYS A 248 ? 0.28100 0.30530 0.28450 -0.06220 0.00380  0.05130  244 LYS A CB    
1816 C  CG    . LYS A 248 ? 0.27180 0.29750 0.28060 -0.06650 0.00450  0.05670  244 LYS A CG    
1817 C  CD    . LYS A 248 ? 0.30210 0.31600 0.30830 -0.06640 0.00520  0.05630  244 LYS A CD    
1818 C  CE    . LYS A 248 ? 0.30800 0.32190 0.31960 -0.07110 0.00560  0.06200  244 LYS A CE    
1819 N  NZ    . LYS A 248 ? 0.37200 0.38230 0.38760 -0.07860 0.00250  0.06110  244 LYS A NZ    
1820 N  N     . SER A 249 ? 0.35810 0.41360 0.37390 -0.05910 0.00720  0.06130  245 SER A N     
1821 C  CA    . SER A 249 ? 0.38240 0.44990 0.40240 -0.05570 0.01070  0.06570  245 SER A CA    
1822 C  C     . SER A 249 ? 0.42630 0.50370 0.45010 -0.05280 0.01030  0.06540  245 SER A C     
1823 O  O     . SER A 249 ? 0.36600 0.45350 0.39340 -0.04900 0.01360  0.06820  245 SER A O     
1824 C  CB    . SER A 249 ? 0.24970 0.31510 0.26450 -0.04990 0.01450  0.06570  245 SER A CB    
1825 O  OG    . SER A 249 ? 0.32700 0.38950 0.33660 -0.04390 0.01490  0.06110  245 SER A OG    
1826 N  N     . SER A 250 ? 0.31430 0.38930 0.33740 -0.05440 0.00670  0.06230  246 SER A N     
1827 C  CA    . SER A 250 ? 0.32580 0.41130 0.35440 -0.05260 0.00580  0.06350  246 SER A CA    
1828 C  C     . SER A 250 ? 0.32890 0.42570 0.36670 -0.05780 0.00460  0.06870  246 SER A C     
1829 O  O     . SER A 250 ? 0.38220 0.49040 0.42680 -0.05560 0.00490  0.07130  246 SER A O     
1830 C  CB    . SER A 250 ? 0.34570 0.42620 0.37050 -0.05300 0.00200  0.05940  246 SER A CB    
1831 O  OG    . SER A 250 ? 0.49650 0.56680 0.51330 -0.04870 0.00290  0.05470  246 SER A OG    
1832 N  N     . PHE A 251 ? 0.30600 0.40010 0.34520 -0.06430 0.00340  0.07060  247 PHE A N     
1833 C  CA    . PHE A 251 ? 0.29420 0.39850 0.34250 -0.07010 0.00200  0.07570  247 PHE A CA    
1834 C  C     . PHE A 251 ? 0.36930 0.47120 0.41880 -0.07370 0.00390  0.07900  247 PHE A C     
1835 O  O     . PHE A 251 ? 0.36490 0.45400 0.40800 -0.07510 0.00360  0.07630  247 PHE A O     
1836 C  CB    . PHE A 251 ? 0.26950 0.37230 0.31860 -0.07690 -0.00380 0.07400  247 PHE A CB    
1837 C  CG    . PHE A 251 ? 0.31240 0.42750 0.37170 -0.08270 -0.00590 0.07940  247 PHE A CG    
1838 C  CD1   . PHE A 251 ? 0.27300 0.40260 0.34030 -0.08010 -0.00580 0.08300  247 PHE A CD1   
1839 C  CD2   . PHE A 251 ? 0.26850 0.38090 0.33030 -0.09090 -0.00810 0.08110  247 PHE A CD2   
1840 C  CE1   . PHE A 251 ? 0.27650 0.41850 0.35410 -0.08550 -0.00790 0.08840  247 PHE A CE1   
1841 C  CE2   . PHE A 251 ? 0.33360 0.45790 0.40550 -0.09680 -0.01030 0.08630  247 PHE A CE2   
1842 C  CZ    . PHE A 251 ? 0.35320 0.49280 0.43290 -0.09410 -0.01030 0.09010  247 PHE A CZ    
1843 N  N     . PRO A 252 ? 0.36220 0.47620 0.42000 -0.07520 0.00610  0.08520  248 PRO A N     
1844 C  CA    . PRO A 252 ? 0.32710 0.43950 0.38610 -0.07830 0.00840  0.08930  248 PRO A CA    
1845 C  C     . PRO A 252 ? 0.38810 0.49110 0.44750 -0.08690 0.00410  0.08890  248 PRO A C     
1846 O  O     . PRO A 252 ? 0.42270 0.53020 0.48800 -0.09310 0.00030  0.09010  248 PRO A O     
1847 C  CB    . PRO A 252 ? 0.32330 0.45300 0.39240 -0.07830 0.01140  0.09630  248 PRO A CB    
1848 C  CG    . PRO A 252 ? 0.40960 0.54950 0.48420 -0.07640 0.00970  0.09590  248 PRO A CG    
1849 C  CD    . PRO A 252 ? 0.37700 0.50710 0.44340 -0.07260 0.00750  0.08900  248 PRO A CD    
1850 N  N     . GLU A 253 ? 0.36370 0.45370 0.41720 -0.08730 0.00470  0.08720  249 GLU A N     
1851 C  CA    . GLU A 253 ? 0.37530 0.45350 0.42810 -0.09460 0.00080  0.08520  249 GLU A CA    
1852 C  C     . GLU A 253 ? 0.37940 0.46160 0.44070 -0.10210 0.00020  0.09160  249 GLU A C     
1853 O  O     . GLU A 253 ? 0.45120 0.52440 0.51350 -0.10910 -0.00350 0.09000  249 GLU A O     
1854 C  CB    . GLU A 253 ? 0.44240 0.50470 0.48670 -0.09180 0.00170  0.08100  249 GLU A CB    
1855 C  CG    . GLU A 253 ? 0.36070 0.41630 0.39720 -0.08730 0.00040  0.07350  249 GLU A CG    
1856 C  CD    . GLU A 253 ? 0.53330 0.57330 0.56230 -0.08510 0.00090  0.06910  249 GLU A CD    
1857 O  OE1   . GLU A 253 ? 0.51850 0.55530 0.54690 -0.08320 0.00350  0.07220  249 GLU A OE1   
1858 O  OE2   . GLU A 253 ? 0.49360 0.52530 0.51750 -0.08520 -0.00140 0.06280  249 GLU A OE2   
1859 N  N     . ASN A 254 ? 0.35850 0.45390 0.42610 -0.10110 0.00370  0.09860  250 ASN A N     
1860 C  CA    . ASN A 254 ? 0.39410 0.49630 0.47130 -0.10840 0.00310  0.10570  250 ASN A CA    
1861 C  C     . ASN A 254 ? 0.41100 0.52710 0.49700 -0.11230 0.00070  0.10800  250 ASN A C     
1862 O  O     . ASN A 254 ? 0.37630 0.50020 0.47150 -0.11880 -0.00010 0.11410  250 ASN A O     
1863 C  CB    . ASN A 254 ? 0.39030 0.50040 0.46970 -0.10560 0.00860  0.11270  250 ASN A CB    
1864 C  CG    . ASN A 254 ? 0.47690 0.60010 0.55550 -0.09740 0.01310  0.11330  250 ASN A CG    
1865 O  OD1   . ASN A 254 ? 0.51030 0.63210 0.58400 -0.09190 0.01270  0.10760  250 ASN A OD1   
1866 N  ND2   . ASN A 254 ? 0.58490 0.72090 0.66860 -0.09650 0.01760  0.12020  250 ASN A ND2   
1867 N  N     . HIS A 255 ? 0.40700 0.52700 0.49100 -0.10850 -0.00070 0.10370  251 HIS A N     
1868 C  CA    . HIS A 255 ? 0.38150 0.51560 0.47410 -0.11150 -0.00330 0.10620  251 HIS A CA    
1869 C  C     . HIS A 255 ? 0.38030 0.50880 0.47480 -0.12120 -0.00990 0.10420  251 HIS A C     
1870 O  O     . HIS A 255 ? 0.39500 0.50790 0.48160 -0.12330 -0.01260 0.09800  251 HIS A O     
1871 C  CB    . HIS A 255 ? 0.44930 0.58810 0.53880 -0.10400 -0.00290 0.10250  251 HIS A CB    
1872 C  CG    . HIS A 255 ? 0.41780 0.57410 0.51760 -0.10450 -0.00400 0.10670  251 HIS A CG    
1873 N  ND1   . HIS A 255 ? 0.41510 0.57500 0.51960 -0.11150 -0.01000 0.10680  251 HIS A ND1   
1874 C  CD2   . HIS A 255 ? 0.40400 0.57530 0.51040 -0.09850 0.00010  0.11080  251 HIS A CD2   
1875 C  CE1   . HIS A 255 ? 0.37900 0.55590 0.49330 -0.11000 -0.00980 0.11150  251 HIS A CE1   
1876 N  NE2   . HIS A 255 ? 0.39950 0.58340 0.51550 -0.10190 -0.00350 0.11380  251 HIS A NE2   
1877 N  N     . ALA A 256 ? 0.32920 0.47080 0.43440 -0.12710 -0.01230 0.10940  252 ALA A N     
1878 C  CA    . ALA A 256 ? 0.38550 0.52300 0.49300 -0.13710 -0.01880 0.10770  252 ALA A CA    
1879 C  C     . ALA A 256 ? 0.40320 0.53460 0.50300 -0.13690 -0.02340 0.10010  252 ALA A C     
1880 O  O     . ALA A 256 ? 0.42200 0.54410 0.51880 -0.14430 -0.02840 0.09590  252 ALA A O     
1881 C  CB    . ALA A 256 ? 0.34110 0.49590 0.46230 -0.14340 -0.02080 0.11530  252 ALA A CB    
1882 N  N     . LEU A 257 ? 0.36810 0.50450 0.46460 -0.12890 -0.02170 0.09840  253 LEU A N     
1883 C  CA    . LEU A 257 ? 0.35640 0.48820 0.44570 -0.12850 -0.02580 0.09200  253 LEU A CA    
1884 C  C     . LEU A 257 ? 0.38340 0.49780 0.45970 -0.12390 -0.02420 0.08440  253 LEU A C     
1885 O  O     . LEU A 257 ? 0.34870 0.45850 0.41790 -0.12330 -0.02710 0.07890  253 LEU A O     
1886 C  CB    . LEU A 257 ? 0.33960 0.48620 0.43320 -0.12250 -0.02530 0.09460  253 LEU A CB    
1887 C  CG    . LEU A 257 ? 0.40990 0.57490 0.51650 -0.12690 -0.02810 0.10150  253 LEU A CG    
1888 C  CD1   . LEU A 257 ? 0.38260 0.56070 0.49380 -0.11890 -0.02640 0.10400  253 LEU A CD1   
1889 C  CD2   . LEU A 257 ? 0.41960 0.58340 0.52610 -0.13710 -0.03580 0.09940  253 LEU A CD2   
1890 N  N     . SER A 258 ? 0.35170 0.45670 0.42480 -0.12130 -0.02010 0.08430  254 SER A N     
1891 C  CA    . SER A 258 ? 0.35070 0.44060 0.41270 -0.11620 -0.01830 0.07780  254 SER A CA    
1892 C  C     . SER A 258 ? 0.36890 0.44350 0.42530 -0.12260 -0.02180 0.07180  254 SER A C     
1893 O  O     . SER A 258 ? 0.39820 0.46780 0.45830 -0.12890 -0.02270 0.07350  254 SER A O     
1894 C  CB    . SER A 258 ? 0.38580 0.47260 0.44680 -0.11050 -0.01260 0.08040  254 SER A CB    
1895 O  OG    . SER A 258 ? 0.36590 0.43720 0.41700 -0.10700 -0.01160 0.07430  254 SER A OG    
1896 N  N     . LEU A 259 ? 0.30820 0.37490 0.35560 -0.12080 -0.02340 0.06480  255 LEU A N     
1897 C  CA    . LEU A 259 ? 0.40080 0.45170 0.44120 -0.12510 -0.02570 0.05770  255 LEU A CA    
1898 C  C     . LEU A 259 ? 0.42650 0.46360 0.46110 -0.11980 -0.02170 0.05480  255 LEU A C     
1899 O  O     . LEU A 259 ? 0.46470 0.48780 0.49440 -0.12270 -0.02270 0.04910  255 LEU A O     
1900 C  CB    . LEU A 259 ? 0.37240 0.42270 0.40570 -0.12600 -0.02920 0.05160  255 LEU A CB    
1901 C  CG    . LEU A 259 ? 0.35290 0.41570 0.39100 -0.13240 -0.03430 0.05390  255 LEU A CG    
1902 C  CD1   . LEU A 259 ? 0.33770 0.40150 0.36800 -0.13170 -0.03730 0.04890  255 LEU A CD1   
1903 C  CD2   . LEU A 259 ? 0.35560 0.41400 0.39700 -0.14260 -0.03800 0.05310  255 LEU A CD2   
1904 N  N     . GLY A 260 ? 0.39680 0.43770 0.43180 -0.11220 -0.01730 0.05840  256 GLY A N     
1905 C  CA    . GLY A 260 ? 0.35230 0.38170 0.38140 -0.10650 -0.01380 0.05570  256 GLY A CA    
1906 C  C     . GLY A 260 ? 0.41050 0.43530 0.43090 -0.10150 -0.01390 0.04940  256 GLY A C     
1907 O  O     . GLY A 260 ? 0.34810 0.38120 0.36760 -0.10030 -0.01540 0.04860  256 GLY A O     
1908 N  N     . VAL A 261 ? 0.29730 0.30900 0.31200 -0.09880 -0.01220 0.04510  257 VAL A N     
1909 C  CA    . VAL A 261 ? 0.29390 0.30040 0.30060 -0.09360 -0.01150 0.03940  257 VAL A CA    
1910 C  C     . VAL A 261 ? 0.36760 0.36610 0.36930 -0.09860 -0.01460 0.03240  257 VAL A C     
1911 O  O     . VAL A 261 ? 0.37190 0.36070 0.37420 -0.10360 -0.01560 0.03000  257 VAL A O     
1912 C  CB    . VAL A 261 ? 0.33870 0.33630 0.34240 -0.08760 -0.00790 0.03880  257 VAL A CB    
1913 C  CG1   . VAL A 261 ? 0.32040 0.31200 0.31630 -0.08290 -0.00730 0.03280  257 VAL A CG1   
1914 C  CG2   . VAL A 261 ? 0.31220 0.31810 0.31940 -0.08270 -0.00480 0.04520  257 VAL A CG2   
1915 N  N     . PHE A 262 ? 0.37860 0.38110 0.37550 -0.09750 -0.01620 0.02910  258 PHE A N     
1916 C  CA    . PHE A 262 ? 0.34880 0.34380 0.33880 -0.10090 -0.01830 0.02180  258 PHE A CA    
1917 C  C     . PHE A 262 ? 0.38450 0.37090 0.36750 -0.09480 -0.01550 0.01700  258 PHE A C     
1918 O  O     . PHE A 262 ? 0.36650 0.35750 0.34840 -0.08840 -0.01370 0.01880  258 PHE A O     
1919 C  CB    . PHE A 262 ? 0.40530 0.41040 0.39370 -0.10420 -0.02210 0.02140  258 PHE A CB    
1920 C  CG    . PHE A 262 ? 0.45480 0.45310 0.43460 -0.10740 -0.02400 0.01370  258 PHE A CG    
1921 C  CD1   . PHE A 262 ? 0.46490 0.45460 0.44290 -0.11440 -0.02590 0.00880  258 PHE A CD1   
1922 C  CD2   . PHE A 262 ? 0.44310 0.44290 0.41630 -0.10320 -0.02350 0.01100  258 PHE A CD2   
1923 C  CE1   . PHE A 262 ? 0.52030 0.50370 0.48960 -0.11720 -0.02720 0.00100  258 PHE A CE1   
1924 C  CE2   . PHE A 262 ? 0.45460 0.44860 0.41930 -0.10600 -0.02470 0.00400  258 PHE A CE2   
1925 C  CZ    . PHE A 262 ? 0.41980 0.40580 0.38210 -0.11290 -0.02640 -0.00130 258 PHE A CZ    
1926 N  N     . GLY A 263 ? 0.36960 0.34350 0.34830 -0.09690 -0.01520 0.01070  259 GLY A N     
1927 C  CA    . GLY A 263 ? 0.38480 0.35130 0.35720 -0.09150 -0.01260 0.00590  259 GLY A CA    
1928 C  C     . GLY A 263 ? 0.39630 0.35160 0.37070 -0.08820 -0.00940 0.00550  259 GLY A C     
1929 O  O     . GLY A 263 ? 0.45930 0.40820 0.43780 -0.09200 -0.00960 0.00610  259 GLY A O     
1930 N  N     . PHE A 264 ? 0.35170 0.30490 0.32360 -0.08140 -0.00660 0.00500  260 PHE A N     
1931 C  CA    . PHE A 264 ? 0.43470 0.37730 0.40820 -0.07800 -0.00380 0.00450  260 PHE A CA    
1932 C  C     . PHE A 264 ? 0.39170 0.33510 0.37230 -0.07860 -0.00340 0.01130  260 PHE A C     
1933 O  O     . PHE A 264 ? 0.37460 0.32790 0.35780 -0.07670 -0.00330 0.01710  260 PHE A O     
1934 C  CB    . PHE A 264 ? 0.38270 0.32540 0.35310 -0.07060 -0.00130 0.00400  260 PHE A CB    
1935 C  CG    . PHE A 264 ? 0.48300 0.41560 0.45520 -0.06700 0.00130  0.00350  260 PHE A CG    
1936 C  CD1   . PHE A 264 ? 0.52220 0.44390 0.49250 -0.06780 0.00240  -0.00280 260 PHE A CD1   
1937 C  CD2   . PHE A 264 ? 0.45320 0.38730 0.42900 -0.06280 0.00270  0.00930  260 PHE A CD2   
1938 C  CE1   . PHE A 264 ? 0.58440 0.49700 0.55760 -0.06400 0.00470  -0.00290 260 PHE A CE1   
1939 C  CE2   . PHE A 264 ? 0.48460 0.41010 0.46250 -0.05950 0.00470  0.00950  260 PHE A CE2   
1940 C  CZ    . PHE A 264 ? 0.54470 0.45940 0.52190 -0.06000 0.00560  0.00360  260 PHE A CZ    
1941 N  N     . ALA A 265 ? 0.38730 0.32020 0.37120 -0.08110 -0.00300 0.01040  261 ALA A N     
1942 C  CA    . ALA A 265 ? 0.40520 0.33760 0.39610 -0.08260 -0.00280 0.01710  261 ALA A CA    
1943 C  C     . ALA A 265 ? 0.42760 0.37020 0.42250 -0.08780 -0.00510 0.02180  261 ALA A C     
1944 O  O     . ALA A 265 ? 0.46570 0.41240 0.46610 -0.08820 -0.00450 0.02880  261 ALA A O     
1945 C  CB    . ALA A 265 ? 0.33360 0.26870 0.32560 -0.07580 -0.00020 0.02240  261 ALA A CB    
1946 N  N     . GLY A 266 ? 0.42890 0.37650 0.42130 -0.09210 -0.00770 0.01850  262 GLY A N     
1947 C  CA    . GLY A 266 ? 0.38480 0.34370 0.38160 -0.09670 -0.01000 0.02320  262 GLY A CA    
1948 C  C     . GLY A 266 ? 0.44750 0.40160 0.45000 -0.10440 -0.01200 0.02440  262 GLY A C     
1949 O  O     . GLY A 266 ? 0.48530 0.42670 0.48900 -0.10570 -0.01130 0.02220  262 GLY A O     
1950 N  N     . HIS A 267 ? 0.38040 0.34480 0.38700 -0.10960 -0.01460 0.02800  263 HIS A N     
1951 C  CA    . HIS A 267 ? 0.45420 0.41680 0.46780 -0.11730 -0.01670 0.03090  263 HIS A CA    
1952 C  C     . HIS A 267 ? 0.48290 0.44310 0.49450 -0.12520 -0.02090 0.02490  263 HIS A C     
1953 O  O     . HIS A 267 ? 0.46950 0.43710 0.47650 -0.12560 -0.02290 0.02210  263 HIS A O     
1954 C  CB    . HIS A 267 ? 0.37120 0.34810 0.39230 -0.11800 -0.01650 0.04010  263 HIS A CB    
1955 C  CG    . HIS A 267 ? 0.40990 0.39020 0.43200 -0.11060 -0.01240 0.04560  263 HIS A CG    
1956 N  ND1   . HIS A 267 ? 0.45440 0.44520 0.47410 -0.10420 -0.01050 0.04730  263 HIS A ND1   
1957 C  CD2   . HIS A 267 ? 0.41170 0.38590 0.43660 -0.10880 -0.00990 0.04960  263 HIS A CD2   
1958 C  CE1   . HIS A 267 ? 0.42250 0.41380 0.44300 -0.09890 -0.00710 0.05170  263 HIS A CE1   
1959 N  NE2   . HIS A 267 ? 0.39770 0.37930 0.42110 -0.10160 -0.00670 0.05350  263 HIS A NE2   
1960 N  N     . GLN A 268 ? 0.48590 0.43550 0.50080 -0.13150 -0.02240 0.02320  264 GLN A N     
1961 C  CA    . GLN A 268 ? 0.53110 0.47680 0.54370 -0.13970 -0.02650 0.01670  264 GLN A CA    
1962 C  C     . GLN A 268 ? 0.49400 0.45550 0.50940 -0.14480 -0.03040 0.02050  264 GLN A C     
1963 O  O     . GLN A 268 ? 0.58130 0.54560 0.59130 -0.14860 -0.03370 0.01520  264 GLN A O     
1964 C  CB    . GLN A 268 ? 0.56720 0.49910 0.58480 -0.14590 -0.02750 0.01540  264 GLN A CB    
1965 C  CG    . GLN A 268 ? 0.60760 0.53110 0.62100 -0.15380 -0.03120 0.00620  264 GLN A CG    
1966 C  CD    . GLN A 268 ? 0.76220 0.67480 0.76540 -0.14980 -0.02930 -0.00400 264 GLN A CD    
1967 O  OE1   . GLN A 268 ? 0.83470 0.75140 0.82990 -0.15130 -0.03120 -0.00990 264 GLN A OE1   
1968 N  NE2   . GLN A 268 ? 0.80560 0.70520 0.80940 -0.14460 -0.02550 -0.00560 264 GLN A NE2   
1969 N  N     . LYS A 269 ? 0.44440 0.41720 0.46830 -0.14470 -0.02990 0.02980  265 LYS A N     
1970 C  CA    . LYS A 269 ? 0.42270 0.41220 0.45090 -0.14870 -0.03310 0.03430  265 LYS A CA    
1971 C  C     . LYS A 269 ? 0.44370 0.44180 0.46510 -0.14460 -0.03380 0.03160  265 LYS A C     
1972 O  O     . LYS A 269 ? 0.45170 0.45660 0.47170 -0.14990 -0.03820 0.02970  265 LYS A O     
1973 C  CB    . LYS A 269 ? 0.47120 0.47210 0.50880 -0.14640 -0.03070 0.04470  265 LYS A CB    
1974 C  CG    . LYS A 269 ? 0.47250 0.49140 0.51700 -0.15010 -0.03340 0.05070  265 LYS A CG    
1975 C  CD    . LYS A 269 ? 0.51490 0.54350 0.56870 -0.14790 -0.03020 0.06050  265 LYS A CD    
1976 C  CE    . LYS A 269 ? 0.61550 0.66200 0.67830 -0.15230 -0.03260 0.06700  265 LYS A CE    
1977 N  NZ    . LYS A 269 ? 0.67070 0.72840 0.74150 -0.14850 -0.02840 0.07620  265 LYS A NZ    
1978 N  N     . ALA A 270 ? 0.41570 0.41330 0.43250 -0.13540 -0.02990 0.03130  266 ALA A N     
1979 C  CA    . ALA A 270 ? 0.43980 0.44480 0.45050 -0.13150 -0.03050 0.02900  266 ALA A CA    
1980 C  C     . ALA A 270 ? 0.47760 0.47350 0.47880 -0.13450 -0.03270 0.01970  266 ALA A C     
1981 O  O     . ALA A 270 ? 0.47950 0.48290 0.47690 -0.13680 -0.03600 0.01790  266 ALA A O     
1982 C  CB    . ALA A 270 ? 0.35730 0.36360 0.36600 -0.12130 -0.02580 0.03100  266 ALA A CB    
1983 N  N     . THR A 271 ? 0.51980 0.49970 0.51710 -0.13470 -0.03100 0.01370  267 THR A N     
1984 C  CA    . THR A 271 ? 0.51510 0.48570 0.50310 -0.13750 -0.03240 0.00410  267 THR A CA    
1985 C  C     . THR A 271 ? 0.58400 0.55750 0.57170 -0.14770 -0.03790 0.00150  267 THR A C     
1986 O  O     . THR A 271 ? 0.60540 0.58220 0.58550 -0.15020 -0.04060 -0.00330 267 THR A O     
1987 C  CB    . THR A 271 ? 0.54080 0.49360 0.52680 -0.13580 -0.02920 -0.00130 267 THR A CB    
1988 O  OG1   . THR A 271 ? 0.58810 0.53940 0.57510 -0.12680 -0.02460 0.00200  267 THR A OG1   
1989 C  CG2   . THR A 271 ? 0.64320 0.58700 0.61900 -0.13740 -0.02960 -0.01180 267 THR A CG2   
1990 N  N     . ASP A 272 ? 0.53230 0.50470 0.52800 -0.15410 -0.03990 0.00470  268 ASP A N     
1991 C  CA    . ASP A 272 ? 0.58390 0.55920 0.58000 -0.16450 -0.04560 0.00240  268 ASP A CA    
1992 C  C     . ASP A 272 ? 0.60380 0.59730 0.60040 -0.16580 -0.04930 0.00670  268 ASP A C     
1993 O  O     . ASP A 272 ? 0.61980 0.61630 0.61040 -0.17170 -0.05370 0.00210  268 ASP A O     
1994 C  CB    . ASP A 272 ? 0.59440 0.56750 0.60110 -0.17090 -0.04710 0.00700  268 ASP A CB    
1995 C  CG    . ASP A 272 ? 0.70300 0.65700 0.71010 -0.17120 -0.04450 0.00260  268 ASP A CG    
1996 O  OD1   . ASP A 272 ? 0.69690 0.63880 0.69560 -0.16760 -0.04210 -0.00550 268 ASP A OD1   
1997 O  OD2   . ASP A 272 ? 0.70930 0.66060 0.72570 -0.17490 -0.04470 0.00770  268 ASP A OD2   
1998 N  N     . TYR A 273 ? 0.54570 0.55190 0.54930 -0.16040 -0.04750 0.01560  269 TYR A N     
1999 C  CA    . TYR A 273 ? 0.55130 0.57530 0.55780 -0.16170 -0.05100 0.02080  269 TYR A CA    
2000 C  C     . TYR A 273 ? 0.55390 0.58060 0.55030 -0.15850 -0.05190 0.01650  269 TYR A C     
2001 O  O     . TYR A 273 ? 0.51590 0.55100 0.50980 -0.16400 -0.05690 0.01560  269 TYR A O     
2002 C  CB    . TYR A 273 ? 0.50860 0.54460 0.52510 -0.15570 -0.04810 0.03060  269 TYR A CB    
2003 C  CG    . TYR A 273 ? 0.47690 0.53070 0.50170 -0.15990 -0.05220 0.03750  269 TYR A CG    
2004 C  CD1   . TYR A 273 ? 0.46110 0.52710 0.48420 -0.15730 -0.05420 0.03920  269 TYR A CD1   
2005 C  CD2   . TYR A 273 ? 0.51740 0.57630 0.55250 -0.16660 -0.05420 0.04260  269 TYR A CD2   
2006 C  CE1   . TYR A 273 ? 0.49210 0.57510 0.52390 -0.16090 -0.05810 0.04600  269 TYR A CE1   
2007 C  CE2   . TYR A 273 ? 0.54880 0.62500 0.59260 -0.17040 -0.05800 0.04920  269 TYR A CE2   
2008 C  CZ    . TYR A 273 ? 0.60630 0.69460 0.64850 -0.16740 -0.06000 0.05080  269 TYR A CZ    
2009 O  OH    . TYR A 273 ? 0.77470 0.88080 0.82650 -0.17090 -0.06380 0.05780  269 TYR A OH    
2010 N  N     . LEU A 274 ? 0.52700 0.54680 0.51740 -0.15010 -0.04720 0.01370  270 LEU A N     
2011 C  CA    . LEU A 274 ? 0.48850 0.51300 0.47130 -0.14560 -0.04720 0.01190  270 LEU A CA    
2012 C  C     . LEU A 274 ? 0.53500 0.55000 0.50540 -0.14880 -0.04840 0.00220  270 LEU A C     
2013 O  O     . LEU A 274 ? 0.54010 0.56180 0.50420 -0.14830 -0.05030 0.00110  270 LEU A O     
2014 C  CB    . LEU A 274 ? 0.42410 0.44730 0.40720 -0.13490 -0.04160 0.01440  270 LEU A CB    
2015 C  CG    . LEU A 274 ? 0.45330 0.48760 0.44700 -0.13050 -0.04000 0.02360  270 LEU A CG    
2016 C  CD1   . LEU A 274 ? 0.49590 0.52780 0.48840 -0.12040 -0.03480 0.02480  270 LEU A CD1   
2017 C  CD2   . LEU A 274 ? 0.47140 0.52240 0.46950 -0.13250 -0.04410 0.02900  270 LEU A CD2   
2018 N  N     . LEU A 275 ? 0.50520 0.50530 0.47230 -0.15190 -0.04710 -0.00480 271 LEU A N     
2019 C  CA    . LEU A 275 ? 0.56640 0.55710 0.52160 -0.15460 -0.04750 -0.01480 271 LEU A CA    
2020 C  C     . LEU A 275 ? 0.62500 0.61330 0.57780 -0.16560 -0.05270 -0.01990 271 LEU A C     
2021 O  O     . LEU A 275 ? 0.65270 0.63260 0.59520 -0.16890 -0.05310 -0.02920 271 LEU A O     
2022 C  CB    . LEU A 275 ? 0.53740 0.51170 0.48950 -0.14920 -0.04180 -0.02050 271 LEU A CB    
2023 C  CG    . LEU A 275 ? 0.49260 0.46770 0.44620 -0.13850 -0.03680 -0.01650 271 LEU A CG    
2024 C  CD1   . LEU A 275 ? 0.54690 0.50610 0.49850 -0.13420 -0.03190 -0.02180 271 LEU A CD1   
2025 C  CD2   . LEU A 275 ? 0.47630 0.46060 0.42320 -0.13470 -0.03710 -0.01610 271 LEU A CD2   
2026 N  N     . SER A 276 ? 0.66480 0.66070 0.62670 -0.17150 -0.05660 -0.01410 272 SER A N     
2027 C  CA    . SER A 276 ? 0.70000 0.69400 0.66100 -0.18270 -0.06200 -0.01840 272 SER A CA    
2028 C  C     . SER A 276 ? 0.70830 0.71100 0.65990 -0.18830 -0.06720 -0.02190 272 SER A C     
2029 O  O     . SER A 276 ? 0.71390 0.71230 0.66070 -0.19760 -0.07140 -0.02840 272 SER A O     
2030 C  CB    . SER A 276 ? 0.69960 0.70210 0.67400 -0.18730 -0.06490 -0.00980 272 SER A CB    
2031 O  OG    . SER A 276 ? 0.71190 0.73350 0.69000 -0.18880 -0.06910 -0.00260 272 SER A OG    
2032 N  N     . GLY A 277 ? 0.70110 0.71610 0.65010 -0.18330 -0.06730 -0.01750 273 GLY A N     
2033 C  CA    . GLY A 277 ? 0.67380 0.69990 0.61570 -0.18890 -0.07300 -0.01850 273 GLY A CA    
2034 C  C     . GLY A 277 ? 0.67360 0.71660 0.62510 -0.19420 -0.07900 -0.00960 273 GLY A C     
2035 O  O     . GLY A 277 ? 0.63030 0.68440 0.57710 -0.19940 -0.08460 -0.00900 273 GLY A O     
2036 N  N     . ASP A 278 ? 0.60710 0.65300 0.57210 -0.19340 -0.07820 -0.00250 274 ASP A N     
2037 C  CA    . ASP A 278 ? 0.68360 0.74610 0.65940 -0.19840 -0.08350 0.00620  274 ASP A CA    
2038 C  C     . ASP A 278 ? 0.55640 0.63400 0.54060 -0.19020 -0.08190 0.01650  274 ASP A C     
2039 O  O     . ASP A 278 ? 0.57800 0.67150 0.57090 -0.19350 -0.08650 0.02410  274 ASP A O     
2040 C  CB    . ASP A 278 ? 0.74610 0.80430 0.73240 -0.20370 -0.08390 0.00810  274 ASP A CB    
2041 C  CG    . ASP A 278 ? 0.85500 0.89850 0.83410 -0.21270 -0.08620 -0.00200 274 ASP A CG    
2042 O  OD1   . ASP A 278 ? 0.90710 0.95310 0.87750 -0.22020 -0.09170 -0.00730 274 ASP A OD1   
2043 O  OD2   . ASP A 278 ? 0.90500 0.93420 0.88680 -0.21220 -0.08260 -0.00490 274 ASP A OD2   
2044 N  N     . VAL A 279 ? 0.50950 0.58230 0.49210 -0.17980 -0.07570 0.01700  275 VAL A N     
2045 C  CA    . VAL A 279 ? 0.45350 0.53930 0.44340 -0.17170 -0.07400 0.02580  275 VAL A CA    
2046 C  C     . VAL A 279 ? 0.44340 0.54020 0.42750 -0.17270 -0.07850 0.02690  275 VAL A C     
2047 O  O     . VAL A 279 ? 0.46430 0.55440 0.43570 -0.17260 -0.07830 0.02030  275 VAL A O     
2048 C  CB    . VAL A 279 ? 0.48560 0.56260 0.47430 -0.16080 -0.06650 0.02530  275 VAL A CB    
2049 C  CG1   . VAL A 279 ? 0.38330 0.47260 0.37710 -0.15280 -0.06530 0.03270  275 VAL A CG1   
2050 C  CG2   . VAL A 279 ? 0.50560 0.57520 0.50210 -0.15940 -0.06240 0.02670  275 VAL A CG2   
2051 N  N     . ASP A 280 ? 0.44480 0.55880 0.43830 -0.17410 -0.08260 0.03550  276 ASP A N     
2052 C  CA    . ASP A 280 ? 0.39780 0.52320 0.38700 -0.17500 -0.08720 0.03790  276 ASP A CA    
2053 C  C     . ASP A 280 ? 0.36360 0.49540 0.35670 -0.16430 -0.08380 0.04400  276 ASP A C     
2054 O  O     . ASP A 280 ? 0.45160 0.58460 0.43630 -0.16230 -0.08480 0.04290  276 ASP A O     
2055 C  CB    . ASP A 280 ? 0.38510 0.52630 0.38150 -0.18380 -0.09510 0.04350  276 ASP A CB    
2056 C  CG    . ASP A 280 ? 0.48440 0.63510 0.49800 -0.18320 -0.09460 0.05190  276 ASP A CG    
2057 O  OD1   . ASP A 280 ? 0.46790 0.61280 0.48740 -0.17630 -0.08820 0.05320  276 ASP A OD1   
2058 O  OD2   . ASP A 280 ? 0.51650 0.68150 0.53780 -0.18990 -0.10080 0.05740  276 ASP A OD2   
2059 N  N     . VAL A 281 ? 0.38960 0.52510 0.39490 -0.15760 -0.07980 0.05020  277 VAL A N     
2060 C  CA    . VAL A 281 ? 0.37210 0.51280 0.38210 -0.14720 -0.07620 0.05560  277 VAL A CA    
2061 C  C     . VAL A 281 ? 0.40920 0.53830 0.42020 -0.13950 -0.06850 0.05340  277 VAL A C     
2062 O  O     . VAL A 281 ? 0.40760 0.53690 0.42720 -0.13950 -0.06620 0.05580  277 VAL A O     
2063 C  CB    . VAL A 281 ? 0.40620 0.56530 0.43120 -0.14600 -0.07880 0.06600  277 VAL A CB    
2064 C  CG1   . VAL A 281 ? 0.36220 0.52520 0.39220 -0.13500 -0.07490 0.07080  277 VAL A CG1   
2065 C  CG2   . VAL A 281 ? 0.39020 0.56170 0.41480 -0.15440 -0.08720 0.06880  277 VAL A CG2   
2066 N  N     . LEU A 282 ? 0.43940 0.55910 0.44190 -0.13330 -0.06470 0.04930  278 LEU A N     
2067 C  CA    . LEU A 282 ? 0.36510 0.47400 0.36750 -0.12580 -0.05780 0.04720  278 LEU A CA    
2068 C  C     . LEU A 282 ? 0.37320 0.48720 0.38000 -0.11610 -0.05480 0.05190  278 LEU A C     
2069 O  O     . LEU A 282 ? 0.36750 0.48360 0.36940 -0.11400 -0.05630 0.05210  278 LEU A O     
2070 C  CB    . LEU A 282 ? 0.30190 0.39450 0.29130 -0.12630 -0.05550 0.03800  278 LEU A CB    
2071 C  CG    . LEU A 282 ? 0.29550 0.37710 0.28430 -0.11850 -0.04880 0.03590  278 LEU A CG    
2072 C  CD1   . LEU A 282 ? 0.29490 0.37410 0.29150 -0.11950 -0.04660 0.03760  278 LEU A CD1   
2073 C  CD2   . LEU A 282 ? 0.30080 0.36820 0.27730 -0.11810 -0.04660 0.02740  278 LEU A CD2   
2074 N  N     . ILE A 283 ? 0.39050 0.50620 0.40610 -0.11030 -0.05050 0.05560  279 ILE A N     
2075 C  CA    . ILE A 283 ? 0.32680 0.44650 0.34740 -0.10090 -0.04710 0.05950  279 ILE A CA    
2076 C  C     . ILE A 283 ? 0.33150 0.43790 0.34680 -0.09490 -0.04110 0.05500  279 ILE A C     
2077 O  O     . ILE A 283 ? 0.29980 0.40200 0.31780 -0.09450 -0.03790 0.05450  279 ILE A O     
2078 C  CB    . ILE A 283 ? 0.33400 0.46710 0.36880 -0.09860 -0.04660 0.06720  279 ILE A CB    
2079 C  CG1   . ILE A 283 ? 0.35020 0.49720 0.39120 -0.10510 -0.05300 0.07220  279 ILE A CG1   
2080 C  CG2   . ILE A 283 ? 0.26760 0.40350 0.30700 -0.08860 -0.04280 0.07020  279 ILE A CG2   
2081 C  CD1   . ILE A 283 ? 0.38900 0.55010 0.44510 -0.10400 -0.05260 0.07970  279 ILE A CD1   
2082 N  N     . VAL A 284 ? 0.28010 0.38030 0.28800 -0.09060 -0.03990 0.05200  280 VAL A N     
2083 C  CA    . VAL A 284 ? 0.32080 0.40970 0.32410 -0.08430 -0.03460 0.04820  280 VAL A CA    
2084 C  C     . VAL A 284 ? 0.28770 0.38190 0.29790 -0.07590 -0.03180 0.05250  280 VAL A C     
2085 O  O     . VAL A 284 ? 0.29140 0.39180 0.30340 -0.07350 -0.03370 0.05540  280 VAL A O     
2086 C  CB    . VAL A 284 ? 0.34810 0.42720 0.33980 -0.08480 -0.03480 0.04220  280 VAL A CB    
2087 C  CG1   . VAL A 284 ? 0.31510 0.38300 0.30290 -0.07830 -0.02960 0.03870  280 VAL A CG1   
2088 C  CG2   . VAL A 284 ? 0.33710 0.41120 0.32210 -0.09320 -0.03750 0.03730  280 VAL A CG2   
2089 N  N     . ILE A 285 ? 0.29070 0.38260 0.30470 -0.07150 -0.02730 0.05300  281 ILE A N     
2090 C  CA    . ILE A 285 ? 0.31600 0.41220 0.33610 -0.06340 -0.02410 0.05620  281 ILE A CA    
2091 C  C     . ILE A 285 ? 0.29410 0.37890 0.30810 -0.05810 -0.01960 0.05190  281 ILE A C     
2092 O  O     . ILE A 285 ? 0.27660 0.35590 0.28920 -0.05850 -0.01690 0.05020  281 ILE A O     
2093 C  CB    . ILE A 285 ? 0.30930 0.41580 0.34030 -0.06250 -0.02250 0.06130  281 ILE A CB    
2094 C  CG1   . ILE A 285 ? 0.42870 0.54550 0.46540 -0.06970 -0.02730 0.06510  281 ILE A CG1   
2095 C  CG2   . ILE A 285 ? 0.30820 0.42060 0.34590 -0.05430 -0.01980 0.06440  281 ILE A CG2   
2096 C  CD1   . ILE A 285 ? 0.37830 0.50760 0.42730 -0.06920 -0.02600 0.07100  281 ILE A CD1   
2097 N  N     . GLY A 286 ? 0.27460 0.35630 0.28550 -0.05320 -0.01910 0.05070  282 GLY A N     
2098 C  CA    . GLY A 286 ? 0.34780 0.42030 0.35440 -0.04770 -0.01510 0.04740  282 GLY A CA    
2099 C  C     . GLY A 286 ? 0.32100 0.38200 0.31910 -0.05020 -0.01410 0.04230  282 GLY A C     
2100 O  O     . GLY A 286 ? 0.31940 0.37480 0.31630 -0.04740 -0.01070 0.04070  282 GLY A O     
2101 N  N     . SER A 287 ? 0.35650 0.41410 0.34890 -0.05550 -0.01690 0.03960  283 SER A N     
2102 C  CA    . SER A 287 ? 0.29580 0.34190 0.28010 -0.05710 -0.01570 0.03410  283 SER A CA    
2103 C  C     . SER A 287 ? 0.36260 0.40530 0.34020 -0.05700 -0.01700 0.03130  283 SER A C     
2104 O  O     . SER A 287 ? 0.33550 0.38440 0.31280 -0.05990 -0.02040 0.03290  283 SER A O     
2105 C  CB    . SER A 287 ? 0.28270 0.32620 0.26570 -0.06400 -0.01720 0.03230  283 SER A CB    
2106 O  OG    . SER A 287 ? 0.36040 0.39270 0.33590 -0.06510 -0.01600 0.02670  283 SER A OG    
2107 N  N     . SER A 288 ? 0.29690 0.33050 0.26930 -0.05390 -0.01450 0.02750  284 SER A N     
2108 C  CA    . SER A 288 ? 0.37820 0.40830 0.34390 -0.05430 -0.01520 0.02460  284 SER A CA    
2109 C  C     . SER A 288 ? 0.34920 0.37530 0.30850 -0.06060 -0.01660 0.02020  284 SER A C     
2110 O  O     . SER A 288 ? 0.34660 0.37090 0.29980 -0.06160 -0.01720 0.01770  284 SER A O     
2111 C  CB    . SER A 288 ? 0.31930 0.34170 0.28240 -0.04900 -0.01200 0.02220  284 SER A CB    
2112 O  OG    . SER A 288 ? 0.41280 0.42720 0.37420 -0.04930 -0.00960 0.01910  284 SER A OG    
2113 N  N     . LEU A 289 ? 0.26090 0.28530 0.22140 -0.06490 -0.01710 0.01920  285 LEU A N     
2114 C  CA    . LEU A 289 ? 0.27940 0.29940 0.23410 -0.07120 -0.01850 0.01440  285 LEU A CA    
2115 C  C     . LEU A 289 ? 0.35840 0.36840 0.30600 -0.06970 -0.01580 0.00860  285 LEU A C     
2116 O  O     . LEU A 289 ? 0.34650 0.35500 0.28720 -0.07300 -0.01680 0.00470  285 LEU A O     
2117 C  CB    . LEU A 289 ? 0.33650 0.36500 0.28920 -0.07640 -0.02290 0.01560  285 LEU A CB    
2118 C  CG    . LEU A 289 ? 0.30960 0.34830 0.27020 -0.07900 -0.02590 0.02120  285 LEU A CG    
2119 C  CD1   . LEU A 289 ? 0.32930 0.37740 0.28830 -0.08440 -0.03090 0.02300  285 LEU A CD1   
2120 C  CD2   . LEU A 289 ? 0.29080 0.32560 0.25430 -0.08280 -0.02550 0.02000  285 LEU A CD2   
2121 N  N     . GLY A 290 ? 0.32740 0.33080 0.27670 -0.06470 -0.01230 0.00810  286 GLY A N     
2122 C  CA    . GLY A 290 ? 0.27830 0.27220 0.22270 -0.06300 -0.00950 0.00300  286 GLY A CA    
2123 C  C     . GLY A 290 ? 0.34900 0.33480 0.29180 -0.06730 -0.00900 -0.00160 286 GLY A C     
2124 O  O     . GLY A 290 ? 0.34930 0.33690 0.29350 -0.07260 -0.01130 -0.00140 286 GLY A O     
2125 N  N     . ASP A 291 ? 0.36870 0.34520 0.30910 -0.06480 -0.00590 -0.00560 287 ASP A N     
2126 C  CA    . ASP A 291 ? 0.39040 0.35750 0.32890 -0.06810 -0.00480 -0.01110 287 ASP A CA    
2127 C  C     . ASP A 291 ? 0.34150 0.30620 0.28590 -0.07060 -0.00550 -0.00890 287 ASP A C     
2128 O  O     . ASP A 291 ? 0.36990 0.33290 0.31380 -0.07660 -0.00750 -0.01110 287 ASP A O     
2129 C  CB    . ASP A 291 ? 0.43490 0.39360 0.37200 -0.06350 -0.00100 -0.01450 287 ASP A CB    
2130 C  CG    . ASP A 291 ? 0.54160 0.48980 0.47740 -0.06600 0.00060  -0.02050 287 ASP A CG    
2131 O  OD1   . ASP A 291 ? 0.51110 0.45720 0.44690 -0.07160 -0.00130 -0.02230 287 ASP A OD1   
2132 O  OD2   . ASP A 291 ? 0.57680 0.51850 0.51180 -0.06230 0.00380  -0.02360 287 ASP A OD2   
2133 N  N     . TRP A 292 ? 0.36290 0.32710 0.31270 -0.06630 -0.00390 -0.00450 288 TRP A N     
2134 C  CA    . TRP A 292 ? 0.33980 0.30180 0.29530 -0.06840 -0.00420 -0.00170 288 TRP A CA    
2135 C  C     . TRP A 292 ? 0.39860 0.36980 0.35740 -0.07290 -0.00730 0.00220  288 TRP A C     
2136 O  O     . TRP A 292 ? 0.39530 0.36470 0.35770 -0.07730 -0.00840 0.00320  288 TRP A O     
2137 C  CB    . TRP A 292 ? 0.39730 0.35810 0.35690 -0.06270 -0.00180 0.00240  288 TRP A CB    
2138 C  CG    . TRP A 292 ? 0.47510 0.42530 0.43410 -0.06000 0.00090  -0.00070 288 TRP A CG    
2139 C  CD1   . TRP A 292 ? 0.54470 0.48680 0.50020 -0.06150 0.00180  -0.00700 288 TRP A CD1   
2140 C  CD2   . TRP A 292 ? 0.46590 0.41290 0.42820 -0.05520 0.00300  0.00230  288 TRP A CD2   
2141 N  NE1   . TRP A 292 ? 0.50940 0.44340 0.46670 -0.05760 0.00440  -0.00780 288 TRP A NE1   
2142 C  CE2   . TRP A 292 ? 0.50300 0.43990 0.46450 -0.05390 0.00490  -0.00190 288 TRP A CE2   
2143 C  CE3   . TRP A 292 ? 0.52500 0.47690 0.49070 -0.05200 0.00340  0.00820  288 TRP A CE3   
2144 C  CZ2   . TRP A 292 ? 0.56360 0.49570 0.52820 -0.04950 0.00690  0.00020  288 TRP A CZ2   
2145 C  CZ3   . TRP A 292 ? 0.59170 0.53870 0.55940 -0.04800 0.00530  0.00990  288 TRP A CZ3   
2146 C  CH2   . TRP A 292 ? 0.49070 0.42810 0.45810 -0.04680 0.00680  0.00630  288 TRP A CH2   
2147 N  N     . GLN A 293 ? 0.38210 0.36340 0.34030 -0.07180 -0.00890 0.00480  289 GLN A N     
2148 C  CA    . GLN A 293 ? 0.37020 0.36160 0.33230 -0.07560 -0.01190 0.00890  289 GLN A CA    
2149 C  C     . GLN A 293 ? 0.37900 0.37080 0.33800 -0.08320 -0.01530 0.00550  289 GLN A C     
2150 O  O     . GLN A 293 ? 0.38840 0.38730 0.35140 -0.08760 -0.01820 0.00870  289 GLN A O     
2151 C  CB    . GLN A 293 ? 0.29480 0.29640 0.25780 -0.07180 -0.01260 0.01270  289 GLN A CB    
2152 C  CG    . GLN A 293 ? 0.32690 0.32890 0.29250 -0.06440 -0.00960 0.01570  289 GLN A CG    
2153 C  CD    . GLN A 293 ? 0.41760 0.41420 0.37800 -0.06000 -0.00780 0.01240  289 GLN A CD    
2154 O  OE1   . GLN A 293 ? 0.44510 0.43310 0.40130 -0.06080 -0.00670 0.00770  289 GLN A OE1   
2155 N  NE2   . GLN A 293 ? 0.30610 0.30760 0.26730 -0.05520 -0.00740 0.01480  289 GLN A NE2   
2156 N  N     . THR A 294 ? 0.42360 0.40800 0.37540 -0.08490 -0.01500 -0.00100 290 THR A N     
2157 C  CA    . THR A 294 ? 0.36230 0.34820 0.30930 -0.09200 -0.01840 -0.00480 290 THR A CA    
2158 C  C     . THR A 294 ? 0.41820 0.39190 0.36090 -0.09580 -0.01750 -0.01230 290 THR A C     
2159 O  O     . THR A 294 ? 0.39310 0.36650 0.32980 -0.10140 -0.01970 -0.01720 290 THR A O     
2160 C  CB    . THR A 294 ? 0.37900 0.37120 0.31970 -0.09100 -0.01950 -0.00570 290 THR A CB    
2161 O  OG1   . THR A 294 ? 0.38170 0.36660 0.31750 -0.08610 -0.01580 -0.00970 290 THR A OG1   
2162 C  CG2   . THR A 294 ? 0.33940 0.34330 0.28530 -0.08750 -0.02080 0.00170  290 THR A CG2   
2163 N  N     . ASN A 295 ? 0.49180 0.45570 0.43780 -0.09290 -0.01430 -0.01320 291 ASN A N     
2164 C  CA    . ASN A 295 ? 0.56310 0.51390 0.50600 -0.09470 -0.01240 -0.02040 291 ASN A CA    
2165 C  C     . ASN A 295 ? 0.45970 0.40810 0.39320 -0.09420 -0.01130 -0.02730 291 ASN A C     
2166 O  O     . ASN A 295 ? 0.48150 0.42650 0.40920 -0.09970 -0.01260 -0.03360 291 ASN A O     
2167 C  CB    . ASN A 295 ? 0.65960 0.60660 0.60450 -0.10260 -0.01520 -0.02230 291 ASN A CB    
2168 C  CG    . ASN A 295 ? 0.84640 0.77840 0.78980 -0.10400 -0.01310 -0.02960 291 ASN A CG    
2169 O  OD1   . ASN A 295 ? 0.91270 0.83650 0.85960 -0.09910 -0.00960 -0.02920 291 ASN A OD1   
2170 N  ND2   . ASN A 295 ? 0.89730 0.82560 0.83530 -0.11080 -0.01520 -0.03640 291 ASN A ND2   
2171 N  N     . SER A 296 ? 0.40650 0.35690 0.33850 -0.08760 -0.00870 -0.02600 292 SER A N     
2172 C  CA    . SER A 296 ? 0.52960 0.48000 0.45360 -0.08620 -0.00710 -0.03090 292 SER A CA    
2173 C  C     . SER A 296 ? 0.51790 0.47660 0.43520 -0.09200 -0.01080 -0.03230 292 SER A C     
2174 O  O     . SER A 296 ? 0.43970 0.39530 0.34920 -0.09550 -0.01060 -0.03920 292 SER A O     
2175 C  CB    . SER A 296 ? 0.52780 0.46560 0.44880 -0.08570 -0.00360 -0.03880 292 SER A CB    
2176 O  OG    . SER A 296 ? 0.58400 0.51430 0.51180 -0.08070 -0.00070 -0.03690 292 SER A OG    
2177 N  N     . TRP A 297 ? 0.45250 0.42250 0.37290 -0.09260 -0.01410 -0.02550 293 TRP A N     
2178 C  CA    . TRP A 297 ? 0.45590 0.43600 0.37120 -0.09720 -0.01810 -0.02470 293 TRP A CA    
2179 C  C     . TRP A 297 ? 0.44520 0.42270 0.35540 -0.10560 -0.02090 -0.03050 293 TRP A C     
2180 O  O     . TRP A 297 ? 0.45050 0.43070 0.35190 -0.10960 -0.02230 -0.03470 293 TRP A O     
2181 C  CB    . TRP A 297 ? 0.44740 0.43070 0.35600 -0.09400 -0.01650 -0.02580 293 TRP A CB    
2182 C  CG    . TRP A 297 ? 0.40430 0.38850 0.31850 -0.08600 -0.01380 -0.02070 293 TRP A CG    
2183 C  CD1   . TRP A 297 ? 0.37030 0.36280 0.29080 -0.08310 -0.01550 -0.01310 293 TRP A CD1   
2184 C  CD2   . TRP A 297 ? 0.35990 0.33610 0.27440 -0.08010 -0.00910 -0.02300 293 TRP A CD2   
2185 N  NE1   . TRP A 297 ? 0.39190 0.38180 0.31580 -0.07610 -0.01220 -0.01100 293 TRP A NE1   
2186 C  CE2   . TRP A 297 ? 0.38200 0.36240 0.30240 -0.07430 -0.00850 -0.01670 293 TRP A CE2   
2187 C  CE3   . TRP A 297 ? 0.44450 0.41080 0.35520 -0.07920 -0.00540 -0.02990 293 TRP A CE3   
2188 C  CZ2   . TRP A 297 ? 0.37300 0.34820 0.29540 -0.06800 -0.00480 -0.01680 293 TRP A CZ2   
2189 C  CZ3   . TRP A 297 ? 0.40620 0.36790 0.31970 -0.07260 -0.00150 -0.02950 293 TRP A CZ3   
2190 C  CH2   . TRP A 297 ? 0.39230 0.35870 0.31140 -0.06730 -0.00150 -0.02300 293 TRP A CH2   
2191 N  N     . ASP A 298 ? 0.45640 0.42920 0.37250 -0.10870 -0.02180 -0.03040 294 ASP A N     
2192 C  CA    . ASP A 298 ? 0.47810 0.44770 0.39100 -0.11720 -0.02490 -0.03550 294 ASP A CA    
2193 C  C     . ASP A 298 ? 0.49200 0.47460 0.40150 -0.12290 -0.03030 -0.03290 294 ASP A C     
2194 O  O     . ASP A 298 ? 0.51440 0.50780 0.43060 -0.12200 -0.03290 -0.02470 294 ASP A O     
2195 C  CB    . ASP A 298 ? 0.48510 0.44960 0.40720 -0.11920 -0.02540 -0.03320 294 ASP A CB    
2196 C  CG    . ASP A 298 ? 0.56910 0.52590 0.48830 -0.12750 -0.02760 -0.04010 294 ASP A CG    
2197 O  OD1   . ASP A 298 ? 0.54190 0.50300 0.45340 -0.13360 -0.03100 -0.04400 294 ASP A OD1   
2198 O  OD2   . ASP A 298 ? 0.59180 0.53840 0.51660 -0.12810 -0.02620 -0.04140 294 ASP A OD2   
2199 N  N     . PRO A 299 ? 0.52680 0.50930 0.42610 -0.12860 -0.03220 -0.03950 295 PRO A N     
2200 C  CA    . PRO A 299 ? 0.47070 0.46630 0.36660 -0.13450 -0.03800 -0.03650 295 PRO A CA    
2201 C  C     . PRO A 299 ? 0.55140 0.55170 0.45440 -0.14110 -0.04300 -0.03300 295 PRO A C     
2202 O  O     . PRO A 299 ? 0.58150 0.59510 0.48610 -0.14430 -0.04780 -0.02720 295 PRO A O     
2203 C  CB    . PRO A 299 ? 0.47760 0.47000 0.35990 -0.13940 -0.03820 -0.04590 295 PRO A CB    
2204 C  CG    . PRO A 299 ? 0.53500 0.51080 0.41580 -0.13830 -0.03350 -0.05460 295 PRO A CG    
2205 C  CD    . PRO A 299 ? 0.54500 0.51640 0.43500 -0.12930 -0.02880 -0.04980 295 PRO A CD    
2206 N  N     . ARG A 300 ? 0.49520 0.48520 0.40290 -0.14330 -0.04200 -0.03600 296 ARG A N     
2207 C  CA    . ARG A 300 ? 0.45140 0.44590 0.36670 -0.14990 -0.04660 -0.03220 296 ARG A CA    
2208 C  C     . ARG A 300 ? 0.49780 0.50370 0.42460 -0.14590 -0.04740 -0.02110 296 ARG A C     
2209 O  O     . ARG A 300 ? 0.47630 0.49000 0.40980 -0.15110 -0.05170 -0.01640 296 ARG A O     
2210 C  CB    . ARG A 300 ? 0.45420 0.43420 0.37270 -0.15270 -0.04500 -0.03730 296 ARG A CB    
2211 C  CG    . ARG A 300 ? 0.52370 0.49390 0.43190 -0.15930 -0.04580 -0.04860 296 ARG A CG    
2212 C  CD    . ARG A 300 ? 0.55080 0.50510 0.46330 -0.16060 -0.04340 -0.05340 296 ARG A CD    
2213 N  NE    . ARG A 300 ? 0.68460 0.63100 0.60140 -0.15110 -0.03720 -0.05190 296 ARG A NE    
2214 C  CZ    . ARG A 300 ? 0.66400 0.59840 0.58780 -0.14970 -0.03450 -0.05240 296 ARG A CZ    
2215 N  NH1   . ARG A 300 ? 0.60900 0.53720 0.53650 -0.15720 -0.03740 -0.05460 296 ARG A NH1   
2216 N  NH2   . ARG A 300 ? 0.53320 0.46190 0.46050 -0.14100 -0.02930 -0.05040 296 ARG A NH2   
2217 N  N     . LEU A 301 ? 0.46340 0.47040 0.39300 -0.13680 -0.04330 -0.01700 297 LEU A N     
2218 C  CA    . LEU A 301 ? 0.45800 0.47650 0.39780 -0.13280 -0.04400 -0.00700 297 LEU A CA    
2219 C  C     . LEU A 301 ? 0.47250 0.50650 0.41200 -0.13570 -0.04910 -0.00210 297 LEU A C     
2220 O  O     . LEU A 301 ? 0.47950 0.52450 0.42860 -0.13500 -0.05110 0.00590  297 LEU A O     
2221 C  CB    . LEU A 301 ? 0.38750 0.40300 0.32930 -0.12270 -0.03860 -0.00470 297 LEU A CB    
2222 C  CG    . LEU A 301 ? 0.46860 0.49300 0.42070 -0.11720 -0.03770 0.00430  297 LEU A CG    
2223 C  CD1   . LEU A 301 ? 0.41470 0.43890 0.37620 -0.11980 -0.03790 0.00770  297 LEU A CD1   
2224 C  CD2   . LEU A 301 ? 0.45660 0.47640 0.40830 -0.10800 -0.03260 0.00480  297 LEU A CD2   
2225 N  N     . THR A 302 ? 0.49660 0.53220 0.42560 -0.13870 -0.05110 -0.00630 298 THR A N     
2226 C  CA    . THR A 302 ? 0.45150 0.50200 0.37990 -0.14150 -0.05630 -0.00120 298 THR A CA    
2227 C  C     . THR A 302 ? 0.46710 0.52650 0.40230 -0.14920 -0.06200 0.00270  298 THR A C     
2228 O  O     . THR A 302 ? 0.45180 0.50530 0.38400 -0.15670 -0.06410 -0.00300 298 THR A O     
2229 C  CB    . THR A 302 ? 0.44480 0.49450 0.35920 -0.14510 -0.05780 -0.00740 298 THR A CB    
2230 O  OG1   . THR A 302 ? 0.49660 0.53860 0.40560 -0.13800 -0.05220 -0.01060 298 THR A OG1   
2231 C  CG2   . THR A 302 ? 0.47310 0.53870 0.38660 -0.14790 -0.06340 -0.00110 298 THR A CG2   
2232 N  N     . PRO A 303 ? 0.52340 0.59670 0.46830 -0.14760 -0.06460 0.01200  299 PRO A N     
2233 C  CA    . PRO A 303 ? 0.50940 0.59290 0.46170 -0.15500 -0.07030 0.01640  299 PRO A CA    
2234 C  C     . PRO A 303 ? 0.54500 0.63640 0.48920 -0.16310 -0.07680 0.01480  299 PRO A C     
2235 O  O     . PRO A 303 ? 0.40170 0.49440 0.33640 -0.16170 -0.07710 0.01300  299 PRO A O     
2236 C  CB    . PRO A 303 ? 0.49280 0.58890 0.45830 -0.14880 -0.07000 0.02690  299 PRO A CB    
2237 C  CG    . PRO A 303 ? 0.47260 0.56870 0.43390 -0.14070 -0.06700 0.02800  299 PRO A CG    
2238 C  CD    . PRO A 303 ? 0.44490 0.52490 0.39530 -0.13870 -0.06230 0.01900  299 PRO A CD    
2239 N  N     . SER A 304 ? 0.50620 0.60380 0.45430 -0.17190 -0.08240 0.01590  300 SER A N     
2240 C  CA    . SER A 304 ? 0.50950 0.61370 0.44870 -0.18090 -0.08910 0.01340  300 SER A CA    
2241 C  C     . SER A 304 ? 0.52480 0.64770 0.46870 -0.18080 -0.09420 0.02300  300 SER A C     
2242 O  O     . SER A 304 ? 0.56310 0.69230 0.49770 -0.18650 -0.09920 0.02170  300 SER A O     
2243 C  CB    . SER A 304 ? 0.38840 0.49070 0.32860 -0.19160 -0.09360 0.00950  300 SER A CB    
2244 O  OG    . SER A 304 ? 0.40300 0.51570 0.35850 -0.19290 -0.09600 0.01820  300 SER A OG    
2245 N  N     . VAL A 305 ? 0.43190 0.56370 0.38970 -0.17420 -0.09290 0.03250  301 VAL A N     
2246 C  CA    . VAL A 305 ? 0.39260 0.54230 0.35690 -0.17370 -0.09780 0.04220  301 VAL A CA    
2247 C  C     . VAL A 305 ? 0.41780 0.56880 0.38520 -0.16260 -0.09330 0.04710  301 VAL A C     
2248 O  O     . VAL A 305 ? 0.47140 0.62850 0.43350 -0.16150 -0.09560 0.04970  301 VAL A O     
2249 C  CB    . VAL A 305 ? 0.42110 0.58370 0.40130 -0.17680 -0.10160 0.05030  301 VAL A CB    
2250 C  CG1   . VAL A 305 ? 0.38440 0.56470 0.37420 -0.17330 -0.10500 0.06130  301 VAL A CG1   
2251 C  CG2   . VAL A 305 ? 0.39870 0.56330 0.37570 -0.18940 -0.10810 0.04670  301 VAL A CG2   
2252 N  N     . ALA A 306 ? 0.39740 0.54310 0.37340 -0.15450 -0.08720 0.04880  302 ALA A N     
2253 C  CA    . ALA A 306 ? 0.38400 0.53140 0.36390 -0.14420 -0.08340 0.05360  302 ALA A CA    
2254 C  C     . ALA A 306 ? 0.36680 0.50110 0.34810 -0.13660 -0.07560 0.05010  302 ALA A C     
2255 O  O     . ALA A 306 ? 0.39440 0.52570 0.38240 -0.13690 -0.07340 0.04980  302 ALA A O     
2256 C  CB    . ALA A 306 ? 0.37990 0.54370 0.37480 -0.14130 -0.08610 0.06460  302 ALA A CB    
2257 N  N     . LEU A 307 ? 0.33490 0.46210 0.30970 -0.13010 -0.07160 0.04780  303 LEU A N     
2258 C  CA    . LEU A 307 ? 0.30320 0.42070 0.28040 -0.12140 -0.06470 0.04630  303 LEU A CA    
2259 C  C     . LEU A 307 ? 0.36280 0.48840 0.34930 -0.11320 -0.06350 0.05410  303 LEU A C     
2260 O  O     . LEU A 307 ? 0.37180 0.50280 0.35600 -0.11190 -0.06580 0.05720  303 LEU A O     
2261 C  CB    . LEU A 307 ? 0.32330 0.42690 0.28760 -0.11980 -0.06100 0.03830  303 LEU A CB    
2262 C  CG    . LEU A 307 ? 0.45070 0.54470 0.41700 -0.11080 -0.05430 0.03700  303 LEU A CG    
2263 C  CD1   . LEU A 307 ? 0.34310 0.43180 0.31570 -0.11040 -0.05130 0.03600  303 LEU A CD1   
2264 C  CD2   . LEU A 307 ? 0.46850 0.55100 0.42290 -0.10890 -0.05110 0.03000  303 LEU A CD2   
2265 N  N     . ILE A 308 ? 0.34730 0.47420 0.34470 -0.10810 -0.06010 0.05750  304 ILE A N     
2266 C  CA    . ILE A 308 ? 0.26990 0.40290 0.27690 -0.09960 -0.05790 0.06380  304 ILE A CA    
2267 C  C     . ILE A 308 ? 0.26460 0.38560 0.26940 -0.09220 -0.05120 0.05980  304 ILE A C     
2268 O  O     . ILE A 308 ? 0.31980 0.43320 0.32390 -0.09280 -0.04800 0.05620  304 ILE A O     
2269 C  CB    . ILE A 308 ? 0.26640 0.41170 0.28790 -0.09960 -0.05900 0.07070  304 ILE A CB    
2270 C  CG1   . ILE A 308 ? 0.28580 0.44360 0.30990 -0.10770 -0.06620 0.07470  304 ILE A CG1   
2271 C  CG2   . ILE A 308 ? 0.26190 0.41280 0.29400 -0.09020 -0.05590 0.07640  304 ILE A CG2   
2272 C  CD1   . ILE A 308 ? 0.31380 0.48180 0.35050 -0.11060 -0.06740 0.07950  304 ILE A CD1   
2273 N  N     . GLN A 309 ? 0.25940 0.37830 0.26300 -0.08570 -0.04930 0.06080  305 GLN A N     
2274 C  CA    . GLN A 309 ? 0.27190 0.37990 0.27350 -0.07880 -0.04330 0.05720  305 GLN A CA    
2275 C  C     . GLN A 309 ? 0.34550 0.45800 0.35620 -0.07040 -0.04110 0.06220  305 GLN A C     
2276 O  O     . GLN A 309 ? 0.31880 0.43710 0.33180 -0.06850 -0.04360 0.06630  305 GLN A O     
2277 C  CB    . GLN A 309 ? 0.30510 0.40240 0.29450 -0.07880 -0.04220 0.05130  305 GLN A CB    
2278 C  CG    . GLN A 309 ? 0.25180 0.33830 0.23970 -0.07210 -0.03640 0.04780  305 GLN A CG    
2279 C  CD    . GLN A 309 ? 0.41370 0.48970 0.39030 -0.07260 -0.03490 0.04170  305 GLN A CD    
2280 O  OE1   . GLN A 309 ? 0.39040 0.46780 0.36020 -0.07670 -0.03780 0.04060  305 GLN A OE1   
2281 N  NE2   . GLN A 309 ? 0.37070 0.43680 0.34530 -0.06840 -0.03030 0.03790  305 GLN A NE2   
2282 N  N     . ILE A 310 ? 0.29820 0.40830 0.31420 -0.06560 -0.03660 0.06200  306 ILE A N     
2283 C  CA    . ILE A 310 ? 0.28130 0.39490 0.30600 -0.05750 -0.03370 0.06560  306 ILE A CA    
2284 C  C     . ILE A 310 ? 0.30100 0.40260 0.32010 -0.05190 -0.02890 0.06080  306 ILE A C     
2285 O  O     . ILE A 310 ? 0.29030 0.38470 0.30550 -0.05230 -0.02590 0.05680  306 ILE A O     
2286 C  CB    . ILE A 310 ? 0.33860 0.46110 0.37440 -0.05640 -0.03220 0.06950  306 ILE A CB    
2287 C  CG1   . ILE A 310 ? 0.34410 0.47970 0.38670 -0.06200 -0.03750 0.07500  306 ILE A CG1   
2288 C  CG2   . ILE A 310 ? 0.25900 0.38340 0.30270 -0.04730 -0.02820 0.07180  306 ILE A CG2   
2289 C  CD1   . ILE A 310 ? 0.28800 0.42990 0.33720 -0.06560 -0.03710 0.07680  306 ILE A CD1   
2290 N  N     . ASP A 311 ? 0.26940 0.36910 0.28840 -0.04680 -0.02850 0.06160  307 ASP A N     
2291 C  CA    . ASP A 311 ? 0.27080 0.35950 0.28450 -0.04200 -0.02450 0.05700  307 ASP A CA    
2292 C  C     . ASP A 311 ? 0.26570 0.35510 0.28450 -0.03510 -0.02360 0.05950  307 ASP A C     
2293 O  O     . ASP A 311 ? 0.30860 0.40370 0.33080 -0.03530 -0.02690 0.06370  307 ASP A O     
2294 C  CB    . ASP A 311 ? 0.27270 0.35260 0.27480 -0.04570 -0.02540 0.05230  307 ASP A CB    
2295 C  CG    . ASP A 311 ? 0.47330 0.54200 0.46980 -0.04290 -0.02110 0.04690  307 ASP A CG    
2296 O  OD1   . ASP A 311 ? 0.34360 0.40790 0.34020 -0.03720 -0.01900 0.04630  307 ASP A OD1   
2297 O  OD2   . ASP A 311 ? 0.42210 0.48640 0.41460 -0.04640 -0.02020 0.04370  307 ASP A OD2   
2298 N  N     . ILE A 312 ? 0.25140 0.33500 0.27090 -0.02920 -0.01930 0.05710  308 ILE A N     
2299 C  CA    . ILE A 312 ? 0.32250 0.40520 0.34670 -0.02280 -0.01830 0.05850  308 ILE A CA    
2300 C  C     . ILE A 312 ? 0.31120 0.38670 0.32860 -0.02300 -0.01970 0.05690  308 ILE A C     
2301 O  O     . ILE A 312 ? 0.28150 0.35680 0.30290 -0.01900 -0.02020 0.05920  308 ILE A O     
2302 C  CB    . ILE A 312 ? 0.35470 0.43340 0.38100 -0.01670 -0.01330 0.05580  308 ILE A CB    
2303 C  CG1   . ILE A 312 ? 0.27280 0.35360 0.30740 -0.01000 -0.01240 0.05810  308 ILE A CG1   
2304 C  CG2   . ILE A 312 ? 0.28870 0.35590 0.30520 -0.01650 -0.01110 0.05000  308 ILE A CG2   
2305 C  CD1   . ILE A 312 ? 0.25630 0.33840 0.29590 -0.00460 -0.00770 0.05670  308 ILE A CD1   
2306 N  N     . ASP A 313 ? 0.31890 0.38840 0.32650 -0.02740 -0.02000 0.05300  309 ASP A N     
2307 C  CA    . ASP A 313 ? 0.32070 0.38380 0.32160 -0.02770 -0.02070 0.05120  309 ASP A CA    
2308 C  C     . ASP A 313 ? 0.31890 0.38720 0.31650 -0.03350 -0.02500 0.05380  309 ASP A C     
2309 O  O     . ASP A 313 ? 0.36880 0.43730 0.36070 -0.03910 -0.02600 0.05140  309 ASP A O     
2310 C  CB    . ASP A 313 ? 0.22350 0.27680 0.21600 -0.02840 -0.01790 0.04510  309 ASP A CB    
2311 C  CG    . ASP A 313 ? 0.28670 0.33410 0.27230 -0.02900 -0.01830 0.04320  309 ASP A CG    
2312 O  OD1   . ASP A 313 ? 0.34070 0.39160 0.32710 -0.02970 -0.02090 0.04670  309 ASP A OD1   
2313 O  OD2   . ASP A 313 ? 0.33700 0.37650 0.31670 -0.02890 -0.01590 0.03860  309 ASP A OD2   
2314 N  N     . PRO A 314 ? 0.32770 0.40020 0.32840 -0.03270 -0.02770 0.05840  310 PRO A N     
2315 C  CA    . PRO A 314 ? 0.31050 0.38940 0.30770 -0.03860 -0.03220 0.06140  310 PRO A CA    
2316 C  C     . PRO A 314 ? 0.34770 0.42110 0.33290 -0.04320 -0.03200 0.05670  310 PRO A C     
2317 O  O     . PRO A 314 ? 0.35970 0.43780 0.33990 -0.04930 -0.03510 0.05710  310 PRO A O     
2318 C  CB    . PRO A 314 ? 0.33020 0.41350 0.33380 -0.03560 -0.03450 0.06780  310 PRO A CB    
2319 C  CG    . PRO A 314 ? 0.26670 0.34150 0.27260 -0.02910 -0.03100 0.06570  310 PRO A CG    
2320 C  CD    . PRO A 314 ? 0.27430 0.34440 0.28050 -0.02670 -0.02690 0.06070  310 PRO A CD    
2321 N  N     . MET A 315 ? 0.23520 0.29880 0.21570 -0.04050 -0.02850 0.05200  311 MET A N     
2322 C  CA    . MET A 315 ? 0.28380 0.34220 0.25370 -0.04410 -0.02770 0.04740  311 MET A CA    
2323 C  C     . MET A 315 ? 0.36750 0.42300 0.33190 -0.04830 -0.02660 0.04210  311 MET A C     
2324 O  O     . MET A 315 ? 0.42160 0.47380 0.37740 -0.05200 -0.02630 0.03800  311 MET A O     
2325 C  CB    . MET A 315 ? 0.28320 0.33280 0.25120 -0.03980 -0.02430 0.04450  311 MET A CB    
2326 C  CG    . MET A 315 ? 0.39960 0.45030 0.37290 -0.03580 -0.02520 0.04930  311 MET A CG    
2327 S  SD    . MET A 315 ? 0.52910 0.59020 0.50390 -0.03940 -0.03030 0.05670  311 MET A SD    
2328 C  CE    . MET A 315 ? 0.58920 0.64940 0.57410 -0.03280 -0.03050 0.06200  311 MET A CE    
2329 N  N     . GLU A 316 ? 0.35020 0.40670 0.31980 -0.04770 -0.02590 0.04190  312 GLU A N     
2330 C  CA    . GLU A 316 ? 0.36270 0.41660 0.32840 -0.05210 -0.02530 0.03770  312 GLU A CA    
2331 C  C     . GLU A 316 ? 0.38670 0.44860 0.35170 -0.05870 -0.02950 0.03950  312 GLU A C     
2332 O  O     . GLU A 316 ? 0.40650 0.46560 0.36660 -0.06360 -0.02960 0.03530  312 GLU A O     
2333 C  CB    . GLU A 316 ? 0.37890 0.43060 0.35030 -0.04900 -0.02260 0.03710  312 GLU A CB    
2334 C  CG    . GLU A 316 ? 0.42150 0.46440 0.39190 -0.04370 -0.01860 0.03410  312 GLU A CG    
2335 C  CD    . GLU A 316 ? 0.49460 0.52870 0.45690 -0.04570 -0.01670 0.02830  312 GLU A CD    
2336 O  OE1   . GLU A 316 ? 0.47440 0.50190 0.43520 -0.04180 -0.01400 0.02620  312 GLU A OE1   
2337 O  OE2   . GLU A 316 ? 0.50920 0.54280 0.46670 -0.05110 -0.01790 0.02580  312 GLU A OE2   
2338 N  N     . ILE A 317 ? 0.32340 0.39490 0.29350 -0.05900 -0.03300 0.04560  313 ILE A N     
2339 C  CA    . ILE A 317 ? 0.37080 0.45150 0.34220 -0.06500 -0.03740 0.04820  313 ILE A CA    
2340 C  C     . ILE A 317 ? 0.37150 0.45240 0.33210 -0.07140 -0.03990 0.04550  313 ILE A C     
2341 O  O     . ILE A 317 ? 0.38100 0.46360 0.33800 -0.07100 -0.04110 0.04750  313 ILE A O     
2342 C  CB    . ILE A 317 ? 0.40670 0.49840 0.38840 -0.06280 -0.04040 0.05630  313 ILE A CB    
2343 C  CG1   . ILE A 317 ? 0.39880 0.49070 0.39090 -0.05670 -0.03740 0.05810  313 ILE A CG1   
2344 C  CG2   . ILE A 317 ? 0.33530 0.43750 0.31770 -0.06970 -0.04570 0.05950  313 ILE A CG2   
2345 C  CD1   . ILE A 317 ? 0.37110 0.47300 0.37470 -0.05310 -0.03950 0.06570  313 ILE A CD1   
2346 N  N     . GLY A 318 ? 0.36510 0.44440 0.32060 -0.07740 -0.04090 0.04110  314 GLY A N     
2347 C  CA    . GLY A 318 ? 0.39710 0.47620 0.34150 -0.08380 -0.04290 0.03720  314 GLY A CA    
2348 C  C     . GLY A 318 ? 0.36450 0.43310 0.29960 -0.08260 -0.03890 0.03060  314 GLY A C     
2349 O  O     . GLY A 318 ? 0.40670 0.47570 0.33220 -0.08670 -0.03990 0.02780  314 GLY A O     
2350 N  N     . LYS A 319 ? 0.30760 0.36730 0.24530 -0.07710 -0.03420 0.02800  315 LYS A N     
2351 C  CA    . LYS A 319 ? 0.35820 0.40850 0.28870 -0.07510 -0.03020 0.02240  315 LYS A CA    
2352 C  C     . LYS A 319 ? 0.38930 0.43410 0.31080 -0.08070 -0.02950 0.01480  315 LYS A C     
2353 O  O     . LYS A 319 ? 0.42780 0.47130 0.34040 -0.08270 -0.02890 0.01130  315 LYS A O     
2354 C  CB    . LYS A 319 ? 0.33110 0.37380 0.26700 -0.06850 -0.02590 0.02160  315 LYS A CB    
2355 C  CG    . LYS A 319 ? 0.44170 0.47570 0.37210 -0.06580 -0.02190 0.01680  315 LYS A CG    
2356 C  CD    . LYS A 319 ? 0.41660 0.44470 0.35290 -0.05920 -0.01850 0.01710  315 LYS A CD    
2357 C  CE    . LYS A 319 ? 0.43930 0.46050 0.37640 -0.05960 -0.01630 0.01310  315 LYS A CE    
2358 N  NZ    . LYS A 319 ? 0.50240 0.52110 0.44630 -0.05400 -0.01420 0.01520  315 LYS A NZ    
2359 N  N     . ASN A 320 ? 0.42090 0.46210 0.34450 -0.08320 -0.02950 0.01210  316 ASN A N     
2360 C  CA    . ASN A 320 ? 0.41320 0.44710 0.32960 -0.08800 -0.02850 0.00440  316 ASN A CA    
2361 C  C     . ASN A 320 ? 0.47320 0.51210 0.38720 -0.09600 -0.03300 0.00350  316 ASN A C     
2362 O  O     . ASN A 320 ? 0.46550 0.49940 0.37130 -0.10090 -0.03280 -0.00340 316 ASN A O     
2363 C  CB    . ASN A 320 ? 0.39910 0.42270 0.31950 -0.08500 -0.02470 0.00120  316 ASN A CB    
2364 C  CG    . ASN A 320 ? 0.40760 0.42460 0.32820 -0.07820 -0.02010 0.00010  316 ASN A CG    
2365 O  OD1   . ASN A 320 ? 0.35180 0.36770 0.26630 -0.07730 -0.01860 -0.00220 316 ASN A OD1   
2366 N  ND2   . ASN A 320 ? 0.36740 0.38050 0.29500 -0.07350 -0.01780 0.00190  316 ASN A ND2   
2367 N  N     . TYR A 321 ? 0.30770 0.35630 0.22890 -0.09750 -0.03700 0.01010  317 TYR A N     
2368 C  CA    . TYR A 321 ? 0.34710 0.40230 0.26740 -0.10540 -0.04210 0.01040  317 TYR A CA    
2369 C  C     . TYR A 321 ? 0.42000 0.48910 0.34340 -0.10610 -0.04670 0.01820  317 TYR A C     
2370 O  O     . TYR A 321 ? 0.38240 0.45610 0.31450 -0.10030 -0.04620 0.02480  317 TYR A O     
2371 C  CB    . TYR A 321 ? 0.38170 0.43560 0.31040 -0.10690 -0.04250 0.01120  317 TYR A CB    
2372 C  CG    . TYR A 321 ? 0.44600 0.48660 0.37240 -0.10740 -0.03880 0.00400  317 TYR A CG    
2373 C  CD1   . TYR A 321 ? 0.44430 0.47650 0.37380 -0.10060 -0.03370 0.00330  317 TYR A CD1   
2374 C  CD2   . TYR A 321 ? 0.42140 0.45760 0.34270 -0.11490 -0.04060 -0.00190 317 TYR A CD2   
2375 C  CE1   . TYR A 321 ? 0.44100 0.46120 0.36930 -0.10080 -0.03050 -0.00240 317 TYR A CE1   
2376 C  CE2   . TYR A 321 ? 0.44470 0.46810 0.36500 -0.11520 -0.03730 -0.00820 317 TYR A CE2   
2377 C  CZ    . TYR A 321 ? 0.38160 0.39730 0.30570 -0.10790 -0.03220 -0.00800 317 TYR A CZ    
2378 O  OH    . TYR A 321 ? 0.45140 0.45460 0.37520 -0.10790 -0.02910 -0.01340 317 TYR A OH    
2379 N  N     . PRO A 322 ? 0.40910 0.48510 0.32560 -0.11300 -0.05140 0.01790  318 PRO A N     
2380 C  CA    . PRO A 322 ? 0.39070 0.48070 0.31120 -0.11390 -0.05640 0.02640  318 PRO A CA    
2381 C  C     . PRO A 322 ? 0.37790 0.47560 0.31130 -0.11390 -0.05910 0.03280  318 PRO A C     
2382 O  O     . PRO A 322 ? 0.39520 0.49120 0.33080 -0.11820 -0.06000 0.03020  318 PRO A O     
2383 C  CB    . PRO A 322 ? 0.42520 0.52010 0.33420 -0.12250 -0.06080 0.02340  318 PRO A CB    
2384 C  CG    . PRO A 322 ? 0.52830 0.61250 0.43010 -0.12710 -0.05890 0.01350  318 PRO A CG    
2385 C  CD    . PRO A 322 ? 0.49570 0.56700 0.39980 -0.11990 -0.05200 0.00960  318 PRO A CD    
2386 N  N     . VAL A 323 ? 0.29950 0.40560 0.24220 -0.10880 -0.06010 0.04120  319 VAL A N     
2387 C  CA    . VAL A 323 ? 0.33220 0.44660 0.28820 -0.10780 -0.06200 0.04770  319 VAL A CA    
2388 C  C     . VAL A 323 ? 0.33080 0.46000 0.28960 -0.11240 -0.06880 0.05470  319 VAL A C     
2389 O  O     . VAL A 323 ? 0.44840 0.58210 0.40120 -0.11360 -0.07140 0.05680  319 VAL A O     
2390 C  CB    . VAL A 323 ? 0.39010 0.50320 0.35650 -0.09820 -0.05780 0.05190  319 VAL A CB    
2391 C  CG1   . VAL A 323 ? 0.33360 0.43270 0.29700 -0.09400 -0.05160 0.04540  319 VAL A CG1   
2392 C  CG2   . VAL A 323 ? 0.39130 0.50890 0.35840 -0.09380 -0.05860 0.05710  319 VAL A CG2   
2393 N  N     . ASP A 324 ? 0.34640 0.48390 0.31490 -0.11510 -0.07180 0.05880  320 ASP A N     
2394 C  CA    . ASP A 324 ? 0.35430 0.50730 0.32860 -0.11890 -0.07840 0.06670  320 ASP A CA    
2395 C  C     . ASP A 324 ? 0.42050 0.58190 0.41000 -0.11140 -0.07790 0.07580  320 ASP A C     
2396 O  O     . ASP A 324 ? 0.39720 0.56970 0.39080 -0.11120 -0.08220 0.08320  320 ASP A O     
2397 C  CB    . ASP A 324 ? 0.31630 0.47430 0.29170 -0.12770 -0.08270 0.06540  320 ASP A CB    
2398 C  CG    . ASP A 324 ? 0.51300 0.66190 0.47290 -0.13540 -0.08330 0.05560  320 ASP A CG    
2399 O  OD1   . ASP A 324 ? 0.55940 0.71170 0.50890 -0.14000 -0.08700 0.05460  320 ASP A OD1   
2400 O  OD2   . ASP A 324 ? 0.53480 0.67280 0.49280 -0.13640 -0.07980 0.04880  320 ASP A OD2   
2401 N  N     . VAL A 325 ? 0.34260 0.49880 0.34030 -0.10500 -0.07260 0.07520  321 VAL A N     
2402 C  CA    . VAL A 325 ? 0.39390 0.55530 0.40500 -0.09650 -0.07050 0.08210  321 VAL A CA    
2403 C  C     . VAL A 325 ? 0.36640 0.51450 0.37490 -0.08890 -0.06340 0.07730  321 VAL A C     
2404 O  O     . VAL A 325 ? 0.35100 0.49120 0.35870 -0.08820 -0.05940 0.07230  321 VAL A O     
2405 C  CB    . VAL A 325 ? 0.31980 0.49090 0.34490 -0.09660 -0.07110 0.08690  321 VAL A CB    
2406 C  CG1   . VAL A 325 ? 0.31780 0.49630 0.35710 -0.08810 -0.06960 0.09440  321 VAL A CG1   
2407 C  CG2   . VAL A 325 ? 0.34170 0.52430 0.36760 -0.10600 -0.07820 0.08980  321 VAL A CG2   
2408 N  N     . GLY A 326 ? 0.31000 0.45570 0.31720 -0.08350 -0.06230 0.07900  322 GLY A N     
2409 C  CA    . GLY A 326 ? 0.32170 0.45570 0.32710 -0.07640 -0.05620 0.07510  322 GLY A CA    
2410 C  C     . GLY A 326 ? 0.29450 0.43210 0.31260 -0.06790 -0.05400 0.08060  322 GLY A C     
2411 O  O     . GLY A 326 ? 0.37150 0.51420 0.39390 -0.06510 -0.05620 0.08610  322 GLY A O     
2412 N  N     . ILE A 327 ? 0.28200 0.41720 0.30640 -0.06400 -0.04980 0.07910  323 ILE A N     
2413 C  CA    . ILE A 327 ? 0.32040 0.46020 0.35770 -0.05630 -0.04730 0.08370  323 ILE A CA    
2414 C  C     . ILE A 327 ? 0.32350 0.45140 0.35780 -0.04930 -0.04180 0.07930  323 ILE A C     
2415 O  O     . ILE A 327 ? 0.36020 0.47990 0.38980 -0.04900 -0.03790 0.07370  323 ILE A O     
2416 C  CB    . ILE A 327 ? 0.31280 0.45970 0.35950 -0.05670 -0.04620 0.08550  323 ILE A CB    
2417 C  CG1   . ILE A 327 ? 0.34280 0.50330 0.39480 -0.06330 -0.05220 0.09110  323 ILE A CG1   
2418 C  CG2   . ILE A 327 ? 0.24270 0.39160 0.30080 -0.04780 -0.04180 0.08810  323 ILE A CG2   
2419 C  CD1   . ILE A 327 ? 0.32630 0.49440 0.38740 -0.06490 -0.05140 0.09300  323 ILE A CD1   
2420 N  N     . ASN A 328 ? 0.31380 0.44100 0.35160 -0.04390 -0.04170 0.08220  324 ASN A N     
2421 C  CA    . ASN A 328 ? 0.32390 0.44070 0.36020 -0.03710 -0.03690 0.07850  324 ASN A CA    
2422 C  C     . ASN A 328 ? 0.31270 0.43310 0.36110 -0.03020 -0.03360 0.08070  324 ASN A C     
2423 O  O     . ASN A 328 ? 0.38570 0.51120 0.44360 -0.02570 -0.03450 0.08570  324 ASN A O     
2424 C  CB    . ASN A 328 ? 0.28720 0.40050 0.32090 -0.03520 -0.03850 0.08020  324 ASN A CB    
2425 C  CG    . ASN A 328 ? 0.34220 0.44520 0.37540 -0.02850 -0.03400 0.07670  324 ASN A CG    
2426 O  OD1   . ASN A 328 ? 0.41940 0.51520 0.44870 -0.02700 -0.03000 0.07110  324 ASN A OD1   
2427 N  ND2   . ASN A 328 ? 0.33340 0.43570 0.37100 -0.02450 -0.03500 0.08030  324 ASN A ND2   
2428 N  N     . ALA A 329 ? 0.25730 0.37510 0.30540 -0.02930 -0.02950 0.07690  325 ALA A N     
2429 C  CA    . ALA A 329 ? 0.26830 0.39060 0.32710 -0.02310 -0.02590 0.07860  325 ALA A CA    
2430 C  C     . ALA A 329 ? 0.32750 0.44350 0.38190 -0.02200 -0.02090 0.07310  325 ALA A C     
2431 O  O     . ALA A 329 ? 0.39160 0.50150 0.43650 -0.02680 -0.02090 0.06900  325 ALA A O     
2432 C  CB    . ALA A 329 ? 0.22150 0.35830 0.29180 -0.02480 -0.02830 0.08500  325 ALA A CB    
2433 N  N     . ASP A 330 ? 0.27470 0.39230 0.33610 -0.01560 -0.01660 0.07300  326 ASP A N     
2434 C  CA    . ASP A 330 ? 0.28070 0.39520 0.33940 -0.01450 -0.01180 0.06920  326 ASP A CA    
2435 C  C     . ASP A 330 ? 0.38210 0.50480 0.44340 -0.02030 -0.01270 0.07150  326 ASP A C     
2436 O  O     . ASP A 330 ? 0.34750 0.48160 0.41780 -0.02210 -0.01540 0.07690  326 ASP A O     
2437 C  CB    . ASP A 330 ? 0.27920 0.39510 0.34510 -0.00630 -0.00710 0.06890  326 ASP A CB    
2438 C  CG    . ASP A 330 ? 0.31160 0.42790 0.37630 -0.00520 -0.00210 0.06640  326 ASP A CG    
2439 O  OD1   . ASP A 330 ? 0.39920 0.50580 0.45510 -0.00420 0.00040  0.06130  326 ASP A OD1   
2440 O  OD2   . ASP A 330 ? 0.37220 0.49890 0.44510 -0.00530 -0.00070 0.06970  326 ASP A OD2   
2441 N  N     . ALA A 331 ? 0.30280 0.41970 0.35680 -0.02330 -0.01070 0.06780  327 ALA A N     
2442 C  CA    . ALA A 331 ? 0.29460 0.41770 0.35050 -0.02950 -0.01170 0.06980  327 ALA A CA    
2443 C  C     . ALA A 331 ? 0.32110 0.45620 0.38880 -0.02680 -0.00900 0.07410  327 ALA A C     
2444 O  O     . ALA A 331 ? 0.36600 0.51120 0.44030 -0.03140 -0.01150 0.07840  327 ALA A O     
2445 C  CB    . ALA A 331 ? 0.22020 0.33380 0.26680 -0.03260 -0.00980 0.06520  327 ALA A CB    
2446 N  N     . SER A 332 ? 0.33480 0.46950 0.40530 -0.01950 -0.00390 0.07290  328 SER A N     
2447 C  CA    . SER A 332 ? 0.34100 0.48750 0.42240 -0.01660 -0.00050 0.07660  328 SER A CA    
2448 C  C     . SER A 332 ? 0.30080 0.45880 0.39460 -0.01460 -0.00300 0.08220  328 SER A C     
2449 O  O     . SER A 332 ? 0.30320 0.47380 0.40680 -0.01660 -0.00350 0.08720  328 SER A O     
2450 C  CB    . SER A 332 ? 0.43350 0.57620 0.51330 -0.00930 0.00590  0.07300  328 SER A CB    
2451 O  OG    . SER A 332 ? 0.58900 0.74270 0.68050 -0.00380 0.00930  0.07610  328 SER A OG    
2452 N  N     . GLU A 333 ? 0.29690 0.45090 0.39080 -0.01090 -0.00490 0.08190  329 GLU A N     
2453 C  CA    . GLU A 333 ? 0.31920 0.48380 0.42530 -0.00900 -0.00780 0.08790  329 GLU A CA    
2454 C  C     . GLU A 333 ? 0.25290 0.42530 0.36080 -0.01730 -0.01410 0.09260  329 GLU A C     
2455 O  O     . GLU A 333 ? 0.31160 0.49750 0.43170 -0.01760 -0.01600 0.09870  329 GLU A O     
2456 C  CB    . GLU A 333 ? 0.37960 0.53700 0.48460 -0.00410 -0.00910 0.08690  329 GLU A CB    
2457 C  CG    . GLU A 333 ? 0.48760 0.63910 0.59390 0.00480  -0.00330 0.08300  329 GLU A CG    
2458 C  CD    . GLU A 333 ? 0.62390 0.78680 0.74360 0.01040  0.00110  0.08580  329 GLU A CD    
2459 O  OE1   . GLU A 333 ? 0.60620 0.78150 0.73790 0.00990  -0.00130 0.09220  329 GLU A OE1   
2460 O  OE2   . GLU A 333 ? 0.68260 0.84260 0.80090 0.01540  0.00720  0.08150  329 GLU A OE2   
2461 N  N     . THR A 334 ? 0.29240 0.45670 0.38840 -0.02400 -0.01760 0.08960  330 THR A N     
2462 C  CA    . THR A 334 ? 0.27160 0.44240 0.36760 -0.03250 -0.02380 0.09290  330 THR A CA    
2463 C  C     . THR A 334 ? 0.28220 0.46230 0.38430 -0.03700 -0.02320 0.09550  330 THR A C     
2464 O  O     . THR A 334 ? 0.22910 0.42190 0.34030 -0.04060 -0.02710 0.10130  330 THR A O     
2465 C  CB    . THR A 334 ? 0.33770 0.49670 0.41880 -0.03840 -0.02660 0.08790  330 THR A CB    
2466 O  OG1   . THR A 334 ? 0.33570 0.48690 0.41170 -0.03460 -0.02710 0.08610  330 THR A OG1   
2467 C  CG2   . THR A 334 ? 0.22710 0.39240 0.30710 -0.04760 -0.03300 0.09040  330 THR A CG2   
2468 N  N     . LEU A 335 ? 0.34910 0.52360 0.44650 -0.03720 -0.01870 0.09170  331 LEU A N     
2469 C  CA    . LEU A 335 ? 0.30500 0.48810 0.40820 -0.04190 -0.01810 0.09450  331 LEU A CA    
2470 C  C     . LEU A 335 ? 0.30370 0.50220 0.42260 -0.03730 -0.01570 0.10050  331 LEU A C     
2471 O  O     . LEU A 335 ? 0.30170 0.51250 0.42960 -0.04210 -0.01850 0.10580  331 LEU A O     
2472 C  CB    . LEU A 335 ? 0.28350 0.45720 0.37860 -0.04250 -0.01350 0.08980  331 LEU A CB    
2473 C  CG    . LEU A 335 ? 0.27840 0.43930 0.36030 -0.04900 -0.01630 0.08480  331 LEU A CG    
2474 C  CD1   . LEU A 335 ? 0.26670 0.41660 0.34060 -0.04680 -0.01130 0.08010  331 LEU A CD1   
2475 C  CD2   . LEU A 335 ? 0.24720 0.41350 0.33110 -0.05880 -0.02100 0.08720  331 LEU A CD2   
2476 N  N     . LYS A 336 ? 0.31280 0.51090 0.43570 -0.02800 -0.01070 0.09970  332 LYS A N     
2477 C  CA    . LYS A 336 ? 0.27700 0.48980 0.41550 -0.02300 -0.00810 0.10520  332 LYS A CA    
2478 C  C     . LYS A 336 ? 0.30870 0.53260 0.45730 -0.02510 -0.01430 0.11170  332 LYS A C     
2479 O  O     . LYS A 336 ? 0.25760 0.49660 0.41900 -0.02680 -0.01520 0.11790  332 LYS A O     
2480 C  CB    . LYS A 336 ? 0.32130 0.53020 0.46160 -0.01240 -0.00200 0.10230  332 LYS A CB    
2481 C  CG    . LYS A 336 ? 0.43290 0.63260 0.56360 -0.01020 0.00410  0.09630  332 LYS A CG    
2482 C  CD    . LYS A 336 ? 0.53040 0.72950 0.66480 -0.00010 0.01070  0.09370  332 LYS A CD    
2483 C  CE    . LYS A 336 ? 0.66150 0.84700 0.78810 0.00450  0.01020  0.08870  332 LYS A CE    
2484 N  NZ    . LYS A 336 ? 0.74270 0.92430 0.86860 0.01300  0.01710  0.08400  332 LYS A NZ    
2485 N  N     . ALA A 337 ? 0.31710 0.53450 0.46040 -0.02530 -0.01880 0.11100  333 ALA A N     
2486 C  CA    . ALA A 337 ? 0.30400 0.53190 0.45590 -0.02770 -0.02520 0.11760  333 ALA A CA    
2487 C  C     . ALA A 337 ? 0.33860 0.57490 0.49130 -0.03800 -0.03070 0.12090  333 ALA A C     
2488 O  O     . ALA A 337 ? 0.34850 0.60010 0.51420 -0.03980 -0.03380 0.12800  333 ALA A O     
2489 C  CB    . ALA A 337 ? 0.27430 0.49270 0.41800 -0.02710 -0.02910 0.11600  333 ALA A CB    
2490 N  N     . LEU A 338 ? 0.31400 0.54030 0.45320 -0.04510 -0.03190 0.11580  334 LEU A N     
2491 C  CA    . LEU A 338 ? 0.30370 0.53610 0.44270 -0.05540 -0.03710 0.11790  334 LEU A CA    
2492 C  C     . LEU A 338 ? 0.35180 0.59700 0.50310 -0.05650 -0.03450 0.12220  334 LEU A C     
2493 O  O     . LEU A 338 ? 0.27410 0.53200 0.43380 -0.06270 -0.03940 0.12780  334 LEU A O     
2494 C  CB    . LEU A 338 ? 0.33100 0.54880 0.45360 -0.06190 -0.03800 0.11070  334 LEU A CB    
2495 C  CG    . LEU A 338 ? 0.38580 0.59350 0.49610 -0.06360 -0.04200 0.10710  334 LEU A CG    
2496 C  CD1   . LEU A 338 ? 0.28680 0.47800 0.38160 -0.06650 -0.04020 0.09900  334 LEU A CD1   
2497 C  CD2   . LEU A 338 ? 0.47300 0.68990 0.58490 -0.07120 -0.05020 0.11130  334 LEU A CD2   
2498 N  N     . ILE A 339 ? 0.35380 0.59620 0.50620 -0.05090 -0.02700 0.12000  335 ILE A N     
2499 C  CA    . ILE A 339 ? 0.31710 0.57250 0.48150 -0.05160 -0.02390 0.12450  335 ILE A CA    
2500 C  C     . ILE A 339 ? 0.34710 0.62000 0.52910 -0.04740 -0.02460 0.13220  335 ILE A C     
2501 O  O     . ILE A 339 ? 0.32260 0.61020 0.51600 -0.05230 -0.02720 0.13830  335 ILE A O     
2502 C  CB    . ILE A 339 ? 0.31150 0.56080 0.47270 -0.04560 -0.01530 0.12060  335 ILE A CB    
2503 C  CG1   . ILE A 339 ? 0.27810 0.51200 0.42380 -0.05060 -0.01480 0.11430  335 ILE A CG1   
2504 C  CG2   . ILE A 339 ? 0.26560 0.53060 0.44090 -0.04440 -0.01100 0.12610  335 ILE A CG2   
2505 C  CD1   . ILE A 339 ? 0.23200 0.45710 0.37140 -0.04400 -0.00710 0.10950  335 ILE A CD1   
2506 N  N     . LEU A 340 ? 0.38420 0.65590 0.56940 -0.03860 -0.02290 0.13220  336 LEU A N     
2507 C  CA    . LEU A 340 ? 0.35960 0.64700 0.56260 -0.03330 -0.02310 0.13950  336 LEU A CA    
2508 C  C     . LEU A 340 ? 0.36290 0.66140 0.57220 -0.04070 -0.03210 0.14610  336 LEU A C     
2509 O  O     . LEU A 340 ? 0.42260 0.73840 0.64780 -0.04140 -0.03340 0.15350  336 LEU A O     
2510 C  CB    . LEU A 340 ? 0.35260 0.63340 0.55610 -0.02310 -0.02040 0.13760  336 LEU A CB    
2511 C  CG    . LEU A 340 ? 0.55260 0.84610 0.77430 -0.01380 -0.01670 0.14270  336 LEU A CG    
2512 C  CD1   . LEU A 340 ? 0.62500 0.91810 0.84850 -0.00730 -0.00710 0.13900  336 LEU A CD1   
2513 C  CD2   . LEU A 340 ? 0.57650 0.86390 0.79930 -0.00710 -0.01820 0.14280  336 LEU A CD2   
2514 N  N     . CYS A 341 ? 0.35260 0.64190 0.54930 -0.04680 -0.03830 0.14350  337 CYS A N     
2515 C  CA    . CYS A 341 ? 0.36950 0.66840 0.56960 -0.05430 -0.04740 0.14920  337 CYS A CA    
2516 C  C     . CYS A 341 ? 0.41770 0.72510 0.62030 -0.06460 -0.05070 0.15140  337 CYS A C     
2517 O  O     . CYS A 341 ? 0.38470 0.70900 0.60080 -0.06800 -0.05510 0.15910  337 CYS A O     
2518 C  CB    . CYS A 341 ? 0.41340 0.69900 0.59730 -0.05790 -0.05230 0.14470  337 CYS A CB    
2519 S  SG    . CYS A 341 ? 0.50040 0.79550 0.68350 -0.06850 -0.06370 0.15000  337 CYS A SG    
2520 N  N     . ILE A 342 ? 0.39050 0.68660 0.58110 -0.06960 -0.04860 0.14500  338 ILE A N     
2521 C  CA    . ILE A 342 ? 0.40510 0.70720 0.59710 -0.08010 -0.05220 0.14650  338 ILE A CA    
2522 C  C     . ILE A 342 ? 0.37700 0.69530 0.58640 -0.07830 -0.04830 0.15290  338 ILE A C     
2523 O  O     . ILE A 342 ? 0.44550 0.77770 0.66470 -0.08560 -0.05320 0.15880  338 ILE A O     
2524 C  CB    . ILE A 342 ? 0.43700 0.72160 0.61230 -0.08520 -0.05050 0.13810  338 ILE A CB    
2525 C  CG1   . ILE A 342 ? 0.56460 0.83680 0.72420 -0.08960 -0.05590 0.13280  338 ILE A CG1   
2526 C  CG2   . ILE A 342 ? 0.40850 0.69830 0.58710 -0.09480 -0.05240 0.13970  338 ILE A CG2   
2527 C  CD1   . ILE A 342 ? 0.59150 0.84420 0.73460 -0.09100 -0.05290 0.12380  338 ILE A CD1   
2528 N  N     . ARG A 343 ? 0.38510 0.70270 0.59890 -0.06880 -0.03970 0.15190  339 ARG A N     
2529 C  CA    . ARG A 343 ? 0.35010 0.68370 0.58040 -0.06640 -0.03510 0.15780  339 ARG A CA    
2530 C  C     . ARG A 343 ? 0.44780 0.80050 0.69640 -0.06400 -0.03850 0.16670  339 ARG A C     
2531 O  O     . ARG A 343 ? 0.46380 0.83250 0.72490 -0.06980 -0.04170 0.17340  339 ARG A O     
2532 C  CB    . ARG A 343 ? 0.34510 0.67370 0.57480 -0.05610 -0.02480 0.15430  339 ARG A CB    
2533 C  CG    . ARG A 343 ? 0.50020 0.81840 0.71910 -0.05970 -0.02060 0.14920  339 ARG A CG    
2534 C  CD    . ARG A 343 ? 0.55800 0.88210 0.78370 -0.05280 -0.01110 0.14990  339 ARG A CD    
2535 N  NE    . ARG A 343 ? 0.64060 0.95590 0.85640 -0.05780 -0.00820 0.14640  339 ARG A NE    
2536 C  CZ    . ARG A 343 ? 0.61200 0.91260 0.81480 -0.05350 -0.00310 0.13970  339 ARG A CZ    
2537 N  NH1   . ARG A 343 ? 0.56950 0.86230 0.76740 -0.04440 -0.00000 0.13540  339 ARG A NH1   
2538 N  NH2   . ARG A 343 ? 0.57460 0.86820 0.76960 -0.05860 -0.00110 0.13770  339 ARG A NH2   
2539 N  N     . SER A 344 ? 0.50500 0.85670 0.75640 -0.05520 -0.03790 0.16720  340 SER A N     
2540 C  CA    . SER A 344 ? 0.50880 0.87780 0.77760 -0.05270 -0.04190 0.17610  340 SER A CA    
2541 C  C     . SER A 344 ? 0.47270 0.85100 0.74330 -0.06440 -0.05230 0.18130  340 SER A C     
2542 O  O     . SER A 344 ? 0.52130 0.91870 0.80920 -0.06570 -0.05560 0.19000  340 SER A O     
2543 C  CB    . SER A 344 ? 0.53090 0.89310 0.79870 -0.04360 -0.04160 0.17520  340 SER A CB    
2544 O  OG    . SER A 344 ? 0.62230 0.97670 0.87830 -0.04940 -0.04960 0.17400  340 SER A OG    
2545 N  N     . SER A 345 ? 0.48670 0.85200 0.73980 -0.07280 -0.05750 0.17580  341 SER A N     
2546 C  CA    . SER A 345 ? 0.49930 0.87180 0.75160 -0.08490 -0.06730 0.17920  341 SER A CA    
2547 C  C     . SER A 345 ? 0.61510 1.00280 0.88010 -0.09160 -0.06800 0.18440  341 SER A C     
2548 O  O     . SER A 345 ? 0.65170 1.05590 0.92840 -0.09730 -0.07500 0.19200  341 SER A O     
2549 C  CB    . SER A 345 ? 0.56820 0.92230 0.79860 -0.09260 -0.07050 0.17050  341 SER A CB    
2550 O  OG    . SER A 345 ? 0.61810 0.97640 0.84670 -0.10510 -0.07670 0.17110  341 SER A OG    
2551 N  N     . GLY A 346 ? 0.60840 0.99060 0.87080 -0.09190 -0.06140 0.18060  342 GLY A N     
2552 C  CA    . GLY A 346 ? 0.58900 0.98240 0.86020 -0.10010 -0.06250 0.18460  342 GLY A CA    
2553 C  C     . GLY A 346 ? 0.62300 1.00920 0.88250 -0.11380 -0.07000 0.18120  342 GLY A C     
2554 O  O     . GLY A 346 ? 0.58620 0.98040 0.85240 -0.12190 -0.07160 0.18420  342 GLY A O     
2555 N  N     . LYS A 347 ? 0.65500 1.02600 0.89710 -0.11660 -0.07430 0.17470  343 LYS A N     
2556 C  CA    . LYS A 347 ? 0.71820 1.08130 0.94800 -0.12930 -0.08150 0.17040  343 LYS A CA    
2557 C  C     . LYS A 347 ? 0.72800 1.07330 0.94500 -0.13210 -0.07680 0.16220  343 LYS A C     
2558 O  O     . LYS A 347 ? 0.68670 1.03550 0.91070 -0.13380 -0.07280 0.16400  343 LYS A O     
2559 C  CB    . LYS A 347 ? 0.70100 1.05650 0.91780 -0.13070 -0.08770 0.16690  343 LYS A CB    
2560 C  CG    . LYS A 347 ? 0.72740 1.09990 0.95560 -0.12960 -0.09390 0.17540  343 LYS A CG    
2561 C  CD    . LYS A 347 ? 0.75510 1.12070 0.96900 -0.13390 -0.10110 0.17220  343 LYS A CD    
2562 C  CE    . LYS A 347 ? 0.81540 1.19010 1.02900 -0.14740 -0.11120 0.17450  343 LYS A CE    
2563 N  NZ    . LYS A 347 ? 0.87910 1.27370 1.10820 -0.14610 -0.11610 0.18510  343 LYS A NZ    
2564 N  N     . GLY A 375 ? 0.59660 0.44560 0.68160 -0.05130 0.00110  0.13170  371 GLY A N     
2565 C  CA    . GLY A 375 ? 0.67310 0.53880 0.74670 -0.05190 0.00150  0.13230  371 GLY A CA    
2566 C  C     . GLY A 375 ? 0.72260 0.59330 0.79440 -0.05880 0.00190  0.13270  371 GLY A C     
2567 O  O     . GLY A 375 ? 0.77030 0.63260 0.85010 -0.06380 0.00130  0.13570  371 GLY A O     
2568 N  N     . ILE A 376 ? 0.63930 0.52390 0.70130 -0.05900 0.00290  0.13030  372 ILE A N     
2569 C  CA    . ILE A 376 ? 0.49090 0.38160 0.55120 -0.06510 0.00340  0.12990  372 ILE A CA    
2570 C  C     . ILE A 376 ? 0.44280 0.32850 0.50090 -0.06610 0.00390  0.11730  372 ILE A C     
2571 O  O     . ILE A 376 ? 0.45250 0.33940 0.50440 -0.06150 0.00460  0.10930  372 ILE A O     
2572 C  CB    . ILE A 376 ? 0.52750 0.43630 0.57920 -0.06460 0.00450  0.13410  372 ILE A CB    
2573 C  CG1   . ILE A 376 ? 0.50060 0.41560 0.55200 -0.06250 0.00400  0.14550  372 ILE A CG1   
2574 C  CG2   . ILE A 376 ? 0.52900 0.44480 0.58150 -0.07110 0.00510  0.13610  372 ILE A CG2   
2575 C  CD1   . ILE A 376 ? 0.42810 0.36070 0.47070 -0.06260 0.00540  0.14960  372 ILE A CD1   
2576 N  N     . HIS A 377 ? 0.43050 0.31120 0.49330 -0.07240 0.00340  0.11570  373 HIS A N     
2577 C  CA    . HIS A 377 ? 0.43910 0.31660 0.49890 -0.07410 0.00350  0.10410  373 HIS A CA    
2578 C  C     . HIS A 377 ? 0.45620 0.34920 0.50670 -0.07310 0.00450  0.10150  373 HIS A C     
2579 O  O     . HIS A 377 ? 0.52120 0.42580 0.57080 -0.07580 0.00480  0.10810  373 HIS A O     
2580 C  CB    . HIS A 377 ? 0.51910 0.38900 0.58560 -0.08180 0.00230  0.10340  373 HIS A CB    
2581 C  CG    . HIS A 377 ? 0.56020 0.42340 0.62430 -0.08360 0.00200  0.09110  373 HIS A CG    
2582 N  ND1   . HIS A 377 ? 0.54560 0.41900 0.60250 -0.08480 0.00210  0.08550  373 HIS A ND1   
2583 C  CD2   . HIS A 377 ? 0.56830 0.41600 0.63600 -0.08430 0.00160  0.08340  373 HIS A CD2   
2584 C  CE1   . HIS A 377 ? 0.54890 0.41380 0.60460 -0.08650 0.00160  0.07520  373 HIS A CE1   
2585 N  NE2   . HIS A 377 ? 0.57840 0.42760 0.64010 -0.08620 0.00140  0.07330  373 HIS A NE2   
2586 N  N     . PRO A 378 ? 0.43180 0.32550 0.47570 -0.06930 0.00510  0.09210  374 PRO A N     
2587 C  CA    . PRO A 378 ? 0.47080 0.37900 0.50630 -0.06750 0.00600  0.09010  374 PRO A CA    
2588 C  C     . PRO A 378 ? 0.51520 0.43180 0.55120 -0.07330 0.00580  0.09100  374 PRO A C     
2589 O  O     . PRO A 378 ? 0.48880 0.41910 0.52050 -0.07240 0.00690  0.09400  374 PRO A O     
2590 C  CB    . PRO A 378 ? 0.45650 0.36060 0.48690 -0.06360 0.00630  0.07950  374 PRO A CB    
2591 C  CG    . PRO A 378 ? 0.46500 0.35580 0.49990 -0.06070 0.00620  0.07840  374 PRO A CG    
2592 C  CD    . PRO A 378 ? 0.50740 0.38930 0.55130 -0.06600 0.00520  0.08340  374 PRO A CD    
2593 N  N     . ALA A 379 ? 0.53290 0.44200 0.57410 -0.07930 0.00450  0.08860  375 ALA A N     
2594 C  CA    . ALA A 379 ? 0.50080 0.41880 0.54370 -0.08530 0.00390  0.09050  375 ALA A CA    
2595 C  C     . ALA A 379 ? 0.48640 0.41360 0.53290 -0.08740 0.00470  0.10210  375 ALA A C     
2596 O  O     . ALA A 379 ? 0.44260 0.38290 0.48830 -0.08960 0.00540  0.10500  375 ALA A O     
2597 C  CB    . ALA A 379 ? 0.48910 0.39640 0.53720 -0.09190 0.00190  0.08590  375 ALA A CB    
2598 N  N     . MET A 380 ? 0.46310 0.38410 0.51390 -0.08660 0.00470  0.10920  376 MET A N     
2599 C  CA    . MET A 380 ? 0.47670 0.40710 0.53000 -0.08830 0.00560  0.12090  376 MET A CA    
2600 C  C     . MET A 380 ? 0.46140 0.40600 0.50650 -0.08270 0.00780  0.12310  376 MET A C     
2601 O  O     . MET A 380 ? 0.44330 0.40090 0.48780 -0.08430 0.00930  0.13010  376 MET A O     
2602 C  CB    . MET A 380 ? 0.44830 0.36810 0.50850 -0.08890 0.00470  0.12830  376 MET A CB    
2603 C  CG    . MET A 380 ? 0.68560 0.59210 0.75540 -0.09550 0.00270  0.12820  376 MET A CG    
2604 S  SD    . MET A 380 ? 0.93060 0.84650 1.00650 -0.10460 0.00240  0.13540  376 MET A SD    
2605 C  CE    . MET A 380 ? 0.86620 0.80470 0.93490 -0.10140 0.00530  0.14250  376 MET A CE    
2606 N  N     . VAL A 381 ? 0.38690 0.32910 0.42560 -0.07630 0.00810  0.11730  377 VAL A N     
2607 C  CA    . VAL A 381 ? 0.46970 0.42450 0.49990 -0.07110 0.00990  0.11760  377 VAL A CA    
2608 C  C     . VAL A 381 ? 0.47070 0.43750 0.49770 -0.07230 0.01120  0.11430  377 VAL A C     
2609 O  O     . VAL A 381 ? 0.44540 0.42560 0.46960 -0.07180 0.01320  0.11910  377 VAL A O     
2610 C  CB    . VAL A 381 ? 0.43820 0.38740 0.46310 -0.06460 0.00950  0.11100  377 VAL A CB    
2611 C  CG1   . VAL A 381 ? 0.39650 0.35820 0.41250 -0.05980 0.01110  0.11010  377 VAL A CG1   
2612 C  CG2   . VAL A 381 ? 0.48190 0.42080 0.51080 -0.06280 0.00830  0.11530  377 VAL A CG2   
2613 N  N     . VAL A 382 ? 0.48570 0.44820 0.51320 -0.07380 0.01010  0.10600  378 VAL A N     
2614 C  CA    . VAL A 382 ? 0.41610 0.38980 0.44150 -0.07480 0.01090  0.10280  378 VAL A CA    
2615 C  C     . VAL A 382 ? 0.38450 0.36710 0.41580 -0.08060 0.01150  0.11020  378 VAL A C     
2616 O  O     . VAL A 382 ? 0.38840 0.38500 0.41790 -0.07990 0.01350  0.11220  378 VAL A O     
2617 C  CB    . VAL A 382 ? 0.33230 0.29910 0.35720 -0.07580 0.00920  0.09310  378 VAL A CB    
2618 C  CG1   . VAL A 382 ? 0.34540 0.32430 0.36910 -0.07680 0.00960  0.09060  378 VAL A CG1   
2619 C  CG2   . VAL A 382 ? 0.35040 0.30990 0.36950 -0.06980 0.00900  0.08630  378 VAL A CG2   
2620 N  N     . GLU A 383 ? 0.37810 0.35290 0.41700 -0.08650 0.01000  0.11440  379 GLU A N     
2621 C  CA    . GLU A 383 ? 0.43800 0.42200 0.48320 -0.09240 0.01050  0.12230  379 GLU A CA    
2622 C  C     . GLU A 383 ? 0.48600 0.48220 0.52880 -0.09000 0.01350  0.13120  379 GLU A C     
2623 O  O     . GLU A 383 ? 0.41000 0.42040 0.45400 -0.09170 0.01550  0.13540  379 GLU A O     
2624 C  CB    . GLU A 383 ? 0.48590 0.45860 0.54010 -0.09930 0.00820  0.12580  379 GLU A CB    
2625 C  CG    . GLU A 383 ? 0.60650 0.58970 0.66780 -0.10580 0.00880  0.13450  379 GLU A CG    
2626 C  CD    . GLU A 383 ? 0.80640 0.77850 0.87730 -0.11310 0.00640  0.13910  379 GLU A CD    
2627 O  OE1   . GLU A 383 ? 0.87970 0.83710 0.95220 -0.11220 0.00500  0.13870  379 GLU A OE1   
2628 O  OE2   . GLU A 383 ? 0.91560 0.89400 0.99330 -0.11980 0.00580  0.14330  379 GLU A OE2   
2629 N  N     . ALA A 384 ? 0.41850 0.40980 0.45820 -0.08620 0.01370  0.13430  380 ALA A N     
2630 C  CA    . ALA A 384 ? 0.44700 0.45020 0.48300 -0.08400 0.01640  0.14250  380 ALA A CA    
2631 C  C     . ALA A 384 ? 0.40200 0.41820 0.42980 -0.07890 0.01900  0.13810  380 ALA A C     
2632 O  O     . ALA A 384 ? 0.38390 0.41440 0.41060 -0.07930 0.02190  0.14320  380 ALA A O     
2633 C  CB    . ALA A 384 ? 0.42100 0.41640 0.45480 -0.08070 0.01550  0.14610  380 ALA A CB    
2634 N  N     . MET A 385 ? 0.35040 0.36190 0.37290 -0.07420 0.01830  0.12860  381 MET A N     
2635 C  CA    . MET A 385 ? 0.43890 0.46140 0.45500 -0.06980 0.02050  0.12370  381 MET A CA    
2636 C  C     . MET A 385 ? 0.44400 0.47700 0.46480 -0.07340 0.02180  0.12420  381 MET A C     
2637 O  O     . MET A 385 ? 0.43870 0.48540 0.45700 -0.07130 0.02490  0.12570  381 MET A O     
2638 C  CB    . MET A 385 ? 0.34830 0.36300 0.35990 -0.06540 0.01900  0.11340  381 MET A CB    
2639 C  CG    . MET A 385 ? 0.43720 0.44380 0.44390 -0.06100 0.01800  0.11250  381 MET A CG    
2640 S  SD    . MET A 385 ? 0.46390 0.45910 0.46780 -0.05750 0.01590  0.10120  381 MET A SD    
2641 C  CE    . MET A 385 ? 0.47160 0.47880 0.46970 -0.05370 0.01780  0.09540  381 MET A CE    
2642 N  N     . GLN A 386 ? 0.45570 0.48250 0.48320 -0.07850 0.01930  0.12220  382 GLN A N     
2643 C  CA    . GLN A 386 ? 0.48420 0.52190 0.51720 -0.08230 0.02010  0.12350  382 GLN A CA    
2644 C  C     . GLN A 386 ? 0.55110 0.60010 0.58800 -0.08550 0.02270  0.13360  382 GLN A C     
2645 O  O     . GLN A 386 ? 0.65090 0.71330 0.69080 -0.08660 0.02480  0.13550  382 GLN A O     
2646 C  CB    . GLN A 386 ? 0.48180 0.51070 0.52160 -0.08850 0.01650  0.12070  382 GLN A CB    
2647 C  CG    . GLN A 386 ? 0.42310 0.46160 0.46680 -0.09110 0.01610  0.11810  382 GLN A CG    
2648 C  CD    . GLN A 386 ? 0.50210 0.53900 0.54060 -0.08680 0.01510  0.10840  382 GLN A CD    
2649 O  OE1   . GLN A 386 ? 0.46460 0.48920 0.50140 -0.08740 0.01220  0.10200  382 GLN A OE1   
2650 N  NE2   . GLN A 386 ? 0.53740 0.58730 0.57380 -0.08260 0.01750  0.10750  382 GLN A NE2   
2651 N  N     . ASN A 387 ? 0.57750 0.62100 0.61600 -0.08760 0.02230  0.14060  383 ASN A N     
2652 C  CA    . ASN A 387 ? 0.47040 0.52310 0.51330 -0.09160 0.02440  0.15160  383 ASN A CA    
2653 C  C     . ASN A 387 ? 0.60670 0.67240 0.64190 -0.08660 0.02860  0.15560  383 ASN A C     
2654 O  O     . ASN A 387 ? 0.74170 0.81580 0.77880 -0.08920 0.03080  0.16480  383 ASN A O     
2655 C  CB    . ASN A 387 ? 0.45790 0.49880 0.50640 -0.09640 0.02200  0.15850  383 ASN A CB    
2656 C  CG    . ASN A 387 ? 0.50270 0.53630 0.56140 -0.10390 0.01880  0.15790  383 ASN A CG    
2657 O  OD1   . ASN A 387 ? 0.58880 0.62890 0.65030 -0.10610 0.01870  0.15420  383 ASN A OD1   
2658 N  ND2   . ASN A 387 ? 0.62190 0.64230 0.68600 -0.10800 0.01630  0.16180  383 ASN A ND2   
2659 N  N     . ARG A 388 ? 0.42270 0.48910 0.44860 -0.07960 0.02970  0.14900  384 ARG A N     
2660 C  CA    . ARG A 388 ? 0.47670 0.55520 0.49390 -0.07470 0.03370  0.15140  384 ARG A CA    
2661 C  C     . ARG A 388 ? 0.53360 0.61950 0.54480 -0.06870 0.03590  0.14300  384 ARG A C     
2662 O  O     . ARG A 388 ? 0.51500 0.61400 0.52220 -0.06630 0.04000  0.14490  384 ARG A O     
2663 C  CB    . ARG A 388 ? 0.55910 0.63000 0.56970 -0.07180 0.03230  0.15320  384 ARG A CB    
2664 C  CG    . ARG A 388 ? 0.65130 0.73550 0.65350 -0.06890 0.03620  0.15870  384 ARG A CG    
2665 C  CD    . ARG A 388 ? 0.67340 0.75150 0.67310 -0.06960 0.03420  0.16590  384 ARG A CD    
2666 N  NE    . ARG A 388 ? 0.64040 0.71540 0.64960 -0.07620 0.03290  0.17560  384 ARG A NE    
2667 C  CZ    . ARG A 388 ? 0.71510 0.80240 0.72730 -0.08020 0.03590  0.18460  384 ARG A CZ    
2668 N  NH1   . ARG A 388 ? 0.69550 0.79890 0.70150 -0.07770 0.04050  0.18450  384 ARG A NH1   
2669 N  NH2   . ARG A 388 ? 0.80130 0.88500 0.82280 -0.08670 0.03440  0.19370  384 ARG A NH2   
2670 N  N     . LEU A 389 ? 0.43940 0.51660 0.44990 -0.06620 0.03350  0.13370  385 LEU A N     
2671 C  CA    . LEU A 389 ? 0.43080 0.51340 0.43470 -0.05990 0.03540  0.12600  385 LEU A CA    
2672 C  C     . LEU A 389 ? 0.45470 0.55160 0.46280 -0.06010 0.03870  0.12630  385 LEU A C     
2673 O  O     . LEU A 389 ? 0.38240 0.48040 0.39930 -0.06470 0.03740  0.12750  385 LEU A O     
2674 C  CB    . LEU A 389 ? 0.34700 0.41720 0.34960 -0.05780 0.03190  0.11710  385 LEU A CB    
2675 C  CG    . LEU A 389 ? 0.46430 0.52100 0.46230 -0.05600 0.02910  0.11540  385 LEU A CG    
2676 C  CD1   . LEU A 389 ? 0.53160 0.57620 0.52970 -0.05470 0.02580  0.10690  385 LEU A CD1   
2677 C  CD2   . LEU A 389 ? 0.44530 0.50620 0.43390 -0.05080 0.03100  0.11550  385 LEU A CD2   
2678 N  N     . PRO A 390 ? 0.40500 0.51300 0.40750 -0.05510 0.04290  0.12500  386 PRO A N     
2679 C  CA    . PRO A 390 ? 0.39710 0.51870 0.40430 -0.05430 0.04630  0.12460  386 PRO A CA    
2680 C  C     . PRO A 390 ? 0.45500 0.57270 0.46710 -0.05380 0.04370  0.11780  386 PRO A C     
2681 O  O     . PRO A 390 ? 0.43450 0.53980 0.44360 -0.05230 0.04010  0.11170  386 PRO A O     
2682 C  CB    . PRO A 390 ? 0.40650 0.53690 0.40470 -0.04780 0.05090  0.12190  386 PRO A CB    
2683 C  CG    . PRO A 390 ? 0.45390 0.57990 0.44410 -0.04780 0.05040  0.12540  386 PRO A CG    
2684 C  CD    . PRO A 390 ? 0.46430 0.57330 0.45610 -0.05030 0.04470  0.12400  386 PRO A CD    
2685 N  N     . ALA A 391 ? 0.48660 0.61570 0.50660 -0.05520 0.04550  0.11950  387 ALA A N     
2686 C  CA    . ALA A 391 ? 0.54030 0.66730 0.56600 -0.05570 0.04270  0.11460  387 ALA A CA    
2687 C  C     . ALA A 391 ? 0.48860 0.61280 0.50850 -0.04860 0.04280  0.10600  387 ALA A C     
2688 O  O     . ALA A 391 ? 0.52500 0.64130 0.54590 -0.04860 0.03910  0.10080  387 ALA A O     
2689 C  CB    . ALA A 391 ? 0.53860 0.68050 0.57480 -0.05840 0.04480  0.11900  387 ALA A CB    
2690 N  N     . ASP A 392 ? 0.50560 0.63580 0.51900 -0.04280 0.04700  0.10440  388 ASP A N     
2691 C  CA    . ASP A 392 ? 0.50350 0.63080 0.51150 -0.03610 0.04740  0.09640  388 ASP A CA    
2692 C  C     . ASP A 392 ? 0.44700 0.56010 0.44580 -0.03420 0.04440  0.09180  388 ASP A C     
2693 O  O     . ASP A 392 ? 0.37280 0.48340 0.36610 -0.02870 0.04490  0.08560  388 ASP A O     
2694 C  CB    . ASP A 392 ? 0.42940 0.56930 0.43480 -0.03060 0.05330  0.09560  388 ASP A CB    
2695 C  CG    . ASP A 392 ? 0.61300 0.75600 0.61050 -0.03020 0.05650  0.09920  388 ASP A CG    
2696 O  OD1   . ASP A 392 ? 0.63560 0.77460 0.63280 -0.03520 0.05460  0.10490  388 ASP A OD1   
2697 O  OD2   . ASP A 392 ? 0.69240 0.84190 0.68390 -0.02490 0.06080  0.09630  388 ASP A OD2   
2698 N  N     . THR A 393 ? 0.37730 0.48110 0.37520 -0.03850 0.04130  0.09480  389 THR A N     
2699 C  CA    . THR A 393 ? 0.34810 0.43930 0.33840 -0.03650 0.03870  0.09100  389 THR A CA    
2700 C  C     . THR A 393 ? 0.38530 0.46790 0.37590 -0.03480 0.03540  0.08380  389 THR A C     
2701 O  O     . THR A 393 ? 0.46330 0.54460 0.46040 -0.03800 0.03320  0.08330  389 THR A O     
2702 C  CB    . THR A 393 ? 0.35740 0.44030 0.34840 -0.04140 0.03610  0.09600  389 THR A CB    
2703 O  OG1   . THR A 393 ? 0.33190 0.42280 0.32240 -0.04330 0.03900  0.10370  389 THR A OG1   
2704 C  CG2   . THR A 393 ? 0.34620 0.41690 0.33020 -0.03890 0.03350  0.09220  389 THR A CG2   
2705 N  N     . ILE A 394 ? 0.34220 0.41940 0.32540 -0.02990 0.03500  0.07830  390 ILE A N     
2706 C  CA    . ILE A 394 ? 0.37910 0.44670 0.36160 -0.02850 0.03170  0.07200  390 ILE A CA    
2707 C  C     . ILE A 394 ? 0.38100 0.43650 0.36060 -0.03030 0.02860  0.07210  390 ILE A C     
2708 O  O     . ILE A 394 ? 0.36480 0.41810 0.33840 -0.02840 0.02900  0.07290  390 ILE A O     
2709 C  CB    . ILE A 394 ? 0.34130 0.41000 0.31880 -0.02230 0.03290  0.06600  390 ILE A CB    
2710 C  CG1   . ILE A 394 ? 0.36100 0.44180 0.34240 -0.01980 0.03640  0.06590  390 ILE A CG1   
2711 C  CG2   . ILE A 394 ? 0.26580 0.32460 0.24280 -0.02120 0.02930  0.06030  390 ILE A CG2   
2712 C  CD1   . ILE A 394 ? 0.39480 0.47750 0.37070 -0.01340 0.03870  0.06070  390 ILE A CD1   
2713 N  N     . LEU A 395 ? 0.32080 0.36880 0.30460 -0.03420 0.02550  0.07140  391 LEU A N     
2714 C  CA    . LEU A 395 ? 0.34640 0.38260 0.32890 -0.03600 0.02290  0.07140  391 LEU A CA    
2715 C  C     . LEU A 395 ? 0.34650 0.37430 0.32600 -0.03330 0.02070  0.06450  391 LEU A C     
2716 O  O     . LEU A 395 ? 0.38130 0.40780 0.36350 -0.03450 0.01920  0.06110  391 LEU A O     
2717 C  CB    . LEU A 395 ? 0.34130 0.37400 0.33040 -0.04230 0.02130  0.07480  391 LEU A CB    
2718 C  CG    . LEU A 395 ? 0.36160 0.38110 0.35080 -0.04420 0.01870  0.07420  391 LEU A CG    
2719 C  CD1   . LEU A 395 ? 0.37900 0.39640 0.36540 -0.04290 0.01940  0.07870  391 LEU A CD1   
2720 C  CD2   . LEU A 395 ? 0.38470 0.40030 0.38070 -0.05060 0.01690  0.07600  391 LEU A CD2   
2721 N  N     . PHE A 396 ? 0.30710 0.33000 0.28120 -0.03000 0.02030  0.06290  392 PHE A N     
2722 C  CA    . PHE A 396 ? 0.36420 0.37860 0.33580 -0.02780 0.01830  0.05720  392 PHE A CA    
2723 C  C     . PHE A 396 ? 0.39310 0.39720 0.36690 -0.03070 0.01630  0.05800  392 PHE A C     
2724 O  O     . PHE A 396 ? 0.33670 0.33900 0.31110 -0.03190 0.01640  0.06280  392 PHE A O     
2725 C  CB    . PHE A 396 ? 0.34120 0.35570 0.30640 -0.02290 0.01870  0.05510  392 PHE A CB    
2726 C  CG    . PHE A 396 ? 0.33960 0.36140 0.30280 -0.01940 0.02030  0.05190  392 PHE A CG    
2727 C  CD1   . PHE A 396 ? 0.25570 0.28750 0.21900 -0.01890 0.02320  0.05470  392 PHE A CD1   
2728 C  CD2   . PHE A 396 ? 0.31730 0.33580 0.27890 -0.01660 0.01920  0.04640  392 PHE A CD2   
2729 C  CE1   . PHE A 396 ? 0.25950 0.29740 0.22150 -0.01520 0.02500  0.05140  392 PHE A CE1   
2730 C  CE2   . PHE A 396 ? 0.33890 0.36320 0.29950 -0.01340 0.02060  0.04370  392 PHE A CE2   
2731 C  CZ    . PHE A 396 ? 0.27720 0.31100 0.23820 -0.01250 0.02360  0.04590  392 PHE A CZ    
2732 N  N     . VAL A 397 ? 0.36700 0.36470 0.34220 -0.03180 0.01450  0.05360  393 VAL A N     
2733 C  CA    . VAL A 397 ? 0.28460 0.27190 0.26200 -0.03420 0.01300  0.05310  393 VAL A CA    
2734 C  C     . VAL A 397 ? 0.30450 0.28550 0.27880 -0.03100 0.01200  0.04770  393 VAL A C     
2735 O  O     . VAL A 397 ? 0.33440 0.31730 0.30690 -0.02960 0.01170  0.04340  393 VAL A O     
2736 C  CB    . VAL A 397 ? 0.37640 0.36190 0.35850 -0.03950 0.01200  0.05250  393 VAL A CB    
2737 C  CG1   . VAL A 397 ? 0.39800 0.37150 0.38200 -0.04160 0.01060  0.05040  393 VAL A CG1   
2738 C  CG2   . VAL A 397 ? 0.31780 0.31010 0.30390 -0.04300 0.01290  0.05870  393 VAL A CG2   
2739 N  N     . ASP A 398 ? 0.30090 0.27490 0.27510 -0.02970 0.01160  0.04830  394 ASP A N     
2740 C  CA    . ASP A 398 ? 0.37300 0.34170 0.34490 -0.02660 0.01090  0.04380  394 ASP A CA    
2741 C  C     . ASP A 398 ? 0.41650 0.37760 0.39070 -0.02890 0.01020  0.03950  394 ASP A C     
2742 O  O     . ASP A 398 ? 0.46890 0.42990 0.44530 -0.03290 0.00990  0.03910  394 ASP A O     
2743 C  CB    . ASP A 398 ? 0.34010 0.30590 0.31140 -0.02390 0.01060  0.04660  394 ASP A CB    
2744 C  CG    . ASP A 398 ? 0.47380 0.43860 0.44190 -0.01980 0.01000  0.04270  394 ASP A CG    
2745 O  OD1   . ASP A 398 ? 0.45900 0.41740 0.42860 -0.01930 0.00960  0.03920  394 ASP A OD1   
2746 O  OD2   . ASP A 398 ? 0.49870 0.46930 0.46290 -0.01720 0.01010  0.04310  394 ASP A OD2   
2747 N  N     . ASN A 399 ? 0.41110 0.36650 0.38450 -0.02650 0.00990  0.03600  395 ASN A N     
2748 C  CA    . ASN A 399 ? 0.46110 0.40950 0.43560 -0.02820 0.00980  0.03120  395 ASN A CA    
2749 C  C     . ASN A 399 ? 0.59040 0.52980 0.56840 -0.02750 0.01010  0.03180  395 ASN A C     
2750 O  O     . ASN A 399 ? 0.80900 0.74780 0.78730 -0.02400 0.01010  0.03390  395 ASN A O     
2751 C  CB    . ASN A 399 ? 0.40410 0.35430 0.37510 -0.02610 0.00960  0.02630  395 ASN A CB    
2752 C  CG    . ASN A 399 ? 0.44660 0.40560 0.41520 -0.02610 0.00930  0.02660  395 ASN A CG    
2753 O  OD1   . ASN A 399 ? 0.48190 0.44360 0.45110 -0.02940 0.00890  0.02610  395 ASN A OD1   
2754 N  ND2   . ASN A 399 ? 0.43520 0.39870 0.40140 -0.02250 0.00940  0.02740  395 ASN A ND2   
2755 N  N     . GLY A 400 ? 0.47380 0.40630 0.45470 -0.03080 0.01020  0.02980  396 GLY A N     
2756 C  CA    . GLY A 400 ? 0.37880 0.30240 0.36470 -0.03130 0.01050  0.03150  396 GLY A CA    
2757 C  C     . GLY A 400 ? 0.43510 0.35580 0.42420 -0.03670 0.01000  0.03240  396 GLY A C     
2758 O  O     . GLY A 400 ? 0.39220 0.31760 0.37930 -0.04000 0.00940  0.03090  396 GLY A O     
2759 N  N     . SER A 401 ? 0.37640 0.28930 0.37090 -0.03780 0.01010  0.03530  397 SER A N     
2760 C  CA    . SER A 401 ? 0.36820 0.27770 0.36620 -0.04350 0.00940  0.03630  397 SER A CA    
2761 C  C     . SER A 401 ? 0.40480 0.32430 0.40250 -0.04620 0.00880  0.04210  397 SER A C     
2762 O  O     . SER A 401 ? 0.36900 0.28860 0.36880 -0.05140 0.00800  0.04240  397 SER A O     
2763 C  CB    . SER A 401 ? 0.35410 0.25310 0.35920 -0.04410 0.00960  0.03930  397 SER A CB    
2764 O  OG    . SER A 401 ? 0.36320 0.26580 0.37050 -0.04210 0.00940  0.04770  397 SER A OG    
2765 N  N     . CYS A 402 ? 0.32370 0.25160 0.31890 -0.04280 0.00910  0.04670  398 CYS A N     
2766 C  CA    . CYS A 402 ? 0.40610 0.34500 0.40020 -0.04450 0.00920  0.05110  398 CYS A CA    
2767 C  C     . CYS A 402 ? 0.39010 0.33400 0.38220 -0.04740 0.00870  0.04690  398 CYS A C     
2768 O  O     . CYS A 402 ? 0.41130 0.36170 0.40530 -0.05090 0.00850  0.05020  398 CYS A O     
2769 C  CB    . CYS A 402 ? 0.42190 0.36890 0.41180 -0.03990 0.00990  0.05430  398 CYS A CB    
2770 S  SG    . CYS A 402 ? 0.53930 0.48830 0.52340 -0.03470 0.01000  0.04780  398 CYS A SG    
2771 N  N     . ILE A 403 ? 0.39130 0.33350 0.37980 -0.04580 0.00850  0.04020  399 ILE A N     
2772 C  CA    . ILE A 403 ? 0.37470 0.32180 0.36170 -0.04880 0.00760  0.03670  399 ILE A CA    
2773 C  C     . ILE A 403 ? 0.40990 0.35360 0.40100 -0.05520 0.00640  0.03720  399 ILE A C     
2774 O  O     . ILE A 403 ? 0.41500 0.36630 0.40790 -0.05870 0.00570  0.03980  399 ILE A O     
2775 C  CB    . ILE A 403 ? 0.35380 0.29770 0.33660 -0.04700 0.00740  0.02960  399 ILE A CB    
2776 C  CG1   . ILE A 403 ? 0.29810 0.24590 0.27710 -0.04120 0.00820  0.02920  399 ILE A CG1   
2777 C  CG2   . ILE A 403 ? 0.35230 0.30100 0.33370 -0.05100 0.00600  0.02660  399 ILE A CG2   
2778 C  CD1   . ILE A 403 ? 0.36220 0.30560 0.33800 -0.03910 0.00840  0.02310  399 ILE A CD1   
2779 N  N     . ASN A 404 ? 0.34190 0.27410 0.33530 -0.05700 0.00620  0.03440  400 ASN A N     
2780 C  CA    . ASN A 404 ? 0.40390 0.33120 0.40120 -0.06350 0.00480  0.03380  400 ASN A CA    
2781 C  C     . ASN A 404 ? 0.40800 0.33980 0.41060 -0.06660 0.00460  0.04180  400 ASN A C     
2782 O  O     . ASN A 404 ? 0.38210 0.31840 0.38710 -0.07190 0.00320  0.04310  400 ASN A O     
2783 C  CB    . ASN A 404 ? 0.37540 0.28840 0.37460 -0.06410 0.00510  0.02950  400 ASN A CB    
2784 C  CG    . ASN A 404 ? 0.48570 0.39470 0.47970 -0.06090 0.00590  0.02170  400 ASN A CG    
2785 O  OD1   . ASN A 404 ? 0.44390 0.35450 0.43550 -0.05520 0.00720  0.02170  400 ASN A OD1   
2786 N  ND2   . ASN A 404 ? 0.51330 0.41750 0.50540 -0.06490 0.00510  0.01500  400 ASN A ND2   
2787 N  N     . TRP A 405 ? 0.38890 0.32010 0.39360 -0.06360 0.00580  0.04770  401 TRP A N     
2788 C  CA    . TRP A 405 ? 0.40920 0.34490 0.41890 -0.06670 0.00580  0.05590  401 TRP A CA    
2789 C  C     . TRP A 405 ? 0.35030 0.30070 0.35840 -0.06690 0.00630  0.05920  401 TRP A C     
2790 O  O     . TRP A 405 ? 0.41570 0.37120 0.42810 -0.07180 0.00570  0.06320  401 TRP A O     
2791 C  CB    . TRP A 405 ? 0.40200 0.33460 0.41340 -0.06320 0.00690  0.06190  401 TRP A CB    
2792 C  CG    . TRP A 405 ? 0.44620 0.36440 0.46090 -0.06290 0.00660  0.05950  401 TRP A CG    
2793 C  CD1   . TRP A 405 ? 0.43780 0.35010 0.45080 -0.05760 0.00730  0.05690  401 TRP A CD1   
2794 C  CD2   . TRP A 405 ? 0.44850 0.35610 0.46940 -0.06810 0.00550  0.05920  401 TRP A CD2   
2795 N  NE1   . TRP A 405 ? 0.34180 0.24080 0.36000 -0.05870 0.00700  0.05500  401 TRP A NE1   
2796 C  CE2   . TRP A 405 ? 0.42070 0.31590 0.44350 -0.06510 0.00590  0.05610  401 TRP A CE2   
2797 C  CE3   . TRP A 405 ? 0.42970 0.33720 0.45530 -0.07510 0.00420  0.06120  401 TRP A CE3   
2798 C  CZ2   . TRP A 405 ? 0.46830 0.35030 0.49740 -0.06860 0.00530  0.05460  401 TRP A CZ2   
2799 C  CZ3   . TRP A 405 ? 0.47820 0.37220 0.50960 -0.07910 0.00320  0.05970  401 TRP A CZ3   
2800 C  CH2   . TRP A 405 ? 0.47870 0.35980 0.51180 -0.07560 0.00390  0.05610  401 TRP A CH2   
2801 N  N     . GLY A 406 ? 0.34700 0.30440 0.34970 -0.06170 0.00740  0.05750  402 GLY A N     
2802 C  CA    . GLY A 406 ? 0.42530 0.39640 0.42720 -0.06120 0.00820  0.06020  402 GLY A CA    
2803 C  C     . GLY A 406 ? 0.44400 0.41940 0.44700 -0.06520 0.00660  0.05700  402 GLY A C     
2804 O  O     . GLY A 406 ? 0.36770 0.35160 0.37480 -0.06870 0.00660  0.06110  402 GLY A O     
2805 N  N     . VAL A 407 ? 0.37240 0.34250 0.37220 -0.06490 0.00530  0.05000  403 VAL A N     
2806 C  CA    . VAL A 407 ? 0.34400 0.31890 0.34420 -0.06870 0.00340  0.04700  403 VAL A CA    
2807 C  C     . VAL A 407 ? 0.43780 0.41090 0.44370 -0.07620 0.00160  0.04890  403 VAL A C     
2808 O  O     . VAL A 407 ? 0.40770 0.39010 0.41700 -0.07980 0.00050  0.05130  403 VAL A O     
2809 C  CB    . VAL A 407 ? 0.30160 0.27060 0.29660 -0.06730 0.00240  0.03920  403 VAL A CB    
2810 C  CG1   . VAL A 407 ? 0.29170 0.26400 0.28690 -0.07250 -0.00020 0.03610  403 VAL A CG1   
2811 C  CG2   . VAL A 407 ? 0.28250 0.25570 0.27280 -0.06050 0.00380  0.03800  403 VAL A CG2   
2812 N  N     . HIS A 408 ? 0.42470 0.38590 0.43260 -0.07860 0.00130  0.04830  404 HIS A N     
2813 C  CA    . HIS A 408 ? 0.35930 0.31650 0.37250 -0.08620 -0.00090 0.04890  404 HIS A CA    
2814 C  C     . HIS A 408 ? 0.36360 0.32650 0.38340 -0.08910 -0.00030 0.05770  404 HIS A C     
2815 O  O     . HIS A 408 ? 0.38190 0.35050 0.40660 -0.09500 -0.00190 0.06010  404 HIS A O     
2816 C  CB    . HIS A 408 ? 0.36150 0.30250 0.37470 -0.08780 -0.00140 0.04400  404 HIS A CB    
2817 C  CG    . HIS A 408 ? 0.43130 0.36690 0.44850 -0.09590 -0.00410 0.04210  404 HIS A CG    
2818 N  ND1   . HIS A 408 ? 0.43480 0.37170 0.44910 -0.10000 -0.00650 0.03610  404 HIS A ND1   
2819 C  CD2   . HIS A 408 ? 0.40670 0.33610 0.43070 -0.10120 -0.00500 0.04580  404 HIS A CD2   
2820 C  CE1   . HIS A 408 ? 0.40640 0.33790 0.42520 -0.10760 -0.00890 0.03550  404 HIS A CE1   
2821 N  NE2   . HIS A 408 ? 0.37160 0.29810 0.39660 -0.10840 -0.00790 0.04140  404 HIS A NE2   
2822 N  N     . CYS A 409 ? 0.33680 0.29870 0.35720 -0.08530 0.00200  0.06280  405 CYS A N     
2823 C  CA    . CYS A 409 ? 0.40580 0.37030 0.43270 -0.08880 0.00250  0.07130  405 CYS A CA    
2824 C  C     . CYS A 409 ? 0.40550 0.38580 0.43300 -0.08690 0.00460  0.07790  405 CYS A C     
2825 O  O     . CYS A 409 ? 0.46030 0.44590 0.49370 -0.09090 0.00500  0.08500  405 CYS A O     
2826 C  CB    . CYS A 409 ? 0.41650 0.37040 0.44450 -0.08660 0.00340  0.07410  405 CYS A CB    
2827 S  SG    . CYS A 409 ? 0.49760 0.43210 0.52730 -0.08960 0.00140  0.06700  405 CYS A SG    
2828 N  N     . TYR A 410 ? 0.41000 0.39780 0.43200 -0.08080 0.00620  0.07580  406 TYR A N     
2829 C  CA    . TYR A 410 ? 0.37820 0.38050 0.40040 -0.07830 0.00880  0.08130  406 TYR A CA    
2830 C  C     . TYR A 410 ? 0.36910 0.38250 0.39430 -0.08090 0.00810  0.08080  406 TYR A C     
2831 O  O     . TYR A 410 ? 0.41820 0.43090 0.44100 -0.08040 0.00640  0.07460  406 TYR A O     
2832 C  CB    . TYR A 410 ? 0.41190 0.41630 0.42680 -0.07050 0.01090  0.07900  406 TYR A CB    
2833 C  CG    . TYR A 410 ? 0.38980 0.40790 0.40390 -0.06740 0.01400  0.08400  406 TYR A CG    
2834 C  CD1   . TYR A 410 ? 0.41890 0.44000 0.43420 -0.06780 0.01590  0.09130  406 TYR A CD1   
2835 C  CD2   . TYR A 410 ? 0.43990 0.46770 0.45200 -0.06380 0.01520  0.08130  406 TYR A CD2   
2836 C  CE1   . TYR A 410 ? 0.50070 0.53470 0.51440 -0.06490 0.01920  0.09530  406 TYR A CE1   
2837 C  CE2   . TYR A 410 ? 0.47310 0.51300 0.48440 -0.06060 0.01850  0.08500  406 TYR A CE2   
2838 C  CZ    . TYR A 410 ? 0.51280 0.55590 0.52440 -0.06120 0.02060  0.09170  406 TYR A CZ    
2839 O  OH    . TYR A 410 ? 0.57980 0.63540 0.58980 -0.05800 0.02430  0.09490  406 TYR A OH    
2840 N  N     . LEU A 411 ? 0.41970 0.44410 0.45050 -0.08370 0.00940  0.08760  407 LEU A N     
2841 C  CA    . LEU A 411 ? 0.40810 0.44480 0.44340 -0.08600 0.00890  0.08830  407 LEU A CA    
2842 C  C     . LEU A 411 ? 0.42600 0.47470 0.45830 -0.07920 0.01220  0.08870  407 LEU A C     
2843 O  O     . LEU A 411 ? 0.46010 0.51510 0.49190 -0.07650 0.01560  0.09360  407 LEU A O     
2844 C  CB    . LEU A 411 ? 0.42300 0.46590 0.46720 -0.09300 0.00860  0.09550  407 LEU A CB    
2845 C  CG    . LEU A 411 ? 0.52880 0.58130 0.57910 -0.09760 0.00640  0.09550  407 LEU A CG    
2846 C  CD1   . LEU A 411 ? 0.53320 0.58530 0.59200 -0.10660 0.00430  0.10050  407 LEU A CD1   
2847 C  CD2   . LEU A 411 ? 0.58860 0.65810 0.64070 -0.09330 0.00970  0.09860  407 LEU A CD2   
2848 N  N     . ALA A 412 ? 0.35090 0.40210 0.38100 -0.07640 0.01120  0.08330  408 ALA A N     
2849 C  CA    . ALA A 412 ? 0.38970 0.45060 0.41730 -0.06970 0.01400  0.08250  408 ALA A CA    
2850 C  C     . ALA A 412 ? 0.43970 0.51520 0.47500 -0.07160 0.01450  0.08600  408 ALA A C     
2851 O  O     . ALA A 412 ? 0.53220 0.60950 0.57100 -0.07490 0.01130  0.08410  408 ALA A O     
2852 C  CB    . ALA A 412 ? 0.43120 0.48610 0.45260 -0.06520 0.01270  0.07520  408 ALA A CB    
2853 N  N     . GLN A 413 ? 0.35210 0.43860 0.38980 -0.06940 0.01840  0.09100  409 GLN A N     
2854 C  CA    . GLN A 413 ? 0.53260 0.63450 0.57850 -0.07050 0.01990  0.09540  409 GLN A CA    
2855 C  C     . GLN A 413 ? 0.49020 0.60200 0.53520 -0.06300 0.02330  0.09370  409 GLN A C     
2856 O  O     . GLN A 413 ? 0.57460 0.69840 0.62710 -0.06310 0.02370  0.09570  409 GLN A O     
2857 C  CB    . GLN A 413 ? 0.54610 0.65430 0.59720 -0.07480 0.02220  0.10340  409 GLN A CB    
2858 C  CG    . GLN A 413 ? 0.82800 0.93010 0.87340 -0.07370 0.02470  0.10630  409 GLN A CG    
2859 C  CD    . GLN A 413 ? 0.85670 0.96150 0.90900 -0.08090 0.02480  0.11450  409 GLN A CD    
2860 O  OE1   . GLN A 413 ? 0.87560 0.99460 0.93360 -0.08160 0.02800  0.12030  409 GLN A OE1   
2861 N  NE2   . GLN A 413 ? 0.86600 0.95740 0.91870 -0.08630 0.02120  0.11470  409 GLN A NE2   
2862 N  N     . THR A 414 ? 0.43220 0.53880 0.46870 -0.05650 0.02540  0.08980  410 THR A N     
2863 C  CA    . THR A 414 ? 0.37110 0.48630 0.40690 -0.04930 0.02890  0.08790  410 THR A CA    
2864 C  C     . THR A 414 ? 0.33970 0.44840 0.37160 -0.04520 0.02660  0.08110  410 THR A C     
2865 O  O     . THR A 414 ? 0.39130 0.48730 0.41680 -0.04560 0.02400  0.07710  410 THR A O     
2866 C  CB    . THR A 414 ? 0.47900 0.59570 0.50830 -0.04460 0.03360  0.08860  410 THR A CB    
2867 O  OG1   . THR A 414 ? 0.55970 0.68650 0.59370 -0.04760 0.03670  0.09570  410 THR A OG1   
2868 C  CG2   . THR A 414 ? 0.55040 0.67270 0.57740 -0.03670 0.03690  0.08460  410 THR A CG2   
2869 N  N     . PRO A 415 ? 0.40200 0.51930 0.43830 -0.04140 0.02750  0.08000  411 PRO A N     
2870 C  CA    . PRO A 415 ? 0.36810 0.47950 0.40160 -0.03800 0.02490  0.07450  411 PRO A CA    
2871 C  C     . PRO A 415 ? 0.38900 0.49020 0.41260 -0.03300 0.02590  0.06940  411 PRO A C     
2872 O  O     . PRO A 415 ? 0.44030 0.54450 0.46060 -0.02810 0.02990  0.06890  411 PRO A O     
2873 C  CB    . PRO A 415 ? 0.38800 0.51200 0.42890 -0.03390 0.02700  0.07550  411 PRO A CB    
2874 C  CG    . PRO A 415 ? 0.47670 0.61300 0.52640 -0.03760 0.02860  0.08180  411 PRO A CG    
2875 C  CD    . PRO A 415 ? 0.42130 0.55440 0.46690 -0.04080 0.03040  0.08460  411 PRO A CD    
2876 N  N     . GLY A 416 ? 0.43320 0.52290 0.45190 -0.03430 0.02220  0.06540  412 GLY A N     
2877 C  CA    . GLY A 416 ? 0.32260 0.40290 0.33290 -0.02980 0.02250  0.06070  412 GLY A CA    
2878 C  C     . GLY A 416 ? 0.36670 0.44120 0.37090 -0.03000 0.02400  0.06140  412 GLY A C     
2879 O  O     . GLY A 416 ? 0.44110 0.50890 0.43860 -0.02630 0.02440  0.05790  412 GLY A O     
2880 N  N     . ALA A 417 ? 0.32300 0.39990 0.32980 -0.03450 0.02470  0.06630  413 ALA A N     
2881 C  CA    . ALA A 417 ? 0.33570 0.40850 0.33750 -0.03460 0.02620  0.06820  413 ALA A CA    
2882 C  C     . ALA A 417 ? 0.36340 0.42280 0.36170 -0.03750 0.02290  0.06660  413 ALA A C     
2883 O  O     . ALA A 417 ? 0.46990 0.52520 0.46510 -0.03810 0.02360  0.06900  413 ALA A O     
2884 C  CB    . ALA A 417 ? 0.28890 0.37060 0.29540 -0.03810 0.02860  0.07500  413 ALA A CB    
2885 N  N     . PHE A 418 ? 0.30500 0.35780 0.30380 -0.03930 0.01960  0.06290  414 PHE A N     
2886 C  CA    . PHE A 418 ? 0.32140 0.36140 0.31680 -0.04120 0.01710  0.06030  414 PHE A CA    
2887 C  C     . PHE A 418 ? 0.36040 0.39520 0.35080 -0.03680 0.01610  0.05450  414 PHE A C     
2888 O  O     . PHE A 418 ? 0.33700 0.37440 0.32890 -0.03630 0.01490  0.05200  414 PHE A O     
2889 C  CB    . PHE A 418 ? 0.33060 0.36690 0.33030 -0.04770 0.01410  0.06060  414 PHE A CB    
2890 C  CG    . PHE A 418 ? 0.36840 0.39140 0.36540 -0.04980 0.01220  0.05810  414 PHE A CG    
2891 C  CD1   . PHE A 418 ? 0.34550 0.36120 0.33890 -0.04870 0.01030  0.05230  414 PHE A CD1   
2892 C  CD2   . PHE A 418 ? 0.39460 0.41280 0.39320 -0.05280 0.01240  0.06180  414 PHE A CD2   
2893 C  CE1   . PHE A 418 ? 0.35120 0.35510 0.34260 -0.05030 0.00900  0.04970  414 PHE A CE1   
2894 C  CE2   . PHE A 418 ? 0.33470 0.34040 0.33180 -0.05430 0.01090  0.05950  414 PHE A CE2   
2895 C  CZ    . PHE A 418 ? 0.35430 0.35290 0.34780 -0.05280 0.00930  0.05310  414 PHE A CZ    
2896 N  N     . GLN A 419 ? 0.33650 0.36520 0.32130 -0.03350 0.01670  0.05290  415 GLN A N     
2897 C  CA    . GLN A 419 ? 0.30780 0.33260 0.28810 -0.02900 0.01620  0.04800  415 GLN A CA    
2898 C  C     . GLN A 419 ? 0.36600 0.37930 0.34340 -0.02990 0.01420  0.04540  415 GLN A C     
2899 O  O     . GLN A 419 ? 0.31580 0.32470 0.29090 -0.02920 0.01470  0.04680  415 GLN A O     
2900 C  CB    . GLN A 419 ? 0.35000 0.37870 0.32630 -0.02400 0.01870  0.04810  415 GLN A CB    
2901 C  CG    . GLN A 419 ? 0.35790 0.39770 0.33680 -0.02190 0.02120  0.04930  415 GLN A CG    
2902 C  CD    . GLN A 419 ? 0.46210 0.50330 0.44270 -0.01960 0.02020  0.04570  415 GLN A CD    
2903 O  OE1   . GLN A 419 ? 0.45640 0.49160 0.43360 -0.01710 0.01890  0.04170  415 GLN A OE1   
2904 N  NE2   . GLN A 419 ? 0.38530 0.43480 0.37200 -0.02070 0.02070  0.04760  415 GLN A NE2   
2905 N  N     . ILE A 420 ? 0.32690 0.33580 0.30450 -0.03140 0.01210  0.04170  416 ILE A N     
2906 C  CA    . ILE A 420 ? 0.33080 0.32950 0.30620 -0.03210 0.01070  0.03870  416 ILE A CA    
2907 C  C     . ILE A 420 ? 0.32830 0.32520 0.30110 -0.02980 0.00970  0.03410  416 ILE A C     
2908 O  O     . ILE A 420 ? 0.30770 0.30950 0.28190 -0.03050 0.00880  0.03320  416 ILE A O     
2909 C  CB    . ILE A 420 ? 0.34320 0.33720 0.32170 -0.03770 0.00940  0.03910  416 ILE A CB    
2910 C  CG1   . ILE A 420 ? 0.33710 0.31990 0.31400 -0.03800 0.00890  0.03680  416 ILE A CG1   
2911 C  CG2   . ILE A 420 ? 0.33140 0.32830 0.31150 -0.04090 0.00760  0.03700  416 ILE A CG2   
2912 C  CD1   . ILE A 420 ? 0.36490 0.34220 0.34540 -0.04320 0.00820  0.03810  416 ILE A CD1   
2913 N  N     . GLY A 421 ? 0.35200 0.34270 0.32150 -0.02710 0.00960  0.03160  417 GLY A N     
2914 C  CA    . GLY A 421 ? 0.30550 0.29480 0.27260 -0.02480 0.00880  0.02780  417 GLY A CA    
2915 C  C     . GLY A 421 ? 0.42380 0.40640 0.39020 -0.02730 0.00760  0.02450  417 GLY A C     
2916 O  O     . GLY A 421 ? 0.42850 0.40510 0.39290 -0.02560 0.00770  0.02230  417 GLY A O     
2917 N  N     . LEU A 422 ? 0.37200 0.35620 0.33980 -0.03140 0.00640  0.02390  418 LEU A N     
2918 C  CA    . LEU A 422 ? 0.38020 0.35800 0.34660 -0.03440 0.00550  0.02030  418 LEU A CA    
2919 C  C     . LEU A 422 ? 0.34950 0.32790 0.31290 -0.03350 0.00470  0.01700  418 LEU A C     
2920 O  O     . LEU A 422 ? 0.40040 0.37390 0.36170 -0.03560 0.00430  0.01360  418 LEU A O     
2921 C  CB    . LEU A 422 ? 0.42730 0.40630 0.39600 -0.04000 0.00430  0.02100  418 LEU A CB    
2922 C  CG    . LEU A 422 ? 0.39070 0.36710 0.36260 -0.04180 0.00510  0.02410  418 LEU A CG    
2923 C  CD1   . LEU A 422 ? 0.33970 0.31640 0.31430 -0.04790 0.00370  0.02440  418 LEU A CD1   
2924 C  CD2   . LEU A 422 ? 0.29830 0.26520 0.26910 -0.03990 0.00630  0.02260  418 LEU A CD2   
2925 N  N     . GLY A 423 ? 0.33920 0.32340 0.30270 -0.03060 0.00440  0.01810  419 GLY A N     
2926 C  CA    . GLY A 423 ? 0.34210 0.32660 0.30310 -0.02970 0.00350  0.01570  419 GLY A CA    
2927 C  C     . GLY A 423 ? 0.41030 0.38790 0.36860 -0.02790 0.00450  0.01280  419 GLY A C     
2928 O  O     . GLY A 423 ? 0.45210 0.42710 0.40800 -0.02970 0.00420  0.00980  419 GLY A O     
2929 N  N     . LEU A 424 ? 0.36610 0.34130 0.32480 -0.02440 0.00560  0.01360  420 LEU A N     
2930 C  CA    . LEU A 424 ? 0.37620 0.34550 0.33360 -0.02260 0.00650  0.01150  420 LEU A CA    
2931 C  C     . LEU A 424 ? 0.37870 0.34250 0.33760 -0.02300 0.00760  0.01200  420 LEU A C     
2932 O  O     . LEU A 424 ? 0.31260 0.27090 0.27140 -0.02220 0.00840  0.00990  420 LEU A O     
2933 C  CB    . LEU A 424 ? 0.38370 0.35460 0.34090 -0.01830 0.00650  0.01220  420 LEU A CB    
2934 C  CG    . LEU A 424 ? 0.43590 0.40300 0.39200 -0.01660 0.00690  0.00990  420 LEU A CG    
2935 C  CD1   . LEU A 424 ? 0.38910 0.35640 0.34350 -0.01890 0.00680  0.00740  420 LEU A CD1   
2936 C  CD2   . LEU A 424 ? 0.45780 0.42710 0.41390 -0.01320 0.00630  0.01070  420 LEU A CD2   
2937 N  N     . ALA A 425 ? 0.30760 0.27290 0.26850 -0.02420 0.00760  0.01500  421 ALA A N     
2938 C  CA    . ALA A 425 ? 0.33190 0.29190 0.29480 -0.02500 0.00840  0.01640  421 ALA A CA    
2939 C  C     . ALA A 425 ? 0.37630 0.33260 0.33940 -0.02130 0.00900  0.01680  421 ALA A C     
2940 O  O     . ALA A 425 ? 0.40640 0.35630 0.37100 -0.02120 0.00970  0.01550  421 ALA A O     
2941 C  CB    . ALA A 425 ? 0.28390 0.23820 0.24740 -0.02890 0.00840  0.01350  421 ALA A CB    
2942 N  N     . ALA A 426 ? 0.29520 0.25570 0.25710 -0.01820 0.00880  0.01850  422 ALA A N     
2943 C  CA    . ALA A 426 ? 0.32020 0.27860 0.28220 -0.01490 0.00880  0.01920  422 ALA A CA    
2944 C  C     . ALA A 426 ? 0.36180 0.31930 0.32550 -0.01480 0.00900  0.02350  422 ALA A C     
2945 O  O     . ALA A 426 ? 0.34640 0.30860 0.30930 -0.01520 0.00900  0.02640  422 ALA A O     
2946 C  CB    . ALA A 426 ? 0.25580 0.21880 0.21550 -0.01200 0.00810  0.01890  422 ALA A CB    
2947 N  N     . MET A 427 ? 0.34510 0.29700 0.31130 -0.01400 0.00920  0.02410  423 MET A N     
2948 C  CA    . MET A 427 ? 0.40100 0.35230 0.36890 -0.01360 0.00900  0.02900  423 MET A CA    
2949 C  C     . MET A 427 ? 0.37760 0.33500 0.34240 -0.01120 0.00820  0.03140  423 MET A C     
2950 O  O     . MET A 427 ? 0.35530 0.31410 0.31820 -0.00880 0.00750  0.02940  423 MET A O     
2951 C  CB    . MET A 427 ? 0.41720 0.36180 0.38920 -0.01240 0.00910  0.02950  423 MET A CB    
2952 C  CG    . MET A 427 ? 0.45890 0.39640 0.43430 -0.01490 0.01010  0.02750  423 MET A CG    
2953 S  SD    . MET A 427 ? 0.49370 0.42360 0.47420 -0.01210 0.01090  0.02630  423 MET A SD    
2954 C  CE    . MET A 427 ? 0.39870 0.33010 0.38190 -0.01000 0.00950  0.03390  423 MET A CE    
2955 N  N     . GLY A 428 ? 0.39280 0.35380 0.35700 -0.01210 0.00830  0.03580  424 GLY A N     
2956 C  CA    . GLY A 428 ? 0.37280 0.33970 0.33310 -0.01010 0.00780  0.03790  424 GLY A CA    
2957 C  C     . GLY A 428 ? 0.41560 0.38900 0.37230 -0.01000 0.00850  0.03630  424 GLY A C     
2958 O  O     . GLY A 428 ? 0.35440 0.33310 0.30760 -0.00870 0.00860  0.03800  424 GLY A O     
2959 N  N     . HIS A 429 ? 0.31910 0.29250 0.27690 -0.01120 0.00900  0.03300  425 HIS A N     
2960 C  CA    . HIS A 429 ? 0.31130 0.29080 0.26720 -0.01090 0.00970  0.03170  425 HIS A CA    
2961 C  C     . HIS A 429 ? 0.39570 0.38120 0.35110 -0.01180 0.01110  0.03570  425 HIS A C     
2962 O  O     . HIS A 429 ? 0.34490 0.33590 0.29700 -0.00980 0.01180  0.03570  425 HIS A O     
2963 C  CB    . HIS A 429 ? 0.38560 0.36410 0.34400 -0.01300 0.00980  0.02920  425 HIS A CB    
2964 C  CG    . HIS A 429 ? 0.51090 0.49550 0.46870 -0.01240 0.01020  0.02790  425 HIS A CG    
2965 N  ND1   . HIS A 429 ? 0.53050 0.51540 0.49000 -0.01390 0.00970  0.02580  425 HIS A ND1   
2966 C  CD2   . HIS A 429 ? 0.52430 0.51500 0.48050 -0.01040 0.01120  0.02860  425 HIS A CD2   
2967 C  CE1   . HIS A 429 ? 0.51300 0.50400 0.47280 -0.01260 0.01020  0.02570  425 HIS A CE1   
2968 N  NE2   . HIS A 429 ? 0.47360 0.46790 0.43150 -0.01040 0.01130  0.02700  425 HIS A NE2   
2969 N  N     . ALA A 430 ? 0.35110 0.33560 0.30970 -0.01490 0.01150  0.03900  426 ALA A N     
2970 C  CA    . ALA A 430 ? 0.36520 0.35600 0.32390 -0.01630 0.01300  0.04330  426 ALA A CA    
2971 C  C     . ALA A 430 ? 0.32420 0.31750 0.27930 -0.01460 0.01320  0.04680  426 ALA A C     
2972 O  O     . ALA A 430 ? 0.34940 0.35020 0.30190 -0.01390 0.01480  0.04860  426 ALA A O     
2973 C  CB    . ALA A 430 ? 0.36550 0.35400 0.32910 -0.02060 0.01310  0.04640  426 ALA A CB    
2974 N  N     . VAL A 431 ? 0.34520 0.33290 0.30020 -0.01380 0.01170  0.04760  427 VAL A N     
2975 C  CA    . VAL A 431 ? 0.42580 0.41610 0.37730 -0.01240 0.01120  0.05130  427 VAL A CA    
2976 C  C     . VAL A 431 ? 0.40720 0.40400 0.35260 -0.00980 0.01190  0.04880  427 VAL A C     
2977 O  O     . VAL A 431 ? 0.46810 0.47120 0.40960 -0.00960 0.01300  0.05180  427 VAL A O     
2978 C  CB    . VAL A 431 ? 0.40480 0.38830 0.35760 -0.01120 0.00910  0.05150  427 VAL A CB    
2979 C  CG1   . VAL A 431 ? 0.36170 0.34890 0.31020 -0.00960 0.00790  0.05470  427 VAL A CG1   
2980 C  CG2   . VAL A 431 ? 0.38180 0.35840 0.34100 -0.01350 0.00880  0.05420  427 VAL A CG2   
2981 N  N     . ALA A 432 ? 0.41940 0.41470 0.36390 -0.00780 0.01140  0.04310  428 ALA A N     
2982 C  CA    . ALA A 432 ? 0.38800 0.38800 0.32730 -0.00510 0.01190  0.03980  428 ALA A CA    
2983 C  C     . ALA A 432 ? 0.36930 0.37460 0.30920 -0.00490 0.01430  0.03790  428 ALA A C     
2984 O  O     . ALA A 432 ? 0.40680 0.41820 0.34270 -0.00330 0.01600  0.03740  428 ALA A O     
2985 C  CB    . ALA A 432 ? 0.32570 0.32100 0.26430 -0.00310 0.00980  0.03510  428 ALA A CB    
2986 N  N     . ALA A 433 ? 0.29910 0.30250 0.24400 -0.00630 0.01450  0.03680  429 ALA A N     
2987 C  CA    . ALA A 433 ? 0.28040 0.28940 0.22680 -0.00580 0.01640  0.03540  429 ALA A CA    
2988 C  C     . ALA A 433 ? 0.30240 0.31940 0.24810 -0.00640 0.01900  0.03920  429 ALA A C     
2989 O  O     . ALA A 433 ? 0.31970 0.34290 0.26460 -0.00440 0.02120  0.03760  429 ALA A O     
2990 C  CB    . ALA A 433 ? 0.34030 0.34690 0.29220 -0.00800 0.01570  0.03460  429 ALA A CB    
2991 N  N     . ALA A 434 ? 0.29950 0.31660 0.24580 -0.00910 0.01910  0.04440  430 ALA A N     
2992 C  CA    . ALA A 434 ? 0.34750 0.37270 0.29350 -0.01030 0.02170  0.04890  430 ALA A CA    
2993 C  C     . ALA A 434 ? 0.35060 0.38220 0.28990 -0.00710 0.02370  0.04750  430 ALA A C     
2994 O  O     . ALA A 434 ? 0.32870 0.36880 0.26780 -0.00680 0.02690  0.04900  430 ALA A O     
2995 C  CB    . ALA A 434 ? 0.29350 0.31680 0.24090 -0.01360 0.02110  0.05510  430 ALA A CB    
2996 N  N     . ILE A 435 ? 0.34320 0.37120 0.27720 -0.00490 0.02200  0.04460  431 ILE A N     
2997 C  CA    . ILE A 435 ? 0.34450 0.37800 0.27130 -0.00220 0.02360  0.04250  431 ILE A CA    
2998 C  C     . ILE A 435 ? 0.40920 0.44580 0.33670 0.00080  0.02580  0.03710  431 ILE A C     
2999 O  O     . ILE A 435 ? 0.36580 0.41000 0.29040 0.00240  0.02920  0.03650  431 ILE A O     
3000 C  CB    . ILE A 435 ? 0.36530 0.39410 0.28660 -0.00110 0.02060  0.04070  431 ILE A CB    
3001 C  CG1   . ILE A 435 ? 0.29730 0.32440 0.21860 -0.00370 0.01880  0.04720  431 ILE A CG1   
3002 C  CG2   . ILE A 435 ? 0.35770 0.39150 0.27080 0.00150  0.02200  0.03710  431 ILE A CG2   
3003 C  CD1   . ILE A 435 ? 0.29520 0.31730 0.21340 -0.00300 0.01520  0.04650  431 ILE A CD1   
3004 N  N     . GLY A 436 ? 0.34250 0.37340 0.27410 0.00160  0.02410  0.03320  432 GLY A N     
3005 C  CA    . GLY A 436 ? 0.26850 0.30220 0.20230 0.00450  0.02600  0.02900  432 GLY A CA    
3006 C  C     . GLY A 436 ? 0.29620 0.33760 0.23530 0.00360  0.02900  0.03210  432 GLY A C     
3007 O  O     . GLY A 436 ? 0.33820 0.38600 0.27760 0.00630  0.03220  0.03010  432 GLY A O     
3008 N  N     . GLY A 437 ? 0.28630 0.32740 0.23010 -0.00030 0.02820  0.03690  433 GLY A N     
3009 C  CA    . GLY A 437 ? 0.31230 0.36130 0.26170 -0.00180 0.03080  0.04040  433 GLY A CA    
3010 C  C     . GLY A 437 ? 0.38540 0.44380 0.33140 -0.00090 0.03480  0.04280  433 GLY A C     
3011 O  O     . GLY A 437 ? 0.34680 0.41340 0.29600 0.00070  0.03810  0.04280  433 GLY A O     
3012 N  N     . LYS A 438 ? 0.26880 0.32670 0.20830 -0.00180 0.03450  0.04520  434 LYS A N     
3013 C  CA    . LYS A 438 ? 0.31420 0.38170 0.24950 -0.00140 0.03840  0.04790  434 LYS A CA    
3014 C  C     . LYS A 438 ? 0.34370 0.41540 0.27440 0.00350  0.04130  0.04180  434 LYS A C     
3015 O  O     . LYS A 438 ? 0.36120 0.44270 0.29210 0.00490  0.04580  0.04250  434 LYS A O     
3016 C  CB    . LYS A 438 ? 0.28070 0.34680 0.20960 -0.00340 0.03700  0.05200  434 LYS A CB    
3017 C  CG    . LYS A 438 ? 0.33000 0.40690 0.25360 -0.00360 0.04090  0.05590  434 LYS A CG    
3018 C  CD    . LYS A 438 ? 0.30350 0.38770 0.23410 -0.00700 0.04330  0.06270  434 LYS A CD    
3019 C  CE    . LYS A 438 ? 0.35040 0.44660 0.27600 -0.00710 0.04780  0.06660  434 LYS A CE    
3020 N  NZ    . LYS A 438 ? 0.39040 0.49180 0.32230 -0.01170 0.04890  0.07520  434 LYS A NZ    
3021 N  N     . LEU A 439 ? 0.34940 0.41390 0.27650 0.00620  0.03910  0.03570  435 LEU A N     
3022 C  CA    . LEU A 439 ? 0.32360 0.39060 0.24700 0.01080  0.04170  0.02920  435 LEU A CA    
3023 C  C     . LEU A 439 ? 0.40250 0.47360 0.33410 0.01320  0.04430  0.02750  435 LEU A C     
3024 O  O     . LEU A 439 ? 0.34150 0.41860 0.27190 0.01680  0.04840  0.02400  435 LEU A O     
3025 C  CB    . LEU A 439 ? 0.28000 0.33760 0.19890 0.01250  0.03810  0.02350  435 LEU A CB    
3026 C  CG    . LEU A 439 ? 0.35620 0.41170 0.26600 0.01110  0.03590  0.02420  435 LEU A CG    
3027 C  CD1   . LEU A 439 ? 0.33720 0.38370 0.24430 0.01230  0.03200  0.01900  435 LEU A CD1   
3028 C  CD2   . LEU A 439 ? 0.29560 0.35980 0.19680 0.01230  0.03970  0.02360  435 LEU A CD2   
3029 N  N     . ALA A 440 ? 0.30360 0.37200 0.24370 0.01110  0.04220  0.02990  436 ALA A N     
3030 C  CA    . ALA A 440 ? 0.31760 0.39040 0.26640 0.01290  0.04400  0.02930  436 ALA A CA    
3031 C  C     . ALA A 440 ? 0.43990 0.52440 0.39320 0.01170  0.04800  0.03440  436 ALA A C     
3032 O  O     . ALA A 440 ? 0.39560 0.48730 0.35440 0.01480  0.05140  0.03330  436 ALA A O     
3033 C  CB    . ALA A 440 ? 0.29900 0.36530 0.25450 0.01060  0.03970  0.03020  436 ALA A CB    
3034 N  N     . ALA A 441 ? 0.37340 0.46050 0.32480 0.00760  0.04800  0.04020  437 ALA A N     
3035 C  CA    . ALA A 441 ? 0.37170 0.46990 0.32770 0.00550  0.05150  0.04600  437 ALA A CA    
3036 C  C     . ALA A 441 ? 0.35480 0.45730 0.30290 0.00400  0.05350  0.04940  437 ALA A C     
3037 O  O     . ALA A 441 ? 0.40590 0.50850 0.35490 -0.00070 0.05220  0.05580  437 ALA A O     
3038 C  CB    . ALA A 441 ? 0.38890 0.48590 0.35350 0.00050  0.04860  0.05120  437 ALA A CB    
3039 N  N     . PRO A 442 ? 0.41050 0.51650 0.35060 0.00780  0.05670  0.04540  438 PRO A N     
3040 C  CA    . PRO A 442 ? 0.40400 0.51300 0.33460 0.00610  0.05780  0.04840  438 PRO A CA    
3041 C  C     . PRO A 442 ? 0.40170 0.52240 0.33500 0.00310  0.06150  0.05610  438 PRO A C     
3042 O  O     . PRO A 442 ? 0.46010 0.58240 0.38770 0.00010  0.06110  0.06130  438 PRO A O     
3043 C  CB    . PRO A 442 ? 0.46770 0.57840 0.38930 0.01110  0.06060  0.04110  438 PRO A CB    
3044 C  CG    . PRO A 442 ? 0.44440 0.55750 0.37300 0.01540  0.06340  0.03610  438 PRO A CG    
3045 C  CD    . PRO A 442 ? 0.36240 0.46930 0.30140 0.01360  0.05940  0.03790  438 PRO A CD    
3046 N  N     . ASP A 443 ? 0.31090 0.43990 0.25300 0.00370  0.06480  0.05760  439 ASP A N     
3047 C  CA    . ASP A 443 ? 0.46020 0.60130 0.40650 0.00070  0.06850  0.06520  439 ASP A CA    
3048 C  C     . ASP A 443 ? 0.46080 0.59870 0.41480 -0.00560 0.06480  0.07260  439 ASP A C     
3049 O  O     . ASP A 443 ? 0.48060 0.62780 0.43960 -0.00890 0.06730  0.07960  439 ASP A O     
3050 C  CB    . ASP A 443 ? 0.47190 0.62440 0.42550 0.00420  0.07390  0.06370  439 ASP A CB    
3051 C  CG    . ASP A 443 ? 0.68320 0.83060 0.64630 0.00600  0.07150  0.06000  439 ASP A CG    
3052 O  OD1   . ASP A 443 ? 0.55510 0.68990 0.51650 0.00630  0.06650  0.05590  439 ASP A OD1   
3053 O  OD2   . ASP A 443 ? 0.75440 0.91120 0.72720 0.00720  0.07450  0.06150  439 ASP A OD2   
3054 N  N     . ARG A 444 ? 0.48630 0.61160 0.44220 -0.00730 0.05910  0.07110  440 ARG A N     
3055 C  CA    . ARG A 444 ? 0.36210 0.48320 0.32540 -0.01300 0.05560  0.07670  440 ARG A CA    
3056 C  C     . ARG A 444 ? 0.42230 0.53300 0.38040 -0.01600 0.05140  0.07900  440 ARG A C     
3057 O  O     . ARG A 444 ? 0.42620 0.52960 0.37670 -0.01330 0.04950  0.07450  440 ARG A O     
3058 C  CB    . ARG A 444 ? 0.34550 0.46120 0.31670 -0.01280 0.05260  0.07320  440 ARG A CB    
3059 C  CG    . ARG A 444 ? 0.46310 0.58990 0.44200 -0.01060 0.05620  0.07260  440 ARG A CG    
3060 C  CD    . ARG A 444 ? 0.46140 0.58350 0.44760 -0.01050 0.05280  0.06960  440 ARG A CD    
3061 N  NE    . ARG A 444 ? 0.44460 0.56280 0.43680 -0.01680 0.04900  0.07420  440 ARG A NE    
3062 C  CZ    . ARG A 444 ? 0.42510 0.53920 0.42330 -0.01830 0.04540  0.07260  440 ARG A CZ    
3063 N  NH1   . ARG A 444 ? 0.48650 0.60020 0.48600 -0.01390 0.04520  0.06740  440 ARG A NH1   
3064 N  NH2   . ARG A 444 ? 0.43710 0.54750 0.43990 -0.02440 0.04190  0.07610  440 ARG A NH2   
3065 N  N     . PRO A 445 ? 0.40270 0.51240 0.36530 -0.02150 0.04980  0.08620  441 PRO A N     
3066 C  CA    . PRO A 445 ? 0.37580 0.47480 0.33520 -0.02410 0.04570  0.08860  441 PRO A CA    
3067 C  C     . PRO A 445 ? 0.37750 0.46380 0.33900 -0.02360 0.04130  0.08300  441 PRO A C     
3068 O  O     . PRO A 445 ? 0.34430 0.42950 0.31270 -0.02450 0.04030  0.08100  441 PRO A O     
3069 C  CB    . PRO A 445 ? 0.39760 0.49890 0.36370 -0.03020 0.04550  0.09750  441 PRO A CB    
3070 C  CG    . PRO A 445 ? 0.40660 0.52170 0.37850 -0.03080 0.04990  0.10010  441 PRO A CG    
3071 C  CD    . PRO A 445 ? 0.39150 0.50860 0.36390 -0.02580 0.05110  0.09220  441 PRO A CD    
3072 N  N     . VAL A 446 ? 0.33300 0.41040 0.28820 -0.02210 0.03850  0.08070  442 VAL A N     
3073 C  CA    . VAL A 446 ? 0.38540 0.45090 0.34180 -0.02150 0.03450  0.07560  442 VAL A CA    
3074 C  C     . VAL A 446 ? 0.37030 0.42690 0.32630 -0.02410 0.03140  0.07930  442 VAL A C     
3075 O  O     . VAL A 446 ? 0.33260 0.38980 0.28270 -0.02330 0.03130  0.08200  442 VAL A O     
3076 C  CB    . VAL A 446 ? 0.35340 0.41670 0.30390 -0.01620 0.03430  0.06800  442 VAL A CB    
3077 C  CG1   . VAL A 446 ? 0.33370 0.38490 0.28540 -0.01610 0.03020  0.06370  442 VAL A CG1   
3078 C  CG2   . VAL A 446 ? 0.26790 0.33880 0.22090 -0.01340 0.03730  0.06420  442 VAL A CG2   
3079 N  N     . VAL A 447 ? 0.38430 0.43280 0.34670 -0.02730 0.02870  0.07960  443 VAL A N     
3080 C  CA    . VAL A 447 ? 0.32220 0.36130 0.28620 -0.02990 0.02590  0.08310  443 VAL A CA    
3081 C  C     . VAL A 447 ? 0.36720 0.39540 0.33310 -0.02930 0.02290  0.07720  443 VAL A C     
3082 O  O     . VAL A 447 ? 0.33600 0.36390 0.30480 -0.02950 0.02270  0.07290  443 VAL A O     
3083 C  CB    . VAL A 447 ? 0.38710 0.42760 0.35800 -0.03540 0.02620  0.09030  443 VAL A CB    
3084 C  CG1   . VAL A 447 ? 0.37360 0.40290 0.34730 -0.03780 0.02330  0.09350  443 VAL A CG1   
3085 C  CG2   . VAL A 447 ? 0.30580 0.35850 0.27470 -0.03600 0.02960  0.09670  443 VAL A CG2   
3086 N  N     . ALA A 448 ? 0.31670 0.33640 0.28090 -0.02840 0.02070  0.07710  444 ALA A N     
3087 C  CA    . ALA A 448 ? 0.33760 0.34710 0.30330 -0.02760 0.01830  0.07180  444 ALA A CA    
3088 C  C     . ALA A 448 ? 0.36720 0.36760 0.33790 -0.03060 0.01650  0.07520  444 ALA A C     
3089 O  O     . ALA A 448 ? 0.43240 0.43170 0.40260 -0.03070 0.01600  0.08060  444 ALA A O     
3090 C  CB    . ALA A 448 ? 0.34740 0.35510 0.30710 -0.02310 0.01740  0.06750  444 ALA A CB    
3091 N  N     . LEU A 449 ? 0.34200 0.33560 0.31740 -0.03300 0.01540  0.07200  445 LEU A N     
3092 C  CA    . LEU A 449 ? 0.39490 0.37830 0.37540 -0.03570 0.01380  0.07380  445 LEU A CA    
3093 C  C     . LEU A 449 ? 0.39320 0.36790 0.37280 -0.03290 0.01240  0.06760  445 LEU A C     
3094 O  O     . LEU A 449 ? 0.35110 0.32450 0.33000 -0.03280 0.01220  0.06160  445 LEU A O     
3095 C  CB    . LEU A 449 ? 0.39580 0.37810 0.38210 -0.04090 0.01370  0.07440  445 LEU A CB    
3096 C  CG    . LEU A 449 ? 0.43790 0.40880 0.43010 -0.04430 0.01230  0.07550  445 LEU A CG    
3097 C  CD1   . LEU A 449 ? 0.31760 0.28820 0.31240 -0.04530 0.01240  0.08400  445 LEU A CD1   
3098 C  CD2   . LEU A 449 ? 0.41180 0.38200 0.40850 -0.04950 0.01180  0.07400  445 LEU A CD2   
3099 N  N     . VAL A 450 ? 0.28710 0.25640 0.26690 -0.03080 0.01150  0.06960  446 VAL A N     
3100 C  CA    . VAL A 450 ? 0.29720 0.26050 0.27570 -0.02740 0.01050  0.06460  446 VAL A CA    
3101 C  C     . VAL A 450 ? 0.35180 0.30550 0.33540 -0.02740 0.00950  0.06690  446 VAL A C     
3102 O  O     . VAL A 450 ? 0.33450 0.28750 0.32130 -0.02880 0.00920  0.07380  446 VAL A O     
3103 C  CB    . VAL A 450 ? 0.36450 0.33390 0.33680 -0.02320 0.01030  0.06400  446 VAL A CB    
3104 C  CG1   . VAL A 450 ? 0.36850 0.34760 0.33630 -0.02290 0.01170  0.06240  446 VAL A CG1   
3105 C  CG2   . VAL A 450 ? 0.39630 0.36740 0.36820 -0.02250 0.00970  0.07090  446 VAL A CG2   
3106 N  N     . GLY A 451 ? 0.32400 0.27050 0.30890 -0.02550 0.00910  0.06150  447 GLY A N     
3107 C  CA    . GLY A 451 ? 0.37190 0.30950 0.36210 -0.02430 0.00840  0.06290  447 GLY A CA    
3108 C  C     . GLY A 451 ? 0.41780 0.35760 0.40670 -0.02020 0.00740  0.06590  447 GLY A C     
3109 O  O     . GLY A 451 ? 0.37850 0.32570 0.36150 -0.01800 0.00700  0.06500  447 GLY A O     
3110 N  N     . ASP A 452 ? 0.37490 0.30790 0.36980 -0.01910 0.00660  0.06940  448 ASP A N     
3111 C  CA    . ASP A 452 ? 0.36990 0.30550 0.36450 -0.01550 0.00510  0.07330  448 ASP A CA    
3112 C  C     . ASP A 452 ? 0.42850 0.36410 0.42120 -0.01190 0.00490  0.06710  448 ASP A C     
3113 O  O     . ASP A 452 ? 0.32500 0.26690 0.31360 -0.00960 0.00360  0.06820  448 ASP A O     
3114 C  CB    . ASP A 452 ? 0.37890 0.30770 0.38180 -0.01520 0.00430  0.07960  448 ASP A CB    
3115 C  CG    . ASP A 452 ? 0.46340 0.38050 0.47360 -0.01490 0.00540  0.07500  448 ASP A CG    
3116 O  OD1   . ASP A 452 ? 0.37650 0.28960 0.38660 -0.01770 0.00680  0.06960  448 ASP A OD1   
3117 O  OD2   . ASP A 452 ? 0.43770 0.34980 0.45400 -0.01180 0.00480  0.07680  448 ASP A OD2   
3118 N  N     . ALA A 453 ? 0.36680 0.29570 0.36220 -0.01170 0.00620  0.06060  449 ALA A N     
3119 C  CA    . ALA A 453 ? 0.38530 0.31530 0.37890 -0.00860 0.00630  0.05510  449 ALA A CA    
3120 C  C     . ALA A 453 ? 0.37190 0.30990 0.35740 -0.00880 0.00610  0.05190  449 ALA A C     
3121 O  O     . ALA A 453 ? 0.34800 0.29010 0.33070 -0.00630 0.00510  0.05070  449 ALA A O     
3122 C  CB    . ALA A 453 ? 0.28940 0.21140 0.28680 -0.00840 0.00810  0.04870  449 ALA A CB    
3123 N  N     . ALA A 454 ? 0.37120 0.31150 0.35370 -0.01180 0.00700  0.05040  450 ALA A N     
3124 C  CA    . ALA A 454 ? 0.31040 0.25830 0.28640 -0.01160 0.00700  0.04780  450 ALA A CA    
3125 C  C     . ALA A 454 ? 0.41190 0.36700 0.38380 -0.01020 0.00580  0.05230  450 ALA A C     
3126 O  O     . ALA A 454 ? 0.39680 0.35660 0.36400 -0.00840 0.00520  0.04990  450 ALA A O     
3127 C  CB    . ALA A 454 ? 0.34930 0.29900 0.32390 -0.01490 0.00810  0.04630  450 ALA A CB    
3128 N  N     . PHE A 455 ? 0.37120 0.32710 0.34460 -0.01130 0.00540  0.05890  451 PHE A N     
3129 C  CA    . PHE A 455 ? 0.43210 0.39540 0.40080 -0.01030 0.00430  0.06330  451 PHE A CA    
3130 C  C     . PHE A 455 ? 0.47790 0.44110 0.44660 -0.00720 0.00220  0.06350  451 PHE A C     
3131 O  O     . PHE A 455 ? 0.38720 0.35660 0.35010 -0.00600 0.00100  0.06360  451 PHE A O     
3132 C  CB    . PHE A 455 ? 0.43770 0.40260 0.40790 -0.01250 0.00430  0.07110  451 PHE A CB    
3133 C  CG    . PHE A 455 ? 0.33710 0.31150 0.30040 -0.01230 0.00400  0.07490  451 PHE A CG    
3134 C  CD1   . PHE A 455 ? 0.43350 0.41440 0.39230 -0.01380 0.00590  0.07410  451 PHE A CD1   
3135 C  CD2   . PHE A 455 ? 0.42260 0.39980 0.38390 -0.01060 0.00170  0.07900  451 PHE A CD2   
3136 C  CE1   . PHE A 455 ? 0.37240 0.36220 0.32430 -0.01350 0.00610  0.07680  451 PHE A CE1   
3137 C  CE2   . PHE A 455 ? 0.40030 0.38650 0.35400 -0.01080 0.00150  0.08190  451 PHE A CE2   
3138 C  CZ    . PHE A 455 ? 0.42770 0.42010 0.37650 -0.01210 0.00390  0.08050  451 PHE A CZ    
3139 N  N     . ALA A 456 ? 0.40520 0.36150 0.38050 -0.00590 0.00170  0.06350  452 ALA A N     
3140 C  CA    . ALA A 456 ? 0.47250 0.42950 0.44880 -0.00300 -0.00030 0.06350  452 ALA A CA    
3141 C  C     . ALA A 456 ? 0.47580 0.43520 0.44800 -0.00160 -0.00040 0.05680  452 ALA A C     
3142 O  O     . ALA A 456 ? 0.46950 0.43230 0.44000 0.00010  -0.00240 0.05710  452 ALA A O     
3143 C  CB    . ALA A 456 ? 0.37700 0.32630 0.36240 -0.00150 -0.00020 0.06450  452 ALA A CB    
3144 N  N     . MET A 457 ? 0.46600 0.42400 0.43660 -0.00270 0.00160  0.05130  453 MET A N     
3145 C  CA    . MET A 457 ? 0.39510 0.35500 0.36240 -0.00160 0.00140  0.04550  453 MET A CA    
3146 C  C     . MET A 457 ? 0.41770 0.38460 0.37770 -0.00160 0.00070  0.04490  453 MET A C     
3147 O  O     . MET A 457 ? 0.43650 0.40560 0.39400 -0.00010 -0.00060 0.04220  453 MET A O     
3148 C  CB    . MET A 457 ? 0.40820 0.36460 0.37650 -0.00280 0.00350  0.04030  453 MET A CB    
3149 C  CG    . MET A 457 ? 0.53580 0.48600 0.50960 -0.00210 0.00440  0.03790  453 MET A CG    
3150 S  SD    . MET A 457 ? 0.54630 0.49480 0.51850 -0.00420 0.00640  0.03190  453 MET A SD    
3151 C  CE    . MET A 457 ? 0.70070 0.64580 0.67620 -0.00210 0.00700  0.02790  453 MET A CE    
3152 N  N     . ASN A 458 ? 0.31820 0.28860 0.27490 -0.00320 0.00180  0.04690  454 ASN A N     
3153 C  CA    . ASN A 458 ? 0.40140 0.37820 0.35130 -0.00290 0.00190  0.04520  454 ASN A CA    
3154 C  C     . ASN A 458 ? 0.43620 0.41840 0.38230 -0.00390 0.00210  0.05040  454 ASN A C     
3155 O  O     . ASN A 458 ? 0.43680 0.42460 0.37730 -0.00370 0.00310  0.04900  454 ASN A O     
3156 C  CB    . ASN A 458 ? 0.41270 0.39010 0.36160 -0.00350 0.00390  0.04070  454 ASN A CB    
3157 C  CG    . ASN A 458 ? 0.49360 0.46730 0.44440 -0.00260 0.00350  0.03560  454 ASN A CG    
3158 O  OD1   . ASN A 458 ? 0.43970 0.40890 0.39460 -0.00350 0.00430  0.03430  454 ASN A OD1   
3159 N  ND2   . ASN A 458 ? 0.45700 0.43270 0.40470 -0.00090 0.00230  0.03260  454 ASN A ND2   
3160 N  N     . GLY A 459 ? 0.36520 0.34590 0.31460 -0.00480 0.00150  0.05650  455 GLY A N     
3161 C  CA    . GLY A 459 ? 0.34450 0.33070 0.29070 -0.00620 0.00190  0.06230  455 GLY A CA    
3162 C  C     . GLY A 459 ? 0.39690 0.38960 0.33590 -0.00510 0.00020  0.06340  455 GLY A C     
3163 O  O     . GLY A 459 ? 0.38380 0.38280 0.31790 -0.00610 0.00100  0.06700  455 GLY A O     
3164 N  N     . MET A 460 ? 0.37780 0.36950 0.31580 -0.00320 -0.00220 0.06040  456 MET A N     
3165 C  CA    . MET A 460 ? 0.36220 0.36020 0.29260 -0.00260 -0.00420 0.06040  456 MET A CA    
3166 C  C     . MET A 460 ? 0.40830 0.41160 0.33110 -0.00260 -0.00190 0.05630  456 MET A C     
3167 O  O     . MET A 460 ? 0.39920 0.40870 0.31450 -0.00270 -0.00250 0.05720  456 MET A O     
3168 C  CB    . MET A 460 ? 0.36750 0.36340 0.29860 -0.00100 -0.00710 0.05670  456 MET A CB    
3169 C  CG    . MET A 460 ? 0.50940 0.50200 0.44740 -0.00040 -0.00960 0.06130  456 MET A CG    
3170 S  SD    . MET A 460 ? 0.60350 0.60170 0.53940 -0.00130 -0.01250 0.07070  456 MET A SD    
3171 C  CE    . MET A 460 ? 0.58750 0.59360 0.51170 -0.00150 -0.01460 0.06740  456 MET A CE    
3172 N  N     . GLU A 461 ? 0.34760 0.34900 0.27250 -0.00250 0.00080  0.05210  457 GLU A N     
3173 C  CA    . GLU A 461 ? 0.35880 0.36520 0.27800 -0.00200 0.00330  0.04830  457 GLU A CA    
3174 C  C     . GLU A 461 ? 0.38160 0.39510 0.29690 -0.00340 0.00550  0.05320  457 GLU A C     
3175 O  O     . GLU A 461 ? 0.39710 0.41630 0.30660 -0.00270 0.00770  0.05030  457 GLU A O     
3176 C  CB    . GLU A 461 ? 0.41130 0.41480 0.33480 -0.00180 0.00560  0.04390  457 GLU A CB    
3177 C  CG    . GLU A 461 ? 0.48510 0.48300 0.41140 -0.00040 0.00400  0.03840  457 GLU A CG    
3178 C  CD    . GLU A 461 ? 0.42910 0.42850 0.34990 0.00130  0.00230  0.03400  457 GLU A CD    
3179 O  OE1   . GLU A 461 ? 0.44580 0.44090 0.36890 0.00210  0.00040  0.03090  457 GLU A OE1   
3180 O  OE2   . GLU A 461 ? 0.45500 0.45970 0.36900 0.00170  0.00300  0.03350  457 GLU A OE2   
3181 N  N     . ILE A 462 ? 0.33230 0.34580 0.25080 -0.00530 0.00510  0.06050  458 ILE A N     
3182 C  CA    . ILE A 462 ? 0.41370 0.43490 0.32790 -0.00680 0.00720  0.06560  458 ILE A CA    
3183 C  C     . ILE A 462 ? 0.41900 0.44680 0.32320 -0.00610 0.00600  0.06550  458 ILE A C     
3184 O  O     . ILE A 462 ? 0.41130 0.44700 0.30950 -0.00680 0.00840  0.06740  458 ILE A O     
3185 C  CB    . ILE A 462 ? 0.42850 0.44810 0.34830 -0.00930 0.00680  0.07420  458 ILE A CB    
3186 C  CG1   . ILE A 462 ? 0.38770 0.40470 0.30860 -0.00920 0.00290  0.07890  458 ILE A CG1   
3187 C  CG2   . ILE A 462 ? 0.33670 0.34980 0.26550 -0.01050 0.00810  0.07330  458 ILE A CG2   
3188 C  CD1   . ILE A 462 ? 0.35470 0.37160 0.28010 -0.01160 0.00260  0.08850  458 ILE A CD1   
3189 N  N     . HIS A 463 ? 0.36200 0.38740 0.26430 -0.00500 0.00240  0.06330  459 HIS A N     
3190 C  CA    . HIS A 463 ? 0.41010 0.44160 0.30220 -0.00460 0.00100  0.06180  459 HIS A CA    
3191 C  C     . HIS A 463 ? 0.35800 0.39240 0.24410 -0.00300 0.00390  0.05370  459 HIS A C     
3192 O  O     . HIS A 463 ? 0.39990 0.44140 0.27680 -0.00300 0.00510  0.05280  459 HIS A O     
3193 C  CB    . HIS A 463 ? 0.38950 0.41770 0.28200 -0.00400 -0.00380 0.06110  459 HIS A CB    
3194 C  CG    . HIS A 463 ? 0.38600 0.42030 0.26790 -0.00420 -0.00600 0.05960  459 HIS A CG    
3195 N  ND1   . HIS A 463 ? 0.36210 0.39520 0.23960 -0.00300 -0.00740 0.05150  459 HIS A ND1   
3196 C  CD2   . HIS A 463 ? 0.38240 0.42420 0.25700 -0.00580 -0.00730 0.06510  459 HIS A CD2   
3197 C  CE1   . HIS A 463 ? 0.44810 0.48740 0.31580 -0.00390 -0.00950 0.05160  459 HIS A CE1   
3198 N  NE2   . HIS A 463 ? 0.36110 0.40620 0.22650 -0.00560 -0.00950 0.05980  459 HIS A NE2   
3199 N  N     . THR A 464 ? 0.38840 0.41730 0.27970 -0.00150 0.00510  0.04790  460 THR A N     
3200 C  CA    . THR A 464 ? 0.35760 0.38860 0.24520 0.00030  0.00810  0.04080  460 THR A CA    
3201 C  C     . THR A 464 ? 0.39340 0.43190 0.27890 -0.00010 0.01270  0.04320  460 THR A C     
3202 O  O     . THR A 464 ? 0.36220 0.40630 0.24060 0.00120  0.01530  0.03930  460 THR A O     
3203 C  CB    . THR A 464 ? 0.36170 0.38580 0.25690 0.00160  0.00840  0.03600  460 THR A CB    
3204 O  OG1   . THR A 464 ? 0.35860 0.37660 0.25560 0.00200  0.00440  0.03390  460 THR A OG1   
3205 C  CG2   . THR A 464 ? 0.36100 0.38700 0.25380 0.00390  0.01140  0.02920  460 THR A CG2   
3206 N  N     . ALA A 465 ? 0.37500 0.41350 0.26700 -0.00190 0.01400  0.04930  461 ALA A N     
3207 C  CA    . ALA A 465 ? 0.40580 0.45220 0.29680 -0.00290 0.01820  0.05280  461 ALA A CA    
3208 C  C     . ALA A 465 ? 0.39390 0.44860 0.27560 -0.00390 0.01860  0.05690  461 ALA A C     
3209 O  O     . ALA A 465 ? 0.40000 0.46300 0.27650 -0.00340 0.02260  0.05620  461 ALA A O     
3210 C  CB    . ALA A 465 ? 0.40710 0.45110 0.30740 -0.00530 0.01870  0.05900  461 ALA A CB    
3211 N  N     . ALA A 466 ? 0.36540 0.41880 0.24510 -0.00530 0.01470  0.06170  462 ALA A N     
3212 C  CA    . ALA A 466 ? 0.41280 0.47450 0.28280 -0.00650 0.01440  0.06600  462 ALA A CA    
3213 C  C     . ALA A 466 ? 0.44470 0.51040 0.30390 -0.00460 0.01490  0.05800  462 ALA A C     
3214 O  O     . ALA A 466 ? 0.40820 0.48290 0.25880 -0.00480 0.01800  0.05810  462 ALA A O     
3215 C  CB    . ALA A 466 ? 0.32610 0.38530 0.19750 -0.00830 0.00940  0.07300  462 ALA A CB    
3216 N  N     . GLU A 467 ? 0.38520 0.44390 0.24480 -0.00280 0.01210  0.05090  463 GLU A N     
3217 C  CA    . GLU A 467 ? 0.34390 0.40450 0.19380 -0.00120 0.01200  0.04270  463 GLU A CA    
3218 C  C     . GLU A 467 ? 0.45620 0.52180 0.30270 0.00080  0.01780  0.03720  463 GLU A C     
3219 O  O     . GLU A 467 ? 0.41590 0.48810 0.25180 0.00130  0.01960  0.03380  463 GLU A O     
3220 C  CB    . GLU A 467 ? 0.39580 0.44730 0.24960 0.00020  0.00840  0.03630  463 GLU A CB    
3221 C  CG    . GLU A 467 ? 0.41330 0.46170 0.26750 -0.00140 0.00240  0.03960  463 GLU A CG    
3222 C  CD    . GLU A 467 ? 0.54330 0.59750 0.38530 -0.00240 -0.00020 0.03830  463 GLU A CD    
3223 O  OE1   . GLU A 467 ? 0.51110 0.56390 0.34750 -0.00130 -0.00070 0.02980  463 GLU A OE1   
3224 O  OE2   . GLU A 467 ? 0.50740 0.56750 0.34560 -0.00460 -0.00170 0.04590  463 GLU A OE2   
3225 N  N     . TYR A 468 ? 0.41660 0.47970 0.27200 0.00210  0.02090  0.03620  464 TYR A N     
3226 C  CA    . TYR A 468 ? 0.37670 0.44460 0.23110 0.00440  0.02650  0.03130  464 TYR A CA    
3227 C  C     . TYR A 468 ? 0.39570 0.47230 0.25170 0.00310  0.03090  0.03800  464 TYR A C     
3228 O  O     . TYR A 468 ? 0.41250 0.49380 0.26980 0.00510  0.03590  0.03510  464 TYR A O     
3229 C  CB    . TYR A 468 ? 0.45190 0.51230 0.31540 0.00680  0.02690  0.02580  464 TYR A CB    
3230 C  CG    . TYR A 468 ? 0.42700 0.47980 0.28860 0.00840  0.02340  0.01820  464 TYR A CG    
3231 C  CD1   . TYR A 468 ? 0.38730 0.44090 0.24260 0.01110  0.02540  0.00980  464 TYR A CD1   
3232 C  CD2   . TYR A 468 ? 0.39350 0.43830 0.25970 0.00720  0.01830  0.01960  464 TYR A CD2   
3233 C  CE1   . TYR A 468 ? 0.33140 0.37750 0.18540 0.01210  0.02190  0.00300  464 TYR A CE1   
3234 C  CE2   . TYR A 468 ? 0.37790 0.41640 0.24300 0.00820  0.01520  0.01320  464 TYR A CE2   
3235 C  CZ    . TYR A 468 ? 0.35290 0.39180 0.21200 0.01050  0.01670  0.00510  464 TYR A CZ    
3236 O  OH    . TYR A 468 ? 0.37270 0.40480 0.23130 0.01110  0.01330  -0.00090 464 TYR A OH    
3237 N  N     . LYS A 469 ? 0.38880 0.46760 0.24570 -0.00010 0.02930  0.04730  465 LYS A N     
3238 C  CA    . LYS A 469 ? 0.43320 0.52050 0.29190 -0.00200 0.03320  0.05470  465 LYS A CA    
3239 C  C     . LYS A 469 ? 0.43010 0.51610 0.29980 -0.00140 0.03620  0.05430  465 LYS A C     
3240 O  O     . LYS A 469 ? 0.38170 0.47570 0.25180 -0.00040 0.04140  0.05370  465 LYS A O     
3241 C  CB    . LYS A 469 ? 0.41200 0.51090 0.25940 -0.00150 0.03740  0.05360  465 LYS A CB    
3242 C  CG    . LYS A 469 ? 0.60430 0.71280 0.45100 -0.00460 0.03990  0.06380  465 LYS A CG    
3243 C  CD    . LYS A 469 ? 0.69890 0.81960 0.53260 -0.00430 0.04390  0.06290  465 LYS A CD    
3244 C  CE    . LYS A 469 ? 0.71860 0.85050 0.55390 -0.00670 0.04860  0.07180  465 LYS A CE    
3245 N  NZ    . LYS A 469 ? 0.74360 0.88410 0.56870 -0.00980 0.04790  0.07930  465 LYS A NZ    
3246 N  N     . ILE A 470 ? 0.42470 0.50120 0.30360 -0.00190 0.03300  0.05440  466 ILE A N     
3247 C  CA    . ILE A 470 ? 0.39070 0.46530 0.28000 -0.00180 0.03490  0.05400  466 ILE A CA    
3248 C  C     . ILE A 470 ? 0.41440 0.48910 0.31050 -0.00580 0.03430  0.06330  466 ILE A C     
3249 O  O     . ILE A 470 ? 0.38140 0.44870 0.28040 -0.00760 0.03020  0.06660  466 ILE A O     
3250 C  CB    . ILE A 470 ? 0.42770 0.49200 0.32220 0.00000  0.03190  0.04780  466 ILE A CB    
3251 C  CG1   . ILE A 470 ? 0.35110 0.41450 0.23890 0.00370  0.03220  0.03900  466 ILE A CG1   
3252 C  CG2   . ILE A 470 ? 0.40760 0.47080 0.31220 -0.00020 0.03360  0.04770  466 ILE A CG2   
3253 C  CD1   . ILE A 470 ? 0.37000 0.42330 0.26150 0.00510  0.02870  0.03340  466 ILE A CD1   
3254 N  N     . PRO A 471 ? 0.38680 0.47000 0.28580 -0.00730 0.03830  0.06780  467 PRO A N     
3255 C  CA    . PRO A 471 ? 0.40540 0.48860 0.31060 -0.01160 0.03750  0.07710  467 PRO A CA    
3256 C  C     . PRO A 471 ? 0.37480 0.45010 0.29110 -0.01310 0.03570  0.07700  467 PRO A C     
3257 O  O     . PRO A 471 ? 0.40620 0.48490 0.32860 -0.01340 0.03830  0.07620  467 PRO A O     
3258 C  CB    . PRO A 471 ? 0.43660 0.53290 0.34070 -0.01280 0.04270  0.08170  467 PRO A CB    
3259 C  CG    . PRO A 471 ? 0.46220 0.56530 0.35850 -0.00860 0.04650  0.07430  467 PRO A CG    
3260 C  CD    . PRO A 471 ? 0.40320 0.49700 0.29890 -0.00510 0.04380  0.06510  467 PRO A CD    
3261 N  N     . VAL A 472 ? 0.34500 0.41000 0.26390 -0.01410 0.03130  0.07760  468 VAL A N     
3262 C  CA    . VAL A 472 ? 0.35750 0.41420 0.28590 -0.01610 0.02930  0.07770  468 VAL A CA    
3263 C  C     . VAL A 472 ? 0.39320 0.44520 0.32490 -0.01950 0.02690  0.08550  468 VAL A C     
3264 O  O     . VAL A 472 ? 0.34700 0.39830 0.27380 -0.01920 0.02500  0.08840  468 VAL A O     
3265 C  CB    . VAL A 472 ? 0.35800 0.40550 0.28700 -0.01340 0.02660  0.07000  468 VAL A CB    
3266 C  CG1   . VAL A 472 ? 0.29440 0.33270 0.23160 -0.01580 0.02410  0.07090  468 VAL A CG1   
3267 C  CG2   . VAL A 472 ? 0.32490 0.37590 0.25340 -0.01040 0.02890  0.06310  468 VAL A CG2   
3268 N  N     . THR A 473 ? 0.36530 0.41360 0.30560 -0.02290 0.02650  0.08860  469 THR A N     
3269 C  CA    . THR A 473 ? 0.32990 0.37210 0.27480 -0.02620 0.02420  0.09560  469 THR A CA    
3270 C  C     . THR A 473 ? 0.40660 0.43640 0.35740 -0.02630 0.02120  0.09170  469 THR A C     
3271 O  O     . THR A 473 ? 0.35990 0.38700 0.31570 -0.02740 0.02150  0.08800  469 THR A O     
3272 C  CB    . THR A 473 ? 0.38280 0.43000 0.33340 -0.03060 0.02610  0.10290  469 THR A CB    
3273 O  OG1   . THR A 473 ? 0.36720 0.42690 0.31210 -0.03040 0.02940  0.10680  469 THR A OG1   
3274 C  CG2   . THR A 473 ? 0.31630 0.35580 0.27220 -0.03380 0.02340  0.11000  469 THR A CG2   
3275 N  N     . TRP A 474 ? 0.29640 0.31910 0.24650 -0.02520 0.01830  0.09250  470 TRP A N     
3276 C  CA    . TRP A 474 ? 0.35200 0.36290 0.30800 -0.02530 0.01580  0.08960  470 TRP A CA    
3277 C  C     . TRP A 474 ? 0.40060 0.40570 0.36380 -0.02890 0.01480  0.09650  470 TRP A C     
3278 O  O     . TRP A 474 ? 0.36310 0.36970 0.32580 -0.02960 0.01400  0.10380  470 TRP A O     
3279 C  CB    . TRP A 474 ? 0.29190 0.29820 0.24440 -0.02170 0.01340  0.08620  470 TRP A CB    
3280 C  CG    . TRP A 474 ? 0.31540 0.32430 0.26250 -0.01850 0.01390  0.07830  470 TRP A CG    
3281 C  CD1   . TRP A 474 ? 0.35940 0.36300 0.30860 -0.01720 0.01340  0.07130  470 TRP A CD1   
3282 C  CD2   . TRP A 474 ? 0.33670 0.35400 0.27570 -0.01620 0.01500  0.07660  470 TRP A CD2   
3283 N  NE1   . TRP A 474 ? 0.33970 0.34750 0.28320 -0.01430 0.01400  0.06580  470 TRP A NE1   
3284 C  CE2   . TRP A 474 ? 0.37630 0.39200 0.31350 -0.01350 0.01500  0.06850  470 TRP A CE2   
3285 C  CE3   . TRP A 474 ? 0.34240 0.36820 0.27500 -0.01620 0.01600  0.08090  470 TRP A CE3   
3286 C  CZ2   . TRP A 474 ? 0.36590 0.38740 0.29590 -0.01090 0.01590  0.06440  470 TRP A CZ2   
3287 C  CZ3   . TRP A 474 ? 0.34730 0.37930 0.27190 -0.01360 0.01710  0.07630  470 TRP A CZ3   
3288 C  CH2   . TRP A 474 ? 0.28820 0.31750 0.21180 -0.01090 0.01700  0.06790  470 TRP A CH2   
3289 N  N     . ILE A 475 ? 0.36330 0.36160 0.33330 -0.03130 0.01450  0.09430  471 ILE A N     
3290 C  CA    . ILE A 475 ? 0.33880 0.32870 0.31650 -0.03470 0.01330  0.09920  471 ILE A CA    
3291 C  C     . ILE A 475 ? 0.38990 0.36820 0.37080 -0.03280 0.01130  0.09380  471 ILE A C     
3292 O  O     . ILE A 475 ? 0.41790 0.39230 0.39970 -0.03280 0.01150  0.08670  471 ILE A O     
3293 C  CB    . ILE A 475 ? 0.34210 0.33290 0.32540 -0.03940 0.01450  0.10050  471 ILE A CB    
3294 C  CG1   . ILE A 475 ? 0.30090 0.30450 0.28190 -0.04120 0.01690  0.10630  471 ILE A CG1   
3295 C  CG2   . ILE A 475 ? 0.30540 0.28570 0.29700 -0.04290 0.01290  0.10430  471 ILE A CG2   
3296 C  CD1   . ILE A 475 ? 0.34280 0.35020 0.32840 -0.04510 0.01830  0.10580  471 ILE A CD1   
3297 N  N     . VAL A 476 ? 0.33300 0.30620 0.31540 -0.03110 0.00960  0.09730  472 VAL A N     
3298 C  CA    . VAL A 476 ? 0.34610 0.30920 0.33180 -0.02870 0.00820  0.09260  472 VAL A CA    
3299 C  C     . VAL A 476 ? 0.37280 0.32540 0.36740 -0.03150 0.00770  0.09510  472 VAL A C     
3300 O  O     . VAL A 476 ? 0.36790 0.31900 0.36660 -0.03290 0.00690  0.10320  472 VAL A O     
3301 C  CB    . VAL A 476 ? 0.33790 0.30190 0.32080 -0.02470 0.00650  0.09460  472 VAL A CB    
3302 C  CG1   . VAL A 476 ? 0.30960 0.26420 0.29650 -0.02190 0.00550  0.08910  472 VAL A CG1   
3303 C  CG2   . VAL A 476 ? 0.35970 0.33390 0.33340 -0.02250 0.00690  0.09220  472 VAL A CG2   
3304 N  N     . LEU A 477 ? 0.34960 0.29490 0.34720 -0.03260 0.00800  0.08810  473 LEU A N     
3305 C  CA    . LEU A 477 ? 0.33120 0.26460 0.33700 -0.03480 0.00760  0.08820  473 LEU A CA    
3306 C  C     . LEU A 477 ? 0.40890 0.33490 0.41770 -0.03060 0.00660  0.08740  473 LEU A C     
3307 O  O     . LEU A 477 ? 0.41250 0.33510 0.41990 -0.02790 0.00690  0.08000  473 LEU A O     
3308 C  CB    . LEU A 477 ? 0.35540 0.28440 0.36190 -0.03750 0.00820  0.08040  473 LEU A CB    
3309 C  CG    . LEU A 477 ? 0.40020 0.33750 0.40460 -0.04150 0.00900  0.08110  473 LEU A CG    
3310 C  CD1   . LEU A 477 ? 0.38710 0.32000 0.39240 -0.04430 0.00900  0.07370  473 LEU A CD1   
3311 C  CD2   . LEU A 477 ? 0.39200 0.33080 0.40110 -0.04560 0.00890  0.09020  473 LEU A CD2   
3312 N  N     . ASN A 478 ? 0.36470 0.28920 0.37770 -0.02990 0.00550  0.09570  474 ASN A N     
3313 C  CA    . ASN A 478 ? 0.39110 0.31050 0.40770 -0.02550 0.00440  0.09650  474 ASN A CA    
3314 C  C     . ASN A 478 ? 0.44100 0.34660 0.46740 -0.02600 0.00460  0.09540  474 ASN A C     
3315 O  O     . ASN A 478 ? 0.37830 0.27910 0.41160 -0.02760 0.00380  0.10270  474 ASN A O     
3316 C  CB    . ASN A 478 ? 0.38940 0.31550 0.40510 -0.02420 0.00270  0.10630  474 ASN A CB    
3317 C  CG    . ASN A 478 ? 0.44270 0.36620 0.46150 -0.01950 0.00110  0.10750  474 ASN A CG    
3318 O  OD1   . ASN A 478 ? 0.40190 0.31780 0.42480 -0.01690 0.00160  0.10140  474 ASN A OD1   
3319 N  ND2   . ASN A 478 ? 0.34220 0.27260 0.35930 -0.01840 -0.00090 0.11580  474 ASN A ND2   
3320 N  N     . ASN A 479 ? 0.42190 0.32090 0.44900 -0.02480 0.00580  0.08610  475 ASN A N     
3321 C  CA    . ASN A 479 ? 0.35270 0.23820 0.38860 -0.02460 0.00640  0.08350  475 ASN A CA    
3322 C  C     . ASN A 479 ? 0.43150 0.31290 0.47140 -0.01900 0.00650  0.08170  475 ASN A C     
3323 O  O     . ASN A 479 ? 0.42600 0.29670 0.47190 -0.01780 0.00790  0.07660  475 ASN A O     
3324 C  CB    . ASN A 479 ? 0.34190 0.22200 0.37630 -0.02790 0.00790  0.07420  475 ASN A CB    
3325 C  CG    . ASN A 479 ? 0.45180 0.33830 0.47770 -0.02640 0.00880  0.06600  475 ASN A CG    
3326 O  OD1   . ASN A 479 ? 0.39950 0.29210 0.42170 -0.02230 0.00850  0.06580  475 ASN A OD1   
3327 N  ND2   . ASN A 479 ? 0.37770 0.26290 0.40060 -0.03010 0.00950  0.05950  475 ASN A ND2   
3328 N  N     . GLY A 480 ? 0.44490 0.33470 0.48180 -0.01550 0.00520  0.08570  476 GLY A N     
3329 C  CA    . GLY A 480 ? 0.35720 0.24460 0.39880 -0.01020 0.00490  0.08540  476 GLY A CA    
3330 C  C     . GLY A 480 ? 0.42210 0.30620 0.46260 -0.00790 0.00700  0.07490  476 GLY A C     
3331 O  O     . GLY A 480 ? 0.35110 0.22780 0.39910 -0.00460 0.00810  0.07280  476 GLY A O     
3332 N  N     . GLY A 481 ? 0.44040 0.33030 0.47200 -0.00940 0.00780  0.06850  477 GLY A N     
3333 C  CA    . GLY A 481 ? 0.40150 0.29010 0.43110 -0.00730 0.00960  0.05950  477 GLY A CA    
3334 C  C     . GLY A 481 ? 0.39090 0.28060 0.41340 -0.01090 0.01080  0.05230  477 GLY A C     
3335 O  O     . GLY A 481 ? 0.34090 0.23580 0.35860 -0.01440 0.00990  0.05440  477 GLY A O     
3336 N  N     . HIS A 482 ? 0.38590 0.27140 0.40810 -0.01000 0.01280  0.04400  478 HIS A N     
3337 C  CA    . HIS A 482 ? 0.36760 0.25520 0.38260 -0.01290 0.01370  0.03680  478 HIS A CA    
3338 C  C     . HIS A 482 ? 0.47190 0.35060 0.48920 -0.01700 0.01480  0.03310  478 HIS A C     
3339 O  O     . HIS A 482 ? 0.40440 0.27510 0.42440 -0.01640 0.01680  0.02700  478 HIS A O     
3340 C  CB    . HIS A 482 ? 0.34230 0.23160 0.35490 -0.00980 0.01520  0.03030  478 HIS A CB    
3341 C  CG    . HIS A 482 ? 0.41580 0.31340 0.42660 -0.00620 0.01390  0.03350  478 HIS A CG    
3342 N  ND1   . HIS A 482 ? 0.42630 0.33210 0.42990 -0.00630 0.01340  0.03100  478 HIS A ND1   
3343 C  CD2   . HIS A 482 ? 0.42110 0.32030 0.43660 -0.00260 0.01280  0.03900  478 HIS A CD2   
3344 C  CE1   . HIS A 482 ? 0.46240 0.37380 0.46600 -0.00320 0.01200  0.03440  478 HIS A CE1   
3345 N  NE2   . HIS A 482 ? 0.42450 0.33240 0.43500 -0.00100 0.01150  0.03930  478 HIS A NE2   
3346 N  N     . GLY A 483 ? 0.40580 0.28600 0.42220 -0.02140 0.01340  0.03700  479 GLY A N     
3347 C  CA    . GLY A 483 ? 0.44400 0.31610 0.46330 -0.02610 0.01370  0.03480  479 GLY A CA    
3348 C  C     . GLY A 483 ? 0.40900 0.27740 0.42440 -0.02840 0.01510  0.02500  479 GLY A C     
3349 O  O     . GLY A 483 ? 0.47520 0.33300 0.49450 -0.02910 0.01640  0.02030  479 GLY A O     
3350 N  N     . LEU A 484 ? 0.36550 0.24260 0.37320 -0.02950 0.01470  0.02200  480 LEU A N     
3351 C  CA    . LEU A 484 ? 0.46150 0.33660 0.46460 -0.03200 0.01560  0.01330  480 LEU A CA    
3352 C  C     . LEU A 484 ? 0.47340 0.34260 0.47740 -0.02830 0.01810  0.00700  480 LEU A C     
3353 O  O     . LEU A 484 ? 0.50170 0.36420 0.50470 -0.03040 0.01950  -0.00020 480 LEU A O     
3354 C  CB    . LEU A 484 ? 0.38080 0.26720 0.37620 -0.03310 0.01460  0.01240  480 LEU A CB    
3355 C  CG    . LEU A 484 ? 0.47660 0.36940 0.47100 -0.03730 0.01260  0.01720  480 LEU A CG    
3356 C  CD1   . LEU A 484 ? 0.46850 0.37160 0.45610 -0.03800 0.01180  0.01540  480 LEU A CD1   
3357 C  CD2   . LEU A 484 ? 0.47420 0.36010 0.47170 -0.04300 0.01200  0.01600  480 LEU A CD2   
3358 N  N     . VAL A 485 ? 0.47200 0.34390 0.47800 -0.02280 0.01880  0.00950  481 VAL A N     
3359 C  CA    . VAL A 485 ? 0.47100 0.33840 0.47880 -0.01890 0.02150  0.00400  481 VAL A CA    
3360 C  C     . VAL A 485 ? 0.48540 0.34030 0.50150 -0.01810 0.02310  0.00300  481 VAL A C     
3361 O  O     . VAL A 485 ? 0.43170 0.27950 0.44830 -0.01800 0.02570  -0.00460 481 VAL A O     
3362 C  CB    . VAL A 485 ? 0.46940 0.34380 0.47790 -0.01360 0.02150  0.00750  481 VAL A CB    
3363 C  CG1   . VAL A 485 ? 0.46880 0.33940 0.48020 -0.00950 0.02450  0.00240  481 VAL A CG1   
3364 C  CG2   . VAL A 485 ? 0.43870 0.32440 0.43930 -0.01440 0.01990  0.00800  481 VAL A CG2   
3365 N  N     . HIS A 486 ? 0.47520 0.32730 0.49810 -0.01780 0.02160  0.01060  482 HIS A N     
3366 C  CA    . HIS A 486 ? 0.43150 0.27110 0.46340 -0.01730 0.02270  0.01080  482 HIS A CA    
3367 C  C     . HIS A 486 ? 0.51740 0.34810 0.54790 -0.02260 0.02340  0.00380  482 HIS A C     
3368 O  O     . HIS A 486 ? 0.48650 0.30620 0.52160 -0.02160 0.02590  -0.00190 482 HIS A O     
3369 C  CB    . HIS A 486 ? 0.45820 0.29820 0.49620 -0.01740 0.02020  0.02150  482 HIS A CB    
3370 C  CG    . HIS A 486 ? 0.61550 0.44290 0.66420 -0.01650 0.02090  0.02360  482 HIS A CG    
3371 N  ND1   . HIS A 486 ? 0.68050 0.50420 0.73760 -0.01070 0.02210  0.02620  482 HIS A ND1   
3372 C  CD2   . HIS A 486 ? 0.64620 0.46390 0.69920 -0.02080 0.02050  0.02390  482 HIS A CD2   
3373 C  CE1   . HIS A 486 ? 0.67800 0.48980 0.74440 -0.01110 0.02240  0.02810  482 HIS A CE1   
3374 N  NE2   . HIS A 486 ? 0.69050 0.49810 0.75460 -0.01730 0.02140  0.02660  482 HIS A NE2   
3375 N  N     . LEU A 487 ? 0.48300 0.31830 0.50780 -0.02830 0.02130  0.00430  483 LEU A N     
3376 C  CA    . LEU A 487 ? 0.52410 0.35170 0.54710 -0.03400 0.02140  -0.00240 483 LEU A CA    
3377 C  C     . LEU A 487 ? 0.47070 0.29740 0.48730 -0.03370 0.02380  -0.01310 483 LEU A C     
3378 O  O     . LEU A 487 ? 0.54800 0.36430 0.56560 -0.03570 0.02550  -0.02060 483 LEU A O     
3379 C  CB    . LEU A 487 ? 0.52520 0.35970 0.54410 -0.04010 0.01840  0.00110  483 LEU A CB    
3380 C  CG    . LEU A 487 ? 0.55810 0.39380 0.58300 -0.04130 0.01620  0.01160  483 LEU A CG    
3381 C  CD1   . LEU A 487 ? 0.54180 0.38870 0.56140 -0.04570 0.01390  0.01530  483 LEU A CD1   
3382 C  CD2   . LEU A 487 ? 0.55690 0.37910 0.59030 -0.04420 0.01610  0.01220  483 LEU A CD2   
3383 N  N     . GLY A 488 ? 0.49300 0.33020 0.50310 -0.03130 0.02420  -0.01410 484 GLY A N     
3384 C  CA    . GLY A 488 ? 0.52670 0.36390 0.53080 -0.03060 0.02680  -0.02330 484 GLY A CA    
3385 C  C     . GLY A 488 ? 0.59010 0.41800 0.60010 -0.02580 0.03070  -0.02800 484 GLY A C     
3386 O  O     . GLY A 488 ? 0.53750 0.35930 0.54460 -0.02700 0.03330  -0.03710 484 GLY A O     
3387 N  N     . GLU A 489 ? 0.54000 0.36690 0.55820 -0.02030 0.03120  -0.02180 485 GLU A N     
3388 C  CA    . GLU A 489 ? 0.52500 0.34310 0.55070 -0.01530 0.03490  -0.02550 485 GLU A CA    
3389 C  C     . GLU A 489 ? 0.54410 0.34770 0.57450 -0.01810 0.03610  -0.03040 485 GLU A C     
3390 O  O     . GLU A 489 ? 0.60330 0.39900 0.63490 -0.01630 0.03990  -0.03880 485 GLU A O     
3391 C  CB    . GLU A 489 ? 0.48830 0.30810 0.52340 -0.00960 0.03440  -0.01650 485 GLU A CB    
3392 C  CG    . GLU A 489 ? 0.54880 0.38170 0.58050 -0.00630 0.03350  -0.01220 485 GLU A CG    
3393 C  CD    . GLU A 489 ? 0.59870 0.43440 0.63830 -0.00250 0.03140  -0.00200 485 GLU A CD    
3394 O  OE1   . GLU A 489 ? 0.64990 0.49500 0.68840 0.00070  0.03080  0.00130  485 GLU A OE1   
3395 O  OE2   . GLU A 489 ? 0.67660 0.50500 0.72350 -0.00300 0.03030  0.00290  485 GLU A OE2   
3396 N  N     . GLN A 490 ? 0.51290 0.31260 0.54600 -0.02250 0.03290  -0.02530 486 GLN A N     
3397 C  CA    . GLN A 490 ? 0.59060 0.37570 0.62910 -0.02560 0.03340  -0.02910 486 GLN A CA    
3398 C  C     . GLN A 490 ? 0.61180 0.39370 0.64130 -0.03150 0.03390  -0.03980 486 GLN A C     
3399 O  O     . GLN A 490 ? 0.64120 0.41120 0.67270 -0.03200 0.03660  -0.04830 486 GLN A O     
3400 C  CB    . GLN A 490 ? 0.60620 0.38950 0.65030 -0.02910 0.02960  -0.01960 486 GLN A CB    
3401 C  CG    . GLN A 490 ? 0.62630 0.41290 0.67880 -0.02410 0.02860  -0.00840 486 GLN A CG    
3402 C  CD    . GLN A 490 ? 0.71390 0.49960 0.77080 -0.02820 0.02510  0.00120  486 GLN A CD    
3403 O  OE1   . GLN A 490 ? 0.70150 0.49250 0.75250 -0.03410 0.02260  0.00220  486 GLN A OE1   
3404 N  NE2   . GLN A 490 ? 0.71370 0.49320 0.78160 -0.02510 0.02480  0.00860  486 GLN A NE2   
3405 N  N     . HIS A 491 ? 0.61310 0.40570 0.63300 -0.03620 0.03130  -0.03950 487 HIS A N     
3406 C  CA    . HIS A 491 ? 0.60500 0.39550 0.61660 -0.04300 0.03060  -0.04790 487 HIS A CA    
3407 C  C     . HIS A 491 ? 0.66640 0.46130 0.66860 -0.04190 0.03340  -0.05710 487 HIS A C     
3408 O  O     . HIS A 491 ? 0.63520 0.42670 0.63060 -0.04700 0.03360  -0.06580 487 HIS A O     
3409 C  CB    . HIS A 491 ? 0.62880 0.42840 0.63610 -0.04910 0.02600  -0.04230 487 HIS A CB    
3410 C  CG    . HIS A 491 ? 0.74110 0.53480 0.75650 -0.05240 0.02340  -0.03540 487 HIS A CG    
3411 N  ND1   . HIS A 491 ? 0.75420 0.55140 0.77650 -0.04930 0.02220  -0.02450 487 HIS A ND1   
3412 C  CD2   . HIS A 491 ? 0.77990 0.56410 0.79780 -0.05880 0.02170  -0.03780 487 HIS A CD2   
3413 C  CE1   . HIS A 491 ? 0.79040 0.58110 0.81920 -0.05350 0.02010  -0.01990 487 HIS A CE1   
3414 N  NE2   . HIS A 491 ? 0.81400 0.59660 0.84070 -0.05930 0.01970  -0.02780 487 HIS A NE2   
3415 N  N     . GLN A 492 ? 0.52450 0.32780 0.52580 -0.03590 0.03540  -0.05520 488 GLN A N     
3416 C  CA    . GLN A 492 ? 0.55650 0.36470 0.54930 -0.03480 0.03830  -0.06300 488 GLN A CA    
3417 C  C     . GLN A 492 ? 0.61010 0.41490 0.60780 -0.02750 0.04340  -0.06620 488 GLN A C     
3418 O  O     . GLN A 492 ? 0.65180 0.45850 0.64310 -0.02680 0.04670  -0.07410 488 GLN A O     
3419 C  CB    . GLN A 492 ? 0.62850 0.45230 0.61380 -0.03530 0.03600  -0.05840 488 GLN A CB    
3420 C  CG    . GLN A 492 ? 0.72260 0.55200 0.70460 -0.04140 0.03110  -0.05350 488 GLN A CG    
3421 C  CD    . GLN A 492 ? 0.81540 0.65940 0.79100 -0.04110 0.02920  -0.04930 488 GLN A CD    
3422 O  OE1   . GLN A 492 ? 0.84570 0.69610 0.82440 -0.03920 0.02720  -0.04080 488 GLN A OE1   
3423 N  NE2   . GLN A 492 ? 0.82710 0.67640 0.79360 -0.04320 0.02980  -0.05520 488 GLN A NE2   
3424 N  N     . PHE A 493 ? 0.61910 0.41970 0.62830 -0.02210 0.04410  -0.06000 489 PHE A N     
3425 C  CA    . PHE A 493 ? 0.59110 0.38960 0.60650 -0.01480 0.04880  -0.06210 489 PHE A CA    
3426 C  C     . PHE A 493 ? 0.60880 0.39330 0.63670 -0.01150 0.05060  -0.06200 489 PHE A C     
3427 O  O     . PHE A 493 ? 0.62450 0.40820 0.66110 -0.00470 0.05350  -0.06000 489 PHE A O     
3428 C  CB    . PHE A 493 ? 0.54550 0.35640 0.56260 -0.01000 0.04780  -0.05380 489 PHE A CB    
3429 C  CG    . PHE A 493 ? 0.54730 0.37100 0.55330 -0.01190 0.04710  -0.05520 489 PHE A CG    
3430 C  CD1   . PHE A 493 ? 0.58080 0.40830 0.58260 -0.00950 0.05130  -0.06180 489 PHE A CD1   
3431 C  CD2   . PHE A 493 ? 0.51440 0.34660 0.51460 -0.01600 0.04250  -0.04960 489 PHE A CD2   
3432 C  CE1   . PHE A 493 ? 0.54780 0.38690 0.53970 -0.01150 0.05040  -0.06230 489 PHE A CE1   
3433 C  CE2   . PHE A 493 ? 0.51340 0.35680 0.50420 -0.01760 0.04180  -0.05050 489 PHE A CE2   
3434 C  CZ    . PHE A 493 ? 0.50700 0.35380 0.49380 -0.01550 0.04560  -0.05660 489 PHE A CZ    
3435 N  N     . ASP A 494 ? 0.58740 0.36080 0.61710 -0.01640 0.04900  -0.06380 490 ASP A N     
3436 C  CA    . ASP A 494 ? 0.66510 0.42300 0.70660 -0.01410 0.05090  -0.06520 490 ASP A CA    
3437 C  C     . ASP A 494 ? 0.67860 0.43680 0.73300 -0.00780 0.05030  -0.05440 490 ASP A C     
3438 O  O     . ASP A 494 ? 0.71490 0.46340 0.78030 -0.00260 0.05350  -0.05550 490 ASP A O     
3439 C  CB    . ASP A 494 ? 0.77910 0.52840 0.82060 -0.01110 0.05690  -0.07750 490 ASP A CB    
3440 C  CG    . ASP A 494 ? 0.91430 0.66330 0.94240 -0.01740 0.05760  -0.08870 490 ASP A CG    
3441 O  OD1   . ASP A 494 ? 0.92090 0.66240 0.94660 -0.02420 0.05490  -0.09130 490 ASP A OD1   
3442 O  OD2   . ASP A 494 ? 0.96850 0.72510 0.98860 -0.01580 0.06090  -0.09470 490 ASP A OD2   
3443 N  N     . SER A 495 ? 0.57280 0.34220 0.62630 -0.00820 0.04620  -0.04380 491 SER A N     
3444 C  CA    . SER A 495 ? 0.59900 0.37000 0.66350 -0.00300 0.04490  -0.03280 491 SER A CA    
3445 C  C     . SER A 495 ? 0.63450 0.40600 0.70600 0.00520  0.04920  -0.03460 491 SER A C     
3446 O  O     . SER A 495 ? 0.70120 0.46850 0.78510 0.01020  0.04950  -0.02830 491 SER A O     
3447 C  CB    . SER A 495 ? 0.66470 0.42340 0.73960 -0.00440 0.04310  -0.02780 491 SER A CB    
3448 O  OG    . SER A 495 ? 0.73300 0.49260 0.80240 -0.01190 0.03910  -0.02490 491 SER A OG    
3449 N  N     . LYS A 496 ? 0.65090 0.42830 0.71500 0.00650  0.05260  -0.04250 492 LYS A N     
3450 C  CA    . LYS A 496 ? 0.60600 0.38510 0.67650 0.01390  0.05710  -0.04470 492 LYS A CA    
3451 C  C     . LYS A 496 ? 0.56030 0.35120 0.63560 0.01840  0.05490  -0.03410 492 LYS A C     
3452 O  O     . LYS A 496 ? 0.63820 0.43000 0.72280 0.02500  0.05780  -0.03300 492 LYS A O     
3453 C  CB    . LYS A 496 ? 0.63210 0.41580 0.69230 0.01340  0.06120  -0.05540 492 LYS A CB    
3454 C  CG    . LYS A 496 ? 0.71920 0.49020 0.77770 0.01180  0.06550  -0.06770 492 LYS A CG    
3455 C  CD    . LYS A 496 ? 0.76710 0.54450 0.81540 0.01190  0.06990  -0.07750 492 LYS A CD    
3456 C  CE    . LYS A 496 ? 0.73940 0.52650 0.77260 0.00490  0.06640  -0.07820 492 LYS A CE    
3457 N  NZ    . LYS A 496 ? 0.73110 0.52990 0.75590 0.00610  0.06920  -0.08210 492 LYS A NZ    
3458 N  N     . PHE A 497 ? 0.57600 0.37650 0.64510 0.01490  0.05000  -0.02680 493 PHE A N     
3459 C  CA    . PHE A 497 ? 0.51640 0.32830 0.58830 0.01840  0.04740  -0.01740 493 PHE A CA    
3460 C  C     . PHE A 497 ? 0.52870 0.34550 0.59590 0.01370  0.04190  -0.00910 493 PHE A C     
3461 O  O     . PHE A 497 ? 0.47540 0.29040 0.53490 0.00780  0.04030  -0.01170 493 PHE A O     
3462 C  CB    . PHE A 497 ? 0.50110 0.32470 0.56640 0.02010  0.04920  -0.02080 493 PHE A CB    
3463 C  CG    . PHE A 497 ? 0.59410 0.42300 0.64480 0.01420  0.04840  -0.02620 493 PHE A CG    
3464 C  CD1   . PHE A 497 ? 0.56360 0.40170 0.60710 0.01070  0.04390  -0.02040 493 PHE A CD1   
3465 C  CD2   . PHE A 497 ? 0.63810 0.46300 0.68250 0.01220  0.05220  -0.03690 493 PHE A CD2   
3466 C  CE1   . PHE A 497 ? 0.56180 0.40490 0.59320 0.00560  0.04300  -0.02480 493 PHE A CE1   
3467 C  CE2   . PHE A 497 ? 0.52380 0.35400 0.55520 0.00670  0.05110  -0.04110 493 PHE A CE2   
3468 C  CZ    . PHE A 497 ? 0.57880 0.41810 0.60430 0.00360  0.04640  -0.03480 493 PHE A CZ    
3469 N  N     . ASP A 498 ? 0.53150 0.35550 0.60340 0.01650  0.03890  0.00070  494 ASP A N     
3470 C  CA    . ASP A 498 ? 0.55890 0.38910 0.62660 0.01290  0.03400  0.00910  494 ASP A CA    
3471 C  C     . ASP A 498 ? 0.54550 0.38930 0.60940 0.01500  0.03190  0.01360  494 ASP A C     
3472 O  O     . ASP A 498 ? 0.56570 0.41290 0.63720 0.01990  0.03170  0.01860  494 ASP A O     
3473 C  CB    . ASP A 498 ? 0.55510 0.37880 0.63270 0.01360  0.03170  0.01780  494 ASP A CB    
3474 C  CG    . ASP A 498 ? 0.63730 0.46780 0.71000 0.00970  0.02710  0.02630  494 ASP A CG    
3475 O  OD1   . ASP A 498 ? 0.63050 0.47280 0.69780 0.01030  0.02500  0.03000  494 ASP A OD1   
3476 O  OD2   . ASP A 498 ? 0.75230 0.57640 0.82670 0.00590  0.02570  0.02920  494 ASP A OD2   
3477 N  N     . ILE A 499 ? 0.50200 0.35370 0.55460 0.01120  0.03040  0.01190  495 ILE A N     
3478 C  CA    . ILE A 499 ? 0.49330 0.35730 0.54140 0.01220  0.02800  0.01610  495 ILE A CA    
3479 C  C     . ILE A 499 ? 0.50920 0.37850 0.55040 0.00790  0.02410  0.02130  495 ILE A C     
3480 O  O     . ILE A 499 ? 0.57600 0.45460 0.60990 0.00700  0.02250  0.02190  495 ILE A O     
3481 C  CB    . ILE A 499 ? 0.50760 0.37720 0.54930 0.01260  0.03030  0.00890  495 ILE A CB    
3482 C  CG1   . ILE A 499 ? 0.48410 0.36520 0.52380 0.01460  0.02810  0.01320  495 ILE A CG1   
3483 C  CG2   . ILE A 499 ? 0.47910 0.34810 0.51060 0.00730  0.03070  0.00270  495 ILE A CG2   
3484 C  CD1   . ILE A 499 ? 0.53390 0.41680 0.58380 0.01970  0.02750  0.01900  495 ILE A CD1   
3485 N  N     . SER A 500 ? 0.55160 0.41470 0.59530 0.00530  0.02300  0.02470  496 SER A N     
3486 C  CA    . SER A 500 ? 0.54900 0.41600 0.58640 0.00060  0.02020  0.02850  496 SER A CA    
3487 C  C     . SER A 500 ? 0.49510 0.36260 0.53740 0.00070  0.01740  0.03860  496 SER A C     
3488 O  O     . SER A 500 ? 0.49240 0.36750 0.52910 -0.00170 0.01500  0.04320  496 SER A O     
3489 C  CB    . SER A 500 ? 0.45730 0.31730 0.49190 -0.00440 0.02130  0.02300  496 SER A CB    
3490 O  OG    . SER A 500 ? 0.55690 0.40480 0.60010 -0.00360 0.02300  0.02160  496 SER A OG    
3491 N  N     . SER A 501 ? 0.44840 0.30840 0.50110 0.00340  0.01780  0.04230  497 SER A N     
3492 C  CA    . SER A 501 ? 0.52140 0.38110 0.57930 0.00300  0.01510  0.05250  497 SER A CA    
3493 C  C     . SER A 501 ? 0.51120 0.37930 0.57140 0.00710  0.01290  0.05950  497 SER A C     
3494 O  O     . SER A 501 ? 0.58780 0.45590 0.65300 0.01160  0.01410  0.05770  497 SER A O     
3495 C  CB    . SER A 501 ? 0.49600 0.34270 0.56510 0.00360  0.01630  0.05380  497 SER A CB    
3496 O  OG    . SER A 501 ? 0.62080 0.45860 0.68840 0.00030  0.01870  0.04560  497 SER A OG    
3497 N  N     . PHE A 502 ? 0.43340 0.30910 0.48970 0.00530  0.00980  0.06730  498 PHE A N     
3498 C  CA    . PHE A 502 ? 0.45580 0.33880 0.51470 0.00860  0.00710  0.07490  498 PHE A CA    
3499 C  C     . PHE A 502 ? 0.47570 0.35170 0.54720 0.01120  0.00650  0.08210  498 PHE A C     
3500 O  O     . PHE A 502 ? 0.46340 0.33140 0.53940 0.00890  0.00670  0.08490  498 PHE A O     
3501 C  CB    . PHE A 502 ? 0.45450 0.34770 0.50480 0.00580  0.00410  0.08090  498 PHE A CB    
3502 C  CG    . PHE A 502 ? 0.40890 0.30940 0.44760 0.00380  0.00450  0.07470  498 PHE A CG    
3503 C  CD1   . PHE A 502 ? 0.38320 0.28440 0.41980 0.00580  0.00620  0.06670  498 PHE A CD1   
3504 C  CD2   . PHE A 502 ? 0.34080 0.24780 0.37130 0.00020  0.00330  0.07720  498 PHE A CD2   
3505 C  CE1   . PHE A 502 ? 0.36260 0.27030 0.38950 0.00410  0.00640  0.06160  498 PHE A CE1   
3506 C  CE2   . PHE A 502 ? 0.37450 0.28800 0.39540 -0.00110 0.00380  0.07160  498 PHE A CE2   
3507 C  CZ    . PHE A 502 ? 0.39980 0.31320 0.41900 0.00080  0.00510  0.06390  498 PHE A CZ    
3508 N  N     . ARG A 503 ? 0.43840 0.31770 0.51620 0.01590  0.00540  0.08550  499 ARG A N     
3509 C  CA    . ARG A 503 ? 0.50390 0.37890 0.59380 0.01860  0.00390  0.09440  499 ARG A CA    
3510 C  C     . ARG A 503 ? 0.49430 0.37490 0.58160 0.01580  0.00010  0.10530  499 ARG A C     
3511 O  O     . ARG A 503 ? 0.42040 0.29480 0.51630 0.01560  -0.00080 0.11260  499 ARG A O     
3512 C  CB    . ARG A 503 ? 0.52070 0.39940 0.61870 0.02430  0.00340  0.09610  499 ARG A CB    
3513 C  CG    . ARG A 503 ? 0.70100 0.57300 0.81420 0.02790  0.00270  0.10390  499 ARG A CG    
3514 C  CD    . ARG A 503 ? 0.77560 0.64870 0.89840 0.03400  0.00400  0.10230  499 ARG A CD    
3515 N  NE    . ARG A 503 ? 0.74130 0.62810 0.85840 0.03470  0.00090  0.10450  499 ARG A NE    
3516 C  CZ    . ARG A 503 ? 0.69610 0.59100 0.81600 0.03570  -0.00380 0.11500  499 ARG A CZ    
3517 N  NH1   . ARG A 503 ? 0.61160 0.50250 0.74030 0.03630  -0.00580 0.12480  499 ARG A NH1   
3518 N  NH2   . ARG A 503 ? 0.63840 0.54530 0.75230 0.03570  -0.00660 0.11580  499 ARG A NH2   
3519 N  N     . LYS A 504 ? 0.50440 0.39650 0.58020 0.01340  -0.00220 0.10690  500 LYS A N     
3520 C  CA    . LYS A 504 ? 0.51590 0.41280 0.58940 0.01060  -0.00520 0.11720  500 LYS A CA    
3521 C  C     . LYS A 504 ? 0.50980 0.41410 0.56890 0.00640  -0.00490 0.11300  500 LYS A C     
3522 O  O     . LYS A 504 ? 0.47440 0.38620 0.52580 0.00720  -0.00520 0.10790  500 LYS A O     
3523 C  CB    . LYS A 504 ? 0.64750 0.55190 0.72480 0.01360  -0.00910 0.12640  500 LYS A CB    
3524 C  CG    . LYS A 504 ? 0.79820 0.70800 0.87470 0.01120  -0.01260 0.13890  500 LYS A CG    
3525 C  CD    . LYS A 504 ? 0.86110 0.78320 0.93460 0.01230  -0.01730 0.14750  500 LYS A CD    
3526 C  CE    . LYS A 504 ? 0.84960 0.78210 0.90820 0.00750  -0.01850 0.14980  500 LYS A CE    
3527 N  NZ    . LYS A 504 ? 0.82730 0.77310 0.87900 0.00780  -0.02290 0.15570  500 LYS A NZ    
3528 N  N     . SER A 505 ? 0.41740 0.31870 0.47390 0.00200  -0.00390 0.11370  501 SER A N     
3529 C  CA    . SER A 505 ? 0.43210 0.34080 0.47640 -0.00180 -0.00340 0.11060  501 SER A CA    
3530 C  C     . SER A 505 ? 0.39470 0.31640 0.43040 -0.00180 -0.00620 0.11590  501 SER A C     
3531 O  O     . SER A 505 ? 0.49390 0.41930 0.53260 -0.00060 -0.00900 0.12480  501 SER A O     
3532 C  CB    . SER A 505 ? 0.43130 0.33560 0.47610 -0.00650 -0.00230 0.11290  501 SER A CB    
3533 O  OG    . SER A 505 ? 0.52970 0.43000 0.58310 -0.00680 -0.00390 0.12290  501 SER A OG    
3534 N  N     . ILE A 506 ? 0.37660 0.30520 0.40150 -0.00320 -0.00540 0.10990  502 ILE A N     
3535 C  CA    . ILE A 506 ? 0.37050 0.31110 0.38570 -0.00360 -0.00740 0.11270  502 ILE A CA    
3536 C  C     . ILE A 506 ? 0.42310 0.36860 0.43450 -0.00730 -0.00780 0.12050  502 ILE A C     
3537 O  O     . ILE A 506 ? 0.37470 0.31650 0.38710 -0.01040 -0.00580 0.12000  502 ILE A O     
3538 C  CB    . ILE A 506 ? 0.46760 0.41250 0.47380 -0.00370 -0.00600 0.10310  502 ILE A CB    
3539 C  CG1   . ILE A 506 ? 0.50120 0.44330 0.51080 0.00000  -0.00610 0.09690  502 ILE A CG1   
3540 C  CG2   . ILE A 506 ? 0.36150 0.31790 0.35660 -0.00490 -0.00730 0.10500  502 ILE A CG2   
3541 C  CD1   . ILE A 506 ? 0.53340 0.47610 0.53690 -0.00020 -0.00410 0.08680  502 ILE A CD1   
3542 N  N     . ASP A 507 ? 0.39290 0.34740 0.39990 -0.00720 -0.01060 0.12770  503 ASP A N     
3543 C  CA    . ASP A 507 ? 0.40780 0.36910 0.40990 -0.01060 -0.01090 0.13560  503 ASP A CA    
3544 C  C     . ASP A 507 ? 0.47820 0.44910 0.46750 -0.01190 -0.00960 0.13050  503 ASP A C     
3545 O  O     . ASP A 507 ? 0.42790 0.40740 0.40920 -0.01090 -0.01140 0.13070  503 ASP A O     
3546 C  CB    . ASP A 507 ? 0.43120 0.39740 0.43510 -0.00980 -0.01450 0.14660  503 ASP A CB    
3547 C  CG    . ASP A 507 ? 0.51800 0.49130 0.51720 -0.01360 -0.01470 0.15590  503 ASP A CG    
3548 O  OD1   . ASP A 507 ? 0.53980 0.51720 0.53210 -0.01640 -0.01200 0.15310  503 ASP A OD1   
3549 O  OD2   . ASP A 507 ? 0.55500 0.53050 0.55790 -0.01370 -0.01750 0.16660  503 ASP A OD2   
3550 N  N     . PHE A 508 ? 0.38910 0.35850 0.37640 -0.01430 -0.00640 0.12560  504 PHE A N     
3551 C  CA    . PHE A 508 ? 0.40680 0.38460 0.38330 -0.01490 -0.00480 0.11980  504 PHE A CA    
3552 C  C     . PHE A 508 ? 0.45900 0.44800 0.42730 -0.01690 -0.00490 0.12650  504 PHE A C     
3553 O  O     . PHE A 508 ? 0.41570 0.41270 0.37420 -0.01630 -0.00430 0.12220  504 PHE A O     
3554 C  CB    . PHE A 508 ? 0.37000 0.34370 0.34770 -0.01660 -0.00160 0.11300  504 PHE A CB    
3555 C  CG    . PHE A 508 ? 0.41150 0.37620 0.39400 -0.01460 -0.00120 0.10480  504 PHE A CG    
3556 C  CD1   . PHE A 508 ? 0.37790 0.34480 0.35560 -0.01200 -0.00140 0.09730  504 PHE A CD1   
3557 C  CD2   . PHE A 508 ? 0.42050 0.37470 0.41260 -0.01530 -0.00060 0.10480  504 PHE A CD2   
3558 C  CE1   . PHE A 508 ? 0.43990 0.39940 0.42180 -0.01020 -0.00090 0.09020  504 PHE A CE1   
3559 C  CE2   . PHE A 508 ? 0.45350 0.40000 0.44930 -0.01340 0.00010  0.09710  504 PHE A CE2   
3560 C  CZ    . PHE A 508 ? 0.45980 0.40950 0.45050 -0.01090 -0.00000 0.09000  504 PHE A CZ    
3561 N  N     . CYS A 509 ? 0.43090 0.42070 0.40280 -0.01900 -0.00580 0.13680  505 CYS A N     
3562 C  CA    . CYS A 509 ? 0.43540 0.43700 0.39870 -0.02090 -0.00590 0.14360  505 CYS A CA    
3563 C  C     . CYS A 509 ? 0.47730 0.48560 0.43370 -0.01870 -0.00910 0.14480  505 CYS A C     
3564 O  O     . CYS A 509 ? 0.52610 0.54460 0.47120 -0.01910 -0.00860 0.14330  505 CYS A O     
3565 C  CB    . CYS A 509 ? 0.54540 0.54640 0.51500 -0.02390 -0.00640 0.15550  505 CYS A CB    
3566 S  SG    . CYS A 509 ? 0.62660 0.62450 0.60110 -0.02810 -0.00260 0.15630  505 CYS A SG    
3567 N  N     . LYS A 510 ? 0.44220 0.44500 0.40550 -0.01650 -0.01240 0.14710  506 LYS A N     
3568 C  CA    . LYS A 510 ? 0.43190 0.44060 0.39000 -0.01450 -0.01610 0.14770  506 LYS A CA    
3569 C  C     . LYS A 510 ? 0.42990 0.44030 0.38090 -0.01250 -0.01550 0.13620  506 LYS A C     
3570 O  O     . LYS A 510 ? 0.38590 0.40460 0.32720 -0.01230 -0.01730 0.13490  506 LYS A O     
3571 C  CB    . LYS A 510 ? 0.48020 0.48240 0.44960 -0.01220 -0.01950 0.15280  506 LYS A CB    
3572 C  CG    . LYS A 510 ? 0.61750 0.61900 0.59370 -0.01390 -0.02100 0.16570  506 LYS A CG    
3573 C  CD    . LYS A 510 ? 0.68300 0.68450 0.66560 -0.01150 -0.02570 0.17260  506 LYS A CD    
3574 C  CE    . LYS A 510 ? 0.74720 0.75270 0.73260 -0.01360 -0.02810 0.18690  506 LYS A CE    
3575 N  NZ    . LYS A 510 ? 0.80520 0.80090 0.80210 -0.01490 -0.02610 0.19200  506 LYS A NZ    
3576 N  N     . MET A 511 ? 0.39540 0.39780 0.35090 -0.01130 -0.01320 0.12770  507 MET A N     
3577 C  CA    . MET A 511 ? 0.43710 0.44100 0.38640 -0.00970 -0.01250 0.11720  507 MET A CA    
3578 C  C     . MET A 511 ? 0.40080 0.41300 0.33860 -0.01120 -0.01010 0.11410  507 MET A C     
3579 O  O     . MET A 511 ? 0.35420 0.37220 0.28320 -0.01030 -0.01110 0.10960  507 MET A O     
3580 C  CB    . MET A 511 ? 0.41940 0.41360 0.37570 -0.00840 -0.01040 0.10960  507 MET A CB    
3581 C  CG    . MET A 511 ? 0.52100 0.51550 0.47300 -0.00640 -0.01050 0.10000  507 MET A CG    
3582 S  SD    . MET A 511 ? 0.71230 0.69860 0.66910 -0.00620 -0.00690 0.09110  507 MET A SD    
3583 C  CE    . MET A 511 ? 0.76500 0.74080 0.73490 -0.00530 -0.00740 0.09440  507 MET A CE    
3584 N  N     . ALA A 512 ? 0.38880 0.40190 0.32710 -0.01350 -0.00690 0.11630  508 ALA A N     
3585 C  CA    . ALA A 512 ? 0.40290 0.42480 0.33130 -0.01470 -0.00400 0.11410  508 ALA A CA    
3586 C  C     . ALA A 512 ? 0.38440 0.41660 0.30300 -0.01530 -0.00590 0.11890  508 ALA A C     
3587 O  O     . ALA A 512 ? 0.39590 0.43440 0.30440 -0.01460 -0.00530 0.11320  508 ALA A O     
3588 C  CB    . ALA A 512 ? 0.42370 0.44580 0.35580 -0.01750 -0.00060 0.11790  508 ALA A CB    
3589 N  N     . GLU A 513 ? 0.33370 0.36740 0.25500 -0.01670 -0.00840 0.12930  509 GLU A N     
3590 C  CA    . GLU A 513 ? 0.41890 0.46270 0.33050 -0.01750 -0.01070 0.13460  509 GLU A CA    
3591 C  C     . GLU A 513 ? 0.46140 0.50670 0.36700 -0.01540 -0.01400 0.12820  509 GLU A C     
3592 O  O     . GLU A 513 ? 0.44350 0.49730 0.33720 -0.01580 -0.01400 0.12520  509 GLU A O     
3593 C  CB    . GLU A 513 ? 0.42380 0.46750 0.34180 -0.01900 -0.01370 0.14730  509 GLU A CB    
3594 C  CG    . GLU A 513 ? 0.57380 0.62850 0.48210 -0.02040 -0.01670 0.15440  509 GLU A CG    
3595 C  CD    . GLU A 513 ? 0.72030 0.77450 0.63630 -0.02150 -0.02030 0.16760  509 GLU A CD    
3596 O  OE1   . GLU A 513 ? 0.76130 0.82410 0.67060 -0.02250 -0.02380 0.17430  509 GLU A OE1   
3597 O  OE2   . GLU A 513 ? 0.77460 0.81960 0.70330 -0.02150 -0.01970 0.17140  509 GLU A OE2   
3598 N  N     . SER A 514 ? 0.37120 0.40850 0.28510 -0.01330 -0.01660 0.12580  510 SER A N     
3599 C  CA    . SER A 514 ? 0.40280 0.44150 0.31240 -0.01160 -0.01990 0.12000  510 SER A CA    
3600 C  C     . SER A 514 ? 0.44030 0.48090 0.34110 -0.01090 -0.01730 0.10900  510 SER A C     
3601 O  O     . SER A 514 ? 0.43840 0.48310 0.33120 -0.01060 -0.01960 0.10460  510 SER A O     
3602 C  CB    . SER A 514 ? 0.40460 0.43420 0.32600 -0.00930 -0.02210 0.11870  510 SER A CB    
3603 O  OG    . SER A 514 ? 0.43870 0.46130 0.36330 -0.00790 -0.01910 0.10930  510 SER A OG    
3604 N  N     . LEU A 515 ? 0.34840 0.38570 0.25100 -0.01080 -0.01270 0.10440  511 LEU A N     
3605 C  CA    . LEU A 515 ? 0.37400 0.41240 0.27010 -0.00980 -0.00990 0.09430  511 LEU A CA    
3606 C  C     . LEU A 515 ? 0.42630 0.47360 0.31270 -0.01110 -0.00630 0.09440  511 LEU A C     
3607 O  O     . LEU A 515 ? 0.40740 0.45540 0.29000 -0.01010 -0.00310 0.08650  511 LEU A O     
3608 C  CB    . LEU A 515 ? 0.34810 0.37790 0.25280 -0.00860 -0.00730 0.08860  511 LEU A CB    
3609 C  CG    . LEU A 515 ? 0.45390 0.47530 0.36730 -0.00700 -0.01010 0.08700  511 LEU A CG    
3610 C  CD1   . LEU A 515 ? 0.36610 0.37950 0.28740 -0.00630 -0.00730 0.08230  511 LEU A CD1   
3611 C  CD2   . LEU A 515 ? 0.44850 0.47140 0.35680 -0.00570 -0.01310 0.08120  511 LEU A CD2   
3612 N  N     . GLY A 516 ? 0.39350 0.44780 0.27630 -0.01330 -0.00660 0.10330  512 GLY A N     
3613 C  CA    . GLY A 516 ? 0.38550 0.44970 0.25830 -0.01460 -0.00310 0.10380  512 GLY A CA    
3614 C  C     . GLY A 516 ? 0.47380 0.53830 0.35060 -0.01530 0.00220  0.10410  512 GLY A C     
3615 O  O     . GLY A 516 ? 0.39620 0.46800 0.26570 -0.01520 0.00630  0.10090  512 GLY A O     
3616 N  N     . VAL A 517 ? 0.41810 0.47530 0.30680 -0.01600 0.00240  0.10820  513 VAL A N     
3617 C  CA    . VAL A 517 ? 0.41360 0.46980 0.30810 -0.01710 0.00660  0.10850  513 VAL A CA    
3618 C  C     . VAL A 517 ? 0.45910 0.51600 0.35950 -0.02020 0.00640  0.12000  513 VAL A C     
3619 O  O     . VAL A 517 ? 0.41670 0.46710 0.32390 -0.02050 0.00280  0.12530  513 VAL A O     
3620 C  CB    . VAL A 517 ? 0.39680 0.44240 0.30040 -0.01560 0.00680  0.10170  513 VAL A CB    
3621 C  CG1   . VAL A 517 ? 0.39910 0.44330 0.31000 -0.01740 0.01030  0.10320  513 VAL A CG1   
3622 C  CG2   . VAL A 517 ? 0.38230 0.42740 0.28070 -0.01270 0.00710  0.09090  513 VAL A CG2   
3623 N  N     . LYS A 518 ? 0.43210 0.49670 0.33050 -0.02240 0.01020  0.12430  514 LYS A N     
3624 C  CA    . LYS A 518 ? 0.42080 0.48580 0.32570 -0.02580 0.01020  0.13550  514 LYS A CA    
3625 C  C     . LYS A 518 ? 0.40420 0.45730 0.32250 -0.02650 0.00970  0.13530  514 LYS A C     
3626 O  O     . LYS A 518 ? 0.37060 0.41860 0.29210 -0.02510 0.01110  0.12690  514 LYS A O     
3627 C  CB    . LYS A 518 ? 0.49380 0.57000 0.39440 -0.02820 0.01490  0.13920  514 LYS A CB    
3628 C  CG    . LYS A 518 ? 0.64060 0.72950 0.52720 -0.02790 0.01600  0.13990  514 LYS A CG    
3629 C  CD    . LYS A 518 ? 0.73110 0.82990 0.61270 -0.02800 0.02200  0.13660  514 LYS A CD    
3630 C  CE    . LYS A 518 ? 0.80430 0.91330 0.67100 -0.02630 0.02350  0.13200  514 LYS A CE    
3631 N  NZ    . LYS A 518 ? 0.76300 0.88020 0.62230 -0.02880 0.02170  0.14190  514 LYS A NZ    
3632 N  N     . SER A 519 ? 0.35660 0.40500 0.28270 -0.02870 0.00760  0.14470  515 SER A N     
3633 C  CA    . SER A 519 ? 0.41870 0.45440 0.35730 -0.02920 0.00660  0.14410  515 SER A CA    
3634 C  C     . SER A 519 ? 0.46730 0.50130 0.41390 -0.03300 0.00650  0.15520  515 SER A C     
3635 O  O     . SER A 519 ? 0.44280 0.48430 0.38610 -0.03480 0.00590  0.16470  515 SER A O     
3636 C  CB    . SER A 519 ? 0.46070 0.48710 0.40300 -0.02610 0.00280  0.14090  515 SER A CB    
3637 O  OG    . SER A 519 ? 0.55260 0.58220 0.49280 -0.02580 -0.00070 0.14870  515 SER A OG    
3638 N  N     . TYR A 520 ? 0.42530 0.44930 0.38250 -0.03450 0.00690  0.15410  516 TYR A N     
3639 C  CA    . TYR A 520 ? 0.42560 0.44500 0.39240 -0.03820 0.00630  0.16380  516 TYR A CA    
3640 C  C     . TYR A 520 ? 0.44180 0.44580 0.41970 -0.03750 0.00430  0.16090  516 TYR A C     
3641 O  O     . TYR A 520 ? 0.45890 0.45690 0.43780 -0.03570 0.00490  0.15080  516 TYR A O     
3642 C  CB    . TYR A 520 ? 0.43180 0.45610 0.40060 -0.04240 0.00980  0.16590  516 TYR A CB    
3643 C  CG    . TYR A 520 ? 0.53630 0.57630 0.49530 -0.04350 0.01290  0.16890  516 TYR A CG    
3644 C  CD1   . TYR A 520 ? 0.52460 0.57260 0.48140 -0.04600 0.01270  0.18060  516 TYR A CD1   
3645 C  CD2   . TYR A 520 ? 0.56320 0.61030 0.51560 -0.04190 0.01610  0.16030  516 TYR A CD2   
3646 C  CE1   . TYR A 520 ? 0.59020 0.65330 0.53760 -0.04700 0.01600  0.18310  516 TYR A CE1   
3647 C  CE2   . TYR A 520 ? 0.55110 0.61260 0.49500 -0.04260 0.01950  0.16240  516 TYR A CE2   
3648 C  CZ    . TYR A 520 ? 0.63360 0.70320 0.57460 -0.04510 0.01960  0.17360  516 TYR A CZ    
3649 O  OH    . TYR A 520 ? 0.64630 0.73090 0.57820 -0.04570 0.02340  0.17560  516 TYR A OH    
3650 N  N     . ARG A 521 ? 0.41590 0.41340 0.40200 -0.03880 0.00210  0.16970  517 ARG A N     
3651 C  CA    . ARG A 521 ? 0.46980 0.45220 0.46760 -0.03850 0.00070  0.16770  517 ARG A CA    
3652 C  C     . ARG A 521 ? 0.51880 0.49680 0.52470 -0.04360 0.00210  0.17230  517 ARG A C     
3653 O  O     . ARG A 521 ? 0.53030 0.51420 0.53710 -0.04690 0.00220  0.18290  517 ARG A O     
3654 C  CB    . ARG A 521 ? 0.48460 0.46150 0.48780 -0.03600 -0.00280 0.17420  517 ARG A CB    
3655 C  CG    . ARG A 521 ? 0.55090 0.51200 0.56750 -0.03580 -0.00380 0.17400  517 ARG A CG    
3656 C  CD    . ARG A 521 ? 0.63360 0.58620 0.65150 -0.03220 -0.00340 0.16150  517 ARG A CD    
3657 N  NE    . ARG A 521 ? 0.74770 0.68560 0.77800 -0.03120 -0.00440 0.16150  517 ARG A NE    
3658 C  CZ    . ARG A 521 ? 0.71140 0.63950 0.74550 -0.02910 -0.00340 0.15140  517 ARG A CZ    
3659 N  NH1   . ARG A 521 ? 0.54350 0.47480 0.57010 -0.02800 -0.00190 0.14090  517 ARG A NH1   
3660 N  NH2   . ARG A 521 ? 0.64430 0.55930 0.68980 -0.02820 -0.00400 0.15200  517 ARG A NH2   
3661 N  N     . ALA A 522 ? 0.48500 0.45320 0.49690 -0.04450 0.00300  0.16460  518 ALA A N     
3662 C  CA    . ALA A 522 ? 0.48490 0.44850 0.50460 -0.04990 0.00390  0.16780  518 ALA A CA    
3663 C  C     . ALA A 522 ? 0.55940 0.50610 0.59020 -0.04990 0.00250  0.16500  518 ALA A C     
3664 O  O     . ALA A 522 ? 0.55450 0.49420 0.58530 -0.04750 0.00270  0.15450  518 ALA A O     
3665 C  CB    . ALA A 522 ? 0.43330 0.40300 0.44890 -0.05220 0.00670  0.16080  518 ALA A CB    
3666 N  N     . GLU A 523 ? 0.41180 0.35190 0.45180 -0.05250 0.00110  0.17450  519 GLU A N     
3667 C  CA    . GLU A 523 ? 0.48740 0.41060 0.53890 -0.05300 0.00000  0.17240  519 GLU A CA    
3668 C  C     . GLU A 523 ? 0.57360 0.49120 0.63270 -0.05950 0.00050  0.17500  519 GLU A C     
3669 O  O     . GLU A 523 ? 0.55320 0.45610 0.62140 -0.06050 -0.00010 0.17150  519 GLU A O     
3670 C  CB    . GLU A 523 ? 0.51850 0.43560 0.57690 -0.05010 -0.00250 0.18070  519 GLU A CB    
3671 C  CG    . GLU A 523 ? 0.62930 0.55230 0.68080 -0.04400 -0.00350 0.17850  519 GLU A CG    
3672 C  CD    . GLU A 523 ? 0.81620 0.73380 0.87530 -0.04090 -0.00620 0.18670  519 GLU A CD    
3673 O  OE1   . GLU A 523 ? 0.88030 0.80120 0.93580 -0.03590 -0.00740 0.18470  519 GLU A OE1   
3674 O  OE2   . GLU A 523 ? 0.85300 0.76330 0.92230 -0.04350 -0.00720 0.19550  519 GLU A OE2   
3675 N  N     . THR A 524 ? 0.54940 0.47870 0.60530 -0.06390 0.00180  0.18060  520 THR A N     
3676 C  CA    . THR A 524 ? 0.53720 0.46370 0.59950 -0.07070 0.00240  0.18260  520 THR A CA    
3677 C  C     . THR A 524 ? 0.57360 0.51360 0.62810 -0.07280 0.00480  0.17820  520 THR A C     
3678 O  O     . THR A 524 ? 0.50830 0.46120 0.55260 -0.06960 0.00620  0.17730  520 THR A O     
3679 C  CB    . THR A 524 ? 0.53690 0.46480 0.60600 -0.07500 0.00150  0.19740  520 THR A CB    
3680 O  OG1   . THR A 524 ? 0.49810 0.44400 0.55850 -0.07520 0.00290  0.20440  520 THR A OG1   
3681 C  CG2   . THR A 524 ? 0.52880 0.44580 0.60540 -0.07210 -0.00100 0.20360  520 THR A CG2   
3682 N  N     . VAL A 525 ? 0.51100 0.44800 0.57070 -0.07830 0.00520  0.17590  521 VAL A N     
3683 C  CA    . VAL A 525 ? 0.53350 0.48350 0.58730 -0.08030 0.00740  0.17230  521 VAL A CA    
3684 C  C     . VAL A 525 ? 0.51190 0.47840 0.56150 -0.08160 0.00930  0.18270  521 VAL A C     
3685 O  O     . VAL A 525 ? 0.54230 0.52260 0.58390 -0.08020 0.01170  0.17990  521 VAL A O     
3686 C  CB    . VAL A 525 ? 0.51670 0.46100 0.57760 -0.08650 0.00710  0.16850  521 VAL A CB    
3687 C  CG1   . VAL A 525 ? 0.47660 0.41800 0.54750 -0.09300 0.00620  0.17960  521 VAL A CG1   
3688 C  CG2   . VAL A 525 ? 0.51530 0.47310 0.57060 -0.08760 0.00910  0.16370  521 VAL A CG2   
3689 N  N     . GLU A 526 ? 0.47850 0.44410 0.53340 -0.08410 0.00840  0.19500  522 GLU A N     
3690 C  CA    . GLU A 526 ? 0.52200 0.50380 0.57240 -0.08550 0.01030  0.20560  522 GLU A CA    
3691 C  C     . GLU A 526 ? 0.48720 0.47860 0.52550 -0.07920 0.01110  0.20410  522 GLU A C     
3692 O  O     . GLU A 526 ? 0.46450 0.47150 0.49430 -0.07860 0.01390  0.20500  522 GLU A O     
3693 C  CB    . GLU A 526 ? 0.52850 0.50650 0.58760 -0.08970 0.00870  0.21960  522 GLU A CB    
3694 C  CG    . GLU A 526 ? 0.66660 0.63620 0.73800 -0.09690 0.00790  0.22230  522 GLU A CG    
3695 C  CD    . GLU A 526 ? 0.77230 0.72100 0.85230 -0.09660 0.00500  0.21590  522 GLU A CD    
3696 O  OE1   . GLU A 526 ? 0.84390 0.78360 0.93390 -0.10260 0.00400  0.21680  522 GLU A OE1   
3697 O  OE2   . GLU A 526 ? 0.75890 0.69990 0.83590 -0.09060 0.00390  0.20970  522 GLU A OE2   
3698 N  N     . ASP A 527 ? 0.43320 0.41540 0.47070 -0.07440 0.00870  0.20150  523 ASP A N     
3699 C  CA    . ASP A 527 ? 0.49380 0.48410 0.52010 -0.06860 0.00900  0.19870  523 ASP A CA    
3700 C  C     . ASP A 527 ? 0.48300 0.47890 0.50120 -0.06570 0.01110  0.18640  523 ASP A C     
3701 O  O     . ASP A 527 ? 0.44180 0.45020 0.44970 -0.06310 0.01290  0.18510  523 ASP A O     
3702 C  CB    . ASP A 527 ? 0.56060 0.53920 0.58930 -0.06410 0.00580  0.19750  523 ASP A CB    
3703 C  CG    . ASP A 527 ? 0.77480 0.74900 0.81100 -0.06580 0.00350  0.21060  523 ASP A CG    
3704 O  OD1   . ASP A 527 ? 0.75460 0.73920 0.78920 -0.06900 0.00420  0.22160  523 ASP A OD1   
3705 O  OD2   . ASP A 527 ? 0.87190 0.83220 0.91590 -0.06370 0.00100  0.20980  523 ASP A OD2   
3706 N  N     . PHE A 528 ? 0.48100 0.46770 0.50380 -0.06640 0.01100  0.17710  524 PHE A N     
3707 C  CA    . PHE A 528 ? 0.41800 0.40960 0.43380 -0.06360 0.01270  0.16590  524 PHE A CA    
3708 C  C     . PHE A 528 ? 0.43320 0.44020 0.44510 -0.06600 0.01600  0.16760  524 PHE A C     
3709 O  O     . PHE A 528 ? 0.45940 0.47640 0.46230 -0.06240 0.01800  0.16290  524 PHE A O     
3710 C  CB    . PHE A 528 ? 0.42290 0.40220 0.44430 -0.06430 0.01160  0.15630  524 PHE A CB    
3711 C  CG    . PHE A 528 ? 0.42580 0.41060 0.44120 -0.06220 0.01320  0.14600  524 PHE A CG    
3712 C  CD1   . PHE A 528 ? 0.42910 0.41620 0.43620 -0.05640 0.01330  0.13960  524 PHE A CD1   
3713 C  CD2   . PHE A 528 ? 0.42050 0.40870 0.43870 -0.06610 0.01440  0.14330  524 PHE A CD2   
3714 C  CE1   . PHE A 528 ? 0.39760 0.38940 0.39970 -0.05430 0.01460  0.13060  524 PHE A CE1   
3715 C  CE2   . PHE A 528 ? 0.47470 0.46830 0.48800 -0.06390 0.01560  0.13450  524 PHE A CE2   
3716 C  CZ    . PHE A 528 ? 0.46430 0.45930 0.46960 -0.05790 0.01580  0.12820  524 PHE A CZ    
3717 N  N     . ASP A 529 ? 0.43770 0.44650 0.45690 -0.07200 0.01670  0.17410  525 ASP A N     
3718 C  CA    . ASP A 529 ? 0.44390 0.46820 0.46090 -0.07440 0.02010  0.17670  525 ASP A CA    
3719 C  C     . ASP A 529 ? 0.47100 0.50940 0.47860 -0.07190 0.02240  0.18240  525 ASP A C     
3720 O  O     . ASP A 529 ? 0.49110 0.54210 0.49180 -0.06990 0.02570  0.17890  525 ASP A O     
3721 C  CB    . ASP A 529 ? 0.56140 0.58520 0.58890 -0.08170 0.02010  0.18460  525 ASP A CB    
3722 C  CG    . ASP A 529 ? 0.77840 0.81750 0.80570 -0.08450 0.02360  0.18590  525 ASP A CG    
3723 O  OD1   . ASP A 529 ? 0.80530 0.84810 0.82990 -0.08230 0.02480  0.17670  525 ASP A OD1   
3724 O  OD2   . ASP A 529 ? 0.81560 0.86370 0.84600 -0.08870 0.02530  0.19650  525 ASP A OD2   
3725 N  N     . ALA A 530 ? 0.41060 0.44710 0.41770 -0.07190 0.02080  0.19110  526 ALA A N     
3726 C  CA    . ALA A 530 ? 0.44070 0.49050 0.43770 -0.06970 0.02250  0.19630  526 ALA A CA    
3727 C  C     . ALA A 530 ? 0.42700 0.47890 0.41310 -0.06320 0.02280  0.18640  526 ALA A C     
3728 O  O     . ALA A 530 ? 0.46370 0.52890 0.44040 -0.06120 0.02580  0.18470  526 ALA A O     
3729 C  CB    . ALA A 530 ? 0.41420 0.46070 0.41350 -0.07110 0.01990  0.20800  526 ALA A CB    
3730 N  N     . ALA A 531 ? 0.38200 0.42110 0.36960 -0.06000 0.01970  0.17940  527 ALA A N     
3731 C  CA    . ALA A 531 ? 0.39730 0.43760 0.37550 -0.05430 0.01950  0.17000  527 ALA A CA    
3732 C  C     . ALA A 531 ? 0.41680 0.46410 0.39120 -0.05290 0.02270  0.16100  527 ALA A C     
3733 O  O     . ALA A 531 ? 0.41890 0.47570 0.38360 -0.04960 0.02480  0.15720  527 ALA A O     
3734 C  CB    . ALA A 531 ? 0.39050 0.41570 0.37270 -0.05160 0.01590  0.16460  527 ALA A CB    
3735 N  N     . LEU A 532 ? 0.44140 0.48420 0.42360 -0.05550 0.02320  0.15750  528 LEU A N     
3736 C  CA    . LEU A 532 ? 0.44860 0.49790 0.42830 -0.05400 0.02590  0.14930  528 LEU A CA    
3737 C  C     . LEU A 532 ? 0.42340 0.48940 0.39830 -0.05460 0.03020  0.15340  528 LEU A C     
3738 O  O     . LEU A 532 ? 0.40940 0.48330 0.37730 -0.05090 0.03270  0.14710  528 LEU A O     
3739 C  CB    . LEU A 532 ? 0.41750 0.45980 0.40680 -0.05750 0.02510  0.14600  528 LEU A CB    
3740 C  CG    . LEU A 532 ? 0.45150 0.49880 0.43930 -0.05560 0.02690  0.13710  528 LEU A CG    
3741 C  CD1   . LEU A 532 ? 0.35710 0.40100 0.33730 -0.04960 0.02610  0.12820  528 LEU A CD1   
3742 C  CD2   . LEU A 532 ? 0.45330 0.49380 0.45020 -0.05960 0.02550  0.13430  528 LEU A CD2   
3743 N  N     . LYS A 533 ? 0.44210 0.51380 0.42080 -0.05920 0.03120  0.16400  529 LYS A N     
3744 C  CA    . LYS A 533 ? 0.50910 0.59770 0.48320 -0.05980 0.03580  0.16850  529 LYS A CA    
3745 C  C     . LYS A 533 ? 0.47980 0.57590 0.44090 -0.05530 0.03710  0.16740  529 LYS A C     
3746 O  O     . LYS A 533 ? 0.47240 0.57980 0.42670 -0.05260 0.04100  0.16300  529 LYS A O     
3747 C  CB    . LYS A 533 ? 0.37990 0.47280 0.36050 -0.06590 0.03650  0.18110  529 LYS A CB    
3748 C  CG    . LYS A 533 ? 0.52810 0.63910 0.50240 -0.06630 0.04130  0.18710  529 LYS A CG    
3749 C  CD    . LYS A 533 ? 0.72080 0.83500 0.69920 -0.07170 0.04100  0.20100  529 LYS A CD    
3750 C  CE    . LYS A 533 ? 0.85440 0.95970 0.84700 -0.07740 0.03890  0.20490  529 LYS A CE    
3751 N  NZ    . LYS A 533 ? 0.97860 1.09680 0.97630 -0.08120 0.04300  0.20840  529 LYS A NZ    
3752 N  N     . GLY A 534 ? 0.43370 0.52380 0.39140 -0.05450 0.03380  0.17100  530 GLY A N     
3753 C  CA    . GLY A 534 ? 0.45940 0.55610 0.40440 -0.05060 0.03420  0.16920  530 GLY A CA    
3754 C  C     . GLY A 534 ? 0.48720 0.58170 0.42650 -0.04530 0.03450  0.15630  530 GLY A C     
3755 O  O     . GLY A 534 ? 0.47260 0.57680 0.40210 -0.04230 0.03740  0.15220  530 GLY A O     
3756 N  N     . ALA A 535 ? 0.42470 0.50620 0.37010 -0.04410 0.03160  0.14970  531 ALA A N     
3757 C  CA    . ALA A 535 ? 0.43230 0.51080 0.37310 -0.03930 0.03140  0.13800  531 ALA A CA    
3758 C  C     . ALA A 535 ? 0.46500 0.55360 0.40400 -0.03800 0.03600  0.13270  531 ALA A C     
3759 O  O     . ALA A 535 ? 0.44980 0.54300 0.38060 -0.03390 0.03770  0.12580  531 ALA A O     
3760 C  CB    . ALA A 535 ? 0.43050 0.49440 0.37910 -0.03900 0.02790  0.13270  531 ALA A CB    
3761 N  N     . LEU A 536 ? 0.40490 0.49680 0.35220 -0.04140 0.03810  0.13580  532 LEU A N     
3762 C  CA    . LEU A 536 ? 0.44520 0.54680 0.39280 -0.04000 0.04240  0.13130  532 LEU A CA    
3763 C  C     . LEU A 536 ? 0.50230 0.61870 0.44070 -0.03820 0.04710  0.13300  532 LEU A C     
3764 O  O     . LEU A 536 ? 0.46670 0.58950 0.40120 -0.03440 0.05030  0.12600  532 LEU A O     
3765 C  CB    . LEU A 536 ? 0.44420 0.54730 0.40330 -0.04480 0.04320  0.13550  532 LEU A CB    
3766 C  CG    . LEU A 536 ? 0.51770 0.60720 0.48470 -0.04590 0.03930  0.13090  532 LEU A CG    
3767 C  CD1   . LEU A 536 ? 0.58130 0.67020 0.55940 -0.05200 0.03890  0.13680  532 LEU A CD1   
3768 C  CD2   . LEU A 536 ? 0.46160 0.55060 0.42730 -0.04170 0.03990  0.12050  532 LEU A CD2   
3769 N  N     . ALA A 537 ? 0.42850 0.55040 0.36330 -0.04080 0.04750  0.14210  533 ALA A N     
3770 C  CA    . ALA A 537 ? 0.47190 0.60860 0.39710 -0.03950 0.05220  0.14390  533 ALA A CA    
3771 C  C     . ALA A 537 ? 0.54830 0.68490 0.46050 -0.03510 0.05140  0.13790  533 ALA A C     
3772 O  O     . ALA A 537 ? 0.57840 0.72700 0.48120 -0.03340 0.05550  0.13710  533 ALA A O     
3773 C  CB    . ALA A 537 ? 0.38620 0.53050 0.31220 -0.04440 0.05320  0.15690  533 ALA A CB    
3774 N  N     . MET A 538 ? 0.49470 0.61870 0.40600 -0.03340 0.04630  0.13370  534 MET A N     
3775 C  CA    . MET A 538 ? 0.58510 0.70910 0.48440 -0.03060 0.04450  0.13060  534 MET A CA    
3776 C  C     . MET A 538 ? 0.59310 0.72150 0.48430 -0.02570 0.04750  0.11960  534 MET A C     
3777 O  O     . MET A 538 ? 0.80400 0.94060 0.68360 -0.02430 0.04930  0.11840  534 MET A O     
3778 C  CB    . MET A 538 ? 0.54950 0.65940 0.45140 -0.03020 0.03830  0.12950  534 MET A CB    
3779 C  CG    . MET A 538 ? 0.68760 0.79640 0.58910 -0.03330 0.03500  0.14010  534 MET A CG    
3780 S  SD    . MET A 538 ? 0.62270 0.71380 0.53300 -0.03300 0.02870  0.13930  534 MET A SD    
3781 C  CE    . MET A 538 ? 0.69910 0.78710 0.60040 -0.02790 0.02670  0.12800  534 MET A CE    
3782 N  N     . ASN A 539 ? 0.52440 0.64710 0.42140 -0.02330 0.04780  0.11150  535 ASN A N     
3783 C  CA    . ASN A 539 ? 0.68310 0.80770 0.57370 -0.01840 0.05000  0.10070  535 ASN A CA    
3784 C  C     . ASN A 539 ? 0.72520 0.84360 0.60640 -0.01610 0.04600  0.09570  535 ASN A C     
3785 O  O     . ASN A 539 ? 0.66150 0.78330 0.53360 -0.01280 0.04770  0.08830  535 ASN A O     
3786 C  CB    . ASN A 539 ? 0.83760 0.97710 0.72300 -0.01720 0.05660  0.10050  535 ASN A CB    
3787 C  CG    . ASN A 539 ? 0.93100 1.07570 0.82730 -0.01810 0.06050  0.10220  535 ASN A CG    
3788 O  OD1   . ASN A 539 ? 0.93520 1.07230 0.84080 -0.01750 0.05890  0.09840  535 ASN A OD1   
3789 N  ND2   . ASN A 539 ? 0.87560 1.03370 0.77130 -0.01990 0.06550  0.10840  535 ASN A ND2   
3790 N  N     . THR A 540 ? 0.65880 0.76790 0.54290 -0.01790 0.04060  0.09950  536 THR A N     
3791 C  CA    . THR A 540 ? 0.54140 0.64120 0.42190 -0.01590 0.03580  0.09430  536 THR A CA    
3792 C  C     . THR A 540 ? 0.49910 0.58690 0.39110 -0.01730 0.03210  0.09590  536 THR A C     
3793 O  O     . THR A 540 ? 0.45910 0.54640 0.35940 -0.02030 0.03280  0.10210  536 THR A O     
3794 C  CB    . THR A 540 ? 0.59080 0.69320 0.46180 -0.01690 0.03270  0.09860  536 THR A CB    
3795 O  OG1   . THR A 540 ? 0.60930 0.70990 0.48560 -0.02050 0.03020  0.10950  536 THR A OG1   
3796 C  CG2   . THR A 540 ? 0.55380 0.66920 0.41210 -0.01630 0.03650  0.09790  536 THR A CG2   
3797 N  N     . PRO A 541 ? 0.42250 0.50070 0.31500 -0.01530 0.02820  0.09030  537 PRO A N     
3798 C  CA    . PRO A 541 ? 0.40550 0.47240 0.30850 -0.01630 0.02520  0.09110  537 PRO A CA    
3799 C  C     . PRO A 541 ? 0.39900 0.46360 0.30630 -0.01970 0.02280  0.10130  537 PRO A C     
3800 O  O     . PRO A 541 ? 0.48700 0.55680 0.38840 -0.02070 0.02180  0.10720  537 PRO A O     
3801 C  CB    . PRO A 541 ? 0.41060 0.46980 0.31140 -0.01340 0.02160  0.08390  537 PRO A CB    
3802 C  CG    . PRO A 541 ? 0.47520 0.54110 0.36470 -0.01110 0.02280  0.07890  537 PRO A CG    
3803 C  CD    . PRO A 541 ? 0.42240 0.49990 0.30580 -0.01250 0.02630  0.08390  537 PRO A CD    
3804 N  N     . CYS A 542 ? 0.39630 0.45280 0.31400 -0.02150 0.02170  0.10320  538 CYS A N     
3805 C  CA    . CYS A 542 ? 0.37200 0.42420 0.29590 -0.02460 0.01950  0.11230  538 CYS A CA    
3806 C  C     . CYS A 542 ? 0.39900 0.43830 0.33250 -0.02480 0.01700  0.10990  538 CYS A C     
3807 O  O     . CYS A 542 ? 0.35800 0.39350 0.29530 -0.02430 0.01800  0.10350  538 CYS A O     
3808 C  CB    . CYS A 542 ? 0.39380 0.45280 0.32120 -0.02840 0.02250  0.11990  538 CYS A CB    
3809 S  SG    . CYS A 542 ? 0.48680 0.54140 0.42140 -0.03250 0.01990  0.13250  538 CYS A SG    
3810 N  N     . LEU A 543 ? 0.34920 0.38200 0.28670 -0.02560 0.01380  0.11540  539 LEU A N     
3811 C  CA    . LEU A 543 ? 0.37810 0.39840 0.32470 -0.02560 0.01170  0.11350  539 LEU A CA    
3812 C  C     . LEU A 543 ? 0.40450 0.42080 0.35930 -0.02920 0.01090  0.12260  539 LEU A C     
3813 O  O     . LEU A 543 ? 0.36250 0.38300 0.31580 -0.03030 0.01000  0.13130  539 LEU A O     
3814 C  CB    . LEU A 543 ? 0.35980 0.37430 0.30540 -0.02240 0.00840  0.11020  539 LEU A CB    
3815 C  CG    . LEU A 543 ? 0.38800 0.39000 0.34280 -0.02190 0.00670  0.10750  539 LEU A CG    
3816 C  CD1   . LEU A 543 ? 0.45160 0.45020 0.40410 -0.01830 0.00510  0.09980  539 LEU A CD1   
3817 C  CD2   . LEU A 543 ? 0.38160 0.37780 0.34360 -0.02320 0.00460  0.11600  539 LEU A CD2   
3818 N  N     . ILE A 544 ? 0.37780 0.38590 0.34100 -0.03110 0.01120  0.12080  540 ILE A N     
3819 C  CA    . ILE A 544 ? 0.37710 0.37900 0.34930 -0.03470 0.01040  0.12830  540 ILE A CA    
3820 C  C     . ILE A 544 ? 0.42910 0.41720 0.40870 -0.03340 0.00820  0.12470  540 ILE A C     
3821 O  O     . ILE A 544 ? 0.35590 0.33860 0.33740 -0.03300 0.00870  0.11640  540 ILE A O     
3822 C  CB    . ILE A 544 ? 0.41460 0.41940 0.39060 -0.03900 0.01290  0.12980  540 ILE A CB    
3823 C  CG1   . ILE A 544 ? 0.35910 0.37880 0.32800 -0.03970 0.01580  0.13320  540 ILE A CG1   
3824 C  CG2   . ILE A 544 ? 0.33840 0.33580 0.32430 -0.04300 0.01180  0.13740  540 ILE A CG2   
3825 C  CD1   . ILE A 544 ? 0.36600 0.39080 0.33850 -0.04340 0.01860  0.13380  540 ILE A CD1   
3826 N  N     . ASP A 545 ? 0.38510 0.36790 0.36900 -0.03290 0.00580  0.13090  541 ASP A N     
3827 C  CA    . ASP A 545 ? 0.41300 0.38310 0.40440 -0.03100 0.00400  0.12810  541 ASP A CA    
3828 C  C     . ASP A 545 ? 0.45390 0.41480 0.45560 -0.03480 0.00410  0.13220  541 ASP A C     
3829 O  O     . ASP A 545 ? 0.44230 0.40310 0.44820 -0.03680 0.00310  0.14210  541 ASP A O     
3830 C  CB    . ASP A 545 ? 0.46150 0.43200 0.45240 -0.02780 0.00130  0.13280  541 ASP A CB    
3831 C  CG    . ASP A 545 ? 0.54070 0.49920 0.53980 -0.02500 -0.00030 0.12990  541 ASP A CG    
3832 O  OD1   . ASP A 545 ? 0.63260 0.58160 0.63760 -0.02590 0.00080  0.12460  541 ASP A OD1   
3833 O  OD2   . ASP A 545 ? 0.50410 0.46290 0.50360 -0.02200 -0.00270 0.13300  541 ASP A OD2   
3834 N  N     . VAL A 546 ? 0.42470 0.37810 0.43030 -0.03610 0.00510  0.12490  542 VAL A N     
3835 C  CA    . VAL A 546 ? 0.39690 0.34190 0.41130 -0.04060 0.00520  0.12730  542 VAL A CA    
3836 C  C     . VAL A 546 ? 0.43070 0.36110 0.45330 -0.03880 0.00400  0.12450  542 VAL A C     
3837 O  O     . VAL A 546 ? 0.43430 0.36040 0.45560 -0.03580 0.00420  0.11560  542 VAL A O     
3838 C  CB    . VAL A 546 ? 0.44150 0.38850 0.45480 -0.04390 0.00700  0.12110  542 VAL A CB    
3839 C  CG1   . VAL A 546 ? 0.39130 0.32970 0.41370 -0.04920 0.00680  0.12370  542 VAL A CG1   
3840 C  CG2   . VAL A 546 ? 0.47730 0.43920 0.48290 -0.04480 0.00870  0.12330  542 VAL A CG2   
3841 N  N     . GLN A 547 ? 0.39190 0.31480 0.42330 -0.04060 0.00290  0.13210  543 GLN A N     
3842 C  CA    . GLN A 547 ? 0.45490 0.36320 0.49530 -0.03900 0.00220  0.12920  543 GLN A CA    
3843 C  C     . GLN A 547 ? 0.45750 0.35700 0.50110 -0.04240 0.00340  0.12110  543 GLN A C     
3844 O  O     . GLN A 547 ? 0.50820 0.40780 0.55410 -0.04770 0.00370  0.12370  543 GLN A O     
3845 C  CB    . GLN A 547 ? 0.54510 0.44740 0.59490 -0.03970 0.00060  0.14010  543 GLN A CB    
3846 C  CG    . GLN A 547 ? 0.60060 0.48790 0.66010 -0.03670 0.00010  0.13720  543 GLN A CG    
3847 C  CD    . GLN A 547 ? 0.65920 0.53830 0.73020 -0.03790 -0.00150 0.14770  543 GLN A CD    
3848 O  OE1   . GLN A 547 ? 0.68510 0.57020 0.75650 -0.04120 -0.00240 0.15810  543 GLN A OE1   
3849 N  NE2   . GLN A 547 ? 0.64010 0.50550 0.72080 -0.03520 -0.00160 0.14490  543 GLN A NE2   
3850 N  N     . VAL A 548 ? 0.37660 0.26890 0.42040 -0.03950 0.00400  0.11130  544 VAL A N     
3851 C  CA    . VAL A 548 ? 0.46430 0.34860 0.50960 -0.04250 0.00500  0.10240  544 VAL A CA    
3852 C  C     . VAL A 548 ? 0.48300 0.35350 0.53470 -0.03960 0.00530  0.09660  544 VAL A C     
3853 O  O     . VAL A 548 ? 0.47990 0.35030 0.53120 -0.03410 0.00540  0.09530  544 VAL A O     
3854 C  CB    . VAL A 548 ? 0.49440 0.38730 0.53020 -0.04250 0.00600  0.09420  544 VAL A CB    
3855 C  CG1   . VAL A 548 ? 0.53480 0.41960 0.57170 -0.04550 0.00670  0.08480  544 VAL A CG1   
3856 C  CG2   . VAL A 548 ? 0.51810 0.42420 0.54880 -0.04560 0.00620  0.09950  544 VAL A CG2   
3857 N  N     . ASP A 549 ? 0.50930 0.36830 0.56690 -0.04330 0.00570  0.09280  545 ASP A N     
3858 C  CA    . ASP A 549 ? 0.48780 0.33280 0.55160 -0.04070 0.00660  0.08640  545 ASP A CA    
3859 C  C     . ASP A 549 ? 0.46160 0.30700 0.51840 -0.03900 0.00820  0.07420  545 ASP A C     
3860 O  O     . ASP A 549 ? 0.45850 0.30680 0.50990 -0.04310 0.00840  0.06860  545 ASP A O     
3861 C  CB    . ASP A 549 ? 0.56230 0.39410 0.63480 -0.04570 0.00630  0.08690  545 ASP A CB    
3862 C  CG    . ASP A 549 ? 0.71090 0.52710 0.79050 -0.04300 0.00760  0.07980  545 ASP A CG    
3863 O  OD1   . ASP A 549 ? 0.76540 0.58150 0.84320 -0.03730 0.00900  0.07430  545 ASP A OD1   
3864 O  OD2   . ASP A 549 ? 0.79430 0.59820 0.88170 -0.04670 0.00740  0.07950  545 ASP A OD2   
3865 N  N     . ILE A 550 ? 0.48020 0.32340 0.53760 -0.03310 0.00920  0.07040  546 ILE A N     
3866 C  CA    . ILE A 550 ? 0.45600 0.30080 0.50670 -0.03120 0.01090  0.05980  546 ILE A CA    
3867 C  C     . ILE A 550 ? 0.49760 0.33170 0.54920 -0.03450 0.01220  0.05030  546 ILE A C     
3868 O  O     . ILE A 550 ? 0.51700 0.35390 0.56160 -0.03500 0.01320  0.04180  546 ILE A O     
3869 C  CB    . ILE A 550 ? 0.42330 0.26800 0.47600 -0.02420 0.01180  0.05890  546 ILE A CB    
3870 C  CG1   . ILE A 550 ? 0.44070 0.29290 0.48440 -0.02210 0.01290  0.05120  546 ILE A CG1   
3871 C  CG2   . ILE A 550 ? 0.47790 0.30810 0.54050 -0.02190 0.01340  0.05590  546 ILE A CG2   
3872 C  CD1   . ILE A 550 ? 0.48350 0.33740 0.52920 -0.01560 0.01370  0.05060  546 ILE A CD1   
3873 N  N     . ASP A 551 ? 0.49260 0.31490 0.55260 -0.03730 0.01200  0.05180  547 ASP A N     
3874 C  CA    . ASP A 551 ? 0.53800 0.34840 0.59940 -0.04060 0.01320  0.04230  547 ASP A CA    
3875 C  C     . ASP A 551 ? 0.56670 0.38000 0.62310 -0.04810 0.01180  0.03990  547 ASP A C     
3876 O  O     . ASP A 551 ? 0.56380 0.36970 0.61870 -0.05130 0.01250  0.03070  547 ASP A O     
3877 C  CB    . ASP A 551 ? 0.48470 0.27990 0.55800 -0.04070 0.01340  0.04470  547 ASP A CB    
3878 C  CG    . ASP A 551 ? 0.76190 0.55050 0.84130 -0.03340 0.01550  0.04300  547 ASP A CG    
3879 O  OD1   . ASP A 551 ? 0.86840 0.66010 0.94260 -0.02960 0.01750  0.03550  547 ASP A OD1   
3880 O  OD2   . ASP A 551 ? 0.91990 0.70050 1.00990 -0.03150 0.01510  0.04960  547 ASP A OD2   
3881 N  N     . VAL A 552 ? 0.54870 0.37280 0.60290 -0.05120 0.00990  0.04780  548 VAL A N     
3882 C  CA    . VAL A 552 ? 0.53770 0.36470 0.58910 -0.05850 0.00850  0.04660  548 VAL A CA    
3883 C  C     . VAL A 552 ? 0.49070 0.32340 0.53280 -0.05930 0.00900  0.03700  548 VAL A C     
3884 O  O     . VAL A 552 ? 0.59970 0.44170 0.63530 -0.05500 0.00970  0.03580  548 VAL A O     
3885 C  CB    . VAL A 552 ? 0.59990 0.43900 0.65090 -0.06080 0.00700  0.05720  548 VAL A CB    
3886 C  CG1   . VAL A 552 ? 0.58500 0.42780 0.63450 -0.06840 0.00560  0.05610  548 VAL A CG1   
3887 C  CG2   . VAL A 552 ? 0.60740 0.44190 0.66740 -0.06020 0.00630  0.06770  548 VAL A CG2   
3888 N  N     . LEU A 553 ? 0.48740 0.31460 0.52860 -0.06500 0.00830  0.03030  549 LEU A N     
3889 C  CA    . LEU A 553 ? 0.55810 0.39050 0.59030 -0.06610 0.00850  0.02150  549 LEU A CA    
3890 C  C     . LEU A 553 ? 0.48620 0.33260 0.51400 -0.07010 0.00660  0.02530  549 LEU A C     
3891 O  O     . LEU A 553 ? 0.53640 0.38270 0.56780 -0.07620 0.00480  0.02880  549 LEU A O     
3892 C  CB    . LEU A 553 ? 0.61430 0.43480 0.64640 -0.07040 0.00860  0.01160  549 LEU A CB    
3893 C  CG    . LEU A 553 ? 0.76590 0.59230 0.78800 -0.07090 0.00890  0.00270  549 LEU A CG    
3894 C  CD1   . LEU A 553 ? 0.81460 0.63670 0.83400 -0.06450 0.01200  -0.00420 549 LEU A CD1   
3895 C  CD2   . LEU A 553 ? 0.83250 0.65450 0.85250 -0.07870 0.00710  -0.00410 549 LEU A CD2   
3896 N  N     . PRO A 554 ? 0.53250 0.39090 0.55330 -0.06680 0.00700  0.02490  550 PRO A N     
3897 C  CA    . PRO A 554 ? 0.53940 0.41140 0.55710 -0.06970 0.00550  0.02920  550 PRO A CA    
3898 C  C     . PRO A 554 ? 0.53230 0.40580 0.54700 -0.07590 0.00380  0.02340  550 PRO A C     
3899 O  O     . PRO A 554 ? 0.46650 0.33310 0.47800 -0.07690 0.00400  0.01460  550 PRO A O     
3900 C  CB    . PRO A 554 ? 0.52170 0.40380 0.53320 -0.06350 0.00670  0.02940  550 PRO A CB    
3901 C  CG    . PRO A 554 ? 0.52030 0.39500 0.53330 -0.05760 0.00840  0.02820  550 PRO A CG    
3902 C  CD    . PRO A 554 ? 0.54390 0.40430 0.56060 -0.05980 0.00890  0.02210  550 PRO A CD    
3903 N  N     . PRO A 555 ? 0.50510 0.38860 0.52030 -0.08020 0.00220  0.02820  551 PRO A N     
3904 C  CA    . PRO A 555 ? 0.51250 0.39920 0.52520 -0.08640 -0.00000 0.02350  551 PRO A CA    
3905 C  C     . PRO A 555 ? 0.58000 0.47000 0.58450 -0.08390 0.00030  0.01590  551 PRO A C     
3906 O  O     . PRO A 555 ? 0.61050 0.50710 0.61120 -0.07800 0.00180  0.01670  551 PRO A O     
3907 C  CB    . PRO A 555 ? 0.52210 0.42260 0.53700 -0.08890 -0.00110 0.03140  551 PRO A CB    
3908 C  CG    . PRO A 555 ? 0.52710 0.42880 0.54650 -0.08560 0.00040  0.04020  551 PRO A CG    
3909 C  CD    . PRO A 555 ? 0.54260 0.43610 0.56070 -0.07910 0.00240  0.03810  551 PRO A CD    
3910 N  N     . GLY A 556 ? 0.56490 0.45030 0.56640 -0.08870 -0.00110 0.00840  552 GLY A N     
3911 C  CA    . GLY A 556 ? 0.61430 0.50360 0.60770 -0.08730 -0.00100 0.00160  552 GLY A CA    
3912 C  C     . GLY A 556 ? 0.74170 0.62310 0.73160 -0.08180 0.00170  -0.00450 552 GLY A C     
3913 O  O     . GLY A 556 ? 0.72730 0.61150 0.71020 -0.08090 0.00200  -0.01040 552 GLY A O     
3914 N  N     . MET A 557 ? 0.77460 0.64620 0.76950 -0.07820 0.00380  -0.00320 553 MET A N     
3915 C  CA    . MET A 557 ? 0.74740 0.61310 0.73990 -0.07210 0.00670  -0.00800 553 MET A CA    
3916 C  C     . MET A 557 ? 0.72750 0.58030 0.71900 -0.07430 0.00780  -0.01740 553 MET A C     
3917 O  O     . MET A 557 ? 0.75600 0.60820 0.74160 -0.07190 0.00960  -0.02440 553 MET A O     
3918 C  CB    . MET A 557 ? 0.69270 0.55550 0.69140 -0.06650 0.00840  -0.00140 553 MET A CB    
3919 C  CG    . MET A 557 ? 0.80130 0.66740 0.79710 -0.05920 0.01060  -0.00210 553 MET A CG    
3920 S  SD    . MET A 557 ? 0.83360 0.71450 0.82080 -0.05830 0.00970  -0.00300 553 MET A SD    
3921 C  CE    . MET A 557 ? 0.85950 0.73760 0.84350 -0.05180 0.01280  -0.00850 553 MET A CE    
3922 N  N     . LYS A 558 ? 0.78170 0.62470 0.77850 -0.07920 0.00680  -0.01810 554 LYS A N     
3923 C  CA    . LYS A 558 ? 0.90540 0.73610 0.90060 -0.08240 0.00750  -0.02810 554 LYS A CA    
3924 C  C     . LYS A 558 ? 1.03220 0.86910 1.01720 -0.08530 0.00670  -0.03560 554 LYS A C     
3925 O  O     . LYS A 558 ? 1.10350 0.93420 1.08340 -0.08470 0.00870  -0.04480 554 LYS A O     
3926 C  CB    . LYS A 558 ? 0.86680 0.68910 0.86820 -0.08940 0.00510  -0.02700 554 LYS A CB    
3927 C  CG    . LYS A 558 ? 0.96100 0.76600 0.96580 -0.09040 0.00680  -0.03450 554 LYS A CG    
3928 C  CD    . LYS A 558 ? 0.98790 0.78980 0.98340 -0.09200 0.00780  -0.04670 554 LYS A CD    
3929 C  CE    . LYS A 558 ? 1.01210 0.79630 1.01110 -0.09110 0.01060  -0.05490 554 LYS A CE    
3930 N  NZ    . LYS A 558 ? 1.02760 0.80810 1.01710 -0.09380 0.01160  -0.06760 554 LYS A NZ    
3931 N  N     . GLN A 559 ? 0.96520 0.81480 0.94740 -0.08850 0.00370  -0.03130 555 GLN A N     
3932 C  CA    . GLN A 559 ? 0.94290 0.79980 0.91680 -0.09320 0.00150  -0.03620 555 GLN A CA    
3933 C  C     . GLN A 559 ? 0.92100 0.78650 0.88750 -0.08810 0.00320  -0.03800 555 GLN A C     
3934 O  O     . GLN A 559 ? 0.95950 0.82650 0.91810 -0.09030 0.00300  -0.04510 555 GLN A O     
3935 C  CB    . GLN A 559 ? 0.98640 0.85330 0.96390 -0.09760 -0.00200 -0.02820 555 GLN A CB    
3936 C  CG    . GLN A 559 ? 1.03530 0.89330 1.01940 -0.10400 -0.00390 -0.02780 555 GLN A CG    
3937 C  CD    . GLN A 559 ? 1.09450 0.95490 1.08730 -0.10130 -0.00350 -0.01710 555 GLN A CD    
3938 O  OE1   . GLN A 559 ? 1.15140 1.02150 1.14370 -0.09590 -0.00240 -0.01140 555 GLN A OE1   
3939 N  NE2   . GLN A 559 ? 1.05930 0.90990 1.05980 -0.10430 -0.00390 -0.01480 555 GLN A NE2   
3940 N  N     . ARG A 560 ? 0.86710 0.73770 0.83610 -0.08150 0.00480  -0.03180 556 ARG A N     
3941 C  CA    . ARG A 560 ? 0.82690 0.70330 0.79020 -0.07610 0.00680  -0.03370 556 ARG A CA    
3942 C  C     . ARG A 560 ? 0.86950 0.73580 0.83160 -0.07230 0.01070  -0.04080 556 ARG A C     
3943 O  O     . ARG A 560 ? 0.91900 0.78760 0.87410 -0.07120 0.01220  -0.04650 556 ARG A O     
3944 C  CB    . ARG A 560 ? 0.78940 0.67420 0.75630 -0.07080 0.00710  -0.02490 556 ARG A CB    
3945 C  CG    . ARG A 560 ? 0.78610 0.68470 0.74860 -0.07110 0.00510  -0.02190 556 ARG A CG    
3946 C  CD    . ARG A 560 ? 0.82910 0.72990 0.78380 -0.06990 0.00620  -0.02810 556 ARG A CD    
3947 N  NE    . ARG A 560 ? 0.88940 0.80230 0.83930 -0.06910 0.00480  -0.02610 556 ARG A NE    
3948 C  CZ    . ARG A 560 ? 0.95560 0.87790 0.90320 -0.07310 0.00160  -0.02410 556 ARG A CZ    
3949 N  NH1   . ARG A 560 ? 0.94900 0.87220 0.89810 -0.07940 -0.00130 -0.02370 556 ARG A NH1   
3950 N  NH2   . ARG A 560 ? 0.98190 0.91320 0.92570 -0.07070 0.00120  -0.02280 556 ARG A NH2   
3951 N  N     . PHE A 561 ? 0.91360 0.76830 0.88270 -0.07090 0.01240  -0.04090 557 PHE A N     
3952 C  CA    . PHE A 561 ? 0.96940 0.81430 0.93910 -0.06650 0.01640  -0.04720 557 PHE A CA    
3953 C  C     . PHE A 561 ? 1.04530 0.88510 1.00760 -0.07020 0.01750  -0.05830 557 PHE A C     
3954 O  O     . PHE A 561 ? 1.13300 0.97200 1.09130 -0.06640 0.02090  -0.06380 557 PHE A O     
3955 C  CB    . PHE A 561 ? 0.88430 0.71750 0.86420 -0.06450 0.01760  -0.04430 557 PHE A CB    
3956 C  CG    . PHE A 561 ? 0.80640 0.64340 0.79230 -0.05790 0.01840  -0.03560 557 PHE A CG    
3957 C  CD1   . PHE A 561 ? 0.81910 0.66480 0.80160 -0.05240 0.01980  -0.03430 557 PHE A CD1   
3958 C  CD2   . PHE A 561 ? 0.80230 0.63470 0.79710 -0.05750 0.01750  -0.02850 557 PHE A CD2   
3959 C  CE1   . PHE A 561 ? 0.83850 0.68790 0.82620 -0.04680 0.02020  -0.02660 557 PHE A CE1   
3960 C  CE2   . PHE A 561 ? 0.80440 0.64080 0.80390 -0.05190 0.01800  -0.02050 557 PHE A CE2   
3961 C  CZ    . PHE A 561 ? 0.80240 0.64730 0.79820 -0.04660 0.01920  -0.01980 557 PHE A CZ    
3970 N  N     . SER B 3   ? 1.01320 0.97680 0.87880 0.00280  0.17130  -0.18640 -1  SER B N     
3971 C  CA    . SER B 3   ? 1.02770 0.97260 0.89790 0.00460  0.17060  -0.19470 -1  SER B CA    
3972 C  C     . SER B 3   ? 1.08490 1.02350 0.97740 0.01400  0.17350  -0.19130 -1  SER B C     
3973 O  O     . SER B 3   ? 1.22040 1.14730 1.11940 0.01900  0.17920  -0.20060 -1  SER B O     
3974 C  CB    . SER B 3   ? 1.01610 0.95510 0.87290 0.00290  0.17780  -0.21130 -1  SER B CB    
3975 O  OG    . SER B 3   ? 1.05050 0.97070 0.90940 0.00270  0.17600  -0.21960 -1  SER B OG    
3976 N  N     . SER B 4   ? 1.04440 0.99050 0.94850 0.01620  0.16900  -0.17760 0   SER B N     
3977 C  CA    . SER B 4   ? 1.01740 0.96020 0.94270 0.02450  0.17010  -0.17170 0   SER B CA    
3978 C  C     . SER B 4   ? 0.98500 0.91220 0.91870 0.02490  0.16300  -0.16930 0   SER B C     
3979 O  O     . SER B 4   ? 0.99490 0.91380 0.91850 0.01880  0.15730  -0.17230 0   SER B O     
3980 C  CB    . SER B 4   ? 0.95500 0.91310 0.88800 0.02580  0.16790  -0.15830 0   SER B CB    
3981 O  OG    . SER B 4   ? 0.91180 0.87620 0.83470 0.01850  0.15950  -0.15040 0   SER B OG    
3982 N  N     . LYS B 5   ? 0.95610 0.87930 0.90890 0.03220  0.16350  -0.16400 1   LYS B N     
3983 C  CA    . LYS B 5   ? 0.89260 0.80290 0.85500 0.03290  0.15650  -0.15940 1   LYS B CA    
3984 C  C     . LYS B 5   ? 0.79550 0.71020 0.75260 0.02670  0.14620  -0.14890 1   LYS B C     
3985 O  O     . LYS B 5   ? 0.81210 0.73990 0.77070 0.02640  0.14400  -0.13960 1   LYS B O     
3986 C  CB    . LYS B 5   ? 0.84030 0.74930 0.82430 0.04180  0.15860  -0.15350 1   LYS B CB    
3987 C  CG    . LYS B 5   ? 0.79970 0.69800 0.79420 0.04260  0.15080  -0.14620 1   LYS B CG    
3988 C  CD    . LYS B 5   ? 0.78140 0.67220 0.79580 0.05140  0.15450  -0.14550 1   LYS B CD    
3989 C  CE    . LYS B 5   ? 0.76810 0.67240 0.79550 0.05760  0.15790  -0.13810 1   LYS B CE    
3990 N  NZ    . LYS B 5   ? 0.71860 0.61710 0.76650 0.06480  0.15690  -0.13180 1   LYS B NZ    
3991 N  N     . THR B 6   ? 0.74280 0.64650 0.69460 0.02200  0.13990  -0.15010 2   THR B N     
3992 C  CA    . THR B 6   ? 0.64710 0.55380 0.59560 0.01680  0.13020  -0.14020 2   THR B CA    
3993 C  C     . THR B 6   ? 0.59530 0.49170 0.55640 0.01920  0.12460  -0.13400 2   THR B C     
3994 O  O     . THR B 6   ? 0.56510 0.44810 0.53230 0.02160  0.12620  -0.13930 2   THR B O     
3995 C  CB    . THR B 6   ? 0.60400 0.50940 0.53490 0.00810  0.12620  -0.14480 2   THR B CB    
3996 O  OG1   . THR B 6   ? 0.68600 0.57570 0.61690 0.00660  0.12440  -0.15100 2   THR B OG1   
3997 C  CG2   . THR B 6   ? 0.61890 0.53210 0.53580 0.00550  0.13220  -0.15320 2   THR B CG2   
3998 N  N     . VAL B 7   ? 0.61030 0.51300 0.57430 0.01780  0.11770  -0.12260 3   VAL B N     
3999 C  CA    . VAL B 7   ? 0.57430 0.46930 0.54650 0.01810  0.11100  -0.11570 3   VAL B CA    
4000 C  C     . VAL B 7   ? 0.57610 0.47520 0.53790 0.01100  0.10320  -0.11050 3   VAL B C     
4001 O  O     . VAL B 7   ? 0.53220 0.44030 0.48230 0.00660  0.10300  -0.11130 3   VAL B O     
4002 C  CB    . VAL B 7   ? 0.44310 0.34230 0.43150 0.02450  0.11040  -0.10630 3   VAL B CB    
4003 C  CG1   . VAL B 7   ? 0.43230 0.32720 0.43260 0.03200  0.11810  -0.11110 3   VAL B CG1   
4004 C  CG2   . VAL B 7   ? 0.45070 0.36530 0.43710 0.02390  0.10930  -0.09920 3   VAL B CG2   
4005 N  N     . THR B 8   ? 0.51430 0.40680 0.48050 0.00990  0.09700  -0.10500 4   THR B N     
4006 C  CA    . THR B 8   ? 0.51430 0.41160 0.47290 0.00410  0.08970  -0.09900 4   THR B CA    
4007 C  C     . THR B 8   ? 0.47450 0.38450 0.43570 0.00550  0.08760  -0.08980 4   THR B C     
4008 O  O     . THR B 8   ? 0.42330 0.33670 0.39510 0.01100  0.09000  -0.08610 4   THR B O     
4009 C  CB    . THR B 8   ? 0.52880 0.41670 0.49190 0.00280  0.08400  -0.09500 4   THR B CB    
4010 O  OG1   . THR B 8   ? 0.48860 0.37520 0.46580 0.00850  0.08330  -0.08800 4   THR B OG1   
4011 C  CG2   . THR B 8   ? 0.48810 0.36270 0.44900 0.00080  0.08570  -0.10410 4   THR B CG2   
4012 N  N     . ALA B 9   ? 0.47040 0.38750 0.42210 0.00020  0.08300  -0.08620 5   ALA B N     
4013 C  CA    . ALA B 9   ? 0.44150 0.36980 0.39550 0.00090  0.08050  -0.07760 5   ALA B CA    
4014 C  C     . ALA B 9   ? 0.48070 0.40720 0.44720 0.00500  0.07720  -0.06980 5   ALA B C     
4015 O  O     . ALA B 9   ? 0.41840 0.35170 0.39210 0.00860  0.07800  -0.06470 5   ALA B O     
4016 C  CB    . ALA B 9   ? 0.39440 0.32860 0.33770 -0.00530 0.07520  -0.07450 5   ALA B CB    
4017 N  N     . VAL B 10  ? 0.44160 0.35930 0.41060 0.00430  0.07340  -0.06850 6   VAL B N     
4018 C  CA    . VAL B 10  ? 0.44050 0.35730 0.42000 0.00760  0.06980  -0.06060 6   VAL B CA    
4019 C  C     . VAL B 10  ? 0.41770 0.33130 0.40960 0.01410  0.07410  -0.06110 6   VAL B C     
4020 O  O     . VAL B 10  ? 0.48650 0.40370 0.48750 0.01770  0.07240  -0.05420 6   VAL B O     
4021 C  CB    . VAL B 10  ? 0.51570 0.42510 0.49390 0.00470  0.06450  -0.05840 6   VAL B CB    
4022 C  CG1   . VAL B 10  ? 0.46900 0.36620 0.45080 0.00560  0.06690  -0.06400 6   VAL B CG1   
4023 C  CG2   . VAL B 10  ? 0.56610 0.47810 0.55130 0.00660  0.05970  -0.04930 6   VAL B CG2   
4024 N  N     . GLU B 11  ? 0.39880 0.30570 0.39150 0.01580  0.07980  -0.06910 7   GLU B N     
4025 C  CA    . GLU B 11  ? 0.42160 0.32660 0.42710 0.02250  0.08440  -0.06940 7   GLU B CA    
4026 C  C     . GLU B 11  ? 0.43760 0.35450 0.44620 0.02540  0.08760  -0.06720 7   GLU B C     
4027 O  O     . GLU B 11  ? 0.40690 0.32700 0.42770 0.03040  0.08800  -0.06190 7   GLU B O     
4028 C  CB    . GLU B 11  ? 0.49120 0.38580 0.49740 0.02420  0.09020  -0.07910 7   GLU B CB    
4029 C  CG    . GLU B 11  ? 0.58240 0.47550 0.60330 0.03180  0.09530  -0.07910 7   GLU B CG    
4030 C  CD    . GLU B 11  ? 0.72960 0.61060 0.75310 0.03410  0.10110  -0.08880 7   GLU B CD    
4031 O  OE1   . GLU B 11  ? 0.71960 0.60150 0.75140 0.03990  0.10760  -0.09210 7   GLU B OE1   
4032 O  OE2   . GLU B 11  ? 0.75110 0.62170 0.76900 0.03030  0.09910  -0.09310 7   GLU B OE2   
4033 N  N     . LEU B 12  ? 0.40950 0.33380 0.40760 0.02200  0.08980  -0.07070 8   LEU B N     
4034 C  CA    . LEU B 12  ? 0.43170 0.36820 0.43240 0.02390  0.09260  -0.06790 8   LEU B CA    
4035 C  C     . LEU B 12  ? 0.41570 0.35860 0.42270 0.02440  0.08680  -0.05750 8   LEU B C     
4036 O  O     . LEU B 12  ? 0.39000 0.33880 0.40760 0.02870  0.08820  -0.05320 8   LEU B O     
4037 C  CB    . LEU B 12  ? 0.43830 0.38190 0.42530 0.01900  0.09440  -0.07170 8   LEU B CB    
4038 C  CG    . LEU B 12  ? 0.56930 0.52580 0.55860 0.02060  0.09800  -0.06910 8   LEU B CG    
4039 C  CD1   . LEU B 12  ? 0.60570 0.56220 0.60160 0.02590  0.10660  -0.07520 8   LEU B CD1   
4040 C  CD2   . LEU B 12  ? 0.57320 0.53770 0.54880 0.01480  0.09740  -0.06970 8   LEU B CD2   
4041 N  N     . LEU B 13  ? 0.46450 0.40630 0.46530 0.02010  0.08010  -0.05350 9   LEU B N     
4042 C  CA    . LEU B 13  ? 0.41000 0.35680 0.41560 0.02030  0.07440  -0.04450 9   LEU B CA    
4043 C  C     . LEU B 13  ? 0.40560 0.34930 0.42490 0.02550  0.07360  -0.04020 9   LEU B C     
4044 O  O     . LEU B 13  ? 0.41310 0.36370 0.44010 0.02780  0.07210  -0.03410 9   LEU B O     
4045 C  CB    . LEU B 13  ? 0.37590 0.32020 0.37290 0.01540  0.06810  -0.04210 9   LEU B CB    
4046 C  CG    . LEU B 13  ? 0.38350 0.32930 0.38510 0.01560  0.06170  -0.03390 9   LEU B CG    
4047 C  CD1   . LEU B 13  ? 0.28630 0.24250 0.28980 0.01560  0.06060  -0.02910 9   LEU B CD1   
4048 C  CD2   . LEU B 13  ? 0.41700 0.35900 0.41040 0.01110  0.05660  -0.03300 9   LEU B CD2   
4049 N  N     . VAL B 14  ? 0.35510 0.28820 0.37760 0.02720  0.07420  -0.04290 10  VAL B N     
4050 C  CA    . VAL B 14  ? 0.41360 0.34340 0.44920 0.03200  0.07310  -0.03820 10  VAL B CA    
4051 C  C     . VAL B 14  ? 0.43940 0.37440 0.48610 0.03750  0.07850  -0.03840 10  VAL B C     
4052 O  O     . VAL B 14  ? 0.38660 0.32710 0.44350 0.04070  0.07650  -0.03160 10  VAL B O     
4053 C  CB    . VAL B 14  ? 0.33000 0.24690 0.36700 0.03240  0.07310  -0.04120 10  VAL B CB    
4054 C  CG1   . VAL B 14  ? 0.39720 0.31070 0.44930 0.03820  0.07360  -0.03710 10  VAL B CG1   
4055 C  CG2   . VAL B 14  ? 0.32500 0.23840 0.35410 0.02740  0.06690  -0.03850 10  VAL B CG2   
4056 N  N     . ARG B 15  ? 0.39720 0.33130 0.44180 0.03870  0.08540  -0.04630 11  ARG B N     
4057 C  CA    . ARG B 15  ? 0.44630 0.38570 0.50160 0.04420  0.09150  -0.04720 11  ARG B CA    
4058 C  C     . ARG B 15  ? 0.42410 0.37750 0.48140 0.04390  0.09070  -0.04160 11  ARG B C     
4059 O  O     . ARG B 15  ? 0.40820 0.36770 0.47820 0.04850  0.09250  -0.03780 11  ARG B O     
4060 C  CB    . ARG B 15  ? 0.44230 0.37830 0.49280 0.04490  0.09940  -0.05770 11  ARG B CB    
4061 C  CG    . ARG B 15  ? 0.48410 0.40590 0.53720 0.04690  0.10170  -0.06390 11  ARG B CG    
4062 C  CD    . ARG B 15  ? 0.55070 0.47010 0.59420 0.04560  0.10850  -0.07500 11  ARG B CD    
4063 N  NE    . ARG B 15  ? 0.62710 0.53270 0.67280 0.04760  0.11210  -0.08280 11  ARG B NE    
4064 C  CZ    . ARG B 15  ? 0.60580 0.50860 0.65990 0.05340  0.11960  -0.08870 11  ARG B CZ    
4065 N  NH1   . ARG B 15  ? 0.53360 0.44720 0.59510 0.05780  0.12460  -0.08730 11  ARG B NH1   
4066 N  NH2   . ARG B 15  ? 0.60570 0.49460 0.66120 0.05470  0.12240  -0.09610 11  ARG B NH2   
4067 N  N     . GLN B 16  ? 0.36320 0.32210 0.40880 0.03840  0.08820  -0.04110 12  GLN B N     
4068 C  CA    . GLN B 16  ? 0.37110 0.34260 0.41900 0.03770  0.08710  -0.03540 12  GLN B CA    
4069 C  C     . GLN B 16  ? 0.38610 0.35990 0.44200 0.03840  0.08020  -0.02640 12  GLN B C     
4070 O  O     . GLN B 16  ? 0.37570 0.35860 0.44010 0.04020  0.07990  -0.02130 12  GLN B O     
4071 C  CB    . GLN B 16  ? 0.36600 0.34210 0.39980 0.03170  0.08600  -0.03690 12  GLN B CB    
4072 C  CG    . GLN B 16  ? 0.30890 0.29780 0.34450 0.03040  0.08550  -0.03150 12  GLN B CG    
4073 C  CD    . GLN B 16  ? 0.38870 0.38540 0.43140 0.03400  0.09310  -0.03350 12  GLN B CD    
4074 O  OE1   . GLN B 16  ? 0.43380 0.43230 0.46960 0.03310  0.09900  -0.03980 12  GLN B OE1   
4075 N  NE2   . GLN B 16  ? 0.39980 0.40180 0.45670 0.03810  0.09300  -0.02820 12  GLN B NE2   
4076 N  N     . MET B 17  ? 0.35300 0.31890 0.40620 0.03690  0.07460  -0.02430 13  MET B N     
4077 C  CA    . MET B 17  ? 0.38610 0.35350 0.44660 0.03790  0.06840  -0.01630 13  MET B CA    
4078 C  C     . MET B 17  ? 0.36450 0.33170 0.44030 0.04400  0.07030  -0.01370 13  MET B C     
4079 O  O     . MET B 17  ? 0.39030 0.36380 0.47480 0.04550  0.06680  -0.00680 13  MET B O     
4080 C  CB    . MET B 17  ? 0.33890 0.29810 0.39260 0.03500  0.06280  -0.01510 13  MET B CB    
4081 C  CG    . MET B 17  ? 0.41260 0.37330 0.45330 0.02930  0.05940  -0.01560 13  MET B CG    
4082 S  SD    . MET B 17  ? 0.44840 0.40270 0.48340 0.02630  0.05230  -0.01220 13  MET B SD    
4083 C  CE    . MET B 17  ? 0.33770 0.27950 0.37320 0.02760  0.05490  -0.01690 13  MET B CE    
4084 N  N     . GLU B 18  ? 0.29710 0.25680 0.37660 0.04740  0.07550  -0.01910 14  GLU B N     
4085 C  CA    . GLU B 18  ? 0.41820 0.37780 0.51330 0.05380  0.07820  -0.01690 14  GLU B CA    
4086 C  C     . GLU B 18  ? 0.46130 0.43360 0.56520 0.05630  0.08120  -0.01430 14  GLU B C     
4087 O  O     . GLU B 18  ? 0.41530 0.39320 0.53150 0.05940  0.07870  -0.00740 14  GLU B O     
4088 C  CB    . GLU B 18  ? 0.39460 0.34440 0.49160 0.05700  0.08470  -0.02470 14  GLU B CB    
4089 C  CG    . GLU B 18  ? 0.51670 0.45340 0.61030 0.05570  0.08180  -0.02590 14  GLU B CG    
4090 C  CD    . GLU B 18  ? 0.56850 0.49460 0.66210 0.05790  0.08840  -0.03510 14  GLU B CD    
4091 O  OE1   . GLU B 18  ? 0.53650 0.45170 0.62380 0.05530  0.08660  -0.03810 14  GLU B OE1   
4092 O  OE2   . GLU B 18  ? 0.57630 0.50520 0.67630 0.06220  0.09530  -0.03950 14  GLU B OE2   
4093 N  N     . ALA B 19  ? 0.44540 0.42310 0.54270 0.05450  0.08610  -0.01930 15  ALA B N     
4094 C  CA    . ALA B 19  ? 0.41310 0.40350 0.51840 0.05650  0.08960  -0.01700 15  ALA B CA    
4095 C  C     . ALA B 19  ? 0.44160 0.44100 0.55020 0.05420  0.08280  -0.00810 15  ALA B C     
4096 O  O     . ALA B 19  ? 0.51290 0.52260 0.63250 0.05660  0.08410  -0.00400 15  ALA B O     
4097 C  CB    . ALA B 19  ? 0.38600 0.38070 0.48130 0.05400  0.09560  -0.02350 15  ALA B CB    
4098 N  N     . GLU B 20  ? 0.42430 0.42040 0.52380 0.04950  0.07560  -0.00530 16  GLU B N     
4099 C  CA    . GLU B 20  ? 0.34400 0.34720 0.44620 0.04720  0.06870  0.00240  16  GLU B CA    
4100 C  C     . GLU B 20  ? 0.40760 0.40910 0.52000 0.05010  0.06370  0.00860  16  GLU B C     
4101 O  O     . GLU B 20  ? 0.46140 0.46810 0.57570 0.04800  0.05740  0.01480  16  GLU B O     
4102 C  CB    . GLU B 20  ? 0.37460 0.37560 0.46250 0.04100  0.06350  0.00240  16  GLU B CB    
4103 C  CG    . GLU B 20  ? 0.49250 0.49880 0.57160 0.03730  0.06660  -0.00070 16  GLU B CG    
4104 C  CD    . GLU B 20  ? 0.50420 0.52140 0.58700 0.03500  0.06370  0.00500  16  GLU B CD    
4105 O  OE1   . GLU B 20  ? 0.51710 0.53990 0.59480 0.03230  0.06650  0.00360  16  GLU B OE1   
4106 O  OE2   . GLU B 20  ? 0.55940 0.57940 0.64980 0.03560  0.05850  0.01100  16  GLU B OE2   
4107 N  N     . GLY B 21  ? 0.43970 0.43390 0.55860 0.05450  0.06620  0.00710  17  GLY B N     
4108 C  CA    . GLY B 21  ? 0.40670 0.39940 0.53520 0.05710  0.06120  0.01370  17  GLY B CA    
4109 C  C     . GLY B 21  ? 0.44600 0.43140 0.56520 0.05350  0.05450  0.01570  17  GLY B C     
4110 O  O     . GLY B 21  ? 0.40630 0.39280 0.53080 0.05420  0.04890  0.02230  17  GLY B O     
4111 N  N     . VAL B 22  ? 0.39260 0.37140 0.49780 0.04960  0.05500  0.01030  18  VAL B N     
4112 C  CA    . VAL B 22  ? 0.39790 0.36950 0.49460 0.04650  0.04950  0.01180  18  VAL B CA    
4113 C  C     . VAL B 22  ? 0.38820 0.35130 0.49180 0.05010  0.04980  0.01290  18  VAL B C     
4114 O  O     . VAL B 22  ? 0.41050 0.36740 0.51730 0.05300  0.05550  0.00780  18  VAL B O     
4115 C  CB    . VAL B 22  ? 0.37500 0.34200 0.45670 0.04190  0.05040  0.00580  18  VAL B CB    
4116 C  CG1   . VAL B 22  ? 0.38390 0.34320 0.45840 0.03930  0.04570  0.00700  18  VAL B CG1   
4117 C  CG2   . VAL B 22  ? 0.40600 0.38140 0.48140 0.03810  0.04890  0.00620  18  VAL B CG2   
4118 N  N     . SER B 23  ? 0.35280 0.31510 0.45820 0.04970  0.04370  0.01940  19  SER B N     
4119 C  CA    . SER B 23  ? 0.39690 0.35150 0.50960 0.05290  0.04340  0.02190  19  SER B CA    
4120 C  C     . SER B 23  ? 0.36980 0.31630 0.47310 0.04950  0.03970  0.02240  19  SER B C     
4121 O  O     . SER B 23  ? 0.36920 0.30730 0.47680 0.05140  0.04050  0.02300  19  SER B O     
4122 C  CB    . SER B 23  ? 0.45370 0.41470 0.57940 0.05630  0.03960  0.03060  19  SER B CB    
4123 O  OG    . SER B 23  ? 0.64130 0.60880 0.77900 0.06060  0.04380  0.03050  19  SER B OG    
4124 N  N     . TYR B 24  ? 0.36560 0.31420 0.45670 0.04450  0.03600  0.02210  20  TYR B N     
4125 C  CA    . TYR B 24  ? 0.35750 0.30020 0.43980 0.04110  0.03250  0.02300  20  TYR B CA    
4126 C  C     . TYR B 24  ? 0.37940 0.32220 0.44800 0.03630  0.03260  0.01800  20  TYR B C     
4127 O  O     . TYR B 24  ? 0.33750 0.28720 0.40290 0.03480  0.03260  0.01670  20  TYR B O     
4128 C  CB    . TYR B 24  ? 0.31310 0.26030 0.39650 0.04040  0.02590  0.03120  20  TYR B CB    
4129 C  CG    . TYR B 24  ? 0.30350 0.25100 0.40020 0.04470  0.02470  0.03760  20  TYR B CG    
4130 C  CD1   . TYR B 24  ? 0.30230 0.24150 0.40250 0.04600  0.02460  0.04000  20  TYR B CD1   
4131 C  CD2   . TYR B 24  ? 0.34780 0.30410 0.45400 0.04740  0.02340  0.04190  20  TYR B CD2   
4132 C  CE1   . TYR B 24  ? 0.31810 0.25770 0.43120 0.05010  0.02320  0.04670  20  TYR B CE1   
4133 C  CE2   . TYR B 24  ? 0.33230 0.28970 0.45160 0.05160  0.02200  0.04850  20  TYR B CE2   
4134 C  CZ    . TYR B 24  ? 0.38360 0.33260 0.50620 0.05300  0.02190  0.05100  20  TYR B CZ    
4135 O  OH    . TYR B 24  ? 0.50060 0.45080 0.63680 0.05720  0.02030  0.05830  20  TYR B OH    
4136 N  N     . VAL B 25  ? 0.32550 0.26080 0.38680 0.03360  0.03230  0.01570  21  VAL B N     
4137 C  CA    . VAL B 25  ? 0.36780 0.30350 0.41650 0.02890  0.03110  0.01240  21  VAL B CA    
4138 C  C     . VAL B 25  ? 0.35130 0.28480 0.39540 0.02650  0.02650  0.01660  21  VAL B C     
4139 O  O     . VAL B 25  ? 0.36240 0.28870 0.40810 0.02670  0.02680  0.01720  21  VAL B O     
4140 C  CB    . VAL B 25  ? 0.39920 0.32900 0.44240 0.02730  0.03570  0.00470  21  VAL B CB    
4141 C  CG1   . VAL B 25  ? 0.35980 0.29060 0.39080 0.02240  0.03380  0.00260  21  VAL B CG1   
4142 C  CG2   . VAL B 25  ? 0.40250 0.33550 0.44940 0.02950  0.04080  0.00040  21  VAL B CG2   
4143 N  N     . PHE B 26  ? 0.37330 0.31280 0.41180 0.02430  0.02230  0.01940  22  PHE B N     
4144 C  CA    . PHE B 26  ? 0.34260 0.28170 0.37610 0.02220  0.01810  0.02330  22  PHE B CA    
4145 C  C     . PHE B 26  ? 0.32700 0.26370 0.35010 0.01820  0.01850  0.01920  22  PHE B C     
4146 O  O     . PHE B 26  ? 0.33690 0.27670 0.35490 0.01660  0.01940  0.01560  22  PHE B O     
4147 C  CB    . PHE B 26  ? 0.32800 0.27480 0.36070 0.02200  0.01360  0.02780  22  PHE B CB    
4148 C  CG    . PHE B 26  ? 0.33910 0.29000 0.38210 0.02540  0.01260  0.03220  22  PHE B CG    
4149 C  CD1   . PHE B 26  ? 0.35130 0.30160 0.39960 0.02700  0.01000  0.03830  22  PHE B CD1   
4150 C  CD2   . PHE B 26  ? 0.33410 0.29000 0.38180 0.02680  0.01410  0.03080  22  PHE B CD2   
4151 C  CE1   . PHE B 26  ? 0.31910 0.27380 0.37760 0.03020  0.00870  0.04300  22  PHE B CE1   
4152 C  CE2   . PHE B 26  ? 0.36680 0.32740 0.42510 0.03000  0.01310  0.03530  22  PHE B CE2   
4153 C  CZ    . PHE B 26  ? 0.34290 0.30280 0.40670 0.03170  0.01020  0.04140  22  PHE B CZ    
4154 N  N     . GLY B 27  ? 0.32560 0.25750 0.34610 0.01660  0.01770  0.02040  23  GLY B N     
4155 C  CA    . GLY B 27  ? 0.31460 0.24530 0.32620 0.01290  0.01770  0.01710  23  GLY B CA    
4156 C  C     . GLY B 27  ? 0.40400 0.32900 0.41460 0.01110  0.01740  0.01850  23  GLY B C     
4157 O  O     . GLY B 27  ? 0.37440 0.29670 0.39050 0.01260  0.01640  0.02300  23  GLY B O     
4158 N  N     . ILE B 28  ? 0.34080 0.26460 0.34460 0.00770  0.01790  0.01510  24  ILE B N     
4159 C  CA    . ILE B 28  ? 0.34690 0.26590 0.34900 0.00500  0.01760  0.01580  24  ILE B CA    
4160 C  C     . ILE B 28  ? 0.34950 0.26420 0.34830 0.00240  0.02020  0.00940  24  ILE B C     
4161 O  O     . ILE B 28  ? 0.36950 0.28790 0.36270 0.00090  0.02060  0.00580  24  ILE B O     
4162 C  CB    . ILE B 28  ? 0.32900 0.25290 0.32540 0.00290  0.01460  0.01940  24  ILE B CB    
4163 C  CG1   . ILE B 28  ? 0.36980 0.29760 0.36900 0.00520  0.01190  0.02560  24  ILE B CG1   
4164 C  CG2   . ILE B 28  ? 0.33160 0.25150 0.32620 -0.00050 0.01470  0.01960  24  ILE B CG2   
4165 C  CD1   . ILE B 28  ? 0.43080 0.36420 0.42390 0.00360  0.00930  0.02870  24  ILE B CD1   
4166 N  N     . PRO B 29  ? 0.33830 0.24530 0.34000 0.00140  0.02170  0.00810  25  PRO B N     
4167 C  CA    . PRO B 29  ? 0.43530 0.33780 0.43360 -0.00140 0.02400  0.00130  25  PRO B CA    
4168 C  C     . PRO B 29  ? 0.49830 0.40350 0.48930 -0.00600 0.02230  0.00060  25  PRO B C     
4169 O  O     . PRO B 29  ? 0.45480 0.36440 0.44380 -0.00700 0.01960  0.00520  25  PRO B O     
4170 C  CB    . PRO B 29  ? 0.41580 0.30840 0.42070 -0.00090 0.02570  0.00070  25  PRO B CB    
4171 C  CG    . PRO B 29  ? 0.38630 0.27910 0.39570 0.00010  0.02310  0.00850  25  PRO B CG    
4172 C  CD    . PRO B 29  ? 0.37490 0.27620 0.38420 0.00300  0.02140  0.01240  25  PRO B CD    
4173 N  N     . GLY B 30  ? 0.49720 0.40000 0.48420 -0.00880 0.02390  -0.00550 26  GLY B N     
4174 C  CA    . GLY B 30  ? 0.38000 0.28470 0.36090 -0.01360 0.02240  -0.00680 26  GLY B CA    
4175 C  C     . GLY B 30  ? 0.45190 0.35220 0.42970 -0.01620 0.02460  -0.01420 26  GLY B C     
4176 O  O     . GLY B 30  ? 0.50220 0.40010 0.48100 -0.01400 0.02760  -0.01840 26  GLY B O     
4177 N  N     . GLY B 31  ? 0.39190 0.29190 0.36560 -0.02110 0.02320  -0.01570 27  GLY B N     
4178 C  CA    . GLY B 31  ? 0.42060 0.31600 0.39070 -0.02460 0.02470  -0.02270 27  GLY B CA    
4179 C  C     . GLY B 31  ? 0.38810 0.28520 0.35450 -0.02310 0.02750  -0.02830 27  GLY B C     
4180 O  O     . GLY B 31  ? 0.44030 0.33090 0.40880 -0.02150 0.03080  -0.03310 27  GLY B O     
4181 N  N     . PRO B 32  ? 0.43870 0.34460 0.39990 -0.02340 0.02650  -0.02750 28  PRO B N     
4182 C  CA    . PRO B 32  ? 0.36770 0.27620 0.32480 -0.02270 0.02920  -0.03230 28  PRO B CA    
4183 C  C     . PRO B 32  ? 0.44680 0.35450 0.40930 -0.01720 0.03220  -0.03210 28  PRO B C     
4184 O  O     . PRO B 32  ? 0.38600 0.29490 0.34630 -0.01630 0.03530  -0.03660 28  PRO B O     
4185 C  CB    . PRO B 32  ? 0.43160 0.35010 0.38350 -0.02420 0.02670  -0.02950 28  PRO B CB    
4186 C  CG    . PRO B 32  ? 0.47910 0.39990 0.43260 -0.02520 0.02310  -0.02370 28  PRO B CG    
4187 C  CD    . PRO B 32  ? 0.46360 0.37740 0.42340 -0.02390 0.02320  -0.02170 28  PRO B CD    
4188 N  N     . LEU B 33  ? 0.39840 0.30480 0.36790 -0.01370 0.03140  -0.02690 29  LEU B N     
4189 C  CA    . LEU B 33  ? 0.43250 0.33880 0.40850 -0.00850 0.03360  -0.02580 29  LEU B CA    
4190 C  C     . LEU B 33  ? 0.37180 0.26870 0.35390 -0.00640 0.03680  -0.02900 29  LEU B C     
4191 O  O     . LEU B 33  ? 0.44440 0.34080 0.43200 -0.00210 0.03960  -0.02960 29  LEU B O     
4192 C  CB    . LEU B 33  ? 0.50850 0.41860 0.48890 -0.00600 0.03070  -0.01830 29  LEU B CB    
4193 C  CG    . LEU B 33  ? 0.43120 0.34510 0.41690 -0.00130 0.03150  -0.01560 29  LEU B CG    
4194 C  CD1   . LEU B 33  ? 0.43740 0.35810 0.41860 -0.00170 0.03270  -0.01800 29  LEU B CD1   
4195 C  CD2   . LEU B 33  ? 0.44670 0.36420 0.43500 0.00000  0.02780  -0.00850 29  LEU B CD2   
4196 N  N     . MET B 34  ? 0.42730 0.31650 0.40900 -0.00940 0.03650  -0.03130 30  MET B N     
4197 C  CA    . MET B 34  ? 0.42070 0.29980 0.40960 -0.00730 0.03900  -0.03370 30  MET B CA    
4198 C  C     . MET B 34  ? 0.43210 0.30870 0.42190 -0.00460 0.04420  -0.04070 30  MET B C     
4199 O  O     . MET B 34  ? 0.42640 0.29740 0.42490 -0.00020 0.04670  -0.04070 30  MET B O     
4200 C  CB    . MET B 34  ? 0.40950 0.28070 0.39710 -0.01200 0.03770  -0.03580 30  MET B CB    
4201 C  CG    . MET B 34  ? 0.44380 0.31680 0.43250 -0.01420 0.03330  -0.02830 30  MET B CG    
4202 S  SD    . MET B 34  ? 0.56930 0.44460 0.56700 -0.00860 0.03200  -0.01910 30  MET B SD    
4203 C  CE    . MET B 34  ? 0.50780 0.37030 0.51580 -0.00580 0.03470  -0.02060 30  MET B CE    
4204 N  N     . PRO B 35  ? 0.46810 0.34860 0.44970 -0.00690 0.04600  -0.04650 31  PRO B N     
4205 C  CA    . PRO B 35  ? 0.45300 0.33180 0.43560 -0.00390 0.05150  -0.05310 31  PRO B CA    
4206 C  C     . PRO B 35  ? 0.41500 0.29860 0.40570 0.00220  0.05340  -0.04910 31  PRO B C     
4207 O  O     . PRO B 35  ? 0.45760 0.33690 0.45480 0.00630  0.05780  -0.05250 31  PRO B O     
4208 C  CB    . PRO B 35  ? 0.51700 0.40210 0.48810 -0.00800 0.05220  -0.05800 31  PRO B CB    
4209 C  CG    . PRO B 35  ? 0.48950 0.37440 0.45430 -0.01400 0.04750  -0.05670 31  PRO B CG    
4210 C  CD    . PRO B 35  ? 0.47840 0.36450 0.44960 -0.01240 0.04350  -0.04780 31  PRO B CD    
4211 N  N     . LEU B 36  ? 0.40700 0.29930 0.39810 0.00290  0.05010  -0.04200 32  LEU B N     
4212 C  CA    . LEU B 36  ? 0.33210 0.22910 0.33140 0.00820  0.05120  -0.03780 32  LEU B CA    
4213 C  C     . LEU B 36  ? 0.39910 0.28900 0.40960 0.01220  0.05140  -0.03460 32  LEU B C     
4214 O  O     . LEU B 36  ? 0.41440 0.30360 0.43330 0.01700  0.05480  -0.03520 32  LEU B O     
4215 C  CB    . LEU B 36  ? 0.35870 0.26530 0.35610 0.00770  0.04700  -0.03100 32  LEU B CB    
4216 C  CG    . LEU B 36  ? 0.40740 0.31900 0.41390 0.01260  0.04700  -0.02580 32  LEU B CG    
4217 C  CD1   . LEU B 36  ? 0.37160 0.28760 0.37970 0.01500  0.05190  -0.02960 32  LEU B CD1   
4218 C  CD2   . LEU B 36  ? 0.39760 0.31660 0.40240 0.01170  0.04200  -0.01900 32  LEU B CD2   
4219 N  N     . TYR B 37  ? 0.42660 0.31170 0.43790 0.01030  0.04770  -0.03080 33  TYR B N     
4220 C  CA    . TYR B 37  ? 0.43910 0.31750 0.46110 0.01370  0.04740  -0.02680 33  TYR B CA    
4221 C  C     . TYR B 37  ? 0.42480 0.29290 0.45170 0.01550  0.05210  -0.03350 33  TYR B C     
4222 O  O     . TYR B 37  ? 0.41500 0.27970 0.45270 0.02060  0.05430  -0.03190 33  TYR B O     
4223 C  CB    . TYR B 37  ? 0.41230 0.28830 0.43330 0.01060  0.04260  -0.02110 33  TYR B CB    
4224 C  CG    . TYR B 37  ? 0.44400 0.32940 0.46410 0.01100  0.03840  -0.01340 33  TYR B CG    
4225 C  CD1   . TYR B 37  ? 0.41260 0.30080 0.44140 0.01540  0.03730  -0.00710 33  TYR B CD1   
4226 C  CD2   . TYR B 37  ? 0.41370 0.30540 0.42460 0.00710  0.03560  -0.01260 33  TYR B CD2   
4227 C  CE1   . TYR B 37  ? 0.38640 0.28290 0.41360 0.01550  0.03340  -0.00080 33  TYR B CE1   
4228 C  CE2   . TYR B 37  ? 0.48060 0.38030 0.49060 0.00760  0.03200  -0.00640 33  TYR B CE2   
4229 C  CZ    . TYR B 37  ? 0.52700 0.42890 0.54480 0.01160  0.03100  -0.00080 33  TYR B CZ    
4230 O  OH    . TYR B 37  ? 0.51660 0.42600 0.53280 0.01180  0.02730  0.00480  33  TYR B OH    
4231 N  N     . GLU B 38  ? 0.46160 0.32460 0.48080 0.01140  0.05380  -0.04120 34  GLU B N     
4232 C  CA    . GLU B 38  ? 0.47710 0.33000 0.49980 0.01300  0.05870  -0.04910 34  GLU B CA    
4233 C  C     . GLU B 38  ? 0.42720 0.28360 0.45480 0.01850  0.06410  -0.05240 34  GLU B C     
4234 O  O     . GLU B 38  ? 0.42600 0.27550 0.46360 0.02320  0.06770  -0.05410 34  GLU B O     
4235 C  CB    . GLU B 38  ? 0.51800 0.36680 0.52960 0.00700  0.05940  -0.05750 34  GLU B CB    
4236 C  CG    . GLU B 38  ? 0.56840 0.40590 0.58220 0.00810  0.06460  -0.06710 34  GLU B CG    
4237 C  CD    . GLU B 38  ? 0.64450 0.47830 0.64660 0.00150  0.06470  -0.07550 34  GLU B CD    
4238 O  OE1   . GLU B 38  ? 0.64470 0.46640 0.64870 -0.00030 0.06540  -0.08040 34  GLU B OE1   
4239 O  OE2   . GLU B 38  ? 0.62580 0.46870 0.61700 -0.00200 0.06380  -0.07710 34  GLU B OE2   
4240 N  N     . ALA B 39  ? 0.43530 0.30260 0.45650 0.01800  0.06490  -0.05290 35  ALA B N     
4241 C  CA    . ALA B 39  ? 0.41420 0.28640 0.44040 0.02300  0.07010  -0.05530 35  ALA B CA    
4242 C  C     . ALA B 39  ? 0.49660 0.37130 0.53640 0.02890  0.06930  -0.04750 35  ALA B C     
4243 O  O     . ALA B 39  ? 0.47670 0.34950 0.52610 0.03430  0.07400  -0.04950 35  ALA B O     
4244 C  CB    . ALA B 39  ? 0.36980 0.25380 0.38670 0.02070  0.07040  -0.05630 35  ALA B CB    
4245 N  N     . ILE B 40  ? 0.44610 0.32550 0.48710 0.02810  0.06350  -0.03860 36  ILE B N     
4246 C  CA    . ILE B 40  ? 0.45440 0.33700 0.50760 0.03310  0.06210  -0.03070 36  ILE B CA    
4247 C  C     . ILE B 40  ? 0.45680 0.32850 0.52140 0.03690  0.06370  -0.03030 36  ILE B C     
4248 O  O     . ILE B 40  ? 0.47910 0.35110 0.55540 0.04270  0.06670  -0.02910 36  ILE B O     
4249 C  CB    . ILE B 40  ? 0.41510 0.30410 0.46600 0.03090  0.05540  -0.02190 36  ILE B CB    
4250 C  CG1   . ILE B 40  ? 0.41720 0.31740 0.46040 0.02880  0.05430  -0.02150 36  ILE B CG1   
4251 C  CG2   . ILE B 40  ? 0.44970 0.34000 0.51310 0.03540  0.05310  -0.01360 36  ILE B CG2   
4252 C  CD1   . ILE B 40  ? 0.45650 0.36230 0.49580 0.02620  0.04810  -0.01450 36  ILE B CD1   
4253 N  N     . PHE B 41  ? 0.46240 0.32440 0.52450 0.03360  0.06170  -0.03100 37  PHE B N     
4254 C  CA    . PHE B 41  ? 0.49780 0.34870 0.57120 0.03680  0.06260  -0.02980 37  PHE B CA    
4255 C  C     . PHE B 41  ? 0.52680 0.36990 0.60480 0.04010  0.06950  -0.03900 37  PHE B C     
4256 O  O     . PHE B 41  ? 0.53030 0.36620 0.62110 0.04500  0.07150  -0.03770 37  PHE B O     
4257 C  CB    . PHE B 41  ? 0.48500 0.32770 0.55440 0.03180  0.05870  -0.02820 37  PHE B CB    
4258 C  CG    . PHE B 41  ? 0.53570 0.38360 0.60600 0.03060  0.05250  -0.01740 37  PHE B CG    
4259 C  CD1   . PHE B 41  ? 0.57350 0.42050 0.65600 0.03480  0.05070  -0.00910 37  PHE B CD1   
4260 C  CD2   . PHE B 41  ? 0.51140 0.36560 0.57040 0.02530  0.04850  -0.01560 37  PHE B CD2   
4261 C  CE1   . PHE B 41  ? 0.57880 0.43110 0.66100 0.03340  0.04510  0.00060  37  PHE B CE1   
4262 C  CE2   . PHE B 41  ? 0.54020 0.39950 0.59940 0.02430  0.04330  -0.00630 37  PHE B CE2   
4263 C  CZ    . PHE B 41  ? 0.55270 0.41110 0.62290 0.02820  0.04150  0.00160  37  PHE B CZ    
4264 N  N     . SER B 42  ? 0.52110 0.36570 0.58920 0.03780  0.07330  -0.04820 38  SER B N     
4265 C  CA    . SER B 42  ? 0.52920 0.36690 0.60080 0.04110  0.08040  -0.05770 38  SER B CA    
4266 C  C     . SER B 42  ? 0.53150 0.37680 0.61290 0.04800  0.08490  -0.05670 38  SER B C     
4267 O  O     . SER B 42  ? 0.54130 0.38030 0.63140 0.05290  0.09060  -0.06200 38  SER B O     
4268 C  CB    . SER B 42  ? 0.59990 0.43740 0.65650 0.03590  0.08290  -0.06810 38  SER B CB    
4269 O  OG    . SER B 42  ? 0.72400 0.57400 0.77570 0.03670  0.08560  -0.06950 38  SER B OG    
4270 N  N     . ARG B 43  ? 0.58070 0.43940 0.66200 0.04850  0.08220  -0.04980 39  ARG B N     
4271 C  CA    . ARG B 43  ? 0.54130 0.40880 0.63210 0.05440  0.08610  -0.04830 39  ARG B CA    
4272 C  C     . ARG B 43  ? 0.58980 0.45750 0.69700 0.06000  0.08400  -0.03900 39  ARG B C     
4273 O  O     . ARG B 43  ? 0.63560 0.50590 0.75470 0.06620  0.08840  -0.03900 39  ARG B O     
4274 C  CB    . ARG B 43  ? 0.49860 0.38070 0.58140 0.05190  0.08450  -0.04570 39  ARG B CB    
4275 C  CG    . ARG B 43  ? 0.52280 0.40740 0.59140 0.04770  0.08800  -0.05470 39  ARG B CG    
4276 C  CD    . ARG B 43  ? 0.51540 0.39980 0.58800 0.05210  0.09660  -0.06280 39  ARG B CD    
4277 N  NE    . ARG B 43  ? 0.56850 0.46410 0.65160 0.05720  0.09880  -0.05800 39  ARG B NE    
4278 C  CZ    . ARG B 43  ? 0.58180 0.47900 0.67300 0.06270  0.10630  -0.06270 39  ARG B CZ    
4279 N  NH1   . ARG B 43  ? 0.58120 0.46890 0.67050 0.06380  0.11240  -0.07300 39  ARG B NH1   
4280 N  NH2   . ARG B 43  ? 0.50210 0.41060 0.60350 0.06690  0.10770  -0.05740 39  ARG B NH2   
4281 N  N     . LYS B 44  ? 0.55400 0.41910 0.66220 0.05800  0.07740  -0.03100 40  LYS B N     
4282 C  CA    . LYS B 44  ? 0.60540 0.47050 0.72860 0.06270  0.07460  -0.02150 40  LYS B CA    
4283 C  C     . LYS B 44  ? 0.58580 0.46420 0.71740 0.06710  0.07510  -0.01630 40  LYS B C     
4284 O  O     . LYS B 44  ? 0.61570 0.49420 0.76240 0.07340  0.07750  -0.01350 40  LYS B O     
4285 C  CB    . LYS B 44  ? 0.68500 0.53670 0.82000 0.06730  0.07860  -0.02450 40  LYS B CB    
4286 C  CG    . LYS B 44  ? 0.74760 0.58540 0.87700 0.06290  0.07700  -0.02770 40  LYS B CG    
4287 C  CD    . LYS B 44  ? 0.82210 0.64770 0.95320 0.06470  0.08390  -0.03910 40  LYS B CD    
4288 C  CE    . LYS B 44  ? 0.88490 0.69950 1.00470 0.05810  0.08250  -0.04500 40  LYS B CE    
4289 N  NZ    . LYS B 44  ? 0.92820 0.73580 1.04200 0.05750  0.08930  -0.05880 40  LYS B NZ    
4290 N  N     . LYS B 45  ? 0.60290 0.49270 0.72530 0.06350  0.07250  -0.01460 41  LYS B N     
4291 C  CA    . LYS B 45  ? 0.52570 0.42860 0.65550 0.06640  0.07120  -0.00820 41  LYS B CA    
4292 C  C     . LYS B 45  ? 0.55900 0.46970 0.68110 0.06170  0.06360  -0.00100 41  LYS B C     
4293 O  O     . LYS B 45  ? 0.58600 0.50050 0.71540 0.06310  0.05860  0.00800  41  LYS B O     
4294 C  CB    . LYS B 45  ? 0.45320 0.36350 0.58180 0.06780  0.07740  -0.01460 41  LYS B CB    
4295 C  CG    . LYS B 45  ? 0.53560 0.43850 0.67190 0.07290  0.08560  -0.02240 41  LYS B CG    
4296 C  CD    . LYS B 45  ? 0.61000 0.52090 0.74410 0.07410  0.09240  -0.02910 41  LYS B CD    
4297 C  CE    . LYS B 45  ? 0.72910 0.63180 0.87000 0.07920  0.10100  -0.03790 41  LYS B CE    
4298 N  NZ    . LYS B 45  ? 0.74090 0.64630 0.90180 0.08730  0.10380  -0.03340 41  LYS B NZ    
4299 N  N     . ILE B 46  ? 0.39770 0.31080 0.50510 0.05620  0.06270  -0.00490 42  ILE B N     
4300 C  CA    . ILE B 46  ? 0.42210 0.34060 0.52120 0.05160  0.05580  0.00070  42  ILE B CA    
4301 C  C     . ILE B 46  ? 0.40910 0.31910 0.50630 0.04960  0.05160  0.00410  42  ILE B C     
4302 O  O     . ILE B 46  ? 0.46370 0.36330 0.55820 0.04850  0.05380  -0.00080 42  ILE B O     
4303 C  CB    . ILE B 46  ? 0.41610 0.33850 0.50080 0.04650  0.05620  -0.00450 42  ILE B CB    
4304 C  CG1   . ILE B 46  ? 0.43710 0.36940 0.52420 0.04810  0.05980  -0.00620 42  ILE B CG1   
4305 C  CG2   . ILE B 46  ? 0.43390 0.35940 0.50960 0.04170  0.04950  0.00030  42  ILE B CG2   
4306 C  CD1   . ILE B 46  ? 0.37170 0.30770 0.44560 0.04350  0.06110  -0.01150 42  ILE B CD1   
4307 N  N     . GLN B 47  ? 0.36360 0.27810 0.46240 0.04900  0.04550  0.01270  43  GLN B N     
4308 C  CA    . GLN B 47  ? 0.35850 0.26650 0.45590 0.04710  0.04140  0.01720  43  GLN B CA    
4309 C  C     . GLN B 47  ? 0.39110 0.30170 0.47450 0.04120  0.03730  0.01740  43  GLN B C     
4310 O  O     . GLN B 47  ? 0.39460 0.31440 0.47420 0.03990  0.03410  0.02050  43  GLN B O     
4311 C  CB    . GLN B 47  ? 0.36690 0.27820 0.47540 0.05040  0.03750  0.02690  43  GLN B CB    
4312 C  CG    . GLN B 47  ? 0.63130 0.53690 0.73890 0.04850  0.03330  0.03270  43  GLN B CG    
4313 C  CD    . GLN B 47  ? 0.79460 0.69550 0.91700 0.05330  0.03330  0.03850  43  GLN B CD    
4314 O  OE1   . GLN B 47  ? 0.75920 0.66190 0.89330 0.05850  0.03630  0.03860  43  GLN B OE1   
4315 N  NE2   . GLN B 47  ? 0.81290 0.70810 0.93550 0.05180  0.03010  0.04390  43  GLN B NE2   
4316 N  N     . PRO B 48  ? 0.37010 0.27290 0.44620 0.03770  0.03730  0.01450  44  PRO B N     
4317 C  CA    . PRO B 48  ? 0.35680 0.26260 0.42110 0.03260  0.03330  0.01570  44  PRO B CA    
4318 C  C     . PRO B 48  ? 0.43230 0.34040 0.49850 0.03230  0.02790  0.02460  44  PRO B C     
4319 O  O     . PRO B 48  ? 0.37700 0.28020 0.45150 0.03450  0.02730  0.02920  44  PRO B O     
4320 C  CB    . PRO B 48  ? 0.35030 0.24700 0.40820 0.02920  0.03530  0.00980  44  PRO B CB    
4321 C  CG    . PRO B 48  ? 0.33870 0.22580 0.40670 0.03250  0.03850  0.00850  44  PRO B CG    
4322 C  CD    . PRO B 48  ? 0.36350 0.25460 0.44220 0.03810  0.04100  0.00960  44  PRO B CD    
4323 N  N     . ILE B 49  ? 0.40940 0.32510 0.46780 0.02960  0.02400  0.02710  45  ILE B N     
4324 C  CA    . ILE B 49  ? 0.41180 0.33080 0.46910 0.02860  0.01890  0.03480  45  ILE B CA    
4325 C  C     . ILE B 49  ? 0.39560 0.31420 0.44120 0.02380  0.01730  0.03330  45  ILE B C     
4326 O  O     . ILE B 49  ? 0.38420 0.30740 0.42180 0.02160  0.01700  0.02990  45  ILE B O     
4327 C  CB    . ILE B 49  ? 0.37070 0.29980 0.42970 0.02990  0.01560  0.03920  45  ILE B CB    
4328 C  CG1   . ILE B 49  ? 0.32010 0.25080 0.39200 0.03480  0.01710  0.04120  45  ILE B CG1   
4329 C  CG2   . ILE B 49  ? 0.31210 0.24500 0.36800 0.02830  0.01020  0.04650  45  ILE B CG2   
4330 C  CD1   . ILE B 49  ? 0.30200 0.22750 0.38420 0.03770  0.01650  0.04720  45  ILE B CD1   
4331 N  N     . LEU B 50  ? 0.38570 0.29890 0.43110 0.02220  0.01630  0.03630  46  LEU B N     
4332 C  CA    . LEU B 50  ? 0.30800 0.22160 0.34380 0.01780  0.01470  0.03600  46  LEU B CA    
4333 C  C     . LEU B 50  ? 0.36190 0.28380 0.39320 0.01700  0.01040  0.04170  46  LEU B C     
4334 O  O     . LEU B 50  ? 0.38170 0.30510 0.41760 0.01850  0.00780  0.04870  46  LEU B O     
4335 C  CB    . LEU B 50  ? 0.33610 0.24130 0.37420 0.01630  0.01520  0.03780  46  LEU B CB    
4336 C  CG    . LEU B 50  ? 0.40280 0.30870 0.43250 0.01170  0.01370  0.03860  46  LEU B CG    
4337 C  CD1   . LEU B 50  ? 0.34630 0.25300 0.36770 0.00890  0.01530  0.03120  46  LEU B CD1   
4338 C  CD2   . LEU B 50  ? 0.33340 0.23120 0.36730 0.01010  0.01400  0.04140  46  LEU B CD2   
4339 N  N     . THR B 51  ? 0.32040 0.24750 0.34270 0.01480  0.00950  0.03890  47  THR B N     
4340 C  CA    . THR B 51  ? 0.31510 0.24940 0.33220 0.01380  0.00570  0.04310  47  THR B CA    
4341 C  C     . THR B 51  ? 0.39200 0.32620 0.40150 0.01040  0.00500  0.04370  47  THR B C     
4342 O  O     . THR B 51  ? 0.34630 0.27520 0.35500 0.00840  0.00720  0.04100  47  THR B O     
4343 C  CB    . THR B 51  ? 0.38090 0.32160 0.39420 0.01400  0.00470  0.04010  47  THR B CB    
4344 O  OG1   . THR B 51  ? 0.36940 0.30950 0.37610 0.01180  0.00660  0.03420  47  THR B OG1   
4345 C  CG2   . THR B 51  ? 0.31410 0.25560 0.33580 0.01730  0.00580  0.03950  47  THR B CG2   
4346 N  N     . LYS B 52  ? 0.36930 0.30980 0.37360 0.00950  0.00200  0.04730  48  LYS B N     
4347 C  CA    . LYS B 52  ? 0.34000 0.28180 0.33750 0.00660  0.00170  0.04830  48  LYS B CA    
4348 C  C     . LYS B 52  ? 0.37510 0.31970 0.36520 0.00490  0.00240  0.04270  48  LYS B C     
4349 O  O     . LYS B 52  ? 0.31010 0.25440 0.29610 0.00240  0.00330  0.04190  48  LYS B O     
4350 C  CB    . LYS B 52  ? 0.37230 0.31970 0.36720 0.00650  -0.00150 0.05490  48  LYS B CB    
4351 C  CG    . LYS B 52  ? 0.35230 0.29740 0.35500 0.00800  -0.00270 0.06190  48  LYS B CG    
4352 C  CD    . LYS B 52  ? 0.29870 0.23640 0.30560 0.00670  -0.00050 0.06310  48  LYS B CD    
4353 C  CE    . LYS B 52  ? 0.40300 0.33330 0.42030 0.00920  0.00110  0.06280  48  LYS B CE    
4354 N  NZ    . LYS B 52  ? 0.45420 0.38680 0.47840 0.01220  -0.00140 0.06920  48  LYS B NZ    
4355 N  N     . HIS B 53  ? 0.34180 0.28910 0.33100 0.00610  0.00210  0.03920  49  HIS B N     
4356 C  CA    . HIS B 53  ? 0.30650 0.25650 0.28960 0.00480  0.00240  0.03460  49  HIS B CA    
4357 C  C     . HIS B 53  ? 0.32120 0.27070 0.30700 0.00610  0.00350  0.03060  49  HIS B C     
4358 O  O     . HIS B 53  ? 0.31720 0.26770 0.30790 0.00820  0.00260  0.03220  49  HIS B O     
4359 C  CB    . HIS B 53  ? 0.31530 0.27160 0.29250 0.00460  -0.00020 0.03610  49  HIS B CB    
4360 C  CG    . HIS B 53  ? 0.36690 0.32550 0.33810 0.00330  0.00020  0.03200  49  HIS B CG    
4361 N  ND1   . HIS B 53  ? 0.42190 0.38050 0.39290 0.00350  0.00070  0.02770  49  HIS B ND1   
4362 C  CD2   . HIS B 53  ? 0.40870 0.37000 0.37440 0.00200  0.00030  0.03200  49  HIS B CD2   
4363 C  CE1   . HIS B 53  ? 0.41300 0.37370 0.37890 0.00250  0.00080  0.02540  49  HIS B CE1   
4364 N  NE2   . HIS B 53  ? 0.38920 0.35170 0.35200 0.00170  0.00070  0.02770  49  HIS B NE2   
4365 N  N     . GLU B 54  ? 0.31350 0.26210 0.29640 0.00470  0.00520  0.02590  50  GLU B N     
4366 C  CA    . GLU B 54  ? 0.27500 0.22370 0.26040 0.00570  0.00650  0.02250  50  GLU B CA    
4367 C  C     . GLU B 54  ? 0.28930 0.24300 0.27440 0.00670  0.00410  0.02320  50  GLU B C     
4368 O  O     . GLU B 54  ? 0.31390 0.26860 0.30350 0.00820  0.00460  0.02260  50  GLU B O     
4369 C  CB    . GLU B 54  ? 0.31080 0.25850 0.29250 0.00360  0.00850  0.01790  50  GLU B CB    
4370 C  CG    . GLU B 54  ? 0.29100 0.23310 0.27380 0.00240  0.01100  0.01600  50  GLU B CG    
4371 C  CD    . GLU B 54  ? 0.39920 0.34040 0.37870 0.00010  0.01030  0.01750  50  GLU B CD    
4372 O  OE1   . GLU B 54  ? 0.38780 0.32490 0.36730 -0.00190 0.01190  0.01550  50  GLU B OE1   
4373 O  OE2   . GLU B 54  ? 0.38850 0.33350 0.36550 0.00010  0.00820  0.02060  50  GLU B OE2   
4374 N  N     . GLU B 55  ? 0.31730 0.27440 0.29750 0.00600  0.00170  0.02450  51  GLU B N     
4375 C  CA    . GLU B 55  ? 0.29390 0.25530 0.27390 0.00670  -0.00100 0.02500  51  GLU B CA    
4376 C  C     . GLU B 55  ? 0.32420 0.28680 0.31010 0.00850  -0.00260 0.02880  51  GLU B C     
4377 O  O     . GLU B 55  ? 0.28710 0.25220 0.27650 0.00930  -0.00370 0.02870  51  GLU B O     
4378 C  CB    . GLU B 55  ? 0.27780 0.24200 0.25110 0.00580  -0.00320 0.02540  51  GLU B CB    
4379 C  CG    . GLU B 55  ? 0.38590 0.35360 0.35820 0.00590  -0.00610 0.02470  51  GLU B CG    
4380 C  CD    . GLU B 55  ? 0.48090 0.45120 0.44670 0.00540  -0.00830 0.02490  51  GLU B CD    
4381 O  OE1   . GLU B 55  ? 0.48010 0.45240 0.44410 0.00510  -0.01060 0.02330  51  GLU B OE1   
4382 O  OE2   . GLU B 55  ? 0.48800 0.45850 0.45060 0.00500  -0.00770 0.02660  51  GLU B OE2   
4383 N  N     . GLY B 56  ? 0.34380 0.30510 0.33120 0.00910  -0.00290 0.03260  52  GLY B N     
4384 C  CA    . GLY B 56  ? 0.29200 0.25460 0.28610 0.01100  -0.00450 0.03700  52  GLY B CA    
4385 C  C     . GLY B 56  ? 0.36850 0.32870 0.37070 0.01290  -0.00180 0.03570  52  GLY B C     
4386 O  O     . GLY B 56  ? 0.35680 0.31990 0.36530 0.01460  -0.00300 0.03790  52  GLY B O     
4387 N  N     . ALA B 57  ? 0.28800 0.24330 0.29010 0.01240  0.00190  0.03200  53  ALA B N     
4388 C  CA    . ALA B 57  ? 0.32980 0.28290 0.33860 0.01420  0.00500  0.02980  53  ALA B CA    
4389 C  C     . ALA B 57  ? 0.28430 0.24210 0.29410 0.01450  0.00480  0.02780  53  ALA B C     
4390 O  O     . ALA B 57  ? 0.32600 0.28570 0.34330 0.01660  0.00550  0.02880  53  ALA B O     
4391 C  CB    . ALA B 57  ? 0.28990 0.23720 0.29670 0.01310  0.00880  0.02540  53  ALA B CB    
4392 N  N     . ALA B 58  ? 0.35180 0.31180 0.35470 0.01220  0.00370  0.02540  54  ALA B N     
4393 C  CA    . ALA B 58  ? 0.31790 0.28220 0.32180 0.01200  0.00310  0.02400  54  ALA B CA    
4394 C  C     . ALA B 58  ? 0.31100 0.28030 0.31870 0.01280  -0.00070 0.02770  54  ALA B C     
4395 O  O     . ALA B 58  ? 0.28130 0.25400 0.29480 0.01360  -0.00060 0.02810  54  ALA B O     
4396 C  CB    . ALA B 58  ? 0.29250 0.25710 0.28860 0.00950  0.00250  0.02100  54  ALA B CB    
4397 N  N     . PHE B 59  ? 0.29300 0.26330 0.29720 0.01220  -0.00420 0.03050  55  PHE B N     
4398 C  CA    . PHE B 59  ? 0.30880 0.28410 0.31630 0.01270  -0.00820 0.03430  55  PHE B CA    
4399 C  C     . PHE B 59  ? 0.28720 0.26350 0.30490 0.01540  -0.00750 0.03780  55  PHE B C     
4400 O  O     . PHE B 59  ? 0.31550 0.29670 0.33930 0.01610  -0.00940 0.03980  55  PHE B O     
4401 C  CB    . PHE B 59  ? 0.24880 0.22510 0.25030 0.01180  -0.01170 0.03690  55  PHE B CB    
4402 C  CG    . PHE B 59  ? 0.32660 0.30340 0.31900 0.00950  -0.01320 0.03380  55  PHE B CG    
4403 C  CD1   . PHE B 59  ? 0.39330 0.37160 0.38500 0.00840  -0.01410 0.03070  55  PHE B CD1   
4404 C  CD2   . PHE B 59  ? 0.32030 0.29610 0.30550 0.00870  -0.01360 0.03410  55  PHE B CD2   
4405 C  CE1   . PHE B 59  ? 0.40930 0.38730 0.39340 0.00660  -0.01540 0.02770  55  PHE B CE1   
4406 C  CE2   . PHE B 59  ? 0.34480 0.32110 0.32210 0.00710  -0.01460 0.03090  55  PHE B CE2   
4407 C  CZ    . PHE B 59  ? 0.35160 0.32860 0.32860 0.00620  -0.01550 0.02750  55  PHE B CZ    
4408 N  N     . MET B 60  ? 0.25710 0.22900 0.27770 0.01700  -0.00480 0.03880  56  MET B N     
4409 C  CA    . MET B 60  ? 0.28720 0.25940 0.31840 0.02010  -0.00390 0.04230  56  MET B CA    
4410 C  C     . MET B 60  ? 0.29040 0.26410 0.32840 0.02170  -0.00060 0.03970  56  MET B C     
4411 O  O     . MET B 60  ? 0.29310 0.27140 0.34010 0.02370  -0.00150 0.04270  56  MET B O     
4412 C  CB    . MET B 60  ? 0.31390 0.27960 0.34690 0.02140  -0.00140 0.04320  56  MET B CB    
4413 C  CG    . MET B 60  ? 0.36920 0.33490 0.39900 0.02070  -0.00470 0.04820  56  MET B CG    
4414 S  SD    . MET B 60  ? 0.46030 0.41800 0.49370 0.02190  -0.00220 0.05030  56  MET B SD    
4415 C  CE    . MET B 60  ? 0.44820 0.40730 0.47100 0.01870  -0.00550 0.05330  56  MET B CE    
4416 N  N     . ALA B 61  ? 0.29970 0.27020 0.33370 0.02070  0.00320  0.03430  57  ALA B N     
4417 C  CA    . ALA B 61  ? 0.26220 0.23500 0.30130 0.02170  0.00660  0.03160  57  ALA B CA    
4418 C  C     . ALA B 61  ? 0.27420 0.25440 0.31530 0.02060  0.00350  0.03320  57  ALA B C     
4419 O  O     . ALA B 61  ? 0.35910 0.34380 0.40890 0.02240  0.00480  0.03440  57  ALA B O     
4420 C  CB    . ALA B 61  ? 0.24280 0.21180 0.27500 0.01990  0.01040  0.02580  57  ALA B CB    
4421 N  N     . GLU B 62  ? 0.27980 0.26120 0.31330 0.01780  -0.00050 0.03330  58  GLU B N     
4422 C  CA    . GLU B 62  ? 0.30420 0.29160 0.33900 0.01620  -0.00390 0.03440  58  GLU B CA    
4423 C  C     . GLU B 62  ? 0.30280 0.29550 0.34600 0.01770  -0.00740 0.03970  58  GLU B C     
4424 O  O     . GLU B 62  ? 0.38820 0.38670 0.43880 0.01790  -0.00800 0.04130  58  GLU B O     
4425 C  CB    . GLU B 62  ? 0.31270 0.29910 0.33750 0.01310  -0.00740 0.03290  58  GLU B CB    
4426 C  CG    . GLU B 62  ? 0.39910 0.38950 0.42370 0.01070  -0.00990 0.03200  58  GLU B CG    
4427 C  CD    . GLU B 62  ? 0.54770 0.54350 0.57630 0.01010  -0.01520 0.03570  58  GLU B CD    
4428 O  OE1   . GLU B 62  ? 0.49420 0.49080 0.52330 0.01110  -0.01760 0.03890  58  GLU B OE1   
4429 O  OE2   . GLU B 62  ? 0.47260 0.47210 0.50380 0.00830  -0.01710 0.03560  58  GLU B OE2   
4430 N  N     . GLY B 63  ? 0.32690 0.31830 0.36940 0.01860  -0.00970 0.04310  59  GLY B N     
4431 C  CA    . GLY B 63  ? 0.29610 0.29290 0.34670 0.02010  -0.01320 0.04880  59  GLY B CA    
4432 C  C     . GLY B 63  ? 0.28770 0.28600 0.35100 0.02390  -0.00970 0.05070  59  GLY B C     
4433 O  O     . GLY B 63  ? 0.30370 0.30880 0.37610 0.02480  -0.01160 0.05430  59  GLY B O     
4434 N  N     . TYR B 64  ? 0.32070 0.31270 0.38490 0.02600  -0.00440 0.04820  60  TYR B N     
4435 C  CA    . TYR B 64  ? 0.29390 0.28670 0.37000 0.02990  -0.00010 0.04880  60  TYR B CA    
4436 C  C     . TYR B 64  ? 0.32030 0.31920 0.40100 0.02960  0.00170  0.04700  60  TYR B C     
4437 O  O     . TYR B 64  ? 0.30740 0.31240 0.39960 0.03200  0.00190  0.05030  60  TYR B O     
4438 C  CB    . TYR B 64  ? 0.24350 0.22780 0.31820 0.03170  0.00550  0.04480  60  TYR B CB    
4439 C  CG    . TYR B 64  ? 0.30800 0.29240 0.39470 0.03600  0.01050  0.04440  60  TYR B CG    
4440 C  CD1   . TYR B 64  ? 0.34940 0.33590 0.43780 0.03640  0.01530  0.03990  60  TYR B CD1   
4441 C  CD2   . TYR B 64  ? 0.32180 0.30460 0.41850 0.03980  0.01060  0.04880  60  TYR B CD2   
4442 C  CE1   . TYR B 64  ? 0.35920 0.34640 0.45860 0.04060  0.02050  0.03910  60  TYR B CE1   
4443 C  CE2   . TYR B 64  ? 0.38590 0.36860 0.49430 0.04430  0.01560  0.04810  60  TYR B CE2   
4444 C  CZ    . TYR B 64  ? 0.47680 0.46180 0.58630 0.04480  0.02070  0.04290  60  TYR B CZ    
4445 O  OH    . TYR B 64  ? 0.61240 0.59770 0.73350 0.04950  0.02630  0.04180  60  TYR B OH    
4446 N  N     . ALA B 65  ? 0.25860 0.25650 0.33080 0.02660  0.00300  0.04230  61  ALA B N     
4447 C  CA    . ALA B 65  ? 0.32580 0.32950 0.40200 0.02590  0.00490  0.04090  61  ALA B CA    
4448 C  C     . ALA B 65  ? 0.34690 0.35900 0.42900 0.02460  -0.00030 0.04550  61  ALA B C     
4449 O  O     . ALA B 65  ? 0.35500 0.37380 0.44750 0.02610  0.00110  0.04750  61  ALA B O     
4450 C  CB    . ALA B 65  ? 0.22880 0.22960 0.29420 0.02250  0.00630  0.03590  61  ALA B CB    
4451 N  N     . ARG B 66  ? 0.26350 0.27560 0.33900 0.02170  -0.00640 0.04700  62  ARG B N     
4452 C  CA    . ARG B 66  ? 0.27640 0.29630 0.35640 0.01970  -0.01180 0.05070  62  ARG B CA    
4453 C  C     . ARG B 66  ? 0.33140 0.35740 0.42420 0.02280  -0.01330 0.05660  62  ARG B C     
4454 O  O     . ARG B 66  ? 0.36100 0.39500 0.46320 0.02260  -0.01440 0.05930  62  ARG B O     
4455 C  CB    . ARG B 66  ? 0.32640 0.34460 0.39610 0.01620  -0.01780 0.05050  62  ARG B CB    
4456 C  CG    . ARG B 66  ? 0.45440 0.46950 0.51470 0.01260  -0.01780 0.04570  62  ARG B CG    
4457 C  CD    . ARG B 66  ? 0.44740 0.46220 0.49960 0.00930  -0.02400 0.04550  62  ARG B CD    
4458 N  NE    . ARG B 66  ? 0.34430 0.36650 0.40300 0.00770  -0.02920 0.04920  62  ARG B NE    
4459 C  CZ    . ARG B 66  ? 0.40100 0.42430 0.45420 0.00450  -0.03520 0.04910  62  ARG B CZ    
4460 N  NH1   . ARG B 66  ? 0.31910 0.33670 0.36040 0.00290  -0.03610 0.04530  62  ARG B NH1   
4461 N  NH2   . ARG B 66  ? 0.40230 0.43270 0.46200 0.00280  -0.04020 0.05260  62  ARG B NH2   
4462 N  N     . VAL B 67  ? 0.33070 0.35340 0.42480 0.02560  -0.01330 0.05900  63  VAL B N     
4463 C  CA    . VAL B 67  ? 0.30050 0.32900 0.40740 0.02870  -0.01510 0.06540  63  VAL B CA    
4464 C  C     . VAL B 67  ? 0.30680 0.33740 0.42620 0.03300  -0.00870 0.06510  63  VAL B C     
4465 O  O     . VAL B 67  ? 0.30000 0.33890 0.43200 0.03470  -0.00970 0.06950  63  VAL B O     
4466 C  CB    . VAL B 67  ? 0.29980 0.32410 0.40460 0.03030  -0.01720 0.06880  63  VAL B CB    
4467 C  CG1   . VAL B 67  ? 0.29840 0.32800 0.41800 0.03430  -0.01830 0.07580  63  VAL B CG1   
4468 C  CG2   . VAL B 67  ? 0.31280 0.33750 0.40620 0.02610  -0.02380 0.06980  63  VAL B CG2   
4469 N  N     . SER B 68  ? 0.28210 0.30560 0.39840 0.03470  -0.00210 0.05990  64  SER B N     
4470 C  CA    . SER B 68  ? 0.34090 0.36590 0.46840 0.03910  0.00450  0.05890  64  SER B CA    
4471 C  C     . SER B 68  ? 0.36640 0.39850 0.49760 0.03790  0.00710  0.05710  64  SER B C     
4472 O  O     . SER B 68  ? 0.35310 0.38980 0.49590 0.04150  0.01190  0.05750  64  SER B O     
4473 C  CB    . SER B 68  ? 0.37740 0.39230 0.49990 0.04110  0.01070  0.05330  64  SER B CB    
4474 O  OG    . SER B 68  ? 0.40860 0.42010 0.51900 0.03750  0.01280  0.04720  64  SER B OG    
4475 N  N     . GLY B 69  ? 0.31920 0.35210 0.44100 0.03300  0.00460  0.05480  65  GLY B N     
4476 C  CA    . GLY B 69  ? 0.35380 0.39210 0.47760 0.03150  0.00780  0.05280  65  GLY B CA    
4477 C  C     . GLY B 69  ? 0.39900 0.43250 0.51870 0.03280  0.01560  0.04680  65  GLY B C     
4478 O  O     . GLY B 69  ? 0.46210 0.50080 0.58460 0.03230  0.01940  0.04540  65  GLY B O     
4479 N  N     . LYS B 70  ? 0.35180 0.37590 0.46470 0.03420  0.01790  0.04330  66  LYS B N     
4480 C  CA    . LYS B 70  ? 0.32150 0.34050 0.43010 0.03540  0.02500  0.03730  66  LYS B CA    
4481 C  C     . LYS B 70  ? 0.36820 0.37960 0.46140 0.03160  0.02390  0.03310  66  LYS B C     
4482 O  O     . LYS B 70  ? 0.37990 0.39010 0.46640 0.02850  0.01810  0.03470  66  LYS B O     
4483 C  CB    . LYS B 70  ? 0.33760 0.35190 0.45320 0.04070  0.02920  0.03650  66  LYS B CB    
4484 C  CG    . LYS B 70  ? 0.45170 0.47370 0.58390 0.04510  0.03050  0.04110  66  LYS B CG    
4485 C  CD    . LYS B 70  ? 0.52050 0.53760 0.66030 0.05070  0.03670  0.03870  66  LYS B CD    
4486 C  CE    . LYS B 70  ? 0.65180 0.65800 0.78650 0.05130  0.03470  0.03840  66  LYS B CE    
4487 N  NZ    . LYS B 70  ? 0.74950 0.75180 0.89590 0.05720  0.03860  0.03900  66  LYS B NZ    
4488 N  N     . LEU B 71  ? 0.32320 0.32990 0.41100 0.03200  0.02950  0.02750  67  LEU B N     
4489 C  CA    . LEU B 71  ? 0.34200 0.34200 0.41610 0.02850  0.02890  0.02360  67  LEU B CA    
4490 C  C     . LEU B 71  ? 0.32560 0.31750 0.39600 0.02920  0.02660  0.02380  67  LEU B C     
4491 O  O     . LEU B 71  ? 0.36150 0.34970 0.43780 0.03280  0.02900  0.02370  67  LEU B O     
4492 C  CB    . LEU B 71  ? 0.33910 0.33740 0.40870 0.02840  0.03550  0.01770  67  LEU B CB    
4493 C  CG    . LEU B 71  ? 0.39240 0.38420 0.44850 0.02500  0.03530  0.01360  67  LEU B CG    
4494 C  CD1   . LEU B 71  ? 0.33670 0.33250 0.38670 0.02070  0.03180  0.01490  67  LEU B CD1   
4495 C  CD2   . LEU B 71  ? 0.39720 0.38620 0.45000 0.02560  0.04190  0.00760  67  LEU B CD2   
4496 N  N     . GLY B 72  ? 0.35360 0.34280 0.41470 0.02590  0.02190  0.02420  68  GLY B N     
4497 C  CA    . GLY B 72  ? 0.35680 0.33850 0.41290 0.02590  0.02030  0.02410  68  GLY B CA    
4498 C  C     . GLY B 72  ? 0.35100 0.32650 0.39730 0.02380  0.02330  0.01860  68  GLY B C     
4499 O  O     . GLY B 72  ? 0.34130 0.31880 0.38180 0.02130  0.02430  0.01590  68  GLY B O     
4500 N  N     . VAL B 73  ? 0.30740 0.27570 0.35220 0.02480  0.02460  0.01710  69  VAL B N     
4501 C  CA    . VAL B 73  ? 0.31950 0.28220 0.35580 0.02270  0.02740  0.01180  69  VAL B CA    
4502 C  C     . VAL B 73  ? 0.33170 0.28830 0.36290 0.02130  0.02460  0.01280  69  VAL B C     
4503 O  O     . VAL B 73  ? 0.28140 0.23480 0.31780 0.02340  0.02370  0.01570  69  VAL B O     
4504 C  CB    . VAL B 73  ? 0.31700 0.27620 0.35690 0.02500  0.03350  0.00730  69  VAL B CB    
4505 C  CG1   . VAL B 73  ? 0.26750 0.22120 0.29760 0.02200  0.03570  0.00170  69  VAL B CG1   
4506 C  CG2   . VAL B 73  ? 0.26930 0.23570 0.31470 0.02650  0.03680  0.00660  69  VAL B CG2   
4507 N  N     . CYS B 74  ? 0.36820 0.32370 0.38970 0.01780  0.02320  0.01090  70  CYS B N     
4508 C  CA    . CYS B 74  ? 0.26950 0.21970 0.28590 0.01620  0.02150  0.01120  70  CYS B CA    
4509 C  C     . CYS B 74  ? 0.32480 0.27130 0.33390 0.01350  0.02400  0.00600  70  CYS B C     
4510 O  O     . CYS B 74  ? 0.32090 0.27010 0.32700 0.01230  0.02610  0.00280  70  CYS B O     
4511 C  CB    . CYS B 74  ? 0.29370 0.24690 0.30590 0.01460  0.01660  0.01480  70  CYS B CB    
4512 S  SG    . CYS B 74  ? 0.40590 0.36500 0.41290 0.01230  0.01490  0.01380  70  CYS B SG    
4513 N  N     . CYS B 75  ? 0.30830 0.24880 0.31500 0.01240  0.02400  0.00530  71  CYS B N     
4514 C  CA    . CYS B 75  ? 0.33000 0.26740 0.32970 0.00930  0.02560  0.00070  71  CYS B CA    
4515 C  C     . CYS B 75  ? 0.35150 0.28730 0.34600 0.00660  0.02260  0.00260  71  CYS B C     
4516 O  O     . CYS B 75  ? 0.36260 0.29710 0.35970 0.00750  0.02040  0.00670  71  CYS B O     
4517 C  CB    . CYS B 75  ? 0.33960 0.27040 0.34170 0.01000  0.02980  -0.00370 71  CYS B CB    
4518 S  SG    . CYS B 75  ? 0.39690 0.32050 0.40620 0.01210  0.02920  -0.00050 71  CYS B SG    
4519 N  N     . ALA B 76  ? 0.30880 0.24580 0.29630 0.00340  0.02240  0.00000  72  ALA B N     
4520 C  CA    . ALA B 76  ? 0.32300 0.25930 0.30570 0.00080  0.02000  0.00130  72  ALA B CA    
4521 C  C     . ALA B 76  ? 0.40660 0.34120 0.38400 -0.00260 0.02140  -0.00300 72  ALA B C     
4522 O  O     . ALA B 76  ? 0.42470 0.36060 0.39980 -0.00340 0.02340  -0.00670 72  ALA B O     
4523 C  CB    . ALA B 76  ? 0.28260 0.22480 0.26230 0.00050  0.01690  0.00420  72  ALA B CB    
4524 N  N     . THR B 77  ? 0.39980 0.33200 0.37500 -0.00500 0.02010  -0.00220 73  THR B N     
4525 C  CA    . THR B 77  ? 0.28540 0.21630 0.25570 -0.00880 0.02070  -0.00590 73  THR B CA    
4526 C  C     . THR B 77  ? 0.36070 0.29810 0.32570 -0.01070 0.01880  -0.00550 73  THR B C     
4527 O  O     . THR B 77  ? 0.33040 0.27250 0.29560 -0.00910 0.01730  -0.00270 73  THR B O     
4528 C  CB    . THR B 77  ? 0.34960 0.27560 0.32080 -0.01090 0.02000  -0.00490 73  THR B CB    
4529 O  OG1   . THR B 77  ? 0.41360 0.33730 0.38100 -0.01460 0.02080  -0.00930 73  THR B OG1   
4530 C  CG2   . THR B 77  ? 0.35220 0.28250 0.32220 -0.01170 0.01700  -0.00010 73  THR B CG2   
4531 N  N     . THR B 78  ? 0.30150 0.23910 0.26210 -0.01440 0.01880  -0.00820 74  THR B N     
4532 C  CA    . THR B 78  ? 0.36340 0.30700 0.31960 -0.01640 0.01690  -0.00740 74  THR B CA    
4533 C  C     . THR B 78  ? 0.35340 0.30040 0.31070 -0.01540 0.01440  -0.00280 74  THR B C     
4534 O  O     . THR B 78  ? 0.34530 0.29000 0.30530 -0.01440 0.01400  -0.00050 74  THR B O     
4535 C  CB    . THR B 78  ? 0.36420 0.30730 0.31640 -0.02090 0.01660  -0.01000 74  THR B CB    
4536 O  OG1   . THR B 78  ? 0.44720 0.38480 0.40170 -0.02200 0.01670  -0.01010 74  THR B OG1   
4537 C  CG2   . THR B 78  ? 0.37550 0.31770 0.32420 -0.02240 0.01880  -0.01500 74  THR B CG2   
4538 N  N     . GLY B 79  ? 0.29610 0.24860 0.25120 -0.01570 0.01280  -0.00150 75  GLY B N     
4539 C  CA    . GLY B 79  ? 0.28420 0.24020 0.23950 -0.01520 0.01070  0.00180  75  GLY B CA    
4540 C  C     . GLY B 79  ? 0.31480 0.27030 0.27280 -0.01200 0.01020  0.00440  75  GLY B C     
4541 O  O     . GLY B 79  ? 0.30790 0.26430 0.26700 -0.00970 0.01000  0.00480  75  GLY B O     
4542 N  N     . PRO B 80  ? 0.30690 0.26160 0.26580 -0.01220 0.00980  0.00660  76  PRO B N     
4543 C  CA    . PRO B 80  ? 0.33330 0.28890 0.29350 -0.00960 0.00890  0.00950  76  PRO B CA    
4544 C  C     . PRO B 80  ? 0.36260 0.31460 0.32580 -0.00750 0.00950  0.00990  76  PRO B C     
4545 O  O     . PRO B 80  ? 0.38300 0.33660 0.34700 -0.00530 0.00840  0.01200  76  PRO B O     
4546 C  CB    . PRO B 80  ? 0.28350 0.23990 0.24370 -0.01100 0.00870  0.01180  76  PRO B CB    
4547 C  CG    . PRO B 80  ? 0.37000 0.32240 0.33090 -0.01400 0.00970  0.01010  76  PRO B CG    
4548 C  CD    . PRO B 80  ? 0.30360 0.25640 0.26250 -0.01520 0.01010  0.00650  76  PRO B CD    
4549 N  N     . GLY B 81  ? 0.32430 0.27180 0.28950 -0.00820 0.01120  0.00800  77  GLY B N     
4550 C  CA    . GLY B 81  ? 0.33230 0.27690 0.30140 -0.00570 0.01210  0.00830  77  GLY B CA    
4551 C  C     . GLY B 81  ? 0.34320 0.29100 0.31270 -0.00380 0.01180  0.00770  77  GLY B C     
4552 O  O     . GLY B 81  ? 0.34000 0.28920 0.31180 -0.00150 0.01060  0.01000  77  GLY B O     
4553 N  N     . ALA B 82  ? 0.31730 0.26670 0.28450 -0.00500 0.01260  0.00490  78  ALA B N     
4554 C  CA    . ALA B 82  ? 0.36680 0.31930 0.33470 -0.00370 0.01230  0.00460  78  ALA B CA    
4555 C  C     . ALA B 82  ? 0.35970 0.31600 0.32650 -0.00300 0.00960  0.00690  78  ALA B C     
4556 O  O     . ALA B 82  ? 0.34320 0.30100 0.31230 -0.00120 0.00860  0.00810  78  ALA B O     
4557 C  CB    . ALA B 82  ? 0.32040 0.27440 0.28570 -0.00560 0.01380  0.00170  78  ALA B CB    
4558 N  N     . THR B 83  ? 0.31090 0.26860 0.27450 -0.00420 0.00850  0.00750  79  THR B N     
4559 C  CA    . THR B 83  ? 0.32510 0.28580 0.28770 -0.00320 0.00630  0.00890  79  THR B CA    
4560 C  C     . THR B 83  ? 0.30780 0.26820 0.27160 -0.00130 0.00510  0.01100  79  THR B C     
4561 O  O     . THR B 83  ? 0.28840 0.25070 0.25220 -0.00020 0.00330  0.01150  79  THR B O     
4562 C  CB    . THR B 83  ? 0.38420 0.34700 0.34400 -0.00440 0.00570  0.00900  79  THR B CB    
4563 O  OG1   . THR B 83  ? 0.32960 0.29150 0.28880 -0.00510 0.00620  0.01010  79  THR B OG1   
4564 C  CG2   . THR B 83  ? 0.37960 0.34360 0.33810 -0.00650 0.00620  0.00760  79  THR B CG2   
4565 N  N     . ASN B 84  ? 0.28200 0.24010 0.24690 -0.00120 0.00580  0.01240  80  ASN B N     
4566 C  CA    . ASN B 84  ? 0.26110 0.21960 0.22720 0.00030  0.00440  0.01520  80  ASN B CA    
4567 C  C     . ASN B 84  ? 0.36320 0.32210 0.33300 0.00210  0.00360  0.01570  80  ASN B C     
4568 O  O     . ASN B 84  ? 0.32950 0.29010 0.29960 0.00320  0.00160  0.01790  80  ASN B O     
4569 C  CB    . ASN B 84  ? 0.26360 0.21920 0.23130 -0.00010 0.00540  0.01730  80  ASN B CB    
4570 C  CG    . ASN B 84  ? 0.34400 0.30130 0.30840 -0.00120 0.00500  0.01900  80  ASN B CG    
4571 O  OD1   . ASN B 84  ? 0.34790 0.30850 0.30890 -0.00130 0.00430  0.01830  80  ASN B OD1   
4572 N  ND2   . ASN B 84  ? 0.36050 0.31550 0.32650 -0.00190 0.00570  0.02140  80  ASN B ND2   
4573 N  N     . ALA B 85  ? 0.34040 0.29830 0.31290 0.00210  0.00520  0.01380  81  ALA B N     
4574 C  CA    . ALA B 85  ? 0.29320 0.25240 0.27030 0.00370  0.00470  0.01450  81  ALA B CA    
4575 C  C     . ALA B 85  ? 0.38750 0.35000 0.36380 0.00360  0.00270  0.01420  81  ALA B C     
4576 O  O     . ALA B 85  ? 0.36830 0.33270 0.34850 0.00460  0.00160  0.01530  81  ALA B O     
4577 C  CB    . ALA B 85  ? 0.24930 0.20670 0.22980 0.00390  0.00780  0.01250  81  ALA B CB    
4578 N  N     . LEU B 86  ? 0.31460 0.27790 0.28660 0.00230  0.00210  0.01280  82  LEU B N     
4579 C  CA    . LEU B 86  ? 0.36310 0.32840 0.33530 0.00190  0.00080  0.01200  82  LEU B CA    
4580 C  C     . LEU B 86  ? 0.32920 0.29630 0.30300 0.00270  -0.00220 0.01330  82  LEU B C     
4581 O  O     . LEU B 86  ? 0.26790 0.23660 0.24510 0.00250  -0.00300 0.01350  82  LEU B O     
4582 C  CB    . LEU B 86  ? 0.38360 0.34910 0.35180 0.00080  0.00040  0.01070  82  LEU B CB    
4583 C  CG    . LEU B 86  ? 0.47360 0.44060 0.44320 0.00020  -0.00070 0.01020  82  LEU B CG    
4584 C  CD1   . LEU B 86  ? 0.44300 0.41040 0.41150 -0.00130 0.00080  0.00940  82  LEU B CD1   
4585 C  CD2   . LEU B 86  ? 0.54210 0.50920 0.51010 0.00060  -0.00350 0.01000  82  LEU B CD2   
4586 N  N     . THR B 87  ? 0.26790 0.23510 0.23890 0.00320  -0.00400 0.01420  83  THR B N     
4587 C  CA    . THR B 87  ? 0.28890 0.25810 0.26040 0.00350  -0.00730 0.01500  83  THR B CA    
4588 C  C     . THR B 87  ? 0.28420 0.25500 0.26180 0.00410  -0.00780 0.01710  83  THR B C     
4589 O  O     . THR B 87  ? 0.31750 0.29030 0.29770 0.00370  -0.01000 0.01730  83  THR B O     
4590 C  CB    . THR B 87  ? 0.31940 0.28910 0.28630 0.00380  -0.00870 0.01590  83  THR B CB    
4591 O  OG1   . THR B 87  ? 0.33020 0.29920 0.29220 0.00350  -0.00800 0.01380  83  THR B OG1   
4592 C  CG2   . THR B 87  ? 0.26690 0.23900 0.23340 0.00380  -0.01250 0.01660  83  THR B CG2   
4593 N  N     . GLY B 88  ? 0.32840 0.29830 0.30900 0.00520  -0.00580 0.01870  84  GLY B N     
4594 C  CA    . GLY B 88  ? 0.23030 0.20200 0.21790 0.00640  -0.00590 0.02080  84  GLY B CA    
4595 C  C     . GLY B 88  ? 0.30360 0.27670 0.29540 0.00600  -0.00430 0.01950  84  GLY B C     
4596 O  O     . GLY B 88  ? 0.30840 0.28480 0.30540 0.00630  -0.00570 0.02100  84  GLY B O     
4597 N  N     . ILE B 89  ? 0.32240 0.29370 0.31190 0.00520  -0.00140 0.01700  85  ILE B N     
4598 C  CA    . ILE B 89  ? 0.31090 0.28420 0.30330 0.00450  0.00010  0.01610  85  ILE B CA    
4599 C  C     . ILE B 89  ? 0.32980 0.30510 0.32180 0.00300  -0.00310 0.01630  85  ILE B C     
4600 O  O     . ILE B 89  ? 0.30500 0.28340 0.30200 0.00260  -0.00360 0.01740  85  ILE B O     
4601 C  CB    . ILE B 89  ? 0.32360 0.29490 0.31260 0.00350  0.00340  0.01360  85  ILE B CB    
4602 C  CG1   . ILE B 89  ? 0.28650 0.25480 0.27580 0.00470  0.00620  0.01290  85  ILE B CG1   
4603 C  CG2   . ILE B 89  ? 0.30950 0.28370 0.30090 0.00260  0.00510  0.01310  85  ILE B CG2   
4604 C  CD1   . ILE B 89  ? 0.29510 0.26430 0.29140 0.00680  0.00760  0.01430  85  ILE B CD1   
4605 N  N     . ALA B 90  ? 0.31690 0.29050 0.30350 0.00230  -0.00540 0.01540  86  ALA B N     
4606 C  CA    . ALA B 90  ? 0.27280 0.24720 0.25930 0.00090  -0.00850 0.01510  86  ALA B CA    
4607 C  C     . ALA B 90  ? 0.33270 0.30980 0.32310 0.00090  -0.01170 0.01680  86  ALA B C     
4608 O  O     . ALA B 90  ? 0.27460 0.25330 0.26810 -0.00050 -0.01380 0.01710  86  ALA B O     
4609 C  CB    . ALA B 90  ? 0.28460 0.25640 0.26480 0.00060  -0.00990 0.01320  86  ALA B CB    
4610 N  N     . CYS B 91  ? 0.29160 0.26950 0.28260 0.00230  -0.01240 0.01850  87  CYS B N     
4611 C  CA    . CYS B 91  ? 0.32310 0.30450 0.31830 0.00210  -0.01590 0.02070  87  CYS B CA    
4612 C  C     . CYS B 91  ? 0.33950 0.32450 0.34340 0.00250  -0.01450 0.02280  87  CYS B C     
4613 O  O     . CYS B 91  ? 0.30180 0.29020 0.31020 0.00130  -0.01730 0.02400  87  CYS B O     
4614 C  CB    . CYS B 91  ? 0.29040 0.27230 0.28410 0.00350  -0.01710 0.02280  87  CYS B CB    
4615 S  SG    . CYS B 91  ? 0.41620 0.39580 0.40000 0.00290  -0.01910 0.02090  87  CYS B SG    
4616 N  N     . ALA B 92  ? 0.31000 0.29440 0.31640 0.00410  -0.01020 0.02280  88  ALA B N     
4617 C  CA    . ALA B 92  ? 0.24660 0.23490 0.26110 0.00470  -0.00800 0.02420  88  ALA B CA    
4618 C  C     . ALA B 92  ? 0.25640 0.24640 0.27190 0.00240  -0.00820 0.02350  88  ALA B C     
4619 O  O     . ALA B 92  ? 0.31740 0.31210 0.33970 0.00180  -0.00910 0.02550  88  ALA B O     
4620 C  CB    . ALA B 92  ? 0.24980 0.23630 0.26550 0.00670  -0.00280 0.02320  88  ALA B CB    
4621 N  N     . TYR B 93  ? 0.25780 0.24440 0.26690 0.00110  -0.00760 0.02110  89  TYR B N     
4622 C  CA    . TYR B 93  ? 0.23530 0.22290 0.24510 -0.00120 -0.00790 0.02100  89  TYR B CA    
4623 C  C     . TYR B 93  ? 0.26770 0.25670 0.28000 -0.00310 -0.01280 0.02210  89  TYR B C     
4624 O  O     . TYR B 93  ? 0.31500 0.30760 0.33320 -0.00470 -0.01350 0.02380  89  TYR B O     
4625 C  CB    . TYR B 93  ? 0.26770 0.25120 0.27050 -0.00210 -0.00700 0.01870  89  TYR B CB    
4626 C  CG    . TYR B 93  ? 0.30370 0.28780 0.30720 -0.00440 -0.00750 0.01910  89  TYR B CG    
4627 C  CD1   . TYR B 93  ? 0.29230 0.27950 0.29840 -0.00510 -0.00410 0.02020  89  TYR B CD1   
4628 C  CD2   . TYR B 93  ? 0.34220 0.32350 0.34370 -0.00580 -0.01100 0.01850  89  TYR B CD2   
4629 C  CE1   . TYR B 93  ? 0.33820 0.32620 0.34510 -0.00740 -0.00470 0.02140  89  TYR B CE1   
4630 C  CE2   . TYR B 93  ? 0.33570 0.31700 0.33870 -0.00780 -0.01160 0.01930  89  TYR B CE2   
4631 C  CZ    . TYR B 93  ? 0.35820 0.34300 0.36390 -0.00880 -0.00860 0.02120  89  TYR B CZ    
4632 O  OH    . TYR B 93  ? 0.40600 0.39100 0.41330 -0.01100 -0.00940 0.02290  89  TYR B OH    
4633 N  N     . SER B 94  ? 0.28810 0.27460 0.29610 -0.00300 -0.01630 0.02110  90  SER B N     
4634 C  CA    . SER B 94  ? 0.28350 0.27070 0.29280 -0.00510 -0.02120 0.02110  90  SER B CA    
4635 C  C     . SER B 94  ? 0.32100 0.31360 0.33750 -0.00530 -0.02360 0.02420  90  SER B C     
4636 O  O     . SER B 94  ? 0.31000 0.30450 0.33000 -0.00780 -0.02740 0.02480  90  SER B O     
4637 C  CB    . SER B 94  ? 0.46060 0.44350 0.46180 -0.00510 -0.02380 0.01840  90  SER B CB    
4638 O  OG    . SER B 94  ? 0.68280 0.66760 0.68310 -0.00400 -0.02560 0.01950  90  SER B OG    
4639 N  N     . ASP B 95  ? 0.25500 0.25040 0.27480 -0.00290 -0.02160 0.02620  91  ASP B N     
4640 C  CA    . ASP B 95  ? 0.32310 0.32450 0.35110 -0.00270 -0.02370 0.02970  91  ASP B CA    
4641 C  C     . ASP B 95  ? 0.34840 0.35470 0.38550 -0.00190 -0.01980 0.03190  91  ASP B C     
4642 O  O     . ASP B 95  ? 0.34620 0.35810 0.39160 -0.00100 -0.02060 0.03520  91  ASP B O     
4643 C  CB    . ASP B 95  ? 0.31120 0.31320 0.33820 -0.00040 -0.02470 0.03130  91  ASP B CB    
4644 C  CG    . ASP B 95  ? 0.45570 0.45490 0.47430 -0.00170 -0.02910 0.02970  91  ASP B CG    
4645 O  OD1   . ASP B 95  ? 0.39060 0.38910 0.40690 -0.00450 -0.03260 0.02790  91  ASP B OD1   
4646 O  OD2   . ASP B 95  ? 0.35650 0.35430 0.37070 0.00000  -0.02890 0.03010  91  ASP B OD2   
4647 N  N     . SER B 96  ? 0.26960 0.27430 0.30530 -0.00200 -0.01560 0.03030  92  SER B N     
4648 C  CA    . SER B 96  ? 0.31620 0.32580 0.35940 -0.00130 -0.01130 0.03200  92  SER B CA    
4649 C  C     . SER B 96  ? 0.28940 0.30130 0.33770 0.00240  -0.00810 0.03320  92  SER B C     
4650 O  O     . SER B 96  ? 0.29430 0.31260 0.35220 0.00340  -0.00710 0.03600  92  SER B O     
4651 C  CB    . SER B 96  ? 0.31670 0.33230 0.36790 -0.00390 -0.01400 0.03490  92  SER B CB    
4652 O  OG    . SER B 96  ? 0.36210 0.37440 0.40900 -0.00740 -0.01730 0.03360  92  SER B OG    
4653 N  N     . THR B 97  ? 0.26690 0.27370 0.30940 0.00450  -0.00640 0.03130  93  THR B N     
4654 C  CA    . THR B 97  ? 0.27820 0.28520 0.32510 0.00810  -0.00320 0.03200  93  THR B CA    
4655 C  C     . THR B 97  ? 0.27360 0.27780 0.31780 0.00930  0.00300  0.02890  93  THR B C     
4656 O  O     . THR B 97  ? 0.32020 0.31940 0.35560 0.00800  0.00370  0.02600  93  THR B O     
4657 C  CB    . THR B 97  ? 0.30740 0.31040 0.35010 0.00930  -0.00580 0.03250  93  THR B CB    
4658 O  OG1   . THR B 97  ? 0.31660 0.32170 0.35870 0.00750  -0.01190 0.03450  93  THR B OG1   
4659 C  CG2   . THR B 97  ? 0.34580 0.34940 0.39530 0.01310  -0.00330 0.03440  93  THR B CG2   
4660 N  N     . PRO B 98  ? 0.29060 0.29790 0.34200 0.01190  0.00750  0.02920  94  PRO B N     
4661 C  CA    . PRO B 98  ? 0.26720 0.27160 0.31530 0.01290  0.01350  0.02550  94  PRO B CA    
4662 C  C     . PRO B 98  ? 0.33040 0.32780 0.37450 0.01490  0.01480  0.02340  94  PRO B C     
4663 O  O     . PRO B 98  ? 0.31390 0.31080 0.36440 0.01810  0.01620  0.02450  94  PRO B O     
4664 C  CB    . PRO B 98  ? 0.29940 0.31010 0.35770 0.01520  0.01790  0.02650  94  PRO B CB    
4665 C  CG    . PRO B 98  ? 0.25790 0.27280 0.32580 0.01700  0.01420  0.03110  94  PRO B CG    
4666 C  CD    . PRO B 98  ? 0.28230 0.29670 0.34560 0.01370  0.00740  0.03290  94  PRO B CD    
4667 N  N     . VAL B 99  ? 0.31490 0.30680 0.34910 0.01290  0.01410  0.02080  95  VAL B N     
4668 C  CA    . VAL B 99  ? 0.28630 0.27150 0.31600 0.01400  0.01530  0.01870  95  VAL B CA    
4669 C  C     . VAL B 99  ? 0.38840 0.37070 0.41130 0.01260  0.01930  0.01430  95  VAL B C     
4670 O  O     . VAL B 99  ? 0.33840 0.32180 0.35560 0.00980  0.01840  0.01350  95  VAL B O     
4671 C  CB    . VAL B 99  ? 0.28440 0.26650 0.30840 0.01280  0.01050  0.02010  95  VAL B CB    
4672 C  CG1   . VAL B 99  ? 0.25450 0.23010 0.27390 0.01330  0.01200  0.01820  95  VAL B CG1   
4673 C  CG2   . VAL B 99  ? 0.32180 0.30700 0.35160 0.01390  0.00650  0.02440  95  VAL B CG2   
4674 N  N     . LEU B 100 ? 0.33290 0.31170 0.35680 0.01440  0.02350  0.01170  96  LEU B N     
4675 C  CA    . LEU B 100 ? 0.25470 0.23020 0.27150 0.01290  0.02690  0.00710  96  LEU B CA    
4676 C  C     . LEU B 100 ? 0.31640 0.28520 0.32750 0.01200  0.02540  0.00590  96  LEU B C     
4677 O  O     . LEU B 100 ? 0.30340 0.26810 0.31800 0.01410  0.02560  0.00650  96  LEU B O     
4678 C  CB    . LEU B 100 ? 0.24530 0.22100 0.26630 0.01510  0.03280  0.00390  96  LEU B CB    
4679 C  CG    . LEU B 100 ? 0.32790 0.29930 0.34160 0.01360  0.03670  -0.00160 96  LEU B CG    
4680 C  CD1   . LEU B 100 ? 0.30920 0.28410 0.31490 0.00980  0.03610  -0.00240 96  LEU B CD1   
4681 C  CD2   . LEU B 100 ? 0.32060 0.29220 0.33930 0.01640  0.04280  -0.00510 96  LEU B CD2   
4682 N  N     . LEU B 101 ? 0.23560 0.20350 0.23850 0.00900  0.02380  0.00480  97  LEU B N     
4683 C  CA    . LEU B 101 ? 0.31410 0.27640 0.31140 0.00770  0.02290  0.00340  97  LEU B CA    
4684 C  C     . LEU B 101 ? 0.33550 0.29540 0.32780 0.00600  0.02660  -0.00130 97  LEU B C     
4685 O  O     . LEU B 101 ? 0.36740 0.33040 0.35490 0.00370  0.02710  -0.00260 97  LEU B O     
4686 C  CB    . LEU B 101 ? 0.28230 0.24560 0.27440 0.00560  0.01870  0.00530  97  LEU B CB    
4687 C  CG    . LEU B 101 ? 0.36790 0.32700 0.35390 0.00370  0.01820  0.00380  97  LEU B CG    
4688 C  CD1   . LEU B 101 ? 0.33800 0.29260 0.32670 0.00530  0.01800  0.00500  97  LEU B CD1   
4689 C  CD2   . LEU B 101 ? 0.32470 0.28560 0.30600 0.00200  0.01470  0.00530  97  LEU B CD2   
4690 N  N     . LEU B 102 ? 0.27230 0.22660 0.26570 0.00700  0.02880  -0.00370 98  LEU B N     
4691 C  CA    . LEU B 102 ? 0.30880 0.25960 0.29700 0.00500  0.03190  -0.00870 98  LEU B CA    
4692 C  C     . LEU B 102 ? 0.35770 0.30480 0.34030 0.00230  0.02920  -0.00870 98  LEU B C     
4693 O  O     . LEU B 102 ? 0.41230 0.35550 0.39760 0.00330  0.02760  -0.00670 98  LEU B O     
4694 C  CB    . LEU B 102 ? 0.30610 0.25200 0.29930 0.00760  0.03600  -0.01180 98  LEU B CB    
4695 C  CG    . LEU B 102 ? 0.35200 0.30190 0.35250 0.01100  0.03910  -0.01170 98  LEU B CG    
4696 C  CD1   . LEU B 102 ? 0.35710 0.30120 0.36410 0.01420  0.04290  -0.01430 98  LEU B CD1   
4697 C  CD2   . LEU B 102 ? 0.34720 0.30250 0.34300 0.00910  0.04190  -0.01450 98  LEU B CD2   
4698 N  N     . THR B 103 ? 0.32430 0.27320 0.29970 -0.00110 0.02870  -0.01050 99  THR B N     
4699 C  CA    . THR B 103 ? 0.32490 0.27120 0.29550 -0.00380 0.02640  -0.01050 99  THR B CA    
4700 C  C     . THR B 103 ? 0.34490 0.28850 0.31020 -0.00680 0.02850  -0.01550 99  THR B C     
4701 O  O     . THR B 103 ? 0.34530 0.29140 0.30760 -0.00770 0.03100  -0.01860 99  THR B O     
4702 C  CB    . THR B 103 ? 0.33150 0.28260 0.29860 -0.00550 0.02280  -0.00740 99  THR B CB    
4703 O  OG1   . THR B 103 ? 0.33690 0.29270 0.30020 -0.00730 0.02340  -0.00850 99  THR B OG1   
4704 C  CG2   . THR B 103 ? 0.26600 0.21930 0.23740 -0.00300 0.02040  -0.00310 99  THR B CG2   
4705 N  N     . ALA B 104 ? 0.31730 0.25650 0.28120 -0.00870 0.02740  -0.01600 100 ALA B N     
4706 C  CA    . ALA B 104 ? 0.36530 0.30180 0.32370 -0.01230 0.02860  -0.02080 100 ALA B CA    
4707 C  C     . ALA B 104 ? 0.39910 0.34110 0.35120 -0.01590 0.02600  -0.01990 100 ALA B C     
4708 O  O     . ALA B 104 ? 0.37460 0.32080 0.32690 -0.01570 0.02310  -0.01560 100 ALA B O     
4709 C  CB    . ALA B 104 ? 0.27730 0.20660 0.23770 -0.01330 0.02820  -0.02160 100 ALA B CB    
4710 N  N     . GLN B 105 ? 0.37410 0.31610 0.32040 -0.01930 0.02720  -0.02430 101 GLN B N     
4711 C  CA    . GLN B 105 ? 0.34280 0.29000 0.28310 -0.02320 0.02470  -0.02360 101 GLN B CA    
4712 C  C     . GLN B 105 ? 0.36590 0.30920 0.30210 -0.02740 0.02460  -0.02780 101 GLN B C     
4713 O  O     . GLN B 105 ? 0.37680 0.31390 0.31320 -0.02730 0.02750  -0.03270 101 GLN B O     
4714 C  CB    . GLN B 105 ? 0.40560 0.35920 0.34190 -0.02380 0.02580  -0.02400 101 GLN B CB    
4715 C  CG    . GLN B 105 ? 0.43400 0.39350 0.36470 -0.02780 0.02290  -0.02240 101 GLN B CG    
4716 C  CD    . GLN B 105 ? 0.49290 0.45540 0.42650 -0.02700 0.01910  -0.01670 101 GLN B CD    
4717 O  OE1   . GLN B 105 ? 0.45860 0.42000 0.39240 -0.02870 0.01680  -0.01570 101 GLN B OE1   
4718 N  NE2   . GLN B 105 ? 0.40870 0.37490 0.34490 -0.02460 0.01850  -0.01300 101 GLN B NE2   
4719 N  N     . VAL B 106 ? 0.34710 0.29380 0.28020 -0.03090 0.02130  -0.02590 102 VAL B N     
4720 C  CA    . VAL B 106 ? 0.36690 0.31080 0.29610 -0.03560 0.02060  -0.02960 102 VAL B CA    
4721 C  C     . VAL B 106 ? 0.37240 0.31710 0.29470 -0.03810 0.02280  -0.03530 102 VAL B C     
4722 O  O     . VAL B 106 ? 0.38770 0.33680 0.30810 -0.03650 0.02460  -0.03530 102 VAL B O     
4723 C  CB    . VAL B 106 ? 0.36810 0.31700 0.29610 -0.03900 0.01630  -0.02580 102 VAL B CB    
4724 C  CG1   . VAL B 106 ? 0.35870 0.30720 0.29310 -0.03640 0.01470  -0.02050 102 VAL B CG1   
4725 C  CG2   . VAL B 106 ? 0.37100 0.32870 0.29500 -0.04010 0.01460  -0.02340 102 VAL B CG2   
4726 N  N     . GLY B 107 ? 0.43390 0.37470 0.35210 -0.04240 0.02280  -0.04040 103 GLY B N     
4727 C  CA    . GLY B 107 ? 0.49620 0.43810 0.40640 -0.04540 0.02480  -0.04640 103 GLY B CA    
4728 C  C     . GLY B 107 ? 0.47880 0.43090 0.38280 -0.04850 0.02220  -0.04370 103 GLY B C     
4729 O  O     . GLY B 107 ? 0.47260 0.42950 0.37740 -0.05040 0.01800  -0.03870 103 GLY B O     
4730 N  N     . THR B 108 ? 0.43730 0.39300 0.33540 -0.04890 0.02490  -0.04680 104 THR B N     
4731 C  CA    . THR B 108 ? 0.45700 0.42270 0.34930 -0.05160 0.02260  -0.04340 104 THR B CA    
4732 C  C     . THR B 108 ? 0.48960 0.45870 0.37710 -0.05760 0.01810  -0.04310 104 THR B C     
4733 O  O     . THR B 108 ? 0.62190 0.59890 0.50890 -0.05910 0.01440  -0.03720 104 THR B O     
4734 C  CB    . THR B 108 ? 0.54950 0.51850 0.43510 -0.05200 0.02660  -0.04750 104 THR B CB    
4735 O  OG1   . THR B 108 ? 0.64270 0.60600 0.52240 -0.05470 0.02930  -0.05630 104 THR B OG1   
4736 C  CG2   . THR B 108 ? 0.51940 0.48740 0.41120 -0.04600 0.03050  -0.04620 104 THR B CG2   
4737 N  N     . ALA B 109 ? 0.51290 0.47600 0.39730 -0.06120 0.01820  -0.04920 105 ALA B N     
4738 C  CA    . ALA B 109 ? 0.50370 0.47050 0.38350 -0.06750 0.01360  -0.04910 105 ALA B CA    
4739 C  C     . ALA B 109 ? 0.50540 0.47490 0.39220 -0.06730 0.00920  -0.04180 105 ALA B C     
4740 O  O     . ALA B 109 ? 0.49000 0.46510 0.37430 -0.07210 0.00490  -0.03970 105 ALA B O     
4741 C  CB    . ALA B 109 ? 0.48290 0.44140 0.35870 -0.07150 0.01460  -0.05750 105 ALA B CB    
4742 N  N     . ALA B 110 ? 0.46180 0.42820 0.35730 -0.06210 0.01000  -0.03780 106 ALA B N     
4743 C  CA    . ALA B 110 ? 0.49520 0.46420 0.39720 -0.06150 0.00650  -0.03140 106 ALA B CA    
4744 C  C     . ALA B 110 ? 0.40760 0.38400 0.31280 -0.05810 0.00510  -0.02440 106 ALA B C     
4745 O  O     . ALA B 110 ? 0.40000 0.37920 0.31070 -0.05710 0.00260  -0.01910 106 ALA B O     
4746 C  CB    . ALA B 110 ? 0.47230 0.43290 0.38160 -0.05850 0.00800  -0.03150 106 ALA B CB    
4747 N  N     . PHE B 111 ? 0.39600 0.37570 0.29800 -0.05650 0.00690  -0.02430 107 PHE B N     
4748 C  CA    . PHE B 111 ? 0.45530 0.44100 0.36070 -0.05330 0.00570  -0.01780 107 PHE B CA    
4749 C  C     . PHE B 111 ? 0.42140 0.41500 0.32730 -0.05610 0.00100  -0.01260 107 PHE B C     
4750 O  O     . PHE B 111 ? 0.44180 0.44000 0.34180 -0.06120 -0.00110 -0.01360 107 PHE B O     
4751 C  CB    . PHE B 111 ? 0.42600 0.41490 0.32700 -0.05250 0.00800  -0.01850 107 PHE B CB    
4752 C  CG    . PHE B 111 ? 0.45810 0.44130 0.36180 -0.04810 0.01250  -0.02130 107 PHE B CG    
4753 C  CD1   . PHE B 111 ? 0.45300 0.42790 0.36090 -0.04580 0.01450  -0.02440 107 PHE B CD1   
4754 C  CD2   . PHE B 111 ? 0.55240 0.53910 0.45490 -0.04630 0.01470  -0.02020 107 PHE B CD2   
4755 C  CE1   . PHE B 111 ? 0.45360 0.42400 0.36470 -0.04160 0.01840  -0.02630 107 PHE B CE1   
4756 C  CE2   . PHE B 111 ? 0.56060 0.54300 0.46640 -0.04220 0.01880  -0.02240 107 PHE B CE2   
4757 C  CZ    . PHE B 111 ? 0.46600 0.44030 0.37610 -0.03980 0.02050  -0.02550 107 PHE B CZ    
4758 N  N     . GLY B 112 ? 0.37450 0.37000 0.28750 -0.05280 -0.00070 -0.00710 108 GLY B N     
4759 C  CA    . GLY B 112 ? 0.38670 0.39000 0.30170 -0.05440 -0.00470 -0.00150 108 GLY B CA    
4760 C  C     . GLY B 112 ? 0.40020 0.40500 0.31640 -0.05820 -0.00740 -0.00150 108 GLY B C     
4761 O  O     . GLY B 112 ? 0.38030 0.39250 0.29850 -0.05990 -0.01100 0.00330  108 GLY B O     
4762 N  N     . LYS B 113 ? 0.35910 0.35710 0.27450 -0.05970 -0.00590 -0.00620 109 LYS B N     
4763 C  CA    . LYS B 113 ? 0.32420 0.32310 0.24150 -0.06360 -0.00840 -0.00620 109 LYS B CA    
4764 C  C     . LYS B 113 ? 0.37070 0.36650 0.29580 -0.06040 -0.00780 -0.00370 109 LYS B C     
4765 O  O     . LYS B 113 ? 0.41080 0.40810 0.33880 -0.06340 -0.00970 -0.00260 109 LYS B O     
4766 C  CB    . LYS B 113 ? 0.40610 0.39920 0.31730 -0.06840 -0.00750 -0.01320 109 LYS B CB    
4767 C  CG    . LYS B 113 ? 0.40780 0.40360 0.30960 -0.07200 -0.00760 -0.01690 109 LYS B CG    
4768 C  CD    . LYS B 113 ? 0.44890 0.43940 0.34460 -0.07740 -0.00730 -0.02430 109 LYS B CD    
4769 C  CE    . LYS B 113 ? 0.45480 0.44930 0.35180 -0.08330 -0.01190 -0.02290 109 LYS B CE    
4770 N  NZ    . LYS B 113 ? 0.55550 0.56190 0.45100 -0.08580 -0.01620 -0.01730 109 LYS B NZ    
4771 N  N     . GLY B 114 ? 0.35220 0.34440 0.28080 -0.05470 -0.00520 -0.00260 110 GLY B N     
4772 C  CA    . GLY B 114 ? 0.30710 0.29670 0.24210 -0.05180 -0.00440 -0.00050 110 GLY B CA    
4773 C  C     . GLY B 114 ? 0.39700 0.37730 0.33160 -0.05200 -0.00180 -0.00480 110 GLY B C     
4774 O  O     . GLY B 114 ? 0.33570 0.31380 0.27340 -0.05370 -0.00220 -0.00450 110 GLY B O     
4775 N  N     . ALA B 115 ? 0.34500 0.32000 0.27650 -0.05010 0.00080  -0.00850 111 ALA B N     
4776 C  CA    . ALA B 115 ? 0.38830 0.35420 0.32020 -0.04970 0.00340  -0.01260 111 ALA B CA    
4777 C  C     . ALA B 115 ? 0.35670 0.31970 0.29470 -0.04540 0.00450  -0.00930 111 ALA B C     
4778 O  O     . ALA B 115 ? 0.32350 0.29080 0.26440 -0.04200 0.00400  -0.00510 111 ALA B O     
4779 C  CB    . ALA B 115 ? 0.32380 0.28590 0.25160 -0.04820 0.00640  -0.01710 111 ALA B CB    
4780 N  N     . LEU B 116 ? 0.34160 0.29720 0.28170 -0.04590 0.00580  -0.01120 112 LEU B N     
4781 C  CA    . LEU B 116 ? 0.38480 0.33760 0.33020 -0.04210 0.00690  -0.00800 112 LEU B CA    
4782 C  C     . LEU B 116 ? 0.37600 0.32860 0.32180 -0.03680 0.00850  -0.00740 112 LEU B C     
4783 O  O     . LEU B 116 ? 0.39180 0.34090 0.33570 -0.03570 0.01050  -0.01100 112 LEU B O     
4784 C  CB    . LEU B 116 ? 0.47830 0.42230 0.42590 -0.04350 0.00820  -0.01030 112 LEU B CB    
4785 C  CG    . LEU B 116 ? 0.59030 0.53090 0.54320 -0.04000 0.00920  -0.00660 112 LEU B CG    
4786 C  CD1   . LEU B 116 ? 0.52320 0.47060 0.47880 -0.03950 0.00750  -0.00080 112 LEU B CD1   
4787 C  CD2   . LEU B 116 ? 0.61670 0.54820 0.57230 -0.04190 0.01020  -0.00860 112 LEU B CD2   
4788 N  N     . GLN B 117 ? 0.33790 0.29480 0.28620 -0.03370 0.00780  -0.00300 113 GLN B N     
4789 C  CA    . GLN B 117 ? 0.37390 0.33100 0.32300 -0.02910 0.00880  -0.00210 113 GLN B CA    
4790 C  C     . GLN B 117 ? 0.42950 0.38860 0.37520 -0.02910 0.00920  -0.00440 113 GLN B C     
4791 O  O     . GLN B 117 ? 0.35320 0.31010 0.29920 -0.02650 0.01090  -0.00580 113 GLN B O     
4792 C  CB    . GLN B 117 ? 0.36750 0.31800 0.31950 -0.02650 0.01070  -0.00260 113 GLN B CB    
4793 C  CG    . GLN B 117 ? 0.38760 0.33670 0.34310 -0.02640 0.01020  0.00070  113 GLN B CG    
4794 C  CD    . GLN B 117 ? 0.40780 0.35060 0.36650 -0.02390 0.01170  0.00100  113 GLN B CD    
4795 O  OE1   . GLN B 117 ? 0.44780 0.38570 0.40680 -0.02320 0.01350  -0.00230 113 GLN B OE1   
4796 N  NE2   . GLN B 117 ? 0.29260 0.23580 0.25390 -0.02250 0.01120  0.00510  113 GLN B NE2   
4797 N  N     . GLU B 118 ? 0.33820 0.30220 0.28090 -0.03230 0.00760  -0.00450 114 GLU B N     
4798 C  CA    . GLU B 118 ? 0.40200 0.36880 0.34090 -0.03290 0.00780  -0.00610 114 GLU B CA    
4799 C  C     . GLU B 118 ? 0.33750 0.30600 0.27820 -0.02880 0.00830  -0.00390 114 GLU B C     
4800 O  O     . GLU B 118 ? 0.36220 0.33360 0.30580 -0.02670 0.00680  -0.00040 114 GLU B O     
4801 C  CB    . GLU B 118 ? 0.36700 0.34030 0.30320 -0.03670 0.00520  -0.00490 114 GLU B CB    
4802 C  CG    . GLU B 118 ? 0.39200 0.36830 0.32340 -0.03800 0.00550  -0.00630 114 GLU B CG    
4803 C  CD    . GLU B 118 ? 0.39880 0.38110 0.32620 -0.04280 0.00290  -0.00580 114 GLU B CD    
4804 O  OE1   . GLU B 118 ? 0.41280 0.39940 0.33680 -0.04360 0.00260  -0.00520 114 GLU B OE1   
4805 O  OE2   . GLU B 118 ? 0.40930 0.39260 0.33720 -0.04590 0.00110  -0.00560 114 GLU B OE2   
4806 N  N     . SER B 119 ? 0.32990 0.29670 0.26940 -0.02770 0.01040  -0.00630 115 SER B N     
4807 C  CA    . SER B 119 ? 0.36980 0.33720 0.31200 -0.02390 0.01100  -0.00450 115 SER B CA    
4808 C  C     . SER B 119 ? 0.42440 0.39640 0.36410 -0.02470 0.01100  -0.00400 115 SER B C     
4809 O  O     . SER B 119 ? 0.34840 0.32050 0.28970 -0.02250 0.01230  -0.00380 115 SER B O     
4810 C  CB    . SER B 119 ? 0.36100 0.32310 0.30570 -0.02140 0.01360  -0.00650 115 SER B CB    
4811 O  OG    . SER B 119 ? 0.36850 0.32650 0.31600 -0.02050 0.01330  -0.00590 115 SER B OG    
4812 N  N     . THR B 120 ? 0.36480 0.34130 0.30120 -0.02790 0.00920  -0.00310 116 THR B N     
4813 C  CA    . THR B 120 ? 0.34950 0.33120 0.28300 -0.02940 0.00870  -0.00180 116 THR B CA    
4814 C  C     . THR B 120 ? 0.37190 0.35770 0.30860 -0.02820 0.00580  0.00330  116 THR B C     
4815 O  O     . THR B 120 ? 0.39490 0.37960 0.33550 -0.02610 0.00450  0.00510  116 THR B O     
4816 C  CB    . THR B 120 ? 0.38880 0.37330 0.31630 -0.03410 0.00830  -0.00390 116 THR B CB    
4817 O  OG1   . THR B 120 ? 0.33560 0.32230 0.26380 -0.03590 0.00520  -0.00180 116 THR B OG1   
4818 C  CG2   . THR B 120 ? 0.43000 0.40910 0.35440 -0.03540 0.01120  -0.00980 116 THR B CG2   
4819 N  N     . VAL B 121 ? 0.30330 0.29410 0.23840 -0.02960 0.00480  0.00560  117 VAL B N     
4820 C  CA    . VAL B 121 ? 0.30190 0.29660 0.24010 -0.02890 0.00190  0.01060  117 VAL B CA    
4821 C  C     . VAL B 121 ? 0.37240 0.36910 0.31150 -0.03010 -0.00050 0.01200  117 VAL B C     
4822 O  O     . VAL B 121 ? 0.36890 0.36730 0.31260 -0.02810 -0.00240 0.01540  117 VAL B O     
4823 C  CB    . VAL B 121 ? 0.50500 0.50500 0.44080 -0.03100 0.00110  0.01340  117 VAL B CB    
4824 C  CG1   . VAL B 121 ? 0.48460 0.48890 0.41440 -0.03560 0.00030  0.01260  117 VAL B CG1   
4825 C  CG2   . VAL B 121 ? 0.53270 0.53520 0.47370 -0.02930 -0.00160 0.01880  117 VAL B CG2   
4826 N  N     . HIS B 122 ? 0.36030 0.35710 0.29560 -0.03340 -0.00030 0.00930  118 HIS B N     
4827 C  CA    . HIS B 122 ? 0.35530 0.35500 0.29210 -0.03500 -0.00270 0.01090  118 HIS B CA    
4828 C  C     . HIS B 122 ? 0.41280 0.40840 0.35340 -0.03270 -0.00190 0.01000  118 HIS B C     
4829 O  O     . HIS B 122 ? 0.36940 0.36780 0.31260 -0.03330 -0.00360 0.01200  118 HIS B O     
4830 C  CB    . HIS B 122 ? 0.39400 0.39570 0.32520 -0.04020 -0.00330 0.00840  118 HIS B CB    
4831 C  CG    . HIS B 122 ? 0.40290 0.40820 0.32830 -0.04300 -0.00330 0.00810  118 HIS B CG    
4832 N  ND1   . HIS B 122 ? 0.43490 0.44730 0.36020 -0.04440 -0.00610 0.01290  118 HIS B ND1   
4833 C  CD2   . HIS B 122 ? 0.37550 0.37860 0.29510 -0.04450 -0.00070 0.00370  118 HIS B CD2   
4834 C  CE1   . HIS B 122 ? 0.45480 0.46960 0.37380 -0.04700 -0.00530 0.01180  118 HIS B CE1   
4835 N  NE2   . HIS B 122 ? 0.40930 0.41870 0.32470 -0.04710 -0.00180 0.00590  118 HIS B NE2   
4836 N  N     . GLY B 123 ? 0.37900 0.36870 0.32020 -0.03020 0.00060  0.00740  119 GLY B N     
4837 C  CA    . GLY B 123 ? 0.36070 0.34700 0.30510 -0.02800 0.00120  0.00720  119 GLY B CA    
4838 C  C     . GLY B 123 ? 0.38810 0.37220 0.33570 -0.02360 0.00190  0.00830  119 GLY B C     
4839 O  O     . GLY B 123 ? 0.38000 0.36690 0.33000 -0.02180 0.00060  0.01100  119 GLY B O     
4840 N  N     . VAL B 124 ? 0.38540 0.36440 0.33330 -0.02190 0.00380  0.00620  120 VAL B N     
4841 C  CA    . VAL B 124 ? 0.34150 0.31840 0.29190 -0.01820 0.00430  0.00680  120 VAL B CA    
4842 C  C     . VAL B 124 ? 0.34860 0.32430 0.29790 -0.01800 0.00560  0.00540  120 VAL B C     
4843 O  O     . VAL B 124 ? 0.33370 0.30610 0.28200 -0.01830 0.00760  0.00280  120 VAL B O     
4844 C  CB    . VAL B 124 ? 0.38050 0.35370 0.33240 -0.01660 0.00530  0.00630  120 VAL B CB    
4845 C  CG1   . VAL B 124 ? 0.42040 0.39130 0.37410 -0.01330 0.00570  0.00650  120 VAL B CG1   
4846 C  CG2   . VAL B 124 ? 0.36810 0.34380 0.32140 -0.01640 0.00420  0.00830  120 VAL B CG2   
4847 N  N     . ASP B 125 ? 0.28750 0.26580 0.23760 -0.01740 0.00460  0.00720  121 ASP B N     
4848 C  CA    . ASP B 125 ? 0.29420 0.27330 0.24310 -0.01810 0.00580  0.00650  121 ASP B CA    
4849 C  C     . ASP B 125 ? 0.28380 0.25990 0.23540 -0.01540 0.00710  0.00580  121 ASP B C     
4850 O  O     . ASP B 125 ? 0.33000 0.30660 0.28450 -0.01370 0.00610  0.00760  121 ASP B O     
4851 C  CB    . ASP B 125 ? 0.27160 0.25490 0.22090 -0.01880 0.00400  0.00970  121 ASP B CB    
4852 C  CG    . ASP B 125 ? 0.38100 0.36650 0.32870 -0.02010 0.00530  0.00970  121 ASP B CG    
4853 O  OD1   . ASP B 125 ? 0.36020 0.34390 0.30710 -0.01980 0.00790  0.00710  121 ASP B OD1   
4854 O  OD2   . ASP B 125 ? 0.39910 0.38840 0.34690 -0.02130 0.00370  0.01280  121 ASP B OD2   
4855 N  N     . LEU B 126 ? 0.26710 0.23990 0.21840 -0.01510 0.00930  0.00310  122 LEU B N     
4856 C  CA    . LEU B 126 ? 0.30740 0.27780 0.26220 -0.01240 0.01040  0.00280  122 LEU B CA    
4857 C  C     . LEU B 126 ? 0.32050 0.29350 0.27680 -0.01210 0.01100  0.00360  122 LEU B C     
4858 O  O     . LEU B 126 ? 0.32540 0.29820 0.28540 -0.01010 0.01020  0.00510  122 LEU B O     
4859 C  CB    . LEU B 126 ? 0.34380 0.31040 0.29860 -0.01220 0.01300  -0.00010 122 LEU B CB    
4860 C  CG    . LEU B 126 ? 0.30300 0.26620 0.25740 -0.01260 0.01260  -0.00060 122 LEU B CG    
4861 C  CD1   . LEU B 126 ? 0.26090 0.21940 0.21670 -0.01200 0.01530  -0.00320 122 LEU B CD1   
4862 C  CD2   . LEU B 126 ? 0.31050 0.27370 0.26710 -0.01050 0.01050  0.00210  122 LEU B CD2   
4863 N  N     . VAL B 127 ? 0.28170 0.25750 0.23520 -0.01430 0.01250  0.00280  123 VAL B N     
4864 C  CA    . VAL B 127 ? 0.30460 0.28350 0.25970 -0.01420 0.01350  0.00400  123 VAL B CA    
4865 C  C     . VAL B 127 ? 0.32930 0.30990 0.28720 -0.01370 0.01050  0.00780  123 VAL B C     
4866 O  O     . VAL B 127 ? 0.34890 0.33010 0.31090 -0.01240 0.01020  0.00910  123 VAL B O     
4867 C  CB    . VAL B 127 ? 0.29120 0.27370 0.24170 -0.01700 0.01560  0.00280  123 VAL B CB    
4868 C  CG1   . VAL B 127 ? 0.28150 0.26850 0.23380 -0.01730 0.01600  0.00550  123 VAL B CG1   
4869 C  CG2   . VAL B 127 ? 0.35230 0.33240 0.30090 -0.01690 0.01930  -0.00180 123 VAL B CG2   
4870 N  N     . SER B 128 ? 0.25060 0.23190 0.20700 -0.01460 0.00800  0.00940  124 SER B N     
4871 C  CA    . SER B 128 ? 0.30860 0.29070 0.26820 -0.01390 0.00530  0.01260  124 SER B CA    
4872 C  C     . SER B 128 ? 0.31150 0.29000 0.27430 -0.01120 0.00380  0.01220  124 SER B C     
4873 O  O     . SER B 128 ? 0.30810 0.28620 0.27430 -0.01030 0.00220  0.01380  124 SER B O     
4874 C  CB    . SER B 128 ? 0.32080 0.30480 0.27880 -0.01530 0.00330  0.01460  124 SER B CB    
4875 O  OG    . SER B 128 ? 0.44010 0.42830 0.39480 -0.01820 0.00400  0.01550  124 SER B OG    
4876 N  N     . ILE B 129 ? 0.25960 0.23570 0.22120 -0.01020 0.00430  0.01030  125 ILE B N     
4877 C  CA    . ILE B 129 ? 0.23800 0.21140 0.20150 -0.00790 0.00300  0.01010  125 ILE B CA    
4878 C  C     . ILE B 129 ? 0.29170 0.26450 0.25840 -0.00670 0.00320  0.01010  125 ILE B C     
4879 O  O     . ILE B 129 ? 0.30700 0.27900 0.27600 -0.00560 0.00120  0.01080  125 ILE B O     
4880 C  CB    . ILE B 129 ? 0.32230 0.29390 0.28380 -0.00730 0.00360  0.00870  125 ILE B CB    
4881 C  CG1   . ILE B 129 ? 0.34240 0.31530 0.30200 -0.00820 0.00280  0.00930  125 ILE B CG1   
4882 C  CG2   . ILE B 129 ? 0.30590 0.27540 0.26890 -0.00510 0.00270  0.00860  125 ILE B CG2   
4883 C  CD1   . ILE B 129 ? 0.26880 0.24060 0.22660 -0.00860 0.00360  0.00840  125 ILE B CD1   
4884 N  N     . PHE B 130 ? 0.28850 0.26190 0.25560 -0.00700 0.00570  0.00910  126 PHE B N     
4885 C  CA    . PHE B 130 ? 0.27020 0.24380 0.24150 -0.00570 0.00610  0.00940  126 PHE B CA    
4886 C  C     . PHE B 130 ? 0.32980 0.30650 0.30400 -0.00660 0.00590  0.01120  126 PHE B C     
4887 O  O     . PHE B 130 ? 0.32460 0.30220 0.30310 -0.00580 0.00540  0.01210  126 PHE B O     
4888 C  CB    . PHE B 130 ? 0.22860 0.20140 0.20040 -0.00510 0.00930  0.00760  126 PHE B CB    
4889 C  CG    . PHE B 130 ? 0.37100 0.34040 0.34270 -0.00350 0.00900  0.00700  126 PHE B CG    
4890 C  CD1   . PHE B 130 ? 0.32680 0.29400 0.29470 -0.00440 0.00940  0.00580  126 PHE B CD1   
4891 C  CD2   . PHE B 130 ? 0.32690 0.29580 0.30250 -0.00150 0.00810  0.00810  126 PHE B CD2   
4892 C  CE1   . PHE B 130 ? 0.31530 0.27970 0.28340 -0.00320 0.00920  0.00590  126 PHE B CE1   
4893 C  CE2   . PHE B 130 ? 0.30220 0.26850 0.27780 -0.00030 0.00770  0.00840  126 PHE B CE2   
4894 C  CZ    . PHE B 130 ? 0.35680 0.32070 0.32870 -0.00120 0.00830  0.00730  126 PHE B CZ    
4895 N  N     . SER B 131 ? 0.29020 0.26900 0.26240 -0.00860 0.00600  0.01220  127 SER B N     
4896 C  CA    . SER B 131 ? 0.28870 0.27090 0.26390 -0.00990 0.00580  0.01460  127 SER B CA    
4897 C  C     . SER B 131 ? 0.28450 0.26580 0.26440 -0.00930 0.00290  0.01630  127 SER B C     
4898 O  O     . SER B 131 ? 0.30570 0.28970 0.28990 -0.00980 0.00330  0.01780  127 SER B O     
4899 C  CB    . SER B 131 ? 0.37900 0.36340 0.35120 -0.01220 0.00550  0.01620  127 SER B CB    
4900 O  OG    . SER B 131 ? 0.61090 0.59810 0.58640 -0.01350 0.00470  0.01940  127 SER B OG    
4901 N  N     . PRO B 132 ? 0.33270 0.31080 0.31230 -0.00850 -0.00010 0.01610  128 PRO B N     
4902 C  CA    . PRO B 132 ? 0.33940 0.31630 0.32320 -0.00830 -0.00310 0.01710  128 PRO B CA    
4903 C  C     . PRO B 132 ? 0.34420 0.32130 0.33090 -0.00720 -0.00350 0.01640  128 PRO B C     
4904 O  O     . PRO B 132 ? 0.30920 0.28670 0.30000 -0.00780 -0.00580 0.01760  128 PRO B O     
4905 C  CB    . PRO B 132 ? 0.31180 0.28500 0.29340 -0.00740 -0.00550 0.01600  128 PRO B CB    
4906 C  CG    . PRO B 132 ? 0.33430 0.30810 0.31200 -0.00770 -0.00390 0.01590  128 PRO B CG    
4907 C  CD    . PRO B 132 ? 0.34710 0.32290 0.32280 -0.00790 -0.00080 0.01500  128 PRO B CD    
4908 N  N     . ILE B 133 ? 0.34240 0.31930 0.32760 -0.00570 -0.00170 0.01500  129 ILE B N     
4909 C  CA    . ILE B 133 ? 0.32960 0.30710 0.31820 -0.00450 -0.00260 0.01510  129 ILE B CA    
4910 C  C     . ILE B 133 ? 0.32760 0.30790 0.31910 -0.00370 0.00080  0.01540  129 ILE B C     
4911 O  O     . ILE B 133 ? 0.31110 0.29160 0.30510 -0.00210 0.00090  0.01540  129 ILE B O     
4912 C  CB    . ILE B 133 ? 0.33860 0.31310 0.32400 -0.00290 -0.00410 0.01370  129 ILE B CB    
4913 C  CG1   . ILE B 133 ? 0.27360 0.24620 0.25400 -0.00250 -0.00200 0.01230  129 ILE B CG1   
4914 C  CG2   . ILE B 133 ? 0.34870 0.32120 0.33290 -0.00330 -0.00770 0.01320  129 ILE B CG2   
4915 C  CD1   . ILE B 133 ? 0.33560 0.30840 0.31630 -0.00160 0.00100  0.01180  129 ILE B CD1   
4916 N  N     . THR B 134 ? 0.32370 0.30650 0.31530 -0.00490 0.00370  0.01560  130 THR B N     
4917 C  CA    . THR B 134 ? 0.31100 0.29690 0.30590 -0.00410 0.00730  0.01560  130 THR B CA    
4918 C  C     . THR B 134 ? 0.28220 0.27300 0.28040 -0.00590 0.00830  0.01770  130 THR B C     
4919 O  O     . THR B 134 ? 0.29450 0.28560 0.29110 -0.00800 0.00670  0.01900  130 THR B O     
4920 C  CB    . THR B 134 ? 0.33640 0.32100 0.32710 -0.00360 0.01110  0.01290  130 THR B CB    
4921 O  OG1   . THR B 134 ? 0.30150 0.28600 0.28670 -0.00570 0.01140  0.01240  130 THR B OG1   
4922 C  CG2   . THR B 134 ? 0.27830 0.25840 0.26730 -0.00180 0.01060  0.01130  130 THR B CG2   
4923 N  N     . LYS B 135 ? 0.28440 0.27940 0.28810 -0.00500 0.01090  0.01840  131 LYS B N     
4924 C  CA    . LYS B 135 ? 0.21910 0.21980 0.22560 -0.00680 0.01300  0.02040  131 LYS B CA    
4925 C  C     . LYS B 135 ? 0.34500 0.34670 0.34540 -0.00780 0.01690  0.01870  131 LYS B C     
4926 O  O     . LYS B 135 ? 0.34180 0.34750 0.34150 -0.01020 0.01780  0.02070  131 LYS B O     
4927 C  CB    . LYS B 135 ? 0.21950 0.22540 0.23420 -0.00540 0.01510  0.02170  131 LYS B CB    
4928 C  CG    . LYS B 135 ? 0.27470 0.28080 0.29590 -0.00470 0.01090  0.02380  131 LYS B CG    
4929 C  CD    . LYS B 135 ? 0.30070 0.31340 0.33120 -0.00340 0.01320  0.02580  131 LYS B CD    
4930 C  CE    . LYS B 135 ? 0.26950 0.28880 0.30420 -0.00600 0.01440  0.02890  131 LYS B CE    
4931 N  NZ    . LYS B 135 ? 0.31560 0.34230 0.36050 -0.00470 0.01650  0.03110  131 LYS B NZ    
4932 N  N     . LEU B 136 ? 0.34090 0.33910 0.33670 -0.00640 0.01910  0.01510  132 LEU B N     
4933 C  CA    . LEU B 136 ? 0.31940 0.31840 0.30870 -0.00770 0.02250  0.01270  132 LEU B CA    
4934 C  C     . LEU B 136 ? 0.32550 0.31840 0.30930 -0.00710 0.02200  0.00950  132 LEU B C     
4935 O  O     . LEU B 136 ? 0.29810 0.28750 0.28420 -0.00470 0.02210  0.00800  132 LEU B O     
4936 C  CB    . LEU B 136 ? 0.27280 0.27590 0.26420 -0.00670 0.02800  0.01100  132 LEU B CB    
4937 C  CG    . LEU B 136 ? 0.35640 0.35970 0.34020 -0.00790 0.03190  0.00720  132 LEU B CG    
4938 C  CD1   . LEU B 136 ? 0.39830 0.40580 0.37680 -0.01170 0.03120  0.00960  132 LEU B CD1   
4939 C  CD2   . LEU B 136 ? 0.37830 0.38420 0.36450 -0.00600 0.03770  0.00420  132 LEU B CD2   
4940 N  N     . SER B 137 ? 0.29890 0.29110 0.27610 -0.00940 0.02120  0.00900  133 SER B N     
4941 C  CA    . SER B 137 ? 0.32730 0.31480 0.29930 -0.00940 0.02080  0.00620  133 SER B CA    
4942 C  C     . SER B 137 ? 0.34340 0.33300 0.30860 -0.01210 0.02300  0.00440  133 SER B C     
4943 O  O     . SER B 137 ? 0.30940 0.30210 0.27190 -0.01450 0.02140  0.00690  133 SER B O     
4944 C  CB    . SER B 137 ? 0.29200 0.27650 0.26310 -0.00960 0.01630  0.00800  133 SER B CB    
4945 O  OG    . SER B 137 ? 0.31420 0.29520 0.28080 -0.00990 0.01620  0.00560  133 SER B OG    
4946 N  N     . VAL B 138 ? 0.36580 0.35320 0.32810 -0.01180 0.02630  0.00010  134 VAL B N     
4947 C  CA    . VAL B 138 ? 0.35830 0.34840 0.31370 -0.01450 0.02880  -0.00240 134 VAL B CA    
4948 C  C     . VAL B 138 ? 0.33290 0.31780 0.28460 -0.01450 0.03050  -0.00750 134 VAL B C     
4949 O  O     . VAL B 138 ? 0.34290 0.32300 0.29870 -0.01190 0.03150  -0.00930 134 VAL B O     
4950 C  CB    . VAL B 138 ? 0.38060 0.37650 0.33730 -0.01450 0.03290  -0.00250 134 VAL B CB    
4951 C  CG1   . VAL B 138 ? 0.24960 0.24360 0.21200 -0.01100 0.03660  -0.00520 134 VAL B CG1   
4952 C  CG2   . VAL B 138 ? 0.42770 0.42730 0.37590 -0.01780 0.03540  -0.00490 134 VAL B CG2   
4953 N  N     . MET B 139 ? 0.36990 0.35570 0.31410 -0.01790 0.03050  -0.00950 135 MET B N     
4954 C  CA    . MET B 139 ? 0.40180 0.38310 0.34160 -0.01890 0.03230  -0.01490 135 MET B CA    
4955 C  C     . MET B 139 ? 0.41560 0.39910 0.35130 -0.01970 0.03740  -0.01950 135 MET B C     
4956 O  O     . MET B 139 ? 0.39930 0.38940 0.33080 -0.02200 0.03810  -0.01820 135 MET B O     
4957 C  CB    . MET B 139 ? 0.32970 0.31080 0.26350 -0.02240 0.02900  -0.01460 135 MET B CB    
4958 C  CG    . MET B 139 ? 0.35680 0.33300 0.28610 -0.02420 0.03030  -0.02030 135 MET B CG    
4959 S  SD    . MET B 139 ? 0.45700 0.43360 0.38140 -0.02830 0.02550  -0.01890 135 MET B SD    
4960 C  CE    . MET B 139 ? 0.45610 0.44010 0.37150 -0.03290 0.02610  -0.01980 135 MET B CE    
4961 N  N     . ILE B 140 ? 0.34460 0.32300 0.28190 -0.01770 0.04100  -0.02460 136 ILE B N     
4962 C  CA    . ILE B 140 ? 0.43580 0.41570 0.36930 -0.01810 0.04640  -0.03010 136 ILE B CA    
4963 C  C     . ILE B 140 ? 0.44000 0.42150 0.36280 -0.02300 0.04580  -0.03310 136 ILE B C     
4964 O  O     . ILE B 140 ? 0.52200 0.49820 0.44190 -0.02490 0.04360  -0.03540 136 ILE B O     
4965 C  CB    . ILE B 140 ? 0.51200 0.48450 0.45010 -0.01470 0.05020  -0.03520 136 ILE B CB    
4966 C  CG1   . ILE B 140 ? 0.53210 0.50230 0.48100 -0.01020 0.04900  -0.03120 136 ILE B CG1   
4967 C  CG2   . ILE B 140 ? 0.44140 0.41650 0.37800 -0.01360 0.05660  -0.04030 136 ILE B CG2   
4968 C  CD1   . ILE B 140 ? 0.53410 0.51080 0.48880 -0.00770 0.05140  -0.02840 136 ILE B CD1   
4969 N  N     . PRO B 141 ? 0.47850 0.46770 0.39520 -0.02560 0.04740  -0.03280 137 PRO B N     
4970 C  CA    . PRO B 141 ? 0.50240 0.49430 0.40840 -0.03090 0.04580  -0.03460 137 PRO B CA    
4971 C  C     . PRO B 141 ? 0.53530 0.52310 0.43450 -0.03250 0.04950  -0.04340 137 PRO B C     
4972 O  O     . PRO B 141 ? 0.55800 0.54450 0.45000 -0.03670 0.04700  -0.04590 137 PRO B O     
4973 C  CB    . PRO B 141 ? 0.47450 0.47660 0.37720 -0.03280 0.04640  -0.03040 137 PRO B CB    
4974 C  CG    . PRO B 141 ? 0.46010 0.46390 0.36900 -0.02880 0.05130  -0.03080 137 PRO B CG    
4975 C  CD    . PRO B 141 ? 0.47070 0.46720 0.39000 -0.02420 0.05030  -0.03000 137 PRO B CD    
4976 N  N     . THR B 142 ? 0.51230 0.49840 0.41380 -0.02940 0.05540  -0.04830 138 THR B N     
4977 C  CA    . THR B 142 ? 0.52980 0.51120 0.42530 -0.03050 0.05970  -0.05760 138 THR B CA    
4978 C  C     . THR B 142 ? 0.48270 0.45780 0.38690 -0.02490 0.06470  -0.06140 138 THR B C     
4979 O  O     . THR B 142 ? 0.47770 0.45540 0.39090 -0.02070 0.06580  -0.05700 138 THR B O     
4980 C  CB    . THR B 142 ? 0.56460 0.55400 0.44940 -0.03380 0.06320  -0.06090 138 THR B CB    
4981 O  OG1   . THR B 142 ? 0.51830 0.51410 0.40780 -0.03050 0.06770  -0.05860 138 THR B OG1   
4982 C  CG2   . THR B 142 ? 0.50940 0.50630 0.38620 -0.03930 0.05810  -0.05600 138 THR B CG2   
4983 N  N     . ALA B 143 ? 0.49940 0.46630 0.40140 -0.02490 0.06750  -0.06960 139 ALA B N     
4984 C  CA    . ALA B 143 ? 0.52770 0.48820 0.43870 -0.01930 0.07250  -0.07340 139 ALA B CA    
4985 C  C     . ALA B 143 ? 0.48780 0.45590 0.40070 -0.01620 0.07870  -0.07410 139 ALA B C     
4986 O  O     . ALA B 143 ? 0.52780 0.49550 0.45180 -0.01090 0.08110  -0.07180 139 ALA B O     
4987 C  CB    . ALA B 143 ? 0.50630 0.45650 0.41370 -0.02030 0.07490  -0.08290 139 ALA B CB    
4988 N  N     . GLU B 144 ? 0.42710 0.40310 0.32950 -0.01980 0.08110  -0.07660 140 GLU B N     
4989 C  CA    . GLU B 144 ? 0.51580 0.50020 0.41900 -0.01750 0.08740  -0.07730 140 GLU B CA    
4990 C  C     . GLU B 144 ? 0.47480 0.46630 0.38800 -0.01460 0.08590  -0.06770 140 GLU B C     
4991 O  O     . GLU B 144 ? 0.47300 0.46950 0.39250 -0.01080 0.09110  -0.06750 140 GLU B O     
4992 C  CB    . GLU B 144 ? 0.64130 0.63420 0.53020 -0.02290 0.08900  -0.07990 140 GLU B CB    
4993 C  CG    . GLU B 144 ? 0.86840 0.87020 0.75600 -0.02100 0.09660  -0.08220 140 GLU B CG    
4994 C  CD    . GLU B 144 ? 1.01170 1.02580 0.90170 -0.02170 0.09520  -0.07240 140 GLU B CD    
4995 O  OE1   . GLU B 144 ? 1.06910 1.08770 0.95290 -0.02650 0.08950  -0.06670 140 GLU B OE1   
4996 O  OE2   . GLU B 144 ? 1.07270 1.09200 0.97130 -0.01760 0.09970  -0.07020 140 GLU B OE2   
4997 N  N     . LYS B 145 ? 0.49130 0.48340 0.40650 -0.01630 0.07880  -0.06000 141 LYS B N     
4998 C  CA    . LYS B 145 ? 0.43870 0.43700 0.36290 -0.01410 0.07680  -0.05130 141 LYS B CA    
4999 C  C     . LYS B 145 ? 0.38430 0.37610 0.32120 -0.00920 0.07510  -0.04860 141 LYS B C     
5000 O  O     . LYS B 145 ? 0.38780 0.38390 0.33250 -0.00750 0.07290  -0.04170 141 LYS B O     
5001 C  CB    . LYS B 145 ? 0.47570 0.47880 0.39540 -0.01850 0.07030  -0.04410 141 LYS B CB    
5002 C  CG    . LYS B 145 ? 0.52080 0.53320 0.42970 -0.02320 0.07150  -0.04370 141 LYS B CG    
5003 C  CD    . LYS B 145 ? 0.54860 0.57100 0.46250 -0.02220 0.07360  -0.03780 141 LYS B CD    
5004 C  CE    . LYS B 145 ? 0.61160 0.64380 0.51540 -0.02590 0.07720  -0.03870 141 LYS B CE    
5005 N  NZ    . LYS B 145 ? 0.75780 0.79310 0.66180 -0.02320 0.08570  -0.04480 141 LYS B NZ    
5006 N  N     . MET B 146 ? 0.42350 0.40530 0.36280 -0.00720 0.07600  -0.05380 142 MET B N     
5007 C  CA    . MET B 146 ? 0.41990 0.39570 0.37080 -0.00280 0.07400  -0.05070 142 MET B CA    
5008 C  C     . MET B 146 ? 0.37490 0.35590 0.33690 0.00210  0.07750  -0.04780 142 MET B C     
5009 O  O     . MET B 146 ? 0.41030 0.39290 0.38080 0.00400  0.07400  -0.04120 142 MET B O     
5010 C  CB    . MET B 146 ? 0.37380 0.33820 0.32560 -0.00140 0.07530  -0.05700 142 MET B CB    
5011 C  CG    . MET B 146 ? 0.44660 0.40490 0.41050 0.00310  0.07350  -0.05370 142 MET B CG    
5012 S  SD    . MET B 146 ? 0.52330 0.48010 0.48810 0.00110  0.06480  -0.04570 142 MET B SD    
5013 C  CE    . MET B 146 ? 0.52870 0.47560 0.48590 -0.00260 0.06280  -0.05090 142 MET B CE    
5014 N  N     . GLY B 147 ? 0.35630 0.34040 0.31870 0.00410  0.08460  -0.05290 143 GLY B N     
5015 C  CA    . GLY B 147 ? 0.34320 0.33300 0.31710 0.00880  0.08840  -0.05020 143 GLY B CA    
5016 C  C     . GLY B 147 ? 0.39910 0.39940 0.37530 0.00730  0.08560  -0.04210 143 GLY B C     
5017 O  O     . GLY B 147 ? 0.48070 0.48290 0.46750 0.00990  0.08310  -0.03610 143 GLY B O     
5018 N  N     . GLU B 148 ? 0.37760 0.38460 0.34380 0.00270  0.08560  -0.04150 144 GLU B N     
5019 C  CA    . GLU B 148 ? 0.39480 0.41140 0.36290 0.00070  0.08300  -0.03370 144 GLU B CA    
5020 C  C     . GLU B 148 ? 0.38640 0.39980 0.35870 -0.00010 0.07510  -0.02710 144 GLU B C     
5021 O  O     . GLU B 148 ? 0.40310 0.42110 0.38390 0.00110  0.07300  -0.02090 144 GLU B O     
5022 C  CB    . GLU B 148 ? 0.40860 0.43170 0.36430 -0.00460 0.08360  -0.03410 144 GLU B CB    
5023 C  CG    . GLU B 148 ? 0.56880 0.59880 0.52100 -0.00410 0.09180  -0.03890 144 GLU B CG    
5024 C  CD    . GLU B 148 ? 0.67600 0.71290 0.61480 -0.00980 0.09220  -0.03910 144 GLU B CD    
5025 O  OE1   . GLU B 148 ? 0.71800 0.75380 0.65090 -0.01380 0.08590  -0.03530 144 GLU B OE1   
5026 O  OE2   . GLU B 148 ? 0.80030 0.84410 0.73460 -0.01000 0.09890  -0.04280 144 GLU B OE2   
5027 N  N     . MET B 149 ? 0.32370 0.32940 0.28990 -0.00210 0.07060  -0.02840 145 MET B N     
5028 C  CA    . MET B 149 ? 0.36320 0.36600 0.33230 -0.00280 0.06350  -0.02270 145 MET B CA    
5029 C  C     . MET B 149 ? 0.33650 0.33520 0.31700 0.00170  0.06240  -0.02090 145 MET B C     
5030 O  O     . MET B 149 ? 0.33770 0.33750 0.32330 0.00190  0.05760  -0.01510 145 MET B O     
5031 C  CB    . MET B 149 ? 0.44190 0.43820 0.40230 -0.00590 0.05970  -0.02480 145 MET B CB    
5032 C  CG    . MET B 149 ? 0.54550 0.54660 0.49510 -0.01080 0.05910  -0.02490 145 MET B CG    
5033 S  SD    . MET B 149 ? 0.64300 0.65170 0.59440 -0.01310 0.05440  -0.01600 145 MET B SD    
5034 C  CE    . MET B 149 ? 0.67770 0.69330 0.61670 -0.01840 0.05580  -0.01680 145 MET B CE    
5035 N  N     . THR B 150 ? 0.32600 0.31960 0.31020 0.00520  0.06630  -0.02570 146 THR B N     
5036 C  CA    . THR B 150 ? 0.36580 0.35610 0.36140 0.00970  0.06530  -0.02340 146 THR B CA    
5037 C  C     . THR B 150 ? 0.33980 0.33870 0.34530 0.01200  0.06670  -0.01880 146 THR B C     
5038 O  O     . THR B 150 ? 0.30250 0.30270 0.31500 0.01290  0.06220  -0.01320 146 THR B O     
5039 C  CB    . THR B 150 ? 0.38260 0.36540 0.38060 0.01300  0.06970  -0.02950 146 THR B CB    
5040 O  OG1   . THR B 150 ? 0.38470 0.35900 0.37450 0.01040  0.06740  -0.03300 146 THR B OG1   
5041 C  CG2   . THR B 150 ? 0.39380 0.37420 0.40460 0.01790  0.06880  -0.02630 146 THR B CG2   
5042 N  N     . ARG B 151 ? 0.28260 0.28820 0.28840 0.01250  0.07260  -0.02100 147 ARG B N     
5043 C  CA    . ARG B 151 ? 0.33410 0.34910 0.34960 0.01430  0.07410  -0.01630 147 ARG B CA    
5044 C  C     . ARG B 151 ? 0.33110 0.35140 0.34570 0.01050  0.06860  -0.00960 147 ARG B C     
5045 O  O     . ARG B 151 ? 0.34700 0.37160 0.37100 0.01160  0.06590  -0.00420 147 ARG B O     
5046 C  CB    . ARG B 151 ? 0.28500 0.30680 0.29990 0.01520  0.08220  -0.02020 147 ARG B CB    
5047 C  CG    . ARG B 151 ? 0.29920 0.31530 0.31780 0.01990  0.08790  -0.02680 147 ARG B CG    
5048 C  CD    . ARG B 151 ? 0.36380 0.38720 0.38350 0.02180  0.09650  -0.03090 147 ARG B CD    
5049 N  NE    . ARG B 151 ? 0.45780 0.48600 0.46450 0.01710  0.09870  -0.03340 147 ARG B NE    
5050 C  CZ    . ARG B 151 ? 0.59160 0.61490 0.58680 0.01530  0.10170  -0.04110 147 ARG B CZ    
5051 N  NH1   . ARG B 151 ? 0.52970 0.54230 0.52500 0.01790  0.10290  -0.04720 147 ARG B NH1   
5052 N  NH2   . ARG B 151 ? 0.67890 0.70830 0.66240 0.01080  0.10330  -0.04230 147 ARG B NH2   
5053 N  N     . ARG B 152 ? 0.33110 0.35110 0.33470 0.00600  0.06640  -0.00980 148 ARG B N     
5054 C  CA    . ARG B 152 ? 0.29140 0.31460 0.29410 0.00250  0.06070  -0.00370 148 ARG B CA    
5055 C  C     . ARG B 152 ? 0.37330 0.39110 0.38080 0.00350  0.05430  -0.00040 148 ARG B C     
5056 O  O     . ARG B 152 ? 0.32230 0.34370 0.33610 0.00300  0.05070  0.00490  148 ARG B O     
5057 C  CB    . ARG B 152 ? 0.32140 0.34400 0.31180 -0.00200 0.05940  -0.00480 148 ARG B CB    
5058 C  CG    . ARG B 152 ? 0.35360 0.37790 0.34260 -0.00540 0.05350  0.00110  148 ARG B CG    
5059 C  CD    . ARG B 152 ? 0.50500 0.53200 0.48330 -0.00970 0.05360  0.00080  148 ARG B CD    
5060 N  NE    . ARG B 152 ? 0.60560 0.63810 0.58540 -0.01270 0.05050  0.00740  148 ARG B NE    
5061 C  CZ    . ARG B 152 ? 0.57000 0.61040 0.54650 -0.01560 0.05280  0.00970  148 ARG B CZ    
5062 N  NH1   . ARG B 152 ? 0.52210 0.56620 0.49230 -0.01600 0.05850  0.00550  148 ARG B NH1   
5063 N  NH2   . ARG B 152 ? 0.70220 0.74660 0.68140 -0.01820 0.04940  0.01630  148 ARG B NH2   
5064 N  N     . ALA B 153 ? 0.34360 0.35270 0.34790 0.00450  0.05260  -0.00350 149 ALA B N     
5065 C  CA    . ALA B 153 ? 0.31680 0.32100 0.32490 0.00560  0.04700  -0.00060 149 ALA B CA    
5066 C  C     . ALA B 153 ? 0.34790 0.35510 0.36800 0.00910  0.04700  0.00240  149 ALA B C     
5067 O  O     . ALA B 153 ? 0.32060 0.32930 0.34510 0.00870  0.04210  0.00700  149 ALA B O     
5068 C  CB    . ALA B 153 ? 0.25660 0.25170 0.26000 0.00630  0.04630  -0.00440 149 ALA B CB    
5069 N  N     . LEU B 154 ? 0.29830 0.30660 0.32410 0.01260  0.05240  -0.00020 150 LEU B N     
5070 C  CA    . LEU B 154 ? 0.31770 0.32930 0.35610 0.01630  0.05240  0.00310  150 LEU B CA    
5071 C  C     . LEU B 154 ? 0.40680 0.42820 0.45130 0.01500  0.05170  0.00800  150 LEU B C     
5072 O  O     . LEU B 154 ? 0.33130 0.35540 0.38380 0.01560  0.04760  0.01270  150 LEU B O     
5073 C  CB    . LEU B 154 ? 0.35860 0.36920 0.40240 0.02070  0.05880  -0.00090 150 LEU B CB    
5074 C  CG    . LEU B 154 ? 0.39660 0.39670 0.43550 0.02190  0.05960  -0.00580 150 LEU B CG    
5075 C  CD1   . LEU B 154 ? 0.28360 0.28190 0.32780 0.02620  0.06650  -0.01060 150 LEU B CD1   
5076 C  CD2   . LEU B 154 ? 0.44480 0.43950 0.48630 0.02260  0.05350  -0.00220 150 LEU B CD2   
5077 N  N     . ARG B 155 ? 0.36960 0.39700 0.41040 0.01270  0.05540  0.00720  151 ARG B N     
5078 C  CA    . ARG B 155 ? 0.30020 0.33690 0.34650 0.01070  0.05460  0.01230  151 ARG B CA    
5079 C  C     . ARG B 155 ? 0.34190 0.37680 0.38640 0.00730  0.04690  0.01660  151 ARG B C     
5080 O  O     . ARG B 155 ? 0.30650 0.34560 0.35920 0.00690  0.04350  0.02130  151 ARG B O     
5081 C  CB    . ARG B 155 ? 0.26840 0.31110 0.30900 0.00830  0.05970  0.01090  151 ARG B CB    
5082 C  CG    . ARG B 155 ? 0.30140 0.35330 0.34580 0.00510  0.05840  0.01670  151 ARG B CG    
5083 C  CD    . ARG B 155 ? 0.26670 0.32610 0.30610 0.00310  0.06460  0.01560  151 ARG B CD    
5084 N  NE    . ARG B 155 ? 0.35260 0.40730 0.37820 0.00030  0.06460  0.01210  151 ARG B NE    
5085 C  CZ    . ARG B 155 ? 0.39140 0.44320 0.40940 0.00140  0.06960  0.00570  151 ARG B CZ    
5086 N  NH1   . ARG B 155 ? 0.32700 0.37950 0.35000 0.00570  0.07540  0.00150  151 ARG B NH1   
5087 N  NH2   . ARG B 155 ? 0.27030 0.31860 0.27600 -0.00180 0.06850  0.00330  151 ARG B NH2   
5088 N  N     . THR B 156 ? 0.30220 0.33070 0.33620 0.00480  0.04420  0.01480  152 THR B N     
5089 C  CA    . THR B 156 ? 0.31510 0.34180 0.34680 0.00160  0.03760  0.01830  152 THR B CA    
5090 C  C     . THR B 156 ? 0.34430 0.36720 0.38100 0.00330  0.03250  0.02000  152 THR B C     
5091 O  O     . THR B 156 ? 0.27550 0.30020 0.31590 0.00150  0.02770  0.02380  152 THR B O     
5092 C  CB    . THR B 156 ? 0.34910 0.37050 0.36920 -0.00090 0.03640  0.01600  152 THR B CB    
5093 O  OG1   . THR B 156 ? 0.35320 0.37900 0.36820 -0.00270 0.04100  0.01470  152 THR B OG1   
5094 C  CG2   . THR B 156 ? 0.29610 0.31570 0.31460 -0.00380 0.03020  0.01940  152 THR B CG2   
5095 N  N     . ALA B 157 ? 0.30130 0.31900 0.33820 0.00650  0.03320  0.01740  153 ALA B N     
5096 C  CA    . ALA B 157 ? 0.38760 0.40190 0.42800 0.00780  0.02820  0.01930  153 ALA B CA    
5097 C  C     . ALA B 157 ? 0.34230 0.36330 0.39410 0.00880  0.02650  0.02360  153 ALA B C     
5098 O  O     . ALA B 157 ? 0.30660 0.32730 0.36030 0.00770  0.02080  0.02640  153 ALA B O     
5099 C  CB    . ALA B 157 ? 0.25100 0.25910 0.29050 0.01110  0.02990  0.01640  153 ALA B CB    
5100 N  N     . GLN B 158 ? 0.31420 0.34170 0.37360 0.01070  0.03140  0.02410  154 GLN B N     
5101 C  CA    . GLN B 158 ? 0.36070 0.39500 0.43260 0.01250  0.03040  0.02820  154 GLN B CA    
5102 C  C     . GLN B 158 ? 0.36550 0.40910 0.44340 0.01000  0.03090  0.03170  154 GLN B C     
5103 O  O     . GLN B 158 ? 0.39880 0.44930 0.48780 0.01100  0.02990  0.03540  154 GLN B O     
5104 C  CB    . GLN B 158 ? 0.37780 0.41280 0.45680 0.01750  0.03540  0.02670  154 GLN B CB    
5105 C  CG    . GLN B 158 ? 0.36520 0.39080 0.43950 0.01970  0.03450  0.02400  154 GLN B CG    
5106 C  CD    . GLN B 158 ? 0.40620 0.43040 0.48590 0.02450  0.04040  0.02140  154 GLN B CD    
5107 O  OE1   . GLN B 158 ? 0.47660 0.50090 0.56510 0.02790  0.03930  0.02380  154 GLN B OE1   
5108 N  NE2   . GLN B 158 ? 0.43260 0.45530 0.50710 0.02480  0.04660  0.01630  154 GLN B NE2   
5109 N  N     . SER B 159 ? 0.30070 0.34520 0.37200 0.00650  0.03200  0.03110  155 SER B N     
5110 C  CA    . SER B 159 ? 0.33490 0.38790 0.41150 0.00350  0.03220  0.03510  155 SER B CA    
5111 C  C     . SER B 159 ? 0.31670 0.36710 0.39070 -0.00080 0.02510  0.03780  155 SER B C     
5112 O  O     . SER B 159 ? 0.29510 0.33740 0.36110 -0.00150 0.02130  0.03580  155 SER B O     
5113 C  CB    . SER B 159 ? 0.30240 0.35860 0.37360 0.00240  0.03840  0.03330  155 SER B CB    
5114 O  OG    . SER B 159 ? 0.37530 0.43370 0.44860 0.00640  0.04540  0.02990  155 SER B OG    
5115 N  N     . GLY B 160 ? 0.28510 0.34270 0.36650 -0.00370 0.02350  0.04230  156 GLY B N     
5116 C  CA    . GLY B 160 ? 0.28910 0.34370 0.36920 -0.00770 0.01660  0.04460  156 GLY B CA    
5117 C  C     . GLY B 160 ? 0.31570 0.36400 0.39470 -0.00670 0.01070  0.04350  156 GLY B C     
5118 O  O     . GLY B 160 ? 0.33040 0.38030 0.41490 -0.00360 0.01050  0.04370  156 GLY B O     
5119 N  N     . ARG B 161 ? 0.29610 0.33720 0.36770 -0.00910 0.00600  0.04240  157 ARG B N     
5120 C  CA    . ARG B 161 ? 0.30350 0.33820 0.37150 -0.00820 0.00110  0.04060  157 ARG B CA    
5121 C  C     . ARG B 161 ? 0.32440 0.35380 0.38560 -0.00450 0.00430  0.03680  157 ARG B C     
5122 O  O     . ARG B 161 ? 0.32320 0.34810 0.37600 -0.00480 0.00650  0.03420  157 ARG B O     
5123 C  CB    . ARG B 161 ? 0.27790 0.30640 0.34010 -0.01150 -0.00420 0.04000  157 ARG B CB    
5124 C  CG    . ARG B 161 ? 0.32890 0.35150 0.38690 -0.01090 -0.00930 0.03790  157 ARG B CG    
5125 C  CD    . ARG B 161 ? 0.36340 0.37990 0.41590 -0.01390 -0.01370 0.03670  157 ARG B CD    
5126 N  NE    . ARG B 161 ? 0.30520 0.31700 0.35390 -0.01380 -0.01870 0.03470  157 ARG B NE    
5127 C  CZ    . ARG B 161 ? 0.36690 0.37440 0.41330 -0.01660 -0.02350 0.03360  157 ARG B CZ    
5128 N  NH1   . ARG B 161 ? 0.35130 0.35810 0.39970 -0.01960 -0.02410 0.03480  157 ARG B NH1   
5129 N  NH2   . ARG B 161 ? 0.26710 0.27080 0.30910 -0.01630 -0.02770 0.03130  157 ARG B NH2   
5130 N  N     . PRO B 162 ? 0.29600 0.32590 0.36090 -0.00120 0.00440  0.03670  158 PRO B N     
5131 C  CA    . PRO B 162 ? 0.23680 0.26160 0.29630 0.00210  0.00790  0.03340  158 PRO B CA    
5132 C  C     . PRO B 162 ? 0.28660 0.30300 0.33530 0.00110  0.00500  0.03070  158 PRO B C     
5133 O  O     . PRO B 162 ? 0.31360 0.32790 0.36010 -0.00110 -0.00030 0.03130  158 PRO B O     
5134 C  CB    . PRO B 162 ? 0.25370 0.28080 0.32080 0.00540  0.00690  0.03520  158 PRO B CB    
5135 C  CG    . PRO B 162 ? 0.32780 0.36380 0.40610 0.00430  0.00550  0.03950  158 PRO B CG    
5136 C  CD    . PRO B 162 ? 0.27570 0.31140 0.35070 -0.00050 0.00150  0.04020  158 PRO B CD    
5137 N  N     . GLY B 163 ? 0.26960 0.28150 0.31180 0.00260  0.00860  0.02740  159 GLY B N     
5138 C  CA    . GLY B 163 ? 0.27940 0.28410 0.31220 0.00200  0.00650  0.02500  159 GLY B CA    
5139 C  C     . GLY B 163 ? 0.33310 0.33360 0.36080 0.00380  0.01060  0.02180  159 GLY B C     
5140 O  O     . GLY B 163 ? 0.31000 0.31250 0.34090 0.00570  0.01540  0.02080  159 GLY B O     
5141 N  N     . PRO B 164 ? 0.34130 0.33600 0.36120 0.00340  0.00900  0.01990  160 PRO B N     
5142 C  CA    . PRO B 164 ? 0.31400 0.30410 0.32920 0.00470  0.01220  0.01690  160 PRO B CA    
5143 C  C     . PRO B 164 ? 0.32780 0.31770 0.33760 0.00310  0.01570  0.01440  160 PRO B C     
5144 O  O     . PRO B 164 ? 0.28300 0.27510 0.29080 0.00070  0.01490  0.01520  160 PRO B O     
5145 C  CB    . PRO B 164 ? 0.30260 0.28790 0.31230 0.00450  0.00860  0.01660  160 PRO B CB    
5146 C  CG    . PRO B 164 ? 0.25540 0.24190 0.26390 0.00230  0.00430  0.01800  160 PRO B CG    
5147 C  CD    . PRO B 164 ? 0.30720 0.29920 0.32350 0.00200  0.00380  0.02050  160 PRO B CD    
5148 N  N     . ILE B 165 ? 0.30770 0.29450 0.31490 0.00430  0.01930  0.01140  161 ILE B N     
5149 C  CA    . ILE B 165 ? 0.36490 0.35140 0.36620 0.00260  0.02280  0.00850  161 ILE B CA    
5150 C  C     . ILE B 165 ? 0.33090 0.31130 0.32600 0.00240  0.02280  0.00580  161 ILE B C     
5151 O  O     . ILE B 165 ? 0.33380 0.31050 0.33100 0.00450  0.02270  0.00540  161 ILE B O     
5152 C  CB    . ILE B 165 ? 0.41270 0.40240 0.41750 0.00400  0.02830  0.00660  161 ILE B CB    
5153 C  CG1   . ILE B 165 ? 0.29090 0.28750 0.30390 0.00470  0.02860  0.00990  161 ILE B CG1   
5154 C  CG2   . ILE B 165 ? 0.32810 0.31800 0.32530 0.00170  0.03150  0.00340  161 ILE B CG2   
5155 C  CD1   . ILE B 165 ? 0.24720 0.24820 0.25850 0.00140  0.02680  0.01240  161 ILE B CD1   
5156 N  N     . HIS B 166 ? 0.30050 0.28040 0.28850 -0.00020 0.02290  0.00420  162 HIS B N     
5157 C  CA    . HIS B 166 ? 0.25760 0.23250 0.23980 -0.00100 0.02320  0.00150  162 HIS B CA    
5158 C  C     . HIS B 166 ? 0.26750 0.24300 0.24530 -0.00250 0.02730  -0.00210 162 HIS B C     
5159 O  O     . HIS B 166 ? 0.34240 0.32180 0.31650 -0.00490 0.02750  -0.00180 162 HIS B O     
5160 C  CB    . HIS B 166 ? 0.25760 0.23150 0.23530 -0.00290 0.01930  0.00300  162 HIS B CB    
5161 C  CG    . HIS B 166 ? 0.28870 0.25920 0.26040 -0.00450 0.01950  0.00070  162 HIS B CG    
5162 N  ND1   . HIS B 166 ? 0.32130 0.29350 0.28790 -0.00720 0.01830  0.00080  162 HIS B ND1   
5163 C  CD2   . HIS B 166 ? 0.31020 0.27610 0.28120 -0.00400 0.02060  -0.00140 162 HIS B CD2   
5164 C  CE1   . HIS B 166 ? 0.38560 0.35470 0.34820 -0.00840 0.01850  -0.00130 162 HIS B CE1   
5165 N  NE2   . HIS B 166 ? 0.32200 0.28710 0.28720 -0.00660 0.01990  -0.00270 162 HIS B NE2   
5166 N  N     . LEU B 167 ? 0.29500 0.26650 0.27320 -0.00120 0.03030  -0.00560 163 LEU B N     
5167 C  CA    . LEU B 167 ? 0.31140 0.28210 0.28440 -0.00280 0.03420  -0.01030 163 LEU B CA    
5168 C  C     . LEU B 167 ? 0.38490 0.34980 0.35290 -0.00450 0.03300  -0.01270 163 LEU B C     
5169 O  O     . LEU B 167 ? 0.34620 0.30570 0.31740 -0.00280 0.03260  -0.01290 163 LEU B O     
5170 C  CB    . LEU B 167 ? 0.34470 0.31490 0.32260 0.00000  0.03910  -0.01320 163 LEU B CB    
5171 C  CG    . LEU B 167 ? 0.43000 0.40720 0.41060 0.00070  0.04250  -0.01290 163 LEU B CG    
5172 C  CD1   . LEU B 167 ? 0.38220 0.35760 0.36710 0.00380  0.04800  -0.01700 163 LEU B CD1   
5173 C  CD2   . LEU B 167 ? 0.41940 0.40150 0.39210 -0.00310 0.04310  -0.01350 163 LEU B CD2   
5174 N  N     . ASN B 168 ? 0.32330 0.28960 0.28380 -0.00810 0.03240  -0.01400 164 ASN B N     
5175 C  CA    . ASN B 168 ? 0.31200 0.27420 0.26770 -0.01050 0.03080  -0.01590 164 ASN B CA    
5176 C  C     . ASN B 168 ? 0.34040 0.30070 0.29120 -0.01230 0.03450  -0.02170 164 ASN B C     
5177 O  O     . ASN B 168 ? 0.40590 0.37090 0.35280 -0.01380 0.03670  -0.02330 164 ASN B O     
5178 C  CB    . ASN B 168 ? 0.34970 0.31560 0.30130 -0.01320 0.02690  -0.01270 164 ASN B CB    
5179 C  CG    . ASN B 168 ? 0.39500 0.35800 0.34240 -0.01580 0.02500  -0.01400 164 ASN B CG    
5180 O  OD1   . ASN B 168 ? 0.43880 0.40450 0.38040 -0.01920 0.02430  -0.01480 164 ASN B OD1   
5181 N  ND2   . ASN B 168 ? 0.36880 0.32680 0.31930 -0.01450 0.02410  -0.01360 164 ASN B ND2   
5182 N  N     . ILE B 169 ? 0.37440 0.32780 0.32520 -0.01250 0.03520  -0.02500 165 ILE B N     
5183 C  CA    . ILE B 169 ? 0.42760 0.37760 0.37480 -0.01370 0.03910  -0.03160 165 ILE B CA    
5184 C  C     . ILE B 169 ? 0.42050 0.36660 0.36180 -0.01780 0.03730  -0.03440 165 ILE B C     
5185 O  O     . ILE B 169 ? 0.41850 0.35870 0.36300 -0.01750 0.03580  -0.03390 165 ILE B O     
5186 C  CB    . ILE B 169 ? 0.43140 0.37560 0.38580 -0.00950 0.04270  -0.03400 165 ILE B CB    
5187 C  CG1   . ILE B 169 ? 0.43700 0.38590 0.39830 -0.00550 0.04400  -0.03050 165 ILE B CG1   
5188 C  CG2   . ILE B 169 ? 0.35690 0.29740 0.30750 -0.01050 0.04730  -0.04160 165 ILE B CG2   
5189 C  CD1   . ILE B 169 ? 0.45020 0.39420 0.42060 -0.00100 0.04650  -0.03110 165 ILE B CD1   
5190 N  N     . PRO B 170 ? 0.44930 0.39890 0.38240 -0.02190 0.03740  -0.03710 166 PRO B N     
5191 C  CA    . PRO B 170 ? 0.45380 0.40010 0.38160 -0.02630 0.03540  -0.04000 166 PRO B CA    
5192 C  C     . PRO B 170 ? 0.47890 0.41580 0.40820 -0.02580 0.03830  -0.04600 166 PRO B C     
5193 O  O     . PRO B 170 ? 0.46940 0.40390 0.39960 -0.02370 0.04290  -0.05070 166 PRO B O     
5194 C  CB    . PRO B 170 ? 0.45520 0.40800 0.37370 -0.03040 0.03550  -0.04210 166 PRO B CB    
5195 C  CG    . PRO B 170 ? 0.43040 0.39110 0.35050 -0.02850 0.03540  -0.03700 166 PRO B CG    
5196 C  CD    . PRO B 170 ? 0.44050 0.39820 0.36880 -0.02310 0.03850  -0.03660 166 PRO B CD    
5197 N  N     . ALA B 171 ? 0.45900 0.39050 0.38950 -0.02780 0.03570  -0.04580 167 ALA B N     
5198 C  CA    . ALA B 171 ? 0.46430 0.38570 0.39850 -0.02690 0.03790  -0.05020 167 ALA B CA    
5199 C  C     . ALA B 171 ? 0.47510 0.39300 0.40290 -0.02960 0.04130  -0.05880 167 ALA B C     
5200 O  O     . ALA B 171 ? 0.54120 0.45140 0.47250 -0.02730 0.04510  -0.06370 167 ALA B O     
5201 C  CB    . ALA B 171 ? 0.50450 0.42150 0.44130 -0.02900 0.03420  -0.04730 167 ALA B CB    
5202 N  N     . ASP B 172 ? 0.44160 0.36520 0.36010 -0.03430 0.04010  -0.06090 168 ASP B N     
5203 C  CA    . ASP B 172 ? 0.50450 0.42540 0.41540 -0.03730 0.04320  -0.06970 168 ASP B CA    
5204 C  C     . ASP B 172 ? 0.56730 0.49120 0.47720 -0.03380 0.04880  -0.07300 168 ASP B C     
5205 O  O     . ASP B 172 ? 0.60270 0.52100 0.51080 -0.03340 0.05330  -0.08090 168 ASP B O     
5206 C  CB    . ASP B 172 ? 0.51620 0.44300 0.41700 -0.04390 0.03960  -0.07050 168 ASP B CB    
5207 C  CG    . ASP B 172 ? 0.59150 0.53000 0.48930 -0.04420 0.03750  -0.06420 168 ASP B CG    
5208 O  OD1   . ASP B 172 ? 0.62540 0.56690 0.52990 -0.04010 0.03690  -0.05770 168 ASP B OD1   
5209 O  OD2   . ASP B 172 ? 0.65430 0.59910 0.54310 -0.04880 0.03620  -0.06570 168 ASP B OD2   
5210 N  N     . ILE B 173 ? 0.53040 0.46300 0.44210 -0.03130 0.04870  -0.06720 169 ILE B N     
5211 C  CA    . ILE B 173 ? 0.54400 0.48030 0.45650 -0.02770 0.05400  -0.06920 169 ILE B CA    
5212 C  C     . ILE B 173 ? 0.52670 0.45530 0.44910 -0.02200 0.05810  -0.07140 169 ILE B C     
5213 O  O     . ILE B 173 ? 0.44150 0.36990 0.36430 -0.01940 0.06380  -0.07640 169 ILE B O     
5214 C  CB    . ILE B 173 ? 0.56300 0.50950 0.47730 -0.02630 0.05230  -0.06140 169 ILE B CB    
5215 C  CG1   . ILE B 173 ? 0.61370 0.56870 0.51810 -0.03150 0.04950  -0.05980 169 ILE B CG1   
5216 C  CG2   . ILE B 173 ? 0.62090 0.57070 0.54000 -0.02160 0.05750  -0.06160 169 ILE B CG2   
5217 C  CD1   . ILE B 173 ? 0.65500 0.60980 0.54880 -0.03580 0.05180  -0.06760 169 ILE B CD1   
5218 N  N     . ALA B 174 ? 0.42720 0.34970 0.35780 -0.02000 0.05540  -0.06750 170 ALA B N     
5219 C  CA    . ALA B 174 ? 0.43000 0.34740 0.37160 -0.01400 0.05810  -0.06660 170 ALA B CA    
5220 C  C     . ALA B 174 ? 0.46730 0.37620 0.41010 -0.01240 0.06360  -0.07520 170 ALA B C     
5221 O  O     . ALA B 174 ? 0.45500 0.36330 0.40500 -0.00720 0.06820  -0.07630 170 ALA B O     
5222 C  CB    . ALA B 174 ? 0.42280 0.33550 0.37150 -0.01300 0.05370  -0.06050 170 ALA B CB    
5223 N  N     . LYS B 175 ? 0.49830 0.40080 0.43440 -0.01680 0.06340  -0.08170 171 LYS B N     
5224 C  CA    . LYS B 175 ? 0.55250 0.44520 0.49000 -0.01530 0.06840  -0.09050 171 LYS B CA    
5225 C  C     . LYS B 175 ? 0.54990 0.44560 0.47620 -0.01820 0.07260  -0.09930 171 LYS B C     
5226 O  O     . LYS B 175 ? 0.54640 0.43350 0.47090 -0.01860 0.07640  -0.10840 171 LYS B O     
5227 C  CB    . LYS B 175 ? 0.58940 0.47060 0.52930 -0.01780 0.06560  -0.09210 171 LYS B CB    
5228 C  CG    . LYS B 175 ? 0.70310 0.57950 0.65590 -0.01340 0.06370  -0.08480 171 LYS B CG    
5229 C  CD    . LYS B 175 ? 0.63790 0.50230 0.59430 -0.01550 0.06150  -0.08610 171 LYS B CD    
5230 C  CE    . LYS B 175 ? 0.68030 0.53310 0.64190 -0.01260 0.06680  -0.09400 171 LYS B CE    
5231 N  NZ    . LYS B 175 ? 0.75120 0.59200 0.72030 -0.01320 0.06450  -0.09260 171 LYS B NZ    
5232 N  N     . HIS B 176 ? 0.54890 0.45640 0.46780 -0.02020 0.07220  -0.09700 172 HIS B N     
5233 C  CA    . HIS B 176 ? 0.52560 0.43730 0.43430 -0.02230 0.07680  -0.10470 172 HIS B CA    
5234 C  C     . HIS B 176 ? 0.49790 0.40970 0.41290 -0.01590 0.08430  -0.10820 172 HIS B C     
5235 O  O     . HIS B 176 ? 0.49470 0.40920 0.42050 -0.01060 0.08490  -0.10190 172 HIS B O     
5236 C  CB    . HIS B 176 ? 0.58480 0.50970 0.48440 -0.02610 0.07420  -0.10010 172 HIS B CB    
5237 C  CG    . HIS B 176 ? 0.67260 0.59870 0.56440 -0.03280 0.06760  -0.09810 172 HIS B CG    
5238 N  ND1   . HIS B 176 ? 0.67450 0.61160 0.56060 -0.03610 0.06370  -0.09180 172 HIS B ND1   
5239 C  CD2   . HIS B 176 ? 0.65440 0.57240 0.54410 -0.03670 0.06420  -0.10110 172 HIS B CD2   
5240 C  CE1   . HIS B 176 ? 0.61490 0.55100 0.49580 -0.04150 0.05820  -0.09100 172 HIS B CE1   
5241 N  NE2   . HIS B 176 ? 0.65000 0.57490 0.53290 -0.04220 0.05840  -0.09660 172 HIS B NE2   
5242 N  N     . PRO B 177 ? 0.60670 0.51580 0.51530 -0.01640 0.09020  -0.11850 173 PRO B N     
5243 C  CA    . PRO B 177 ? 0.56830 0.47820 0.48310 -0.01010 0.09810  -0.12240 173 PRO B CA    
5244 C  C     . PRO B 177 ? 0.58210 0.50690 0.49420 -0.00940 0.10030  -0.11800 173 PRO B C     
5245 O  O     . PRO B 177 ? 0.65190 0.58540 0.55230 -0.01470 0.09820  -0.11700 173 PRO B O     
5246 C  CB    . PRO B 177 ? 0.55830 0.46080 0.46500 -0.01190 0.10340  -0.13560 173 PRO B CB    
5247 C  CG    . PRO B 177 ? 0.64820 0.54550 0.54490 -0.01940 0.09760  -0.13830 173 PRO B CG    
5248 C  CD    . PRO B 177 ? 0.60610 0.51130 0.50160 -0.02280 0.08980  -0.12730 173 PRO B CD    
5249 N  N     . VAL B 178 ? 0.55100 0.47900 0.47470 -0.00280 0.10420  -0.11460 174 VAL B N     
5250 C  CA    . VAL B 178 ? 0.52250 0.46430 0.44590 -0.00140 0.10720  -0.11050 174 VAL B CA    
5251 C  C     . VAL B 178 ? 0.52090 0.46280 0.45310 0.00530  0.11580  -0.11520 174 VAL B C     
5252 O  O     . VAL B 178 ? 0.57110 0.50260 0.51310 0.00990  0.11800  -0.11840 174 VAL B O     
5253 C  CB    . VAL B 178 ? 0.46300 0.41170 0.39390 -0.00060 0.10150  -0.09820 174 VAL B CB    
5254 C  CG1   . VAL B 178 ? 0.46100 0.40890 0.38510 -0.00650 0.09310  -0.09350 174 VAL B CG1   
5255 C  CG2   . VAL B 178 ? 0.43730 0.38050 0.38460 0.00600  0.10160  -0.09430 174 VAL B CG2   
5256 N  N     . PRO B 179 ? 0.62600 0.57970 0.55520 0.00600  0.12090  -0.11530 175 PRO B N     
5257 C  CA    . PRO B 179 ? 0.58370 0.53940 0.52300 0.01290  0.12920  -0.11840 175 PRO B CA    
5258 C  C     . PRO B 179 ? 0.52570 0.48100 0.48300 0.01880  0.12710  -0.10970 175 PRO B C     
5259 O  O     . PRO B 179 ? 0.51350 0.47410 0.47390 0.01730  0.12080  -0.09970 175 PRO B O     
5260 C  CB    . PRO B 179 ? 0.61040 0.58150 0.54240 0.01120  0.13350  -0.11750 175 PRO B CB    
5261 C  CG    . PRO B 179 ? 0.58940 0.56380 0.50460 0.00290  0.12850  -0.11740 175 PRO B CG    
5262 C  CD    . PRO B 179 ? 0.58600 0.55250 0.50390 0.00070  0.11930  -0.11150 175 PRO B CD    
5263 N  N     . LEU B 180 ? 0.50010 0.44880 0.46930 0.02530  0.13230  -0.11350 176 LEU B N     
5264 C  CA    . LEU B 180 ? 0.54670 0.49500 0.53350 0.03120  0.13050  -0.10560 176 LEU B CA    
5265 C  C     . LEU B 180 ? 0.54160 0.50480 0.53490 0.03390  0.13360  -0.09960 176 LEU B C     
5266 O  O     . LEU B 180 ? 0.53120 0.49870 0.53020 0.03860  0.14170  -0.10380 176 LEU B O     
5267 C  CB    . LEU B 180 ? 0.56420 0.50050 0.56210 0.03740  0.13490  -0.11140 176 LEU B CB    
5268 C  CG    . LEU B 180 ? 0.59060 0.52690 0.60780 0.04420  0.13410  -0.10370 176 LEU B CG    
5269 C  CD1   . LEU B 180 ? 0.45460 0.38990 0.47480 0.04190  0.12430  -0.09320 176 LEU B CD1   
5270 C  CD2   . LEU B 180 ? 0.61680 0.54040 0.64420 0.05000  0.13870  -0.11020 176 LEU B CD2   
5271 N  N     . GLU B 181 ? 0.52780 0.49910 0.52100 0.03090  0.12730  -0.08980 177 GLU B N     
5272 C  CA    . GLU B 181 ? 0.56840 0.55440 0.56640 0.03190  0.12910  -0.08340 177 GLU B CA    
5273 C  C     . GLU B 181 ? 0.54090 0.52860 0.55090 0.03350  0.12230  -0.07250 177 GLU B C     
5274 O  O     . GLU B 181 ? 0.50680 0.49620 0.51180 0.02900  0.11500  -0.06640 177 GLU B O     
5275 C  CB    . GLU B 181 ? 0.63020 0.62540 0.61330 0.02530  0.12810  -0.08270 177 GLU B CB    
5276 C  CG    . GLU B 181 ? 0.81660 0.82610 0.80060 0.02620  0.13450  -0.08170 177 GLU B CG    
5277 C  CD    . GLU B 181 ? 0.93130 0.94070 0.91100 0.02850  0.14440  -0.09260 177 GLU B CD    
5278 O  OE1   . GLU B 181 ? 0.93110 0.94970 0.91840 0.03260  0.15150  -0.09270 177 GLU B OE1   
5279 O  OE2   . GLU B 181 ? 0.96180 0.96180 0.93060 0.02610  0.14500  -0.10120 177 GLU B OE2   
5280 N  N     . VAL B 182 ? 0.52240 0.51030 0.54830 0.04000  0.12480  -0.07030 178 VAL B N     
5281 C  CA    . VAL B 182 ? 0.54130 0.53100 0.57960 0.04200  0.11870  -0.06040 178 VAL B CA    
5282 C  C     . VAL B 182 ? 0.48940 0.49240 0.53920 0.04550  0.12250  -0.05570 178 VAL B C     
5283 O  O     . VAL B 182 ? 0.45530 0.46100 0.51120 0.05010  0.13070  -0.06040 178 VAL B O     
5284 C  CB    . VAL B 182 ? 0.56820 0.54600 0.61650 0.04640  0.11700  -0.06070 178 VAL B CB    
5285 C  CG1   . VAL B 182 ? 0.49070 0.47200 0.55160 0.04850  0.11090  -0.05030 178 VAL B CG1   
5286 C  CG2   . VAL B 182 ? 0.55280 0.51800 0.59030 0.04250  0.11290  -0.06470 178 VAL B CG2   
5287 N  N     . PHE B 183 ? 0.48110 0.49210 0.53440 0.04330  0.11680  -0.04640 179 PHE B N     
5288 C  CA    . PHE B 183 ? 0.49390 0.51870 0.55720 0.04510  0.11920  -0.04080 179 PHE B CA    
5289 C  C     . PHE B 183 ? 0.43100 0.45700 0.50940 0.04810  0.11380  -0.03240 179 PHE B C     
5290 O  O     . PHE B 183 ? 0.42240 0.44110 0.49960 0.04660  0.10640  -0.02910 179 PHE B O     
5291 C  CB    . PHE B 183 ? 0.42200 0.45660 0.47610 0.03890  0.11690  -0.03680 179 PHE B CB    
5292 C  CG    . PHE B 183 ? 0.43480 0.47130 0.47430 0.03550  0.12220  -0.04370 179 PHE B CG    
5293 C  CD1   . PHE B 183 ? 0.46000 0.48750 0.48490 0.03140  0.11960  -0.04850 179 PHE B CD1   
5294 C  CD2   . PHE B 183 ? 0.53320 0.58140 0.57360 0.03630  0.12970  -0.04500 179 PHE B CD2   
5295 C  CE1   . PHE B 183 ? 0.49010 0.52000 0.50110 0.02790  0.12390  -0.05470 179 PHE B CE1   
5296 C  CE2   . PHE B 183 ? 0.53120 0.58190 0.55730 0.03290  0.13460  -0.05120 179 PHE B CE2   
5297 C  CZ    . PHE B 183 ? 0.47770 0.51930 0.48890 0.02860  0.13140  -0.05600 179 PHE B CZ    
5298 N  N     . PRO B 184 ? 0.45430 0.49000 0.54720 0.05240  0.11750  -0.02890 180 PRO B N     
5299 C  CA    . PRO B 184 ? 0.40770 0.44700 0.51410 0.05410  0.11140  -0.01980 180 PRO B CA    
5300 C  C     . PRO B 184 ? 0.41370 0.45870 0.51480 0.04810  0.10410  -0.01300 180 PRO B C     
5301 O  O     . PRO B 184 ? 0.37240 0.42310 0.46400 0.04360  0.10550  -0.01370 180 PRO B O     
5302 C  CB    . PRO B 184 ? 0.44620 0.49650 0.56840 0.05960  0.11810  -0.01820 180 PRO B CB    
5303 C  CG    . PRO B 184 ? 0.45290 0.50910 0.56760 0.05880  0.12660  -0.02440 180 PRO B CG    
5304 C  CD    . PRO B 184 ? 0.46060 0.50530 0.55800 0.05570  0.12720  -0.03270 180 PRO B CD    
5305 N  N     . PRO B 185 ? 0.45530 0.49870 0.56190 0.04750  0.09600  -0.00630 181 PRO B N     
5306 C  CA    . PRO B 185 ? 0.42570 0.47300 0.52690 0.04160  0.08880  -0.00050 181 PRO B CA    
5307 C  C     . PRO B 185 ? 0.46780 0.52850 0.57230 0.03940  0.09090  0.00330  181 PRO B C     
5308 O  O     . PRO B 185 ? 0.50380 0.56670 0.59960 0.03390  0.08740  0.00540  181 PRO B O     
5309 C  CB    . PRO B 185 ? 0.44010 0.48520 0.55020 0.04290  0.08130  0.00580  181 PRO B CB    
5310 C  CG    . PRO B 185 ? 0.39900 0.43410 0.51230 0.04770  0.08300  0.00220  181 PRO B CG    
5311 C  CD    . PRO B 185 ? 0.42510 0.46180 0.54160 0.05180  0.09290  -0.00410 181 PRO B CD    
5312 N  N     . MET B 186 ? 0.44240 0.51260 0.56000 0.04350  0.09650  0.00460  182 MET B N     
5313 C  CA    . MET B 186 ? 0.43530 0.51930 0.55770 0.04100  0.09790  0.00950  182 MET B CA    
5314 C  C     . MET B 186 ? 0.42670 0.51420 0.53670 0.03750  0.10320  0.00540  182 MET B C     
5315 O  O     . MET B 186 ? 0.43830 0.53530 0.54810 0.03340  0.10260  0.01010  182 MET B O     
5316 C  CB    . MET B 186 ? 0.49050 0.58440 0.63070 0.04650  0.10300  0.01200  182 MET B CB    
5317 C  CG    . MET B 186 ? 0.65120 0.74420 0.79300 0.05210  0.11320  0.00440  182 MET B CG    
5318 S  SD    . MET B 186 ? 0.75490 0.86450 0.91540 0.05720  0.12160  0.00710  182 MET B SD    
5319 C  CE    . MET B 186 ? 0.68140 0.80410 0.83540 0.05020  0.12240  0.01100  182 MET B CE    
5320 N  N     . ASN B 187 ? 0.42350 0.50320 0.52250 0.03830  0.10790  -0.00280 183 ASN B N     
5321 C  CA    . ASN B 187 ? 0.38140 0.46470 0.46760 0.03490  0.11300  -0.00700 183 ASN B CA    
5322 C  C     . ASN B 187 ? 0.39330 0.47340 0.46570 0.02800  0.10650  -0.00490 183 ASN B C     
5323 O  O     . ASN B 187 ? 0.41290 0.49990 0.47740 0.02400  0.10910  -0.00460 183 ASN B O     
5324 C  CB    . ASN B 187 ? 0.47840 0.55410 0.55730 0.03790  0.12000  -0.01710 183 ASN B CB    
5325 C  CG    . ASN B 187 ? 0.55320 0.63550 0.64300 0.04400  0.12950  -0.02050 183 ASN B CG    
5326 O  OD1   . ASN B 187 ? 0.59560 0.67050 0.68450 0.04820  0.13480  -0.02830 183 ASN B OD1   
5327 N  ND2   . ASN B 187 ? 0.55680 0.65290 0.65740 0.04460  0.13190  -0.01470 183 ASN B ND2   
5328 N  N     . TYR B 188 ? 0.29800 0.36860 0.36760 0.02650  0.09840  -0.00320 184 TYR B N     
5329 C  CA    . TYR B 188 ? 0.36200 0.42840 0.41830 0.02060  0.09290  -0.00220 184 TYR B CA    
5330 C  C     . TYR B 188 ? 0.37420 0.44060 0.43450 0.01780  0.08400  0.00530  184 TYR B C     
5331 O  O     . TYR B 188 ? 0.36170 0.42260 0.41230 0.01370  0.07850  0.00600  184 TYR B O     
5332 C  CB    . TYR B 188 ? 0.33450 0.38820 0.37970 0.02050  0.09190  -0.00880 184 TYR B CB    
5333 C  CG    . TYR B 188 ? 0.34770 0.39190 0.39950 0.02440  0.08860  -0.00950 184 TYR B CG    
5334 C  CD1   . TYR B 188 ? 0.33740 0.37640 0.38930 0.02270  0.08020  -0.00500 184 TYR B CD1   
5335 C  CD2   . TYR B 188 ? 0.33680 0.37710 0.39440 0.02980  0.09400  -0.01450 184 TYR B CD2   
5336 C  CE1   . TYR B 188 ? 0.31190 0.34300 0.36920 0.02590  0.07720  -0.00500 184 TYR B CE1   
5337 C  CE2   . TYR B 188 ? 0.36290 0.39460 0.42680 0.03320  0.09090  -0.01430 184 TYR B CE2   
5338 C  CZ    . TYR B 188 ? 0.42080 0.44830 0.48420 0.03110  0.08240  -0.00930 184 TYR B CZ    
5339 O  OH    . TYR B 188 ? 0.43180 0.45160 0.50110 0.03420  0.07930  -0.00840 184 TYR B OH    
5340 N  N     . ARG B 189 ? 0.26090 0.33310 0.33500 0.01970  0.08230  0.01070  185 ARG B N     
5341 C  CA    . ARG B 189 ? 0.45440 0.52820 0.53220 0.01640  0.07440  0.01760  185 ARG B CA    
5342 C  C     . ARG B 189 ? 0.47300 0.55850 0.56530 0.01740  0.07560  0.02330  185 ARG B C     
5343 O  O     . ARG B 189 ? 0.47100 0.56100 0.57300 0.02210  0.08090  0.02220  185 ARG B O     
5344 C  CB    . ARG B 189 ? 0.38190 0.44570 0.45980 0.01730  0.06720  0.01820  185 ARG B CB    
5345 C  CG    . ARG B 189 ? 0.43950 0.49970 0.52620 0.02290  0.06830  0.01660  185 ARG B CG    
5346 C  CD    . ARG B 189 ? 0.41390 0.46260 0.49480 0.02260  0.06190  0.01580  185 ARG B CD    
5347 N  NE    . ARG B 189 ? 0.55710 0.60170 0.64630 0.02740  0.06140  0.01580  185 ARG B NE    
5348 C  CZ    . ARG B 189 ? 0.58660 0.63520 0.68740 0.02910  0.05750  0.02120  185 ARG B CZ    
5349 N  NH1   . ARG B 189 ? 0.50970 0.56640 0.61540 0.02620  0.05390  0.02660  185 ARG B NH1   
5350 N  NH2   . ARG B 189 ? 0.57950 0.62420 0.68730 0.03350  0.05710  0.02140  185 ARG B NH2   
5351 N  N     . GLY B 190 ? 0.44380 0.53420 0.53810 0.01290  0.07060  0.02940  186 GLY B N     
5352 C  CA    . GLY B 190 ? 0.32220 0.42480 0.42970 0.01240  0.07130  0.03540  186 GLY B CA    
5353 C  C     . GLY B 190 ? 0.34050 0.44350 0.45990 0.01360  0.06500  0.03990  186 GLY B C     
5354 O  O     . GLY B 190 ? 0.39950 0.49350 0.51720 0.01530  0.06050  0.03830  186 GLY B O     
5355 N  N     . GLY B 191 ? 0.34430 0.45850 0.47590 0.01240  0.06470  0.04580  187 GLY B N     
5356 C  CA    . GLY B 191 ? 0.39160 0.50840 0.53550 0.01300  0.05870  0.05060  187 GLY B CA    
5357 C  C     . GLY B 191 ? 0.40200 0.51460 0.54240 0.00740  0.04940  0.05410  187 GLY B C     
5358 O  O     . GLY B 191 ? 0.38480 0.49020 0.51280 0.00400  0.04710  0.05230  187 GLY B O     
5359 N  N     . LYS B 192 ? 0.32180 0.43910 0.47350 0.00670  0.04390  0.05920  188 LYS B N     
5360 C  CA    . LYS B 192 ? 0.42310 0.53590 0.57250 0.00180  0.03460  0.06190  188 LYS B CA    
5361 C  C     . LYS B 192 ? 0.35200 0.47360 0.50790 -0.00360 0.03280  0.06750  188 LYS B C     
5362 O  O     . LYS B 192 ? 0.36160 0.49520 0.52910 -0.00300 0.03690  0.07110  188 LYS B O     
5363 C  CB    . LYS B 192 ? 0.46800 0.57970 0.62470 0.00370  0.02850  0.06360  188 LYS B CB    
5364 C  CG    . LYS B 192 ? 0.58710 0.69150 0.74030 0.00940  0.03060  0.05930  188 LYS B CG    
5365 C  CD    . LYS B 192 ? 0.65020 0.74960 0.80410 0.00970  0.02270  0.06060  188 LYS B CD    
5366 C  CE    . LYS B 192 ? 0.72170 0.80840 0.86280 0.01170  0.02230  0.05540  188 LYS B CE    
5367 N  NZ    . LYS B 192 ? 0.74800 0.82830 0.88360 0.00900  0.01370  0.05600  188 LYS B NZ    
5368 N  N     . PRO B 193 ? 0.29340 0.40920 0.44260 -0.00890 0.02680  0.06840  189 PRO B N     
5369 C  CA    . PRO B 193 ? 0.29490 0.41810 0.45100 -0.01450 0.02450  0.07410  189 PRO B CA    
5370 C  C     . PRO B 193 ? 0.33370 0.46310 0.50330 -0.01600 0.01850  0.07880  189 PRO B C     
5371 O  O     . PRO B 193 ? 0.28780 0.41230 0.45750 -0.01470 0.01300  0.07760  189 PRO B O     
5372 C  CB    . PRO B 193 ? 0.25310 0.36600 0.39740 -0.01900 0.01970  0.07290  189 PRO B CB    
5373 C  CG    . PRO B 193 ? 0.28300 0.38410 0.41800 -0.01610 0.01640  0.06760  189 PRO B CG    
5374 C  CD    . PRO B 193 ? 0.29070 0.39310 0.42580 -0.01000 0.02280  0.06420  189 PRO B CD    
5375 N  N     . ALA B 194 ? 0.29930 0.44030 0.48020 -0.01910 0.01950  0.08450  190 ALA B N     
5376 C  CA    . ALA B 194 ? 0.24580 0.39490 0.44090 -0.02160 0.01400  0.08990  190 ALA B CA    
5377 C  C     . ALA B 194 ? 0.30530 0.45400 0.50180 -0.02920 0.00810  0.09380  190 ALA B C     
5378 O  O     . ALA B 194 ? 0.29680 0.44200 0.48580 -0.03210 0.01000  0.09360  190 ALA B O     
5379 C  CB    . ALA B 194 ? 0.26650 0.43110 0.47660 -0.01870 0.02050  0.09390  190 ALA B CB    
5380 N  N     . PRO B 195 ? 0.28420 0.43640 0.49040 -0.03270 0.00070  0.09750  191 PRO B N     
5381 C  CA    . PRO B 195 ? 0.29750 0.45000 0.50710 -0.04030 -0.00480 0.10160  191 PRO B CA    
5382 C  C     . PRO B 195 ? 0.28060 0.44710 0.50160 -0.04270 0.00050  0.10790  191 PRO B C     
5383 O  O     . PRO B 195 ? 0.29180 0.46990 0.52150 -0.03880 0.00710  0.10980  191 PRO B O     
5384 C  CB    . PRO B 195 ? 0.29040 0.44370 0.50760 -0.04280 -0.01390 0.10310  191 PRO B CB    
5385 C  CG    . PRO B 195 ? 0.31370 0.47670 0.54020 -0.03700 -0.01050 0.10420  191 PRO B CG    
5386 C  CD    . PRO B 195 ? 0.26250 0.41970 0.47830 -0.03020 -0.00290 0.09880  191 PRO B CD    
5387 N  N     . THR B 196 ? 0.26520 0.43060 0.48660 -0.04930 -0.00230 0.11140  192 THR B N     
5388 C  CA    . THR B 196 ? 0.29280 0.47170 0.52580 -0.05290 0.00160  0.11850  192 THR B CA    
5389 C  C     . THR B 196 ? 0.33340 0.52320 0.58370 -0.05600 -0.00330 0.12410  192 THR B C     
5390 O  O     . THR B 196 ? 0.28640 0.47120 0.53810 -0.05740 -0.01160 0.12270  192 THR B O     
5391 C  CB    . THR B 196 ? 0.34280 0.51660 0.57120 -0.05930 -0.00020 0.12120  192 THR B CB    
5392 O  OG1   . THR B 196 ? 0.35800 0.52360 0.58810 -0.06490 -0.01050 0.12170  192 THR B OG1   
5393 C  CG2   . THR B 196 ? 0.32590 0.48850 0.53710 -0.05680 0.00340  0.11610  192 THR B CG2   
5394 N  N     . ILE B 197 ? 0.27090 0.47650 0.53430 -0.05720 0.00190  0.13050  193 ILE B N     
5395 C  CA    . ILE B 197 ? 0.31770 0.53540 0.59900 -0.06070 -0.00260 0.13670  193 ILE B CA    
5396 C  C     . ILE B 197 ? 0.33110 0.54190 0.61390 -0.06930 -0.01310 0.13900  193 ILE B C     
5397 O  O     . ILE B 197 ? 0.35420 0.56640 0.64480 -0.07170 -0.02090 0.14000  193 ILE B O     
5398 C  CB    . ILE B 197 ? 0.42960 0.66600 0.72470 -0.06080 0.00550  0.14360  193 ILE B CB    
5399 C  CG1   . ILE B 197 ? 0.51870 0.76180 0.81340 -0.05180 0.01570  0.14050  193 ILE B CG1   
5400 C  CG2   . ILE B 197 ? 0.42880 0.67830 0.74340 -0.06480 0.00040  0.15050  193 ILE B CG2   
5401 C  CD1   . ILE B 197 ? 0.53840 0.78760 0.84390 -0.04690 0.01390  0.14030  193 ILE B CD1   
5402 N  N     . MET B 198 ? 0.30990 0.51210 0.58470 -0.07390 -0.01390 0.13920  194 MET B N     
5403 C  CA    . MET B 198 ? 0.40540 0.59910 0.68150 -0.08160 -0.02410 0.14040  194 MET B CA    
5404 C  C     . MET B 198 ? 0.36380 0.54560 0.63310 -0.08070 -0.03240 0.13400  194 MET B C     
5405 O  O     . MET B 198 ? 0.36410 0.54580 0.64070 -0.08580 -0.04100 0.13540  194 MET B O     
5406 C  CB    . MET B 198 ? 0.60950 0.78950 0.87380 -0.08490 -0.02510 0.13880  194 MET B CB    
5407 C  CG    . MET B 198 ? 0.77620 0.95420 1.04820 -0.09410 -0.03190 0.14410  194 MET B CG    
5408 S  SD    . MET B 198 ? 0.88950 1.06330 1.15680 -0.09820 -0.02840 0.14840  194 MET B SD    
5409 C  CE    . MET B 198 ? 0.85310 1.00490 1.10000 -0.09410 -0.03160 0.13810  194 MET B CE    
5410 N  N     . ASP B 199 ? 0.23670 0.40790 0.49120 -0.07470 -0.03000 0.12690  195 ASP B N     
5411 C  CA    . ASP B 199 ? 0.31890 0.47700 0.56450 -0.07460 -0.03780 0.12070  195 ASP B CA    
5412 C  C     . ASP B 199 ? 0.32930 0.49490 0.58280 -0.07250 -0.04130 0.12090  195 ASP B C     
5413 O  O     . ASP B 199 ? 0.36720 0.52820 0.62110 -0.07600 -0.05030 0.11930  195 ASP B O     
5414 C  CB    . ASP B 199 ? 0.34650 0.49180 0.57450 -0.06910 -0.03430 0.11350  195 ASP B CB    
5415 C  CG    . ASP B 199 ? 0.54250 0.67740 0.76170 -0.07230 -0.03380 0.11280  195 ASP B CG    
5416 O  OD1   . ASP B 199 ? 0.58440 0.71890 0.81000 -0.07910 -0.03810 0.11700  195 ASP B OD1   
5417 O  OD2   . ASP B 199 ? 0.55560 0.68250 0.76180 -0.06810 -0.02960 0.10840  195 ASP B OD2   
5418 N  N     . VAL B 200 ? 0.26230 0.44040 0.52330 -0.06700 -0.03450 0.12330  196 VAL B N     
5419 C  CA    . VAL B 200 ? 0.29530 0.48260 0.56660 -0.06490 -0.03760 0.12510  196 VAL B CA    
5420 C  C     . VAL B 200 ? 0.32870 0.52450 0.61450 -0.07260 -0.04530 0.13100  196 VAL B C     
5421 O  O     . VAL B 200 ? 0.37690 0.57050 0.66390 -0.07520 -0.05410 0.13000  196 VAL B O     
5422 C  CB    . VAL B 200 ? 0.33330 0.53340 0.61240 -0.05770 -0.02800 0.12740  196 VAL B CB    
5423 C  CG1   . VAL B 200 ? 0.34170 0.55360 0.63510 -0.05620 -0.03160 0.13110  196 VAL B CG1   
5424 C  CG2   . VAL B 200 ? 0.24590 0.43680 0.51050 -0.05020 -0.02140 0.12070  196 VAL B CG2   
5425 N  N     . VAL B 201 ? 0.29320 0.49860 0.58970 -0.07680 -0.04220 0.13730  197 VAL B N     
5426 C  CA    . VAL B 201 ? 0.33660 0.55080 0.64820 -0.08460 -0.04930 0.14360  197 VAL B CA    
5427 C  C     . VAL B 201 ? 0.32710 0.52690 0.63130 -0.09160 -0.05960 0.14010  197 VAL B C     
5428 O  O     . VAL B 201 ? 0.30540 0.50790 0.61710 -0.09670 -0.06860 0.14160  197 VAL B O     
5429 C  CB    . VAL B 201 ? 0.38070 0.60730 0.70430 -0.08800 -0.04340 0.15120  197 VAL B CB    
5430 C  CG1   . VAL B 201 ? 0.37400 0.60970 0.71380 -0.09660 -0.05100 0.15790  197 VAL B CG1   
5431 C  CG2   . VAL B 201 ? 0.44360 0.68470 0.77430 -0.08080 -0.03270 0.15380  197 VAL B CG2   
5432 N  N     . ARG B 202 ? 0.28240 0.46700 0.57210 -0.09210 -0.05880 0.13540  198 ARG B N     
5433 C  CA    . ARG B 202 ? 0.39620 0.56660 0.67920 -0.09820 -0.06830 0.13140  198 ARG B CA    
5434 C  C     . ARG B 202 ? 0.37900 0.54220 0.65380 -0.09610 -0.07490 0.12510  198 ARG B C     
5435 O  O     . ARG B 202 ? 0.33810 0.49720 0.61430 -0.10210 -0.08440 0.12380  198 ARG B O     
5436 C  CB    . ARG B 202 ? 0.46670 0.62270 0.73740 -0.09900 -0.06600 0.12830  198 ARG B CB    
5437 C  CG    . ARG B 202 ? 0.62670 0.76740 0.89030 -0.10420 -0.07550 0.12310  198 ARG B CG    
5438 C  CD    . ARG B 202 ? 0.78250 0.92460 1.05740 -0.11320 -0.07980 0.12870  198 ARG B CD    
5439 N  NE    . ARG B 202 ? 0.85680 0.98380 1.12640 -0.11890 -0.08890 0.12390  198 ARG B NE    
5440 C  CZ    . ARG B 202 ? 0.93460 1.06180 1.21480 -0.12770 -0.09570 0.12740  198 ARG B CZ    
5441 N  NH1   . ARG B 202 ? 0.96640 1.10940 1.26340 -0.13170 -0.09470 0.13630  198 ARG B NH1   
5442 N  NH2   . ARG B 202 ? 0.95400 1.06610 1.22840 -0.13240 -0.10360 0.12190  198 ARG B NH2   
5443 N  N     . VAL B 203 ? 0.35510 0.51650 0.62090 -0.08800 -0.07020 0.12100  199 VAL B N     
5444 C  CA    . VAL B 203 ? 0.30580 0.46180 0.56410 -0.08590 -0.07620 0.11580  199 VAL B CA    
5445 C  C     . VAL B 203 ? 0.33100 0.50080 0.60360 -0.08820 -0.08180 0.12070  199 VAL B C     
5446 O  O     . VAL B 203 ? 0.31770 0.48410 0.58830 -0.09210 -0.09100 0.11840  199 VAL B O     
5447 C  CB    . VAL B 203 ? 0.31700 0.46850 0.56370 -0.07690 -0.06950 0.11120  199 VAL B CB    
5448 C  CG1   . VAL B 203 ? 0.26680 0.41600 0.50820 -0.07450 -0.07530 0.10770  199 VAL B CG1   
5449 C  CG2   . VAL B 203 ? 0.30370 0.43990 0.53470 -0.07550 -0.06600 0.10560  199 VAL B CG2   
5450 N  N     . ALA B 204 ? 0.30960 0.49590 0.59710 -0.08580 -0.07640 0.12750  200 ALA B N     
5451 C  CA    . ALA B 204 ? 0.38340 0.58440 0.68640 -0.08780 -0.08160 0.13310  200 ALA B CA    
5452 C  C     . ALA B 204 ? 0.41420 0.61600 0.72450 -0.09800 -0.09140 0.13550  200 ALA B C     
5453 O  O     . ALA B 204 ? 0.39750 0.60180 0.71080 -0.10140 -0.10040 0.13560  200 ALA B O     
5454 C  CB    . ALA B 204 ? 0.35880 0.57740 0.67760 -0.08360 -0.07310 0.14030  200 ALA B CB    
5455 N  N     . GLU B 205 ? 0.39160 0.59080 0.70460 -0.10330 -0.09000 0.13750  201 GLU B N     
5456 C  CA    . GLU B 205 ? 0.37280 0.57120 0.69280 -0.11350 -0.09930 0.13960  201 GLU B CA    
5457 C  C     . GLU B 205 ? 0.38970 0.57140 0.69530 -0.11690 -0.10850 0.13130  201 GLU B C     
5458 O  O     . GLU B 205 ? 0.43580 0.61900 0.74630 -0.12360 -0.11830 0.13160  201 GLU B O     
5459 C  CB    . GLU B 205 ? 0.44380 0.64090 0.76820 -0.11800 -0.09550 0.14330  201 GLU B CB    
5460 C  CG    . GLU B 205 ? 0.71810 0.91310 1.05060 -0.12900 -0.10450 0.14570  201 GLU B CG    
5461 C  CD    . GLU B 205 ? 0.92960 1.11060 1.25510 -0.13260 -0.10330 0.14400  201 GLU B CD    
5462 O  OE1   . GLU B 205 ? 0.98980 1.16160 1.31560 -0.14060 -0.11160 0.14240  201 GLU B OE1   
5463 O  OE2   . GLU B 205 ? 0.93840 1.11700 1.25740 -0.12730 -0.09410 0.14390  201 GLU B OE2   
5464 N  N     . LEU B 206 ? 0.38710 0.55310 0.67480 -0.11240 -0.10540 0.12380  202 LEU B N     
5465 C  CA    . LEU B 206 ? 0.38890 0.53920 0.66240 -0.11510 -0.11330 0.11560  202 LEU B CA    
5466 C  C     . LEU B 206 ? 0.41230 0.56730 0.68390 -0.11370 -0.11930 0.11380  202 LEU B C     
5467 O  O     . LEU B 206 ? 0.41920 0.56900 0.68720 -0.11940 -0.12890 0.11010  202 LEU B O     
5468 C  CB    . LEU B 206 ? 0.30760 0.44160 0.56330 -0.11000 -0.10810 0.10840  202 LEU B CB    
5469 C  CG    . LEU B 206 ? 0.35850 0.48250 0.61250 -0.11370 -0.10620 0.10820  202 LEU B CG    
5470 C  CD1   . LEU B 206 ? 0.32650 0.43900 0.56540 -0.10690 -0.09890 0.10320  202 LEU B CD1   
5471 C  CD2   . LEU B 206 ? 0.34610 0.45910 0.59870 -0.12220 -0.11580 0.10460  202 LEU B CD2   
5472 N  N     . ILE B 207 ? 0.36610 0.53080 0.64010 -0.10610 -0.11400 0.11640  203 ILE B N     
5473 C  CA    . ILE B 207 ? 0.38040 0.55080 0.65390 -0.10460 -0.11980 0.11600  203 ILE B CA    
5474 C  C     . ILE B 207 ? 0.40910 0.59370 0.69930 -0.11150 -0.12760 0.12250  203 ILE B C     
5475 O  O     . ILE B 207 ? 0.49460 0.67910 0.78220 -0.11560 -0.13710 0.12050  203 ILE B O     
5476 C  CB    . ILE B 207 ? 0.38240 0.55960 0.65600 -0.09480 -0.11200 0.11780  203 ILE B CB    
5477 C  CG1   . ILE B 207 ? 0.37530 0.53780 0.63100 -0.08850 -0.10560 0.11080  203 ILE B CG1   
5478 C  CG2   . ILE B 207 ? 0.40570 0.59080 0.68170 -0.09350 -0.11820 0.11940  203 ILE B CG2   
5479 C  CD1   . ILE B 207 ? 0.31910 0.48730 0.57610 -0.07910 -0.09650 0.11260  203 ILE B CD1   
5480 N  N     . PHE B 208 ? 0.35010 0.54790 0.65780 -0.11310 -0.12380 0.13040  204 PHE B N     
5481 C  CA    . PHE B 208 ? 0.44460 0.65770 0.77020 -0.11960 -0.13080 0.13750  204 PHE B CA    
5482 C  C     . PHE B 208 ? 0.43880 0.64400 0.76170 -0.13010 -0.14220 0.13410  204 PHE B C     
5483 O  O     . PHE B 208 ? 0.42460 0.63850 0.75500 -0.13530 -0.15140 0.13660  204 PHE B O     
5484 C  CB    . PHE B 208 ? 0.53240 0.75950 0.87640 -0.12030 -0.12420 0.14610  204 PHE B CB    
5485 C  CG    . PHE B 208 ? 0.62330 0.86240 0.97440 -0.11080 -0.11370 0.15050  204 PHE B CG    
5486 C  CD1   . PHE B 208 ? 0.61560 0.85700 0.96270 -0.10340 -0.11300 0.14910  204 PHE B CD1   
5487 C  CD2   . PHE B 208 ? 0.65320 0.90140 1.01530 -0.10930 -0.10450 0.15600  204 PHE B CD2   
5488 C  CE1   . PHE B 208 ? 0.62930 0.88080 0.98360 -0.09450 -0.10330 0.15270  204 PHE B CE1   
5489 C  CE2   . PHE B 208 ? 0.59090 0.84980 0.95940 -0.10040 -0.09460 0.15920  204 PHE B CE2   
5490 C  CZ    . PHE B 208 ? 0.60890 0.86890 0.97370 -0.09300 -0.09400 0.15730  204 PHE B CZ    
5491 N  N     . HIS B 209 ? 0.46950 0.65820 0.78160 -0.13320 -0.14210 0.12830  205 HIS B N     
5492 C  CA    . HIS B 209 ? 0.39900 0.57860 0.70900 -0.14320 -0.15210 0.12460  205 HIS B CA    
5493 C  C     . HIS B 209 ? 0.41110 0.57420 0.70090 -0.14300 -0.15760 0.11410  205 HIS B C     
5494 O  O     . HIS B 209 ? 0.45100 0.60540 0.73720 -0.15090 -0.16640 0.10950  205 HIS B O     
5495 C  CB    . HIS B 209 ? 0.43490 0.60710 0.74840 -0.14750 -0.14890 0.12580  205 HIS B CB    
5496 C  CG    . HIS B 209 ? 0.54630 0.73520 0.88020 -0.14950 -0.14460 0.13640  205 HIS B CG    
5497 N  ND1   . HIS B 209 ? 0.59640 0.80230 0.94810 -0.15480 -0.15020 0.14370  205 HIS B ND1   
5498 C  CD2   . HIS B 209 ? 0.55680 0.74880 0.89620 -0.14710 -0.13510 0.14120  205 HIS B CD2   
5499 C  CE1   . HIS B 209 ? 0.58110 0.79860 0.94670 -0.15450 -0.14340 0.15190  205 HIS B CE1   
5500 N  NE2   . HIS B 209 ? 0.59800 0.80860 0.95810 -0.15080 -0.13480 0.15110  205 HIS B NE2   
5501 N  N     . ALA B 210 ? 0.38300 0.54180 0.65970 -0.13430 -0.15260 0.11000  206 ALA B N     
5502 C  CA    . ALA B 210 ? 0.40770 0.55100 0.66450 -0.13350 -0.15650 0.10000  206 ALA B CA    
5503 C  C     . ALA B 210 ? 0.50920 0.65830 0.76470 -0.13740 -0.16690 0.09890  206 ALA B C     
5504 O  O     . ALA B 210 ? 0.55430 0.71950 0.81990 -0.13550 -0.16800 0.10550  206 ALA B O     
5505 C  CB    . ALA B 210 ? 0.32390 0.46170 0.56790 -0.12310 -0.14770 0.09680  206 ALA B CB    
5506 N  N     . LYS B 211 ? 0.48500 0.62130 0.72790 -0.14280 -0.17450 0.09050  207 LYS B N     
5507 C  CA    . LYS B 211 ? 0.49060 0.63150 0.72970 -0.14700 -0.18470 0.08860  207 LYS B CA    
5508 C  C     . LYS B 211 ? 0.49850 0.63330 0.71900 -0.14080 -0.18400 0.08230  207 LYS B C     
5509 O  O     . LYS B 211 ? 0.47930 0.62280 0.69830 -0.14170 -0.19030 0.08370  207 LYS B O     
5510 C  CB    . LYS B 211 ? 0.55170 0.68420 0.78940 -0.15790 -0.19460 0.08330  207 LYS B CB    
5511 C  CG    . LYS B 211 ? 0.64680 0.78860 0.90530 -0.16550 -0.19750 0.09090  207 LYS B CG    
5512 C  CD    . LYS B 211 ? 0.70850 0.87040 0.98110 -0.16810 -0.20290 0.09920  207 LYS B CD    
5513 C  CE    . LYS B 211 ? 0.79700 0.96160 1.08100 -0.17530 -0.20590 0.10260  207 LYS B CE    
5514 N  NZ    . LYS B 211 ? 0.80910 0.99300 1.11270 -0.17330 -0.20180 0.11440  207 LYS B NZ    
5515 N  N     . ARG B 212 ? 0.43190 0.55290 0.63860 -0.13470 -0.17660 0.07630  208 ARG B N     
5516 C  CA    . ARG B 212 ? 0.41830 0.53450 0.60840 -0.12810 -0.17460 0.07140  208 ARG B CA    
5517 C  C     . ARG B 212 ? 0.40340 0.51330 0.58870 -0.11910 -0.16290 0.07090  208 ARG B C     
5518 O  O     . ARG B 212 ? 0.37980 0.47460 0.55100 -0.11700 -0.15980 0.06330  208 ARG B O     
5519 C  CB    . ARG B 212 ? 0.49210 0.59460 0.66440 -0.13230 -0.18120 0.06070  208 ARG B CB    
5520 C  CG    . ARG B 212 ? 0.60040 0.70620 0.76000 -0.12900 -0.18400 0.05870  208 ARG B CG    
5521 C  CD    . ARG B 212 ? 0.73230 0.82880 0.87630 -0.13480 -0.19240 0.04900  208 ARG B CD    
5522 N  NE    . ARG B 212 ? 0.84090 0.94480 0.97580 -0.13370 -0.19710 0.04920  208 ARG B NE    
5523 C  CZ    . ARG B 212 ? 0.91490 1.01060 1.03100 -0.13000 -0.19570 0.04230  208 ARG B CZ    
5524 N  NH1   . ARG B 212 ? 0.91400 0.99380 1.01890 -0.12690 -0.18970 0.03440  208 ARG B NH1   
5525 N  NH2   . ARG B 212 ? 0.93720 1.04100 1.04600 -0.12940 -0.20030 0.04360  208 ARG B NH2   
5526 N  N     . PRO B 213 ? 0.38620 0.50760 0.58320 -0.11370 -0.15620 0.07890  209 PRO B N     
5527 C  CA    . PRO B 213 ? 0.34800 0.46420 0.54030 -0.10530 -0.14530 0.07840  209 PRO B CA    
5528 C  C     . PRO B 213 ? 0.34760 0.46010 0.52560 -0.09870 -0.14340 0.07470  209 PRO B C     
5529 O  O     . PRO B 213 ? 0.33350 0.45180 0.50860 -0.09940 -0.14930 0.07530  209 PRO B O     
5530 C  CB    . PRO B 213 ? 0.34660 0.47810 0.55700 -0.10230 -0.13990 0.08810  209 PRO B CB    
5531 C  CG    . PRO B 213 ? 0.35950 0.50570 0.58010 -0.10560 -0.14770 0.09360  209 PRO B CG    
5532 C  CD    . PRO B 213 ? 0.35670 0.49690 0.57170 -0.11470 -0.15850 0.08850  209 PRO B CD    
5533 N  N     . ALA B 214 ? 0.38510 0.48840 0.55420 -0.09240 -0.13490 0.07140  210 ALA B N     
5534 C  CA    . ALA B 214 ? 0.37120 0.47110 0.52770 -0.08590 -0.13200 0.06860  210 ALA B CA    
5535 C  C     . ALA B 214 ? 0.34410 0.44110 0.50000 -0.07840 -0.12120 0.06950  210 ALA B C     
5536 O  O     . ALA B 214 ? 0.33220 0.42460 0.49100 -0.07890 -0.11650 0.06920  210 ALA B O     
5537 C  CB    . ALA B 214 ? 0.38550 0.47190 0.52360 -0.08780 -0.13600 0.05930  210 ALA B CB    
5538 N  N     . ILE B 215 ? 0.32670 0.42630 0.47870 -0.07180 -0.11750 0.07070  211 ILE B N     
5539 C  CA    . ILE B 215 ? 0.32900 0.42510 0.47830 -0.06460 -0.10760 0.07060  211 ILE B CA    
5540 C  C     . ILE B 215 ? 0.39940 0.48420 0.53090 -0.06140 -0.10660 0.06400  211 ILE B C     
5541 O  O     . ILE B 215 ? 0.33740 0.42350 0.46230 -0.06150 -0.11160 0.06300  211 ILE B O     
5542 C  CB    . ILE B 215 ? 0.31960 0.42810 0.48070 -0.05920 -0.10330 0.07780  211 ILE B CB    
5543 C  CG1   . ILE B 215 ? 0.25950 0.38020 0.43910 -0.06190 -0.10330 0.08450  211 ILE B CG1   
5544 C  CG2   . ILE B 215 ? 0.25680 0.36030 0.41290 -0.05170 -0.09340 0.07640  211 ILE B CG2   
5545 C  CD1   . ILE B 215 ? 0.35870 0.49370 0.55160 -0.05800 -0.10230 0.09190  211 ILE B CD1   
5546 N  N     . LEU B 216 ? 0.31830 0.39290 0.44220 -0.05870 -0.10030 0.05980  212 LEU B N     
5547 C  CA    . LEU B 216 ? 0.29760 0.36280 0.40650 -0.05440 -0.09720 0.05450  212 LEU B CA    
5548 C  C     . LEU B 216 ? 0.35050 0.41690 0.46180 -0.04770 -0.08810 0.05690  212 LEU B C     
5549 O  O     . LEU B 216 ? 0.29180 0.35540 0.40570 -0.04690 -0.08260 0.05680  212 LEU B O     
5550 C  CB    . LEU B 216 ? 0.32240 0.37430 0.42020 -0.05680 -0.09770 0.04710  212 LEU B CB    
5551 C  CG    . LEU B 216 ? 0.33850 0.38120 0.42100 -0.05240 -0.09450 0.04170  212 LEU B CG    
5552 C  CD1   . LEU B 216 ? 0.42810 0.47360 0.50310 -0.05180 -0.09900 0.04090  212 LEU B CD1   
5553 C  CD2   . LEU B 216 ? 0.31540 0.34540 0.38880 -0.05450 -0.09460 0.03470  212 LEU B CD2   
5554 N  N     . ALA B 217 ? 0.30550 0.37620 0.41610 -0.04310 -0.08670 0.05930  213 ALA B N     
5555 C  CA    . ALA B 217 ? 0.33060 0.40300 0.44450 -0.03680 -0.07850 0.06160  213 ALA B CA    
5556 C  C     . ALA B 217 ? 0.35530 0.41770 0.45490 -0.03300 -0.07510 0.05670  213 ALA B C     
5557 O  O     . ALA B 217 ? 0.28150 0.34130 0.37190 -0.03330 -0.07920 0.05460  213 ALA B O     
5558 C  CB    . ALA B 217 ? 0.24610 0.32990 0.37110 -0.03370 -0.07870 0.06820  213 ALA B CB    
5559 N  N     . GLY B 218 ? 0.29610 0.35340 0.39340 -0.03000 -0.06780 0.05490  214 GLY B N     
5560 C  CA    . GLY B 218 ? 0.27460 0.32300 0.35960 -0.02660 -0.06400 0.05050  214 GLY B CA    
5561 C  C     . GLY B 218 ? 0.28070 0.33090 0.36800 -0.02070 -0.05760 0.05270  214 GLY B C     
5562 O  O     . GLY B 218 ? 0.30410 0.36270 0.40260 -0.01860 -0.05610 0.05760  214 GLY B O     
5563 N  N     . HIS B 219 ? 0.23510 0.27720 0.31200 -0.01800 -0.05360 0.04890  215 HIS B N     
5564 C  CA    . HIS B 219 ? 0.32730 0.36900 0.40460 -0.01280 -0.04750 0.04980  215 HIS B CA    
5565 C  C     . HIS B 219 ? 0.31170 0.35790 0.39890 -0.01080 -0.04140 0.05200  215 HIS B C     
5566 O  O     . HIS B 219 ? 0.28020 0.32840 0.37150 -0.00650 -0.03690 0.05370  215 HIS B O     
5567 C  CB    . HIS B 219 ? 0.30720 0.33910 0.37140 -0.01140 -0.04480 0.04480  215 HIS B CB    
5568 C  CG    . HIS B 219 ? 0.32040 0.35040 0.38400 -0.00670 -0.03850 0.04490  215 HIS B CG    
5569 N  ND1   . HIS B 219 ? 0.31530 0.34850 0.38270 -0.00340 -0.03820 0.04810  215 HIS B ND1   
5570 C  CD2   . HIS B 219 ? 0.30610 0.33100 0.36560 -0.00490 -0.03270 0.04210  215 HIS B CD2   
5571 C  CE1   . HIS B 219 ? 0.30130 0.33080 0.36730 0.00020  -0.03220 0.04700  215 HIS B CE1   
5572 N  NE2   . HIS B 219 ? 0.35570 0.38040 0.41650 -0.00080 -0.02890 0.04320  215 HIS B NE2   
5573 N  N     . GLY B 220 ? 0.27300 0.32050 0.36400 -0.01390 -0.04090 0.05200  216 GLY B N     
5574 C  CA    . GLY B 220 ? 0.31300 0.36620 0.41330 -0.01240 -0.03510 0.05440  216 GLY B CA    
5575 C  C     . GLY B 220 ? 0.35460 0.41810 0.46810 -0.01010 -0.03470 0.05960  216 GLY B C     
5576 O  O     . GLY B 220 ? 0.30500 0.37260 0.42530 -0.00680 -0.02840 0.06100  216 GLY B O     
5577 N  N     . ILE B 221 ? 0.31590 0.38390 0.43340 -0.01190 -0.04140 0.06240  217 ILE B N     
5578 C  CA    . ILE B 221 ? 0.31470 0.39290 0.44550 -0.00940 -0.04160 0.06790  217 ILE B CA    
5579 C  C     . ILE B 221 ? 0.25880 0.33490 0.38930 -0.00320 -0.03640 0.06790  217 ILE B C     
5580 O  O     . ILE B 221 ? 0.25960 0.34190 0.40100 0.00060  -0.03170 0.07080  217 ILE B O     
5581 C  CB    . ILE B 221 ? 0.28660 0.36940 0.41980 -0.01250 -0.05050 0.07090  217 ILE B CB    
5582 C  CG1   . ILE B 221 ? 0.30380 0.38940 0.43980 -0.01890 -0.05550 0.07120  217 ILE B CG1   
5583 C  CG2   . ILE B 221 ? 0.24690 0.34010 0.39370 -0.00910 -0.05080 0.07710  217 ILE B CG2   
5584 C  CD1   . ILE B 221 ? 0.26080 0.35710 0.41240 -0.01960 -0.05330 0.07590  217 ILE B CD1   
5585 N  N     . GLU B 222 ? 0.25080 0.31810 0.36910 -0.00200 -0.03690 0.06460  218 GLU B N     
5586 C  CA    . GLU B 222 ? 0.30840 0.37270 0.42640 0.00350  -0.03210 0.06450  218 GLU B CA    
5587 C  C     . GLU B 222 ? 0.35270 0.41400 0.47040 0.00600  -0.02360 0.06140  218 GLU B C     
5588 O  O     . GLU B 222 ? 0.27330 0.33680 0.39830 0.01050  -0.01840 0.06260  218 GLU B O     
5589 C  CB    . GLU B 222 ? 0.30550 0.36150 0.41070 0.00370  -0.03460 0.06200  218 GLU B CB    
5590 C  CG    . GLU B 222 ? 0.45040 0.50230 0.55530 0.00890  -0.02940 0.06180  218 GLU B CG    
5591 C  CD    . GLU B 222 ? 0.53420 0.57830 0.62690 0.00900  -0.03120 0.05980  218 GLU B CD    
5592 O  OE1   . GLU B 222 ? 0.55200 0.58850 0.63610 0.00970  -0.02700 0.05530  218 GLU B OE1   
5593 O  OE2   . GLU B 222 ? 0.63740 0.68370 0.72910 0.00850  -0.03670 0.06290  218 GLU B OE2   
5594 N  N     . CYS B 223 ? 0.26970 0.32600 0.37900 0.00310  -0.02220 0.05730  219 CYS B N     
5595 C  CA    . CYS B 223 ? 0.31510 0.36890 0.42280 0.00500  -0.01450 0.05440  219 CYS B CA    
5596 C  C     . CYS B 223 ? 0.34790 0.41110 0.46870 0.00650  -0.01020 0.05740  219 CYS B C     
5597 O  O     . CYS B 223 ? 0.36280 0.42600 0.48590 0.01020  -0.00330 0.05600  219 CYS B O     
5598 C  CB    . CYS B 223 ? 0.33610 0.38450 0.43400 0.00120  -0.01460 0.05080  219 CYS B CB    
5599 S  SG    . CYS B 223 ? 0.38320 0.42070 0.46560 -0.00050 -0.01850 0.04660  219 CYS B SG    
5600 N  N     . ALA B 224 ? 0.31670 0.38810 0.44650 0.00360  -0.01420 0.06140  220 ALA B N     
5601 C  CA    . ALA B 224 ? 0.30980 0.39160 0.45310 0.00470  -0.01040 0.06490  220 ALA B CA    
5602 C  C     . ALA B 224 ? 0.25480 0.34370 0.41080 0.00900  -0.01020 0.06910  220 ALA B C     
5603 O  O     . ALA B 224 ? 0.36980 0.46830 0.53850 0.01070  -0.00640 0.07220  220 ALA B O     
5604 C  CB    . ALA B 224 ? 0.34960 0.43760 0.49780 -0.00100 -0.01490 0.06780  220 ALA B CB    
5605 N  N     . LYS B 225 ? 0.27560 0.36060 0.42880 0.01090  -0.01390 0.06970  221 LYS B N     
5606 C  CA    . LYS B 225 ? 0.29970 0.39130 0.46510 0.01480  -0.01500 0.07460  221 LYS B CA    
5607 C  C     . LYS B 225 ? 0.32190 0.42610 0.50110 0.01250  -0.01890 0.08040  221 LYS B C     
5608 O  O     . LYS B 225 ? 0.32450 0.43770 0.51830 0.01600  -0.01570 0.08430  221 LYS B O     
5609 C  CB    . LYS B 225 ? 0.30010 0.39110 0.47140 0.02120  -0.00640 0.07350  221 LYS B CB    
5610 C  CG    . LYS B 225 ? 0.36480 0.44330 0.52320 0.02340  -0.00270 0.06790  221 LYS B CG    
5611 C  CD    . LYS B 225 ? 0.42900 0.50660 0.59220 0.02870  0.00660  0.06530  221 LYS B CD    
5612 C  CE    . LYS B 225 ? 0.58100 0.64630 0.73250 0.03060  0.00960  0.06000  221 LYS B CE    
5613 N  NZ    . LYS B 225 ? 0.59720 0.65650 0.73570 0.02770  0.01290  0.05420  221 LYS B NZ    
5614 N  N     . ALA B 226 ? 0.29080 0.39560 0.46590 0.00640  -0.02590 0.08090  222 ALA B N     
5615 C  CA    . ALA B 226 ? 0.24500 0.36120 0.43210 0.00270  -0.02970 0.08570  222 ALA B CA    
5616 C  C     . ALA B 226 ? 0.28870 0.41030 0.48040 0.00080  -0.03880 0.09040  222 ALA B C     
5617 O  O     . ALA B 226 ? 0.27430 0.40300 0.47200 -0.00410 -0.04440 0.09340  222 ALA B O     
5618 C  CB    . ALA B 226 ? 0.23680 0.35070 0.41790 -0.00330 -0.03100 0.08320  222 ALA B CB    
5619 N  N     . TRP B 227 ? 0.29200 0.41060 0.48120 0.00430  -0.04050 0.09140  223 TRP B N     
5620 C  CA    . TRP B 227 ? 0.32050 0.44410 0.51220 0.00220  -0.04950 0.09590  223 TRP B CA    
5621 C  C     . TRP B 227 ? 0.34110 0.47960 0.55160 0.00190  -0.05210 0.10310  223 TRP B C     
5622 O  O     . TRP B 227 ? 0.33370 0.47810 0.54650 -0.00350 -0.06020 0.10590  223 TRP B O     
5623 C  CB    . TRP B 227 ? 0.32450 0.44350 0.51230 0.00680  -0.04980 0.09700  223 TRP B CB    
5624 C  CG    . TRP B 227 ? 0.31450 0.42010 0.48490 0.00700  -0.04780 0.09070  223 TRP B CG    
5625 C  CD1   . TRP B 227 ? 0.30480 0.40370 0.46040 0.00250  -0.05300 0.08710  223 TRP B CD1   
5626 C  CD2   . TRP B 227 ? 0.32680 0.42420 0.49300 0.01190  -0.03980 0.08700  223 TRP B CD2   
5627 N  NE1   . TRP B 227 ? 0.29460 0.38220 0.43760 0.00440  -0.04880 0.08190  223 TRP B NE1   
5628 C  CE2   . TRP B 227 ? 0.36190 0.44830 0.51090 0.00990  -0.04090 0.08180  223 TRP B CE2   
5629 C  CE3   . TRP B 227 ? 0.33630 0.43440 0.51150 0.01770  -0.03180 0.08740  223 TRP B CE3   
5630 C  CZ2   . TRP B 227 ? 0.36990 0.44660 0.51090 0.01320  -0.03470 0.07750  223 TRP B CZ2   
5631 C  CZ3   . TRP B 227 ? 0.32070 0.40840 0.48720 0.02080  -0.02560 0.08240  223 TRP B CZ3   
5632 C  CH2   . TRP B 227 ? 0.31630 0.39360 0.46600 0.01840  -0.02730 0.07780  223 TRP B CH2   
5633 N  N     . GLU B 228 ? 0.31450 0.45930 0.53890 0.00760  -0.04530 0.10610  224 GLU B N     
5634 C  CA    . GLU B 228 ? 0.27730 0.43730 0.52110 0.00810  -0.04770 0.11370  224 GLU B CA    
5635 C  C     . GLU B 228 ? 0.30510 0.47260 0.55500 0.00260  -0.04860 0.11450  224 GLU B C     
5636 O  O     . GLU B 228 ? 0.35350 0.53220 0.61420 -0.00100 -0.05520 0.12010  224 GLU B O     
5637 C  CB    . GLU B 228 ? 0.41420 0.57870 0.67180 0.01630  -0.03960 0.11640  224 GLU B CB    
5638 C  CG    . GLU B 228 ? 0.68520 0.86650 0.96500 0.01760  -0.04020 0.12420  224 GLU B CG    
5639 C  CD    . GLU B 228 ? 0.84630 1.03150 1.14020 0.02650  -0.03380 0.12750  224 GLU B CD    
5640 O  OE1   . GLU B 228 ? 0.89220 1.09150 1.20550 0.02860  -0.03340 0.13390  224 GLU B OE1   
5641 O  OE2   . GLU B 228 ? 0.90630 1.08070 1.19270 0.03130  -0.02920 0.12380  224 GLU B OE2   
5642 N  N     . GLU B 229 ? 0.34130 0.50310 0.58420 0.00120  -0.04270 0.10930  225 GLU B N     
5643 C  CA    . GLU B 229 ? 0.39780 0.56590 0.64580 -0.00450 -0.04380 0.11030  225 GLU B CA    
5644 C  C     . GLU B 229 ? 0.33620 0.50090 0.57560 -0.01250 -0.05380 0.10940  225 GLU B C     
5645 O  O     . GLU B 229 ? 0.25760 0.43150 0.50640 -0.01770 -0.05910 0.11330  225 GLU B O     
5646 C  CB    . GLU B 229 ? 0.40460 0.56670 0.64590 -0.00400 -0.03510 0.10530  225 GLU B CB    
5647 C  CG    . GLU B 229 ? 0.50400 0.67100 0.75470 0.00300  -0.02470 0.10580  225 GLU B CG    
5648 C  CD    . GLU B 229 ? 0.61810 0.77450 0.85970 0.00930  -0.01960 0.10130  225 GLU B CD    
5649 O  OE1   . GLU B 229 ? 0.64990 0.79680 0.87990 0.00870  -0.02460 0.09900  225 GLU B OE1   
5650 O  OE2   . GLU B 229 ? 0.69400 0.85170 0.94030 0.01470  -0.01060 0.09990  225 GLU B OE2   
5651 N  N     . LEU B 230 ? 0.28100 0.43300 0.50300 -0.01350 -0.05670 0.10400  226 LEU B N     
5652 C  CA    . LEU B 230 ? 0.28250 0.43070 0.49570 -0.02060 -0.06600 0.10230  226 LEU B CA    
5653 C  C     . LEU B 230 ? 0.29930 0.45780 0.52140 -0.02270 -0.07480 0.10820  226 LEU B C     
5654 O  O     . LEU B 230 ? 0.32890 0.49190 0.55390 -0.02940 -0.08210 0.10950  226 LEU B O     
5655 C  CB    . LEU B 230 ? 0.24260 0.37610 0.43620 -0.02030 -0.06660 0.09550  226 LEU B CB    
5656 C  CG    . LEU B 230 ? 0.34670 0.47490 0.52930 -0.02690 -0.07570 0.09240  226 LEU B CG    
5657 C  CD1   . LEU B 230 ? 0.29120 0.41880 0.47510 -0.03320 -0.07730 0.09090  226 LEU B CD1   
5658 C  CD2   . LEU B 230 ? 0.24530 0.36020 0.40930 -0.02550 -0.07540 0.08620  226 LEU B CD2   
5659 N  N     . LEU B 231 ? 0.31850 0.48070 0.54530 -0.01740 -0.07460 0.11190  227 LEU B N     
5660 C  CA    . LEU B 231 ? 0.28280 0.45550 0.51810 -0.01930 -0.08330 0.11820  227 LEU B CA    
5661 C  C     . LEU B 231 ? 0.27600 0.46380 0.53100 -0.02140 -0.08460 0.12470  227 LEU B C     
5662 O  O     . LEU B 231 ? 0.29360 0.48860 0.55280 -0.02770 -0.09350 0.12770  227 LEU B O     
5663 C  CB    . LEU B 231 ? 0.34410 0.51780 0.58180 -0.01250 -0.08210 0.12170  227 LEU B CB    
5664 C  CG    . LEU B 231 ? 0.41590 0.60210 0.66480 -0.01330 -0.09040 0.12990  227 LEU B CG    
5665 C  CD1   . LEU B 231 ? 0.37790 0.56310 0.61570 -0.02100 -0.10150 0.12870  227 LEU B CD1   
5666 C  CD2   . LEU B 231 ? 0.36530 0.55150 0.61760 -0.00580 -0.08800 0.13380  227 LEU B CD2   
5667 N  N     . ASP B 232 ? 0.29870 0.49200 0.56600 -0.01650 -0.07570 0.12670  228 ASP B N     
5668 C  CA    . ASP B 232 ? 0.35910 0.56750 0.64570 -0.01850 -0.07600 0.13290  228 ASP B CA    
5669 C  C     . ASP B 232 ? 0.28480 0.49280 0.56910 -0.02670 -0.07910 0.13090  228 ASP B C     
5670 O  O     . ASP B 232 ? 0.29190 0.51110 0.58780 -0.03200 -0.08560 0.13590  228 ASP B O     
5671 C  CB    . ASP B 232 ? 0.51190 0.72690 0.81240 -0.01070 -0.06540 0.13550  228 ASP B CB    
5672 C  CG    . ASP B 232 ? 0.82350 1.05650 1.14620 -0.01170 -0.06550 0.14310  228 ASP B CG    
5673 O  OD1   . ASP B 232 ? 0.91210 1.15700 1.24830 -0.01160 -0.07150 0.15030  228 ASP B OD1   
5674 O  OD2   . ASP B 232 ? 0.90920 1.14460 1.23710 -0.01010 -0.05670 0.14200  228 ASP B OD2   
5675 N  N     . PHE B 233 ? 0.36780 0.56300 0.63750 -0.02840 -0.07550 0.12380  229 PHE B N     
5676 C  CA    . PHE B 233 ? 0.35270 0.54630 0.62020 -0.03650 -0.07940 0.12210  229 PHE B CA    
5677 C  C     . PHE B 233 ? 0.34490 0.53710 0.60650 -0.04350 -0.09140 0.12160  229 PHE B C     
5678 O  O     . PHE B 233 ? 0.31130 0.51040 0.58100 -0.05030 -0.09750 0.12450  229 PHE B O     
5679 C  CB    . PHE B 233 ? 0.31250 0.49190 0.56490 -0.03640 -0.07350 0.11490  229 PHE B CB    
5680 C  CG    . PHE B 233 ? 0.32430 0.50000 0.57350 -0.04440 -0.07740 0.11290  229 PHE B CG    
5681 C  CD1   . PHE B 233 ? 0.31960 0.50510 0.58260 -0.04780 -0.07570 0.11750  229 PHE B CD1   
5682 C  CD2   . PHE B 233 ? 0.38140 0.54340 0.61400 -0.04830 -0.08230 0.10650  229 PHE B CD2   
5683 C  CE1   . PHE B 233 ? 0.36880 0.55020 0.62940 -0.05530 -0.07930 0.11600  229 PHE B CE1   
5684 C  CE2   . PHE B 233 ? 0.38450 0.54200 0.61470 -0.05530 -0.08570 0.10460  229 PHE B CE2   
5685 C  CZ    . PHE B 233 ? 0.36870 0.53570 0.61310 -0.05900 -0.08440 0.10950  229 PHE B CZ    
5686 N  N     . ALA B 234 ? 0.36320 0.54670 0.61070 -0.04210 -0.09500 0.11800  230 ALA B N     
5687 C  CA    . ALA B 234 ? 0.33730 0.51910 0.57740 -0.04880 -0.10620 0.11670  230 ALA B CA    
5688 C  C     . ALA B 234 ? 0.37010 0.56790 0.62590 -0.05140 -0.11370 0.12470  230 ALA B C     
5689 O  O     . ALA B 234 ? 0.35710 0.55810 0.61400 -0.05930 -0.12250 0.12500  230 ALA B O     
5690 C  CB    . ALA B 234 ? 0.35980 0.53060 0.58210 -0.04630 -0.10780 0.11180  230 ALA B CB    
5691 N  N     . GLU B 235 ? 0.33690 0.54520 0.60570 -0.04500 -0.11050 0.13120  231 GLU B N     
5692 C  CA    . GLU B 235 ? 0.39360 0.61830 0.67870 -0.04690 -0.11760 0.13970  231 GLU B CA    
5693 C  C     . GLU B 235 ? 0.44290 0.67980 0.74590 -0.05110 -0.11770 0.14440  231 GLU B C     
5694 O  O     . GLU B 235 ? 0.34450 0.59210 0.65660 -0.05720 -0.12680 0.14910  231 GLU B O     
5695 C  CB    . GLU B 235 ? 0.36760 0.59930 0.66240 -0.03820 -0.11380 0.14550  231 GLU B CB    
5696 C  CG    . GLU B 235 ? 0.41500 0.63760 0.69460 -0.03490 -0.11580 0.14300  231 GLU B CG    
5697 C  CD    . GLU B 235 ? 0.42290 0.65150 0.71320 -0.02620 -0.11160 0.14910  231 GLU B CD    
5698 O  OE1   . GLU B 235 ? 0.47930 0.70440 0.76130 -0.02420 -0.11520 0.14980  231 GLU B OE1   
5699 O  OE2   . GLU B 235 ? 0.48320 0.71990 0.79020 -0.02130 -0.10460 0.15310  231 GLU B OE2   
5700 N  N     . LEU B 236 ? 0.39490 0.63140 0.70350 -0.04790 -0.10770 0.14380  232 LEU B N     
5701 C  CA    . LEU B 236 ? 0.37730 0.62590 0.70310 -0.05160 -0.10650 0.14860  232 LEU B CA    
5702 C  C     . LEU B 236 ? 0.38070 0.62560 0.70150 -0.06210 -0.11450 0.14600  232 LEU B C     
5703 O  O     . LEU B 236 ? 0.35420 0.61140 0.68990 -0.06780 -0.11910 0.15160  232 LEU B O     
5704 C  CB    . LEU B 236 ? 0.32660 0.57370 0.65560 -0.04630 -0.09380 0.14730  232 LEU B CB    
5705 C  CG    . LEU B 236 ? 0.35270 0.61020 0.69640 -0.05050 -0.09120 0.15140  232 LEU B CG    
5706 C  CD1   . LEU B 236 ? 0.23500 0.51310 0.60280 -0.04920 -0.09200 0.16100  232 LEU B CD1   
5707 C  CD2   . LEU B 236 ? 0.30350 0.55510 0.64300 -0.04640 -0.07910 0.14770  232 LEU B CD2   
5708 N  N     . THR B 237 ? 0.36770 0.59570 0.66840 -0.06480 -0.11590 0.13760  233 THR B N     
5709 C  CA    . THR B 237 ? 0.32980 0.55160 0.62480 -0.07420 -0.12240 0.13400  233 THR B CA    
5710 C  C     . THR B 237 ? 0.30570 0.52380 0.59080 -0.08020 -0.13430 0.13120  233 THR B C     
5711 O  O     . THR B 237 ? 0.36840 0.58420 0.65230 -0.08880 -0.14130 0.12920  233 THR B O     
5712 C  CB    . THR B 237 ? 0.31550 0.52050 0.59510 -0.07370 -0.11630 0.12610  233 THR B CB    
5713 O  OG1   . THR B 237 ? 0.34810 0.54060 0.60990 -0.06890 -0.11480 0.12000  233 THR B OG1   
5714 C  CG2   . THR B 237 ? 0.29160 0.50020 0.57970 -0.06910 -0.10490 0.12850  233 THR B CG2   
5715 N  N     . GLY B 238 ? 0.37900 0.59650 0.65670 -0.07610 -0.13670 0.13090  234 GLY B N     
5716 C  CA    . GLY B 238 ? 0.34120 0.55330 0.60560 -0.08160 -0.14710 0.12690  234 GLY B CA    
5717 C  C     . GLY B 238 ? 0.39790 0.59090 0.64070 -0.08360 -0.14680 0.11650  234 GLY B C     
5718 O  O     . GLY B 238 ? 0.46000 0.64790 0.69200 -0.08970 -0.15550 0.11200  234 GLY B O     
5719 N  N     . ILE B 239 ? 0.35270 0.53520 0.58890 -0.07870 -0.13720 0.11230  235 ILE B N     
5720 C  CA    . ILE B 239 ? 0.32570 0.49050 0.54290 -0.08050 -0.13660 0.10280  235 ILE B CA    
5721 C  C     . ILE B 239 ? 0.31530 0.47240 0.51610 -0.07580 -0.13640 0.09860  235 ILE B C     
5722 O  O     . ILE B 239 ? 0.28530 0.44460 0.48750 -0.06810 -0.13000 0.10130  235 ILE B O     
5723 C  CB    . ILE B 239 ? 0.33830 0.49590 0.55560 -0.07780 -0.12690 0.10070  235 ILE B CB    
5724 C  CG1   . ILE B 239 ? 0.33450 0.49930 0.56710 -0.08350 -0.12760 0.10490  235 ILE B CG1   
5725 C  CG2   . ILE B 239 ? 0.33800 0.47760 0.53630 -0.07850 -0.12580 0.09140  235 ILE B CG2   
5726 C  CD1   . ILE B 239 ? 0.34110 0.50290 0.57680 -0.08040 -0.11760 0.10520  235 ILE B CD1   
5727 N  N     . PRO B 240 ? 0.32390 0.47240 0.50940 -0.08020 -0.14310 0.09210  236 PRO B N     
5728 C  CA    . PRO B 240 ? 0.38410 0.52530 0.55330 -0.07580 -0.14240 0.08810  236 PRO B CA    
5729 C  C     . PRO B 240 ? 0.42880 0.55690 0.58750 -0.07030 -0.13290 0.08260  236 PRO B C     
5730 O  O     . PRO B 240 ? 0.40660 0.52740 0.56510 -0.07160 -0.12900 0.07930  236 PRO B O     
5731 C  CB    . PRO B 240 ? 0.38030 0.51650 0.53670 -0.08300 -0.15210 0.08220  236 PRO B CB    
5732 C  CG    . PRO B 240 ? 0.42020 0.55600 0.58390 -0.09070 -0.15630 0.08100  236 PRO B CG    
5733 C  CD    . PRO B 240 ? 0.31960 0.46690 0.50380 -0.08960 -0.15250 0.08920  236 PRO B CD    
5734 N  N     . VAL B 241 ? 0.33200 0.45740 0.48220 -0.06420 -0.12950 0.08210  237 VAL B N     
5735 C  CA    . VAL B 241 ? 0.33880 0.45440 0.48150 -0.05800 -0.12010 0.07860  237 VAL B CA    
5736 C  C     . VAL B 241 ? 0.35840 0.46350 0.48180 -0.05710 -0.12120 0.07210  237 VAL B C     
5737 O  O     . VAL B 241 ? 0.34550 0.45460 0.46460 -0.05560 -0.12450 0.07420  237 VAL B O     
5738 C  CB    . VAL B 241 ? 0.27130 0.39410 0.42450 -0.05060 -0.11310 0.08490  237 VAL B CB    
5739 C  CG1   . VAL B 241 ? 0.26590 0.37810 0.40960 -0.04450 -0.10410 0.08070  237 VAL B CG1   
5740 C  CG2   . VAL B 241 ? 0.27040 0.40360 0.44270 -0.05110 -0.11070 0.09080  237 VAL B CG2   
5741 N  N     . ALA B 242 ? 0.34430 0.43680 0.45660 -0.05790 -0.11850 0.06460  238 ALA B N     
5742 C  CA    . ALA B 242 ? 0.31870 0.40080 0.41370 -0.05540 -0.11650 0.05850  238 ALA B CA    
5743 C  C     . ALA B 242 ? 0.32400 0.40090 0.41820 -0.04870 -0.10670 0.05820  238 ALA B C     
5744 O  O     . ALA B 242 ? 0.32470 0.40290 0.42860 -0.04730 -0.10150 0.06040  238 ALA B O     
5745 C  CB    . ALA B 242 ? 0.29230 0.36340 0.37570 -0.06020 -0.11970 0.05000  238 ALA B CB    
5746 N  N     . THR B 243 ? 0.28560 0.35720 0.36810 -0.04480 -0.10410 0.05580  239 THR B N     
5747 C  CA    . THR B 243 ? 0.38040 0.44510 0.45940 -0.03930 -0.09530 0.05390  239 THR B CA    
5748 C  C     . THR B 243 ? 0.38610 0.43880 0.44930 -0.03990 -0.09440 0.04600  239 THR B C     
5749 O  O     . THR B 243 ? 0.33020 0.38020 0.38380 -0.04330 -0.10010 0.04200  239 THR B O     
5750 C  CB    . THR B 243 ? 0.39040 0.45890 0.47100 -0.03330 -0.09150 0.05840  239 THR B CB    
5751 O  OG1   . THR B 243 ? 0.39450 0.46090 0.46290 -0.03320 -0.09490 0.05680  239 THR B OG1   
5752 C  CG2   . THR B 243 ? 0.26150 0.34240 0.35830 -0.03230 -0.09290 0.06650  239 THR B CG2   
5753 N  N     . THR B 244 ? 0.26600 0.31170 0.32690 -0.03650 -0.08720 0.04370  240 THR B N     
5754 C  CA    . THR B 244 ? 0.26790 0.30320 0.31500 -0.03530 -0.08490 0.03720  240 THR B CA    
5755 C  C     . THR B 244 ? 0.32830 0.36430 0.36750 -0.03170 -0.08400 0.03800  240 THR B C     
5756 O  O     . THR B 244 ? 0.33430 0.37770 0.38000 -0.02940 -0.08400 0.04380  240 THR B O     
5757 C  CB    . THR B 244 ? 0.30020 0.32930 0.34790 -0.03260 -0.07750 0.03560  240 THR B CB    
5758 O  OG1   . THR B 244 ? 0.28180 0.31470 0.33450 -0.02770 -0.07180 0.03980  240 THR B OG1   
5759 C  CG2   . THR B 244 ? 0.26040 0.28970 0.31700 -0.03610 -0.07780 0.03610  240 THR B CG2   
5760 N  N     . PRO B 245 ? 0.30090 0.32930 0.32660 -0.03110 -0.08320 0.03250  241 PRO B N     
5761 C  CA    . PRO B 245 ? 0.32710 0.35620 0.34550 -0.02780 -0.08180 0.03370  241 PRO B CA    
5762 C  C     . PRO B 245 ? 0.37670 0.40740 0.40160 -0.02270 -0.07540 0.03820  241 PRO B C     
5763 O  O     . PRO B 245 ? 0.30900 0.34550 0.33710 -0.02060 -0.07610 0.04340  241 PRO B O     
5764 C  CB    . PRO B 245 ? 0.32740 0.34750 0.33190 -0.02780 -0.08040 0.02650  241 PRO B CB    
5765 C  CG    . PRO B 245 ? 0.37510 0.39210 0.37830 -0.03270 -0.08500 0.02180  241 PRO B CG    
5766 C  CD    . PRO B 245 ? 0.31710 0.33690 0.33390 -0.03390 -0.08450 0.02520  241 PRO B CD    
5767 N  N     . LYS B 246 ? 0.30510 0.33070 0.33200 -0.02070 -0.06940 0.03640  242 LYS B N     
5768 C  CA    . LYS B 246 ? 0.29450 0.32100 0.32670 -0.01610 -0.06330 0.03980  242 LYS B CA    
5769 C  C     . LYS B 246 ? 0.33690 0.37190 0.38340 -0.01530 -0.06350 0.04580  242 LYS B C     
5770 O  O     . LYS B 246 ? 0.35820 0.39590 0.41000 -0.01150 -0.06020 0.04960  242 LYS B O     
5771 C  CB    . LYS B 246 ? 0.32360 0.34310 0.35370 -0.01470 -0.05720 0.03610  242 LYS B CB    
5772 C  CG    . LYS B 246 ? 0.39890 0.41750 0.43100 -0.01010 -0.05070 0.03800  242 LYS B CG    
5773 C  CD    . LYS B 246 ? 0.46150 0.47270 0.48770 -0.00900 -0.04560 0.03370  242 LYS B CD    
5774 C  CE    . LYS B 246 ? 0.44570 0.45710 0.47830 -0.01020 -0.04320 0.03340  242 LYS B CE    
5775 N  NZ    . LYS B 246 ? 0.45220 0.45650 0.47820 -0.01040 -0.04010 0.02920  242 LYS B NZ    
5776 N  N     . GLY B 247 ? 0.29430 0.33360 0.34800 -0.01890 -0.06710 0.04670  243 GLY B N     
5777 C  CA    . GLY B 247 ? 0.26750 0.31610 0.33560 -0.01850 -0.06760 0.05260  243 GLY B CA    
5778 C  C     . GLY B 247 ? 0.26130 0.31790 0.33320 -0.01870 -0.07310 0.05770  243 GLY B C     
5779 O  O     . GLY B 247 ? 0.34220 0.40750 0.42720 -0.01810 -0.07390 0.06320  243 GLY B O     
5780 N  N     . LYS B 248 ? 0.31830 0.37280 0.37940 -0.01930 -0.07680 0.05640  244 LYS B N     
5781 C  CA    . LYS B 248 ? 0.32490 0.38740 0.38880 -0.01960 -0.08230 0.06190  244 LYS B CA    
5782 C  C     . LYS B 248 ? 0.34920 0.41700 0.42490 -0.01440 -0.07860 0.06840  244 LYS B C     
5783 O  O     . LYS B 248 ? 0.33640 0.39900 0.41110 -0.01010 -0.07190 0.06760  244 LYS B O     
5784 C  CB    . LYS B 248 ? 0.43020 0.48910 0.47930 -0.02020 -0.08510 0.05950  244 LYS B CB    
5785 C  CG    . LYS B 248 ? 0.33070 0.39810 0.37990 -0.02180 -0.09230 0.06470  244 LYS B CG    
5786 C  CD    . LYS B 248 ? 0.35560 0.41880 0.38860 -0.02230 -0.09370 0.06180  244 LYS B CD    
5787 C  CE    . LYS B 248 ? 0.30210 0.37410 0.33370 -0.02370 -0.10050 0.06770  244 LYS B CE    
5788 N  NZ    . LYS B 248 ? 0.36170 0.44000 0.39440 -0.02950 -0.10880 0.06740  244 LYS B NZ    
5789 N  N     . SER B 249 ? 0.34920 0.42740 0.43650 -0.01500 -0.08290 0.07480  245 SER B N     
5790 C  CA    . SER B 249 ? 0.35990 0.44510 0.46170 -0.01040 -0.08050 0.08190  245 SER B CA    
5791 C  C     . SER B 249 ? 0.34180 0.42990 0.45680 -0.00900 -0.07550 0.08250  245 SER B C     
5792 O  O     . SER B 249 ? 0.29600 0.38930 0.42360 -0.00460 -0.07200 0.08740  245 SER B O     
5793 C  CB    . SER B 249 ? 0.32080 0.40110 0.41980 -0.00490 -0.07550 0.08320  245 SER B CB    
5794 O  OG    . SER B 249 ? 0.39690 0.46920 0.49410 -0.00190 -0.06730 0.07870  245 SER B OG    
5795 N  N     . SER B 250 ? 0.30130 0.38640 0.41400 -0.01260 -0.07470 0.07780  246 SER B N     
5796 C  CA    . SER B 250 ? 0.31640 0.40670 0.44230 -0.01210 -0.07100 0.07950  246 SER B CA    
5797 C  C     . SER B 250 ? 0.33930 0.44220 0.47900 -0.01460 -0.07670 0.08570  246 SER B C     
5798 O  O     . SER B 250 ? 0.36490 0.47470 0.51850 -0.01320 -0.07330 0.08900  246 SER B O     
5799 C  CB    . SER B 250 ? 0.29350 0.37770 0.41390 -0.01560 -0.06910 0.07380  246 SER B CB    
5800 O  OG    . SER B 250 ? 0.54250 0.61540 0.64940 -0.01420 -0.06510 0.06800  246 SER B OG    
5801 N  N     . PHE B 251 ? 0.34320 0.44980 0.47940 -0.01820 -0.08530 0.08750  247 PHE B N     
5802 C  CA    . PHE B 251 ? 0.32680 0.44570 0.47500 -0.02130 -0.09210 0.09360  247 PHE B CA    
5803 C  C     . PHE B 251 ? 0.37950 0.50220 0.52370 -0.02150 -0.09880 0.09740  247 PHE B C     
5804 O  O     . PHE B 251 ? 0.34000 0.45530 0.46820 -0.02300 -0.10110 0.09310  247 PHE B O     
5805 C  CB    . PHE B 251 ? 0.33310 0.45210 0.47940 -0.02870 -0.09740 0.09030  247 PHE B CB    
5806 C  CG    . PHE B 251 ? 0.34340 0.47560 0.50390 -0.03240 -0.10390 0.09650  247 PHE B CG    
5807 C  CD1   . PHE B 251 ? 0.28760 0.42810 0.46500 -0.03140 -0.10030 0.10070  247 PHE B CD1   
5808 C  CD2   . PHE B 251 ? 0.31270 0.44970 0.46970 -0.03720 -0.11370 0.09810  247 PHE B CD2   
5809 C  CE1   . PHE B 251 ? 0.27610 0.42970 0.46760 -0.03490 -0.10630 0.10680  247 PHE B CE1   
5810 C  CE2   . PHE B 251 ? 0.38040 0.53040 0.55110 -0.04100 -0.12020 0.10410  247 PHE B CE2   
5811 C  CZ    . PHE B 251 ? 0.29860 0.45690 0.48710 -0.03980 -0.11650 0.10860  247 PHE B CZ    
5812 N  N     . PRO B 252 ? 0.38560 0.52020 0.54390 -0.02000 -0.10210 0.10560  248 PRO B N     
5813 C  CA    . PRO B 252 ? 0.41230 0.55100 0.56690 -0.01980 -0.10830 0.11030  248 PRO B CA    
5814 C  C     . PRO B 252 ? 0.40480 0.54380 0.54720 -0.02720 -0.11770 0.10740  248 PRO B C     
5815 O  O     . PRO B 252 ? 0.38390 0.52910 0.53160 -0.03270 -0.12310 0.10770  248 PRO B O     
5816 C  CB    . PRO B 252 ? 0.37880 0.53140 0.55390 -0.01710 -0.11000 0.12010  248 PRO B CB    
5817 C  CG    . PRO B 252 ? 0.37340 0.53070 0.56170 -0.01780 -0.10670 0.12000  248 PRO B CG    
5818 C  CD    . PRO B 252 ? 0.27470 0.41990 0.45310 -0.01800 -0.09980 0.11140  248 PRO B CD    
5819 N  N     . GLU B 253 ? 0.37790 0.51030 0.50380 -0.02760 -0.11930 0.10420  249 GLU B N     
5820 C  CA    . GLU B 253 ? 0.37070 0.50160 0.48250 -0.03450 -0.12700 0.09960  249 GLU B CA    
5821 C  C     . GLU B 253 ? 0.41400 0.55740 0.52970 -0.03820 -0.13700 0.10630  249 GLU B C     
5822 O  O     . GLU B 253 ? 0.42590 0.56990 0.53180 -0.04480 -0.14440 0.10260  249 GLU B O     
5823 C  CB    . GLU B 253 ? 0.36720 0.48710 0.45950 -0.03350 -0.12460 0.09350  249 GLU B CB    
5824 C  CG    . GLU B 253 ? 0.40590 0.51310 0.49120 -0.03250 -0.11720 0.08500  249 GLU B CG    
5825 C  CD    . GLU B 253 ? 0.52040 0.61740 0.58660 -0.03220 -0.11540 0.07850  249 GLU B CD    
5826 O  OE1   . GLU B 253 ? 0.56860 0.66730 0.62840 -0.03050 -0.11680 0.08170  249 GLU B OE1   
5827 O  OE2   . GLU B 253 ? 0.50890 0.59640 0.56660 -0.03360 -0.11240 0.07060  249 GLU B OE2   
5828 N  N     . ASN B 254 ? 0.34800 0.50160 0.47840 -0.03440 -0.13770 0.11590  250 ASN B N     
5829 C  CA    . ASN B 254 ? 0.44370 0.61130 0.58150 -0.03780 -0.14730 0.12370  250 ASN B CA    
5830 C  C     . ASN B 254 ? 0.45820 0.63570 0.61360 -0.04060 -0.15000 0.12710  250 ASN B C     
5831 O  O     . ASN B 254 ? 0.43150 0.62160 0.59480 -0.04400 -0.15850 0.13370  250 ASN B O     
5832 C  CB    . ASN B 254 ? 0.42120 0.59510 0.56680 -0.03200 -0.14700 0.13340  250 ASN B CB    
5833 C  CG    . ASN B 254 ? 0.53940 0.71260 0.70130 -0.02410 -0.13770 0.13700  250 ASN B CG    
5834 O  OD1   . ASN B 254 ? 0.59520 0.75970 0.75670 -0.02200 -0.12970 0.13080  250 ASN B OD1   
5835 N  ND2   . ASN B 254 ? 0.63860 0.82100 0.81480 -0.01960 -0.13870 0.14690  250 ASN B ND2   
5836 N  N     . HIS B 255 ? 0.42390 0.59680 0.58570 -0.03960 -0.14340 0.12310  251 HIS B N     
5837 C  CA    . HIS B 255 ? 0.34990 0.53280 0.52930 -0.04220 -0.14530 0.12680  251 HIS B CA    
5838 C  C     . HIS B 255 ? 0.34790 0.53210 0.52090 -0.05160 -0.15420 0.12270  251 HIS B C     
5839 O  O     . HIS B 255 ? 0.40720 0.58060 0.56230 -0.05530 -0.15540 0.11410  251 HIS B O     
5840 C  CB    . HIS B 255 ? 0.37250 0.54990 0.55940 -0.03830 -0.13500 0.12380  251 HIS B CB    
5841 C  CG    . HIS B 255 ? 0.36130 0.55040 0.56880 -0.03920 -0.13490 0.12910  251 HIS B CG    
5842 N  ND1   . HIS B 255 ? 0.37840 0.57170 0.58890 -0.04680 -0.14070 0.12780  251 HIS B ND1   
5843 C  CD2   . HIS B 255 ? 0.38030 0.57810 0.60680 -0.03340 -0.12950 0.13580  251 HIS B CD2   
5844 C  CE1   . HIS B 255 ? 0.42200 0.62670 0.65270 -0.04590 -0.13910 0.13400  251 HIS B CE1   
5845 N  NE2   . HIS B 255 ? 0.40180 0.60970 0.64240 -0.03760 -0.13200 0.13870  251 HIS B NE2   
5846 N  N     . ALA B 256 ? 0.32350 0.52110 0.51180 -0.05550 -0.16040 0.12880  252 ALA B N     
5847 C  CA    . ALA B 256 ? 0.30560 0.50510 0.48910 -0.06500 -0.16960 0.12530  252 ALA B CA    
5848 C  C     . ALA B 256 ? 0.36490 0.55260 0.54220 -0.06840 -0.16590 0.11610  252 ALA B C     
5849 O  O     . ALA B 256 ? 0.43850 0.62180 0.60530 -0.07580 -0.17240 0.11000  252 ALA B O     
5850 C  CB    . ALA B 256 ? 0.30680 0.52380 0.51050 -0.06840 -0.17640 0.13430  252 ALA B CB    
5851 N  N     . LEU B 257 ? 0.35010 0.53270 0.53360 -0.06330 -0.15580 0.11500  253 LEU B N     
5852 C  CA    . LEU B 257 ? 0.35650 0.52840 0.53540 -0.06620 -0.15200 0.10740  253 LEU B CA    
5853 C  C     . LEU B 257 ? 0.36840 0.52380 0.52790 -0.06370 -0.14660 0.09850  253 LEU B C     
5854 O  O     . LEU B 257 ? 0.33530 0.48090 0.49030 -0.06520 -0.14280 0.09230  253 LEU B O     
5855 C  CB    . LEU B 257 ? 0.34360 0.52000 0.53980 -0.06270 -0.14410 0.11130  253 LEU B CB    
5856 C  CG    . LEU B 257 ? 0.36500 0.55780 0.58210 -0.06610 -0.14870 0.11950  253 LEU B CG    
5857 C  CD1   . LEU B 257 ? 0.38400 0.58150 0.61710 -0.06120 -0.13930 0.12330  253 LEU B CD1   
5858 C  CD2   . LEU B 257 ? 0.29070 0.48350 0.50630 -0.07610 -0.15730 0.11640  253 LEU B CD2   
5859 N  N     . SER B 258 ? 0.38470 0.53710 0.53280 -0.06000 -0.14640 0.09810  254 SER B N     
5860 C  CA    . SER B 258 ? 0.34490 0.48280 0.47610 -0.05700 -0.14060 0.09050  254 SER B CA    
5861 C  C     . SER B 258 ? 0.35710 0.48710 0.47110 -0.06330 -0.14680 0.08230  254 SER B C     
5862 O  O     . SER B 258 ? 0.40970 0.54520 0.51850 -0.06740 -0.15520 0.08330  254 SER B O     
5863 C  CB    . SER B 258 ? 0.38330 0.52110 0.51030 -0.05030 -0.13710 0.09380  254 SER B CB    
5864 O  OG    . SER B 258 ? 0.46240 0.58790 0.57030 -0.04940 -0.13470 0.08630  254 SER B OG    
5865 N  N     . LEU B 259 ? 0.33290 0.45030 0.43840 -0.06410 -0.14260 0.07420  255 LEU B N     
5866 C  CA    . LEU B 259 ? 0.42630 0.53360 0.51460 -0.06870 -0.14640 0.06510  255 LEU B CA    
5867 C  C     . LEU B 259 ? 0.41860 0.51760 0.49040 -0.06430 -0.14240 0.06070  255 LEU B C     
5868 O  O     . LEU B 259 ? 0.45380 0.54500 0.51020 -0.06730 -0.14510 0.05310  255 LEU B O     
5869 C  CB    . LEU B 259 ? 0.41810 0.51580 0.50690 -0.07170 -0.14400 0.05890  255 LEU B CB    
5870 C  CG    . LEU B 259 ? 0.40540 0.51000 0.50950 -0.07720 -0.14830 0.06230  255 LEU B CG    
5871 C  CD1   . LEU B 259 ? 0.34670 0.44220 0.45380 -0.07830 -0.14350 0.05830  255 LEU B CD1   
5872 C  CD2   . LEU B 259 ? 0.41180 0.52050 0.51250 -0.08520 -0.15940 0.06070  255 LEU B CD2   
5873 N  N     . GLY B 260 ? 0.36920 0.46950 0.44410 -0.05740 -0.13590 0.06520  256 GLY B N     
5874 C  CA    . GLY B 260 ? 0.32750 0.41940 0.38800 -0.05330 -0.13110 0.06130  256 GLY B CA    
5875 C  C     . GLY B 260 ? 0.37960 0.45910 0.43570 -0.05120 -0.12360 0.05460  256 GLY B C     
5876 O  O     . GLY B 260 ? 0.33890 0.41760 0.40540 -0.05110 -0.12020 0.05520  256 GLY B O     
5877 N  N     . VAL B 261 ? 0.40580 0.47640 0.44650 -0.04970 -0.12120 0.04860  257 VAL B N     
5878 C  CA    . VAL B 261 ? 0.29860 0.35790 0.33420 -0.04710 -0.11390 0.04280  257 VAL B CA    
5879 C  C     . VAL B 261 ? 0.33880 0.39010 0.36700 -0.05220 -0.11710 0.03470  257 VAL B C     
5880 O  O     . VAL B 261 ? 0.31700 0.36730 0.33440 -0.05580 -0.12270 0.03040  257 VAL B O     
5881 C  CB    . VAL B 261 ? 0.37040 0.42470 0.39440 -0.04230 -0.10900 0.04120  257 VAL B CB    
5882 C  CG1   . VAL B 261 ? 0.35900 0.40160 0.37660 -0.04010 -0.10230 0.03460  257 VAL B CG1   
5883 C  CG2   . VAL B 261 ? 0.34420 0.40510 0.37670 -0.03710 -0.10560 0.04920  257 VAL B CG2   
5884 N  N     . PHE B 262 ? 0.36430 0.40980 0.39820 -0.05240 -0.11340 0.03240  258 PHE B N     
5885 C  CA    . PHE B 262 ? 0.40610 0.44150 0.43320 -0.05600 -0.11470 0.02440  258 PHE B CA    
5886 C  C     . PHE B 262 ? 0.39570 0.42050 0.41290 -0.05170 -0.10780 0.01910  258 PHE B C     
5887 O  O     . PHE B 262 ? 0.44250 0.46650 0.46400 -0.04710 -0.10100 0.02190  258 PHE B O     
5888 C  CB    . PHE B 262 ? 0.42710 0.46240 0.46690 -0.05940 -0.11540 0.02580  258 PHE B CB    
5889 C  CG    . PHE B 262 ? 0.46450 0.48830 0.49870 -0.06260 -0.11620 0.01810  258 PHE B CG    
5890 C  CD1   . PHE B 262 ? 0.37860 0.39920 0.40540 -0.06800 -0.12330 0.01220  258 PHE B CD1   
5891 C  CD2   . PHE B 262 ? 0.41200 0.42790 0.44780 -0.06010 -0.10980 0.01650  258 PHE B CD2   
5892 C  CE1   . PHE B 262 ? 0.46970 0.47870 0.49180 -0.07060 -0.12380 0.00470  258 PHE B CE1   
5893 C  CE2   . PHE B 262 ? 0.43510 0.44010 0.46670 -0.06270 -0.11060 0.00980  258 PHE B CE2   
5894 C  CZ    . PHE B 262 ? 0.48180 0.48290 0.50680 -0.06780 -0.11740 0.00370  258 PHE B CZ    
5895 N  N     . GLY B 263 ? 0.35290 0.36990 0.35720 -0.05330 -0.10960 0.01130  259 GLY B N     
5896 C  CA    . GLY B 263 ? 0.32150 0.32880 0.31710 -0.04960 -0.10340 0.00610  259 GLY B CA    
5897 C  C     . GLY B 263 ? 0.43870 0.44580 0.42070 -0.04690 -0.10230 0.00370  259 GLY B C     
5898 O  O     . GLY B 263 ? 0.49360 0.50560 0.46930 -0.04930 -0.10760 0.00340  259 GLY B O     
5899 N  N     . PHE B 264 ? 0.38350 0.38600 0.36130 -0.04190 -0.09550 0.00280  260 PHE B N     
5900 C  CA    . PHE B 264 ? 0.46050 0.46200 0.42510 -0.03960 -0.09390 -0.00010 260 PHE B CA    
5901 C  C     . PHE B 264 ? 0.38480 0.39630 0.34830 -0.03950 -0.09700 0.00580  260 PHE B C     
5902 O  O     . PHE B 264 ? 0.38120 0.39880 0.35420 -0.03740 -0.09560 0.01330  260 PHE B O     
5903 C  CB    . PHE B 264 ? 0.46890 0.46540 0.43190 -0.03440 -0.08590 -0.00040 260 PHE B CB    
5904 C  CG    . PHE B 264 ? 0.52210 0.51700 0.47210 -0.03200 -0.08370 -0.00360 260 PHE B CG    
5905 C  CD1   . PHE B 264 ? 0.59890 0.58780 0.53830 -0.03330 -0.08450 -0.01180 260 PHE B CD1   
5906 C  CD2   . PHE B 264 ? 0.54120 0.54090 0.48990 -0.02860 -0.08060 0.00150  260 PHE B CD2   
5907 C  CE1   . PHE B 264 ? 0.66270 0.65120 0.59020 -0.03110 -0.08190 -0.01460 260 PHE B CE1   
5908 C  CE2   . PHE B 264 ? 0.58320 0.58220 0.52020 -0.02680 -0.07850 -0.00090 260 PHE B CE2   
5909 C  CZ    . PHE B 264 ? 0.62370 0.61760 0.55000 -0.02800 -0.07900 -0.00890 260 PHE B CZ    
5910 N  N     . ALA B 265 ? 0.39290 0.40600 0.34450 -0.04170 -0.10100 0.00260  261 ALA B N     
5911 C  CA    . ALA B 265 ? 0.41560 0.43840 0.36450 -0.04220 -0.10480 0.00820  261 ALA B CA    
5912 C  C     . ALA B 265 ? 0.41530 0.44700 0.37590 -0.04530 -0.11090 0.01460  261 ALA B C     
5913 O  O     . ALA B 265 ? 0.44260 0.48320 0.40550 -0.04480 -0.11340 0.02170  261 ALA B O     
5914 C  CB    . ALA B 265 ? 0.35160 0.37660 0.30080 -0.03680 -0.09910 0.01380  261 ALA B CB    
5915 N  N     . GLY B 266 ? 0.41980 0.44920 0.38780 -0.04880 -0.11350 0.01240  262 GLY B N     
5916 C  CA    . GLY B 266 ? 0.34130 0.37920 0.32240 -0.05170 -0.11850 0.01870  262 GLY B CA    
5917 C  C     . GLY B 266 ? 0.46530 0.51000 0.44170 -0.05720 -0.12760 0.01850  262 GLY B C     
5918 O  O     . GLY B 266 ? 0.45540 0.49930 0.41730 -0.05870 -0.13010 0.01410  262 GLY B O     
5919 N  N     . HIS B 267 ? 0.40630 0.45830 0.39510 -0.06060 -0.13270 0.02340  263 HIS B N     
5920 C  CA    . HIS B 267 ? 0.42780 0.48880 0.41520 -0.06600 -0.14200 0.02540  263 HIS B CA    
5921 C  C     . HIS B 267 ? 0.44080 0.49800 0.42830 -0.07280 -0.14780 0.01910  263 HIS B C     
5922 O  O     . HIS B 267 ? 0.40000 0.45240 0.39710 -0.07360 -0.14570 0.01790  263 HIS B O     
5923 C  CB    . HIS B 267 ? 0.38970 0.46340 0.39230 -0.06500 -0.14410 0.03660  263 HIS B CB    
5924 C  CG    . HIS B 267 ? 0.45840 0.53500 0.46160 -0.05840 -0.13870 0.04270  263 HIS B CG    
5925 N  ND1   . HIS B 267 ? 0.40660 0.48120 0.42010 -0.05280 -0.13090 0.04630  263 HIS B ND1   
5926 C  CD2   . HIS B 267 ? 0.41110 0.49150 0.40480 -0.05670 -0.13960 0.04530  263 HIS B CD2   
5927 C  CE1   . HIS B 267 ? 0.45280 0.52950 0.46400 -0.04800 -0.12750 0.05080  263 HIS B CE1   
5928 N  NE2   . HIS B 267 ? 0.42480 0.50510 0.42430 -0.05020 -0.13270 0.05070  263 HIS B NE2   
5929 N  N     . GLN B 268 ? 0.45490 0.51430 0.43110 -0.07800 -0.15510 0.01500  264 GLN B N     
5930 C  CA    . GLN B 268 ? 0.49690 0.55250 0.47210 -0.08520 -0.16170 0.00840  264 GLN B CA    
5931 C  C     . GLN B 268 ? 0.45310 0.51580 0.44700 -0.08860 -0.16560 0.01500  264 GLN B C     
5932 O  O     . GLN B 268 ? 0.53330 0.59010 0.53240 -0.09270 -0.16740 0.01090  264 GLN B O     
5933 C  CB    . GLN B 268 ? 0.53730 0.59680 0.49780 -0.09040 -0.16960 0.00430  264 GLN B CB    
5934 C  CG    . GLN B 268 ? 0.61710 0.66760 0.56980 -0.09680 -0.17430 -0.00680 264 GLN B CG    
5935 C  CD    . GLN B 268 ? 0.72850 0.76390 0.67190 -0.09350 -0.16710 -0.01650 264 GLN B CD    
5936 O  OE1   . GLN B 268 ? 0.81380 0.84680 0.74560 -0.08870 -0.16180 -0.01870 264 GLN B OE1   
5937 N  NE2   . GLN B 268 ? 0.75150 0.77690 0.70070 -0.09590 -0.16680 -0.02200 264 GLN B NE2   
5938 N  N     . LYS B 269 ? 0.46480 0.54040 0.46940 -0.08680 -0.16700 0.02550  265 LYS B N     
5939 C  CA    . LYS B 269 ? 0.46980 0.55380 0.49370 -0.08920 -0.16980 0.03280  265 LYS B CA    
5940 C  C     . LYS B 269 ? 0.47970 0.55610 0.51410 -0.08700 -0.16290 0.03190  265 LYS B C     
5941 O  O     . LYS B 269 ? 0.39000 0.46680 0.43460 -0.09180 -0.16610 0.03190  265 LYS B O     
5942 C  CB    . LYS B 269 ? 0.46330 0.56100 0.49750 -0.08530 -0.16980 0.04430  265 LYS B CB    
5943 C  CG    . LYS B 269 ? 0.50290 0.61180 0.55720 -0.08760 -0.17320 0.05260  265 LYS B CG    
5944 C  CD    . LYS B 269 ? 0.55070 0.67310 0.61350 -0.08360 -0.17380 0.06340  265 LYS B CD    
5945 C  CE    . LYS B 269 ? 0.57830 0.71420 0.66100 -0.08630 -0.17860 0.07200  265 LYS B CE    
5946 N  NZ    . LYS B 269 ? 0.61980 0.76690 0.71340 -0.08040 -0.17670 0.08270  265 LYS B NZ    
5947 N  N     . ALA B 270 ? 0.39660 0.46670 0.42880 -0.08000 -0.15360 0.03150  266 ALA B N     
5948 C  CA    . ALA B 270 ? 0.43360 0.49690 0.47460 -0.07810 -0.14710 0.03090  266 ALA B CA    
5949 C  C     . ALA B 270 ? 0.45030 0.50040 0.48340 -0.08170 -0.14770 0.02100  266 ALA B C     
5950 O  O     . ALA B 270 ? 0.44690 0.49390 0.48960 -0.08470 -0.14780 0.02080  266 ALA B O     
5951 C  CB    . ALA B 270 ? 0.35400 0.41450 0.39470 -0.06990 -0.13730 0.03310  266 ALA B CB    
5952 N  N     . THR B 271 ? 0.48920 0.53140 0.50520 -0.08160 -0.14810 0.01300  267 THR B N     
5953 C  CA    . THR B 271 ? 0.53450 0.56340 0.54300 -0.08450 -0.14840 0.00320  267 THR B CA    
5954 C  C     . THR B 271 ? 0.54190 0.57150 0.55630 -0.09280 -0.15670 0.00130  267 THR B C     
5955 O  O     . THR B 271 ? 0.57380 0.59560 0.59450 -0.09520 -0.15610 -0.00140 267 THR B O     
5956 C  CB    . THR B 271 ? 0.56030 0.58280 0.54960 -0.08320 -0.14800 -0.00500 267 THR B CB    
5957 O  OG1   . THR B 271 ? 0.53800 0.56080 0.52270 -0.07590 -0.14050 -0.00250 267 THR B OG1   
5958 C  CG2   . THR B 271 ? 0.53980 0.54770 0.52220 -0.08510 -0.14710 -0.01550 267 THR B CG2   
5959 N  N     . ASP B 272 ? 0.48220 0.52140 0.49530 -0.09750 -0.16500 0.00320  268 ASP B N     
5960 C  CA    . ASP B 272 ? 0.56330 0.60380 0.58180 -0.10600 -0.17370 0.00150  268 ASP B CA    
5961 C  C     . ASP B 272 ? 0.63270 0.67800 0.67140 -0.10760 -0.17320 0.00900  268 ASP B C     
5962 O  O     . ASP B 272 ? 0.67260 0.71220 0.71710 -0.11320 -0.17650 0.00590  268 ASP B O     
5963 C  CB    . ASP B 272 ? 0.50550 0.55760 0.51960 -0.11060 -0.18270 0.00370  268 ASP B CB    
5964 C  CG    . ASP B 272 ? 0.55820 0.60600 0.55120 -0.11040 -0.18420 -0.00440 268 ASP B CG    
5965 O  OD1   . ASP B 272 ? 0.53470 0.56970 0.51660 -0.10750 -0.17880 -0.01280 268 ASP B OD1   
5966 O  OD2   . ASP B 272 ? 0.65370 0.71170 0.64130 -0.11330 -0.19080 -0.00190 268 ASP B OD2   
5967 N  N     . TYR B 273 ? 0.47420 0.53030 0.52440 -0.10300 -0.16920 0.01890  269 TYR B N     
5968 C  CA    . TYR B 273 ? 0.47560 0.53800 0.54510 -0.10460 -0.16870 0.02630  269 TYR B CA    
5969 C  C     . TYR B 273 ? 0.49840 0.54950 0.57160 -0.10300 -0.16210 0.02350  269 TYR B C     
5970 O  O     . TYR B 273 ? 0.48210 0.53220 0.56590 -0.10810 -0.16450 0.02440  269 TYR B O     
5971 C  CB    . TYR B 273 ? 0.47990 0.55600 0.56050 -0.09920 -0.16520 0.03690  269 TYR B CB    
5972 C  CG    . TYR B 273 ? 0.54370 0.63200 0.64420 -0.10270 -0.16820 0.04540  269 TYR B CG    
5973 C  CD1   . TYR B 273 ? 0.52910 0.61700 0.64280 -0.10140 -0.16240 0.04890  269 TYR B CD1   
5974 C  CD2   . TYR B 273 ? 0.58520 0.68640 0.69160 -0.10750 -0.17700 0.05010  269 TYR B CD2   
5975 C  CE1   . TYR B 273 ? 0.52920 0.62910 0.66140 -0.10460 -0.16470 0.05690  269 TYR B CE1   
5976 C  CE2   . TYR B 273 ? 0.58390 0.69720 0.70960 -0.11070 -0.17970 0.05830  269 TYR B CE2   
5977 C  CZ    . TYR B 273 ? 0.61630 0.72900 0.75500 -0.10910 -0.17330 0.06160  269 TYR B CZ    
5978 O  OH    . TYR B 273 ? 0.71200 0.83740 0.87020 -0.11220 -0.17540 0.06980  269 TYR B OH    
5979 N  N     . LEU B 274 ? 0.48810 0.53070 0.55270 -0.09640 -0.15400 0.02030  270 LEU B N     
5980 C  CA    . LEU B 274 ? 0.44280 0.47720 0.51240 -0.09380 -0.14680 0.01990  270 LEU B CA    
5981 C  C     . LEU B 274 ? 0.53470 0.55360 0.59650 -0.09680 -0.14770 0.01070  270 LEU B C     
5982 O  O     . LEU B 274 ? 0.47970 0.49280 0.54900 -0.09730 -0.14450 0.01130  270 LEU B O     
5983 C  CB    . LEU B 274 ? 0.42510 0.45840 0.49060 -0.08520 -0.13750 0.02170  270 LEU B CB    
5984 C  CG    . LEU B 274 ? 0.46490 0.51160 0.54010 -0.08090 -0.13450 0.03110  270 LEU B CG    
5985 C  CD1   . LEU B 274 ? 0.48380 0.52730 0.55500 -0.07300 -0.12510 0.03180  270 LEU B CD1   
5986 C  CD2   . LEU B 274 ? 0.47640 0.53170 0.56980 -0.08390 -0.13530 0.03820  270 LEU B CD2   
5987 N  N     . LEU B 275 ? 0.53720 0.54950 0.58440 -0.09860 -0.15170 0.00220  271 LEU B N     
5988 C  CA    . LEU B 275 ? 0.59220 0.58900 0.63170 -0.10080 -0.15220 -0.00740 271 LEU B CA    
5989 C  C     . LEU B 275 ? 0.67820 0.67230 0.71750 -0.10950 -0.16170 -0.01250 271 LEU B C     
5990 O  O     . LEU B 275 ? 0.69110 0.67180 0.72420 -0.11180 -0.16280 -0.02120 271 LEU B O     
5991 C  CB    . LEU B 275 ? 0.48000 0.46910 0.50220 -0.09560 -0.14810 -0.01480 271 LEU B CB    
5992 C  CG    . LEU B 275 ? 0.51910 0.50940 0.53980 -0.08720 -0.13890 -0.01110 271 LEU B CG    
5993 C  CD1   . LEU B 275 ? 0.54410 0.52810 0.54770 -0.08320 -0.13630 -0.01840 271 LEU B CD1   
5994 C  CD2   . LEU B 275 ? 0.51820 0.50210 0.54790 -0.08480 -0.13280 -0.00890 271 LEU B CD2   
5995 N  N     . SER B 276 ? 0.64850 0.65490 0.69490 -0.11450 -0.16860 -0.00720 272 SER B N     
5996 C  CA    . SER B 276 ? 0.65700 0.66230 0.70320 -0.12350 -0.17850 -0.01170 272 SER B CA    
5997 C  C     . SER B 276 ? 0.70580 0.70340 0.76380 -0.12880 -0.18020 -0.01230 272 SER B C     
5998 O  O     . SER B 276 ? 0.71870 0.71150 0.77570 -0.13650 -0.18790 -0.01780 272 SER B O     
5999 C  CB    . SER B 276 ? 0.64130 0.66350 0.69360 -0.12720 -0.18550 -0.00460 272 SER B CB    
6000 O  OG    . SER B 276 ? 0.73630 0.76960 0.80690 -0.12640 -0.18330 0.00660  272 SER B OG    
6001 N  N     . GLY B 277 ? 0.59340 0.59030 0.66280 -0.12540 -0.17340 -0.00630 273 GLY B N     
6002 C  CA    . GLY B 277 ? 0.58880 0.58060 0.67120 -0.13060 -0.17500 -0.00460 273 GLY B CA    
6003 C  C     . GLY B 277 ? 0.55010 0.55610 0.64990 -0.13570 -0.17920 0.00520  273 GLY B C     
6004 O  O     . GLY B 277 ? 0.63730 0.64060 0.74940 -0.14060 -0.18060 0.00780  273 GLY B O     
6005 N  N     . ASP B 278 ? 0.49770 0.51910 0.59980 -0.13490 -0.18130 0.01120  274 ASP B N     
6006 C  CA    . ASP B 278 ? 0.58530 0.62130 0.70480 -0.13980 -0.18570 0.02050  274 ASP B CA    
6007 C  C     . ASP B 278 ? 0.57170 0.61860 0.70460 -0.13420 -0.17790 0.03110  274 ASP B C     
6008 O  O     . ASP B 278 ? 0.50250 0.56030 0.65200 -0.13810 -0.18000 0.03910  274 ASP B O     
6009 C  CB    . ASP B 278 ? 0.66620 0.71410 0.78270 -0.14310 -0.19390 0.02150  274 ASP B CB    
6010 C  CG    . ASP B 278 ? 0.82330 0.86140 0.92520 -0.14900 -0.20180 0.01050  274 ASP B CG    
6011 O  OD1   . ASP B 278 ? 0.85030 0.87730 0.95370 -0.15520 -0.20550 0.00490  274 ASP B OD1   
6012 O  OD2   . ASP B 278 ? 0.87790 0.91920 0.96660 -0.14740 -0.20430 0.00730  274 ASP B OD2   
6013 N  N     . VAL B 279 ? 0.50930 0.55380 0.63570 -0.12540 -0.16890 0.03140  275 VAL B N     
6014 C  CA    . VAL B 279 ? 0.45060 0.50500 0.58890 -0.12010 -0.16120 0.04060  275 VAL B CA    
6015 C  C     . VAL B 279 ? 0.38100 0.43110 0.53030 -0.12260 -0.15810 0.04330  275 VAL B C     
6016 O  O     . VAL B 279 ? 0.44160 0.47750 0.58430 -0.12180 -0.15510 0.03790  275 VAL B O     
6017 C  CB    . VAL B 279 ? 0.43920 0.49110 0.56720 -0.11050 -0.15270 0.03960  275 VAL B CB    
6018 C  CG1   . VAL B 279 ? 0.32920 0.38800 0.46850 -0.10540 -0.14390 0.04740  275 VAL B CG1   
6019 C  CG2   . VAL B 279 ? 0.44540 0.50540 0.56640 -0.10800 -0.15550 0.04000  275 VAL B CG2   
6020 N  N     . ASP B 280 ? 0.40660 0.46940 0.57320 -0.12560 -0.15870 0.05220  276 ASP B N     
6021 C  CA    . ASP B 280 ? 0.36780 0.42790 0.54540 -0.12830 -0.15560 0.05590  276 ASP B CA    
6022 C  C     . ASP B 280 ? 0.40440 0.46880 0.58590 -0.12080 -0.14490 0.06140  276 ASP B C     
6023 O  O     . ASP B 280 ? 0.43770 0.49350 0.61880 -0.12000 -0.13990 0.06090  276 ASP B O     
6024 C  CB    . ASP B 280 ? 0.38190 0.45270 0.57670 -0.13670 -0.16220 0.06240  276 ASP B CB    
6025 C  CG    . ASP B 280 ? 0.45760 0.54800 0.66300 -0.13540 -0.16320 0.07040  276 ASP B CG    
6026 O  OD1   . ASP B 280 ? 0.49640 0.59140 0.69530 -0.12840 -0.15970 0.07060  276 ASP B OD1   
6027 O  OD2   . ASP B 280 ? 0.48660 0.58820 0.70780 -0.14160 -0.16780 0.07690  276 ASP B OD2   
6028 N  N     . VAL B 281 ? 0.37240 0.44920 0.55670 -0.11520 -0.14110 0.06630  277 VAL B N     
6029 C  CA    . VAL B 281 ? 0.35480 0.43590 0.54210 -0.10800 -0.13070 0.07080  277 VAL B CA    
6030 C  C     . VAL B 281 ? 0.36870 0.44820 0.54340 -0.10010 -0.12680 0.06750  277 VAL B C     
6031 O  O     . VAL B 281 ? 0.31410 0.40240 0.48930 -0.09850 -0.12960 0.06920  277 VAL B O     
6032 C  CB    . VAL B 281 ? 0.36750 0.46600 0.57310 -0.10850 -0.12850 0.08080  277 VAL B CB    
6033 C  CG1   . VAL B 281 ? 0.37760 0.48040 0.58450 -0.10060 -0.11760 0.08430  277 VAL B CG1   
6034 C  CG2   . VAL B 281 ? 0.30480 0.40460 0.52300 -0.11670 -0.13200 0.08460  277 VAL B CG2   
6035 N  N     . LEU B 282 ? 0.35510 0.42360 0.51890 -0.09520 -0.12050 0.06310  278 LEU B N     
6036 C  CA    . LEU B 282 ? 0.34900 0.41510 0.50110 -0.08780 -0.11600 0.06000  278 LEU B CA    
6037 C  C     . LEU B 282 ? 0.37810 0.44840 0.53400 -0.08150 -0.10610 0.06430  278 LEU B C     
6038 O  O     . LEU B 282 ? 0.37050 0.43630 0.52820 -0.08180 -0.10170 0.06490  278 LEU B O     
6039 C  CB    . LEU B 282 ? 0.31510 0.36530 0.45050 -0.08690 -0.11670 0.05090  278 LEU B CB    
6040 C  CG    . LEU B 282 ? 0.31310 0.36030 0.43620 -0.07950 -0.11180 0.04790  278 LEU B CG    
6041 C  CD1   . LEU B 282 ? 0.38280 0.43800 0.50370 -0.07870 -0.11620 0.04880  278 LEU B CD1   
6042 C  CD2   . LEU B 282 ? 0.39220 0.42410 0.50070 -0.07870 -0.11130 0.03950  278 LEU B CD2   
6043 N  N     . ILE B 283 ? 0.32670 0.40550 0.48410 -0.07600 -0.10280 0.06730  279 ILE B N     
6044 C  CA    . ILE B 283 ? 0.34570 0.42860 0.50620 -0.06970 -0.09340 0.07060  279 ILE B CA    
6045 C  C     . ILE B 283 ? 0.32430 0.39960 0.47070 -0.06330 -0.08940 0.06570  279 ILE B C     
6046 O  O     . ILE B 283 ? 0.29440 0.37270 0.43740 -0.06070 -0.09140 0.06550  279 ILE B O     
6047 C  CB    . ILE B 283 ? 0.29760 0.39660 0.47310 -0.06810 -0.09170 0.07820  279 ILE B CB    
6048 C  CG1   . ILE B 283 ? 0.33220 0.43920 0.52200 -0.07510 -0.09620 0.08320  279 ILE B CG1   
6049 C  CG2   . ILE B 283 ? 0.24900 0.35130 0.42690 -0.06170 -0.08150 0.08060  279 ILE B CG2   
6050 C  CD1   . ILE B 283 ? 0.37010 0.49380 0.57550 -0.07440 -0.09650 0.09060  279 ILE B CD1   
6051 N  N     . VAL B 284 ? 0.31090 0.37690 0.44950 -0.06090 -0.08380 0.06240  280 VAL B N     
6052 C  CA    . VAL B 284 ? 0.29990 0.35880 0.42580 -0.05500 -0.07940 0.05820  280 VAL B CA    
6053 C  C     . VAL B 284 ? 0.31500 0.38020 0.44570 -0.04950 -0.07090 0.06190  280 VAL B C     
6054 O  O     . VAL B 284 ? 0.29900 0.36570 0.43460 -0.04970 -0.06610 0.06410  280 VAL B O     
6055 C  CB    . VAL B 284 ? 0.29850 0.34370 0.41320 -0.05570 -0.07860 0.05220  280 VAL B CB    
6056 C  CG1   . VAL B 284 ? 0.25330 0.29240 0.35620 -0.04960 -0.07340 0.04850  280 VAL B CG1   
6057 C  CG2   . VAL B 284 ? 0.29520 0.33360 0.40490 -0.06090 -0.08680 0.04760  280 VAL B CG2   
6058 N  N     . ILE B 285 ? 0.28000 0.34870 0.40920 -0.04460 -0.06910 0.06250  281 ILE B N     
6059 C  CA    . ILE B 285 ? 0.32310 0.39720 0.45670 -0.03890 -0.06120 0.06520  281 ILE B CA    
6060 C  C     . ILE B 285 ? 0.32410 0.39000 0.44520 -0.03390 -0.05740 0.06080  281 ILE B C     
6061 O  O     . ILE B 285 ? 0.28360 0.34830 0.39960 -0.03210 -0.06030 0.05970  281 ILE B O     
6062 C  CB    . ILE B 285 ? 0.26800 0.35480 0.41430 -0.03720 -0.06180 0.07090  281 ILE B CB    
6063 C  CG1   . ILE B 285 ? 0.29220 0.38690 0.44940 -0.04310 -0.06840 0.07480  281 ILE B CG1   
6064 C  CG2   . ILE B 285 ? 0.30050 0.39320 0.45380 -0.03210 -0.05280 0.07370  281 ILE B CG2   
6065 C  CD1   . ILE B 285 ? 0.38820 0.49670 0.55960 -0.04150 -0.06920 0.08120  281 ILE B CD1   
6066 N  N     . GLY B 286 ? 0.28140 0.34230 0.39790 -0.03180 -0.05100 0.05890  282 GLY B N     
6067 C  CA    . GLY B 286 ? 0.25510 0.30930 0.36120 -0.02690 -0.04670 0.05530  282 GLY B CA    
6068 C  C     . GLY B 286 ? 0.27020 0.31490 0.36350 -0.02750 -0.05070 0.05030  282 GLY B C     
6069 O  O     . GLY B 286 ? 0.31360 0.35620 0.40090 -0.02390 -0.05000 0.04900  282 GLY B O     
6070 N  N     . SER B 287 ? 0.29200 0.33070 0.38110 -0.03180 -0.05480 0.04760  283 SER B N     
6071 C  CA    . SER B 287 ? 0.33620 0.36510 0.41260 -0.03190 -0.05730 0.04200  283 SER B CA    
6072 C  C     . SER B 287 ? 0.33520 0.35590 0.40680 -0.03300 -0.05500 0.03910  283 SER B C     
6073 O  O     . SER B 287 ? 0.25150 0.27320 0.32960 -0.03650 -0.05570 0.04090  283 SER B O     
6074 C  CB    . SER B 287 ? 0.40060 0.42890 0.47520 -0.03590 -0.06530 0.04040  283 SER B CB    
6075 O  OG    . SER B 287 ? 0.41210 0.43040 0.47470 -0.03640 -0.06700 0.03430  283 SER B OG    
6076 N  N     . SER B 288 ? 0.24780 0.26090 0.30870 -0.03030 -0.05260 0.03490  284 SER B N     
6077 C  CA    . SER B 288 ? 0.35180 0.35680 0.40800 -0.03130 -0.05130 0.03210  284 SER B CA    
6078 C  C     . SER B 288 ? 0.34890 0.34720 0.40170 -0.03500 -0.05720 0.02830  284 SER B C     
6079 O  O     . SER B 288 ? 0.25990 0.25130 0.31060 -0.03610 -0.05680 0.02630  284 SER B O     
6080 C  CB    . SER B 288 ? 0.35280 0.35270 0.39960 -0.02700 -0.04670 0.02920  284 SER B CB    
6081 O  OG    . SER B 288 ? 0.38800 0.38480 0.42650 -0.02550 -0.04890 0.02570  284 SER B OG    
6082 N  N     . LEU B 289 ? 0.27040 0.27060 0.32280 -0.03700 -0.06280 0.02720  285 LEU B N     
6083 C  CA    . LEU B 289 ? 0.27290 0.26690 0.32200 -0.04090 -0.06870 0.02290  285 LEU B CA    
6084 C  C     . LEU B 289 ? 0.33660 0.32020 0.37490 -0.03900 -0.06730 0.01690  285 LEU B C     
6085 O  O     . LEU B 289 ? 0.39200 0.36810 0.42970 -0.04120 -0.06910 0.01390  285 LEU B O     
6086 C  CB    . LEU B 289 ? 0.27750 0.27160 0.33630 -0.04590 -0.07140 0.02520  285 LEU B CB    
6087 C  CG    . LEU B 289 ? 0.30760 0.31260 0.37810 -0.04860 -0.07380 0.03100  285 LEU B CG    
6088 C  CD1   . LEU B 289 ? 0.26660 0.27180 0.34700 -0.05370 -0.07580 0.03390  285 LEU B CD1   
6089 C  CD2   . LEU B 289 ? 0.28800 0.29680 0.35670 -0.05040 -0.08000 0.02980  285 LEU B CD2   
6090 N  N     . GLY B 290 ? 0.31190 0.29520 0.34230 -0.03470 -0.06410 0.01540  286 GLY B N     
6091 C  CA    . GLY B 290 ? 0.27680 0.25190 0.29680 -0.03260 -0.06290 0.00980  286 GLY B CA    
6092 C  C     . GLY B 290 ? 0.38220 0.35420 0.39490 -0.03440 -0.06810 0.00460  286 GLY B C     
6093 O  O     . GLY B 290 ? 0.35320 0.32820 0.36880 -0.03820 -0.07350 0.00480  286 GLY B O     
6094 N  N     . ASP B 291 ? 0.35790 0.32430 0.36070 -0.03180 -0.06630 -0.00030 287 ASP B N     
6095 C  CA    . ASP B 291 ? 0.35880 0.32070 0.35310 -0.03320 -0.07030 -0.00660 287 ASP B CA    
6096 C  C     . ASP B 291 ? 0.38510 0.35410 0.37700 -0.03500 -0.07470 -0.00560 287 ASP B C     
6097 O  O     . ASP B 291 ? 0.34470 0.31350 0.33640 -0.03910 -0.08050 -0.00790 287 ASP B O     
6098 C  CB    . ASP B 291 ? 0.46140 0.41820 0.44590 -0.02920 -0.06630 -0.01100 287 ASP B CB    
6099 C  CG    . ASP B 291 ? 0.53570 0.48780 0.51050 -0.03020 -0.06940 -0.01830 287 ASP B CG    
6100 O  OD1   . ASP B 291 ? 0.55440 0.50710 0.52900 -0.03430 -0.07500 -0.02020 287 ASP B OD1   
6101 O  OD2   . ASP B 291 ? 0.58050 0.52860 0.54770 -0.02710 -0.06610 -0.02220 287 ASP B OD2   
6102 N  N     . TRP B 292 ? 0.38380 0.35890 0.37360 -0.03190 -0.07220 -0.00200 288 TRP B N     
6103 C  CA    . TRP B 292 ? 0.44850 0.43050 0.43570 -0.03320 -0.07640 -0.00050 288 TRP B CA    
6104 C  C     . TRP B 292 ? 0.44810 0.43710 0.44600 -0.03670 -0.08070 0.00450  288 TRP B C     
6105 O  O     . TRP B 292 ? 0.39580 0.38930 0.39220 -0.03960 -0.08630 0.00460  288 TRP B O     
6106 C  CB    . TRP B 292 ? 0.40540 0.39160 0.38880 -0.02890 -0.07260 0.00280  288 TRP B CB    
6107 C  CG    . TRP B 292 ? 0.47560 0.45760 0.44660 -0.02700 -0.07090 -0.00220 288 TRP B CG    
6108 C  CD1   . TRP B 292 ? 0.52100 0.49600 0.48450 -0.02800 -0.07180 -0.00930 288 TRP B CD1   
6109 C  CD2   . TRP B 292 ? 0.57390 0.55850 0.53890 -0.02350 -0.06770 -0.00040 288 TRP B CD2   
6110 N  NE1   . TRP B 292 ? 0.48480 0.45870 0.43790 -0.02530 -0.06920 -0.01210 288 TRP B NE1   
6111 C  CE2   . TRP B 292 ? 0.53260 0.51240 0.48640 -0.02280 -0.06680 -0.00640 288 TRP B CE2   
6112 C  CE3   . TRP B 292 ? 0.60300 0.59350 0.57160 -0.02100 -0.06550 0.00580  288 TRP B CE3   
6113 C  CZ2   . TRP B 292 ? 0.59590 0.57720 0.54180 -0.01990 -0.06370 -0.00600 288 TRP B CZ2   
6114 C  CZ3   . TRP B 292 ? 0.68130 0.67230 0.64220 -0.01830 -0.06280 0.00610  288 TRP B CZ3   
6115 C  CH2   . TRP B 292 ? 0.64590 0.63280 0.59560 -0.01790 -0.06190 0.00050  288 TRP B CH2   
6116 N  N     . GLN B 293 ? 0.38030 0.37080 0.38900 -0.03660 -0.07810 0.00860  289 GLN B N     
6117 C  CA    . GLN B 293 ? 0.33370 0.33160 0.35400 -0.03970 -0.08150 0.01380  289 GLN B CA    
6118 C  C     . GLN B 293 ? 0.37440 0.36950 0.39720 -0.04540 -0.08750 0.01090  289 GLN B C     
6119 O  O     . GLN B 293 ? 0.40280 0.40480 0.43450 -0.04890 -0.09170 0.01480  289 GLN B O     
6120 C  CB    . GLN B 293 ? 0.27140 0.27200 0.30190 -0.03780 -0.07620 0.01880  289 GLN B CB    
6121 C  CG    . GLN B 293 ? 0.28220 0.28520 0.31140 -0.03230 -0.06990 0.02150  289 GLN B CG    
6122 C  CD    . GLN B 293 ? 0.40630 0.40120 0.42860 -0.02940 -0.06460 0.01790  289 GLN B CD    
6123 O  OE1   . GLN B 293 ? 0.41850 0.40680 0.43140 -0.02940 -0.06550 0.01260  289 GLN B OE1   
6124 N  NE2   . GLN B 293 ? 0.34740 0.34320 0.37440 -0.02710 -0.05910 0.02070  289 GLN B NE2   
6125 N  N     . THR B 294 ? 0.34640 0.33160 0.36230 -0.04660 -0.08820 0.00430  290 THR B N     
6126 C  CA    . THR B 294 ? 0.32170 0.30240 0.34120 -0.05200 -0.09320 0.00140  290 THR B CA    
6127 C  C     . THR B 294 ? 0.40260 0.37570 0.41100 -0.05400 -0.09720 -0.00700 290 THR B C     
6128 O  O     . THR B 294 ? 0.42050 0.38660 0.43050 -0.05790 -0.10050 -0.01100 290 THR B O     
6129 C  CB    . THR B 294 ? 0.42290 0.39760 0.44900 -0.05190 -0.08970 0.00210  290 THR B CB    
6130 O  OG1   . THR B 294 ? 0.41060 0.37750 0.42830 -0.04760 -0.08470 -0.00190 290 THR B OG1   
6131 C  CG2   . THR B 294 ? 0.41760 0.40040 0.45480 -0.05070 -0.08600 0.01010  290 THR B CG2   
6132 N  N     . ASN B 295 ? 0.40860 0.38250 0.40560 -0.05140 -0.09670 -0.00990 291 ASN B N     
6133 C  CA    . ASN B 295 ? 0.49000 0.45650 0.47490 -0.05250 -0.09900 -0.01860 291 ASN B CA    
6134 C  C     . ASN B 295 ? 0.50740 0.46190 0.49150 -0.05150 -0.09610 -0.02410 291 ASN B C     
6135 O  O     . ASN B 295 ? 0.50820 0.45530 0.49160 -0.05520 -0.09990 -0.02990 291 ASN B O     
6136 C  CB    . ASN B 295 ? 0.54660 0.51550 0.53110 -0.05880 -0.10730 -0.02080 291 ASN B CB    
6137 C  CG    . ASN B 295 ? 0.75820 0.72310 0.72820 -0.05970 -0.11000 -0.02910 291 ASN B CG    
6138 O  OD1   . ASN B 295 ? 0.92420 0.89090 0.88430 -0.05590 -0.10690 -0.03020 291 ASN B OD1   
6139 N  ND2   . ASN B 295 ? 0.64320 0.60250 0.61150 -0.06500 -0.11570 -0.03530 291 ASN B ND2   
6140 N  N     . SER B 296 ? 0.46470 0.41730 0.44900 -0.04650 -0.08930 -0.02240 292 SER B N     
6141 C  CA    . SER B 296 ? 0.51580 0.45840 0.50130 -0.04470 -0.08580 -0.02560 292 SER B CA    
6142 C  C     . SER B 296 ? 0.43120 0.36970 0.42750 -0.04910 -0.08880 -0.02430 292 SER B C     
6143 O  O     . SER B 296 ? 0.47930 0.40820 0.47500 -0.05090 -0.09070 -0.02990 292 SER B O     
6144 C  CB    . SER B 296 ? 0.53660 0.47090 0.51060 -0.04320 -0.08530 -0.03460 292 SER B CB    
6145 O  OG    . SER B 296 ? 0.61680 0.55600 0.58100 -0.03980 -0.08290 -0.03520 292 SER B OG    
6146 N  N     . TRP B 297 ? 0.43280 0.37880 0.43960 -0.05050 -0.08890 -0.01660 293 TRP B N     
6147 C  CA    . TRP B 297 ? 0.38770 0.33130 0.40600 -0.05440 -0.09080 -0.01360 293 TRP B CA    
6148 C  C     . TRP B 297 ? 0.42040 0.35860 0.43870 -0.06030 -0.09790 -0.01890 293 TRP B C     
6149 O  O     . TRP B 297 ? 0.38440 0.31350 0.40680 -0.06260 -0.09930 -0.02140 293 TRP B O     
6150 C  CB    . TRP B 297 ? 0.36410 0.30060 0.38510 -0.05160 -0.08580 -0.01310 293 TRP B CB    
6151 C  CG    . TRP B 297 ? 0.39340 0.33500 0.41220 -0.04610 -0.07920 -0.00920 293 TRP B CG    
6152 C  CD1   . TRP B 297 ? 0.42700 0.37760 0.45240 -0.04530 -0.07630 -0.00180 293 TRP B CD1   
6153 C  CD2   . TRP B 297 ? 0.36690 0.30530 0.37630 -0.04100 -0.07480 -0.01270 293 TRP B CD2   
6154 N  NE1   . TRP B 297 ? 0.39940 0.35170 0.41980 -0.04010 -0.07060 -0.00090 293 TRP B NE1   
6155 C  CE2   . TRP B 297 ? 0.43280 0.37800 0.44370 -0.03760 -0.06970 -0.00710 293 TRP B CE2   
6156 C  CE3   . TRP B 297 ? 0.38820 0.31870 0.38840 -0.03900 -0.07440 -0.02010 293 TRP B CE3   
6157 C  CZ2   . TRP B 297 ? 0.38480 0.32920 0.38860 -0.03270 -0.06480 -0.00840 293 TRP B CZ2   
6158 C  CZ3   . TRP B 297 ? 0.41900 0.34960 0.41250 -0.03380 -0.06910 -0.02100 293 TRP B CZ3   
6159 C  CH2   . TRP B 297 ? 0.43290 0.37030 0.42830 -0.03090 -0.06470 -0.01500 293 TRP B CH2   
6160 N  N     . ASP B 298 ? 0.44070 0.38450 0.45460 -0.06270 -0.10270 -0.02040 294 ASP B N     
6161 C  CA    . ASP B 298 ? 0.44850 0.38880 0.46210 -0.06900 -0.11010 -0.02520 294 ASP B CA    
6162 C  C     . ASP B 298 ? 0.47620 0.41710 0.50430 -0.07420 -0.11320 -0.02020 294 ASP B C     
6163 O  O     . ASP B 298 ? 0.48260 0.43400 0.52000 -0.07490 -0.11280 -0.01200 294 ASP B O     
6164 C  CB    . ASP B 298 ? 0.44210 0.39190 0.45020 -0.07090 -0.11480 -0.02500 294 ASP B CB    
6165 C  CG    . ASP B 298 ? 0.53740 0.48260 0.54020 -0.07680 -0.12240 -0.03240 294 ASP B CG    
6166 O  OD1   . ASP B 298 ? 0.51830 0.45590 0.52720 -0.08130 -0.12560 -0.03500 294 ASP B OD1   
6167 O  OD2   . ASP B 298 ? 0.52860 0.47810 0.52120 -0.07730 -0.12530 -0.03560 294 ASP B OD2   
6168 N  N     . PRO B 299 ? 0.48520 0.41520 0.51600 -0.07780 -0.11600 -0.02480 295 PRO B N     
6169 C  CA    . PRO B 299 ? 0.49430 0.42500 0.53930 -0.08330 -0.11920 -0.01950 295 PRO B CA    
6170 C  C     . PRO B 299 ? 0.52260 0.46260 0.57290 -0.08950 -0.12610 -0.01670 295 PRO B C     
6171 O  O     . PRO B 299 ? 0.53540 0.48090 0.59890 -0.09330 -0.12760 -0.00970 295 PRO B O     
6172 C  CB    . PRO B 299 ? 0.50160 0.41670 0.54640 -0.08570 -0.12120 -0.02640 295 PRO B CB    
6173 C  CG    . PRO B 299 ? 0.52900 0.43730 0.55900 -0.08340 -0.12160 -0.03670 295 PRO B CG    
6174 C  CD    . PRO B 299 ? 0.51000 0.42620 0.53200 -0.07670 -0.11580 -0.03450 295 PRO B CD    
6175 N  N     . ARG B 300 ? 0.52240 0.46500 0.56320 -0.09080 -0.13050 -0.02160 296 ARG B N     
6176 C  CA    . ARG B 300 ? 0.48840 0.44100 0.53430 -0.09680 -0.13770 -0.01860 296 ARG B CA    
6177 C  C     . ARG B 300 ? 0.48420 0.45200 0.53940 -0.09490 -0.13530 -0.00800 296 ARG B C     
6178 O  O     . ARG B 300 ? 0.46990 0.44740 0.53380 -0.09970 -0.14060 -0.00320 296 ARG B O     
6179 C  CB    . ARG B 300 ? 0.47690 0.42970 0.50910 -0.09820 -0.14260 -0.02590 296 ARG B CB    
6180 C  CG    . ARG B 300 ? 0.46280 0.40210 0.48840 -0.10270 -0.14740 -0.03650 296 ARG B CG    
6181 C  CD    . ARG B 300 ? 0.53900 0.47870 0.54850 -0.10290 -0.15060 -0.04430 296 ARG B CD    
6182 N  NE    . ARG B 300 ? 0.60230 0.54440 0.60170 -0.09510 -0.14380 -0.04430 296 ARG B NE    
6183 C  CZ    . ARG B 300 ? 0.64920 0.59450 0.63440 -0.09380 -0.14490 -0.04880 296 ARG B CZ    
6184 N  NH1   . ARG B 300 ? 0.71120 0.65800 0.69010 -0.09980 -0.15260 -0.05380 296 ARG B NH1   
6185 N  NH2   . ARG B 300 ? 0.49560 0.44300 0.47290 -0.08690 -0.13840 -0.04800 296 ARG B NH2   
6186 N  N     . LEU B 301 ? 0.46620 0.43660 0.52030 -0.08790 -0.12740 -0.00430 297 LEU B N     
6187 C  CA    . LEU B 301 ? 0.49080 0.47470 0.55450 -0.08570 -0.12440 0.00530  297 LEU B CA    
6188 C  C     . LEU B 301 ? 0.47280 0.46040 0.55240 -0.08960 -0.12480 0.01210  297 LEU B C     
6189 O  O     . LEU B 301 ? 0.47810 0.47840 0.56780 -0.09020 -0.12480 0.01960  297 LEU B O     
6190 C  CB    . LEU B 301 ? 0.47430 0.45820 0.53290 -0.07780 -0.11580 0.00680  297 LEU B CB    
6191 C  CG    . LEU B 301 ? 0.42970 0.42650 0.49470 -0.07410 -0.11190 0.01500  297 LEU B CG    
6192 C  CD1   . LEU B 301 ? 0.42590 0.43250 0.48970 -0.07540 -0.11710 0.01650  297 LEU B CD1   
6193 C  CD2   . LEU B 301 ? 0.41740 0.41180 0.47560 -0.06670 -0.10380 0.01470  297 LEU B CD2   
6194 N  N     . THR B 302 ? 0.51820 0.49540 0.60090 -0.09230 -0.12490 0.00980  298 THR B N     
6195 C  CA    . THR B 302 ? 0.45890 0.43890 0.55640 -0.09610 -0.12470 0.01650  298 THR B CA    
6196 C  C     . THR B 302 ? 0.43830 0.42850 0.54640 -0.10270 -0.13150 0.02080  298 THR B C     
6197 O  O     . THR B 302 ? 0.43420 0.42050 0.53950 -0.10820 -0.13910 0.01570  298 THR B O     
6198 C  CB    . THR B 302 ? 0.50040 0.46580 0.59810 -0.09870 -0.12540 0.01220  298 THR B CB    
6199 O  OG1   . THR B 302 ? 0.51270 0.46950 0.60110 -0.09220 -0.11910 0.00860  298 THR B OG1   
6200 C  CG2   . THR B 302 ? 0.44630 0.41440 0.55940 -0.10280 -0.12510 0.01990  298 THR B CG2   
6201 N  N     . PRO B 303 ? 0.44770 0.45090 0.56840 -0.10270 -0.12920 0.03000  299 PRO B N     
6202 C  CA    . PRO B 303 ? 0.42640 0.44030 0.55890 -0.10910 -0.13570 0.03490  299 PRO B CA    
6203 C  C     . PRO B 303 ? 0.46210 0.47030 0.60420 -0.11660 -0.13980 0.03560  299 PRO B C     
6204 O  O     . PRO B 303 ? 0.45050 0.44890 0.59310 -0.11610 -0.13630 0.03500  299 PRO B O     
6205 C  CB    . PRO B 303 ? 0.38610 0.41530 0.52910 -0.10540 -0.13010 0.04440  299 PRO B CB    
6206 C  CG    . PRO B 303 ? 0.39460 0.41820 0.53490 -0.09970 -0.12100 0.04520  299 PRO B CG    
6207 C  CD    . PRO B 303 ? 0.37730 0.38630 0.50160 -0.09670 -0.12040 0.03610  299 PRO B CD    
6208 N  N     . SER B 304 ? 0.44600 0.46060 0.59630 -0.12380 -0.14760 0.03750  300 SER B N     
6209 C  CA    . SER B 304 ? 0.45530 0.46360 0.61420 -0.13200 -0.15300 0.03730  300 SER B CA    
6210 C  C     . SER B 304 ? 0.48980 0.50650 0.66590 -0.13430 -0.14990 0.04750  300 SER B C     
6211 O  O     . SER B 304 ? 0.52980 0.53920 0.71280 -0.14000 -0.15240 0.04810  300 SER B O     
6212 C  CB    . SER B 304 ? 0.42850 0.43970 0.58860 -0.13950 -0.16340 0.03440  300 SER B CB    
6213 O  OG    . SER B 304 ? 0.51170 0.54100 0.68480 -0.14170 -0.16540 0.04330  300 SER B OG    
6214 N  N     . VAL B 305 ? 0.45360 0.48510 0.63650 -0.13010 -0.14440 0.05550  301 VAL B N     
6215 C  CA    . VAL B 305 ? 0.41540 0.45640 0.61460 -0.13250 -0.14130 0.06520  301 VAL B CA    
6216 C  C     . VAL B 305 ? 0.41550 0.45830 0.61290 -0.12490 -0.13070 0.06880  301 VAL B C     
6217 O  O     . VAL B 305 ? 0.55100 0.58940 0.75270 -0.12580 -0.12700 0.07180  301 VAL B O     
6218 C  CB    . VAL B 305 ? 0.43250 0.49200 0.64540 -0.13570 -0.14460 0.07260  301 VAL B CB    
6219 C  CG1   . VAL B 305 ? 0.33940 0.41020 0.56830 -0.13670 -0.13930 0.08290  301 VAL B CG1   
6220 C  CG2   . VAL B 305 ? 0.46900 0.52720 0.68560 -0.14490 -0.15570 0.07000  301 VAL B CG2   
6221 N  N     . ALA B 306 ? 0.39550 0.44500 0.58690 -0.11760 -0.12590 0.06870  302 ALA B N     
6222 C  CA    . ALA B 306 ? 0.37100 0.42350 0.56100 -0.11060 -0.11590 0.07200  302 ALA B CA    
6223 C  C     . ALA B 306 ? 0.43280 0.48290 0.60900 -0.10290 -0.11250 0.06690  302 ALA B C     
6224 O  O     . ALA B 306 ? 0.39110 0.44760 0.56570 -0.10160 -0.11540 0.06610  302 ALA B O     
6225 C  CB    . ALA B 306 ? 0.32310 0.39320 0.52800 -0.11030 -0.11180 0.08170  302 ALA B CB    
6226 N  N     . LEU B 307 ? 0.33730 0.37850 0.50420 -0.09780 -0.10630 0.06400  303 LEU B N     
6227 C  CA    . LEU B 307 ? 0.34920 0.38990 0.50510 -0.09010 -0.10110 0.06100  303 LEU B CA    
6228 C  C     . LEU B 307 ? 0.41890 0.46950 0.58090 -0.08560 -0.09250 0.06740  303 LEU B C     
6229 O  O     . LEU B 307 ? 0.35080 0.39970 0.51600 -0.08630 -0.08830 0.07040  303 LEU B O     
6230 C  CB    . LEU B 307 ? 0.38200 0.40720 0.52360 -0.08740 -0.09980 0.05340  303 LEU B CB    
6231 C  CG    . LEU B 307 ? 0.38930 0.41370 0.52060 -0.07940 -0.09310 0.05130  303 LEU B CG    
6232 C  CD1   . LEU B 307 ? 0.33260 0.36340 0.46020 -0.07690 -0.09530 0.05000  303 LEU B CD1   
6233 C  CD2   . LEU B 307 ? 0.44880 0.45870 0.56760 -0.07710 -0.09180 0.04460  303 LEU B CD2   
6234 N  N     . ILE B 308 ? 0.30530 0.36650 0.46950 -0.08140 -0.09000 0.06980  304 ILE B N     
6235 C  CA    . ILE B 308 ? 0.32100 0.39130 0.48990 -0.07640 -0.08150 0.07460  304 ILE B CA    
6236 C  C     . ILE B 308 ? 0.30440 0.36940 0.46050 -0.06920 -0.07680 0.07000  304 ILE B C     
6237 O  O     . ILE B 308 ? 0.36700 0.43040 0.51670 -0.06740 -0.08010 0.06650  304 ILE B O     
6238 C  CB    . ILE B 308 ? 0.32930 0.41590 0.51200 -0.07670 -0.08170 0.08110  304 ILE B CB    
6239 C  CG1   . ILE B 308 ? 0.30500 0.39780 0.50160 -0.08440 -0.08650 0.08630  304 ILE B CG1   
6240 C  CG2   . ILE B 308 ? 0.25630 0.35140 0.44220 -0.07020 -0.07220 0.08460  304 ILE B CG2   
6241 C  CD1   . ILE B 308 ? 0.31360 0.41960 0.52180 -0.08650 -0.09140 0.09050  304 ILE B CD1   
6242 N  N     . GLN B 309 ? 0.28690 0.34920 0.43870 -0.06550 -0.06940 0.07000  305 GLN B N     
6243 C  CA    . GLN B 309 ? 0.30780 0.36540 0.44820 -0.05900 -0.06480 0.06590  305 GLN B CA    
6244 C  C     . GLN B 309 ? 0.32310 0.38910 0.46760 -0.05440 -0.05640 0.06960  305 GLN B C     
6245 O  O     . GLN B 309 ? 0.28660 0.35440 0.43440 -0.05550 -0.05210 0.07260  305 GLN B O     
6246 C  CB    . GLN B 309 ? 0.34050 0.38410 0.46850 -0.05850 -0.06450 0.06030  305 GLN B CB    
6247 C  CG    . GLN B 309 ? 0.31540 0.35470 0.43200 -0.05210 -0.05980 0.05630  305 GLN B CG    
6248 C  CD    . GLN B 309 ? 0.42180 0.44780 0.52640 -0.05140 -0.06030 0.05060  305 GLN B CD    
6249 O  OE1   . GLN B 309 ? 0.36800 0.38790 0.47340 -0.05490 -0.06200 0.05040  305 GLN B OE1   
6250 N  NE2   . GLN B 309 ? 0.36010 0.38180 0.45440 -0.04690 -0.05870 0.04630  305 GLN B NE2   
6251 N  N     . ILE B 310 ? 0.30730 0.37790 0.45100 -0.04940 -0.05400 0.06930  306 ILE B N     
6252 C  CA    . ILE B 310 ? 0.32620 0.40430 0.47350 -0.04440 -0.04590 0.07180  306 ILE B CA    
6253 C  C     . ILE B 310 ? 0.37140 0.44110 0.50570 -0.03920 -0.04180 0.06670  306 ILE B C     
6254 O  O     . ILE B 310 ? 0.37150 0.43690 0.49940 -0.03710 -0.04470 0.06350  306 ILE B O     
6255 C  CB    . ILE B 310 ? 0.30830 0.39850 0.46680 -0.04250 -0.04610 0.07580  306 ILE B CB    
6256 C  CG1   . ILE B 310 ? 0.27450 0.37450 0.44730 -0.04790 -0.05000 0.08150  306 ILE B CG1   
6257 C  CG2   . ILE B 310 ? 0.25610 0.35170 0.41660 -0.03620 -0.03730 0.07670  306 ILE B CG2   
6258 C  CD1   . ILE B 310 ? 0.23250 0.34170 0.41470 -0.04800 -0.05500 0.08450  306 ILE B CD1   
6259 N  N     . ASP B 311 ? 0.35590 0.42370 0.48610 -0.03730 -0.03530 0.06620  307 ASP B N     
6260 C  CA    . ASP B 311 ? 0.31550 0.37550 0.43370 -0.03280 -0.03150 0.06150  307 ASP B CA    
6261 C  C     . ASP B 311 ? 0.25240 0.31590 0.37040 -0.03010 -0.02320 0.06240  307 ASP B C     
6262 O  O     . ASP B 311 ? 0.28940 0.35650 0.41130 -0.03280 -0.02090 0.06550  307 ASP B O     
6263 C  CB    . ASP B 311 ? 0.22750 0.27550 0.33500 -0.03480 -0.03490 0.05730  307 ASP B CB    
6264 C  CG    . ASP B 311 ? 0.41470 0.45530 0.51080 -0.03070 -0.03410 0.05230  307 ASP B CG    
6265 O  OD1   . ASP B 311 ? 0.29310 0.33220 0.38410 -0.02730 -0.02830 0.05100  307 ASP B OD1   
6266 O  OD2   . ASP B 311 ? 0.36460 0.40140 0.45700 -0.03100 -0.03930 0.04990  307 ASP B OD2   
6267 N  N     . ILE B 312 ? 0.26250 0.32480 0.37550 -0.02490 -0.01860 0.05980  308 ILE B N     
6268 C  CA    . ILE B 312 ? 0.32780 0.39260 0.43900 -0.02240 -0.01070 0.05960  308 ILE B CA    
6269 C  C     . ILE B 312 ? 0.33970 0.39650 0.44030 -0.02380 -0.00960 0.05710  308 ILE B C     
6270 O  O     . ILE B 312 ? 0.41900 0.47850 0.51790 -0.02350 -0.00400 0.05780  308 ILE B O     
6271 C  CB    . ILE B 312 ? 0.30450 0.36990 0.41430 -0.01660 -0.00630 0.05720  308 ILE B CB    
6272 C  CG1   . ILE B 312 ? 0.23240 0.30450 0.34540 -0.01420 0.00200  0.05800  308 ILE B CG1   
6273 C  CG2   . ILE B 312 ? 0.26990 0.32430 0.36690 -0.01450 -0.00700 0.05210  308 ILE B CG2   
6274 C  CD1   . ILE B 312 ? 0.27120 0.34450 0.38570 -0.00850 0.00630  0.05600  308 ILE B CD1   
6275 N  N     . ASP B 313 ? 0.31910 0.36670 0.41260 -0.02550 -0.01480 0.05450  309 ASP B N     
6276 C  CA    . ASP B 313 ? 0.27750 0.31750 0.36180 -0.02640 -0.01420 0.05240  309 ASP B CA    
6277 C  C     . ASP B 313 ? 0.34720 0.38630 0.43550 -0.03160 -0.01810 0.05540  309 ASP B C     
6278 O  O     . ASP B 313 ? 0.36370 0.39850 0.45310 -0.03400 -0.02430 0.05470  309 ASP B O     
6279 C  CB    . ASP B 313 ? 0.27440 0.30460 0.34870 -0.02440 -0.01680 0.04750  309 ASP B CB    
6280 C  CG    . ASP B 313 ? 0.36790 0.39060 0.43320 -0.02490 -0.01610 0.04540  309 ASP B CG    
6281 O  OD1   . ASP B 313 ? 0.30280 0.32710 0.36990 -0.02760 -0.01490 0.04820  309 ASP B OD1   
6282 O  OD2   . ASP B 313 ? 0.36110 0.37700 0.41800 -0.02270 -0.01670 0.04140  309 ASP B OD2   
6283 N  N     . PRO B 314 ? 0.38290 0.42560 0.47310 -0.03370 -0.01490 0.05890  310 PRO B N     
6284 C  CA    . PRO B 314 ? 0.34940 0.39140 0.44510 -0.03900 -0.01880 0.06260  310 PRO B CA    
6285 C  C     . PRO B 314 ? 0.36640 0.39670 0.45560 -0.04030 -0.02360 0.05970  310 PRO B C     
6286 O  O     . PRO B 314 ? 0.30590 0.33330 0.39990 -0.04440 -0.02870 0.06130  310 PRO B O     
6287 C  CB    . PRO B 314 ? 0.34260 0.39110 0.43990 -0.04030 -0.01340 0.06700  310 PRO B CB    
6288 C  CG    . PRO B 314 ? 0.30410 0.35210 0.39240 -0.03600 -0.00770 0.06370  310 PRO B CG    
6289 C  CD    . PRO B 314 ? 0.31350 0.36040 0.40030 -0.03180 -0.00770 0.05940  310 PRO B CD    
6290 N  N     . MET B 315 ? 0.24790 0.27140 0.32680 -0.03700 -0.02220 0.05520  311 MET B N     
6291 C  CA    . MET B 315 ? 0.32020 0.33290 0.39310 -0.03750 -0.02610 0.05220  311 MET B CA    
6292 C  C     . MET B 315 ? 0.39920 0.40670 0.47180 -0.03790 -0.03190 0.04840  311 MET B C     
6293 O  O     . MET B 315 ? 0.39520 0.39400 0.46470 -0.03910 -0.03570 0.04600  311 MET B O     
6294 C  CB    . MET B 315 ? 0.32110 0.32950 0.38370 -0.03390 -0.02270 0.04890  311 MET B CB    
6295 C  CG    . MET B 315 ? 0.38110 0.39480 0.44210 -0.03350 -0.01700 0.05180  311 MET B CG    
6296 S  SD    . MET B 315 ? 0.47900 0.49770 0.54820 -0.03860 -0.01710 0.05900  311 MET B SD    
6297 C  CE    . MET B 315 ? 0.48000 0.50790 0.54600 -0.03720 -0.00930 0.06120  311 MET B CE    
6298 N  N     . GLU B 316 ? 0.33870 0.35120 0.41430 -0.03690 -0.03280 0.04800  312 GLU B N     
6299 C  CA    . GLU B 316 ? 0.33340 0.34210 0.40840 -0.03770 -0.03860 0.04480  312 GLU B CA    
6300 C  C     . GLU B 316 ? 0.33220 0.34260 0.41620 -0.04290 -0.04380 0.04750  312 GLU B C     
6301 O  O     . GLU B 316 ? 0.36890 0.37450 0.45170 -0.04470 -0.04950 0.04440  312 GLU B O     
6302 C  CB    . GLU B 316 ? 0.29840 0.31200 0.37260 -0.03440 -0.03780 0.04370  312 GLU B CB    
6303 C  CG    . GLU B 316 ? 0.36170 0.37190 0.42640 -0.02960 -0.03390 0.04030  312 GLU B CG    
6304 C  CD    . GLU B 316 ? 0.47300 0.47350 0.52840 -0.02910 -0.03690 0.03530  312 GLU B CD    
6305 O  OE1   . GLU B 316 ? 0.54870 0.54580 0.59630 -0.02570 -0.03410 0.03260  312 GLU B OE1   
6306 O  OE2   . GLU B 316 ? 0.53250 0.52890 0.58880 -0.03210 -0.04210 0.03390  312 GLU B OE2   
6307 N  N     . ILE B 317 ? 0.34320 0.36080 0.43630 -0.04550 -0.04200 0.05300  313 ILE B N     
6308 C  CA    . ILE B 317 ? 0.37330 0.39470 0.47670 -0.05060 -0.04670 0.05640  313 ILE B CA    
6309 C  C     . ILE B 317 ? 0.43430 0.44600 0.53750 -0.05470 -0.05140 0.05530  313 ILE B C     
6310 O  O     . ILE B 317 ? 0.41760 0.42590 0.52010 -0.05540 -0.04910 0.05720  313 ILE B O     
6311 C  CB    . ILE B 317 ? 0.36190 0.39500 0.47550 -0.05200 -0.04270 0.06310  313 ILE B CB    
6312 C  CG1   . ILE B 317 ? 0.30400 0.34620 0.41890 -0.04770 -0.03840 0.06360  313 ILE B CG1   
6313 C  CG2   . ILE B 317 ? 0.37710 0.41400 0.50210 -0.05800 -0.04770 0.06720  313 ILE B CG2   
6314 C  CD1   . ILE B 317 ? 0.33090 0.38540 0.45540 -0.04810 -0.03320 0.06950  313 ILE B CD1   
6315 N  N     . GLY B 318 ? 0.37970 0.38690 0.48360 -0.05750 -0.05790 0.05220  314 GLY B N     
6316 C  CA    . GLY B 318 ? 0.32930 0.32610 0.43330 -0.06130 -0.06260 0.05030  314 GLY B CA    
6317 C  C     . GLY B 318 ? 0.34520 0.33040 0.43830 -0.05810 -0.06190 0.04460  314 GLY B C     
6318 O  O     . GLY B 318 ? 0.38910 0.36540 0.48270 -0.06030 -0.06420 0.04360  314 GLY B O     
6319 N  N     . LYS B 319 ? 0.33150 0.31670 0.41550 -0.05290 -0.05880 0.04100  315 LYS B N     
6320 C  CA    . LYS B 319 ? 0.37590 0.35150 0.45030 -0.04960 -0.05760 0.03610  315 LYS B CA    
6321 C  C     . LYS B 319 ? 0.47090 0.43630 0.54190 -0.05140 -0.06330 0.03010  315 LYS B C     
6322 O  O     . LYS B 319 ? 0.50200 0.45830 0.57210 -0.05190 -0.06410 0.02830  315 LYS B O     
6323 C  CB    . LYS B 319 ? 0.36960 0.34790 0.43550 -0.04420 -0.05340 0.03370  315 LYS B CB    
6324 C  CG    . LYS B 319 ? 0.30910 0.27930 0.36550 -0.04060 -0.05140 0.02930  315 LYS B CG    
6325 C  CD    . LYS B 319 ? 0.35850 0.33260 0.40800 -0.03590 -0.04720 0.02800  315 LYS B CD    
6326 C  CE    . LYS B 319 ? 0.42550 0.40000 0.47080 -0.03510 -0.05030 0.02420  315 LYS B CE    
6327 N  NZ    . LYS B 319 ? 0.40540 0.38480 0.44640 -0.03110 -0.04660 0.02430  315 LYS B NZ    
6328 N  N     . ASN B 320 ? 0.42720 0.39430 0.49670 -0.05250 -0.06730 0.02700  316 ASN B N     
6329 C  CA    . ASN B 320 ? 0.37270 0.33080 0.43730 -0.05410 -0.07250 0.02020  316 ASN B CA    
6330 C  C     . ASN B 320 ? 0.42130 0.37920 0.49330 -0.06030 -0.07900 0.02050  316 ASN B C     
6331 O  O     . ASN B 320 ? 0.43260 0.38120 0.50190 -0.06250 -0.08330 0.01500  316 ASN B O     
6332 C  CB    . ASN B 320 ? 0.33410 0.29360 0.38870 -0.05070 -0.07250 0.01540  316 ASN B CB    
6333 C  CG    . ASN B 320 ? 0.34030 0.29700 0.38640 -0.04500 -0.06710 0.01350  316 ASN B CG    
6334 O  OD1   . ASN B 320 ? 0.40430 0.35420 0.44930 -0.04390 -0.06520 0.01250  316 ASN B OD1   
6335 N  ND2   . ASN B 320 ? 0.32000 0.28220 0.36080 -0.04170 -0.06480 0.01330  316 ASN B ND2   
6336 N  N     . TYR B 321 ? 0.41580 0.38390 0.49740 -0.06320 -0.07970 0.02670  317 TYR B N     
6337 C  CA    . TYR B 321 ? 0.37070 0.34030 0.46080 -0.06960 -0.08590 0.02800  317 TYR B CA    
6338 C  C     . TYR B 321 ? 0.41090 0.38680 0.51340 -0.07260 -0.08410 0.03620  317 TYR B C     
6339 O  O     . TYR B 321 ? 0.36390 0.34920 0.46910 -0.06980 -0.07880 0.04140  317 TYR B O     
6340 C  CB    . TYR B 321 ? 0.31930 0.29740 0.40930 -0.07050 -0.08950 0.02770  317 TYR B CB    
6341 C  CG    . TYR B 321 ? 0.31920 0.29180 0.39740 -0.06900 -0.09250 0.01990  317 TYR B CG    
6342 C  CD1   . TYR B 321 ? 0.40910 0.38290 0.47760 -0.06310 -0.08840 0.01780  317 TYR B CD1   
6343 C  CD2   . TYR B 321 ? 0.37640 0.34280 0.45280 -0.07380 -0.09950 0.01460  317 TYR B CD2   
6344 C  CE1   . TYR B 321 ? 0.39070 0.36020 0.44800 -0.06180 -0.09090 0.01120  317 TYR B CE1   
6345 C  CE2   . TYR B 321 ? 0.42070 0.38290 0.48530 -0.07250 -0.10200 0.00740  317 TYR B CE2   
6346 C  CZ    . TYR B 321 ? 0.37880 0.34290 0.43400 -0.06640 -0.09750 0.00590  317 TYR B CZ    
6347 O  OH    . TYR B 321 ? 0.41630 0.37700 0.45960 -0.06530 -0.09980 -0.00080 317 TYR B OH    
6348 N  N     . PRO B 322 ? 0.41760 0.38870 0.52780 -0.07830 -0.08820 0.03760  318 PRO B N     
6349 C  CA    . PRO B 322 ? 0.48660 0.46490 0.60910 -0.08160 -0.08660 0.04620  318 PRO B CA    
6350 C  C     . PRO B 322 ? 0.39180 0.38470 0.52240 -0.08340 -0.08720 0.05110  318 PRO B C     
6351 O  O     . PRO B 322 ? 0.40630 0.40120 0.53770 -0.08600 -0.09270 0.04870  318 PRO B O     
6352 C  CB    . PRO B 322 ? 0.47620 0.44500 0.60490 -0.08780 -0.09220 0.04570  318 PRO B CB    
6353 C  CG    . PRO B 322 ? 0.40060 0.36100 0.52240 -0.08900 -0.09810 0.03700  318 PRO B CG    
6354 C  CD    . PRO B 322 ? 0.38120 0.34030 0.48960 -0.08210 -0.09460 0.03140  318 PRO B CD    
6355 N  N     . VAL B 323 ? 0.33990 0.34330 0.47650 -0.08190 -0.08150 0.05810  319 VAL B N     
6356 C  CA    . VAL B 323 ? 0.36920 0.38730 0.51450 -0.08270 -0.08100 0.06320  319 VAL B CA    
6357 C  C     . VAL B 323 ? 0.41770 0.44200 0.57710 -0.08880 -0.08240 0.07050  319 VAL B C     
6358 O  O     . VAL B 323 ? 0.39320 0.41310 0.55530 -0.09100 -0.08100 0.07350  319 VAL B O     
6359 C  CB    . VAL B 323 ? 0.40920 0.43630 0.55200 -0.07640 -0.07320 0.06560  319 VAL B CB    
6360 C  CG1   . VAL B 323 ? 0.49390 0.51470 0.62320 -0.07050 -0.07170 0.05880  319 VAL B CG1   
6361 C  CG2   . VAL B 323 ? 0.41020 0.43900 0.55530 -0.07580 -0.06700 0.07050  319 VAL B CG2   
6362 N  N     . ASP B 324 ? 0.43940 0.47480 0.60830 -0.09170 -0.08530 0.07400  320 ASP B N     
6363 C  CA    . ASP B 324 ? 0.40640 0.45110 0.59030 -0.09740 -0.08610 0.08190  320 ASP B CA    
6364 C  C     . ASP B 324 ? 0.40360 0.46380 0.59420 -0.09420 -0.07880 0.08860  320 ASP B C     
6365 O  O     . ASP B 324 ? 0.37460 0.44130 0.57430 -0.09700 -0.07580 0.09550  320 ASP B O     
6366 C  CB    . ASP B 324 ? 0.34570 0.39280 0.53700 -0.10360 -0.09480 0.08160  320 ASP B CB    
6367 C  CG    . ASP B 324 ? 0.47350 0.50470 0.65800 -0.10710 -0.10180 0.07440  320 ASP B CG    
6368 O  OD1   . ASP B 324 ? 0.53280 0.55610 0.72110 -0.11160 -0.10360 0.07560  320 ASP B OD1   
6369 O  OD2   . ASP B 324 ? 0.53000 0.55620 0.70490 -0.10520 -0.10530 0.06730  320 ASP B OD2   
6370 N  N     . VAL B 325 ? 0.34330 0.40940 0.52960 -0.08830 -0.07570 0.08660  321 VAL B N     
6371 C  CA    . VAL B 325 ? 0.31220 0.39100 0.50280 -0.08390 -0.06770 0.09130  321 VAL B CA    
6372 C  C     . VAL B 325 ? 0.33580 0.40920 0.51290 -0.07640 -0.06260 0.08600  321 VAL B C     
6373 O  O     . VAL B 325 ? 0.33660 0.40790 0.50770 -0.07320 -0.06470 0.08140  321 VAL B O     
6374 C  CB    . VAL B 325 ? 0.33370 0.42720 0.53620 -0.08440 -0.06910 0.09540  321 VAL B CB    
6375 C  CG1   . VAL B 325 ? 0.35710 0.46350 0.56520 -0.07970 -0.06010 0.10020  321 VAL B CG1   
6376 C  CG2   . VAL B 325 ? 0.29840 0.39630 0.51400 -0.09260 -0.07550 0.10020  321 VAL B CG2   
6377 N  N     . GLY B 326 ? 0.30370 0.37480 0.47580 -0.07390 -0.05610 0.08670  322 GLY B N     
6378 C  CA    . GLY B 326 ? 0.35070 0.41690 0.51050 -0.06730 -0.05100 0.08200  322 GLY B CA    
6379 C  C     . GLY B 326 ? 0.34520 0.42270 0.50780 -0.06280 -0.04280 0.08510  322 GLY B C     
6380 O  O     . GLY B 326 ? 0.30470 0.38690 0.47000 -0.06360 -0.03760 0.08920  322 GLY B O     
6381 N  N     . ILE B 327 ? 0.31010 0.39210 0.47220 -0.05820 -0.04150 0.08310  323 ILE B N     
6382 C  CA    . ILE B 327 ? 0.28360 0.37690 0.45060 -0.05390 -0.03410 0.08580  323 ILE B CA    
6383 C  C     . ILE B 327 ? 0.32880 0.41630 0.48360 -0.04780 -0.02870 0.08080  323 ILE B C     
6384 O  O     . ILE B 327 ? 0.24790 0.32900 0.39550 -0.04470 -0.03100 0.07620  323 ILE B O     
6385 C  CB    . ILE B 327 ? 0.29380 0.39700 0.47110 -0.05290 -0.03640 0.08800  323 ILE B CB    
6386 C  CG1   . ILE B 327 ? 0.27470 0.38500 0.46520 -0.05960 -0.04190 0.09340  323 ILE B CG1   
6387 C  CG2   . ILE B 327 ? 0.27110 0.38450 0.45300 -0.04730 -0.02830 0.08970  323 ILE B CG2   
6388 C  CD1   . ILE B 327 ? 0.26260 0.38290 0.46390 -0.05930 -0.04550 0.09590  323 ILE B CD1   
6389 N  N     . ASN B 328 ? 0.32300 0.41280 0.47520 -0.04630 -0.02160 0.08200  324 ASN B N     
6390 C  CA    . ASN B 328 ? 0.35820 0.44350 0.49940 -0.04080 -0.01600 0.07750  324 ASN B CA    
6391 C  C     . ASN B 328 ? 0.32110 0.41660 0.46820 -0.03620 -0.00980 0.07840  324 ASN B C     
6392 O  O     . ASN B 328 ? 0.32990 0.43430 0.48180 -0.03600 -0.00370 0.08160  324 ASN B O     
6393 C  CB    . ASN B 328 ? 0.30820 0.38970 0.44220 -0.04200 -0.01240 0.07770  324 ASN B CB    
6394 C  CG    . ASN B 328 ? 0.32150 0.39890 0.44440 -0.03700 -0.00690 0.07310  324 ASN B CG    
6395 O  OD1   . ASN B 328 ? 0.32650 0.39850 0.44390 -0.03340 -0.00790 0.06850  324 ASN B OD1   
6396 N  ND2   . ASN B 328 ? 0.28440 0.36510 0.40400 -0.03700 -0.00100 0.07440  324 ASN B ND2   
6397 N  N     . ALA B 329 ? 0.23840 0.33290 0.38550 -0.03240 -0.01140 0.07580  325 ALA B N     
6398 C  CA    . ALA B 329 ? 0.25420 0.35810 0.40870 -0.02770 -0.00600 0.07690  325 ALA B CA    
6399 C  C     . ALA B 329 ? 0.30680 0.40550 0.45750 -0.02330 -0.00820 0.07330  325 ALA B C     
6400 O  O     . ALA B 329 ? 0.31600 0.40670 0.46070 -0.02480 -0.01470 0.07100  325 ALA B O     
6401 C  CB    . ALA B 329 ? 0.22820 0.34530 0.39900 -0.02990 -0.00700 0.08320  325 ALA B CB    
6402 N  N     . ASP B 330 ? 0.27880 0.38260 0.43340 -0.01800 -0.00250 0.07300  326 ASP B N     
6403 C  CA    . ASP B 330 ? 0.27720 0.37810 0.43110 -0.01370 -0.00420 0.07100  326 ASP B CA    
6404 C  C     . ASP B 330 ? 0.35840 0.46490 0.52230 -0.01570 -0.01150 0.07500  326 ASP B C     
6405 O  O     . ASP B 330 ? 0.27860 0.39540 0.45470 -0.01840 -0.01240 0.08000  326 ASP B O     
6406 C  CB    . ASP B 330 ? 0.32570 0.43120 0.48360 -0.00760 0.00400  0.07020  326 ASP B CB    
6407 C  CG    . ASP B 330 ? 0.39030 0.49500 0.55150 -0.00290 0.00250  0.06990  326 ASP B CG    
6408 O  OD1   . ASP B 330 ? 0.40960 0.50470 0.56060 -0.00030 0.00290  0.06560  326 ASP B OD1   
6409 O  OD2   . ASP B 330 ? 0.40160 0.51570 0.57610 -0.00190 0.00110  0.07440  326 ASP B OD2   
6410 N  N     . ALA B 331 ? 0.30450 0.40470 0.46310 -0.01490 -0.01700 0.07310  327 ALA B N     
6411 C  CA    . ALA B 331 ? 0.30290 0.40770 0.46880 -0.01750 -0.02500 0.07650  327 ALA B CA    
6412 C  C     . ALA B 331 ? 0.28760 0.40500 0.46910 -0.01430 -0.02320 0.08160  327 ALA B C     
6413 O  O     . ALA B 331 ? 0.29220 0.41840 0.48470 -0.01760 -0.02820 0.08630  327 ALA B O     
6414 C  CB    . ALA B 331 ? 0.23810 0.33410 0.39380 -0.01690 -0.03060 0.07330  327 ALA B CB    
6415 N  N     . SER B 332 ? 0.31140 0.42980 0.49470 -0.00800 -0.01650 0.08070  328 SER B N     
6416 C  CA    . SER B 332 ? 0.27860 0.40860 0.47750 -0.00420 -0.01440 0.08550  328 SER B CA    
6417 C  C     . SER B 332 ? 0.33630 0.47820 0.54750 -0.00560 -0.00990 0.08930  328 SER B C     
6418 O  O     . SER B 332 ? 0.29150 0.44510 0.51750 -0.00630 -0.01220 0.09490  328 SER B O     
6419 C  CB    . SER B 332 ? 0.36930 0.49580 0.56670 0.00310  -0.00790 0.08290  328 SER B CB    
6420 O  OG    . SER B 332 ? 0.59900 0.73680 0.81190 0.00740  -0.00260 0.08660  328 SER B OG    
6421 N  N     . GLU B 333 ? 0.32660 0.46610 0.53180 -0.00630 -0.00360 0.08660  329 GLU B N     
6422 C  CA    . GLU B 333 ? 0.31120 0.46230 0.52710 -0.00800 0.00100  0.09050  329 GLU B CA    
6423 C  C     . GLU B 333 ? 0.23560 0.39180 0.45780 -0.01530 -0.00640 0.09510  329 GLU B C     
6424 O  O     . GLU B 333 ? 0.26680 0.43620 0.50420 -0.01650 -0.00600 0.10080  329 GLU B O     
6425 C  CB    . GLU B 333 ? 0.30040 0.44750 0.50670 -0.00780 0.00850  0.08680  329 GLU B CB    
6426 C  CG    . GLU B 333 ? 0.46560 0.60960 0.66780 -0.00080 0.01690  0.08230  329 GLU B CG    
6427 C  CD    . GLU B 333 ? 0.55650 0.71220 0.77460 0.00460  0.02200  0.08530  329 GLU B CD    
6428 O  OE1   . GLU B 333 ? 0.52070 0.68930 0.75190 0.00290  0.02310  0.09050  329 GLU B OE1   
6429 O  OE2   . GLU B 333 ? 0.60400 0.75600 0.82210 0.01060  0.02470  0.08270  329 GLU B OE2   
6430 N  N     . THR B 334 ? 0.28290 0.42890 0.49440 -0.02000 -0.01340 0.09270  330 THR B N     
6431 C  CA    . THR B 334 ? 0.22960 0.37850 0.44620 -0.02730 -0.02100 0.09630  330 THR B CA    
6432 C  C     . THR B 334 ? 0.23410 0.39180 0.46310 -0.02790 -0.02750 0.10070  330 THR B C     
6433 O  O     . THR B 334 ? 0.27100 0.43970 0.51320 -0.03190 -0.02990 0.10630  330 THR B O     
6434 C  CB    . THR B 334 ? 0.30970 0.44450 0.51150 -0.03130 -0.02690 0.09170  330 THR B CB    
6435 O  OG1   . THR B 334 ? 0.29330 0.42060 0.48430 -0.03060 -0.02110 0.08820  330 THR B OG1   
6436 C  CG2   . THR B 334 ? 0.25050 0.38690 0.45740 -0.03910 -0.03480 0.09470  330 THR B CG2   
6437 N  N     . LEU B 335 ? 0.28660 0.44010 0.51150 -0.02440 -0.03060 0.09890  331 LEU B N     
6438 C  CA    . LEU B 335 ? 0.28790 0.44990 0.52390 -0.02520 -0.03740 0.10340  331 LEU B CA    
6439 C  C     . LEU B 335 ? 0.24190 0.41970 0.49650 -0.02180 -0.03260 0.10950  331 LEU B C     
6440 O  O     . LEU B 335 ? 0.26360 0.45260 0.53180 -0.02510 -0.03770 0.11530  331 LEU B O     
6441 C  CB    . LEU B 335 ? 0.29890 0.45360 0.52640 -0.02160 -0.04100 0.10070  331 LEU B CB    
6442 C  CG    . LEU B 335 ? 0.31260 0.45430 0.52390 -0.02590 -0.04790 0.09570  331 LEU B CG    
6443 C  CD1   . LEU B 335 ? 0.25350 0.38640 0.45360 -0.02130 -0.04820 0.09200  331 LEU B CD1   
6444 C  CD2   . LEU B 335 ? 0.31690 0.46290 0.53290 -0.03280 -0.05810 0.09840  331 LEU B CD2   
6445 N  N     . LYS B 336 ? 0.25540 0.43440 0.51140 -0.01520 -0.02290 0.10820  332 LYS B N     
6446 C  CA    . LYS B 336 ? 0.23670 0.43080 0.51070 -0.01140 -0.01710 0.11340  332 LYS B CA    
6447 C  C     . LYS B 336 ? 0.25080 0.45570 0.53500 -0.01690 -0.01640 0.11800  332 LYS B C     
6448 O  O     . LYS B 336 ? 0.25430 0.47370 0.55590 -0.01750 -0.01770 0.12440  332 LYS B O     
6449 C  CB    . LYS B 336 ? 0.32020 0.51200 0.59170 -0.00380 -0.00610 0.10970  332 LYS B CB    
6450 C  CG    . LYS B 336 ? 0.50160 0.68440 0.76630 0.00220  -0.00580 0.10620  332 LYS B CG    
6451 C  CD    . LYS B 336 ? 0.64930 0.83430 0.91890 0.01020  0.00480  0.10440  332 LYS B CD    
6452 C  CE    . LYS B 336 ? 0.75260 0.92360 1.00470 0.01240  0.01030  0.09660  332 LYS B CE    
6453 N  NZ    . LYS B 336 ? 0.81750 0.97990 1.06540 0.01810  0.01040  0.09390  332 LYS B NZ    
6454 N  N     . ALA B 337 ? 0.23390 0.43250 0.50820 -0.02080 -0.01420 0.11520  333 ALA B N     
6455 C  CA    . ALA B 337 ? 0.23900 0.44720 0.52250 -0.02650 -0.01360 0.12000  333 ALA B CA    
6456 C  C     . ALA B 337 ? 0.31860 0.53090 0.60980 -0.03360 -0.02450 0.12440  333 ALA B C     
6457 O  O     . ALA B 337 ? 0.30550 0.53210 0.61310 -0.03640 -0.02530 0.13100  333 ALA B O     
6458 C  CB    . ALA B 337 ? 0.29070 0.48990 0.56100 -0.02960 -0.01020 0.11640  333 ALA B CB    
6459 N  N     . LEU B 338 ? 0.31220 0.51250 0.59170 -0.03670 -0.03290 0.12070  334 LEU B N     
6460 C  CA    . LEU B 338 ? 0.28190 0.48490 0.56700 -0.04370 -0.04370 0.12380  334 LEU B CA    
6461 C  C     . LEU B 338 ? 0.27580 0.49260 0.57690 -0.04170 -0.04690 0.12950  334 LEU B C     
6462 O  O     . LEU B 338 ? 0.29290 0.52040 0.60720 -0.04710 -0.05250 0.13520  334 LEU B O     
6463 C  CB    . LEU B 338 ? 0.32460 0.51180 0.59280 -0.04620 -0.05110 0.11770  334 LEU B CB    
6464 C  CG    . LEU B 338 ? 0.37330 0.54730 0.62800 -0.05040 -0.05120 0.11310  334 LEU B CG    
6465 C  CD1   . LEU B 338 ? 0.27170 0.43050 0.50960 -0.05080 -0.05690 0.10640  334 LEU B CD1   
6466 C  CD2   . LEU B 338 ? 0.44940 0.62800 0.71270 -0.05880 -0.05560 0.11720  334 LEU B CD2   
6467 N  N     . ILE B 339 ? 0.28970 0.50660 0.59060 -0.03400 -0.04370 0.12850  335 ILE B N     
6468 C  CA    . ILE B 339 ? 0.33250 0.56310 0.64980 -0.03140 -0.04620 0.13470  335 ILE B CA    
6469 C  C     . ILE B 339 ? 0.30430 0.55190 0.64100 -0.03020 -0.03970 0.14100  335 ILE B C     
6470 O  O     . ILE B 339 ? 0.33580 0.59740 0.68910 -0.03290 -0.04440 0.14790  335 ILE B O     
6471 C  CB    . ILE B 339 ? 0.29810 0.52410 0.61130 -0.02310 -0.04370 0.13250  335 ILE B CB    
6472 C  CG1   . ILE B 339 ? 0.29550 0.50760 0.59170 -0.02530 -0.05170 0.12770  335 ILE B CG1   
6473 C  CG2   . ILE B 339 ? 0.36760 0.60920 0.70040 -0.01940 -0.04500 0.13980  335 ILE B CG2   
6474 C  CD1   . ILE B 339 ? 0.30420 0.50800 0.59180 -0.01780 -0.04830 0.12420  335 ILE B CD1   
6475 N  N     . LEU B 340 ? 0.26780 0.51490 0.60250 -0.02650 -0.02890 0.13880  336 LEU B N     
6476 C  CA    . LEU B 340 ? 0.30840 0.57180 0.66030 -0.02580 -0.02190 0.14450  336 LEU B CA    
6477 C  C     . LEU B 340 ? 0.34300 0.61420 0.70320 -0.03500 -0.02730 0.14970  336 LEU B C     
6478 O  O     . LEU B 340 ? 0.36340 0.65130 0.74280 -0.03620 -0.02780 0.15690  336 LEU B O     
6479 C  CB    . LEU B 340 ? 0.47980 0.74010 0.82470 -0.02170 -0.00990 0.14050  336 LEU B CB    
6480 C  CG    . LEU B 340 ? 0.60780 0.88530 0.96980 -0.01830 -0.00030 0.14540  336 LEU B CG    
6481 C  CD1   . LEU B 340 ? 0.68610 0.97720 1.06710 -0.01290 0.00000  0.15050  336 LEU B CD1   
6482 C  CD2   . LEU B 340 ? 0.56540 0.83870 0.91790 -0.01360 0.01180  0.14010  336 LEU B CD2   
6483 N  N     . CYS B 341 ? 0.39410 0.65330 0.74080 -0.04160 -0.03190 0.14620  337 CYS B N     
6484 C  CA    . CYS B 341 ? 0.37280 0.63810 0.72720 -0.05060 -0.03670 0.15090  337 CYS B CA    
6485 C  C     . CYS B 341 ? 0.37490 0.64730 0.74030 -0.05580 -0.04800 0.15560  337 CYS B C     
6486 O  O     . CYS B 341 ? 0.37550 0.66350 0.75890 -0.05950 -0.04950 0.16290  337 CYS B O     
6487 C  CB    . CYS B 341 ? 0.35560 0.60470 0.69280 -0.05600 -0.03890 0.14580  337 CYS B CB    
6488 S  SG    . CYS B 341 ? 0.40980 0.66290 0.75500 -0.06760 -0.04530 0.15100  337 CYS B SG    
6489 N  N     . ILE B 342 ? 0.39700 0.65930 0.75210 -0.05580 -0.05590 0.15160  338 ILE B N     
6490 C  CA    . ILE B 342 ? 0.40320 0.67080 0.76570 -0.06170 -0.06770 0.15510  338 ILE B CA    
6491 C  C     . ILE B 342 ? 0.40560 0.69200 0.78860 -0.05800 -0.06760 0.16270  338 ILE B C     
6492 O  O     . ILE B 342 ? 0.40350 0.70260 0.80160 -0.06380 -0.07400 0.16920  338 ILE B O     
6493 C  CB    . ILE B 342 ? 0.37290 0.62500 0.71760 -0.06230 -0.07550 0.14860  338 ILE B CB    
6494 C  CG1   . ILE B 342 ? 0.41980 0.65510 0.74750 -0.06740 -0.07700 0.14200  338 ILE B CG1   
6495 C  CG2   . ILE B 342 ? 0.33140 0.59050 0.68350 -0.06740 -0.08740 0.15220  338 ILE B CG2   
6496 C  CD1   . ILE B 342 ? 0.38430 0.60280 0.69180 -0.06540 -0.08020 0.13410  338 ILE B CD1   
6497 N  N     . ARG B 343 ? 0.36440 0.65310 0.74920 -0.04830 -0.06020 0.16230  339 ARG B N     
6498 C  CA    . ARG B 343 ? 0.40340 0.70950 0.80850 -0.04400 -0.05980 0.16960  339 ARG B CA    
6499 C  C     . ARG B 343 ? 0.47670 0.80080 0.90190 -0.04550 -0.05450 0.17670  339 ARG B C     
6500 O  O     . ARG B 343 ? 0.41450 0.75360 0.85710 -0.04960 -0.06060 0.18410  339 ARG B O     
6501 C  CB    . ARG B 343 ? 0.44670 0.75010 0.84970 -0.03290 -0.05210 0.16720  339 ARG B CB    
6502 C  CG    . ARG B 343 ? 0.45480 0.74790 0.84630 -0.03090 -0.05890 0.16410  339 ARG B CG    
6503 C  CD    . ARG B 343 ? 0.52520 0.82710 0.92930 -0.02230 -0.05650 0.16840  339 ARG B CD    
6504 N  NE    . ARG B 343 ? 0.62980 0.91840 1.01910 -0.01870 -0.05940 0.16390  339 ARG B NE    
6505 C  CZ    . ARG B 343 ? 0.63840 0.91610 1.01770 -0.01130 -0.05120 0.15850  339 ARG B CZ    
6506 N  NH1   . ARG B 343 ? 0.65960 0.93830 1.04180 -0.00660 -0.03950 0.15640  339 ARG B NH1   
6507 N  NH2   . ARG B 343 ? 0.57460 0.84090 0.94100 -0.00880 -0.05470 0.15520  339 ARG B NH2   
6508 N  N     . SER B 344 ? 0.39130 0.71480 0.81460 -0.04200 -0.04300 0.17470  340 SER B N     
6509 C  CA    . SER B 344 ? 0.43330 0.77360 0.87400 -0.04330 -0.03650 0.18100  340 SER B CA    
6510 C  C     . SER B 344 ? 0.36360 0.71080 0.81280 -0.05450 -0.04540 0.18650  340 SER B C     
6511 O  O     . SER B 344 ? 0.38360 0.74970 0.85370 -0.05640 -0.04480 0.19460  340 SER B O     
6512 C  CB    . SER B 344 ? 0.48450 0.81880 0.91510 -0.03980 -0.02440 0.17630  340 SER B CB    
6513 O  OG    . SER B 344 ? 0.63680 0.98050 1.07530 -0.04540 -0.02080 0.18080  340 SER B OG    
6514 N  N     . SER B 345 ? 0.37000 0.70250 0.80400 -0.06210 -0.05350 0.18220  341 SER B N     
6515 C  CA    . SER B 345 ? 0.35910 0.69580 0.80020 -0.07330 -0.06330 0.18650  341 SER B CA    
6516 C  C     . SER B 345 ? 0.44780 0.79860 0.90550 -0.07560 -0.07210 0.19310  341 SER B C     
6517 O  O     . SER B 345 ? 0.52920 0.88640 0.99480 -0.08130 -0.07530 0.19760  341 SER B O     
6518 C  CB    . SER B 345 ? 0.44880 0.76510 0.86950 -0.07960 -0.07100 0.17940  341 SER B CB    
6519 O  OG    . SER B 345 ? 0.47420 0.78540 0.88980 -0.08100 -0.08170 0.17720  341 SER B OG    
6520 N  N     . GLY B 346 ? 0.49670 0.84530 0.95140 -0.07080 -0.07650 0.19150  342 GLY B N     
6521 C  CA    . GLY B 346 ? 0.46260 0.81830 0.92490 -0.07280 -0.08560 0.19570  342 GLY B CA    
6522 C  C     . GLY B 346 ? 0.51110 0.85790 0.96370 -0.08260 -0.09920 0.19330  342 GLY B C     
6523 O  O     . GLY B 346 ? 0.50910 0.86120 0.96640 -0.08510 -0.10700 0.19660  342 GLY B O     
6524 N  N     . LYS B 347 ? 0.62480 0.95790 1.06400 -0.08820 -0.10230 0.18740  343 LYS B N     
6525 C  CA    . LYS B 347 ? 0.65540 0.97840 1.08430 -0.09770 -0.11480 0.18390  343 LYS B CA    
6526 C  C     . LYS B 347 ? 0.62620 0.94100 1.04250 -0.09590 -0.12210 0.17920  343 LYS B C     
6527 O  O     . LYS B 347 ? 0.64470 0.96620 1.06490 -0.09470 -0.12760 0.18220  343 LYS B O     
6528 C  CB    . LYS B 347 ? 0.68480 0.99540 1.10450 -0.10430 -0.11450 0.17950  343 LYS B CB    
6529 C  CG    . LYS B 347 ? 0.76020 1.06520 1.17740 -0.11510 -0.12450 0.17870  343 LYS B CG    
6530 C  CD    . LYS B 347 ? 0.80590 1.12480 1.23890 -0.11770 -0.12410 0.18640  343 LYS B CD    
6531 C  CE    . LYS B 347 ? 0.79890 1.12120 1.23890 -0.11860 -0.11510 0.18990  343 LYS B CE    
6532 N  NZ    . LYS B 347 ? 0.75000 1.08940 1.20730 -0.11730 -0.11110 0.19810  343 LYS B NZ    
6533 N  N     . GLY B 375 ? 0.66790 0.79100 0.44460 -0.04050 -0.09580 0.07420  371 GLY B N     
6534 C  CA    . GLY B 375 ? 0.71770 0.83620 0.51470 -0.03760 -0.09650 0.08210  371 GLY B CA    
6535 C  C     . GLY B 375 ? 0.75580 0.87660 0.56110 -0.03950 -0.10480 0.08460  371 GLY B C     
6536 O  O     . GLY B 375 ? 0.79820 0.92590 0.59320 -0.04380 -0.11120 0.08240  371 GLY B O     
6537 N  N     . ILE B 376 ? 0.66160 0.77690 0.48580 -0.03650 -0.10480 0.08890  372 ILE B N     
6538 C  CA    . ILE B 376 ? 0.60610 0.72360 0.44060 -0.03790 -0.11200 0.09140  372 ILE B CA    
6539 C  C     . ILE B 376 ? 0.52430 0.63390 0.35980 -0.03830 -0.11140 0.07880  372 ILE B C     
6540 O  O     . ILE B 376 ? 0.56290 0.66270 0.40210 -0.03520 -0.10470 0.07200  372 ILE B O     
6541 C  CB    . ILE B 376 ? 0.61610 0.73210 0.47090 -0.03430 -0.11190 0.10220  372 ILE B CB    
6542 C  CG1   . ILE B 376 ? 0.63490 0.75650 0.49020 -0.03330 -0.11130 0.11460  372 ILE B CG1   
6543 C  CG2   . ILE B 376 ? 0.57640 0.69720 0.44180 -0.03580 -0.11970 0.10610  372 ILE B CG2   
6544 C  CD1   . ILE B 376 ? 0.61420 0.73310 0.48980 -0.02930 -0.11080 0.12460  372 ILE B CD1   
6545 N  N     . HIS B 377 ? 0.51770 0.63170 0.35040 -0.04230 -0.11870 0.07600  373 HIS B N     
6546 C  CA    . HIS B 377 ? 0.49990 0.60650 0.33530 -0.04310 -0.11890 0.06510  373 HIS B CA    
6547 C  C     . HIS B 377 ? 0.49950 0.60010 0.35550 -0.03950 -0.11700 0.06830  373 HIS B C     
6548 O  O     . HIS B 377 ? 0.49620 0.60220 0.36460 -0.03880 -0.12080 0.07850  373 HIS B O     
6549 C  CB    . HIS B 377 ? 0.51220 0.62520 0.34070 -0.04890 -0.12780 0.06190  373 HIS B CB    
6550 C  CG    . HIS B 377 ? 0.63320 0.73810 0.46110 -0.05040 -0.12790 0.04940  373 HIS B CG    
6551 N  ND1   . HIS B 377 ? 0.61390 0.71270 0.45810 -0.04890 -0.12770 0.04860  373 HIS B ND1   
6552 C  CD2   . HIS B 377 ? 0.65380 0.75530 0.46710 -0.05340 -0.12800 0.03730  373 HIS B CD2   
6553 C  CE1   . HIS B 377 ? 0.61580 0.70800 0.45580 -0.05100 -0.12800 0.03710  373 HIS B CE1   
6554 N  NE2   . HIS B 377 ? 0.64120 0.73430 0.46270 -0.05370 -0.12820 0.02980  373 HIS B NE2   
6555 N  N     . PRO B 378 ? 0.50570 0.59570 0.36600 -0.03690 -0.11110 0.06020  374 PRO B N     
6556 C  CA    . PRO B 378 ? 0.49800 0.58260 0.37680 -0.03320 -0.10830 0.06360  374 PRO B CA    
6557 C  C     . PRO B 378 ? 0.55640 0.64560 0.44750 -0.03500 -0.11500 0.06770  374 PRO B C     
6558 O  O     . PRO B 378 ? 0.46220 0.55150 0.36910 -0.03190 -0.11410 0.07480  374 PRO B O     
6559 C  CB    . PRO B 378 ? 0.52980 0.60320 0.40760 -0.03160 -0.10210 0.05260  374 PRO B CB    
6560 C  CG    . PRO B 378 ? 0.50690 0.57960 0.36720 -0.03220 -0.09890 0.04660  374 PRO B CG    
6561 C  CD    . PRO B 378 ? 0.50040 0.58300 0.34890 -0.03690 -0.10600 0.04840  374 PRO B CD    
6562 N  N     . ALA B 379 ? 0.54740 0.64060 0.43180 -0.03990 -0.12160 0.06320  375 ALA B N     
6563 C  CA    . ALA B 379 ? 0.57370 0.67270 0.47030 -0.04200 -0.12850 0.06780  375 ALA B CA    
6564 C  C     . ALA B 379 ? 0.59470 0.70390 0.49790 -0.04140 -0.13260 0.08100  375 ALA B C     
6565 O  O     . ALA B 379 ? 0.48360 0.59720 0.40250 -0.04070 -0.13590 0.08800  375 ALA B O     
6566 C  CB    . ALA B 379 ? 0.51170 0.61360 0.39850 -0.04820 -0.13550 0.06070  375 ALA B CB    
6567 N  N     . MET B 380 ? 0.58930 0.70300 0.48110 -0.04170 -0.13260 0.08500  376 MET B N     
6568 C  CA    . MET B 380 ? 0.55850 0.68240 0.45760 -0.04140 -0.13750 0.09820  376 MET B CA    
6569 C  C     . MET B 380 ? 0.53930 0.65920 0.45290 -0.03540 -0.13150 0.10610  376 MET B C     
6570 O  O     . MET B 380 ? 0.52900 0.65460 0.45660 -0.03370 -0.13450 0.11660  376 MET B O     
6571 C  CB    . MET B 380 ? 0.61400 0.74700 0.49610 -0.04540 -0.14220 0.10100  376 MET B CB    
6572 C  CG    . MET B 380 ? 0.90200 1.04380 0.78620 -0.05040 -0.15210 0.10220  376 MET B CG    
6573 S  SD    . MET B 380 ? 1.14480 1.30020 1.01290 -0.05650 -0.16110 0.10650  376 MET B SD    
6574 C  CE    . MET B 380 ? 1.03810 1.19930 0.92800 -0.05220 -0.16260 0.12300  376 MET B CE    
6575 N  N     . VAL B 381 ? 0.44960 0.55950 0.36090 -0.03200 -0.12290 0.10070  377 VAL B N     
6576 C  CA    . VAL B 381 ? 0.50050 0.60450 0.42630 -0.02650 -0.11680 0.10560  377 VAL B CA    
6577 C  C     . VAL B 381 ? 0.48460 0.58710 0.42840 -0.02470 -0.11750 0.10640  377 VAL B C     
6578 O  O     . VAL B 381 ? 0.44280 0.54770 0.40170 -0.02150 -0.11760 0.11540  377 VAL B O     
6579 C  CB    . VAL B 381 ? 0.45730 0.55070 0.37660 -0.02420 -0.10810 0.09760  377 VAL B CB    
6580 C  CG1   . VAL B 381 ? 0.40890 0.49510 0.34290 -0.01910 -0.10190 0.10060  377 VAL B CG1   
6581 C  CG2   . VAL B 381 ? 0.50180 0.59770 0.40470 -0.02560 -0.10680 0.09810  377 VAL B CG2   
6582 N  N     . VAL B 382 ? 0.41530 0.51410 0.35820 -0.02660 -0.11770 0.09700  378 VAL B N     
6583 C  CA    . VAL B 382 ? 0.42550 0.52340 0.38510 -0.02520 -0.11800 0.09740  378 VAL B CA    
6584 C  C     . VAL B 382 ? 0.44600 0.55540 0.41540 -0.02680 -0.12590 0.10660  378 VAL B C     
6585 O  O     . VAL B 382 ? 0.47760 0.58890 0.46450 -0.02360 -0.12540 0.11290  378 VAL B O     
6586 C  CB    . VAL B 382 ? 0.46800 0.56010 0.42390 -0.02770 -0.11730 0.08610  378 VAL B CB    
6587 C  CG1   . VAL B 382 ? 0.42960 0.52240 0.40310 -0.02670 -0.11780 0.08740  378 VAL B CG1   
6588 C  CG2   . VAL B 382 ? 0.45990 0.54090 0.40800 -0.02560 -0.10930 0.07770  378 VAL B CG2   
6589 N  N     . GLU B 383 ? 0.44590 0.56360 0.40460 -0.03180 -0.13350 0.10770  379 GLU B N     
6590 C  CA    . GLU B 383 ? 0.45290 0.58260 0.42060 -0.03360 -0.14170 0.11730  379 GLU B CA    
6591 C  C     . GLU B 383 ? 0.52540 0.65900 0.50400 -0.02910 -0.14070 0.12980  379 GLU B C     
6592 O  O     . GLU B 383 ? 0.49510 0.63370 0.49150 -0.02680 -0.14270 0.13760  379 GLU B O     
6593 C  CB    . GLU B 383 ? 0.55290 0.69090 0.50470 -0.04010 -0.14990 0.11610  379 GLU B CB    
6594 C  CG    . GLU B 383 ? 0.71780 0.86950 0.67830 -0.04280 -0.15950 0.12610  379 GLU B CG    
6595 C  CD    . GLU B 383 ? 0.91690 1.07670 0.86080 -0.05000 -0.16800 0.12340  379 GLU B CD    
6596 O  OE1   . GLU B 383 ? 0.97930 1.14500 0.91180 -0.05130 -0.17060 0.12860  379 GLU B OE1   
6597 O  OE2   . GLU B 383 ? 0.97440 1.13450 0.91650 -0.05450 -0.17220 0.11620  379 GLU B OE2   
6598 N  N     . ALA B 384 ? 0.52120 0.65210 0.49020 -0.02770 -0.13720 0.13190  380 ALA B N     
6599 C  CA    . ALA B 384 ? 0.49250 0.62570 0.47170 -0.02350 -0.13610 0.14380  380 ALA B CA    
6600 C  C     . ALA B 384 ? 0.46230 0.58790 0.45990 -0.01750 -0.12930 0.14470  380 ALA B C     
6601 O  O     . ALA B 384 ? 0.42790 0.55750 0.44180 -0.01410 -0.13050 0.15450  380 ALA B O     
6602 C  CB    . ALA B 384 ? 0.51760 0.64840 0.48250 -0.02350 -0.13290 0.14490  380 ALA B CB    
6603 N  N     . MET B 385 ? 0.43390 0.54860 0.42920 -0.01600 -0.12220 0.13450  381 MET B N     
6604 C  CA    . MET B 385 ? 0.46040 0.56830 0.47200 -0.01080 -0.11580 0.13410  381 MET B CA    
6605 C  C     . MET B 385 ? 0.45230 0.56680 0.48010 -0.01050 -0.11970 0.13740  381 MET B C     
6606 O  O     . MET B 385 ? 0.47060 0.58560 0.51550 -0.00580 -0.11760 0.14380  381 MET B O     
6607 C  CB    . MET B 385 ? 0.42780 0.52450 0.43290 -0.01040 -0.10880 0.12210  381 MET B CB    
6608 C  CG    . MET B 385 ? 0.40970 0.49890 0.40280 -0.00950 -0.10320 0.11900  381 MET B CG    
6609 S  SD    . MET B 385 ? 0.47960 0.55780 0.46480 -0.00990 -0.09670 0.10480  381 MET B SD    
6610 C  CE    . MET B 385 ? 0.44690 0.52100 0.45180 -0.00580 -0.09250 0.10460  381 MET B CE    
6611 N  N     . GLN B 386 ? 0.48920 0.60880 0.51240 -0.01530 -0.12530 0.13290  382 GLN B N     
6612 C  CA    . GLN B 386 ? 0.55610 0.68310 0.59480 -0.01570 -0.12940 0.13620  382 GLN B CA    
6613 C  C     . GLN B 386 ? 0.55540 0.69320 0.60650 -0.01410 -0.13480 0.14950  382 GLN B C     
6614 O  O     . GLN B 386 ? 0.57030 0.71220 0.64030 -0.01090 -0.13470 0.15470  382 GLN B O     
6615 C  CB    . GLN B 386 ? 0.57880 0.70990 0.60860 -0.02220 -0.13570 0.12980  382 GLN B CB    
6616 C  CG    . GLN B 386 ? 0.60070 0.73650 0.64570 -0.02300 -0.13800 0.12970  382 GLN B CG    
6617 C  CD    . GLN B 386 ? 0.57130 0.69690 0.61740 -0.02190 -0.13100 0.12000  382 GLN B CD    
6618 O  OE1   . GLN B 386 ? 0.55740 0.67700 0.59000 -0.02550 -0.13060 0.11050  382 GLN B OE1   
6619 N  NE2   . GLN B 386 ? 0.50360 0.62710 0.56600 -0.01690 -0.12520 0.12220  382 GLN B NE2   
6620 N  N     . ASN B 387 ? 0.50510 0.64820 0.54630 -0.01610 -0.13960 0.15540  383 ASN B N     
6621 C  CA    . ASN B 387 ? 0.48970 0.64390 0.54240 -0.01500 -0.14560 0.16880  383 ASN B CA    
6622 C  C     . ASN B 387 ? 0.49720 0.64700 0.56380 -0.00800 -0.14000 0.17650  383 ASN B C     
6623 O  O     . ASN B 387 ? 0.52040 0.67810 0.60290 -0.00540 -0.14350 0.18730  383 ASN B O     
6624 C  CB    . ASN B 387 ? 0.62610 0.78830 0.66280 -0.02000 -0.15310 0.17320  383 ASN B CB    
6625 C  CG    . ASN B 387 ? 0.62030 0.78940 0.64610 -0.02710 -0.16060 0.16760  383 ASN B CG    
6626 O  OD1   . ASN B 387 ? 0.65090 0.82040 0.68380 -0.02850 -0.16150 0.16260  383 ASN B OD1   
6627 N  ND2   . ASN B 387 ? 0.65720 0.83150 0.66500 -0.03200 -0.16590 0.16810  383 ASN B ND2   
6628 N  N     . ARG B 388 ? 0.44840 0.58580 0.51120 -0.00480 -0.13130 0.17090  384 ARG B N     
6629 C  CA    . ARG B 388 ? 0.44730 0.57950 0.52150 0.00130  -0.12610 0.17770  384 ARG B CA    
6630 C  C     . ARG B 388 ? 0.42180 0.54450 0.50890 0.00660  -0.11750 0.17240  384 ARG B C     
6631 O  O     . ARG B 388 ? 0.48530 0.60590 0.58780 0.01200  -0.11440 0.17890  384 ARG B O     
6632 C  CB    . ARG B 388 ? 0.50680 0.63280 0.56600 0.00070  -0.12330 0.17760  384 ARG B CB    
6633 C  CG    . ARG B 388 ? 0.55630 0.69240 0.60780 -0.00260 -0.13100 0.18730  384 ARG B CG    
6634 C  CD    . ARG B 388 ? 0.56760 0.70420 0.63220 0.00190  -0.13060 0.19990  384 ARG B CD    
6635 N  NE    . ARG B 388 ? 0.57790 0.72430 0.63420 -0.00140 -0.13780 0.20980  384 ARG B NE    
6636 C  CZ    . ARG B 388 ? 0.51370 0.66860 0.58260 0.00020  -0.14320 0.22350  384 ARG B CZ    
6637 N  NH1   . ARG B 388 ? 0.52850 0.68310 0.61980 0.00570  -0.14190 0.22860  384 ARG B NH1   
6638 N  NH2   . ARG B 388 ? 0.53750 0.69950 0.59630 -0.00360 -0.14760 0.22920  384 ARG B NH2   
6639 N  N     . LEU B 389 ? 0.39300 0.50960 0.47420 0.00510  -0.11360 0.16100  385 LEU B N     
6640 C  CA    . LEU B 389 ? 0.45920 0.56700 0.55090 0.00980  -0.10510 0.15580  385 LEU B CA    
6641 C  C     . LEU B 389 ? 0.47160 0.58630 0.58380 0.01270  -0.10630 0.16050  385 LEU B C     
6642 O  O     . LEU B 389 ? 0.51410 0.63790 0.62810 0.00920  -0.11210 0.16080  385 LEU B O     
6643 C  CB    . LEU B 389 ? 0.45310 0.55360 0.53310 0.00720  -0.10120 0.14310  385 LEU B CB    
6644 C  CG    . LEU B 389 ? 0.41880 0.51140 0.47990 0.00510  -0.09830 0.13710  385 LEU B CG    
6645 C  CD1   . LEU B 389 ? 0.36240 0.44750 0.41550 0.00350  -0.09390 0.12520  385 LEU B CD1   
6646 C  CD2   . LEU B 389 ? 0.40950 0.49490 0.47360 0.00940  -0.09300 0.14100  385 LEU B CD2   
6647 N  N     . PRO B 390 ? 0.43050 0.54150 0.55870 0.01900  -0.10070 0.16400  386 PRO B N     
6648 C  CA    . PRO B 390 ? 0.42710 0.54470 0.57520 0.02220  -0.10060 0.16750  386 PRO B CA    
6649 C  C     . PRO B 390 ? 0.54310 0.66040 0.68990 0.01990  -0.09840 0.15810  386 PRO B C     
6650 O  O     . PRO B 390 ? 0.57520 0.68420 0.70830 0.01750  -0.09470 0.14850  386 PRO B O     
6651 C  CB    . PRO B 390 ? 0.37550 0.48550 0.53720 0.02950  -0.09300 0.16980  386 PRO B CB    
6652 C  CG    . PRO B 390 ? 0.40520 0.50820 0.55640 0.02950  -0.09250 0.17220  386 PRO B CG    
6653 C  CD    . PRO B 390 ? 0.41290 0.51340 0.54200 0.02340  -0.09430 0.16470  386 PRO B CD    
6654 N  N     . ALA B 391 ? 0.58170 0.70850 0.74390 0.02060  -0.10070 0.16160  387 ALA B N     
6655 C  CA    . ALA B 391 ? 0.54130 0.66980 0.70310 0.01760  -0.09990 0.15420  387 ALA B CA    
6656 C  C     . ALA B 391 ? 0.49290 0.61060 0.65480 0.02060  -0.08990 0.14540  387 ALA B C     
6657 O  O     . ALA B 391 ? 0.47160 0.58620 0.62510 0.01710  -0.08840 0.13710  387 ALA B O     
6658 C  CB    . ALA B 391 ? 0.57240 0.71430 0.75270 0.01800  -0.10410 0.16080  387 ALA B CB    
6659 N  N     . ASP B 392 ? 0.46850 0.58030 0.63960 0.02690  -0.08300 0.14700  388 ASP B N     
6660 C  CA    . ASP B 392 ? 0.51670 0.61870 0.68790 0.02990  -0.07350 0.13880  388 ASP B CA    
6661 C  C     . ASP B 392 ? 0.49090 0.58020 0.64390 0.02850  -0.06990 0.13180  388 ASP B C     
6662 O  O     . ASP B 392 ? 0.44530 0.52550 0.59810 0.03130  -0.06210 0.12600  388 ASP B O     
6663 C  CB    . ASP B 392 ? 0.45350 0.55480 0.64330 0.03730  -0.06760 0.14290  388 ASP B CB    
6664 C  CG    . ASP B 392 ? 0.56560 0.66360 0.75830 0.04080  -0.06840 0.15000  388 ASP B CG    
6665 O  OD1   . ASP B 392 ? 0.64200 0.74220 0.82520 0.03740  -0.07510 0.15430  388 ASP B OD1   
6666 O  OD2   . ASP B 392 ? 0.65220 0.74530 0.85670 0.04690  -0.06230 0.15120  388 ASP B OD2   
6667 N  N     . THR B 393 ? 0.42330 0.51230 0.56130 0.02410  -0.07540 0.13210  389 THR B N     
6668 C  CA    . THR B 393 ? 0.35480 0.43300 0.47650 0.02280  -0.07210 0.12620  389 THR B CA    
6669 C  C     . THR B 393 ? 0.37560 0.44800 0.48860 0.02050  -0.06790 0.11570  389 THR B C     
6670 O  O     . THR B 393 ? 0.39360 0.47090 0.50460 0.01680  -0.07120 0.11290  389 THR B O     
6671 C  CB    . THR B 393 ? 0.33550 0.41640 0.44320 0.01850  -0.07890 0.12890  389 THR B CB    
6672 O  OG1   . THR B 393 ? 0.37350 0.45910 0.48860 0.02080  -0.08240 0.13930  389 THR B OG1   
6673 C  CG2   . THR B 393 ? 0.35410 0.42470 0.44490 0.01700  -0.07510 0.12230  389 THR B CG2   
6674 N  N     . ILE B 394 ? 0.32480 0.38670 0.43280 0.02250  -0.06090 0.11020  390 ILE B N     
6675 C  CA    . ILE B 394 ? 0.31340 0.36920 0.41090 0.02000  -0.05730 0.10070  390 ILE B CA    
6676 C  C     . ILE B 394 ? 0.35320 0.40450 0.43300 0.01650  -0.05940 0.09770  390 ILE B C     
6677 O  O     . ILE B 394 ? 0.32350 0.36970 0.39890 0.01800  -0.05750 0.09930  390 ILE B O     
6678 C  CB    . ILE B 394 ? 0.36710 0.41490 0.46900 0.02380  -0.04870 0.09600  390 ILE B CB    
6679 C  CG1   . ILE B 394 ? 0.32370 0.37670 0.44350 0.02770  -0.04620 0.09920  390 ILE B CG1   
6680 C  CG2   . ILE B 394 ? 0.39850 0.44100 0.48980 0.02090  -0.04560 0.08710  390 ILE B CG2   
6681 C  CD1   . ILE B 394 ? 0.33580 0.38130 0.46070 0.03190  -0.03740 0.09510  390 ILE B CD1   
6682 N  N     . LEU B 395 ? 0.31090 0.36450 0.38110 0.01190  -0.06340 0.09370  391 LEU B N     
6683 C  CA    . LEU B 395 ? 0.33140 0.38220 0.38500 0.00840  -0.06570 0.09050  391 LEU B CA    
6684 C  C     . LEU B 395 ? 0.35120 0.39390 0.39590 0.00740  -0.06090 0.08140  391 LEU B C     
6685 O  O     . LEU B 395 ? 0.38890 0.43200 0.43420 0.00540  -0.06100 0.07690  391 LEU B O     
6686 C  CB    . LEU B 395 ? 0.32580 0.38470 0.37450 0.00400  -0.07380 0.09200  391 LEU B CB    
6687 C  CG    . LEU B 395 ? 0.39190 0.44810 0.42270 0.00050  -0.07580 0.08780  391 LEU B CG    
6688 C  CD1   . LEU B 395 ? 0.35000 0.40480 0.37570 0.00210  -0.07500 0.09250  391 LEU B CD1   
6689 C  CD2   . LEU B 395 ? 0.30410 0.36720 0.32860 -0.00450 -0.08360 0.08710  391 LEU B CD2   
6690 N  N     . PHE B 396 ? 0.27190 0.30740 0.30900 0.00850  -0.05680 0.07930  392 PHE B N     
6691 C  CA    . PHE B 396 ? 0.26680 0.29510 0.29400 0.00730  -0.05290 0.07140  392 PHE B CA    
6692 C  C     . PHE B 396 ? 0.32770 0.35640 0.34040 0.00380  -0.05650 0.06880  392 PHE B C     
6693 O  O     . PHE B 396 ? 0.36920 0.40050 0.37690 0.00340  -0.05910 0.07300  392 PHE B O     
6694 C  CB    . PHE B 396 ? 0.33070 0.35150 0.35820 0.01030  -0.04650 0.07050  392 PHE B CB    
6695 C  CG    . PHE B 396 ? 0.34840 0.36700 0.38780 0.01350  -0.04160 0.07010  392 PHE B CG    
6696 C  CD1   . PHE B 396 ? 0.28790 0.30990 0.34010 0.01660  -0.04170 0.07620  392 PHE B CD1   
6697 C  CD2   . PHE B 396 ? 0.32970 0.34330 0.36740 0.01350  -0.03680 0.06370  392 PHE B CD2   
6698 C  CE1   . PHE B 396 ? 0.29260 0.31270 0.35570 0.01980  -0.03660 0.07520  392 PHE B CE1   
6699 C  CE2   . PHE B 396 ? 0.38420 0.39620 0.43170 0.01620  -0.03200 0.06300  392 PHE B CE2   
6700 C  CZ    . PHE B 396 ? 0.32530 0.34060 0.38540 0.01950  -0.03170 0.06840  392 PHE B CZ    
6701 N  N     . VAL B 397 ? 0.29130 0.31780 0.29740 0.00140  -0.05660 0.06200  393 VAL B N     
6702 C  CA    . VAL B 397 ? 0.33090 0.35730 0.32340 -0.00180 -0.05960 0.05820  393 VAL B CA    
6703 C  C     . VAL B 397 ? 0.39210 0.41090 0.37720 -0.00160 -0.05460 0.05130  393 VAL B C     
6704 O  O     . VAL B 397 ? 0.35710 0.37220 0.34650 -0.00110 -0.05150 0.04770  393 VAL B O     
6705 C  CB    . VAL B 397 ? 0.33380 0.36490 0.32550 -0.00540 -0.06550 0.05650  393 VAL B CB    
6706 C  CG1   . VAL B 397 ? 0.38370 0.41330 0.36090 -0.00840 -0.06770 0.05080  393 VAL B CG1   
6707 C  CG2   . VAL B 397 ? 0.32130 0.36130 0.32020 -0.00590 -0.07110 0.06410  393 VAL B CG2   
6708 N  N     . ASP B 398 ? 0.37250 0.38960 0.34670 -0.00200 -0.05380 0.04990  394 ASP B N     
6709 C  CA    . ASP B 398 ? 0.35310 0.36370 0.32110 -0.00160 -0.04910 0.04400  394 ASP B CA    
6710 C  C     . ASP B 398 ? 0.40310 0.41240 0.36400 -0.00410 -0.05120 0.03730  394 ASP B C     
6711 O  O     . ASP B 398 ? 0.40580 0.41810 0.36860 -0.00630 -0.05560 0.03660  394 ASP B O     
6712 C  CB    . ASP B 398 ? 0.38840 0.39780 0.34910 -0.00060 -0.04660 0.04560  394 ASP B CB    
6713 C  CG    . ASP B 398 ? 0.45130 0.45420 0.41140 0.00100  -0.04060 0.04200  394 ASP B CG    
6714 O  OD1   . ASP B 398 ? 0.43630 0.43650 0.38950 0.00010  -0.03920 0.03630  394 ASP B OD1   
6715 O  OD2   . ASP B 398 ? 0.44810 0.44860 0.41500 0.00300  -0.03730 0.04490  394 ASP B OD2   
6716 N  N     . ASN B 399 ? 0.41410 0.41850 0.36790 -0.00380 -0.04770 0.03210  395 ASN B N     
6717 C  CA    . ASN B 399 ? 0.40210 0.40390 0.34940 -0.00570 -0.04870 0.02530  395 ASN B CA    
6718 C  C     . ASN B 399 ? 0.54840 0.55090 0.48340 -0.00620 -0.04880 0.02300  395 ASN B C     
6719 O  O     . ASN B 399 ? 0.81640 0.81890 0.74830 -0.00460 -0.04550 0.02500  395 ASN B O     
6720 C  CB    . ASN B 399 ? 0.41760 0.41340 0.36860 -0.00450 -0.04440 0.02140  395 ASN B CB    
6721 C  CG    . ASN B 399 ? 0.51110 0.50700 0.47390 -0.00380 -0.04360 0.02440  395 ASN B CG    
6722 O  OD1   . ASN B 399 ? 0.52160 0.51950 0.48930 -0.00560 -0.04690 0.02440  395 ASN B OD1   
6723 N  ND2   . ASN B 399 ? 0.41210 0.40650 0.37960 -0.00150 -0.03930 0.02690  395 ASN B ND2   
6724 N  N     . GLY B 400 ? 0.45960 0.46330 0.38800 -0.00860 -0.05260 0.01900  396 GLY B N     
6725 C  CA    . GLY B 400 ? 0.37330 0.38020 0.28980 -0.00970 -0.05410 0.01760  396 GLY B CA    
6726 C  C     . GLY B 400 ? 0.41900 0.43040 0.33330 -0.01290 -0.06070 0.01760  396 GLY B C     
6727 O  O     . GLY B 400 ? 0.41930 0.43060 0.34140 -0.01430 -0.06370 0.01780  396 GLY B O     
6728 N  N     . SER B 401 ? 0.37560 0.39180 0.27930 -0.01450 -0.06320 0.01760  397 SER B N     
6729 C  CA    . SER B 401 ? 0.46570 0.48700 0.36690 -0.01810 -0.07010 0.01780  397 SER B CA    
6730 C  C     . SER B 401 ? 0.40130 0.42810 0.31330 -0.01840 -0.07380 0.02640  397 SER B C     
6731 O  O     . SER B 401 ? 0.41770 0.44860 0.33140 -0.02140 -0.07980 0.02700  397 SER B O     
6732 C  CB    . SER B 401 ? 0.40550 0.43180 0.29230 -0.01990 -0.07220 0.01660  397 SER B CB    
6733 O  OG    . SER B 401 ? 0.47410 0.50640 0.36070 -0.01890 -0.07190 0.02500  397 SER B OG    
6734 N  N     . CYS B 402 ? 0.36180 0.38920 0.28130 -0.01540 -0.07050 0.03310  398 CYS B N     
6735 C  CA    . CYS B 402 ? 0.37170 0.40340 0.30370 -0.01480 -0.07320 0.04080  398 CYS B CA    
6736 C  C     . CYS B 402 ? 0.36930 0.39970 0.31060 -0.01610 -0.07530 0.03840  398 CYS B C     
6737 O  O     . CYS B 402 ? 0.34060 0.37670 0.29040 -0.01710 -0.07970 0.04350  398 CYS B O     
6738 C  CB    . CYS B 402 ? 0.38080 0.41100 0.32070 -0.01110 -0.06830 0.04650  398 CYS B CB    
6739 S  SG    . CYS B 402 ? 0.49310 0.51400 0.43610 -0.00820 -0.06050 0.04150  398 CYS B SG    
6740 N  N     . ILE B 403 ? 0.34500 0.36830 0.28690 -0.01570 -0.07180 0.03180  399 ILE B N     
6741 C  CA    . ILE B 403 ? 0.37540 0.39750 0.32610 -0.01720 -0.07380 0.03000  399 ILE B CA    
6742 C  C     . ILE B 403 ? 0.39500 0.42220 0.34310 -0.02160 -0.08130 0.02910  399 ILE B C     
6743 O  O     . ILE B 403 ? 0.42910 0.46150 0.38690 -0.02290 -0.08520 0.03350  399 ILE B O     
6744 C  CB    . ILE B 403 ? 0.35920 0.37300 0.30850 -0.01690 -0.06980 0.02270  399 ILE B CB    
6745 C  CG1   . ILE B 403 ? 0.37930 0.38860 0.33230 -0.01300 -0.06280 0.02370  399 ILE B CG1   
6746 C  CG2   . ILE B 403 ? 0.35180 0.36500 0.30980 -0.01930 -0.07260 0.02130  399 ILE B CG2   
6747 C  CD1   . ILE B 403 ? 0.39330 0.39510 0.34230 -0.01240 -0.05890 0.01690  399 ILE B CD1   
6748 N  N     . ASN B 404 ? 0.39070 0.41660 0.32580 -0.02400 -0.08340 0.02320  400 ASN B N     
6749 C  CA    . ASN B 404 ? 0.43330 0.46320 0.36450 -0.02870 -0.09070 0.02110  400 ASN B CA    
6750 C  C     . ASN B 404 ? 0.40760 0.44770 0.34150 -0.02990 -0.09600 0.02940  400 ASN B C     
6751 O  O     . ASN B 404 ? 0.38440 0.42950 0.32580 -0.03270 -0.10150 0.03210  400 ASN B O     
6752 C  CB    . ASN B 404 ? 0.40220 0.42880 0.31750 -0.03060 -0.09130 0.01290  400 ASN B CB    
6753 C  CG    . ASN B 404 ? 0.48850 0.50520 0.40150 -0.02880 -0.08570 0.00520  400 ASN B CG    
6754 O  OD1   . ASN B 404 ? 0.46040 0.47390 0.37380 -0.02490 -0.07950 0.00600  400 ASN B OD1   
6755 N  ND2   . ASN B 404 ? 0.44230 0.45410 0.35320 -0.03170 -0.08820 -0.00210 400 ASN B ND2   
6756 N  N     . TRP B 405 ? 0.42670 0.47020 0.35560 -0.02780 -0.09450 0.03420  401 TRP B N     
6757 C  CA    . TRP B 405 ? 0.48530 0.53880 0.41670 -0.02890 -0.09980 0.04270  401 TRP B CA    
6758 C  C     . TRP B 405 ? 0.44030 0.49720 0.38930 -0.02700 -0.10020 0.05020  401 TRP B C     
6759 O  O     . TRP B 405 ? 0.43620 0.50100 0.39140 -0.02930 -0.10640 0.05530  401 TRP B O     
6760 C  CB    . TRP B 405 ? 0.42850 0.48440 0.35200 -0.02680 -0.09740 0.04720  401 TRP B CB    
6761 C  CG    . TRP B 405 ? 0.42740 0.48180 0.33370 -0.02860 -0.09700 0.04050  401 TRP B CG    
6762 C  CD1   . TRP B 405 ? 0.43710 0.48600 0.33560 -0.02620 -0.09050 0.03650  401 TRP B CD1   
6763 C  CD2   . TRP B 405 ? 0.50350 0.56220 0.39800 -0.03330 -0.10300 0.03650  401 TRP B CD2   
6764 N  NE1   . TRP B 405 ? 0.53990 0.58970 0.42270 -0.02870 -0.09180 0.03030  401 TRP B NE1   
6765 C  CE2   . TRP B 405 ? 0.50030 0.55570 0.37980 -0.03320 -0.09940 0.02980  401 TRP B CE2   
6766 C  CE3   . TRP B 405 ? 0.55640 0.62180 0.45150 -0.03780 -0.11130 0.03780  401 TRP B CE3   
6767 C  CZ2   . TRP B 405 ? 0.52360 0.58180 0.38830 -0.03710 -0.10340 0.02400  401 TRP B CZ2   
6768 C  CZ3   . TRP B 405 ? 0.53120 0.59930 0.41130 -0.04220 -0.11580 0.03210  401 TRP B CZ3   
6769 C  CH2   . TRP B 405 ? 0.57080 0.63510 0.43560 -0.04170 -0.11160 0.02490  401 TRP B CH2   
6770 N  N     . GLY B 406 ? 0.36270 0.41400 0.32010 -0.02280 -0.09350 0.05100  402 GLY B N     
6771 C  CA    . GLY B 406 ? 0.42250 0.47700 0.39660 -0.02050 -0.09290 0.05760  402 GLY B CA    
6772 C  C     . GLY B 406 ? 0.39540 0.45110 0.37830 -0.02300 -0.09580 0.05560  402 GLY B C     
6773 O  O     . GLY B 406 ? 0.37570 0.43920 0.36910 -0.02390 -0.10020 0.06150  402 GLY B O     
6774 N  N     . VAL B 407 ? 0.36220 0.41070 0.34170 -0.02430 -0.09360 0.04760  403 VAL B N     
6775 C  CA    . VAL B 407 ? 0.30630 0.35550 0.29420 -0.02710 -0.09630 0.04580  403 VAL B CA    
6776 C  C     . VAL B 407 ? 0.35780 0.41410 0.34350 -0.03230 -0.10510 0.04640  403 VAL B C     
6777 O  O     . VAL B 407 ? 0.40410 0.46650 0.40130 -0.03420 -0.10900 0.05020  403 VAL B O     
6778 C  CB    . VAL B 407 ? 0.36660 0.40600 0.35010 -0.02770 -0.09250 0.03730  403 VAL B CB    
6779 C  CG1   . VAL B 407 ? 0.34770 0.38760 0.33670 -0.03210 -0.09700 0.03460  403 VAL B CG1   
6780 C  CG2   . VAL B 407 ? 0.39510 0.42910 0.38450 -0.02300 -0.08440 0.03770  403 VAL B CG2   
6781 N  N     . HIS B 408 ? 0.39580 0.45200 0.36680 -0.03480 -0.10840 0.04280  404 HIS B N     
6782 C  CA    . HIS B 408 ? 0.36620 0.42800 0.33310 -0.04060 -0.11700 0.04160  404 HIS B CA    
6783 C  C     . HIS B 408 ? 0.38910 0.46270 0.36040 -0.04130 -0.12270 0.05090  404 HIS B C     
6784 O  O     . HIS B 408 ? 0.35050 0.43140 0.32930 -0.04480 -0.12920 0.05400  404 HIS B O     
6785 C  CB    . HIS B 408 ? 0.34330 0.40040 0.29190 -0.04340 -0.11840 0.03280  404 HIS B CB    
6786 C  CG    . HIS B 408 ? 0.41510 0.47570 0.35910 -0.04990 -0.12690 0.02930  404 HIS B CG    
6787 N  ND1   . HIS B 408 ? 0.43230 0.48790 0.37980 -0.05330 -0.12880 0.02320  404 HIS B ND1   
6788 C  CD2   . HIS B 408 ? 0.43310 0.50200 0.36970 -0.05380 -0.13420 0.03120  404 HIS B CD2   
6789 C  CE1   . HIS B 408 ? 0.45800 0.51810 0.40050 -0.05920 -0.13700 0.02110  404 HIS B CE1   
6790 N  NE2   . HIS B 408 ? 0.38270 0.45120 0.31810 -0.05970 -0.14040 0.02570  404 HIS B NE2   
6791 N  N     . CYS B 409 ? 0.41570 0.49170 0.38270 -0.03800 -0.12060 0.05590  405 CYS B N     
6792 C  CA    . CYS B 409 ? 0.41190 0.49890 0.37950 -0.03920 -0.12660 0.06440  405 CYS B CA    
6793 C  C     . CYS B 409 ? 0.37470 0.46750 0.35960 -0.03520 -0.12550 0.07480  405 CYS B C     
6794 O  O     . CYS B 409 ? 0.41220 0.51520 0.40170 -0.03640 -0.13160 0.08280  405 CYS B O     
6795 C  CB    . CYS B 409 ? 0.40330 0.49040 0.35580 -0.03840 -0.12560 0.06480  405 CYS B CB    
6796 S  SG    . CYS B 409 ? 0.48500 0.56710 0.41620 -0.04290 -0.12700 0.05300  405 CYS B SG    
6797 N  N     . TYR B 410 ? 0.43410 0.52080 0.42810 -0.03030 -0.11800 0.07510  406 TYR B N     
6798 C  CA    . TYR B 410 ? 0.41220 0.50360 0.42240 -0.02590 -0.11610 0.08430  406 TYR B CA    
6799 C  C     . TYR B 410 ? 0.39720 0.49330 0.42300 -0.02680 -0.11810 0.08610  406 TYR B C     
6800 O  O     . TYR B 410 ? 0.45930 0.55000 0.48660 -0.02800 -0.11570 0.07970  406 TYR B O     
6801 C  CB    . TYR B 410 ? 0.37010 0.45290 0.38230 -0.02030 -0.10690 0.08350  406 TYR B CB    
6802 C  CG    . TYR B 410 ? 0.41560 0.50190 0.44370 -0.01540 -0.10430 0.09220  406 TYR B CG    
6803 C  CD1   . TYR B 410 ? 0.48690 0.57860 0.51630 -0.01370 -0.10670 0.10070  406 TYR B CD1   
6804 C  CD2   . TYR B 410 ? 0.41340 0.49730 0.45520 -0.01230 -0.09930 0.09190  406 TYR B CD2   
6805 C  CE1   . TYR B 410 ? 0.50270 0.59670 0.54750 -0.00880 -0.10420 0.10850  406 TYR B CE1   
6806 C  CE2   . TYR B 410 ? 0.43340 0.52000 0.48970 -0.00740 -0.09640 0.09900  406 TYR B CE2   
6807 C  CZ    . TYR B 410 ? 0.46090 0.55200 0.51900 -0.00550 -0.09890 0.10720  406 TYR B CZ    
6808 O  OH    . TYR B 410 ? 0.49260 0.58530 0.56600 -0.00030 -0.09580 0.11400  406 TYR B OH    
6809 N  N     . LEU B 411 ? 0.38380 0.49040 0.42180 -0.02640 -0.12270 0.09520  407 LEU B N     
6810 C  CA    . LEU B 411 ? 0.39980 0.51250 0.45430 -0.02700 -0.12450 0.09810  407 LEU B CA    
6811 C  C     . LEU B 411 ? 0.40020 0.51140 0.47000 -0.02050 -0.11700 0.10220  407 LEU B C     
6812 O  O     . LEU B 411 ? 0.38030 0.49490 0.45660 -0.01640 -0.11610 0.10970  407 LEU B O     
6813 C  CB    . LEU B 411 ? 0.44710 0.57310 0.50750 -0.03040 -0.13400 0.10570  407 LEU B CB    
6814 C  CG    . LEU B 411 ? 0.53020 0.66250 0.60560 -0.03270 -0.13660 0.10680  407 LEU B CG    
6815 C  CD1   . LEU B 411 ? 0.52120 0.66220 0.59320 -0.04000 -0.14720 0.10730  407 LEU B CD1   
6816 C  CD2   . LEU B 411 ? 0.53140 0.67080 0.62720 -0.02730 -0.13410 0.11610  407 LEU B CD2   
6817 N  N     . ALA B 412 ? 0.35070 0.45670 0.42580 -0.01960 -0.11160 0.09720  408 ALA B N     
6818 C  CA    . ALA B 412 ? 0.42100 0.52480 0.50910 -0.01370 -0.10370 0.09940  408 ALA B CA    
6819 C  C     . ALA B 412 ? 0.42180 0.53590 0.52860 -0.01350 -0.10570 0.10510  408 ALA B C     
6820 O  O     . ALA B 412 ? 0.44990 0.56640 0.55950 -0.01760 -0.10810 0.10230  408 ALA B O     
6821 C  CB    . ALA B 412 ? 0.40110 0.49390 0.48350 -0.01280 -0.09630 0.09090  408 ALA B CB    
6822 N  N     . GLN B 413 ? 0.40740 0.52750 0.52760 -0.00870 -0.10470 0.11330  409 GLN B N     
6823 C  CA    . GLN B 413 ? 0.40200 0.53300 0.54150 -0.00780 -0.10620 0.11960  409 GLN B CA    
6824 C  C     . GLN B 413 ? 0.39940 0.52810 0.55200 -0.00160 -0.09690 0.11980  409 GLN B C     
6825 O  O     . GLN B 413 ? 0.53060 0.66680 0.69800 -0.00130 -0.09610 0.12220  409 GLN B O     
6826 C  CB    . GLN B 413 ? 0.49640 0.63830 0.64410 -0.00690 -0.11270 0.12970  409 GLN B CB    
6827 C  CG    . GLN B 413 ? 0.69570 0.84140 0.83010 -0.01290 -0.12230 0.13040  409 GLN B CG    
6828 C  CD    . GLN B 413 ? 0.80500 0.96080 0.94630 -0.01150 -0.12830 0.14120  409 GLN B CD    
6829 O  OE1   . GLN B 413 ? 0.85440 1.01650 1.01370 -0.00660 -0.12650 0.14880  409 GLN B OE1   
6830 N  NE2   . GLN B 413 ? 0.82950 0.98740 0.95680 -0.01570 -0.13530 0.14210  409 GLN B NE2   
6831 N  N     . THR B 414 ? 0.36390 0.48260 0.51090 0.00270  -0.08980 0.11670  410 THR B N     
6832 C  CA    . THR B 414 ? 0.41810 0.53520 0.57780 0.00870  -0.08130 0.11730  410 THR B CA    
6833 C  C     . THR B 414 ? 0.36000 0.46830 0.51320 0.00820  -0.07450 0.10860  410 THR B C     
6834 O  O     . THR B 414 ? 0.34790 0.44740 0.48500 0.00560  -0.07420 0.10230  410 THR B O     
6835 C  CB    . THR B 414 ? 0.48710 0.59880 0.64720 0.01440  -0.07760 0.12040  410 THR B CB    
6836 O  OG1   . THR B 414 ? 0.48880 0.60970 0.65860 0.01580  -0.08330 0.13000  410 THR B OG1   
6837 C  CG2   . THR B 414 ? 0.50100 0.60800 0.67080 0.02050  -0.06770 0.11830  410 THR B CG2   
6838 N  N     . PRO B 415 ? 0.35410 0.46560 0.51990 0.01060  -0.06910 0.10840  411 PRO B N     
6839 C  CA    . PRO B 415 ? 0.37580 0.48050 0.53610 0.00960  -0.06300 0.10090  411 PRO B CA    
6840 C  C     . PRO B 415 ? 0.36960 0.46160 0.51750 0.01200  -0.05710 0.09530  411 PRO B C     
6841 O  O     . PRO B 415 ? 0.39470 0.48360 0.54640 0.01720  -0.05260 0.09690  411 PRO B O     
6842 C  CB    . PRO B 415 ? 0.36410 0.47570 0.54180 0.01320  -0.05730 0.10340  411 PRO B CB    
6843 C  CG    . PRO B 415 ? 0.34030 0.46410 0.53280 0.01410  -0.06250 0.11190  411 PRO B CG    
6844 C  CD    . PRO B 415 ? 0.33210 0.45480 0.51820 0.01400  -0.06860 0.11560  411 PRO B CD    
6845 N  N     . GLY B 416 ? 0.41040 0.49500 0.54390 0.00820  -0.05740 0.08870  412 GLY B N     
6846 C  CA    . GLY B 416 ? 0.35970 0.43300 0.48210 0.01010  -0.05160 0.08320  412 GLY B CA    
6847 C  C     . GLY B 416 ? 0.43000 0.49840 0.54420 0.01170  -0.05300 0.08450  412 GLY B C     
6848 O  O     . GLY B 416 ? 0.45970 0.51930 0.56680 0.01380  -0.04790 0.08080  412 GLY B O     
6849 N  N     . ALA B 417 ? 0.36970 0.44390 0.48490 0.01060  -0.05980 0.09000  413 ALA B N     
6850 C  CA    . ALA B 417 ? 0.30160 0.37230 0.41030 0.01210  -0.06120 0.09260  413 ALA B CA    
6851 C  C     . ALA B 417 ? 0.37840 0.44370 0.46900 0.00810  -0.06420 0.08800  413 ALA B C     
6852 O  O     . ALA B 417 ? 0.47010 0.53340 0.55390 0.00870  -0.06580 0.09030  413 ALA B O     
6853 C  CB    . ALA B 417 ? 0.25570 0.33610 0.37420 0.01300  -0.06710 0.10170  413 ALA B CB    
6854 N  N     . PHE B 418 ? 0.32720 0.38990 0.41000 0.00420  -0.06480 0.08170  414 PHE B N     
6855 C  CA    . PHE B 418 ? 0.35090 0.40780 0.41700 0.00090  -0.06670 0.07640  414 PHE B CA    
6856 C  C     . PHE B 418 ? 0.36620 0.41380 0.42630 0.00170  -0.06000 0.06950  414 PHE B C     
6857 O  O     . PHE B 418 ? 0.32190 0.36900 0.38520 0.00040  -0.05820 0.06620  414 PHE B O     
6858 C  CB    . PHE B 418 ? 0.34860 0.41000 0.41050 -0.00460 -0.07380 0.07490  414 PHE B CB    
6859 C  CG    . PHE B 418 ? 0.39250 0.44920 0.43750 -0.00780 -0.07650 0.06990  414 PHE B CG    
6860 C  CD1   . PHE B 418 ? 0.36200 0.41080 0.39830 -0.00930 -0.07360 0.06220  414 PHE B CD1   
6861 C  CD2   . PHE B 418 ? 0.34890 0.40940 0.38690 -0.00920 -0.08180 0.07310  414 PHE B CD2   
6862 C  CE1   . PHE B 418 ? 0.38130 0.42580 0.40280 -0.01180 -0.07550 0.05730  414 PHE B CE1   
6863 C  CE2   . PHE B 418 ? 0.33000 0.38660 0.35210 -0.01200 -0.08370 0.06800  414 PHE B CE2   
6864 C  CZ    . PHE B 418 ? 0.37430 0.42280 0.38840 -0.01310 -0.08040 0.05990  414 PHE B CZ    
6865 N  N     . GLN B 419 ? 0.31760 0.35840 0.36940 0.00360  -0.05650 0.06770  415 GLN B N     
6866 C  CA    . GLN B 419 ? 0.30550 0.33790 0.35290 0.00490  -0.04990 0.06220  415 GLN B CA    
6867 C  C     . GLN B 419 ? 0.35950 0.38620 0.39190 0.00250  -0.05060 0.05700  415 GLN B C     
6868 O  O     . GLN B 419 ? 0.36760 0.39220 0.39290 0.00320  -0.05060 0.05800  415 GLN B O     
6869 C  CB    . GLN B 419 ? 0.36420 0.39340 0.41680 0.00940  -0.04450 0.06450  415 GLN B CB    
6870 C  CG    . GLN B 419 ? 0.37650 0.41030 0.44450 0.01250  -0.04240 0.06840  415 GLN B CG    
6871 C  CD    . GLN B 419 ? 0.43440 0.46720 0.50620 0.01240  -0.03790 0.06420  415 GLN B CD    
6872 O  OE1   . GLN B 419 ? 0.41840 0.44450 0.48280 0.01210  -0.03390 0.05880  415 GLN B OE1   
6873 N  NE2   . GLN B 419 ? 0.33620 0.37640 0.41970 0.01260  -0.03870 0.06690  415 GLN B NE2   
6874 N  N     . ILE B 420 ? 0.26970 0.29400 0.29770 -0.00020 -0.05080 0.05170  416 ILE B N     
6875 C  CA    . ILE B 420 ? 0.36940 0.38840 0.38420 -0.00220 -0.05120 0.04630  416 ILE B CA    
6876 C  C     . ILE B 420 ? 0.28360 0.29690 0.29740 -0.00230 -0.04670 0.04120  416 ILE B C     
6877 O  O     . ILE B 420 ? 0.31110 0.32610 0.33230 -0.00310 -0.04630 0.04090  416 ILE B O     
6878 C  CB    . ILE B 420 ? 0.33010 0.35230 0.33930 -0.00620 -0.05800 0.04500  416 ILE B CB    
6879 C  CG1   . ILE B 420 ? 0.40710 0.42430 0.40220 -0.00750 -0.05810 0.03970  416 ILE B CG1   
6880 C  CG2   . ILE B 420 ? 0.25880 0.28270 0.27410 -0.00880 -0.06000 0.04330  416 ILE B CG2   
6881 C  CD1   . ILE B 420 ? 0.35400 0.37460 0.34150 -0.01110 -0.06480 0.03850  416 ILE B CD1   
6882 N  N     . GLY B 421 ? 0.31350 0.32070 0.31890 -0.00150 -0.04340 0.03760  417 GLY B N     
6883 C  CA    . GLY B 421 ? 0.37650 0.37870 0.38100 -0.00130 -0.03910 0.03340  417 GLY B CA    
6884 C  C     . GLY B 421 ? 0.39180 0.39050 0.38870 -0.00400 -0.04100 0.02840  417 GLY B C     
6885 O  O     . GLY B 421 ? 0.33740 0.33150 0.32630 -0.00350 -0.03900 0.02510  417 GLY B O     
6886 N  N     . LEU B 422 ? 0.37210 0.37300 0.37210 -0.00670 -0.04490 0.02770  418 LEU B N     
6887 C  CA    . LEU B 422 ? 0.35640 0.35350 0.34950 -0.00930 -0.04740 0.02270  418 LEU B CA    
6888 C  C     . LEU B 422 ? 0.39200 0.38430 0.38640 -0.00960 -0.04430 0.01970  418 LEU B C     
6889 O  O     . LEU B 422 ? 0.42430 0.41220 0.41340 -0.01110 -0.04560 0.01540  418 LEU B O     
6890 C  CB    . LEU B 422 ? 0.31590 0.31680 0.31130 -0.01270 -0.05360 0.02310  418 LEU B CB    
6891 C  CG    . LEU B 422 ? 0.39750 0.40340 0.38960 -0.01320 -0.05790 0.02570  418 LEU B CG    
6892 C  CD1   . LEU B 422 ? 0.33460 0.34520 0.33000 -0.01700 -0.06450 0.02630  418 LEU B CD1   
6893 C  CD2   . LEU B 422 ? 0.36080 0.36340 0.34040 -0.01270 -0.05760 0.02220  418 LEU B CD2   
6894 N  N     . GLY B 423 ? 0.34790 0.34090 0.34900 -0.00820 -0.04020 0.02180  419 GLY B N     
6895 C  CA    . GLY B 423 ? 0.37870 0.36760 0.38010 -0.00860 -0.03740 0.01950  419 GLY B CA    
6896 C  C     . GLY B 423 ? 0.36140 0.34460 0.35380 -0.00760 -0.03550 0.01570  419 GLY B C     
6897 O  O     . GLY B 423 ? 0.43300 0.41220 0.42240 -0.00890 -0.03650 0.01240  419 GLY B O     
6898 N  N     . LEU B 424 ? 0.32670 0.30960 0.31520 -0.00520 -0.03280 0.01630  420 LEU B N     
6899 C  CA    . LEU B 424 ? 0.36010 0.33880 0.34060 -0.00420 -0.03090 0.01320  420 LEU B CA    
6900 C  C     . LEU B 424 ? 0.34340 0.32280 0.31670 -0.00390 -0.03310 0.01240  420 LEU B C     
6901 O  O     . LEU B 424 ? 0.34220 0.31870 0.30860 -0.00340 -0.03220 0.00920  420 LEU B O     
6902 C  CB    . LEU B 424 ? 0.34470 0.32230 0.32550 -0.00210 -0.02590 0.01420  420 LEU B CB    
6903 C  CG    . LEU B 424 ? 0.41700 0.39060 0.39210 -0.00140 -0.02340 0.01130  420 LEU B CG    
6904 C  CD1   . LEU B 424 ? 0.35500 0.32580 0.33070 -0.00280 -0.02430 0.00890  420 LEU B CD1   
6905 C  CD2   . LEU B 424 ? 0.31380 0.28710 0.29010 -0.00000 -0.01900 0.01260  420 LEU B CD2   
6906 N  N     . ALA B 425 ? 0.33210 0.31590 0.30710 -0.00420 -0.03580 0.01550  421 ALA B N     
6907 C  CA    . ALA B 425 ? 0.31820 0.30380 0.28610 -0.00440 -0.03840 0.01540  421 ALA B CA    
6908 C  C     . ALA B 425 ? 0.40430 0.38800 0.36580 -0.00250 -0.03490 0.01480  421 ALA B C     
6909 O  O     . ALA B 425 ? 0.35830 0.34070 0.31170 -0.00270 -0.03520 0.01160  421 ALA B O     
6910 C  CB    . ALA B 425 ? 0.33800 0.32250 0.30100 -0.00680 -0.04260 0.01120  421 ALA B CB    
6911 N  N     . ALA B 426 ? 0.40790 0.39140 0.37320 -0.00070 -0.03130 0.01770  422 ALA B N     
6912 C  CA    . ALA B 426 ? 0.40900 0.39080 0.36960 0.00080  -0.02790 0.01780  422 ALA B CA    
6913 C  C     . ALA B 426 ? 0.41240 0.39770 0.36980 0.00110  -0.02950 0.02140  422 ALA B C     
6914 O  O     . ALA B 426 ? 0.33160 0.31960 0.29440 0.00150  -0.03080 0.02580  422 ALA B O     
6915 C  CB    . ALA B 426 ? 0.26570 0.24550 0.23170 0.00210  -0.02370 0.01910  422 ALA B CB    
6916 N  N     . MET B 427 ? 0.42860 0.41410 0.37750 0.00100  -0.02920 0.01990  423 MET B N     
6917 C  CA    . MET B 427 ? 0.39680 0.38590 0.34240 0.00120  -0.03010 0.02410  423 MET B CA    
6918 C  C     . MET B 427 ? 0.45230 0.44030 0.40360 0.00270  -0.02720 0.02850  423 MET B C     
6919 O  O     . MET B 427 ? 0.37060 0.35500 0.32360 0.00350  -0.02330 0.02700  423 MET B O     
6920 C  CB    . MET B 427 ? 0.36370 0.35340 0.29930 0.00090  -0.02920 0.02170  423 MET B CB    
6921 C  CG    . MET B 427 ? 0.41420 0.40560 0.34280 -0.00060 -0.03250 0.01770  423 MET B CG    
6922 S  SD    . MET B 427 ? 0.51600 0.50750 0.43390 -0.00000 -0.02940 0.01370  423 MET B SD    
6923 C  CE    . MET B 427 ? 0.49450 0.49020 0.41060 0.00040  -0.02780 0.02070  423 MET B CE    
6924 N  N     . GLY B 428 ? 0.40180 0.39300 0.35630 0.00300  -0.02910 0.03410  424 GLY B N     
6925 C  CA    . GLY B 428 ? 0.31300 0.30260 0.27360 0.00450  -0.02660 0.03840  424 GLY B CA    
6926 C  C     . GLY B 428 ? 0.40720 0.39550 0.37830 0.00570  -0.02590 0.03950  424 GLY B C     
6927 O  O     . GLY B 428 ? 0.41070 0.39790 0.38780 0.00720  -0.02440 0.04350  424 GLY B O     
6928 N  N     . HIS B 429 ? 0.35990 0.34830 0.33350 0.00520  -0.02680 0.03630  425 HIS B N     
6929 C  CA    . HIS B 429 ? 0.36900 0.35720 0.35240 0.00630  -0.02570 0.03720  425 HIS B CA    
6930 C  C     . HIS B 429 ? 0.36290 0.35470 0.35360 0.00760  -0.02780 0.04320  425 HIS B C     
6931 O  O     . HIS B 429 ? 0.40290 0.39300 0.40100 0.00970  -0.02500 0.04550  425 HIS B O     
6932 C  CB    . HIS B 429 ? 0.42170 0.41130 0.40640 0.00490  -0.02760 0.03400  425 HIS B CB    
6933 C  CG    . HIS B 429 ? 0.47730 0.46760 0.47170 0.00580  -0.02600 0.03460  425 HIS B CG    
6934 N  ND1   . HIS B 429 ? 0.52340 0.51430 0.51990 0.00440  -0.02660 0.03200  425 HIS B ND1   
6935 C  CD2   . HIS B 429 ? 0.50890 0.49950 0.51170 0.00800  -0.02360 0.03760  425 HIS B CD2   
6936 C  CE1   . HIS B 429 ? 0.49920 0.49150 0.50460 0.00560  -0.02450 0.03350  425 HIS B CE1   
6937 N  NE2   . HIS B 429 ? 0.46630 0.45830 0.47560 0.00800  -0.02260 0.03650  425 HIS B NE2   
6938 N  N     . ALA B 430 ? 0.32030 0.31720 0.30920 0.00640  -0.03270 0.04590  426 ALA B N     
6939 C  CA    . ALA B 430 ? 0.35010 0.35140 0.34670 0.00760  -0.03530 0.05230  426 ALA B CA    
6940 C  C     . ALA B 430 ? 0.39910 0.39870 0.39620 0.00920  -0.03380 0.05700  426 ALA B C     
6941 O  O     . ALA B 430 ? 0.36350 0.36370 0.37010 0.01140  -0.03340 0.06180  426 ALA B O     
6942 C  CB    . ALA B 430 ? 0.28700 0.29470 0.28050 0.00540  -0.04150 0.05420  426 ALA B CB    
6943 N  N     . VAL B 431 ? 0.40010 0.39770 0.38780 0.00820  -0.03270 0.05580  427 VAL B N     
6944 C  CA    . VAL B 431 ? 0.40890 0.40480 0.39690 0.00920  -0.03130 0.06060  427 VAL B CA    
6945 C  C     . VAL B 431 ? 0.33160 0.32230 0.32940 0.01170  -0.02720 0.06140  427 VAL B C     
6946 O  O     . VAL B 431 ? 0.38090 0.37150 0.38600 0.01350  -0.02740 0.06710  427 VAL B O     
6947 C  CB    . VAL B 431 ? 0.41380 0.40790 0.39100 0.00770  -0.02950 0.05810  427 VAL B CB    
6948 C  CG1   . VAL B 431 ? 0.29430 0.28630 0.27280 0.00830  -0.02770 0.06310  427 VAL B CG1   
6949 C  CG2   . VAL B 431 ? 0.44690 0.44630 0.41390 0.00540  -0.03340 0.05720  427 VAL B CG2   
6950 N  N     . ALA B 432 ? 0.31890 0.30530 0.31730 0.01190  -0.02330 0.05560  428 ALA B N     
6951 C  CA    . ALA B 432 ? 0.36300 0.34410 0.36930 0.01410  -0.01910 0.05510  428 ALA B CA    
6952 C  C     . ALA B 432 ? 0.30130 0.28440 0.31780 0.01600  -0.01880 0.05520  428 ALA B C     
6953 O  O     . ALA B 432 ? 0.35970 0.34060 0.38540 0.01860  -0.01670 0.05760  428 ALA B O     
6954 C  CB    . ALA B 432 ? 0.38080 0.35670 0.38220 0.01310  -0.01490 0.04920  428 ALA B CB    
6955 N  N     . ALA B 433 ? 0.29930 0.28620 0.31480 0.01480  -0.02070 0.05260  429 ALA B N     
6956 C  CA    . ALA B 433 ? 0.32070 0.31020 0.34620 0.01640  -0.02000 0.05280  429 ALA B CA    
6957 C  C     . ALA B 433 ? 0.33560 0.32890 0.37120 0.01880  -0.02210 0.05940  429 ALA B C     
6958 O  O     . ALA B 433 ? 0.31860 0.31220 0.36460 0.02140  -0.01960 0.06020  429 ALA B O     
6959 C  CB    . ALA B 433 ? 0.27820 0.27200 0.30120 0.01420  -0.02260 0.05010  429 ALA B CB    
6960 N  N     . ALA B 434 ? 0.32180 0.31840 0.35460 0.01800  -0.02660 0.06450  430 ALA B N     
6961 C  CA    . ALA B 434 ? 0.33000 0.33110 0.37290 0.02020  -0.02930 0.07180  430 ALA B CA    
6962 C  C     . ALA B 434 ? 0.26860 0.26440 0.32080 0.02380  -0.02520 0.07410  430 ALA B C     
6963 O  O     . ALA B 434 ? 0.28100 0.27960 0.34530 0.02670  -0.02540 0.07830  430 ALA B O     
6964 C  CB    . ALA B 434 ? 0.27090 0.27640 0.30760 0.01830  -0.03480 0.07700  430 ALA B CB    
6965 N  N     . ILE B 435 ? 0.32060 0.30890 0.36800 0.02370  -0.02130 0.07120  431 ILE B N     
6966 C  CA    . ILE B 435 ? 0.32760 0.30970 0.38350 0.02690  -0.01730 0.07250  431 ILE B CA    
6967 C  C     . ILE B 435 ? 0.28200 0.26260 0.34630 0.02940  -0.01280 0.06820  431 ILE B C     
6968 O  O     . ILE B 435 ? 0.28450 0.26390 0.36050 0.03300  -0.01080 0.07080  431 ILE B O     
6969 C  CB    . ILE B 435 ? 0.37270 0.34720 0.42080 0.02530  -0.01450 0.06990  431 ILE B CB    
6970 C  CG1   . ILE B 435 ? 0.38400 0.36090 0.42390 0.02290  -0.01850 0.07450  431 ILE B CG1   
6971 C  CG2   . ILE B 435 ? 0.40070 0.36750 0.45740 0.02820  -0.01030 0.07040  431 ILE B CG2   
6972 C  CD1   . ILE B 435 ? 0.35140 0.32260 0.38220 0.02070  -0.01610 0.07170  431 ILE B CD1   
6973 N  N     . GLY B 436 ? 0.28460 0.26530 0.34310 0.02750  -0.01080 0.06170  432 GLY B N     
6974 C  CA    . GLY B 436 ? 0.25890 0.23970 0.32440 0.02950  -0.00660 0.05780  432 GLY B CA    
6975 C  C     . GLY B 436 ? 0.33330 0.32220 0.40950 0.03140  -0.00890 0.06210  432 GLY B C     
6976 O  O     . GLY B 436 ? 0.32280 0.31200 0.40990 0.03490  -0.00540 0.06220  432 GLY B O     
6977 N  N     . GLY B 437 ? 0.29040 0.28600 0.36380 0.02920  -0.01470 0.06550  433 GLY B N     
6978 C  CA    . GLY B 437 ? 0.24900 0.25310 0.33280 0.03050  -0.01780 0.07020  433 GLY B CA    
6979 C  C     . GLY B 437 ? 0.32250 0.32730 0.41880 0.03460  -0.01780 0.07670  433 GLY B C     
6980 O  O     . GLY B 437 ? 0.32810 0.33710 0.43720 0.03770  -0.01630 0.07860  433 GLY B O     
6981 N  N     . LYS B 438 ? 0.28020 0.28110 0.37360 0.03480  -0.01940 0.08050  434 LYS B N     
6982 C  CA    . LYS B 438 ? 0.30390 0.30490 0.40970 0.03880  -0.01980 0.08760  434 LYS B CA    
6983 C  C     . LYS B 438 ? 0.30750 0.30200 0.42300 0.04310  -0.01280 0.08430  434 LYS B C     
6984 O  O     . LYS B 438 ? 0.31110 0.30800 0.44100 0.04740  -0.01190 0.08850  434 LYS B O     
6985 C  CB    . LYS B 438 ? 0.26810 0.26590 0.36820 0.03760  -0.02280 0.09250  434 LYS B CB    
6986 C  CG    . LYS B 438 ? 0.32730 0.32530 0.44030 0.04140  -0.02410 0.10120  434 LYS B CG    
6987 C  CD    . LYS B 438 ? 0.30710 0.31640 0.42820 0.04200  -0.03020 0.10890  434 LYS B CD    
6988 C  CE    . LYS B 438 ? 0.31910 0.32840 0.45440 0.04620  -0.03120 0.11800  434 LYS B CE    
6989 N  NZ    . LYS B 438 ? 0.42200 0.44260 0.56210 0.04560  -0.03880 0.12730  434 LYS B NZ    
6990 N  N     . LEU B 439 ? 0.33650 0.32310 0.44450 0.04210  -0.00780 0.07680  435 LEU B N     
6991 C  CA    . LEU B 439 ? 0.36800 0.34840 0.48370 0.04580  -0.00090 0.07240  435 LEU B CA    
6992 C  C     . LEU B 439 ? 0.26400 0.25100 0.38800 0.04780  0.00170  0.07020  435 LEU B C     
6993 O  O     . LEU B 439 ? 0.33260 0.31780 0.46780 0.05220  0.00650  0.06930  435 LEU B O     
6994 C  CB    . LEU B 439 ? 0.26650 0.23800 0.37110 0.04350  0.00330  0.06450  435 LEU B CB    
6995 C  CG    . LEU B 439 ? 0.38260 0.34640 0.48080 0.04190  0.00220  0.06610  435 LEU B CG    
6996 C  CD1   . LEU B 439 ? 0.26910 0.22590 0.35640 0.03900  0.00590  0.05820  435 LEU B CD1   
6997 C  CD2   . LEU B 439 ? 0.37850 0.33660 0.48850 0.04590  0.00370  0.07050  435 LEU B CD2   
6998 N  N     . ALA B 440 ? 0.33770 0.33220 0.45670 0.04470  -0.00130 0.06940  436 ALA B N     
6999 C  CA    . ALA B 440 ? 0.35260 0.35430 0.47990 0.04610  0.00100  0.06820  436 ALA B CA    
7000 C  C     . ALA B 440 ? 0.32270 0.33300 0.46460 0.04910  -0.00230 0.07600  436 ALA B C     
7001 O  O     . ALA B 440 ? 0.34350 0.35830 0.49740 0.05250  0.00130  0.07600  436 ALA B O     
7002 C  CB    . ALA B 440 ? 0.28190 0.28830 0.39960 0.04130  -0.00130 0.06490  436 ALA B CB    
7003 N  N     . ALA B 441 ? 0.37110 0.38410 0.51260 0.04800  -0.00880 0.08290  437 ALA B N     
7004 C  CA    . ALA B 441 ? 0.28170 0.30410 0.43630 0.05020  -0.01330 0.09130  437 ALA B CA    
7005 C  C     . ALA B 441 ? 0.33680 0.35590 0.49500 0.05220  -0.01610 0.09820  437 ALA B C     
7006 O  O     . ALA B 441 ? 0.36100 0.38470 0.51530 0.04970  -0.02300 0.10420  437 ALA B O     
7007 C  CB    . ALA B 441 ? 0.31700 0.34890 0.46650 0.04550  -0.02010 0.09340  437 ALA B CB    
7008 N  N     . PRO B 442 ? 0.36610 0.37710 0.53170 0.05670  -0.01090 0.09770  438 PRO B N     
7009 C  CA    . PRO B 442 ? 0.41140 0.41730 0.57890 0.05800  -0.01320 0.10400  438 PRO B CA    
7010 C  C     . PRO B 442 ? 0.34980 0.36460 0.52980 0.06020  -0.01900 0.11480  438 PRO B C     
7011 O  O     . PRO B 442 ? 0.43680 0.45030 0.61570 0.05970  -0.02330 0.12170  438 PRO B O     
7012 C  CB    . PRO B 442 ? 0.43090 0.42590 0.60540 0.06250  -0.00560 0.09970  438 PRO B CB    
7013 C  CG    . PRO B 442 ? 0.36810 0.36680 0.55110 0.06550  -0.00020 0.09480  438 PRO B CG    
7014 C  CD    . PRO B 442 ? 0.36290 0.37010 0.53700 0.06090  -0.00280 0.09200  438 PRO B CD    
7015 N  N     . ASP B 443 ? 0.38270 0.40710 0.57450 0.06230  -0.01940 0.11690  439 ASP B N     
7016 C  CA    . ASP B 443 ? 0.46670 0.50140 0.67180 0.06430  -0.02520 0.12740  439 ASP B CA    
7017 C  C     . ASP B 443 ? 0.42280 0.46720 0.61890 0.05870  -0.03400 0.13180  439 ASP B C     
7018 O  O     . ASP B 443 ? 0.46510 0.51870 0.67040 0.05940  -0.03990 0.14100  439 ASP B O     
7019 C  CB    . ASP B 443 ? 0.48890 0.53080 0.71080 0.06870  -0.02160 0.12740  439 ASP B CB    
7020 C  CG    . ASP B 443 ? 0.72010 0.76610 0.93500 0.06540  -0.01940 0.11960  439 ASP B CG    
7021 O  OD1   . ASP B 443 ? 0.73190 0.76990 0.93260 0.06250  -0.01590 0.11100  439 ASP B OD1   
7022 O  OD2   . ASP B 443 ? 0.81070 0.86830 1.03480 0.06540  -0.02160 0.12250  439 ASP B OD2   
7023 N  N     . ARG B 444 ? 0.40960 0.45250 0.58850 0.05320  -0.03510 0.12540  440 ARG B N     
7024 C  CA    . ARG B 444 ? 0.34360 0.39540 0.51390 0.04780  -0.04300 0.12800  440 ARG B CA    
7025 C  C     . ARG B 444 ? 0.41320 0.46010 0.56630 0.04360  -0.04630 0.12790  440 ARG B C     
7026 O  O     . ARG B 444 ? 0.38970 0.42620 0.53440 0.04360  -0.04160 0.12260  440 ARG B O     
7027 C  CB    . ARG B 444 ? 0.33310 0.38850 0.49840 0.04450  -0.04200 0.12080  440 ARG B CB    
7028 C  CG    . ARG B 444 ? 0.43300 0.49630 0.61560 0.04800  -0.03980 0.12230  440 ARG B CG    
7029 C  CD    . ARG B 444 ? 0.44250 0.50960 0.62090 0.04450  -0.03880 0.11590  440 ARG B CD    
7030 N  NE    . ARG B 444 ? 0.43620 0.51060 0.60670 0.03870  -0.04700 0.11770  440 ARG B NE    
7031 C  CZ    . ARG B 444 ? 0.46050 0.53800 0.62560 0.03440  -0.04800 0.11290  440 ARG B CZ    
7032 N  NH1   . ARG B 444 ? 0.54360 0.61830 0.71040 0.03540  -0.04130 0.10670  440 ARG B NH1   
7033 N  NH2   . ARG B 444 ? 0.50120 0.58430 0.65890 0.02910  -0.05560 0.11430  440 ARG B NH2   
7034 N  N     . PRO B 445 ? 0.38250 0.43720 0.53040 0.04010  -0.05420 0.13380  441 PRO B N     
7035 C  CA    . PRO B 445 ? 0.35710 0.40840 0.48800 0.03600  -0.05700 0.13330  441 PRO B CA    
7036 C  C     . PRO B 445 ? 0.36120 0.40870 0.47660 0.03190  -0.05510 0.12310  441 PRO B C     
7037 O  O     . PRO B 445 ? 0.36820 0.42030 0.48370 0.02990  -0.05600 0.11910  441 PRO B O     
7038 C  CB    . PRO B 445 ? 0.33390 0.39640 0.46380 0.03320  -0.06610 0.14190  441 PRO B CB    
7039 C  CG    . PRO B 445 ? 0.34210 0.41360 0.49120 0.03660  -0.06810 0.14820  441 PRO B CG    
7040 C  CD    . PRO B 445 ? 0.36020 0.42810 0.51660 0.03920  -0.06100 0.14060  441 PRO B CD    
7041 N  N     . VAL B 446 ? 0.30240 0.34150 0.40560 0.03050  -0.05240 0.11930  442 VAL B N     
7042 C  CA    . VAL B 446 ? 0.31300 0.34800 0.40190 0.02690  -0.05040 0.11000  442 VAL B CA    
7043 C  C     . VAL B 446 ? 0.33710 0.37200 0.41070 0.02310  -0.05400 0.11070  442 VAL B C     
7044 O  O     . VAL B 446 ? 0.33780 0.36900 0.40950 0.02400  -0.05320 0.11470  442 VAL B O     
7045 C  CB    . VAL B 446 ? 0.36130 0.38600 0.45030 0.02910  -0.04230 0.10280  442 VAL B CB    
7046 C  CG1   . VAL B 446 ? 0.37720 0.39760 0.45050 0.02530  -0.04080 0.09450  442 VAL B CG1   
7047 C  CG2   . VAL B 446 ? 0.34830 0.37430 0.45030 0.03220  -0.03860 0.10080  442 VAL B CG2   
7048 N  N     . VAL B 447 ? 0.41070 0.44990 0.47370 0.01890  -0.05770 0.10700  443 VAL B N     
7049 C  CA    . VAL B 447 ? 0.38070 0.42110 0.42850 0.01520  -0.06110 0.10690  443 VAL B CA    
7050 C  C     . VAL B 447 ? 0.37820 0.41460 0.41380 0.01230  -0.05910 0.09700  443 VAL B C     
7051 O  O     . VAL B 447 ? 0.33510 0.37240 0.37310 0.01150  -0.05900 0.09230  443 VAL B O     
7052 C  CB    . VAL B 447 ? 0.36330 0.41430 0.41000 0.01260  -0.06930 0.11330  443 VAL B CB    
7053 C  CG1   . VAL B 447 ? 0.31210 0.36450 0.34110 0.00840  -0.07230 0.11140  443 VAL B CG1   
7054 C  CG2   . VAL B 447 ? 0.29120 0.34600 0.35010 0.01570  -0.07140 0.12410  443 VAL B CG2   
7055 N  N     . ALA B 448 ? 0.32270 0.35500 0.34580 0.01070  -0.05750 0.09440  444 ALA B N     
7056 C  CA    . ALA B 448 ? 0.34730 0.37580 0.35880 0.00830  -0.05560 0.08560  444 ALA B CA    
7057 C  C     . ALA B 448 ? 0.37590 0.40860 0.37350 0.00470  -0.06000 0.08540  444 ALA B C     
7058 O  O     . ALA B 448 ? 0.43550 0.47000 0.42870 0.00450  -0.06100 0.09050  444 ALA B O     
7059 C  CB    . ALA B 448 ? 0.27210 0.29170 0.28120 0.00980  -0.04890 0.08150  444 ALA B CB    
7060 N  N     . LEU B 449 ? 0.30860 0.34320 0.29960 0.00180  -0.06250 0.07970  445 LEU B N     
7061 C  CA    . LEU B 449 ? 0.36670 0.40470 0.34350 -0.00160 -0.06620 0.07770  445 LEU B CA    
7062 C  C     . LEU B 449 ? 0.39080 0.42230 0.35800 -0.00230 -0.06180 0.06890  445 LEU B C     
7063 O  O     . LEU B 449 ? 0.33590 0.36380 0.30480 -0.00260 -0.06040 0.06270  445 LEU B O     
7064 C  CB    . LEU B 449 ? 0.37280 0.41780 0.34940 -0.00470 -0.07290 0.07750  445 LEU B CB    
7065 C  CG    . LEU B 449 ? 0.38530 0.43320 0.34640 -0.00860 -0.07660 0.07340  445 LEU B CG    
7066 C  CD1   . LEU B 449 ? 0.36820 0.42190 0.32260 -0.00930 -0.07930 0.08030  445 LEU B CD1   
7067 C  CD2   . LEU B 449 ? 0.34850 0.40090 0.31030 -0.01190 -0.08260 0.07080  445 LEU B CD2   
7068 N  N     . VAL B 450 ? 0.31850 0.34850 0.27630 -0.00240 -0.05950 0.06880  446 VAL B N     
7069 C  CA    . VAL B 450 ? 0.33570 0.35930 0.28640 -0.00220 -0.05440 0.06170  446 VAL B CA    
7070 C  C     . VAL B 450 ? 0.35180 0.37810 0.28840 -0.00410 -0.05490 0.06020  446 VAL B C     
7071 O  O     . VAL B 450 ? 0.38850 0.42050 0.32120 -0.00500 -0.05790 0.06610  446 VAL B O     
7072 C  CB    . VAL B 450 ? 0.32620 0.34380 0.28370 0.00070  -0.04860 0.06310  446 VAL B CB    
7073 C  CG1   . VAL B 450 ? 0.36810 0.38430 0.33970 0.00280  -0.04810 0.06530  446 VAL B CG1   
7074 C  CG2   . VAL B 450 ? 0.35380 0.37300 0.30960 0.00120  -0.04810 0.06990  446 VAL B CG2   
7075 N  N     . GLY B 451 ? 0.32870 0.35100 0.25770 -0.00450 -0.05200 0.05240  447 GLY B N     
7076 C  CA    . GLY B 451 ? 0.36480 0.38900 0.28070 -0.00570 -0.05100 0.04990  447 GLY B CA    
7077 C  C     . GLY B 451 ? 0.42890 0.45120 0.34390 -0.00420 -0.04590 0.05270  447 GLY B C     
7078 O  O     . GLY B 451 ? 0.40190 0.41960 0.32580 -0.00220 -0.04260 0.05470  447 GLY B O     
7079 N  N     . ASP B 452 ? 0.34320 0.36930 0.24690 -0.00530 -0.04530 0.05270  448 ASP B N     
7080 C  CA    . ASP B 452 ? 0.37050 0.39610 0.27310 -0.00440 -0.04080 0.05610  448 ASP B CA    
7081 C  C     . ASP B 452 ? 0.42280 0.44210 0.32650 -0.00300 -0.03530 0.05000  448 ASP B C     
7082 O  O     . ASP B 452 ? 0.38070 0.39670 0.29030 -0.00180 -0.03180 0.05280  448 ASP B O     
7083 C  CB    . ASP B 452 ? 0.36980 0.40250 0.26000 -0.00620 -0.04140 0.05810  448 ASP B CB    
7084 C  CG    . ASP B 452 ? 0.42230 0.45650 0.30090 -0.00740 -0.04160 0.04940  448 ASP B CG    
7085 O  OD1   . ASP B 452 ? 0.42830 0.46110 0.30710 -0.00810 -0.04480 0.04440  448 ASP B OD1   
7086 O  OD2   . ASP B 452 ? 0.43780 0.47470 0.30730 -0.00760 -0.03840 0.04750  448 ASP B OD2   
7087 N  N     . ALA B 453 ? 0.38250 0.39990 0.28130 -0.00310 -0.03460 0.04160  449 ALA B N     
7088 C  CA    . ALA B 453 ? 0.40270 0.41450 0.30370 -0.00160 -0.02980 0.03660  449 ALA B CA    
7089 C  C     . ALA B 453 ? 0.45480 0.46100 0.36760 -0.00030 -0.02890 0.03740  449 ALA B C     
7090 O  O     . ALA B 453 ? 0.45620 0.45880 0.37320 0.00070  -0.02500 0.03760  449 ALA B O     
7091 C  CB    . ALA B 453 ? 0.35890 0.36930 0.25340 -0.00170 -0.02950 0.02780  449 ALA B CB    
7092 N  N     . ALA B 454 ? 0.40840 0.41430 0.32680 -0.00060 -0.03260 0.03800  450 ALA B N     
7093 C  CA    . ALA B 454 ? 0.42730 0.42870 0.35680 0.00070  -0.03140 0.03910  450 ALA B CA    
7094 C  C     . ALA B 454 ? 0.39730 0.39820 0.33280 0.00170  -0.02980 0.04590  450 ALA B C     
7095 O  O     . ALA B 454 ? 0.40560 0.40180 0.34790 0.00290  -0.02670 0.04570  450 ALA B O     
7096 C  CB    . ALA B 454 ? 0.41310 0.41560 0.34780 0.00020  -0.03560 0.03900  450 ALA B CB    
7097 N  N     . PHE B 455 ? 0.36610 0.37180 0.29940 0.00100  -0.03210 0.05200  451 PHE B N     
7098 C  CA    . PHE B 455 ? 0.37460 0.37910 0.31410 0.00190  -0.03070 0.05890  451 PHE B CA    
7099 C  C     . PHE B 455 ? 0.42370 0.42550 0.36070 0.00190  -0.02600 0.05820  451 PHE B C     
7100 O  O     . PHE B 455 ? 0.38130 0.37880 0.32530 0.00280  -0.02360 0.06090  451 PHE B O     
7101 C  CB    . PHE B 455 ? 0.36420 0.37480 0.30220 0.00110  -0.03460 0.06650  451 PHE B CB    
7102 C  CG    . PHE B 455 ? 0.31720 0.32590 0.26530 0.00250  -0.03440 0.07400  451 PHE B CG    
7103 C  CD1   . PHE B 455 ? 0.29860 0.30670 0.25710 0.00400  -0.03650 0.07630  451 PHE B CD1   
7104 C  CD2   . PHE B 455 ? 0.41710 0.42440 0.36540 0.00240  -0.03180 0.07860  451 PHE B CD2   
7105 C  CE1   . PHE B 455 ? 0.35670 0.36220 0.32550 0.00580  -0.03600 0.08280  451 PHE B CE1   
7106 C  CE2   . PHE B 455 ? 0.41570 0.42010 0.37420 0.00370  -0.03160 0.08520  451 PHE B CE2   
7107 C  CZ    . PHE B 455 ? 0.40950 0.41270 0.37830 0.00560  -0.03360 0.08720  451 PHE B CZ    
7108 N  N     . ALA B 456 ? 0.45100 0.45510 0.37830 0.00100  -0.02470 0.05450  452 ALA B N     
7109 C  CA    . ALA B 456 ? 0.41660 0.41870 0.34250 0.00090  -0.02010 0.05350  452 ALA B CA    
7110 C  C     . ALA B 456 ? 0.44090 0.43670 0.37260 0.00190  -0.01720 0.04850  452 ALA B C     
7111 O  O     . ALA B 456 ? 0.44210 0.43520 0.37600 0.00180  -0.01390 0.04890  452 ALA B O     
7112 C  CB    . ALA B 456 ? 0.34740 0.35410 0.26240 0.00010  -0.01890 0.05010  452 ALA B CB    
7113 N  N     . MET B 457 ? 0.39640 0.39010 0.33050 0.00250  -0.01860 0.04410  453 MET B N     
7114 C  CA    . MET B 457 ? 0.42740 0.41590 0.36630 0.00320  -0.01590 0.03980  453 MET B CA    
7115 C  C     . MET B 457 ? 0.40460 0.38890 0.35280 0.00400  -0.01490 0.04280  453 MET B C     
7116 O  O     . MET B 457 ? 0.41000 0.39050 0.36100 0.00400  -0.01170 0.04140  453 MET B O     
7117 C  CB    . MET B 457 ? 0.49910 0.48680 0.43760 0.00340  -0.01750 0.03440  453 MET B CB    
7118 C  CG    . MET B 457 ? 0.55430 0.54450 0.48450 0.00290  -0.01820 0.02990  453 MET B CG    
7119 S  SD    . MET B 457 ? 0.54630 0.53270 0.47920 0.00320  -0.01860 0.02350  453 MET B SD    
7120 C  CE    . MET B 457 ? 0.69280 0.67480 0.63330 0.00390  -0.01490 0.02440  453 MET B CE    
7121 N  N     . ASN B 458 ? 0.44010 0.42520 0.39340 0.00460  -0.01740 0.04690  454 ASN B N     
7122 C  CA    . ASN B 458 ? 0.40390 0.38470 0.36680 0.00590  -0.01620 0.04890  454 ASN B CA    
7123 C  C     . ASN B 458 ? 0.38220 0.36410 0.35000 0.00650  -0.01790 0.05620  454 ASN B C     
7124 O  O     . ASN B 458 ? 0.38890 0.36740 0.36570 0.00800  -0.01700 0.05800  454 ASN B O     
7125 C  CB    . ASN B 458 ? 0.43200 0.41210 0.39980 0.00680  -0.01690 0.04550  454 ASN B CB    
7126 C  CG    . ASN B 458 ? 0.55160 0.52920 0.51710 0.00630  -0.01460 0.03910  454 ASN B CG    
7127 O  OD1   . ASN B 458 ? 0.51010 0.48960 0.47110 0.00560  -0.01600 0.03560  454 ASN B OD1   
7128 N  ND2   . ASN B 458 ? 0.51240 0.48550 0.48090 0.00650  -0.01110 0.03760  454 ASN B ND2   
7129 N  N     . GLY B 459 ? 0.40270 0.38930 0.36520 0.00550  -0.02000 0.06060  455 GLY B N     
7130 C  CA    . GLY B 459 ? 0.42280 0.41120 0.38990 0.00600  -0.02230 0.06850  455 GLY B CA    
7131 C  C     . GLY B 459 ? 0.35870 0.34170 0.33240 0.00660  -0.01960 0.07230  455 GLY B C     
7132 O  O     . GLY B 459 ? 0.34880 0.33150 0.32950 0.00760  -0.02110 0.07880  455 GLY B O     
7133 N  N     . MET B 460 ? 0.35370 0.33250 0.32580 0.00570  -0.01580 0.06870  456 MET B N     
7134 C  CA    . MET B 460 ? 0.38860 0.36130 0.36720 0.00580  -0.01340 0.07160  456 MET B CA    
7135 C  C     . MET B 460 ? 0.35390 0.32160 0.34340 0.00830  -0.01300 0.07180  456 MET B C     
7136 O  O     . MET B 460 ? 0.39080 0.35360 0.38740 0.00890  -0.01200 0.07580  456 MET B O     
7137 C  CB    . MET B 460 ? 0.42820 0.39710 0.40400 0.00430  -0.00970 0.06660  456 MET B CB    
7138 C  CG    . MET B 460 ? 0.54600 0.51980 0.51260 0.00220  -0.00930 0.06680  456 MET B CG    
7139 S  SD    . MET B 460 ? 0.58660 0.56350 0.55280 0.00070  -0.01040 0.07650  456 MET B SD    
7140 C  CE    . MET B 460 ? 0.45530 0.42310 0.43070 0.00010  -0.00760 0.07810  456 MET B CE    
7141 N  N     . GLU B 461 ? 0.32570 0.29440 0.31700 0.00970  -0.01360 0.06770  457 GLU B N     
7142 C  CA    . GLU B 461 ? 0.36770 0.33250 0.36960 0.01220  -0.01260 0.06740  457 GLU B CA    
7143 C  C     . GLU B 461 ? 0.38700 0.35320 0.39690 0.01410  -0.01510 0.07520  457 GLU B C     
7144 O  O     . GLU B 461 ? 0.36400 0.32610 0.38390 0.01670  -0.01360 0.07560  457 GLU B O     
7145 C  CB    . GLU B 461 ? 0.41250 0.37950 0.41460 0.01310  -0.01270 0.06210  457 GLU B CB    
7146 C  CG    . GLU B 461 ? 0.45050 0.41530 0.44670 0.01160  -0.01000 0.05460  457 GLU B CG    
7147 C  CD    . GLU B 461 ? 0.46270 0.42030 0.46210 0.01160  -0.00580 0.05160  457 GLU B CD    
7148 O  OE1   . GLU B 461 ? 0.43270 0.38900 0.42680 0.01000  -0.00390 0.04650  457 GLU B OE1   
7149 O  OE2   . GLU B 461 ? 0.40630 0.35930 0.41360 0.01320  -0.00440 0.05400  457 GLU B OE2   
7150 N  N     . ILE B 462 ? 0.36790 0.34010 0.37390 0.01310  -0.01890 0.08130  458 ILE B N     
7151 C  CA    . ILE B 462 ? 0.36620 0.33960 0.38060 0.01490  -0.02140 0.08960  458 ILE B CA    
7152 C  C     . ILE B 462 ? 0.32860 0.29420 0.35010 0.01560  -0.01870 0.09290  458 ILE B C     
7153 O  O     . ILE B 462 ? 0.35550 0.31910 0.38760 0.01800  -0.01950 0.09850  458 ILE B O     
7154 C  CB    . ILE B 462 ? 0.39890 0.38080 0.40680 0.01320  -0.02620 0.09610  458 ILE B CB    
7155 C  CG1   . ILE B 462 ? 0.38960 0.37170 0.38880 0.01040  -0.02520 0.09810  458 ILE B CG1   
7156 C  CG2   . ILE B 462 ? 0.28280 0.27160 0.28410 0.01230  -0.02910 0.09230  458 ILE B CG2   
7157 C  CD1   . ILE B 462 ? 0.46920 0.45960 0.46250 0.00880  -0.02950 0.10560  458 ILE B CD1   
7158 N  N     . HIS B 463 ? 0.33810 0.29900 0.35470 0.01350  -0.01560 0.08940  459 HIS B N     
7159 C  CA    . HIS B 463 ? 0.43640 0.38870 0.46040 0.01390  -0.01290 0.09130  459 HIS B CA    
7160 C  C     . HIS B 463 ? 0.35450 0.30000 0.38820 0.01690  -0.01000 0.08670  459 HIS B C     
7161 O  O     . HIS B 463 ? 0.36130 0.30070 0.40520 0.01890  -0.00910 0.09010  459 HIS B O     
7162 C  CB    . HIS B 463 ? 0.38540 0.33460 0.40230 0.01060  -0.01030 0.08810  459 HIS B CB    
7163 C  CG    . HIS B 463 ? 0.40940 0.34990 0.43340 0.01020  -0.00810 0.09040  459 HIS B CG    
7164 N  ND1   . HIS B 463 ? 0.36810 0.30030 0.39480 0.01000  -0.00440 0.08370  459 HIS B ND1   
7165 C  CD2   . HIS B 463 ? 0.41430 0.35250 0.44380 0.00990  -0.00930 0.09880  459 HIS B CD2   
7166 C  CE1   . HIS B 463 ? 0.39860 0.32350 0.43190 0.00940  -0.00340 0.08730  459 HIS B CE1   
7167 N  NE2   . HIS B 463 ? 0.38540 0.31350 0.42100 0.00940  -0.00630 0.09670  459 HIS B NE2   
7168 N  N     . THR B 464 ? 0.38720 0.33390 0.41810 0.01730  -0.00860 0.07910  460 THR B N     
7169 C  CA    . THR B 464 ? 0.43630 0.37830 0.47570 0.02020  -0.00560 0.07460  460 THR B CA    
7170 C  C     . THR B 464 ? 0.34690 0.29130 0.39700 0.02390  -0.00770 0.08030  460 THR B C     
7171 O  O     . THR B 464 ? 0.32600 0.26450 0.38690 0.02680  -0.00530 0.08090  460 THR B O     
7172 C  CB    . THR B 464 ? 0.38660 0.33120 0.42010 0.01960  -0.00430 0.06670  460 THR B CB    
7173 O  OG1   . THR B 464 ? 0.46030 0.40300 0.48450 0.01630  -0.00270 0.06210  460 THR B OG1   
7174 C  CG2   . THR B 464 ? 0.32760 0.26820 0.36900 0.02240  -0.00070 0.06180  460 THR B CG2   
7175 N  N     . ALA B 465 ? 0.35000 0.30330 0.39780 0.02370  -0.01210 0.08490  461 ALA B N     
7176 C  CA    . ALA B 465 ? 0.37620 0.33320 0.43470 0.02690  -0.01470 0.09140  461 ALA B CA    
7177 C  C     . ALA B 465 ? 0.39980 0.35230 0.46640 0.02820  -0.01530 0.09940  461 ALA B C     
7178 O  O     . ALA B 465 ? 0.35970 0.30980 0.43920 0.03200  -0.01470 0.10270  461 ALA B O     
7179 C  CB    . ALA B 465 ? 0.32890 0.29650 0.38200 0.02550  -0.02000 0.09490  461 ALA B CB    
7180 N  N     . ALA B 466 ? 0.46070 0.41220 0.52050 0.02520  -0.01630 0.10290  462 ALA B N     
7181 C  CA    . ALA B 466 ? 0.44540 0.39200 0.51290 0.02590  -0.01680 0.11100  462 ALA B CA    
7182 C  C     . ALA B 466 ? 0.40430 0.33900 0.48090 0.02790  -0.01200 0.10700  462 ALA B C     
7183 O  O     . ALA B 466 ? 0.35900 0.28910 0.44840 0.03120  -0.01170 0.11190  462 ALA B O     
7184 C  CB    . ALA B 466 ? 0.37320 0.32170 0.43090 0.02180  -0.01840 0.11510  462 ALA B CB    
7185 N  N     . GLU B 467 ? 0.33750 0.26710 0.40780 0.02600  -0.00810 0.09790  463 GLU B N     
7186 C  CA    . GLU B 467 ? 0.36070 0.27890 0.43770 0.02720  -0.00360 0.09310  463 GLU B CA    
7187 C  C     . GLU B 467 ? 0.35150 0.26710 0.44100 0.03230  -0.00150 0.09140  463 GLU B C     
7188 O  O     . GLU B 467 ? 0.36370 0.27070 0.46410 0.03480  0.00060  0.09280  463 GLU B O     
7189 C  CB    . GLU B 467 ? 0.36350 0.27900 0.43070 0.02410  -0.00030 0.08320  463 GLU B CB    
7190 C  CG    . GLU B 467 ? 0.37670 0.29220 0.43460 0.01950  -0.00110 0.08450  463 GLU B CG    
7191 C  CD    . GLU B 467 ? 0.47870 0.38430 0.54270 0.01850  0.00030  0.08720  463 GLU B CD    
7192 O  OE1   . GLU B 467 ? 0.57210 0.47880 0.63810 0.01740  -0.00230 0.09610  463 GLU B OE1   
7193 O  OE2   . GLU B 467 ? 0.48440 0.38120 0.55140 0.01850  0.00390  0.08040  463 GLU B OE2   
7194 N  N     . TYR B 468 ? 0.32320 0.24620 0.41180 0.03390  -0.00190 0.08850  464 TYR B N     
7195 C  CA    . TYR B 468 ? 0.39160 0.31340 0.49200 0.03870  0.00060  0.08630  464 TYR B CA    
7196 C  C     . TYR B 468 ? 0.42780 0.35660 0.53840 0.04210  -0.00320 0.09540  464 TYR B C     
7197 O  O     . TYR B 468 ? 0.36840 0.29820 0.48970 0.04640  -0.00140 0.09450  464 TYR B O     
7198 C  CB    . TYR B 468 ? 0.32960 0.25500 0.42450 0.03840  0.00320  0.07730  464 TYR B CB    
7199 C  CG    . TYR B 468 ? 0.41590 0.33400 0.50320 0.03580  0.00740  0.06820  464 TYR B CG    
7200 C  CD1   . TYR B 468 ? 0.40800 0.31730 0.50150 0.03810  0.01260  0.06220  464 TYR B CD1   
7201 C  CD2   . TYR B 468 ? 0.33340 0.25340 0.40730 0.03120  0.00620  0.06570  464 TYR B CD2   
7202 C  CE1   . TYR B 468 ? 0.38450 0.28760 0.47040 0.03520  0.01600  0.05390  464 TYR B CE1   
7203 C  CE2   . TYR B 468 ? 0.38310 0.29710 0.45050 0.02860  0.00960  0.05800  464 TYR B CE2   
7204 C  CZ    . TYR B 468 ? 0.30170 0.20750 0.37480 0.03040  0.01430  0.05230  464 TYR B CZ    
7205 O  OH    . TYR B 468 ? 0.34580 0.24620 0.41180 0.02730  0.01720  0.04470  464 TYR B OH    
7206 N  N     . LYS B 469 ? 0.40990 0.34410 0.51790 0.04030  -0.00840 0.10440  465 LYS B N     
7207 C  CA    . LYS B 469 ? 0.42950 0.37110 0.54690 0.04310  -0.01290 0.11400  465 LYS B CA    
7208 C  C     . LYS B 469 ? 0.37960 0.33100 0.49760 0.04430  -0.01420 0.11180  465 LYS B C     
7209 O  O     . LYS B 469 ? 0.42510 0.37950 0.55600 0.04850  -0.01440 0.11490  465 LYS B O     
7210 C  CB    . LYS B 469 ? 0.39900 0.33330 0.53350 0.04800  -0.01100 0.11860  465 LYS B CB    
7211 C  CG    . LYS B 469 ? 0.58240 0.50440 0.71840 0.04700  -0.00850 0.11910  465 LYS B CG    
7212 C  CD    . LYS B 469 ? 0.67650 0.59160 0.83060 0.05220  -0.00760 0.12510  465 LYS B CD    
7213 C  CE    . LYS B 469 ? 0.74980 0.65010 0.90720 0.05180  -0.00340 0.12170  465 LYS B CE    
7214 N  NZ    . LYS B 469 ? 0.84390 0.73600 1.01980 0.05770  -0.00100 0.12430  465 LYS B NZ    
7215 N  N     . ILE B 470 ? 0.33900 0.29570 0.44360 0.04050  -0.01530 0.10660  466 ILE B N     
7216 C  CA    . ILE B 470 ? 0.38910 0.35460 0.49300 0.04080  -0.01670 0.10380  466 ILE B CA    
7217 C  C     . ILE B 470 ? 0.39130 0.36740 0.49080 0.03860  -0.02370 0.11120  466 ILE B C     
7218 O  O     . ILE B 470 ? 0.40440 0.38240 0.49050 0.03440  -0.02590 0.11080  466 ILE B O     
7219 C  CB    . ILE B 470 ? 0.37430 0.33850 0.46690 0.03800  -0.01360 0.09350  466 ILE B CB    
7220 C  CG1   . ILE B 470 ? 0.36500 0.31950 0.46130 0.03980  -0.00690 0.08610  466 ILE B CG1   
7221 C  CG2   . ILE B 470 ? 0.33430 0.30750 0.42570 0.03760  -0.01550 0.09110  466 ILE B CG2   
7222 C  CD1   . ILE B 470 ? 0.38910 0.34110 0.47290 0.03640  -0.00400 0.07670  466 ILE B CD1   
7223 N  N     . PRO B 471 ? 0.40100 0.38420 0.51120 0.04110  -0.02730 0.11830  467 PRO B N     
7224 C  CA    . PRO B 471 ? 0.41520 0.40840 0.52060 0.03860  -0.03450 0.12600  467 PRO B CA    
7225 C  C     . PRO B 471 ? 0.39800 0.39940 0.49350 0.03530  -0.03740 0.12140  467 PRO B C     
7226 O  O     . PRO B 471 ? 0.44300 0.45090 0.54520 0.03650  -0.03900 0.12150  467 PRO B O     
7227 C  CB    . PRO B 471 ? 0.41630 0.41410 0.53840 0.04280  -0.03720 0.13530  467 PRO B CB    
7228 C  CG    . PRO B 471 ? 0.35590 0.34530 0.49160 0.04780  -0.03100 0.13220  467 PRO B CG    
7229 C  CD    . PRO B 471 ? 0.30260 0.28490 0.43020 0.04650  -0.02510 0.12040  467 PRO B CD    
7230 N  N     . VAL B 472 ? 0.44100 0.44210 0.52070 0.03100  -0.03820 0.11780  468 VAL B N     
7231 C  CA    . VAL B 472 ? 0.40660 0.41450 0.47550 0.02740  -0.04130 0.11360  468 VAL B CA    
7232 C  C     . VAL B 472 ? 0.40310 0.41650 0.46130 0.02400  -0.04660 0.11890  468 VAL B C     
7233 O  O     . VAL B 472 ? 0.30430 0.31440 0.35950 0.02360  -0.04600 0.12300  468 VAL B O     
7234 C  CB    . VAL B 472 ? 0.39730 0.39970 0.45680 0.02560  -0.03680 0.10290  468 VAL B CB    
7235 C  CG1   . VAL B 472 ? 0.32520 0.33340 0.37200 0.02160  -0.04030 0.09910  468 VAL B CG1   
7236 C  CG2   . VAL B 472 ? 0.31750 0.31640 0.38640 0.02850  -0.03210 0.09760  468 VAL B CG2   
7237 N  N     . THR B 473 ? 0.33830 0.36050 0.39090 0.02140  -0.05180 0.11920  469 THR B N     
7238 C  CA    . THR B 473 ? 0.36660 0.39480 0.40690 0.01770  -0.05660 0.12280  469 THR B CA    
7239 C  C     . THR B 473 ? 0.43240 0.46110 0.45800 0.01410  -0.05650 0.11370  469 THR B C     
7240 O  O     . THR B 473 ? 0.37700 0.40870 0.40290 0.01320  -0.05800 0.10910  469 THR B O     
7241 C  CB    . THR B 473 ? 0.40620 0.44470 0.45150 0.01730  -0.06370 0.13130  469 THR B CB    
7242 O  OG1   . THR B 473 ? 0.41000 0.44750 0.46960 0.02110  -0.06360 0.14020  469 THR B OG1   
7243 C  CG2   . THR B 473 ? 0.35010 0.39530 0.38090 0.01310  -0.06870 0.13440  469 THR B CG2   
7244 N  N     . TRP B 474 ? 0.29600 0.32150 0.30970 0.01210  -0.05440 0.11140  470 TRP B N     
7245 C  CA    . TRP B 474 ? 0.31610 0.34240 0.31530 0.00890  -0.05440 0.10370  470 TRP B CA    
7246 C  C     . TRP B 474 ? 0.36890 0.40380 0.35750 0.00570  -0.06000 0.10760  470 TRP B C     
7247 O  O     . TRP B 474 ? 0.39340 0.43060 0.37990 0.00530  -0.06130 0.11480  470 TRP B O     
7248 C  CB    . TRP B 474 ? 0.30760 0.32640 0.30010 0.00870  -0.04870 0.09870  470 TRP B CB    
7249 C  CG    . TRP B 474 ? 0.34540 0.35630 0.34530 0.01100  -0.04330 0.09310  470 TRP B CG    
7250 C  CD1   . TRP B 474 ? 0.34030 0.34830 0.33730 0.01050  -0.04100 0.08440  470 TRP B CD1   
7251 C  CD2   . TRP B 474 ? 0.31250 0.31700 0.32350 0.01390  -0.03960 0.09560  470 TRP B CD2   
7252 N  NE1   . TRP B 474 ? 0.38750 0.38860 0.39250 0.01280  -0.03610 0.08170  470 TRP B NE1   
7253 C  CE2   . TRP B 474 ? 0.36790 0.36660 0.38140 0.01500  -0.03510 0.08800  470 TRP B CE2   
7254 C  CE3   . TRP B 474 ? 0.35640 0.35930 0.37530 0.01580  -0.03970 0.10370  470 TRP B CE3   
7255 C  CZ2   . TRP B 474 ? 0.34770 0.33920 0.37060 0.01770  -0.03060 0.08740  470 TRP B CZ2   
7256 C  CZ3   . TRP B 474 ? 0.33840 0.33340 0.36780 0.01860  -0.03520 0.10300  470 TRP B CZ3   
7257 C  CH2   . TRP B 474 ? 0.36630 0.35570 0.39690 0.01950  -0.03070 0.09450  470 TRP B CH2   
7258 N  N     . ILE B 475 ? 0.35220 0.39150 0.33400 0.00320  -0.06340 0.10260  471 ILE B N     
7259 C  CA    . ILE B 475 ? 0.36150 0.40840 0.33070 -0.00040 -0.06840 0.10370  471 ILE B CA    
7260 C  C     . ILE B 475 ? 0.44130 0.48490 0.39690 -0.00230 -0.06550 0.09400  471 ILE B C     
7261 O  O     . ILE B 475 ? 0.38930 0.43020 0.34420 -0.00280 -0.06480 0.08620  471 ILE B O     
7262 C  CB    . ILE B 475 ? 0.35620 0.41090 0.32840 -0.00200 -0.07510 0.10540  471 ILE B CB    
7263 C  CG1   . ILE B 475 ? 0.32840 0.38650 0.31610 0.00050  -0.07760 0.11520  471 ILE B CG1   
7264 C  CG2   . ILE B 475 ? 0.39290 0.45540 0.35040 -0.00620 -0.08050 0.10550  471 ILE B CG2   
7265 C  CD1   . ILE B 475 ? 0.36750 0.43170 0.36300 -0.00020 -0.08270 0.11580  471 ILE B CD1   
7266 N  N     . VAL B 476 ? 0.41740 0.46130 0.36290 -0.00330 -0.06340 0.09490  472 VAL B N     
7267 C  CA    . VAL B 476 ? 0.35220 0.39310 0.28560 -0.00450 -0.05990 0.08630  472 VAL B CA    
7268 C  C     . VAL B 476 ? 0.43740 0.48550 0.35690 -0.00790 -0.06420 0.08410  472 VAL B C     
7269 O  O     . VAL B 476 ? 0.33110 0.38590 0.24430 -0.00950 -0.06680 0.09040  472 VAL B O     
7270 C  CB    . VAL B 476 ? 0.42940 0.46670 0.36050 -0.00360 -0.05460 0.08800  472 VAL B CB    
7271 C  CG1   . VAL B 476 ? 0.45430 0.48910 0.37460 -0.00440 -0.05070 0.07910  472 VAL B CG1   
7272 C  CG2   . VAL B 476 ? 0.36800 0.39790 0.31270 -0.00060 -0.05080 0.09030  472 VAL B CG2   
7273 N  N     . LEU B 477 ? 0.37390 0.42060 0.28850 -0.00920 -0.06490 0.07520  473 LEU B N     
7274 C  CA    . LEU B 477 ? 0.34600 0.39780 0.24620 -0.01240 -0.06810 0.07080  473 LEU B CA    
7275 C  C     . LEU B 477 ? 0.40740 0.45740 0.29660 -0.01230 -0.06290 0.06670  473 LEU B C     
7276 O  O     . LEU B 477 ? 0.42880 0.47300 0.31560 -0.01140 -0.05890 0.05830  473 LEU B O     
7277 C  CB    . LEU B 477 ? 0.35630 0.40590 0.25640 -0.01380 -0.07060 0.06250  473 LEU B CB    
7278 C  CG    . LEU B 477 ? 0.41200 0.46440 0.32390 -0.01410 -0.07570 0.06690  473 LEU B CG    
7279 C  CD1   . LEU B 477 ? 0.38790 0.43790 0.30000 -0.01590 -0.07790 0.05890  473 LEU B CD1   
7280 C  CD2   . LEU B 477 ? 0.34630 0.40860 0.25540 -0.01630 -0.08210 0.07520  473 LEU B CD2   
7281 N  N     . ASN B 478 ? 0.42120 0.47690 0.30420 -0.01310 -0.06290 0.07320  474 ASN B N     
7282 C  CA    . ASN B 478 ? 0.41920 0.47430 0.29360 -0.01270 -0.05740 0.07090  474 ASN B CA    
7283 C  C     . ASN B 478 ? 0.47320 0.53320 0.33130 -0.01520 -0.05860 0.06450  474 ASN B C     
7284 O  O     . ASN B 478 ? 0.44190 0.51020 0.29060 -0.01750 -0.06120 0.06890  474 ASN B O     
7285 C  CB    . ASN B 478 ? 0.43960 0.49790 0.31640 -0.01230 -0.05620 0.08140  474 ASN B CB    
7286 C  CG    . ASN B 478 ? 0.43900 0.49650 0.30920 -0.01190 -0.05010 0.07970  474 ASN B CG    
7287 O  OD1   . ASN B 478 ? 0.42220 0.47740 0.28560 -0.01170 -0.04680 0.07070  474 ASN B OD1   
7288 N  ND2   . ASN B 478 ? 0.40130 0.46090 0.27400 -0.01190 -0.04860 0.08870  474 ASN B ND2   
7289 N  N     . ASN B 479 ? 0.48280 0.53770 0.33750 -0.01480 -0.05650 0.05380  475 ASN B N     
7290 C  CA    . ASN B 479 ? 0.46800 0.52590 0.30780 -0.01670 -0.05660 0.04600  475 ASN B CA    
7291 C  C     . ASN B 479 ? 0.40970 0.46560 0.24340 -0.01490 -0.04940 0.04120  475 ASN B C     
7292 O  O     . ASN B 479 ? 0.45450 0.51030 0.27800 -0.01540 -0.04790 0.03240  475 ASN B O     
7293 C  CB    . ASN B 479 ? 0.42090 0.47460 0.26050 -0.01770 -0.05980 0.03710  475 ASN B CB    
7294 C  CG    . ASN B 479 ? 0.45860 0.50270 0.30920 -0.01510 -0.05640 0.03230  475 ASN B CG    
7295 O  OD1   . ASN B 479 ? 0.47290 0.51320 0.32930 -0.01250 -0.05110 0.03400  475 ASN B OD1   
7296 N  ND2   . ASN B 479 ? 0.45180 0.49210 0.30520 -0.01610 -0.05960 0.02650  475 ASN B ND2   
7297 N  N     . GLY B 480 ? 0.46340 0.51780 0.30360 -0.01300 -0.04490 0.04680  476 GLY B N     
7298 C  CA    . GLY B 480 ? 0.41850 0.47250 0.25410 -0.01160 -0.03830 0.04380  476 GLY B CA    
7299 C  C     . GLY B 480 ? 0.43610 0.48300 0.27270 -0.00960 -0.03450 0.03340  476 GLY B C     
7300 O  O     . GLY B 480 ? 0.47560 0.52400 0.30380 -0.00890 -0.03040 0.02790  476 GLY B O     
7301 N  N     . GLY B 481 ? 0.39390 0.43330 0.24100 -0.00840 -0.03540 0.03110  477 GLY B N     
7302 C  CA    . GLY B 481 ? 0.41420 0.44690 0.26360 -0.00640 -0.03180 0.02260  477 GLY B CA    
7303 C  C     . GLY B 481 ? 0.39600 0.42270 0.25170 -0.00660 -0.03530 0.01820  477 GLY B C     
7304 O  O     . GLY B 481 ? 0.39420 0.42110 0.25640 -0.00760 -0.03960 0.02300  477 GLY B O     
7305 N  N     . HIS B 482 ? 0.41280 0.43440 0.26750 -0.00550 -0.03330 0.00950  478 HIS B N     
7306 C  CA    . HIS B 482 ? 0.38890 0.40380 0.25080 -0.00550 -0.03560 0.00530  478 HIS B CA    
7307 C  C     . HIS B 482 ? 0.44760 0.46340 0.30220 -0.00800 -0.04050 -0.00030 478 HIS B C     
7308 O  O     . HIS B 482 ? 0.42250 0.43540 0.27110 -0.00770 -0.03930 -0.00860 478 HIS B O     
7309 C  CB    . HIS B 482 ? 0.41470 0.42320 0.28090 -0.00310 -0.03090 -0.00010 478 HIS B CB    
7310 C  CG    . HIS B 482 ? 0.41730 0.42510 0.29000 -0.00120 -0.02640 0.00470  478 HIS B CG    
7311 N  ND1   . HIS B 482 ? 0.40660 0.40920 0.29000 -0.00010 -0.02540 0.00600  478 HIS B ND1   
7312 C  CD2   . HIS B 482 ? 0.39230 0.40430 0.26220 -0.00050 -0.02280 0.00870  478 HIS B CD2   
7313 C  CE1   . HIS B 482 ? 0.38610 0.38930 0.27280 0.00110  -0.02150 0.01000  478 HIS B CE1   
7314 N  NE2   . HIS B 482 ? 0.43910 0.44780 0.31810 0.00080  -0.02000 0.01190  478 HIS B NE2   
7315 N  N     . GLY B 483 ? 0.45150 0.47120 0.30720 -0.01040 -0.04620 0.00440  479 GLY B N     
7316 C  CA    . GLY B 483 ? 0.43020 0.45190 0.27880 -0.01350 -0.05170 0.00020  479 GLY B CA    
7317 C  C     . GLY B 483 ? 0.46920 0.48350 0.31990 -0.01390 -0.05270 -0.00850 479 GLY B C     
7318 O  O     . GLY B 483 ? 0.41910 0.43220 0.26020 -0.01500 -0.05330 -0.01640 479 GLY B O     
7319 N  N     . LEU B 484 ? 0.38350 0.39270 0.24670 -0.01320 -0.05300 -0.00720 480 LEU B N     
7320 C  CA    . LEU B 484 ? 0.45230 0.45450 0.31840 -0.01390 -0.05430 -0.01450 480 LEU B CA    
7321 C  C     . LEU B 484 ? 0.48060 0.47730 0.34170 -0.01160 -0.04930 -0.02240 480 LEU B C     
7322 O  O     . LEU B 484 ? 0.48310 0.47540 0.34030 -0.01280 -0.05080 -0.03030 480 LEU B O     
7323 C  CB    . LEU B 484 ? 0.42720 0.42560 0.30760 -0.01320 -0.05450 -0.01090 480 LEU B CB    
7324 C  CG    . LEU B 484 ? 0.51940 0.52220 0.40660 -0.01560 -0.06000 -0.00480 480 LEU B CG    
7325 C  CD1   . LEU B 484 ? 0.53010 0.52890 0.43080 -0.01500 -0.05970 -0.00300 480 LEU B CD1   
7326 C  CD2   . LEU B 484 ? 0.45180 0.45750 0.33210 -0.01970 -0.06660 -0.00820 480 LEU B CD2   
7327 N  N     . VAL B 485 ? 0.44190 0.43900 0.30340 -0.00850 -0.04340 -0.02050 481 VAL B N     
7328 C  CA    . VAL B 485 ? 0.42750 0.42040 0.28500 -0.00600 -0.03850 -0.02750 481 VAL B CA    
7329 C  C     . VAL B 485 ? 0.50670 0.50330 0.35020 -0.00680 -0.03850 -0.03300 481 VAL B C     
7330 O  O     . VAL B 485 ? 0.47110 0.46320 0.31000 -0.00630 -0.03740 -0.04170 481 VAL B O     
7331 C  CB    . VAL B 485 ? 0.44380 0.43710 0.30620 -0.00280 -0.03250 -0.02360 481 VAL B CB    
7332 C  CG1   . VAL B 485 ? 0.42450 0.41410 0.28410 -0.00000 -0.02760 -0.03050 481 VAL B CG1   
7333 C  CG2   . VAL B 485 ? 0.41350 0.40320 0.28880 -0.00220 -0.03260 -0.01880 481 VAL B CG2   
7334 N  N     . HIS B 486 ? 0.45500 0.45990 0.29150 -0.00820 -0.03960 -0.02780 482 HIS B N     
7335 C  CA    . HIS B 486 ? 0.51780 0.52760 0.33970 -0.00950 -0.03990 -0.03240 482 HIS B CA    
7336 C  C     . HIS B 486 ? 0.53150 0.53790 0.34820 -0.01240 -0.04490 -0.04040 482 HIS B C     
7337 O  O     . HIS B 486 ? 0.49700 0.50180 0.30410 -0.01210 -0.04330 -0.04930 482 HIS B O     
7338 C  CB    . HIS B 486 ? 0.48120 0.50090 0.29770 -0.01130 -0.04180 -0.02400 482 HIS B CB    
7339 C  CG    . HIS B 486 ? 0.62760 0.65380 0.42820 -0.01290 -0.04180 -0.02770 482 HIS B CG    
7340 N  ND1   . HIS B 486 ? 0.66880 0.69820 0.46190 -0.01060 -0.03550 -0.03000 482 HIS B ND1   
7341 C  CD2   . HIS B 486 ? 0.63820 0.66930 0.42870 -0.01670 -0.04730 -0.02920 482 HIS B CD2   
7342 C  CE1   . HIS B 486 ? 0.64850 0.68430 0.42710 -0.01280 -0.03680 -0.03300 482 HIS B CE1   
7343 N  NE2   . HIS B 486 ? 0.65460 0.69140 0.43100 -0.01660 -0.04410 -0.03260 482 HIS B NE2   
7344 N  N     . LEU B 487 ? 0.52700 0.53250 0.35010 -0.01530 -0.05110 -0.03750 483 LEU B N     
7345 C  CA    . LEU B 487 ? 0.54470 0.54690 0.36360 -0.01860 -0.05650 -0.04480 483 LEU B CA    
7346 C  C     . LEU B 487 ? 0.56010 0.55160 0.38310 -0.01690 -0.05410 -0.05370 483 LEU B C     
7347 O  O     . LEU B 487 ? 0.59360 0.58120 0.40920 -0.01840 -0.05570 -0.06290 483 LEU B O     
7348 C  CB    . LEU B 487 ? 0.49270 0.49700 0.31910 -0.02210 -0.06350 -0.03880 483 LEU B CB    
7349 C  CG    . LEU B 487 ? 0.53450 0.54950 0.35720 -0.02410 -0.06690 -0.03000 483 LEU B CG    
7350 C  CD1   . LEU B 487 ? 0.50850 0.52530 0.34390 -0.02560 -0.07170 -0.02190 483 LEU B CD1   
7351 C  CD2   . LEU B 487 ? 0.53120 0.55160 0.33850 -0.02780 -0.07110 -0.03450 483 LEU B CD2   
7352 N  N     . GLY B 488 ? 0.48750 0.47400 0.32230 -0.01390 -0.05050 -0.05100 484 GLY B N     
7353 C  CA    . GLY B 488 ? 0.55060 0.52750 0.39010 -0.01190 -0.04790 -0.05830 484 GLY B CA    
7354 C  C     . GLY B 488 ? 0.58300 0.55830 0.41310 -0.00910 -0.04270 -0.06640 484 GLY B C     
7355 O  O     . GLY B 488 ? 0.60760 0.57540 0.43610 -0.00880 -0.04260 -0.07540 484 GLY B O     
7356 N  N     . GLU B 489 ? 0.51890 0.50110 0.34350 -0.00680 -0.03800 -0.06310 485 GLU B N     
7357 C  CA    . GLU B 489 ? 0.53450 0.51690 0.34990 -0.00400 -0.03260 -0.07040 485 GLU B CA    
7358 C  C     . GLU B 489 ? 0.57450 0.55720 0.37650 -0.00670 -0.03550 -0.07910 485 GLU B C     
7359 O  O     . GLU B 489 ? 0.57600 0.55360 0.37330 -0.00490 -0.03260 -0.08890 485 GLU B O     
7360 C  CB    . GLU B 489 ? 0.46490 0.45640 0.27650 -0.00200 -0.02760 -0.06430 485 GLU B CB    
7361 C  CG    . GLU B 489 ? 0.51900 0.51000 0.34260 0.00090  -0.02370 -0.05710 485 GLU B CG    
7362 C  CD    . GLU B 489 ? 0.66610 0.66650 0.48740 0.00110  -0.02140 -0.04840 485 GLU B CD    
7363 O  OE1   . GLU B 489 ? 0.72070 0.72120 0.55070 0.00310  -0.01820 -0.04280 485 GLU B OE1   
7364 O  OE2   . GLU B 489 ? 0.74880 0.75640 0.55940 -0.00110 -0.02300 -0.04710 485 GLU B OE2   
7365 N  N     . GLN B 490 ? 0.54770 0.53660 0.34340 -0.01110 -0.04140 -0.07570 486 GLN B N     
7366 C  CA    . GLN B 490 ? 0.62580 0.61600 0.40760 -0.01450 -0.04490 -0.08370 486 GLN B CA    
7367 C  C     . GLN B 490 ? 0.62920 0.60910 0.41430 -0.01680 -0.04950 -0.09180 486 GLN B C     
7368 O  O     . GLN B 490 ? 0.62790 0.60350 0.40410 -0.01730 -0.04920 -0.10270 486 GLN B O     
7369 C  CB    . GLN B 490 ? 0.56870 0.56910 0.34370 -0.01880 -0.05050 -0.07660 486 GLN B CB    
7370 C  CG    . GLN B 490 ? 0.70430 0.71490 0.47610 -0.01730 -0.04700 -0.06760 486 GLN B CG    
7371 C  CD    . GLN B 490 ? 0.84970 0.86990 0.61650 -0.02170 -0.05320 -0.05970 486 GLN B CD    
7372 O  OE1   . GLN B 490 ? 0.85000 0.86940 0.62360 -0.02470 -0.05980 -0.05620 486 GLN B OE1   
7373 N  NE2   . GLN B 490 ? 0.90710 0.93710 0.66240 -0.02200 -0.05130 -0.05660 486 GLN B NE2   
7374 N  N     . HIS B 491 ? 0.58440 0.56060 0.38230 -0.01850 -0.05380 -0.08670 487 HIS B N     
7375 C  CA    . HIS B 491 ? 0.63210 0.60010 0.43350 -0.02190 -0.05940 -0.09270 487 HIS B CA    
7376 C  C     . HIS B 491 ? 0.68760 0.64370 0.49850 -0.01880 -0.05600 -0.09840 487 HIS B C     
7377 O  O     . HIS B 491 ? 0.73250 0.68030 0.54420 -0.02110 -0.05950 -0.10590 487 HIS B O     
7378 C  CB    . HIS B 491 ? 0.59470 0.56600 0.40510 -0.02580 -0.06610 -0.08400 487 HIS B CB    
7379 C  CG    . HIS B 491 ? 0.76670 0.74770 0.56740 -0.03030 -0.07190 -0.08110 487 HIS B CG    
7380 N  ND1   . HIS B 491 ? 0.76100 0.75270 0.55820 -0.02970 -0.07110 -0.07220 487 HIS B ND1   
7381 C  CD2   . HIS B 491 ? 0.77060 0.75240 0.56420 -0.03570 -0.07900 -0.08580 487 HIS B CD2   
7382 C  CE1   . HIS B 491 ? 0.80440 0.80340 0.59310 -0.03440 -0.07730 -0.07100 487 HIS B CE1   
7383 N  NE2   . HIS B 491 ? 0.77810 0.77160 0.56420 -0.03820 -0.08230 -0.07920 487 HIS B NE2   
7384 N  N     . GLN B 492 ? 0.60530 0.56030 0.42370 -0.01380 -0.04960 -0.09480 488 GLN B N     
7385 C  CA    . GLN B 492 ? 0.62470 0.56910 0.45240 -0.01070 -0.04660 -0.09930 488 GLN B CA    
7386 C  C     . GLN B 492 ? 0.62720 0.57010 0.45160 -0.00520 -0.03880 -0.10440 488 GLN B C     
7387 O  O     . GLN B 492 ? 0.72650 0.65990 0.55660 -0.00260 -0.03650 -0.11040 488 GLN B O     
7388 C  CB    . GLN B 492 ? 0.59410 0.53700 0.43730 -0.00980 -0.04660 -0.09030 488 GLN B CB    
7389 C  CG    . GLN B 492 ? 0.63750 0.58290 0.48580 -0.01460 -0.05350 -0.08430 488 GLN B CG    
7390 C  CD    . GLN B 492 ? 0.79440 0.73710 0.65760 -0.01370 -0.05310 -0.07720 488 GLN B CD    
7391 O  OE1   . GLN B 492 ? 0.82010 0.76920 0.68770 -0.01350 -0.05280 -0.06830 488 GLN B OE1   
7392 N  NE2   . GLN B 492 ? 0.85200 0.78500 0.72300 -0.01310 -0.05290 -0.08110 488 GLN B NE2   
7393 N  N     . PHE B 493 ? 0.59580 0.54790 0.41170 -0.00330 -0.03460 -0.10210 489 PHE B N     
7394 C  CA    . PHE B 493 ? 0.61270 0.56490 0.42620 0.00200  -0.02690 -0.10630 489 PHE B CA    
7395 C  C     . PHE B 493 ? 0.64940 0.60830 0.44630 0.00180  -0.02460 -0.11210 489 PHE B C     
7396 O  O     . PHE B 493 ? 0.64250 0.60550 0.43610 0.00590  -0.01780 -0.11320 489 PHE B O     
7397 C  CB    . PHE B 493 ? 0.58930 0.54660 0.41120 0.00530  -0.02230 -0.09680 489 PHE B CB    
7398 C  CG    . PHE B 493 ? 0.60940 0.56030 0.44680 0.00610  -0.02330 -0.09200 489 PHE B CG    
7399 C  CD1   . PHE B 493 ? 0.55590 0.50830 0.39990 0.00290  -0.02800 -0.08380 489 PHE B CD1   
7400 C  CD2   . PHE B 493 ? 0.57650 0.52020 0.42200 0.01020  -0.01930 -0.09550 489 PHE B CD2   
7401 C  CE1   . PHE B 493 ? 0.56100 0.50820 0.41850 0.00350  -0.02860 -0.07960 489 PHE B CE1   
7402 C  CE2   . PHE B 493 ? 0.59890 0.53740 0.45810 0.01060  -0.02030 -0.09060 489 PHE B CE2   
7403 C  CZ    . PHE B 493 ? 0.57600 0.51630 0.44060 0.00720  -0.02490 -0.08290 489 PHE B CZ    
7404 N  N     . ASP B 494 ? 0.62630 0.58680 0.41280 -0.00300 -0.03030 -0.11570 490 ASP B N     
7405 C  CA    . ASP B 494 ? 0.70170 0.66770 0.47090 -0.00380 -0.02880 -0.12290 490 ASP B CA    
7406 C  C     . ASP B 494 ? 0.68840 0.66680 0.45110 -0.00180 -0.02360 -0.11640 490 ASP B C     
7407 O  O     . ASP B 494 ? 0.63290 0.61520 0.38470 0.00030  -0.01840 -0.12250 490 ASP B O     
7408 C  CB    . ASP B 494 ? 0.84900 0.80610 0.61470 -0.00070 -0.02470 -0.13640 490 ASP B CB    
7409 C  CG    . ASP B 494 ? 1.01170 0.95720 0.77950 -0.00410 -0.03080 -0.14430 490 ASP B CG    
7410 O  OD1   . ASP B 494 ? 1.03630 0.98290 0.79200 -0.00880 -0.03570 -0.15000 490 ASP B OD1   
7411 O  OD2   . ASP B 494 ? 1.06750 1.00290 0.84900 -0.00220 -0.03080 -0.14470 490 ASP B OD2   
7412 N  N     . SER B 495 ? 0.67020 0.65500 0.43950 -0.00270 -0.02500 -0.10410 491 SER B N     
7413 C  CA    . SER B 495 ? 0.67040 0.66660 0.43480 -0.00140 -0.02080 -0.09660 491 SER B CA    
7414 C  C     . SER B 495 ? 0.66260 0.65950 0.42780 0.00420  -0.01180 -0.10000 491 SER B C     
7415 O  O     . SER B 495 ? 0.63270 0.63910 0.38910 0.00520  -0.00730 -0.09830 491 SER B O     
7416 C  CB    . SER B 495 ? 0.62910 0.63490 0.37680 -0.00530 -0.02350 -0.09710 491 SER B CB    
7417 O  OG    . SER B 495 ? 0.63440 0.63820 0.37970 -0.01050 -0.03200 -0.09800 491 SER B OG    
7418 N  N     . LYS B 496 ? 0.63670 0.62410 0.41300 0.00780  -0.00920 -0.10400 492 LYS B N     
7419 C  CA    . LYS B 496 ? 0.62790 0.61570 0.40670 0.01340  -0.00080 -0.10710 492 LYS B CA    
7420 C  C     . LYS B 496 ? 0.61760 0.61360 0.40270 0.01530  0.00320  -0.09630 492 LYS B C     
7421 O  O     . LYS B 496 ? 0.60190 0.60240 0.38630 0.01920  0.01020  -0.09740 492 LYS B O     
7422 C  CB    . LYS B 496 ? 0.64690 0.62260 0.43750 0.01680  0.00030  -0.11280 492 LYS B CB    
7423 C  CG    . LYS B 496 ? 0.76940 0.73680 0.55350 0.01700  -0.00020 -0.12610 492 LYS B CG    
7424 C  CD    . LYS B 496 ? 0.78370 0.73990 0.58070 0.02140  0.00240  -0.13080 492 LYS B CD    
7425 C  CE    . LYS B 496 ? 0.69870 0.64760 0.50910 0.01910  -0.00340 -0.12480 492 LYS B CE    
7426 N  NZ    . LYS B 496 ? 0.74820 0.68950 0.57280 0.02380  0.00010  -0.12520 492 LYS B NZ    
7427 N  N     . PHE B 497 ? 0.56770 0.56540 0.35950 0.01260  -0.00100 -0.08600 493 PHE B N     
7428 C  CA    . PHE B 497 ? 0.56640 0.57060 0.36480 0.01400  0.00230  -0.07590 493 PHE B CA    
7429 C  C     . PHE B 497 ? 0.59330 0.60100 0.39340 0.00980  -0.00340 -0.06610 493 PHE B C     
7430 O  O     . PHE B 497 ? 0.51710 0.52070 0.31750 0.00660  -0.00970 -0.06660 493 PHE B O     
7431 C  CB    . PHE B 497 ? 0.48410 0.48230 0.29730 0.01760  0.00530  -0.07470 493 PHE B CB    
7432 C  CG    . PHE B 497 ? 0.47570 0.46390 0.29860 0.01630  -0.00000 -0.07490 493 PHE B CG    
7433 C  CD1   . PHE B 497 ? 0.46650 0.45500 0.29640 0.01360  -0.00410 -0.06610 493 PHE B CD1   
7434 C  CD2   . PHE B 497 ? 0.45940 0.43810 0.28460 0.01760  -0.00060 -0.08380 493 PHE B CD2   
7435 C  CE1   . PHE B 497 ? 0.51740 0.49780 0.35630 0.01240  -0.00860 -0.06600 493 PHE B CE1   
7436 C  CE2   . PHE B 497 ? 0.51720 0.48730 0.35150 0.01610  -0.00540 -0.08330 493 PHE B CE2   
7437 C  CZ    . PHE B 497 ? 0.49390 0.46520 0.33490 0.01340  -0.00930 -0.07430 493 PHE B CZ    
7438 N  N     . ASP B 498 ? 0.53290 0.54820 0.33480 0.00990  -0.00090 -0.05700 494 ASP B N     
7439 C  CA    . ASP B 498 ? 0.53890 0.55760 0.34370 0.00670  -0.00540 -0.04700 494 ASP B CA    
7440 C  C     . ASP B 498 ? 0.55000 0.56840 0.36710 0.00840  -0.00270 -0.03930 494 ASP B C     
7441 O  O     . ASP B 498 ? 0.58990 0.61400 0.40680 0.01010  0.00250  -0.03630 494 ASP B O     
7442 C  CB    . ASP B 498 ? 0.56190 0.59100 0.35460 0.00410  -0.00610 -0.04280 494 ASP B CB    
7443 C  CG    . ASP B 498 ? 0.71100 0.74290 0.50730 0.00090  -0.01140 -0.03240 494 ASP B CG    
7444 O  OD1   . ASP B 498 ? 0.65440 0.68490 0.46190 0.00170  -0.01070 -0.02530 494 ASP B OD1   
7445 O  OD2   . ASP B 498 ? 0.76240 0.79810 0.55080 -0.00250 -0.01650 -0.03150 494 ASP B OD2   
7446 N  N     . ILE B 499 ? 0.53760 0.54980 0.36530 0.00770  -0.00630 -0.03630 495 ILE B N     
7447 C  CA    . ILE B 499 ? 0.53490 0.54650 0.37370 0.00840  -0.00490 -0.02870 495 ILE B CA    
7448 C  C     . ILE B 499 ? 0.54800 0.56010 0.39040 0.00540  -0.01010 -0.02120 495 ILE B C     
7449 O  O     . ILE B 499 ? 0.59030 0.59890 0.44300 0.00550  -0.01070 -0.01680 495 ILE B O     
7450 C  CB    . ILE B 499 ? 0.50690 0.51060 0.35610 0.01090  -0.00330 -0.03210 495 ILE B CB    
7451 C  CG1   . ILE B 499 ? 0.47950 0.48360 0.33870 0.01170  -0.00110 -0.02510 495 ILE B CG1   
7452 C  CG2   . ILE B 499 ? 0.51520 0.51130 0.36860 0.00930  -0.00870 -0.03490 495 ILE B CG2   
7453 C  CD1   . ILE B 499 ? 0.41580 0.42700 0.27350 0.01310  0.00430  -0.02200 495 ILE B CD1   
7454 N  N     . SER B 500 ? 0.52820 0.54450 0.36220 0.00270  -0.01400 -0.02010 496 SER B N     
7455 C  CA    . SER B 500 ? 0.46250 0.47910 0.30020 -0.00000 -0.01970 -0.01400 496 SER B CA    
7456 C  C     . SER B 500 ? 0.50390 0.52880 0.33690 -0.00180 -0.02090 -0.00580 496 SER B C     
7457 O  O     . SER B 500 ? 0.56600 0.59110 0.40600 -0.00290 -0.02380 0.00160  496 SER B O     
7458 C  CB    . SER B 500 ? 0.44730 0.46100 0.28150 -0.00210 -0.02520 -0.01970 496 SER B CB    
7459 O  OG    . SER B 500 ? 0.56770 0.58560 0.38830 -0.00310 -0.02540 -0.02490 496 SER B OG    
7460 N  N     . SER B 501 ? 0.44730 0.47910 0.26900 -0.00220 -0.01870 -0.00670 497 SER B N     
7461 C  CA    . SER B 501 ? 0.55630 0.59670 0.37220 -0.00440 -0.02030 0.00130  497 SER B CA    
7462 C  C     . SER B 501 ? 0.50910 0.55310 0.32850 -0.00320 -0.01530 0.00810  497 SER B C     
7463 O  O     . SER B 501 ? 0.55460 0.59900 0.37310 -0.00100 -0.00970 0.00450  497 SER B O     
7464 C  CB    . SER B 501 ? 0.54650 0.59330 0.34680 -0.00600 -0.02110 -0.00320 497 SER B CB    
7465 O  OG    . SER B 501 ? 0.67980 0.72180 0.47660 -0.00680 -0.02440 -0.01230 497 SER B OG    
7466 N  N     . PHE B 502 ? 0.40960 0.45620 0.23410 -0.00460 -0.01740 0.01810  498 PHE B N     
7467 C  CA    . PHE B 502 ? 0.46490 0.51550 0.29170 -0.00420 -0.01330 0.02530  498 PHE B CA    
7468 C  C     . PHE B 502 ? 0.47940 0.54010 0.29330 -0.00550 -0.01130 0.02690  498 PHE B C     
7469 O  O     . PHE B 502 ? 0.47570 0.54130 0.27990 -0.00760 -0.01500 0.02670  498 PHE B O     
7470 C  CB    . PHE B 502 ? 0.39750 0.44700 0.23380 -0.00530 -0.01620 0.03540  498 PHE B CB    
7471 C  CG    . PHE B 502 ? 0.43840 0.47890 0.28730 -0.00410 -0.01770 0.03430  498 PHE B CG    
7472 C  CD1   . PHE B 502 ? 0.43850 0.47290 0.29210 -0.00200 -0.01440 0.02760  498 PHE B CD1   
7473 C  CD2   . PHE B 502 ? 0.41350 0.45210 0.26980 -0.00500 -0.02210 0.04030  498 PHE B CD2   
7474 C  CE1   . PHE B 502 ? 0.43240 0.45930 0.29680 -0.00110 -0.01560 0.02690  498 PHE B CE1   
7475 C  CE2   . PHE B 502 ? 0.41870 0.44980 0.28600 -0.00380 -0.02290 0.03920  498 PHE B CE2   
7476 C  CZ    . PHE B 502 ? 0.43080 0.45610 0.30170 -0.00210 -0.01970 0.03250  498 PHE B CZ    
7477 N  N     . ARG B 503 ? 0.47120 0.53540 0.28500 -0.00440 -0.00540 0.02830  499 ARG B N     
7478 C  CA    . ARG B 503 ? 0.50990 0.58460 0.31440 -0.00580 -0.00280 0.03330  499 ARG B CA    
7479 C  C     . ARG B 503 ? 0.54320 0.62220 0.34890 -0.00870 -0.00670 0.04520  499 ARG B C     
7480 O  O     . ARG B 503 ? 0.49210 0.57970 0.28710 -0.01090 -0.00830 0.04870  499 ARG B O     
7481 C  CB    . ARG B 503 ? 0.61200 0.68780 0.42040 -0.00370 0.00440  0.03220  499 ARG B CB    
7482 C  CG    . ARG B 503 ? 0.80090 0.88710 0.60220 -0.00360 0.01080  0.03390  499 ARG B CG    
7483 C  CD    . ARG B 503 ? 0.86190 0.94560 0.67610 -0.00440 0.01100  0.04340  499 ARG B CD    
7484 N  NE    . ARG B 503 ? 0.97000 1.05930 0.78760 -0.00630 0.01330  0.05390  499 ARG B NE    
7485 C  CZ    . ARG B 503 ? 1.01420 1.10800 0.83150 -0.00920 0.01110  0.06440  499 ARG B CZ    
7486 N  NH1   . ARG B 503 ? 1.07140 1.17320 0.87750 -0.01130 0.00900  0.06810  499 ARG B NH1   
7487 N  NH2   . ARG B 503 ? 0.97240 1.06490 0.80000 -0.00990 0.01330  0.07120  499 ARG B NH2   
7488 N  N     . LYS B 504 ? 0.44050 0.51350 0.25890 -0.00860 -0.00890 0.05110  500 LYS B N     
7489 C  CA    . LYS B 504 ? 0.43970 0.51590 0.26080 -0.01090 -0.01270 0.06250  500 LYS B CA    
7490 C  C     . LYS B 504 ? 0.46000 0.52780 0.29260 -0.01040 -0.01750 0.06420  500 LYS B C     
7491 O  O     . LYS B 504 ? 0.49980 0.56000 0.34350 -0.00880 -0.01560 0.06320  500 LYS B O     
7492 C  CB    . LYS B 504 ? 0.44050 0.52020 0.26560 -0.01170 -0.00890 0.07140  500 LYS B CB    
7493 C  CG    . LYS B 504 ? 0.68140 0.76500 0.50850 -0.01410 -0.01280 0.08380  500 LYS B CG    
7494 C  CD    . LYS B 504 ? 0.82870 0.90830 0.66810 -0.01420 -0.01060 0.09160  500 LYS B CD    
7495 C  CE    . LYS B 504 ? 0.87490 0.95160 0.72310 -0.01510 -0.01560 0.10140  500 LYS B CE    
7496 N  NZ    . LYS B 504 ? 0.78030 0.84550 0.64250 -0.01320 -0.01650 0.09920  500 LYS B NZ    
7497 N  N     . SER B 505 ? 0.44760 0.51750 0.27750 -0.01190 -0.02350 0.06640  501 SER B N     
7498 C  CA    . SER B 505 ? 0.48900 0.55300 0.33000 -0.01150 -0.02820 0.06950  501 SER B CA    
7499 C  C     . SER B 505 ? 0.42680 0.48690 0.28020 -0.01090 -0.02670 0.07790  501 SER B C     
7500 O  O     . SER B 505 ? 0.46110 0.52540 0.31350 -0.01190 -0.02450 0.08500  501 SER B O     
7501 C  CB    . SER B 505 ? 0.52260 0.59270 0.35890 -0.01370 -0.03480 0.07440  501 SER B CB    
7502 O  OG    . SER B 505 ? 0.73450 0.80480 0.56340 -0.01430 -0.03760 0.06570  501 SER B OG    
7503 N  N     . ILE B 506 ? 0.45620 0.50820 0.32140 -0.00930 -0.02780 0.07690  502 ILE B N     
7504 C  CA    . ILE B 506 ? 0.40680 0.45410 0.28430 -0.00870 -0.02700 0.08420  502 ILE B CA    
7505 C  C     . ILE B 506 ? 0.43350 0.48440 0.31410 -0.00970 -0.03210 0.09430  502 ILE B C     
7506 O  O     . ILE B 506 ? 0.40950 0.46330 0.28800 -0.01020 -0.03700 0.09410  502 ILE B O     
7507 C  CB    . ILE B 506 ? 0.45910 0.49670 0.34740 -0.00660 -0.02610 0.07900  502 ILE B CB    
7508 C  CG1   . ILE B 506 ? 0.46980 0.50420 0.35630 -0.00560 -0.02080 0.07120  502 ILE B CG1   
7509 C  CG2   . ILE B 506 ? 0.36240 0.39490 0.26340 -0.00590 -0.02630 0.08630  502 ILE B CG2   
7510 C  CD1   . ILE B 506 ? 0.47280 0.49910 0.36710 -0.00390 -0.02000 0.06470  502 ILE B CD1   
7511 N  N     . ASP B 507 ? 0.40240 0.45330 0.28870 -0.01020 -0.03100 0.10340  503 ASP B N     
7512 C  CA    . ASP B 507 ? 0.34720 0.40070 0.23870 -0.01090 -0.03550 0.11420  503 ASP B CA    
7513 C  C     . ASP B 507 ? 0.41100 0.45540 0.31790 -0.00850 -0.03620 0.11540  503 ASP B C     
7514 O  O     . ASP B 507 ? 0.43440 0.47270 0.35010 -0.00790 -0.03330 0.11860  503 ASP B O     
7515 C  CB    . ASP B 507 ? 0.38440 0.44260 0.27410 -0.01270 -0.03410 0.12400  503 ASP B CB    
7516 C  CG    . ASP B 507 ? 0.45030 0.51190 0.34530 -0.01340 -0.03910 0.13590  503 ASP B CG    
7517 O  OD1   . ASP B 507 ? 0.53330 0.59230 0.43580 -0.01190 -0.04310 0.13670  503 ASP B OD1   
7518 O  OD2   . ASP B 507 ? 0.51300 0.58030 0.40500 -0.01540 -0.03900 0.14500  503 ASP B OD2   
7519 N  N     . PHE B 508 ? 0.43330 0.47670 0.34370 -0.00740 -0.04000 0.11250  504 PHE B N     
7520 C  CA    . PHE B 508 ? 0.40850 0.44360 0.33320 -0.00490 -0.03990 0.11230  504 PHE B CA    
7521 C  C     . PHE B 508 ? 0.45870 0.49290 0.39420 -0.00420 -0.04200 0.12340  504 PHE B C     
7522 O  O     . PHE B 508 ? 0.44090 0.46700 0.38850 -0.00200 -0.04010 0.12380  504 PHE B O     
7523 C  CB    . PHE B 508 ? 0.37820 0.41320 0.30400 -0.00400 -0.04290 0.10600  504 PHE B CB    
7524 C  CG    . PHE B 508 ? 0.39850 0.43160 0.31670 -0.00420 -0.04030 0.09480  504 PHE B CG    
7525 C  CD1   . PHE B 508 ? 0.37910 0.40420 0.30250 -0.00260 -0.03570 0.08870  504 PHE B CD1   
7526 C  CD2   . PHE B 508 ? 0.38370 0.42300 0.28930 -0.00600 -0.04220 0.09030  504 PHE B CD2   
7527 C  CE1   . PHE B 508 ? 0.43370 0.45720 0.35100 -0.00270 -0.03340 0.07920  504 PHE B CE1   
7528 C  CE2   . PHE B 508 ? 0.37710 0.41390 0.27660 -0.00590 -0.03970 0.08020  504 PHE B CE2   
7529 C  CZ    . PHE B 508 ? 0.40230 0.43130 0.30810 -0.00420 -0.03530 0.07500  504 PHE B CZ    
7530 N  N     . CYS B 509 ? 0.40120 0.44330 0.33250 -0.00590 -0.04540 0.13260  505 CYS B N     
7531 C  CA    . CYS B 509 ? 0.45280 0.49360 0.39540 -0.00510 -0.04740 0.14390  505 CYS B CA    
7532 C  C     . CYS B 509 ? 0.49900 0.53300 0.44710 -0.00510 -0.04270 0.14680  505 CYS B C     
7533 O  O     . CYS B 509 ? 0.49100 0.51720 0.45260 -0.00300 -0.04180 0.15000  505 CYS B O     
7534 C  CB    . CYS B 509 ? 0.49750 0.54910 0.43360 -0.00730 -0.05240 0.15370  505 CYS B CB    
7535 S  SG    . CYS B 509 ? 0.56490 0.62460 0.49760 -0.00770 -0.05940 0.15290  505 CYS B SG    
7536 N  N     . LYS B 510 ? 0.45800 0.49490 0.39610 -0.00740 -0.03940 0.14520  506 LYS B N     
7537 C  CA    . LYS B 510 ? 0.46640 0.49720 0.40950 -0.00790 -0.03490 0.14730  506 LYS B CA    
7538 C  C     . LYS B 510 ? 0.35360 0.37390 0.30380 -0.00590 -0.03110 0.13810  506 LYS B C     
7539 O  O     . LYS B 510 ? 0.40870 0.42090 0.36920 -0.00540 -0.02890 0.14040  506 LYS B O     
7540 C  CB    . LYS B 510 ? 0.54830 0.58590 0.47890 -0.01090 -0.03210 0.14730  506 LYS B CB    
7541 C  CG    . LYS B 510 ? 0.72530 0.77360 0.64850 -0.01330 -0.03530 0.15730  506 LYS B CG    
7542 C  CD    . LYS B 510 ? 0.83870 0.88680 0.76580 -0.01530 -0.03330 0.16740  506 LYS B CD    
7543 C  CE    . LYS B 510 ? 0.85560 0.89920 0.79640 -0.01430 -0.03670 0.17830  506 LYS B CE    
7544 N  NZ    . LYS B 510 ? 0.86900 0.91020 0.81540 -0.01640 -0.03450 0.18720  506 LYS B NZ    
7545 N  N     . MET B 511 ? 0.40190 0.42220 0.34680 -0.00510 -0.03030 0.12780  507 MET B N     
7546 C  CA    . MET B 511 ? 0.40540 0.41660 0.35690 -0.00330 -0.02720 0.11940  507 MET B CA    
7547 C  C     . MET B 511 ? 0.41930 0.42360 0.38450 -0.00070 -0.02860 0.12190  507 MET B C     
7548 O  O     . MET B 511 ? 0.40180 0.39730 0.37550 0.00030  -0.02560 0.12000  507 MET B O     
7549 C  CB    . MET B 511 ? 0.37910 0.39210 0.32290 -0.00280 -0.02680 0.10900  507 MET B CB    
7550 C  CG    . MET B 511 ? 0.55580 0.56070 0.50390 -0.00170 -0.02290 0.10040  507 MET B CG    
7551 S  SD    . MET B 511 ? 0.66200 0.66770 0.60520 -0.00050 -0.02380 0.08990  507 MET B SD    
7552 C  CE    . MET B 511 ? 0.76800 0.76350 0.72240 0.00150  -0.02100 0.08460  507 MET B CE    
7553 N  N     . ALA B 512 ? 0.41280 0.42130 0.38040 0.00050  -0.03310 0.12570  508 ALA B N     
7554 C  CA    . ALA B 512 ? 0.39250 0.39550 0.37420 0.00340  -0.03430 0.12890  508 ALA B CA    
7555 C  C     . ALA B 512 ? 0.42560 0.42320 0.41660 0.00350  -0.03320 0.13720  508 ALA B C     
7556 O  O     . ALA B 512 ? 0.37910 0.36730 0.38070 0.00550  -0.03060 0.13550  508 ALA B O     
7557 C  CB    . ALA B 512 ? 0.35560 0.36590 0.33880 0.00420  -0.03990 0.13340  508 ALA B CB    
7558 N  N     . GLU B 513 ? 0.42690 0.43020 0.41360 0.00130  -0.03500 0.14610  509 GLU B N     
7559 C  CA    . GLU B 513 ? 0.47390 0.47220 0.46920 0.00090  -0.03420 0.15490  509 GLU B CA    
7560 C  C     . GLU B 513 ? 0.47100 0.45970 0.46910 0.00030  -0.02890 0.14940  509 GLU B C     
7561 O  O     . GLU B 513 ? 0.44460 0.42390 0.45450 0.00160  -0.02750 0.15130  509 GLU B O     
7562 C  CB    . GLU B 513 ? 0.43800 0.44530 0.42550 -0.00210 -0.03650 0.16460  509 GLU B CB    
7563 C  CG    . GLU B 513 ? 0.57310 0.57610 0.56950 -0.00300 -0.03630 0.17520  509 GLU B CG    
7564 C  CD    . GLU B 513 ? 0.66880 0.68160 0.65600 -0.00660 -0.03790 0.18460  509 GLU B CD    
7565 O  OE1   . GLU B 513 ? 0.71470 0.72460 0.70740 -0.00810 -0.03710 0.19300  509 GLU B OE1   
7566 O  OE2   . GLU B 513 ? 0.70480 0.72840 0.67920 -0.00800 -0.03990 0.18340  509 GLU B OE2   
7567 N  N     . SER B 514 ? 0.40650 0.39770 0.39400 -0.00190 -0.02610 0.14250  510 SER B N     
7568 C  CA    . SER B 514 ? 0.36430 0.34750 0.35400 -0.00290 -0.02160 0.13720  510 SER B CA    
7569 C  C     . SER B 514 ? 0.39670 0.36990 0.39590 -0.00020 -0.01980 0.13020  510 SER B C     
7570 O  O     . SER B 514 ? 0.39670 0.36120 0.40210 -0.00070 -0.01690 0.12850  510 SER B O     
7571 C  CB    . SER B 514 ? 0.34820 0.33670 0.32550 -0.00510 -0.01910 0.13030  510 SER B CB    
7572 O  OG    . SER B 514 ? 0.41290 0.39940 0.38810 -0.00340 -0.01790 0.11970  510 SER B OG    
7573 N  N     . LEU B 515 ? 0.33020 0.30480 0.33040 0.00250  -0.02140 0.12600  511 LEU B N     
7574 C  CA    . LEU B 515 ? 0.40740 0.37400 0.41560 0.00520  -0.01950 0.11900  511 LEU B CA    
7575 C  C     . LEU B 515 ? 0.44240 0.40470 0.46400 0.00840  -0.02110 0.12450  511 LEU B C     
7576 O  O     . LEU B 515 ? 0.41510 0.37190 0.44360 0.01120  -0.01950 0.11910  511 LEU B O     
7577 C  CB    . LEU B 515 ? 0.38530 0.35600 0.38720 0.00610  -0.01970 0.11050  511 LEU B CB    
7578 C  CG    . LEU B 515 ? 0.41920 0.39320 0.40910 0.00370  -0.01770 0.10380  511 LEU B CG    
7579 C  CD1   . LEU B 515 ? 0.33020 0.30710 0.31520 0.00470  -0.01810 0.09570  511 LEU B CD1   
7580 C  CD2   . LEU B 515 ? 0.40200 0.36890 0.39350 0.00220  -0.01360 0.10020  511 LEU B CD2   
7581 N  N     . GLY B 516 ? 0.39030 0.35500 0.41580 0.00830  -0.02390 0.13530  512 GLY B N     
7582 C  CA    . GLY B 516 ? 0.38510 0.34550 0.42460 0.01160  -0.02540 0.14140  512 GLY B CA    
7583 C  C     . GLY B 516 ? 0.49140 0.45810 0.53420 0.01440  -0.02890 0.14260  512 GLY B C     
7584 O  O     . GLY B 516 ? 0.53750 0.49970 0.59310 0.01810  -0.02880 0.14390  512 GLY B O     
7585 N  N     . VAL B 517 ? 0.41130 0.38840 0.44320 0.01280  -0.03200 0.14220  513 VAL B N     
7586 C  CA    . VAL B 517 ? 0.37540 0.35940 0.40910 0.01470  -0.03570 0.14250  513 VAL B CA    
7587 C  C     . VAL B 517 ? 0.44070 0.43530 0.46940 0.01300  -0.04120 0.15230  513 VAL B C     
7588 O  O     . VAL B 517 ? 0.39250 0.39270 0.40800 0.00950  -0.04190 0.15240  513 VAL B O     
7589 C  CB    . VAL B 517 ? 0.41110 0.39790 0.43590 0.01400  -0.03470 0.13170  513 VAL B CB    
7590 C  CG1   . VAL B 517 ? 0.38550 0.38070 0.41120 0.01500  -0.03930 0.13290  513 VAL B CG1   
7591 C  CG2   . VAL B 517 ? 0.41190 0.38920 0.44180 0.01580  -0.02950 0.12250  513 VAL B CG2   
7592 N  N     . LYS B 518 ? 0.43770 0.43560 0.47640 0.01530  -0.04520 0.16020  514 LYS B N     
7593 C  CA    . LYS B 518 ? 0.40870 0.41760 0.44240 0.01340  -0.05110 0.16980  514 LYS B CA    
7594 C  C     . LYS B 518 ? 0.43520 0.45360 0.45500 0.01090  -0.05380 0.16400  514 LYS B C     
7595 O  O     . LYS B 518 ? 0.43450 0.45190 0.45410 0.01200  -0.05270 0.15500  514 LYS B O     
7596 C  CB    . LYS B 518 ? 0.50390 0.51520 0.55230 0.01660  -0.05520 0.17940  514 LYS B CB    
7597 C  CG    . LYS B 518 ? 0.54650 0.56990 0.58950 0.01430  -0.06190 0.19040  514 LYS B CG    
7598 C  CD    . LYS B 518 ? 0.62870 0.65540 0.68680 0.01740  -0.06650 0.20120  514 LYS B CD    
7599 C  CE    . LYS B 518 ? 0.72040 0.75310 0.77740 0.01530  -0.07080 0.21540  514 LYS B CE    
7600 N  NZ    . LYS B 518 ? 0.78080 0.82600 0.81970 0.01050  -0.07500 0.21680  514 LYS B NZ    
7601 N  N     . SER B 519 ? 0.38750 0.41500 0.39570 0.00760  -0.05730 0.16930  515 SER B N     
7602 C  CA    . SER B 519 ? 0.44320 0.47890 0.43640 0.00470  -0.05950 0.16310  515 SER B CA    
7603 C  C     . SER B 519 ? 0.46890 0.51670 0.45550 0.00230  -0.06590 0.17220  515 SER B C     
7604 O  O     . SER B 519 ? 0.41980 0.46990 0.41040 0.00200  -0.06800 0.18360  515 SER B O     
7605 C  CB    . SER B 519 ? 0.49870 0.53220 0.47880 0.00230  -0.05480 0.15520  515 SER B CB    
7606 O  OG    . SER B 519 ? 0.56010 0.59300 0.53800 0.00070  -0.05300 0.16200  515 SER B OG    
7607 N  N     . TYR B 520 ? 0.45520 0.51050 0.43140 0.00020  -0.06930 0.16700  516 TYR B N     
7608 C  CA    . TYR B 520 ? 0.43230 0.49990 0.39880 -0.00290 -0.07550 0.17320  516 TYR B CA    
7609 C  C     . TYR B 520 ? 0.44440 0.51610 0.39250 -0.00620 -0.07490 0.16340  516 TYR B C     
7610 O  O     . TYR B 520 ? 0.44320 0.51010 0.38960 -0.00560 -0.07210 0.15220  516 TYR B O     
7611 C  CB    . TYR B 520 ? 0.51310 0.58690 0.48790 -0.00200 -0.08200 0.17730  516 TYR B CB    
7612 C  CG    . TYR B 520 ? 0.47410 0.54540 0.46830 0.00180  -0.08350 0.18720  516 TYR B CG    
7613 C  CD1   . TYR B 520 ? 0.55580 0.63300 0.55370 0.00130  -0.08780 0.20100  516 TYR B CD1   
7614 C  CD2   . TYR B 520 ? 0.47520 0.53840 0.48400 0.00590  -0.08060 0.18280  516 TYR B CD2   
7615 C  CE1   . TYR B 520 ? 0.57020 0.64490 0.58700 0.00520  -0.08910 0.21010  516 TYR B CE1   
7616 C  CE2   . TYR B 520 ? 0.44280 0.50370 0.46980 0.00970  -0.08150 0.19120  516 TYR B CE2   
7617 C  CZ    . TYR B 520 ? 0.55300 0.61930 0.58430 0.00950  -0.08580 0.20480  516 TYR B CZ    
7618 O  OH    . TYR B 520 ? 0.63340 0.69710 0.68400 0.01380  -0.08660 0.21330  516 TYR B OH    
7619 N  N     . ARG B 521 ? 0.44820 0.52880 0.38270 -0.00970 -0.07720 0.16760  517 ARG B N     
7620 C  CA    . ARG B 521 ? 0.47110 0.55680 0.38790 -0.01270 -0.07730 0.15860  517 ARG B CA    
7621 C  C     . ARG B 521 ? 0.51930 0.61550 0.43050 -0.01530 -0.08500 0.16110  517 ARG B C     
7622 O  O     . ARG B 521 ? 0.51500 0.61870 0.42830 -0.01630 -0.09000 0.17270  517 ARG B O     
7623 C  CB    . ARG B 521 ? 0.47180 0.56050 0.37570 -0.01510 -0.07370 0.15990  517 ARG B CB    
7624 C  CG    . ARG B 521 ? 0.53610 0.63230 0.42040 -0.01840 -0.07430 0.15240  517 ARG B CG    
7625 C  CD    . ARG B 521 ? 0.60900 0.69820 0.48870 -0.01740 -0.06920 0.13780  517 ARG B CD    
7626 N  NE    . ARG B 521 ? 0.71790 0.81360 0.57920 -0.02030 -0.06890 0.13100  517 ARG B NE    
7627 C  CZ    . ARG B 521 ? 0.70780 0.79960 0.56230 -0.02000 -0.06580 0.11820  517 ARG B CZ    
7628 N  NH1   . ARG B 521 ? 0.58970 0.67170 0.45410 -0.01730 -0.06300 0.11130  517 ARG B NH1   
7629 N  NH2   . ARG B 521 ? 0.66790 0.76590 0.50570 -0.02240 -0.06550 0.11250  517 ARG B NH2   
7630 N  N     . ALA B 522 ? 0.40460 0.50150 0.30890 -0.01650 -0.08640 0.15050  518 ALA B N     
7631 C  CA    . ALA B 522 ? 0.53310 0.63950 0.43240 -0.01930 -0.09410 0.15180  518 ALA B CA    
7632 C  C     . ALA B 522 ? 0.51150 0.62230 0.39090 -0.02290 -0.09440 0.14230  518 ALA B C     
7633 O  O     . ALA B 522 ? 0.46760 0.57210 0.34340 -0.02250 -0.09080 0.13020  518 ALA B O     
7634 C  CB    . ALA B 522 ? 0.52850 0.63180 0.44110 -0.01740 -0.09690 0.14880  518 ALA B CB    
7635 N  N     . GLU B 523 ? 0.48400 0.60560 0.35070 -0.02660 -0.09850 0.14770  519 GLU B N     
7636 C  CA    . GLU B 523 ? 0.50880 0.63560 0.35590 -0.03030 -0.09940 0.13880  519 GLU B CA    
7637 C  C     . GLU B 523 ? 0.47260 0.60920 0.31380 -0.03410 -0.10830 0.14010  519 GLU B C     
7638 O  O     . GLU B 523 ? 0.49080 0.63120 0.31560 -0.03740 -0.10970 0.13160  519 GLU B O     
7639 C  CB    . GLU B 523 ? 0.59830 0.73020 0.43150 -0.03190 -0.09570 0.14180  519 GLU B CB    
7640 C  CG    . GLU B 523 ? 0.73090 0.85360 0.56910 -0.02870 -0.08700 0.13970  519 GLU B CG    
7641 C  CD    . GLU B 523 ? 0.86280 0.99130 0.69000 -0.03020 -0.08330 0.14460  519 GLU B CD    
7642 O  OE1   . GLU B 523 ? 0.88940 1.01160 0.71960 -0.02820 -0.07630 0.14300  519 GLU B OE1   
7643 O  OE2   . GLU B 523 ? 0.84880 0.98860 0.66420 -0.03370 -0.08760 0.15030  519 GLU B OE2   
7644 N  N     . THR B 524 ? 0.49440 0.63510 0.34860 -0.03370 -0.11440 0.15020  520 THR B N     
7645 C  CA    . THR B 524 ? 0.56540 0.71510 0.41730 -0.03720 -0.12350 0.15180  520 THR B CA    
7646 C  C     . THR B 524 ? 0.59580 0.74160 0.46800 -0.03450 -0.12610 0.15370  520 THR B C     
7647 O  O     . THR B 524 ? 0.49860 0.63690 0.38670 -0.02990 -0.12180 0.15750  520 THR B O     
7648 C  CB    . THR B 524 ? 0.55570 0.71860 0.40240 -0.04020 -0.12990 0.16530  520 THR B CB    
7649 O  OG1   . THR B 524 ? 0.57640 0.73870 0.44180 -0.03670 -0.13060 0.17860  520 THR B OG1   
7650 C  CG2   . THR B 524 ? 0.58630 0.75250 0.41570 -0.04210 -0.12550 0.16450  520 THR B CG2   
7651 N  N     . VAL B 525 ? 0.64030 0.79170 0.51210 -0.03750 -0.13320 0.15120  521 VAL B N     
7652 C  CA    . VAL B 525 ? 0.60850 0.75790 0.49990 -0.03510 -0.13580 0.15350  521 VAL B CA    
7653 C  C     . VAL B 525 ? 0.58230 0.73590 0.48970 -0.03220 -0.13820 0.16900  521 VAL B C     
7654 O  O     . VAL B 525 ? 0.52090 0.66870 0.44720 -0.02780 -0.13590 0.17160  521 VAL B O     
7655 C  CB    . VAL B 525 ? 0.60040 0.75660 0.48820 -0.03960 -0.14380 0.14900  521 VAL B CB    
7656 C  CG1   . VAL B 525 ? 0.68200 0.83290 0.55440 -0.04240 -0.14150 0.13340  521 VAL B CG1   
7657 C  CG2   . VAL B 525 ? 0.69170 0.86220 0.57160 -0.04390 -0.15250 0.15850  521 VAL B CG2   
7658 N  N     . GLU B 526 ? 0.60170 0.76510 0.50210 -0.03450 -0.14240 0.17960  522 GLU B N     
7659 C  CA    . GLU B 526 ? 0.52120 0.68770 0.43780 -0.03160 -0.14420 0.19400  522 GLU B CA    
7660 C  C     . GLU B 526 ? 0.51380 0.67030 0.44090 -0.02640 -0.13680 0.19790  522 GLU B C     
7661 O  O     . GLU B 526 ? 0.55770 0.71080 0.50470 -0.02200 -0.13630 0.20480  522 GLU B O     
7662 C  CB    . GLU B 526 ? 0.59830 0.77370 0.50590 -0.03490 -0.14670 0.20000  522 GLU B CB    
7663 C  CG    . GLU B 526 ? 0.77040 0.95590 0.67440 -0.03920 -0.15460 0.19930  522 GLU B CG    
7664 C  CD    . GLU B 526 ? 0.96460 1.15090 0.85110 -0.04360 -0.15640 0.18580  522 GLU B CD    
7665 O  OE1   . GLU B 526 ? 0.97450 1.15590 0.84630 -0.04420 -0.15140 0.17780  522 GLU B OE1   
7666 O  OE2   . GLU B 526 ? 0.98020 1.17180 0.86810 -0.04650 -0.16270 0.18310  522 GLU B OE2   
7667 N  N     . ASP B 527 ? 0.53950 0.69030 0.45430 -0.02670 -0.13010 0.19220  523 ASP B N     
7668 C  CA    . ASP B 527 ? 0.51670 0.65610 0.44130 -0.02220 -0.12210 0.19320  523 ASP B CA    
7669 C  C     . ASP B 527 ? 0.45510 0.58350 0.39310 -0.01820 -0.11760 0.18450  523 ASP B C     
7670 O  O     . ASP B 527 ? 0.52560 0.64660 0.47960 -0.01370 -0.11380 0.18860  523 ASP B O     
7671 C  CB    . ASP B 527 ? 0.61460 0.75100 0.52300 -0.02370 -0.11600 0.18790  523 ASP B CB    
7672 C  CG    . ASP B 527 ? 0.82560 0.97250 0.72260 -0.02700 -0.11920 0.19820  523 ASP B CG    
7673 O  OD1   . ASP B 527 ? 0.90760 1.05860 0.81540 -0.02630 -0.12240 0.20940  523 ASP B OD1   
7674 O  OD2   . ASP B 527 ? 0.94080 1.09050 0.81960 -0.03000 -0.11670 0.19270  523 ASP B OD2   
7675 N  N     . PHE B 528 ? 0.44110 0.56820 0.37280 -0.01990 -0.11790 0.17250  524 PHE B N     
7676 C  CA    . PHE B 528 ? 0.47720 0.59440 0.42070 -0.01650 -0.11350 0.16430  524 PHE B CA    
7677 C  C     . PHE B 528 ? 0.52390 0.64310 0.48780 -0.01350 -0.11690 0.17170  524 PHE B C     
7678 O  O     . PHE B 528 ? 0.44950 0.56030 0.42820 -0.00890 -0.11200 0.17150  524 PHE B O     
7679 C  CB    . PHE B 528 ? 0.48570 0.60160 0.41850 -0.01920 -0.11360 0.15080  524 PHE B CB    
7680 C  CG    . PHE B 528 ? 0.43750 0.54440 0.38210 -0.01620 -0.10950 0.14310  524 PHE B CG    
7681 C  CD1   . PHE B 528 ? 0.44990 0.54560 0.39730 -0.01300 -0.10130 0.13780  524 PHE B CD1   
7682 C  CD2   . PHE B 528 ? 0.47940 0.58950 0.43310 -0.01670 -0.11400 0.14200  524 PHE B CD2   
7683 C  CE1   . PHE B 528 ? 0.43830 0.52640 0.39610 -0.01030 -0.09750 0.13120  524 PHE B CE1   
7684 C  CE2   . PHE B 528 ? 0.47740 0.57980 0.44220 -0.01390 -0.10990 0.13550  524 PHE B CE2   
7685 C  CZ    . PHE B 528 ? 0.39620 0.48750 0.36250 -0.01070 -0.10160 0.13020  524 PHE B CZ    
7686 N  N     . ASP B 529 ? 0.53560 0.66620 0.50060 -0.01610 -0.12540 0.17820  525 ASP B N     
7687 C  CA    . ASP B 529 ? 0.50300 0.63720 0.48810 -0.01320 -0.12910 0.18630  525 ASP B CA    
7688 C  C     . ASP B 529 ? 0.50120 0.63200 0.50070 -0.00850 -0.12640 0.19750  525 ASP B C     
7689 O  O     . ASP B 529 ? 0.49780 0.62340 0.51560 -0.00370 -0.12360 0.19910  525 ASP B O     
7690 C  CB    . ASP B 529 ? 0.53410 0.68270 0.51650 -0.01740 -0.13940 0.19280  525 ASP B CB    
7691 C  CG    . ASP B 529 ? 0.55950 0.71320 0.56340 -0.01460 -0.14360 0.20050  525 ASP B CG    
7692 O  OD1   . ASP B 529 ? 0.59990 0.74910 0.61400 -0.01260 -0.14110 0.19390  525 ASP B OD1   
7693 O  OD2   . ASP B 529 ? 0.62220 0.78480 0.63310 -0.01430 -0.14920 0.21370  525 ASP B OD2   
7694 N  N     . ALA B 530 ? 0.48150 0.61480 0.47280 -0.00980 -0.12690 0.20500  526 ALA B N     
7695 C  CA    . ALA B 530 ? 0.53890 0.66790 0.54350 -0.00560 -0.12420 0.21560  526 ALA B CA    
7696 C  C     . ALA B 530 ? 0.52080 0.63480 0.53140 -0.00150 -0.11470 0.20810  526 ALA B C     
7697 O  O     . ALA B 530 ? 0.46640 0.57420 0.49510 0.00340  -0.11180 0.21240  526 ALA B O     
7698 C  CB    . ALA B 530 ? 0.51550 0.65040 0.50860 -0.00860 -0.12660 0.22500  526 ALA B CB    
7699 N  N     . ALA B 531 ? 0.48050 0.58880 0.47650 -0.00350 -0.10960 0.19670  527 ALA B N     
7700 C  CA    . ALA B 531 ? 0.46610 0.56100 0.46670 -0.00030 -0.10090 0.18920  527 ALA B CA    
7701 C  C     . ALA B 531 ? 0.51820 0.60770 0.53370 0.00350  -0.09870 0.18370  527 ALA B C     
7702 O  O     . ALA B 531 ? 0.46680 0.54720 0.49550 0.00780  -0.09360 0.18400  527 ALA B O     
7703 C  CB    . ALA B 531 ? 0.43500 0.52640 0.41720 -0.00320 -0.09680 0.17790  527 ALA B CB    
7704 N  N     . LEU B 532 ? 0.43550 0.53030 0.44880 0.00160  -0.10240 0.17810  528 LEU B N     
7705 C  CA    . LEU B 532 ? 0.47560 0.56630 0.50260 0.00480  -0.10010 0.17290  528 LEU B CA    
7706 C  C     . LEU B 532 ? 0.44530 0.53820 0.49300 0.00910  -0.10190 0.18330  528 LEU B C     
7707 O  O     . LEU B 532 ? 0.46460 0.55030 0.52630 0.01370  -0.09690 0.18110  528 LEU B O     
7708 C  CB    . LEU B 532 ? 0.48870 0.58540 0.50940 0.00130  -0.10440 0.16590  528 LEU B CB    
7709 C  CG    . LEU B 532 ? 0.52940 0.62310 0.56350 0.00400  -0.10210 0.16040  528 LEU B CG    
7710 C  CD1   . LEU B 532 ? 0.47680 0.55750 0.51300 0.00710  -0.09290 0.15190  528 LEU B CD1   
7711 C  CD2   . LEU B 532 ? 0.52690 0.62650 0.55340 -0.00030 -0.10670 0.15380  528 LEU B CD2   
7712 N  N     . LYS B 533 ? 0.43850 0.54170 0.48840 0.00790  -0.10900 0.19480  529 LYS B N     
7713 C  CA    . LYS B 533 ? 0.44360 0.54930 0.51400 0.01240  -0.11100 0.20580  529 LYS B CA    
7714 C  C     . LYS B 533 ? 0.52740 0.62210 0.60730 0.01700  -0.10460 0.20920  529 LYS B C     
7715 O  O     . LYS B 533 ? 0.57460 0.66400 0.67230 0.02220  -0.10120 0.21030  529 LYS B O     
7716 C  CB    . LYS B 533 ? 0.44770 0.56710 0.51700 0.00970  -0.12030 0.21810  529 LYS B CB    
7717 C  CG    . LYS B 533 ? 0.50030 0.62220 0.58930 0.01410  -0.12250 0.23190  529 LYS B CG    
7718 C  CD    . LYS B 533 ? 0.66140 0.79500 0.74430 0.01010  -0.12970 0.24120  529 LYS B CD    
7719 C  CE    . LYS B 533 ? 0.77930 0.90850 0.86640 0.01170  -0.12690 0.24940  529 LYS B CE    
7720 N  NZ    . LYS B 533 ? 0.84130 0.97850 0.91230 0.00610  -0.13090 0.25350  529 LYS B NZ    
7721 N  N     . GLY B 534 ? 0.48700 0.57770 0.55510 0.01500  -0.10260 0.21050  530 GLY B N     
7722 C  CA    . GLY B 534 ? 0.43810 0.51740 0.51440 0.01860  -0.09650 0.21270  530 GLY B CA    
7723 C  C     . GLY B 534 ? 0.50090 0.56800 0.58110 0.02150  -0.08830 0.20070  530 GLY B C     
7724 O  O     . GLY B 534 ? 0.45480 0.51360 0.55020 0.02630  -0.08400 0.20200  530 GLY B O     
7725 N  N     . ALA B 535 ? 0.45240 0.51830 0.51910 0.01860  -0.08620 0.18890  531 ALA B N     
7726 C  CA    . ALA B 535 ? 0.51050 0.56560 0.57940 0.02070  -0.07870 0.17750  531 ALA B CA    
7727 C  C     . ALA B 535 ? 0.51490 0.56880 0.60160 0.02530  -0.07730 0.17660  531 ALA B C     
7728 O  O     . ALA B 535 ? 0.52040 0.56460 0.61680 0.02920  -0.07110 0.17330  531 ALA B O     
7729 C  CB    . ALA B 535 ? 0.37410 0.42960 0.42600 0.01670  -0.07770 0.16600  531 ALA B CB    
7730 N  N     . LEU B 536 ? 0.45490 0.51930 0.54620 0.02480  -0.08290 0.17940  532 LEU B N     
7731 C  CA    . LEU B 536 ? 0.44290 0.50780 0.55100 0.02890  -0.08140 0.17820  532 LEU B CA    
7732 C  C     . LEU B 536 ? 0.49220 0.55300 0.61950 0.03470  -0.07920 0.18630  532 LEU B C     
7733 O  O     . LEU B 536 ? 0.53770 0.59360 0.67800 0.03910  -0.07430 0.18260  532 LEU B O     
7734 C  CB    . LEU B 536 ? 0.37350 0.45150 0.48310 0.02660  -0.08870 0.18090  532 LEU B CB    
7735 C  CG    . LEU B 536 ? 0.45530 0.53520 0.54940 0.02170  -0.08950 0.17040  532 LEU B CG    
7736 C  CD1   . LEU B 536 ? 0.43370 0.52680 0.52540 0.01790  -0.09810 0.17390  532 LEU B CD1   
7737 C  CD2   . LEU B 536 ? 0.44570 0.51830 0.54420 0.02380  -0.08270 0.15980  532 LEU B CD2   
7738 N  N     . ALA B 537 ? 0.49820 0.56090 0.62750 0.03480  -0.08280 0.19740  533 ALA B N     
7739 C  CA    . ALA B 537 ? 0.48370 0.54190 0.63140 0.04030  -0.08110 0.20600  533 ALA B CA    
7740 C  C     . ALA B 537 ? 0.58630 0.62970 0.73400 0.04220  -0.07390 0.20230  533 ALA B C     
7741 O  O     . ALA B 537 ? 0.62120 0.65840 0.78490 0.04710  -0.07130 0.20750  533 ALA B O     
7742 C  CB    . ALA B 537 ? 0.45970 0.52700 0.61030 0.03940  -0.08880 0.22080  533 ALA B CB    
7743 N  N     . MET B 538 ? 0.52100 0.55890 0.65180 0.03840  -0.07060 0.19360  534 MET B N     
7744 C  CA    . MET B 538 ? 0.66100 0.68710 0.78870 0.03840  -0.06570 0.19250  534 MET B CA    
7745 C  C     . MET B 538 ? 0.73520 0.74900 0.87640 0.04350  -0.05850 0.18740  534 MET B C     
7746 O  O     . MET B 538 ? 0.92930 0.93410 1.07740 0.04540  -0.05580 0.19130  534 MET B O     
7747 C  CB    . MET B 538 ? 0.66340 0.68780 0.77060 0.03330  -0.06380 0.18370  534 MET B CB    
7748 C  CG    . MET B 538 ? 0.74220 0.77590 0.83500 0.02840  -0.06960 0.18910  534 MET B CG    
7749 S  SD    . MET B 538 ? 0.89850 0.92520 0.97370 0.02440  -0.06500 0.18200  534 MET B SD    
7750 C  CE    . MET B 538 ? 0.88890 0.90090 0.97800 0.02830  -0.05870 0.18350  534 MET B CE    
7751 N  N     . ASN B 539 ? 0.57390 0.58680 0.71770 0.04520  -0.05500 0.17790  535 ASN B N     
7752 C  CA    . ASN B 539 ? 0.60310 0.60570 0.75750 0.04960  -0.04770 0.17080  535 ASN B CA    
7753 C  C     . ASN B 539 ? 0.71780 0.70820 0.86220 0.04760  -0.04220 0.16340  535 ASN B C     
7754 O  O     . ASN B 539 ? 0.79490 0.77440 0.94810 0.05090  -0.03630 0.15930  535 ASN B O     
7755 C  CB    . ASN B 539 ? 0.82260 0.82200 0.99840 0.05580  -0.04680 0.17850  535 ASN B CB    
7756 C  CG    . ASN B 539 ? 1.04070 1.05330 1.22650 0.05730  -0.05370 0.18920  535 ASN B CG    
7757 O  OD1   . ASN B 539 ? 1.11600 1.13440 1.31170 0.06020  -0.05350 0.18760  535 ASN B OD1   
7758 N  ND2   . ASN B 539 ? 1.03320 1.04940 1.21990 0.05620  -0.05920 0.20110  535 ASN B ND2   
7759 N  N     . THR B 540 ? 0.58580 0.57800 0.71300 0.04230  -0.04370 0.16120  536 THR B N     
7760 C  CA    . THR B 540 ? 0.59690 0.58090 0.71190 0.03940  -0.03920 0.15270  536 THR B CA    
7761 C  C     . THR B 540 ? 0.51270 0.50410 0.61030 0.03460  -0.04150 0.14740  536 THR B C     
7762 O  O     . THR B 540 ? 0.47710 0.47910 0.57160 0.03320  -0.04700 0.15160  536 THR B O     
7763 C  CB    . THR B 540 ? 0.70000 0.67800 0.81380 0.03800  -0.03920 0.15930  536 THR B CB    
7764 O  OG1   . THR B 540 ? 0.71480 0.70240 0.82050 0.03460  -0.04530 0.16790  536 THR B OG1   
7765 C  CG2   . THR B 540 ? 0.78960 0.76040 0.92170 0.04270  -0.03780 0.16570  536 THR B CG2   
7766 N  N     . PRO B 541 ? 0.47040 0.45650 0.55660 0.03200  -0.03760 0.13840  537 PRO B N     
7767 C  CA    . PRO B 541 ? 0.46260 0.45510 0.53300 0.02780  -0.03950 0.13320  537 PRO B CA    
7768 C  C     . PRO B 541 ? 0.40670 0.40650 0.46750 0.02440  -0.04460 0.14060  537 PRO B C     
7769 O  O     . PRO B 541 ? 0.35620 0.35420 0.41930 0.02430  -0.04540 0.14850  537 PRO B O     
7770 C  CB    . PRO B 541 ? 0.40650 0.39060 0.46890 0.02630  -0.03400 0.12370  537 PRO B CB    
7771 C  CG    . PRO B 541 ? 0.44370 0.41720 0.51750 0.02930  -0.02930 0.12350  537 PRO B CG    
7772 C  CD    . PRO B 541 ? 0.48170 0.45580 0.56870 0.03240  -0.03180 0.13360  537 PRO B CD    
7773 N  N     . CYS B 542 ? 0.35370 0.36180 0.40330 0.02150  -0.04800 0.13780  538 CYS B N     
7774 C  CA    . CYS B 542 ? 0.38360 0.40000 0.42260 0.01810  -0.05300 0.14390  538 CYS B CA    
7775 C  C     . CYS B 542 ? 0.39700 0.41750 0.42000 0.01440  -0.05360 0.13580  538 CYS B C     
7776 O  O     . CYS B 542 ? 0.42050 0.44080 0.44300 0.01470  -0.05270 0.12790  538 CYS B O     
7777 C  CB    . CYS B 542 ? 0.46210 0.48750 0.50890 0.01900  -0.05930 0.15350  538 CYS B CB    
7778 S  SG    . CYS B 542 ? 0.53430 0.57060 0.56880 0.01480  -0.06580 0.16260  538 CYS B SG    
7779 N  N     . LEU B 543 ? 0.33780 0.36220 0.34790 0.01110  -0.05490 0.13790  539 LEU B N     
7780 C  CA    . LEU B 543 ? 0.36340 0.39170 0.35800 0.00790  -0.05530 0.13040  539 LEU B CA    
7781 C  C     . LEU B 543 ? 0.41560 0.45470 0.40070 0.00490  -0.06130 0.13630  539 LEU B C     
7782 O  O     . LEU B 543 ? 0.39960 0.44170 0.38460 0.00420  -0.06300 0.14560  539 LEU B O     
7783 C  CB    . LEU B 543 ? 0.31780 0.34020 0.30410 0.00660  -0.04990 0.12480  539 LEU B CB    
7784 C  CG    . LEU B 543 ? 0.39300 0.41820 0.36440 0.00400  -0.04930 0.11620  539 LEU B CG    
7785 C  CD1   . LEU B 543 ? 0.43080 0.44800 0.39980 0.00420  -0.04310 0.10820  539 LEU B CD1   
7786 C  CD2   . LEU B 543 ? 0.32120 0.35460 0.28000 0.00090  -0.05210 0.12080  539 LEU B CD2   
7787 N  N     . ILE B 544 ? 0.41340 0.45820 0.39040 0.00280  -0.06450 0.13090  540 ILE B N     
7788 C  CA    . ILE B 544 ? 0.41780 0.47300 0.38360 -0.00060 -0.07030 0.13470  540 ILE B CA    
7789 C  C     . ILE B 544 ? 0.41540 0.47110 0.36480 -0.00340 -0.06850 0.12510  540 ILE B C     
7790 O  O     . ILE B 544 ? 0.39200 0.44480 0.33980 -0.00340 -0.06740 0.11580  540 ILE B O     
7791 C  CB    . ILE B 544 ? 0.39930 0.46180 0.37070 -0.00090 -0.07680 0.13760  540 ILE B CB    
7792 C  CG1   . ILE B 544 ? 0.33720 0.39890 0.32680 0.00260  -0.07800 0.14670  540 ILE B CG1   
7793 C  CG2   . ILE B 544 ? 0.34420 0.41780 0.30300 -0.00490 -0.08310 0.14160  540 ILE B CG2   
7794 C  CD1   . ILE B 544 ? 0.35220 0.42160 0.34940 0.00260  -0.08420 0.14970  540 ILE B CD1   
7795 N  N     . ASP B 545 ? 0.38850 0.44820 0.32610 -0.00560 -0.06800 0.12780  541 ASP B N     
7796 C  CA    . ASP B 545 ? 0.36050 0.42100 0.28240 -0.00790 -0.06550 0.11940  541 ASP B CA    
7797 C  C     . ASP B 545 ? 0.38160 0.45210 0.29160 -0.01130 -0.07140 0.11930  541 ASP B C     
7798 O  O     . ASP B 545 ? 0.44580 0.52410 0.35050 -0.01320 -0.07470 0.12770  541 ASP B O     
7799 C  CB    . ASP B 545 ? 0.42740 0.48680 0.34460 -0.00820 -0.06090 0.12270  541 ASP B CB    
7800 C  CG    . ASP B 545 ? 0.64950 0.71010 0.55150 -0.01010 -0.05740 0.11440  541 ASP B CG    
7801 O  OD1   . ASP B 545 ? 0.77390 0.83700 0.66720 -0.01140 -0.05910 0.10660  541 ASP B OD1   
7802 O  OD2   . ASP B 545 ? 0.67690 0.73600 0.57630 -0.01010 -0.05270 0.11570  541 ASP B OD2   
7803 N  N     . VAL B 546 ? 0.41540 0.48570 0.32120 -0.01230 -0.07310 0.11020  542 VAL B N     
7804 C  CA    . VAL B 546 ? 0.43140 0.51050 0.32720 -0.01570 -0.07950 0.10950  542 VAL B CA    
7805 C  C     . VAL B 546 ? 0.49400 0.57430 0.37230 -0.01800 -0.07730 0.10060  542 VAL B C     
7806 O  O     . VAL B 546 ? 0.48550 0.55890 0.36220 -0.01700 -0.07290 0.09070  542 VAL B O     
7807 C  CB    . VAL B 546 ? 0.45550 0.53440 0.35890 -0.01590 -0.08390 0.10600  542 VAL B CB    
7808 C  CG1   . VAL B 546 ? 0.37650 0.46510 0.26930 -0.02020 -0.09130 0.10600  542 VAL B CG1   
7809 C  CG2   . VAL B 546 ? 0.43000 0.50750 0.35180 -0.01300 -0.08510 0.11410  542 VAL B CG2   
7810 N  N     . GLN B 547 ? 0.45000 0.53940 0.31530 -0.02100 -0.08030 0.10400  543 GLN B N     
7811 C  CA    . GLN B 547 ? 0.48040 0.57190 0.32840 -0.02320 -0.07830 0.09520  543 GLN B CA    
7812 C  C     . GLN B 547 ? 0.51750 0.60880 0.36060 -0.02520 -0.08230 0.08570  543 GLN B C     
7813 O  O     . GLN B 547 ? 0.49020 0.58780 0.33340 -0.02770 -0.08940 0.08910  543 GLN B O     
7814 C  CB    . GLN B 547 ? 0.45200 0.55410 0.28700 -0.02600 -0.08010 0.10180  543 GLN B CB    
7815 C  CG    . GLN B 547 ? 0.56150 0.66550 0.37890 -0.02750 -0.07630 0.09290  543 GLN B CG    
7816 C  CD    . GLN B 547 ? 0.72450 0.84080 0.52650 -0.03120 -0.07950 0.09810  543 GLN B CD    
7817 O  OE1   . GLN B 547 ? 0.68810 0.81150 0.49310 -0.03260 -0.08460 0.10960  543 GLN B OE1   
7818 N  NE2   . GLN B 547 ? 0.78240 0.90150 0.56820 -0.03260 -0.07640 0.08960  543 GLN B NE2   
7819 N  N     . VAL B 548 ? 0.46190 0.54630 0.30070 -0.02440 -0.07800 0.07410  544 VAL B N     
7820 C  CA    . VAL B 548 ? 0.45810 0.54050 0.29320 -0.02620 -0.08120 0.06420  544 VAL B CA    
7821 C  C     . VAL B 548 ? 0.50740 0.58790 0.32770 -0.02680 -0.07710 0.05330  544 VAL B C     
7822 O  O     . VAL B 548 ? 0.45840 0.53550 0.27710 -0.02440 -0.07030 0.05150  544 VAL B O     
7823 C  CB    . VAL B 548 ? 0.53510 0.60870 0.38540 -0.02390 -0.08040 0.06120  544 VAL B CB    
7824 C  CG1   . VAL B 548 ? 0.55620 0.62680 0.40240 -0.02600 -0.08300 0.05060  544 VAL B CG1   
7825 C  CG2   . VAL B 548 ? 0.59890 0.67520 0.46380 -0.02330 -0.08460 0.07150  544 VAL B CG2   
7826 N  N     . ASP B 549 ? 0.50630 0.58920 0.31610 -0.03010 -0.08140 0.04600  545 ASP B N     
7827 C  CA    . ASP B 549 ? 0.58870 0.66970 0.38420 -0.03070 -0.07800 0.03460  545 ASP B CA    
7828 C  C     . ASP B 549 ? 0.58410 0.65370 0.38630 -0.02830 -0.07420 0.02460  545 ASP B C     
7829 O  O     . ASP B 549 ? 0.50450 0.56990 0.31470 -0.02920 -0.07810 0.02210  545 ASP B O     
7830 C  CB    . ASP B 549 ? 0.64660 0.73460 0.42850 -0.03540 -0.08460 0.03090  545 ASP B CB    
7831 C  CG    . ASP B 549 ? 0.77850 0.86480 0.54460 -0.03620 -0.08130 0.01840  545 ASP B CG    
7832 O  OD1   . ASP B 549 ? 0.76230 0.84210 0.52890 -0.03280 -0.07400 0.01260  545 ASP B OD1   
7833 O  OD2   . ASP B 549 ? 0.83520 0.92700 0.58830 -0.04030 -0.08630 0.01430  545 ASP B OD2   
7834 N  N     . ILE B 550 ? 0.54790 0.61300 0.34710 -0.02550 -0.06680 0.01930  546 ILE B N     
7835 C  CA    . ILE B 550 ? 0.55390 0.60850 0.36000 -0.02290 -0.06290 0.01100  546 ILE B CA    
7836 C  C     . ILE B 550 ? 0.60730 0.65790 0.40700 -0.02500 -0.06580 -0.00020 546 ILE B C     
7837 O  O     . ILE B 550 ? 0.55830 0.60020 0.36580 -0.02360 -0.06460 -0.00600 546 ILE B O     
7838 C  CB    . ILE B 550 ? 0.51590 0.56790 0.32020 -0.01940 -0.05450 0.00880  546 ILE B CB    
7839 C  CG1   . ILE B 550 ? 0.50510 0.54690 0.32130 -0.01630 -0.05070 0.00450  546 ILE B CG1   
7840 C  CG2   . ILE B 550 ? 0.48030 0.53540 0.26830 -0.02000 -0.05180 0.00060  546 ILE B CG2   
7841 C  CD1   . ILE B 550 ? 0.44680 0.48680 0.26430 -0.01300 -0.04310 0.00440  546 ILE B CD1   
7842 N  N     . ASP B 551 ? 0.53970 0.59640 0.32550 -0.02850 -0.06980 -0.00330 547 ASP B N     
7843 C  CA    . ASP B 551 ? 0.60020 0.65300 0.37830 -0.03090 -0.07250 -0.01480 547 ASP B CA    
7844 C  C     . ASP B 551 ? 0.60940 0.66110 0.39430 -0.03430 -0.08050 -0.01430 547 ASP B C     
7845 O  O     . ASP B 551 ? 0.67570 0.72160 0.45800 -0.03610 -0.08270 -0.02390 547 ASP B O     
7846 C  CB    . ASP B 551 ? 0.70120 0.76140 0.46000 -0.03350 -0.07330 -0.01900 547 ASP B CB    
7847 C  CG    . ASP B 551 ? 0.81290 0.87230 0.56330 -0.03030 -0.06490 -0.02460 547 ASP B CG    
7848 O  OD1   . ASP B 551 ? 0.84060 0.89140 0.59830 -0.02660 -0.05940 -0.02950 547 ASP B OD1   
7849 O  OD2   . ASP B 551 ? 0.93700 1.00510 0.67350 -0.03160 -0.06380 -0.02370 547 ASP B OD2   
7850 N  N     . VAL B 552 ? 0.57240 0.62940 0.36630 -0.03530 -0.08490 -0.00350 548 VAL B N     
7851 C  CA    . VAL B 552 ? 0.58510 0.64330 0.38510 -0.03900 -0.09300 -0.00240 548 VAL B CA    
7852 C  C     . VAL B 552 ? 0.53170 0.57930 0.34350 -0.03780 -0.09190 -0.00800 548 VAL B C     
7853 O  O     . VAL B 552 ? 0.56440 0.60650 0.38730 -0.03380 -0.08670 -0.00580 548 VAL B O     
7854 C  CB    . VAL B 552 ? 0.59270 0.65880 0.40200 -0.03940 -0.09710 0.01100  548 VAL B CB    
7855 C  CG1   . VAL B 552 ? 0.60940 0.67680 0.42780 -0.04270 -0.10480 0.01240  548 VAL B CG1   
7856 C  CG2   . VAL B 552 ? 0.61100 0.68830 0.40800 -0.04130 -0.09920 0.01700  548 VAL B CG2   
7857 N  N     . LEU B 553 ? 0.54590 0.59100 0.35570 -0.04160 -0.09730 -0.01500 549 LEU B N     
7858 C  CA    . LEU B 553 ? 0.58150 0.61660 0.40180 -0.04110 -0.09660 -0.02060 549 LEU B CA    
7859 C  C     . LEU B 553 ? 0.56900 0.60630 0.40540 -0.04200 -0.10100 -0.01240 549 LEU B C     
7860 O  O     . LEU B 553 ? 0.53900 0.58280 0.37540 -0.04620 -0.10850 -0.00940 549 LEU B O     
7861 C  CB    . LEU B 553 ? 0.65120 0.68160 0.46230 -0.04490 -0.10020 -0.03230 549 LEU B CB    
7862 C  CG    . LEU B 553 ? 0.73920 0.75790 0.55820 -0.04440 -0.09880 -0.04010 549 LEU B CG    
7863 C  CD1   . LEU B 553 ? 0.86400 0.88240 0.69900 -0.04620 -0.10340 -0.03440 549 LEU B CD1   
7864 C  CD2   . LEU B 553 ? 0.66650 0.67770 0.48870 -0.03880 -0.08990 -0.04240 549 LEU B CD2   
7865 N  N     . PRO B 554 ? 0.58190 0.61440 0.43200 -0.03830 -0.09660 -0.00880 550 PRO B N     
7866 C  CA    . PRO B 554 ? 0.54690 0.58260 0.41250 -0.03850 -0.09980 -0.00040 550 PRO B CA    
7867 C  C     . PRO B 554 ? 0.54550 0.57820 0.41740 -0.04230 -0.10500 -0.00450 550 PRO B C     
7868 O  O     . PRO B 554 ? 0.63160 0.65680 0.49880 -0.04370 -0.10470 -0.01410 550 PRO B O     
7869 C  CB    . PRO B 554 ? 0.60290 0.63330 0.47890 -0.03330 -0.09240 0.00280  550 PRO B CB    
7870 C  CG    . PRO B 554 ? 0.58200 0.60950 0.44740 -0.03050 -0.08610 -0.00110 550 PRO B CG    
7871 C  CD    . PRO B 554 ? 0.56750 0.59320 0.41920 -0.03340 -0.08810 -0.01090 550 PRO B CD    
7872 N  N     . PRO B 555 ? 0.54990 0.58830 0.43340 -0.04400 -0.10990 0.00280  551 PRO B N     
7873 C  CA    . PRO B 555 ? 0.54260 0.57920 0.43330 -0.04800 -0.11510 -0.00020 551 PRO B CA    
7874 C  C     . PRO B 555 ? 0.59410 0.61980 0.49140 -0.04620 -0.11030 -0.00610 551 PRO B C     
7875 O  O     . PRO B 555 ? 0.58540 0.60740 0.48920 -0.04160 -0.10380 -0.00360 551 PRO B O     
7876 C  CB    . PRO B 555 ? 0.51510 0.56030 0.42020 -0.04820 -0.11870 0.01050  551 PRO B CB    
7877 C  CG    . PRO B 555 ? 0.52970 0.58220 0.43210 -0.04550 -0.11750 0.01860  551 PRO B CG    
7878 C  CD    . PRO B 555 ? 0.55270 0.59940 0.44470 -0.04190 -0.11030 0.01430  551 PRO B CD    
7879 N  N     . GLY B 556 ? 0.54380 0.56430 0.43930 -0.05020 -0.11400 -0.01380 552 GLY B N     
7880 C  CA    . GLY B 556 ? 0.53770 0.54810 0.44030 -0.04950 -0.11090 -0.01870 552 GLY B CA    
7881 C  C     . GLY B 556 ? 0.68980 0.69080 0.58500 -0.04590 -0.10400 -0.02600 552 GLY B C     
7882 O  O     . GLY B 556 ? 0.80250 0.79480 0.70330 -0.04540 -0.10170 -0.03030 552 GLY B O     
7883 N  N     . MET B 557 ? 0.70500 0.70780 0.58830 -0.04350 -0.10080 -0.02740 553 MET B N     
7884 C  CA    . MET B 557 ? 0.75710 0.75190 0.63490 -0.03960 -0.09380 -0.03350 553 MET B CA    
7885 C  C     . MET B 557 ? 0.79810 0.78640 0.66480 -0.04170 -0.09510 -0.04490 553 MET B C     
7886 O  O     . MET B 557 ? 0.78260 0.76160 0.64970 -0.03940 -0.09070 -0.05120 553 MET B O     
7887 C  CB    . MET B 557 ? 0.74850 0.74810 0.61970 -0.03560 -0.08880 -0.02960 553 MET B CB    
7888 C  CG    . MET B 557 ? 0.80210 0.80470 0.68470 -0.03230 -0.08550 -0.02010 553 MET B CG    
7889 S  SD    . MET B 557 ? 0.79440 0.78740 0.68760 -0.02860 -0.07900 -0.02190 553 MET B SD    
7890 C  CE    . MET B 557 ? 0.73530 0.72110 0.61670 -0.02650 -0.07420 -0.03180 553 MET B CE    
7891 N  N     . LYS B 558 ? 0.87570 0.86850 0.73260 -0.04620 -0.10110 -0.04780 554 LYS B N     
7892 C  CA    . LYS B 558 ? 0.91000 0.89590 0.75740 -0.04910 -0.10320 -0.05940 554 LYS B CA    
7893 C  C     . LYS B 558 ? 0.98410 0.95950 0.84210 -0.05020 -0.10390 -0.06370 554 LYS B C     
7894 O  O     . LYS B 558 ? 1.03160 0.99710 0.88670 -0.04850 -0.10050 -0.07240 554 LYS B O     
7895 C  CB    . LYS B 558 ? 0.86620 0.85910 0.70460 -0.05500 -0.11140 -0.06070 554 LYS B CB    
7896 C  CG    . LYS B 558 ? 0.92980 0.91560 0.75700 -0.05840 -0.11390 -0.07340 554 LYS B CG    
7897 C  CD    . LYS B 558 ? 0.95440 0.94400 0.76300 -0.05770 -0.11180 -0.07860 554 LYS B CD    
7898 C  CE    . LYS B 558 ? 1.00430 0.98370 0.80280 -0.05850 -0.11060 -0.09300 554 LYS B CE    
7899 N  NZ    . LYS B 558 ? 1.01410 0.98470 0.82030 -0.06290 -0.11600 -0.09840 554 LYS B NZ    
7900 N  N     . GLN B 559 ? 0.92850 0.90620 0.79990 -0.05260 -0.10790 -0.05720 555 GLN B N     
7901 C  CA    . GLN B 559 ? 0.92300 0.89170 0.80430 -0.05480 -0.10960 -0.06080 555 GLN B CA    
7902 C  C     . GLN B 559 ? 0.91440 0.87620 0.80460 -0.04960 -0.10230 -0.05930 555 GLN B C     
7903 O  O     . GLN B 559 ? 0.94140 0.89310 0.83610 -0.04990 -0.10140 -0.06470 555 GLN B O     
7904 C  CB    . GLN B 559 ? 0.93880 0.91350 0.83170 -0.05950 -0.11630 -0.05400 555 GLN B CB    
7905 C  CG    . GLN B 559 ? 1.02140 1.00420 0.90670 -0.06510 -0.12430 -0.05430 555 GLN B CG    
7906 C  CD    . GLN B 559 ? 1.05210 1.04780 0.93600 -0.06360 -0.12490 -0.04490 555 GLN B CD    
7907 O  OE1   . GLN B 559 ? 1.07450 1.07190 0.95700 -0.05820 -0.11860 -0.04100 555 GLN B OE1   
7908 N  NE2   . GLN B 559 ? 0.99400 0.99890 0.87900 -0.06860 -0.13270 -0.04080 555 GLN B NE2   
7909 N  N     . ARG B 560 ? 0.82600 0.79280 0.71850 -0.04490 -0.09700 -0.05230 556 ARG B N     
7910 C  CA    . ARG B 560 ? 0.79140 0.75230 0.69020 -0.04000 -0.08990 -0.05150 556 ARG B CA    
7911 C  C     . ARG B 560 ? 0.88390 0.83730 0.77290 -0.03710 -0.08540 -0.06040 556 ARG B C     
7912 O  O     . ARG B 560 ? 0.87280 0.81770 0.76690 -0.03470 -0.08170 -0.06340 556 ARG B O     
7913 C  CB    . ARG B 560 ? 0.74270 0.71080 0.64540 -0.03610 -0.08570 -0.04240 556 ARG B CB    
7914 C  CG    . ARG B 560 ? 0.81150 0.77630 0.72640 -0.03320 -0.08120 -0.03790 556 ARG B CG    
7915 C  CD    . ARG B 560 ? 0.83560 0.80260 0.76320 -0.03640 -0.08520 -0.03270 556 ARG B CD    
7916 N  NE    . ARG B 560 ? 0.86690 0.82800 0.80460 -0.03480 -0.08170 -0.03160 556 ARG B NE    
7917 C  CZ    . ARG B 560 ? 0.87490 0.83740 0.82450 -0.03700 -0.08350 -0.02690 556 ARG B CZ    
7918 N  NH1   . ARG B 560 ? 0.88450 0.85410 0.83850 -0.04060 -0.08890 -0.02300 556 ARG B NH1   
7919 N  NH2   . ARG B 560 ? 0.86630 0.82370 0.82380 -0.03560 -0.08010 -0.02590 556 ARG B NH2   
7920 N  N     . PHE B 561 ? 0.93510 0.89190 0.81010 -0.03710 -0.08560 -0.06460 557 PHE B N     
7921 C  CA    . PHE B 561 ? 0.95350 0.90390 0.81930 -0.03430 -0.08110 -0.07370 557 PHE B CA    
7922 C  C     . PHE B 561 ? 0.96870 0.90840 0.83470 -0.03700 -0.08400 -0.08320 557 PHE B C     
7923 O  O     . PHE B 561 ? 0.99520 0.92580 0.86320 -0.03400 -0.07980 -0.08860 557 PHE B O     
7924 C  CB    . PHE B 561 ? 0.87470 0.83220 0.72500 -0.03420 -0.08070 -0.07580 557 PHE B CB    
7925 C  CG    . PHE B 561 ? 0.82090 0.78620 0.67030 -0.03030 -0.07580 -0.06800 557 PHE B CG    
7926 C  CD1   . PHE B 561 ? 0.76060 0.72320 0.61840 -0.02560 -0.06970 -0.06430 557 PHE B CD1   
7927 C  CD2   . PHE B 561 ? 0.78730 0.76290 0.62750 -0.03160 -0.07760 -0.06410 557 PHE B CD2   
7928 C  CE1   . PHE B 561 ? 0.72790 0.69720 0.58520 -0.02250 -0.06540 -0.05740 557 PHE B CE1   
7929 C  CE2   . PHE B 561 ? 0.72610 0.70820 0.56630 -0.02820 -0.07320 -0.05660 557 PHE B CE2   
7930 C  CZ    . PHE B 561 ? 0.69250 0.67120 0.54120 -0.02370 -0.06710 -0.05350 557 PHE B CZ    
7931 N  N     . ASP B 562 ? 0.93340 0.87420 0.79790 -0.04290 -0.09150 -0.08510 558 ASP B N     
7932 C  CA    . ASP B 562 ? 0.99730 0.92780 0.86220 -0.04650 -0.09520 -0.09410 558 ASP B CA    
7933 C  C     . ASP B 562 ? 0.98680 0.91200 0.86810 -0.04830 -0.09740 -0.09000 558 ASP B C     
7934 O  O     . ASP B 562 ? 0.96130 0.88080 0.85140 -0.04450 -0.09250 -0.08820 558 ASP B O     
7935 C  CB    . ASP B 562 ? 1.01670 0.95120 0.87090 -0.05250 -0.10250 -0.09890 558 ASP B CB    
7936 C  CG    . ASP B 562 ? 1.04560 0.98510 0.88240 -0.05090 -0.10010 -0.10360 558 ASP B CG    
7937 O  OD1   . ASP B 562 ? 1.03770 0.97520 0.87090 -0.04510 -0.09260 -0.10560 558 ASP B OD1   
7938 O  OD2   . ASP B 562 ? 1.03210 0.97820 0.85900 -0.05540 -0.10570 -0.10510 558 ASP B OD2   
7939 P  PB    . ADP C .   ? 0.45000 0.47000 0.42720 -0.05000 -0.00620 0.02710  601 ADP A PB    
7940 O  O1B   . ADP C .   ? 0.28510 0.31270 0.26900 -0.05130 -0.00600 0.03160  601 ADP A O1B   
7941 O  O2B   . ADP C .   ? 0.34550 0.35470 0.31850 -0.05020 -0.00450 0.02360  601 ADP A O2B   
7942 O  O3B   . ADP C .   ? 0.35660 0.37850 0.33080 -0.05350 -0.00920 0.02550  601 ADP A O3B   
7943 P  PA    . ADP C .   ? 0.31220 0.33170 0.28620 -0.03940 -0.00460 0.02620  601 ADP A PA    
7944 O  O1A   . ADP C .   ? 0.31580 0.33490 0.29120 -0.03320 -0.00220 0.02690  601 ADP A O1A   
7945 O  O2A   . ADP C .   ? 0.29860 0.31070 0.26650 -0.04210 -0.00520 0.02190  601 ADP A O2A   
7946 O  O3A   . ADP C .   ? 0.37000 0.39190 0.34780 -0.04290 -0.00430 0.02830  601 ADP A O3A   
7947 O  "O5'" . ADP C .   ? 0.33210 0.36070 0.30950 -0.04040 -0.00740 0.02900  601 ADP A "O5'" 
7948 C  "C5'" . ADP C .   ? 0.34870 0.38480 0.33260 -0.03680 -0.00670 0.03280  601 ADP A "C5'" 
7949 C  "C4'" . ADP C .   ? 0.36580 0.40950 0.35260 -0.03810 -0.00980 0.03560  601 ADP A "C4'" 
7950 O  "O4'" . ADP C .   ? 0.31180 0.36430 0.30670 -0.03540 -0.00940 0.03970  601 ADP A "O4'" 
7951 C  "C3'" . ADP C .   ? 0.30890 0.35030 0.29280 -0.03560 -0.01080 0.03480  601 ADP A "C3'" 
7952 O  "O3'" . ADP C .   ? 0.34660 0.39070 0.32780 -0.04090 -0.01420 0.03500  601 ADP A "O3'" 
7953 C  "C2'" . ADP C .   ? 0.22260 0.26990 0.21350 -0.03040 -0.01040 0.03830  601 ADP A "C2'" 
7954 O  "O2'" . ADP C .   ? 0.34580 0.39610 0.33750 -0.03030 -0.01310 0.04040  601 ADP A "O2'" 
7955 C  "C1'" . ADP C .   ? 0.26540 0.32130 0.26310 -0.03200 -0.01060 0.04170  601 ADP A "C1'" 
7956 N  N9    . ADP C .   ? 0.27110 0.33170 0.27600 -0.02620 -0.00810 0.04400  601 ADP A N9    
7957 C  C8    . ADP C .   ? 0.26810 0.32420 0.27220 -0.02080 -0.00480 0.04190  601 ADP A C8    
7958 N  N7    . ADP C .   ? 0.29580 0.35850 0.30730 -0.01660 -0.00300 0.04440  601 ADP A N7    
7959 C  C5    . ADP C .   ? 0.23270 0.30470 0.25060 -0.01920 -0.00530 0.04850  601 ADP A C5    
7960 C  C6    . ADP C .   ? 0.27190 0.35490 0.30010 -0.01710 -0.00500 0.05300  601 ADP A C6    
7961 N  N6    . ADP C .   ? 0.26730 0.35160 0.29980 -0.01080 -0.00120 0.05260  601 ADP A N6    
7962 N  N1    . ADP C .   ? 0.32720 0.41890 0.36050 -0.02140 -0.00840 0.05720  601 ADP A N1    
7963 C  C2    . ADP C .   ? 0.33320 0.42290 0.36100 -0.02790 -0.01200 0.05660  601 ADP A C2    
7964 N  N3    . ADP C .   ? 0.26630 0.34560 0.28410 -0.03000 -0.01210 0.05210  601 ADP A N3    
7965 C  C4    . ADP C .   ? 0.25790 0.32860 0.27110 -0.02590 -0.00890 0.04830  601 ADP A C4    
7978 N  "N1'" . TPP D .   ? 0.36150 0.29690 0.33670 -0.00770 0.01200  0.01560  602 TPP A "N1'" 
7979 C  "C2'" . TPP D .   ? 0.40720 0.34740 0.37830 -0.00930 0.01080  0.01660  602 TPP A "C2'" 
7980 C  CM2   . TPP D .   ? 0.38930 0.33550 0.35800 -0.00730 0.00930  0.01850  602 TPP A CM2   
7981 N  "N3'" . TPP D .   ? 0.41500 0.35540 0.38470 -0.01260 0.01100  0.01590  602 TPP A "N3'" 
7982 C  "C4'" . TPP D .   ? 0.42220 0.35670 0.39370 -0.01480 0.01210  0.01370  602 TPP A "C4'" 
7983 N  "N4'" . TPP D .   ? 0.39580 0.33090 0.36600 -0.01850 0.01190  0.01310  602 TPP A "N4'" 
7984 C  "C5'" . TPP D .   ? 0.40900 0.33710 0.38430 -0.01320 0.01360  0.01190  602 TPP A "C5'" 
7985 C  "C6'" . TPP D .   ? 0.37650 0.30580 0.35360 -0.00940 0.01350  0.01320  602 TPP A "C6'" 
7986 C  "C7'" . TPP D .   ? 0.39500 0.31540 0.37240 -0.01550 0.01510  0.00860  602 TPP A "C7'" 
7987 N  N3    . TPP D .   ? 0.42100 0.33760 0.40160 -0.01760 0.01460  0.01200  602 TPP A N3    
7988 C  C2    . TPP D .   ? 0.49840 0.41500 0.47760 -0.02190 0.01400  0.01160  602 TPP A C2    
7989 S  S1    . TPP D .   ? 0.48750 0.39960 0.47180 -0.02380 0.01340  0.01680  602 TPP A S1    
7990 C  C5    . TPP D .   ? 0.43100 0.34120 0.41940 -0.01840 0.01390  0.01970  602 TPP A C5    
7991 C  C4    . TPP D .   ? 0.47540 0.38860 0.46140 -0.01550 0.01450  0.01660  602 TPP A C4    
7992 C  CM4   . TPP D .   ? 0.48350 0.39700 0.47230 -0.01090 0.01470  0.01800  602 TPP A CM4   
7993 C  C6    . TPP D .   ? 0.38990 0.29650 0.38390 -0.01760 0.01330  0.02590  602 TPP A C6    
7994 C  C7    . TPP D .   ? 0.40760 0.32200 0.39940 -0.01830 0.01170  0.03220  602 TPP A C7    
7995 O  O7    . TPP D .   ? 0.32850 0.24050 0.32530 -0.01740 0.01100  0.03890  602 TPP A O7    
7996 P  PA    . TPP D .   ? 0.36610 0.28390 0.36200 -0.01930 0.00980  0.04630  602 TPP A PA    
7997 O  O1A   . TPP D .   ? 0.34320 0.25820 0.34430 -0.01790 0.00900  0.05320  602 TPP A O1A   
7998 O  O2A   . TPP D .   ? 0.33800 0.26610 0.32680 -0.01840 0.00920  0.04590  602 TPP A O2A   
7999 O  O3A   . TPP D .   ? 0.37750 0.29160 0.37480 -0.02440 0.01020  0.04500  602 TPP A O3A   
8000 P  PB    . TPP D .   ? 0.39000 0.29380 0.39340 -0.02800 0.01060  0.04450  602 TPP A PB    
8001 O  O1B   . TPP D .   ? 0.42110 0.31710 0.43130 -0.02520 0.01070  0.04740  602 TPP A O1B   
8002 O  O2B   . TPP D .   ? 0.47110 0.37090 0.47240 -0.02960 0.01150  0.03560  602 TPP A O2B   
8003 O  O3B   . TPP D .   ? 0.41180 0.32000 0.41560 -0.03240 0.00980  0.05010  602 TPP A O3B   
8020 MG MG    . MG  E .   ? 0.36150 0.26490 0.37250 -0.02030 0.00910  0.05770  603 MG  A MG    
8021 P  PB    . ADP F .   ? 0.29170 0.30900 0.33830 -0.02260 -0.05610 0.03380  601 ADP B PB    
8022 O  O1B   . ADP F .   ? 0.48000 0.50680 0.53580 -0.02320 -0.05940 0.03890  601 ADP B O1B   
8023 O  O2B   . ADP F .   ? 0.37570 0.38720 0.40990 -0.02140 -0.05720 0.02980  601 ADP B O2B   
8024 O  O3B   . ADP F .   ? 0.34460 0.35820 0.39300 -0.02620 -0.05700 0.03200  601 ADP B O3B   
8025 P  PA    . ADP F .   ? 0.32600 0.33760 0.37100 -0.01740 -0.04300 0.03290  601 ADP B PA    
8026 O  O1A   . ADP F .   ? 0.31000 0.32170 0.35370 -0.01300 -0.03720 0.03350  601 ADP B O1A   
8027 O  O2A   . ADP F .   ? 0.29320 0.29690 0.32960 -0.01930 -0.04530 0.02830  601 ADP B O2A   
8028 O  O3A   . ADP F .   ? 0.38600 0.40350 0.43450 -0.01820 -0.04840 0.03540  601 ADP B O3A   
8029 O  "O5'" . ADP F .   ? 0.30730 0.32370 0.36250 -0.01960 -0.04190 0.03600  601 ADP B "O5'" 
8030 C  "C5'" . ADP F .   ? 0.37720 0.40100 0.44120 -0.01750 -0.03810 0.04000  601 ADP B "C5'" 
8031 C  "C4'" . ADP F .   ? 0.31320 0.34100 0.38540 -0.02020 -0.03690 0.04240  601 ADP B "C4'" 
8032 O  "O4'" . ADP F .   ? 0.32180 0.35860 0.40430 -0.01840 -0.03380 0.04660  601 ADP B "O4'" 
8033 C  "C3'" . ADP F .   ? 0.28040 0.30350 0.34810 -0.02030 -0.03240 0.04080  601 ADP B "C3'" 
8034 O  "O3'" . ADP F .   ? 0.37480 0.39600 0.44450 -0.02480 -0.03620 0.04110  601 ADP B "O3'" 
8035 C  "C2'" . ADP F .   ? 0.28790 0.31740 0.36170 -0.01800 -0.02600 0.04350  601 ADP B "C2'" 
8036 O  "O2'" . ADP F .   ? 0.39310 0.42330 0.46850 -0.02020 -0.02340 0.04470  601 ADP B "O2'" 
8037 C  "C1'" . ADP F .   ? 0.29440 0.33300 0.37940 -0.01820 -0.02800 0.04750  601 ADP B "C1'" 
8038 N  N9    . ADP F .   ? 0.23640 0.28130 0.32740 -0.01420 -0.02230 0.04940  601 ADP B N9    
8039 C  C8    . ADP F .   ? 0.25310 0.29530 0.33980 -0.00980 -0.01760 0.04740  601 ADP B C8    
8040 N  N7    . ADP F .   ? 0.27200 0.32170 0.36780 -0.00690 -0.01300 0.04990  601 ADP B N7    
8041 C  C5    . ADP F .   ? 0.29090 0.34870 0.39710 -0.00950 -0.01500 0.05390  601 ADP B C5    
8042 C  C6    . ADP F .   ? 0.27540 0.34430 0.39510 -0.00860 -0.01230 0.05820  601 ADP B C6    
8043 N  N6    . ADP F .   ? 0.28640 0.35810 0.40970 -0.00370 -0.00620 0.05800  601 ADP B N6    
8044 N  N1    . ADP F .   ? 0.32110 0.39690 0.44960 -0.01260 -0.01600 0.06210  601 ADP B N1    
8045 C  C2    . ADP F .   ? 0.30720 0.37880 0.43180 -0.01760 -0.02210 0.06170  601 ADP B C2    
8046 N  N3    . ADP F .   ? 0.29040 0.35140 0.40250 -0.01830 -0.02470 0.05730  601 ADP B N3    
8047 C  C4    . ADP F .   ? 0.24680 0.30120 0.34970 -0.01450 -0.02140 0.05360  601 ADP B C4    
8060 N  "N1'" . TPP G .   ? 0.36480 0.34390 0.29200 0.00290  -0.02090 0.00480  602 TPP B "N1'" 
8061 C  "C2'" . TPP G .   ? 0.35040 0.32940 0.28440 0.00230  -0.02240 0.00800  602 TPP B "C2'" 
8062 C  CM2   . TPP G .   ? 0.32280 0.30100 0.26210 0.00300  -0.01950 0.01160  602 TPP B CM2   
8063 N  "N3'" . TPP G .   ? 0.34840 0.32800 0.28470 0.00110  -0.02610 0.00810  602 TPP B "N3'" 
8064 C  "C4'" . TPP G .   ? 0.36980 0.34960 0.30090 -0.00000 -0.02900 0.00430  602 TPP B "C4'" 
8065 N  "N4'" . TPP G .   ? 0.35610 0.33670 0.29000 -0.00170 -0.03310 0.00460  602 TPP B "N4'" 
8066 C  "C5'" . TPP G .   ? 0.35440 0.33370 0.27750 0.00060  -0.02760 0.00010  602 TPP B "C5'" 
8067 C  "C6'" . TPP G .   ? 0.37470 0.35390 0.29680 0.00230  -0.02330 0.00080  602 TPP B "C6'" 
8068 C  "C7'" . TPP G .   ? 0.44790 0.42680 0.36450 -0.00050 -0.03050 -0.00500 602 TPP B "C7'" 
8069 N  N3    . TPP G .   ? 0.53560 0.51950 0.44710 -0.00220 -0.03420 -0.00300 602 TPP B N3    
8070 C  C2    . TPP G .   ? 0.54190 0.52690 0.45530 -0.00440 -0.03900 -0.00260 602 TPP B C2    
8071 S  S1    . TPP G .   ? 0.48110 0.47300 0.38750 -0.00620 -0.04290 0.00040  602 TPP B S1    
8072 C  C5    . TPP G .   ? 0.50130 0.49450 0.40180 -0.00380 -0.03740 0.00130  602 TPP B C5    
8073 C  C4    . TPP G .   ? 0.54840 0.53690 0.45270 -0.00180 -0.03310 -0.00090 602 TPP B C4    
8074 C  CM4   . TPP G .   ? 0.55630 0.54490 0.45840 0.00030  -0.02790 -0.00070 602 TPP B CM4   
8075 C  C6    . TPP G .   ? 0.44750 0.44710 0.34030 -0.00440 -0.03810 0.00500  602 TPP B C6    
8076 C  C7    . TPP G .   ? 0.41630 0.41950 0.31550 -0.00460 -0.03980 0.01340  602 TPP B C7    
8077 O  O7    . TPP G .   ? 0.35970 0.36880 0.25210 -0.00510 -0.04000 0.01790  602 TPP B O7    
8078 P  PA    . TPP G .   ? 0.39540 0.40950 0.29200 -0.00570 -0.04310 0.02690  602 TPP B PA    
8079 O  O1A   . TPP G .   ? 0.41360 0.43320 0.30240 -0.00600 -0.04210 0.03100  602 TPP B O1A   
8080 O  O2A   . TPP G .   ? 0.35890 0.36940 0.26850 -0.00400 -0.04150 0.03080  602 TPP B O2A   
8081 O  O3A   . TPP G .   ? 0.35030 0.36750 0.24520 -0.00830 -0.04940 0.02560  602 TPP B O3A   
8082 P  PB    . TPP G .   ? 0.38780 0.40940 0.27150 -0.01120 -0.05420 0.02190  602 TPP B PB    
8083 O  O1B   . TPP G .   ? 0.41460 0.43970 0.28600 -0.01130 -0.05170 0.02080  602 TPP B O1B   
8084 O  O2B   . TPP G .   ? 0.40330 0.41930 0.28720 -0.01200 -0.05490 0.01330  602 TPP B O2B   
8085 O  O3B   . TPP G .   ? 0.44270 0.47030 0.33090 -0.01300 -0.06010 0.02900  602 TPP B O3B   
8102 MG MG    . MG  H .   ? 0.45460 0.48350 0.32760 -0.00920 -0.04680 0.03120  603 MG  B MG    
# 
