data_9II8
# 
_entry.id   9II8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9II8         pdb_00009ii8 10.2210/pdb9ii8/pdb 
WWPDB D_1300048821 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9II8 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8ZEF 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              kaiyingcheng@hznu.edu.cn 
_pdbx_contact_author.name_first         Kaiying 
_pdbx_contact_author.name_last          Cheng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8613-6467 
# 
_audit_author.name               'Cheng, K.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structure of Staphylococcus aureus DinG' 
_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 'Cheng, K.' 1 ? 
primary 'Gao, T.'   2 ? 
primary 'Hao, W.'   3 ? 
# 
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 syn 
;DNA (5'-D(P*TP*TP*TP*T)-3')
;
1171.814   1 ?       ? ? ? 
2 polymer man 
;3'-5' exonuclease DinG
;
104475.500 1 3.1.-.- ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 polydeoxyribonucleotide no no '(DT)(DT)(DT)(DT)' TTTT B ? 
2 'polypeptide(L)'        no no 
;MGMATYAVVDLETTGNQLDFDDIIQIGITFVRNNQIIDTYHSMIRTNLEIPPFIQALTSIEENMLQQAPYFNQVAQEIYD
KIKDCIFVAHNVDFDLNFIKKAFKDCNIQYRPKKVIDTLEIFKIAFPTDKSYQLSELAEAHGITLANAHRADEDAATTAK
LMILAFEKFEKLPLDTLKQLYYLSKQLKYDLYDIFFEMVRQYDAKPLDKFYEKFEQIIYRKQVDFKKPTTNYNGSLKSLY
RKAVDQLGLTYRPQQLYLAETILDQLMHSEKAMIEASLGSGKSLAYLLAALMYNIETGKHVMISTNTKLLQSQLLEKDIP
AMNEALNFKINALLIKSKSDYISLGLISQILKDDTSNYEVNILKMQLLIWITETPSGDIQELNLKGGQKMYFDQKIETYV
PARHDVHYYNFIKRNAQNIQIGITNHAHLIHSDVENSIYQLFDDCIVDEAHRLPDYALNQVTNELSYADIKYQLGLIGKN
ENEKLLKAIDQLEKQRILEKLDIAPIDIFGLKASMNEIHELNEQLFSTIFTIINDSDVYDDDIHRFHNVFTFETKDILKD
LHAIIDKLNKTLEIFNGISHKTVKSLRKQLLYLKDKFKNIEQSLKAGHTSFISIKNLSQKSTIRLYVKDYAVKDVLTKQV
LEKFKSLIFISGTLKFNHSFEAFKQLFNKDVHFNTFEVNTSLQSAKNTSVFIPSDVASYQYKNIDEYVASIVSYIIEYTT
ITSSKCLVLFTSYKMMHMVQDMLNELPEFEDYVVLTQQQNQNYKIVQQFNNFDKAILLGTSTFFEGFDFQANGIKCVMIA
KLPFMNKHNAKYWLMDSEFTSTFKEYVLPDAVTRFRQGLGRLIRNENDRGIIVSFDDRLINSNYKNFFEQTLENYRQKKG
DIQQFGKLLRQIQKKKK
;
;MGMATYAVVDLETTGNQLDFDDIIQIGITFVRNNQIIDTYHSMIRTNLEIPPFIQALTSIEENMLQQAPYFNQVAQEIYD
KIKDCIFVAHNVDFDLNFIKKAFKDCNIQYRPKKVIDTLEIFKIAFPTDKSYQLSELAEAHGITLANAHRADEDAATTAK
LMILAFEKFEKLPLDTLKQLYYLSKQLKYDLYDIFFEMVRQYDAKPLDKFYEKFEQIIYRKQVDFKKPTTNYNGSLKSLY
RKAVDQLGLTYRPQQLYLAETILDQLMHSEKAMIEASLGSGKSLAYLLAALMYNIETGKHVMISTNTKLLQSQLLEKDIP
AMNEALNFKINALLIKSKSDYISLGLISQILKDDTSNYEVNILKMQLLIWITETPSGDIQELNLKGGQKMYFDQKIETYV
PARHDVHYYNFIKRNAQNIQIGITNHAHLIHSDVENSIYQLFDDCIVDEAHRLPDYALNQVTNELSYADIKYQLGLIGKN
ENEKLLKAIDQLEKQRILEKLDIAPIDIFGLKASMNEIHELNEQLFSTIFTIINDSDVYDDDIHRFHNVFTFETKDILKD
LHAIIDKLNKTLEIFNGISHKTVKSLRKQLLYLKDKFKNIEQSLKAGHTSFISIKNLSQKSTIRLYVKDYAVKDVLTKQV
LEKFKSLIFISGTLKFNHSFEAFKQLFNKDVHFNTFEVNTSLQSAKNTSVFIPSDVASYQYKNIDEYVASIVSYIIEYTT
ITSSKCLVLFTSYKMMHMVQDMLNELPEFEDYVVLTQQQNQNYKIVQQFNNFDKAILLGTSTFFEGFDFQANGIKCVMIA
KLPFMNKHNAKYWLMDSEFTSTFKEYVLPDAVTRFRQGLGRLIRNENDRGIIVSFDDRLINSNYKNFFEQTLENYRQKKG
DIQQFGKLLRQIQKKKK
;
A ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   DT  n 
1 2   DT  n 
1 3   DT  n 
1 4   DT  n 
2 1   MET n 
2 2   GLY n 
2 3   MET n 
2 4   ALA n 
2 5   THR n 
2 6   TYR n 
2 7   ALA n 
2 8   VAL n 
2 9   VAL n 
2 10  ASP n 
2 11  LEU n 
2 12  GLU n 
2 13  THR n 
2 14  THR n 
2 15  GLY n 
2 16  ASN n 
2 17  GLN n 
2 18  LEU n 
2 19  ASP n 
2 20  PHE n 
2 21  ASP n 
2 22  ASP n 
2 23  ILE n 
2 24  ILE n 
2 25  GLN n 
2 26  ILE n 
2 27  GLY n 
2 28  ILE n 
2 29  THR n 
2 30  PHE n 
2 31  VAL n 
2 32  ARG n 
2 33  ASN n 
2 34  ASN n 
2 35  GLN n 
2 36  ILE n 
2 37  ILE n 
2 38  ASP n 
2 39  THR n 
2 40  TYR n 
2 41  HIS n 
2 42  SER n 
2 43  MET n 
2 44  ILE n 
2 45  ARG n 
2 46  THR n 
2 47  ASN n 
2 48  LEU n 
2 49  GLU n 
2 50  ILE n 
2 51  PRO n 
2 52  PRO n 
2 53  PHE n 
2 54  ILE n 
2 55  GLN n 
2 56  ALA n 
2 57  LEU n 
2 58  THR n 
2 59  SER n 
2 60  ILE n 
2 61  GLU n 
2 62  GLU n 
2 63  ASN n 
2 64  MET n 
2 65  LEU n 
2 66  GLN n 
2 67  GLN n 
2 68  ALA n 
2 69  PRO n 
2 70  TYR n 
2 71  PHE n 
2 72  ASN n 
2 73  GLN n 
2 74  VAL n 
2 75  ALA n 
2 76  GLN n 
2 77  GLU n 
2 78  ILE n 
2 79  TYR n 
2 80  ASP n 
2 81  LYS n 
2 82  ILE n 
2 83  LYS n 
2 84  ASP n 
2 85  CYS n 
2 86  ILE n 
2 87  PHE n 
2 88  VAL n 
2 89  ALA n 
2 90  HIS n 
2 91  ASN n 
2 92  VAL n 
2 93  ASP n 
2 94  PHE n 
2 95  ASP n 
2 96  LEU n 
2 97  ASN n 
2 98  PHE n 
2 99  ILE n 
2 100 LYS n 
2 101 LYS n 
2 102 ALA n 
2 103 PHE n 
2 104 LYS n 
2 105 ASP n 
2 106 CYS n 
2 107 ASN n 
2 108 ILE n 
2 109 GLN n 
2 110 TYR n 
2 111 ARG n 
2 112 PRO n 
2 113 LYS n 
2 114 LYS n 
2 115 VAL n 
2 116 ILE n 
2 117 ASP n 
2 118 THR n 
2 119 LEU n 
2 120 GLU n 
2 121 ILE n 
2 122 PHE n 
2 123 LYS n 
2 124 ILE n 
2 125 ALA n 
2 126 PHE n 
2 127 PRO n 
2 128 THR n 
2 129 ASP n 
2 130 LYS n 
2 131 SER n 
2 132 TYR n 
2 133 GLN n 
2 134 LEU n 
2 135 SER n 
2 136 GLU n 
2 137 LEU n 
2 138 ALA n 
2 139 GLU n 
2 140 ALA n 
2 141 HIS n 
2 142 GLY n 
2 143 ILE n 
2 144 THR n 
2 145 LEU n 
2 146 ALA n 
2 147 ASN n 
2 148 ALA n 
2 149 HIS n 
2 150 ARG n 
2 151 ALA n 
2 152 ASP n 
2 153 GLU n 
2 154 ASP n 
2 155 ALA n 
2 156 ALA n 
2 157 THR n 
2 158 THR n 
2 159 ALA n 
2 160 LYS n 
2 161 LEU n 
2 162 MET n 
2 163 ILE n 
2 164 LEU n 
2 165 ALA n 
2 166 PHE n 
2 167 GLU n 
2 168 LYS n 
2 169 PHE n 
2 170 GLU n 
2 171 LYS n 
2 172 LEU n 
2 173 PRO n 
2 174 LEU n 
2 175 ASP n 
2 176 THR n 
2 177 LEU n 
2 178 LYS n 
2 179 GLN n 
2 180 LEU n 
2 181 TYR n 
2 182 TYR n 
2 183 LEU n 
2 184 SER n 
2 185 LYS n 
2 186 GLN n 
2 187 LEU n 
2 188 LYS n 
2 189 TYR n 
2 190 ASP n 
2 191 LEU n 
2 192 TYR n 
2 193 ASP n 
2 194 ILE n 
2 195 PHE n 
2 196 PHE n 
2 197 GLU n 
2 198 MET n 
2 199 VAL n 
2 200 ARG n 
2 201 GLN n 
2 202 TYR n 
2 203 ASP n 
2 204 ALA n 
2 205 LYS n 
2 206 PRO n 
2 207 LEU n 
2 208 ASP n 
2 209 LYS n 
2 210 PHE n 
2 211 TYR n 
2 212 GLU n 
2 213 LYS n 
2 214 PHE n 
2 215 GLU n 
2 216 GLN n 
2 217 ILE n 
2 218 ILE n 
2 219 TYR n 
2 220 ARG n 
2 221 LYS n 
2 222 GLN n 
2 223 VAL n 
2 224 ASP n 
2 225 PHE n 
2 226 LYS n 
2 227 LYS n 
2 228 PRO n 
2 229 THR n 
2 230 THR n 
2 231 ASN n 
2 232 TYR n 
2 233 ASN n 
2 234 GLY n 
2 235 SER n 
2 236 LEU n 
2 237 LYS n 
2 238 SER n 
2 239 LEU n 
2 240 TYR n 
2 241 ARG n 
2 242 LYS n 
2 243 ALA n 
2 244 VAL n 
2 245 ASP n 
2 246 GLN n 
2 247 LEU n 
2 248 GLY n 
2 249 LEU n 
2 250 THR n 
2 251 TYR n 
2 252 ARG n 
2 253 PRO n 
2 254 GLN n 
2 255 GLN n 
2 256 LEU n 
2 257 TYR n 
2 258 LEU n 
2 259 ALA n 
2 260 GLU n 
2 261 THR n 
2 262 ILE n 
2 263 LEU n 
2 264 ASP n 
2 265 GLN n 
2 266 LEU n 
2 267 MET n 
2 268 HIS n 
2 269 SER n 
2 270 GLU n 
2 271 LYS n 
2 272 ALA n 
2 273 MET n 
2 274 ILE n 
2 275 GLU n 
2 276 ALA n 
2 277 SER n 
2 278 LEU n 
2 279 GLY n 
2 280 SER n 
2 281 GLY n 
2 282 LYS n 
2 283 SER n 
2 284 LEU n 
2 285 ALA n 
2 286 TYR n 
2 287 LEU n 
2 288 LEU n 
2 289 ALA n 
2 290 ALA n 
2 291 LEU n 
2 292 MET n 
2 293 TYR n 
2 294 ASN n 
2 295 ILE n 
2 296 GLU n 
2 297 THR n 
2 298 GLY n 
2 299 LYS n 
2 300 HIS n 
2 301 VAL n 
2 302 MET n 
2 303 ILE n 
2 304 SER n 
2 305 THR n 
2 306 ASN n 
2 307 THR n 
2 308 LYS n 
2 309 LEU n 
2 310 LEU n 
2 311 GLN n 
2 312 SER n 
2 313 GLN n 
2 314 LEU n 
2 315 LEU n 
2 316 GLU n 
2 317 LYS n 
2 318 ASP n 
2 319 ILE n 
2 320 PRO n 
2 321 ALA n 
2 322 MET n 
2 323 ASN n 
2 324 GLU n 
2 325 ALA n 
2 326 LEU n 
2 327 ASN n 
2 328 PHE n 
2 329 LYS n 
2 330 ILE n 
2 331 ASN n 
2 332 ALA n 
2 333 LEU n 
2 334 LEU n 
2 335 ILE n 
2 336 LYS n 
2 337 SER n 
2 338 LYS n 
2 339 SER n 
2 340 ASP n 
2 341 TYR n 
2 342 ILE n 
2 343 SER n 
2 344 LEU n 
2 345 GLY n 
2 346 LEU n 
2 347 ILE n 
2 348 SER n 
2 349 GLN n 
2 350 ILE n 
2 351 LEU n 
2 352 LYS n 
2 353 ASP n 
2 354 ASP n 
2 355 THR n 
2 356 SER n 
2 357 ASN n 
2 358 TYR n 
2 359 GLU n 
2 360 VAL n 
2 361 ASN n 
2 362 ILE n 
2 363 LEU n 
2 364 LYS n 
2 365 MET n 
2 366 GLN n 
2 367 LEU n 
2 368 LEU n 
2 369 ILE n 
2 370 TRP n 
2 371 ILE n 
2 372 THR n 
2 373 GLU n 
2 374 THR n 
2 375 PRO n 
2 376 SER n 
2 377 GLY n 
2 378 ASP n 
2 379 ILE n 
2 380 GLN n 
2 381 GLU n 
2 382 LEU n 
2 383 ASN n 
2 384 LEU n 
2 385 LYS n 
2 386 GLY n 
2 387 GLY n 
2 388 GLN n 
2 389 LYS n 
2 390 MET n 
2 391 TYR n 
2 392 PHE n 
2 393 ASP n 
2 394 GLN n 
2 395 LYS n 
2 396 ILE n 
2 397 GLU n 
2 398 THR n 
2 399 TYR n 
2 400 VAL n 
2 401 PRO n 
2 402 ALA n 
2 403 ARG n 
2 404 HIS n 
2 405 ASP n 
2 406 VAL n 
2 407 HIS n 
2 408 TYR n 
2 409 TYR n 
2 410 ASN n 
2 411 PHE n 
2 412 ILE n 
2 413 LYS n 
2 414 ARG n 
2 415 ASN n 
2 416 ALA n 
2 417 GLN n 
2 418 ASN n 
2 419 ILE n 
2 420 GLN n 
2 421 ILE n 
2 422 GLY n 
2 423 ILE n 
2 424 THR n 
2 425 ASN n 
2 426 HIS n 
2 427 ALA n 
2 428 HIS n 
2 429 LEU n 
2 430 ILE n 
2 431 HIS n 
2 432 SER n 
2 433 ASP n 
2 434 VAL n 
2 435 GLU n 
2 436 ASN n 
2 437 SER n 
2 438 ILE n 
2 439 TYR n 
2 440 GLN n 
2 441 LEU n 
2 442 PHE n 
2 443 ASP n 
2 444 ASP n 
2 445 CYS n 
2 446 ILE n 
2 447 VAL n 
2 448 ASP n 
2 449 GLU n 
2 450 ALA n 
2 451 HIS n 
2 452 ARG n 
2 453 LEU n 
2 454 PRO n 
2 455 ASP n 
2 456 TYR n 
2 457 ALA n 
2 458 LEU n 
2 459 ASN n 
2 460 GLN n 
2 461 VAL n 
2 462 THR n 
2 463 ASN n 
2 464 GLU n 
2 465 LEU n 
2 466 SER n 
2 467 TYR n 
2 468 ALA n 
2 469 ASP n 
2 470 ILE n 
2 471 LYS n 
2 472 TYR n 
2 473 GLN n 
2 474 LEU n 
2 475 GLY n 
2 476 LEU n 
2 477 ILE n 
2 478 GLY n 
2 479 LYS n 
2 480 ASN n 
2 481 GLU n 
2 482 ASN n 
2 483 GLU n 
2 484 LYS n 
2 485 LEU n 
2 486 LEU n 
2 487 LYS n 
2 488 ALA n 
2 489 ILE n 
2 490 ASP n 
2 491 GLN n 
2 492 LEU n 
2 493 GLU n 
2 494 LYS n 
2 495 GLN n 
2 496 ARG n 
2 497 ILE n 
2 498 LEU n 
2 499 GLU n 
2 500 LYS n 
2 501 LEU n 
2 502 ASP n 
2 503 ILE n 
2 504 ALA n 
2 505 PRO n 
2 506 ILE n 
2 507 ASP n 
2 508 ILE n 
2 509 PHE n 
2 510 GLY n 
2 511 LEU n 
2 512 LYS n 
2 513 ALA n 
2 514 SER n 
2 515 MET n 
2 516 ASN n 
2 517 GLU n 
2 518 ILE n 
2 519 HIS n 
2 520 GLU n 
2 521 LEU n 
2 522 ASN n 
2 523 GLU n 
2 524 GLN n 
2 525 LEU n 
2 526 PHE n 
2 527 SER n 
2 528 THR n 
2 529 ILE n 
2 530 PHE n 
2 531 THR n 
2 532 ILE n 
2 533 ILE n 
2 534 ASN n 
2 535 ASP n 
2 536 SER n 
2 537 ASP n 
2 538 VAL n 
2 539 TYR n 
2 540 ASP n 
2 541 ASP n 
2 542 ASP n 
2 543 ILE n 
2 544 HIS n 
2 545 ARG n 
2 546 PHE n 
2 547 HIS n 
2 548 ASN n 
2 549 VAL n 
2 550 PHE n 
2 551 THR n 
2 552 PHE n 
2 553 GLU n 
2 554 THR n 
2 555 LYS n 
2 556 ASP n 
2 557 ILE n 
2 558 LEU n 
2 559 LYS n 
2 560 ASP n 
2 561 LEU n 
2 562 HIS n 
2 563 ALA n 
2 564 ILE n 
2 565 ILE n 
2 566 ASP n 
2 567 LYS n 
2 568 LEU n 
2 569 ASN n 
2 570 LYS n 
2 571 THR n 
2 572 LEU n 
2 573 GLU n 
2 574 ILE n 
2 575 PHE n 
2 576 ASN n 
2 577 GLY n 
2 578 ILE n 
2 579 SER n 
2 580 HIS n 
2 581 LYS n 
2 582 THR n 
2 583 VAL n 
2 584 LYS n 
2 585 SER n 
2 586 LEU n 
2 587 ARG n 
2 588 LYS n 
2 589 GLN n 
2 590 LEU n 
2 591 LEU n 
2 592 TYR n 
2 593 LEU n 
2 594 LYS n 
2 595 ASP n 
2 596 LYS n 
2 597 PHE n 
2 598 LYS n 
2 599 ASN n 
2 600 ILE n 
2 601 GLU n 
2 602 GLN n 
2 603 SER n 
2 604 LEU n 
2 605 LYS n 
2 606 ALA n 
2 607 GLY n 
2 608 HIS n 
2 609 THR n 
2 610 SER n 
2 611 PHE n 
2 612 ILE n 
2 613 SER n 
2 614 ILE n 
2 615 LYS n 
2 616 ASN n 
2 617 LEU n 
2 618 SER n 
2 619 GLN n 
2 620 LYS n 
2 621 SER n 
2 622 THR n 
2 623 ILE n 
2 624 ARG n 
2 625 LEU n 
2 626 TYR n 
2 627 VAL n 
2 628 LYS n 
2 629 ASP n 
2 630 TYR n 
2 631 ALA n 
2 632 VAL n 
2 633 LYS n 
2 634 ASP n 
2 635 VAL n 
2 636 LEU n 
2 637 THR n 
2 638 LYS n 
2 639 GLN n 
2 640 VAL n 
2 641 LEU n 
2 642 GLU n 
2 643 LYS n 
2 644 PHE n 
2 645 LYS n 
2 646 SER n 
2 647 LEU n 
2 648 ILE n 
2 649 PHE n 
2 650 ILE n 
2 651 SER n 
2 652 GLY n 
2 653 THR n 
2 654 LEU n 
2 655 LYS n 
2 656 PHE n 
2 657 ASN n 
2 658 HIS n 
2 659 SER n 
2 660 PHE n 
2 661 GLU n 
2 662 ALA n 
2 663 PHE n 
2 664 LYS n 
2 665 GLN n 
2 666 LEU n 
2 667 PHE n 
2 668 ASN n 
2 669 LYS n 
2 670 ASP n 
2 671 VAL n 
2 672 HIS n 
2 673 PHE n 
2 674 ASN n 
2 675 THR n 
2 676 PHE n 
2 677 GLU n 
2 678 VAL n 
2 679 ASN n 
2 680 THR n 
2 681 SER n 
2 682 LEU n 
2 683 GLN n 
2 684 SER n 
2 685 ALA n 
2 686 LYS n 
2 687 ASN n 
2 688 THR n 
2 689 SER n 
2 690 VAL n 
2 691 PHE n 
2 692 ILE n 
2 693 PRO n 
2 694 SER n 
2 695 ASP n 
2 696 VAL n 
2 697 ALA n 
2 698 SER n 
2 699 TYR n 
2 700 GLN n 
2 701 TYR n 
2 702 LYS n 
2 703 ASN n 
2 704 ILE n 
2 705 ASP n 
2 706 GLU n 
2 707 TYR n 
2 708 VAL n 
2 709 ALA n 
2 710 SER n 
2 711 ILE n 
2 712 VAL n 
2 713 SER n 
2 714 TYR n 
2 715 ILE n 
2 716 ILE n 
2 717 GLU n 
2 718 TYR n 
2 719 THR n 
2 720 THR n 
2 721 ILE n 
2 722 THR n 
2 723 SER n 
2 724 SER n 
2 725 LYS n 
2 726 CYS n 
2 727 LEU n 
2 728 VAL n 
2 729 LEU n 
2 730 PHE n 
2 731 THR n 
2 732 SER n 
2 733 TYR n 
2 734 LYS n 
2 735 MET n 
2 736 MET n 
2 737 HIS n 
2 738 MET n 
2 739 VAL n 
2 740 GLN n 
2 741 ASP n 
2 742 MET n 
2 743 LEU n 
2 744 ASN n 
2 745 GLU n 
2 746 LEU n 
2 747 PRO n 
2 748 GLU n 
2 749 PHE n 
2 750 GLU n 
2 751 ASP n 
2 752 TYR n 
2 753 VAL n 
2 754 VAL n 
2 755 LEU n 
2 756 THR n 
2 757 GLN n 
2 758 GLN n 
2 759 GLN n 
2 760 ASN n 
2 761 GLN n 
2 762 ASN n 
2 763 TYR n 
2 764 LYS n 
2 765 ILE n 
2 766 VAL n 
2 767 GLN n 
2 768 GLN n 
2 769 PHE n 
2 770 ASN n 
2 771 ASN n 
2 772 PHE n 
2 773 ASP n 
2 774 LYS n 
2 775 ALA n 
2 776 ILE n 
2 777 LEU n 
2 778 LEU n 
2 779 GLY n 
2 780 THR n 
2 781 SER n 
2 782 THR n 
2 783 PHE n 
2 784 PHE n 
2 785 GLU n 
2 786 GLY n 
2 787 PHE n 
2 788 ASP n 
2 789 PHE n 
2 790 GLN n 
2 791 ALA n 
2 792 ASN n 
2 793 GLY n 
2 794 ILE n 
2 795 LYS n 
2 796 CYS n 
2 797 VAL n 
2 798 MET n 
2 799 ILE n 
2 800 ALA n 
2 801 LYS n 
2 802 LEU n 
2 803 PRO n 
2 804 PHE n 
2 805 MET n 
2 806 ASN n 
2 807 LYS n 
2 808 HIS n 
2 809 ASN n 
2 810 ALA n 
2 811 LYS n 
2 812 TYR n 
2 813 TRP n 
2 814 LEU n 
2 815 MET n 
2 816 ASP n 
2 817 SER n 
2 818 GLU n 
2 819 PHE n 
2 820 THR n 
2 821 SER n 
2 822 THR n 
2 823 PHE n 
2 824 LYS n 
2 825 GLU n 
2 826 TYR n 
2 827 VAL n 
2 828 LEU n 
2 829 PRO n 
2 830 ASP n 
2 831 ALA n 
2 832 VAL n 
2 833 THR n 
2 834 ARG n 
2 835 PHE n 
2 836 ARG n 
2 837 GLN n 
2 838 GLY n 
2 839 LEU n 
2 840 GLY n 
2 841 ARG n 
2 842 LEU n 
2 843 ILE n 
2 844 ARG n 
2 845 ASN n 
2 846 GLU n 
2 847 ASN n 
2 848 ASP n 
2 849 ARG n 
2 850 GLY n 
2 851 ILE n 
2 852 ILE n 
2 853 VAL n 
2 854 SER n 
2 855 PHE n 
2 856 ASP n 
2 857 ASP n 
2 858 ARG n 
2 859 LEU n 
2 860 ILE n 
2 861 ASN n 
2 862 SER n 
2 863 ASN n 
2 864 TYR n 
2 865 LYS n 
2 866 ASN n 
2 867 PHE n 
2 868 PHE n 
2 869 GLU n 
2 870 GLN n 
2 871 THR n 
2 872 LEU n 
2 873 GLU n 
2 874 ASN n 
2 875 TYR n 
2 876 ARG n 
2 877 GLN n 
2 878 LYS n 
2 879 LYS n 
2 880 GLY n 
2 881 ASP n 
2 882 ILE n 
2 883 GLN n 
2 884 GLN n 
2 885 PHE n 
2 886 GLY n 
2 887 LYS n 
2 888 LEU n 
2 889 LEU n 
2 890 ARG n 
2 891 GLN n 
2 892 ILE n 
2 893 GLN n 
2 894 LYS n 
2 895 LYS n 
2 896 LYS n 
2 897 LYS n 
# 
_entity_src_gen.entity_id                          2 
_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                   897 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'dinG, SAOUHSC_01472' 
_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      'Staphylococcus aureus (strain NCTC 8325 / PS 47)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     93061 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              1 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       4 
_pdbx_entity_src_syn.organism_scientific    'Escherichia coli' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       562 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                      ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                     ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                   ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'              ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                     ? 'C3 H7 N O2 S'    121.158 
DT  'DNA linking'       y "THYMIDINE-5'-MONOPHOSPHATE" ? 'C10 H15 N2 O8 P' 322.208 
GLN 'L-peptide linking' y GLUTAMINE                    ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'              ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                      ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                    ? 'C6 H10 N3 O2 1'  156.162 
ILE 'L-peptide linking' y ISOLEUCINE                   ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                      ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                       ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                   ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE                ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                      ? 'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                       ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                    ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                   ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                     ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                       ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   DT  1   2   2   DT  DT  B . n 
A 1 2   DT  2   3   3   DT  DT  B . n 
A 1 3   DT  3   4   4   DT  DT  B . n 
A 1 4   DT  4   5   5   DT  DT  B . n 
B 2 1   MET 1   1   1   MET MET A . n 
B 2 2   GLY 2   2   2   GLY GLY A . n 
B 2 3   MET 3   3   3   MET MET A . n 
B 2 4   ALA 4   4   4   ALA ALA A . n 
B 2 5   THR 5   5   5   THR THR A . n 
B 2 6   TYR 6   6   6   TYR TYR A . n 
B 2 7   ALA 7   7   7   ALA ALA A . n 
B 2 8   VAL 8   8   8   VAL VAL A . n 
B 2 9   VAL 9   9   9   VAL VAL A . n 
B 2 10  ASP 10  10  10  ASP ASP A . n 
B 2 11  LEU 11  11  11  LEU LEU A . n 
B 2 12  GLU 12  12  12  GLU GLU A . n 
B 2 13  THR 13  13  13  THR THR A . n 
B 2 14  THR 14  14  14  THR THR A . n 
B 2 15  GLY 15  15  15  GLY GLY A . n 
B 2 16  ASN 16  16  16  ASN ASN A . n 
B 2 17  GLN 17  17  17  GLN GLN A . n 
B 2 18  LEU 18  18  18  LEU LEU A . n 
B 2 19  ASP 19  19  19  ASP ASP A . n 
B 2 20  PHE 20  20  20  PHE PHE A . n 
B 2 21  ASP 21  21  21  ASP ASP A . n 
B 2 22  ASP 22  22  22  ASP ASP A . n 
B 2 23  ILE 23  23  23  ILE ILE A . n 
B 2 24  ILE 24  24  24  ILE ILE A . n 
B 2 25  GLN 25  25  25  GLN GLN A . n 
B 2 26  ILE 26  26  26  ILE ILE A . n 
B 2 27  GLY 27  27  27  GLY GLY A . n 
B 2 28  ILE 28  28  28  ILE ILE A . n 
B 2 29  THR 29  29  29  THR THR A . n 
B 2 30  PHE 30  30  30  PHE PHE A . n 
B 2 31  VAL 31  31  31  VAL VAL A . n 
B 2 32  ARG 32  32  32  ARG ARG A . n 
B 2 33  ASN 33  33  33  ASN ASN A . n 
B 2 34  ASN 34  34  34  ASN ASN A . n 
B 2 35  GLN 35  35  35  GLN GLN A . n 
B 2 36  ILE 36  36  36  ILE ILE A . n 
B 2 37  ILE 37  37  37  ILE ILE A . n 
B 2 38  ASP 38  38  38  ASP ASP A . n 
B 2 39  THR 39  39  39  THR THR A . n 
B 2 40  TYR 40  40  40  TYR TYR A . n 
B 2 41  HIS 41  41  41  HIS HIS A . n 
B 2 42  SER 42  42  42  SER SER A . n 
B 2 43  MET 43  43  43  MET MET A . n 
B 2 44  ILE 44  44  44  ILE ILE A . n 
B 2 45  ARG 45  45  45  ARG ARG A . n 
B 2 46  THR 46  46  46  THR THR A . n 
B 2 47  ASN 47  47  47  ASN ASN A . n 
B 2 48  LEU 48  48  48  LEU LEU A . n 
B 2 49  GLU 49  49  49  GLU GLU A . n 
B 2 50  ILE 50  50  50  ILE ILE A . n 
B 2 51  PRO 51  51  51  PRO PRO A . n 
B 2 52  PRO 52  52  52  PRO PRO A . n 
B 2 53  PHE 53  53  53  PHE PHE A . n 
B 2 54  ILE 54  54  54  ILE ILE A . n 
B 2 55  GLN 55  55  55  GLN GLN A . n 
B 2 56  ALA 56  56  56  ALA ALA A . n 
B 2 57  LEU 57  57  57  LEU LEU A . n 
B 2 58  THR 58  58  58  THR THR A . n 
B 2 59  SER 59  59  59  SER SER A . n 
B 2 60  ILE 60  60  60  ILE ILE A . n 
B 2 61  GLU 61  61  61  GLU GLU A . n 
B 2 62  GLU 62  62  62  GLU GLU A . n 
B 2 63  ASN 63  63  63  ASN ASN A . n 
B 2 64  MET 64  64  64  MET MET A . n 
B 2 65  LEU 65  65  65  LEU LEU A . n 
B 2 66  GLN 66  66  66  GLN GLN A . n 
B 2 67  GLN 67  67  67  GLN GLN A . n 
B 2 68  ALA 68  68  68  ALA ALA A . n 
B 2 69  PRO 69  69  69  PRO PRO A . n 
B 2 70  TYR 70  70  70  TYR TYR A . n 
B 2 71  PHE 71  71  71  PHE PHE A . n 
B 2 72  ASN 72  72  72  ASN ASN A . n 
B 2 73  GLN 73  73  73  GLN GLN A . n 
B 2 74  VAL 74  74  74  VAL VAL A . n 
B 2 75  ALA 75  75  75  ALA ALA A . n 
B 2 76  GLN 76  76  76  GLN GLN A . n 
B 2 77  GLU 77  77  77  GLU GLU A . n 
B 2 78  ILE 78  78  78  ILE ILE A . n 
B 2 79  TYR 79  79  79  TYR TYR A . n 
B 2 80  ASP 80  80  80  ASP ASP A . n 
B 2 81  LYS 81  81  81  LYS LYS A . n 
B 2 82  ILE 82  82  82  ILE ILE A . n 
B 2 83  LYS 83  83  83  LYS LYS A . n 
B 2 84  ASP 84  84  84  ASP ASP A . n 
B 2 85  CYS 85  85  85  CYS CYS A . n 
B 2 86  ILE 86  86  86  ILE ILE A . n 
B 2 87  PHE 87  87  87  PHE PHE A . n 
B 2 88  VAL 88  88  88  VAL VAL A . n 
B 2 89  ALA 89  89  89  ALA ALA A . n 
B 2 90  HIS 90  90  90  HIS HIS A . n 
B 2 91  ASN 91  91  91  ASN ASN A . n 
B 2 92  VAL 92  92  92  VAL VAL A . n 
B 2 93  ASP 93  93  93  ASP ASP A . n 
B 2 94  PHE 94  94  94  PHE PHE A . n 
B 2 95  ASP 95  95  95  ASP ASP A . n 
B 2 96  LEU 96  96  96  LEU LEU A . n 
B 2 97  ASN 97  97  97  ASN ASN A . n 
B 2 98  PHE 98  98  98  PHE PHE A . n 
B 2 99  ILE 99  99  99  ILE ILE A . n 
B 2 100 LYS 100 100 100 LYS LYS A . n 
B 2 101 LYS 101 101 101 LYS LYS A . n 
B 2 102 ALA 102 102 102 ALA ALA A . n 
B 2 103 PHE 103 103 103 PHE PHE A . n 
B 2 104 LYS 104 104 104 LYS LYS A . n 
B 2 105 ASP 105 105 105 ASP ASP A . n 
B 2 106 CYS 106 106 106 CYS CYS A . n 
B 2 107 ASN 107 107 107 ASN ASN A . n 
B 2 108 ILE 108 108 108 ILE ILE A . n 
B 2 109 GLN 109 109 109 GLN GLN A . n 
B 2 110 TYR 110 110 110 TYR TYR A . n 
B 2 111 ARG 111 111 111 ARG ARG A . n 
B 2 112 PRO 112 112 112 PRO PRO A . n 
B 2 113 LYS 113 113 113 LYS LYS A . n 
B 2 114 LYS 114 114 114 LYS LYS A . n 
B 2 115 VAL 115 115 115 VAL VAL A . n 
B 2 116 ILE 116 116 116 ILE ILE A . n 
B 2 117 ASP 117 117 117 ASP ASP A . n 
B 2 118 THR 118 118 118 THR THR A . n 
B 2 119 LEU 119 119 119 LEU LEU A . n 
B 2 120 GLU 120 120 120 GLU GLU A . n 
B 2 121 ILE 121 121 121 ILE ILE A . n 
B 2 122 PHE 122 122 122 PHE PHE A . n 
B 2 123 LYS 123 123 123 LYS LYS A . n 
B 2 124 ILE 124 124 124 ILE ILE A . n 
B 2 125 ALA 125 125 125 ALA ALA A . n 
B 2 126 PHE 126 126 126 PHE PHE A . n 
B 2 127 PRO 127 127 127 PRO PRO A . n 
B 2 128 THR 128 128 128 THR THR A . n 
B 2 129 ASP 129 129 129 ASP ASP A . n 
B 2 130 LYS 130 130 130 LYS LYS A . n 
B 2 131 SER 131 131 131 SER SER A . n 
B 2 132 TYR 132 132 132 TYR TYR A . n 
B 2 133 GLN 133 133 133 GLN GLN A . n 
B 2 134 LEU 134 134 134 LEU LEU A . n 
B 2 135 SER 135 135 135 SER SER A . n 
B 2 136 GLU 136 136 136 GLU GLU A . n 
B 2 137 LEU 137 137 137 LEU LEU A . n 
B 2 138 ALA 138 138 138 ALA ALA A . n 
B 2 139 GLU 139 139 139 GLU GLU A . n 
B 2 140 ALA 140 140 140 ALA ALA A . n 
B 2 141 HIS 141 141 141 HIS HIS A . n 
B 2 142 GLY 142 142 142 GLY GLY A . n 
B 2 143 ILE 143 143 143 ILE ILE A . n 
B 2 144 THR 144 144 144 THR THR A . n 
B 2 145 LEU 145 145 145 LEU LEU A . n 
B 2 146 ALA 146 146 146 ALA ALA A . n 
B 2 147 ASN 147 147 147 ASN ASN A . n 
B 2 148 ALA 148 148 148 ALA ALA A . n 
B 2 149 HIS 149 149 149 HIS HIS A . n 
B 2 150 ARG 150 150 150 ARG ARG A . n 
B 2 151 ALA 151 151 151 ALA ALA A . n 
B 2 152 ASP 152 152 152 ASP ASP A . n 
B 2 153 GLU 153 153 153 GLU GLU A . n 
B 2 154 ASP 154 154 154 ASP ASP A . n 
B 2 155 ALA 155 155 155 ALA ALA A . n 
B 2 156 ALA 156 156 156 ALA ALA A . n 
B 2 157 THR 157 157 157 THR THR A . n 
B 2 158 THR 158 158 158 THR THR A . n 
B 2 159 ALA 159 159 159 ALA ALA A . n 
B 2 160 LYS 160 160 160 LYS LYS A . n 
B 2 161 LEU 161 161 161 LEU LEU A . n 
B 2 162 MET 162 162 162 MET MET A . n 
B 2 163 ILE 163 163 163 ILE ILE A . n 
B 2 164 LEU 164 164 164 LEU LEU A . n 
B 2 165 ALA 165 165 165 ALA ALA A . n 
B 2 166 PHE 166 166 166 PHE PHE A . n 
B 2 167 GLU 167 167 167 GLU GLU A . n 
B 2 168 LYS 168 168 168 LYS LYS A . n 
B 2 169 PHE 169 169 169 PHE PHE A . n 
B 2 170 GLU 170 170 170 GLU GLU A . n 
B 2 171 LYS 171 171 171 LYS LYS A . n 
B 2 172 LEU 172 172 172 LEU LEU A . n 
B 2 173 PRO 173 173 173 PRO PRO A . n 
B 2 174 LEU 174 174 174 LEU LEU A . n 
B 2 175 ASP 175 175 175 ASP ASP A . n 
B 2 176 THR 176 176 176 THR THR A . n 
B 2 177 LEU 177 177 177 LEU LEU A . n 
B 2 178 LYS 178 178 178 LYS LYS A . n 
B 2 179 GLN 179 179 179 GLN GLN A . n 
B 2 180 LEU 180 180 180 LEU LEU A . n 
B 2 181 TYR 181 181 181 TYR TYR A . n 
B 2 182 TYR 182 182 182 TYR TYR A . n 
B 2 183 LEU 183 183 183 LEU LEU A . n 
B 2 184 SER 184 184 184 SER SER A . n 
B 2 185 LYS 185 185 185 LYS LYS A . n 
B 2 186 GLN 186 186 186 GLN GLN A . n 
B 2 187 LEU 187 187 187 LEU LEU A . n 
B 2 188 LYS 188 188 188 LYS LYS A . n 
B 2 189 TYR 189 189 189 TYR TYR A . n 
B 2 190 ASP 190 190 190 ASP ASP A . n 
B 2 191 LEU 191 191 191 LEU LEU A . n 
B 2 192 TYR 192 192 192 TYR TYR A . n 
B 2 193 ASP 193 193 193 ASP ASP A . n 
B 2 194 ILE 194 194 194 ILE ILE A . n 
B 2 195 PHE 195 195 195 PHE PHE A . n 
B 2 196 PHE 196 196 196 PHE PHE A . n 
B 2 197 GLU 197 197 197 GLU GLU A . n 
B 2 198 MET 198 198 198 MET MET A . n 
B 2 199 VAL 199 199 199 VAL VAL A . n 
B 2 200 ARG 200 200 200 ARG ARG A . n 
B 2 201 GLN 201 201 201 GLN GLN A . n 
B 2 202 TYR 202 202 202 TYR TYR A . n 
B 2 203 ASP 203 203 203 ASP ASP A . n 
B 2 204 ALA 204 204 204 ALA ALA A . n 
B 2 205 LYS 205 205 205 LYS LYS A . n 
B 2 206 PRO 206 206 206 PRO PRO A . n 
B 2 207 LEU 207 207 207 LEU LEU A . n 
B 2 208 ASP 208 208 208 ASP ASP A . n 
B 2 209 LYS 209 209 209 LYS LYS A . n 
B 2 210 PHE 210 210 210 PHE PHE A . n 
B 2 211 TYR 211 211 211 TYR TYR A . n 
B 2 212 GLU 212 212 212 GLU GLU A . n 
B 2 213 LYS 213 213 213 LYS LYS A . n 
B 2 214 PHE 214 214 214 PHE PHE A . n 
B 2 215 GLU 215 215 215 GLU GLU A . n 
B 2 216 GLN 216 216 216 GLN GLN A . n 
B 2 217 ILE 217 217 217 ILE ILE A . n 
B 2 218 ILE 218 218 218 ILE ILE A . n 
B 2 219 TYR 219 219 219 TYR TYR A . n 
B 2 220 ARG 220 220 220 ARG ARG A . n 
B 2 221 LYS 221 221 221 LYS LYS A . n 
B 2 222 GLN 222 222 222 GLN GLN A . n 
B 2 223 VAL 223 223 223 VAL VAL A . n 
B 2 224 ASP 224 224 224 ASP ASP A . n 
B 2 225 PHE 225 225 225 PHE PHE A . n 
B 2 226 LYS 226 226 226 LYS LYS A . n 
B 2 227 LYS 227 227 227 LYS LYS A . n 
B 2 228 PRO 228 228 228 PRO PRO A . n 
B 2 229 THR 229 229 229 THR THR A . n 
B 2 230 THR 230 230 230 THR THR A . n 
B 2 231 ASN 231 231 231 ASN ASN A . n 
B 2 232 TYR 232 232 232 TYR TYR A . n 
B 2 233 ASN 233 233 233 ASN ASN A . n 
B 2 234 GLY 234 234 234 GLY GLY A . n 
B 2 235 SER 235 235 235 SER SER A . n 
B 2 236 LEU 236 236 236 LEU LEU A . n 
B 2 237 LYS 237 237 237 LYS LYS A . n 
B 2 238 SER 238 238 238 SER SER A . n 
B 2 239 LEU 239 239 239 LEU LEU A . n 
B 2 240 TYR 240 240 240 TYR TYR A . n 
B 2 241 ARG 241 241 241 ARG ARG A . n 
B 2 242 LYS 242 242 242 LYS LYS A . n 
B 2 243 ALA 243 243 243 ALA ALA A . n 
B 2 244 VAL 244 244 244 VAL VAL A . n 
B 2 245 ASP 245 245 245 ASP ASP A . n 
B 2 246 GLN 246 246 246 GLN GLN A . n 
B 2 247 LEU 247 247 247 LEU LEU A . n 
B 2 248 GLY 248 248 248 GLY GLY A . n 
B 2 249 LEU 249 249 249 LEU LEU A . n 
B 2 250 THR 250 250 250 THR THR A . n 
B 2 251 TYR 251 251 251 TYR TYR A . n 
B 2 252 ARG 252 252 252 ARG ARG A . n 
B 2 253 PRO 253 253 253 PRO PRO A . n 
B 2 254 GLN 254 254 254 GLN GLN A . n 
B 2 255 GLN 255 255 255 GLN GLN A . n 
B 2 256 LEU 256 256 256 LEU LEU A . n 
B 2 257 TYR 257 257 257 TYR TYR A . n 
B 2 258 LEU 258 258 258 LEU LEU A . n 
B 2 259 ALA 259 259 259 ALA ALA A . n 
B 2 260 GLU 260 260 260 GLU GLU A . n 
B 2 261 THR 261 261 261 THR THR A . n 
B 2 262 ILE 262 262 262 ILE ILE A . n 
B 2 263 LEU 263 263 263 LEU LEU A . n 
B 2 264 ASP 264 264 264 ASP ASP A . n 
B 2 265 GLN 265 265 265 GLN GLN A . n 
B 2 266 LEU 266 266 266 LEU LEU A . n 
B 2 267 MET 267 267 267 MET MET A . n 
B 2 268 HIS 268 268 268 HIS HIS A . n 
B 2 269 SER 269 269 269 SER SER A . n 
B 2 270 GLU 270 270 270 GLU GLU A . n 
B 2 271 LYS 271 271 271 LYS LYS A . n 
B 2 272 ALA 272 272 272 ALA ALA A . n 
B 2 273 MET 273 273 273 MET MET A . n 
B 2 274 ILE 274 274 274 ILE ILE A . n 
B 2 275 GLU 275 275 275 GLU GLU A . n 
B 2 276 ALA 276 276 276 ALA ALA A . n 
B 2 277 SER 277 277 277 SER SER A . n 
B 2 278 LEU 278 278 278 LEU LEU A . n 
B 2 279 GLY 279 279 279 GLY GLY A . n 
B 2 280 SER 280 280 280 SER SER A . n 
B 2 281 GLY 281 281 281 GLY GLY A . n 
B 2 282 LYS 282 282 282 LYS LYS A . n 
B 2 283 SER 283 283 283 SER SER A . n 
B 2 284 LEU 284 284 284 LEU LEU A . n 
B 2 285 ALA 285 285 285 ALA ALA A . n 
B 2 286 TYR 286 286 286 TYR TYR A . n 
B 2 287 LEU 287 287 287 LEU LEU A . n 
B 2 288 LEU 288 288 288 LEU LEU A . n 
B 2 289 ALA 289 289 289 ALA ALA A . n 
B 2 290 ALA 290 290 290 ALA ALA A . n 
B 2 291 LEU 291 291 291 LEU LEU A . n 
B 2 292 MET 292 292 292 MET MET A . n 
B 2 293 TYR 293 293 293 TYR TYR A . n 
B 2 294 ASN 294 294 294 ASN ASN A . n 
B 2 295 ILE 295 295 295 ILE ILE A . n 
B 2 296 GLU 296 296 296 GLU GLU A . n 
B 2 297 THR 297 297 297 THR THR A . n 
B 2 298 GLY 298 298 298 GLY GLY A . n 
B 2 299 LYS 299 299 299 LYS LYS A . n 
B 2 300 HIS 300 300 300 HIS HIS A . n 
B 2 301 VAL 301 301 301 VAL VAL A . n 
B 2 302 MET 302 302 302 MET MET A . n 
B 2 303 ILE 303 303 303 ILE ILE A . n 
B 2 304 SER 304 304 304 SER SER A . n 
B 2 305 THR 305 305 305 THR THR A . n 
B 2 306 ASN 306 306 306 ASN ASN A . n 
B 2 307 THR 307 307 307 THR THR A . n 
B 2 308 LYS 308 308 308 LYS LYS A . n 
B 2 309 LEU 309 309 309 LEU LEU A . n 
B 2 310 LEU 310 310 310 LEU LEU A . n 
B 2 311 GLN 311 311 311 GLN GLN A . n 
B 2 312 SER 312 312 312 SER SER A . n 
B 2 313 GLN 313 313 313 GLN GLN A . n 
B 2 314 LEU 314 314 314 LEU LEU A . n 
B 2 315 LEU 315 315 315 LEU LEU A . n 
B 2 316 GLU 316 316 316 GLU GLU A . n 
B 2 317 LYS 317 317 317 LYS LYS A . n 
B 2 318 ASP 318 318 318 ASP ASP A . n 
B 2 319 ILE 319 319 319 ILE ILE A . n 
B 2 320 PRO 320 320 320 PRO PRO A . n 
B 2 321 ALA 321 321 321 ALA ALA A . n 
B 2 322 MET 322 322 322 MET MET A . n 
B 2 323 ASN 323 323 323 ASN ASN A . n 
B 2 324 GLU 324 324 324 GLU GLU A . n 
B 2 325 ALA 325 325 325 ALA ALA A . n 
B 2 326 LEU 326 326 326 LEU LEU A . n 
B 2 327 ASN 327 327 327 ASN ASN A . n 
B 2 328 PHE 328 328 328 PHE PHE A . n 
B 2 329 LYS 329 329 329 LYS LYS A . n 
B 2 330 ILE 330 330 330 ILE ILE A . n 
B 2 331 ASN 331 331 331 ASN ASN A . n 
B 2 332 ALA 332 332 332 ALA ALA A . n 
B 2 333 LEU 333 333 333 LEU LEU A . n 
B 2 334 LEU 334 334 334 LEU LEU A . n 
B 2 335 ILE 335 335 335 ILE ILE A . n 
B 2 336 LYS 336 336 336 LYS LYS A . n 
B 2 337 SER 337 337 337 SER SER A . n 
B 2 338 LYS 338 338 338 LYS LYS A . n 
B 2 339 SER 339 339 339 SER SER A . n 
B 2 340 ASP 340 340 340 ASP ASP A . n 
B 2 341 TYR 341 341 341 TYR TYR A . n 
B 2 342 ILE 342 342 342 ILE ILE A . n 
B 2 343 SER 343 343 343 SER SER A . n 
B 2 344 LEU 344 344 344 LEU LEU A . n 
B 2 345 GLY 345 345 345 GLY GLY A . n 
B 2 346 LEU 346 346 346 LEU LEU A . n 
B 2 347 ILE 347 347 347 ILE ILE A . n 
B 2 348 SER 348 348 348 SER SER A . n 
B 2 349 GLN 349 349 349 GLN GLN A . n 
B 2 350 ILE 350 350 350 ILE ILE A . n 
B 2 351 LEU 351 351 351 LEU LEU A . n 
B 2 352 LYS 352 352 352 LYS LYS A . n 
B 2 353 ASP 353 353 353 ASP ASP A . n 
B 2 354 ASP 354 354 354 ASP ASP A . n 
B 2 355 THR 355 355 355 THR THR A . n 
B 2 356 SER 356 356 356 SER SER A . n 
B 2 357 ASN 357 357 357 ASN ASN A . n 
B 2 358 TYR 358 358 358 TYR TYR A . n 
B 2 359 GLU 359 359 359 GLU GLU A . n 
B 2 360 VAL 360 360 360 VAL VAL A . n 
B 2 361 ASN 361 361 361 ASN ASN A . n 
B 2 362 ILE 362 362 362 ILE ILE A . n 
B 2 363 LEU 363 363 363 LEU LEU A . n 
B 2 364 LYS 364 364 364 LYS LYS A . n 
B 2 365 MET 365 365 365 MET MET A . n 
B 2 366 GLN 366 366 366 GLN GLN A . n 
B 2 367 LEU 367 367 367 LEU LEU A . n 
B 2 368 LEU 368 368 368 LEU LEU A . n 
B 2 369 ILE 369 369 369 ILE ILE A . n 
B 2 370 TRP 370 370 370 TRP TRP A . n 
B 2 371 ILE 371 371 371 ILE ILE A . n 
B 2 372 THR 372 372 372 THR THR A . n 
B 2 373 GLU 373 373 373 GLU GLU A . n 
B 2 374 THR 374 374 374 THR THR A . n 
B 2 375 PRO 375 375 375 PRO PRO A . n 
B 2 376 SER 376 376 376 SER SER A . n 
B 2 377 GLY 377 377 377 GLY GLY A . n 
B 2 378 ASP 378 378 378 ASP ASP A . n 
B 2 379 ILE 379 379 379 ILE ILE A . n 
B 2 380 GLN 380 380 380 GLN GLN A . n 
B 2 381 GLU 381 381 381 GLU GLU A . n 
B 2 382 LEU 382 382 382 LEU LEU A . n 
B 2 383 ASN 383 383 383 ASN ASN A . n 
B 2 384 LEU 384 384 384 LEU LEU A . n 
B 2 385 LYS 385 385 385 LYS LYS A . n 
B 2 386 GLY 386 386 386 GLY GLY A . n 
B 2 387 GLY 387 387 387 GLY GLY A . n 
B 2 388 GLN 388 388 388 GLN GLN A . n 
B 2 389 LYS 389 389 389 LYS LYS A . n 
B 2 390 MET 390 390 390 MET MET A . n 
B 2 391 TYR 391 391 391 TYR TYR A . n 
B 2 392 PHE 392 392 392 PHE PHE A . n 
B 2 393 ASP 393 393 393 ASP ASP A . n 
B 2 394 GLN 394 394 394 GLN GLN A . n 
B 2 395 LYS 395 395 395 LYS LYS A . n 
B 2 396 ILE 396 396 396 ILE ILE A . n 
B 2 397 GLU 397 397 397 GLU GLU A . n 
B 2 398 THR 398 398 398 THR THR A . n 
B 2 399 TYR 399 399 399 TYR TYR A . n 
B 2 400 VAL 400 400 400 VAL VAL A . n 
B 2 401 PRO 401 401 401 PRO PRO A . n 
B 2 402 ALA 402 402 402 ALA ALA A . n 
B 2 403 ARG 403 403 403 ARG ARG A . n 
B 2 404 HIS 404 404 404 HIS HIS A . n 
B 2 405 ASP 405 405 405 ASP ASP A . n 
B 2 406 VAL 406 406 406 VAL VAL A . n 
B 2 407 HIS 407 407 407 HIS HIS A . n 
B 2 408 TYR 408 408 408 TYR TYR A . n 
B 2 409 TYR 409 409 409 TYR TYR A . n 
B 2 410 ASN 410 410 410 ASN ASN A . n 
B 2 411 PHE 411 411 411 PHE PHE A . n 
B 2 412 ILE 412 412 412 ILE ILE A . n 
B 2 413 LYS 413 413 413 LYS LYS A . n 
B 2 414 ARG 414 414 414 ARG ARG A . n 
B 2 415 ASN 415 415 415 ASN ASN A . n 
B 2 416 ALA 416 416 416 ALA ALA A . n 
B 2 417 GLN 417 417 417 GLN GLN A . n 
B 2 418 ASN 418 418 418 ASN ASN A . n 
B 2 419 ILE 419 419 419 ILE ILE A . n 
B 2 420 GLN 420 420 420 GLN GLN A . n 
B 2 421 ILE 421 421 421 ILE ILE A . n 
B 2 422 GLY 422 422 422 GLY GLY A . n 
B 2 423 ILE 423 423 423 ILE ILE A . n 
B 2 424 THR 424 424 424 THR THR A . n 
B 2 425 ASN 425 425 425 ASN ASN A . n 
B 2 426 HIS 426 426 426 HIS HIS A . n 
B 2 427 ALA 427 427 427 ALA ALA A . n 
B 2 428 HIS 428 428 428 HIS HIS A . n 
B 2 429 LEU 429 429 429 LEU LEU A . n 
B 2 430 ILE 430 430 430 ILE ILE A . n 
B 2 431 HIS 431 431 431 HIS HIS A . n 
B 2 432 SER 432 432 432 SER SER A . n 
B 2 433 ASP 433 433 433 ASP ASP A . n 
B 2 434 VAL 434 434 434 VAL VAL A . n 
B 2 435 GLU 435 435 435 GLU GLU A . n 
B 2 436 ASN 436 436 436 ASN ASN A . n 
B 2 437 SER 437 437 437 SER SER A . n 
B 2 438 ILE 438 438 438 ILE ILE A . n 
B 2 439 TYR 439 439 439 TYR TYR A . n 
B 2 440 GLN 440 440 440 GLN GLN A . n 
B 2 441 LEU 441 441 441 LEU LEU A . n 
B 2 442 PHE 442 442 442 PHE PHE A . n 
B 2 443 ASP 443 443 443 ASP ASP A . n 
B 2 444 ASP 444 444 444 ASP ASP A . n 
B 2 445 CYS 445 445 445 CYS CYS A . n 
B 2 446 ILE 446 446 446 ILE ILE A . n 
B 2 447 VAL 447 447 447 VAL VAL A . n 
B 2 448 ASP 448 448 448 ASP ASP A . n 
B 2 449 GLU 449 449 449 GLU GLU A . n 
B 2 450 ALA 450 450 450 ALA ALA A . n 
B 2 451 HIS 451 451 451 HIS HIS A . n 
B 2 452 ARG 452 452 452 ARG ARG A . n 
B 2 453 LEU 453 453 453 LEU LEU A . n 
B 2 454 PRO 454 454 454 PRO PRO A . n 
B 2 455 ASP 455 455 455 ASP ASP A . n 
B 2 456 TYR 456 456 456 TYR TYR A . n 
B 2 457 ALA 457 457 457 ALA ALA A . n 
B 2 458 LEU 458 458 458 LEU LEU A . n 
B 2 459 ASN 459 459 459 ASN ASN A . n 
B 2 460 GLN 460 460 460 GLN GLN A . n 
B 2 461 VAL 461 461 461 VAL VAL A . n 
B 2 462 THR 462 462 462 THR THR A . n 
B 2 463 ASN 463 463 463 ASN ASN A . n 
B 2 464 GLU 464 464 464 GLU GLU A . n 
B 2 465 LEU 465 465 465 LEU LEU A . n 
B 2 466 SER 466 466 466 SER SER A . n 
B 2 467 TYR 467 467 467 TYR TYR A . n 
B 2 468 ALA 468 468 468 ALA ALA A . n 
B 2 469 ASP 469 469 469 ASP ASP A . n 
B 2 470 ILE 470 470 470 ILE ILE A . n 
B 2 471 LYS 471 471 471 LYS LYS A . n 
B 2 472 TYR 472 472 472 TYR TYR A . n 
B 2 473 GLN 473 473 473 GLN GLN A . n 
B 2 474 LEU 474 474 474 LEU LEU A . n 
B 2 475 GLY 475 475 475 GLY GLY A . n 
B 2 476 LEU 476 476 476 LEU LEU A . n 
B 2 477 ILE 477 477 477 ILE ILE A . n 
B 2 478 GLY 478 478 478 GLY GLY A . n 
B 2 479 LYS 479 479 479 LYS LYS A . n 
B 2 480 ASN 480 480 480 ASN ASN A . n 
B 2 481 GLU 481 481 481 GLU GLU A . n 
B 2 482 ASN 482 482 482 ASN ASN A . n 
B 2 483 GLU 483 483 483 GLU GLU A . n 
B 2 484 LYS 484 484 484 LYS LYS A . n 
B 2 485 LEU 485 485 485 LEU LEU A . n 
B 2 486 LEU 486 486 486 LEU LEU A . n 
B 2 487 LYS 487 487 487 LYS LYS A . n 
B 2 488 ALA 488 488 488 ALA ALA A . n 
B 2 489 ILE 489 489 489 ILE ILE A . n 
B 2 490 ASP 490 490 490 ASP ASP A . n 
B 2 491 GLN 491 491 491 GLN GLN A . n 
B 2 492 LEU 492 492 492 LEU LEU A . n 
B 2 493 GLU 493 493 493 GLU GLU A . n 
B 2 494 LYS 494 494 494 LYS LYS A . n 
B 2 495 GLN 495 495 495 GLN GLN A . n 
B 2 496 ARG 496 496 496 ARG ARG A . n 
B 2 497 ILE 497 497 497 ILE ILE A . n 
B 2 498 LEU 498 498 498 LEU LEU A . n 
B 2 499 GLU 499 499 499 GLU GLU A . n 
B 2 500 LYS 500 500 500 LYS LYS A . n 
B 2 501 LEU 501 501 501 LEU LEU A . n 
B 2 502 ASP 502 502 502 ASP ASP A . n 
B 2 503 ILE 503 503 503 ILE ILE A . n 
B 2 504 ALA 504 504 504 ALA ALA A . n 
B 2 505 PRO 505 505 505 PRO PRO A . n 
B 2 506 ILE 506 506 506 ILE ILE A . n 
B 2 507 ASP 507 507 507 ASP ASP A . n 
B 2 508 ILE 508 508 508 ILE ILE A . n 
B 2 509 PHE 509 509 509 PHE PHE A . n 
B 2 510 GLY 510 510 510 GLY GLY A . n 
B 2 511 LEU 511 511 511 LEU LEU A . n 
B 2 512 LYS 512 512 512 LYS LYS A . n 
B 2 513 ALA 513 513 513 ALA ALA A . n 
B 2 514 SER 514 514 514 SER SER A . n 
B 2 515 MET 515 515 515 MET MET A . n 
B 2 516 ASN 516 516 516 ASN ASN A . n 
B 2 517 GLU 517 517 517 GLU GLU A . n 
B 2 518 ILE 518 518 518 ILE ILE A . n 
B 2 519 HIS 519 519 519 HIS HIS A . n 
B 2 520 GLU 520 520 520 GLU GLU A . n 
B 2 521 LEU 521 521 521 LEU LEU A . n 
B 2 522 ASN 522 522 522 ASN ASN A . n 
B 2 523 GLU 523 523 523 GLU GLU A . n 
B 2 524 GLN 524 524 524 GLN GLN A . n 
B 2 525 LEU 525 525 525 LEU LEU A . n 
B 2 526 PHE 526 526 526 PHE PHE A . n 
B 2 527 SER 527 527 527 SER SER A . n 
B 2 528 THR 528 528 528 THR THR A . n 
B 2 529 ILE 529 529 529 ILE ILE A . n 
B 2 530 PHE 530 530 530 PHE PHE A . n 
B 2 531 THR 531 531 531 THR THR A . n 
B 2 532 ILE 532 532 532 ILE ILE A . n 
B 2 533 ILE 533 533 533 ILE ILE A . n 
B 2 534 ASN 534 534 534 ASN ASN A . n 
B 2 535 ASP 535 535 535 ASP ASP A . n 
B 2 536 SER 536 536 536 SER SER A . n 
B 2 537 ASP 537 537 537 ASP ASP A . n 
B 2 538 VAL 538 538 538 VAL VAL A . n 
B 2 539 TYR 539 539 539 TYR TYR A . n 
B 2 540 ASP 540 540 540 ASP ASP A . n 
B 2 541 ASP 541 541 541 ASP ASP A . n 
B 2 542 ASP 542 542 542 ASP ASP A . n 
B 2 543 ILE 543 543 543 ILE ILE A . n 
B 2 544 HIS 544 544 544 HIS HIS A . n 
B 2 545 ARG 545 545 545 ARG ARG A . n 
B 2 546 PHE 546 546 546 PHE PHE A . n 
B 2 547 HIS 547 547 547 HIS HIS A . n 
B 2 548 ASN 548 548 548 ASN ASN A . n 
B 2 549 VAL 549 549 549 VAL VAL A . n 
B 2 550 PHE 550 550 550 PHE PHE A . n 
B 2 551 THR 551 551 551 THR THR A . n 
B 2 552 PHE 552 552 552 PHE PHE A . n 
B 2 553 GLU 553 553 553 GLU GLU A . n 
B 2 554 THR 554 554 554 THR THR A . n 
B 2 555 LYS 555 555 555 LYS LYS A . n 
B 2 556 ASP 556 556 556 ASP ASP A . n 
B 2 557 ILE 557 557 557 ILE ILE A . n 
B 2 558 LEU 558 558 558 LEU LEU A . n 
B 2 559 LYS 559 559 559 LYS LYS A . n 
B 2 560 ASP 560 560 560 ASP ASP A . n 
B 2 561 LEU 561 561 561 LEU LEU A . n 
B 2 562 HIS 562 562 562 HIS HIS A . n 
B 2 563 ALA 563 563 563 ALA ALA A . n 
B 2 564 ILE 564 564 564 ILE ILE A . n 
B 2 565 ILE 565 565 565 ILE ILE A . n 
B 2 566 ASP 566 566 566 ASP ASP A . n 
B 2 567 LYS 567 567 567 LYS LYS A . n 
B 2 568 LEU 568 568 568 LEU LEU A . n 
B 2 569 ASN 569 569 569 ASN ASN A . n 
B 2 570 LYS 570 570 570 LYS LYS A . n 
B 2 571 THR 571 571 571 THR THR A . n 
B 2 572 LEU 572 572 572 LEU LEU A . n 
B 2 573 GLU 573 573 573 GLU GLU A . n 
B 2 574 ILE 574 574 574 ILE ILE A . n 
B 2 575 PHE 575 575 575 PHE PHE A . n 
B 2 576 ASN 576 576 576 ASN ASN A . n 
B 2 577 GLY 577 577 577 GLY GLY A . n 
B 2 578 ILE 578 578 578 ILE ILE A . n 
B 2 579 SER 579 579 579 SER SER A . n 
B 2 580 HIS 580 580 580 HIS HIS A . n 
B 2 581 LYS 581 581 581 LYS LYS A . n 
B 2 582 THR 582 582 582 THR THR A . n 
B 2 583 VAL 583 583 583 VAL VAL A . n 
B 2 584 LYS 584 584 584 LYS LYS A . n 
B 2 585 SER 585 585 585 SER SER A . n 
B 2 586 LEU 586 586 586 LEU LEU A . n 
B 2 587 ARG 587 587 587 ARG ARG A . n 
B 2 588 LYS 588 588 588 LYS LYS A . n 
B 2 589 GLN 589 589 589 GLN GLN A . n 
B 2 590 LEU 590 590 590 LEU LEU A . n 
B 2 591 LEU 591 591 591 LEU LEU A . n 
B 2 592 TYR 592 592 592 TYR TYR A . n 
B 2 593 LEU 593 593 593 LEU LEU A . n 
B 2 594 LYS 594 594 594 LYS LYS A . n 
B 2 595 ASP 595 595 595 ASP ASP A . n 
B 2 596 LYS 596 596 596 LYS LYS A . n 
B 2 597 PHE 597 597 597 PHE PHE A . n 
B 2 598 LYS 598 598 598 LYS LYS A . n 
B 2 599 ASN 599 599 599 ASN ASN A . n 
B 2 600 ILE 600 600 600 ILE ILE A . n 
B 2 601 GLU 601 601 601 GLU GLU A . n 
B 2 602 GLN 602 602 602 GLN GLN A . n 
B 2 603 SER 603 603 603 SER SER A . n 
B 2 604 LEU 604 604 604 LEU LEU A . n 
B 2 605 LYS 605 605 605 LYS LYS A . n 
B 2 606 ALA 606 606 606 ALA ALA A . n 
B 2 607 GLY 607 607 607 GLY GLY A . n 
B 2 608 HIS 608 608 608 HIS HIS A . n 
B 2 609 THR 609 609 609 THR THR A . n 
B 2 610 SER 610 610 610 SER SER A . n 
B 2 611 PHE 611 611 611 PHE PHE A . n 
B 2 612 ILE 612 612 612 ILE ILE A . n 
B 2 613 SER 613 613 613 SER SER A . n 
B 2 614 ILE 614 614 614 ILE ILE A . n 
B 2 615 LYS 615 615 615 LYS LYS A . n 
B 2 616 ASN 616 616 616 ASN ASN A . n 
B 2 617 LEU 617 617 617 LEU LEU A . n 
B 2 618 SER 618 618 618 SER SER A . n 
B 2 619 GLN 619 619 619 GLN GLN A . n 
B 2 620 LYS 620 620 620 LYS LYS A . n 
B 2 621 SER 621 621 621 SER SER A . n 
B 2 622 THR 622 622 622 THR THR A . n 
B 2 623 ILE 623 623 623 ILE ILE A . n 
B 2 624 ARG 624 624 624 ARG ARG A . n 
B 2 625 LEU 625 625 625 LEU LEU A . n 
B 2 626 TYR 626 626 626 TYR TYR A . n 
B 2 627 VAL 627 627 627 VAL VAL A . n 
B 2 628 LYS 628 628 628 LYS LYS A . n 
B 2 629 ASP 629 629 629 ASP ASP A . n 
B 2 630 TYR 630 630 630 TYR TYR A . n 
B 2 631 ALA 631 631 631 ALA ALA A . n 
B 2 632 VAL 632 632 632 VAL VAL A . n 
B 2 633 LYS 633 633 633 LYS LYS A . n 
B 2 634 ASP 634 634 634 ASP ASP A . n 
B 2 635 VAL 635 635 635 VAL VAL A . n 
B 2 636 LEU 636 636 636 LEU LEU A . n 
B 2 637 THR 637 637 637 THR THR A . n 
B 2 638 LYS 638 638 638 LYS LYS A . n 
B 2 639 GLN 639 639 639 GLN GLN A . n 
B 2 640 VAL 640 640 640 VAL VAL A . n 
B 2 641 LEU 641 641 641 LEU LEU A . n 
B 2 642 GLU 642 642 642 GLU GLU A . n 
B 2 643 LYS 643 643 643 LYS LYS A . n 
B 2 644 PHE 644 644 644 PHE PHE A . n 
B 2 645 LYS 645 645 645 LYS LYS A . n 
B 2 646 SER 646 646 646 SER SER A . n 
B 2 647 LEU 647 647 647 LEU LEU A . n 
B 2 648 ILE 648 648 648 ILE ILE A . n 
B 2 649 PHE 649 649 649 PHE PHE A . n 
B 2 650 ILE 650 650 650 ILE ILE A . n 
B 2 651 SER 651 651 651 SER SER A . n 
B 2 652 GLY 652 652 652 GLY GLY A . n 
B 2 653 THR 653 653 653 THR THR A . n 
B 2 654 LEU 654 654 654 LEU LEU A . n 
B 2 655 LYS 655 655 655 LYS LYS A . n 
B 2 656 PHE 656 656 656 PHE PHE A . n 
B 2 657 ASN 657 657 657 ASN ASN A . n 
B 2 658 HIS 658 658 658 HIS HIS A . n 
B 2 659 SER 659 659 659 SER SER A . n 
B 2 660 PHE 660 660 660 PHE PHE A . n 
B 2 661 GLU 661 661 661 GLU GLU A . n 
B 2 662 ALA 662 662 662 ALA ALA A . n 
B 2 663 PHE 663 663 663 PHE PHE A . n 
B 2 664 LYS 664 664 664 LYS LYS A . n 
B 2 665 GLN 665 665 665 GLN GLN A . n 
B 2 666 LEU 666 666 666 LEU LEU A . n 
B 2 667 PHE 667 667 667 PHE PHE A . n 
B 2 668 ASN 668 668 668 ASN ASN A . n 
B 2 669 LYS 669 669 669 LYS LYS A . n 
B 2 670 ASP 670 670 670 ASP ASP A . n 
B 2 671 VAL 671 671 671 VAL VAL A . n 
B 2 672 HIS 672 672 672 HIS HIS A . n 
B 2 673 PHE 673 673 673 PHE PHE A . n 
B 2 674 ASN 674 674 674 ASN ASN A . n 
B 2 675 THR 675 675 675 THR THR A . n 
B 2 676 PHE 676 676 676 PHE PHE A . n 
B 2 677 GLU 677 677 677 GLU GLU A . n 
B 2 678 VAL 678 678 678 VAL VAL A . n 
B 2 679 ASN 679 679 679 ASN ASN A . n 
B 2 680 THR 680 680 680 THR THR A . n 
B 2 681 SER 681 681 681 SER SER A . n 
B 2 682 LEU 682 682 682 LEU LEU A . n 
B 2 683 GLN 683 683 683 GLN GLN A . n 
B 2 684 SER 684 684 684 SER SER A . n 
B 2 685 ALA 685 685 685 ALA ALA A . n 
B 2 686 LYS 686 686 686 LYS LYS A . n 
B 2 687 ASN 687 687 687 ASN ASN A . n 
B 2 688 THR 688 688 688 THR THR A . n 
B 2 689 SER 689 689 689 SER SER A . n 
B 2 690 VAL 690 690 690 VAL VAL A . n 
B 2 691 PHE 691 691 691 PHE PHE A . n 
B 2 692 ILE 692 692 692 ILE ILE A . n 
B 2 693 PRO 693 693 693 PRO PRO A . n 
B 2 694 SER 694 694 694 SER SER A . n 
B 2 695 ASP 695 695 695 ASP ASP A . n 
B 2 696 VAL 696 696 696 VAL VAL A . n 
B 2 697 ALA 697 697 697 ALA ALA A . n 
B 2 698 SER 698 698 698 SER SER A . n 
B 2 699 TYR 699 699 699 TYR TYR A . n 
B 2 700 GLN 700 700 700 GLN GLN A . n 
B 2 701 TYR 701 701 701 TYR TYR A . n 
B 2 702 LYS 702 702 702 LYS LYS A . n 
B 2 703 ASN 703 703 703 ASN ASN A . n 
B 2 704 ILE 704 704 704 ILE ILE A . n 
B 2 705 ASP 705 705 705 ASP ASP A . n 
B 2 706 GLU 706 706 706 GLU GLU A . n 
B 2 707 TYR 707 707 707 TYR TYR A . n 
B 2 708 VAL 708 708 708 VAL VAL A . n 
B 2 709 ALA 709 709 709 ALA ALA A . n 
B 2 710 SER 710 710 710 SER SER A . n 
B 2 711 ILE 711 711 711 ILE ILE A . n 
B 2 712 VAL 712 712 712 VAL VAL A . n 
B 2 713 SER 713 713 713 SER SER A . n 
B 2 714 TYR 714 714 714 TYR TYR A . n 
B 2 715 ILE 715 715 715 ILE ILE A . n 
B 2 716 ILE 716 716 716 ILE ILE A . n 
B 2 717 GLU 717 717 717 GLU GLU A . n 
B 2 718 TYR 718 718 718 TYR TYR A . n 
B 2 719 THR 719 719 719 THR THR A . n 
B 2 720 THR 720 720 720 THR THR A . n 
B 2 721 ILE 721 721 721 ILE ILE A . n 
B 2 722 THR 722 722 722 THR THR A . n 
B 2 723 SER 723 723 723 SER SER A . n 
B 2 724 SER 724 724 724 SER SER A . n 
B 2 725 LYS 725 725 725 LYS LYS A . n 
B 2 726 CYS 726 726 726 CYS CYS A . n 
B 2 727 LEU 727 727 727 LEU LEU A . n 
B 2 728 VAL 728 728 728 VAL VAL A . n 
B 2 729 LEU 729 729 729 LEU LEU A . n 
B 2 730 PHE 730 730 730 PHE PHE A . n 
B 2 731 THR 731 731 731 THR THR A . n 
B 2 732 SER 732 732 732 SER SER A . n 
B 2 733 TYR 733 733 733 TYR TYR A . n 
B 2 734 LYS 734 734 734 LYS LYS A . n 
B 2 735 MET 735 735 735 MET MET A . n 
B 2 736 MET 736 736 736 MET MET A . n 
B 2 737 HIS 737 737 737 HIS HIS A . n 
B 2 738 MET 738 738 738 MET MET A . n 
B 2 739 VAL 739 739 739 VAL VAL A . n 
B 2 740 GLN 740 740 740 GLN GLN A . n 
B 2 741 ASP 741 741 741 ASP ASP A . n 
B 2 742 MET 742 742 742 MET MET A . n 
B 2 743 LEU 743 743 743 LEU LEU A . n 
B 2 744 ASN 744 744 744 ASN ASN A . n 
B 2 745 GLU 745 745 745 GLU GLU A . n 
B 2 746 LEU 746 746 746 LEU LEU A . n 
B 2 747 PRO 747 747 747 PRO PRO A . n 
B 2 748 GLU 748 748 748 GLU GLU A . n 
B 2 749 PHE 749 749 749 PHE PHE A . n 
B 2 750 GLU 750 750 750 GLU GLU A . n 
B 2 751 ASP 751 751 751 ASP ASP A . n 
B 2 752 TYR 752 752 752 TYR TYR A . n 
B 2 753 VAL 753 753 753 VAL VAL A . n 
B 2 754 VAL 754 754 754 VAL VAL A . n 
B 2 755 LEU 755 755 755 LEU LEU A . n 
B 2 756 THR 756 756 756 THR THR A . n 
B 2 757 GLN 757 757 757 GLN GLN A . n 
B 2 758 GLN 758 758 758 GLN GLN A . n 
B 2 759 GLN 759 759 759 GLN GLN A . n 
B 2 760 ASN 760 760 760 ASN ASN A . n 
B 2 761 GLN 761 761 761 GLN GLN A . n 
B 2 762 ASN 762 762 762 ASN ASN A . n 
B 2 763 TYR 763 763 763 TYR TYR A . n 
B 2 764 LYS 764 764 764 LYS LYS A . n 
B 2 765 ILE 765 765 765 ILE ILE A . n 
B 2 766 VAL 766 766 766 VAL VAL A . n 
B 2 767 GLN 767 767 767 GLN GLN A . n 
B 2 768 GLN 768 768 768 GLN GLN A . n 
B 2 769 PHE 769 769 769 PHE PHE A . n 
B 2 770 ASN 770 770 770 ASN ASN A . n 
B 2 771 ASN 771 771 771 ASN ASN A . n 
B 2 772 PHE 772 772 772 PHE PHE A . n 
B 2 773 ASP 773 773 773 ASP ASP A . n 
B 2 774 LYS 774 774 774 LYS LYS A . n 
B 2 775 ALA 775 775 775 ALA ALA A . n 
B 2 776 ILE 776 776 776 ILE ILE A . n 
B 2 777 LEU 777 777 777 LEU LEU A . n 
B 2 778 LEU 778 778 778 LEU LEU A . n 
B 2 779 GLY 779 779 779 GLY GLY A . n 
B 2 780 THR 780 780 780 THR THR A . n 
B 2 781 SER 781 781 781 SER SER A . n 
B 2 782 THR 782 782 782 THR THR A . n 
B 2 783 PHE 783 783 783 PHE PHE A . n 
B 2 784 PHE 784 784 784 PHE PHE A . n 
B 2 785 GLU 785 785 785 GLU GLU A . n 
B 2 786 GLY 786 786 786 GLY GLY A . n 
B 2 787 PHE 787 787 787 PHE PHE A . n 
B 2 788 ASP 788 788 788 ASP ASP A . n 
B 2 789 PHE 789 789 789 PHE PHE A . n 
B 2 790 GLN 790 790 790 GLN GLN A . n 
B 2 791 ALA 791 791 791 ALA ALA A . n 
B 2 792 ASN 792 792 792 ASN ASN A . n 
B 2 793 GLY 793 793 793 GLY GLY A . n 
B 2 794 ILE 794 794 794 ILE ILE A . n 
B 2 795 LYS 795 795 795 LYS LYS A . n 
B 2 796 CYS 796 796 796 CYS CYS A . n 
B 2 797 VAL 797 797 797 VAL VAL A . n 
B 2 798 MET 798 798 798 MET MET A . n 
B 2 799 ILE 799 799 799 ILE ILE A . n 
B 2 800 ALA 800 800 800 ALA ALA A . n 
B 2 801 LYS 801 801 801 LYS LYS A . n 
B 2 802 LEU 802 802 802 LEU LEU A . n 
B 2 803 PRO 803 803 803 PRO PRO A . n 
B 2 804 PHE 804 804 804 PHE PHE A . n 
B 2 805 MET 805 805 805 MET MET A . n 
B 2 806 ASN 806 806 806 ASN ASN A . n 
B 2 807 LYS 807 807 807 LYS LYS A . n 
B 2 808 HIS 808 808 808 HIS HIS A . n 
B 2 809 ASN 809 809 809 ASN ASN A . n 
B 2 810 ALA 810 810 810 ALA ALA A . n 
B 2 811 LYS 811 811 811 LYS LYS A . n 
B 2 812 TYR 812 812 812 TYR TYR A . n 
B 2 813 TRP 813 813 813 TRP TRP A . n 
B 2 814 LEU 814 814 814 LEU LEU A . n 
B 2 815 MET 815 815 815 MET MET A . n 
B 2 816 ASP 816 816 816 ASP ASP A . n 
B 2 817 SER 817 817 817 SER SER A . n 
B 2 818 GLU 818 818 818 GLU GLU A . n 
B 2 819 PHE 819 819 819 PHE PHE A . n 
B 2 820 THR 820 820 820 THR THR A . n 
B 2 821 SER 821 821 821 SER SER A . n 
B 2 822 THR 822 822 822 THR THR A . n 
B 2 823 PHE 823 823 823 PHE PHE A . n 
B 2 824 LYS 824 824 824 LYS LYS A . n 
B 2 825 GLU 825 825 825 GLU GLU A . n 
B 2 826 TYR 826 826 826 TYR TYR A . n 
B 2 827 VAL 827 827 827 VAL VAL A . n 
B 2 828 LEU 828 828 828 LEU LEU A . n 
B 2 829 PRO 829 829 829 PRO PRO A . n 
B 2 830 ASP 830 830 830 ASP ASP A . n 
B 2 831 ALA 831 831 831 ALA ALA A . n 
B 2 832 VAL 832 832 832 VAL VAL A . n 
B 2 833 THR 833 833 833 THR THR A . n 
B 2 834 ARG 834 834 834 ARG ARG A . n 
B 2 835 PHE 835 835 835 PHE PHE A . n 
B 2 836 ARG 836 836 836 ARG ARG A . n 
B 2 837 GLN 837 837 837 GLN GLN A . n 
B 2 838 GLY 838 838 838 GLY GLY A . n 
B 2 839 LEU 839 839 839 LEU LEU A . n 
B 2 840 GLY 840 840 840 GLY GLY A . n 
B 2 841 ARG 841 841 841 ARG ARG A . n 
B 2 842 LEU 842 842 842 LEU LEU A . n 
B 2 843 ILE 843 843 843 ILE ILE A . n 
B 2 844 ARG 844 844 844 ARG ARG A . n 
B 2 845 ASN 845 845 845 ASN ASN A . n 
B 2 846 GLU 846 846 846 GLU GLU A . n 
B 2 847 ASN 847 847 847 ASN ASN A . n 
B 2 848 ASP 848 848 848 ASP ASP A . n 
B 2 849 ARG 849 849 849 ARG ARG A . n 
B 2 850 GLY 850 850 850 GLY GLY A . n 
B 2 851 ILE 851 851 851 ILE ILE A . n 
B 2 852 ILE 852 852 852 ILE ILE A . n 
B 2 853 VAL 853 853 853 VAL VAL A . n 
B 2 854 SER 854 854 854 SER SER A . n 
B 2 855 PHE 855 855 855 PHE PHE A . n 
B 2 856 ASP 856 856 856 ASP ASP A . n 
B 2 857 ASP 857 857 857 ASP ASP A . n 
B 2 858 ARG 858 858 858 ARG ARG A . n 
B 2 859 LEU 859 859 859 LEU LEU A . n 
B 2 860 ILE 860 860 860 ILE ILE A . n 
B 2 861 ASN 861 861 861 ASN ASN A . n 
B 2 862 SER 862 862 862 SER SER A . n 
B 2 863 ASN 863 863 863 ASN ASN A . n 
B 2 864 TYR 864 864 864 TYR TYR A . n 
B 2 865 LYS 865 865 865 LYS LYS A . n 
B 2 866 ASN 866 866 866 ASN ASN A . n 
B 2 867 PHE 867 867 867 PHE PHE A . n 
B 2 868 PHE 868 868 868 PHE PHE A . n 
B 2 869 GLU 869 869 869 GLU GLU A . n 
B 2 870 GLN 870 870 870 GLN GLN A . n 
B 2 871 THR 871 871 871 THR THR A . n 
B 2 872 LEU 872 872 872 LEU LEU A . n 
B 2 873 GLU 873 873 873 GLU GLU A . n 
B 2 874 ASN 874 874 874 ASN ASN A . n 
B 2 875 TYR 875 875 875 TYR TYR A . n 
B 2 876 ARG 876 876 876 ARG ARG A . n 
B 2 877 GLN 877 877 877 GLN GLN A . n 
B 2 878 LYS 878 878 878 LYS LYS A . n 
B 2 879 LYS 879 879 879 LYS LYS A . n 
B 2 880 GLY 880 880 880 GLY GLY A . n 
B 2 881 ASP 881 881 881 ASP ASP A . n 
B 2 882 ILE 882 882 882 ILE ILE A . n 
B 2 883 GLN 883 883 883 GLN GLN A . n 
B 2 884 GLN 884 884 884 GLN GLN A . n 
B 2 885 PHE 885 885 885 PHE PHE A . n 
B 2 886 GLY 886 886 886 GLY GLY A . n 
B 2 887 LYS 887 887 887 LYS LYS A . n 
B 2 888 LEU 888 888 888 LEU LEU A . n 
B 2 889 LEU 889 889 889 LEU LEU A . n 
B 2 890 ARG 890 890 890 ARG ARG A . n 
B 2 891 GLN 891 891 891 GLN GLN A . n 
B 2 892 ILE 892 892 892 ILE ILE A . n 
B 2 893 GLN 893 893 893 GLN GLN A . n 
B 2 894 LYS 894 894 894 LYS LYS A . n 
B 2 895 LYS 895 895 895 LYS LYS A . n 
B 2 896 LYS 896 896 896 LYS LYS A . n 
B 2 897 LYS 897 897 ?   ?   ?   A . n 
# 
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   ? ? ? 1.20.1_4487 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                     9II8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     229.170 
_cell.length_a_esd                 ? 
_cell.length_b                     229.170 
_cell.length_b_esd                 ? 
_cell.length_c                     128.030 
_cell.length_c_esd                 ? 
_cell.volume                       6723993.346 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9II8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                97 
_symmetry.space_group_name_Hall            'I 4 2' 
_symmetry.space_group_name_H-M             'I 4 2 2' 
_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                   9II8 
_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             3.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          69.21 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M LiSO4, 0.1 M MES (pH 6.5), and 15% Polyethylene glycol 4000' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315r' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-01-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97936 
_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 BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97936 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          115.64 
_reflns.entry_id                                       9II8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.16 
_reflns.d_resolution_low                               111.77 
_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                                     29417 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.95 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.4 
_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                              0.055 
_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                                    3.16 
_reflns_shell.d_res_low                                     3.273 
_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                             2913 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.55 
_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                               119.65 
_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                                 9II8 
_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                            3.16 
_refine.ls_d_res_low                             111.77 
_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                     29417 
_refine.ls_number_reflns_R_free                  1478 
_refine.ls_number_reflns_R_work                  27939 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2699 
_refine.ls_R_factor_R_free                       0.2930 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2687 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.2855 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.5623 
_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                       3.16 
_refine_hist.d_res_low                        111.77 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               7432 
_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        7352 
_refine_hist.pdbx_number_atoms_nucleic_acid   80 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.0113 ? 7582  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.3762 ? 10242 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0968 ? 1153  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0189 ? 1290  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.1206 ? 1000  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.16 3.26   . . 141 2490 100.00 . . . . 0.5044 . . . . . . . . . . . 0.4906 
'X-RAY DIFFRACTION' 3.26 3.38   . . 122 2524 100.00 . . . . 0.3983 . . . . . . . . . . . 0.4600 
'X-RAY DIFFRACTION' 3.38 3.51   . . 140 2488 100.00 . . . . 0.3274 . . . . . . . . . . . 0.3437 
'X-RAY DIFFRACTION' 3.51 3.67   . . 138 2501 100.00 . . . . 0.2945 . . . . . . . . . . . 0.3308 
'X-RAY DIFFRACTION' 3.67 3.87   . . 127 2545 99.96  . . . . 0.3078 . . . . . . . . . . . 0.3276 
'X-RAY DIFFRACTION' 3.87 4.11   . . 119 2505 100.00 . . . . 0.2989 . . . . . . . . . . . 0.3065 
'X-RAY DIFFRACTION' 4.11 4.43   . . 130 2533 100.00 . . . . 0.2546 . . . . . . . . . . . 0.2775 
'X-RAY DIFFRACTION' 4.43 4.87   . . 148 2517 99.96  . . . . 0.2371 . . . . . . . . . . . 0.2674 
'X-RAY DIFFRACTION' 4.87 5.58   . . 148 2553 100.00 . . . . 0.2513 . . . . . . . . . . . 0.2575 
'X-RAY DIFFRACTION' 5.58 7.03   . . 128 2581 100.00 . . . . 0.2959 . . . . . . . . . . . 0.3072 
'X-RAY DIFFRACTION' 7.03 111.77 . . 137 2702 99.58  . . . . 0.2239 . . . . . . . . . . . 0.2606 
# 
_struct.entry_id                     9II8 
_struct.title                        'Crystal structure of Staphylococcus aureus DinG protein in complex with ssDNA' 
_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        9II8 
_struct_keywords.text            'helicase, nuclease, HYDROLASE/DNA, HYDROLASE-DNA complex' 
_struct_keywords.pdbx_keywords   HYDROLASE/DNA 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9II8       9II8   ? 1 ? 1 
2 UNP DING_STAA8 Q2FYH5 ? 2 
;MGMATYAVVDLETTGNQLDFDDIIQIGITFVRNNQIIDTYHSMIRTNLEIPPFIQALTSIEENMLQQAPYFNQVAQEIYD
KIKDCIFVAHNVDFDLNFIKKAFKDCNIQYRPKKVIDTLEIFKIAFPTDKSYQLSELAEAHGITLANAHRADEDAATTAK
LMILAFEKFEKLPLDTLKQLYYLSKQLKYDLYDIFFEMVRQYDAKPLDKSYEKFEQIIYRKQVDFKKPTTNYNGSLKSLY
SKAVDQLGLTYRPQQLYLAETILDQLMHSEKAMIEASLGSGKSLAYLLAALMYNIETGKHVMISTNTKLLQSQLLEKDIP
AMNEALNFKINALLIKSKSDYISLGLISQILKDDTSNYEVNILKMQLLIWITETPSGDIQELNLKGGQKMYFDQKIETYV
PARHDVHYYNFIKRNAQNIQIGITNHAHLIHSDVENSIYQLFDDCIVDEAHRLPDYALNQVTNELSYADIKYQLGLIGKN
ENEKLLKAIDQLEKQRILEKLDIAPIDIFGLKASMNEIHELNEQLFSTIFTIINDSDVYDDDIHRFHNVFTFETKDILKD
LHAIIDKLNKTLEIFNGISHKTVKSLRKQLLYLKDKFKNIEQSLKAGHTSFISIKNLSQKSTIRLYVKDYAVKDVLTKQV
LEKFKSLIFISGTLKFNHSFEAFKQLFNKDVHFNTFEVNTSLQSAKNTSVFIPSDVASYQYKNIDEYVASIVSYIIEYTT
ITSSKCLVLFTSYKMMHMVQDMLNELPEFEDYVVLTQQQNQNYKIVQQFNNFDKAILLGTSTFFEGFDFQANGIKCVMIA
KLPFMNKHNAKYWLMDSEFTSTFKEYVLPDAVTRFRQGLGRLIRNENDRGIIVSFDDRLINSNYKNFFEQTLENYRQKKG
DIQQFGKLLRQIQKKKK
;
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 9II8 B 1 ? 4   ? 9II8   2 ? 5   ? 2 5   
2 2 9II8 A 1 ? 897 ? Q2FYH5 1 ? 897 ? 1 897 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 9II8 PHE A 210 ? UNP Q2FYH5 SER 210 conflict 210 1 
2 9II8 ARG A 241 ? UNP Q2FYH5 SER 241 conflict 241 2 
# 
_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)' 1270  ? 
1 MORE         -6    ? 
1 'SSA (A^2)'  41710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'native gel electrophoresis' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO B 51  ? SER B 59  ? PRO A 51  SER A 59  1 ? 9  
HELX_P HELX_P2  AA2 GLU B 61  ? GLN B 66  ? GLU A 61  GLN A 66  5 ? 6  
HELX_P HELX_P3  AA3 TYR B 70  ? LYS B 83  ? TYR A 70  LYS A 83  1 ? 14 
HELX_P HELX_P4  AA4 ASN B 91  ? CYS B 106 ? ASN A 91  CYS A 106 1 ? 16 
HELX_P HELX_P5  AA5 THR B 118 ? PHE B 126 ? THR A 118 PHE A 126 1 ? 9  
HELX_P HELX_P6  AA6 GLN B 133 ? HIS B 141 ? GLN A 133 HIS A 141 1 ? 9  
HELX_P HELX_P7  AA7 ASP B 152 ? PHE B 169 ? ASP A 152 PHE A 169 1 ? 18 
HELX_P HELX_P8  AA8 LEU B 172 ? SER B 184 ? LEU A 172 SER A 184 1 ? 13 
HELX_P HELX_P9  AA9 ASP B 190 ? GLN B 201 ? ASP A 190 GLN A 201 1 ? 12 
HELX_P HELX_P10 AB1 SER B 235 ? GLY B 248 ? SER A 235 GLY A 248 1 ? 14 
HELX_P HELX_P11 AB2 ARG B 252 ? HIS B 268 ? ARG A 252 HIS A 268 1 ? 17 
HELX_P HELX_P12 AB3 GLY B 281 ? GLU B 296 ? GLY A 281 GLU A 296 1 ? 16 
HELX_P HELX_P13 AB4 LYS B 308 ? LYS B 317 ? LYS A 308 LYS A 317 1 ? 10 
HELX_P HELX_P14 AB5 LYS B 317 ? ASN B 327 ? LYS A 317 ASN A 327 1 ? 11 
HELX_P HELX_P15 AB6 SER B 337 ? TYR B 341 ? SER A 337 TYR A 341 5 ? 5  
HELX_P HELX_P16 AB7 GLY B 345 ? LYS B 352 ? GLY A 345 LYS A 352 1 ? 8  
HELX_P HELX_P17 AB8 ASN B 357 ? THR B 374 ? ASN A 357 THR A 374 1 ? 18 
HELX_P HELX_P18 AB9 LYS B 385 ? TYR B 399 ? LYS A 385 TYR A 399 1 ? 15 
HELX_P HELX_P19 AC1 TYR B 408 ? ASN B 415 ? TYR A 408 ASN A 415 1 ? 8  
HELX_P HELX_P20 AC2 HIS B 426 ? ILE B 430 ? HIS A 426 ILE A 430 1 ? 5  
HELX_P HELX_P21 AC3 ASN B 436 ? PHE B 442 ? ASN A 436 PHE A 442 5 ? 7  
HELX_P HELX_P22 AC4 ARG B 452 ? GLN B 460 ? ARG A 452 GLN A 460 1 ? 9  
HELX_P HELX_P23 AC5 TYR B 467 ? GLY B 478 ? TYR A 467 GLY A 478 1 ? 12 
HELX_P HELX_P24 AC6 GLU B 483 ? LEU B 498 ? GLU A 483 LEU A 498 1 ? 16 
HELX_P HELX_P25 AC7 ASP B 507 ? ASP B 535 ? ASP A 507 ASP A 535 1 ? 29 
HELX_P HELX_P26 AC8 THR B 554 ? PHE B 575 ? THR A 554 PHE A 575 1 ? 22 
HELX_P HELX_P27 AC9 HIS B 580 ? ALA B 606 ? HIS A 580 ALA A 606 1 ? 27 
HELX_P HELX_P28 AD1 GLN B 619 ? SER B 621 ? GLN A 619 SER A 621 5 ? 3  
HELX_P HELX_P29 AD2 ALA B 631 ? GLN B 639 ? ALA A 631 GLN A 639 1 ? 9  
HELX_P HELX_P30 AD3 PHE B 660 ? GLN B 665 ? PHE A 660 GLN A 665 1 ? 6  
HELX_P HELX_P31 AD4 GLN B 683 ? ASN B 687 ? GLN A 683 ASN A 687 1 ? 5  
HELX_P HELX_P32 AD5 ASN B 703 ? THR B 722 ? ASN A 703 THR A 722 1 ? 20 
HELX_P HELX_P33 AD6 SER B 732 ? LEU B 746 ? SER A 732 LEU A 746 1 ? 15 
HELX_P HELX_P34 AD7 PRO B 747 ? GLU B 750 ? PRO A 747 GLU A 750 5 ? 4  
HELX_P HELX_P35 AD8 TYR B 763 ? GLN B 768 ? TYR A 763 GLN A 768 1 ? 6  
HELX_P HELX_P36 AD9 ASN B 809 ? LEU B 814 ? ASN A 809 LEU A 814 1 ? 6  
HELX_P HELX_P37 AE1 MET B 815 ? PHE B 819 ? MET A 815 PHE A 819 5 ? 5  
HELX_P HELX_P38 AE2 SER B 821 ? TYR B 826 ? SER A 821 TYR A 826 1 ? 6  
HELX_P HELX_P39 AE3 TYR B 826 ? GLY B 840 ? TYR A 826 GLY A 840 1 ? 15 
HELX_P HELX_P40 AE4 ASP B 857 ? SER B 862 ? ASP A 857 SER A 862 1 ? 6  
HELX_P HELX_P41 AE5 TYR B 864 ? GLN B 870 ? TYR A 864 GLN A 870 1 ? 7  
HELX_P HELX_P42 AE6 THR B 871 ? GLU B 873 ? THR A 871 GLU A 873 5 ? 3  
HELX_P HELX_P43 AE7 ASP B 881 ? LYS B 894 ? ASP A 881 LYS A 894 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 5 ? 
AA5 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? parallel      
AA5 6 7 ? 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 ILE B 36  ? MET B 43  ? ILE A 36  MET A 43  
AA1 2 ILE B 23  ? VAL B 31  ? ILE A 23  VAL A 31  
AA1 3 TYR B 6   ? THR B 13  ? TYR A 6   THR A 13  
AA1 4 ILE B 86  ? ALA B 89  ? ILE A 86  ALA A 89  
AA1 5 VAL B 115 ? ASP B 117 ? VAL A 115 ASP A 117 
AA2 1 LYS B 213 ? PHE B 214 ? LYS A 213 PHE A 214 
AA2 2 ILE B 217 ? ILE B 218 ? ILE A 217 ILE A 218 
AA3 1 ALA B 332 ? LEU B 334 ? ALA A 332 LEU A 334 
AA3 2 ILE B 421 ? ASN B 425 ? ILE A 421 ASN A 425 
AA3 3 VAL B 301 ? THR B 305 ? VAL A 301 THR A 305 
AA3 4 ASP B 444 ? ASP B 448 ? ASP A 444 ASP A 448 
AA3 5 SER B 646 ? SER B 651 ? SER A 646 SER A 651 
AA3 6 ALA B 272 ? ALA B 276 ? ALA A 272 ALA A 276 
AA3 7 ASN B 674 ? VAL B 678 ? ASN A 674 VAL A 678 
AA4 1 THR B 462 ? SER B 466 ? THR A 462 SER A 466 
AA4 2 ILE B 623 ? LYS B 628 ? ILE A 623 LYS A 628 
AA4 3 SER B 610 ? ILE B 614 ? SER A 610 ILE A 614 
AA4 4 HIS B 547 ? VAL B 549 ? HIS A 547 VAL A 549 
AA4 5 TYR B 539 ? ASP B 540 ? TYR A 539 ASP A 540 
AA5 1 VAL B 753 ? THR B 756 ? VAL A 753 THR A 756 
AA5 2 ILE B 776 ? THR B 780 ? ILE A 776 THR A 780 
AA5 3 CYS B 726 ? LEU B 729 ? CYS A 726 LEU A 729 
AA5 4 LYS B 795 ? ILE B 799 ? LYS A 795 ILE A 799 
AA5 5 GLY B 850 ? SER B 854 ? GLY A 850 SER A 854 
AA5 6 THR B 688 ? PHE B 691 ? THR A 688 PHE A 691 
AA5 7 GLN B 877 ? LYS B 878 ? GLN A 877 LYS A 878 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O TYR B 40  ? O TYR A 40  N ILE B 28  ? N ILE A 28  
AA1 2 3 O ILE B 24  ? O ILE A 24  N GLU B 12  ? N GLU A 12  
AA1 3 4 N ALA B 7   ? N ALA A 7   O ILE B 86  ? O ILE A 86  
AA1 4 5 N PHE B 87  ? N PHE A 87  O ILE B 116 ? O ILE A 116 
AA2 1 2 N PHE B 214 ? N PHE A 214 O ILE B 217 ? O ILE A 217 
AA3 1 2 N LEU B 333 ? N LEU A 333 O ILE B 423 ? O ILE A 423 
AA3 2 3 O GLY B 422 ? O GLY A 422 N VAL B 301 ? N VAL A 301 
AA3 3 4 N MET B 302 ? N MET A 302 O ASP B 444 ? O ASP A 444 
AA3 4 5 N VAL B 447 ? N VAL A 447 O ILE B 650 ? O ILE A 650 
AA3 5 6 O PHE B 649 ? O PHE A 649 N ILE B 274 ? N ILE A 274 
AA3 6 7 N MET B 273 ? N MET A 273 O ASN B 674 ? O ASN A 674 
AA4 1 2 N ASN B 463 ? N ASN A 463 O VAL B 627 ? O VAL A 627 
AA4 2 3 O ARG B 624 ? O ARG A 624 N SER B 613 ? N SER A 613 
AA4 3 4 O ILE B 614 ? O ILE A 614 N HIS B 547 ? N HIS A 547 
AA4 4 5 O ASN B 548 ? O ASN A 548 N TYR B 539 ? N TYR A 539 
AA5 1 2 N LEU B 755 ? N LEU A 755 O GLY B 779 ? O GLY A 779 
AA5 2 3 O LEU B 778 ? O LEU A 778 N VAL B 728 ? N VAL A 728 
AA5 3 4 N LEU B 727 ? N LEU A 727 O MET B 798 ? O MET A 798 
AA5 4 5 N LYS B 795 ? N LYS A 795 O ILE B 851 ? O ILE A 851 
AA5 5 6 O ILE B 852 ? O ILE A 852 N PHE B 691 ? N PHE A 691 
AA5 6 7 N VAL B 690 ? N VAL A 690 O LYS B 878 ? O LYS A 878 
# 
_pdbx_entry_details.entry_id                   9II8 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG1 A THR 780 ? ? CE1 A PHE 783 ? ? 1.60 
2 1 O   A SER 724 ? ? OH  A TYR 752 ? ? 1.83 
3 1 CB  A THR 780 ? ? CE1 A PHE 783 ? ? 2.11 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NE2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    GLN 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    CD 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    ARG 
_pdbx_validate_symm_contact.auth_seq_id_2     241 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              1.96 
# 
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 ALA A 146 ? ? 50.14   -139.11 
2  1 ASP A 152 ? ? -84.16  -71.72  
3  1 PHE A 169 ? ? -66.15  1.97    
4  1 LYS A 171 ? ? -121.22 -164.62 
5  1 LEU A 187 ? ? -177.19 -175.49 
6  1 GLN A 201 ? ? -92.60  50.64   
7  1 GLU A 215 ? ? 47.63   -119.83 
8  1 GLN A 216 ? ? -105.45 43.16   
9  1 LYS A 226 ? ? -109.02 -166.19 
10 1 LEU A 249 ? ? -107.71 -154.81 
11 1 LYS A 299 ? ? -129.49 -165.08 
12 1 LYS A 317 ? ? -137.88 -66.22  
13 1 ASN A 327 ? ? 75.75   -4.71   
14 1 LYS A 484 ? ? 43.17   -133.95 
15 1 LEU A 498 ? ? -99.58  -63.87  
16 1 SER A 579 ? ? -145.18 -9.58   
17 1 LEU A 617 ? ? -65.09  0.10    
18 1 VAL A 640 ? ? -133.94 -63.45  
19 1 ASN A 657 ? ? 47.94   -126.72 
20 1 ASN A 668 ? ? -90.63  -70.89  
21 1 THR A 680 ? ? 55.30   18.98   
22 1 LEU A 682 ? ? 56.28   -139.24 
23 1 TYR A 752 ? ? -150.82 80.27   
24 1 TYR A 826 ? ? -136.92 -69.98  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 252 ? ? 0.077 'SIDE CHAIN' 
2 1 ARG A 834 ? ? 0.098 'SIDE CHAIN' 
3 1 ARG A 836 ? ? 0.128 'SIDE CHAIN' 
4 1 ARG A 841 ? ? 0.122 'SIDE CHAIN' 
5 1 ARG A 844 ? ? 0.088 'SIDE CHAIN' 
6 1 ARG A 876 ? ? 0.285 'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1  x,y,z                
2  -y,x,z               
3  y,-x,z               
4  x,-y,-z              
5  -x,y,-z              
6  -x,-y,z              
7  y,x,-z               
8  -y,-x,-z             
9  x+1/2,y+1/2,z+1/2    
10 -y+1/2,x+1/2,z+1/2   
11 y+1/2,-x+1/2,z+1/2   
12 x+1/2,-y+1/2,-z+1/2  
13 -x+1/2,y+1/2,-z+1/2  
14 -x+1/2,-y+1/2,z+1/2  
15 y+1/2,x+1/2,-z+1/2   
16 -y+1/2,-x+1/2,-z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         5.86308597258 
_pdbx_refine_tls.origin_y         52.9556964717 
_pdbx_refine_tls.origin_z         31.4544964426 
_pdbx_refine_tls.T[1][1]          0.664777645483 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.11155299355 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.074823334506 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.74737970334 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0590778709053 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.586231251681 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.897111263931 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.363333717919 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0171460994621 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.29722546 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.420967729634 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.309383887361 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0933945867278 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.345503088028 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.263354024583 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.375607564948 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0982395304446 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0250662657282 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0415789989298 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0968496983927 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.00418778686157 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    B 
_pdbx_refine_tls_group.beg_auth_seq_id     2 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   B 
_pdbx_refine_tls_group.end_label_seq_id    896 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     896 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     LYS 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      897 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    LYS 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     897 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
DT  OP3    O N N 88  
DT  P      P N N 89  
DT  OP1    O N N 90  
DT  OP2    O N N 91  
DT  "O5'"  O N N 92  
DT  "C5'"  C N N 93  
DT  "C4'"  C N R 94  
DT  "O4'"  O N N 95  
DT  "C3'"  C N S 96  
DT  "O3'"  O N N 97  
DT  "C2'"  C N N 98  
DT  "C1'"  C N R 99  
DT  N1     N N N 100 
DT  C2     C N N 101 
DT  O2     O N N 102 
DT  N3     N N N 103 
DT  C4     C N N 104 
DT  O4     O N N 105 
DT  C5     C N N 106 
DT  C7     C N N 107 
DT  C6     C N N 108 
DT  HOP3   H N N 109 
DT  HOP2   H N N 110 
DT  "H5'"  H N N 111 
DT  "H5''" H N N 112 
DT  "H4'"  H N N 113 
DT  "H3'"  H N N 114 
DT  "HO3'" H N N 115 
DT  "H2'"  H N N 116 
DT  "H2''" H N N 117 
DT  "H1'"  H N N 118 
DT  H3     H N N 119 
DT  H71    H N N 120 
DT  H72    H N N 121 
DT  H73    H N N 122 
DT  H6     H N N 123 
GLN N      N N N 124 
GLN CA     C N S 125 
GLN C      C N N 126 
GLN O      O N N 127 
GLN CB     C N N 128 
GLN CG     C N N 129 
GLN CD     C N N 130 
GLN OE1    O N N 131 
GLN NE2    N N N 132 
GLN OXT    O N N 133 
GLN H      H N N 134 
GLN H2     H N N 135 
GLN HA     H N N 136 
GLN HB2    H N N 137 
GLN HB3    H N N 138 
GLN HG2    H N N 139 
GLN HG3    H N N 140 
GLN HE21   H N N 141 
GLN HE22   H N N 142 
GLN HXT    H N N 143 
GLU N      N N N 144 
GLU CA     C N S 145 
GLU C      C N N 146 
GLU O      O N N 147 
GLU CB     C N N 148 
GLU CG     C N N 149 
GLU CD     C N N 150 
GLU OE1    O N N 151 
GLU OE2    O N N 152 
GLU OXT    O N N 153 
GLU H      H N N 154 
GLU H2     H N N 155 
GLU HA     H N N 156 
GLU HB2    H N N 157 
GLU HB3    H N N 158 
GLU HG2    H N N 159 
GLU HG3    H N N 160 
GLU HE2    H N N 161 
GLU HXT    H N N 162 
GLY N      N N N 163 
GLY CA     C N N 164 
GLY C      C N N 165 
GLY O      O N N 166 
GLY OXT    O N N 167 
GLY H      H N N 168 
GLY H2     H N N 169 
GLY HA2    H N N 170 
GLY HA3    H N N 171 
GLY HXT    H N N 172 
HIS N      N N N 173 
HIS CA     C N S 174 
HIS C      C N N 175 
HIS O      O N N 176 
HIS CB     C N N 177 
HIS CG     C Y N 178 
HIS ND1    N Y N 179 
HIS CD2    C Y N 180 
HIS CE1    C Y N 181 
HIS NE2    N Y N 182 
HIS OXT    O N N 183 
HIS H      H N N 184 
HIS H2     H N N 185 
HIS HA     H N N 186 
HIS HB2    H N N 187 
HIS HB3    H N N 188 
HIS HD1    H N N 189 
HIS HD2    H N N 190 
HIS HE1    H N N 191 
HIS HE2    H N N 192 
HIS HXT    H N N 193 
ILE N      N N N 194 
ILE CA     C N S 195 
ILE C      C N N 196 
ILE O      O N N 197 
ILE CB     C N S 198 
ILE CG1    C N N 199 
ILE CG2    C N N 200 
ILE CD1    C N N 201 
ILE OXT    O N N 202 
ILE H      H N N 203 
ILE H2     H N N 204 
ILE HA     H N N 205 
ILE HB     H N N 206 
ILE HG12   H N N 207 
ILE HG13   H N N 208 
ILE HG21   H N N 209 
ILE HG22   H N N 210 
ILE HG23   H N N 211 
ILE HD11   H N N 212 
ILE HD12   H N N 213 
ILE HD13   H N N 214 
ILE HXT    H N N 215 
LEU N      N N N 216 
LEU CA     C N S 217 
LEU C      C N N 218 
LEU O      O N N 219 
LEU CB     C N N 220 
LEU CG     C N N 221 
LEU CD1    C N N 222 
LEU CD2    C N N 223 
LEU OXT    O N N 224 
LEU H      H N N 225 
LEU H2     H N N 226 
LEU HA     H N N 227 
LEU HB2    H N N 228 
LEU HB3    H N N 229 
LEU HG     H N N 230 
LEU HD11   H N N 231 
LEU HD12   H N N 232 
LEU HD13   H N N 233 
LEU HD21   H N N 234 
LEU HD22   H N N 235 
LEU HD23   H N N 236 
LEU HXT    H N N 237 
LYS N      N N N 238 
LYS CA     C N S 239 
LYS C      C N N 240 
LYS O      O N N 241 
LYS CB     C N N 242 
LYS CG     C N N 243 
LYS CD     C N N 244 
LYS CE     C N N 245 
LYS NZ     N N N 246 
LYS OXT    O N N 247 
LYS H      H N N 248 
LYS H2     H N N 249 
LYS HA     H N N 250 
LYS HB2    H N N 251 
LYS HB3    H N N 252 
LYS HG2    H N N 253 
LYS HG3    H N N 254 
LYS HD2    H N N 255 
LYS HD3    H N N 256 
LYS HE2    H N N 257 
LYS HE3    H N N 258 
LYS HZ1    H N N 259 
LYS HZ2    H N N 260 
LYS HZ3    H N N 261 
LYS HXT    H N N 262 
MET N      N N N 263 
MET CA     C N S 264 
MET C      C N N 265 
MET O      O N N 266 
MET CB     C N N 267 
MET CG     C N N 268 
MET SD     S N N 269 
MET CE     C N N 270 
MET OXT    O N N 271 
MET H      H N N 272 
MET H2     H N N 273 
MET HA     H N N 274 
MET HB2    H N N 275 
MET HB3    H N N 276 
MET HG2    H N N 277 
MET HG3    H N N 278 
MET HE1    H N N 279 
MET HE2    H N N 280 
MET HE3    H N N 281 
MET HXT    H N N 282 
PHE N      N N N 283 
PHE CA     C N S 284 
PHE C      C N N 285 
PHE O      O N N 286 
PHE CB     C N N 287 
PHE CG     C Y N 288 
PHE CD1    C Y N 289 
PHE CD2    C Y N 290 
PHE CE1    C Y N 291 
PHE CE2    C Y N 292 
PHE CZ     C Y N 293 
PHE OXT    O N N 294 
PHE H      H N N 295 
PHE H2     H N N 296 
PHE HA     H N N 297 
PHE HB2    H N N 298 
PHE HB3    H N N 299 
PHE HD1    H N N 300 
PHE HD2    H N N 301 
PHE HE1    H N N 302 
PHE HE2    H N N 303 
PHE HZ     H N N 304 
PHE HXT    H N N 305 
PRO N      N N N 306 
PRO CA     C N S 307 
PRO C      C N N 308 
PRO O      O N N 309 
PRO CB     C N N 310 
PRO CG     C N N 311 
PRO CD     C N N 312 
PRO OXT    O N N 313 
PRO H      H N N 314 
PRO HA     H N N 315 
PRO HB2    H N N 316 
PRO HB3    H N N 317 
PRO HG2    H N N 318 
PRO HG3    H N N 319 
PRO HD2    H N N 320 
PRO HD3    H N N 321 
PRO HXT    H N N 322 
SER N      N N N 323 
SER CA     C N S 324 
SER C      C N N 325 
SER O      O N N 326 
SER CB     C N N 327 
SER OG     O N N 328 
SER OXT    O N N 329 
SER H      H N N 330 
SER H2     H N N 331 
SER HA     H N N 332 
SER HB2    H N N 333 
SER HB3    H N N 334 
SER HG     H N N 335 
SER HXT    H N N 336 
THR N      N N N 337 
THR CA     C N S 338 
THR C      C N N 339 
THR O      O N N 340 
THR CB     C N R 341 
THR OG1    O N N 342 
THR CG2    C N N 343 
THR OXT    O N N 344 
THR H      H N N 345 
THR H2     H N N 346 
THR HA     H N N 347 
THR HB     H N N 348 
THR HG1    H N N 349 
THR HG21   H N N 350 
THR HG22   H N N 351 
THR HG23   H N N 352 
THR HXT    H N N 353 
TRP N      N N N 354 
TRP CA     C N S 355 
TRP C      C N N 356 
TRP O      O N N 357 
TRP CB     C N N 358 
TRP CG     C Y N 359 
TRP CD1    C Y N 360 
TRP CD2    C Y N 361 
TRP NE1    N Y N 362 
TRP CE2    C Y N 363 
TRP CE3    C Y N 364 
TRP CZ2    C Y N 365 
TRP CZ3    C Y N 366 
TRP CH2    C Y N 367 
TRP OXT    O N N 368 
TRP H      H N N 369 
TRP H2     H N N 370 
TRP HA     H N N 371 
TRP HB2    H N N 372 
TRP HB3    H N N 373 
TRP HD1    H N N 374 
TRP HE1    H N N 375 
TRP HE3    H N N 376 
TRP HZ2    H N N 377 
TRP HZ3    H N N 378 
TRP HH2    H N N 379 
TRP HXT    H N N 380 
TYR N      N N N 381 
TYR CA     C N S 382 
TYR C      C N N 383 
TYR O      O N N 384 
TYR CB     C N N 385 
TYR CG     C Y N 386 
TYR CD1    C Y N 387 
TYR CD2    C Y N 388 
TYR CE1    C Y N 389 
TYR CE2    C Y N 390 
TYR CZ     C Y N 391 
TYR OH     O N N 392 
TYR OXT    O N N 393 
TYR H      H N N 394 
TYR H2     H N N 395 
TYR HA     H N N 396 
TYR HB2    H N N 397 
TYR HB3    H N N 398 
TYR HD1    H N N 399 
TYR HD2    H N N 400 
TYR HE1    H N N 401 
TYR HE2    H N N 402 
TYR HH     H N N 403 
TYR HXT    H N N 404 
VAL N      N N N 405 
VAL CA     C N S 406 
VAL C      C N N 407 
VAL O      O N N 408 
VAL CB     C N N 409 
VAL CG1    C N N 410 
VAL CG2    C N N 411 
VAL OXT    O N N 412 
VAL H      H N N 413 
VAL H2     H N N 414 
VAL HA     H N N 415 
VAL HB     H N N 416 
VAL HG11   H N N 417 
VAL HG12   H N N 418 
VAL HG13   H N N 419 
VAL HG21   H N N 420 
VAL HG22   H N N 421 
VAL HG23   H N N 422 
VAL HXT    H N N 423 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
DT  OP3   P      sing N N 83  
DT  OP3   HOP3   sing N N 84  
DT  P     OP1    doub N N 85  
DT  P     OP2    sing N N 86  
DT  P     "O5'"  sing N N 87  
DT  OP2   HOP2   sing N N 88  
DT  "O5'" "C5'"  sing N N 89  
DT  "C5'" "C4'"  sing N N 90  
DT  "C5'" "H5'"  sing N N 91  
DT  "C5'" "H5''" sing N N 92  
DT  "C4'" "O4'"  sing N N 93  
DT  "C4'" "C3'"  sing N N 94  
DT  "C4'" "H4'"  sing N N 95  
DT  "O4'" "C1'"  sing N N 96  
DT  "C3'" "O3'"  sing N N 97  
DT  "C3'" "C2'"  sing N N 98  
DT  "C3'" "H3'"  sing N N 99  
DT  "O3'" "HO3'" sing N N 100 
DT  "C2'" "C1'"  sing N N 101 
DT  "C2'" "H2'"  sing N N 102 
DT  "C2'" "H2''" sing N N 103 
DT  "C1'" N1     sing N N 104 
DT  "C1'" "H1'"  sing N N 105 
DT  N1    C2     sing N N 106 
DT  N1    C6     sing N N 107 
DT  C2    O2     doub N N 108 
DT  C2    N3     sing N N 109 
DT  N3    C4     sing N N 110 
DT  N3    H3     sing N N 111 
DT  C4    O4     doub N N 112 
DT  C4    C5     sing N N 113 
DT  C5    C7     sing N N 114 
DT  C5    C6     doub N N 115 
DT  C7    H71    sing N N 116 
DT  C7    H72    sing N N 117 
DT  C7    H73    sing N N 118 
DT  C6    H6     sing N N 119 
GLN N     CA     sing N N 120 
GLN N     H      sing N N 121 
GLN N     H2     sing N N 122 
GLN CA    C      sing N N 123 
GLN CA    CB     sing N N 124 
GLN CA    HA     sing N N 125 
GLN C     O      doub N N 126 
GLN C     OXT    sing N N 127 
GLN CB    CG     sing N N 128 
GLN CB    HB2    sing N N 129 
GLN CB    HB3    sing N N 130 
GLN CG    CD     sing N N 131 
GLN CG    HG2    sing N N 132 
GLN CG    HG3    sing N N 133 
GLN CD    OE1    doub N N 134 
GLN CD    NE2    sing N N 135 
GLN NE2   HE21   sing N N 136 
GLN NE2   HE22   sing N N 137 
GLN OXT   HXT    sing N N 138 
GLU N     CA     sing N N 139 
GLU N     H      sing N N 140 
GLU N     H2     sing N N 141 
GLU CA    C      sing N N 142 
GLU CA    CB     sing N N 143 
GLU CA    HA     sing N N 144 
GLU C     O      doub N N 145 
GLU C     OXT    sing N N 146 
GLU CB    CG     sing N N 147 
GLU CB    HB2    sing N N 148 
GLU CB    HB3    sing N N 149 
GLU CG    CD     sing N N 150 
GLU CG    HG2    sing N N 151 
GLU CG    HG3    sing N N 152 
GLU CD    OE1    doub N N 153 
GLU CD    OE2    sing N N 154 
GLU OE2   HE2    sing N N 155 
GLU OXT   HXT    sing N N 156 
GLY N     CA     sing N N 157 
GLY N     H      sing N N 158 
GLY N     H2     sing N N 159 
GLY CA    C      sing N N 160 
GLY CA    HA2    sing N N 161 
GLY CA    HA3    sing N N 162 
GLY C     O      doub N N 163 
GLY C     OXT    sing N N 164 
GLY OXT   HXT    sing N N 165 
HIS N     CA     sing N N 166 
HIS N     H      sing N N 167 
HIS N     H2     sing N N 168 
HIS CA    C      sing N N 169 
HIS CA    CB     sing N N 170 
HIS CA    HA     sing N N 171 
HIS C     O      doub N N 172 
HIS C     OXT    sing N N 173 
HIS CB    CG     sing N N 174 
HIS CB    HB2    sing N N 175 
HIS CB    HB3    sing N N 176 
HIS CG    ND1    sing Y N 177 
HIS CG    CD2    doub Y N 178 
HIS ND1   CE1    doub Y N 179 
HIS ND1   HD1    sing N N 180 
HIS CD2   NE2    sing Y N 181 
HIS CD2   HD2    sing N N 182 
HIS CE1   NE2    sing Y N 183 
HIS CE1   HE1    sing N N 184 
HIS NE2   HE2    sing N N 185 
HIS OXT   HXT    sing N N 186 
ILE N     CA     sing N N 187 
ILE N     H      sing N N 188 
ILE N     H2     sing N N 189 
ILE CA    C      sing N N 190 
ILE CA    CB     sing N N 191 
ILE CA    HA     sing N N 192 
ILE C     O      doub N N 193 
ILE C     OXT    sing N N 194 
ILE CB    CG1    sing N N 195 
ILE CB    CG2    sing N N 196 
ILE CB    HB     sing N N 197 
ILE CG1   CD1    sing N N 198 
ILE CG1   HG12   sing N N 199 
ILE CG1   HG13   sing N N 200 
ILE CG2   HG21   sing N N 201 
ILE CG2   HG22   sing N N 202 
ILE CG2   HG23   sing N N 203 
ILE CD1   HD11   sing N N 204 
ILE CD1   HD12   sing N N 205 
ILE CD1   HD13   sing N N 206 
ILE OXT   HXT    sing N N 207 
LEU N     CA     sing N N 208 
LEU N     H      sing N N 209 
LEU N     H2     sing N N 210 
LEU CA    C      sing N N 211 
LEU CA    CB     sing N N 212 
LEU CA    HA     sing N N 213 
LEU C     O      doub N N 214 
LEU C     OXT    sing N N 215 
LEU CB    CG     sing N N 216 
LEU CB    HB2    sing N N 217 
LEU CB    HB3    sing N N 218 
LEU CG    CD1    sing N N 219 
LEU CG    CD2    sing N N 220 
LEU CG    HG     sing N N 221 
LEU CD1   HD11   sing N N 222 
LEU CD1   HD12   sing N N 223 
LEU CD1   HD13   sing N N 224 
LEU CD2   HD21   sing N N 225 
LEU CD2   HD22   sing N N 226 
LEU CD2   HD23   sing N N 227 
LEU OXT   HXT    sing N N 228 
LYS N     CA     sing N N 229 
LYS N     H      sing N N 230 
LYS N     H2     sing N N 231 
LYS CA    C      sing N N 232 
LYS CA    CB     sing N N 233 
LYS CA    HA     sing N N 234 
LYS C     O      doub N N 235 
LYS C     OXT    sing N N 236 
LYS CB    CG     sing N N 237 
LYS CB    HB2    sing N N 238 
LYS CB    HB3    sing N N 239 
LYS CG    CD     sing N N 240 
LYS CG    HG2    sing N N 241 
LYS CG    HG3    sing N N 242 
LYS CD    CE     sing N N 243 
LYS CD    HD2    sing N N 244 
LYS CD    HD3    sing N N 245 
LYS CE    NZ     sing N N 246 
LYS CE    HE2    sing N N 247 
LYS CE    HE3    sing N N 248 
LYS NZ    HZ1    sing N N 249 
LYS NZ    HZ2    sing N N 250 
LYS NZ    HZ3    sing N N 251 
LYS OXT   HXT    sing N N 252 
MET N     CA     sing N N 253 
MET N     H      sing N N 254 
MET N     H2     sing N N 255 
MET CA    C      sing N N 256 
MET CA    CB     sing N N 257 
MET CA    HA     sing N N 258 
MET C     O      doub N N 259 
MET C     OXT    sing N N 260 
MET CB    CG     sing N N 261 
MET CB    HB2    sing N N 262 
MET CB    HB3    sing N N 263 
MET CG    SD     sing N N 264 
MET CG    HG2    sing N N 265 
MET CG    HG3    sing N N 266 
MET SD    CE     sing N N 267 
MET CE    HE1    sing N N 268 
MET CE    HE2    sing N N 269 
MET CE    HE3    sing N N 270 
MET OXT   HXT    sing N N 271 
PHE N     CA     sing N N 272 
PHE N     H      sing N N 273 
PHE N     H2     sing N N 274 
PHE CA    C      sing N N 275 
PHE CA    CB     sing N N 276 
PHE CA    HA     sing N N 277 
PHE C     O      doub N N 278 
PHE C     OXT    sing N N 279 
PHE CB    CG     sing N N 280 
PHE CB    HB2    sing N N 281 
PHE CB    HB3    sing N N 282 
PHE CG    CD1    doub Y N 283 
PHE CG    CD2    sing Y N 284 
PHE CD1   CE1    sing Y N 285 
PHE CD1   HD1    sing N N 286 
PHE CD2   CE2    doub Y N 287 
PHE CD2   HD2    sing N N 288 
PHE CE1   CZ     doub Y N 289 
PHE CE1   HE1    sing N N 290 
PHE CE2   CZ     sing Y N 291 
PHE CE2   HE2    sing N N 292 
PHE CZ    HZ     sing N N 293 
PHE OXT   HXT    sing N N 294 
PRO N     CA     sing N N 295 
PRO N     CD     sing N N 296 
PRO N     H      sing N N 297 
PRO CA    C      sing N N 298 
PRO CA    CB     sing N N 299 
PRO CA    HA     sing N N 300 
PRO C     O      doub N N 301 
PRO C     OXT    sing N N 302 
PRO CB    CG     sing N N 303 
PRO CB    HB2    sing N N 304 
PRO CB    HB3    sing N N 305 
PRO CG    CD     sing N N 306 
PRO CG    HG2    sing N N 307 
PRO CG    HG3    sing N N 308 
PRO CD    HD2    sing N N 309 
PRO CD    HD3    sing N N 310 
PRO OXT   HXT    sing N N 311 
SER N     CA     sing N N 312 
SER N     H      sing N N 313 
SER N     H2     sing N N 314 
SER CA    C      sing N N 315 
SER CA    CB     sing N N 316 
SER CA    HA     sing N N 317 
SER C     O      doub N N 318 
SER C     OXT    sing N N 319 
SER CB    OG     sing N N 320 
SER CB    HB2    sing N N 321 
SER CB    HB3    sing N N 322 
SER OG    HG     sing N N 323 
SER OXT   HXT    sing N N 324 
THR N     CA     sing N N 325 
THR N     H      sing N N 326 
THR N     H2     sing N N 327 
THR CA    C      sing N N 328 
THR CA    CB     sing N N 329 
THR CA    HA     sing N N 330 
THR C     O      doub N N 331 
THR C     OXT    sing N N 332 
THR CB    OG1    sing N N 333 
THR CB    CG2    sing N N 334 
THR CB    HB     sing N N 335 
THR OG1   HG1    sing N N 336 
THR CG2   HG21   sing N N 337 
THR CG2   HG22   sing N N 338 
THR CG2   HG23   sing N N 339 
THR OXT   HXT    sing N N 340 
TRP N     CA     sing N N 341 
TRP N     H      sing N N 342 
TRP N     H2     sing N N 343 
TRP CA    C      sing N N 344 
TRP CA    CB     sing N N 345 
TRP CA    HA     sing N N 346 
TRP C     O      doub N N 347 
TRP C     OXT    sing N N 348 
TRP CB    CG     sing N N 349 
TRP CB    HB2    sing N N 350 
TRP CB    HB3    sing N N 351 
TRP CG    CD1    doub Y N 352 
TRP CG    CD2    sing Y N 353 
TRP CD1   NE1    sing Y N 354 
TRP CD1   HD1    sing N N 355 
TRP CD2   CE2    doub Y N 356 
TRP CD2   CE3    sing Y N 357 
TRP NE1   CE2    sing Y N 358 
TRP NE1   HE1    sing N N 359 
TRP CE2   CZ2    sing Y N 360 
TRP CE3   CZ3    doub Y N 361 
TRP CE3   HE3    sing N N 362 
TRP CZ2   CH2    doub Y N 363 
TRP CZ2   HZ2    sing N N 364 
TRP CZ3   CH2    sing Y N 365 
TRP CZ3   HZ3    sing N N 366 
TRP CH2   HH2    sing N N 367 
TRP OXT   HXT    sing N N 368 
TYR N     CA     sing N N 369 
TYR N     H      sing N N 370 
TYR N     H2     sing N N 371 
TYR CA    C      sing N N 372 
TYR CA    CB     sing N N 373 
TYR CA    HA     sing N N 374 
TYR C     O      doub N N 375 
TYR C     OXT    sing N N 376 
TYR CB    CG     sing N N 377 
TYR CB    HB2    sing N N 378 
TYR CB    HB3    sing N N 379 
TYR CG    CD1    doub Y N 380 
TYR CG    CD2    sing Y N 381 
TYR CD1   CE1    sing Y N 382 
TYR CD1   HD1    sing N N 383 
TYR CD2   CE2    doub Y N 384 
TYR CD2   HD2    sing N N 385 
TYR CE1   CZ     doub Y N 386 
TYR CE1   HE1    sing N N 387 
TYR CE2   CZ     sing Y N 388 
TYR CE2   HE2    sing N N 389 
TYR CZ    OH     sing N N 390 
TYR OH    HH     sing N N 391 
TYR OXT   HXT    sing N N 392 
VAL N     CA     sing N N 393 
VAL N     H      sing N N 394 
VAL N     H2     sing N N 395 
VAL CA    C      sing N N 396 
VAL CA    CB     sing N N 397 
VAL CA    HA     sing N N 398 
VAL C     O      doub N N 399 
VAL C     OXT    sing N N 400 
VAL CB    CG1    sing N N 401 
VAL CB    CG2    sing N N 402 
VAL CB    HB     sing N N 403 
VAL CG1   HG11   sing N N 404 
VAL CG1   HG12   sing N N 405 
VAL CG1   HG13   sing N N 406 
VAL CG2   HG21   sing N N 407 
VAL CG2   HG22   sing N N 408 
VAL CG2   HG23   sing N N 409 
VAL OXT   HXT    sing N N 410 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32270043 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6FWR 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 4 2 2' 
_space_group.name_Hall        'I 4 2' 
_space_group.IT_number        97 
_space_group.crystal_system   tetragonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9II8 
_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]   0.004364 
_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]   0.004364 
_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]   0.007811 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 6.96715 ?       ? ? 11.43723 ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 7.96527 ?       ? ? 9.05267  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    P P     . DT  A 1 1   ? -13.41800 36.67700  58.73700 1.000 166.05633 ? 2   DT  B P     1 
ATOM 2    O OP1   . DT  A 1 1   ? -14.75000 36.23800  58.16100 1.000 152.36831 ? 2   DT  B OP1   1 
ATOM 3    O OP2   . DT  A 1 1   ? -13.52700 37.91600  59.60400 1.000 126.37597 ? 2   DT  B OP2   1 
ATOM 4    O "O5'" . DT  A 1 1   ? -12.95400 35.49000  59.72200 1.000 146.88159 ? 2   DT  B "O5'" 1 
ATOM 5    C "C5'" . DT  A 1 1   ? -12.18300 34.39200  59.17800 1.000 110.79377 ? 2   DT  B "C5'" 1 
ATOM 6    C "C4'" . DT  A 1 1   ? -10.88500 34.91700  58.61800 1.000 111.22679 ? 2   DT  B "C4'" 1 
ATOM 7    O "O4'" . DT  A 1 1   ? -10.41000 36.00500  59.43600 1.000 136.76265 ? 2   DT  B "O4'" 1 
ATOM 8    C "C3'" . DT  A 1 1   ? -9.74400  33.91300  58.62300 1.000 126.92021 ? 2   DT  B "C3'" 1 
ATOM 9    O "O3'" . DT  A 1 1   ? -8.73500  34.31600  57.70700 1.000 117.19716 ? 2   DT  B "O3'" 1 
ATOM 10   C "C2'" . DT  A 1 1   ? -9.22000  34.04500  60.04500 1.000 126.88022 ? 2   DT  B "C2'" 1 
ATOM 11   C "C1'" . DT  A 1 1   ? -9.47500  35.51000  60.38700 1.000 137.28720 ? 2   DT  B "C1'" 1 
ATOM 12   N N1    . DT  A 1 1   ? -10.03300 35.71300  61.74300 1.000 159.17744 ? 2   DT  B N1    1 
ATOM 13   C C2    . DT  A 1 1   ? -10.75200 36.86000  62.01900 1.000 162.41823 ? 2   DT  B C2    1 
ATOM 14   O O2    . DT  A 1 1   ? -10.92900 37.76200  61.21000 1.000 142.02329 ? 2   DT  B O2    1 
ATOM 15   N N3    . DT  A 1 1   ? -11.23300 36.94000  63.30200 1.000 164.81859 ? 2   DT  B N3    1 
ATOM 16   C C4    . DT  A 1 1   ? -11.09200 36.00400  64.30900 1.000 160.00197 ? 2   DT  B C4    1 
ATOM 17   O O4    . DT  A 1 1   ? -11.58900 36.21500  65.41800 1.000 145.82633 ? 2   DT  B O4    1 
ATOM 18   C C5    . DT  A 1 1   ? -10.34500 34.82100  63.94700 1.000 156.60673 ? 2   DT  B C5    1 
ATOM 19   C C7    . DT  A 1 1   ? -10.14400 33.75200  64.98000 1.000 140.35158 ? 2   DT  B C7    1 
ATOM 20   C C6    . DT  A 1 1   ? -9.86300  34.73200  62.69800 1.000 146.42876 ? 2   DT  B C6    1 
ATOM 21   P P     . DT  A 1 2   ? -7.50700  33.35000  57.33700 1.000 105.33508 ? 3   DT  B P     1 
ATOM 22   O OP1   . DT  A 1 2   ? -7.83200  32.37400  56.22800 1.000 120.00973 ? 3   DT  B OP1   1 
ATOM 23   O OP2   . DT  A 1 2   ? -6.83500  32.71700  58.53600 1.000 87.86802  ? 3   DT  B OP2   1 
ATOM 24   O "O5'" . DT  A 1 2   ? -6.47000  34.41800  56.73600 1.000 109.30519 ? 3   DT  B "O5'" 1 
ATOM 25   C "C5'" . DT  A 1 2   ? -6.96800  35.45700  55.86200 1.000 85.30627  ? 3   DT  B "C5'" 1 
ATOM 26   C "C4'" . DT  A 1 2   ? -5.84400  36.41800  55.57300 1.000 93.90207  ? 3   DT  B "C4'" 1 
ATOM 27   O "O4'" . DT  A 1 2   ? -5.65200  37.31500  56.68600 1.000 112.24002 ? 3   DT  B "O4'" 1 
ATOM 28   C "C3'" . DT  A 1 2   ? -4.48900  35.75400  55.38800 1.000 112.49873 ? 3   DT  B "C3'" 1 
ATOM 29   O "O3'" . DT  A 1 2   ? -4.35600  35.29500  54.04800 1.000 110.66483 ? 3   DT  B "O3'" 1 
ATOM 30   C "C2'" . DT  A 1 2   ? -3.52400  36.88600  55.71400 1.000 123.95232 ? 3   DT  B "C2'" 1 
ATOM 31   C "C1'" . DT  A 1 2   ? -4.30100  37.76500  56.69200 1.000 110.81429 ? 3   DT  B "C1'" 1 
ATOM 32   N N1    . DT  A 1 2   ? -3.77300  37.74100  58.08000 1.000 122.23343 ? 3   DT  B N1    1 
ATOM 33   C C2    . DT  A 1 2   ? -4.18400  36.76200  58.96500 1.000 126.14164 ? 3   DT  B C2    1 
ATOM 34   O O2    . DT  A 1 2   ? -4.97000  35.87000  58.68000 1.000 128.04385 ? 3   DT  B O2    1 
ATOM 35   N N3    . DT  A 1 2   ? -3.62500  36.84500  60.21600 1.000 122.60382 ? 3   DT  B N3    1 
ATOM 36   C C4    . DT  A 1 2   ? -2.72500  37.78900  60.66900 1.000 128.00977 ? 3   DT  B C4    1 
ATOM 37   O O4    . DT  A 1 2   ? -2.31100  37.73400  61.83000 1.000 133.66782 ? 3   DT  B O4    1 
ATOM 38   C C5    . DT  A 1 2   ? -2.33800  38.78500  59.69700 1.000 136.94522 ? 3   DT  B C5    1 
ATOM 39   C C7    . DT  A 1 2   ? -1.36300  39.84800  60.10500 1.000 121.00100 ? 3   DT  B C7    1 
ATOM 40   C C6    . DT  A 1 2   ? -2.87400  38.71300  58.46900 1.000 125.92632 ? 3   DT  B C6    1 
ATOM 41   P P     . DT  A 1 3   ? -3.06300  34.46400  53.58800 1.000 103.30133 ? 4   DT  B P     1 
ATOM 42   O OP1   . DT  A 1 3   ? -3.23500  33.83200  52.22500 1.000 99.31567  ? 4   DT  B OP1   1 
ATOM 43   O OP2   . DT  A 1 3   ? -2.59600  33.50300  54.65500 1.000 89.15112  ? 4   DT  B OP2   1 
ATOM 44   O "O5'" . DT  A 1 3   ? -1.92900  35.59600  53.45700 1.000 112.25390 ? 4   DT  B "O5'" 1 
ATOM 45   C "C5'" . DT  A 1 3   ? -0.58000  35.18300  53.14600 1.000 117.81820 ? 4   DT  B "C5'" 1 
ATOM 46   C "C4'" . DT  A 1 3   ? 0.39300   36.17800  53.72500 1.000 115.90026 ? 4   DT  B "C4'" 1 
ATOM 47   O "O4'" . DT  A 1 3   ? -0.07100  36.60700  55.02200 1.000 119.17419 ? 4   DT  B "O4'" 1 
ATOM 48   C "C3'" . DT  A 1 3   ? 1.80300   35.62100  53.91100 1.000 113.55482 ? 4   DT  B "C3'" 1 
ATOM 49   O "O3'" . DT  A 1 3   ? 2.72200   36.27900  53.04100 1.000 137.50775 ? 4   DT  B "O3'" 1 
ATOM 50   C "C2'" . DT  A 1 3   ? 2.15100   35.86900  55.37500 1.000 115.88948 ? 4   DT  B "C2'" 1 
ATOM 51   C "C1'" . DT  A 1 3   ? 1.02600   36.74300  55.91300 1.000 115.16595 ? 4   DT  B "C1'" 1 
ATOM 52   N N1    . DT  A 1 3   ? 0.59000   36.38000  57.28500 1.000 118.42631 ? 4   DT  B N1    1 
ATOM 53   C C2    . DT  A 1 3   ? -0.37200  35.40300  57.47000 1.000 126.02700 ? 4   DT  B C2    1 
ATOM 54   O O2    . DT  A 1 3   ? -0.90300  34.78700  56.55700 1.000 126.16869 ? 4   DT  B O2    1 
ATOM 55   N N3    . DT  A 1 3   ? -0.68900  35.14900  58.78000 1.000 127.28892 ? 4   DT  B N3    1 
ATOM 56   C C4    . DT  A 1 3   ? -0.16200  35.75600  59.90200 1.000 130.19324 ? 4   DT  B C4    1 
ATOM 57   O O4    . DT  A 1 3   ? -0.55100  35.41900  61.02200 1.000 134.86597 ? 4   DT  B O4    1 
ATOM 58   C C5    . DT  A 1 3   ? 0.83500   36.76800  59.64000 1.000 126.77694 ? 4   DT  B C5    1 
ATOM 59   C C7    . DT  A 1 3   ? 1.46000   37.48000  60.80200 1.000 134.59065 ? 4   DT  B C7    1 
ATOM 60   C C6    . DT  A 1 3   ? 1.15800   37.02600  58.36400 1.000 114.55172 ? 4   DT  B C6    1 
ATOM 61   P P     . DT  A 1 4   ? 3.02300   35.72800  51.55900 1.000 167.09294 ? 5   DT  B P     1 
ATOM 62   O OP1   . DT  A 1 4   ? 4.08000   36.55200  50.85200 1.000 133.32566 ? 5   DT  B OP1   1 
ATOM 63   O OP2   . DT  A 1 4   ? 1.74400   35.58700  50.75900 1.000 119.71593 ? 5   DT  B OP2   1 
ATOM 64   O "O5'" . DT  A 1 4   ? 3.61200   34.23300  51.74700 1.000 146.28954 ? 5   DT  B "O5'" 1 
ATOM 65   C "C5'" . DT  A 1 4   ? 4.53400   33.94400  52.83600 1.000 134.35474 ? 5   DT  B "C5'" 1 
ATOM 66   C "C4'" . DT  A 1 4   ? 5.82500   34.69900  52.64200 1.000 143.11929 ? 5   DT  B "C4'" 1 
ATOM 67   O "O4'" . DT  A 1 4   ? 5.73400   35.99300  53.27200 1.000 143.31640 ? 5   DT  B "O4'" 1 
ATOM 68   C "C3'" . DT  A 1 4   ? 7.04800   34.05500  53.28000 1.000 139.84701 ? 5   DT  B "C3'" 1 
ATOM 69   O "O3'" . DT  A 1 4   ? 7.65200   33.13100  52.37900 1.000 142.82190 ? 5   DT  B "O3'" 1 
ATOM 70   C "C2'" . DT  A 1 4   ? 7.97400   35.23900  53.53000 1.000 133.23383 ? 5   DT  B "C2'" 1 
ATOM 71   C "C1'" . DT  A 1 4   ? 7.04700   36.45500  53.56500 1.000 152.25750 ? 5   DT  B "C1'" 1 
ATOM 72   N N1    . DT  A 1 4   ? 7.03700   37.16700  54.86700 1.000 165.67441 ? 5   DT  B N1    1 
ATOM 73   C C2    . DT  A 1 4   ? 6.25400   36.69500  55.90400 1.000 159.97563 ? 5   DT  B C2    1 
ATOM 74   O O2    . DT  A 1 4   ? 5.56900   35.68300  55.83200 1.000 154.73336 ? 5   DT  B O2    1 
ATOM 75   N N3    . DT  A 1 4   ? 6.32400   37.43300  57.05900 1.000 153.91656 ? 5   DT  B N3    1 
ATOM 76   C C4    . DT  A 1 4   ? 7.06300   38.58100  57.27600 1.000 139.72072 ? 5   DT  B C4    1 
ATOM 77   O O4    . DT  A 1 4   ? 7.01800   39.14200  58.37300 1.000 125.85338 ? 5   DT  B O4    1 
ATOM 78   C C5    . DT  A 1 4   ? 7.84800   39.02700  56.14800 1.000 144.18084 ? 5   DT  B C5    1 
ATOM 79   C C7    . DT  A 1 4   ? 8.68100   40.26600  56.29600 1.000 114.43860 ? 5   DT  B C7    1 
ATOM 80   C C6    . DT  A 1 4   ? 7.79500   38.31100  55.01500 1.000 149.67575 ? 5   DT  B C6    1 
ATOM 81   N N     . MET B 2 1   ? 36.57900  76.55800  0.17600  1.000 177.70592 ? 1   MET A N     1 
ATOM 82   C CA    . MET B 2 1   ? 36.66200  75.25700  0.82900  1.000 189.34882 ? 1   MET A CA    1 
ATOM 83   C C     . MET B 2 1   ? 35.86900  74.20900  0.06300  1.000 192.69944 ? 1   MET A C     1 
ATOM 84   O O     . MET B 2 1   ? 34.69000  74.41000  -0.22700 1.000 189.67236 ? 1   MET A O     1 
ATOM 85   C CB    . MET B 2 1   ? 36.14600  75.33700  2.26900  1.000 181.01160 ? 1   MET A CB    1 
ATOM 86   C CG    . MET B 2 1   ? 37.15200  75.86700  3.27300  1.000 176.77869 ? 1   MET A CG    1 
ATOM 87   S SD    . MET B 2 1   ? 36.42500  76.04000  4.91500  1.000 176.23270 ? 1   MET A SD    1 
ATOM 88   C CE    . MET B 2 1   ? 37.89300  76.35100  5.89100  1.000 185.25702 ? 1   MET A CE    1 
ATOM 89   N N     . GLY B 2 2   ? 36.51700  73.09600  -0.26900 1.000 194.31925 ? 2   GLY A N     1 
ATOM 90   C CA    . GLY B 2 2   ? 35.78100  71.97400  -0.82500 1.000 173.21651 ? 2   GLY A CA    1 
ATOM 91   C C     . GLY B 2 2   ? 34.77800  71.44000  0.18200  1.000 186.02402 ? 2   GLY A C     1 
ATOM 92   O O     . GLY B 2 2   ? 35.03800  71.40200  1.38600  1.000 185.50039 ? 2   GLY A O     1 
ATOM 93   N N     . MET B 2 3   ? 33.61100  71.04000  -0.31900 1.000 187.61185 ? 3   MET A N     1 
ATOM 94   C CA    . MET B 2 3   ? 32.55100  70.57100  0.56400  1.000 168.44912 ? 3   MET A CA    1 
ATOM 95   C C     . MET B 2 3   ? 32.99700  69.32500  1.32000  1.000 167.83464 ? 3   MET A C     1 
ATOM 96   O O     . MET B 2 3   ? 33.61500  68.41900  0.75400  1.000 174.51842 ? 3   MET A O     1 
ATOM 97   C CB    . MET B 2 3   ? 31.27400  70.29300  -0.23200 1.000 158.72060 ? 3   MET A CB    1 
ATOM 98   C CG    . MET B 2 3   ? 30.71600  71.53000  -0.92200 1.000 160.57032 ? 3   MET A CG    1 
ATOM 99   S SD    . MET B 2 3   ? 29.11200  71.27700  -1.70800 1.000 162.79619 ? 3   MET A SD    1 
ATOM 100  C CE    . MET B 2 3   ? 28.01200  71.35100  -0.29500 1.000 154.90504 ? 3   MET A CE    1 
ATOM 101  N N     . ALA B 2 4   ? 32.67900  69.29200  2.61200  1.000 158.29099 ? 4   ALA A N     1 
ATOM 102  C CA    . ALA B 2 4   ? 33.19200  68.26600  3.50800  1.000 155.55484 ? 4   ALA A CA    1 
ATOM 103  C C     . ALA B 2 4   ? 32.69600  66.87800  3.11600  1.000 160.25968 ? 4   ALA A C     1 
ATOM 104  O O     . ALA B 2 4   ? 31.56400  66.69700  2.66000  1.000 153.60080 ? 4   ALA A O     1 
ATOM 105  C CB    . ALA B 2 4   ? 32.78500  68.57100  4.95100  1.000 151.08073 ? 4   ALA A CB    1 
ATOM 106  N N     . THR B 2 5   ? 33.56600  65.89100  3.30500  1.000 166.83525 ? 5   THR A N     1 
ATOM 107  C CA    . THR B 2 5   ? 33.24300  64.48800  3.09300  1.000 162.49493 ? 5   THR A CA    1 
ATOM 108  C C     . THR B 2 5   ? 33.14100  63.79300  4.44300  1.000 155.75927 ? 5   THR A C     1 
ATOM 109  O O     . THR B 2 5   ? 34.02800  63.93800  5.29000  1.000 157.42931 ? 5   THR A O     1 
ATOM 110  C CB    . THR B 2 5   ? 34.30300  63.80700  2.22400  1.000 165.88666 ? 5   THR A CB    1 
ATOM 111  O OG1   . THR B 2 5   ? 34.45100  64.53800  1.00300  1.000 170.47334 ? 5   THR A OG1   1 
ATOM 112  C CG2   . THR B 2 5   ? 33.89700  62.37800  1.89800  1.000 159.73149 ? 5   THR A CG2   1 
ATOM 113  N N     . TYR B 2 6   ? 32.06400  63.04400  4.64000  1.000 155.18684 ? 6   TYR A N     1 
ATOM 114  C CA    . TYR B 2 6   ? 31.82200  62.30900  5.87300  1.000 153.22262 ? 6   TYR A CA    1 
ATOM 115  C C     . TYR B 2 6   ? 32.25700  60.86100  5.70300  1.000 157.29747 ? 6   TYR A C     1 
ATOM 116  O O     . TYR B 2 6   ? 31.82900  60.18700  4.75900  1.000 169.37523 ? 6   TYR A O     1 
ATOM 117  C CB    . TYR B 2 6   ? 30.34500  62.36700  6.25800  1.000 154.99747 ? 6   TYR A CB    1 
ATOM 118  C CG    . TYR B 2 6   ? 29.82800  63.76800  6.42200  1.000 157.74795 ? 6   TYR A CG    1 
ATOM 119  C CD1   . TYR B 2 6   ? 29.92600  64.41700  7.63800  1.000 154.87712 ? 6   TYR A CD1   1 
ATOM 120  C CD2   . TYR B 2 6   ? 29.25300  64.45100  5.35500  1.000 157.76414 ? 6   TYR A CD2   1 
ATOM 121  C CE1   . TYR B 2 6   ? 29.46500  65.69600  7.79300  1.000 150.62241 ? 6   TYR A CE1   1 
ATOM 122  C CE2   . TYR B 2 6   ? 28.78400  65.74200  5.50400  1.000 146.08008 ? 6   TYR A CE2   1 
ATOM 123  C CZ    . TYR B 2 6   ? 28.89200  66.36000  6.72800  1.000 147.23820 ? 6   TYR A CZ    1 
ATOM 124  O OH    . TYR B 2 6   ? 28.42600  67.64500  6.88600  1.000 145.07761 ? 6   TYR A OH    1 
ATOM 125  N N     . ALA B 2 7   ? 33.10500  60.39100  6.61400  1.000 149.24721 ? 7   ALA A N     1 
ATOM 126  C CA    . ALA B 2 7   ? 33.48200  58.98200  6.68300  1.000 149.40822 ? 7   ALA A CA    1 
ATOM 127  C C     . ALA B 2 7   ? 32.65400  58.34800  7.79500  1.000 152.94885 ? 7   ALA A C     1 
ATOM 128  O O     . ALA B 2 7   ? 32.99900  58.44600  8.97600  1.000 151.25436 ? 7   ALA A O     1 
ATOM 129  C CB    . ALA B 2 7   ? 34.98000  58.82400  6.92300  1.000 150.93800 ? 7   ALA A CB    1 
ATOM 130  N N     . VAL B 2 8   ? 31.54700  57.71600  7.41300  1.000 151.04054 ? 8   VAL A N     1 
ATOM 131  C CA    . VAL B 2 8   ? 30.68400  57.03400  8.37200  1.000 144.09679 ? 8   VAL A CA    1 
ATOM 132  C C     . VAL B 2 8   ? 31.22500  55.62700  8.58100  1.000 150.62558 ? 8   VAL A C     1 
ATOM 133  O O     . VAL B 2 8   ? 31.18400  54.79300  7.67000  1.000 155.75563 ? 8   VAL A O     1 
ATOM 134  C CB    . VAL B 2 8   ? 29.22700  57.00200  7.89100  1.000 143.45303 ? 8   VAL A CB    1 
ATOM 135  C CG1   . VAL B 2 8   ? 28.34000  56.38400  8.95300  1.000 156.41228 ? 8   VAL A CG1   1 
ATOM 136  C CG2   . VAL B 2 8   ? 28.75000  58.40300  7.54200  1.000 143.07899 ? 8   VAL A CG2   1 
ATOM 137  N N     . VAL B 2 9   ? 31.71500  55.35800  9.78600  1.000 159.18078 ? 9   VAL A N     1 
ATOM 138  C CA    . VAL B 2 9   ? 32.50600  54.17100  10.08100 1.000 158.08601 ? 9   VAL A CA    1 
ATOM 139  C C     . VAL B 2 9   ? 31.74400  53.27600  11.04700 1.000 162.48176 ? 9   VAL A C     1 
ATOM 140  O O     . VAL B 2 9   ? 31.03800  53.76500  11.93400 1.000 167.58876 ? 9   VAL A O     1 
ATOM 141  C CB    . VAL B 2 9   ? 33.87500  54.56700  10.67400 1.000 150.30431 ? 9   VAL A CB    1 
ATOM 142  C CG1   . VAL B 2 9   ? 34.67000  53.34200  11.08100 1.000 150.25400 ? 9   VAL A CG1   1 
ATOM 143  C CG2   . VAL B 2 9   ? 34.65600  55.41700  9.68300  1.000 151.59941 ? 9   VAL A CG2   1 
ATOM 144  N N     . ASP B 2 10  ? 31.87900  51.96300  10.86500 1.000 157.72777 ? 10  ASP A N     1 
ATOM 145  C CA    . ASP B 2 10  ? 31.43500  50.99200  11.85100 1.000 158.34112 ? 10  ASP A CA    1 
ATOM 146  C C     . ASP B 2 10  ? 32.42700  49.84100  11.91100 1.000 163.54859 ? 10  ASP A C     1 
ATOM 147  O O     . ASP B 2 10  ? 33.06400  49.48900  10.91200 1.000 173.17583 ? 10  ASP A O     1 
ATOM 148  C CB    . ASP B 2 10  ? 30.04400  50.44400  11.55400 1.000 158.07237 ? 10  ASP A CB    1 
ATOM 149  C CG    . ASP B 2 10  ? 29.55500  49.49400  12.64000 1.000 167.08388 ? 10  ASP A CG    1 
ATOM 150  O OD1   . ASP B 2 10  ? 29.19800  49.97400  13.73700 1.000 157.72454 ? 10  ASP A OD1   1 
ATOM 151  O OD2   . ASP B 2 10  ? 29.50900  48.27200  12.38600 1.000 173.68748 ? 10  ASP A OD2   1 
ATOM 152  N N     . LEU B 2 11  ? 32.54100  49.25500  13.10100 1.000 161.41806 ? 11  LEU A N     1 
ATOM 153  C CA    . LEU B 2 11  ? 33.51600  48.21400  13.37200 1.000 164.66376 ? 11  LEU A CA    1 
ATOM 154  C C     . LEU B 2 11  ? 32.84700  47.04700  14.07700 1.000 169.64705 ? 11  LEU A C     1 
ATOM 155  O O     . LEU B 2 11  ? 31.96600  47.23600  14.92200 1.000 178.77220 ? 11  LEU A O     1 
ATOM 156  C CB    . LEU B 2 11  ? 34.66400  48.74500  14.23900 1.000 160.00168 ? 11  LEU A CB    1 
ATOM 157  C CG    . LEU B 2 11  ? 35.39600  49.97600  13.70700 1.000 159.17829 ? 11  LEU A CG    1 
ATOM 158  C CD1   . LEU B 2 11  ? 36.41200  50.47700  14.71500 1.000 162.16514 ? 11  LEU A CD1   1 
ATOM 159  C CD2   . LEU B 2 11  ? 36.06400  49.64600  12.38600 1.000 161.24745 ? 11  LEU A CD2   1 
ATOM 160  N N     . GLU B 2 12  ? 33.27100  45.84300  13.71500 1.000 171.38280 ? 12  GLU A N     1 
ATOM 161  C CA    . GLU B 2 12  ? 33.01000  44.64300  14.48900 1.000 169.29660 ? 12  GLU A CA    1 
ATOM 162  C C     . GLU B 2 12  ? 34.32400  44.14000  15.06600 1.000 180.36832 ? 12  GLU A C     1 
ATOM 163  O O     . GLU B 2 12  ? 35.33800  44.06500  14.35800 1.000 185.56553 ? 12  GLU A O     1 
ATOM 164  C CB    . GLU B 2 12  ? 32.34700  43.55600  13.63700 1.000 163.10890 ? 12  GLU A CB    1 
ATOM 165  C CG    . GLU B 2 12  ? 30.99700  43.96300  13.05200 1.000 162.08649 ? 12  GLU A CG    1 
ATOM 166  C CD    . GLU B 2 12  ? 29.90500  44.11800  14.10300 1.000 168.65065 ? 12  GLU A CD    1 
ATOM 167  O OE1   . GLU B 2 12  ? 30.18700  43.93400  15.30600 1.000 180.63597 ? 12  GLU A OE1   1 
ATOM 168  O OE2   . GLU B 2 12  ? 28.75500  44.42000  13.72100 1.000 164.18219 ? 12  GLU A OE2   1 
ATOM 169  N N     . THR B 2 13  ? 34.30200  43.81300  16.35700 1.000 184.15893 ? 13  THR A N     1 
ATOM 170  C CA    . THR B 2 13  ? 35.49800  43.45800  17.10400 1.000 189.16285 ? 13  THR A CA    1 
ATOM 171  C C     . THR B 2 13  ? 35.28800  42.12200  17.80400 1.000 189.70560 ? 13  THR A C     1 
ATOM 172  O O     . THR B 2 13  ? 34.17100  41.60400  17.88400 1.000 184.04753 ? 13  THR A O     1 
ATOM 173  C CB    . THR B 2 13  ? 35.86100  44.54500  18.13200 1.000 183.14516 ? 13  THR A CB    1 
ATOM 174  O OG1   . THR B 2 13  ? 34.77700  44.72300  19.05200 1.000 184.65132 ? 13  THR A OG1   1 
ATOM 175  C CG2   . THR B 2 13  ? 36.13400  45.87400  17.44000 1.000 172.31369 ? 13  THR A CG2   1 
ATOM 176  N N     . THR B 2 14  ? 36.38800  41.55900  18.31000 1.000 189.74528 ? 14  THR A N     1 
ATOM 177  C CA    . THR B 2 14  ? 36.31400  40.34700  19.12000 1.000 187.58631 ? 14  THR A CA    1 
ATOM 178  C C     . THR B 2 14  ? 35.71500  40.60700  20.49600 1.000 175.19230 ? 14  THR A C     1 
ATOM 179  O O     . THR B 2 14  ? 35.46500  39.65000  21.23700 1.000 165.29534 ? 14  THR A O     1 
ATOM 180  C CB    . THR B 2 14  ? 37.70600  39.72100  19.28000 1.000 186.02760 ? 14  THR A CB    1 
ATOM 181  O OG1   . THR B 2 14  ? 38.60100  40.67300  19.87200 1.000 177.21213 ? 14  THR A OG1   1 
ATOM 182  C CG2   . THR B 2 14  ? 38.26600  39.28900  17.93500 1.000 181.37779 ? 14  THR A CG2   1 
ATOM 183  N N     . GLY B 2 15  ? 35.47800  41.86800  20.84300 1.000 178.74590 ? 15  GLY A N     1 
ATOM 184  C CA    . GLY B 2 15  ? 34.95800  42.22300  22.14700 1.000 174.96294 ? 15  GLY A CA    1 
ATOM 185  C C     . GLY B 2 15  ? 34.99200  43.72800  22.33500 1.000 179.05740 ? 15  GLY A C     1 
ATOM 186  O O     . GLY B 2 15  ? 35.31000  44.48100  21.41000 1.000 185.57651 ? 15  GLY A O     1 
ATOM 187  N N     . ASN B 2 16  ? 34.66700  44.15200  23.55500 1.000 169.32294 ? 16  ASN A N     1 
ATOM 188  C CA    . ASN B 2 16  ? 34.51100  45.56600  23.87300 1.000 164.73272 ? 16  ASN A CA    1 
ATOM 189  C C     . ASN B 2 16  ? 35.68000  46.13900  24.66900 1.000 172.88875 ? 16  ASN A C     1 
ATOM 190  O O     . ASN B 2 16  ? 35.61600  47.29500  25.09700 1.000 167.76496 ? 16  ASN A O     1 
ATOM 191  C CB    . ASN B 2 16  ? 33.20500  45.78900  24.63700 1.000 149.71045 ? 16  ASN A CB    1 
ATOM 192  C CG    . ASN B 2 16  ? 31.98000  45.44500  23.80900 1.000 164.67160 ? 16  ASN A CG    1 
ATOM 193  O OD1   . ASN B 2 16  ? 32.07700  45.19000  22.60800 1.000 165.62324 ? 16  ASN A OD1   1 
ATOM 194  N ND2   . ASN B 2 16  ? 30.81600  45.45000  24.44600 1.000 157.39424 ? 16  ASN A ND2   1 
ATOM 195  N N     . GLN B 2 17  ? 36.74400  45.36800  24.87400 1.000 179.57342 ? 17  GLN A N     1 
ATOM 196  C CA    . GLN B 2 17  ? 37.90700  45.81700  25.63700 1.000 174.65055 ? 17  GLN A CA    1 
ATOM 197  C C     . GLN B 2 17  ? 38.95000  46.35700  24.66400 1.000 171.26941 ? 17  GLN A C     1 
ATOM 198  O O     . GLN B 2 17  ? 39.49200  45.60900  23.84400 1.000 170.60919 ? 17  GLN A O     1 
ATOM 199  C CB    . GLN B 2 17  ? 38.47000  44.68500  26.49400 1.000 178.20722 ? 17  GLN A CB    1 
ATOM 200  C CG    . GLN B 2 17  ? 37.51400  44.26000  27.59700 1.000 173.67049 ? 17  GLN A CG    1 
ATOM 201  C CD    . GLN B 2 17  ? 38.12400  43.28600  28.58600 1.000 178.05796 ? 17  GLN A CD    1 
ATOM 202  O OE1   . GLN B 2 17  ? 39.03500  42.52700  28.25800 1.000 185.41762 ? 17  GLN A OE1   1 
ATOM 203  N NE2   . GLN B 2 17  ? 37.61600  43.30400  29.81300 1.000 175.77155 ? 17  GLN A NE2   1 
ATOM 204  N N     . LEU B 2 18  ? 39.23700  47.65800  24.77100 1.000 157.05308 ? 18  LEU A N     1 
ATOM 205  C CA    . LEU B 2 18  ? 40.12100  48.31500  23.81400 1.000 171.97209 ? 18  LEU A CA    1 
ATOM 206  C C     . LEU B 2 18  ? 41.51500  47.70000  23.82100 1.000 186.21786 ? 18  LEU A C     1 
ATOM 207  O O     . LEU B 2 18  ? 42.13900  47.54900  22.76500 1.000 186.38355 ? 18  LEU A O     1 
ATOM 208  C CB    . LEU B 2 18  ? 40.19300  49.81100  24.12000 1.000 162.47004 ? 18  LEU A CB    1 
ATOM 209  C CG    . LEU B 2 18  ? 41.06500  50.67600  23.20600 1.000 169.46667 ? 18  LEU A CG    1 
ATOM 210  C CD1   . LEU B 2 18  ? 40.52700  50.64600  21.78800 1.000 165.85027 ? 18  LEU A CD1   1 
ATOM 211  C CD2   . LEU B 2 18  ? 41.14100  52.10300  23.73000 1.000 167.97721 ? 18  LEU A CD2   1 
ATOM 212  N N     . ASP B 2 19  ? 42.01600  47.32500  24.99800 1.000 185.15736 ? 19  ASP A N     1 
ATOM 213  C CA    . ASP B 2 19  ? 43.38900  46.84800  25.11500 1.000 185.01110 ? 19  ASP A CA    1 
ATOM 214  C C     . ASP B 2 19  ? 43.55800  45.38400  24.71800 1.000 176.28666 ? 19  ASP A C     1 
ATOM 215  O O     . ASP B 2 19  ? 44.68300  44.97100  24.41600 1.000 169.05875 ? 19  ASP A O     1 
ATOM 216  C CB    . ASP B 2 19  ? 43.89300  47.05100  26.54800 1.000 187.39228 ? 19  ASP A CB    1 
ATOM 217  C CG    . ASP B 2 19  ? 44.13100  48.51500  26.88700 1.000 192.63967 ? 19  ASP A CG    1 
ATOM 218  O OD1   . ASP B 2 19  ? 44.57600  49.27500  26.00000 1.000 188.51204 ? 19  ASP A OD1   1 
ATOM 219  O OD2   . ASP B 2 19  ? 43.87600  48.90200  28.04500 1.000 187.72197 ? 19  ASP A OD2   1 
ATOM 220  N N     . PHE B 2 20  ? 42.48000  44.59300  24.70100 1.000 189.09724 ? 20  PHE A N     1 
ATOM 221  C CA    . PHE B 2 20  ? 42.59200  43.15600  24.48200 1.000 195.29439 ? 20  PHE A CA    1 
ATOM 222  C C     . PHE B 2 20  ? 41.93400  42.65900  23.20400 1.000 199.10342 ? 20  PHE A C     1 
ATOM 223  O O     . PHE B 2 20  ? 42.22300  41.53600  22.78200 1.000 194.34252 ? 20  PHE A O     1 
ATOM 224  C CB    . PHE B 2 20  ? 41.98400  42.38700  25.66400 1.000 179.26942 ? 20  PHE A CB    1 
ATOM 225  C CG    . PHE B 2 20  ? 42.62800  42.69400  26.98300 1.000 183.49856 ? 20  PHE A CG    1 
ATOM 226  C CD1   . PHE B 2 20  ? 43.80900  42.07200  27.35500 1.000 182.83301 ? 20  PHE A CD1   1 
ATOM 227  C CD2   . PHE B 2 20  ? 42.04700  43.60000  27.85600 1.000 169.67594 ? 20  PHE A CD2   1 
ATOM 228  C CE1   . PHE B 2 20  ? 44.40300  42.35300  28.57300 1.000 169.35099 ? 20  PHE A CE1   1 
ATOM 229  C CE2   . PHE B 2 20  ? 42.63600  43.88400  29.07500 1.000 177.82297 ? 20  PHE A CE2   1 
ATOM 230  C CZ    . PHE B 2 20  ? 43.81500  43.26000  29.43400 1.000 176.43146 ? 20  PHE A CZ    1 
ATOM 231  N N     . ASP B 2 21  ? 41.07000  43.45100  22.58000 1.000 194.20263 ? 21  ASP A N     1 
ATOM 232  C CA    . ASP B 2 21  ? 40.27100  42.99300  21.45400 1.000 187.02798 ? 21  ASP A CA    1 
ATOM 233  C C     . ASP B 2 21  ? 40.74500  43.61400  20.14600 1.000 187.13210 ? 21  ASP A C     1 
ATOM 234  O O     . ASP B 2 21  ? 41.23900  44.74500  20.11400 1.000 177.02200 ? 21  ASP A O     1 
ATOM 235  C CB    . ASP B 2 21  ? 38.79400  43.31100  21.68600 1.000 176.04885 ? 21  ASP A CB    1 
ATOM 236  C CG    . ASP B 2 21  ? 38.19200  42.46600  22.78900 1.000 179.70726 ? 21  ASP A CG    1 
ATOM 237  O OD1   . ASP B 2 21  ? 38.24700  41.22300  22.67900 1.000 185.54670 ? 21  ASP A OD1   1 
ATOM 238  O OD2   . ASP B 2 21  ? 37.67400  43.03900  23.76900 1.000 181.99785 ? 21  ASP A OD2   1 
ATOM 239  N N     . ASP B 2 22  ? 40.58400  42.85500  19.06500 1.000 186.80013 ? 22  ASP A N     1 
ATOM 240  C CA    . ASP B 2 22  ? 40.98300  43.27200  17.73000 1.000 189.51840 ? 22  ASP A CA    1 
ATOM 241  C C     . ASP B 2 22  ? 39.76100  43.61300  16.88600 1.000 185.94287 ? 22  ASP A C     1 
ATOM 242  O O     . ASP B 2 22  ? 38.65200  43.13700  17.14300 1.000 176.59005 ? 22  ASP A O     1 
ATOM 243  C CB    . ASP B 2 22  ? 41.79500  42.17500  17.03000 1.000 187.12714 ? 22  ASP A CB    1 
ATOM 244  C CG    . ASP B 2 22  ? 43.21600  42.06700  17.55100 1.000 181.58625 ? 22  ASP A CG    1 
ATOM 245  O OD1   . ASP B 2 22  ? 43.69800  43.03000  18.18100 1.000 179.40349 ? 22  ASP A OD1   1 
ATOM 246  O OD2   . ASP B 2 22  ? 43.85500  41.02000  17.31600 1.000 188.74043 ? 22  ASP A OD2   1 
ATOM 247  N N     . ILE B 2 23  ? 39.98000  44.44900  15.87200 1.000 187.40327 ? 23  ILE A N     1 
ATOM 248  C CA    . ILE B 2 23  ? 38.96400  44.69100  14.85500 1.000 181.45273 ? 23  ILE A CA    1 
ATOM 249  C C     . ILE B 2 23  ? 38.89300  43.48100  13.93300 1.000 186.42458 ? 23  ILE A C     1 
ATOM 250  O O     . ILE B 2 23  ? 39.91900  43.01300  13.42300 1.000 177.36122 ? 23  ILE A O     1 
ATOM 251  C CB    . ILE B 2 23  ? 39.29000  45.97400  14.07400 1.000 171.12886 ? 23  ILE A CB    1 
ATOM 252  C CG1   . ILE B 2 23  ? 39.32800  47.18400  15.01300 1.000 166.97005 ? 23  ILE A CG1   1 
ATOM 253  C CG2   . ILE B 2 23  ? 38.29200  46.19300  12.94800 1.000 177.08361 ? 23  ILE A CG2   1 
ATOM 254  C CD1   . ILE B 2 23  ? 39.77500  48.46800  14.33700 1.000 187.17055 ? 23  ILE A CD1   1 
ATOM 255  N N     . ILE B 2 24  ? 37.68600  42.95300  13.72700 1.000 185.36018 ? 24  ILE A N     1 
ATOM 256  C CA    . ILE B 2 24  ? 37.48900  41.84600  12.80000 1.000 191.34688 ? 24  ILE A CA    1 
ATOM 257  C C     . ILE B 2 24  ? 36.73300  42.25500  11.54200 1.000 189.34168 ? 24  ILE A C     1 
ATOM 258  O O     . ILE B 2 24  ? 36.79100  41.52200  10.54200 1.000 189.99982 ? 24  ILE A O     1 
ATOM 259  C CB    . ILE B 2 24  ? 36.79200  40.64400  13.47500 1.000 187.03188 ? 24  ILE A CB    1 
ATOM 260  C CG1   . ILE B 2 24  ? 35.42500  41.03600  14.04300 1.000 174.79432 ? 24  ILE A CG1   1 
ATOM 261  C CG2   . ILE B 2 24  ? 37.68500  40.05500  14.54800 1.000 190.44481 ? 24  ILE A CG2   1 
ATOM 262  C CD1   . ILE B 2 24  ? 34.67000  39.88600  14.68100 1.000 169.06725 ? 24  ILE A CD1   1 
ATOM 263  N N     . GLN B 2 25  ? 36.03900  43.39200  11.54600 1.000 186.76119 ? 25  GLN A N     1 
ATOM 264  C CA    . GLN B 2 25  ? 35.41800  43.88500  10.32500 1.000 179.88797 ? 25  GLN A CA    1 
ATOM 265  C C     . GLN B 2 25  ? 35.33400  45.40200  10.37400 1.000 184.54493 ? 25  GLN A C     1 
ATOM 266  O O     . GLN B 2 25  ? 35.01100  45.97700  11.41600 1.000 185.70779 ? 25  GLN A O     1 
ATOM 267  C CB    . GLN B 2 25  ? 34.02000  43.29300  10.11700 1.000 179.63204 ? 25  GLN A CB    1 
ATOM 268  C CG    . GLN B 2 25  ? 33.46000  43.57400  8.73100  1.000 174.43953 ? 25  GLN A CG    1 
ATOM 269  C CD    . GLN B 2 25  ? 32.04200  43.07900  8.54800  1.000 171.43442 ? 25  GLN A CD    1 
ATOM 270  O OE1   . GLN B 2 25  ? 31.42000  42.57200  9.48100  1.000 172.52163 ? 25  GLN A OE1   1 
ATOM 271  N NE2   . GLN B 2 25  ? 31.51900  43.23000  7.33700  1.000 173.52368 ? 25  GLN A NE2   1 
ATOM 272  N N     . ILE B 2 26  ? 35.61600  46.04700  9.24500  1.000 187.45303 ? 26  ILE A N     1 
ATOM 273  C CA    . ILE B 2 26  ? 35.50200  47.49600  9.13200  1.000 183.89414 ? 26  ILE A CA    1 
ATOM 274  C C     . ILE B 2 26  ? 34.63300  47.83300  7.93400  1.000 179.65868 ? 26  ILE A C     1 
ATOM 275  O O     . ILE B 2 26  ? 34.80800  47.26400  6.84000  1.000 183.80984 ? 26  ILE A O     1 
ATOM 276  C CB    . ILE B 2 26  ? 36.88400  48.18200  9.03900  1.000 174.79105 ? 26  ILE A CB    1 
ATOM 277  C CG1   . ILE B 2 26  ? 36.73000  49.69600  8.84600  1.000 167.98251 ? 26  ILE A CG1   1 
ATOM 278  C CG2   . ILE B 2 26  ? 37.73700  47.56500  7.93900  1.000 185.71972 ? 26  ILE A CG2   1 
ATOM 279  C CD1   . ILE B 2 26  ? 38.00900  50.48400  9.08000  1.000 167.96370 ? 26  ILE A CD1   1 
ATOM 280  N N     . GLY B 2 27  ? 33.67400  48.72500  8.12900  1.000 175.92050 ? 27  GLY A N     1 
ATOM 281  C CA    . GLY B 2 27  ? 32.87700  49.25800  7.04700  1.000 173.02195 ? 27  GLY A CA    1 
ATOM 282  C C     . GLY B 2 27  ? 32.83900  50.78100  7.09800  1.000 175.05612 ? 27  GLY A C     1 
ATOM 283  O O     . GLY B 2 27  ? 32.69600  51.36000  8.17100  1.000 169.79535 ? 27  GLY A O     1 
ATOM 284  N N     . ILE B 2 28  ? 32.97700  51.39300  5.93500  1.000 181.36756 ? 28  ILE A N     1 
ATOM 285  C CA    . ILE B 2 28  ? 33.02600  52.84800  5.81400  1.000 168.87019 ? 28  ILE A CA    1 
ATOM 286  C C     . ILE B 2 28  ? 32.15000  53.25200  4.63500  1.000 162.41956 ? 28  ILE A C     1 
ATOM 287  O O     . ILE B 2 28  ? 32.24700  52.66400  3.55400  1.000 163.80337 ? 28  ILE A O     1 
ATOM 288  C CB    . ILE B 2 28  ? 34.46500  53.37200  5.61700  1.000 160.49041 ? 28  ILE A CB    1 
ATOM 289  C CG1   . ILE B 2 28  ? 35.41600  52.78400  6.67000  1.000 158.30899 ? 28  ILE A CG1   1 
ATOM 290  C CG2   . ILE B 2 28  ? 34.48300  54.89300  5.66900  1.000 157.45366 ? 28  ILE A CG2   1 
ATOM 291  C CD1   . ILE B 2 28  ? 36.87300  53.16300  6.46700  1.000 160.69920 ? 28  ILE A CD1   1 
ATOM 292  N N     . THR B 2 29  ? 31.29100  54.24600  4.84300  1.000 169.59363 ? 29  THR A N     1 
ATOM 293  C CA    . THR B 2 29  ? 30.47200  54.82600  3.78800  1.000 166.73639 ? 29  THR A CA    1 
ATOM 294  C C     . THR B 2 29  ? 30.75600  56.31900  3.72400  1.000 161.78809 ? 29  THR A C     1 
ATOM 295  O O     . THR B 2 29  ? 30.61900  57.02600  4.72900  1.000 164.31334 ? 29  THR A O     1 
ATOM 296  C CB    . THR B 2 29  ? 28.98100  54.57500  4.03300  1.000 156.44215 ? 29  THR A CB    1 
ATOM 297  O OG1   . THR B 2 29  ? 28.70400  53.17200  3.93400  1.000 158.87630 ? 29  THR A OG1   1 
ATOM 298  C CG2   . THR B 2 29  ? 28.13800  55.32000  3.01000  1.000 154.57154 ? 29  THR A CG2   1 
ATOM 299  N N     . PHE B 2 30  ? 31.14500  56.79300  2.54700  1.000 162.38650 ? 30  PHE A N     1 
ATOM 300  C CA    . PHE B 2 30  ? 31.52300  58.18200  2.34100  1.000 163.76057 ? 30  PHE A CA    1 
ATOM 301  C C     . PHE B 2 30  ? 30.33000  58.96800  1.81400  1.000 161.43258 ? 30  PHE A C     1 
ATOM 302  O O     . PHE B 2 30  ? 29.73000  58.59600  0.79900  1.000 157.38875 ? 30  PHE A O     1 
ATOM 303  C CB    . PHE B 2 30  ? 32.70400  58.27700  1.37600  1.000 160.63375 ? 30  PHE A CB    1 
ATOM 304  C CG    . PHE B 2 30  ? 33.92900  57.57000  1.86400  1.000 161.54602 ? 30  PHE A CG    1 
ATOM 305  C CD1   . PHE B 2 30  ? 34.82900  58.21700  2.69200  1.000 159.45400 ? 30  PHE A CD1   1 
ATOM 306  C CD2   . PHE B 2 30  ? 34.17000  56.25100  1.51400  1.000 166.88387 ? 30  PHE A CD2   1 
ATOM 307  C CE1   . PHE B 2 30  ? 35.95600  57.56800  3.15400  1.000 160.45031 ? 30  PHE A CE1   1 
ATOM 308  C CE2   . PHE B 2 30  ? 35.29800  55.59500  1.97300  1.000 169.52725 ? 30  PHE A CE2   1 
ATOM 309  C CZ    . PHE B 2 30  ? 36.19200  56.25600  2.79400  1.000 165.62104 ? 30  PHE A CZ    1 
ATOM 310  N N     . VAL B 2 31  ? 29.99900  60.05700  2.50200  1.000 168.41540 ? 31  VAL A N     1 
ATOM 311  C CA    . VAL B 2 31  ? 28.85000  60.89100  2.17200  1.000 166.32623 ? 31  VAL A CA    1 
ATOM 312  C C     . VAL B 2 31  ? 29.33600  62.28200  1.79700  1.000 154.98351 ? 31  VAL A C     1 
ATOM 313  O O     . VAL B 2 31  ? 30.20200  62.85000  2.47000  1.000 153.59662 ? 31  VAL A O     1 
ATOM 314  C CB    . VAL B 2 31  ? 27.84900  60.96300  3.34400  1.000 167.27752 ? 31  VAL A CB    1 
ATOM 315  C CG1   . VAL B 2 31  ? 26.68700  61.89300  3.00600  1.000 158.88737 ? 31  VAL A CG1   1 
ATOM 316  C CG2   . VAL B 2 31  ? 27.34200  59.58000  3.68100  1.000 166.10129 ? 31  VAL A CG2   1 
ATOM 317  N N     . ARG B 2 32  ? 28.77700  62.82700  0.72000  1.000 149.42232 ? 32  ARG A N     1 
ATOM 318  C CA    . ARG B 2 32  ? 29.07400  64.18600  0.29100  1.000 149.12319 ? 32  ARG A CA    1 
ATOM 319  C C     . ARG B 2 32  ? 27.82900  64.75500  -0.37000 1.000 150.35073 ? 32  ARG A C     1 
ATOM 320  O O     . ARG B 2 32  ? 27.23000  64.10300  -1.23100 1.000 163.54997 ? 32  ARG A O     1 
ATOM 321  C CB    . ARG B 2 32  ? 30.27100  64.21500  -0.66800 1.000 154.06051 ? 32  ARG A CB    1 
ATOM 322  C CG    . ARG B 2 32  ? 30.76000  65.61300  -1.02100 1.000 153.96501 ? 32  ARG A CG    1 
ATOM 323  C CD    . ARG B 2 32  ? 31.90100  65.55300  -2.02200 1.000 162.54838 ? 32  ARG A CD    1 
ATOM 324  N NE    . ARG B 2 32  ? 33.10700  64.96400  -1.44500 1.000 180.05690 ? 32  ARG A NE    1 
ATOM 325  C CZ    . ARG B 2 32  ? 34.18600  64.62900  -2.14600 1.000 186.14496 ? 32  ARG A CZ    1 
ATOM 326  N NH1   . ARG B 2 32  ? 34.21500  64.81700  -3.45800 1.000 185.05049 ? 32  ARG A NH1   1 
ATOM 327  N NH2   . ARG B 2 32  ? 35.23800  64.10200  -1.53600 1.000 178.90112 ? 32  ARG A NH2   1 
ATOM 328  N N     . ASN B 2 33  ? 27.44000  65.96100  0.05100  1.000 152.00067 ? 33  ASN A N     1 
ATOM 329  C CA    . ASN B 2 33  ? 26.25800  66.65100  -0.46700 1.000 149.23597 ? 33  ASN A CA    1 
ATOM 330  C C     . ASN B 2 33  ? 24.99500  65.81300  -0.26700 1.000 154.13028 ? 33  ASN A C     1 
ATOM 331  O O     . ASN B 2 33  ? 24.15500  65.69000  -1.16000 1.000 147.18343 ? 33  ASN A O     1 
ATOM 332  C CB    . ASN B 2 33  ? 26.44700  67.02700  -1.93900 1.000 150.46626 ? 33  ASN A CB    1 
ATOM 333  C CG    . ASN B 2 33  ? 27.60700  67.97200  -2.15400 1.000 163.01514 ? 33  ASN A CG    1 
ATOM 334  O OD1   . ASN B 2 33  ? 28.38500  68.24500  -1.23900 1.000 155.33717 ? 33  ASN A OD1   1 
ATOM 335  N ND2   . ASN B 2 33  ? 27.73400  68.47300  -3.37500 1.000 173.02498 ? 33  ASN A ND2   1 
ATOM 336  N N     . ASN B 2 34  ? 24.87600  65.22200  0.92300  1.000 155.96849 ? 34  ASN A N     1 
ATOM 337  C CA    . ASN B 2 34  ? 23.72600  64.39300  1.29500  1.000 154.77490 ? 34  ASN A CA    1 
ATOM 338  C C     . ASN B 2 34  ? 23.51200  63.24500  0.31100  1.000 159.60918 ? 34  ASN A C     1 
ATOM 339  O O     . ASN B 2 34  ? 22.38000  62.88600  -0.01600 1.000 166.26992 ? 34  ASN A O     1 
ATOM 340  C CB    . ASN B 2 34  ? 22.45900  65.24400  1.44700  1.000 149.08074 ? 34  ASN A CB    1 
ATOM 341  C CG    . ASN B 2 34  ? 22.54700  66.19600  2.62500  1.000 136.61971 ? 34  ASN A CG    1 
ATOM 342  O OD1   . ASN B 2 34  ? 23.39500  66.02700  3.50000  1.000 135.12463 ? 34  ASN A OD1   1 
ATOM 343  N ND2   . ASN B 2 34  ? 21.66900  67.19000  2.66100  1.000 135.41221 ? 34  ASN A ND2   1 
ATOM 344  N N     . GLN B 2 35  ? 24.61800  62.66300  -0.15800 1.000 152.57818 ? 35  GLN A N     1 
ATOM 345  C CA    . GLN B 2 35  ? 24.59600  61.55200  -1.09900 1.000 160.70438 ? 35  GLN A CA    1 
ATOM 346  C C     . GLN B 2 35  ? 25.76800  60.62500  -0.80700 1.000 169.53919 ? 35  GLN A C     1 
ATOM 347  O O     . GLN B 2 35  ? 26.88300  61.08400  -0.54700 1.000 161.77670 ? 35  GLN A O     1 
ATOM 348  C CB    . GLN B 2 35  ? 24.66400  62.04200  -2.55500 1.000 166.30899 ? 35  GLN A CB    1 
ATOM 349  C CG    . GLN B 2 35  ? 23.36500  62.63400  -3.07100 1.000 161.65588 ? 35  GLN A CG    1 
ATOM 350  C CD    . GLN B 2 35  ? 23.43800  62.96900  -4.54000 1.000 174.62487 ? 35  GLN A CD    1 
ATOM 351  O OE1   . GLN B 2 35  ? 24.50300  62.89100  -5.14800 1.000 176.66202 ? 35  GLN A OE1   1 
ATOM 352  N NE2   . GLN B 2 35  ? 22.30200  63.33900  -5.12500 1.000 177.42649 ? 35  GLN A NE2   1 
ATOM 353  N N     . ILE B 2 36  ? 25.50100  59.32100  -0.83600 1.000 175.32821 ? 36  ILE A N     1 
ATOM 354  C CA    . ILE B 2 36  ? 26.56100  58.33300  -0.68900 1.000 166.17851 ? 36  ILE A CA    1 
ATOM 355  C C     . ILE B 2 36  ? 27.35700  58.28500  -1.98700 1.000 160.71019 ? 36  ILE A C     1 
ATOM 356  O O     . ILE B 2 36  ? 26.80000  58.04100  -3.06400 1.000 162.04473 ? 36  ILE A O     1 
ATOM 357  C CB    . ILE B 2 36  ? 25.98300  56.95900  -0.33200 1.000 155.96083 ? 36  ILE A CB    1 
ATOM 358  C CG1   . ILE B 2 36  ? 25.29800  57.01300  1.03900  1.000 153.16379 ? 36  ILE A CG1   1 
ATOM 359  C CG2   . ILE B 2 36  ? 27.07500  55.91400  -0.35700 1.000 162.83262 ? 36  ILE A CG2   1 
ATOM 360  C CD1   . ILE B 2 36  ? 24.57000  55.73900  1.42000  1.000 148.69560 ? 36  ILE A CD1   1 
ATOM 361  N N     . ILE B 2 37  ? 28.66200  58.53700  -1.89100 1.000 165.68277 ? 37  ILE A N     1 
ATOM 362  C CA    . ILE B 2 37  ? 29.52000  58.61600  -3.06500 1.000 169.02513 ? 37  ILE A CA    1 
ATOM 363  C C     . ILE B 2 37  ? 30.46400  57.42500  -3.19600 1.000 174.92945 ? 37  ILE A C     1 
ATOM 364  O O     . ILE B 2 37  ? 30.93400  57.15400  -4.31200 1.000 183.29923 ? 37  ILE A O     1 
ATOM 365  C CB    . ILE B 2 37  ? 30.32600  59.93300  -3.07900 1.000 165.26483 ? 37  ILE A CB    1 
ATOM 366  C CG1   . ILE B 2 37  ? 31.22400  60.02800  -1.84100 1.000 162.70113 ? 37  ILE A CG1   1 
ATOM 367  C CG2   . ILE B 2 37  ? 29.39000  61.13200  -3.16800 1.000 163.47515 ? 37  ILE A CG2   1 
ATOM 368  C CD1   . ILE B 2 37  ? 32.21000  61.17900  -1.88400 1.000 163.25994 ? 37  ILE A CD1   1 
ATOM 369  N N     . ASP B 2 38  ? 30.75400  56.71000  -2.11100 1.000 173.04171 ? 38  ASP A N     1 
ATOM 370  C CA    . ASP B 2 38  ? 31.70800  55.60700  -2.14900 1.000 173.99445 ? 38  ASP A CA    1 
ATOM 371  C C     . ASP B 2 38  ? 31.55400  54.77800  -0.88000 1.000 176.85659 ? 38  ASP A C     1 
ATOM 372  O O     . ASP B 2 38  ? 31.02000  55.25000  0.12800  1.000 183.26369 ? 38  ASP A O     1 
ATOM 373  C CB    . ASP B 2 38  ? 33.14800  56.11900  -2.28700 1.000 174.60314 ? 38  ASP A CB    1 
ATOM 374  C CG    . ASP B 2 38  ? 34.11900  55.03000  -2.70200 1.000 183.59088 ? 38  ASP A CG    1 
ATOM 375  O OD1   . ASP B 2 38  ? 33.65400  53.94600  -3.11300 1.000 186.33141 ? 38  ASP A OD1   1 
ATOM 376  O OD2   . ASP B 2 38  ? 35.34500  55.25600  -2.61700 1.000 181.06352 ? 38  ASP A OD2   1 
ATOM 377  N N     . THR B 2 39  ? 32.02100  53.53000  -0.94600 1.000 174.80971 ? 39  THR A N     1 
ATOM 378  C CA    . THR B 2 39  ? 32.04500  52.65000  0.21300  1.000 176.97762 ? 39  THR A CA    1 
ATOM 379  C C     . THR B 2 39  ? 33.34600  51.86000  0.22600  1.000 182.24551 ? 39  THR A C     1 
ATOM 380  O O     . THR B 2 39  ? 33.93900  51.58500  -0.82000 1.000 181.38552 ? 39  THR A O     1 
ATOM 381  C CB    . THR B 2 39  ? 30.85400  51.67000  0.24100  1.000 170.24837 ? 39  THR A CB    1 
ATOM 382  O OG1   . THR B 2 39  ? 30.85300  50.87900  -0.95200 1.000 179.33291 ? 39  THR A OG1   1 
ATOM 383  C CG2   . THR B 2 39  ? 29.52300  52.40800  0.35800  1.000 169.54119 ? 39  THR A CG2   1 
ATOM 384  N N     . TYR B 2 40  ? 33.77900  51.50700  1.43200  1.000 189.43612 ? 40  TYR A N     1 
ATOM 385  C CA    . TYR B 2 40  ? 34.94100  50.66600  1.66500  1.000 189.98294 ? 40  TYR A CA    1 
ATOM 386  C C     . TYR B 2 40  ? 34.56100  49.63200  2.71200  1.000 189.82214 ? 40  TYR A C     1 
ATOM 387  O O     . TYR B 2 40  ? 33.86900  49.94900  3.68000  1.000 185.86961 ? 40  TYR A O     1 
ATOM 388  C CB    . TYR B 2 40  ? 36.14800  51.49500  2.12900  1.000 180.37248 ? 40  TYR A CB    1 
ATOM 389  C CG    . TYR B 2 40  ? 37.34600  50.67600  2.54900  1.000 175.56493 ? 40  TYR A CG    1 
ATOM 390  C CD1   . TYR B 2 40  ? 38.30800  50.29200  1.62400  1.000 180.18858 ? 40  TYR A CD1   1 
ATOM 391  C CD2   . TYR B 2 40  ? 37.51800  50.28900  3.87200  1.000 177.13663 ? 40  TYR A CD2   1 
ATOM 392  C CE1   . TYR B 2 40  ? 39.40600  49.54200  2.00600  1.000 186.39408 ? 40  TYR A CE1   1 
ATOM 393  C CE2   . TYR B 2 40  ? 38.60800  49.53800  4.26300  1.000 174.25592 ? 40  TYR A CE2   1 
ATOM 394  C CZ    . TYR B 2 40  ? 39.55100  49.16800  3.32700  1.000 179.84213 ? 40  TYR A CZ    1 
ATOM 395  O OH    . TYR B 2 40  ? 40.64100  48.42100  3.71400  1.000 184.94813 ? 40  TYR A OH    1 
ATOM 396  N N     . HIS B 2 41  ? 34.99500  48.39500  2.51100  1.000 186.61931 ? 41  HIS A N     1 
ATOM 397  C CA    . HIS B 2 41  ? 34.69000  47.32600  3.44600  1.000 183.09817 ? 41  HIS A CA    1 
ATOM 398  C C     . HIS B 2 41  ? 35.86400  46.36500  3.47800  1.000 186.19292 ? 41  HIS A C     1 
ATOM 399  O O     . HIS B 2 41  ? 36.52000  46.14700  2.45600  1.000 193.07685 ? 41  HIS A O     1 
ATOM 400  C CB    . HIS B 2 41  ? 33.41200  46.58300  3.04800  1.000 179.34095 ? 41  HIS A CB    1 
ATOM 401  C CG    . HIS B 2 41  ? 33.51700  45.88000  1.73200  1.000 195.43531 ? 41  HIS A CG    1 
ATOM 402  N ND1   . HIS B 2 41  ? 33.29100  46.51500  0.52900  1.000 194.95530 ? 41  HIS A ND1   1 
ATOM 403  C CD2   . HIS B 2 41  ? 33.84700  44.60200  1.42900  1.000 210.02789 ? 41  HIS A CD2   1 
ATOM 404  C CE1   . HIS B 2 41  ? 33.46800  45.65300  -0.45700 1.000 202.69982 ? 41  HIS A CE1   1 
ATOM 405  N NE2   . HIS B 2 41  ? 33.80600  44.48600  0.06200  1.000 211.36309 ? 41  HIS A NE2   1 
ATOM 406  N N     . SER B 2 42  ? 36.13600  45.80100  4.65200  1.000 186.85006 ? 42  SER A N     1 
ATOM 407  C CA    . SER B 2 42  ? 37.21200  44.82600  4.75700  1.000 194.77266 ? 42  SER A CA    1 
ATOM 408  C C     . SER B 2 42  ? 37.00000  43.96500  5.99000  1.000 189.57577 ? 42  SER A C     1 
ATOM 409  O O     . SER B 2 42  ? 36.82000  44.49100  7.09400  1.000 187.30065 ? 42  SER A O     1 
ATOM 410  C CB    . SER B 2 42  ? 38.58100  45.51500  4.81900  1.000 194.31994 ? 42  SER A CB    1 
ATOM 411  O OG    . SER B 2 42  ? 39.63100  44.56200  4.81700  1.000 199.39323 ? 42  SER A OG    1 
ATOM 412  N N     . MET B 2 43  ? 36.99900  42.65100  5.79400  1.000 184.81299 ? 43  MET A N     1 
ATOM 413  C CA    . MET B 2 43  ? 37.20600  41.74200  6.90700  1.000 182.34726 ? 43  MET A CA    1 
ATOM 414  C C     . MET B 2 43  ? 38.65700  41.84400  7.35900  1.000 192.42595 ? 43  MET A C     1 
ATOM 415  O O     . MET B 2 43  ? 39.57100  42.00800  6.54700  1.000 203.61888 ? 43  MET A O     1 
ATOM 416  C CB    . MET B 2 43  ? 36.86900  40.30500  6.50400  1.000 184.80451 ? 43  MET A CB    1 
ATOM 417  C CG    . MET B 2 43  ? 35.49200  40.14000  5.87900  1.000 188.19366 ? 43  MET A CG    1 
ATOM 418  S SD    . MET B 2 43  ? 34.14000  40.42600  7.03800  1.000 182.89882 ? 43  MET A SD    1 
ATOM 419  C CE    . MET B 2 43  ? 34.19300  38.92000  8.00700  1.000 178.69229 ? 43  MET A CE    1 
ATOM 420  N N     . ILE B 2 44  ? 38.87000  41.77400  8.66700  1.000 191.18258 ? 44  ILE A N     1 
ATOM 421  C CA    . ILE B 2 44  ? 40.20000  41.92000  9.24500  1.000 199.28280 ? 44  ILE A CA    1 
ATOM 422  C C     . ILE B 2 44  ? 40.55500  40.62000  9.95300  1.000 205.32592 ? 44  ILE A C     1 
ATOM 423  O O     . ILE B 2 44  ? 39.74200  40.07600  10.71000 1.000 194.84031 ? 44  ILE A O     1 
ATOM 424  C CB    . ILE B 2 44  ? 40.27200  43.12500  10.20200 1.000 184.57850 ? 44  ILE A CB    1 
ATOM 425  C CG1   . ILE B 2 44  ? 39.89500  44.40900  9.46300  1.000 180.27916 ? 44  ILE A CG1   1 
ATOM 426  C CG2   . ILE B 2 44  ? 41.67200  43.27600  10.78000 1.000 191.61552 ? 44  ILE A CG2   1 
ATOM 427  C CD1   . ILE B 2 44  ? 40.81500  44.74000  8.30000  1.000 183.53837 ? 44  ILE A CD1   1 
ATOM 428  N N     . ARG B 2 45  ? 41.76000  40.11500  9.69300  1.000 203.37306 ? 45  ARG A N     1 
ATOM 429  C CA    . ARG B 2 45  ? 42.19400  38.85300  10.27800 1.000 199.19984 ? 45  ARG A CA    1 
ATOM 430  C C     . ARG B 2 45  ? 42.83300  39.08700  11.64200 1.000 206.81377 ? 45  ARG A C     1 
ATOM 431  O O     . ARG B 2 45  ? 43.67800  39.97400  11.80300 1.000 205.92200 ? 45  ARG A O     1 
ATOM 432  C CB    . ARG B 2 45  ? 43.17200  38.13100  9.34700  1.000 209.34560 ? 45  ARG A CB    1 
ATOM 433  C CG    . ARG B 2 45  ? 43.78400  36.86100  9.94900  1.000 211.48558 ? 45  ARG A CG    1 
ATOM 434  C CD    . ARG B 2 45  ? 44.50100  36.02000  8.89800  1.000 211.91027 ? 45  ARG A CD    1 
ATOM 435  N NE    . ARG B 2 45  ? 45.36700  34.99600  9.48400  1.000 215.21038 ? 45  ARG A NE    1 
ATOM 436  C CZ    . ARG B 2 45  ? 45.89100  33.98200  8.80100  1.000 210.95008 ? 45  ARG A CZ    1 
ATOM 437  N NH1   . ARG B 2 45  ? 45.63000  33.85000  7.50900  1.000 212.51603 ? 45  ARG A NH1   1 
ATOM 438  N NH2   . ARG B 2 45  ? 46.67100  33.09600  9.40800  1.000 208.01374 ? 45  ARG A NH2   1 
ATOM 439  N N     . THR B 2 46  ? 42.42500  38.28400  12.62200 1.000 208.14001 ? 46  THR A N     1 
ATOM 440  C CA    . THR B 2 46  ? 42.97000  38.32600  13.96900 1.000 203.92501 ? 46  THR A CA    1 
ATOM 441  C C     . THR B 2 46  ? 43.50400  36.95200  14.35500 1.000 201.11615 ? 46  THR A C     1 
ATOM 442  O O     . THR B 2 46  ? 43.12100  35.92600  13.78500 1.000 199.42733 ? 46  THR A O     1 
ATOM 443  C CB    . THR B 2 46  ? 41.91200  38.77900  14.98600 1.000 195.71828 ? 46  THR A CB    1 
ATOM 444  O OG1   . THR B 2 46  ? 42.48200  38.78900  16.30000 1.000 188.36834 ? 46  THR A OG1   1 
ATOM 445  C CG2   . THR B 2 46  ? 40.72000  37.83800  14.96100 1.000 189.92956 ? 46  THR A CG2   1 
ATOM 446  N N     . ASN B 2 47  ? 44.40800  36.94800  15.33300 1.000 199.74396 ? 47  ASN A N     1 
ATOM 447  C CA    . ASN B 2 47  ? 44.93500  35.72100  15.91200 1.000 203.08279 ? 47  ASN A CA    1 
ATOM 448  C C     . ASN B 2 47  ? 44.20900  35.32700  17.19200 1.000 193.13924 ? 47  ASN A C     1 
ATOM 449  O O     . ASN B 2 47  ? 44.57700  34.33000  17.82100 1.000 194.83343 ? 47  ASN A O     1 
ATOM 450  C CB    . ASN B 2 47  ? 46.43800  35.86800  16.18400 1.000 193.74513 ? 47  ASN A CB    1 
ATOM 451  C CG    . ASN B 2 47  ? 47.24800  36.07500  14.91300 1.000 193.75570 ? 47  ASN A CG    1 
ATOM 452  O OD1   . ASN B 2 47  ? 46.90500  35.55600  13.85200 1.000 195.65600 ? 47  ASN A OD1   1 
ATOM 453  N ND2   . ASN B 2 47  ? 48.32900  36.84000  15.01900 1.000 204.01909 ? 47  ASN A ND2   1 
ATOM 454  N N     . LEU B 2 48  ? 43.18700  36.08000  17.58200 1.000 189.50926 ? 48  LEU A N     1 
ATOM 455  C CA    . LEU B 2 48  ? 42.41000  35.79800  18.77800 1.000 198.59292 ? 48  LEU A CA    1 
ATOM 456  C C     . LEU B 2 48  ? 41.21800  34.91000  18.44900 1.000 194.79631 ? 48  LEU A C     1 
ATOM 457  O O     . LEU B 2 48  ? 40.65500  34.96500  17.35200 1.000 194.66579 ? 48  LEU A O     1 
ATOM 458  C CB    . LEU B 2 48  ? 41.91300  37.09500  19.41900 1.000 187.56311 ? 48  LEU A CB    1 
ATOM 459  C CG    . LEU B 2 48  ? 42.95500  38.14700  19.79700 1.000 181.92908 ? 48  LEU A CG    1 
ATOM 460  C CD1   . LEU B 2 48  ? 42.27800  39.44300  20.21900 1.000 173.17612 ? 48  LEU A CD1   1 
ATOM 461  C CD2   . LEU B 2 48  ? 43.86100  37.62800  20.90100 1.000 187.02955 ? 48  LEU A CD2   1 
ATOM 462  N N     . GLU B 2 49  ? 40.83300  34.09300  19.42300 1.000 192.47048 ? 49  GLU A N     1 
ATOM 463  C CA    . GLU B 2 49  ? 39.61900  33.30000  19.29900 1.000 189.77100 ? 49  GLU A CA    1 
ATOM 464  C C     . GLU B 2 49  ? 38.39900  34.20000  19.45500 1.000 193.16936 ? 49  GLU A C     1 
ATOM 465  O O     . GLU B 2 49  ? 38.32300  35.00600  20.38600 1.000 189.67888 ? 49  GLU A O     1 
ATOM 466  C CB    . GLU B 2 49  ? 39.60800  32.19500  20.35000 1.000 184.34814 ? 49  GLU A CB    1 
ATOM 467  C CG    . GLU B 2 49  ? 38.43800  31.24000  20.24800 1.000 176.76367 ? 49  GLU A CG    1 
ATOM 468  C CD    . GLU B 2 49  ? 38.47700  30.17200  21.32000 1.000 178.41425 ? 49  GLU A CD    1 
ATOM 469  O OE1   . GLU B 2 49  ? 39.47500  30.11500  22.06900 1.000 182.00335 ? 49  GLU A OE1   1 
ATOM 470  O OE2   . GLU B 2 49  ? 37.50700  29.39300  21.41600 1.000 172.48948 ? 49  GLU A OE2   1 
ATOM 471  N N     . ILE B 2 50  ? 37.44700  34.08000  18.53100 1.000 194.56251 ? 50  ILE A N     1 
ATOM 472  C CA    . ILE B 2 50  ? 36.23400  34.87900  18.55100 1.000 188.46434 ? 50  ILE A CA    1 
ATOM 473  C C     . ILE B 2 50  ? 35.24300  34.20000  19.49500 1.000 185.73591 ? 50  ILE A C     1 
ATOM 474  O O     . ILE B 2 50  ? 34.85500  33.04800  19.23600 1.000 193.39262 ? 50  ILE A O     1 
ATOM 475  C CB    . ILE B 2 50  ? 35.63400  35.03600  17.14500 1.000 187.05575 ? 50  ILE A CB    1 
ATOM 476  C CG1   . ILE B 2 50  ? 36.70400  35.53300  16.16500 1.000 182.25380 ? 50  ILE A CG1   1 
ATOM 477  C CG2   . ILE B 2 50  ? 34.45700  36.00000  17.17500 1.000 190.55591 ? 50  ILE A CG2   1 
ATOM 478  C CD1   . ILE B 2 50  ? 36.18700  35.75400  14.75900 1.000 179.82544 ? 50  ILE A CD1   1 
ATOM 479  N N     . PRO B 2 51  ? 34.83000  34.84800  20.58200 1.000 177.74150 ? 51  PRO A N     1 
ATOM 480  C CA    . PRO B 2 51  ? 33.88100  34.22100  21.51100 1.000 178.04584 ? 51  PRO A CA    1 
ATOM 481  C C     . PRO B 2 51  ? 32.57100  33.90100  20.81300 1.000 180.13278 ? 51  PRO A C     1 
ATOM 482  O O     . PRO B 2 51  ? 32.12800  34.65800  19.93700 1.000 179.37391 ? 51  PRO A O     1 
ATOM 483  C CB    . PRO B 2 51  ? 33.69000  35.29100  22.59700 1.000 179.04978 ? 51  PRO A CB    1 
ATOM 484  C CG    . PRO B 2 51  ? 34.93100  36.11700  22.53100 1.000 172.86295 ? 51  PRO A CG    1 
ATOM 485  C CD    . PRO B 2 51  ? 35.30300  36.15200  21.07600 1.000 178.21835 ? 51  PRO A CD    1 
ATOM 486  N N     . PRO B 2 52  ? 31.92900  32.78300  21.16600 1.000 188.34109 ? 52  PRO A N     1 
ATOM 487  C CA    . PRO B 2 52  ? 30.68300  32.40000  20.47700 1.000 189.01885 ? 52  PRO A CA    1 
ATOM 488  C C     . PRO B 2 52  ? 29.58700  33.44900  20.55700 1.000 185.80976 ? 52  PRO A C     1 
ATOM 489  O O     . PRO B 2 52  ? 28.75600  33.53700  19.64400 1.000 188.11487 ? 52  PRO A O     1 
ATOM 490  C CB    . PRO B 2 52  ? 30.28000  31.10000  21.18800 1.000 177.98230 ? 52  PRO A CB    1 
ATOM 491  C CG    . PRO B 2 52  ? 31.56400  30.54700  21.71800 1.000 175.91523 ? 52  PRO A CG    1 
ATOM 492  C CD    . PRO B 2 52  ? 32.38700  31.74500  22.10400 1.000 183.54231 ? 52  PRO A CD    1 
ATOM 493  N N     . PHE B 2 53  ? 29.56100  34.25300  21.62100 1.000 180.15250 ? 53  PHE A N     1 
ATOM 494  C CA    . PHE B 2 53  ? 28.59500  35.34600  21.70300 1.000 177.59094 ? 53  PHE A CA    1 
ATOM 495  C C     . PHE B 2 53  ? 28.82900  36.37300  20.60100 1.000 183.29816 ? 53  PHE A C     1 
ATOM 496  O O     . PHE B 2 53  ? 27.87100  36.88000  20.00100 1.000 185.26821 ? 53  PHE A O     1 
ATOM 497  C CB    . PHE B 2 53  ? 28.67200  36.00000  23.08400 1.000 179.46195 ? 53  PHE A CB    1 
ATOM 498  C CG    . PHE B 2 53  ? 27.86300  37.25800  23.21100 1.000 170.39934 ? 53  PHE A CG    1 
ATOM 499  C CD1   . PHE B 2 53  ? 26.49700  37.20100  23.43600 1.000 169.23522 ? 53  PHE A CD1   1 
ATOM 500  C CD2   . PHE B 2 53  ? 28.47100  38.50000  23.10900 1.000 166.43861 ? 53  PHE A CD2   1 
ATOM 501  C CE1   . PHE B 2 53  ? 25.75000  38.36000  23.55400 1.000 167.21442 ? 53  PHE A CE1   1 
ATOM 502  C CE2   . PHE B 2 53  ? 27.72900  39.66300  23.22600 1.000 166.51514 ? 53  PHE A CE2   1 
ATOM 503  C CZ    . PHE B 2 53  ? 26.36800  39.59300  23.44900 1.000 174.73043 ? 53  PHE A CZ    1 
ATOM 504  N N     . ILE B 2 54  ? 30.09500  36.68500  20.31300 1.000 187.94901 ? 54  ILE A N     1 
ATOM 505  C CA    . ILE B 2 54  ? 30.40200  37.63300  19.24800 1.000 187.35239 ? 54  ILE A CA    1 
ATOM 506  C C     . ILE B 2 54  ? 30.09000  37.02700  17.88400 1.000 183.76246 ? 54  ILE A C     1 
ATOM 507  O O     . ILE B 2 54  ? 29.61300  37.72000  16.97700 1.000 184.32561 ? 54  ILE A O     1 
ATOM 508  C CB    . ILE B 2 54  ? 31.86800  38.09300  19.34700 1.000 175.96051 ? 54  ILE A CB    1 
ATOM 509  C CG1   . ILE B 2 54  ? 32.10400  38.85600  20.65300 1.000 177.06140 ? 54  ILE A CG1   1 
ATOM 510  C CG2   . ILE B 2 54  ? 32.24200  38.96100  18.15500 1.000 167.77952 ? 54  ILE A CG2   1 
ATOM 511  C CD1   . ILE B 2 54  ? 31.29500  40.13200  20.77800 1.000 166.25468 ? 54  ILE A CD1   1 
ATOM 512  N N     . GLN B 2 55  ? 30.34500  35.72500  17.71700 1.000 185.51309 ? 55  GLN A N     1 
ATOM 513  C CA    . GLN B 2 55  ? 29.98900  35.05700  16.46800 1.000 183.58760 ? 55  GLN A CA    1 
ATOM 514  C C     . GLN B 2 55  ? 28.48400  35.08600  16.24200 1.000 182.20737 ? 55  GLN A C     1 
ATOM 515  O O     . GLN B 2 55  ? 28.02100  35.25200  15.10700 1.000 179.53989 ? 55  GLN A O     1 
ATOM 516  C CB    . GLN B 2 55  ? 30.49000  33.61100  16.47200 1.000 182.86524 ? 55  GLN A CB    1 
ATOM 517  C CG    . GLN B 2 55  ? 31.99200  33.45800  16.61100 1.000 183.46692 ? 55  GLN A CG    1 
ATOM 518  C CD    . GLN B 2 55  ? 32.44200  32.01400  16.48800 1.000 183.10169 ? 55  GLN A CD    1 
ATOM 519  O OE1   . GLN B 2 55  ? 31.76500  31.18800  15.87600 1.000 179.65318 ? 55  GLN A OE1   1 
ATOM 520  N NE2   . GLN B 2 55  ? 33.59100  31.70300  17.07700 1.000 184.62380 ? 55  GLN A NE2   1 
ATOM 521  N N     . ALA B 2 56  ? 27.70400  34.92600  17.31200 1.000 187.14620 ? 56  ALA A N     1 
ATOM 522  C CA    . ALA B 2 56  ? 26.25200  34.97000  17.18800 1.000 186.15705 ? 56  ALA A CA    1 
ATOM 523  C C     . ALA B 2 56  ? 25.74600  36.39000  16.96800 1.000 188.27781 ? 56  ALA A C     1 
ATOM 524  O O     . ALA B 2 56  ? 24.70600  36.58200  16.33000 1.000 189.19209 ? 56  ALA A O     1 
ATOM 525  C CB    . ALA B 2 56  ? 25.60600  34.36000  18.43200 1.000 182.32345 ? 56  ALA A CB    1 
ATOM 526  N N     . LEU B 2 57  ? 26.46200  37.39200  17.48500 1.000 186.49606 ? 57  LEU A N     1 
ATOM 527  C CA    . LEU B 2 57  ? 26.04300  38.78100  17.32700 1.000 182.59754 ? 57  LEU A CA    1 
ATOM 528  C C     . LEU B 2 57  ? 26.36700  39.31500  15.93500 1.000 180.40244 ? 57  LEU A C     1 
ATOM 529  O O     . LEU B 2 57  ? 25.55500  40.03100  15.33700 1.000 175.44343 ? 57  LEU A O     1 
ATOM 530  C CB    . LEU B 2 57  ? 26.70700  39.64800  18.40200 1.000 183.79270 ? 57  LEU A CB    1 
ATOM 531  C CG    . LEU B 2 57  ? 26.37200  41.14400  18.40900 1.000 175.97946 ? 57  LEU A CG    1 
ATOM 532  C CD1   . LEU B 2 57  ? 24.90200  41.36200  18.72300 1.000 165.04778 ? 57  LEU A CD1   1 
ATOM 533  C CD2   . LEU B 2 57  ? 27.25400  41.89500  19.39900 1.000 184.43911 ? 57  LEU A CD2   1 
ATOM 534  N N     . THR B 2 58  ? 27.54300  38.97600  15.40300 1.000 186.82625 ? 58  THR A N     1 
ATOM 535  C CA    . THR B 2 58  ? 28.02400  39.54900  14.15200 1.000 187.05968 ? 58  THR A CA    1 
ATOM 536  C C     . THR B 2 58  ? 27.88900  38.61100  12.96000 1.000 181.85404 ? 58  THR A C     1 
ATOM 537  O O     . THR B 2 58  ? 28.05900  39.06200  11.82200 1.000 181.46762 ? 58  THR A O     1 
ATOM 538  C CB    . THR B 2 58  ? 29.49500  39.96800  14.28400 1.000 181.12174 ? 58  THR A CB    1 
ATOM 539  O OG1   . THR B 2 58  ? 30.32200  38.80300  14.38800 1.000 174.90922 ? 58  THR A OG1   1 
ATOM 540  C CG2   . THR B 2 58  ? 29.69800  40.82900  15.51900 1.000 186.33134 ? 58  THR A CG2   1 
ATOM 541  N N     . SER B 2 59  ? 27.60000  37.33000  13.19400 1.000 182.73384 ? 59  SER A N     1 
ATOM 542  C CA    . SER B 2 59  ? 27.52700  36.31200  12.14200 1.000 184.76713 ? 59  SER A CA    1 
ATOM 543  C C     . SER B 2 59  ? 28.87000  36.12100  11.44100 1.000 186.74014 ? 59  SER A C     1 
ATOM 544  O O     . SER B 2 59  ? 28.92100  35.69800  10.28200 1.000 189.44943 ? 59  SER A O     1 
ATOM 545  C CB    . SER B 2 59  ? 26.42600  36.63300  11.12500 1.000 184.02183 ? 59  SER A CB    1 
ATOM 546  O OG    . SER B 2 59  ? 25.16300  36.71900  11.76900 1.000 189.49055 ? 59  SER A OG    1 
ATOM 547  N N     . ILE B 2 60  ? 29.96100  36.42600  12.14500 1.000 192.82916 ? 60  ILE A N     1 
ATOM 548  C CA    . ILE B 2 60  ? 31.31700  36.28400  11.62500 1.000 191.56759 ? 60  ILE A CA    1 
ATOM 549  C C     . ILE B 2 60  ? 31.94700  35.05700  12.26400 1.000 191.03496 ? 60  ILE A C     1 
ATOM 550  O O     . ILE B 2 60  ? 32.17200  35.02500  13.48000 1.000 184.98058 ? 60  ILE A O     1 
ATOM 551  C CB    . ILE B 2 60  ? 32.16400  37.53800  11.90000 1.000 190.97261 ? 60  ILE A CB    1 
ATOM 552  C CG1   . ILE B 2 60  ? 31.53500  38.76700  11.22900 1.000 192.12687 ? 60  ILE A CG1   1 
ATOM 553  C CG2   . ILE B 2 60  ? 33.59900  37.32600  11.42000 1.000 181.68503 ? 60  ILE A CG2   1 
ATOM 554  C CD1   . ILE B 2 60  ? 32.30900  40.04500  11.46300 1.000 187.39454 ? 60  ILE A CD1   1 
ATOM 555  N N     . GLU B 2 61  ? 32.25000  34.05900  11.44500 1.000 198.16885 ? 61  GLU A N     1 
ATOM 556  C CA    . GLU B 2 61  ? 32.95100  32.86300  11.88000 1.000 200.63957 ? 61  GLU A CA    1 
ATOM 557  C C     . GLU B 2 61  ? 34.44200  33.00800  11.60900 1.000 213.22041 ? 61  GLU A C     1 
ATOM 558  O O     . GLU B 2 61  ? 34.87200  33.82500  10.79200 1.000 219.46580 ? 61  GLU A O     1 
ATOM 559  C CB    . GLU B 2 61  ? 32.40400  31.62500  11.16700 1.000 194.64004 ? 61  GLU A CB    1 
ATOM 560  C CG    . GLU B 2 61  ? 30.97000  31.28800  11.53300 1.000 209.97086 ? 61  GLU A CG    1 
ATOM 561  C CD    . GLU B 2 61  ? 30.44800  30.06700  10.79700 1.000 210.81482 ? 61  GLU A CD    1 
ATOM 562  O OE1   . GLU B 2 61  ? 31.25500  29.35600  10.16200 1.000 197.24380 ? 61  GLU A OE1   1 
ATOM 563  O OE2   . GLU B 2 61  ? 29.22600  29.82000  10.85500 1.000 206.64245 ? 61  GLU A OE2   1 
ATOM 564  N N     . GLU B 2 62  ? 35.23400  32.19700  12.31300 1.000 209.71146 ? 62  GLU A N     1 
ATOM 565  C CA    . GLU B 2 62  ? 36.68600  32.26600  12.16100 1.000 205.12246 ? 62  GLU A CA    1 
ATOM 566  C C     . GLU B 2 62  ? 37.11600  31.91200  10.74200 1.000 209.94093 ? 62  GLU A C     1 
ATOM 567  O O     . GLU B 2 62  ? 38.04400  32.52200  10.19700 1.000 216.32960 ? 62  GLU A O     1 
ATOM 568  C CB    . GLU B 2 62  ? 37.36300  31.33900  13.16700 1.000 201.62530 ? 62  GLU A CB    1 
ATOM 569  C CG    . GLU B 2 62  ? 37.11600  31.72000  14.62200 1.000 200.31485 ? 62  GLU A CG    1 
ATOM 570  C CD    . GLU B 2 62  ? 37.91900  30.86900  15.58700 1.000 189.83317 ? 62  GLU A CD    1 
ATOM 571  O OE1   . GLU B 2 62  ? 38.47600  29.84100  15.15000 1.000 184.62522 ? 62  GLU A OE1   1 
ATOM 572  O OE2   . GLU B 2 62  ? 37.99400  31.23100  16.77900 1.000 179.93916 ? 62  GLU A OE2   1 
ATOM 573  N N     . ASN B 2 63  ? 36.43300  30.94600  10.12200 1.000 207.17661 ? 63  ASN A N     1 
ATOM 574  C CA    . ASN B 2 63  ? 36.78700  30.51600  8.77200  1.000 202.22679 ? 63  ASN A CA    1 
ATOM 575  C C     . ASN B 2 63  ? 36.65500  31.65000  7.76200  1.000 203.36992 ? 63  ASN A C     1 
ATOM 576  O O     . ASN B 2 63  ? 37.34300  31.65000  6.73600  1.000 204.07730 ? 63  ASN A O     1 
ATOM 577  C CB    . ASN B 2 63  ? 35.92200  29.31600  8.36300  1.000 198.92432 ? 63  ASN A CB    1 
ATOM 578  C CG    . ASN B 2 63  ? 34.42600  29.58700  8.49200  1.000 207.54994 ? 63  ASN A CG    1 
ATOM 579  O OD1   . ASN B 2 63  ? 33.99000  30.73600  8.55200  1.000 205.45461 ? 63  ASN A OD1   1 
ATOM 580  N ND2   . ASN B 2 63  ? 33.63300  28.52100  8.52200  1.000 206.70126 ? 63  ASN A ND2   1 
ATOM 581  N N     . MET B 2 64  ? 35.78500  32.62500  8.03600  1.000 212.29053 ? 64  MET A N     1 
ATOM 582  C CA    . MET B 2 64  ? 35.61700  33.76800  7.14700  1.000 205.96704 ? 64  MET A CA    1 
ATOM 583  C C     . MET B 2 64  ? 36.82000  34.70100  7.17500  1.000 208.71545 ? 64  MET A C     1 
ATOM 584  O O     . MET B 2 64  ? 37.02300  35.46200  6.22200  1.000 207.85491 ? 64  MET A O     1 
ATOM 585  C CB    . MET B 2 64  ? 34.34400  34.53900  7.52000  1.000 202.11541 ? 64  MET A CB    1 
ATOM 586  C CG    . MET B 2 64  ? 33.06800  33.70400  7.47900  1.000 204.13780 ? 64  MET A CG    1 
ATOM 587  S SD    . MET B 2 64  ? 31.61600  34.55400  8.14400  1.000 184.20847 ? 64  MET A SD    1 
ATOM 588  C CE    . MET B 2 64  ? 31.40600  35.88500  6.96000  1.000 184.91192 ? 64  MET A CE    1 
ATOM 589  N N     . LEU B 2 65  ? 37.62200  34.65600  8.23600  1.000 213.14377 ? 65  LEU A N     1 
ATOM 590  C CA    . LEU B 2 65  ? 38.72600  35.59200  8.41400  1.000 209.63732 ? 65  LEU A CA    1 
ATOM 591  C C     . LEU B 2 65  ? 40.06800  35.04100  7.94700  1.000 204.15475 ? 65  LEU A C     1 
ATOM 592  O O     . LEU B 2 65  ? 41.07400  35.75600  8.02300  1.000 207.26738 ? 65  LEU A O     1 
ATOM 593  C CB    . LEU B 2 65  ? 38.84000  36.00400  9.88800  1.000 205.47892 ? 65  LEU A CB    1 
ATOM 594  C CG    . LEU B 2 65  ? 37.65400  36.72200  10.53700 1.000 201.92255 ? 65  LEU A CG    1 
ATOM 595  C CD1   . LEU B 2 65  ? 37.97900  37.15200  11.96600 1.000 200.29611 ? 65  LEU A CD1   1 
ATOM 596  C CD2   . LEU B 2 65  ? 37.22900  37.91900  9.70900  1.000 202.25125 ? 65  LEU A CD2   1 
ATOM 597  N N     . GLN B 2 66  ? 40.10900  33.79200  7.47000  1.000 198.14370 ? 66  GLN A N     1 
ATOM 598  C CA    . GLN B 2 66  ? 41.37600  33.17600  7.08600  1.000 207.86041 ? 66  GLN A CA    1 
ATOM 599  C C     . GLN B 2 66  ? 41.96300  33.82300  5.83500  1.000 212.95768 ? 66  GLN A C     1 
ATOM 600  O O     . GLN B 2 66  ? 43.19000  33.92500  5.70800  1.000 212.96554 ? 66  GLN A O     1 
ATOM 601  C CB    . GLN B 2 66  ? 41.17900  31.66800  6.88700  1.000 204.70732 ? 66  GLN A CB    1 
ATOM 602  C CG    . GLN B 2 66  ? 40.76200  30.92800  8.15400  1.000 199.82018 ? 66  GLN A CG    1 
ATOM 603  C CD    . GLN B 2 66  ? 40.19600  29.54600  7.87200  1.000 197.84488 ? 66  GLN A CD    1 
ATOM 604  O OE1   . GLN B 2 66  ? 40.31700  29.03100  6.76300  1.000 205.78774 ? 66  GLN A OE1   1 
ATOM 605  N NE2   . GLN B 2 66  ? 39.56700  28.94200  8.87900  1.000 195.76558 ? 66  GLN A NE2   1 
ATOM 606  N N     . GLN B 2 67  ? 41.11200  34.26800  4.91200  1.000 211.45320 ? 67  GLN A N     1 
ATOM 607  C CA    . GLN B 2 67  ? 41.55800  34.93000  3.69300  1.000 211.47293 ? 67  GLN A CA    1 
ATOM 608  C C     . GLN B 2 67  ? 41.56300  36.44900  3.80700  1.000 204.99853 ? 67  GLN A C     1 
ATOM 609  O O     . GLN B 2 67  ? 41.87900  37.13200  2.82600  1.000 210.22163 ? 67  GLN A O     1 
ATOM 610  C CB    . GLN B 2 67  ? 40.67800  34.51500  2.50800  1.000 215.38472 ? 67  GLN A CB    1 
ATOM 611  C CG    . GLN B 2 67  ? 40.64900  33.02400  2.22800  1.000 213.22247 ? 67  GLN A CG    1 
ATOM 612  C CD    . GLN B 2 67  ? 42.01200  32.46300  1.88500  1.000 211.88339 ? 67  GLN A CD    1 
ATOM 613  O OE1   . GLN B 2 67  ? 42.85700  33.15200  1.31600  1.000 216.68130 ? 67  GLN A OE1   1 
ATOM 614  N NE2   . GLN B 2 67  ? 42.23600  31.20500  2.23900  1.000 211.23148 ? 67  GLN A NE2   1 
ATOM 615  N N     . ALA B 2 68  ? 41.19800  36.95000  4.99100  1.000 206.54869 ? 68  ALA A N     1 
ATOM 616  C CA    . ALA B 2 68  ? 41.14900  38.41200  5.22700  1.000 203.63882 ? 68  ALA A CA    1 
ATOM 617  C C     . ALA B 2 68  ? 42.54400  38.91700  5.59600  1.000 207.98971 ? 68  ALA A C     1 
ATOM 618  O O     . ALA B 2 68  ? 43.35100  38.13700  6.14400  1.000 211.22371 ? 68  ALA A O     1 
ATOM 619  C CB    . ALA B 2 68  ? 40.15200  38.70800  6.32200  1.000 194.14656 ? 68  ALA A CB    1 
ATOM 620  N N     . PRO B 2 69  ? 42.87400  40.19400  5.30700  1.000 199.58791 ? 69  PRO A N     1 
ATOM 621  C CA    . PRO B 2 69  ? 44.17300  40.74000  5.66600  1.000 201.81466 ? 69  PRO A CA    1 
ATOM 622  C C     . PRO B 2 69  ? 44.24000  41.27000  7.08800  1.000 207.58430 ? 69  PRO A C     1 
ATOM 623  O O     . PRO B 2 69  ? 43.18300  41.53400  7.69300  1.000 199.88142 ? 69  PRO A O     1 
ATOM 624  C CB    . PRO B 2 69  ? 44.30100  41.86500  4.63000  1.000 200.93900 ? 69  PRO A CB    1 
ATOM 625  C CG    . PRO B 2 69  ? 42.88900  42.38400  4.49200  1.000 194.41201 ? 69  PRO A CG    1 
ATOM 626  C CD    . PRO B 2 69  ? 42.02300  41.14000  4.59800  1.000 194.56747 ? 69  PRO A CD    1 
ATOM 627  N N     . TYR B 2 70  ? 45.45600  41.41200  7.62100  1.000 210.91609 ? 70  TYR A N     1 
ATOM 628  C CA    . TYR B 2 70  ? 45.61900  42.01000  8.97400  1.000 205.44380 ? 70  TYR A CA    1 
ATOM 629  C C     . TYR B 2 70  ? 45.45400  43.52200  8.84000  1.000 201.97879 ? 70  TYR A C     1 
ATOM 630  O O     . TYR B 2 70  ? 45.47000  44.03800  7.70100  1.000 210.44993 ? 70  TYR A O     1 
ATOM 631  C CB    . TYR B 2 70  ? 46.96800  41.61000  9.57700  1.000 205.59371 ? 70  TYR A CB    1 
ATOM 632  C CG    . TYR B 2 70  ? 47.05000  40.16100  10.03600 1.000 205.37121 ? 70  TYR A CG    1 
ATOM 633  C CD1   . TYR B 2 70  ? 47.44100  39.15100  9.16500  1.000 213.26840 ? 70  TYR A CD1   1 
ATOM 634  C CD2   . TYR B 2 70  ? 46.74300  39.80400  11.34300 1.000 205.33577 ? 70  TYR A CD2   1 
ATOM 635  C CE1   . TYR B 2 70  ? 47.51900  37.83200  9.58000  1.000 215.29672 ? 70  TYR A CE1   1 
ATOM 636  C CE2   . TYR B 2 70  ? 46.81500  38.48900  11.76900 1.000 210.66949 ? 70  TYR A CE2   1 
ATOM 637  C CZ    . TYR B 2 70  ? 47.20600  37.50000  10.88500 1.000 215.58985 ? 70  TYR A CZ    1 
ATOM 638  O OH    . TYR B 2 70  ? 47.28000  36.20100  11.29700 1.000 214.32817 ? 70  TYR A OH    1 
ATOM 639  N N     . PHE B 2 71  ? 45.31500  44.22400  9.96500  1.000 186.55634 ? 71  PHE A N     1 
ATOM 640  C CA    . PHE B 2 71  ? 45.04100  45.68600  9.89800  1.000 186.21786 ? 71  PHE A CA    1 
ATOM 641  C C     . PHE B 2 71  ? 46.21500  46.42100  9.24800  1.000 200.21623 ? 71  PHE A C     1 
ATOM 642  O O     . PHE B 2 71  ? 45.96300  47.34500  8.45400  1.000 201.09039 ? 71  PHE A O     1 
ATOM 643  C CB    . PHE B 2 71  ? 44.73200  46.21900  11.29900 1.000 184.60712 ? 71  PHE A CB    1 
ATOM 644  C CG    . PHE B 2 71  ? 44.05800  47.58400  11.29700 1.000 195.76251 ? 71  PHE A CG    1 
ATOM 645  C CD1   . PHE B 2 71  ? 42.67700  47.69500  11.19200 1.000 186.87293 ? 71  PHE A CD1   1 
ATOM 646  C CD2   . PHE B 2 71  ? 44.80600  48.75100  11.40100 1.000 197.93733 ? 71  PHE A CD2   1 
ATOM 647  C CE1   . PHE B 2 71  ? 42.06400  48.93800  11.18800 1.000 176.36930 ? 71  PHE A CE1   1 
ATOM 648  C CE2   . PHE B 2 71  ? 44.18700  49.99100  11.39700 1.000 196.70330 ? 71  PHE A CE2   1 
ATOM 649  C CZ    . PHE B 2 71  ? 42.81900  50.08200  11.29100 1.000 188.57858 ? 71  PHE A CZ    1 
ATOM 650  N N     . ASN B 2 72  ? 47.45200  46.02000  9.54700  1.000 209.72859 ? 72  ASN A N     1 
ATOM 651  C CA    . ASN B 2 72  ? 48.63900  46.76700  9.03600  1.000 207.19253 ? 72  ASN A CA    1 
ATOM 652  C C     . ASN B 2 72  ? 48.46100  47.12700  7.55700  1.000 211.93437 ? 72  ASN A C     1 
ATOM 653  O O     . ASN B 2 72  ? 48.57000  48.33000  7.22300  1.000 214.11230 ? 72  ASN A O     1 
ATOM 654  C CB    . ASN B 2 72  ? 49.93200  45.99300  9.27300  1.000 201.47782 ? 72  ASN A CB    1 
ATOM 655  C CG    . ASN B 2 72  ? 49.83200  44.55300  8.82700  1.000 206.77133 ? 72  ASN A CG    1 
ATOM 656  O OD1   . ASN B 2 72  ? 48.78000  44.12000  8.34500  1.000 206.74603 ? 72  ASN A OD1   1 
ATOM 657  N ND2   . ASN B 2 72  ? 50.91000  43.79800  8.98100  1.000 208.58789 ? 72  ASN A ND2   1 
ATOM 658  N N     . GLN B 2 73  ? 48.18900  46.13600  6.70500  1.000 211.40954 ? 73  GLN A N     1 
ATOM 659  C CA    . GLN B 2 73  ? 48.09300  46.39400  5.24500  1.000 206.69208 ? 73  GLN A CA    1 
ATOM 660  C C     . GLN B 2 73  ? 46.99600  47.43400  4.96800  1.000 214.10986 ? 73  GLN A C     1 
ATOM 661  O O     . GLN B 2 73  ? 47.31400  48.51400  4.40900  1.000 209.08551 ? 73  GLN A O     1 
ATOM 662  C CB    . GLN B 2 73  ? 47.79500  45.06600  4.55300  1.000 198.29677 ? 73  GLN A CB    1 
ATOM 663  C CG    . GLN B 2 73  ? 48.82100  43.97900  4.85200  1.000 200.77257 ? 73  GLN A CG    1 
ATOM 664  C CD    . GLN B 2 73  ? 48.19900  42.62800  5.13000  1.000 201.57251 ? 73  GLN A CD    1 
ATOM 665  O OE1   . GLN B 2 73  ? 47.42300  42.45900  6.07500  1.000 204.36995 ? 73  GLN A OE1   1 
ATOM 666  N NE2   . GLN B 2 73  ? 48.54100  41.64800  4.30700  1.000 206.11006 ? 73  GLN A NE2   1 
ATOM 667  N N     . VAL B 2 74  ? 45.76000  47.13700  5.37300  1.000 209.51678 ? 74  VAL A N     1 
ATOM 668  C CA    . VAL B 2 74  ? 44.62300  48.05900  5.07700  1.000 199.15030 ? 74  VAL A CA    1 
ATOM 669  C C     . VAL B 2 74  ? 44.87400  49.39900  5.78700  1.000 199.70143 ? 74  VAL A C     1 
ATOM 670  O O     . VAL B 2 74  ? 44.48500  50.44100  5.22200  1.000 197.81873 ? 74  VAL A O     1 
ATOM 671  C CB    . VAL B 2 74  ? 43.27100  47.43800  5.47800  1.000 195.56189 ? 74  VAL A CB    1 
ATOM 672  C CG1   . VAL B 2 74  ? 42.97900  46.17000  4.68500  1.000 193.50021 ? 74  VAL A CG1   1 
ATOM 673  C CG2   . VAL B 2 74  ? 43.18300  47.16100  6.97300  1.000 198.05101 ? 74  VAL A CG2   1 
ATOM 674  N N     . ALA B 2 75  ? 45.52500  49.37400  6.95300  1.000 203.83207 ? 75  ALA A N     1 
ATOM 675  C CA    . ALA B 2 75  ? 45.73400  50.61700  7.73300  1.000 202.82510 ? 75  ALA A CA    1 
ATOM 676  C C     . ALA B 2 75  ? 46.30800  51.70000  6.82200  1.000 200.04935 ? 75  ALA A C     1 
ATOM 677  O O     . ALA B 2 75  ? 45.76100  52.82300  6.79000  1.000 198.58186 ? 75  ALA A O     1 
ATOM 678  C CB    . ALA B 2 75  ? 46.65800  50.35000  8.89900  1.000 194.06266 ? 75  ALA A CB    1 
ATOM 679  N N     . GLN B 2 76  ? 47.37400  51.36500  6.09400  1.000 206.85654 ? 76  GLN A N     1 
ATOM 680  C CA    . GLN B 2 76  ? 48.03300  52.37900  5.23300  1.000 206.95392 ? 76  GLN A CA    1 
ATOM 681  C C     . GLN B 2 76  ? 47.01300  52.89800  4.20900  1.000 208.29115 ? 76  GLN A C     1 
ATOM 682  O O     . GLN B 2 76  ? 46.92300  54.13200  4.04000  1.000 201.53700 ? 76  GLN A O     1 
ATOM 683  C CB    . GLN B 2 76  ? 49.24900  51.75700  4.55000  1.000 205.49321 ? 76  GLN A CB    1 
ATOM 684  C CG    . GLN B 2 76  ? 49.95400  50.69300  5.38500  1.000 199.27018 ? 76  GLN A CG    1 
ATOM 685  C CD    . GLN B 2 76  ? 50.82500  51.25400  6.48800  1.000 200.39553 ? 76  GLN A CD    1 
ATOM 686  O OE1   . GLN B 2 76  ? 51.38900  50.51300  7.30100  1.000 198.28643 ? 76  GLN A OE1   1 
ATOM 687  N NE2   . GLN B 2 76  ? 50.94200  52.57300  6.53400  1.000 201.96410 ? 76  GLN A NE2   1 
ATOM 688  N N     . GLU B 2 77  ? 46.26700  51.99100  3.57000  1.000 209.29584 ? 77  GLU A N     1 
ATOM 689  C CA    . GLU B 2 77  ? 45.30100  52.39900  2.51500  1.000 200.71605 ? 77  GLU A CA    1 
ATOM 690  C C     . GLU B 2 77  ? 44.13900  53.19400  3.12700  1.000 196.93070 ? 77  GLU A C     1 
ATOM 691  O O     . GLU B 2 77  ? 43.82300  54.28100  2.59600  1.000 193.67150 ? 77  GLU A O     1 
ATOM 692  C CB    . GLU B 2 77  ? 44.75600  51.15800  1.80900  1.000 193.46991 ? 77  GLU A CB    1 
ATOM 693  C CG    . GLU B 2 77  ? 43.72100  51.48100  0.73600  1.000 193.09432 ? 77  GLU A CG    1 
ATOM 694  C CD    . GLU B 2 77  ? 42.99300  50.26700  0.18700  1.000 194.83892 ? 77  GLU A CD    1 
ATOM 695  O OE1   . GLU B 2 77  ? 43.29700  49.14300  0.63900  1.000 195.94840 ? 77  GLU A OE1   1 
ATOM 696  O OE2   . GLU B 2 77  ? 42.12000  50.44500  -0.68700 1.000 195.32518 ? 77  GLU A OE2   1 
ATOM 697  N N     . ILE B 2 78  ? 43.54100  52.68500  4.20600  1.000 198.14012 ? 78  ILE A N     1 
ATOM 698  C CA    . ILE B 2 78  ? 42.33900  53.34500  4.80200  1.000 195.95822 ? 78  ILE A CA    1 
ATOM 699  C C     . ILE B 2 78  ? 42.67900  54.78200  5.22600  1.000 198.97751 ? 78  ILE A C     1 
ATOM 700  O O     . ILE B 2 78  ? 41.90200  55.69600  4.87700  1.000 197.14743 ? 78  ILE A O     1 
ATOM 701  C CB    . ILE B 2 78  ? 41.82100  52.53100  6.00100  1.000 185.51919 ? 78  ILE A CB    1 
ATOM 702  C CG1   . ILE B 2 78  ? 41.46200  51.10300  5.60700  1.000 184.62210 ? 78  ILE A CG1   1 
ATOM 703  C CG2   . ILE B 2 78  ? 40.64600  53.23900  6.67600  1.000 184.83470 ? 78  ILE A CG2   1 
ATOM 704  C CD1   . ILE B 2 78  ? 41.05900  50.22800  6.77900  1.000 186.71961 ? 78  ILE A CD1   1 
ATOM 705  N N     . TYR B 2 79  ? 43.79800  54.97800  5.92700  1.000 200.86025 ? 79  TYR A N     1 
ATOM 706  C CA    . TYR B 2 79  ? 44.11600  56.32800  6.47000  1.000 196.84225 ? 79  TYR A CA    1 
ATOM 707  C C     . TYR B 2 79  ? 44.01200  57.37500  5.36600  1.000 199.52105 ? 79  TYR A C     1 
ATOM 708  O O     . TYR B 2 79  ? 43.43000  58.44800  5.61700  1.000 199.89215 ? 79  TYR A O     1 
ATOM 709  C CB    . TYR B 2 79  ? 45.50400  56.31300  7.11800  1.000 189.59549 ? 79  TYR A CB    1 
ATOM 710  C CG    . TYR B 2 79  ? 45.92400  57.64300  7.72800  1.000 191.09078 ? 79  TYR A CG    1 
ATOM 711  C CD1   . TYR B 2 79  ? 45.54400  57.98900  9.01800  1.000 190.96443 ? 79  TYR A CD1   1 
ATOM 712  C CD2   . TYR B 2 79  ? 46.70800  58.54400  7.01900  1.000 183.62291 ? 79  TYR A CD2   1 
ATOM 713  C CE1   . TYR B 2 79  ? 45.92400  59.19500  9.58300  1.000 187.05031 ? 79  TYR A CE1   1 
ATOM 714  C CE2   . TYR B 2 79  ? 47.09500  59.75300  7.57300  1.000 181.45827 ? 79  TYR A CE2   1 
ATOM 715  C CZ    . TYR B 2 79  ? 46.70100  60.08000  8.85800  1.000 180.45686 ? 79  TYR A CZ    1 
ATOM 716  O OH    . TYR B 2 79  ? 47.07800  61.26800  9.41200  1.000 178.16366 ? 79  TYR A OH    1 
ATOM 717  N N     . ASP B 2 80  ? 44.53000  57.07400  4.17500  1.000 197.50130 ? 80  ASP A N     1 
ATOM 718  C CA    . ASP B 2 80  ? 44.55300  58.08700  3.08400  1.000 194.79552 ? 80  ASP A CA    1 
ATOM 719  C C     . ASP B 2 80  ? 43.13500  58.58900  2.79500  1.000 194.12443 ? 80  ASP A C     1 
ATOM 720  O O     . ASP B 2 80  ? 42.97700  59.80700  2.56900  1.000 192.28645 ? 80  ASP A O     1 
ATOM 721  C CB    . ASP B 2 80  ? 45.20800  57.53200  1.83000  1.000 194.79790 ? 80  ASP A CB    1 
ATOM 722  C CG    . ASP B 2 80  ? 46.52400  56.80200  2.05200  1.000 201.97493 ? 80  ASP A CG    1 
ATOM 723  O OD1   . ASP B 2 80  ? 47.44700  57.42000  2.62200  1.000 209.43315 ? 80  ASP A OD1   1 
ATOM 724  O OD2   . ASP B 2 80  ? 46.61700  55.62700  1.64100  1.000 201.09094 ? 80  ASP A OD2   1 
ATOM 725  N N     . LYS B 2 81  ? 42.14700  57.69400  2.79000  1.000 194.95219 ? 81  LYS A N     1 
ATOM 726  C CA    . LYS B 2 81  ? 40.76400  58.09200  2.42100  1.000 189.14546 ? 81  LYS A CA    1 
ATOM 727  C C     . LYS B 2 81  ? 40.11100  58.93300  3.52800  1.000 181.87729 ? 81  LYS A C     1 
ATOM 728  O O     . LYS B 2 81  ? 39.43000  59.92100  3.18500  1.000 173.95971 ? 81  LYS A O     1 
ATOM 729  C CB    . LYS B 2 81  ? 39.90600  56.84200  2.20900  1.000 191.30516 ? 81  LYS A CB    1 
ATOM 730  C CG    . LYS B 2 81  ? 40.64400  55.61100  1.70700  1.000 191.12105 ? 81  LYS A CG    1 
ATOM 731  C CD    . LYS B 2 81  ? 39.83900  54.33600  1.92400  1.000 182.24200 ? 81  LYS A CD    1 
ATOM 732  C CE    . LYS B 2 81  ? 40.56000  53.11800  1.44700  1.000 192.30176 ? 81  LYS A CE    1 
ATOM 733  N NZ    . LYS B 2 81  ? 40.81400  53.18000  0.00600  1.000 196.83703 ? 81  LYS A NZ    1 
ATOM 734  N N     . ILE B 2 82  ? 40.30700  58.56400  4.79600  1.000 185.28857 ? 82  ILE A N     1 
ATOM 735  C CA    . ILE B 2 82  ? 39.58400  59.25900  5.90700  1.000 175.38349 ? 82  ILE A CA    1 
ATOM 736  C C     . ILE B 2 82  ? 40.44000  60.38100  6.51800  1.000 179.88758 ? 82  ILE A C     1 
ATOM 737  O O     . ILE B 2 82  ? 39.88900  61.14100  7.34200  1.000 180.78967 ? 82  ILE A O     1 
ATOM 738  C CB    . ILE B 2 82  ? 39.17100  58.23300  6.97700  1.000 175.25610 ? 82  ILE A CB    1 
ATOM 739  C CG1   . ILE B 2 82  ? 40.38700  57.67500  7.71500  1.000 182.46194 ? 82  ILE A CG1   1 
ATOM 740  C CG2   . ILE B 2 82  ? 38.32100  57.12000  6.36500  1.000 170.50619 ? 82  ILE A CG2   1 
ATOM 741  C CD1   . ILE B 2 82  ? 40.05100  56.62900  8.76300  1.000 181.52536 ? 82  ILE A CD1   1 
ATOM 742  N N     . LYS B 2 83  ? 41.71500  60.49800  6.13700  1.000 185.29319 ? 83  LYS A N     1 
ATOM 743  C CA    . LYS B 2 83  ? 42.59400  61.50700  6.78800  1.000 173.15719 ? 83  LYS A CA    1 
ATOM 744  C C     . LYS B 2 83  ? 42.04500  62.91800  6.51700  1.000 165.89708 ? 83  LYS A C     1 
ATOM 745  O O     . LYS B 2 83  ? 42.41600  63.84900  7.26300  1.000 165.90858 ? 83  LYS A O     1 
ATOM 746  C CB    . LYS B 2 83  ? 44.04600  61.38600  6.31600  1.000 180.02974 ? 83  LYS A CB    1 
ATOM 747  C CG    . LYS B 2 83  ? 44.28500  61.66500  4.84100  1.000 188.87844 ? 83  LYS A CG    1 
ATOM 748  C CD    . LYS B 2 83  ? 45.72900  61.41600  4.42700  1.000 180.98200 ? 83  LYS A CD    1 
ATOM 749  C CE    . LYS B 2 83  ? 45.96000  61.66400  2.97100  1.000 181.02933 ? 83  LYS A CE    1 
ATOM 750  N NZ    . LYS B 2 83  ? 47.33800  61.35000  2.58700  1.000 185.85669 ? 83  LYS A NZ    1 
ATOM 751  N N     . ASP B 2 84  ? 41.20500  63.06400  5.48900  1.000 164.79298 ? 84  ASP A N     1 
ATOM 752  C CA    . ASP B 2 84  ? 40.61800  64.39000  5.15300  1.000 171.08929 ? 84  ASP A CA    1 
ATOM 753  C C     . ASP B 2 84  ? 39.08900  64.28800  5.14900  1.000 163.17073 ? 84  ASP A C     1 
ATOM 754  O O     . ASP B 2 84  ? 38.44100  65.13600  4.50000  1.000 163.59896 ? 84  ASP A O     1 
ATOM 755  C CB    . ASP B 2 84  ? 41.17400  64.91700  3.84000  1.000 173.41974 ? 84  ASP A CB    1 
ATOM 756  C CG    . ASP B 2 84  ? 42.69100  65.02400  3.77500  1.000 172.96561 ? 84  ASP A CG    1 
ATOM 757  O OD1   . ASP B 2 84  ? 43.26300  65.75600  4.61000  1.000 168.36538 ? 84  ASP A OD1   1 
ATOM 758  O OD2   . ASP B 2 84  ? 43.28800  64.37100  2.89400  1.000 182.81200 ? 84  ASP A OD2   1 
ATOM 759  N N     . CYS B 2 85  ? 38.53700  63.29200  5.84800  1.000 166.78373 ? 85  CYS A N     1 
ATOM 760  C CA    . CYS B 2 85  ? 37.06100  63.11900  5.91100  1.000 159.43859 ? 85  CYS A CA    1 
ATOM 761  C C     . CYS B 2 85  ? 36.58500  63.22100  7.37000  1.000 155.60688 ? 85  CYS A C     1 
ATOM 762  O O     . CYS B 2 85  ? 37.24800  62.62800  8.24800  1.000 157.61771 ? 85  CYS A O     1 
ATOM 763  C CB    . CYS B 2 85  ? 36.64400  61.77900  5.31700  1.000 159.34007 ? 85  CYS A CB    1 
ATOM 764  S SG    . CYS B 2 85  ? 37.14700  61.56900  3.58900  1.000 179.57073 ? 85  CYS A SG    1 
ATOM 765  N N     . ILE B 2 86  ? 35.48500  63.94100  7.61000  1.000 149.60370 ? 86  ILE A N     1 
ATOM 766  C CA    . ILE B 2 86  ? 34.93100  64.08700  8.99100  1.000 146.29585 ? 86  ILE A CA    1 
ATOM 767  C C     . ILE B 2 86  ? 34.59100  62.69100  9.53200  1.000 143.52765 ? 86  ILE A C     1 
ATOM 768  O O     . ILE B 2 86  ? 33.88300  61.94400  8.82500  1.000 155.39819 ? 86  ILE A O     1 
ATOM 769  C CB    . ILE B 2 86  ? 33.70000  65.00900  8.99100  1.000 141.56118 ? 86  ILE A CB    1 
ATOM 770  C CG1   . ILE B 2 86  ? 34.00400  66.34800  8.32700  1.000 153.10393 ? 86  ILE A CG1   1 
ATOM 771  C CG2   . ILE B 2 86  ? 33.15800  65.19300  10.40800 1.000 144.53059 ? 86  ILE A CG2   1 
ATOM 772  C CD1   . ILE B 2 86  ? 32.85900  67.34000  8.38900  1.000 140.81427 ? 86  ILE A CD1   1 
ATOM 773  N N     . PHE B 2 87  ? 35.06900  62.35800  10.73400 1.000 145.66289 ? 87  PHE A N     1 
ATOM 774  C CA    . PHE B 2 87  ? 34.83900  61.02500  11.27200 1.000 155.09517 ? 87  PHE A CA    1 
ATOM 775  C C     . PHE B 2 87  ? 33.45300  60.94600  11.90100 1.000 153.01308 ? 87  PHE A C     1 
ATOM 776  O O     . PHE B 2 87  ? 33.11900  61.73300  12.79100 1.000 148.29273 ? 87  PHE A O     1 
ATOM 777  C CB    . PHE B 2 87  ? 35.90900  60.66000  12.29800 1.000 161.85984 ? 87  PHE A CB    1 
ATOM 778  C CG    . PHE B 2 87  ? 35.90000  59.21100  12.67700 1.000 161.59949 ? 87  PHE A CG    1 
ATOM 779  C CD1   . PHE B 2 87  ? 36.61700  58.28600  11.93500 1.000 160.65008 ? 87  PHE A CD1   1 
ATOM 780  C CD2   . PHE B 2 87  ? 35.16100  58.76600  13.76200 1.000 150.26244 ? 87  PHE A CD2   1 
ATOM 781  C CE1   . PHE B 2 87  ? 36.60900  56.94800  12.27600 1.000 158.83192 ? 87  PHE A CE1   1 
ATOM 782  C CE2   . PHE B 2 87  ? 35.14800  57.42900  14.10600 1.000 153.63612 ? 87  PHE A CE2   1 
ATOM 783  C CZ    . PHE B 2 87  ? 35.87300  56.51900  13.36200 1.000 165.22350 ? 87  PHE A CZ    1 
ATOM 784  N N     . VAL B 2 88  ? 32.65000  59.99300  11.43700 1.000 154.34835 ? 88  VAL A N     1 
ATOM 785  C CA    . VAL B 2 88  ? 31.27300  59.82900  11.88700 1.000 152.96589 ? 88  VAL A CA    1 
ATOM 786  C C     . VAL B 2 88  ? 31.07800  58.38300  12.32100 1.000 155.59064 ? 88  VAL A C     1 
ATOM 787  O O     . VAL B 2 88  ? 31.68600  57.47200  11.74900 1.000 161.50312 ? 88  VAL A O     1 
ATOM 788  C CB    . VAL B 2 88  ? 30.27200  60.20600  10.77200 1.000 146.73741 ? 88  VAL A CB    1 
ATOM 789  C CG1   . VAL B 2 88  ? 28.85900  60.21500  11.30100 1.000 145.02414 ? 88  VAL A CG1   1 
ATOM 790  C CG2   . VAL B 2 88  ? 30.61600  61.55900  10.17600 1.000 139.88184 ? 88  VAL A CG2   1 
ATOM 791  N N     . ALA B 2 89  ? 30.23800  58.17300  13.33800 1.000 141.61978 ? 89  ALA A N     1 
ATOM 792  C CA    . ALA B 2 89  ? 29.90500  56.82900  13.80200 1.000 144.37535 ? 89  ALA A CA    1 
ATOM 793  C C     . ALA B 2 89  ? 28.71300  56.90100  14.75100 1.000 147.43175 ? 89  ALA A C     1 
ATOM 794  O O     . ALA B 2 89  ? 28.33900  57.97100  15.23500 1.000 143.39190 ? 89  ALA A O     1 
ATOM 795  C CB    . ALA B 2 89  ? 31.10200  56.15800  14.48500 1.000 147.35941 ? 89  ALA A CB    1 
ATOM 796  N N     . HIS B 2 90  ? 28.11700  55.73800  15.01100 1.000 148.27046 ? 90  HIS A N     1 
ATOM 797  C CA    . HIS B 2 90  ? 27.02700  55.60500  15.97400 1.000 132.41714 ? 90  HIS A CA    1 
ATOM 798  C C     . HIS B 2 90  ? 27.62900  55.21800  17.32100 1.000 143.28380 ? 90  HIS A C     1 
ATOM 799  O O     . HIS B 2 90  ? 28.22800  54.14500  17.45000 1.000 145.89301 ? 90  HIS A O     1 
ATOM 800  C CB    . HIS B 2 90  ? 26.00900  54.57200  15.49700 1.000 127.69429 ? 90  HIS A CB    1 
ATOM 801  C CG    . HIS B 2 90  ? 24.74300  54.56100  16.29400 1.000 131.26842 ? 90  HIS A CG    1 
ATOM 802  N ND1   . HIS B 2 90  ? 23.80800  55.57100  16.22000 1.000 139.54590 ? 90  HIS A ND1   1 
ATOM 803  C CD2   . HIS B 2 90  ? 24.25900  53.66300  17.18600 1.000 137.28402 ? 90  HIS A CD2   1 
ATOM 804  C CE1   . HIS B 2 90  ? 22.80200  55.29300  17.03000 1.000 131.18167 ? 90  HIS A CE1   1 
ATOM 805  N NE2   . HIS B 2 90  ? 23.05100  54.14100  17.62900 1.000 134.32085 ? 90  HIS A NE2   1 
ATOM 806  N N     . ASN B 2 91  ? 27.47100  56.09100  18.32000 1.000 150.06575 ? 91  ASN A N     1 
ATOM 807  C CA    . ASN B 2 91  ? 28.22000  55.99300  19.57400 1.000 149.30654 ? 91  ASN A CA    1 
ATOM 808  C C     . ASN B 2 91  ? 29.72500  56.01300  19.27600 1.000 147.49077 ? 91  ASN A C     1 
ATOM 809  O O     . ASN B 2 91  ? 30.44000  55.01900  19.44600 1.000 145.50611 ? 91  ASN A O     1 
ATOM 810  C CB    . ASN B 2 91  ? 27.80100  54.74300  20.36100 1.000 141.73769 ? 91  ASN A CB    1 
ATOM 811  C CG    . ASN B 2 91  ? 28.36100  54.71800  21.76900 1.000 149.89392 ? 91  ASN A CG    1 
ATOM 812  O OD1   . ASN B 2 91  ? 28.44600  55.75000  22.43700 1.000 150.63612 ? 91  ASN A OD1   1 
ATOM 813  N ND2   . ASN B 2 91  ? 28.73900  53.53200  22.23200 1.000 151.23787 ? 91  ASN A ND2   1 
ATOM 814  N N     . VAL B 2 92  ? 30.19300  57.18800  18.83000 1.000 147.61744 ? 92  VAL A N     1 
ATOM 815  C CA    . VAL B 2 92  ? 31.46100  57.29600  18.10800 1.000 141.80493 ? 92  VAL A CA    1 
ATOM 816  C C     . VAL B 2 92  ? 32.68400  56.97700  18.96600 1.000 146.18047 ? 92  VAL A C     1 
ATOM 817  O O     . VAL B 2 92  ? 33.75300  56.68900  18.42000 1.000 151.28226 ? 92  VAL A O     1 
ATOM 818  C CB    . VAL B 2 92  ? 31.57600  58.70400  17.47600 1.000 145.11875 ? 92  VAL A CB    1 
ATOM 819  C CG1   . VAL B 2 92  ? 31.77500  59.77600  18.54500 1.000 149.71469 ? 92  VAL A CG1   1 
ATOM 820  C CG2   . VAL B 2 92  ? 32.68800  58.75800  16.42500 1.000 148.19936 ? 92  VAL A CG2   1 
ATOM 821  N N     . ASP B 2 93  ? 32.56200  57.01900  20.29700 1.000 148.92128 ? 93  ASP A N     1 
ATOM 822  C CA    . ASP B 2 93  ? 33.71500  56.74400  21.15800 1.000 147.41893 ? 93  ASP A CA    1 
ATOM 823  C C     . ASP B 2 93  ? 34.32600  55.37700  20.85900 1.000 156.54677 ? 93  ASP A C     1 
ATOM 824  O O     . ASP B 2 93  ? 35.55000  55.24400  20.73800 1.000 156.03342 ? 93  ASP A O     1 
ATOM 825  C CB    . ASP B 2 93  ? 33.30600  56.82800  22.63200 1.000 139.18485 ? 93  ASP A CB    1 
ATOM 826  C CG    . ASP B 2 93  ? 33.25300  58.25300  23.15100 1.000 156.93476 ? 93  ASP A CG    1 
ATOM 827  O OD1   . ASP B 2 93  ? 34.25600  58.98200  23.00600 1.000 163.96593 ? 93  ASP A OD1   1 
ATOM 828  O OD2   . ASP B 2 93  ? 32.20300  58.64000  23.70500 1.000 158.73860 ? 93  ASP A OD2   1 
ATOM 829  N N     . PHE B 2 94  ? 33.48300  54.35600  20.72800 1.000 154.00056 ? 94  PHE A N     1 
ATOM 830  C CA    . PHE B 2 94  ? 33.88500  52.98600  20.43400 1.000 158.82119 ? 94  PHE A CA    1 
ATOM 831  C C     . PHE B 2 94  ? 34.74800  52.90800  19.17800 1.000 160.02936 ? 94  PHE A C     1 
ATOM 832  O O     . PHE B 2 94  ? 35.94700  52.59500  19.24200 1.000 168.60349 ? 94  PHE A O     1 
ATOM 833  C CB    . PHE B 2 94  ? 32.62600  52.12300  20.28500 1.000 149.02806 ? 94  PHE A CB    1 
ATOM 834  C CG    . PHE B 2 94  ? 32.89500  50.66900  20.03700 1.000 147.50135 ? 94  PHE A CG    1 
ATOM 835  C CD1   . PHE B 2 94  ? 33.18000  49.82300  21.09500 1.000 149.89078 ? 94  PHE A CD1   1 
ATOM 836  C CD2   . PHE B 2 94  ? 32.83100  50.13600  18.75600 1.000 151.14627 ? 94  PHE A CD2   1 
ATOM 837  C CE1   . PHE B 2 94  ? 33.41100  48.47500  20.88400 1.000 149.55424 ? 94  PHE A CE1   1 
ATOM 838  C CE2   . PHE B 2 94  ? 33.06400  48.78200  18.53900 1.000 152.68266 ? 94  PHE A CE2   1 
ATOM 839  C CZ    . PHE B 2 94  ? 33.35500  47.95400  19.60600 1.000 151.81527 ? 94  PHE A CZ    1 
ATOM 840  N N     . ASP B 2 95  ? 34.13100  53.20300  18.03000 1.000 150.97989 ? 95  ASP A N     1 
ATOM 841  C CA    . ASP B 2 95  ? 34.81700  53.08500  16.74600 1.000 152.98279 ? 95  ASP A CA    1 
ATOM 842  C C     . ASP B 2 95  ? 36.06600  53.95800  16.68600 1.000 161.12021 ? 95  ASP A C     1 
ATOM 843  O O     . ASP B 2 95  ? 37.13200  53.50900  16.24200 1.000 167.21305 ? 95  ASP A O     1 
ATOM 844  C CB    . ASP B 2 95  ? 33.86000  53.46100  15.61800 1.000 145.62228 ? 95  ASP A CB    1 
ATOM 845  C CG    . ASP B 2 95  ? 32.55100  52.69300  15.68400 1.000 158.91590 ? 95  ASP A CG    1 
ATOM 846  O OD1   . ASP B 2 95  ? 31.61500  53.16800  16.36200 1.000 170.26869 ? 95  ASP A OD1   1 
ATOM 847  O OD2   . ASP B 2 95  ? 32.46700  51.60300  15.07900 1.000 156.25691 ? 95  ASP A OD2   1 
ATOM 848  N N     . LEU B 2 96  ? 35.95600  55.20700  17.14300 1.000 156.51745 ? 96  LEU A N     1 
ATOM 849  C CA    . LEU B 2 96  ? 37.08300  56.12900  17.06500 1.000 154.94369 ? 96  LEU A CA    1 
ATOM 850  C C     . LEU B 2 96  ? 38.26200  55.63800  17.89200 1.000 161.04731 ? 96  LEU A C     1 
ATOM 851  O O     . LEU B 2 96  ? 39.41700  55.72800  17.45600 1.000 156.25151 ? 96  LEU A O     1 
ATOM 852  C CB    . LEU B 2 96  ? 36.64900  57.52200  17.52300 1.000 152.34104 ? 96  LEU A CB    1 
ATOM 853  C CG    . LEU B 2 96  ? 37.70900  58.62200  17.45000 1.000 158.17276 ? 96  LEU A CG    1 
ATOM 854  C CD1   . LEU B 2 96  ? 38.22100  58.74700  16.02900 1.000 156.87011 ? 96  LEU A CD1   1 
ATOM 855  C CD2   . LEU B 2 96  ? 37.14400  59.94700  17.94000 1.000 157.46765 ? 96  LEU A CD2   1 
ATOM 856  N N     . ASN B 2 97  ? 37.99300  55.11600  19.09100 1.000 162.43292 ? 97  ASN A N     1 
ATOM 857  C CA    . ASN B 2 97  ? 39.07900  54.66000  19.95200 1.000 173.29676 ? 97  ASN A CA    1 
ATOM 858  C C     . ASN B 2 97  ? 39.72000  53.38700  19.41000 1.000 173.41377 ? 97  ASN A C     1 
ATOM 859  O O     . ASN B 2 97  ? 40.95200  53.25100  19.42600 1.000 167.59570 ? 97  ASN A O     1 
ATOM 860  C CB    . ASN B 2 97  ? 38.56300  54.44900  21.37500 1.000 158.48201 ? 97  ASN A CB    1 
ATOM 861  C CG    . ASN B 2 97  ? 38.30900  55.76000  22.10600 1.000 142.14175 ? 97  ASN A CG    1 
ATOM 862  O OD1   . ASN B 2 97  ? 39.00400  56.75100  21.88900 1.000 151.37032 ? 97  ASN A OD1   1 
ATOM 863  N ND2   . ASN B 2 97  ? 37.31000  55.76400  22.98300 1.000 141.73173 ? 97  ASN A ND2   1 
ATOM 864  N N     . PHE B 2 98  ? 38.90400  52.44800  18.92200 1.000 168.61323 ? 98  PHE A N     1 
ATOM 865  C CA    . PHE B 2 98  ? 39.46000  51.22300  18.35300 1.000 172.88728 ? 98  PHE A CA    1 
ATOM 866  C C     . PHE B 2 98  ? 40.30800  51.52100  17.12100 1.000 177.96035 ? 98  PHE A C     1 
ATOM 867  O O     . PHE B 2 98  ? 41.41000  50.97900  16.97000 1.000 177.55882 ? 98  PHE A O     1 
ATOM 868  C CB    . PHE B 2 98  ? 38.33600  50.24200  18.01400 1.000 164.83139 ? 98  PHE A CB    1 
ATOM 869  C CG    . PHE B 2 98  ? 38.05300  49.24700  19.10200 1.000 161.33361 ? 98  PHE A CG    1 
ATOM 870  C CD1   . PHE B 2 98  ? 38.79700  48.08200  19.19700 1.000 162.64514 ? 98  PHE A CD1   1 
ATOM 871  C CD2   . PHE B 2 98  ? 37.05000  49.47500  20.03100 1.000 155.88463 ? 98  PHE A CD2   1 
ATOM 872  C CE1   . PHE B 2 98  ? 38.54400  47.16000  20.19600 1.000 168.08883 ? 98  PHE A CE1   1 
ATOM 873  C CE2   . PHE B 2 98  ? 36.79500  48.55300  21.03500 1.000 154.44731 ? 98  PHE A CE2   1 
ATOM 874  C CZ    . PHE B 2 98  ? 37.54200  47.39600  21.11500 1.000 163.57066 ? 98  PHE A CZ    1 
ATOM 875  N N     . ILE B 2 99  ? 39.81900  52.39700  16.24000 1.000 179.50479 ? 99  ILE A N     1 
ATOM 876  C CA    . ILE B 2 99  ? 40.57600  52.75100  15.04300 1.000 178.85118 ? 99  ILE A CA    1 
ATOM 877  C C     . ILE B 2 99  ? 41.84900  53.50100  15.41400 1.000 181.73901 ? 99  ILE A C     1 
ATOM 878  O O     . ILE B 2 99  ? 42.90700  53.29000  14.80700 1.000 186.14586 ? 99  ILE A O     1 
ATOM 879  C CB    . ILE B 2 99  ? 39.68600  53.55800  14.07900 1.000 174.79230 ? 99  ILE A CB    1 
ATOM 880  C CG1   . ILE B 2 99  ? 38.85100  52.60600  13.22100 1.000 169.31782 ? 99  ILE A CG1   1 
ATOM 881  C CG2   . ILE B 2 99  ? 40.51700  54.49100  13.21000 1.000 179.56484 ? 99  ILE A CG2   1 
ATOM 882  C CD1   . ILE B 2 99  ? 38.02700  53.30200  12.17100 1.000 166.25295 ? 99  ILE A CD1   1 
ATOM 883  N N     . LYS B 2 100 ? 41.77600  54.37600  16.42300 1.000 176.31519 ? 100 LYS A N     1 
ATOM 884  C CA    . LYS B 2 100 ? 42.97100  55.08100  16.87600 1.000 179.12012 ? 100 LYS A CA    1 
ATOM 885  C C     . LYS B 2 100 ? 44.02800  54.11100  17.38900 1.000 183.15628 ? 100 LYS A C     1 
ATOM 886  O O     . LYS B 2 100 ? 45.21600  54.25300  17.07100 1.000 178.71275 ? 100 LYS A O     1 
ATOM 887  C CB    . LYS B 2 100 ? 42.60600  56.09400  17.95700 1.000 177.42327 ? 100 LYS A CB    1 
ATOM 888  C CG    . LYS B 2 100 ? 42.10100  57.41800  17.41500 1.000 165.29924 ? 100 LYS A CG    1 
ATOM 889  C CD    . LYS B 2 100 ? 41.62100  58.31900  18.53700 1.000 153.48009 ? 100 LYS A CD    1 
ATOM 890  C CE    . LYS B 2 100 ? 41.16000  59.66100  17.99900 1.000 154.99176 ? 100 LYS A CE    1 
ATOM 891  N NZ    . LYS B 2 100 ? 40.42400  60.43800  19.03100 1.000 171.06654 ? 100 LYS A NZ    1 
ATOM 892  N N     . LYS B 2 101 ? 43.61700  53.11400  18.18000 1.000 187.74461 ? 101 LYS A N     1 
ATOM 893  C CA    . LYS B 2 101 ? 44.57800  52.13500  18.67800 1.000 185.82866 ? 101 LYS A CA    1 
ATOM 894  C C     . LYS B 2 101 ? 45.17000  51.31100  17.54100 1.000 178.81094 ? 101 LYS A C     1 
ATOM 895  O O     . LYS B 2 101 ? 46.38900  51.11600  17.47100 1.000 186.40436 ? 101 LYS A O     1 
ATOM 896  C CB    . LYS B 2 101 ? 43.92700  51.21100  19.70400 1.000 177.40797 ? 101 LYS A CB    1 
ATOM 897  C CG    . LYS B 2 101 ? 44.86300  50.09100  20.13500 1.000 180.31409 ? 101 LYS A CG    1 
ATOM 898  C CD    . LYS B 2 101 ? 44.14400  49.00100  20.89500 1.000 176.75611 ? 101 LYS A CD    1 
ATOM 899  C CE    . LYS B 2 101 ? 45.07400  47.82600  21.15800 1.000 170.67002 ? 101 LYS A CE    1 
ATOM 900  N NZ    . LYS B 2 101 ? 44.38600  46.70400  21.85300 1.000 170.52173 ? 101 LYS A NZ    1 
ATOM 901  N N     . ALA B 2 102 ? 44.31500  50.80900  16.64500 1.000 171.48032 ? 102 ALA A N     1 
ATOM 902  C CA    . ALA B 2 102 ? 44.79400  49.95600  15.56100 1.000 183.67100 ? 102 ALA A CA    1 
ATOM 903  C C     . ALA B 2 102 ? 45.73600  50.71400  14.63100 1.000 193.87040 ? 102 ALA A C     1 
ATOM 904  O O     . ALA B 2 102 ? 46.70700  50.14400  14.11800 1.000 189.36359 ? 102 ALA A O     1 
ATOM 905  C CB    . ALA B 2 102 ? 43.60700  49.38100  14.79100 1.000 171.32012 ? 102 ALA A CB    1 
ATOM 906  N N     . PHE B 2 103 ? 45.46600  52.00100  14.40200 1.000 192.23899 ? 103 PHE A N     1 
ATOM 907  C CA    . PHE B 2 103 ? 46.40600  52.82900  13.65200 1.000 193.38873 ? 103 PHE A CA    1 
ATOM 908  C C     . PHE B 2 103 ? 47.71100  53.00800  14.41600 1.000 190.58597 ? 103 PHE A C     1 
ATOM 909  O O     . PHE B 2 103 ? 48.79900  52.92300  13.83300 1.000 188.20613 ? 103 PHE A O     1 
ATOM 910  C CB    . PHE B 2 103 ? 45.77800  54.18800  13.34700 1.000 193.84295 ? 103 PHE A CB    1 
ATOM 911  C CG    . PHE B 2 103 ? 44.90600  54.19700  12.12500 1.000 191.89639 ? 103 PHE A CG    1 
ATOM 912  C CD1   . PHE B 2 103 ? 45.14600  53.32500  11.07700 1.000 190.40701 ? 103 PHE A CD1   1 
ATOM 913  C CD2   . PHE B 2 103 ? 43.85000  55.08800  12.02000 1.000 185.32044 ? 103 PHE A CD2   1 
ATOM 914  C CE1   . PHE B 2 103 ? 44.34600  53.33900  9.94700  1.000 187.27643 ? 103 PHE A CE1   1 
ATOM 915  C CE2   . PHE B 2 103 ? 43.05000  55.11000  10.89000 1.000 180.36316 ? 103 PHE A CE2   1 
ATOM 916  C CZ    . PHE B 2 103 ? 43.29700  54.23300  9.85300  1.000 183.02822 ? 103 PHE A CZ    1 
ATOM 917  N N     . LYS B 2 104 ? 47.61900  53.25300  15.72600 1.000 194.54097 ? 104 LYS A N     1 
ATOM 918  C CA    . LYS B 2 104 ? 48.81200  53.47900  16.53300 1.000 190.06053 ? 104 LYS A CA    1 
ATOM 919  C C     . LYS B 2 104 ? 49.72500  52.25900  16.53400 1.000 192.87821 ? 104 LYS A C     1 
ATOM 920  O O     . LYS B 2 104 ? 50.95300  52.39500  16.49500 1.000 202.84791 ? 104 LYS A O     1 
ATOM 921  C CB    . LYS B 2 104 ? 48.40500  53.84900  17.95600 1.000 183.15538 ? 104 LYS A CB    1 
ATOM 922  C CG    . LYS B 2 104 ? 49.56900  54.07200  18.90000 1.000 176.84543 ? 104 LYS A CG    1 
ATOM 923  C CD    . LYS B 2 104 ? 49.07100  54.24000  20.32200 1.000 164.52288 ? 104 LYS A CD    1 
ATOM 924  C CE    . LYS B 2 104 ? 50.22400  54.32400  21.30500 1.000 164.72670 ? 104 LYS A CE    1 
ATOM 925  N NZ    . LYS B 2 104 ? 49.74300  54.30100  22.71400 1.000 161.23786 ? 104 LYS A NZ    1 
ATOM 926  N N     . ASP B 2 105 ? 49.14500  51.05600  16.57200 1.000 181.21022 ? 105 ASP A N     1 
ATOM 927  C CA    . ASP B 2 105 ? 49.94800  49.84100  16.50400 1.000 184.27645 ? 105 ASP A CA    1 
ATOM 928  C C     . ASP B 2 105 ? 50.61700  49.67100  15.14500 1.000 196.85078 ? 105 ASP A C     1 
ATOM 929  O O     . ASP B 2 105 ? 51.58000  48.90300  15.03200 1.000 203.47898 ? 105 ASP A O     1 
ATOM 930  C CB    . ASP B 2 105 ? 49.08200  48.62100  16.82900 1.000 182.87367 ? 105 ASP A CB    1 
ATOM 931  C CG    . ASP B 2 105 ? 48.47300  48.68800  18.22200 1.000 194.89062 ? 105 ASP A CG    1 
ATOM 932  O OD1   . ASP B 2 105 ? 49.05500  49.35500  19.10600 1.000 195.08940 ? 105 ASP A OD1   1 
ATOM 933  O OD2   . ASP B 2 105 ? 47.41000  48.06600  18.43400 1.000 192.30976 ? 105 ASP A OD2   1 
ATOM 934  N N     . CYS B 2 106 ? 50.13200  50.36900  14.11900 1.000 202.87042 ? 106 CYS A N     1 
ATOM 935  C CA    . CYS B 2 106 ? 50.76500  50.39900  12.80800 1.000 202.78369 ? 106 CYS A CA    1 
ATOM 936  C C     . CYS B 2 106 ? 51.59700  51.65400  12.60100 1.000 200.85207 ? 106 CYS A C     1 
ATOM 937  O O     . CYS B 2 106 ? 51.94500  51.97500  11.45800 1.000 203.91258 ? 106 CYS A O     1 
ATOM 938  C CB    . CYS B 2 106 ? 49.71100  50.29100  11.70700 1.000 202.42782 ? 106 CYS A CB    1 
ATOM 939  S SG    . CYS B 2 106 ? 48.63800  48.85400  11.84600 1.000 183.95993 ? 106 CYS A SG    1 
ATOM 940  N N     . ASN B 2 107 ? 51.91700  52.34300  13.70200 1.000 198.10133 ? 107 ASN A N     1 
ATOM 941  C CA    . ASN B 2 107 ? 52.73300  53.58800  13.63300 1.000 202.19326 ? 107 ASN A CA    1 
ATOM 942  C C     . ASN B 2 107 ? 51.97100  54.64300  12.82600 1.000 202.51853 ? 107 ASN A C     1 
ATOM 943  O O     . ASN B 2 107 ? 52.60900  55.33400  12.00200 1.000 193.15534 ? 107 ASN A O     1 
ATOM 944  C CB    . ASN B 2 107 ? 54.13100  53.31500  13.08600 1.000 201.57108 ? 107 ASN A CB    1 
ATOM 945  C CG    . ASN B 2 107 ? 54.79700  52.16500  13.80200 1.000 204.39739 ? 107 ASN A CG    1 
ATOM 946  O OD1   . ASN B 2 107 ? 54.96500  52.20700  15.02600 1.000 192.67574 ? 107 ASN A OD1   1 
ATOM 947  N ND2   . ASN B 2 107 ? 55.17000  51.12900  13.06500 1.000 209.71447 ? 107 ASN A ND2   1 
ATOM 948  N N     . ILE B 2 108 ? 50.66000  54.75900  13.05700 1.000 198.67614 ? 108 ILE A N     1 
ATOM 949  C CA    . ILE B 2 108 ? 49.83700  55.78500  12.34800 1.000 193.70239 ? 108 ILE A CA    1 
ATOM 950  C C     . ILE B 2 108 ? 49.12300  56.65000  13.39800 1.000 188.78208 ? 108 ILE A C     1 
ATOM 951  O O     . ILE B 2 108 ? 48.49400  56.07200  14.31000 1.000 177.87551 ? 108 ILE A O     1 
ATOM 952  C CB    . ILE B 2 108 ? 48.83900  55.11900  11.38400 1.000 194.57871 ? 108 ILE A CB    1 
ATOM 953  C CG1   . ILE B 2 108 ? 49.53800  54.16500  10.41600 1.000 187.70591 ? 108 ILE A CG1   1 
ATOM 954  C CG2   . ILE B 2 108 ? 48.01100  56.16900  10.64300 1.000 184.42725 ? 108 ILE A CG2   1 
ATOM 955  C CD1   . ILE B 2 108 ? 48.60200  53.48900  9.43100  1.000 191.77945 ? 108 ILE A CD1   1 
ATOM 956  N N     . GLN B 2 109 ? 49.22900  57.97600  13.27500 1.000 187.07544 ? 109 GLN A N     1 
ATOM 957  C CA    . GLN B 2 109 ? 48.56000  58.89800  14.22900 1.000 185.53349 ? 109 GLN A CA    1 
ATOM 958  C C     . GLN B 2 109 ? 47.30500  59.48100  13.56400 1.000 187.92980 ? 109 GLN A C     1 
ATOM 959  O O     . GLN B 2 109 ? 47.44700  60.41100  12.73900 1.000 182.07970 ? 109 GLN A O     1 
ATOM 960  C CB    . GLN B 2 109 ? 49.51200  60.01800  14.64500 1.000 174.30948 ? 109 GLN A CB    1 
ATOM 961  C CG    . GLN B 2 109 ? 48.91100  61.01500  15.62900 1.000 178.07507 ? 109 GLN A CG    1 
ATOM 962  C CD    . GLN B 2 109 ? 49.85300  62.14600  15.97600 1.000 181.38218 ? 109 GLN A CD    1 
ATOM 963  O OE1   . GLN B 2 109 ? 50.98300  62.22000  15.47900 1.000 174.16790 ? 109 GLN A OE1   1 
ATOM 964  N NE2   . GLN B 2 109 ? 49.39600  63.04400  16.83600 1.000 177.03442 ? 109 GLN A NE2   1 
ATOM 965  N N     . TYR B 2 110 ? 46.12900  58.95200  13.91100 1.000 188.59949 ? 110 TYR A N     1 
ATOM 966  C CA    . TYR B 2 110 ? 44.85800  59.45600  13.32500 1.000 186.43655 ? 110 TYR A CA    1 
ATOM 967  C C     . TYR B 2 110 ? 44.24300  60.46600  14.28100 1.000 181.65622 ? 110 TYR A C     1 
ATOM 968  O O     . TYR B 2 110 ? 43.84300  60.08200  15.40000 1.000 176.61633 ? 110 TYR A O     1 
ATOM 969  C CB    . TYR B 2 110 ? 43.86600  58.32000  13.06300 1.000 182.42559 ? 110 TYR A CB    1 
ATOM 970  C CG    . TYR B 2 110 ? 42.60400  58.75900  12.33400 1.000 185.02664 ? 110 TYR A CG    1 
ATOM 971  C CD1   . TYR B 2 110 ? 42.64000  59.77700  11.38800 1.000 182.08260 ? 110 TYR A CD1   1 
ATOM 972  C CD2   . TYR B 2 110 ? 41.37600  58.16800  12.60300 1.000 181.09063 ? 110 TYR A CD2   1 
ATOM 973  C CE1   . TYR B 2 110 ? 41.49500  60.18600  10.72500 1.000 183.51093 ? 110 TYR A CE1   1 
ATOM 974  C CE2   . TYR B 2 110 ? 40.22400  58.56900  11.94700 1.000 172.61759 ? 110 TYR A CE2   1 
ATOM 975  C CZ    . TYR B 2 110 ? 40.28400  59.58100  11.00600 1.000 176.72878 ? 110 TYR A CZ    1 
ATOM 976  O OH    . TYR B 2 110 ? 39.15400  59.98200  10.35500 1.000 163.21171 ? 110 TYR A OH    1 
ATOM 977  N N     . ARG B 2 111 ? 44.16200  61.72700  13.85300 1.000 182.89672 ? 111 ARG A N     1 
ATOM 978  C CA    . ARG B 2 111 ? 43.53100  62.77400  14.69600 1.000 177.47575 ? 111 ARG A CA    1 
ATOM 979  C C     . ARG B 2 111 ? 42.51400  63.55300  13.84600 1.000 166.15018 ? 111 ARG A C     1 
ATOM 980  O O     . ARG B 2 111 ? 42.82900  64.68800  13.43000 1.000 170.00691 ? 111 ARG A O     1 
ATOM 981  C CB    . ARG B 2 111 ? 44.59400  63.70000  15.29700 1.000 183.32454 ? 111 ARG A CB    1 
ATOM 982  C CG    . ARG B 2 111 ? 45.38900  63.05400  16.42200 1.000 178.89935 ? 111 ARG A CG    1 
ATOM 983  C CD    . ARG B 2 111 ? 46.12300  64.08700  17.25900 1.000 180.10261 ? 111 ARG A CD    1 
ATOM 984  N NE    . ARG B 2 111 ? 46.69500  63.50200  18.47700 1.000 191.25779 ? 111 ARG A NE    1 
ATOM 985  C CZ    . ARG B 2 111 ? 47.36800  64.18300  19.39500 1.000 184.68075 ? 111 ARG A CZ    1 
ATOM 986  N NH1   . ARG B 2 111 ? 47.54800  65.48400  19.25300 1.000 174.85837 ? 111 ARG A NH1   1 
ATOM 987  N NH2   . ARG B 2 111 ? 47.85700  63.56100  20.45300 1.000 185.98796 ? 111 ARG A NH2   1 
ATOM 988  N N     . PRO B 2 112 ? 41.31300  62.99600  13.58000 1.000 165.43022 ? 112 PRO A N     1 
ATOM 989  C CA    . PRO B 2 112 ? 40.33600  63.67900  12.74700 1.000 173.43563 ? 112 PRO A CA    1 
ATOM 990  C C     . PRO B 2 112 ? 40.02400  65.03200  13.36200 1.000 176.39538 ? 112 PRO A C     1 
ATOM 991  O O     . PRO B 2 112 ? 39.68100  65.09900  14.55800 1.000 182.64880 ? 112 PRO A O     1 
ATOM 992  C CB    . PRO B 2 112 ? 39.12200  62.73900  12.74000 1.000 171.28891 ? 112 PRO A CB    1 
ATOM 993  C CG    . PRO B 2 112 ? 39.34300  61.82900  13.92900 1.000 167.99970 ? 112 PRO A CG    1 
ATOM 994  C CD    . PRO B 2 112 ? 40.85000  61.71800  14.08700 1.000 172.28985 ? 112 PRO A CD    1 
ATOM 995  N N     . LYS B 2 113 ? 40.13800  66.09400  12.56200 1.000 168.39235 ? 113 LYS A N     1 
ATOM 996  C CA    . LYS B 2 113 ? 39.89400  67.46600  13.07500 1.000 159.20007 ? 113 LYS A CA    1 
ATOM 997  C C     . LYS B 2 113 ? 38.43700  67.57500  13.54800 1.000 165.41334 ? 113 LYS A C     1 
ATOM 998  O O     . LYS B 2 113 ? 38.20300  68.19500  14.60700 1.000 167.67955 ? 113 LYS A O     1 
ATOM 999  C CB    . LYS B 2 113 ? 40.21400  68.47500  11.96900 1.000 153.01576 ? 113 LYS A CB    1 
ATOM 1000 C CG    . LYS B 2 113 ? 41.58600  68.27600  11.33900 1.000 152.99358 ? 113 LYS A CG    1 
ATOM 1001 C CD    . LYS B 2 113 ? 41.82900  69.11700  10.09300 1.000 156.94782 ? 113 LYS A CD    1 
ATOM 1002 C CE    . LYS B 2 113 ? 43.14400  68.79600  9.45500  1.000 159.31205 ? 113 LYS A CE    1 
ATOM 1003 N NZ    . LYS B 2 113 ? 43.35200  69.56000  8.22300  1.000 162.97609 ? 113 LYS A NZ    1 
ATOM 1004 N N     . LYS B 2 114 ? 37.50400  66.98900  12.79400 1.000 160.90199 ? 114 LYS A N     1 
ATOM 1005 C CA    . LYS B 2 114 ? 36.06500  67.07500  13.15300 1.000 157.14292 ? 114 LYS A CA    1 
ATOM 1006 C C     . LYS B 2 114 ? 35.53100  65.67500  13.49800 1.000 161.26509 ? 114 LYS A C     1 
ATOM 1007 O O     . LYS B 2 114 ? 35.74500  64.74500  12.68900 1.000 160.94236 ? 114 LYS A O     1 
ATOM 1008 C CB    . LYS B 2 114 ? 35.27700  67.71400  12.00400 1.000 143.50379 ? 114 LYS A CB    1 
ATOM 1009 C CG    . LYS B 2 114 ? 35.62600  69.17000  11.73400 1.000 153.26877 ? 114 LYS A CG    1 
ATOM 1010 C CD    . LYS B 2 114 ? 34.67700  69.85900  10.76200 1.000 156.96682 ? 114 LYS A CD    1 
ATOM 1011 C CE    . LYS B 2 114 ? 35.04700  71.29200  10.54200 1.000 168.15231 ? 114 LYS A CE    1 
ATOM 1012 N NZ    . LYS B 2 114 ? 34.11000  71.97100  9.64500  1.000 158.48505 ? 114 LYS A NZ    1 
ATOM 1013 N N     . VAL B 2 115 ? 34.86800  65.53700  14.65100 1.000 153.94043 ? 115 VAL A N     1 
ATOM 1014 C CA    . VAL B 2 115 ? 34.27400  64.22600  15.05700 1.000 138.23722 ? 115 VAL A CA    1 
ATOM 1015 C C     . VAL B 2 115 ? 32.75700  64.41100  15.20900 1.000 135.22134 ? 115 VAL A C     1 
ATOM 1016 O O     . VAL B 2 115 ? 32.34100  65.47700  15.71000 1.000 138.17726 ? 115 VAL A O     1 
ATOM 1017 C CB    . VAL B 2 115 ? 34.90700  63.68500  16.35200 1.000 131.58487 ? 115 VAL A CB    1 
ATOM 1018 C CG1   . VAL B 2 115 ? 34.31200  62.34100  16.75600 1.000 131.94229 ? 115 VAL A CG1   1 
ATOM 1019 C CG2   . VAL B 2 115 ? 36.42300  63.58600  16.24200 1.000 144.23662 ? 115 VAL A CG2   1 
ATOM 1020 N N     . ILE B 2 116 ? 31.97100  63.41800  14.78600 1.000 131.83896 ? 116 ILE A N     1 
ATOM 1021 C CA    . ILE B 2 116 ? 30.48300  63.52400  14.84900 1.000 132.53469 ? 116 ILE A CA    1 
ATOM 1022 C C     . ILE B 2 116 ? 29.91500  62.23900  15.47000 1.000 142.99069 ? 116 ILE A C     1 
ATOM 1023 O O     . ILE B 2 116 ? 30.41300  61.15000  15.11500 1.000 151.76882 ? 116 ILE A O     1 
ATOM 1024 C CB    . ILE B 2 116 ? 29.90800  63.74800  13.44000 1.000 138.84001 ? 116 ILE A CB    1 
ATOM 1025 C CG1   . ILE B 2 116 ? 30.27000  65.11800  12.88000 1.000 132.19882 ? 116 ILE A CG1   1 
ATOM 1026 C CG2   . ILE B 2 116 ? 28.39700  63.51600  13.41700 1.000 140.10539 ? 116 ILE A CG2   1 
ATOM 1027 C CD1   . ILE B 2 116 ? 29.69600  65.37300  11.49900 1.000 137.54288 ? 116 ILE A CD1   1 
ATOM 1028 N N     . ASP B 2 117 ? 28.91900  62.35700  16.35300 1.000 125.22009 ? 117 ASP A N     1 
ATOM 1029 C CA    . ASP B 2 117 ? 28.25500  61.14300  16.90500 1.000 127.40791 ? 117 ASP A CA    1 
ATOM 1030 C C     . ASP B 2 117 ? 26.80600  61.11900  16.41100 1.000 136.59103 ? 117 ASP A C     1 
ATOM 1031 O O     . ASP B 2 117 ? 26.03400  62.02600  16.78700 1.000 139.23241 ? 117 ASP A O     1 
ATOM 1032 C CB    . ASP B 2 117 ? 28.35100  61.07700  18.42000 1.000 127.66606 ? 117 ASP A CB    1 
ATOM 1033 C CG    . ASP B 2 117 ? 27.83600  59.79100  19.05100 1.000 145.51674 ? 117 ASP A CG    1 
ATOM 1034 O OD1   . ASP B 2 117 ? 27.40000  58.89800  18.29600 1.000 149.55628 ? 117 ASP A OD1   1 
ATOM 1035 O OD2   . ASP B 2 117 ? 27.87600  59.69400  20.29500 1.000 152.11855 ? 117 ASP A OD2   1 
ATOM 1036 N N     . THR B 2 118 ? 26.45700  60.11900  15.60000 1.000 134.43437 ? 118 THR A N     1 
ATOM 1037 C CA    . THR B 2 118 ? 25.09000  60.03700  15.04900 1.000 130.12883 ? 118 THR A CA    1 
ATOM 1038 C C     . THR B 2 118 ? 24.11300  59.91800  16.19400 1.000 131.52645 ? 118 THR A C     1 
ATOM 1039 O O     . THR B 2 118 ? 22.99700  60.45800  16.07200 1.000 128.09122 ? 118 THR A O     1 
ATOM 1040 C CB    . THR B 2 118 ? 24.96900  58.85000  14.09700 1.000 129.88364 ? 118 THR A CB    1 
ATOM 1041 O OG1   . THR B 2 118 ? 25.01700  57.70300  14.93700 1.000 140.57125 ? 118 THR A OG1   1 
ATOM 1042 C CG2   . THR B 2 118 ? 26.08100  58.81200  13.06400 1.000 129.04352 ? 118 THR A CG2   1 
ATOM 1043 N N     . LEU B 2 119 ? 24.49700  59.22400  17.26800 1.000 135.58809 ? 119 LEU A N     1 
ATOM 1044 C CA    . LEU B 2 119 ? 23.53000  59.02100  18.34100 1.000 141.05420 ? 119 LEU A CA    1 
ATOM 1045 C C     . LEU B 2 119 ? 22.98000  60.35400  18.83400 1.000 134.52208 ? 119 LEU A C     1 
ATOM 1046 O O     . LEU B 2 119 ? 21.76700  60.49500  19.03800 1.000 126.83648 ? 119 LEU A O     1 
ATOM 1047 C CB    . LEU B 2 119 ? 24.17100  58.22800  19.48100 1.000 140.89448 ? 119 LEU A CB    1 
ATOM 1048 C CG    . LEU B 2 119 ? 23.27100  57.81400  20.65200 1.000 142.50112 ? 119 LEU A CG    1 
ATOM 1049 C CD1   . LEU B 2 119 ? 22.04300  57.06700  20.15400 1.000 144.65648 ? 119 LEU A CD1   1 
ATOM 1050 C CD2   . LEU B 2 119 ? 24.05000  56.96500  21.64600 1.000 137.55226 ? 119 LEU A CD2   1 
ATOM 1051 N N     . GLU B 2 120 ? 23.85800  61.34600  19.01800 1.000 122.56060 ? 120 GLU A N     1 
ATOM 1052 C CA    . GLU B 2 120 ? 23.39900  62.69300  19.34200 1.000 116.38418 ? 120 GLU A CA    1 
ATOM 1053 C C     . GLU B 2 120 ? 22.50500  63.24100  18.23700 1.000 121.22419 ? 120 GLU A C     1 
ATOM 1054 O O     . GLU B 2 120 ? 21.43400  63.80300  18.50400 1.000 119.21240 ? 120 GLU A O     1 
ATOM 1055 C CB    . GLU B 2 120 ? 24.59300  63.62200  19.56100 1.000 108.63632 ? 120 GLU A CB    1 
ATOM 1056 C CG    . GLU B 2 120 ? 25.56200  63.18900  20.64700 1.000 126.94041 ? 120 GLU A CG    1 
ATOM 1057 C CD    . GLU B 2 120 ? 26.71400  64.16400  20.79500 1.000 137.88657 ? 120 GLU A CD    1 
ATOM 1058 O OE1   . GLU B 2 120 ? 27.29700  64.54200  19.75800 1.000 145.56981 ? 120 GLU A OE1   1 
ATOM 1059 O OE2   . GLU B 2 120 ? 27.02800  64.56600  21.93800 1.000 141.34179 ? 120 GLU A OE2   1 
ATOM 1060 N N     . ILE B 2 121 ? 22.92900  63.07000  16.98200 1.000 118.60262 ? 121 ILE A N     1 
ATOM 1061 C CA    . ILE B 2 121 ? 22.16700  63.58900  15.84800 1.000 108.49297 ? 121 ILE A CA    1 
ATOM 1062 C C     . ILE B 2 121 ? 20.77800  62.96600  15.80600 1.000 125.41413 ? 121 ILE A C     1 
ATOM 1063 O O     . ILE B 2 121 ? 19.78300  63.65200  15.55600 1.000 129.25019 ? 121 ILE A O     1 
ATOM 1064 C CB    . ILE B 2 121 ? 22.92700  63.34800  14.53000 1.000 116.71940 ? 121 ILE A CB    1 
ATOM 1065 C CG1   . ILE B 2 121 ? 24.17000  64.23200  14.44100 1.000 122.71189 ? 121 ILE A CG1   1 
ATOM 1066 C CG2   . ILE B 2 121 ? 22.02400  63.61700  13.34500 1.000 118.32974 ? 121 ILE A CG2   1 
ATOM 1067 C CD1   . ILE B 2 121 ? 24.82500  64.19900  13.07200 1.000 116.17779 ? 121 ILE A CD1   1 
ATOM 1068 N N     . PHE B 2 122 ? 20.68900  61.65600  16.04800 1.000 122.73252 ? 122 PHE A N     1 
ATOM 1069 C CA    . PHE B 2 122 ? 19.40400  60.96900  15.96300 1.000 121.48197 ? 122 PHE A CA    1 
ATOM 1070 C C     . PHE B 2 122 ? 18.50900  61.33300  17.13800 1.000 121.79063 ? 122 PHE A C     1 
ATOM 1071 O O     . PHE B 2 122 ? 17.29500  61.49700  16.97300 1.000 122.29676 ? 122 PHE A O     1 
ATOM 1072 C CB    . PHE B 2 122 ? 19.61400  59.45600  15.89800 1.000 127.60722 ? 122 PHE A CB    1 
ATOM 1073 C CG    . PHE B 2 122 ? 20.40100  58.99600  14.70100 1.000 130.23312 ? 122 PHE A CG    1 
ATOM 1074 C CD1   . PHE B 2 122 ? 20.48900  59.78200  13.56500 1.000 119.23137 ? 122 PHE A CD1   1 
ATOM 1075 C CD2   . PHE B 2 122 ? 21.06400  57.77600  14.72100 1.000 133.23958 ? 122 PHE A CD2   1 
ATOM 1076 C CE1   . PHE B 2 122 ? 21.21900  59.36200  12.47000 1.000 135.02401 ? 122 PHE A CE1   1 
ATOM 1077 C CE2   . PHE B 2 122 ? 21.79300  57.35100  13.62700 1.000 139.35896 ? 122 PHE A CE2   1 
ATOM 1078 C CZ    . PHE B 2 122 ? 21.87100  58.14400  12.50100 1.000 140.44898 ? 122 PHE A CZ    1 
ATOM 1079 N N     . LYS B 2 123 ? 19.12800  61.56600  18.29200 1.000 119.69192 ? 123 LYS A N     1 
ATOM 1080 C CA    . LYS B 2 123 ? 18.33700  62.01900  19.45800 1.000 115.03388 ? 123 LYS A CA    1 
ATOM 1081 C C     . LYS B 2 123 ? 17.68700  63.35400  19.10300 1.000 113.97559 ? 123 LYS A C     1 
ATOM 1082 O O     . LYS B 2 123 ? 16.46900  63.49800  19.31600 1.000 116.78458 ? 123 LYS A O     1 
ATOM 1083 C CB    . LYS B 2 123 ? 19.25900  62.20800  20.66100 1.000 102.67075 ? 123 LYS A CB    1 
ATOM 1084 C CG    . LYS B 2 123 ? 19.58100  60.94300  21.43700 1.000 111.48677 ? 123 LYS A CG    1 
ATOM 1085 C CD    . LYS B 2 123 ? 20.89400  61.06800  22.19800 1.000 130.72371 ? 123 LYS A CD    1 
ATOM 1086 C CE    . LYS B 2 123 ? 21.14700  59.90200  23.09600 1.000 138.61331 ? 123 LYS A CE    1 
ATOM 1087 N NZ    . LYS B 2 123 ? 22.51500  59.92400  23.61800 1.000 142.65402 ? 123 LYS A NZ    1 
ATOM 1088 N N     . ILE B 2 124 ? 18.47500  64.28200  18.56500 1.000 113.22822 ? 124 ILE A N     1 
ATOM 1089 C CA    . ILE B 2 124 ? 17.94300  65.64100  18.26200 1.000 107.78332 ? 124 ILE A CA    1 
ATOM 1090 C C     . ILE B 2 124 ? 16.98900  65.54900  17.06700 1.000 111.51676 ? 124 ILE A C     1 
ATOM 1091 O O     . ILE B 2 124 ? 15.84100  66.01000  17.19900 1.000 115.89492 ? 124 ILE A O     1 
ATOM 1092 C CB    . ILE B 2 124 ? 19.09900  66.61800  17.99100 1.000 98.03802  ? 124 ILE A CB    1 
ATOM 1093 C CG1   . ILE B 2 124 ? 20.11500  66.61200  19.12200 1.000 106.81854 ? 124 ILE A CG1   1 
ATOM 1094 C CG2   . ILE B 2 124 ? 18.57700  68.02800  17.72900 1.000 97.88256  ? 124 ILE A CG2   1 
ATOM 1095 C CD1   . ILE B 2 124 ? 21.49600  67.06900  18.69500 1.000 98.13357  ? 124 ILE A CD1   1 
ATOM 1096 N N     . ALA B 2 125 ? 17.43300  64.94600  15.96400 1.000 116.87612 ? 125 ALA A N     1 
ATOM 1097 C CA    . ALA B 2 125 ? 16.60700  64.91900  14.73200 1.000 118.51512 ? 125 ALA A CA    1 
ATOM 1098 C C     . ALA B 2 125 ? 15.34500  64.08000  14.91900 1.000 119.27781 ? 125 ALA A C     1 
ATOM 1099 O O     . ALA B 2 125 ? 14.29300  64.45500  14.36700 1.000 112.98437 ? 125 ALA A O     1 
ATOM 1100 C CB    . ALA B 2 125 ? 17.43000  64.39100  13.58800 1.000 105.76268 ? 125 ALA A CB    1 
ATOM 1101 N N     . PHE B 2 126 ? 15.44500  62.96800  15.64400 1.000 123.87600 ? 126 PHE A N     1 
ATOM 1102 C CA    . PHE B 2 126 ? 14.27600  62.06100  15.76700 1.000 117.54180 ? 126 PHE A CA    1 
ATOM 1103 C C     . PHE B 2 126 ? 13.89400  61.90100  17.22700 1.000 119.24658 ? 126 PHE A C     1 
ATOM 1104 O O     . PHE B 2 126 ? 14.07700  60.80400  17.78200 1.000 114.97903 ? 126 PHE A O     1 
ATOM 1105 C CB    . PHE B 2 126 ? 14.68700  60.71600  15.17100 1.000 116.51844 ? 126 PHE A CB    1 
ATOM 1106 C CG    . PHE B 2 126 ? 15.33000  60.75700  13.79100 1.000 113.11545 ? 126 PHE A CG    1 
ATOM 1107 C CD1   . PHE B 2 126 ? 14.59300  61.11900  12.67100 1.000 109.49289 ? 126 PHE A CD1   1 
ATOM 1108 C CD2   . PHE B 2 126 ? 16.66400  60.41300  13.61700 1.000 117.24026 ? 126 PHE A CD2   1 
ATOM 1109 C CE1   . PHE B 2 126 ? 15.18100  61.14700  11.41700 1.000 112.40396 ? 126 PHE A CE1   1 
ATOM 1110 C CE2   . PHE B 2 126 ? 17.24600  60.44400  12.36100 1.000 111.59221 ? 126 PHE A CE2   1 
ATOM 1111 C CZ    . PHE B 2 126 ? 16.50500  60.81000  11.26400 1.000 113.47559 ? 126 PHE A CZ    1 
ATOM 1112 N N     . PRO B 2 127 ? 13.33300  62.93200  17.89000 1.000 124.50985 ? 127 PRO A N     1 
ATOM 1113 C CA    . PRO B 2 127 ? 13.05000  62.82300  19.31200 1.000 123.50123 ? 127 PRO A CA    1 
ATOM 1114 C C     . PRO B 2 127 ? 11.89800  61.87500  19.57900 1.000 123.16575 ? 127 PRO A C     1 
ATOM 1115 O O     . PRO B 2 127 ? 11.95700  61.12400  20.56800 1.000 121.94765 ? 127 PRO A O     1 
ATOM 1116 C CB    . PRO B 2 127 ? 12.72000  64.26300  19.71600 1.000 105.17278 ? 127 PRO A CB    1 
ATOM 1117 C CG    . PRO B 2 127 ? 12.23900  64.91600  18.44200 1.000 110.52034 ? 127 PRO A CG    1 
ATOM 1118 C CD    . PRO B 2 127 ? 12.93100  64.19600  17.30500 1.000 120.82138 ? 127 PRO A CD    1 
ATOM 1119 N N     . THR B 2 128 ? 10.88300  61.88000  18.71400 1.000 134.62746 ? 128 THR A N     1 
ATOM 1120 C CA    . THR B 2 128 ? 9.70400   61.06900  18.99100 1.000 118.11244 ? 128 THR A CA    1 
ATOM 1121 C C     . THR B 2 128 ? 9.96300   59.57300  18.89900 1.000 125.59000 ? 128 THR A C     1 
ATOM 1122 O O     . THR B 2 128 ? 9.08100   58.78800  19.25500 1.000 133.16659 ? 128 THR A O     1 
ATOM 1123 C CB    . THR B 2 128 ? 8.56200   61.42600  18.03700 1.000 130.12720 ? 128 THR A CB    1 
ATOM 1124 O OG1   . THR B 2 128 ? 9.03700   61.40300  16.68600 1.000 151.53529 ? 128 THR A OG1   1 
ATOM 1125 C CG2   . THR B 2 128 ? 7.99500   62.79400  18.35400 1.000 135.00207 ? 128 THR A CG2   1 
ATOM 1126 N N     . ASP B 2 129 ? 11.13300  59.15700  18.42800 1.000 126.57952 ? 129 ASP A N     1 
ATOM 1127 C CA    . ASP B 2 129 ? 11.40100  57.73800  18.24500 1.000 132.29285 ? 129 ASP A CA    1 
ATOM 1128 C C     . ASP B 2 129 ? 11.62200  57.03900  19.58200 1.000 131.48132 ? 129 ASP A C     1 
ATOM 1129 O O     . ASP B 2 129 ? 12.32300  57.54600  20.46400 1.000 114.76818 ? 129 ASP A O     1 
ATOM 1130 C CB    . ASP B 2 129 ? 12.60500  57.53200  17.32400 1.000 118.55471 ? 129 ASP A CB    1 
ATOM 1131 C CG    . ASP B 2 129 ? 12.22300  57.60100  15.85800 1.000 130.73571 ? 129 ASP A CG    1 
ATOM 1132 O OD1   . ASP B 2 129 ? 11.11400  57.14200  15.51200 1.000 142.80266 ? 129 ASP A OD1   1 
ATOM 1133 O OD2   . ASP B 2 129 ? 13.01800  58.11200  15.05000 1.000 135.85103 ? 129 ASP A OD2   1 
ATOM 1134 N N     . LYS B 2 130 ? 11.01200  55.85800  19.72000 1.000 139.54928 ? 130 LYS A N     1 
ATOM 1135 C CA    . LYS B 2 130 ? 11.07100  55.09700  20.96400 1.000 134.04999 ? 130 LYS A CA    1 
ATOM 1136 C C     . LYS B 2 130 ? 12.44700  54.49400  21.21900 1.000 131.35185 ? 130 LYS A C     1 
ATOM 1137 O O     . LYS B 2 130 ? 12.75600  54.14400  22.36400 1.000 132.92973 ? 130 LYS A O     1 
ATOM 1138 C CB    . LYS B 2 130 ? 10.01200  53.99200  20.94700 1.000 111.04447 ? 130 LYS A CB    1 
ATOM 1139 C CG    . LYS B 2 130 ? 8.60200   54.50700  20.70600 1.000 139.20804 ? 130 LYS A CG    1 
ATOM 1140 C CD    . LYS B 2 130 ? 7.62900   53.37200  20.43400 1.000 146.79767 ? 130 LYS A CD    1 
ATOM 1141 C CE    . LYS B 2 130 ? 6.22300   53.90100  20.22400 1.000 135.33300 ? 130 LYS A CE    1 
ATOM 1142 N NZ    . LYS B 2 130 ? 5.28800   52.81700  19.82600 1.000 137.15013 ? 130 LYS A NZ    1 
ATOM 1143 N N     . SER B 2 131 ? 13.27400  54.36300  20.18400 1.000 123.35558 ? 131 SER A N     1 
ATOM 1144 C CA    . SER B 2 131 ? 14.59900  53.78800  20.34200 1.000 116.17756 ? 131 SER A CA    1 
ATOM 1145 C C     . SER B 2 131 ? 15.55700  54.40900  19.33900 1.000 127.29516 ? 131 SER A C     1 
ATOM 1146 O O     . SER B 2 131 ? 15.16200  54.81100  18.24200 1.000 128.61407 ? 131 SER A O     1 
ATOM 1147 C CB    . SER B 2 131 ? 14.57800  52.26800  20.16500 1.000 123.19898 ? 131 SER A CB    1 
ATOM 1148 O OG    . SER B 2 131 ? 15.89000  51.73000  20.22800 1.000 152.82851 ? 131 SER A OG    1 
ATOM 1149 N N     . TYR B 2 132 ? 16.82600  54.47800  19.73800 1.000 108.93071 ? 132 TYR A N     1 
ATOM 1150 C CA    . TYR B 2 132 ? 17.90100  54.96000  18.88400 1.000 126.82867 ? 132 TYR A CA    1 
ATOM 1151 C C     . TYR B 2 132 ? 18.90100  53.85800  18.55700 1.000 139.91578 ? 132 TYR A C     1 
ATOM 1152 O O     . TYR B 2 132 ? 20.01300  54.14600  18.10500 1.000 142.68162 ? 132 TYR A O     1 
ATOM 1153 C CB    . TYR B 2 132 ? 18.58400  56.16200  19.53800 1.000 118.33135 ? 132 TYR A CB    1 
ATOM 1154 C CG    . TYR B 2 132 ? 17.61000  57.28400  19.81600 1.000 116.51777 ? 132 TYR A CG    1 
ATOM 1155 C CD1   . TYR B 2 132 ? 17.12500  58.07300  18.78100 1.000 127.58269 ? 132 TYR A CD1   1 
ATOM 1156 C CD2   . TYR B 2 132 ? 17.15300  57.53700  21.10400 1.000 117.83304 ? 132 TYR A CD2   1 
ATOM 1157 C CE1   . TYR B 2 132 ? 16.22200  59.09100  19.01900 1.000 118.99899 ? 132 TYR A CE1   1 
ATOM 1158 C CE2   . TYR B 2 132 ? 16.24800  58.55500  21.35300 1.000 115.17619 ? 132 TYR A CE2   1 
ATOM 1159 C CZ    . TYR B 2 132 ? 15.78800  59.32800  20.30600 1.000 112.89952 ? 132 TYR A CZ    1 
ATOM 1160 O OH    . TYR B 2 132 ? 14.89000  60.34300  20.54500 1.000 117.42393 ? 132 TYR A OH    1 
ATOM 1161 N N     . GLN B 2 133 ? 18.53100  52.60100  18.79600 1.000 137.97803 ? 133 GLN A N     1 
ATOM 1162 C CA    . GLN B 2 133 ? 19.27300  51.48200  18.23200 1.000 146.71426 ? 133 GLN A CA    1 
ATOM 1163 C C     . GLN B 2 133 ? 19.11000  51.49600  16.71800 1.000 140.40799 ? 133 GLN A C     1 
ATOM 1164 O O     . GLN B 2 133 ? 18.03700  51.82000  16.20500 1.000 140.98674 ? 133 GLN A O     1 
ATOM 1165 C CB    . GLN B 2 133 ? 18.77400  50.16000  18.81500 1.000 142.30818 ? 133 GLN A CB    1 
ATOM 1166 C CG    . GLN B 2 133 ? 19.11000  49.97600  20.28400 1.000 136.05196 ? 133 GLN A CG    1 
ATOM 1167 C CD    . GLN B 2 133 ? 18.81300  48.57600  20.77600 1.000 147.66700 ? 133 GLN A CD    1 
ATOM 1168 O OE1   . GLN B 2 133 ? 17.77300  47.99600  20.46000 1.000 153.04362 ? 133 GLN A OE1   1 
ATOM 1169 N NE2   . GLN B 2 133 ? 19.73200  48.02100  21.55600 1.000 140.23187 ? 133 GLN A NE2   1 
ATOM 1170 N N     . LEU B 2 134 ? 20.18200  51.15200  15.99700 1.000 126.10467 ? 134 LEU A N     1 
ATOM 1171 C CA    . LEU B 2 134 ? 20.20600  51.42000  14.56000 1.000 136.12482 ? 134 LEU A CA    1 
ATOM 1172 C C     . LEU B 2 134 ? 19.13100  50.63900  13.81100 1.000 139.31058 ? 134 LEU A C     1 
ATOM 1173 O O     . LEU B 2 134 ? 18.48000  51.18300  12.91400 1.000 137.12578 ? 134 LEU A O     1 
ATOM 1174 C CB    . LEU B 2 134 ? 21.58300  51.11000  13.97400 1.000 134.56415 ? 134 LEU A CB    1 
ATOM 1175 C CG    . LEU B 2 134 ? 21.61600  51.43400  12.47400 1.000 132.52369 ? 134 LEU A CG    1 
ATOM 1176 C CD1   . LEU B 2 134 ? 21.39200  52.94400  12.26100 1.000 131.44599 ? 134 LEU A CD1   1 
ATOM 1177 C CD2   . LEU B 2 134 ? 22.86300  50.88100  11.74700 1.000 152.09663 ? 134 LEU A CD2   1 
ATOM 1178 N N     . SER B 2 135 ? 18.94600  49.36100  14.14300 1.000 140.20591 ? 135 SER A N     1 
ATOM 1179 C CA    . SER B 2 135 ? 17.96700  48.55300  13.42000 1.000 148.87446 ? 135 SER A CA    1 
ATOM 1180 C C     . SER B 2 135 ? 16.55400  49.09400  13.61500 1.000 151.78890 ? 135 SER A C     1 
ATOM 1181 O O     . SER B 2 135 ? 15.82900  49.33800  12.64000 1.000 146.31819 ? 135 SER A O     1 
ATOM 1182 C CB    . SER B 2 135 ? 18.06300  47.09200  13.86700 1.000 153.50786 ? 135 SER A CB    1 
ATOM 1183 O OG    . SER B 2 135 ? 18.06300  46.97400  15.28200 1.000 158.66750 ? 135 SER A OG    1 
ATOM 1184 N N     . GLU B 2 136 ? 16.15600  49.31000  14.87200 1.000 148.69950 ? 136 GLU A N     1 
ATOM 1185 C CA    . GLU B 2 136 ? 14.80600  49.78700  15.15500 1.000 154.96393 ? 136 GLU A CA    1 
ATOM 1186 C C     . GLU B 2 136 ? 14.58500  51.19900  14.62800 1.000 148.17314 ? 136 GLU A C     1 
ATOM 1187 O O     . GLU B 2 136 ? 13.45400  51.56200  14.28400 1.000 141.99576 ? 136 GLU A O     1 
ATOM 1188 C CB    . GLU B 2 136 ? 14.53600  49.72200  16.66000 1.000 145.52108 ? 136 GLU A CB    1 
ATOM 1189 C CG    . GLU B 2 136 ? 14.79100  48.34900  17.25700 1.000 144.61229 ? 136 GLU A CG    1 
ATOM 1190 C CD    . GLU B 2 136 ? 14.43100  48.25900  18.72800 1.000 152.82857 ? 136 GLU A CD    1 
ATOM 1191 O OE1   . GLU B 2 136 ? 14.29900  49.31200  19.38400 1.000 158.08379 ? 136 GLU A OE1   1 
ATOM 1192 O OE2   . GLU B 2 136 ? 14.27600  47.12400  19.22900 1.000 155.11210 ? 136 GLU A OE2   1 
ATOM 1193 N N     . LEU B 2 137 ? 15.64400  52.00500  14.55600 1.000 142.20763 ? 137 LEU A N     1 
ATOM 1194 C CA    . LEU B 2 137 ? 15.50800  53.34500  13.99500 1.000 144.68638 ? 137 LEU A CA    1 
ATOM 1195 C C     . LEU B 2 137 ? 15.38500  53.29500  12.47600 1.000 135.26411 ? 137 LEU A C     1 
ATOM 1196 O O     . LEU B 2 137 ? 14.60000  54.04600  11.88300 1.000 134.00375 ? 137 LEU A O     1 
ATOM 1197 C CB    . LEU B 2 137 ? 16.70000  54.20600  14.41300 1.000 155.41640 ? 137 LEU A CB    1 
ATOM 1198 C CG    . LEU B 2 137 ? 16.63300  55.69300  14.05200 1.000 153.22462 ? 137 LEU A CG    1 
ATOM 1199 C CD1   . LEU B 2 137 ? 15.46900  56.33800  14.75800 1.000 132.67219 ? 137 LEU A CD1   1 
ATOM 1200 C CD2   . LEU B 2 137 ? 17.92300  56.38900  14.42000 1.000 131.44393 ? 137 LEU A CD2   1 
ATOM 1201 N N     . ALA B 2 138 ? 16.15100  52.41100  11.83400 1.000 142.91000 ? 138 ALA A N     1 
ATOM 1202 C CA    . ALA B 2 138 ? 16.09500  52.28100  10.38300 1.000 149.33021 ? 138 ALA A CA    1 
ATOM 1203 C C     . ALA B 2 138 ? 14.74600  51.74000  9.93900  1.000 143.99347 ? 138 ALA A C     1 
ATOM 1204 O O     . ALA B 2 138 ? 14.21300  52.14900  8.90000  1.000 140.04359 ? 138 ALA A O     1 
ATOM 1205 C CB    . ALA B 2 138 ? 17.22700  51.37800  9.89700  1.000 135.88029 ? 138 ALA A CB    1 
ATOM 1206 N N     . GLU B 2 139 ? 14.24600  50.73400  10.64800 1.000 148.04991 ? 139 GLU A N     1 
ATOM 1207 C CA    . GLU B 2 139 ? 12.89400  50.24700  10.27900 1.000 151.04489 ? 139 GLU A CA    1 
ATOM 1208 C C     . GLU B 2 139 ? 11.90100  51.35000  10.64200 1.000 155.61481 ? 139 GLU A C     1 
ATOM 1209 O O     . GLU B 2 139 ? 10.80900  51.39400  10.05800 1.000 150.17097 ? 139 GLU A O     1 
ATOM 1210 C CB    . GLU B 2 139 ? 12.51700  48.99200  11.06300 1.000 149.02733 ? 139 GLU A CB    1 
ATOM 1211 C CG    . GLU B 2 139 ? 11.16000  48.43700  10.66700 1.000 142.94743 ? 139 GLU A CG    1 
ATOM 1212 C CD    . GLU B 2 139 ? 11.16100  47.01400  10.13700 1.000 152.69587 ? 139 GLU A CD    1 
ATOM 1213 O OE1   . GLU B 2 139 ? 11.90900  46.17900  10.68500 1.000 158.91665 ? 139 GLU A OE1   1 
ATOM 1214 O OE2   . GLU B 2 139 ? 10.42800  46.74900  9.16500  1.000 147.31571 ? 139 GLU A OE2   1 
ATOM 1215 N N     . ALA B 2 140 ? 12.28400  52.19000  11.60300 1.000 146.93788 ? 140 ALA A N     1 
ATOM 1216 C CA    . ALA B 2 140 ? 11.41400  53.27900  12.07900 1.000 131.87352 ? 140 ALA A CA    1 
ATOM 1217 C C     . ALA B 2 140 ? 11.14400  54.22900  10.92000 1.000 139.14669 ? 140 ALA A C     1 
ATOM 1218 O O     . ALA B 2 140 ? 9.98600   54.61600  10.74700 1.000 134.84491 ? 140 ALA A O     1 
ATOM 1219 C CB    . ALA B 2 140 ? 12.11500  53.99300  13.19800 1.000 149.15301 ? 140 ALA A CB    1 
ATOM 1220 N N     . HIS B 2 141 ? 12.18900  54.61000  10.17900 1.000 136.92259 ? 141 HIS A N     1 
ATOM 1221 C CA    . HIS B 2 141 ? 12.01000  55.62900  9.10900  1.000 135.90136 ? 141 HIS A CA    1 
ATOM 1222 C C     . HIS B 2 141 ? 12.18300  54.99200  7.72800  1.000 143.60938 ? 141 HIS A C     1 
ATOM 1223 O O     . HIS B 2 141 ? 12.85600  55.59000  6.86400  1.000 138.63061 ? 141 HIS A O     1 
ATOM 1224 C CB    . HIS B 2 141 ? 12.96300  56.80700  9.32900  1.000 149.40045 ? 141 HIS A CB    1 
ATOM 1225 C CG    . HIS B 2 141 ? 12.45700  58.08800  8.75500  1.000 156.17665 ? 141 HIS A CG    1 
ATOM 1226 N ND1   . HIS B 2 141 ? 11.64500  58.94700  9.46200  1.000 150.75095 ? 141 HIS A ND1   1 
ATOM 1227 C CD2   . HIS B 2 141 ? 12.63000  58.64900  7.55200  1.000 161.18639 ? 141 HIS A CD2   1 
ATOM 1228 C CE1   . HIS B 2 141 ? 11.35000  59.99300  8.70400  1.000 152.15311 ? 141 HIS A CE1   1 
ATOM 1229 N NE2   . HIS B 2 141 ? 11.93800  59.83200  7.53900  1.000 162.67525 ? 141 HIS A NE2   1 
ATOM 1230 N N     . GLY B 2 142 ? 11.60300  53.80900  7.52600  1.000 148.26041 ? 142 GLY A N     1 
ATOM 1231 C CA    . GLY B 2 142 ? 11.62900  53.17500  6.19200  1.000 156.38202 ? 142 GLY A CA    1 
ATOM 1232 C C     . GLY B 2 142 ? 13.01300  53.11900  5.57900  1.000 155.45934 ? 142 GLY A C     1 
ATOM 1233 O O     . GLY B 2 142 ? 13.14000  53.48600  4.39300  1.000 160.48930 ? 142 GLY A O     1 
ATOM 1234 N N     . ILE B 2 143 ? 14.01500  52.67000  6.33400  1.000 150.19477 ? 143 ILE A N     1 
ATOM 1235 C CA    . ILE B 2 143 ? 15.37100  52.48700  5.73700  1.000 150.78437 ? 143 ILE A CA    1 
ATOM 1236 C C     . ILE B 2 143 ? 15.65600  50.98100  5.69300  1.000 160.19435 ? 143 ILE A C     1 
ATOM 1237 O O     . ILE B 2 143 ? 15.39300  50.30400  6.71100  1.000 167.38085 ? 143 ILE A O     1 
ATOM 1238 C CB    . ILE B 2 143 ? 16.44000  53.25800  6.52900  1.000 156.17845 ? 143 ILE A CB    1 
ATOM 1239 C CG1   . ILE B 2 143 ? 16.10300  54.74100  6.60600  1.000 154.64107 ? 143 ILE A CG1   1 
ATOM 1240 C CG2   . ILE B 2 143 ? 17.82700  53.03200  5.93200  1.000 145.56179 ? 143 ILE A CG2   1 
ATOM 1241 C CD1   . ILE B 2 143 ? 15.97500  55.40600  5.24800  1.000 147.48461 ? 143 ILE A CD1   1 
ATOM 1242 N N     . THR B 2 144 ? 16.16000  50.48100  4.56400  1.000 161.50587 ? 144 THR A N     1 
ATOM 1243 C CA    . THR B 2 144 ? 16.38700  49.02700  4.41400  1.000 164.80620 ? 144 THR A CA    1 
ATOM 1244 C C     . THR B 2 144 ? 17.56700  48.62100  5.26600  1.000 169.53195 ? 144 THR A C     1 
ATOM 1245 O O     . THR B 2 144 ? 18.68200  48.56800  4.72100  1.000 173.89341 ? 144 THR A O     1 
ATOM 1246 C CB    . THR B 2 144 ? 16.62100  48.70900  2.94000  1.000 159.87059 ? 144 THR A CB    1 
ATOM 1247 O OG1   . THR B 2 144 ? 17.72200  49.52300  2.55000  1.000 155.73336 ? 144 THR A OG1   1 
ATOM 1248 C CG2   . THR B 2 144 ? 15.41600  49.03900  2.07800  1.000 166.26698 ? 144 THR A CG2   1 
ATOM 1249 N N     . LEU B 2 145 ? 17.33200  48.32600  6.54800  1.000 160.84262 ? 145 LEU A N     1 
ATOM 1250 C CA    . LEU B 2 145 ? 18.42900  47.95300  7.47900  1.000 158.12775 ? 145 LEU A CA    1 
ATOM 1251 C C     . LEU B 2 145 ? 19.00300  46.59500  7.05400  1.000 170.60735 ? 145 LEU A C     1 
ATOM 1252 O O     . LEU B 2 145 ? 20.13700  46.27300  7.46800  1.000 175.58852 ? 145 LEU A O     1 
ATOM 1253 C CB    . LEU B 2 145 ? 17.88300  47.92600  8.90500  1.000 171.44277 ? 145 LEU A CB    1 
ATOM 1254 C CG    . LEU B 2 145 ? 18.87500  47.56800  10.01600 1.000 169.47164 ? 145 LEU A CG    1 
ATOM 1255 C CD1   . LEU B 2 145 ? 19.10000  46.07000  10.11800 1.000 156.94699 ? 145 LEU A CD1   1 
ATOM 1256 C CD2   . LEU B 2 145 ? 20.19300  48.30100  9.85700  1.000 162.59866 ? 145 LEU A CD2   1 
ATOM 1257 N N     . ALA B 2 146 ? 18.24100  45.82500  6.27500  1.000 176.76837 ? 146 ALA A N     1 
ATOM 1258 C CA    . ALA B 2 146 ? 18.74600  44.52800  5.76400  1.000 181.06826 ? 146 ALA A CA    1 
ATOM 1259 C C     . ALA B 2 146 ? 19.32200  43.70400  6.91700  1.000 176.54922 ? 146 ALA A C     1 
ATOM 1260 O O     . ALA B 2 146 ? 18.72100  43.68500  8.01300  1.000 178.55200 ? 146 ALA A O     1 
ATOM 1261 C CB    . ALA B 2 146 ? 19.78300  44.77100  4.68800  1.000 177.23133 ? 146 ALA A CB    1 
ATOM 1262 N N     . ASN B 2 147 ? 20.45300  43.03800  6.67400  1.000 174.33708 ? 147 ASN A N     1 
ATOM 1263 C CA    . ASN B 2 147 ? 21.11900  42.26200  7.75600  1.000 180.19550 ? 147 ASN A CA    1 
ATOM 1264 C C     . ASN B 2 147 ? 21.70200  43.25300  8.76700  1.000 178.77428 ? 147 ASN A C     1 
ATOM 1265 O O     . ASN B 2 147 ? 22.29700  44.26000  8.33100  1.000 184.78160 ? 147 ASN A O     1 
ATOM 1266 C CB    . ASN B 2 147 ? 22.16600  41.30500  7.19700  1.000 179.29123 ? 147 ASN A CB    1 
ATOM 1267 C CG    . ASN B 2 147 ? 22.98700  40.65600  8.28500  1.000 186.98172 ? 147 ASN A CG    1 
ATOM 1268 O OD1   . ASN B 2 147 ? 24.20900  40.83800  8.33400  1.000 178.56500 ? 147 ASN A OD1   1 
ATOM 1269 N ND2   . ASN B 2 147 ? 22.34100  39.90600  9.16500  1.000 185.37237 ? 147 ASN A ND2   1 
ATOM 1270 N N     . ALA B 2 148 ? 21.52500  42.98700  10.06200 1.000 176.18412 ? 148 ALA A N     1 
ATOM 1271 C CA    . ALA B 2 148 ? 22.01100  43.92100  11.10400 1.000 167.22803 ? 148 ALA A CA    1 
ATOM 1272 C C     . ALA B 2 148 ? 23.39000  43.48300  11.58900 1.000 156.97406 ? 148 ALA A C     1 
ATOM 1273 O O     . ALA B 2 148 ? 23.97400  42.55600  10.99100 1.000 161.68941 ? 148 ALA A O     1 
ATOM 1274 C CB    . ALA B 2 148 ? 21.03200  43.96400  12.25200 1.000 156.81084 ? 148 ALA A CB    1 
ATOM 1275 N N     . HIS B 2 149 ? 23.89300  44.14000  12.63400 1.000 156.55716 ? 149 HIS A N     1 
ATOM 1276 C CA    . HIS B 2 149 ? 25.19100  43.73200  13.23300 1.000 161.93767 ? 149 HIS A CA    1 
ATOM 1277 C C     . HIS B 2 149 ? 26.24300  43.57600  12.13300 1.000 168.55075 ? 149 HIS A C     1 
ATOM 1278 O O     . HIS B 2 149 ? 27.12900  42.70300  12.26100 1.000 166.22891 ? 149 HIS A O     1 
ATOM 1279 C CB    . HIS B 2 149 ? 24.98800  42.46700  14.06600 1.000 168.49261 ? 149 HIS A CB    1 
ATOM 1280 C CG    . HIS B 2 149 ? 23.93000  42.61600  15.10600 1.000 172.62889 ? 149 HIS A CG    1 
ATOM 1281 N ND1   . HIS B 2 149 ? 23.11600  41.57600  15.49900 1.000 179.65538 ? 149 HIS A ND1   1 
ATOM 1282 C CD2   . HIS B 2 149 ? 23.54300  43.68000  15.82000 1.000 154.28610 ? 149 HIS A CD2   1 
ATOM 1283 C CE1   . HIS B 2 149 ? 22.27400  42.00900  16.42600 1.000 172.02808 ? 149 HIS A CE1   1 
ATOM 1284 N NE2   . HIS B 2 149 ? 22.51700  43.28400  16.63700 1.000 160.53134 ? 149 HIS A NE2   1 
ATOM 1285 N N     . ARG B 2 150 ? 26.16500  44.40600  11.09000 1.000 171.45587 ? 150 ARG A N     1 
ATOM 1286 C CA    . ARG B 2 150 ? 27.20300  44.36300  10.02700 1.000 169.39968 ? 150 ARG A CA    1 
ATOM 1287 C C     . ARG B 2 150 ? 27.87400  45.74100  9.92900  1.000 169.79763 ? 150 ARG A C     1 
ATOM 1288 O O     . ARG B 2 150 ? 27.16200  46.76100  10.05300 1.000 170.97122 ? 150 ARG A O     1 
ATOM 1289 C CB    . ARG B 2 150 ? 26.60600  43.93200  8.68400  1.000 166.35524 ? 150 ARG A CB    1 
ATOM 1290 C CG    . ARG B 2 150 ? 25.51400  44.83300  8.12800  1.000 172.41156 ? 150 ARG A CG    1 
ATOM 1291 C CD    . ARG B 2 150 ? 25.20300  44.46800  6.68700  1.000 169.64468 ? 150 ARG A CD    1 
ATOM 1292 N NE    . ARG B 2 150 ? 24.91000  43.03900  6.53900  1.000 169.73236 ? 150 ARG A NE    1 
ATOM 1293 C CZ    . ARG B 2 150 ? 25.60200  42.20900  5.77000  1.000 178.44485 ? 150 ARG A CZ    1 
ATOM 1294 N NH1   . ARG B 2 150 ? 26.51400  42.68300  4.94000  1.000 163.51195 ? 150 ARG A NH1   1 
ATOM 1295 N NH2   . ARG B 2 150 ? 25.38500  40.90800  5.83900  1.000 180.10388 ? 150 ARG A NH2   1 
ATOM 1296 N N     . ALA B 2 151 ? 29.19900  45.75300  9.75900  1.000 171.13996 ? 151 ALA A N     1 
ATOM 1297 C CA    . ALA B 2 151 ? 29.93800  47.02800  9.61500  1.000 171.26870 ? 151 ALA A CA    1 
ATOM 1298 C C     . ALA B 2 151 ? 29.53600  47.67400  8.29400  1.000 174.37420 ? 151 ALA A C     1 
ATOM 1299 O O     . ALA B 2 151 ? 29.95900  48.81400  8.02400  1.000 175.99981 ? 151 ALA A O     1 
ATOM 1300 C CB    . ALA B 2 151 ? 31.42100  46.76900  9.66800  1.000 166.63348 ? 151 ALA A CB    1 
ATOM 1301 N N     . ASP B 2 152 ? 28.73300  46.96200  7.50100  1.000 173.49953 ? 152 ASP A N     1 
ATOM 1302 C CA    . ASP B 2 152 ? 28.32100  47.48100  6.17100  1.000 166.61478 ? 152 ASP A CA    1 
ATOM 1303 C C     . ASP B 2 152 ? 27.11300  48.40400  6.34800  1.000 174.56939 ? 152 ASP A C     1 
ATOM 1304 O O     . ASP B 2 152 ? 27.28200  49.63200  6.21100  1.000 181.79140 ? 152 ASP A O     1 
ATOM 1305 C CB    . ASP B 2 152 ? 28.05700  46.33600  5.20900  1.000 168.84115 ? 152 ASP A CB    1 
ATOM 1306 C CG    . ASP B 2 152 ? 29.15500  45.28500  5.14100  1.000 178.58399 ? 152 ASP A CG    1 
ATOM 1307 O OD1   . ASP B 2 152 ? 30.29400  45.64900  4.78200  1.000 188.01058 ? 152 ASP A OD1   1 
ATOM 1308 O OD2   . ASP B 2 152 ? 28.86300  44.11200  5.45500  1.000 173.89611 ? 152 ASP A OD2   1 
ATOM 1309 N N     . GLU B 2 153 ? 25.94500  47.83300  6.65700  1.000 174.39135 ? 153 GLU A N     1 
ATOM 1310 C CA    . GLU B 2 153 ? 24.71900  48.65000  6.85300  1.000 179.63440 ? 153 GLU A CA    1 
ATOM 1311 C C     . GLU B 2 153 ? 24.93500  49.59300  8.04700  1.000 173.04025 ? 153 GLU A C     1 
ATOM 1312 O O     . GLU B 2 153 ? 24.55300  50.77400  7.94800  1.000 168.31412 ? 153 GLU A O     1 
ATOM 1313 C CB    . GLU B 2 153 ? 23.47300  47.79200  7.07800  1.000 175.16047 ? 153 GLU A CB    1 
ATOM 1314 C CG    . GLU B 2 153 ? 23.02800  47.01700  5.84100  1.000 177.73271 ? 153 GLU A CG    1 
ATOM 1315 C CD    . GLU B 2 153 ? 22.41800  47.83700  4.71800  1.000 174.85818 ? 153 GLU A CD    1 
ATOM 1316 O OE1   . GLU B 2 153 ? 22.33000  49.07400  4.84900  1.000 164.21664 ? 153 GLU A OE1   1 
ATOM 1317 O OE2   . GLU B 2 153 ? 22.02100  47.22600  3.70400  1.000 181.62717 ? 153 GLU A OE2   1 
ATOM 1318 N N     . ASP B 2 154 ? 25.56700  49.09700  9.11400  1.000 170.08940 ? 154 ASP A N     1 
ATOM 1319 C CA    . ASP B 2 154 ? 25.83300  49.95700  10.30000 1.000 173.45424 ? 154 ASP A CA    1 
ATOM 1320 C C     . ASP B 2 154 ? 26.65000  51.16900  9.84500  1.000 172.10653 ? 154 ASP A C     1 
ATOM 1321 O O     . ASP B 2 154 ? 26.70600  52.15400  10.60600 1.000 173.12261 ? 154 ASP A O     1 
ATOM 1322 C CB    . ASP B 2 154 ? 26.45800  49.18200  11.44900 1.000 173.95551 ? 154 ASP A CB    1 
ATOM 1323 C CG    . ASP B 2 154 ? 25.50900  48.27500  12.22000 1.000 170.24761 ? 154 ASP A CG    1 
ATOM 1324 O OD1   . ASP B 2 154 ? 24.89100  47.39500  11.58500 1.000 166.14020 ? 154 ASP A OD1   1 
ATOM 1325 O OD2   . ASP B 2 154 ? 25.40000  48.45400  13.45000 1.000 180.56569 ? 154 ASP A OD2   1 
ATOM 1326 N N     . ALA B 2 155 ? 27.28300  51.09100  8.67400  1.000 160.03454 ? 155 ALA A N     1 
ATOM 1327 C CA    . ALA B 2 155 ? 27.98500  52.27800  8.13500  1.000 162.23426 ? 155 ALA A CA    1 
ATOM 1328 C C     . ALA B 2 155 ? 27.10700  52.90600  7.05400  1.000 166.16002 ? 155 ALA A C     1 
ATOM 1329 O O     . ALA B 2 155 ? 27.16300  54.13700  6.86900  1.000 169.27194 ? 155 ALA A O     1 
ATOM 1330 C CB    . ALA B 2 155 ? 29.33900  51.88900  7.59600  1.000 160.16687 ? 155 ALA A CB    1 
ATOM 1331 N N     . ALA B 2 156 ? 26.30100  52.08600  6.37700  1.000 166.06869 ? 156 ALA A N     1 
ATOM 1332 C CA    . ALA B 2 156 ? 25.46400  52.59600  5.26400  1.000 164.87004 ? 156 ALA A CA    1 
ATOM 1333 C C     . ALA B 2 156 ? 24.18100  53.22000  5.80700  1.000 160.03707 ? 156 ALA A C     1 
ATOM 1334 O O     . ALA B 2 156 ? 23.89500  54.38600  5.47300  1.000 163.70129 ? 156 ALA A O     1 
ATOM 1335 C CB    . ALA B 2 156 ? 25.15400  51.47400  4.30300  1.000 166.79388 ? 156 ALA A CB    1 
ATOM 1336 N N     . THR B 2 157 ? 23.42900  52.46900  6.61400  1.000 158.32624 ? 157 THR A N     1 
ATOM 1337 C CA    . THR B 2 157 ? 22.13200  52.97900  7.10600  1.000 160.39847 ? 157 THR A CA    1 
ATOM 1338 C C     . THR B 2 157 ? 22.36600  54.18400  7.98900  1.000 162.95075 ? 157 THR A C     1 
ATOM 1339 O O     . THR B 2 157 ? 21.59900  55.15900  7.86500  1.000 164.28330 ? 157 THR A O     1 
ATOM 1340 C CB    . THR B 2 157 ? 21.37500  51.87100  7.83400  1.000 160.72138 ? 157 THR A CB    1 
ATOM 1341 O OG1   . THR B 2 157 ? 22.34000  51.23800  8.66500  1.000 168.08596 ? 157 THR A OG1   1 
ATOM 1342 C CG2   . THR B 2 157 ? 20.77100  50.86100  6.87600  1.000 165.14335 ? 157 THR A CG2   1 
ATOM 1343 N N     . THR B 2 158 ? 23.39200  54.14000  8.84100  1.000 163.75291 ? 158 THR A N     1 
ATOM 1344 C CA    . THR B 2 158 ? 23.71300  55.31400  9.67700  1.000 152.87780 ? 158 THR A CA    1 
ATOM 1345 C C     . THR B 2 158 ? 23.89500  56.50200  8.77000  1.000 141.55127 ? 158 THR A C     1 
ATOM 1346 O O     . THR B 2 158 ? 23.30200  57.56300  9.05300  1.000 133.28433 ? 158 THR A O     1 
ATOM 1347 C CB    . THR B 2 158 ? 24.97800  55.04400  10.48400 1.000 156.09814 ? 158 THR A CB    1 
ATOM 1348 O OG1   . THR B 2 158 ? 25.81000  54.30600  9.59600  1.000 159.46963 ? 158 THR A OG1   1 
ATOM 1349 C CG2   . THR B 2 158 ? 24.70400  54.24600  11.74500 1.000 151.50780 ? 158 THR A CG2   1 
ATOM 1350 N N     . ALA B 2 159 ? 24.67700  56.32700  7.70700  1.000 140.38357 ? 159 ALA A N     1 
ATOM 1351 C CA    . ALA B 2 159 ? 24.93500  57.43300  6.76000  1.000 142.53499 ? 159 ALA A CA    1 
ATOM 1352 C C     . ALA B 2 159 ? 23.61700  57.88300  6.13300  1.000 142.57596 ? 159 ALA A C     1 
ATOM 1353 O O     . ALA B 2 159 ? 23.36500  59.10200  6.04700  1.000 149.85378 ? 159 ALA A O     1 
ATOM 1354 C CB    . ALA B 2 159 ? 25.91300  56.97200  5.71200  1.000 144.87370 ? 159 ALA A CB    1 
ATOM 1355 N N     . LYS B 2 160 ? 22.79400  56.92200  5.71400  1.000 135.01507 ? 160 LYS A N     1 
ATOM 1356 C CA    . LYS B 2 160 ? 21.50000  57.26800  5.07500  1.000 140.57342 ? 160 LYS A CA    1 
ATOM 1357 C C     . LYS B 2 160 ? 20.69600  58.13300  6.05300  1.000 146.56397 ? 160 LYS A C     1 
ATOM 1358 O O     . LYS B 2 160 ? 20.09700  59.13200  5.61200  1.000 149.27811 ? 160 LYS A O     1 
ATOM 1359 C CB    . LYS B 2 160 ? 20.72200  56.00200  4.70400  1.000 146.43990 ? 160 LYS A CB    1 
ATOM 1360 C CG    . LYS B 2 160 ? 21.38300  55.10900  3.66500  1.000 158.04497 ? 160 LYS A CG    1 
ATOM 1361 C CD    . LYS B 2 160 ? 20.56400  53.86200  3.35600  1.000 160.56433 ? 160 LYS A CD    1 
ATOM 1362 C CE    . LYS B 2 160 ? 21.20100  52.98800  2.32300  1.000 152.11464 ? 160 LYS A CE    1 
ATOM 1363 N NZ    . LYS B 2 160 ? 20.36500  51.82500  2.01500  1.000 150.81097 ? 160 LYS A NZ    1 
ATOM 1364 N N     . LEU B 2 161 ? 20.69400  57.75700  7.33200  1.000 146.34638 ? 161 LEU A N     1 
ATOM 1365 C CA    . LEU B 2 161 ? 19.96000  58.54200  8.35400  1.000 132.10350 ? 161 LEU A CA    1 
ATOM 1366 C C     . LEU B 2 161 ? 20.67200  59.88600  8.53900  1.000 138.23023 ? 161 LEU A C     1 
ATOM 1367 O O     . LEU B 2 161 ? 19.98400  60.92400  8.55000  1.000 138.92200 ? 161 LEU A O     1 
ATOM 1368 C CB    . LEU B 2 161 ? 19.90400  57.73700  9.64800  1.000 140.30425 ? 161 LEU A CB    1 
ATOM 1369 C CG    . LEU B 2 161 ? 19.05100  56.46500  9.60600  1.000 146.88363 ? 161 LEU A CG    1 
ATOM 1370 C CD1   . LEU B 2 161 ? 19.33800  55.58300  10.80600 1.000 137.12724 ? 161 LEU A CD1   1 
ATOM 1371 C CD2   . LEU B 2 161 ? 17.57600  56.81700  9.55400  1.000 142.60037 ? 161 LEU A CD2   1 
ATOM 1372 N N     . MET B 2 162 ? 21.99800  59.86700  8.67700  1.000 136.60826 ? 162 MET A N     1 
ATOM 1373 C CA    . MET B 2 162 ? 22.72400  61.12700  8.77200  1.000 126.61599 ? 162 MET A CA    1 
ATOM 1374 C C     . MET B 2 162 ? 22.25300  62.08500  7.68900  1.000 129.21781 ? 162 MET A C     1 
ATOM 1375 O O     . MET B 2 162 ? 21.97600  63.26500  7.94900  1.000 137.35524 ? 162 MET A O     1 
ATOM 1376 C CB    . MET B 2 162 ? 24.22400  60.85700  8.65000  1.000 133.00154 ? 162 MET A CB    1 
ATOM 1377 C CG    . MET B 2 162 ? 25.11400  62.04000  8.94900  1.000 127.83998 ? 162 MET A CG    1 
ATOM 1378 S SD    . MET B 2 162 ? 26.56700  62.06300  7.88900  1.000 148.07226 ? 162 MET A SD    1 
ATOM 1379 C CE    . MET B 2 162 ? 27.66100  60.97000  8.79100  1.000 153.08227 ? 162 MET A CE    1 
ATOM 1380 N N     . ILE B 2 163 ? 22.14500  61.57400  6.46000  1.000 131.13253 ? 163 ILE A N     1 
ATOM 1381 C CA    . ILE B 2 163 ? 21.54900  62.32100  5.35700  1.000 132.92184 ? 163 ILE A CA    1 
ATOM 1382 C C     . ILE B 2 163 ? 20.16300  62.81200  5.74800  1.000 129.71703 ? 163 ILE A C     1 
ATOM 1383 O O     . ILE B 2 163 ? 19.87600  64.00900  5.69600  1.000 140.53268 ? 163 ILE A O     1 
ATOM 1384 C CB    . ILE B 2 163 ? 21.50300  61.45500  4.08600  1.000 132.63172 ? 163 ILE A CB    1 
ATOM 1385 C CG1   . ILE B 2 163 ? 22.89300  61.37100  3.45700  1.000 137.62734 ? 163 ILE A CG1   1 
ATOM 1386 C CG2   . ILE B 2 163 ? 20.49600  62.00300  3.08600  1.000 134.74920 ? 163 ILE A CG2   1 
ATOM 1387 C CD1   . ILE B 2 163 ? 22.94400  60.52500  2.21000  1.000 149.92640 ? 163 ILE A CD1   1 
ATOM 1388 N N     . LEU B 2 164 ? 19.29700  61.88900  6.18100  1.000 125.51116 ? 164 LEU A N     1 
ATOM 1389 C CA    . LEU B 2 164 ? 17.91800  62.23700  6.51500  1.000 133.78401 ? 164 LEU A CA    1 
ATOM 1390 C C     . LEU B 2 164 ? 17.86200  63.34000  7.56500  1.000 129.23399 ? 164 LEU A C     1 
ATOM 1391 O O     . LEU B 2 164 ? 16.99700  64.22500  7.50500  1.000 130.97497 ? 164 LEU A O     1 
ATOM 1392 C CB    . LEU B 2 164 ? 17.17100  60.99300  6.99600  1.000 137.46988 ? 164 LEU A CB    1 
ATOM 1393 C CG    . LEU B 2 164 ? 17.02100  59.86600  5.96800  1.000 141.96871 ? 164 LEU A CG    1 
ATOM 1394 C CD1   . LEU B 2 164 ? 16.44200  58.60700  6.60100  1.000 147.44971 ? 164 LEU A CD1   1 
ATOM 1395 C CD2   . LEU B 2 164 ? 16.17500  60.31600  4.78800  1.000 137.84138 ? 164 LEU A CD2   1 
ATOM 1396 N N     . ALA B 2 165 ? 18.78100  63.30700  8.53000  1.000 134.88741 ? 165 ALA A N     1 
ATOM 1397 C CA    . ALA B 2 165 ? 18.90600  64.41300  9.46900  1.000 125.62709 ? 165 ALA A CA    1 
ATOM 1398 C C     . ALA B 2 165 ? 19.21900  65.70700  8.73200  1.000 127.71463 ? 165 ALA A C     1 
ATOM 1399 O O     . ALA B 2 165 ? 18.51500  66.71100  8.89100  1.000 131.38952 ? 165 ALA A O     1 
ATOM 1400 C CB    . ALA B 2 165 ? 19.98800  64.10300  10.50300 1.000 120.84861 ? 165 ALA A CB    1 
ATOM 1401 N N     . PHE B 2 166 ? 20.31300  65.72000  7.97800  1.000 123.00865 ? 166 PHE A N     1 
ATOM 1402 C CA    . PHE B 2 166 ? 20.70000  66.95600  7.25700  1.000 116.97466 ? 166 PHE A CA    1 
ATOM 1403 C C     . PHE B 2 166 ? 19.53900  67.40200  6.38200  1.000 118.75505 ? 166 PHE A C     1 
ATOM 1404 O O     . PHE B 2 166 ? 19.20600  68.58700  6.36300  1.000 120.78216 ? 166 PHE A O     1 
ATOM 1405 C CB    . PHE B 2 166 ? 21.98800  66.70400  6.49000  1.000 122.20341 ? 166 PHE A CB    1 
ATOM 1406 C CG    . PHE B 2 166 ? 23.06500  66.23700  7.42100  1.000 127.26138 ? 166 PHE A CG    1 
ATOM 1407 C CD1   . PHE B 2 166 ? 22.87800  66.33700  8.78300  1.000 125.30616 ? 166 PHE A CD1   1 
ATOM 1408 C CD2   . PHE B 2 166 ? 24.25000  65.71400  6.94600  1.000 127.71214 ? 166 PHE A CD2   1 
ATOM 1409 C CE1   . PHE B 2 166 ? 23.86000  65.91200  9.65700  1.000 126.95306 ? 166 PHE A CE1   1 
ATOM 1410 C CE2   . PHE B 2 166 ? 25.23000  65.28700  7.82400  1.000 135.04979 ? 166 PHE A CE2   1 
ATOM 1411 C CZ    . PHE B 2 166 ? 25.03300  65.38600  9.17700  1.000 126.26233 ? 166 PHE A CZ    1 
ATOM 1412 N N     . GLU B 2 167 ? 18.85500  66.43200  5.79600  1.000 119.52990 ? 167 GLU A N     1 
ATOM 1413 C CA    . GLU B 2 167 ? 17.67600  66.79800  4.99200  1.000 123.24668 ? 167 GLU A CA    1 
ATOM 1414 C C     . GLU B 2 167 ? 16.65200  67.42600  5.93100  1.000 123.63418 ? 167 GLU A C     1 
ATOM 1415 O O     . GLU B 2 167 ? 16.15700  68.50600  5.60800  1.000 126.47852 ? 167 GLU A O     1 
ATOM 1416 C CB    . GLU B 2 167 ? 17.06100  65.54100  4.39700  1.000 137.06221 ? 167 GLU A CB    1 
ATOM 1417 C CG    . GLU B 2 167 ? 18.06000  64.68000  3.66900  1.000 131.56070 ? 167 GLU A CG    1 
ATOM 1418 C CD    . GLU B 2 167 ? 17.39400  63.94100  2.53100  1.000 145.74566 ? 167 GLU A CD    1 
ATOM 1419 O OE1   . GLU B 2 167 ? 16.32300  64.39300  2.09400  1.000 157.19199 ? 167 GLU A OE1   1 
ATOM 1420 O OE2   . GLU B 2 167 ? 17.94200  62.92000  2.09500  1.000 160.56432 ? 167 GLU A OE2   1 
ATOM 1421 N N     . LYS B 2 168 ? 16.43600  66.83700  7.10600  1.000 128.53513 ? 168 LYS A N     1 
ATOM 1422 C CA    . LYS B 2 168 ? 15.43900  67.37700  8.06400  1.000 116.89744 ? 168 LYS A CA    1 
ATOM 1423 C C     . LYS B 2 168 ? 15.87200  68.76100  8.55500  1.000 126.80622 ? 168 LYS A C     1 
ATOM 1424 O O     . LYS B 2 168 ? 14.99500  69.62800  8.73500  1.000 116.49842 ? 168 LYS A O     1 
ATOM 1425 C CB    . LYS B 2 168 ? 15.33300  66.48500  9.30100  1.000 114.42881 ? 168 LYS A CB    1 
ATOM 1426 C CG    . LYS B 2 168 ? 14.10900  66.72800  10.16200 1.000 116.85016 ? 168 LYS A CG    1 
ATOM 1427 C CD    . LYS B 2 168 ? 13.05100  65.66800  9.89100  1.000 127.20661 ? 168 LYS A CD    1 
ATOM 1428 C CE    . LYS B 2 168 ? 13.51400  64.32200  10.34500 1.000 148.53336 ? 168 LYS A CE    1 
ATOM 1429 N NZ    . LYS B 2 168 ? 13.64800  64.27000  11.80300 1.000 132.61684 ? 168 LYS A NZ    1 
ATOM 1430 N N     . PHE B 2 169 ? 17.17300  68.96300  8.75100  1.000 133.57213 ? 169 PHE A N     1 
ATOM 1431 C CA    . PHE B 2 169 ? 17.65900  70.24100  9.34200  1.000 111.79412 ? 169 PHE A CA    1 
ATOM 1432 C C     . PHE B 2 169 ? 17.40000  71.42300  8.41000  1.000 124.94758 ? 169 PHE A C     1 
ATOM 1433 O O     . PHE B 2 169 ? 17.77400  72.55300  8.77500  1.000 133.98395 ? 169 PHE A O     1 
ATOM 1434 C CB    . PHE B 2 169 ? 19.14700  70.10400  9.66900  1.000 117.92143 ? 169 PHE A CB    1 
ATOM 1435 C CG    . PHE B 2 169 ? 19.46000  69.15600  10.81900 1.000 120.41147 ? 169 PHE A CG    1 
ATOM 1436 C CD1   . PHE B 2 169 ? 18.54700  68.95700  11.84800 1.000 110.06968 ? 169 PHE A CD1   1 
ATOM 1437 C CD2   . PHE B 2 169 ? 20.66900  68.47400  10.87400 1.000 121.14129 ? 169 PHE A CD2   1 
ATOM 1438 C CE1   . PHE B 2 169 ? 18.83600  68.09700  12.89400 1.000 103.14695 ? 169 PHE A CE1   1 
ATOM 1439 C CE2   . PHE B 2 169 ? 20.95200  67.61500  11.92400 1.000 106.60200 ? 169 PHE A CE2   1 
ATOM 1440 C CZ    . PHE B 2 169 ? 20.03600  67.42900  12.93100 1.000 103.92318 ? 169 PHE A CZ    1 
ATOM 1441 N N     . GLU B 2 170 ? 16.76700  71.18900  7.26100  1.000 133.15724 ? 170 GLU A N     1 
ATOM 1442 C CA    . GLU B 2 170 ? 16.42200  72.31600  6.35600  1.000 126.07857 ? 170 GLU A CA    1 
ATOM 1443 C C     . GLU B 2 170 ? 15.16000  73.00900  6.88400  1.000 123.20682 ? 170 GLU A C     1 
ATOM 1444 O O     . GLU B 2 170 ? 14.07400  72.76800  6.31700  1.000 118.72322 ? 170 GLU A O     1 
ATOM 1445 C CB    . GLU B 2 170 ? 16.21500  71.81400  4.93100  1.000 130.18284 ? 170 GLU A CB    1 
ATOM 1446 C CG    . GLU B 2 170 ? 17.47400  71.20200  4.32400  1.000 146.27527 ? 170 GLU A CG    1 
ATOM 1447 C CD    . GLU B 2 170 ? 17.25300  70.58500  2.95400  1.000 160.54273 ? 170 GLU A CD    1 
ATOM 1448 O OE1   . GLU B 2 170 ? 16.82400  71.31800  2.03900  1.000 155.65030 ? 170 GLU A OE1   1 
ATOM 1449 O OE2   . GLU B 2 170 ? 17.51100  69.37300  2.80100  1.000 157.51401 ? 170 GLU A OE2   1 
ATOM 1450 N N     . LYS B 2 171 ? 15.30300  73.83700  7.92000  1.000 141.63786 ? 171 LYS A N     1 
ATOM 1451 C CA    . LYS B 2 171 ? 14.13500  74.51400  8.54000  1.000 136.84495 ? 171 LYS A CA    1 
ATOM 1452 C C     . LYS B 2 171 ? 14.32000  76.03500  8.46900  1.000 133.00846 ? 171 LYS A C     1 
ATOM 1453 O O     . LYS B 2 171 ? 15.19000  76.49100  7.70100  1.000 137.56508 ? 171 LYS A O     1 
ATOM 1454 C CB    . LYS B 2 171 ? 14.01300  74.06500  9.99700  1.000 121.58092 ? 171 LYS A CB    1 
ATOM 1455 C CG    . LYS B 2 171 ? 15.32100  74.08500  10.77100 1.000 126.16858 ? 171 LYS A CG    1 
ATOM 1456 C CD    . LYS B 2 171 ? 15.17900  73.53900  12.18600 1.000 130.77428 ? 171 LYS A CD    1 
ATOM 1457 C CE    . LYS B 2 171 ? 14.55200  72.18300  12.20300 1.000 130.69952 ? 171 LYS A CE    1 
ATOM 1458 N NZ    . LYS B 2 171 ? 15.31900  71.21800  11.41200 1.000 144.39832 ? 171 LYS A NZ    1 
ATOM 1459 N N     . LEU B 2 172 ? 13.53400  76.78400  9.24600  1.000 115.32637 ? 172 LEU A N     1 
ATOM 1460 C CA    . LEU B 2 172 ? 13.64900  78.26400  9.24100  1.000 124.77628 ? 172 LEU A CA    1 
ATOM 1461 C C     . LEU B 2 172 ? 15.09300  78.63200  9.60600  1.000 132.27592 ? 172 LEU A C     1 
ATOM 1462 O O     . LEU B 2 172 ? 15.70900  77.89400  10.40300 1.000 129.74705 ? 172 LEU A O     1 
ATOM 1463 C CB    . LEU B 2 172 ? 12.63000  78.89800  10.18400 1.000 113.71359 ? 172 LEU A CB    1 
ATOM 1464 C CG    . LEU B 2 172 ? 11.20700  79.04600  9.63800  1.000 135.16382 ? 172 LEU A CG    1 
ATOM 1465 C CD1   . LEU B 2 172 ? 11.20700  79.84100  8.34500  1.000 152.51933 ? 172 LEU A CD1   1 
ATOM 1466 C CD2   . LEU B 2 172 ? 10.52100  77.70600  9.44300  1.000 130.49569 ? 172 LEU A CD2   1 
ATOM 1467 N N     . PRO B 2 173 ? 15.66000  79.73800  9.07900  1.000 127.46108 ? 173 PRO A N     1 
ATOM 1468 C CA    . PRO B 2 173 ? 17.06800  80.03700  9.31300  1.000 121.49914 ? 173 PRO A CA    1 
ATOM 1469 C C     . PRO B 2 173 ? 17.36600  80.23500  10.77900 1.000 117.03053 ? 173 PRO A C     1 
ATOM 1470 O O     . PRO B 2 173 ? 18.16400  79.47100  11.35500 1.000 119.83866 ? 173 PRO A O     1 
ATOM 1471 C CB    . PRO B 2 173 ? 17.33300  81.33000  8.52700  1.000 130.05243 ? 173 PRO A CB    1 
ATOM 1472 C CG    . PRO B 2 173 ? 16.09000  81.55200  7.69200  1.000 146.62875 ? 173 PRO A CG    1 
ATOM 1473 C CD    . PRO B 2 173 ? 14.96400  80.74000  8.30100  1.000 129.02721 ? 173 PRO A CD    1 
ATOM 1474 N N     . LEU B 2 174 ? 16.73500  81.24300  11.37800 1.000 115.20302 ? 174 LEU A N     1 
ATOM 1475 C CA    . LEU B 2 174 ? 17.03300  81.56300  12.79500 1.000 132.68771 ? 174 LEU A CA    1 
ATOM 1476 C C     . LEU B 2 174 ? 17.03600  80.26300  13.60900 1.000 131.89102 ? 174 LEU A C     1 
ATOM 1477 O O     . LEU B 2 174 ? 17.81600  80.17300  14.57700 1.000 128.09390 ? 174 LEU A O     1 
ATOM 1478 C CB    . LEU B 2 174 ? 16.01000  82.56800  13.31700 1.000 141.59110 ? 174 LEU A CB    1 
ATOM 1479 C CG    . LEU B 2 174 ? 15.99800  83.92900  12.61500 1.000 107.93595 ? 174 LEU A CG    1 
ATOM 1480 C CD1   . LEU B 2 174 ? 14.96000  84.84700  13.23500 1.000 121.47146 ? 174 LEU A CD1   1 
ATOM 1481 C CD2   . LEU B 2 174 ? 17.37400  84.56600  12.67000 1.000 103.87334 ? 174 LEU A CD2   1 
ATOM 1482 N N     . ASP B 2 175 ? 16.21200  79.29000  13.22100 1.000 119.69719 ? 175 ASP A N     1 
ATOM 1483 C CA    . ASP B 2 175 ? 16.11800  78.05600  14.05100 1.000 119.49891 ? 175 ASP A CA    1 
ATOM 1484 C C     . ASP B 2 175 ? 17.44500  77.29600  14.01000 1.000 117.97462 ? 175 ASP A C     1 
ATOM 1485 O O     . ASP B 2 175 ? 17.88700  76.81100  15.07000 1.000 109.77923 ? 175 ASP A O     1 
ATOM 1486 C CB    . ASP B 2 175 ? 14.99000  77.15000  13.59500 1.000 110.87470 ? 175 ASP A CB    1 
ATOM 1487 C CG    . ASP B 2 175 ? 13.67100  77.84700  13.30600 1.000 131.34088 ? 175 ASP A CG    1 
ATOM 1488 O OD1   . ASP B 2 175 ? 13.54100  79.03500  13.66500 1.000 139.95813 ? 175 ASP A OD1   1 
ATOM 1489 O OD2   . ASP B 2 175 ? 12.81000  77.20800  12.66900 1.000 134.85245 ? 175 ASP A OD2   1 
ATOM 1490 N N     . THR B 2 176 ? 18.03200  77.16100  12.82200 1.000 100.47171 ? 176 THR A N     1 
ATOM 1491 C CA    . THR B 2 176 ? 19.32100  76.45400  12.70300 1.000 101.62842 ? 176 THR A CA    1 
ATOM 1492 C C     . THR B 2 176 ? 20.32400  77.16200  13.58400 1.000 113.39056 ? 176 THR A C     1 
ATOM 1493 O O     . THR B 2 176 ? 21.15500  76.47500  14.21600 1.000 121.14392 ? 176 THR A O     1 
ATOM 1494 C CB    . THR B 2 176 ? 19.75100  76.42600  11.23800 1.000 109.45884 ? 176 THR A CB    1 
ATOM 1495 O OG1   . THR B 2 176 ? 18.76000  75.64600  10.57900 1.000 116.97643 ? 176 THR A OG1   1 
ATOM 1496 C CG2   . THR B 2 176 ? 21.11800  75.79800  11.04100 1.000 112.11853 ? 176 THR A CG2   1 
ATOM 1497 N N     . LEU B 2 177 ? 20.23800  78.49100  13.64800 1.000 108.48461 ? 177 LEU A N     1 
ATOM 1498 C CA    . LEU B 2 177 ? 21.17600  79.28600  14.48000 1.000 106.87202 ? 177 LEU A CA    1 
ATOM 1499 C C     . LEU B 2 177 ? 20.98900  78.90800  15.95500 1.000 105.40330 ? 177 LEU A C     1 
ATOM 1500 O O     . LEU B 2 177 ? 22.00300  78.82100  16.68000 1.000 96.51841  ? 177 LEU A O     1 
ATOM 1501 C CB    . LEU B 2 177 ? 20.90900  80.76900  14.23700 1.000 103.58090 ? 177 LEU A CB    1 
ATOM 1502 C CG    . LEU B 2 177 ? 21.26900  81.29300  12.84400 1.000 119.09682 ? 177 LEU A CG    1 
ATOM 1503 C CD1   . LEU B 2 177 ? 20.68600  82.67600  12.62600 1.000 126.86221 ? 177 LEU A CD1   1 
ATOM 1504 C CD2   . LEU B 2 177 ? 22.77800  81.32800  12.69400 1.000 128.44211 ? 177 LEU A CD2   1 
ATOM 1505 N N     . LYS B 2 178 ? 19.74000  78.69300  16.37300 1.000 107.19526 ? 178 LYS A N     1 
ATOM 1506 C CA    . LYS B 2 178 ? 19.45900  78.33500  17.78500 1.000 108.72490 ? 178 LYS A CA    1 
ATOM 1507 C C     . LYS B 2 178 ? 20.24100  77.06500  18.13400 1.000 107.44029 ? 178 LYS A C     1 
ATOM 1508 O O     . LYS B 2 178 ? 20.92000  77.05200  19.18100 1.000 110.47659 ? 178 LYS A O     1 
ATOM 1509 C CB    . LYS B 2 178 ? 17.96100  78.08700  17.98300 1.000 102.85362 ? 178 LYS A CB    1 
ATOM 1510 C CG    . LYS B 2 178 ? 17.04500  79.22300  17.55800 1.000 118.34972 ? 178 LYS A CG    1 
ATOM 1511 C CD    . LYS B 2 178 ? 15.57000  78.84900  17.62800 1.000 92.84680  ? 178 LYS A CD    1 
ATOM 1512 C CE    . LYS B 2 178 ? 14.68400  79.90300  17.04700 1.000 127.47374 ? 178 LYS A CE    1 
ATOM 1513 N NZ    . LYS B 2 178 ? 13.28600  79.46800  17.02200 1.000 120.57925 ? 178 LYS A NZ    1 
ATOM 1514 N N     . GLN B 2 179 ? 20.16400  76.05200  17.27300 1.000 95.91703  ? 179 GLN A N     1 
ATOM 1515 C CA    . GLN B 2 179 ? 20.84000  74.76100  17.55900 1.000 96.27324  ? 179 GLN A CA    1 
ATOM 1516 C C     . GLN B 2 179 ? 22.36300  74.95800  17.50900 1.000 110.64656 ? 179 GLN A C     1 
ATOM 1517 O O     . GLN B 2 179 ? 23.07000  74.29700  18.29300 1.000 119.40458 ? 179 GLN A O     1 
ATOM 1518 C CB    . GLN B 2 179 ? 20.34200  73.71100  16.56800 1.000 101.23880 ? 179 GLN A CB    1 
ATOM 1519 C CG    . GLN B 2 179 ? 18.84500  73.80100  16.29300 1.000 123.05484 ? 179 GLN A CG    1 
ATOM 1520 C CD    . GLN B 2 179 ? 18.26600  72.54700  15.67600 1.000 135.54152 ? 179 GLN A CD    1 
ATOM 1521 O OE1   . GLN B 2 179 ? 18.95700  71.54000  15.49000 1.000 142.23828 ? 179 GLN A OE1   1 
ATOM 1522 N NE2   . GLN B 2 179 ? 16.97900  72.59300  15.36600 1.000 126.91041 ? 179 GLN A NE2   1 
ATOM 1523 N N     . LEU B 2 180 ? 22.84400  75.83400  16.62500 1.000 107.77275 ? 180 LEU A N     1 
ATOM 1524 C CA    . LEU B 2 180 ? 24.30000  76.12000  16.55300 1.000 98.18929  ? 180 LEU A CA    1 
ATOM 1525 C C     . LEU B 2 180 ? 24.79700  76.52200  17.94700 1.000 94.35883  ? 180 LEU A C     1 
ATOM 1526 O O     . LEU B 2 180 ? 25.70900  75.84900  18.47700 1.000 92.14384  ? 180 LEU A O     1 
ATOM 1527 C CB    . LEU B 2 180 ? 24.54500  77.23400  15.53900 1.000 99.77181  ? 180 LEU A CB    1 
ATOM 1528 C CG    . LEU B 2 180 ? 25.94600  77.85500  15.54900 1.000 103.53280 ? 180 LEU A CG    1 
ATOM 1529 C CD1   . LEU B 2 180 ? 26.99000  76.87500  15.04800 1.000 109.18863 ? 180 LEU A CD1   1 
ATOM 1530 C CD2   . LEU B 2 180 ? 25.98300  79.14200  14.74700 1.000 101.16071 ? 180 LEU A CD2   1 
ATOM 1531 N N     . TYR B 2 181 ? 24.20600  77.57300  18.51700 1.000 93.85064  ? 181 TYR A N     1 
ATOM 1532 C CA    . TYR B 2 181 ? 24.65300  78.07800  19.84000 1.000 90.05025  ? 181 TYR A CA    1 
ATOM 1533 C C     . TYR B 2 181 ? 24.52300  76.97200  20.87400 1.000 94.94335  ? 181 TYR A C     1 
ATOM 1534 O O     . TYR B 2 181 ? 25.43100  76.80500  21.71100 1.000 99.21211  ? 181 TYR A O     1 
ATOM 1535 C CB    . TYR B 2 181 ? 23.80000  79.30600  20.15900 1.000 88.50255  ? 181 TYR A CB    1 
ATOM 1536 C CG    . TYR B 2 181 ? 24.05700  80.48900  19.23700 1.000 105.37079 ? 181 TYR A CG    1 
ATOM 1537 C CD1   . TYR B 2 181 ? 25.32600  80.73700  18.73000 1.000 97.57230  ? 181 TYR A CD1   1 
ATOM 1538 C CD2   . TYR B 2 181 ? 23.03000  81.34400  18.86100 1.000 108.60926 ? 181 TYR A CD2   1 
ATOM 1539 C CE1   . TYR B 2 181 ? 25.56900  81.80900  17.88800 1.000 96.01874  ? 181 TYR A CE1   1 
ATOM 1540 C CE2   . TYR B 2 181 ? 23.25900  82.41800  18.01800 1.000 103.99633 ? 181 TYR A CE2   1 
ATOM 1541 C CZ    . TYR B 2 181 ? 24.53200  82.65100  17.53100 1.000 102.30745 ? 181 TYR A CZ    1 
ATOM 1542 O OH    . TYR B 2 181 ? 24.76600  83.70800  16.70000 1.000 112.79690 ? 181 TYR A OH    1 
ATOM 1543 N N     . TYR B 2 182 ? 23.42300  76.22300  20.81600 1.000 92.89200  ? 182 TYR A N     1 
ATOM 1544 C CA    . TYR B 2 182 ? 23.19700  75.12500  21.78900 1.000 90.79270  ? 182 TYR A CA    1 
ATOM 1545 C C     . TYR B 2 182 ? 24.30400  74.10100  21.66200 1.000 94.38467  ? 182 TYR A C     1 
ATOM 1546 O O     . TYR B 2 182 ? 24.84900  73.65600  22.69100 1.000 104.04382 ? 182 TYR A O     1 
ATOM 1547 C CB    . TYR B 2 182 ? 21.87000  74.43400  21.47800 1.000 90.36068  ? 182 TYR A CB    1 
ATOM 1548 C CG    . TYR B 2 182 ? 20.62500  75.05400  22.09300 1.000 90.27800  ? 182 TYR A CG    1 
ATOM 1549 C CD1   . TYR B 2 182 ? 20.68000  75.71200  23.31400 1.000 104.62977 ? 182 TYR A CD1   1 
ATOM 1550 C CD2   . TYR B 2 182 ? 19.39500  74.96600  21.45500 1.000 92.46938  ? 182 TYR A CD2   1 
ATOM 1551 C CE1   . TYR B 2 182 ? 19.54700  76.27300  23.87900 1.000 118.83799 ? 182 TYR A CE1   1 
ATOM 1552 C CE2   . TYR B 2 182 ? 18.25600  75.52200  22.00900 1.000 125.86934 ? 182 TYR A CE2   1 
ATOM 1553 C CZ    . TYR B 2 182 ? 18.33300  76.17700  23.22500 1.000 138.95926 ? 182 TYR A CZ    1 
ATOM 1554 O OH    . TYR B 2 182 ? 17.21200  76.72300  23.77600 1.000 142.14564 ? 182 TYR A OH    1 
ATOM 1555 N N     . LEU B 2 183 ? 24.65600  73.74500  20.42800 1.000 97.47263  ? 183 LEU A N     1 
ATOM 1556 C CA    . LEU B 2 183 ? 25.64900  72.66300  20.21400 1.000 102.81900 ? 183 LEU A CA    1 
ATOM 1557 C C     . LEU B 2 183 ? 26.95500  72.96700  20.95300 1.000 108.16176 ? 183 LEU A C     1 
ATOM 1558 O O     . LEU B 2 183 ? 27.57700  72.01300  21.46200 1.000 123.70611 ? 183 LEU A O     1 
ATOM 1559 C CB    . LEU B 2 183 ? 25.87700  72.51000  18.71500 1.000 107.60270 ? 183 LEU A CB    1 
ATOM 1560 C CG    . LEU B 2 183 ? 24.90000  71.56900  18.01000 1.000 149.34019 ? 183 LEU A CG    1 
ATOM 1561 C CD1   . LEU B 2 183 ? 24.60100  72.05800  16.61200 1.000 136.01075 ? 183 LEU A CD1   1 
ATOM 1562 C CD2   . LEU B 2 183 ? 25.45900  70.15900  17.99500 1.000 158.91390 ? 183 LEU A CD2   1 
ATOM 1563 N N     . SER B 2 184 ? 27.34300  74.23800  21.03000 1.000 103.00308 ? 184 SER A N     1 
ATOM 1564 C CA    . SER B 2 184 ? 28.65200  74.58300  21.64300 1.000 104.28442 ? 184 SER A CA    1 
ATOM 1565 C C     . SER B 2 184 ? 28.81200  73.88900  23.00100 1.000 125.48317 ? 184 SER A C     1 
ATOM 1566 O O     . SER B 2 184 ? 29.97100  73.67200  23.40800 1.000 150.04373 ? 184 SER A O     1 
ATOM 1567 C CB    . SER B 2 184 ? 28.80200  76.07000  21.78200 1.000 121.60662 ? 184 SER A CB    1 
ATOM 1568 O OG    . SER B 2 184 ? 27.83000  76.58900  22.68000 1.000 142.50375 ? 184 SER A OG    1 
ATOM 1569 N N     . LYS B 2 185 ? 27.70800  73.55700  23.67600 1.000 113.50220 ? 185 LYS A N     1 
ATOM 1570 C CA    . LYS B 2 185 ? 27.80600  72.97900  25.04200 1.000 114.50257 ? 185 LYS A CA    1 
ATOM 1571 C C     . LYS B 2 185 ? 27.36800  71.50700  25.05700 1.000 113.59081 ? 185 LYS A C     1 
ATOM 1572 O O     . LYS B 2 185 ? 26.90100  71.05900  26.12200 1.000 138.49748 ? 185 LYS A O     1 
ATOM 1573 C CB    . LYS B 2 185 ? 26.90600  73.77600  25.99100 1.000 126.85690 ? 185 LYS A CB    1 
ATOM 1574 C CG    . LYS B 2 185 ? 27.13900  75.27800  26.02000 1.000 121.03770 ? 185 LYS A CG    1 
ATOM 1575 C CD    . LYS B 2 185 ? 26.20700  75.99000  26.99100 1.000 129.06951 ? 185 LYS A CD    1 
ATOM 1576 C CE    . LYS B 2 185 ? 26.46300  77.46200  27.06200 1.000 136.64994 ? 185 LYS A CE    1 
ATOM 1577 N NZ    . LYS B 2 185 ? 25.58000  78.12100  28.02800 1.000 132.12975 ? 185 LYS A NZ    1 
ATOM 1578 N N     . GLN B 2 186 ? 27.51000  70.78400  23.94300 1.000 111.05993 ? 186 GLN A N     1 
ATOM 1579 C CA    . GLN B 2 186 ? 27.00800  69.38400  23.88500 1.000 143.98868 ? 186 GLN A CA    1 
ATOM 1580 C C     . GLN B 2 186 ? 28.10700  68.39200  24.28500 1.000 158.20746 ? 186 GLN A C     1 
ATOM 1581 O O     . GLN B 2 186 ? 27.84400  67.51900  25.18300 1.000 157.94713 ? 186 GLN A O     1 
ATOM 1582 C CB    . GLN B 2 186 ? 26.54600  69.06800  22.46700 1.000 124.10346 ? 186 GLN A CB    1 
ATOM 1583 C CG    . GLN B 2 186 ? 25.07100  69.36700  22.23400 1.000 116.95782 ? 186 GLN A CG    1 
ATOM 1584 C CD    . GLN B 2 186 ? 24.40000  68.33100  21.36500 1.000 135.95819 ? 186 GLN A CD    1 
ATOM 1585 O OE1   . GLN B 2 186 ? 25.04300  67.43100  20.81400 1.000 162.03745 ? 186 GLN A OE1   1 
ATOM 1586 N NE2   . GLN B 2 186 ? 23.08900  68.45200  21.23500 1.000 127.15278 ? 186 GLN A NE2   1 
ATOM 1587 N N     . LEU B 2 187 ? 29.26900  68.49900  23.63400 1.000 142.06002 ? 187 LEU A N     1 
ATOM 1588 C CA    . LEU B 2 187 ? 30.41100  67.59500  23.92500 1.000 151.98826 ? 187 LEU A CA    1 
ATOM 1589 C C     . LEU B 2 187 ? 31.59000  68.04500  23.05300 1.000 147.89331 ? 187 LEU A C     1 
ATOM 1590 O O     . LEU B 2 187 ? 31.44700  69.06800  22.34900 1.000 156.98579 ? 187 LEU A O     1 
ATOM 1591 C CB    . LEU B 2 187 ? 30.03600  66.14100  23.64400 1.000 155.87687 ? 187 LEU A CB    1 
ATOM 1592 C CG    . LEU B 2 187 ? 30.88300  65.08000  24.35300 1.000 159.29724 ? 187 LEU A CG    1 
ATOM 1593 C CD1   . LEU B 2 187 ? 31.27900  65.54300  25.74400 1.000 155.88680 ? 187 LEU A CD1   1 
ATOM 1594 C CD2   . LEU B 2 187 ? 30.16200  63.74700  24.41600 1.000 154.62844 ? 187 LEU A CD2   1 
ATOM 1595 N N     . LYS B 2 188 ? 32.70000  67.30800  23.08800 1.000 158.90568 ? 188 LYS A N     1 
ATOM 1596 C CA    . LYS B 2 188 ? 33.84900  67.63900  22.20800 1.000 177.24082 ? 188 LYS A CA    1 
ATOM 1597 C C     . LYS B 2 188 ? 33.38700  67.50900  20.75000 1.000 168.18696 ? 188 LYS A C     1 
ATOM 1598 O O     . LYS B 2 188 ? 34.00600  68.15000  19.87300 1.000 164.49593 ? 188 LYS A O     1 
ATOM 1599 C CB    . LYS B 2 188 ? 35.02200  66.69600  22.49100 1.000 174.61528 ? 188 LYS A CB    1 
ATOM 1600 C CG    . LYS B 2 188 ? 34.89400  65.31200  21.86600 1.000 161.53835 ? 188 LYS A CG    1 
ATOM 1601 C CD    . LYS B 2 188 ? 35.77800  64.25300  22.51100 1.000 147.62588 ? 188 LYS A CD    1 
ATOM 1602 C CE    . LYS B 2 188 ? 35.26000  63.83700  23.85000 1.000 155.76724 ? 188 LYS A CE    1 
ATOM 1603 N NZ    . LYS B 2 188 ? 33.91400  63.26700  23.74500 1.000 154.99217 ? 188 LYS A NZ    1 
ATOM 1604 N N     . TYR B 2 189 ? 32.31000  66.75200  20.52200 1.000 152.20451 ? 189 TYR A N     1 
ATOM 1605 C CA    . TYR B 2 189 ? 31.82200  66.51000  19.13700 1.000 153.62712 ? 189 TYR A CA    1 
ATOM 1606 C C     . TYR B 2 189 ? 31.55700  67.85200  18.46300 1.000 153.74213 ? 189 TYR A C     1 
ATOM 1607 O O     . TYR B 2 189 ? 30.70100  68.61800  18.95100 1.000 150.79837 ? 189 TYR A O     1 
ATOM 1608 C CB    . TYR B 2 189 ? 30.62400  65.56100  19.22800 1.000 145.52663 ? 189 TYR A CB    1 
ATOM 1609 C CG    . TYR B 2 189 ? 30.96900  64.25900  19.93800 1.000 155.86251 ? 189 TYR A CG    1 
ATOM 1610 C CD1   . TYR B 2 189 ? 32.25700  63.74000  19.89600 1.000 142.03833 ? 189 TYR A CD1   1 
ATOM 1611 C CD2   . TYR B 2 189 ? 30.01300  63.55500  20.65700 1.000 158.85215 ? 189 TYR A CD2   1 
ATOM 1612 C CE1   . TYR B 2 189 ? 32.58300  62.56300  20.54800 1.000 146.65090 ? 189 TYR A CE1   1 
ATOM 1613 C CE2   . TYR B 2 189 ? 30.32300  62.37200  21.30600 1.000 143.54220 ? 189 TYR A CE2   1 
ATOM 1614 C CZ    . TYR B 2 189 ? 31.61200  61.87700  21.25500 1.000 151.46364 ? 189 TYR A CZ    1 
ATOM 1615 O OH    . TYR B 2 189 ? 31.92000  60.71300  21.89500 1.000 160.28971 ? 189 TYR A OH    1 
ATOM 1616 N N     . ASP B 2 190 ? 32.26300  68.12200  17.36200 1.000 152.34546 ? 190 ASP A N     1 
ATOM 1617 C CA    . ASP B 2 190 ? 32.14300  69.43600  16.67400 1.000 151.74661 ? 190 ASP A CA    1 
ATOM 1618 C C     . ASP B 2 190 ? 30.96300  69.42500  15.70000 1.000 152.23905 ? 190 ASP A C     1 
ATOM 1619 O O     . ASP B 2 190 ? 31.19600  69.63800  14.49300 1.000 159.63434 ? 190 ASP A O     1 
ATOM 1620 C CB    . ASP B 2 190 ? 33.44300  69.78600  15.97100 1.000 151.17127 ? 190 ASP A CB    1 
ATOM 1621 C CG    . ASP B 2 190 ? 34.70000  69.57800  16.80300 1.000 162.68853 ? 190 ASP A CG    1 
ATOM 1622 O OD1   . ASP B 2 190 ? 34.82900  70.24900  17.84700 1.000 175.98552 ? 190 ASP A OD1   1 
ATOM 1623 O OD2   . ASP B 2 190 ? 35.53000  68.73300  16.40600 1.000 162.01739 ? 190 ASP A OD2   1 
ATOM 1624 N N     . LEU B 2 191 ? 29.74600  69.20300  16.19900 1.000 130.95279 ? 191 LEU A N     1 
ATOM 1625 C CA    . LEU B 2 191 ? 28.55100  69.27200  15.32000 1.000 131.57371 ? 191 LEU A CA    1 
ATOM 1626 C C     . LEU B 2 191 ? 28.15500  70.74400  15.15400 1.000 136.14491 ? 191 LEU A C     1 
ATOM 1627 O O     . LEU B 2 191 ? 27.38100  71.05200  14.22300 1.000 136.69167 ? 191 LEU A O     1 
ATOM 1628 C CB    . LEU B 2 191 ? 27.41800  68.44100  15.91400 1.000 138.88891 ? 191 LEU A CB    1 
ATOM 1629 C CG    . LEU B 2 191 ? 27.48400  66.93800  15.63500 1.000 152.79126 ? 191 LEU A CG    1 
ATOM 1630 C CD1   . LEU B 2 191 ? 26.52800  66.18200  16.53900 1.000 146.43141 ? 191 LEU A CD1   1 
ATOM 1631 C CD2   . LEU B 2 191 ? 27.13000  66.71800  14.17700 1.000 146.46746 ? 191 LEU A CD2   1 
ATOM 1632 N N     . TYR B 2 192 ? 28.66700  71.61400  16.02600 1.000 140.71862 ? 192 TYR A N     1 
ATOM 1633 C CA    . TYR B 2 192 ? 28.39800  73.06800  15.88100 1.000 136.14681 ? 192 TYR A CA    1 
ATOM 1634 C C     . TYR B 2 192 ? 28.96100  73.50600  14.54300 1.000 135.26633 ? 192 TYR A C     1 
ATOM 1635 O O     . TYR B 2 192 ? 28.27800  74.22800  13.79100 1.000 134.47568 ? 192 TYR A O     1 
ATOM 1636 C CB    . TYR B 2 192 ? 29.03200  73.85100  17.03300 1.000 137.11757 ? 192 TYR A CB    1 
ATOM 1637 C CG    . TYR B 2 192 ? 30.44601  73.42919  17.40839 1.000 142.32828 ? 192 TYR A CG    1 
ATOM 1638 C CD1   . TYR B 2 192 ? 30.70326  72.77188  18.60494 1.000 154.90094 ? 192 TYR A CD1   1 
ATOM 1639 C CD2   . TYR B 2 192 ? 31.52484  73.70551  16.57821 1.000 139.09777 ? 192 TYR A CD2   1 
ATOM 1640 C CE1   . TYR B 2 192 ? 31.98601  72.39121  18.95953 1.000 167.12098 ? 192 TYR A CE1   1 
ATOM 1641 C CE2   . TYR B 2 192 ? 32.81319  73.33281  16.92225 1.000 150.19719 ? 192 TYR A CE2   1 
ATOM 1642 C CZ    . TYR B 2 192 ? 33.04467  72.67191  18.11539 1.000 175.92240 ? 192 TYR A CZ    1 
ATOM 1643 O OH    . TYR B 2 192 ? 34.30893  72.29553  18.46415 1.000 193.75980 ? 192 TYR A OH    1 
ATOM 1644 N N     . ASP B 2 193 ? 30.17600  73.04900  14.23700 1.000 133.61112 ? 193 ASP A N     1 
ATOM 1645 C CA    . ASP B 2 193 ? 30.81000  73.39700  12.93900 1.000 136.56407 ? 193 ASP A CA    1 
ATOM 1646 C C     . ASP B 2 193 ? 29.87300  72.95900  11.81400 1.000 132.61014 ? 193 ASP A C     1 
ATOM 1647 O O     . ASP B 2 193 ? 29.67100  73.74700  10.87200 1.000 139.36662 ? 193 ASP A O     1 
ATOM 1648 C CB    . ASP B 2 193 ? 32.18600  72.76900  12.81200 1.000 155.55914 ? 193 ASP A CB    1 
ATOM 1649 C CG    . ASP B 2 193 ? 33.15600  73.08900  13.94100 1.000 163.94050 ? 193 ASP A CG    1 
ATOM 1650 O OD1   . ASP B 2 193 ? 32.75900  73.83700  14.85800 1.000 157.24331 ? 193 ASP A OD1   1 
ATOM 1651 O OD2   . ASP B 2 193 ? 34.29800  72.58800  13.89300 1.000 162.64714 ? 193 ASP A OD2   1 
ATOM 1652 N N     . ILE B 2 194 ? 29.31000  71.75500  11.92500 1.000 128.43649 ? 194 ILE A N     1 
ATOM 1653 C CA    . ILE B 2 194 ? 28.42400  71.22400  10.84700 1.000 135.49183 ? 194 ILE A CA    1 
ATOM 1654 C C     . ILE B 2 194 ? 27.24700  72.19200  10.67000 1.000 126.23760 ? 194 ILE A C     1 
ATOM 1655 O O     . ILE B 2 194 ? 26.96400  72.58200  9.51900  1.000 144.44006 ? 194 ILE A O     1 
ATOM 1656 C CB    . ILE B 2 194 ? 27.94300  69.80400  11.19100 1.000 134.42254 ? 194 ILE A CB    1 
ATOM 1657 C CG1   . ILE B 2 194 ? 29.11800  68.88800  11.51100 1.000 136.34575 ? 194 ILE A CG1   1 
ATOM 1658 C CG2   . ILE B 2 194 ? 27.06800  69.23500  10.07400 1.000 133.74058 ? 194 ILE A CG2   1 
ATOM 1659 C CD1   . ILE B 2 194 ? 30.17600  68.84200  10.42500 1.000 143.75870 ? 194 ILE A CD1   1 
ATOM 1660 N N     . PHE B 2 195 ? 26.61200  72.57800  11.77400 1.000 118.27110 ? 195 PHE A N     1 
ATOM 1661 C CA    . PHE B 2 195 ? 25.44800  73.49900  11.69800 1.000 122.55324 ? 195 PHE A CA    1 
ATOM 1662 C C     . PHE B 2 195 ? 25.91300  74.83700  11.13500 1.000 131.74711 ? 195 PHE A C     1 
ATOM 1663 O O     . PHE B 2 195 ? 25.18200  75.44600  10.33000 1.000 133.94206 ? 195 PHE A O     1 
ATOM 1664 C CB    . PHE B 2 195 ? 24.82100  73.58800  13.09100 1.000 122.91111 ? 195 PHE A CB    1 
ATOM 1665 C CG    . PHE B 2 195 ? 23.66200  72.62200  13.28900 1.000 129.02831 ? 195 PHE A CG    1 
ATOM 1666 C CD1   . PHE B 2 195 ? 23.89100  71.27200  13.52700 1.000 134.27334 ? 195 PHE A CD1   1 
ATOM 1667 C CD2   . PHE B 2 195 ? 22.34700  73.06900  13.24900 1.000 137.09590 ? 195 PHE A CD2   1 
ATOM 1668 C CE1   . PHE B 2 195 ? 22.83500  70.39600  13.71100 1.000 119.05022 ? 195 PHE A CE1   1 
ATOM 1669 C CE2   . PHE B 2 195 ? 21.29500  72.18700  13.43000 1.000 136.93249 ? 195 PHE A CE2   1 
ATOM 1670 C CZ    . PHE B 2 195 ? 21.54000  70.85500  13.66300 1.000 125.78967 ? 195 PHE A CZ    1 
ATOM 1671 N N     . PHE B 2 196 ? 27.10600  75.27800  11.53500 1.000 126.77441 ? 196 PHE A N     1 
ATOM 1672 C CA    . PHE B 2 196 ? 27.64600  76.57400  11.04400 1.000 119.53433 ? 196 PHE A CA    1 
ATOM 1673 C C     . PHE B 2 196 ? 27.78100  76.51000  9.52800  1.000 123.38508 ? 196 PHE A C     1 
ATOM 1674 O O     . PHE B 2 196 ? 27.38000  77.46700  8.83600  1.000 124.58088 ? 196 PHE A O     1 
ATOM 1675 C CB    . PHE B 2 196 ? 28.97800  76.86400  11.74000 1.000 118.84918 ? 196 PHE A CB    1 
ATOM 1676 C CG    . PHE B 2 196 ? 29.70200  78.10700  11.24500 1.000 119.98676 ? 196 PHE A CG    1 
ATOM 1677 C CD1   . PHE B 2 196 ? 29.34000  79.36900  11.69900 1.000 113.93374 ? 196 PHE A CD1   1 
ATOM 1678 C CD2   . PHE B 2 196 ? 30.76300  78.00800  10.35300 1.000 118.50573 ? 196 PHE A CD2   1 
ATOM 1679 C CE1   . PHE B 2 196 ? 30.00300  80.50000  11.25200 1.000 124.37303 ? 196 PHE A CE1   1 
ATOM 1680 C CE2   . PHE B 2 196 ? 31.42600  79.14200  9.91400  1.000 120.86471 ? 196 PHE A CE2   1 
ATOM 1681 C CZ    . PHE B 2 196 ? 31.04500  80.38400  10.36200 1.000 120.42125 ? 196 PHE A CZ    1 
ATOM 1682 N N     . GLU B 2 197 ? 28.32500  75.40300  9.02000  1.000 127.85840 ? 197 GLU A N     1 
ATOM 1683 C CA    . GLU B 2 197 ? 28.48200  75.24300  7.55300  1.000 133.94987 ? 197 GLU A CA    1 
ATOM 1684 C C     . GLU B 2 197 ? 27.10100  75.37500  6.90400  1.000 131.44189 ? 197 GLU A C     1 
ATOM 1685 O O     . GLU B 2 197 ? 26.97700  76.11900  5.91100  1.000 138.93518 ? 197 GLU A O     1 
ATOM 1686 C CB    . GLU B 2 197 ? 29.06800  73.87800  7.20300  1.000 139.21736 ? 197 GLU A CB    1 
ATOM 1687 C CG    . GLU B 2 197 ? 30.41200  73.59900  7.86700  1.000 154.62347 ? 197 GLU A CG    1 
ATOM 1688 C CD    . GLU B 2 197 ? 30.73500  72.11800  7.94000  1.000 166.57618 ? 197 GLU A CD    1 
ATOM 1689 O OE1   . GLU B 2 197 ? 29.91200  71.31000  7.46000  1.000 157.17458 ? 197 GLU A OE1   1 
ATOM 1690 O OE2   . GLU B 2 197 ? 31.80300  71.77100  8.48300  1.000 177.14853 ? 197 GLU A OE2   1 
ATOM 1691 N N     . MET B 2 198 ? 26.10600  74.68000  7.45800  1.000 127.94893 ? 198 MET A N     1 
ATOM 1692 C CA    . MET B 2 198 ? 24.73500  74.73500  6.89400  1.000 124.01010 ? 198 MET A CA    1 
ATOM 1693 C C     . MET B 2 198 ? 24.24900  76.18900  6.94600  1.000 128.98394 ? 198 MET A C     1 
ATOM 1694 O O     . MET B 2 198 ? 23.58400  76.62600  5.98700  1.000 137.32550 ? 198 MET A O     1 
ATOM 1695 C CB    . MET B 2 198 ? 23.77600  73.83300  7.67900  1.000 122.94625 ? 198 MET A CB    1 
ATOM 1696 C CG    . MET B 2 198 ? 24.23300  72.39000  7.78200  1.000 128.40701 ? 198 MET A CG    1 
ATOM 1697 S SD    . MET B 2 198 ? 22.95300  71.28000  8.40200  1.000 104.62642 ? 198 MET A SD    1 
ATOM 1698 C CE    . MET B 2 198 ? 22.36300  72.22700  9.81100  1.000 121.69394 ? 198 MET A CE    1 
ATOM 1699 N N     . VAL B 2 199 ? 24.58200  76.90500  8.02100  1.000 130.29716 ? 199 VAL A N     1 
ATOM 1700 C CA    . VAL B 2 199 ? 24.15600  78.32900  8.16200  1.000 128.90627 ? 199 VAL A CA    1 
ATOM 1701 C C     . VAL B 2 199 ? 24.74700  79.12400  6.98800  1.000 125.85811 ? 199 VAL A C     1 
ATOM 1702 O O     . VAL B 2 199 ? 24.00100  79.91300  6.37000  1.000 122.52814 ? 199 VAL A O     1 
ATOM 1703 C CB    . VAL B 2 199 ? 24.59100  78.92100  9.51500  1.000 118.08888 ? 199 VAL A CB    1 
ATOM 1704 C CG1   . VAL B 2 199 ? 24.46600  80.43900  9.53900  1.000 125.46172 ? 199 VAL A CG1   1 
ATOM 1705 C CG2   . VAL B 2 199 ? 23.82900  78.30000  10.68000 1.000 111.58704 ? 199 VAL A CG2   1 
ATOM 1706 N N     . ARG B 2 200 ? 26.03100  78.91100  6.69200  1.000 131.07783 ? 200 ARG A N     1 
ATOM 1707 C CA    . ARG B 2 200 ? 26.69100  79.64100  5.58200  1.000 129.78295 ? 200 ARG A CA    1 
ATOM 1708 C C     . ARG B 2 200 ? 26.02900  79.25500  4.25400  1.000 131.33168 ? 200 ARG A C     1 
ATOM 1709 O O     . ARG B 2 200 ? 25.63000  80.16900  3.50200  1.000 141.57956 ? 200 ARG A O     1 
ATOM 1710 C CB    . ARG B 2 200 ? 28.17600  79.28000  5.50600  1.000 136.66880 ? 200 ARG A CB    1 
ATOM 1711 C CG    . ARG B 2 200 ? 28.98800  79.52200  6.76800  1.000 130.16227 ? 200 ARG A CG    1 
ATOM 1712 C CD    . ARG B 2 200 ? 30.06700  78.45900  6.85700  1.000 147.52505 ? 200 ARG A CD    1 
ATOM 1713 N NE    . ARG B 2 200 ? 30.73800  78.25100  5.57000  1.000 166.45238 ? 200 ARG A NE    1 
ATOM 1714 C CZ    . ARG B 2 200 ? 31.67400  77.33800  5.35100  1.000 167.98013 ? 200 ARG A CZ    1 
ATOM 1715 N NH1   . ARG B 2 200 ? 32.00500  76.48900  6.30700  1.000 155.34748 ? 200 ARG A NH1   1 
ATOM 1716 N NH2   . ARG B 2 200 ? 32.26800  77.27100  4.17300  1.000 158.79427 ? 200 ARG A NH2   1 
ATOM 1717 N N     . GLN B 2 201 ? 25.91400  77.95300  3.98400  1.000 128.50707 ? 201 GLN A N     1 
ATOM 1718 C CA    . GLN B 2 201 ? 25.33900  77.48700  2.69600  1.000 130.36484 ? 201 GLN A CA    1 
ATOM 1719 C C     . GLN B 2 201 ? 23.83400  77.26200  2.87400  1.000 128.38186 ? 201 GLN A C     1 
ATOM 1720 O O     . GLN B 2 201 ? 23.35200  76.17400  2.49900  1.000 140.91736 ? 201 GLN A O     1 
ATOM 1721 C CB    . GLN B 2 201 ? 26.03200  76.19800  2.26100  1.000 132.26778 ? 201 GLN A CB    1 
ATOM 1722 C CG    . GLN B 2 201 ? 27.55100  76.30400  2.18700  1.000 140.04538 ? 201 GLN A CG    1 
ATOM 1723 C CD    . GLN B 2 201 ? 28.04400  77.10500  1.00100  1.000 167.22801 ? 201 GLN A CD    1 
ATOM 1724 O OE1   . GLN B 2 201 ? 27.26400  77.56200  0.15800  1.000 173.95310 ? 201 GLN A OE1   1 
ATOM 1725 N NE2   . GLN B 2 201 ? 29.35600  77.27300  0.91800  1.000 163.17720 ? 201 GLN A NE2   1 
ATOM 1726 N N     . TYR B 2 202 ? 23.12600  78.25000  3.42000  1.000 129.42992 ? 202 TYR A N     1 
ATOM 1727 C CA    . TYR B 2 202 ? 21.67800  78.06000  3.70200  1.000 135.26348 ? 202 TYR A CA    1 
ATOM 1728 C C     . TYR B 2 202 ? 20.85900  78.59000  2.54000  1.000 134.27943 ? 202 TYR A C     1 
ATOM 1729 O O     . TYR B 2 202 ? 21.21400  79.64100  1.96800  1.000 132.98669 ? 202 TYR A O     1 
ATOM 1730 C CB    . TYR B 2 202 ? 21.26700  78.74700  5.00800  1.000 129.01866 ? 202 TYR A CB    1 
ATOM 1731 C CG    . TYR B 2 202 ? 19.77600  78.66600  5.30400  1.000 125.04075 ? 202 TYR A CG    1 
ATOM 1732 C CD1   . TYR B 2 202 ? 19.23000  77.55600  5.93500  1.000 123.84102 ? 202 TYR A CD1   1 
ATOM 1733 C CD2   . TYR B 2 202 ? 18.91800  79.70200  4.95800  1.000 121.71424 ? 202 TYR A CD2   1 
ATOM 1734 C CE1   . TYR B 2 202 ? 17.87500  77.47300  6.20400  1.000 124.20362 ? 202 TYR A CE1   1 
ATOM 1735 C CE2   . TYR B 2 202 ? 17.56100  79.63200  5.22300  1.000 127.17829 ? 202 TYR A CE2   1 
ATOM 1736 C CZ    . TYR B 2 202 ? 17.03800  78.51500  5.84800  1.000 128.70322 ? 202 TYR A CZ    1 
ATOM 1737 O OH    . TYR B 2 202 ? 15.70100  78.44400  6.11100  1.000 117.74550 ? 202 TYR A OH    1 
ATOM 1738 N N     . ASP B 2 203 ? 19.78100  77.88100  2.19900  1.000 142.73682 ? 203 ASP A N     1 
ATOM 1739 C CA    . ASP B 2 203 ? 18.89700  78.34900  1.14100  1.000 140.13752 ? 203 ASP A CA    1 
ATOM 1740 C C     . ASP B 2 203 ? 17.55500  78.72400  1.75300  1.000 133.63873 ? 203 ASP A C     1 
ATOM 1741 O O     . ASP B 2 203 ? 16.93500  77.90800  2.44300  1.000 148.05913 ? 203 ASP A O     1 
ATOM 1742 C CB    . ASP B 2 203 ? 18.72100  77.27000  0.07200  1.000 154.41301 ? 203 ASP A CB    1 
ATOM 1743 C CG    . ASP B 2 203 ? 20.04300  76.66700  -0.36400 1.000 159.52173 ? 203 ASP A CG    1 
ATOM 1744 O OD1   . ASP B 2 203 ? 20.80400  77.35000  -1.08100 1.000 148.52601 ? 203 ASP A OD1   1 
ATOM 1745 O OD2   . ASP B 2 203 ? 20.32900  75.51700  0.03100  1.000 172.83686 ? 203 ASP A OD2   1 
ATOM 1746 N N     . ALA B 2 204 ? 17.10700  79.95000  1.49600  1.000 137.68879 ? 204 ALA A N     1 
ATOM 1747 C CA    . ALA B 2 204 ? 15.96700  80.53200  2.19200  1.000 153.22528 ? 204 ALA A CA    1 
ATOM 1748 C C     . ALA B 2 204 ? 14.66900  80.31600  1.42300  1.000 155.59925 ? 204 ALA A C     1 
ATOM 1749 O O     . ALA B 2 204 ? 14.62400  80.46700  0.19900  1.000 163.82674 ? 204 ALA A O     1 
ATOM 1750 C CB    . ALA B 2 204 ? 16.18700  82.02900  2.42100  1.000 151.79008 ? 204 ALA A CB    1 
ATOM 1751 N N     . LYS B 2 205 ? 13.61400  79.96900  2.15800  1.000 145.95924 ? 205 LYS A N     1 
ATOM 1752 C CA    . LYS B 2 205 ? 12.26500  79.85400  1.62000  1.000 141.37590 ? 205 LYS A CA    1 
ATOM 1753 C C     . LYS B 2 205 ? 11.28300  79.83100  2.78500  1.000 165.53338 ? 205 LYS A C     1 
ATOM 1754 O O     . LYS B 2 205 ? 11.65500  79.46500  3.90700  1.000 169.98775 ? 205 LYS A O     1 
ATOM 1755 C CB    . LYS B 2 205 ? 12.10800  78.59100  0.75600  1.000 142.65790 ? 205 LYS A CB    1 
ATOM 1756 C CG    . LYS B 2 205 ? 11.81900  78.89200  -0.70500 1.000 152.16514 ? 205 LYS A CG    1 
ATOM 1757 C CD    . LYS B 2 205 ? 11.18800  77.70700  -1.41700 1.000 156.34822 ? 205 LYS A CD    1 
ATOM 1758 C CE    . LYS B 2 205 ? 10.81400  78.07600  -2.84500 1.000 174.98530 ? 205 LYS A CE    1 
ATOM 1759 N NZ    . LYS B 2 205 ? 10.12200  76.96900  -3.55800 1.000 164.52559 ? 205 LYS A NZ    1 
ATOM 1760 N N     . PRO B 2 206 ? 10.00000  80.24800  2.62500  1.000 176.30854 ? 206 PRO A N     1 
ATOM 1761 C CA    . PRO B 2 206 ? 9.03700   80.14000  3.71600  1.000 165.47286 ? 206 PRO A CA    1 
ATOM 1762 C C     . PRO B 2 206 ? 8.10200   78.93200  3.64200  1.000 153.17937 ? 206 PRO A C     1 
ATOM 1763 O O     . PRO B 2 206 ? 7.90500   78.38200  2.54000  1.000 160.10360 ? 206 PRO A O     1 
ATOM 1764 C CB    . PRO B 2 206 ? 8.28300   81.46500  3.53700  1.000 162.24790 ? 206 PRO A CB    1 
ATOM 1765 C CG    . PRO B 2 206 ? 8.20300   81.63600  2.03500  1.000 142.57005 ? 206 PRO A CG    1 
ATOM 1766 C CD    . PRO B 2 206 ? 9.41400   80.91600  1.45700  1.000 143.78405 ? 206 PRO A CD    1 
ATOM 1767 N N     . LEU B 2 207 ? 7.53700   78.52400  4.78500  1.000 147.17653 ? 207 LEU A N     1 
ATOM 1768 C CA    . LEU B 2 207 ? 6.57600   77.38600  4.81300  1.000 150.86235 ? 207 LEU A CA    1 
ATOM 1769 C C     . LEU B 2 207 ? 5.27700   77.84800  5.49100  1.000 145.97744 ? 207 LEU A C     1 
ATOM 1770 O O     . LEU B 2 207 ? 5.32000   78.87000  6.20700  1.000 159.93284 ? 207 LEU A O     1 
ATOM 1771 C CB    . LEU B 2 207 ? 7.16800   76.17400  5.52800  1.000 139.64714 ? 207 LEU A CB    1 
ATOM 1772 C CG    . LEU B 2 207 ? 8.44300   75.58500  4.91700  1.000 156.17611 ? 207 LEU A CG    1 
ATOM 1773 C CD1   . LEU B 2 207 ? 8.88600   74.35100  5.68300  1.000 142.28061 ? 207 LEU A CD1   1 
ATOM 1774 C CD2   . LEU B 2 207 ? 8.25200   75.25700  3.44600  1.000 140.91631 ? 207 LEU A CD2   1 
ATOM 1775 N N     . ASP B 2 208 ? 4.17300   77.12800  5.27400  1.000 137.26709 ? 208 ASP A N     1 
ATOM 1776 C CA    . ASP B 2 208 ? 2.86000   77.56700  5.82800  1.000 141.57143 ? 208 ASP A CA    1 
ATOM 1777 C C     . ASP B 2 208 ? 2.41500   76.62600  6.95100  1.000 147.27705 ? 208 ASP A C     1 
ATOM 1778 O O     . ASP B 2 208 ? 1.40500   76.93800  7.61700  1.000 145.72706 ? 208 ASP A O     1 
ATOM 1779 C CB    . ASP B 2 208 ? 1.80900   77.68300  4.73700  1.000 153.31567 ? 208 ASP A CB    1 
ATOM 1780 C CG    . ASP B 2 208 ? 2.05700   78.77200  3.70300  1.000 172.60985 ? 208 ASP A CG    1 
ATOM 1781 O OD1   . ASP B 2 208 ? 3.07600   79.48300  3.83300  1.000 174.79051 ? 208 ASP A OD1   1 
ATOM 1782 O OD2   . ASP B 2 208 ? 1.23000   78.90100  2.77700  1.000 166.58500 ? 208 ASP A OD2   1 
ATOM 1783 N N     . LYS B 2 209 ? 3.08800   75.48000  7.08700  1.000 152.22910 ? 209 LYS A N     1 
ATOM 1784 C CA    . LYS B 2 209 ? 2.75600   74.52400  8.17300  1.000 142.39300 ? 209 LYS A CA    1 
ATOM 1785 C C     . LYS B 2 209 ? 2.67800   75.31900  9.47600  1.000 129.38757 ? 209 LYS A C     1 
ATOM 1786 O O     . LYS B 2 209 ? 1.81200   75.00500  10.31700 1.000 129.08028 ? 209 LYS A O     1 
ATOM 1787 C CB    . LYS B 2 209 ? 3.82800   73.43800  8.31000  1.000 141.29662 ? 209 LYS A CB    1 
ATOM 1788 C CG    . LYS B 2 209 ? 4.08000   72.57400  7.08200  1.000 143.00677 ? 209 LYS A CG    1 
ATOM 1789 C CD    . LYS B 2 209 ? 4.91000   73.24000  5.99200  1.000 128.88265 ? 209 LYS A CD    1 
ATOM 1790 C CE    . LYS B 2 209 ? 5.02700   72.38200  4.77400  1.000 140.22654 ? 209 LYS A CE    1 
ATOM 1791 N NZ    . LYS B 2 209 ? 5.68400   73.09000  3.67300  1.000 141.61234 ? 209 LYS A NZ    1 
ATOM 1792 N N     . PHE B 2 210 ? 3.55700   76.31000  9.62100  1.000 139.63712 ? 210 PHE A N     1 
ATOM 1793 C CA    . PHE B 2 210 ? 3.56500   77.15700  10.83900 1.000 131.93130 ? 210 PHE A CA    1 
ATOM 1794 C C     . PHE B 2 210 ? 2.89700   78.47600  10.49300 1.000 148.96106 ? 210 PHE A C     1 
ATOM 1795 O O     . PHE B 2 210 ? 3.58100   79.38800  9.98500  1.000 153.18794 ? 210 PHE A O     1 
ATOM 1796 C CB    . PHE B 2 210 ? 5.02600   77.29000  11.27200 1.000 109.61750 ? 210 PHE A CB    1 
ATOM 1797 C CG    . PHE B 2 210 ? 5.82700   76.01600  11.04000 1.000 123.21656 ? 210 PHE A CG    1 
ATOM 1798 C CD1   . PHE B 2 210 ? 5.59400   74.87900  11.80100 1.000 143.78254 ? 210 PHE A CD1   1 
ATOM 1799 C CD2   . PHE B 2 210 ? 6.81200   75.96100  10.06100 1.000 113.17660 ? 210 PHE A CD2   1 
ATOM 1800 C CE1   . PHE B 2 210 ? 6.31600   73.71900  11.58000 1.000 146.03903 ? 210 PHE A CE1   1 
ATOM 1801 C CE2   . PHE B 2 210 ? 7.53600   74.79800  9.85000  1.000 108.37622 ? 210 PHE A CE2   1 
ATOM 1802 C CZ    . PHE B 2 210 ? 7.28900   73.68100  10.61000 1.000 115.73930 ? 210 PHE A CZ    1 
ATOM 1803 N N     . TYR B 2 211 ? 1.59000   78.57700  10.75300 1.000 165.78380 ? 211 TYR A N     1 
ATOM 1804 C CA    . TYR B 2 211 ? 0.83600   79.81800  10.42600 1.000 155.84427 ? 211 TYR A CA    1 
ATOM 1805 C C     . TYR B 2 211 ? 1.49400   80.97500  11.16300 1.000 160.90476 ? 211 TYR A C     1 
ATOM 1806 O O     . TYR B 2 211 ? 1.43600   82.12400  10.67400 1.000 164.77144 ? 211 TYR A O     1 
ATOM 1807 C CB    . TYR B 2 211 ? -0.64400  79.68300  10.80000 1.000 140.67194 ? 211 TYR A CB    1 
ATOM 1808 C CG    . TYR B 2 211 ? -1.04400  80.35100  12.10800 1.000 159.05142 ? 211 TYR A CG    1 
ATOM 1809 C CD1   . TYR B 2 211 ? -0.93200  79.68200  13.32100 1.000 167.71991 ? 211 TYR A CD1   1 
ATOM 1810 C CD2   . TYR B 2 211 ? -1.54700  81.64600  12.12800 1.000 156.55298 ? 211 TYR A CD2   1 
ATOM 1811 C CE1   . TYR B 2 211 ? -1.29600  80.28500  14.51300 1.000 169.75645 ? 211 TYR A CE1   1 
ATOM 1812 C CE2   . TYR B 2 211 ? -1.91300  82.26000  13.31300 1.000 165.63487 ? 211 TYR A CE2   1 
ATOM 1813 C CZ    . TYR B 2 211 ? -1.78800  81.57700  14.50900 1.000 173.24063 ? 211 TYR A CZ    1 
ATOM 1814 O OH    . TYR B 2 211 ? -2.15100  82.17800  15.68000 1.000 161.19036 ? 211 TYR A OH    1 
ATOM 1815 N N     . GLU B 2 212 ? 2.10600   80.68100  12.31400 1.000 141.79816 ? 212 GLU A N     1 
ATOM 1816 C CA    . GLU B 2 212 ? 2.80700   81.73300  13.09100 1.000 145.62038 ? 212 GLU A CA    1 
ATOM 1817 C C     . GLU B 2 212 ? 3.90100   81.07800  13.94600 1.000 127.57464 ? 212 GLU A C     1 
ATOM 1818 O O     . GLU B 2 212 ? 4.02300   79.83500  13.90100 1.000 126.77134 ? 212 GLU A O     1 
ATOM 1819 C CB    . GLU B 2 212 ? 1.78000   82.47900  13.94300 1.000 152.93357 ? 212 GLU A CB    1 
ATOM 1820 C CG    . GLU B 2 212 ? 2.23600   83.86700  14.38200 1.000 163.71543 ? 212 GLU A CG    1 
ATOM 1821 C CD    . GLU B 2 212 ? 1.19600   84.62000  15.19100 1.000 168.02337 ? 212 GLU A CD    1 
ATOM 1822 O OE1   . GLU B 2 212 ? 0.09300   84.85900  14.65600 1.000 171.96596 ? 212 GLU A OE1   1 
ATOM 1823 O OE2   . GLU B 2 212 ? 1.48800   84.96500  16.35500 1.000 154.84397 ? 212 GLU A OE2   1 
ATOM 1824 N N     . LYS B 2 213 ? 4.67700   81.88600  14.67100 1.000 117.72578 ? 213 LYS A N     1 
ATOM 1825 C CA    . LYS B 2 213 ? 5.71300   81.34300  15.58400 1.000 112.02506 ? 213 LYS A CA    1 
ATOM 1826 C C     . LYS B 2 213 ? 5.50100   81.98000  16.96500 1.000 115.79825 ? 213 LYS A C     1 
ATOM 1827 O O     . LYS B 2 213 ? 5.17000   83.18300  17.02100 1.000 123.34227 ? 213 LYS A O     1 
ATOM 1828 C CB    . LYS B 2 213 ? 7.11600   81.62500  15.03600 1.000 115.90978 ? 213 LYS A CB    1 
ATOM 1829 C CG    . LYS B 2 213 ? 7.44200   83.08900  14.78200 1.000 108.42270 ? 213 LYS A CG    1 
ATOM 1830 C CD    . LYS B 2 213 ? 8.77400   83.28100  14.06800 1.000 112.53120 ? 213 LYS A CD    1 
ATOM 1831 C CE    . LYS B 2 213 ? 9.94100   82.83800  14.88900 1.000 121.67394 ? 213 LYS A CE    1 
ATOM 1832 N NZ    . LYS B 2 213 ? 10.12800  83.70900  16.05100 1.000 132.95644 ? 213 LYS A NZ    1 
ATOM 1833 N N     . PHE B 2 214 ? 5.68000   81.20000  18.03400 1.000 112.99235 ? 214 PHE A N     1 
ATOM 1834 C CA    . PHE B 2 214 ? 5.51800   81.73900  19.41100 1.000 107.63236 ? 214 PHE A CA    1 
ATOM 1835 C C     . PHE B 2 214 ? 6.85300   82.31200  19.87700 1.000 115.69586 ? 214 PHE A C     1 
ATOM 1836 O O     . PHE B 2 214 ? 7.83800   81.55000  19.97300 1.000 126.18444 ? 214 PHE A O     1 
ATOM 1837 C CB    . PHE B 2 214 ? 5.02200   80.65500  20.37200 1.000 98.31763  ? 214 PHE A CB    1 
ATOM 1838 C CG    . PHE B 2 214 ? 4.85300   81.14200  21.80500 1.000 95.07887  ? 214 PHE A CG    1 
ATOM 1839 C CD1   . PHE B 2 214 ? 3.65200   81.69400  22.23100 1.000 96.65661  ? 214 PHE A CD1   1 
ATOM 1840 C CD2   . PHE B 2 214 ? 5.89600   81.04800  22.72000 1.000 125.73134 ? 214 PHE A CD2   1 
ATOM 1841 C CE1   . PHE B 2 214 ? 3.50000   82.14000  23.53400 1.000 95.28518  ? 214 PHE A CE1   1 
ATOM 1842 C CE2   . PHE B 2 214 ? 5.73700   81.49500  24.02100 1.000 129.76266 ? 214 PHE A CE2   1 
ATOM 1843 C CZ    . PHE B 2 214 ? 4.54100   82.03800  24.42600 1.000 127.93937 ? 214 PHE A CZ    1 
ATOM 1844 N N     . GLU B 2 215 ? 6.88600   83.61700  20.16300 1.000 110.18851 ? 215 GLU A N     1 
ATOM 1845 C CA    . GLU B 2 215 ? 8.14400   84.27200  20.60600 1.000 119.86323 ? 215 GLU A CA    1 
ATOM 1846 C C     . GLU B 2 215 ? 9.27300   83.84500  19.65600 1.000 132.28941 ? 215 GLU A C     1 
ATOM 1847 O O     . GLU B 2 215 ? 9.15900   84.12000  18.44100 1.000 137.37628 ? 215 GLU A O     1 
ATOM 1848 C CB    . GLU B 2 215 ? 8.47000   83.91200  22.05700 1.000 116.85202 ? 215 GLU A CB    1 
ATOM 1849 C CG    . GLU B 2 215 ? 7.39300   84.35300  23.04500 1.000 120.54344 ? 215 GLU A CG    1 
ATOM 1850 C CD    . GLU B 2 215 ? 7.32200   85.84400  23.32300 1.000 137.73738 ? 215 GLU A CD    1 
ATOM 1851 O OE1   . GLU B 2 215 ? 8.15700   86.60000  22.78500 1.000 132.45139 ? 215 GLU A OE1   1 
ATOM 1852 O OE2   . GLU B 2 215 ? 6.41900   86.24800  24.08400 1.000 149.45808 ? 215 GLU A OE2   1 
ATOM 1853 N N     . GLN B 2 216 ? 10.31300  83.19700  20.19000 1.000 115.23260 ? 216 GLN A N     1 
ATOM 1854 C CA    . GLN B 2 216 ? 11.42600  82.70600  19.33500 1.000 111.64805 ? 216 GLN A CA    1 
ATOM 1855 C C     . GLN B 2 216 ? 11.30600  81.18000  19.18900 1.000 127.16072 ? 216 GLN A C     1 
ATOM 1856 O O     . GLN B 2 216 ? 12.34100  80.48900  19.30300 1.000 135.39318 ? 216 GLN A O     1 
ATOM 1857 C CB    . GLN B 2 216 ? 12.77400  83.13700  19.91500 1.000 136.10668 ? 216 GLN A CB    1 
ATOM 1858 C CG    . GLN B 2 216 ? 13.91800  83.11100  18.90600 1.000 146.51496 ? 216 GLN A CG    1 
ATOM 1859 C CD    . GLN B 2 216 ? 13.58500  83.81300  17.60800 1.000 150.29503 ? 216 GLN A CD    1 
ATOM 1860 O OE1   . GLN B 2 216 ? 13.59800  83.21300  16.52700 1.000 147.78149 ? 216 GLN A OE1   1 
ATOM 1861 N NE2   . GLN B 2 216 ? 13.28000  85.09900  17.70200 1.000 135.35901 ? 216 GLN A NE2   1 
ATOM 1862 N N     . ILE B 2 217 ? 10.08800  80.67500  18.96900 1.000 135.31801 ? 217 ILE A N     1 
ATOM 1863 C CA    . ILE B 2 217 ? 9.89900   79.21200  18.73500 1.000 122.21256 ? 217 ILE A CA    1 
ATOM 1864 C C     . ILE B 2 217 ? 8.99000   79.05800  17.51100 1.000 101.18094 ? 217 ILE A C     1 
ATOM 1865 O O     . ILE B 2 217 ? 8.01500   79.82500  17.41100 1.000 108.38859 ? 217 ILE A O     1 
ATOM 1866 C CB    . ILE B 2 217 ? 9.28200   78.53200  19.96900 1.000 103.64646 ? 217 ILE A CB    1 
ATOM 1867 C CG1   . ILE B 2 217 ? 9.99000   78.93800  21.25800 1.000 100.62483 ? 217 ILE A CG1   1 
ATOM 1868 C CG2   . ILE B 2 217 ? 9.25100   77.01300  19.79800 1.000 99.67491  ? 217 ILE A CG2   1 
ATOM 1869 C CD1   . ILE B 2 217 ? 9.35900   78.35300  22.50500 1.000 124.99405 ? 217 ILE A CD1   1 
ATOM 1870 N N     . ILE B 2 218 ? 9.28800   78.09900  16.63300 1.000 102.16997 ? 218 ILE A N     1 
ATOM 1871 C CA    . ILE B 2 218 ? 8.37800   77.86700  15.46900 1.000 112.06449 ? 218 ILE A CA    1 
ATOM 1872 C C     . ILE B 2 218 ? 7.63800   76.54600  15.73000 1.000 121.75877 ? 218 ILE A C     1 
ATOM 1873 O O     . ILE B 2 218 ? 8.24400   75.65800  16.36300 1.000 131.10322 ? 218 ILE A O     1 
ATOM 1874 C CB    . ILE B 2 218 ? 9.16100   77.83900  14.14400 1.000 129.45247 ? 218 ILE A CB    1 
ATOM 1875 C CG1   . ILE B 2 218 ? 9.98100   76.55900  13.99700 1.000 146.46381 ? 218 ILE A CG1   1 
ATOM 1876 C CG2   . ILE B 2 218 ? 10.02900  79.08900  13.99500 1.000 108.67637 ? 218 ILE A CG2   1 
ATOM 1877 C CD1   . ILE B 2 218 ? 10.29100  76.18900  12.55900 1.000 144.44361 ? 218 ILE A CD1   1 
ATOM 1878 N N     . TYR B 2 219 ? 6.38800   76.41400  15.27600 1.000 109.50526 ? 219 TYR A N     1 
ATOM 1879 C CA    . TYR B 2 219 ? 5.61200   75.19300  15.62600 1.000 106.60983 ? 219 TYR A CA    1 
ATOM 1880 C C     . TYR B 2 219 ? 4.69100   74.77500  14.48700 1.000 126.45766 ? 219 TYR A C     1 
ATOM 1881 O O     . TYR B 2 219 ? 4.13900   75.65300  13.79900 1.000 133.62767 ? 219 TYR A O     1 
ATOM 1882 C CB    . TYR B 2 219 ? 4.80400   75.49000  16.89100 1.000 108.00630 ? 219 TYR A CB    1 
ATOM 1883 C CG    . TYR B 2 219 ? 3.84000   76.66500  16.79300 1.000 103.51018 ? 219 TYR A CG    1 
ATOM 1884 C CD1   . TYR B 2 219 ? 2.52900   76.48600  16.36800 1.000 105.06084 ? 219 TYR A CD1   1 
ATOM 1885 C CD2   . TYR B 2 219 ? 4.23800   77.95000  17.13800 1.000 106.58314 ? 219 TYR A CD2   1 
ATOM 1886 C CE1   . TYR B 2 219 ? 1.64800   77.55100  16.27700 1.000 105.44719 ? 219 TYR A CE1   1 
ATOM 1887 C CE2   . TYR B 2 219 ? 3.36600   79.02200  17.05500 1.000 112.87525 ? 219 TYR A CE2   1 
ATOM 1888 C CZ    . TYR B 2 219 ? 2.06800   78.82200  16.62300 1.000 105.78332 ? 219 TYR A CZ    1 
ATOM 1889 O OH    . TYR B 2 219 ? 1.20900   79.87800  16.54000 1.000 131.16210 ? 219 TYR A OH    1 
ATOM 1890 N N     . ARG B 2 220 ? 4.50500   73.46300  14.30900 1.000 130.08506 ? 220 ARG A N     1 
ATOM 1891 C CA    . ARG B 2 220 ? 3.57300   72.95700  13.27000 1.000 112.20504 ? 220 ARG A CA    1 
ATOM 1892 C C     . ARG B 2 220 ? 2.13700   73.19200  13.74800 1.000 110.67627 ? 220 ARG A C     1 
ATOM 1893 O O     . ARG B 2 220 ? 1.69800   72.48000  14.67400 1.000 119.62564 ? 220 ARG A O     1 
ATOM 1894 C CB    . ARG B 2 220 ? 3.79300   71.46600  13.00000 1.000 122.27398 ? 220 ARG A CB    1 
ATOM 1895 C CG    . ARG B 2 220 ? 2.87200   70.89500  11.93200 1.000 142.17851 ? 220 ARG A CG    1 
ATOM 1896 C CD    . ARG B 2 220 ? 3.26100   69.46900  11.58100 1.000 140.18980 ? 220 ARG A CD    1 
ATOM 1897 N NE    . ARG B 2 220 ? 4.65200   69.39400  11.12400 1.000 155.86079 ? 220 ARG A NE    1 
ATOM 1898 C CZ    . ARG B 2 220 ? 5.26500   68.27900  10.75100 1.000 149.14753 ? 220 ARG A CZ    1 
ATOM 1899 N NH1   . ARG B 2 220 ? 4.59600   67.14000  10.71000 1.000 138.76353 ? 220 ARG A NH1   1 
ATOM 1900 N NH2   . ARG B 2 220 ? 6.54500   68.30700  10.42400 1.000 149.12220 ? 220 ARG A NH2   1 
ATOM 1901 N N     . LYS B 2 221 ? 1.44200   74.15500  13.14300 1.000 113.57785 ? 221 LYS A N     1 
ATOM 1902 C CA    . LYS B 2 221 ? 0.05700   74.48000  13.56400 1.000 121.90372 ? 221 LYS A CA    1 
ATOM 1903 C C     . LYS B 2 221 ? -0.74100  73.17300  13.66400 1.000 133.14413 ? 221 LYS A C     1 
ATOM 1904 O O     . LYS B 2 221 ? -0.71900  72.39100  12.69000 1.000 118.82576 ? 221 LYS A O     1 
ATOM 1905 C CB    . LYS B 2 221 ? -0.58400  75.43900  12.55800 1.000 126.24234 ? 221 LYS A CB    1 
ATOM 1906 C CG    . LYS B 2 221 ? -2.00600  75.87200  12.88400 1.000 140.51805 ? 221 LYS A CG    1 
ATOM 1907 C CD    . LYS B 2 221 ? -2.62200  76.73600  11.79100 1.000 142.06683 ? 221 LYS A CD    1 
ATOM 1908 C CE    . LYS B 2 221 ? -3.95300  77.29700  12.17900 1.000 140.10416 ? 221 LYS A CE    1 
ATOM 1909 N NZ    . LYS B 2 221 ? -4.47200  78.20400  11.15200 1.000 148.68166 ? 221 LYS A NZ    1 
ATOM 1910 N N     . GLN B 2 222 ? -1.41900  72.95300  14.79300 1.000 126.94729 ? 222 GLN A N     1 
ATOM 1911 C CA    . GLN B 2 222 ? -2.17100  71.68700  14.99600 1.000 124.21646 ? 222 GLN A CA    1 
ATOM 1912 C C     . GLN B 2 222 ? -3.34900  71.62800  14.01200 1.000 129.50461 ? 222 GLN A C     1 
ATOM 1913 O O     . GLN B 2 222 ? -4.18500  72.55600  14.03200 1.000 130.23990 ? 222 GLN A O     1 
ATOM 1914 C CB    . GLN B 2 222 ? -2.64300  71.57500  16.44500 1.000 126.55803 ? 222 GLN A CB    1 
ATOM 1915 C CG    . GLN B 2 222 ? -1.54400  71.17700  17.42400 1.000 123.83039 ? 222 GLN A CG    1 
ATOM 1916 C CD    . GLN B 2 222 ? -2.03000  71.06300  18.85200 1.000 117.50799 ? 222 GLN A CD    1 
ATOM 1917 O OE1   . GLN B 2 222 ? -2.48700  72.03900  19.45700 1.000 111.91248 ? 222 GLN A OE1   1 
ATOM 1918 N NE2   . GLN B 2 222 ? -1.92900  69.86500  19.40700 1.000 105.61106 ? 222 GLN A NE2   1 
ATOM 1919 N N     . VAL B 2 223 ? -3.40700  70.57400  13.19300 1.000 126.32940 ? 223 VAL A N     1 
ATOM 1920 C CA    . VAL B 2 223 ? -4.52600  70.40500  12.21700 1.000 121.66123 ? 223 VAL A CA    1 
ATOM 1921 C C     . VAL B 2 223 ? -5.80200  70.06400  13.00100 1.000 122.57952 ? 223 VAL A C     1 
ATOM 1922 O O     . VAL B 2 223 ? -5.79100  69.05000  13.72900 1.000 128.40701 ? 223 VAL A O     1 
ATOM 1923 C CB    . VAL B 2 223 ? -4.19300  69.30900  11.18900 1.000 114.88636 ? 223 VAL A CB    1 
ATOM 1924 C CG1   . VAL B 2 223 ? -5.34700  69.06600  10.22400 1.000 133.50521 ? 223 VAL A CG1   1 
ATOM 1925 C CG2   . VAL B 2 223 ? -2.91000  69.61900  10.42800 1.000 114.07272 ? 223 VAL A CG2   1 
ATOM 1926 N N     . ASP B 2 224 ? -6.85600  70.86900  12.84800 1.000 126.55340 ? 224 ASP A N     1 
ATOM 1927 C CA    . ASP B 2 224 ? -8.10300  70.65000  13.63300 1.000 124.10368 ? 224 ASP A CA    1 
ATOM 1928 C C     . ASP B 2 224 ? -8.86500  69.43900  13.08500 1.000 128.48307 ? 224 ASP A C     1 
ATOM 1929 O O     . ASP B 2 224 ? -8.33500  68.76100  12.17900 1.000 126.35097 ? 224 ASP A O     1 
ATOM 1930 C CB    . ASP B 2 224 ? -8.95500  71.90800  13.69100 1.000 124.16273 ? 224 ASP A CB    1 
ATOM 1931 C CG    . ASP B 2 224 ? -8.39600  73.02700  14.55700 1.000 138.45838 ? 224 ASP A CG    1 
ATOM 1932 O OD1   . ASP B 2 224 ? -7.30000  72.83600  15.12400 1.000 155.71680 ? 224 ASP A OD1   1 
ATOM 1933 O OD2   . ASP B 2 224 ? -9.06500  74.07600  14.66100 1.000 138.83916 ? 224 ASP A OD2   1 
ATOM 1934 N N     . PHE B 2 225 ? -10.06300 69.17800  13.61700 1.000 134.27130 ? 225 PHE A N     1 
ATOM 1935 C CA    . PHE B 2 225 ? -10.84500 67.98200  13.20100 1.000 131.51951 ? 225 PHE A CA    1 
ATOM 1936 C C     . PHE B 2 225 ? -12.14900 68.40900  12.54600 1.000 134.38635 ? 225 PHE A C     1 
ATOM 1937 O O     . PHE B 2 225 ? -12.62100 69.53700  12.80100 1.000 146.43849 ? 225 PHE A O     1 
ATOM 1938 C CB    . PHE B 2 225 ? -11.13800 67.12700  14.43500 1.000 132.78811 ? 225 PHE A CB    1 
ATOM 1939 C CG    . PHE B 2 225 ? -10.13300 66.01500  14.69900 1.000 136.21809 ? 225 PHE A CG    1 
ATOM 1940 C CD1   . PHE B 2 225 ? -9.48600  65.37500  13.64900 1.000 129.84827 ? 225 PHE A CD1   1 
ATOM 1941 C CD2   . PHE B 2 225 ? -9.83800  65.61500  15.99600 1.000 128.21667 ? 225 PHE A CD2   1 
ATOM 1942 C CE1   . PHE B 2 225 ? -8.57400  64.36200  13.89200 1.000 120.79774 ? 225 PHE A CE1   1 
ATOM 1943 C CE2   . PHE B 2 225 ? -8.92500  64.60100  16.23400 1.000 134.15105 ? 225 PHE A CE2   1 
ATOM 1944 C CZ    . PHE B 2 225 ? -8.29600  63.97700  15.18200 1.000 141.34373 ? 225 PHE A CZ    1 
ATOM 1945 N N     . LYS B 2 226 ? -12.72400 67.52800  11.72500 1.000 130.42543 ? 226 LYS A N     1 
ATOM 1946 C CA    . LYS B 2 226 ? -14.03200 67.82200  11.08600 1.000 143.61505 ? 226 LYS A CA    1 
ATOM 1947 C C     . LYS B 2 226 ? -15.09800 66.92200  11.73200 1.000 155.64615 ? 226 LYS A C     1 
ATOM 1948 O O     . LYS B 2 226 ? -14.80200 66.32800  12.79100 1.000 155.42052 ? 226 LYS A O     1 
ATOM 1949 C CB    . LYS B 2 226 ? -13.92600 67.60200  9.57300  1.000 143.32379 ? 226 LYS A CB    1 
ATOM 1950 C CG    . LYS B 2 226 ? -14.84100 68.47300  8.72400  1.000 150.43179 ? 226 LYS A CG    1 
ATOM 1951 C CD    . LYS B 2 226 ? -14.58600 69.96200  8.92100  1.000 148.62724 ? 226 LYS A CD    1 
ATOM 1952 C CE    . LYS B 2 226 ? -13.18200 70.35200  8.58400  1.000 144.98246 ? 226 LYS A CE    1 
ATOM 1953 N NZ    . LYS B 2 226 ? -12.84900 70.03600  7.19300  1.000 148.40590 ? 226 LYS A NZ    1 
ATOM 1954 N N     . LYS B 2 227 ? -16.28100 66.82100  11.11900 1.000 149.30810 ? 227 LYS A N     1 
ATOM 1955 C CA    . LYS B 2 227 ? -17.37200 65.97700  11.67500 1.000 154.92336 ? 227 LYS A CA    1 
ATOM 1956 C C     . LYS B 2 227 ? -17.86800 64.99400  10.60300 1.000 165.21141 ? 227 LYS A C     1 
ATOM 1957 O O     . LYS B 2 227 ? -19.02100 65.15200  10.14600 1.000 160.06700 ? 227 LYS A O     1 
ATOM 1958 C CB    . LYS B 2 227 ? -18.51100 66.87100  12.17200 1.000 148.84665 ? 227 LYS A CB    1 
ATOM 1959 C CG    . LYS B 2 227 ? -19.04600 67.84600  11.13600 1.000 145.22637 ? 227 LYS A CG    1 
ATOM 1960 C CD    . LYS B 2 227 ? -19.52900 69.15000  11.76000 1.000 148.97494 ? 227 LYS A CD    1 
ATOM 1961 C CE    . LYS B 2 227 ? -20.07700 70.09200  10.73800 1.000 153.84206 ? 227 LYS A CE    1 
ATOM 1962 N NZ    . LYS B 2 227 ? -19.19100 70.21100  9.57800  1.000 155.83207 ? 227 LYS A NZ    1 
ATOM 1963 N N     . PRO B 2 228 ? -17.07000 63.98300  10.19200 1.000 170.87468 ? 228 PRO A N     1 
ATOM 1964 C CA    . PRO B 2 228 ? -17.47100 63.07300  9.12900  1.000 175.09288 ? 228 PRO A CA    1 
ATOM 1965 C C     . PRO B 2 228 ? -18.26800 61.88600  9.64500  1.000 178.25075 ? 228 PRO A C     1 
ATOM 1966 O O     . PRO B 2 228 ? -17.65600 60.92000  10.14200 1.000 180.46197 ? 228 PRO A O     1 
ATOM 1967 C CB    . PRO B 2 228 ? -16.11700 62.64000  8.53200  1.000 168.57327 ? 228 PRO A CB    1 
ATOM 1968 C CG    . PRO B 2 228 ? -15.06700 63.28300  9.42200  1.000 156.82065 ? 228 PRO A CG    1 
ATOM 1969 C CD    . PRO B 2 228 ? -15.76000 63.67400  10.71400 1.000 160.44985 ? 228 PRO A CD    1 
ATOM 1970 N N     . THR B 2 229 ? -19.59800 61.95000  9.53100  1.000 169.92154 ? 229 THR A N     1 
ATOM 1971 C CA    . THR B 2 229 ? -20.45600 60.82300  9.96000  1.000 160.43635 ? 229 THR A CA    1 
ATOM 1972 C C     . THR B 2 229 ? -21.66100 60.74100  9.04900  1.000 175.62602 ? 229 THR A C     1 
ATOM 1973 O O     . THR B 2 229 ? -22.29900 61.79000  8.81500  1.000 180.87965 ? 229 THR A O     1 
ATOM 1974 C CB    . THR B 2 229 ? -20.86000 61.00100  11.42200 1.000 157.04968 ? 229 THR A CB    1 
ATOM 1975 O OG1   . THR B 2 229 ? -21.92600 60.07700  11.61700 1.000 160.33692 ? 229 THR A OG1   1 
ATOM 1976 C CG2   . THR B 2 229 ? -21.32700 62.41100  11.73700 1.000 155.97564 ? 229 THR A CG2   1 
ATOM 1977 N N     . THR B 2 230 ? -21.96800 59.54300  8.54500  1.000 184.32149 ? 230 THR A N     1 
ATOM 1978 C CA    . THR B 2 230 ? -23.15800 59.35800  7.68500  1.000 177.01514 ? 230 THR A CA    1 
ATOM 1979 C C     . THR B 2 230 ? -24.18400 58.55400  8.45200  1.000 165.48821 ? 230 THR A C     1 
ATOM 1980 O O     . THR B 2 230 ? -23.85600 57.43000  8.88700  1.000 165.30883 ? 230 THR A O     1 
ATOM 1981 C CB    . THR B 2 230 ? -22.77000 58.67800  6.37200  1.000 169.62328 ? 230 THR A CB    1 
ATOM 1982 O OG1   . THR B 2 230 ? -22.60500 57.29600  6.67400  1.000 161.92708 ? 230 THR A OG1   1 
ATOM 1983 C CG2   . THR B 2 230 ? -21.49000 59.24100  5.78100  1.000 163.68949 ? 230 THR A CG2   1 
ATOM 1984 N N     . ASN B 2 231 ? -25.38700 59.10700  8.61500  1.000 155.38015 ? 231 ASN A N     1 
ATOM 1985 C CA    . ASN B 2 231 ? -26.46800 58.38500  9.33700  1.000 156.38603 ? 231 ASN A CA    1 
ATOM 1986 C C     . ASN B 2 231 ? -26.60500 56.99400  8.71100  1.000 165.22459 ? 231 ASN A C     1 
ATOM 1987 O O     . ASN B 2 231 ? -26.76300 56.91400  7.47500  1.000 184.44433 ? 231 ASN A O     1 
ATOM 1988 C CB    . ASN B 2 231 ? -27.76600 59.18400  9.31400  1.000 161.27169 ? 231 ASN A CB    1 
ATOM 1989 C CG    . ASN B 2 231 ? -28.78600 58.66600  10.29900 1.000 167.48932 ? 231 ASN A CG    1 
ATOM 1990 O OD1   . ASN B 2 231 ? -28.97400 57.45000  10.41400 1.000 173.38299 ? 231 ASN A OD1   1 
ATOM 1991 N ND2   . ASN B 2 231 ? -29.45400 59.56000  11.01200 1.000 161.57011 ? 231 ASN A ND2   1 
ATOM 1992 N N     . TYR B 2 232 ? -26.47700 55.94800  9.52700  1.000 162.15344 ? 232 TYR A N     1 
ATOM 1993 C CA    . TYR B 2 232 ? -26.61100 54.56100  9.01500  1.000 163.00341 ? 232 TYR A CA    1 
ATOM 1994 C C     . TYR B 2 232 ? -28.01500 54.39100  8.47700  1.000 173.48869 ? 232 TYR A C     1 
ATOM 1995 O O     . TYR B 2 232 ? -28.26700 53.43900  7.70900  1.000 167.75454 ? 232 TYR A O     1 
ATOM 1996 C CB    . TYR B 2 232 ? -26.35800 53.56800  10.15100 1.000 150.84708 ? 232 TYR A CB    1 
ATOM 1997 C CG    . TYR B 2 232 ? -26.38700 52.10600  9.73000  1.000 153.95132 ? 232 TYR A CG    1 
ATOM 1998 C CD1   . TYR B 2 232 ? -25.45100 51.60000  8.83800  1.000 157.33684 ? 232 TYR A CD1   1 
ATOM 1999 C CD2   . TYR B 2 232 ? -27.35800 51.24000  10.21300 1.000 161.56211 ? 232 TYR A CD2   1 
ATOM 2000 C CE1   . TYR B 2 232 ? -25.47600 50.27400  8.44300  1.000 159.02726 ? 232 TYR A CE1   1 
ATOM 2001 C CE2   . TYR B 2 232 ? -27.39700 49.91400  9.82100  1.000 162.65023 ? 232 TYR A CE2   1 
ATOM 2002 C CZ    . TYR B 2 232 ? -26.45200 49.42900  8.93600  1.000 163.39883 ? 232 TYR A CZ    1 
ATOM 2003 O OH    . TYR B 2 232 ? -26.47400 48.12300  8.54300  1.000 157.28528 ? 232 TYR A OH    1 
ATOM 2004 N N     . ASN B 2 233 ? -28.91800 55.29300  8.86900  1.000 174.81268 ? 233 ASN A N     1 
ATOM 2005 C CA    . ASN B 2 233 ? -30.34300 55.14900  8.46700  1.000 168.65497 ? 233 ASN A CA    1 
ATOM 2006 C C     . ASN B 2 233 ? -30.77800 53.72300  8.81300  1.000 174.09472 ? 233 ASN A C     1 
ATOM 2007 O O     . ASN B 2 233 ? -31.45700 53.09100  7.97800  1.000 176.31376 ? 233 ASN A O     1 
ATOM 2008 C CB    . ASN B 2 233 ? -30.55400 55.52100  7.00400  1.000 176.72002 ? 233 ASN A CB    1 
ATOM 2009 C CG    . ASN B 2 233 ? -29.79100 56.76600  6.62700  1.000 170.75548 ? 233 ASN A CG    1 
ATOM 2010 O OD1   . ASN B 2 233 ? -30.06300 57.84700  7.16100  1.000 173.82189 ? 233 ASN A OD1   1 
ATOM 2011 N ND2   . ASN B 2 233 ? -28.83100 56.63700  5.72400  1.000 176.46197 ? 233 ASN A ND2   1 
ATOM 2012 N N     . GLY B 2 234 ? -30.38800 53.23900  9.99600  1.000 175.71813 ? 234 GLY A N     1 
ATOM 2013 C CA    . GLY B 2 234 ? -30.75400 51.87700  10.43100 1.000 168.04012 ? 234 GLY A CA    1 
ATOM 2014 C C     . GLY B 2 234 ? -30.48000 51.67800  11.90800 1.000 154.12216 ? 234 GLY A C     1 
ATOM 2015 O O     . GLY B 2 234 ? -29.92900 52.60200  12.53400 1.000 154.18069 ? 234 GLY A O     1 
ATOM 2016 N N     . SER B 2 235 ? -30.85700 50.51800  12.44900 1.000 154.63924 ? 235 SER A N     1 
ATOM 2017 C CA    . SER B 2 235 ? -30.59500 50.21400  13.87800 1.000 160.96781 ? 235 SER A CA    1 
ATOM 2018 C C     . SER B 2 235 ? -29.22000 49.55000  14.03000 1.000 156.88765 ? 235 SER A C     1 
ATOM 2019 O O     . SER B 2 235 ? -28.65200 49.12300  13.00000 1.000 155.81759 ? 235 SER A O     1 
ATOM 2020 C CB    . SER B 2 235 ? -31.67700 49.34400  14.44500 1.000 172.85764 ? 235 SER A CB    1 
ATOM 2021 O OG    . SER B 2 235 ? -31.68200 48.07500  13.80400 1.000 168.42982 ? 235 SER A OG    1 
ATOM 2022 N N     . LEU B 2 236 ? -28.72200 49.44800  15.26400 1.000 145.25890 ? 236 LEU A N     1 
ATOM 2023 C CA    . LEU B 2 236 ? -27.35500 48.90400  15.48600 1.000 152.29687 ? 236 LEU A CA    1 
ATOM 2024 C C     . LEU B 2 236 ? -27.33000 47.40000  15.18400 1.000 151.22563 ? 236 LEU A C     1 
ATOM 2025 O O     . LEU B 2 236 ? -26.25200 46.89500  14.82500 1.000 147.42871 ? 236 LEU A O     1 
ATOM 2026 C CB    . LEU B 2 236 ? -26.86100 49.19600  16.90300 1.000 153.10202 ? 236 LEU A CB    1 
ATOM 2027 C CG    . LEU B 2 236 ? -27.40400 48.30700  18.02700 1.000 167.85264 ? 236 LEU A CG    1 
ATOM 2028 C CD1   . LEU B 2 236 ? -26.53700 48.47500  19.26200 1.000 141.51083 ? 236 LEU A CD1   1 
ATOM 2029 C CD2   . LEU B 2 236 ? -28.86000 48.60200  18.34800 1.000 173.14132 ? 236 LEU A CD2   1 
ATOM 2030 N N     . LYS B 2 237 ? -28.46100 46.71600  15.33100 1.000 157.35729 ? 237 LYS A N     1 
ATOM 2031 C CA    . LYS B 2 237 ? -28.49100 45.28100  14.96000 1.000 160.53976 ? 237 LYS A CA    1 
ATOM 2032 C C     . LYS B 2 237 ? -28.03800 45.17300  13.50300 1.000 153.21712 ? 237 LYS A C     1 
ATOM 2033 O O     . LYS B 2 237 ? -27.15400 44.34400  13.20500 1.000 149.13778 ? 237 LYS A O     1 
ATOM 2034 C CB    . LYS B 2 237 ? -29.90800 44.73400  15.14900 1.000 157.33185 ? 237 LYS A CB    1 
ATOM 2035 C CG    . LYS B 2 237 ? -30.63826 45.31021  16.35394 1.000 162.69714 ? 237 LYS A CG    1 
ATOM 2036 C CD    . LYS B 2 237 ? -30.85817 46.81442  16.26749 1.000 166.11558 ? 237 LYS A CD    1 
ATOM 2037 C CE    . LYS B 2 237 ? -31.46672 47.37531  17.51308 1.000 164.35757 ? 237 LYS A CE    1 
ATOM 2038 N NZ    . LYS B 2 237 ? -31.49634 48.83999  17.49074 1.000 168.46976 ? 237 LYS A NZ    1 
ATOM 2039 N N     . SER B 2 238 ? -28.62100 46.00500  12.64100 1.000 151.26003 ? 238 SER A N     1 
ATOM 2040 C CA    . SER B 2 238 ? -28.25600 45.99500  11.20500 1.000 148.35474 ? 238 SER A CA    1 
ATOM 2041 C C     . SER B 2 238 ? -26.78200 46.38300  11.07300 1.000 146.31384 ? 238 SER A C     1 
ATOM 2042 O O     . SER B 2 238 ? -26.05800 45.72600  10.30100 1.000 142.69408 ? 238 SER A O     1 
ATOM 2043 C CB    . SER B 2 238 ? -29.13200 46.94600  10.45000 1.000 156.14301 ? 238 SER A CB    1 
ATOM 2044 O OG    . SER B 2 238 ? -30.44600 46.96700  10.99000 1.000 173.03269 ? 238 SER A OG    1 
ATOM 2045 N N     . LEU B 2 239 ? -26.36700 47.41200  11.81000 1.000 154.25478 ? 239 LEU A N     1 
ATOM 2046 C CA    . LEU B 2 239 ? -24.96200 47.87800  11.74600 1.000 145.59079 ? 239 LEU A CA    1 
ATOM 2047 C C     . LEU B 2 239 ? -24.03500 46.73300  12.16700 1.000 146.59571 ? 239 LEU A C     1 
ATOM 2048 O O     . LEU B 2 239 ? -23.05900 46.46300  11.44100 1.000 143.58754 ? 239 LEU A O     1 
ATOM 2049 C CB    . LEU B 2 239 ? -24.84400 49.08100  12.67600 1.000 140.98963 ? 239 LEU A CB    1 
ATOM 2050 C CG    . LEU B 2 239 ? -23.45900 49.72200  12.78700 1.000 144.25978 ? 239 LEU A CG    1 
ATOM 2051 C CD1   . LEU B 2 239 ? -22.99200 50.21900  11.43200 1.000 155.34742 ? 239 LEU A CD1   1 
ATOM 2052 C CD2   . LEU B 2 239 ? -23.53900 50.86600  13.77800 1.000 146.18703 ? 239 LEU A CD2   1 
ATOM 2053 N N     . TYR B 2 240 ? -24.34700 46.07900  13.28900 1.000 149.45595 ? 240 TYR A N     1 
ATOM 2054 C CA    . TYR B 2 240 ? -23.50300 44.96000  13.78400 1.000 134.50540 ? 240 TYR A CA    1 
ATOM 2055 C C     . TYR B 2 240 ? -23.44700 43.91900  12.69200 1.000 140.27880 ? 240 TYR A C     1 
ATOM 2056 O O     . TYR B 2 240 ? -22.35500 43.41800  12.36500 1.000 139.37052 ? 240 TYR A O     1 
ATOM 2057 C CB    . TYR B 2 240 ? -24.10900 44.38700  15.06700 1.000 130.24749 ? 240 TYR A CB    1 
ATOM 2058 C CG    . TYR B 2 240 ? -23.39800 43.16600  15.63500 1.000 134.05495 ? 240 TYR A CG    1 
ATOM 2059 C CD1   . TYR B 2 240 ? -22.35000 43.29900  16.53500 1.000 135.06509 ? 240 TYR A CD1   1 
ATOM 2060 C CD2   . TYR B 2 240 ? -23.78600 41.88000  15.28100 1.000 138.72348 ? 240 TYR A CD2   1 
ATOM 2061 C CE1   . TYR B 2 240 ? -21.70300 42.19100  17.05800 1.000 133.47637 ? 240 TYR A CE1   1 
ATOM 2062 C CE2   . TYR B 2 240 ? -23.14800 40.76500  15.79600 1.000 140.67564 ? 240 TYR A CE2   1 
ATOM 2063 C CZ    . TYR B 2 240 ? -22.10300 40.92000  16.68800 1.000 134.65980 ? 240 TYR A CZ    1 
ATOM 2064 O OH    . TYR B 2 240 ? -21.47400 39.82200  17.19600 1.000 138.50085 ? 240 TYR A OH    1 
ATOM 2065 N N     . ARG B 2 241 ? -24.60900 43.61700  12.11700 1.000 148.92754 ? 241 ARG A N     1 
ATOM 2066 C CA    . ARG B 2 241 ? -24.67100 42.61000  11.03400 1.000 153.11158 ? 241 ARG A CA    1 
ATOM 2067 C C     . ARG B 2 241 ? -23.79200 43.09300  9.87500  1.000 158.99868 ? 241 ARG A C     1 
ATOM 2068 O O     . ARG B 2 241 ? -22.92100 42.32300  9.42700  1.000 160.86873 ? 241 ARG A O     1 
ATOM 2069 C CB    . ARG B 2 241 ? -26.13200 42.44600  10.60800 1.000 147.06163 ? 241 ARG A CB    1 
ATOM 2070 C CG    . ARG B 2 241 ? -26.56400 41.05400  10.17000 1.000 172.85612 ? 241 ARG A CG    1 
ATOM 2071 C CD    . ARG B 2 241 ? -27.66300 41.03400  9.11800  1.000 193.45225 ? 241 ARG A CD    1 
ATOM 2072 N NE    . ARG B 2 241 ? -27.16400 41.26400  7.75700  1.000 197.21026 ? 241 ARG A NE    1 
ATOM 2073 C CZ    . ARG B 2 241 ? -26.43600 40.39300  7.07300  1.000 192.25807 ? 241 ARG A CZ    1 
ATOM 2074 N NH1   . ARG B 2 241 ? -26.18600 39.20100  7.58100  1.000 189.86112 ? 241 ARG A NH1   1 
ATOM 2075 N NH2   . ARG B 2 241 ? -25.95500 40.72000  5.88500  1.000 185.52066 ? 241 ARG A NH2   1 
ATOM 2076 N N     . LYS B 2 242 ? -23.99200 44.33700  9.43800  1.000 158.02716 ? 242 LYS A N     1 
ATOM 2077 C CA    . LYS B 2 242 ? -23.22900 44.85200  8.27400  1.000 161.86049 ? 242 LYS A CA    1 
ATOM 2078 C C     . LYS B 2 242 ? -21.73300 44.76700  8.59200  1.000 155.49789 ? 242 LYS A C     1 
ATOM 2079 O O     . LYS B 2 242 ? -20.95700 44.31300  7.72600  1.000 157.61317 ? 242 LYS A O     1 
ATOM 2080 C CB    . LYS B 2 242 ? -23.61100 46.30200  7.96600  1.000 156.99469 ? 242 LYS A CB    1 
ATOM 2081 C CG    . LYS B 2 242 ? -22.94700 46.86300  6.71800  1.000 152.55159 ? 242 LYS A CG    1 
ATOM 2082 C CD    . LYS B 2 242 ? -23.33500 46.08700  5.46600  1.000 158.59637 ? 242 LYS A CD    1 
ATOM 2083 C CE    . LYS B 2 242 ? -22.17600 45.84800  4.55300  1.000 167.55773 ? 242 LYS A CE    1 
ATOM 2084 N NZ    . LYS B 2 242 ? -21.16400 44.99700  5.18400  1.000 163.68234 ? 242 LYS A NZ    1 
ATOM 2085 N N     . ALA B 2 243 ? -21.35600 45.18700  9.79600  1.000 147.91724 ? 243 ALA A N     1 
ATOM 2086 C CA    . ALA B 2 243 ? -19.92900 45.17400  10.17900 1.000 145.54516 ? 243 ALA A CA    1 
ATOM 2087 C C     . ALA B 2 243 ? -19.41300 43.73800  10.16600 1.000 158.11760 ? 243 ALA A C     1 
ATOM 2088 O O     . ALA B 2 243 ? -18.48100 43.43400  9.39400  1.000 165.92049 ? 243 ALA A O     1 
ATOM 2089 C CB    . ALA B 2 243 ? -19.78300 45.78600  11.54700 1.000 151.62368 ? 243 ALA A CB    1 
ATOM 2090 N N     . VAL B 2 244 ? -20.01700 42.87600  10.98400 1.000 158.40289 ? 244 VAL A N     1 
ATOM 2091 C CA    . VAL B 2 244 ? -19.50600 41.47900  11.08500 1.000 154.08381 ? 244 VAL A CA    1 
ATOM 2092 C C     . VAL B 2 244 ? -19.45700 40.91100  9.65900  1.000 162.23966 ? 244 VAL A C     1 
ATOM 2093 O O     . VAL B 2 244 ? -18.54700 40.10700  9.37100  1.000 168.42212 ? 244 VAL A O     1 
ATOM 2094 C CB    . VAL B 2 244 ? -20.33500 40.59100  12.03600 1.000 141.00554 ? 244 VAL A CB    1 
ATOM 2095 C CG1   . VAL B 2 244 ? -21.75400 40.35800  11.53700 1.000 151.82118 ? 244 VAL A CG1   1 
ATOM 2096 C CG2   . VAL B 2 244 ? -19.64400 39.26700  12.32600 1.000 143.82673 ? 244 VAL A CG2   1 
ATOM 2097 N N     . ASP B 2 245 ? -20.38600 41.34700  8.80300  1.000 152.70071 ? 245 ASP A N     1 
ATOM 2098 C CA    . ASP B 2 245 ? -20.41300 40.82400  7.41300  1.000 160.96687 ? 245 ASP A CA    1 
ATOM 2099 C C     . ASP B 2 245 ? -19.09500 41.18900  6.72800  1.000 160.96401 ? 245 ASP A C     1 
ATOM 2100 O O     . ASP B 2 245 ? -18.47700 40.29100  6.11900  1.000 159.34227 ? 245 ASP A O     1 
ATOM 2101 C CB    . ASP B 2 245 ? -21.61400 41.35400  6.64900  1.000 170.02959 ? 245 ASP A CB    1 
ATOM 2102 C CG    . ASP B 2 245 ? -21.73600 40.87800  5.21000  1.000 170.46966 ? 245 ASP A CG    1 
ATOM 2103 O OD1   . ASP B 2 245 ? -21.86200 39.65200  5.00900  1.000 170.08940 ? 245 ASP A OD1   1 
ATOM 2104 O OD2   . ASP B 2 245 ? -21.71000 41.73700  4.30500  1.000 170.89754 ? 245 ASP A OD2   1 
ATOM 2105 N N     . GLN B 2 246 ? -18.66800 42.44700  6.85500  1.000 161.32368 ? 246 GLN A N     1 
ATOM 2106 C CA    . GLN B 2 246 ? -17.42700 42.89300  6.17100  1.000 159.61286 ? 246 GLN A CA    1 
ATOM 2107 C C     . GLN B 2 246 ? -16.20600 42.39200  6.95700  1.000 159.04708 ? 246 GLN A C     1 
ATOM 2108 O O     . GLN B 2 246 ? -15.19100 42.04800  6.31700  1.000 165.06106 ? 246 GLN A O     1 
ATOM 2109 C CB    . GLN B 2 246 ? -17.42700 44.41200  6.00700  1.000 163.24986 ? 246 GLN A CB    1 
ATOM 2110 C CG    . GLN B 2 246 ? -17.75400 44.86800  4.58900  1.000 172.92127 ? 246 GLN A CG    1 
ATOM 2111 C CD    . GLN B 2 246 ? -18.08100 46.34100  4.49000  1.000 183.15731 ? 246 GLN A CD    1 
ATOM 2112 O OE1   . GLN B 2 246 ? -19.05300 46.82500  5.07800  1.000 187.58595 ? 246 GLN A OE1   1 
ATOM 2113 N NE2   . GLN B 2 246 ? -17.27500 47.06800  3.73000  1.000 171.89638 ? 246 GLN A NE2   1 
ATOM 2114 N N     . LEU B 2 247 ? -16.30800 42.34700  8.28600  1.000 155.85818 ? 247 LEU A N     1 
ATOM 2115 C CA    . LEU B 2 247 ? -15.18900 41.84700  9.12300  1.000 148.36385 ? 247 LEU A CA    1 
ATOM 2116 C C     . LEU B 2 247 ? -15.02800 40.33900  8.90100  1.000 155.64599 ? 247 LEU A C     1 
ATOM 2117 O O     . LEU B 2 247 ? -13.89900 39.83100  9.07000  1.000 143.71332 ? 247 LEU A O     1 
ATOM 2118 C CB    . LEU B 2 247 ? -15.47400 42.16400  10.58700 1.000 157.59593 ? 247 LEU A CB    1 
ATOM 2119 C CG    . LEU B 2 247 ? -15.49400 43.64900  10.95500 1.000 163.58661 ? 247 LEU A CG    1 
ATOM 2120 C CD1   . LEU B 2 247 ? -15.75900 43.82200  12.43900 1.000 157.39509 ? 247 LEU A CD1   1 
ATOM 2121 C CD2   . LEU B 2 247 ? -14.18000 44.30200  10.56500 1.000 160.11918 ? 247 LEU A CD2   1 
ATOM 2122 N N     . GLY B 2 248 ? -16.11800 39.65800  8.54300  1.000 167.63331 ? 248 GLY A N     1 
ATOM 2123 C CA    . GLY B 2 248 ? -16.06800 38.19900  8.33500  1.000 161.36844 ? 248 GLY A CA    1 
ATOM 2124 C C     . GLY B 2 248 ? -15.86900 37.46900  9.64700  1.000 162.43033 ? 248 GLY A C     1 
ATOM 2125 O O     . GLY B 2 248 ? -15.05700 36.52200  9.68200  1.000 166.13112 ? 248 GLY A O     1 
ATOM 2126 N N     . LEU B 2 249 ? -16.57500 37.89900  10.69400 1.000 149.62675 ? 249 LEU A N     1 
ATOM 2127 C CA    . LEU B 2 249 ? -16.47500 37.22700  12.01400 1.000 146.22207 ? 249 LEU A CA    1 
ATOM 2128 C C     . LEU B 2 249 ? -17.76900 36.44300  12.27300 1.000 155.28749 ? 249 LEU A C     1 
ATOM 2129 O O     . LEU B 2 249 ? -18.44100 36.07200  11.28900 1.000 166.99358 ? 249 LEU A O     1 
ATOM 2130 C CB    . LEU B 2 249 ? -16.22300 38.28000  13.09000 1.000 151.68055 ? 249 LEU A CB    1 
ATOM 2131 C CG    . LEU B 2 249 ? -15.08000 39.25900  12.81000 1.000 155.82184 ? 249 LEU A CG    1 
ATOM 2132 C CD1   . LEU B 2 249 ? -14.96000 40.27300  13.93300 1.000 147.31788 ? 249 LEU A CD1   1 
ATOM 2133 C CD2   . LEU B 2 249 ? -13.77000 38.51700  12.61600 1.000 161.82819 ? 249 LEU A CD2   1 
ATOM 2134 N N     . THR B 2 250 ? -18.10300 36.20900  13.54400 1.000 146.68339 ? 250 THR A N     1 
ATOM 2135 C CA    . THR B 2 250 ? -19.31800 35.44400  13.88500 1.000 146.63555 ? 250 THR A CA    1 
ATOM 2136 C C     . THR B 2 250 ? -20.34200 36.37700  14.48400 1.000 152.53751 ? 250 THR A C     1 
ATOM 2137 O O     . THR B 2 250 ? -19.93400 37.35600  15.14200 1.000 157.60318 ? 250 THR A O     1 
ATOM 2138 C CB    . THR B 2 250 ? -18.95500 34.32700  14.85700 1.000 146.50387 ? 250 THR A CB    1 
ATOM 2139 O OG1   . THR B 2 250 ? -18.51200 35.00400  16.02800 1.000 163.87586 ? 250 THR A OG1   1 
ATOM 2140 C CG2   . THR B 2 250 ? -17.85600 33.42500  14.32400 1.000 138.52791 ? 250 THR A CG2   1 
ATOM 2141 N N     . TYR B 2 251 ? -21.62700 36.08900  14.27600 1.000 131.82320 ? 251 TYR A N     1 
ATOM 2142 C CA    . TYR B 2 251 ? -22.70900 36.91800  14.86600 1.000 130.39335 ? 251 TYR A CA    1 
ATOM 2143 C C     . TYR B 2 251 ? -22.95000 36.43800  16.28500 1.000 132.57513 ? 251 TYR A C     1 
ATOM 2144 O O     . TYR B 2 251 ? -23.93200 35.70800  16.51700 1.000 135.34681 ? 251 TYR A O     1 
ATOM 2145 C CB    . TYR B 2 251 ? -23.97900 36.78500  14.02400 1.000 131.05721 ? 251 TYR A CB    1 
ATOM 2146 C CG    . TYR B 2 251 ? -25.06500 37.82400  14.27200 1.000 128.87455 ? 251 TYR A CG    1 
ATOM 2147 C CD1   . TYR B 2 251 ? -26.02900 37.63800  15.25400 1.000 127.59938 ? 251 TYR A CD1   1 
ATOM 2148 C CD2   . TYR B 2 251 ? -25.14200 38.97500  13.49900 1.000 130.16435 ? 251 TYR A CD2   1 
ATOM 2149 C CE1   . TYR B 2 251 ? -27.02400 38.57400  15.47600 1.000 126.60668 ? 251 TYR A CE1   1 
ATOM 2150 C CE2   . TYR B 2 251 ? -26.13400 39.91800  13.70900 1.000 136.02285 ? 251 TYR A CE2   1 
ATOM 2151 C CZ    . TYR B 2 251 ? -27.07700 39.71700  14.70000 1.000 129.67568 ? 251 TYR A CZ    1 
ATOM 2152 O OH    . TYR B 2 251 ? -28.05600 40.64400  14.90800 1.000 133.79248 ? 251 TYR A OH    1 
ATOM 2153 N N     . ARG B 2 252 ? -22.06600 36.81600  17.21200 1.000 140.54249 ? 252 ARG A N     1 
ATOM 2154 C CA    . ARG B 2 252 ? -22.25900 36.44400  18.63600 1.000 125.92244 ? 252 ARG A CA    1 
ATOM 2155 C C     . ARG B 2 252 ? -23.38400 37.31100  19.21200 1.000 125.51168 ? 252 ARG A C     1 
ATOM 2156 O O     . ARG B 2 252 ? -23.20600 38.54200  19.29800 1.000 129.40261 ? 252 ARG A O     1 
ATOM 2157 C CB    . ARG B 2 252 ? -20.97500 36.62000  19.45100 1.000 125.62125 ? 252 ARG A CB    1 
ATOM 2158 C CG    . ARG B 2 252 ? -21.17100 36.22100  20.90600 1.000 135.37017 ? 252 ARG A CG    1 
ATOM 2159 C CD    . ARG B 2 252 ? -21.60200 34.76900  21.00700 1.000 135.16325 ? 252 ARG A CD    1 
ATOM 2160 N NE    . ARG B 2 252 ? -22.24600 34.45800  22.28600 1.000 133.65814 ? 252 ARG A NE    1 
ATOM 2161 C CZ    . ARG B 2 252 ? -21.78700 33.56300  23.14900 1.000 159.22551 ? 252 ARG A CZ    1 
ATOM 2162 N NH1   . ARG B 2 252 ? -20.54800 33.12100  23.03900 1.000 161.35337 ? 252 ARG A NH1   1 
ATOM 2163 N NH2   . ARG B 2 252 ? -22.56400 33.11900  24.12000 1.000 166.03284 ? 252 ARG A NH2   1 
ATOM 2164 N N     . PRO B 2 253 ? -24.53200 36.72400  19.59900 1.000 121.98561 ? 253 PRO A N     1 
ATOM 2165 C CA    . PRO B 2 253 ? -25.64900 37.51800  20.08400 1.000 130.56819 ? 253 PRO A CA    1 
ATOM 2166 C C     . PRO B 2 253 ? -25.28300 38.27100  21.35200 1.000 130.43519 ? 253 PRO A C     1 
ATOM 2167 O O     . PRO B 2 253 ? -25.70900 39.43100  21.51600 1.000 123.70431 ? 253 PRO A O     1 
ATOM 2168 C CB    . PRO B 2 253 ? -26.72700 36.45600  20.32600 1.000 124.51366 ? 253 PRO A CB    1 
ATOM 2169 C CG    . PRO B 2 253 ? -25.94800 35.18400  20.56000 1.000 129.78331 ? 253 PRO A CG    1 
ATOM 2170 C CD    . PRO B 2 253 ? -24.77800 35.29500  19.60200 1.000 122.41319 ? 253 PRO A CD    1 
ATOM 2171 N N     . GLN B 2 254 ? -24.50600 37.63400  22.23000 1.000 122.59030 ? 254 GLN A N     1 
ATOM 2172 C CA    . GLN B 2 254 ? -24.14800 38.26900  23.52400 1.000 118.37695 ? 254 GLN A CA    1 
ATOM 2173 C C     . GLN B 2 254 ? -23.30400 39.52800  23.26500 1.000 127.71463 ? 254 GLN A C     1 
ATOM 2174 O O     . GLN B 2 254 ? -23.55100 40.55100  23.93500 1.000 128.99939 ? 254 GLN A O     1 
ATOM 2175 C CB    . GLN B 2 254 ? -23.41300 37.27200  24.41900 1.000 134.23830 ? 254 GLN A CB    1 
ATOM 2176 C CG    . GLN B 2 254 ? -24.27400 36.10400  24.88800 1.000 137.72618 ? 254 GLN A CG    1 
ATOM 2177 C CD    . GLN B 2 254 ? -25.22800 36.45700  26.01000 1.000 148.52143 ? 254 GLN A CD    1 
ATOM 2178 O OE1   . GLN B 2 254 ? -25.15000 35.91000  27.11500 1.000 159.69875 ? 254 GLN A OE1   1 
ATOM 2179 N NE2   . GLN B 2 254 ? -26.14700 37.37300  25.74000 1.000 141.12052 ? 254 GLN A NE2   1 
ATOM 2180 N N     . GLN B 2 255 ? -22.35500 39.45900  22.32600 1.000 128.83896 ? 255 GLN A N     1 
ATOM 2181 C CA    . GLN B 2 255 ? -21.57400 40.68000  22.00000 1.000 124.14717 ? 255 GLN A CA    1 
ATOM 2182 C C     . GLN B 2 255 ? -22.55700 41.81000  21.66700 1.000 119.29759 ? 255 GLN A C     1 
ATOM 2183 O O     . GLN B 2 255 ? -22.42300 42.91300  22.23900 1.000 123.21659 ? 255 GLN A O     1 
ATOM 2184 C CB    . GLN B 2 255 ? -20.64700 40.40500  20.81900 1.000 118.83016 ? 255 GLN A CB    1 
ATOM 2185 C CG    . GLN B 2 255 ? -19.87500 41.62500  20.33000 1.000 128.15815 ? 255 GLN A CG    1 
ATOM 2186 C CD    . GLN B 2 255 ? -19.05900 41.34500  19.08800 1.000 124.51040 ? 255 GLN A CD    1 
ATOM 2187 O OE1   . GLN B 2 255 ? -19.06000 40.23100  18.55300 1.000 120.32937 ? 255 GLN A OE1   1 
ATOM 2188 N NE2   . GLN B 2 255 ? -18.35300 42.36000  18.61600 1.000 135.36616 ? 255 GLN A NE2   1 
ATOM 2189 N N     . LEU B 2 256 ? -23.51700 41.53400  20.78400 1.000 114.96082 ? 256 LEU A N     1 
ATOM 2190 C CA    . LEU B 2 256 ? -24.50100 42.56800  20.37400 1.000 123.41011 ? 256 LEU A CA    1 
ATOM 2191 C C     . LEU B 2 256 ? -25.29900 43.02100  21.60400 1.000 124.89012 ? 256 LEU A C     1 
ATOM 2192 O O     . LEU B 2 256 ? -25.54100 44.23700  21.74200 1.000 125.05300 ? 256 LEU A O     1 
ATOM 2193 C CB    . LEU B 2 256 ? -25.40900 41.99000  19.29200 1.000 124.11560 ? 256 LEU A CB    1 
ATOM 2194 C CG    . LEU B 2 256 ? -26.54200 42.90000  18.80800 1.000 123.94665 ? 256 LEU A CG    1 
ATOM 2195 C CD1   . LEU B 2 256 ? -26.00900 44.24500  18.34900 1.000 131.76753 ? 256 LEU A CD1   1 
ATOM 2196 C CD2   . LEU B 2 256 ? -27.32000 42.22700  17.69300 1.000 130.64842 ? 256 LEU A CD2   1 
ATOM 2197 N N     . TYR B 2 257 ? -25.68000 42.07500  22.46300 1.000 119.19123 ? 257 TYR A N     1 
ATOM 2198 C CA    . TYR B 2 257 ? -26.46900 42.41700  23.67400 1.000 122.22616 ? 257 TYR A CA    1 
ATOM 2199 C C     . TYR B 2 257 ? -25.72400 43.49800  24.43800 1.000 126.05334 ? 257 TYR A C     1 
ATOM 2200 O O     . TYR B 2 257 ? -26.34700 44.49700  24.85900 1.000 119.60288 ? 257 TYR A O     1 
ATOM 2201 C CB    . TYR B 2 257 ? -26.63100 41.14900  24.51300 1.000 121.58113 ? 257 TYR A CB    1 
ATOM 2202 C CG    . TYR B 2 257 ? -27.32300 41.32500  25.85800 1.000 109.01649 ? 257 TYR A CG    1 
ATOM 2203 C CD1   . TYR B 2 257 ? -28.39500 42.19400  26.00900 1.000 111.28205 ? 257 TYR A CD1   1 
ATOM 2204 C CD2   . TYR B 2 257 ? -26.88800 40.63100  26.98000 1.000 117.90332 ? 257 TYR A CD2   1 
ATOM 2205 C CE1   . TYR B 2 257 ? -29.02500 42.35400  27.23200 1.000 106.87618 ? 257 TYR A CE1   1 
ATOM 2206 C CE2   . TYR B 2 257 ? -27.50600 40.78600  28.20900 1.000 128.48153 ? 257 TYR A CE2   1 
ATOM 2207 C CZ    . TYR B 2 257 ? -28.57700 41.65100  28.33500 1.000 109.13141 ? 257 TYR A CZ    1 
ATOM 2208 O OH    . TYR B 2 257 ? -29.19100 41.80900  29.54300 1.000 120.49245 ? 257 TYR A OH    1 
ATOM 2209 N N     . LEU B 2 258 ? -24.41200 43.31600  24.60200 1.000 116.93955 ? 258 LEU A N     1 
ATOM 2210 C CA    . LEU B 2 258 ? -23.59700 44.29800  25.36100 1.000 114.08318 ? 258 LEU A CA    1 
ATOM 2211 C C     . LEU B 2 258 ? -23.71600 45.67100  24.68900 1.000 116.62709 ? 258 LEU A C     1 
ATOM 2212 O O     . LEU B 2 258 ? -24.03100 46.65100  25.38800 1.000 122.15783 ? 258 LEU A O     1 
ATOM 2213 C CB    . LEU B 2 258 ? -22.14900 43.81600  25.40100 1.000 122.43451 ? 258 LEU A CB    1 
ATOM 2214 C CG    . LEU B 2 258 ? -21.16400 44.69400  26.17600 1.000 108.81334 ? 258 LEU A CG    1 
ATOM 2215 C CD1   . LEU B 2 258 ? -21.62200 44.87400  27.61200 1.000 103.46444 ? 258 LEU A CD1   1 
ATOM 2216 C CD2   . LEU B 2 258 ? -19.78100 44.07000  26.13300 1.000 102.69774 ? 258 LEU A CD2   1 
ATOM 2217 N N     . ALA B 2 259 ? -23.50000 45.72400  23.37500 1.000 112.33451 ? 259 ALA A N     1 
ATOM 2218 C CA    . ALA B 2 259 ? -23.54700 47.02000  22.66400 1.000 114.12114 ? 259 ALA A CA    1 
ATOM 2219 C C     . ALA B 2 259 ? -24.90100 47.67600  22.91800 1.000 110.60583 ? 259 ALA A C     1 
ATOM 2220 O O     . ALA B 2 259 ? -24.94400 48.88400  23.22800 1.000 105.23480 ? 259 ALA A O     1 
ATOM 2221 C CB    . ALA B 2 259 ? -23.31500 46.80000  21.19100 1.000 114.89268 ? 259 ALA A CB    1 
ATOM 2222 N N     . GLU B 2 260 ? -25.97500 46.89200  22.81100 1.000 120.88688 ? 260 GLU A N     1 
ATOM 2223 C CA    . GLU B 2 260 ? -27.34000 47.45000  22.98500 1.000 117.34859 ? 260 GLU A CA    1 
ATOM 2224 C C     . GLU B 2 260 ? -27.49900 47.99500  24.41200 1.000 111.84532 ? 260 GLU A C     1 
ATOM 2225 O O     . GLU B 2 260 ? -28.03000 49.11400  24.55900 1.000 107.07708 ? 260 GLU A O     1 
ATOM 2226 C CB    . GLU B 2 260 ? -28.36700 46.36900  22.65400 1.000 120.35650 ? 260 GLU A CB    1 
ATOM 2227 C CG    . GLU B 2 260 ? -28.37500 45.99500  21.17500 1.000 125.25883 ? 260 GLU A CG    1 
ATOM 2228 C CD    . GLU B 2 260 ? -29.20800 44.77100  20.84300 1.000 157.74270 ? 260 GLU A CD    1 
ATOM 2229 O OE1   . GLU B 2 260 ? -29.75700 44.15800  21.78300 1.000 174.53208 ? 260 GLU A OE1   1 
ATOM 2230 O OE2   . GLU B 2 260 ? -29.31600 44.43600  19.64600 1.000 150.90645 ? 260 GLU A OE2   1 
ATOM 2231 N N     . THR B 2 261 ? -27.05200 47.23600  25.41600 1.000 112.34631 ? 261 THR A N     1 
ATOM 2232 C CA    . THR B 2 261 ? -27.21500 47.67800  26.81700 1.000 113.10589 ? 261 THR A CA    1 
ATOM 2233 C C     . THR B 2 261 ? -26.44600 48.96400  27.01400 1.000 113.52784 ? 261 THR A C     1 
ATOM 2234 O O     . THR B 2 261 ? -27.01700 49.91500  27.59000 1.000 111.31250 ? 261 THR A O     1 
ATOM 2235 C CB    . THR B 2 261 ? -26.74300 46.58800  27.77500 1.000 103.58703 ? 261 THR A CB    1 
ATOM 2236 O OG1   . THR B 2 261 ? -25.44900 46.21700  27.31700 1.000 129.74193 ? 261 THR A OG1   1 
ATOM 2237 C CG2   . THR B 2 261 ? -27.65700 45.37800  27.77100 1.000 105.67474 ? 261 THR A CG2   1 
ATOM 2238 N N     . ILE B 2 262 ? -25.20300 49.00800  26.53100 1.000 107.46534 ? 262 ILE A N     1 
ATOM 2239 C CA    . ILE B 2 262 ? -24.36600 50.23600  26.66800 1.000 113.15393 ? 262 ILE A CA    1 
ATOM 2240 C C     . ILE B 2 262 ? -25.10800 51.39500  25.99100 1.000 108.57178 ? 262 ILE A C     1 
ATOM 2241 O O     . ILE B 2 262 ? -25.30200 52.43600  26.64900 1.000 113.30611 ? 262 ILE A O     1 
ATOM 2242 C CB    . ILE B 2 262 ? -22.97500 50.02300  26.04500 1.000 104.17386 ? 262 ILE A CB    1 
ATOM 2243 C CG1   . ILE B 2 262 ? -22.22000 48.88800  26.72400 1.000 113.32890 ? 262 ILE A CG1   1 
ATOM 2244 C CG2   . ILE B 2 262 ? -22.16600 51.31900  26.05500 1.000 97.03388  ? 262 ILE A CG2   1 
ATOM 2245 C CD1   . ILE B 2 262 ? -20.94000 48.49600  26.01000 1.000 116.59242 ? 262 ILE A CD1   1 
ATOM 2246 N N     . LEU B 2 263 ? -25.53700 51.20100  24.74200 1.000 98.33550  ? 263 LEU A N     1 
ATOM 2247 C CA    . LEU B 2 263 ? -26.19100 52.30200  23.99200 1.000 101.77262 ? 263 LEU A CA    1 
ATOM 2248 C C     . LEU B 2 263 ? -27.45000 52.75100  24.74300 1.000 107.43809 ? 263 LEU A C     1 
ATOM 2249 O O     . LEU B 2 263 ? -27.68100 53.97200  24.84200 1.000 95.30947  ? 263 LEU A O     1 
ATOM 2250 C CB    . LEU B 2 263 ? -26.52200 51.82200  22.58200 1.000 106.26108 ? 263 LEU A CB    1 
ATOM 2251 C CG    . LEU B 2 263 ? -27.15900 52.86100  21.65700 1.000 110.52203 ? 263 LEU A CG    1 
ATOM 2252 C CD1   . LEU B 2 263 ? -26.18700 53.99100  21.36700 1.000 119.38900 ? 263 LEU A CD1   1 
ATOM 2253 C CD2   . LEU B 2 263 ? -27.62800 52.20800  20.37100 1.000 114.01083 ? 263 LEU A CD2   1 
ATOM 2254 N N     . ASP B 2 264 ? -28.22700 51.79400  25.25000 1.000 109.38677 ? 264 ASP A N     1 
ATOM 2255 C CA    . ASP B 2 264 ? -29.49100 52.13900  25.94900 1.000 111.38197 ? 264 ASP A CA    1 
ATOM 2256 C C     . ASP B 2 264 ? -29.15300 53.03200  27.14200 1.000 119.54310 ? 264 ASP A C     1 
ATOM 2257 O O     . ASP B 2 264 ? -29.80100 54.08700  27.30100 1.000 120.77913 ? 264 ASP A O     1 
ATOM 2258 C CB    . ASP B 2 264 ? -30.24400 50.89100  26.37600 1.000 104.50673 ? 264 ASP A CB    1 
ATOM 2259 C CG    . ASP B 2 264 ? -31.57800 51.13900  27.06400 1.000 130.78474 ? 264 ASP A CG    1 
ATOM 2260 O OD1   . ASP B 2 264 ? -32.46900 51.72300  26.41500 1.000 138.87024 ? 264 ASP A OD1   1 
ATOM 2261 O OD2   . ASP B 2 264 ? -31.71000 50.75000  28.24200 1.000 130.92527 ? 264 ASP A OD2   1 
ATOM 2262 N N     . GLN B 2 265 ? -28.16000 52.62700  27.93300 1.000 113.91402 ? 265 GLN A N     1 
ATOM 2263 C CA    . GLN B 2 265 ? -27.78700 53.40300  29.14200 1.000 117.25181 ? 265 GLN A CA    1 
ATOM 2264 C C     . GLN B 2 265 ? -27.25000 54.77600  28.71900 1.000 112.45098 ? 265 GLN A C     1 
ATOM 2265 O O     . GLN B 2 265 ? -27.59000 55.76900  29.38900 1.000 112.25836 ? 265 GLN A O     1 
ATOM 2266 C CB    . GLN B 2 265 ? -26.75500 52.61300  29.94200 1.000 110.34789 ? 265 GLN A CB    1 
ATOM 2267 C CG    . GLN B 2 265 ? -27.30700 51.32500  30.54100 1.000 104.35962 ? 265 GLN A CG    1 
ATOM 2268 C CD    . GLN B 2 265 ? -28.40200 51.57700  31.55300 1.000 111.45914 ? 265 GLN A CD    1 
ATOM 2269 O OE1   . GLN B 2 265 ? -28.19200 52.24900  32.56700 1.000 115.79860 ? 265 GLN A OE1   1 
ATOM 2270 N NE2   . GLN B 2 265 ? -29.58500 51.04600  31.28200 1.000 116.48411 ? 265 GLN A NE2   1 
ATOM 2271 N N     . LEU B 2 266 ? -26.44100 54.82000  27.65800 1.000 107.54647 ? 266 LEU A N     1 
ATOM 2272 C CA    . LEU B 2 266 ? -25.84400 56.09900  27.19000 1.000 121.73568 ? 266 LEU A CA    1 
ATOM 2273 C C     . LEU B 2 266 ? -26.95100 57.02300  26.66400 1.000 126.65588 ? 266 LEU A C     1 
ATOM 2274 O O     . LEU B 2 266 ? -26.88300 58.23800  26.93600 1.000 118.45461 ? 266 LEU A O     1 
ATOM 2275 C CB    . LEU B 2 266 ? -24.80200 55.82300  26.10900 1.000 110.55859 ? 266 LEU A CB    1 
ATOM 2276 C CG    . LEU B 2 266 ? -23.45700 55.26800  26.58500 1.000 96.18688  ? 266 LEU A CG    1 
ATOM 2277 C CD1   . LEU B 2 266 ? -22.59200 54.92200  25.38600 1.000 96.25849  ? 266 LEU A CD1   1 
ATOM 2278 C CD2   . LEU B 2 266 ? -22.75900 56.28800  27.46500 1.000 98.35781  ? 266 LEU A CD2   1 
ATOM 2279 N N     . MET B 2 267 ? -27.92400 56.47000  25.93600 1.000 115.78390 ? 267 MET A N     1 
ATOM 2280 C CA    . MET B 2 267 ? -28.97800 57.31800  25.32100 1.000 109.27231 ? 267 MET A CA    1 
ATOM 2281 C C     . MET B 2 267 ? -29.68800 58.10500  26.42900 1.000 113.43752 ? 267 MET A C     1 
ATOM 2282 O O     . MET B 2 267 ? -29.95000 59.30800  26.22500 1.000 110.52038 ? 267 MET A O     1 
ATOM 2283 C CB    . MET B 2 267 ? -29.99000 56.46100  24.55700 1.000 107.96921 ? 267 MET A CB    1 
ATOM 2284 C CG    . MET B 2 267 ? -30.79000 57.23200  23.52800 1.000 124.47971 ? 267 MET A CG    1 
ATOM 2285 S SD    . MET B 2 267 ? -29.74000 57.90200  22.22300 1.000 108.09109 ? 267 MET A SD    1 
ATOM 2286 C CE    . MET B 2 267 ? -29.02700 56.38700  21.56800 1.000 103.87239 ? 267 MET A CE    1 
ATOM 2287 N N     . HIS B 2 268 ? -29.98200 57.44900  27.55100 1.000 106.98304 ? 268 HIS A N     1 
ATOM 2288 C CA    . HIS B 2 268 ? -30.60500 58.15400  28.70100 1.000 105.86567 ? 268 HIS A CA    1 
ATOM 2289 C C     . HIS B 2 268 ? -29.49600 58.63000  29.64100 1.000 130.08086 ? 268 HIS A C     1 
ATOM 2290 O O     . HIS B 2 268 ? -28.31000 58.35700  29.37900 1.000 130.72134 ? 268 HIS A O     1 
ATOM 2291 C CB    . HIS B 2 268 ? -31.58400 57.23200  29.43200 1.000 107.52063 ? 268 HIS A CB    1 
ATOM 2292 C CG    . HIS B 2 268 ? -32.42300 56.40400  28.51900 1.000 135.53410 ? 268 HIS A CG    1 
ATOM 2293 N ND1   . HIS B 2 268 ? -32.05800 55.13900  28.11300 1.000 139.14917 ? 268 HIS A ND1   1 
ATOM 2294 C CD2   . HIS B 2 268 ? -33.60300 56.65300  27.94100 1.000 139.89331 ? 268 HIS A CD2   1 
ATOM 2295 C CE1   . HIS B 2 268 ? -32.99500 54.65200  27.31200 1.000 127.62404 ? 268 HIS A CE1   1 
ATOM 2296 N NE2   . HIS B 2 268 ? -33.94200 55.55500  27.19400 1.000 120.55536 ? 268 HIS A NE2   1 
ATOM 2297 N N     . SER B 2 269 ? -29.86600 59.34500  30.70300 1.000 132.56305 ? 269 SER A N     1 
ATOM 2298 C CA    . SER B 2 269 ? -28.85200 59.76500  31.70300 1.000 126.98386 ? 269 SER A CA    1 
ATOM 2299 C C     . SER B 2 269 ? -28.79400 58.70000  32.80000 1.000 130.47467 ? 269 SER A C     1 
ATOM 2300 O O     . SER B 2 269 ? -29.06700 59.04200  33.97000 1.000 148.65945 ? 269 SER A O     1 
ATOM 2301 C CB    . SER B 2 269 ? -29.17500 61.11500  32.27200 1.000 137.57532 ? 269 SER A CB    1 
ATOM 2302 O OG    . SER B 2 269 ? -30.45100 61.10600  32.89700 1.000 178.30954 ? 269 SER A OG    1 
ATOM 2303 N N     . GLU B 2 270 ? -28.45000 57.46300  32.43700 1.000 123.78538 ? 270 GLU A N     1 
ATOM 2304 C CA    . GLU B 2 270 ? -28.48900 56.36600  33.43600 1.000 132.15416 ? 270 GLU A CA    1 
ATOM 2305 C C     . GLU B 2 270 ? -27.07400 55.91100  33.80800 1.000 102.73906 ? 270 GLU A C     1 
ATOM 2306 O O     . GLU B 2 270 ? -26.21800 55.83200  32.90300 1.000 102.67883 ? 270 GLU A O     1 
ATOM 2307 C CB    . GLU B 2 270 ? -29.26500 55.17300  32.88000 1.000 115.95673 ? 270 GLU A CB    1 
ATOM 2308 C CG    . GLU B 2 270 ? -30.73900 55.46400  32.62000 1.000 111.62208 ? 270 GLU A CG    1 
ATOM 2309 C CD    . GLU B 2 270 ? -31.48300 54.23300  32.13800 1.000 146.82296 ? 270 GLU A CD    1 
ATOM 2310 O OE1   . GLU B 2 270 ? -31.09600 53.68700  31.08400 1.000 148.57067 ? 270 GLU A OE1   1 
ATOM 2311 O OE2   . GLU B 2 270 ? -32.44400 53.81800  32.81800 1.000 160.14779 ? 270 GLU A OE2   1 
ATOM 2312 N N     . LYS B 2 271 ? -26.84800 55.62500  35.09100 1.000 93.92863  ? 271 LYS A N     1 
ATOM 2313 C CA    . LYS B 2 271 ? -25.53900 55.08200  35.52800 1.000 92.45494  ? 271 LYS A CA    1 
ATOM 2314 C C     . LYS B 2 271 ? -25.71200 53.56600  35.67300 1.000 92.83940  ? 271 LYS A C     1 
ATOM 2315 O O     . LYS B 2 271 ? -26.75800 53.15100  36.21400 1.000 98.12890  ? 271 LYS A O     1 
ATOM 2316 C CB    . LYS B 2 271 ? -25.11500 55.77400  36.82600 1.000 87.20395  ? 271 LYS A CB    1 
ATOM 2317 C CG    . LYS B 2 271 ? -24.88300 57.26800  36.67400 1.000 108.60429 ? 271 LYS A CG    1 
ATOM 2318 C CD    . LYS B 2 271 ? -24.45400 57.95800  37.96300 1.000 111.52661 ? 271 LYS A CD    1 
ATOM 2319 C CE    . LYS B 2 271 ? -24.12100 59.39500  37.72900 1.000 88.61136  ? 271 LYS A CE    1 
ATOM 2320 N NZ    . LYS B 2 271 ? -23.06800 59.53000  36.72100 1.000 104.82861 ? 271 LYS A NZ    1 
ATOM 2321 N N     . ALA B 2 272 ? -24.74600 52.77400  35.20400 1.000 84.25952  ? 272 ALA A N     1 
ATOM 2322 C CA    . ALA B 2 272 ? -24.95300 51.30700  35.22000 1.000 86.02101  ? 272 ALA A CA    1 
ATOM 2323 C C     . ALA B 2 272 ? -23.65900 50.54200  35.48800 1.000 84.94851  ? 272 ALA A C     1 
ATOM 2324 O O     . ALA B 2 272 ? -22.56500 51.09200  35.24500 1.000 93.36597  ? 272 ALA A O     1 
ATOM 2325 C CB    . ALA B 2 272 ? -25.55500 50.87800  33.90500 1.000 86.25277  ? 272 ALA A CB    1 
ATOM 2326 N N     . MET B 2 273 ? -23.78900 49.30500  35.97300 1.000 81.83468  ? 273 MET A N     1 
ATOM 2327 C CA    . MET B 2 273 ? -22.61100 48.43400  36.20700 1.000 80.22813  ? 273 MET A CA    1 
ATOM 2328 C C     . MET B 2 273 ? -22.84700 47.12700  35.43900 1.000 89.27701  ? 273 MET A C     1 
ATOM 2329 O O     . MET B 2 273 ? -23.74200 46.36400  35.84600 1.000 95.68651  ? 273 MET A O     1 
ATOM 2330 C CB    . MET B 2 273 ? -22.44900 48.12700  37.69700 1.000 73.92934  ? 273 MET A CB    1 
ATOM 2331 C CG    . MET B 2 273 ? -22.20100 49.34200  38.56200 1.000 87.42688  ? 273 MET A CG    1 
ATOM 2332 S SD    . MET B 2 273 ? -22.04500 48.88300  40.29900 1.000 69.77032  ? 273 MET A SD    1 
ATOM 2333 C CE    . MET B 2 273 ? -21.54300 50.46500  40.98900 1.000 98.73430  ? 273 MET A CE    1 
ATOM 2334 N N     . ILE B 2 274 ? -22.09100 46.88800  34.36700 1.000 84.91067  ? 274 ILE A N     1 
ATOM 2335 C CA    . ILE B 2 274 ? -22.31600 45.67900  33.52000 1.000 78.82302  ? 274 ILE A CA    1 
ATOM 2336 C C     . ILE B 2 274 ? -21.17500 44.68100  33.76700 1.000 78.94015  ? 274 ILE A C     1 
ATOM 2337 O O     . ILE B 2 274 ? -20.00700 45.11300  33.76700 1.000 87.65486  ? 274 ILE A O     1 
ATOM 2338 C CB    . ILE B 2 274 ? -22.41000 46.07800  32.03700 1.000 82.39814  ? 274 ILE A CB    1 
ATOM 2339 C CG1   . ILE B 2 274 ? -23.37500 47.24300  31.83000 1.000 83.13493  ? 274 ILE A CG1   1 
ATOM 2340 C CG2   . ILE B 2 274 ? -22.77800 44.87600  31.16900 1.000 83.00290  ? 274 ILE A CG2   1 
ATOM 2341 C CD1   . ILE B 2 274 ? -23.46700 47.72100  30.39300 1.000 93.15197  ? 274 ILE A CD1   1 
ATOM 2342 N N     . GLU B 2 275 ? -21.50500 43.40400  33.97500 1.000 84.36827  ? 275 GLU A N     1 
ATOM 2343 C CA    . GLU B 2 275 ? -20.45900 42.36700  34.16500 1.000 80.94374  ? 275 GLU A CA    1 
ATOM 2344 C C     . GLU B 2 275 ? -20.40100 41.47300  32.92000 1.000 84.46199  ? 275 GLU A C     1 
ATOM 2345 O O     . GLU B 2 275 ? -21.32700 40.65900  32.73300 1.000 96.81920  ? 275 GLU A O     1 
ATOM 2346 C CB    . GLU B 2 275 ? -20.70700 41.52000  35.41300 1.000 83.15506  ? 275 GLU A CB    1 
ATOM 2347 C CG    . GLU B 2 275 ? -19.73900 40.34700  35.52700 1.000 89.62485  ? 275 GLU A CG    1 
ATOM 2348 C CD    . GLU B 2 275 ? -19.57400 39.79600  36.92900 1.000 97.83749  ? 275 GLU A CD    1 
ATOM 2349 O OE1   . GLU B 2 275 ? -19.12200 40.56300  37.80200 1.000 109.32764 ? 275 GLU A OE1   1 
ATOM 2350 O OE2   . GLU B 2 275 ? -19.89200 38.61000  37.15000 1.000 112.28834 ? 275 GLU A OE2   1 
ATOM 2351 N N     . ALA B 2 276 ? -19.34900 41.63200  32.11400 1.000 95.19518  ? 276 ALA A N     1 
ATOM 2352 C CA    . ALA B 2 276 ? -19.24500 40.88700  30.84000 1.000 91.64229  ? 276 ALA A CA    1 
ATOM 2353 C C     . ALA B 2 276 ? -18.00000 40.00600  30.82600 1.000 100.86438 ? 276 ALA A C     1 
ATOM 2354 O O     . ALA B 2 276 ? -16.91200 40.50200  31.16900 1.000 105.83551 ? 276 ALA A O     1 
ATOM 2355 C CB    . ALA B 2 276 ? -19.18500 41.87600  29.70600 1.000 91.41095  ? 276 ALA A CB    1 
ATOM 2356 N N     . SER B 2 277 ? -18.15300 38.74600  30.42100 1.000 108.86461 ? 277 SER A N     1 
ATOM 2357 C CA    . SER B 2 277 ? -16.97500 37.85600  30.27300 1.000 116.30215 ? 277 SER A CA    1 
ATOM 2358 C C     . SER B 2 277 ? -16.83900 37.50700  28.78800 1.000 130.52424 ? 277 SER A C     1 
ATOM 2359 O O     . SER B 2 277 ? -16.32800 36.41100  28.47700 1.000 139.42856 ? 277 SER A O     1 
ATOM 2360 C CB    . SER B 2 277 ? -17.10900 36.62600  31.12100 1.000 154.46709 ? 277 SER A CB    1 
ATOM 2361 O OG    . SER B 2 277 ? -15.93900 35.82400  31.03700 1.000 161.34389 ? 277 SER A OG    1 
ATOM 2362 N N     . LEU B 2 278 ? -17.28300 38.41300  27.91200 1.000 131.83609 ? 278 LEU A N     1 
ATOM 2363 C CA    . LEU B 2 278 ? -17.22000 38.17900  26.44700 1.000 126.19066 ? 278 LEU A CA    1 
ATOM 2364 C C     . LEU B 2 278 ? -15.80800 37.71000  26.07900 1.000 125.11792 ? 278 LEU A C     1 
ATOM 2365 O O     . LEU B 2 278 ? -14.83200 38.32100  26.56800 1.000 146.22633 ? 278 LEU A O     1 
ATOM 2366 C CB    . LEU B 2 278 ? -17.57500 39.49200  25.75500 1.000 123.89964 ? 278 LEU A CB    1 
ATOM 2367 C CG    . LEU B 2 278 ? -18.37900 39.40200  24.45500 1.000 140.84817 ? 278 LEU A CG    1 
ATOM 2368 C CD1   . LEU B 2 278 ? -18.69800 40.81300  23.99800 1.000 131.99732 ? 278 LEU A CD1   1 
ATOM 2369 C CD2   . LEU B 2 278 ? -17.63500 38.64900  23.36700 1.000 144.56917 ? 278 LEU A CD2   1 
ATOM 2370 N N     . GLY B 2 279 ? -15.70700 36.68100  25.23700 1.000 118.78127 ? 279 GLY A N     1 
ATOM 2371 C CA    . GLY B 2 279 ? -14.38900 36.13600  24.86500 1.000 124.97339 ? 279 GLY A CA    1 
ATOM 2372 C C     . GLY B 2 279 ? -13.66000 37.06500  23.91800 1.000 131.65320 ? 279 GLY A C     1 
ATOM 2373 O O     . GLY B 2 279 ? -13.68600 36.79900  22.69900 1.000 142.28653 ? 279 GLY A O     1 
ATOM 2374 N N     . SER B 2 280 ? -13.03900 38.12000  24.45000 1.000 135.26921 ? 280 SER A N     1 
ATOM 2375 C CA    . SER B 2 280 ? -12.23500 39.04400  23.60900 1.000 135.12944 ? 280 SER A CA    1 
ATOM 2376 C C     . SER B 2 280 ? -13.07600 39.58300  22.44400 1.000 128.19805 ? 280 SER A C     1 
ATOM 2377 O O     . SER B 2 280 ? -12.68400 39.35300  21.28100 1.000 138.12832 ? 280 SER A O     1 
ATOM 2378 C CB    . SER B 2 280 ? -10.98600 38.36400  23.11200 1.000 145.39837 ? 280 SER A CB    1 
ATOM 2379 O OG    . SER B 2 280 ? -10.22900 37.84100  24.19500 1.000 155.07505 ? 280 SER A OG    1 
ATOM 2380 N N     . GLY B 2 281 ? -14.18600 40.26300  22.74200 1.000 113.98820 ? 281 GLY A N     1 
ATOM 2381 C CA    . GLY B 2 281 ? -15.00100 40.88300  21.67900 1.000 115.36005 ? 281 GLY A CA    1 
ATOM 2382 C C     . GLY B 2 281 ? -15.65500 42.15400  22.18000 1.000 135.00539 ? 281 GLY A C     1 
ATOM 2383 O O     . GLY B 2 281 ? -16.58200 42.64400  21.50300 1.000 132.40292 ? 281 GLY A O     1 
ATOM 2384 N N     . LYS B 2 282 ? -15.19300 42.67700  23.31800 1.000 121.80710 ? 282 LYS A N     1 
ATOM 2385 C CA    . LYS B 2 282 ? -15.82800 43.87200  23.93200 1.000 107.03677 ? 282 LYS A CA    1 
ATOM 2386 C C     . LYS B 2 282 ? -15.47900 45.13800  23.13700 1.000 103.64306 ? 282 LYS A C     1 
ATOM 2387 O O     . LYS B 2 282 ? -16.34200 46.03500  23.05100 1.000 95.40626  ? 282 LYS A O     1 
ATOM 2388 C CB    . LYS B 2 282 ? -15.35700 43.97900  25.38500 1.000 105.98864 ? 282 LYS A CB    1 
ATOM 2389 C CG    . LYS B 2 282 ? -15.58800 42.72500  26.21400 1.000 118.87724 ? 282 LYS A CG    1 
ATOM 2390 C CD    . LYS B 2 282 ? -15.11200 42.84400  27.65600 1.000 104.06140 ? 282 LYS A CD    1 
ATOM 2391 C CE    . LYS B 2 282 ? -15.29200 41.57000  28.41600 1.000 118.62440 ? 282 LYS A CE    1 
ATOM 2392 N NZ    . LYS B 2 282 ? -14.86600 41.71400  29.81000 1.000 109.62916 ? 282 LYS A NZ    1 
ATOM 2393 N N     . SER B 2 283 ? -14.27200 45.20100  22.57500 1.000 113.09203 ? 283 SER A N     1 
ATOM 2394 C CA    . SER B 2 283 ? -13.82600 46.43200  21.87100 1.000 113.19621 ? 283 SER A CA    1 
ATOM 2395 C C     . SER B 2 283 ? -14.85600 46.84300  20.81400 1.000 121.91459 ? 283 SER A C     1 
ATOM 2396 O O     . SER B 2 283 ? -15.31500 48.00500  20.85500 1.000 110.79694 ? 283 SER A O     1 
ATOM 2397 C CB    . SER B 2 283 ? -12.47800 46.22400  21.24300 1.000 115.44886 ? 283 SER A CB    1 
ATOM 2398 O OG    . SER B 2 283 ? -11.53000 45.78400  22.20500 1.000 146.38249 ? 283 SER A OG    1 
ATOM 2399 N N     . LEU B 2 284 ? -15.21300 45.92200  19.91800 1.000 122.39839 ? 284 LEU A N     1 
ATOM 2400 C CA    . LEU B 2 284 ? -16.14400 46.26900  18.81500 1.000 125.50813 ? 284 LEU A CA    1 
ATOM 2401 C C     . LEU B 2 284 ? -17.46300 46.77600  19.41300 1.000 120.32350 ? 284 LEU A C     1 
ATOM 2402 O O     . LEU B 2 284 ? -17.93200 47.84800  18.99000 1.000 117.28081 ? 284 LEU A O     1 
ATOM 2403 C CB    . LEU B 2 284 ? -16.36200 45.05400  17.91500 1.000 123.78054 ? 284 LEU A CB    1 
ATOM 2404 C CG    . LEU B 2 284 ? -17.11800 45.31900  16.61000 1.000 119.82485 ? 284 LEU A CG    1 
ATOM 2405 C CD1   . LEU B 2 284 ? -16.36100 46.31600  15.75100 1.000 124.67359 ? 284 LEU A CD1   1 
ATOM 2406 C CD2   . LEU B 2 284 ? -17.35800 44.02900  15.84800 1.000 120.33306 ? 284 LEU A CD2   1 
ATOM 2407 N N     . ALA B 2 285 ? -18.01700 46.04800  20.38300 1.000 117.51977 ? 285 ALA A N     1 
ATOM 2408 C CA    . ALA B 2 285 ? -19.31800 46.44300  20.97000 1.000 118.90393 ? 285 ALA A CA    1 
ATOM 2409 C C     . ALA B 2 285 ? -19.21900 47.87100  21.50400 1.000 120.97346 ? 285 ALA A C     1 
ATOM 2410 O O     . ALA B 2 285 ? -20.12000 48.68800  21.21900 1.000 111.84741 ? 285 ALA A O     1 
ATOM 2411 C CB    . ALA B 2 285 ? -19.69900 45.47600  22.06400 1.000 109.03333 ? 285 ALA A CB    1 
ATOM 2412 N N     . TYR B 2 286 ? -18.14400 48.16800  22.23800 1.000 115.22229 ? 286 TYR A N     1 
ATOM 2413 C CA    . TYR B 2 286 ? -18.00000 49.51400  22.84900 1.000 103.37487 ? 286 TYR A CA    1 
ATOM 2414 C C     . TYR B 2 286 ? -18.04300 50.56400  21.75200 1.000 114.23124 ? 286 TYR A C     1 
ATOM 2415 O O     . TYR B 2 286 ? -18.87400 51.49300  21.82600 1.000 118.66362 ? 286 TYR A O     1 
ATOM 2416 C CB    . TYR B 2 286 ? -16.67400 49.64700  23.60000 1.000 111.67723 ? 286 TYR A CB    1 
ATOM 2417 C CG    . TYR B 2 286 ? -16.45000 48.69400  24.76500 1.000 121.27830 ? 286 TYR A CG    1 
ATOM 2418 C CD1   . TYR B 2 286 ? -17.51600 48.14900  25.46900 1.000 106.20415 ? 286 TYR A CD1   1 
ATOM 2419 C CD2   . TYR B 2 286 ? -15.16600 48.35900  25.17400 1.000 120.64794 ? 286 TYR A CD2   1 
ATOM 2420 C CE1   . TYR B 2 286 ? -17.31100 47.28600  26.53100 1.000 98.96536  ? 286 TYR A CE1   1 
ATOM 2421 C CE2   . TYR B 2 286 ? -14.94700 47.50200  26.23900 1.000 116.45566 ? 286 TYR A CE2   1 
ATOM 2422 C CZ    . TYR B 2 286 ? -16.02300 46.96500  26.92000 1.000 106.45147 ? 286 TYR A CZ    1 
ATOM 2423 O OH    . TYR B 2 286 ? -15.81200 46.11800  27.96800 1.000 123.39430 ? 286 TYR A OH    1 
ATOM 2424 N N     . LEU B 2 287 ? -17.17800 50.42200  20.74500 1.000 115.39063 ? 287 LEU A N     1 
ATOM 2425 C CA    . LEU B 2 287 ? -17.10500 51.47200  19.69400 1.000 121.74111 ? 287 LEU A CA    1 
ATOM 2426 C C     . LEU B 2 287 ? -18.44400 51.51500  18.93900 1.000 129.00025 ? 287 LEU A C     1 
ATOM 2427 O O     . LEU B 2 287 ? -18.94300 52.62900  18.68500 1.000 130.20995 ? 287 LEU A O     1 
ATOM 2428 C CB    . LEU B 2 287 ? -15.91000 51.27400  18.75700 1.000 116.29019 ? 287 LEU A CB    1 
ATOM 2429 C CG    . LEU B 2 287 ? -15.79600 49.93200  18.03000 1.000 131.50635 ? 287 LEU A CG    1 
ATOM 2430 C CD1   . LEU B 2 287 ? -16.35600 50.02200  16.62100 1.000 137.17738 ? 287 LEU A CD1   1 
ATOM 2431 C CD2   . LEU B 2 287 ? -14.34800 49.47700  17.99600 1.000 123.87204 ? 287 LEU A CD2   1 
ATOM 2432 N N     . LEU B 2 288 ? -19.00100 50.34700  18.61400 1.000 121.96434 ? 288 LEU A N     1 
ATOM 2433 C CA    . LEU B 2 288 ? -20.27300 50.30800  17.85000 1.000 114.22620 ? 288 LEU A CA    1 
ATOM 2434 C C     . LEU B 2 288 ? -21.30200 51.17100  18.59200 1.000 121.73876 ? 288 LEU A C     1 
ATOM 2435 O O     . LEU B 2 288 ? -21.95600 52.00400  17.93700 1.000 130.87489 ? 288 LEU A O     1 
ATOM 2436 C CB    . LEU B 2 288 ? -20.76200 48.87400  17.66600 1.000 129.78008 ? 288 LEU A CB    1 
ATOM 2437 C CG    . LEU B 2 288 ? -20.02000 48.04700  16.61100 1.000 123.82884 ? 288 LEU A CG    1 
ATOM 2438 C CD1   . LEU B 2 288 ? -20.62900 46.66300  16.48400 1.000 119.84474 ? 288 LEU A CD1   1 
ATOM 2439 C CD2   . LEU B 2 288 ? -20.02300 48.75900  15.27100 1.000 122.47435 ? 288 LEU A CD2   1 
ATOM 2440 N N     . ALA B 2 289 ? -21.41700 50.98400  19.90800 1.000 110.23841 ? 289 ALA A N     1 
ATOM 2441 C CA    . ALA B 2 289 ? -22.41300 51.74900  20.69300 1.000 109.92697 ? 289 ALA A CA    1 
ATOM 2442 C C     . ALA B 2 289 ? -22.08500 53.23800  20.61000 1.000 125.11878 ? 289 ALA A C     1 
ATOM 2443 O O     . ALA B 2 289 ? -23.00700 54.06000  20.43100 1.000 127.55057 ? 289 ALA A O     1 
ATOM 2444 C CB    . ALA B 2 289 ? -22.41300 51.26600  22.12100 1.000 108.95809 ? 289 ALA A CB    1 
ATOM 2445 N N     . ALA B 2 290 ? -20.79900 53.56800  20.71500 1.000 125.74286 ? 290 ALA A N     1 
ATOM 2446 C CA    . ALA B 2 290 ? -20.38700 54.98900  20.69700 1.000 125.38567 ? 290 ALA A CA    1 
ATOM 2447 C C     . ALA B 2 290 ? -20.75600 55.61600  19.35500 1.000 122.46126 ? 290 ALA A C     1 
ATOM 2448 O O     . ALA B 2 290 ? -21.42200 56.66800  19.33700 1.000 113.22160 ? 290 ALA A O     1 
ATOM 2449 C CB    . ALA B 2 290 ? -18.90400 55.08100  20.95300 1.000 126.99616 ? 290 ALA A CB    1 
ATOM 2450 N N     . LEU B 2 291 ? -20.31400 54.99300  18.26200 1.000 117.85885 ? 291 LEU A N     1 
ATOM 2451 C CA    . LEU B 2 291 ? -20.58100 55.56900  16.92000 1.000 121.75590 ? 291 LEU A CA    1 
ATOM 2452 C C     . LEU B 2 291 ? -22.09200 55.50900  16.66600 1.000 138.53058 ? 291 LEU A C     1 
ATOM 2453 O O     . LEU B 2 291 ? -22.60100 56.36700  15.92000 1.000 143.34700 ? 291 LEU A O     1 
ATOM 2454 C CB    . LEU B 2 291 ? -19.77700 54.85900  15.83000 1.000 120.54102 ? 291 LEU A CB    1 
ATOM 2455 C CG    . LEU B 2 291 ? -20.07000 53.37400  15.60100 1.000 134.30708 ? 291 LEU A CG    1 
ATOM 2456 C CD1   . LEU B 2 291 ? -21.12300 53.18500  14.52500 1.000 157.32454 ? 291 LEU A CD1   1 
ATOM 2457 C CD2   . LEU B 2 291 ? -18.79100 52.64900  15.22400 1.000 132.08573 ? 291 LEU A CD2   1 
ATOM 2458 N N     . MET B 2 292 ? -22.77400 54.52700  17.25800 1.000 127.21310 ? 292 MET A N     1 
ATOM 2459 C CA    . MET B 2 292 ? -24.25000 54.48200  17.11300 1.000 131.34104 ? 292 MET A CA    1 
ATOM 2460 C C     . MET B 2 292 ? -24.82900 55.65900  17.90200 1.000 135.10830 ? 292 MET A C     1 
ATOM 2461 O O     . MET B 2 292 ? -25.73700 56.33400  17.37900 1.000 152.62727 ? 292 MET A O     1 
ATOM 2462 C CB    . MET B 2 292 ? -24.84200 53.16400  17.61800 1.000 123.20693 ? 292 MET A CB    1 
ATOM 2463 C CG    . MET B 2 292 ? -26.26300 52.94300  17.15100 1.000 128.71683 ? 292 MET A CG    1 
ATOM 2464 S SD    . MET B 2 292 ? -26.40100 53.06200  15.35600 1.000 114.94403 ? 292 MET A SD    1 
ATOM 2465 C CE    . MET B 2 292 ? -28.18000 53.27400  15.20800 1.000 145.09331 ? 292 MET A CE    1 
ATOM 2466 N N     . TYR B 2 293 ? -24.30500 55.90400  19.10300 1.000 124.79003 ? 293 TYR A N     1 
ATOM 2467 C CA    . TYR B 2 293 ? -24.76200 57.10000  19.85200 1.000 128.58049 ? 293 TYR A CA    1 
ATOM 2468 C C     . TYR B 2 293 ? -24.56200 58.26400  18.90800 1.000 139.78204 ? 293 TYR A C     1 
ATOM 2469 O O     . TYR B 2 293 ? -25.51400 59.02700  18.66900 1.000 147.00847 ? 293 TYR A O     1 
ATOM 2470 C CB    . TYR B 2 293 ? -23.94100 57.21200  21.13900 1.000 119.47866 ? 293 TYR A CB    1 
ATOM 2471 C CG    . TYR B 2 293 ? -24.49700 58.11700  22.22900 1.000 112.17477 ? 293 TYR A CG    1 
ATOM 2472 C CD1   . TYR B 2 293 ? -25.86400 58.29000  22.39900 1.000 122.49949 ? 293 TYR A CD1   1 
ATOM 2473 C CD2   . TYR B 2 293 ? -23.64800 58.78800  23.10000 1.000 112.25444 ? 293 TYR A CD2   1 
ATOM 2474 C CE1   . TYR B 2 293 ? -26.36700 59.10700  23.39800 1.000 138.45965 ? 293 TYR A CE1   1 
ATOM 2475 C CE2   . TYR B 2 293 ? -24.13700 59.60800  24.10100 1.000 105.66477 ? 293 TYR A CE2   1 
ATOM 2476 C CZ    . TYR B 2 293 ? -25.50200 59.76700  24.25100 1.000 123.80373 ? 293 TYR A CZ    1 
ATOM 2477 O OH    . TYR B 2 293 ? -25.98800 60.57500  25.23700 1.000 131.15599 ? 293 TYR A OH    1 
ATOM 2478 N N     . ASN B 2 294 ? -23.37300 58.33900  18.30900 1.000 132.85363 ? 294 ASN A N     1 
ATOM 2479 C CA    . ASN B 2 294 ? -23.05600 59.44000  17.36300 1.000 148.64108 ? 294 ASN A CA    1 
ATOM 2480 C C     . ASN B 2 294 ? -24.14900 59.56300  16.30800 1.000 155.23791 ? 294 ASN A C     1 
ATOM 2481 O O     . ASN B 2 294 ? -24.82200 60.61500  16.26200 1.000 155.19130 ? 294 ASN A O     1 
ATOM 2482 C CB    . ASN B 2 294 ? -21.71500 59.19900  16.67900 1.000 155.63933 ? 294 ASN A CB    1 
ATOM 2483 C CG    . ASN B 2 294 ? -21.55700 59.99700  15.40600 1.000 165.97271 ? 294 ASN A CG    1 
ATOM 2484 O OD1   . ASN B 2 294 ? -21.62600 61.23000  15.42900 1.000 162.69144 ? 294 ASN A OD1   1 
ATOM 2485 N ND2   . ASN B 2 294 ? -21.34800 59.31600  14.28900 1.000 171.83598 ? 294 ASN A ND2   1 
ATOM 2486 N N     . ILE B 2 295 ? -24.32200 58.51600  15.50500 1.000 140.91619 ? 295 ILE A N     1 
ATOM 2487 C CA    . ILE B 2 295 ? -25.31200 58.57900  14.39600 1.000 144.67671 ? 295 ILE A CA    1 
ATOM 2488 C C     . ILE B 2 295 ? -26.65200 59.02600  14.98900 1.000 146.10126 ? 295 ILE A C     1 
ATOM 2489 O O     . ILE B 2 295 ? -27.30500 59.89900  14.38000 1.000 154.83958 ? 295 ILE A O     1 
ATOM 2490 C CB    . ILE B 2 295 ? -25.40700 57.20400  13.71600 1.000 150.60622 ? 295 ILE A CB    1 
ATOM 2491 C CG1   . ILE B 2 295 ? -24.13200 56.88100  12.93800 1.000 148.74363 ? 295 ILE A CG1   1 
ATOM 2492 C CG2   . ILE B 2 295 ? -26.65100 57.10600  12.83400 1.000 170.12983 ? 295 ILE A CG2   1 
ATOM 2493 C CD1   . ILE B 2 295 ? -24.04500 55.44100  12.46700 1.000 165.61334 ? 295 ILE A CD1   1 
ATOM 2494 N N     . GLU B 2 296 ? -27.02000 58.47900  16.14800 1.000 148.42776 ? 296 GLU A N     1 
ATOM 2495 C CA    . GLU B 2 296 ? -28.33800 58.80200  16.75100 1.000 161.84071 ? 296 GLU A CA    1 
ATOM 2496 C C     . GLU B 2 296 ? -28.25000 60.16000  17.46300 1.000 162.45674 ? 296 GLU A C     1 
ATOM 2497 O O     . GLU B 2 296 ? -28.46400 60.20100  18.69200 1.000 169.20170 ? 296 GLU A O     1 
ATOM 2498 C CB    . GLU B 2 296 ? -28.76400 57.67100  17.68900 1.000 153.41453 ? 296 GLU A CB    1 
ATOM 2499 C CG    . GLU B 2 296 ? -30.22500 57.75800  18.12100 1.000 156.56600 ? 296 GLU A CG    1 
ATOM 2500 C CD    . GLU B 2 296 ? -31.20600 57.88100  16.96900 1.000 168.59763 ? 296 GLU A CD    1 
ATOM 2501 O OE1   . GLU B 2 296 ? -31.24000 56.96500  16.12100 1.000 175.66213 ? 296 GLU A OE1   1 
ATOM 2502 O OE2   . GLU B 2 296 ? -31.93500 58.89400  16.92000 1.000 164.41855 ? 296 GLU A OE2   1 
ATOM 2503 N N     . THR B 2 297 ? -27.91800 61.22300  16.72400 1.000 154.83347 ? 297 THR A N     1 
ATOM 2504 C CA    . THR B 2 297 ? -27.88000 62.57900  17.31300 1.000 166.07730 ? 297 THR A CA    1 
ATOM 2505 C C     . THR B 2 297 ? -27.18600 62.51600  18.65400 1.000 158.21120 ? 297 THR A C     1 
ATOM 2506 O O     . THR B 2 297 ? -27.62900 63.22100  19.58600 1.000 143.81354 ? 297 THR A O     1 
ATOM 2507 C CB    . THR B 2 297 ? -29.30100 63.13000  17.43300 1.000 167.03232 ? 297 THR A CB    1 
ATOM 2508 O OG1   . THR B 2 297 ? -29.94100 62.37700  18.46000 1.000 165.25876 ? 297 THR A OG1   1 
ATOM 2509 C CG2   . THR B 2 297 ? -30.08200 63.00500  16.13700 1.000 161.85102 ? 297 THR A CG2   1 
ATOM 2510 N N     . GLY B 2 298 ? -26.13100 61.70600  18.75700 1.000 147.08368 ? 298 GLY A N     1 
ATOM 2511 C CA    . GLY B 2 298 ? -25.42100 61.54900  20.03700 1.000 140.13159 ? 298 GLY A CA    1 
ATOM 2512 C C     . GLY B 2 298 ? -24.30200 62.55600  20.16000 1.000 155.63063 ? 298 GLY A C     1 
ATOM 2513 O O     . GLY B 2 298 ? -24.15100 63.39400  19.24700 1.000 147.39093 ? 298 GLY A O     1 
ATOM 2514 N N     . LYS B 2 299 ? -23.53400 62.47500  21.24500 1.000 134.98056 ? 299 LYS A N     1 
ATOM 2515 C CA    . LYS B 2 299 ? -22.46900 63.47500  21.48200 1.000 136.69434 ? 299 LYS A CA    1 
ATOM 2516 C C     . LYS B 2 299 ? -21.15100 62.75700  21.78500 1.000 141.68369 ? 299 LYS A C     1 
ATOM 2517 O O     . LYS B 2 299 ? -21.05900 61.54000  21.52400 1.000 135.77358 ? 299 LYS A O     1 
ATOM 2518 C CB    . LYS B 2 299 ? -22.86900 64.35400  22.66800 1.000 147.12720 ? 299 LYS A CB    1 
ATOM 2519 C CG    . LYS B 2 299 ? -22.97800 63.59600  23.98300 1.000 159.27064 ? 299 LYS A CG    1 
ATOM 2520 C CD    . LYS B 2 299 ? -23.19100 64.48400  25.20200 1.000 158.87019 ? 299 LYS A CD    1 
ATOM 2521 C CE    . LYS B 2 299 ? -23.01800 63.71500  26.47100 1.000 151.31113 ? 299 LYS A CE    1 
ATOM 2522 N NZ    . LYS B 2 299 ? -21.66000 63.17500  26.57700 1.000 148.91478 ? 299 LYS A NZ    1 
ATOM 2523 N N     . HIS B 2 300 ? -20.17700 63.49400  22.31700 1.000 150.18160 ? 300 HIS A N     1 
ATOM 2524 C CA    . HIS B 2 300 ? -18.85400 62.90900  22.64900 1.000 142.91483 ? 300 HIS A CA    1 
ATOM 2525 C C     . HIS B 2 300 ? -19.03900 61.77500  23.65900 1.000 129.92933 ? 300 HIS A C     1 
ATOM 2526 O O     . HIS B 2 300 ? -19.85100 61.92100  24.59700 1.000 125.50482 ? 300 HIS A O     1 
ATOM 2527 C CB    . HIS B 2 300 ? -17.94400 64.01200  23.19600 1.000 119.79702 ? 300 HIS A CB    1 
ATOM 2528 C CG    . HIS B 2 300 ? -18.69300 65.00400  24.01800 1.000 134.95299 ? 300 HIS A CG    1 
ATOM 2529 N ND1   . HIS B 2 300 ? -19.08200 64.74700  25.31400 1.000 142.37230 ? 300 HIS A ND1   1 
ATOM 2530 C CD2   . HIS B 2 300 ? -19.17500 66.21500  23.71900 1.000 136.12885 ? 300 HIS A CD2   1 
ATOM 2531 C CE1   . HIS B 2 300 ? -19.75400 65.78800  25.78200 1.000 144.66824 ? 300 HIS A CE1   1 
ATOM 2532 N NE2   . HIS B 2 300 ? -19.81600 66.69400  24.83200 1.000 153.25983 ? 300 HIS A NE2   1 
ATOM 2533 N N     . VAL B 2 301 ? -18.31400 60.67100  23.46900 1.000 113.54930 ? 301 VAL A N     1 
ATOM 2534 C CA    . VAL B 2 301 ? -18.36500 59.54300  24.44600 1.000 115.48379 ? 301 VAL A CA    1 
ATOM 2535 C C     . VAL B 2 301 ? -16.92400 59.22700  24.87400 1.000 125.24974 ? 301 VAL A C     1 
ATOM 2536 O O     . VAL B 2 301 ? -16.04100 59.22300  23.99300 1.000 129.54636 ? 301 VAL A O     1 
ATOM 2537 C CB    . VAL B 2 301 ? -19.03800 58.29400  23.85200 1.000 123.60724 ? 301 VAL A CB    1 
ATOM 2538 C CG1   . VAL B 2 301 ? -19.41900 57.29000  24.93200 1.000 117.13439 ? 301 VAL A CG1   1 
ATOM 2539 C CG2   . VAL B 2 301 ? -20.24800 58.64800  22.99700 1.000 142.64354 ? 301 VAL A CG2   1 
ATOM 2540 N N     . MET B 2 302 ? -16.69400 58.97600  26.16500 1.000 120.66111 ? 302 MET A N     1 
ATOM 2541 C CA    . MET B 2 302 ? -15.33000 58.67600  26.66900 1.000 114.88937 ? 302 MET A CA    1 
ATOM 2542 C C     . MET B 2 302 ? -15.21900 57.17600  26.95300 1.000 113.85577 ? 302 MET A C     1 
ATOM 2543 O O     . MET B 2 302 ? -16.27000 56.53100  27.09700 1.000 121.38562 ? 302 MET A O     1 
ATOM 2544 C CB    . MET B 2 302 ? -15.04800 59.44200  27.96400 1.000 109.65643 ? 302 MET A CB    1 
ATOM 2545 C CG    . MET B 2 302 ? -13.58100 59.64300  28.27300 1.000 122.75362 ? 302 MET A CG    1 
ATOM 2546 S SD    . MET B 2 302 ? -12.73400 60.54900  26.96600 1.000 138.23136 ? 302 MET A SD    1 
ATOM 2547 C CE    . MET B 2 302 ? -12.65700 62.18900  27.69700 1.000 124.44940 ? 302 MET A CE    1 
ATOM 2548 N N     . ILE B 2 303 ? -13.99800 56.65000  27.02400 1.000 94.82909  ? 303 ILE A N     1 
ATOM 2549 C CA    . ILE B 2 303 ? -13.81300 55.21500  27.39200 1.000 96.21073  ? 303 ILE A CA    1 
ATOM 2550 C C     . ILE B 2 303 ? -12.44800 55.05100  28.07800 1.000 91.17942  ? 303 ILE A C     1 
ATOM 2551 O O     . ILE B 2 303 ? -11.41600 55.24700  27.40500 1.000 98.31241  ? 303 ILE A O     1 
ATOM 2552 C CB    . ILE B 2 303 ? -13.96800 54.30700  26.15800 1.000 96.83788  ? 303 ILE A CB    1 
ATOM 2553 C CG1   . ILE B 2 303 ? -13.73200 52.83600  26.50000 1.000 103.85846 ? 303 ILE A CG1   1 
ATOM 2554 C CG2   . ILE B 2 303 ? -13.07100 54.77400  25.01300 1.000 105.96388 ? 303 ILE A CG2   1 
ATOM 2555 C CD1   . ILE B 2 303 ? -14.00600 51.88500  25.35000 1.000 132.37915 ? 303 ILE A CD1   1 
ATOM 2556 N N     . SER B 2 304 ? -12.45500 54.72700  29.37500 1.000 93.92911  ? 304 SER A N     1 
ATOM 2557 C CA    . SER B 2 304 ? -11.18600 54.54200  30.10900 1.000 85.13011  ? 304 SER A CA    1 
ATOM 2558 C C     . SER B 2 304 ? -10.73000 53.09700  29.96500 1.000 80.68296  ? 304 SER A C     1 
ATOM 2559 O O     . SER B 2 304 ? -11.56800 52.23400  29.78800 1.000 88.85573  ? 304 SER A O     1 
ATOM 2560 C CB    . SER B 2 304 ? -11.31800 54.93700  31.54000 1.000 89.02910  ? 304 SER A CB    1 
ATOM 2561 O OG    . SER B 2 304 ? -10.45500 54.16300  32.35900 1.000 100.97273 ? 304 SER A OG    1 
ATOM 2562 N N     . THR B 2 305 ? -9.43900  52.80900  30.08600 1.000 87.56455  ? 305 THR A N     1 
ATOM 2563 C CA    . THR B 2 305 ? -9.00600  51.39900  29.94300 1.000 83.49715  ? 305 THR A CA    1 
ATOM 2564 C C     . THR B 2 305 ? -7.91600  51.07900  30.95600 1.000 93.47884  ? 305 THR A C     1 
ATOM 2565 O O     . THR B 2 305 ? -7.00800  51.88200  31.07800 1.000 93.64394  ? 305 THR A O     1 
ATOM 2566 C CB    . THR B 2 305 ? -8.29500  51.20600  28.61300 1.000 89.95925  ? 305 THR A CB    1 
ATOM 2567 O OG1   . THR B 2 305 ? -7.29600  52.21700  28.66700 1.000 107.92380 ? 305 THR A OG1   1 
ATOM 2568 C CG2   . THR B 2 305 ? -9.19900  51.44300  27.42900 1.000 92.50194  ? 305 THR A CG2   1 
ATOM 2569 N N     . ASN B 2 306 ? -7.99600  49.91700  31.59700 1.000 93.25275  ? 306 ASN A N     1 
ATOM 2570 C CA    . ASN B 2 306 ? -6.99600  49.51600  32.61600 1.000 91.28902  ? 306 ASN A CA    1 
ATOM 2571 C C     . ASN B 2 306 ? -5.61800  49.33200  31.99900 1.000 95.63181  ? 306 ASN A C     1 
ATOM 2572 O O     . ASN B 2 306 ? -4.66300  49.84300  32.56100 1.000 105.22848 ? 306 ASN A O     1 
ATOM 2573 C CB    . ASN B 2 306 ? -7.31500  48.15900  33.22600 1.000 74.31336  ? 306 ASN A CB    1 
ATOM 2574 C CG    . ASN B 2 306 ? -6.16300  47.64000  34.04800 1.000 83.49583  ? 306 ASN A CG    1 
ATOM 2575 O OD1   . ASN B 2 306 ? -5.37100  48.41500  34.55500 1.000 93.14103  ? 306 ASN A OD1   1 
ATOM 2576 N ND2   . ASN B 2 306 ? -6.06100  46.33400  34.18500 1.000 97.65440  ? 306 ASN A ND2   1 
ATOM 2577 N N     . THR B 2 307 ? -5.54800  48.67800  30.83900 1.000 104.50143 ? 307 THR A N     1 
ATOM 2578 C CA    . THR B 2 307 ? -4.26100  48.53200  30.12900 1.000 101.08073 ? 307 THR A CA    1 
ATOM 2579 C C     . THR B 2 307 ? -4.29800  49.41300  28.90300 1.000 111.45458 ? 307 THR A C     1 
ATOM 2580 O O     . THR B 2 307 ? -5.25700  50.19800  28.77400 1.000 107.00683 ? 307 THR A O     1 
ATOM 2581 C CB    . THR B 2 307 ? -4.02900  47.07200  29.75600 1.000 101.63743 ? 307 THR A CB    1 
ATOM 2582 O OG1   . THR B 2 307 ? -4.97500  46.80500  28.72600 1.000 128.24630 ? 307 THR A OG1   1 
ATOM 2583 C CG2   . THR B 2 307 ? -4.24200  46.13200  30.92800 1.000 114.17146 ? 307 THR A CG2   1 
ATOM 2584 N N     . LYS B 2 308 ? -3.29800  49.29100  28.02900 1.000 124.56213 ? 308 LYS A N     1 
ATOM 2585 C CA    . LYS B 2 308 ? -3.22000  50.16500  26.83000 1.000 121.41426 ? 308 LYS A CA    1 
ATOM 2586 C C     . LYS B 2 308 ? -3.19200  49.29800  25.56500 1.000 122.21806 ? 308 LYS A C     1 
ATOM 2587 O O     . LYS B 2 308 ? -3.39500  49.84700  24.46400 1.000 122.15552 ? 308 LYS A O     1 
ATOM 2588 C CB    . LYS B 2 308 ? -1.98400  51.06000  26.95200 1.000 106.13759 ? 308 LYS A CB    1 
ATOM 2589 C CG    . LYS B 2 308 ? -2.13200  52.16800  27.98600 1.000 121.06487 ? 308 LYS A CG    1 
ATOM 2590 C CD    . LYS B 2 308 ? -0.81700  52.70900  28.53200 1.000 145.22321 ? 308 LYS A CD    1 
ATOM 2591 C CE    . LYS B 2 308 ? -0.11700  51.71300  29.40100 1.000 145.06577 ? 308 LYS A CE    1 
ATOM 2592 N NZ    . LYS B 2 308 ? 1.08200   52.28100  30.02400 1.000 151.46283 ? 308 LYS A NZ    1 
ATOM 2593 N N     . LEU B 2 309 ? -2.95500  47.99500  25.72100 1.000 117.78689 ? 309 LEU A N     1 
ATOM 2594 C CA    . LEU B 2 309 ? -2.98200  47.08300  24.55000 1.000 130.08510 ? 309 LEU A CA    1 
ATOM 2595 C C     . LEU B 2 309 ? -4.38000  47.14700  23.92700 1.000 125.39594 ? 309 LEU A C     1 
ATOM 2596 O O     . LEU B 2 309 ? -4.47600  47.29800  22.69200 1.000 139.50657 ? 309 LEU A O     1 
ATOM 2597 C CB    . LEU B 2 309 ? -2.62800  45.66800  24.99400 1.000 135.33769 ? 309 LEU A CB    1 
ATOM 2598 C CG    . LEU B 2 309 ? -1.24100  45.49600  25.62100 1.000 138.04961 ? 309 LEU A CG    1 
ATOM 2599 C CD1   . LEU B 2 309 ? -0.96800  44.04000  25.95300 1.000 130.89089 ? 309 LEU A CD1   1 
ATOM 2600 C CD2   . LEU B 2 309 ? -0.16100  46.05000  24.70700 1.000 114.90776 ? 309 LEU A CD2   1 
ATOM 2601 N N     . LEU B 2 310 ? -5.41700  47.05700  24.75900 1.000 120.58139 ? 310 LEU A N     1 
ATOM 2602 C CA    . LEU B 2 310 ? -6.80600  47.16500  24.25200 1.000 141.15128 ? 310 LEU A CA    1 
ATOM 2603 C C     . LEU B 2 310 ? -6.96700  48.54400  23.60500 1.000 134.54646 ? 310 LEU A C     1 
ATOM 2604 O O     . LEU B 2 310 ? -7.53600  48.62400  22.49800 1.000 142.09701 ? 310 LEU A O     1 
ATOM 2605 C CB    . LEU B 2 310 ? -7.77700  46.98500  25.41500 1.000 134.03898 ? 310 LEU A CB    1 
ATOM 2606 C CG    . LEU B 2 310 ? -7.45200  45.84800  26.38800 1.000 139.68744 ? 310 LEU A CG    1 
ATOM 2607 C CD1   . LEU B 2 310 ? -8.36000  45.90400  27.60400 1.000 124.11843 ? 310 LEU A CD1   1 
ATOM 2608 C CD2   . LEU B 2 310 ? -7.56400  44.49900  25.69900 1.000 143.90351 ? 310 LEU A CD2   1 
ATOM 2609 N N     . GLN B 2 311 ? -6.45900  49.57900  24.27100 1.000 124.45850 ? 311 GLN A N     1 
ATOM 2610 C CA    . GLN B 2 311 ? -6.58200  50.95700  23.74400 1.000 128.73137 ? 311 GLN A CA    1 
ATOM 2611 C C     . GLN B 2 311 ? -6.08200  50.96500  22.29800 1.000 123.18381 ? 311 GLN A C     1 
ATOM 2612 O O     . GLN B 2 311 ? -6.83900  51.38800  21.40500 1.000 127.23820 ? 311 GLN A O     1 
ATOM 2613 C CB    . GLN B 2 311 ? -5.74700  51.86300  24.64600 1.000 120.77658 ? 311 GLN A CB    1 
ATOM 2614 C CG    . GLN B 2 311 ? -5.67200  53.31800  24.20100 1.000 118.46171 ? 311 GLN A CG    1 
ATOM 2615 C CD    . GLN B 2 311 ? -4.97200  54.20100  25.21000 1.000 119.15667 ? 311 GLN A CD    1 
ATOM 2616 O OE1   . GLN B 2 311 ? -3.79700  54.00000  25.53800 1.000 118.11598 ? 311 GLN A OE1   1 
ATOM 2617 N NE2   . GLN B 2 311 ? -5.69300  55.18700  25.72000 1.000 120.00907 ? 311 GLN A NE2   1 
ATOM 2618 N N     . SER B 2 312 ? -4.86500  50.47200  22.08300 1.000 117.59305 ? 312 SER A N     1 
ATOM 2619 C CA    . SER B 2 312 ? -4.28500  50.47600  20.72000 1.000 129.06520 ? 312 SER A CA    1 
ATOM 2620 C C     . SER B 2 312 ? -5.13200  49.58600  19.80700 1.000 134.34668 ? 312 SER A C     1 
ATOM 2621 O O     . SER B 2 312 ? -5.50200  50.04700  18.71300 1.000 146.59592 ? 312 SER A O     1 
ATOM 2622 C CB    . SER B 2 312 ? -2.85500  50.02000  20.74700 1.000 138.66271 ? 312 SER A CB    1 
ATOM 2623 O OG    . SER B 2 312 ? -2.07300  50.85900  21.58500 1.000 141.82601 ? 312 SER A OG    1 
ATOM 2624 N N     . GLN B 2 313 ? -5.45600  48.37500  20.25800 1.000 127.93569 ? 313 GLN A N     1 
ATOM 2625 C CA    . GLN B 2 313 ? -6.20200  47.42600  19.39300 1.000 135.79266 ? 313 GLN A CA    1 
ATOM 2626 C C     . GLN B 2 313 ? -7.39700  48.15000  18.75700 1.000 132.00440 ? 313 GLN A C     1 
ATOM 2627 O O     . GLN B 2 313 ? -7.52800  48.11000  17.52000 1.000 132.98681 ? 313 GLN A O     1 
ATOM 2628 C CB    . GLN B 2 313 ? -6.65600  46.22400  20.22000 1.000 138.44110 ? 313 GLN A CB    1 
ATOM 2629 C CG    . GLN B 2 313 ? -7.38100  45.14900  19.41800 1.000 137.28576 ? 313 GLN A CG    1 
ATOM 2630 C CD    . GLN B 2 313 ? -8.88500  45.29900  19.44100 1.000 146.67443 ? 313 GLN A CD    1 
ATOM 2631 O OE1   . GLN B 2 313 ? -9.43200  46.21000  20.07200 1.000 144.96422 ? 313 GLN A OE1   1 
ATOM 2632 N NE2   . GLN B 2 313 ? -9.57000  44.39800  18.75400 1.000 136.75121 ? 313 GLN A NE2   1 
ATOM 2633 N N     . LEU B 2 314 ? -8.23100  48.78900  19.57300 1.000 127.97274 ? 314 LEU A N     1 
ATOM 2634 C CA    . LEU B 2 314 ? -9.44000  49.44800  19.02400 1.000 133.35854 ? 314 LEU A CA    1 
ATOM 2635 C C     . LEU B 2 314 ? -9.02400  50.72600  18.28400 1.000 131.74437 ? 314 LEU A C     1 
ATOM 2636 O O     . LEU B 2 314 ? -9.77200  51.14900  17.38400 1.000 130.11576 ? 314 LEU A O     1 
ATOM 2637 C CB    . LEU B 2 314 ? -10.42900 49.73800  20.15100 1.000 137.97473 ? 314 LEU A CB    1 
ATOM 2638 C CG    . LEU B 2 314 ? -9.92600  50.62400  21.29600 1.000 132.04425 ? 314 LEU A CG    1 
ATOM 2639 C CD1   . LEU B 2 314 ? -10.24000 52.09200  21.06200 1.000 132.93590 ? 314 LEU A CD1   1 
ATOM 2640 C CD2   . LEU B 2 314 ? -10.49000 50.16400  22.62700 1.000 124.44028 ? 314 LEU A CD2   1 
ATOM 2641 N N     . LEU B 2 315 ? -7.87200  51.30200  18.63500 1.000 141.15194 ? 315 LEU A N     1 
ATOM 2642 C CA    . LEU B 2 315 ? -7.46600  52.60100  18.03600 1.000 142.26423 ? 315 LEU A CA    1 
ATOM 2643 C C     . LEU B 2 315 ? -6.69200  52.38300  16.72900 1.000 139.80004 ? 315 LEU A C     1 
ATOM 2644 O O     . LEU B 2 315 ? -6.92100  53.15600  15.77600 1.000 132.33001 ? 315 LEU A O     1 
ATOM 2645 C CB    . LEU B 2 315 ? -6.62300  53.36100  19.05700 1.000 118.53670 ? 315 LEU A CB    1 
ATOM 2646 C CG    . LEU B 2 315 ? -6.44500  54.86000  18.80300 1.000 111.11826 ? 315 LEU A CG    1 
ATOM 2647 C CD1   . LEU B 2 315 ? -7.79300  55.55800  18.81800 1.000 107.62607 ? 315 LEU A CD1   1 
ATOM 2648 C CD2   . LEU B 2 315 ? -5.52300  55.45500  19.85100 1.000 132.67045 ? 315 LEU A CD2   1 
ATOM 2649 N N     . GLU B 2 316 ? -5.82000  51.37500  16.67900 1.000 139.35842 ? 316 GLU A N     1 
ATOM 2650 C CA    . GLU B 2 316 ? -4.96100  51.20700  15.47900 1.000 137.11405 ? 316 GLU A CA    1 
ATOM 2651 C C     . GLU B 2 316 ? -5.48400  50.08400  14.56800 1.000 134.65216 ? 316 GLU A C     1 
ATOM 2652 O O     . GLU B 2 316 ? -4.84300  49.83900  13.52600 1.000 144.02903 ? 316 GLU A O     1 
ATOM 2653 C CB    . GLU B 2 316 ? -3.52800  50.93200  15.93400 1.000 139.76203 ? 316 GLU A CB    1 
ATOM 2654 C CG    . GLU B 2 316 ? -3.33800  49.54500  16.54000 1.000 145.28191 ? 316 GLU A CG    1 
ATOM 2655 C CD    . GLU B 2 316 ? -1.97200  49.33600  17.16300 1.000 162.07923 ? 316 GLU A CD    1 
ATOM 2656 O OE1   . GLU B 2 316 ? -1.16800  50.29100  17.15000 1.000 166.97536 ? 316 GLU A OE1   1 
ATOM 2657 O OE2   . GLU B 2 316 ? -1.71000  48.22100  17.65900 1.000 161.58492 ? 316 GLU A OE2   1 
ATOM 2658 N N     . LYS B 2 317 ? -6.60600  49.44700  14.91800 1.000 141.44922 ? 317 LYS A N     1 
ATOM 2659 C CA    . LYS B 2 317 ? -7.09000  48.30100  14.10400 1.000 149.06666 ? 317 LYS A CA    1 
ATOM 2660 C C     . LYS B 2 317 ? -8.61300  48.37100  13.91500 1.000 137.28845 ? 317 LYS A C     1 
ATOM 2661 O O     . LYS B 2 317 ? -9.05600  48.56500  12.76200 1.000 137.62664 ? 317 LYS A O     1 
ATOM 2662 C CB    . LYS B 2 317 ? -6.74200  46.96200  14.76500 1.000 139.01192 ? 317 LYS A CB    1 
ATOM 2663 C CG    . LYS B 2 317 ? -5.32600  46.83000  15.30400 1.000 139.98457 ? 317 LYS A CG    1 
ATOM 2664 C CD    . LYS B 2 317 ? -5.11500  45.55500  16.11100 1.000 135.50081 ? 317 LYS A CD    1 
ATOM 2665 C CE    . LYS B 2 317 ? -3.81700  45.56500  16.85200 1.000 138.52803 ? 317 LYS A CE    1 
ATOM 2666 N NZ    . LYS B 2 317 ? -2.68400  45.79800  15.95300 1.000 152.86483 ? 317 LYS A NZ    1 
ATOM 2667 N N     . ASP B 2 318 ? -9.38200  48.21900  14.99600 1.000 129.97590 ? 318 ASP A N     1 
ATOM 2668 C CA    . ASP B 2 318 ? -10.86500 48.15800  14.86600 1.000 143.28111 ? 318 ASP A CA    1 
ATOM 2669 C C     . ASP B 2 318 ? -11.40500 49.42500  14.19900 1.000 145.46106 ? 318 ASP A C     1 
ATOM 2670 O O     . ASP B 2 318 ? -12.17100 49.29200  13.22400 1.000 152.76710 ? 318 ASP A O     1 
ATOM 2671 C CB    . ASP B 2 318 ? -11.53100 47.91700  16.21000 1.000 151.33680 ? 318 ASP A CB    1 
ATOM 2672 C CG    . ASP B 2 318 ? -11.12400 46.63400  16.91700 1.000 164.96861 ? 318 ASP A CG    1 
ATOM 2673 O OD1   . ASP B 2 318 ? -10.26300 45.91200  16.37100 1.000 174.98574 ? 318 ASP A OD1   1 
ATOM 2674 O OD2   . ASP B 2 318 ? -11.67600 46.36400  18.00300 1.000 167.90744 ? 318 ASP A OD2   1 
ATOM 2675 N N     . ILE B 2 319 ? -11.03800 50.60300  14.70500 1.000 134.22081 ? 319 ILE A N     1 
ATOM 2676 C CA    . ILE B 2 319 ? -11.62300 51.85800  14.13900 1.000 143.91313 ? 319 ILE A CA    1 
ATOM 2677 C C     . ILE B 2 319 ? -11.31700 51.90800  12.63200 1.000 147.61149 ? 319 ILE A C     1 
ATOM 2678 O O     . ILE B 2 319 ? -12.27500 52.09000  11.85400 1.000 145.36911 ? 319 ILE A O     1 
ATOM 2679 C CB    . ILE B 2 319 ? -11.12700 53.10900  14.89000 1.000 143.65285 ? 319 ILE A CB    1 
ATOM 2680 C CG1   . ILE B 2 319 ? -11.76500 53.21900  16.27100 1.000 124.94475 ? 319 ILE A CG1   1 
ATOM 2681 C CG2   . ILE B 2 319 ? -11.36500 54.37300  14.06600 1.000 139.84234 ? 319 ILE A CG2   1 
ATOM 2682 C CD1   . ILE B 2 319 ? -13.28200 53.19500  16.25000 1.000 140.39759 ? 319 ILE A CD1   1 
ATOM 2683 N N     . PRO B 2 320 ? -10.05800 51.73300  12.17000 1.000 151.27154 ? 320 PRO A N     1 
ATOM 2684 C CA    . PRO B 2 320 ? -9.78900  51.70200  10.73900 1.000 149.52442 ? 320 PRO A CA    1 
ATOM 2685 C C     . PRO B 2 320 ? -10.67400 50.70700  10.00600 1.000 146.87991 ? 320 PRO A C     1 
ATOM 2686 O O     . PRO B 2 320 ? -11.25300 51.05600  8.95600  1.000 151.35998 ? 320 PRO A O     1 
ATOM 2687 C CB    . PRO B 2 320 ? -8.31500  51.28000  10.70200 1.000 154.52833 ? 320 PRO A CB    1 
ATOM 2688 C CG    . PRO B 2 320 ? -7.73800  51.86000  11.96900 1.000 144.63123 ? 320 PRO A CG    1 
ATOM 2689 C CD    . PRO B 2 320 ? -8.84800  51.65700  12.98100 1.000 140.73913 ? 320 PRO A CD    1 
ATOM 2690 N N     . ALA B 2 321 ? -10.78300 49.49000  10.54300 1.000 147.95855 ? 321 ALA A N     1 
ATOM 2691 C CA    . ALA B 2 321 ? -11.58000 48.43500  9.87300  1.000 157.82983 ? 321 ALA A CA    1 
ATOM 2692 C C     . ALA B 2 321 ? -13.03300 48.89100  9.73700  1.000 150.85311 ? 321 ALA A C     1 
ATOM 2693 O O     . ALA B 2 321 ? -13.67800 48.57900  8.71800  1.000 143.52309 ? 321 ALA A O     1 
ATOM 2694 C CB    . ALA B 2 321 ? -11.47700 47.14400  10.65200 1.000 144.98642 ? 321 ALA A CB    1 
ATOM 2695 N N     . MET B 2 322 ? -13.54200 49.59000  10.75100 1.000 148.72138 ? 322 MET A N     1 
ATOM 2696 C CA    . MET B 2 322 ? -14.93800 50.09500  10.70000 1.000 145.13212 ? 322 MET A CA    1 
ATOM 2697 C C     . MET B 2 322 ? -15.01700 51.28800  9.73700  1.000 160.46590 ? 322 MET A C     1 
ATOM 2698 O O     . MET B 2 322 ? -16.08400 51.48000  9.12600  1.000 171.97107 ? 322 MET A O     1 
ATOM 2699 C CB    . MET B 2 322 ? -15.42200 50.51200  12.09200 1.000 150.27168 ? 322 MET A CB    1 
ATOM 2700 C CG    . MET B 2 322 ? -15.72800 49.34700  13.01400 1.000 157.41807 ? 322 MET A CG    1 
ATOM 2701 S SD    . MET B 2 322 ? -17.19100 48.41200  12.52200 1.000 167.74422 ? 322 MET A SD    1 
ATOM 2702 C CE    . MET B 2 322 ? -16.51500 47.23300  11.34400 1.000 146.26804 ? 322 MET A CE    1 
ATOM 2703 N N     . ASN B 2 323 ? -13.93000 52.05200  9.60800  1.000 161.92479 ? 323 ASN A N     1 
ATOM 2704 C CA    . ASN B 2 323 ? -13.96000 53.26600  8.74800  1.000 153.34551 ? 323 ASN A CA    1 
ATOM 2705 C C     . ASN B 2 323 ? -14.43400 52.86500  7.34900  1.000 166.41342 ? 323 ASN A C     1 
ATOM 2706 O O     . ASN B 2 323 ? -15.36300 53.51900  6.82700  1.000 172.22608 ? 323 ASN A O     1 
ATOM 2707 C CB    . ASN B 2 323 ? -12.59900 53.94700  8.68700  1.000 148.51524 ? 323 ASN A CB    1 
ATOM 2708 C CG    . ASN B 2 323 ? -12.18300 54.52600  10.01700 1.000 158.95562 ? 323 ASN A CG    1 
ATOM 2709 O OD1   . ASN B 2 323 ? -11.03700 54.96000  10.17100 1.000 165.74036 ? 323 ASN A OD1   1 
ATOM 2710 N ND2   . ASN B 2 323 ? -13.08100 54.51800  10.99100 1.000 161.20891 ? 323 ASN A ND2   1 
ATOM 2711 N N     . GLU B 2 324 ? -13.83000 51.81900  6.77600  1.000 164.23794 ? 324 GLU A N     1 
ATOM 2712 C CA    . GLU B 2 324 ? -14.19600 51.39700  5.39800  1.000 164.35261 ? 324 GLU A CA    1 
ATOM 2713 C C     . GLU B 2 324 ? -15.66300 50.93700  5.38700  1.000 168.75797 ? 324 GLU A C     1 
ATOM 2714 O O     . GLU B 2 324 ? -16.39800 51.33000  4.45800  1.000 178.17113 ? 324 GLU A O     1 
ATOM 2715 C CB    . GLU B 2 324 ? -13.24000 50.32200  4.87400  1.000 158.08449 ? 324 GLU A CB    1 
ATOM 2716 C CG    . GLU B 2 324 ? -13.08700 49.11100  5.79000  1.000 157.85038 ? 324 GLU A CG    1 
ATOM 2717 C CD    . GLU B 2 324 ? -14.03900 47.95800  5.52400  1.000 167.27529 ? 324 GLU A CD    1 
ATOM 2718 O OE1   . GLU B 2 324 ? -14.84500 48.05600  4.57600  1.000 166.93516 ? 324 GLU A OE1   1 
ATOM 2719 O OE2   . GLU B 2 324 ? -13.97700 46.95900  6.27000  1.000 158.82712 ? 324 GLU A OE2   1 
ATOM 2720 N N     . ALA B 2 325 ? -16.06900 50.15000  6.38600  1.000 164.96754 ? 325 ALA A N     1 
ATOM 2721 C CA    . ALA B 2 325 ? -17.45100 49.62100  6.42800  1.000 158.42748 ? 325 ALA A CA    1 
ATOM 2722 C C     . ALA B 2 325 ? -18.43900 50.78100  6.55000  1.000 170.44610 ? 325 ALA A C     1 
ATOM 2723 O O     . ALA B 2 325 ? -19.45400 50.78300  5.82300  1.000 179.79840 ? 325 ALA A O     1 
ATOM 2724 C CB    . ALA B 2 325 ? -17.59100 48.65200  7.57700  1.000 155.31267 ? 325 ALA A CB    1 
ATOM 2725 N N     . LEU B 2 326 ? -18.14700 51.74300  7.42900  1.000 189.60951 ? 326 LEU A N     1 
ATOM 2726 C CA    . LEU B 2 326 ? -19.06700 52.89000  7.65300  1.000 188.31545 ? 326 LEU A CA    1 
ATOM 2727 C C     . LEU B 2 326 ? -18.96800 53.86400  6.47000  1.000 190.26350 ? 326 LEU A C     1 
ATOM 2728 O O     . LEU B 2 326 ? -19.86300 54.73000  6.35700  1.000 188.89418 ? 326 LEU A O     1 
ATOM 2729 C CB    . LEU B 2 326 ? -18.73200 53.58900  8.96900  1.000 169.53371 ? 326 LEU A CB    1 
ATOM 2730 C CG    . LEU B 2 326 ? -19.43200 53.05500  10.22300 1.000 167.36246 ? 326 LEU A CG    1 
ATOM 2731 C CD1   . LEU B 2 326 ? -19.08700 51.60500  10.51400 1.000 171.11298 ? 326 LEU A CD1   1 
ATOM 2732 C CD2   . LEU B 2 326 ? -19.09700 53.93300  11.41500 1.000 161.40261 ? 326 LEU A CD2   1 
ATOM 2733 N N     . ASN B 2 327 ? -17.90800 53.74800  5.66100  1.000 194.57588 ? 327 ASN A N     1 
ATOM 2734 C CA    . ASN B 2 327 ? -17.69700 54.64800  4.48900  1.000 194.28756 ? 327 ASN A CA    1 
ATOM 2735 C C     . ASN B 2 327 ? -17.21000 56.01400  4.98400  1.000 189.67338 ? 327 ASN A C     1 
ATOM 2736 O O     . ASN B 2 327 ? -16.88500 56.86800  4.13000  1.000 193.08398 ? 327 ASN A O     1 
ATOM 2737 C CB    . ASN B 2 327 ? -18.93400 54.73700  3.60000  1.000 178.28502 ? 327 ASN A CB    1 
ATOM 2738 C CG    . ASN B 2 327 ? -19.41600 53.37400  3.16500  1.000 192.76438 ? 327 ASN A CG    1 
ATOM 2739 O OD1   . ASN B 2 327 ? -18.67000 52.62600  2.52500  1.000 196.77211 ? 327 ASN A OD1   1 
ATOM 2740 N ND2   . ASN B 2 327 ? -20.64900 53.03100  3.50700  1.000 189.61003 ? 327 ASN A ND2   1 
ATOM 2741 N N     . PHE B 2 328 ? -17.15100 56.21000  6.30400  1.000 185.34525 ? 328 PHE A N     1 
ATOM 2742 C CA    . PHE B 2 328 ? -16.62600 57.48300  6.86900  1.000 168.03403 ? 328 PHE A CA    1 
ATOM 2743 C C     . PHE B 2 328 ? -15.83400 57.16500  8.12700  1.000 159.26972 ? 328 PHE A C     1 
ATOM 2744 O O     . PHE B 2 328 ? -15.95600 56.04400  8.66300  1.000 173.14737 ? 328 PHE A O     1 
ATOM 2745 C CB    . PHE B 2 328 ? -17.71500 58.50300  7.21200  1.000 163.35852 ? 328 PHE A CB    1 
ATOM 2746 C CG    . PHE B 2 328 ? -18.65980 58.02508  8.30465  1.000 183.34579 ? 328 PHE A CG    1 
ATOM 2747 C CD1   . PHE B 2 328 ? -18.50710 58.46093  9.61544  1.000 176.72697 ? 328 PHE A CD1   1 
ATOM 2748 C CD2   . PHE B 2 328 ? -19.71440 57.16700  8.01746  1.000 196.54133 ? 328 PHE A CD2   1 
ATOM 2749 C CE1   . PHE B 2 328 ? -19.37328 58.03491  10.61044 1.000 179.19911 ? 328 PHE A CE1   1 
ATOM 2750 C CE2   . PHE B 2 328 ? -20.57591 56.74193  9.01516  1.000 186.78420 ? 328 PHE A CE2   1 
ATOM 2751 C CZ    . PHE B 2 328 ? -20.40448 57.17772  10.30839 1.000 180.41987 ? 328 PHE A CZ    1 
ATOM 2752 N N     . LYS B 2 329 ? -15.04000 58.13100  8.58700  1.000 156.85464 ? 329 LYS A N     1 
ATOM 2753 C CA    . LYS B 2 329 ? -14.22800 57.92800  9.81200  1.000 153.72442 ? 329 LYS A CA    1 
ATOM 2754 C C     . LYS B 2 329 ? -14.66800 58.94400  10.87300 1.000 163.25806 ? 329 LYS A C     1 
ATOM 2755 O O     . LYS B 2 329 ? -14.63400 60.15800  10.57800 1.000 158.22510 ? 329 LYS A O     1 
ATOM 2756 C CB    . LYS B 2 329 ? -12.74200 58.07000  9.46500  1.000 167.66997 ? 329 LYS A CB    1 
ATOM 2757 C CG    . LYS B 2 329 ? -11.80200 58.47300  10.59700 1.000 170.97925 ? 329 LYS A CG    1 
ATOM 2758 C CD    . LYS B 2 329 ? -11.78600 57.54400  11.80500 1.000 155.91190 ? 329 LYS A CD    1 
ATOM 2759 C CE    . LYS B 2 329 ? -10.57500 57.74500  12.65900 1.000 157.52551 ? 329 LYS A CE    1 
ATOM 2760 N NZ    . LYS B 2 329 ? -10.40900 59.14500  13.05400 1.000 147.63257 ? 329 LYS A NZ    1 
ATOM 2761 N N     . ILE B 2 330 ? -15.08400 58.46600  12.04900 1.000 162.46241 ? 330 ILE A N     1 
ATOM 2762 C CA    . ILE B 2 330 ? -15.41900 59.41100  13.15500 1.000 159.77788 ? 330 ILE A CA    1 
ATOM 2763 C C     . ILE B 2 330 ? -14.09900 59.74300  13.86500 1.000 157.34664 ? 330 ILE A C     1 
ATOM 2764 O O     . ILE B 2 330 ? -13.46400 58.81600  14.41200 1.000 156.63975 ? 330 ILE A O     1 
ATOM 2765 C CB    . ILE B 2 330 ? -16.48400 58.82800  14.10200 1.000 137.69903 ? 330 ILE A CB    1 
ATOM 2766 C CG1   . ILE B 2 330 ? -16.71000 59.72700  15.31900 1.000 137.07969 ? 330 ILE A CG1   1 
ATOM 2767 C CG2   . ILE B 2 330 ? -16.14400 57.39200  14.50800 1.000 148.34854 ? 330 ILE A CG2   1 
ATOM 2768 C CD1   . ILE B 2 330 ? -17.26900 61.09700  14.98000 1.000 133.77200 ? 330 ILE A CD1   1 
ATOM 2769 N N     . ASN B 2 331 ? -13.69000 61.01000  13.83000 1.000 153.89565 ? 331 ASN A N     1 
ATOM 2770 C CA    . ASN B 2 331 ? -12.37000 61.38500  14.40700 1.000 151.82965 ? 331 ASN A CA    1 
ATOM 2771 C C     . ASN B 2 331 ? -12.27600 60.87700  15.85100 1.000 148.81970 ? 331 ASN A C     1 
ATOM 2772 O O     . ASN B 2 331 ? -13.22900 61.11300  16.62800 1.000 147.76782 ? 331 ASN A O     1 
ATOM 2773 C CB    . ASN B 2 331 ? -12.11600 62.87900  14.24100 1.000 160.74437 ? 331 ASN A CB    1 
ATOM 2774 C CG    . ASN B 2 331 ? -13.33900 63.70700  14.55000 1.000 144.11800 ? 331 ASN A CG    1 
ATOM 2775 O OD1   . ASN B 2 331 ? -14.39800 63.50300  13.94700 1.000 131.75047 ? 331 ASN A OD1   1 
ATOM 2776 N ND2   . ASN B 2 331 ? -13.21700 64.63900  15.48300 1.000 141.93574 ? 331 ASN A ND2   1 
ATOM 2777 N N     . ALA B 2 332 ? -11.17400 60.19900  16.18900 1.000 142.38137 ? 332 ALA A N     1 
ATOM 2778 C CA    . ALA B 2 332 ? -10.95900 59.69600  17.56700 1.000 127.42671 ? 332 ALA A CA    1 
ATOM 2779 C C     . ALA B 2 332 ? -9.58700  60.16000  18.05700 1.000 136.18030 ? 332 ALA A C     1 
ATOM 2780 O O     . ALA B 2 332 ? -8.64900  60.20700  17.23300 1.000 148.79616 ? 332 ALA A O     1 
ATOM 2781 C CB    . ALA B 2 332 ? -11.07100 58.19100  17.58500 1.000 127.58912 ? 332 ALA A CB    1 
ATOM 2782 N N     . LEU B 2 333 ? -9.47400  60.49200  19.34700 1.000 132.26634 ? 333 LEU A N     1 
ATOM 2783 C CA    . LEU B 2 333 ? -8.19600  61.03000  19.88400 1.000 129.01069 ? 333 LEU A CA    1 
ATOM 2784 C C     . LEU B 2 333 ? -7.92300  60.43100  21.27300 1.000 125.31316 ? 333 LEU A C     1 
ATOM 2785 O O     . LEU B 2 333 ? -8.89900  60.18800  22.01700 1.000 118.24711 ? 333 LEU A O     1 
ATOM 2786 C CB    . LEU B 2 333 ? -8.30600  62.55300  19.93100 1.000 117.34706 ? 333 LEU A CB    1 
ATOM 2787 C CG    . LEU B 2 333 ? -6.99000  63.33900  19.93500 1.000 119.52647 ? 333 LEU A CG    1 
ATOM 2788 C CD1   . LEU B 2 333 ? -7.22400  64.73500  19.38700 1.000 137.06620 ? 333 LEU A CD1   1 
ATOM 2789 C CD2   . LEU B 2 333 ? -6.39100  63.42200  21.32800 1.000 134.68507 ? 333 LEU A CD2   1 
ATOM 2790 N N     . LEU B 2 334 ? -6.64700  60.20800  21.60700 1.000 118.65027 ? 334 LEU A N     1 
ATOM 2791 C CA    . LEU B 2 334 ? -6.28400  59.68700  22.95100 1.000 115.81952 ? 334 LEU A CA    1 
ATOM 2792 C C     . LEU B 2 334 ? -6.26900  60.86300  23.94000 1.000 112.63323 ? 334 LEU A C     1 
ATOM 2793 O O     . LEU B 2 334 ? -5.23400  61.56000  24.01800 1.000 122.87336 ? 334 LEU A O     1 
ATOM 2794 C CB    . LEU B 2 334 ? -4.92700  58.98900  22.88300 1.000 88.30478  ? 334 LEU A CB    1 
ATOM 2795 C CG    . LEU B 2 334 ? -4.66200  57.90200  23.93100 1.000 107.35810 ? 334 LEU A CG    1 
ATOM 2796 C CD1   . LEU B 2 334 ? -3.32600  57.23000  23.67400 1.000 115.11835 ? 334 LEU A CD1   1 
ATOM 2797 C CD2   . LEU B 2 334 ? -4.73300  58.41100  25.36100 1.000 112.28641 ? 334 LEU A CD2   1 
ATOM 2798 N N     . ILE B 2 335 ? -7.37500  61.06800  24.66100 1.000 114.09104 ? 335 ILE A N     1 
ATOM 2799 C CA    . ILE B 2 335 ? -7.46800  62.20100  25.63000 1.000 106.91604 ? 335 ILE A CA    1 
ATOM 2800 C C     . ILE B 2 335 ? -6.49800  61.93100  26.79100 1.000 105.26603 ? 335 ILE A C     1 
ATOM 2801 O O     . ILE B 2 335 ? -6.45600  60.77600  27.26700 1.000 109.46311 ? 335 ILE A O     1 
ATOM 2802 C CB    . ILE B 2 335 ? -8.91600  62.37100  26.12600 1.000 116.68198 ? 335 ILE A CB    1 
ATOM 2803 C CG1   . ILE B 2 335 ? -9.92800  62.16100  24.99700 1.000 131.87834 ? 335 ILE A CG1   1 
ATOM 2804 C CG2   . ILE B 2 335 ? -9.10400  63.72300  26.81500 1.000 93.94019  ? 335 ILE A CG2   1 
ATOM 2805 C CD1   . ILE B 2 335 ? -9.82600  63.17400  23.87100 1.000 121.58277 ? 335 ILE A CD1   1 
ATOM 2806 N N     . LYS B 2 336 ? -5.75000  62.95200  27.22100 1.000 116.31866 ? 336 LYS A N     1 
ATOM 2807 C CA    . LYS B 2 336 ? -4.80600  62.79800  28.36100 1.000 102.17284 ? 336 LYS A CA    1 
ATOM 2808 C C     . LYS B 2 336 ? -4.95600  64.00000  29.30800 1.000 104.53592 ? 336 LYS A C     1 
ATOM 2809 O O     . LYS B 2 336 ? -5.74800  64.91400  28.98700 1.000 108.39336 ? 336 LYS A O     1 
ATOM 2810 C CB    . LYS B 2 336 ? -3.35500  62.67600  27.88100 1.000 86.24942  ? 336 LYS A CB    1 
ATOM 2811 C CG    . LYS B 2 336 ? -3.02300  61.39000  27.14000 1.000 85.58039  ? 336 LYS A CG    1 
ATOM 2812 C CD    . LYS B 2 336 ? -1.53300  61.21300  26.88100 1.000 110.20977 ? 336 LYS A CD    1 
ATOM 2813 C CE    . LYS B 2 336 ? -1.22500  59.92300  26.19000 1.000 116.15333 ? 336 LYS A CE    1 
ATOM 2814 N NZ    . LYS B 2 336 ? 0.21800   59.70400  26.06200 1.000 101.34787 ? 336 LYS A NZ    1 
ATOM 2815 N N     . SER B 2 337 ? -4.20500  64.01000  30.41100 1.000 91.01545  ? 337 SER A N     1 
ATOM 2816 C CA    . SER B 2 337 ? -4.29900  65.12200  31.39300 1.000 105.63038 ? 337 SER A CA    1 
ATOM 2817 C C     . SER B 2 337 ? -3.61600  66.38000  30.83700 1.000 100.17764 ? 337 SER A C     1 
ATOM 2818 O O     . SER B 2 337 ? -2.81800  66.24900  29.88500 1.000 96.05129  ? 337 SER A O     1 
ATOM 2819 C CB    . SER B 2 337 ? -3.72600  64.72100  32.72500 1.000 113.41042 ? 337 SER A CB    1 
ATOM 2820 O OG    . SER B 2 337 ? -4.54900  63.73400  33.33000 1.000 117.20207 ? 337 SER A OG    1 
ATOM 2821 N N     . LYS B 2 338 ? -3.90800  67.54500  31.42200 1.000 99.80368  ? 338 LYS A N     1 
ATOM 2822 C CA    . LYS B 2 338 ? -3.34700  68.82400  30.91000 1.000 113.82737 ? 338 LYS A CA    1 
ATOM 2823 C C     . LYS B 2 338 ? -1.81200  68.75500  30.91000 1.000 102.30539 ? 338 LYS A C     1 
ATOM 2824 O O     . LYS B 2 338 ? -1.20100  69.18800  29.90800 1.000 97.27977  ? 338 LYS A O     1 
ATOM 2825 C CB    . LYS B 2 338 ? -3.86400  69.98200  31.77200 1.000 98.01247  ? 338 LYS A CB    1 
ATOM 2826 C CG    . LYS B 2 338 ? -3.57400  71.37100  31.23000 1.000 102.02009 ? 338 LYS A CG    1 
ATOM 2827 C CD    . LYS B 2 338 ? -4.33100  72.47500  31.95800 1.000 131.55869 ? 338 LYS A CD    1 
ATOM 2828 C CE    . LYS B 2 338 ? -4.13500  73.80800  31.31200 1.000 113.86319 ? 338 LYS A CE    1 
ATOM 2829 N NZ    . LYS B 2 338 ? -4.89100  74.85800  31.99900 1.000 107.55693 ? 338 LYS A NZ    1 
ATOM 2830 N N     . SER B 2 339 ? -1.21900  68.21300  31.97700 1.000 103.89592 ? 339 SER A N     1 
ATOM 2831 C CA    . SER B 2 339 ? 0.26300   68.14500  32.08500 1.000 100.35187 ? 339 SER A CA    1 
ATOM 2832 C C     . SER B 2 339 ? 0.84400   67.37300  30.89200 1.000 93.84437  ? 339 SER A C     1 
ATOM 2833 O O     . SER B 2 339 ? 1.94500   67.74300  30.43000 1.000 99.32806  ? 339 SER A O     1 
ATOM 2834 C CB    . SER B 2 339 ? 0.68200   67.52500  33.39200 1.000 114.97058 ? 339 SER A CB    1 
ATOM 2835 O OG    . SER B 2 339 ? 0.20300   68.28900  34.49000 1.000 117.32256 ? 339 SER A OG    1 
ATOM 2836 N N     . ASP B 2 340 ? 0.13300   66.34900  30.41200 1.000 99.77905  ? 340 ASP A N     1 
ATOM 2837 C CA    . ASP B 2 340 ? 0.65500   65.50800  29.29800 1.000 101.01255 ? 340 ASP A CA    1 
ATOM 2838 C C     . ASP B 2 340 ? 0.93300   66.38400  28.07100 1.000 110.59642 ? 340 ASP A C     1 
ATOM 2839 O O     . ASP B 2 340 ? 1.92800   66.11500  27.37700 1.000 122.70969 ? 340 ASP A O     1 
ATOM 2840 C CB    . ASP B 2 340 ? -0.28400  64.35400  28.98400 1.000 107.98991 ? 340 ASP A CB    1 
ATOM 2841 C CG    . ASP B 2 340 ? -0.47100  63.35200  30.11300 1.000 107.26928 ? 340 ASP A CG    1 
ATOM 2842 O OD1   . ASP B 2 340 ? 0.53700   62.75000  30.53500 1.000 96.01948  ? 340 ASP A OD1   1 
ATOM 2843 O OD2   . ASP B 2 340 ? -1.62100  63.19000  30.56700 1.000 112.53467 ? 340 ASP A OD2   1 
ATOM 2844 N N     . TYR B 2 341 ? 0.08400   67.38100  27.80900 1.000 110.42163 ? 341 TYR A N     1 
ATOM 2845 C CA    . TYR B 2 341 ? 0.25500   68.23700  26.60200 1.000 96.65137  ? 341 TYR A CA    1 
ATOM 2846 C C     . TYR B 2 341 ? 1.33500   69.28800  26.88000 1.000 102.68462 ? 341 TYR A C     1 
ATOM 2847 O O     . TYR B 2 341 ? 1.50900   69.68400  28.05300 1.000 119.80359 ? 341 TYR A O     1 
ATOM 2848 C CB    . TYR B 2 341 ? -1.10300  68.82200  26.20300 1.000 104.31602 ? 341 TYR A CB    1 
ATOM 2849 C CG    . TYR B 2 341 ? -2.14400  67.75300  25.90300 1.000 121.24092 ? 341 TYR A CG    1 
ATOM 2850 C CD1   . TYR B 2 341 ? -2.28100  67.22200  24.62600 1.000 135.37647 ? 341 TYR A CD1   1 
ATOM 2851 C CD2   . TYR B 2 341 ? -2.98100  67.26600  26.89900 1.000 98.44789  ? 341 TYR A CD2   1 
ATOM 2852 C CE1   . TYR B 2 341 ? -3.22100  66.24300  24.35000 1.000 132.86562 ? 341 TYR A CE1   1 
ATOM 2853 C CE2   . TYR B 2 341 ? -3.92600  66.28900  26.63500 1.000 98.22801  ? 341 TYR A CE2   1 
ATOM 2854 C CZ    . TYR B 2 341 ? -4.04700  65.77500  25.35700 1.000 102.78093 ? 341 TYR A CZ    1 
ATOM 2855 O OH    . TYR B 2 341 ? -4.97800  64.81200  25.09400 1.000 129.47508 ? 341 TYR A OH    1 
ATOM 2856 N N     . ILE B 2 342 ? 2.04000   69.73100  25.83300 1.000 114.65816 ? 342 ILE A N     1 
ATOM 2857 C CA    . ILE B 2 342 ? 3.16700   70.69600  26.02200 1.000 115.95868 ? 342 ILE A CA    1 
ATOM 2858 C C     . ILE B 2 342 ? 2.66700   72.13100  25.79000 1.000 101.76004 ? 342 ILE A C     1 
ATOM 2859 O O     . ILE B 2 342 ? 1.76400   72.31600  24.94100 1.000 105.62906 ? 342 ILE A O     1 
ATOM 2860 C CB    . ILE B 2 342 ? 4.34600   70.34500  25.09300 1.000 107.39515 ? 342 ILE A CB    1 
ATOM 2861 C CG1   . ILE B 2 342 ? 5.60700   71.12300  25.46200 1.000 76.66534  ? 342 ILE A CG1   1 
ATOM 2862 C CG2   . ILE B 2 342 ? 3.97100   70.54200  23.62300 1.000 84.18603  ? 342 ILE A CG2   1 
ATOM 2863 C CD1   . ILE B 2 342 ? 5.97300   71.03900  26.93200 1.000 96.66933  ? 342 ILE A CD1   1 
ATOM 2864 N N     . SER B 2 343 ? 3.22700   73.10200  26.52000 1.000 105.15323 ? 343 SER A N     1 
ATOM 2865 C CA    . SER B 2 343 ? 2.84800   74.52300  26.33100 1.000 109.06511 ? 343 SER A CA    1 
ATOM 2866 C C     . SER B 2 343 ? 3.99200   75.19100  25.56400 1.000 116.40864 ? 343 SER A C     1 
ATOM 2867 O O     . SER B 2 343 ? 5.05400   74.55100  25.41800 1.000 102.78403 ? 343 SER A O     1 
ATOM 2868 C CB    . SER B 2 343 ? 2.60000   75.21200  27.63900 1.000 95.98265  ? 343 SER A CB    1 
ATOM 2869 O OG    . SER B 2 343 ? 2.34600   76.59600  27.44100 1.000 105.81769 ? 343 SER A OG    1 
ATOM 2870 N N     . LEU B 2 344 ? 3.79900   76.43000  25.11700 1.000 118.01488 ? 344 LEU A N     1 
ATOM 2871 C CA    . LEU B 2 344 ? 4.91400   77.13900  24.44000 1.000 99.72207  ? 344 LEU A CA    1 
ATOM 2872 C C     . LEU B 2 344 ? 5.79400   77.80700  25.50600 1.000 119.59810 ? 344 LEU A C     1 
ATOM 2873 O O     . LEU B 2 344 ? 6.55300   78.72900  25.14800 1.000 109.03199 ? 344 LEU A O     1 
ATOM 2874 C CB    . LEU B 2 344 ? 4.37400   78.11700  23.40000 1.000 100.69363 ? 344 LEU A CB    1 
ATOM 2875 C CG    . LEU B 2 344 ? 4.28400   77.56400  21.97400 1.000 104.83248 ? 344 LEU A CG    1 
ATOM 2876 C CD1   . LEU B 2 344 ? 5.66800   77.20400  21.46700 1.000 132.56823 ? 344 LEU A CD1   1 
ATOM 2877 C CD2   . LEU B 2 344 ? 3.36900   76.35500  21.89400 1.000 106.85840 ? 344 LEU A CD2   1 
ATOM 2878 N N     . GLY B 2 345 ? 5.71600   77.33800  26.75700 1.000 124.20272 ? 345 GLY A N     1 
ATOM 2879 C CA    . GLY B 2 345 ? 6.60500   77.85100  27.81900 1.000 89.60414  ? 345 GLY A CA    1 
ATOM 2880 C C     . GLY B 2 345 ? 8.01500   77.37200  27.55100 1.000 107.74204 ? 345 GLY A C     1 
ATOM 2881 O O     . GLY B 2 345 ? 8.91100   77.68900  28.35600 1.000 112.65097 ? 345 GLY A O     1 
ATOM 2882 N N     . LEU B 2 346 ? 8.20800   76.63300  26.45600 1.000 107.25699 ? 346 LEU A N     1 
ATOM 2883 C CA    . LEU B 2 346 ? 9.55800   76.17000  26.05500 1.000 112.00459 ? 346 LEU A CA    1 
ATOM 2884 C C     . LEU B 2 346 ? 10.48600  77.38700  25.97700 1.000 113.48006 ? 346 LEU A C     1 
ATOM 2885 O O     . LEU B 2 346 ? 11.69400  77.23300  26.22600 1.000 109.65094 ? 346 LEU A O     1 
ATOM 2886 C CB    . LEU B 2 346 ? 9.40500   75.49600  24.69500 1.000 101.06706 ? 346 LEU A CB    1 
ATOM 2887 C CG    . LEU B 2 346 ? 10.30400  74.28800  24.41100 1.000 119.03558 ? 346 LEU A CG    1 
ATOM 2888 C CD1   . LEU B 2 346 ? 9.83000   73.61300  23.13600 1.000 104.15000 ? 346 LEU A CD1   1 
ATOM 2889 C CD2   . LEU B 2 346 ? 11.76500  74.67900  24.28500 1.000 102.34223 ? 346 LEU A CD2   1 
ATOM 2890 N N     . ILE B 2 347 ? 9.93100   78.55300  25.64100 1.000 107.01240 ? 347 ILE A N     1 
ATOM 2891 C CA    . ILE B 2 347 ? 10.75600  79.79000  25.52900 1.000 93.16056  ? 347 ILE A CA    1 
ATOM 2892 C C     . ILE B 2 347 ? 11.43600  80.03100  26.88600 1.000 108.08400 ? 347 ILE A C     1 
ATOM 2893 O O     . ILE B 2 347 ? 12.64300  80.33800  26.89200 1.000 118.79067 ? 347 ILE A O     1 
ATOM 2894 C CB    . ILE B 2 347 ? 9.90300   80.98800  25.06800 1.000 86.56873  ? 347 ILE A CB    1 
ATOM 2895 C CG1   . ILE B 2 347 ? 10.76800  82.21200  24.76900 1.000 114.77121 ? 347 ILE A CG1   1 
ATOM 2896 C CG2   . ILE B 2 347 ? 8.78900   81.30600  26.06700 1.000 93.11636  ? 347 ILE A CG2   1 
ATOM 2897 C CD1   . ILE B 2 347 ? 11.75800  82.00500  23.63800 1.000 84.54052  ? 347 ILE A CD1   1 
ATOM 2898 N N     . SER B 2 348 ? 10.70200  79.86000  27.98600 1.000 105.49581 ? 348 SER A N     1 
ATOM 2899 C CA    . SER B 2 348 ? 11.31000  80.01500  29.33000 1.000 106.22960 ? 348 SER A CA    1 
ATOM 2900 C C     . SER B 2 348 ? 12.44400  78.99600  29.47700 1.000 108.83935 ? 348 SER A C     1 
ATOM 2901 O O     . SER B 2 348 ? 13.52100  79.37200  29.98500 1.000 106.20530 ? 348 SER A O     1 
ATOM 2902 C CB    . SER B 2 348 ? 10.28200  79.84400  30.41200 1.000 108.75924 ? 348 SER A CB    1 
ATOM 2903 O OG    . SER B 2 348 ? 10.89600  79.83600  31.69400 1.000 135.14897 ? 348 SER A OG    1 
ATOM 2904 N N     . GLN B 2 349 ? 12.20500  77.76200  29.03400 1.000 102.81189 ? 349 GLN A N     1 
ATOM 2905 C CA    . GLN B 2 349 ? 13.23300  76.69600  29.13600 1.000 97.39607  ? 349 GLN A CA    1 
ATOM 2906 C C     . GLN B 2 349 ? 14.44600  77.10800  28.29200 1.000 103.26462 ? 349 GLN A C     1 
ATOM 2907 O O     . GLN B 2 349 ? 15.58600  76.86300  28.73100 1.000 106.20594 ? 349 GLN A O     1 
ATOM 2908 C CB    . GLN B 2 349 ? 12.59200  75.38400  28.68800 1.000 81.56517  ? 349 GLN A CB    1 
ATOM 2909 C CG    . GLN B 2 349 ? 13.31100  74.13000  29.16900 1.000 92.92014  ? 349 GLN A CG    1 
ATOM 2910 C CD    . GLN B 2 349 ? 14.52100  73.78200  28.33400 1.000 119.72261 ? 349 GLN A CD    1 
ATOM 2911 O OE1   . GLN B 2 349 ? 14.42200  73.54600  27.12500 1.000 123.51515 ? 349 GLN A OE1   1 
ATOM 2912 N NE2   . GLN B 2 349 ? 15.68000  73.74800  28.97500 1.000 128.99753 ? 349 GLN A NE2   1 
ATOM 2913 N N     . ILE B 2 350 ? 14.20200  77.72300  27.13400 1.000 105.77322 ? 350 ILE A N     1 
ATOM 2914 C CA    . ILE B 2 350 ? 15.31100  78.17000  26.23900 1.000 93.19927  ? 350 ILE A CA    1 
ATOM 2915 C C     . ILE B 2 350 ? 16.15000  79.21800  26.98200 1.000 98.06596  ? 350 ILE A C     1 
ATOM 2916 O O     . ILE B 2 350 ? 17.39300  79.09500  26.97300 1.000 108.43907 ? 350 ILE A O     1 
ATOM 2917 C CB    . ILE B 2 350 ? 14.74000  78.73200  24.92500 1.000 97.93411  ? 350 ILE A CB    1 
ATOM 2918 C CG1   . ILE B 2 350 ? 14.16900  77.62500  24.04100 1.000 95.70825  ? 350 ILE A CG1   1 
ATOM 2919 C CG2   . ILE B 2 350 ? 15.78100  79.56700  24.18100 1.000 120.46223 ? 350 ILE A CG2   1 
ATOM 2920 C CD1   . ILE B 2 350 ? 13.65100  78.11300  22.70100 1.000 104.21177 ? 350 ILE A CD1   1 
ATOM 2921 N N     . LEU B 2 351 ? 15.49500  80.19600  27.61000 1.000 106.16375 ? 351 LEU A N     1 
ATOM 2922 C CA    . LEU B 2 351 ? 16.22200  81.28800  28.31200 1.000 106.00502 ? 351 LEU A CA    1 
ATOM 2923 C C     . LEU B 2 351 ? 17.16200  80.69800  29.37500 1.000 106.63870 ? 351 LEU A C     1 
ATOM 2924 O O     . LEU B 2 351 ? 18.32800  81.14100  29.44200 1.000 118.26681 ? 351 LEU A O     1 
ATOM 2925 C CB    . LEU B 2 351 ? 15.21400  82.25300  28.93400 1.000 98.19953  ? 351 LEU A CB    1 
ATOM 2926 C CG    . LEU B 2 351 ? 14.80000  83.45400  28.07800 1.000 103.46145 ? 351 LEU A CG    1 
ATOM 2927 C CD1   . LEU B 2 351 ? 14.33700  83.04700  26.69000 1.000 112.64674 ? 351 LEU A CD1   1 
ATOM 2928 C CD2   . LEU B 2 351 ? 13.71900  84.25300  28.78300 1.000 110.01136 ? 351 LEU A CD2   1 
ATOM 2929 N N     . LYS B 2 352 ? 16.67900  79.74200  30.17000 1.000 91.04639  ? 352 LYS A N     1 
ATOM 2930 C CA    . LYS B 2 352 ? 17.50700  79.18900  31.27200 1.000 105.91339 ? 352 LYS A CA    1 
ATOM 2931 C C     . LYS B 2 352 ? 18.83100  78.66500  30.70200 1.000 110.29406 ? 352 LYS A C     1 
ATOM 2932 O O     . LYS B 2 352 ? 18.79800  77.99800  29.64700 1.000 109.32214 ? 352 LYS A O     1 
ATOM 2933 C CB    . LYS B 2 352 ? 16.79000  78.05200  32.00700 1.000 109.21674 ? 352 LYS A CB    1 
ATOM 2934 C CG    . LYS B 2 352 ? 17.51300  77.57100  33.25700 1.000 117.55464 ? 352 LYS A CG    1 
ATOM 2935 C CD    . LYS B 2 352 ? 17.59600  76.05700  33.40600 1.000 110.25610 ? 352 LYS A CD    1 
ATOM 2936 C CE    . LYS B 2 352 ? 18.40600  75.67200  34.60200 1.000 138.95284 ? 352 LYS A CE    1 
ATOM 2937 N NZ    . LYS B 2 352 ? 18.51500  74.21900  34.75900 1.000 130.62698 ? 352 LYS A NZ    1 
ATOM 2938 N N     . ASP B 2 353 ? 19.94300  78.94900  31.38200 1.000 105.77042 ? 353 ASP A N     1 
ATOM 2939 C CA    . ASP B 2 353 ? 21.26700  78.43400  30.93500 1.000 123.94303 ? 353 ASP A CA    1 
ATOM 2940 C C     . ASP B 2 353 ? 21.69500  77.29000  31.85700 1.000 127.88313 ? 353 ASP A C     1 
ATOM 2941 O O     . ASP B 2 353 ? 21.75700  77.50700  33.08400 1.000 133.98674 ? 353 ASP A O     1 
ATOM 2942 C CB    . ASP B 2 353 ? 22.29500  79.55100  30.84900 1.000 120.63747 ? 353 ASP A CB    1 
ATOM 2943 C CG    . ASP B 2 353 ? 23.10680  79.79350  32.11263 1.000 143.26937 ? 353 ASP A CG    1 
ATOM 2944 O OD1   . ASP B 2 353 ? 24.22668  80.33436  31.99844 1.000 164.33167 ? 353 ASP A OD1   1 
ATOM 2945 O OD2   . ASP B 2 353 ? 22.61006  79.44091  33.20339 1.000 123.89000 ? 353 ASP A OD2   1 
ATOM 2946 N N     . ASP B 2 354 ? 21.96500  76.11600  31.28400 1.000 123.18735 ? 354 ASP A N     1 
ATOM 2947 C CA    . ASP B 2 354 ? 22.37700  74.93700  32.09200 1.000 124.48184 ? 354 ASP A CA    1 
ATOM 2948 C C     . ASP B 2 354 ? 23.45900  74.18400  31.31900 1.000 123.05209 ? 354 ASP A C     1 
ATOM 2949 O O     . ASP B 2 354 ? 23.22700  73.01100  30.95400 1.000 129.76270 ? 354 ASP A O     1 
ATOM 2950 C CB    . ASP B 2 354 ? 21.18100  74.06600  32.43700 1.000 115.02964 ? 354 ASP A CB    1 
ATOM 2951 C CG    . ASP B 2 354 ? 21.41200  73.03400  33.53100 1.000 140.40426 ? 354 ASP A CG    1 
ATOM 2952 O OD1   . ASP B 2 354 ? 22.54900  72.96500  34.04500 1.000 147.32040 ? 354 ASP A OD1   1 
ATOM 2953 O OD2   . ASP B 2 354 ? 20.45000  72.31200  33.86500 1.000 134.15466 ? 354 ASP A OD2   1 
ATOM 2954 N N     . THR B 2 355 ? 24.60200  74.83100  31.09300 1.000 109.87820 ? 355 THR A N     1 
ATOM 2955 C CA    . THR B 2 355 ? 25.67800  74.20600  30.29700 1.000 127.61560 ? 355 THR A CA    1 
ATOM 2956 C C     . THR B 2 355 ? 26.04700  72.87400  30.90500 1.000 127.83992 ? 355 THR A C     1 
ATOM 2957 O O     . THR B 2 355 ? 26.26200  71.91500  30.13400 1.000 132.74016 ? 355 THR A O     1 
ATOM 2958 C CB    . THR B 2 355 ? 26.87700  75.15100  30.25000 1.000 155.69362 ? 355 THR A CB    1 
ATOM 2959 O OG1   . THR B 2 355 ? 27.94200  74.37000  29.71500 1.000 151.68843 ? 355 THR A OG1   1 
ATOM 2960 C CG2   . THR B 2 355 ? 27.26000  75.68700  31.61700 1.000 142.72501 ? 355 THR A CG2   1 
ATOM 2961 N N     . SER B 2 356 ? 26.10100  72.79700  32.23500 1.000 130.13008 ? 356 SER A N     1 
ATOM 2962 C CA    . SER B 2 356 ? 26.55200  71.55200  32.90700 1.000 150.64054 ? 356 SER A CA    1 
ATOM 2963 C C     . SER B 2 356 ? 25.70100  70.35700  32.45900 1.000 156.78244 ? 356 SER A C     1 
ATOM 2964 O O     . SER B 2 356 ? 26.27700  69.26400  32.27500 1.000 152.04530 ? 356 SER A O     1 
ATOM 2965 C CB    . SER B 2 356 ? 26.51200  71.71000  34.40600 1.000 132.03712 ? 356 SER A CB    1 
ATOM 2966 O OG    . SER B 2 356 ? 26.87300  70.49700  35.05100 1.000 135.64666 ? 356 SER A OG    1 
ATOM 2967 N N     . ASN B 2 357 ? 24.38600  70.55000  32.35100 1.000 128.21575 ? 357 ASN A N     1 
ATOM 2968 C CA    . ASN B 2 357 ? 23.49600  69.40700  32.01100 1.000 126.70055 ? 357 ASN A CA    1 
ATOM 2969 C C     . ASN B 2 357 ? 23.55700  69.15300  30.50300 1.000 126.36404 ? 357 ASN A C     1 
ATOM 2970 O O     . ASN B 2 357 ? 22.75200  69.75800  29.76100 1.000 122.43332 ? 357 ASN A O     1 
ATOM 2971 C CB    . ASN B 2 357 ? 22.09000  69.61800  32.55700 1.000 124.97685 ? 357 ASN A CB    1 
ATOM 2972 C CG    . ASN B 2 357 ? 21.98400  69.20600  34.00500 1.000 137.62788 ? 357 ASN A CG    1 
ATOM 2973 O OD1   . ASN B 2 357 ? 22.22900  68.04100  34.33800 1.000 145.59624 ? 357 ASN A OD1   1 
ATOM 2974 N ND2   . ASN B 2 357 ? 21.62500  70.13600  34.87800 1.000 139.24356 ? 357 ASN A ND2   1 
ATOM 2975 N N     . TYR B 2 358 ? 24.47700  68.28400  30.07600 1.000 126.59063 ? 358 TYR A N     1 
ATOM 2976 C CA    . TYR B 2 358 ? 24.59500  67.92100  28.64000 1.000 110.01160 ? 358 TYR A CA    1 
ATOM 2977 C C     . TYR B 2 358 ? 23.22200  67.47800  28.15400 1.000 112.69300 ? 358 TYR A C     1 
ATOM 2978 O O     . TYR B 2 358 ? 22.82300  67.84400  27.02900 1.000 116.53743 ? 358 TYR A O     1 
ATOM 2979 C CB    . TYR B 2 358 ? 25.69600  66.85700  28.68600 1.000 120.88686 ? 358 TYR A CB    1 
ATOM 2980 C CG    . TYR B 2 358 ? 25.86700  65.90800  27.50800 1.000 125.70372 ? 358 TYR A CG    1 
ATOM 2981 C CD1   . TYR B 2 358 ? 25.51500  66.27400  26.21600 1.000 122.35112 ? 358 TYR A CD1   1 
ATOM 2982 C CD2   . TYR B 2 358 ? 26.39800  64.63700  27.69700 1.000 153.06757 ? 358 TYR A CD2   1 
ATOM 2983 C CE1   . TYR B 2 358 ? 25.69600  65.40900  25.14900 1.000 133.09570 ? 358 TYR A CE1   1 
ATOM 2984 C CE2   . TYR B 2 358 ? 26.57400  63.76000  26.64000 1.000 156.96719 ? 358 TYR A CE2   1 
ATOM 2985 C CZ    . TYR B 2 358 ? 26.21900  64.14700  25.36100 1.000 141.01943 ? 358 TYR A CZ    1 
ATOM 2986 O OH    . TYR B 2 358 ? 26.38600  63.29000  24.31200 1.000 142.40131 ? 358 TYR A OH    1 
ATOM 2987 N N     . GLU B 2 359 ? 22.50000  66.73400  28.99600 1.000 118.70190 ? 359 GLU A N     1 
ATOM 2988 C CA    . GLU B 2 359 ? 21.14600  66.24600  28.63300 1.000 119.97909 ? 359 GLU A CA    1 
ATOM 2989 C C     . GLU B 2 359 ? 20.18100  67.43300  28.48500 1.000 116.16535 ? 359 GLU A C     1 
ATOM 2990 O O     . GLU B 2 359 ? 19.51100  67.51600  27.43500 1.000 132.19859 ? 359 GLU A O     1 
ATOM 2991 C CB    . GLU B 2 359 ? 20.65400  65.28500  29.71500 1.000 113.95228 ? 359 GLU A CB    1 
ATOM 2992 C CG    . GLU B 2 359 ? 21.70000  64.25800  30.14100 1.000 116.33186 ? 359 GLU A CG    1 
ATOM 2993 C CD    . GLU B 2 359 ? 22.55000  64.66800  31.33100 1.000 154.79757 ? 359 GLU A CD    1 
ATOM 2994 O OE1   . GLU B 2 359 ? 23.24800  65.70100  31.24400 1.000 145.38706 ? 359 GLU A OE1   1 
ATOM 2995 O OE2   . GLU B 2 359 ? 22.51100  63.94900  32.35100 1.000 164.60967 ? 359 GLU A OE2   1 
ATOM 2996 N N     . VAL B 2 360 ? 20.10900  68.30900  29.49400 1.000 89.97195  ? 360 VAL A N     1 
ATOM 2997 C CA    . VAL B 2 360 ? 19.13400  69.44100  29.45700 1.000 93.60754  ? 360 VAL A CA    1 
ATOM 2998 C C     . VAL B 2 360 ? 19.34600  70.22500  28.15300 1.000 99.14986  ? 360 VAL A C     1 
ATOM 2999 O O     . VAL B 2 360 ? 18.34100  70.58800  27.50900 1.000 109.75068 ? 360 VAL A O     1 
ATOM 3000 C CB    . VAL B 2 360 ? 19.26100  70.35100  30.69300 1.000 82.60380  ? 360 VAL A CB    1 
ATOM 3001 C CG1   . VAL B 2 360 ? 18.44200  71.62700  30.54900 1.000 97.70955  ? 360 VAL A CG1   1 
ATOM 3002 C CG2   . VAL B 2 360 ? 18.88800  69.61400  31.97200 1.000 90.71371  ? 360 VAL A CG2   1 
ATOM 3003 N N     . ASN B 2 361 ? 20.60500  70.45700  27.77200 1.000 96.39874  ? 361 ASN A N     1 
ATOM 3004 C CA    . ASN B 2 361 ? 20.90700  71.20700  26.52200 1.000 105.17219 ? 361 ASN A CA    1 
ATOM 3005 C C     . ASN B 2 361 ? 20.35700  70.43000  25.32200 1.000 101.14711 ? 361 ASN A C     1 
ATOM 3006 O O     . ASN B 2 361 ? 19.66500  71.04300  24.48500 1.000 107.67942 ? 361 ASN A O     1 
ATOM 3007 C CB    . ASN B 2 361 ? 22.39700  71.49100  26.38400 1.000 112.32631 ? 361 ASN A CB    1 
ATOM 3008 C CG    . ASN B 2 361 ? 22.89200  72.43000  27.45800 1.000 129.14714 ? 361 ASN A CG    1 
ATOM 3009 O OD1   . ASN B 2 361 ? 22.44400  73.57900  27.53100 1.000 134.80227 ? 361 ASN A OD1   1 
ATOM 3010 N ND2   . ASN B 2 361 ? 23.81100  71.96600  28.29300 1.000 132.37452 ? 361 ASN A ND2   1 
ATOM 3011 N N     . ILE B 2 362 ? 20.63900  69.12700  25.25500 1.000 101.06244 ? 362 ILE A N     1 
ATOM 3012 C CA    . ILE B 2 362 ? 20.12800  68.28300  24.13400 1.000 94.52199  ? 362 ILE A CA    1 
ATOM 3013 C C     . ILE B 2 362 ? 18.59400  68.32500  24.17100 1.000 98.78076  ? 362 ILE A C     1 
ATOM 3014 O O     . ILE B 2 362 ? 17.97800  68.39900  23.09100 1.000 104.63016 ? 362 ILE A O     1 
ATOM 3015 C CB    . ILE B 2 362 ? 20.66800  66.84600  24.22900 1.000 91.39831  ? 362 ILE A CB    1 
ATOM 3016 C CG1   . ILE B 2 362 ? 22.18800  66.81000  24.11300 1.000 111.52883 ? 362 ILE A CG1   1 
ATOM 3017 C CG2   . ILE B 2 362 ? 20.01000  65.94300  23.18700 1.000 97.39640  ? 362 ILE A CG2   1 
ATOM 3018 C CD1   . ILE B 2 362 ? 22.76900  65.41000  24.03900 1.000 115.17047 ? 362 ILE A CD1   1 
ATOM 3019 N N     . LEU B 2 363 ? 18.01200  68.30500  25.37200 1.000 90.70254  ? 363 LEU A N     1 
ATOM 3020 C CA    . LEU B 2 363 ? 16.53500  68.34700  25.50500 1.000 94.63824  ? 363 LEU A CA    1 
ATOM 3021 C C     . LEU B 2 363 ? 16.03000  69.59500  24.77400 1.000 92.20756  ? 363 LEU A C     1 
ATOM 3022 O O     . LEU B 2 363 ? 15.06800  69.47800  23.99300 1.000 85.17465  ? 363 LEU A O     1 
ATOM 3023 C CB    . LEU B 2 363 ? 16.14300  68.37400  26.98000 1.000 96.47260  ? 363 LEU A CB    1 
ATOM 3024 C CG    . LEU B 2 363 ? 14.66362  68.62320  27.29062 1.000 90.77522  ? 363 LEU A CG    1 
ATOM 3025 C CD1   . LEU B 2 363 ? 13.81607  67.49525  26.72961 1.000 89.45204  ? 363 LEU A CD1   1 
ATOM 3026 C CD2   . LEU B 2 363 ? 14.41637  68.79423  28.77674 1.000 84.77212  ? 363 LEU A CD2   1 
ATOM 3027 N N     . LYS B 2 364 ? 16.68100  70.73600  25.00500 1.000 100.86870 ? 364 LYS A N     1 
ATOM 3028 C CA    . LYS B 2 364 ? 16.25400  71.99900  24.35600 1.000 101.22939 ? 364 LYS A CA    1 
ATOM 3029 C C     . LYS B 2 364 ? 16.23100  71.78500  22.84000 1.000 90.82329  ? 364 LYS A C     1 
ATOM 3030 O O     . LYS B 2 364 ? 15.20200  72.10300  22.20800 1.000 97.66549  ? 364 LYS A O     1 
ATOM 3031 C CB    . LYS B 2 364 ? 17.23800  73.11800  24.70400 1.000 84.34290  ? 364 LYS A CB    1 
ATOM 3032 C CG    . LYS B 2 364 ? 17.45200  73.39700  26.18200 1.000 87.04086  ? 364 LYS A CG    1 
ATOM 3033 C CD    . LYS B 2 364 ? 18.73600  74.17200  26.45400 1.000 115.41170 ? 364 LYS A CD    1 
ATOM 3034 C CE    . LYS B 2 364 ? 18.83100  74.70700  27.84600 1.000 116.32564 ? 364 LYS A CE    1 
ATOM 3035 N NZ    . LYS B 2 364 ? 17.90700  75.82300  28.05600 1.000 94.14481  ? 364 LYS A NZ    1 
ATOM 3036 N N     . MET B 2 365 ? 17.31700  71.24000  22.28900 1.000 90.29160  ? 365 MET A N     1 
ATOM 3037 C CA    . MET B 2 365 ? 17.41500  71.04100  20.82000 1.000 101.13729 ? 365 MET A CA    1 
ATOM 3038 C C     . MET B 2 365 ? 16.33600  70.04700  20.36100 1.000 98.55722  ? 365 MET A C     1 
ATOM 3039 O O     . MET B 2 365 ? 15.65400  70.33100  19.35200 1.000 99.75938  ? 365 MET A O     1 
ATOM 3040 C CB    . MET B 2 365 ? 18.81000  70.52400  20.45400 1.000 93.72457  ? 365 MET A CB    1 
ATOM 3041 C CG    . MET B 2 365 ? 19.92800  71.28600  21.13600 1.000 85.46701  ? 365 MET A CG    1 
ATOM 3042 S SD    . MET B 2 365 ? 21.57000  70.73000  20.64000 1.000 75.46388  ? 365 MET A SD    1 
ATOM 3043 C CE    . MET B 2 365 ? 21.42500  70.96300  18.86400 1.000 95.64866  ? 365 MET A CE    1 
ATOM 3044 N N     . GLN B 2 366 ? 16.17900  68.93700  21.08500 1.000 101.30966 ? 366 GLN A N     1 
ATOM 3045 C CA    . GLN B 2 366 ? 15.16700  67.91500  20.71600 1.000 96.36367  ? 366 GLN A CA    1 
ATOM 3046 C C     . GLN B 2 366 ? 13.78400  68.57000  20.69400 1.000 85.53065  ? 366 GLN A C     1 
ATOM 3047 O O     . GLN B 2 366 ? 13.05200  68.37600  19.70500 1.000 91.91287  ? 366 GLN A O     1 
ATOM 3048 C CB    . GLN B 2 366 ? 15.15300  66.77400  21.72900 1.000 86.01120  ? 366 GLN A CB    1 
ATOM 3049 C CG    . GLN B 2 366 ? 16.38600  65.87900  21.68900 1.000 100.20584 ? 366 GLN A CG    1 
ATOM 3050 C CD    . GLN B 2 366 ? 16.37000  64.81300  22.76200 1.000 116.26736 ? 366 GLN A CD    1 
ATOM 3051 O OE1   . GLN B 2 366 ? 15.45600  64.74900  23.59100 1.000 114.82320 ? 366 GLN A OE1   1 
ATOM 3052 N NE2   . GLN B 2 366 ? 17.38900  63.96800  22.76300 1.000 110.63957 ? 366 GLN A NE2   1 
ATOM 3053 N N     . LEU B 2 367 ? 13.45400  69.32900  21.73800 1.000 86.84614  ? 367 LEU A N     1 
ATOM 3054 C CA    . LEU B 2 367 ? 12.10800  69.94700  21.83000 1.000 89.05491  ? 367 LEU A CA    1 
ATOM 3055 C C     . LEU B 2 367 ? 11.88900  70.84300  20.60600 1.000 91.73440  ? 367 LEU A C     1 
ATOM 3056 O O     . LEU B 2 367 ? 10.75700  70.86300  20.08300 1.000 104.71910 ? 367 LEU A O     1 
ATOM 3057 C CB    . LEU B 2 367 ? 11.99000  70.73400  23.13200 1.000 80.98372  ? 367 LEU A CB    1 
ATOM 3058 C CG    . LEU B 2 367 ? 11.94800  69.91000  24.42200 1.000 76.20140  ? 367 LEU A CG    1 
ATOM 3059 C CD1   . LEU B 2 367 ? 12.05500  70.82300  25.63000 1.000 82.09342  ? 367 LEU A CD1   1 
ATOM 3060 C CD2   . LEU B 2 367 ? 10.67600  69.08900  24.48900 1.000 85.01438  ? 367 LEU A CD2   1 
ATOM 3061 N N     . LEU B 2 368 ? 12.93200  71.55000  20.16800 1.000 92.72109  ? 368 LEU A N     1 
ATOM 3062 C CA    . LEU B 2 368 ? 12.77800  72.49500  19.03400 1.000 91.42377  ? 368 LEU A CA    1 
ATOM 3063 C C     . LEU B 2 368 ? 12.33900  71.71400  17.78600 1.000 98.07918  ? 368 LEU A C     1 
ATOM 3064 O O     . LEU B 2 368 ? 11.32400  72.09800  17.16300 1.000 113.24067 ? 368 LEU A O     1 
ATOM 3065 C CB    . LEU B 2 368 ? 14.10500  73.21800  18.82500 1.000 87.71046  ? 368 LEU A CB    1 
ATOM 3066 C CG    . LEU B 2 368 ? 14.01500  74.71000  18.49500 1.000 102.38459 ? 368 LEU A CG    1 
ATOM 3067 C CD1   . LEU B 2 368 ? 13.18100  75.42900  19.54000 1.000 86.29664  ? 368 LEU A CD1   1 
ATOM 3068 C CD2   . LEU B 2 368 ? 15.41300  75.29700  18.43600 1.000 115.75980 ? 368 LEU A CD2   1 
ATOM 3069 N N     . ILE B 2 369 ? 13.05400  70.63700  17.45800 1.000 102.68364 ? 369 ILE A N     1 
ATOM 3070 C CA    . ILE B 2 369 ? 12.67600  69.79700  16.28200 1.000 108.12046 ? 369 ILE A CA    1 
ATOM 3071 C C     . ILE B 2 369 ? 11.30500  69.16400  16.56000 1.000 99.95420  ? 369 ILE A C     1 
ATOM 3072 O O     . ILE B 2 369 ? 10.47700  69.10700  15.62900 1.000 102.40526 ? 369 ILE A O     1 
ATOM 3073 C CB    . ILE B 2 369 ? 13.75800  68.74000  16.00200 1.000 96.11269  ? 369 ILE A CB    1 
ATOM 3074 C CG1   . ILE B 2 369 ? 15.11800  69.39400  15.78400 1.000 97.88599  ? 369 ILE A CG1   1 
ATOM 3075 C CG2   . ILE B 2 369 ? 13.36700  67.84300  14.82800 1.000 95.28977  ? 369 ILE A CG2   1 
ATOM 3076 C CD1   . ILE B 2 369 ? 16.09800  68.53700  15.00600 1.000 111.48502 ? 369 ILE A CD1   1 
ATOM 3077 N N     . TRP B 2 370 ? 11.07300  68.73100  17.79900 1.000 94.84522  ? 370 TRP A N     1 
ATOM 3078 C CA    . TRP B 2 370 ? 9.79700   68.06000  18.15100 1.000 102.16354 ? 370 TRP A CA    1 
ATOM 3079 C C     . TRP B 2 370 ? 8.62100   69.00300  17.91800 1.000 112.80193 ? 370 TRP A C     1 
ATOM 3080 O O     . TRP B 2 370 ? 7.63700   68.56800  17.29200 1.000 121.08531 ? 370 TRP A O     1 
ATOM 3081 C CB    . TRP B 2 370 ? 9.83600   67.60600  19.61600 1.000 103.09149 ? 370 TRP A CB    1 
ATOM 3082 C CG    . TRP B 2 370 ? 8.58700   66.90500  20.07800 1.000 106.95015 ? 370 TRP A CG    1 
ATOM 3083 C CD1   . TRP B 2 370 ? 7.93100   65.89100  19.44700 1.000 108.72217 ? 370 TRP A CD1   1 
ATOM 3084 C CD2   . TRP B 2 370 ? 7.82300   67.19700  21.26800 1.000 109.28912 ? 370 TRP A CD2   1 
ATOM 3085 N NE1   . TRP B 2 370 ? 6.83000   65.51400  20.16800 1.000 107.54441 ? 370 TRP A NE1   1 
ATOM 3086 C CE2   . TRP B 2 370 ? 6.73400   66.30100  21.28500 1.000 99.81378  ? 370 TRP A CE2   1 
ATOM 3087 C CE3   . TRP B 2 370 ? 7.95500   68.11700  22.31300 1.000 106.51228 ? 370 TRP A CE3   1 
ATOM 3088 C CZ2   . TRP B 2 370 ? 5.78700   66.30300  22.30500 1.000 100.98899 ? 370 TRP A CZ2   1 
ATOM 3089 C CZ3   . TRP B 2 370 ? 7.01700   68.11800  23.32100 1.000 106.32200 ? 370 TRP A CZ3   1 
ATOM 3090 C CH2   . TRP B 2 370 ? 5.94800   67.22400  23.31400 1.000 107.07572 ? 370 TRP A CH2   1 
ATOM 3091 N N     . ILE B 2 371 ? 8.72100   70.25200  18.37600 1.000 105.56912 ? 371 ILE A N     1 
ATOM 3092 C CA    . ILE B 2 371 ? 7.55700   71.18600  18.27800 1.000 92.14111  ? 371 ILE A CA    1 
ATOM 3093 C C     . ILE B 2 371 ? 7.25500   71.45800  16.79600 1.000 94.43997  ? 371 ILE A C     1 
ATOM 3094 O O     . ILE B 2 371 ? 6.16700   71.99400  16.50400 1.000 104.26297 ? 371 ILE A O     1 
ATOM 3095 C CB    . ILE B 2 371 ? 7.82200   72.48000  19.07000 1.000 88.22563  ? 371 ILE A CB    1 
ATOM 3096 C CG1   . ILE B 2 371 ? 6.52700   73.22400  19.39600 1.000 88.18881  ? 371 ILE A CG1   1 
ATOM 3097 C CG2   . ILE B 2 371 ? 8.82600   73.37700  18.34900 1.000 106.58407 ? 371 ILE A CG2   1 
ATOM 3098 C CD1   . ILE B 2 371 ? 5.61300   72.48100  20.35400 1.000 104.43099 ? 371 ILE A CD1   1 
ATOM 3099 N N     . THR B 2 372 ? 8.17600   71.09000  15.90300 1.000 104.37631 ? 372 THR A N     1 
ATOM 3100 C CA    . THR B 2 372 ? 7.97000   71.30900  14.45500 1.000 112.66424 ? 372 THR A CA    1 
ATOM 3101 C C     . THR B 2 372 ? 7.29900   70.09700  13.83800 1.000 111.55563 ? 372 THR A C     1 
ATOM 3102 O O     . THR B 2 372 ? 6.75900   70.23200  12.72100 1.000 106.48425 ? 372 THR A O     1 
ATOM 3103 C CB    . THR B 2 372 ? 9.32200   71.62600  13.81500 1.000 119.55859 ? 372 THR A CB    1 
ATOM 3104 O OG1   . THR B 2 372 ? 9.00167   72.08281  12.50567 1.000 136.80971 ? 372 THR A OG1   1 
ATOM 3105 C CG2   . THR B 2 372 ? 10.25594  70.43086  13.74359 1.000 105.90339 ? 372 THR A CG2   1 
ATOM 3106 N N     . GLU B 2 373 ? 7.29200   68.95800  14.53800 1.000 119.64954 ? 373 GLU A N     1 
ATOM 3107 C CA    . GLU B 2 373 ? 6.73800   67.70800  13.95300 1.000 115.56775 ? 373 GLU A CA    1 
ATOM 3108 C C     . GLU B 2 373 ? 5.55600   67.17600  14.77800 1.000 112.79694 ? 373 GLU A C     1 
ATOM 3109 O O     . GLU B 2 373 ? 4.65300   66.56200  14.17300 1.000 113.38819 ? 373 GLU A O     1 
ATOM 3110 C CB    . GLU B 2 373 ? 7.81100   66.62100  13.92000 1.000 101.84683 ? 373 GLU A CB    1 
ATOM 3111 C CG    . GLU B 2 373 ? 9.05900   67.01300  13.13500 1.000 102.17262 ? 373 GLU A CG    1 
ATOM 3112 C CD    . GLU B 2 373 ? 10.12300  65.93200  13.15400 1.000 107.40545 ? 373 GLU A CD    1 
ATOM 3113 O OE1   . GLU B 2 373 ? 9.88800   64.88400  13.78900 1.000 109.34618 ? 373 GLU A OE1   1 
ATOM 3114 O OE2   . GLU B 2 373 ? 11.18400  66.13600  12.53100 1.000 128.82902 ? 373 GLU A OE2   1 
ATOM 3115 N N     . THR B 2 374 ? 5.55600   67.39100  16.09600 1.000 111.49434 ? 374 THR A N     1 
ATOM 3116 C CA    . THR B 2 374 ? 4.49900   66.80100  16.95100 1.000 112.26576 ? 374 THR A CA    1 
ATOM 3117 C C     . THR B 2 374 ? 3.13600   67.26100  16.48800 1.000 108.93827 ? 374 THR A C     1 
ATOM 3118 O O     . THR B 2 374 ? 2.96500   68.47100  16.22900 1.000 103.77878 ? 374 THR A O     1 
ATOM 3119 C CB    . THR B 2 374 ? 4.74200   67.14200  18.42200 1.000 115.84944 ? 374 THR A CB    1 
ATOM 3120 O OG1   . THR B 2 374 ? 3.69500   66.48700  19.13100 1.000 115.36565 ? 374 THR A OG1   1 
ATOM 3121 C CG2   . THR B 2 374 ? 4.70500   68.63300  18.70800 1.000 114.50628 ? 374 THR A CG2   1 
ATOM 3122 N N     . PRO B 2 375 ? 2.15400   66.34700  16.33600 1.000 114.41686 ? 375 PRO A N     1 
ATOM 3123 C CA    . PRO B 2 375 ? 0.79800   66.74500  15.99600 1.000 102.24742 ? 375 PRO A CA    1 
ATOM 3124 C C     . PRO B 2 375 ? -0.09500  66.84100  17.22000 1.000 102.11243 ? 375 PRO A C     1 
ATOM 3125 O O     . PRO B 2 375 ? -1.19900  67.40800  17.11300 1.000 95.30075  ? 375 PRO A O     1 
ATOM 3126 C CB    . PRO B 2 375 ? 0.41700   65.57000  15.09700 1.000 102.33267 ? 375 PRO A CB    1 
ATOM 3127 C CG    . PRO B 2 375 ? 1.06900   64.37500  15.75800 1.000 104.37216 ? 375 PRO A CG    1 
ATOM 3128 C CD    . PRO B 2 375 ? 2.33600   64.90600  16.40900 1.000 115.82122 ? 375 PRO A CD    1 
ATOM 3129 N N     . SER B 2 376 ? 0.36500   66.31300  18.35800 1.000 102.09406 ? 376 SER A N     1 
ATOM 3130 C CA    . SER B 2 376 ? -0.47300  66.28500  19.58500 1.000 106.29323 ? 376 SER A CA    1 
ATOM 3131 C C     . SER B 2 376 ? 0.15500   67.15700  20.67600 1.000 113.31146 ? 376 SER A C     1 
ATOM 3132 O O     . SER B 2 376 ? -0.57800  67.96400  21.28100 1.000 107.09551 ? 376 SER A O     1 
ATOM 3133 C CB    . SER B 2 376 ? -0.64100  64.87700  20.07100 1.000 122.66982 ? 376 SER A CB    1 
ATOM 3134 O OG    . SER B 2 376 ? 0.62300   64.29000  20.34700 1.000 119.25050 ? 376 SER A OG    1 
ATOM 3135 N N     . GLY B 2 377 ? 1.45300   66.98000  20.92300 1.000 121.48039 ? 377 GLY A N     1 
ATOM 3136 C CA    . GLY B 2 377 ? 2.14000   67.76000  21.96800 1.000 112.17257 ? 377 GLY A CA    1 
ATOM 3137 C C     . GLY B 2 377 ? 2.24500   66.97600  23.25900 1.000 116.99854 ? 377 GLY A C     1 
ATOM 3138 O O     . GLY B 2 377 ? 2.72200   67.54300  24.26000 1.000 118.91405 ? 377 GLY A O     1 
ATOM 3139 N N     . ASP B 2 378 ? 1.82300   65.71300  23.24200 1.000 107.22263 ? 378 ASP A N     1 
ATOM 3140 C CA    . ASP B 2 378 ? 1.96200   64.86000  24.45100 1.000 105.07318 ? 378 ASP A CA    1 
ATOM 3141 C C     . ASP B 2 378 ? 3.44200   64.80600  24.83800 1.000 109.73223 ? 378 ASP A C     1 
ATOM 3142 O O     . ASP B 2 378 ? 4.24000   64.28000  24.04200 1.000 104.26747 ? 378 ASP A O     1 
ATOM 3143 C CB    . ASP B 2 378 ? 1.36700   63.48100  24.22400 1.000 114.82770 ? 378 ASP A CB    1 
ATOM 3144 C CG    . ASP B 2 378 ? 1.76900   62.42400  25.23900 1.000 121.94382 ? 378 ASP A CG    1 
ATOM 3145 O OD1   . ASP B 2 378 ? 1.51600   62.64200  26.44200 1.000 117.77312 ? 378 ASP A OD1   1 
ATOM 3146 O OD2   . ASP B 2 378 ? 2.32700   61.39200  24.81600 1.000 124.65767 ? 378 ASP A OD2   1 
ATOM 3147 N N     . ILE B 2 379 ? 3.78600   65.30100  26.02800 1.000 100.46100 ? 379 ILE A N     1 
ATOM 3148 C CA    . ILE B 2 379 ? 5.21500   65.34600  26.46100 1.000 91.26167  ? 379 ILE A CA    1 
ATOM 3149 C C     . ILE B 2 379 ? 5.74000   63.90700  26.57900 1.000 99.12370  ? 379 ILE A C     1 
ATOM 3150 O O     . ILE B 2 379 ? 6.97300   63.73300  26.64700 1.000 102.57765 ? 379 ILE A O     1 
ATOM 3151 C CB    . ILE B 2 379 ? 5.35400   66.10800  27.78800 1.000 86.69654  ? 379 ILE A CB    1 
ATOM 3152 C CG1   . ILE B 2 379 ? 4.75500   65.31900  28.95100 1.000 115.39618 ? 379 ILE A CG1   1 
ATOM 3153 C CG2   . ILE B 2 379 ? 4.74600   67.50600  27.67900 1.000 96.58862  ? 379 ILE A CG2   1 
ATOM 3154 C CD1   . ILE B 2 379 ? 5.04000   65.91700  30.31600 1.000 116.81920 ? 379 ILE A CD1   1 
ATOM 3155 N N     . GLN B 2 380 ? 4.83700   62.92500  26.60800 1.000 106.26859 ? 380 GLN A N     1 
ATOM 3156 C CA    . GLN B 2 380 ? 5.24800   61.50800  26.77500 1.000 111.70886 ? 380 GLN A CA    1 
ATOM 3157 C C     . GLN B 2 380 ? 5.65600   60.92800  25.41300 1.000 95.84551  ? 380 GLN A C     1 
ATOM 3158 O O     . GLN B 2 380 ? 6.25300   59.83200  25.39900 1.000 90.85623  ? 380 GLN A O     1 
ATOM 3159 C CB    . GLN B 2 380 ? 4.11200   60.71000  27.41400 1.000 92.67546  ? 380 GLN A CB    1 
ATOM 3160 C CG    . GLN B 2 380 ? 3.59500   61.31300  28.71500 1.000 111.25850 ? 380 GLN A CG    1 
ATOM 3161 C CD    . GLN B 2 380 ? 2.43300   60.54700  29.30800 1.000 144.55215 ? 380 GLN A CD    1 
ATOM 3162 O OE1   . GLN B 2 380 ? 1.38000   60.38800  28.68200 1.000 128.31278 ? 380 GLN A OE1   1 
ATOM 3163 N NE2   . GLN B 2 380 ? 2.61600   60.06000  30.52700 1.000 155.35239 ? 380 GLN A NE2   1 
ATOM 3164 N N     . GLU B 2 381 ? 5.35600   61.63300  24.31900 1.000 99.30152  ? 381 GLU A N     1 
ATOM 3165 C CA    . GLU B 2 381 ? 5.82000   61.15500  22.99200 1.000 103.78531 ? 381 GLU A CA    1 
ATOM 3166 C C     . GLU B 2 381 ? 7.32800   60.91900  23.10400 1.000 94.20713  ? 381 GLU A C     1 
ATOM 3167 O O     . GLU B 2 381 ? 7.80100   59.85000  22.66700 1.000 114.98244 ? 381 GLU A O     1 
ATOM 3168 C CB    . GLU B 2 381 ? 5.52400   62.17100  21.89100 1.000 107.56710 ? 381 GLU A CB    1 
ATOM 3169 C CG    . GLU B 2 381 ? 4.03700   62.34800  21.59800 1.000 106.23997 ? 381 GLU A CG    1 
ATOM 3170 C CD    . GLU B 2 381 ? 3.75000   63.48700  20.63600 1.000 125.84981 ? 381 GLU A CD    1 
ATOM 3171 O OE1   . GLU B 2 381 ? 4.24300   63.43400  19.49000 1.000 112.51123 ? 381 GLU A OE1   1 
ATOM 3172 O OE2   . GLU B 2 381 ? 3.03800   64.43200  21.03400 1.000 123.41121 ? 381 GLU A OE2   1 
ATOM 3173 N N     . LEU B 2 382 ? 8.04600   61.88300  23.68100 1.000 91.78813  ? 382 LEU A N     1 
ATOM 3174 C CA    . LEU B 2 382 ? 9.50000   61.70500  23.90900 1.000 109.74481 ? 382 LEU A CA    1 
ATOM 3175 C C     . LEU B 2 382 ? 9.67500   60.78300  25.12100 1.000 117.96625 ? 382 LEU A C     1 
ATOM 3176 O O     . LEU B 2 382 ? 8.92900   60.95200  26.10700 1.000 116.00493 ? 382 LEU A O     1 
ATOM 3177 C CB    . LEU B 2 382 ? 10.14100  63.07300  24.13300 1.000 98.77113  ? 382 LEU A CB    1 
ATOM 3178 C CG    . LEU B 2 382 ? 11.61400  63.07400  24.55400 1.000 113.32341 ? 382 LEU A CG    1 
ATOM 3179 C CD1   . LEU B 2 382 ? 12.48000  62.34000  23.54700 1.000 94.89257  ? 382 LEU A CD1   1 
ATOM 3180 C CD2   . LEU B 2 382 ? 12.10000  64.50000  24.73100 1.000 124.20732 ? 382 LEU A CD2   1 
ATOM 3181 N N     . ASN B 2 383 ? 10.62500  59.85000  25.04700 1.000 110.32166 ? 383 ASN A N     1 
ATOM 3182 C CA    . ASN B 2 383 ? 10.85300  58.89600  26.16400 1.000 108.30912 ? 383 ASN A CA    1 
ATOM 3183 C C     . ASN B 2 383 ? 11.59600  59.62600  27.28500 1.000 115.16798 ? 383 ASN A C     1 
ATOM 3184 O O     . ASN B 2 383 ? 12.75900  59.26500  27.55500 1.000 127.71301 ? 383 ASN A O     1 
ATOM 3185 C CB    . ASN B 2 383 ? 11.62800  57.67400  25.69100 1.000 139.55805 ? 383 ASN A CB    1 
ATOM 3186 C CG    . ASN B 2 383 ? 11.16400  57.20500  24.33300 1.000 140.66269 ? 383 ASN A CG    1 
ATOM 3187 O OD1   . ASN B 2 383 ? 11.94900  57.19500  23.38000 1.000 136.63528 ? 383 ASN A OD1   1 
ATOM 3188 N ND2   . ASN B 2 383 ? 9.89900   56.82600  24.22100 1.000 108.65870 ? 383 ASN A ND2   1 
ATOM 3189 N N     . LEU B 2 384 ? 10.95000  60.61500  27.90600 1.000 112.58798 ? 384 LEU A N     1 
ATOM 3190 C CA    . LEU B 2 384 ? 11.62200  61.41400  28.96000 1.000 105.72539 ? 384 LEU A CA    1 
ATOM 3191 C C     . LEU B 2 384 ? 12.08200  60.47000  30.07700 1.000 115.74712 ? 384 LEU A C     1 
ATOM 3192 O O     . LEU B 2 384 ? 11.22500  59.76200  30.64300 1.000 123.19148 ? 384 LEU A O     1 
ATOM 3193 C CB    . LEU B 2 384 ? 10.66900  62.48200  29.48700 1.000 117.57124 ? 384 LEU A CB    1 
ATOM 3194 C CG    . LEU B 2 384 ? 10.44500  63.68900  28.57200 1.000 106.72498 ? 384 LEU A CG    1 
ATOM 3195 C CD1   . LEU B 2 384 ? 9.29900   64.53000  29.10200 1.000 119.67165 ? 384 LEU A CD1   1 
ATOM 3196 C CD2   . LEU B 2 384 ? 11.71700  64.51300  28.48900 1.000 82.17934  ? 384 LEU A CD2   1 
ATOM 3197 N N     . LYS B 2 385 ? 13.38100  60.47400  30.37900 1.000 113.04088 ? 385 LYS A N     1 
ATOM 3198 C CA    . LYS B 2 385 ? 13.92900  59.58600  31.43500 1.000 102.35175 ? 385 LYS A CA    1 
ATOM 3199 C C     . LYS B 2 385 ? 15.19700  60.22100  32.01900 1.000 95.35806  ? 385 LYS A C     1 
ATOM 3200 O O     . LYS B 2 385 ? 15.74000  61.15000  31.38800 1.000 131.67313 ? 385 LYS A O     1 
ATOM 3201 C CB    . LYS B 2 385 ? 14.22200  58.19600  30.86200 1.000 106.20671 ? 385 LYS A CB    1 
ATOM 3202 C CG    . LYS B 2 385 ? 15.09700  58.17700  29.61800 1.000 117.92226 ? 385 LYS A CG    1 
ATOM 3203 C CD    . LYS B 2 385 ? 15.13100  56.80900  28.94800 1.000 133.40485 ? 385 LYS A CD    1 
ATOM 3204 C CE    . LYS B 2 385 ? 15.85700  56.82400  27.64200 1.000 143.99763 ? 385 LYS A CE    1 
ATOM 3205 N NZ    . LYS B 2 385 ? 15.82400  55.51000  26.99300 1.000 134.73303 ? 385 LYS A NZ    1 
ATOM 3206 N N     . GLY B 2 386 ? 15.63300  59.74500  33.18500 1.000 90.03292  ? 386 GLY A N     1 
ATOM 3207 C CA    . GLY B 2 386 ? 16.86600  60.26500  33.80200 1.000 93.14400  ? 386 GLY A CA    1 
ATOM 3208 C C     . GLY B 2 386 ? 16.74400  61.73400  34.14800 1.000 112.55494 ? 386 GLY A C     1 
ATOM 3209 O O     . GLY B 2 386 ? 15.61500  62.18500  34.43100 1.000 107.25940 ? 386 GLY A O     1 
ATOM 3210 N N     . GLY B 2 387 ? 17.86300  62.46100  34.11700 1.000 100.25712 ? 387 GLY A N     1 
ATOM 3211 C CA    . GLY B 2 387 ? 17.85800  63.88600  34.49700 1.000 100.81657 ? 387 GLY A CA    1 
ATOM 3212 C C     . GLY B 2 387 ? 16.90600  64.68100  33.63000 1.000 104.24413 ? 387 GLY A C     1 
ATOM 3213 O O     . GLY B 2 387 ? 16.25500  65.60500  34.15700 1.000 110.10689 ? 387 GLY A O     1 
ATOM 3214 N N     . GLN B 2 388 ? 16.82400  64.33400  32.34600 1.000 93.42005  ? 388 GLN A N     1 
ATOM 3215 C CA    . GLN B 2 388 ? 15.92800  65.06400  31.41800 1.000 96.68180  ? 388 GLN A CA    1 
ATOM 3216 C C     . GLN B 2 388 ? 14.50800  65.02400  31.99400 1.000 90.72492  ? 388 GLN A C     1 
ATOM 3217 O O     . GLN B 2 388 ? 13.86700  66.09200  32.07600 1.000 99.14276  ? 388 GLN A O     1 
ATOM 3218 C CB    . GLN B 2 388 ? 15.99000  64.42700  30.03200 1.000 92.76791  ? 388 GLN A CB    1 
ATOM 3219 C CG    . GLN B 2 388 ? 17.33000  64.60900  29.32800 1.000 101.17116 ? 388 GLN A CG    1 
ATOM 3220 C CD    . GLN B 2 388 ? 17.29200  64.22400  27.86600 1.000 126.01177 ? 388 GLN A CD    1 
ATOM 3221 O OE1   . GLN B 2 388 ? 16.25900  63.80100  27.33700 1.000 129.46758 ? 388 GLN A OE1   1 
ATOM 3222 N NE2   . GLN B 2 388 ? 18.42500  64.37100  27.19500 1.000 121.81959 ? 388 GLN A NE2   1 
ATOM 3223 N N     . LYS B 2 389 ? 14.05500  63.83900  32.40400 1.000 91.77580  ? 389 LYS A N     1 
ATOM 3224 C CA    . LYS B 2 389 ? 12.67800  63.69600  32.94000 1.000 94.36584  ? 389 LYS A CA    1 
ATOM 3225 C C     . LYS B 2 389 ? 12.54800  64.53500  34.21600 1.000 91.85975  ? 389 LYS A C     1 
ATOM 3226 O O     . LYS B 2 389 ? 11.58000  65.31600  34.31900 1.000 87.87423  ? 389 LYS A O     1 
ATOM 3227 C CB    . LYS B 2 389 ? 12.37900  62.22600  33.24500 1.000 102.80661 ? 389 LYS A CB    1 
ATOM 3228 C CG    . LYS B 2 389 ? 11.02600  61.97600  33.88700 1.000 107.06104 ? 389 LYS A CG    1 
ATOM 3229 C CD    . LYS B 2 389 ? 10.73000  60.50800  34.16500 1.000 108.81042 ? 389 LYS A CD    1 
ATOM 3230 C CE    . LYS B 2 389 ? 9.48200   60.34800  34.97300 1.000 132.26376 ? 389 LYS A CE    1 
ATOM 3231 N NZ    . LYS B 2 389 ? 8.35700   61.07000  34.37600 1.000 131.11790 ? 389 LYS A NZ    1 
ATOM 3232 N N     . MET B 2 390 ? 13.50600  64.39500  35.13200 1.000 91.42300  ? 390 MET A N     1 
ATOM 3233 C CA    . MET B 2 390 ? 13.44100  65.13600  36.41600 1.000 97.84206  ? 390 MET A CA    1 
ATOM 3234 C C     . MET B 2 390 ? 13.33500  66.63400  36.10900 1.000 106.67277 ? 390 MET A C     1 
ATOM 3235 O O     . MET B 2 390 ? 12.43800  67.29300  36.67700 1.000 113.66721 ? 390 MET A O     1 
ATOM 3236 C CB    . MET B 2 390 ? 14.70000  64.86500  37.24500 1.000 79.63352  ? 390 MET A CB    1 
ATOM 3237 C CG    . MET B 2 390 ? 14.48500  64.93300  38.74200 1.000 105.39404 ? 390 MET A CG    1 
ATOM 3238 S SD    . MET B 2 390 ? 15.91600  64.29100  39.63300 1.000 120.38398 ? 390 MET A SD    1 
ATOM 3239 C CE    . MET B 2 390 ? 16.21100  62.77100  38.72000 1.000 74.25186  ? 390 MET A CE    1 
ATOM 3240 N N     . TYR B 2 391 ? 14.18600  67.13600  35.21200 1.000 85.69583  ? 391 TYR A N     1 
ATOM 3241 C CA    . TYR B 2 391 ? 14.20100  68.59100  34.90200 1.000 87.32965  ? 391 TYR A CA    1 
ATOM 3242 C C     . TYR B 2 391 ? 12.86600  69.01500  34.31600 1.000 91.22173  ? 391 TYR A C     1 
ATOM 3243 O O     . TYR B 2 391 ? 12.27000  69.99500  34.80700 1.000 96.09986  ? 391 TYR A O     1 
ATOM 3244 C CB    . TYR B 2 391 ? 15.32900  68.88900  33.91100 1.000 93.06513  ? 391 TYR A CB    1 
ATOM 3245 C CG    . TYR B 2 391 ? 15.31800  70.30300  33.34600 1.000 91.77355  ? 391 TYR A CG    1 
ATOM 3246 C CD1   . TYR B 2 391 ? 15.93400  71.34800  34.02200 1.000 93.46619  ? 391 TYR A CD1   1 
ATOM 3247 C CD2   . TYR B 2 391 ? 14.70300  70.58800  32.13400 1.000 91.96471  ? 391 TYR A CD2   1 
ATOM 3248 C CE1   . TYR B 2 391 ? 15.92900  72.63600  33.51500 1.000 115.97178 ? 391 TYR A CE1   1 
ATOM 3249 C CE2   . TYR B 2 391 ? 14.69000  71.87200  31.61700 1.000 93.46521  ? 391 TYR A CE2   1 
ATOM 3250 C CZ    . TYR B 2 391 ? 15.30600  72.89900  32.30800 1.000 111.52024 ? 391 TYR A CZ    1 
ATOM 3251 O OH    . TYR B 2 391 ? 15.30100  74.16700  31.80600 1.000 116.57852 ? 391 TYR A OH    1 
ATOM 3252 N N     . PHE B 2 392 ? 12.39300  68.29800  33.29900 1.000 82.87687  ? 392 PHE A N     1 
ATOM 3253 C CA    . PHE B 2 392 ? 11.15100  68.73700  32.61000 1.000 79.60350  ? 392 PHE A CA    1 
ATOM 3254 C C     . PHE B 2 392 ? 9.99500   68.73000  33.60300 1.000 89.40717  ? 392 PHE A C     1 
ATOM 3255 O O     . PHE B 2 392 ? 9.19300   69.68200  33.59900 1.000 100.64707 ? 392 PHE A O     1 
ATOM 3256 C CB    . PHE B 2 392 ? 10.87300  67.86200  31.38600 1.000 81.65736  ? 392 PHE A CB    1 
ATOM 3257 C CG    . PHE B 2 392 ? 10.22900  68.62100  30.23600 1.000 89.18112  ? 392 PHE A CG    1 
ATOM 3258 C CD1   . PHE B 2 392 ? 10.65974  69.89876  29.89977 1.000 77.45589  ? 392 PHE A CD1   1 
ATOM 3259 C CD2   . PHE B 2 392 ? 9.19170   68.06216  29.50003 1.000 102.31430 ? 392 PHE A CD2   1 
ATOM 3260 C CE1   . PHE B 2 392 ? 10.07318  70.59196  28.85465 1.000 90.97661  ? 392 PHE A CE1   1 
ATOM 3261 C CE2   . PHE B 2 392 ? 8.60884   68.75997  28.45527 1.000 104.68695 ? 392 PHE A CE2   1 
ATOM 3262 C CZ    . PHE B 2 392 ? 9.04986   70.02151  28.13530 1.000 100.95974 ? 392 PHE A CZ    1 
ATOM 3263 N N     . ASP B 2 393 ? 9.90400   67.68800  34.43000 1.000 71.81442  ? 393 ASP A N     1 
ATOM 3264 C CA    . ASP B 2 393 ? 8.74800   67.58800  35.36200 1.000 85.12622  ? 393 ASP A CA    1 
ATOM 3265 C C     . ASP B 2 393 ? 8.78500   68.78500  36.31500 1.000 90.01487  ? 393 ASP A C     1 
ATOM 3266 O O     . ASP B 2 393 ? 7.72700   69.41000  36.52800 1.000 89.18736  ? 393 ASP A O     1 
ATOM 3267 C CB    . ASP B 2 393 ? 8.72000   66.25200  36.08500 1.000 100.39616 ? 393 ASP A CB    1 
ATOM 3268 C CG    . ASP B 2 393 ? 8.31900   65.05600  35.23300 1.000 110.82913 ? 393 ASP A CG    1 
ATOM 3269 O OD1   . ASP B 2 393 ? 7.22900   65.10800  34.62800 1.000 113.17521 ? 393 ASP A OD1   1 
ATOM 3270 O OD2   . ASP B 2 393 ? 9.08900   64.07600  35.20000 1.000 103.45595 ? 393 ASP A OD2   1 
ATOM 3271 N N     . GLN B 2 394 ? 9.96500   69.09800  36.85000 1.000 97.21914  ? 394 GLN A N     1 
ATOM 3272 C CA    . GLN B 2 394 ? 10.10800  70.26100  37.75900 1.000 98.05358  ? 394 GLN A CA    1 
ATOM 3273 C C     . GLN B 2 394 ? 9.64600   71.52000  37.01900 1.000 97.13752  ? 394 GLN A C     1 
ATOM 3274 O O     . GLN B 2 394 ? 8.84100   72.28300  37.58800 1.000 99.46781  ? 394 GLN A O     1 
ATOM 3275 C CB    . GLN B 2 394 ? 11.57100  70.38500  38.18000 1.000 88.11467  ? 394 GLN A CB    1 
ATOM 3276 C CG    . GLN B 2 394 ? 11.94000  71.73000  38.79300 1.000 99.21717  ? 394 GLN A CG    1 
ATOM 3277 C CD    . GLN B 2 394 ? 11.73700  71.77200  40.29000 1.000 105.46967 ? 394 GLN A CD    1 
ATOM 3278 O OE1   . GLN B 2 394 ? 11.32300  70.78600  40.90900 1.000 124.69780 ? 394 GLN A OE1   1 
ATOM 3279 N NE2   . GLN B 2 394 ? 12.04100  72.91500  40.88800 1.000 93.54916  ? 394 GLN A NE2   1 
ATOM 3280 N N     . LYS B 2 395 ? 10.12100  71.70900  35.78600 1.000 82.57281  ? 395 LYS A N     1 
ATOM 3281 C CA    . LYS B 2 395 ? 9.77200   72.92600  35.01200 1.000 91.87948  ? 395 LYS A CA    1 
ATOM 3282 C C     . LYS B 2 395 ? 8.25600   72.97100  34.78400 1.000 85.00382  ? 395 LYS A C     1 
ATOM 3283 O O     . LYS B 2 395 ? 7.66700   74.05600  34.96000 1.000 85.04130  ? 395 LYS A O     1 
ATOM 3284 C CB    . LYS B 2 395 ? 10.52500  72.91900  33.67800 1.000 75.78815  ? 395 LYS A CB    1 
ATOM 3285 C CG    . LYS B 2 395 ? 11.43600  74.11400  33.44900 1.000 89.45052  ? 395 LYS A CG    1 
ATOM 3286 C CD    . LYS B 2 395 ? 12.51700  74.25500  34.51300 1.000 83.74670  ? 395 LYS A CD    1 
ATOM 3287 C CE    . LYS B 2 395 ? 13.35600  75.47400  34.30500 1.000 113.15410 ? 395 LYS A CE    1 
ATOM 3288 N NZ    . LYS B 2 395 ? 14.42800  75.56800  35.29800 1.000 124.67095 ? 395 LYS A NZ    1 
ATOM 3289 N N     . ILE B 2 396 ? 7.65200   71.83800  34.42000 1.000 94.08499  ? 396 ILE A N     1 
ATOM 3290 C CA    . ILE B 2 396 ? 6.19100   71.81900  34.10300 1.000 98.15966  ? 396 ILE A CA    1 
ATOM 3291 C C     . ILE B 2 396 ? 5.40300   72.10000  35.39000 1.000 93.33696  ? 396 ILE A C     1 
ATOM 3292 O O     . ILE B 2 396 ? 4.30800   72.69200  35.29600 1.000 84.77711  ? 396 ILE A O     1 
ATOM 3293 C CB    . ILE B 2 396 ? 5.78700   70.48900  33.43700 1.000 74.82794  ? 396 ILE A CB    1 
ATOM 3294 C CG1   . ILE B 2 396 ? 4.76500   70.71500  32.32400 1.000 86.56183  ? 396 ILE A CG1   1 
ATOM 3295 C CG2   . ILE B 2 396 ? 5.29100   69.46800  34.46100 1.000 88.74517  ? 396 ILE A CG2   1 
ATOM 3296 C CD1   . ILE B 2 396 ? 4.61200   69.53900  31.37900 1.000 97.88357  ? 396 ILE A CD1   1 
ATOM 3297 N N     . GLU B 2 397 ? 5.94800   71.69900  36.53900 1.000 90.74318  ? 397 GLU A N     1 
ATOM 3298 C CA    . GLU B 2 397 ? 5.25600   71.91100  37.83500 1.000 97.41379  ? 397 GLU A CA    1 
ATOM 3299 C C     . GLU B 2 397 ? 5.42000   73.37100  38.26900 1.000 92.57499  ? 397 GLU A C     1 
ATOM 3300 O O     . GLU B 2 397 ? 4.44500   73.94200  38.79700 1.000 93.58075  ? 397 GLU A O     1 
ATOM 3301 C CB    . GLU B 2 397 ? 5.84600   70.95600  38.87000 1.000 92.87272  ? 397 GLU A CB    1 
ATOM 3302 C CG    . GLU B 2 397 ? 5.16400   71.04000  40.23200 1.000 108.96442 ? 397 GLU A CG    1 
ATOM 3303 C CD    . GLU B 2 397 ? 5.72500   70.05600  41.24100 1.000 116.74243 ? 397 GLU A CD    1 
ATOM 3304 O OE1   . GLU B 2 397 ? 6.64800   69.30000  40.87400 1.000 104.41399 ? 397 GLU A OE1   1 
ATOM 3305 O OE2   . GLU B 2 397 ? 5.24200   70.04800  42.39200 1.000 112.99362 ? 397 GLU A OE2   1 
ATOM 3306 N N     . THR B 2 398 ? 6.59800   73.95500  38.03700 1.000 89.76640  ? 398 THR A N     1 
ATOM 3307 C CA    . THR B 2 398 ? 6.87000   75.33300  38.50400 1.000 83.57832  ? 398 THR A CA    1 
ATOM 3308 C C     . THR B 2 398 ? 6.50600   76.33700  37.43100 1.000 90.85419  ? 398 THR A C     1 
ATOM 3309 O O     . THR B 2 398 ? 6.77700   77.53800  37.63900 1.000 93.12436  ? 398 THR A O     1 
ATOM 3310 C CB    . THR B 2 398 ? 8.34400   75.43100  38.88700 1.000 80.61894  ? 398 THR A CB    1 
ATOM 3311 O OG1   . THR B 2 398 ? 9.04900   75.07800  37.70200 1.000 108.05074 ? 398 THR A OG1   1 
ATOM 3312 C CG2   . THR B 2 398 ? 8.71900   74.48400  40.01200 1.000 71.23073  ? 398 THR A CG2   1 
ATOM 3313 N N     . TYR B 2 399 ? 5.92000   75.88100  36.32300 1.000 87.17057  ? 399 TYR A N     1 
ATOM 3314 C CA    . TYR B 2 399 ? 5.59500   76.79500  35.19400 1.000 95.79250  ? 399 TYR A CA    1 
ATOM 3315 C C     . TYR B 2 399 ? 4.46200   77.72300  35.60100 1.000 103.64311 ? 399 TYR A C     1 
ATOM 3316 O O     . TYR B 2 399 ? 3.46900   77.24400  36.18400 1.000 111.73027 ? 399 TYR A O     1 
ATOM 3317 C CB    . TYR B 2 399 ? 5.18600   76.00900  33.94600 1.000 85.07562  ? 399 TYR A CB    1 
ATOM 3318 C CG    . TYR B 2 399 ? 4.82800   76.86200  32.73700 1.000 105.22135 ? 399 TYR A CG    1 
ATOM 3319 C CD1   . TYR B 2 399 ? 5.49400   78.05300  32.47200 1.000 97.18451  ? 399 TYR A CD1   1 
ATOM 3320 C CD2   . TYR B 2 399 ? 3.81300   76.48300  31.86800 1.000 116.13507 ? 399 TYR A CD2   1 
ATOM 3321 C CE1   . TYR B 2 399 ? 5.16600   78.83500  31.37800 1.000 105.73426 ? 399 TYR A CE1   1 
ATOM 3322 C CE2   . TYR B 2 399 ? 3.47700   77.25500  30.76900 1.000 117.13726 ? 399 TYR A CE2   1 
ATOM 3323 C CZ    . TYR B 2 399 ? 4.15600   78.43500  30.52300 1.000 119.12209 ? 399 TYR A CZ    1 
ATOM 3324 O OH    . TYR B 2 399 ? 3.82900   79.20100  29.44300 1.000 124.33099 ? 399 TYR A OH    1 
ATOM 3325 N N     . VAL B 2 400 ? 4.60100   79.01700  35.30400 1.000 105.83338 ? 400 VAL A N     1 
ATOM 3326 C CA    . VAL B 2 400 ? 3.50200   79.99000  35.58100 1.000 103.99318 ? 400 VAL A CA    1 
ATOM 3327 C C     . VAL B 2 400 ? 3.03500   80.54000  34.22800 1.000 111.46803 ? 400 VAL A C     1 
ATOM 3328 O O     . VAL B 2 400 ? 3.56800   81.58100  33.79300 1.000 96.21604  ? 400 VAL A O     1 
ATOM 3329 C CB    . VAL B 2 400 ? 3.94500   81.12400  36.52200 1.000 103.03896 ? 400 VAL A CB    1 
ATOM 3330 C CG1   . VAL B 2 400 ? 2.77100   82.00700  36.92900 1.000 105.90208 ? 400 VAL A CG1   1 
ATOM 3331 C CG2   . VAL B 2 400 ? 4.66000   80.58700  37.75500 1.000 94.66183  ? 400 VAL A CG2   1 
ATOM 3332 N N     . PRO B 2 401 ? 2.07300   79.88600  33.54500 1.000 126.85602 ? 401 PRO A N     1 
ATOM 3333 C CA    . PRO B 2 401 ? 1.65800   80.32200  32.21800 1.000 134.73413 ? 401 PRO A CA    1 
ATOM 3334 C C     . PRO B 2 401 ? 1.08700   81.72900  32.22100 1.000 132.35189 ? 401 PRO A C     1 
ATOM 3335 O O     . PRO B 2 401 ? 0.43500   82.11700  33.21100 1.000 150.03766 ? 401 PRO A O     1 
ATOM 3336 C CB    . PRO B 2 401 ? 0.60600   79.27200  31.83000 1.000 123.13549 ? 401 PRO A CB    1 
ATOM 3337 C CG    . PRO B 2 401 ? 0.11700   78.72900  33.15100 1.000 123.28836 ? 401 PRO A CG    1 
ATOM 3338 C CD    . PRO B 2 401 ? 1.35200   78.72400  34.03000 1.000 116.13084 ? 401 PRO A CD    1 
ATOM 3339 N N     . ALA B 2 402 ? 1.32000   82.47300  31.13600 1.000 117.74196 ? 402 ALA A N     1 
ATOM 3340 C CA    . ALA B 2 402 ? 0.80900   83.86000  31.03600 1.000 128.45129 ? 402 ALA A CA    1 
ATOM 3341 C C     . ALA B 2 402 ? 0.94000   84.37000  29.60000 1.000 136.97695 ? 402 ALA A C     1 
ATOM 3342 O O     . ALA B 2 402 ? 1.41900   83.60500  28.73500 1.000 137.34745 ? 402 ALA A O     1 
ATOM 3343 C CB    . ALA B 2 402 ? 1.56000   84.75100  31.99900 1.000 134.44979 ? 402 ALA A CB    1 
ATOM 3344 N N     . ARG B 2 403 ? 0.51200   85.61200  29.35200 1.000 142.62473 ? 403 ARG A N     1 
ATOM 3345 C CA    . ARG B 2 403 ? 0.65300   86.22900  28.00500 1.000 145.73592 ? 403 ARG A CA    1 
ATOM 3346 C C     . ARG B 2 403 ? 0.04900   85.30500  26.93500 1.000 141.37939 ? 403 ARG A C     1 
ATOM 3347 O O     . ARG B 2 403 ? 0.69900   85.11800  25.88300 1.000 136.51719 ? 403 ARG A O     1 
ATOM 3348 C CB    . ARG B 2 403 ? 2.12800   86.54700  27.73300 1.000 139.20346 ? 403 ARG A CB    1 
ATOM 3349 C CG    . ARG B 2 403 ? 2.74600   87.45400  28.78700 1.000 141.28843 ? 403 ARG A CG    1 
ATOM 3350 C CD    . ARG B 2 403 ? 4.23900   87.65200  28.58300 1.000 145.09713 ? 403 ARG A CD    1 
ATOM 3351 N NE    . ARG B 2 403 ? 4.98300   86.39100  28.66400 1.000 174.79199 ? 403 ARG A NE    1 
ATOM 3352 C CZ    . ARG B 2 403 ? 5.73200   85.89900  27.68500 1.000 157.79360 ? 403 ARG A CZ    1 
ATOM 3353 N NH1   . ARG B 2 403 ? 5.88700   86.58600  26.56900 1.000 136.33838 ? 403 ARG A NH1   1 
ATOM 3354 N NH2   . ARG B 2 403 ? 6.32300   84.72700  27.82700 1.000 142.93888 ? 403 ARG A NH2   1 
ATOM 3355 N N     . HIS B 2 404 ? -1.13500  84.74800  27.19700 1.000 134.14709 ? 404 HIS A N     1 
ATOM 3356 C CA    . HIS B 2 404 ? -1.83000  83.90100  26.18800 1.000 144.55294 ? 404 HIS A CA    1 
ATOM 3357 C C     . HIS B 2 404 ? -0.86200  82.86500  25.60800 1.000 135.86233 ? 404 HIS A C     1 
ATOM 3358 O O     . HIS B 2 404 ? -0.78200  82.73000  24.36800 1.000 123.36690 ? 404 HIS A O     1 
ATOM 3359 C CB    . HIS B 2 404 ? -2.45600  84.77300  25.09400 1.000 143.99727 ? 404 HIS A CB    1 
ATOM 3360 C CG    . HIS B 2 404 ? -3.43700  84.04300  24.23800 1.000 159.09422 ? 404 HIS A CG    1 
ATOM 3361 N ND1   . HIS B 2 404 ? -3.66200  84.35500  22.91500 1.000 161.40261 ? 404 HIS A ND1   1 
ATOM 3362 C CD2   . HIS B 2 404 ? -4.24300  83.01100  24.51700 1.000 151.73472 ? 404 HIS A CD2   1 
ATOM 3363 C CE1   . HIS B 2 404 ? -4.57900  83.53400  22.42300 1.000 147.10435 ? 404 HIS A CE1   1 
ATOM 3364 N NE2   . HIS B 2 404 ? -4.94600  82.71000  23.37900 1.000 134.50117 ? 404 HIS A NE2   1 
ATOM 3365 N N     . ASP B 2 405 ? -0.14300  82.14700  26.47300 1.000 143.76308 ? 405 ASP A N     1 
ATOM 3366 C CA    . ASP B 2 405 ? 0.73800   81.05800  25.97000 1.000 140.33255 ? 405 ASP A CA    1 
ATOM 3367 C C     . ASP B 2 405 ? -0.15600  79.97700  25.35500 1.000 128.95200 ? 405 ASP A C     1 
ATOM 3368 O O     . ASP B 2 405 ? -1.19100  79.64500  25.97000 1.000 139.32816 ? 405 ASP A O     1 
ATOM 3369 C CB    . ASP B 2 405 ? 1.64300   80.51400  27.06200 1.000 127.89456 ? 405 ASP A CB    1 
ATOM 3370 C CG    . ASP B 2 405 ? 0.92300   79.91700  28.26100 1.000 132.60539 ? 405 ASP A CG    1 
ATOM 3371 O OD1   . ASP B 2 405 ? 0.14500   80.65400  28.90100 1.000 141.05754 ? 405 ASP A OD1   1 
ATOM 3372 O OD2   . ASP B 2 405 ? 1.14600   78.72100  28.54100 1.000 129.62492 ? 405 ASP A OD2   1 
ATOM 3373 N N     . VAL B 2 406 ? 0.22400   79.46100  24.18500 1.000 98.57615  ? 406 VAL A N     1 
ATOM 3374 C CA    . VAL B 2 406 ? -0.59400  78.41700  23.50200 1.000 113.25642 ? 406 VAL A CA    1 
ATOM 3375 C C     . VAL B 2 406 ? -0.30500  77.05700  24.15700 1.000 112.32038 ? 406 VAL A C     1 
ATOM 3376 O O     . VAL B 2 406 ? 0.88700   76.69100  24.25500 1.000 112.00295 ? 406 VAL A O     1 
ATOM 3377 C CB    . VAL B 2 406 ? -0.31700  78.39900  21.98700 1.000 117.55609 ? 406 VAL A CB    1 
ATOM 3378 C CG1   . VAL B 2 406 ? 1.17110   78.32541  21.67309 1.000 103.19384 ? 406 VAL A CG1   1 
ATOM 3379 C CG2   . VAL B 2 406 ? -1.09753  77.30900  21.26145 1.000 117.17643 ? 406 VAL A CG2   1 
ATOM 3380 N N     . HIS B 2 407 ? -1.35200  76.35900  24.60900 1.000 103.81831 ? 407 HIS A N     1 
ATOM 3381 C CA    . HIS B 2 407 ? -1.17100  75.00900  25.20900 1.000 119.06030 ? 407 HIS A CA    1 
ATOM 3382 C C     . HIS B 2 407 ? -1.85200  73.97800  24.30600 1.000 115.55614 ? 407 HIS A C     1 
ATOM 3383 O O     . HIS B 2 407 ? -3.02500  74.18300  23.93400 1.000 107.68776 ? 407 HIS A O     1 
ATOM 3384 C CB    . HIS B 2 407 ? -1.69200  74.96900  26.64900 1.000 100.94638 ? 407 HIS A CB    1 
ATOM 3385 C CG    . HIS B 2 407 ? -1.27200  73.73700  27.37700 1.000 114.50757 ? 407 HIS A CG    1 
ATOM 3386 N ND1   . HIS B 2 407 ? -1.96700  73.20100  28.43800 1.000 121.69337 ? 407 HIS A ND1   1 
ATOM 3387 C CD2   . HIS B 2 407 ? -0.21000  72.94500  27.19300 1.000 114.65525 ? 407 HIS A CD2   1 
ATOM 3388 C CE1   . HIS B 2 407 ? -1.33600  72.11800  28.86700 1.000 130.58136 ? 407 HIS A CE1   1 
ATOM 3389 N NE2   . HIS B 2 407 ? -0.26700  71.94300  28.12400 1.000 125.26644 ? 407 HIS A NE2   1 
ATOM 3390 N N     . TYR B 2 408 ? -1.14600  72.89300  23.97900 1.000 112.54657 ? 408 TYR A N     1 
ATOM 3391 C CA    . TYR B 2 408 ? -1.69200  71.87900  23.03300 1.000 114.78784 ? 408 TYR A CA    1 
ATOM 3392 C C     . TYR B 2 408 ? -2.88200  71.15200  23.66600 1.000 114.93106 ? 408 TYR A C     1 
ATOM 3393 O O     . TYR B 2 408 ? -3.59900  70.43100  22.94300 1.000 109.06656 ? 408 TYR A O     1 
ATOM 3394 C CB    . TYR B 2 408 ? -0.55100  70.94800  22.61100 1.000 94.69783  ? 408 TYR A CB    1 
ATOM 3395 C CG    . TYR B 2 408 ? 0.34200   71.50200  21.50800 1.000 106.33173 ? 408 TYR A CG    1 
ATOM 3396 C CD1   . TYR B 2 408 ? 0.52500   72.87000  21.34400 1.000 101.23441 ? 408 TYR A CD1   1 
ATOM 3397 C CD2   . TYR B 2 408 ? 1.00100   70.65500  20.62600 1.000 120.04291 ? 408 TYR A CD2   1 
ATOM 3398 C CE1   . TYR B 2 408 ? 1.33400   73.37500  20.34000 1.000 109.89241 ? 408 TYR A CE1   1 
ATOM 3399 C CE2   . TYR B 2 408 ? 1.81300   71.14600  19.61800 1.000 98.71377  ? 408 TYR A CE2   1 
ATOM 3400 C CZ    . TYR B 2 408 ? 1.98000   72.51100  19.47500 1.000 99.36447  ? 408 TYR A CZ    1 
ATOM 3401 O OH    . TYR B 2 408 ? 2.77900   73.00100  18.48300 1.000 105.23990 ? 408 TYR A OH    1 
ATOM 3402 N N     . TYR B 2 409 ? -3.08500  71.32200  24.97400 1.000 112.27895 ? 409 TYR A N     1 
ATOM 3403 C CA    . TYR B 2 409 ? -4.25400  70.70200  25.65600 1.000 108.56592 ? 409 TYR A CA    1 
ATOM 3404 C C     . TYR B 2 409 ? -5.52300  71.41500  25.20000 1.000 113.73222 ? 409 TYR A C     1 
ATOM 3405 O O     . TYR B 2 409 ? -6.57500  70.75900  25.05800 1.000 124.49012 ? 409 TYR A O     1 
ATOM 3406 C CB    . TYR B 2 409 ? -4.04400  70.75000  27.17200 1.000 111.68813 ? 409 TYR A CB    1 
ATOM 3407 C CG    . TYR B 2 409 ? -5.24400  70.38900  28.03700 1.000 105.39785 ? 409 TYR A CG    1 
ATOM 3408 C CD1   . TYR B 2 409 ? -5.55200  69.06600  28.32500 1.000 97.94787  ? 409 TYR A CD1   1 
ATOM 3409 C CD2   . TYR B 2 409 ? -6.04600  71.37600  28.59800 1.000 110.59855 ? 409 TYR A CD2   1 
ATOM 3410 C CE1   . TYR B 2 409 ? -6.63500  68.73300  29.12300 1.000 100.02445 ? 409 TYR A CE1   1 
ATOM 3411 C CE2   . TYR B 2 409 ? -7.12900  71.05700  29.39900 1.000 113.86975 ? 409 TYR A CE2   1 
ATOM 3412 C CZ    . TYR B 2 409 ? -7.42500  69.73200  29.66200 1.000 110.63083 ? 409 TYR A CZ    1 
ATOM 3413 O OH    . TYR B 2 409 ? -8.49100  69.41600  30.45100 1.000 113.01254 ? 409 TYR A OH    1 
ATOM 3414 N N     . ASN B 2 410 ? -5.43000  72.72600  24.96700 1.000 100.69139 ? 410 ASN A N     1 
ATOM 3415 C CA    . ASN B 2 410 ? -6.62700  73.51500  24.56300 1.000 103.40334 ? 410 ASN A CA    1 
ATOM 3416 C C     . ASN B 2 410 ? -7.13700  73.00800  23.20900 1.000 109.55846 ? 410 ASN A C     1 
ATOM 3417 O O     . ASN B 2 410 ? -8.33800  73.19300  22.92300 1.000 112.03530 ? 410 ASN A O     1 
ATOM 3418 C CB    . ASN B 2 410 ? -6.32700  75.00800  24.57000 1.000 113.98734 ? 410 ASN A CB    1 
ATOM 3419 C CG    . ASN B 2 410 ? -5.86900  75.48100  25.92900 1.000 129.24194 ? 410 ASN A CG    1 
ATOM 3420 O OD1   . ASN B 2 410 ? -5.79000  74.68300  26.86900 1.000 120.37676 ? 410 ASN A OD1   1 
ATOM 3421 N ND2   . ASN B 2 410 ? -5.56800  76.76400  26.05400 1.000 118.17761 ? 410 ASN A ND2   1 
ATOM 3422 N N     . PHE B 2 411 ? -6.26300  72.38800  22.41300 1.000 120.37530 ? 411 PHE A N     1 
ATOM 3423 C CA    . PHE B 2 411 ? -6.67800  71.82100  21.10400 1.000 119.97175 ? 411 PHE A CA    1 
ATOM 3424 C C     . PHE B 2 411 ? -7.80800  70.83600  21.33400 1.000 121.48270 ? 411 PHE A C     1 
ATOM 3425 O O     . PHE B 2 411 ? -8.84000  70.90100  20.63100 1.000 129.01980 ? 411 PHE A O     1 
ATOM 3426 C CB    . PHE B 2 411 ? -5.47300  71.10500  20.49400 1.000 98.60725  ? 411 PHE A CB    1 
ATOM 3427 C CG    . PHE B 2 411 ? -5.74000  70.38100  19.18200 1.000 121.47188 ? 411 PHE A CG    1 
ATOM 3428 C CD1   . PHE B 2 411 ? -6.57900  70.92900  18.22000 1.000 133.18242 ? 411 PHE A CD1   1 
ATOM 3429 C CD2   . PHE B 2 411 ? -5.16600  69.14200  18.92600 1.000 122.75562 ? 411 PHE A CD2   1 
ATOM 3430 C CE1   . PHE B 2 411 ? -6.81900  70.26300  17.03000 1.000 132.51649 ? 411 PHE A CE1   1 
ATOM 3431 C CE2   . PHE B 2 411 ? -5.41300  68.47900  17.73600 1.000 126.28187 ? 411 PHE A CE2   1 
ATOM 3432 C CZ    . PHE B 2 411 ? -6.24000  69.03900  16.79300 1.000 130.75832 ? 411 PHE A CZ    1 
ATOM 3433 N N     . ILE B 2 412 ? -7.62800  69.94700  22.31200 1.000 114.18253 ? 412 ILE A N     1 
ATOM 3434 C CA    . ILE B 2 412 ? -8.65600  68.90600  22.59800 1.000 104.49073 ? 412 ILE A CA    1 
ATOM 3435 C C     . ILE B 2 412 ? -9.98400  69.61000  22.89500 1.000 108.02356 ? 412 ILE A C     1 
ATOM 3436 O O     . ILE B 2 412 ? -11.01800 69.18000  22.34500 1.000 133.34576 ? 412 ILE A O     1 
ATOM 3437 C CB    . ILE B 2 412 ? -8.21200  68.03500  23.78500 1.000 103.13001 ? 412 ILE A CB    1 
ATOM 3438 C CG1   . ILE B 2 412 ? -6.73700  67.64700  23.68500 1.000 100.72616 ? 412 ILE A CG1   1 
ATOM 3439 C CG2   . ILE B 2 412 ? -9.11500  66.81100  23.93100 1.000 121.49878 ? 412 ILE A CG2   1 
ATOM 3440 C CD1   . ILE B 2 412 ? -6.39900  66.79700  22.47500 1.000 118.82493 ? 412 ILE A CD1   1 
ATOM 3441 N N     . LYS B 2 413 ? -9.94900  70.66200  23.71300 1.000 99.18811  ? 413 LYS A N     1 
ATOM 3442 C CA    . LYS B 2 413 ? -11.19900 71.35500  24.11900 1.000 116.64637 ? 413 LYS A CA    1 
ATOM 3443 C C     . LYS B 2 413 ? -11.90000 71.94500  22.88600 1.000 124.90585 ? 413 LYS A C     1 
ATOM 3444 O O     . LYS B 2 413 ? -13.14000 71.83000  22.79800 1.000 139.55283 ? 413 LYS A O     1 
ATOM 3445 C CB    . LYS B 2 413 ? -10.83600 72.42400  25.15400 1.000 105.38956 ? 413 LYS A CB    1 
ATOM 3446 C CG    . LYS B 2 413 ? -9.75600  71.97500  26.13000 1.000 121.91366 ? 413 LYS A CG    1 
ATOM 3447 C CD    . LYS B 2 413 ? -9.44000  72.97500  27.23500 1.000 126.90653 ? 413 LYS A CD    1 
ATOM 3448 C CE    . LYS B 2 413 ? -10.54300 73.08100  28.23700 1.000 124.35840 ? 413 LYS A CE    1 
ATOM 3449 N NZ    . LYS B 2 413 ? -10.18400 73.97600  29.34000 1.000 126.92308 ? 413 LYS A NZ    1 
ATOM 3450 N N     . ARG B 2 414 ? -11.13900 72.54800  21.97200 1.000 114.82024 ? 414 ARG A N     1 
ATOM 3451 C CA    . ARG B 2 414 ? -11.74700 73.20200  20.78500 1.000 112.72941 ? 414 ARG A CA    1 
ATOM 3452 C C     . ARG B 2 414 ? -12.41000 72.14900  19.88500 1.000 127.22420 ? 414 ARG A C     1 
ATOM 3453 O O     . ARG B 2 414 ? -13.49900 72.43700  19.34800 1.000 145.37062 ? 414 ARG A O     1 
ATOM 3454 C CB    . ARG B 2 414 ? -10.67700 73.97400  20.00800 1.000 125.31120 ? 414 ARG A CB    1 
ATOM 3455 C CG    . ARG B 2 414 ? -10.03000 75.08300  20.82600 1.000 139.18734 ? 414 ARG A CG    1 
ATOM 3456 C CD    . ARG B 2 414 ? -8.97100  75.84400  20.04500 1.000 133.67537 ? 414 ARG A CD    1 
ATOM 3457 N NE    . ARG B 2 414 ? -7.82600  75.00600  19.67500 1.000 135.11020 ? 414 ARG A NE    1 
ATOM 3458 C CZ    . ARG B 2 414 ? -6.58000  75.23400  20.06500 1.000 120.85970 ? 414 ARG A CZ    1 
ATOM 3459 N NH1   . ARG B 2 414 ? -6.34200  76.09400  21.03900 1.000 107.92788 ? 414 ARG A NH1   1 
ATOM 3460 N NH2   . ARG B 2 414 ? -5.57700  74.60000  19.48500 1.000 118.96958 ? 414 ARG A NH2   1 
ATOM 3461 N N     . ASN B 2 415 ? -11.77800 70.98400  19.72600 1.000 118.44052 ? 415 ASN A N     1 
ATOM 3462 C CA    . ASN B 2 415 ? -12.31800 69.95000  18.80000 1.000 135.61606 ? 415 ASN A CA    1 
ATOM 3463 C C     . ASN B 2 415 ? -13.17500 68.93800  19.56700 1.000 138.95372 ? 415 ASN A C     1 
ATOM 3464 O O     . ASN B 2 415 ? -13.58100 67.93300  18.94800 1.000 144.85391 ? 415 ASN A O     1 
ATOM 3465 C CB    . ASN B 2 415 ? -11.20000 69.23300  18.05400 1.000 131.17701 ? 415 ASN A CB    1 
ATOM 3466 C CG    . ASN B 2 415 ? -10.58600 70.08500  16.97100 1.000 145.30971 ? 415 ASN A CG    1 
ATOM 3467 O OD1   . ASN B 2 415 ? -9.68600  69.62500  16.26200 1.000 147.08406 ? 415 ASN A OD1   1 
ATOM 3468 N ND2   . ASN B 2 415 ? -11.05900 71.31300  16.81600 1.000 150.35645 ? 415 ASN A ND2   1 
ATOM 3469 N N     . ALA B 2 416 ? -13.46400 69.19800  20.84400 1.000 134.79338 ? 416 ALA A N     1 
ATOM 3470 C CA    . ALA B 2 416 ? -14.20500 68.21100  21.66900 1.000 132.16305 ? 416 ALA A CA    1 
ATOM 3471 C C     . ALA B 2 416 ? -15.51400 67.80900  20.98700 1.000 128.03464 ? 416 ALA A C     1 
ATOM 3472 O O     . ALA B 2 416 ? -15.81500 66.60100  20.92300 1.000 133.26851 ? 416 ALA A O     1 
ATOM 3473 C CB    . ALA B 2 416 ? -14.46400 68.78300  23.04000 1.000 131.67155 ? 416 ALA A CB    1 
ATOM 3474 N N     . GLN B 2 417 ? -16.27100 68.78800  20.49300 1.000 126.14879 ? 417 GLN A N     1 
ATOM 3475 C CA    . GLN B 2 417 ? -17.58700 68.48900  19.87400 1.000 127.71379 ? 417 GLN A CA    1 
ATOM 3476 C C     . GLN B 2 417 ? -17.38100 67.52400  18.69800 1.000 122.07003 ? 417 GLN A C     1 
ATOM 3477 O O     . GLN B 2 417 ? -18.21500 66.61200  18.52500 1.000 127.08790 ? 417 GLN A O     1 
ATOM 3478 C CB    . GLN B 2 417 ? -18.25700 69.78300  19.41300 1.000 127.55495 ? 417 GLN A CB    1 
ATOM 3479 C CG    . GLN B 2 417 ? -18.56300 70.76500  20.54000 1.000 146.79909 ? 417 GLN A CG    1 
ATOM 3480 C CD    . GLN B 2 417 ? -17.35800 71.55100  21.01000 1.000 159.96525 ? 417 GLN A CD    1 
ATOM 3481 O OE1   . GLN B 2 417 ? -16.24500 71.40500  20.49300 1.000 142.86888 ? 417 GLN A OE1   1 
ATOM 3482 N NE2   . GLN B 2 417 ? -17.57200 72.40300  22.00200 1.000 152.45332 ? 417 GLN A NE2   1 
ATOM 3483 N N     . ASN B 2 418 ? -16.31300 67.72200  17.92500 1.000 113.11341 ? 418 ASN A N     1 
ATOM 3484 C CA    . ASN B 2 418 ? -16.06800 66.87400  16.72600 1.000 117.82114 ? 418 ASN A CA    1 
ATOM 3485 C C     . ASN B 2 418 ? -15.61700 65.47100  17.14900 1.000 111.15146 ? 418 ASN A C     1 
ATOM 3486 O O     . ASN B 2 418 ? -15.99000 64.50300  16.45900 1.000 134.50373 ? 418 ASN A O     1 
ATOM 3487 C CB    . ASN B 2 418 ? -15.08100 67.53400  15.77100 1.000 143.29748 ? 418 ASN A CB    1 
ATOM 3488 C CG    . ASN B 2 418 ? -15.66300 68.76800  15.12600 1.000 143.03077 ? 418 ASN A CG    1 
ATOM 3489 O OD1   . ASN B 2 418 ? -16.80700 69.13700  15.41200 1.000 127.35546 ? 418 ASN A OD1   1 
ATOM 3490 N ND2   . ASN B 2 418 ? -14.90000 69.41700  14.26000 1.000 142.85836 ? 418 ASN A ND2   1 
ATOM 3491 N N     . ILE B 2 419 ? -14.83900 65.36500  18.22900 1.000 115.60691 ? 419 ILE A N     1 
ATOM 3492 C CA    . ILE B 2 419 ? -14.41000 64.01900  18.72100 1.000 129.66565 ? 419 ILE A CA    1 
ATOM 3493 C C     . ILE B 2 419 ? -15.53200 63.41900  19.58400 1.000 129.62992 ? 419 ILE A C     1 
ATOM 3494 O O     . ILE B 2 419 ? -15.57500 63.70700  20.79800 1.000 136.85745 ? 419 ILE A O     1 
ATOM 3495 C CB    . ILE B 2 419 ? -13.06100 64.07100  19.46600 1.000 132.77993 ? 419 ILE A CB    1 
ATOM 3496 C CG1   . ILE B 2 419 ? -12.95100 65.27900  20.38700 1.000 123.97309 ? 419 ILE A CG1   1 
ATOM 3497 C CG2   . ILE B 2 419 ? -11.89300 64.01500  18.48100 1.000 141.44799 ? 419 ILE A CG2   1 
ATOM 3498 C CD1   . ILE B 2 419 ? -11.58600 65.44200  21.03000 1.000 127.83146 ? 419 ILE A CD1   1 
ATOM 3499 N N     . GLN B 2 420 ? -16.39800 62.60800  18.97300 1.000 123.71432 ? 420 GLN A N     1 
ATOM 3500 C CA    . GLN B 2 420 ? -17.50800 61.97000  19.72600 1.000 123.29309 ? 420 GLN A CA    1 
ATOM 3501 C C     . GLN B 2 420 ? -17.02100 60.62500  20.28000 1.000 132.35242 ? 420 GLN A C     1 
ATOM 3502 O O     . GLN B 2 420 ? -17.77600 59.99900  21.05200 1.000 126.79839 ? 420 GLN A O     1 
ATOM 3503 C CB    . GLN B 2 420 ? -18.74000 61.80900  18.83700 1.000 141.10920 ? 420 GLN A CB    1 
ATOM 3504 C CG    . GLN B 2 420 ? -19.35100 63.13200  18.39100 1.000 150.64188 ? 420 GLN A CG    1 
ATOM 3505 C CD    . GLN B 2 420 ? -20.85300 63.06800  18.22200 1.000 146.21612 ? 420 GLN A CD    1 
ATOM 3506 O OE1   . GLN B 2 420 ? -21.48400 62.03200  18.45700 1.000 131.95520 ? 420 GLN A OE1   1 
ATOM 3507 N NE2   . GLN B 2 420 ? -21.44500 64.18400  17.82400 1.000 147.31846 ? 420 GLN A NE2   1 
ATOM 3508 N N     . ILE B 2 421 ? -15.81700 60.19700  19.89400 1.000 132.53644 ? 421 ILE A N     1 
ATOM 3509 C CA    . ILE B 2 421 ? -15.24200 58.94400  20.47000 1.000 129.87735 ? 421 ILE A CA    1 
ATOM 3510 C C     . ILE B 2 421 ? -13.82700 59.25200  20.98600 1.000 111.93075 ? 421 ILE A C     1 
ATOM 3511 O O     . ILE B 2 421 ? -12.90800 59.40000  20.15600 1.000 115.97531 ? 421 ILE A O     1 
ATOM 3512 C CB    . ILE B 2 421 ? -15.27300 57.79300  19.44500 1.000 139.82214 ? 421 ILE A CB    1 
ATOM 3513 C CG1   . ILE B 2 421 ? -14.49100 56.57600  19.93900 1.000 122.10699 ? 421 ILE A CG1   1 
ATOM 3514 C CG2   . ILE B 2 421 ? -14.79500 58.25800  18.06900 1.000 148.72819 ? 421 ILE A CG2   1 
ATOM 3515 C CD1   . ILE B 2 421 ? -14.61500 55.35800  19.04200 1.000 115.07887 ? 421 ILE A CD1   1 
ATOM 3516 N N     . GLY B 2 422 ? -13.67100 59.36500  22.30800 1.000 113.52648 ? 422 GLY A N     1 
ATOM 3517 C CA    . GLY B 2 422 ? -12.35700 59.69000  22.89400 1.000 115.78510 ? 422 GLY A CA    1 
ATOM 3518 C C     . GLY B 2 422 ? -11.92700 58.62600  23.88100 1.000 118.24340 ? 422 GLY A C     1 
ATOM 3519 O O     . GLY B 2 422 ? -12.80900 58.06800  24.56300 1.000 123.79244 ? 422 GLY A O     1 
ATOM 3520 N N     . ILE B 2 423 ? -10.62300 58.34900  23.95900 1.000 111.09158 ? 423 ILE A N     1 
ATOM 3521 C CA    . ILE B 2 423 ? -10.12700 57.26100  24.85200 1.000 110.38675 ? 423 ILE A CA    1 
ATOM 3522 C C     . ILE B 2 423 ? -9.18500  57.86500  25.90500 1.000 106.60164 ? 423 ILE A C     1 
ATOM 3523 O O     . ILE B 2 423 ? -8.56300  58.90700  25.61200 1.000 108.93663 ? 423 ILE A O     1 
ATOM 3524 C CB    . ILE B 2 423 ? -9.44600  56.15300  24.03100 1.000 100.86012 ? 423 ILE A CB    1 
ATOM 3525 C CG1   . ILE B 2 423 ? -8.09600  56.59900  23.49900 1.000 130.30233 ? 423 ILE A CG1   1 
ATOM 3526 C CG2   . ILE B 2 423 ? -10.35800 55.66900  22.90300 1.000 107.21990 ? 423 ILE A CG2   1 
ATOM 3527 C CD1   . ILE B 2 423 ? -7.49100  55.62400  22.51100 1.000 148.12145 ? 423 ILE A CD1   1 
ATOM 3528 N N     . THR B 2 424 ? -9.10300  57.24300  27.08500 1.000 105.46126 ? 424 THR A N     1 
ATOM 3529 C CA    . THR B 2 424 ? -8.26100  57.77000  28.17900 1.000 89.22037  ? 424 THR A CA    1 
ATOM 3530 C C     . THR B 2 424 ? -7.71000  56.60000  28.95800 1.000 82.70079  ? 424 THR A C     1 
ATOM 3531 O O     . THR B 2 424 ? -7.83100  55.45900  28.46700 1.000 93.57184  ? 424 THR A O     1 
ATOM 3532 C CB    . THR B 2 424 ? -9.09200  58.68600  29.07700 1.000 94.14807  ? 424 THR A CB    1 
ATOM 3533 O OG1   . THR B 2 424 ? -9.79134  59.59483  28.23149 1.000 124.24575 ? 424 THR A OG1   1 
ATOM 3534 C CG2   . THR B 2 424 ? -8.24251  59.48162  30.05226 1.000 82.67174  ? 424 THR A CG2   1 
ATOM 3535 N N     . ASN B 2 425 ? -7.12400  56.86100  30.12800 1.000 98.71896  ? 425 ASN A N     1 
ATOM 3536 C CA    . ASN B 2 425 ? -6.61200  55.77000  31.00100 1.000 88.41666  ? 425 ASN A CA    1 
ATOM 3537 C C     . ASN B 2 425 ? -7.18900  55.96700  32.40600 1.000 90.33507  ? 425 ASN A C     1 
ATOM 3538 O O     . ASN B 2 425 ? -7.41800  57.13100  32.79300 1.000 90.60095  ? 425 ASN A O     1 
ATOM 3539 C CB    . ASN B 2 425 ? -5.08900  55.71800  30.98900 1.000 90.69082  ? 425 ASN A CB    1 
ATOM 3540 C CG    . ASN B 2 425 ? -4.54000  54.48700  31.66900 1.000 112.79214 ? 425 ASN A CG    1 
ATOM 3541 O OD1   . ASN B 2 425 ? -4.72900  54.30200  32.87600 1.000 130.08891 ? 425 ASN A OD1   1 
ATOM 3542 N ND2   . ASN B 2 425 ? -3.84500  53.64400  30.91900 1.000 110.03635 ? 425 ASN A ND2   1 
ATOM 3543 N N     . HIS B 2 426 ? -7.40700  54.87300  33.13900 1.000 93.89486  ? 426 HIS A N     1 
ATOM 3544 C CA    . HIS B 2 426 ? -7.94900  54.95700  34.52000 1.000 90.84398  ? 426 HIS A CA    1 
ATOM 3545 C C     . HIS B 2 426 ? -7.15700  55.99300  35.31500 1.000 97.23860  ? 426 HIS A C     1 
ATOM 3546 O O     . HIS B 2 426 ? -7.76400  56.81500  36.03400 1.000 93.79204  ? 426 HIS A O     1 
ATOM 3547 C CB    . HIS B 2 426 ? -7.79400  53.62000  35.24400 1.000 97.47764  ? 426 HIS A CB    1 
ATOM 3548 C CG    . HIS B 2 426 ? -8.81500  52.57600  34.94700 1.000 71.96213  ? 426 HIS A CG    1 
ATOM 3549 N ND1   . HIS B 2 426 ? -8.49100  51.23800  34.95200 1.000 98.46368  ? 426 HIS A ND1   1 
ATOM 3550 C CD2   . HIS B 2 426 ? -10.11800 52.63800  34.66500 1.000 82.58368  ? 426 HIS A CD2   1 
ATOM 3551 C CE1   . HIS B 2 426 ? -9.57000  50.52700  34.66800 1.000 96.65588  ? 426 HIS A CE1   1 
ATOM 3552 N NE2   . HIS B 2 426 ? -10.56900 51.35800  34.48600 1.000 90.88342  ? 426 HIS A NE2   1 
ATOM 3553 N N     . ALA B 2 427 ? -5.82900  55.95200  35.19400 1.000 96.95584  ? 427 ALA A N     1 
ATOM 3554 C CA    . ALA B 2 427 ? -4.97300  56.87900  35.96800 1.000 92.45782  ? 427 ALA A CA    1 
ATOM 3555 C C     . ALA B 2 427 ? -5.37900  58.32000  35.66700 1.000 82.82294  ? 427 ALA A C     1 
ATOM 3556 O O     . ALA B 2 427 ? -5.52200  59.12000  36.61000 1.000 103.81720 ? 427 ALA A O     1 
ATOM 3557 C CB    . ALA B 2 427 ? -3.52700  56.63700  35.62000 1.000 91.12727  ? 427 ALA A CB    1 
ATOM 3558 N N     . HIS B 2 428 ? -5.55700  58.63800  34.38600 1.000 78.76945  ? 428 HIS A N     1 
ATOM 3559 C CA    . HIS B 2 428 ? -5.93400  60.02000  33.99400 1.000 80.84416  ? 428 HIS A CA    1 
ATOM 3560 C C     . HIS B 2 428 ? -7.35500  60.30700  34.48200 1.000 83.42217  ? 428 HIS A C     1 
ATOM 3561 O O     . HIS B 2 428 ? -7.61300  61.42100  34.96100 1.000 95.96673  ? 428 HIS A O     1 
ATOM 3562 C CB    . HIS B 2 428 ? -5.80100  60.20700  32.48000 1.000 91.72813  ? 428 HIS A CB    1 
ATOM 3563 C CG    . HIS B 2 428 ? -4.39500  60.18500  31.98500 1.000 97.00255  ? 428 HIS A CG    1 
ATOM 3564 N ND1   . HIS B 2 428 ? -3.76600  59.03800  31.55200 1.000 88.66398  ? 428 HIS A ND1   1 
ATOM 3565 C CD2   . HIS B 2 428 ? -3.50200  61.17100  31.84500 1.000 85.33840  ? 428 HIS A CD2   1 
ATOM 3566 C CE1   . HIS B 2 428 ? -2.53300  59.33400  31.17000 1.000 82.99980  ? 428 HIS A CE1   1 
ATOM 3567 N NE2   . HIS B 2 428 ? -2.35100  60.62500  31.34100 1.000 99.41332  ? 428 HIS A NE2   1 
ATOM 3568 N N     . LEU B 2 429 ? -8.24400  59.31900  34.39900 1.000 82.66659  ? 429 LEU A N     1 
ATOM 3569 C CA    . LEU B 2 429 ? -9.66600  59.55400  34.76400 1.000 77.70479  ? 429 LEU A CA    1 
ATOM 3570 C C     . LEU B 2 429 ? -9.77000  60.10100  36.19400 1.000 84.08724  ? 429 LEU A C     1 
ATOM 3571 O O     . LEU B 2 429 ? -10.62700 60.97800  36.42300 1.000 88.71688  ? 429 LEU A O     1 
ATOM 3572 C CB    . LEU B 2 429 ? -10.43500 58.24400  34.61500 1.000 82.35047  ? 429 LEU A CB    1 
ATOM 3573 C CG    . LEU B 2 429 ? -11.96100 58.35100  34.67900 1.000 81.41318  ? 429 LEU A CG    1 
ATOM 3574 C CD1   . LEU B 2 429 ? -12.45800 59.18200  33.51300 1.000 89.81334  ? 429 LEU A CD1   1 
ATOM 3575 C CD2   . LEU B 2 429 ? -12.59200 56.97100  34.66100 1.000 89.74718  ? 429 LEU A CD2   1 
ATOM 3576 N N     . ILE B 2 430 ? -8.93300  59.61700  37.11400 1.000 77.48159  ? 430 ILE A N     1 
ATOM 3577 C CA    . ILE B 2 430 ? -9.05700  60.03000  38.54500 1.000 83.47400  ? 430 ILE A CA    1 
ATOM 3578 C C     . ILE B 2 430 ? -8.30300  61.34700  38.79000 1.000 90.68102  ? 430 ILE A C     1 
ATOM 3579 O O     . ILE B 2 430 ? -8.32100  61.82300  39.94300 1.000 94.90740  ? 430 ILE A O     1 
ATOM 3580 C CB    . ILE B 2 430 ? -8.54300  58.91100  39.46700 1.000 81.51002  ? 430 ILE A CB    1 
ATOM 3581 C CG1   . ILE B 2 430 ? -7.03800  58.71400  39.31500 1.000 108.77222 ? 430 ILE A CG1   1 
ATOM 3582 C CG2   . ILE B 2 430 ? -9.31100  57.61100  39.22900 1.000 89.50725  ? 430 ILE A CG2   1 
ATOM 3583 C CD1   . ILE B 2 430 ? -6.51600  57.43800  39.94700 1.000 115.52984 ? 430 ILE A CD1   1 
ATOM 3584 N N     . HIS B 2 431 ? -7.67500  61.91600  37.75800 1.000 92.99739  ? 431 HIS A N     1 
ATOM 3585 C CA    . HIS B 2 431 ? -6.86000  63.14700  37.95100 1.000 93.64063  ? 431 HIS A CA    1 
ATOM 3586 C C     . HIS B 2 431 ? -7.76500  64.31100  38.36200 1.000 91.79991  ? 431 HIS A C     1 
ATOM 3587 O O     . HIS B 2 431 ? -8.97600  64.26900  38.06700 1.000 92.31904  ? 431 HIS A O     1 
ATOM 3588 C CB    . HIS B 2 431 ? -6.04000  63.47400  36.69800 1.000 90.54744  ? 431 HIS A CB    1 
ATOM 3589 C CG    . HIS B 2 431 ? -4.73600  62.75600  36.61400 1.000 88.15109  ? 431 HIS A CG    1 
ATOM 3590 N ND1   . HIS B 2 431 ? -4.50700  61.52900  37.19800 1.000 115.82174 ? 431 HIS A ND1   1 
ATOM 3591 C CD2   . HIS B 2 431 ? -3.58800  63.10200  36.02100 1.000 99.93599  ? 431 HIS A CD2   1 
ATOM 3592 C CE1   . HIS B 2 431 ? -3.25900  61.15600  36.95300 1.000 115.49579 ? 431 HIS A CE1   1 
ATOM 3593 N NE2   . HIS B 2 431 ? -2.68400  62.09600  36.23800 1.000 87.00955  ? 431 HIS A NE2   1 
ATOM 3594 N N     . SER B 2 432 ? -7.18500  65.33300  38.99300 1.000 95.72290  ? 432 SER A N     1 
ATOM 3595 C CA    . SER B 2 432 ? -7.98000  66.47900  39.50700 1.000 103.76154 ? 432 SER A CA    1 
ATOM 3596 C C     . SER B 2 432 ? -8.68100  67.22700  38.36700 1.000 122.51216 ? 432 SER A C     1 
ATOM 3597 O O     . SER B 2 432 ? -8.19800  67.15400  37.21800 1.000 116.32061 ? 432 SER A O     1 
ATOM 3598 C CB    . SER B 2 432 ? -7.10400  67.41300  40.28500 1.000 111.99062 ? 432 SER A CB    1 
ATOM 3599 O OG    . SER B 2 432 ? -6.03700  67.88300  39.47300 1.000 106.29191 ? 432 SER A OG    1 
ATOM 3600 N N     . ASP B 2 433 ? -9.76100  67.94100  38.69300 1.000 122.32505 ? 433 ASP A N     1 
ATOM 3601 C CA    . ASP B 2 433 ? -10.51400 68.71600  37.67000 1.000 126.89780 ? 433 ASP A CA    1 
ATOM 3602 C C     . ASP B 2 433 ? -9.58800  69.75300  37.03200 1.000 129.09846 ? 433 ASP A C     1 
ATOM 3603 O O     . ASP B 2 433 ? -9.65400  69.92600  35.80000 1.000 134.59634 ? 433 ASP A O     1 
ATOM 3604 C CB    . ASP B 2 433 ? -11.74000 69.38100  38.27100 1.000 134.95524 ? 433 ASP A CB    1 
ATOM 3605 C CG    . ASP B 2 433 ? -12.55000 70.23600  37.30800 1.000 159.18467 ? 433 ASP A CG    1 
ATOM 3606 O OD1   . ASP B 2 433 ? -13.02400 69.68600  36.29200 1.000 148.94324 ? 433 ASP A OD1   1 
ATOM 3607 O OD2   . ASP B 2 433 ? -12.69900 71.44600  37.57900 1.000 163.78634 ? 433 ASP A OD2   1 
ATOM 3608 N N     . VAL B 2 434 ? -8.75600  70.41500  37.83800 1.000 126.18917 ? 434 VAL A N     1 
ATOM 3609 C CA    . VAL B 2 434 ? -7.87000  71.49200  37.30200 1.000 134.12412 ? 434 VAL A CA    1 
ATOM 3610 C C     . VAL B 2 434 ? -6.98300  70.89700  36.19500 1.000 129.30996 ? 434 VAL A C     1 
ATOM 3611 O O     . VAL B 2 434 ? -6.63000  71.64600  35.26100 1.000 123.80559 ? 434 VAL A O     1 
ATOM 3612 C CB    . VAL B 2 434 ? -7.02700  72.15600  38.40700 1.000 109.90866 ? 434 VAL A CB    1 
ATOM 3613 C CG1   . VAL B 2 434 ? -7.90400  72.82000  39.46100 1.000 117.52759 ? 434 VAL A CG1   1 
ATOM 3614 C CG2   . VAL B 2 434 ? -6.05900  71.17600  39.05800 1.000 126.50907 ? 434 VAL A CG2   1 
ATOM 3615 N N     . GLU B 2 435 ? -6.64400  69.60800  36.29700 1.000 111.00732 ? 435 GLU A N     1 
ATOM 3616 C CA    . GLU B 2 435 ? -5.76600  68.95900  35.28900 1.000 123.35581 ? 435 GLU A CA    1 
ATOM 3617 C C     . GLU B 2 435 ? -6.63600  68.21600  34.26500 1.000 121.08894 ? 435 GLU A C     1 
ATOM 3618 O O     . GLU B 2 435 ? -6.15400  67.98200  33.13600 1.000 113.90476 ? 435 GLU A O     1 
ATOM 3619 C CB    . GLU B 2 435 ? -4.77400  68.01700  35.96900 1.000 123.99604 ? 435 GLU A CB    1 
ATOM 3620 C CG    . GLU B 2 435 ? -3.66200  67.54900  35.03500 1.000 130.47117 ? 435 GLU A CG    1 
ATOM 3621 C CD    . GLU B 2 435 ? -2.44100  66.99300  35.74200 1.000 130.41501 ? 435 GLU A CD    1 
ATOM 3622 O OE1   . GLU B 2 435 ? -1.83400  67.74200  36.53400 1.000 137.12184 ? 435 GLU A OE1   1 
ATOM 3623 O OE2   . GLU B 2 435 ? -2.09200  65.82100  35.49500 1.000 110.09403 ? 435 GLU A OE2   1 
ATOM 3624 N N     . ASN B 2 436 ? -7.86800  67.87200  34.64600 1.000 124.84623 ? 436 ASN A N     1 
ATOM 3625 C CA    . ASN B 2 436 ? -8.79700  67.17600  33.71300 1.000 125.29502 ? 436 ASN A CA    1 
ATOM 3626 C C     . ASN B 2 436 ? -10.05700 68.02700  33.53700 1.000 128.57448 ? 436 ASN A C     1 
ATOM 3627 O O     . ASN B 2 436 ? -11.15400 67.54500  33.89000 1.000 121.10419 ? 436 ASN A O     1 
ATOM 3628 C CB    . ASN B 2 436 ? -9.10600  65.76100  34.18400 1.000 93.49237  ? 436 ASN A CB    1 
ATOM 3629 C CG    . ASN B 2 436 ? -8.04100  64.78500  33.74800 1.000 115.44252 ? 436 ASN A CG    1 
ATOM 3630 O OD1   . ASN B 2 436 ? -7.06400  65.17600  33.10300 1.000 130.57343 ? 436 ASN A OD1   1 
ATOM 3631 N ND2   . ASN B 2 436 ? -8.21300  63.51700  34.08200 1.000 98.22039  ? 436 ASN A ND2   1 
ATOM 3632 N N     . SER B 2 437 ? -9.89600  69.24600  33.01400 1.000 122.64717 ? 437 SER A N     1 
ATOM 3633 C CA    . SER B 2 437 ? -11.04900 70.15800  32.80500 1.000 119.35114 ? 437 SER A CA    1 
ATOM 3634 C C     . SER B 2 437 ? -11.74500 69.81700  31.48100 1.000 121.90641 ? 437 SER A C     1 
ATOM 3635 O O     . SER B 2 437 ? -12.86100 70.32300  31.25100 1.000 130.83660 ? 437 SER A O     1 
ATOM 3636 C CB    . SER B 2 437 ? -10.60300 71.59300  32.83300 1.000 123.30113 ? 437 SER A CB    1 
ATOM 3637 O OG    . SER B 2 437 ? -9.61800  71.83500  31.83800 1.000 132.18039 ? 437 SER A OG    1 
ATOM 3638 N N     . ILE B 2 438 ? -11.10800 68.99000  30.64900 1.000 109.66272 ? 438 ILE A N     1 
ATOM 3639 C CA    . ILE B 2 438 ? -11.72200 68.57400  29.35300 1.000 109.96102 ? 438 ILE A CA    1 
ATOM 3640 C C     . ILE B 2 438 ? -13.00400 67.78100  29.65400 1.000 122.54100 ? 438 ILE A C     1 
ATOM 3641 O O     . ILE B 2 438 ? -13.94500 67.84600  28.83600 1.000 112.06014 ? 438 ILE A O     1 
ATOM 3642 C CB    . ILE B 2 438 ? -10.72000 67.75800  28.51600 1.000 122.83981 ? 438 ILE A CB    1 
ATOM 3643 C CG1   . ILE B 2 438 ? -11.33000 67.28100  27.19800 1.000 102.20196 ? 438 ILE A CG1   1 
ATOM 3644 C CG2   . ILE B 2 438 ? -10.14900 66.59500  29.32700 1.000 131.26146 ? 438 ILE A CG2   1 
ATOM 3645 C CD1   . ILE B 2 438 ? -11.78100 68.40300  26.28100 1.000 118.17599 ? 438 ILE A CD1   1 
ATOM 3646 N N     . TYR B 2 439 ? -13.04800 67.08600  30.79400 1.000 127.84724 ? 439 TYR A N     1 
ATOM 3647 C CA    . TYR B 2 439 ? -14.22500 66.23500  31.12600 1.000 124.08326 ? 439 TYR A CA    1 
ATOM 3648 C C     . TYR B 2 439 ? -15.47500 67.11100  31.21700 1.000 124.43811 ? 439 TYR A C     1 
ATOM 3649 O O     . TYR B 2 439 ? -16.59700 66.58400  31.10900 1.000 131.21845 ? 439 TYR A O     1 
ATOM 3650 C CB    . TYR B 2 439 ? -13.98700 65.43800  32.41300 1.000 106.30577 ? 439 TYR A CB    1 
ATOM 3651 C CG    . TYR B 2 439 ? -12.87300 64.40500  32.32300 1.000 102.19913 ? 439 TYR A CG    1 
ATOM 3652 C CD1   . TYR B 2 439 ? -12.47100 63.89000  31.09700 1.000 103.06678 ? 439 TYR A CD1   1 
ATOM 3653 C CD2   . TYR B 2 439 ? -12.24500 63.92700  33.46500 1.000 108.74640 ? 439 TYR A CD2   1 
ATOM 3654 C CE1   . TYR B 2 439 ? -11.46000 62.94800  31.00900 1.000 105.55908 ? 439 TYR A CE1   1 
ATOM 3655 C CE2   . TYR B 2 439 ? -11.23800 62.98000  33.39000 1.000 98.58753  ? 439 TYR A CE2   1 
ATOM 3656 C CZ    . TYR B 2 439 ? -10.84300 62.49100  32.15900 1.000 93.96259  ? 439 TYR A CZ    1 
ATOM 3657 O OH    . TYR B 2 439 ? -9.85000  61.56100  32.07800 1.000 111.05591 ? 439 TYR A OH    1 
ATOM 3658 N N     . GLN B 2 440 ? -15.29900 68.41900  31.41200 1.000 108.57919 ? 440 GLN A N     1 
ATOM 3659 C CA    . GLN B 2 440 ? -16.47200 69.33000  31.41900 1.000 118.48742 ? 440 GLN A CA    1 
ATOM 3660 C C     . GLN B 2 440 ? -17.13700 69.27300  30.03600 1.000 116.75507 ? 440 GLN A C     1 
ATOM 3661 O O     . GLN B 2 440 ? -18.36000 69.50300  29.95600 1.000 125.93572 ? 440 GLN A O     1 
ATOM 3662 C CB    . GLN B 2 440 ? -16.03800 70.74600  31.79500 1.000 113.57400 ? 440 GLN A CB    1 
ATOM 3663 C CG    . GLN B 2 440 ? -15.41800 70.84300  33.18500 1.000 125.13121 ? 440 GLN A CG    1 
ATOM 3664 C CD    . GLN B 2 440 ? -14.90100 72.22600  33.51500 1.000 138.96782 ? 440 GLN A CD    1 
ATOM 3665 O OE1   . GLN B 2 440 ? -15.00700 73.16300  32.71700 1.000 153.41518 ? 440 GLN A OE1   1 
ATOM 3666 N NE2   . GLN B 2 440 ? -14.33300 72.36400  34.70500 1.000 139.78602 ? 440 GLN A NE2   1 
ATOM 3667 N N     . LEU B 2 441 ? -16.35600 68.97300  28.99700 1.000 109.85537 ? 441 LEU A N     1 
ATOM 3668 C CA    . LEU B 2 441 ? -16.90800 68.87200  27.62200 1.000 109.50119 ? 441 LEU A CA    1 
ATOM 3669 C C     . LEU B 2 441 ? -17.03100 67.38800  27.24700 1.000 131.85203 ? 441 LEU A C     1 
ATOM 3670 O O     . LEU B 2 441 ? -17.15000 67.09700  26.04000 1.000 138.56415 ? 441 LEU A O     1 
ATOM 3671 C CB    . LEU B 2 441 ? -16.00400 69.63900  26.66200 1.000 114.48550 ? 441 LEU A CB    1 
ATOM 3672 C CG    . LEU B 2 441 ? -16.70700 70.32400  25.48700 1.000 139.34669 ? 441 LEU A CG    1 
ATOM 3673 C CD1   . LEU B 2 441 ? -18.04900 70.87300  25.93500 1.000 137.41127 ? 441 LEU A CD1   1 
ATOM 3674 C CD2   . LEU B 2 441 ? -15.83300 71.44700  24.95600 1.000 131.98261 ? 441 LEU A CD2   1 
ATOM 3675 N N     . PHE B 2 442 ? -16.96600 66.49300  28.23600 1.000 132.40822 ? 442 PHE A N     1 
ATOM 3676 C CA    . PHE B 2 442 ? -17.15200 65.03500  27.99200 1.000 119.94967 ? 442 PHE A CA    1 
ATOM 3677 C C     . PHE B 2 442 ? -17.94500 64.49400  29.16800 1.000 111.47482 ? 442 PHE A C     1 
ATOM 3678 O O     . PHE B 2 442 ? -17.33000 64.17600  30.19700 1.000 112.38981 ? 442 PHE A O     1 
ATOM 3679 C CB    . PHE B 2 442 ? -15.80400 64.32400  27.85800 1.000 122.21449 ? 442 PHE A CB    1 
ATOM 3680 C CG    . PHE B 2 442 ? -15.17700 64.34500  26.47200 1.000 124.09452 ? 442 PHE A CG    1 
ATOM 3681 C CD1   . PHE B 2 442 ? -14.35900 65.39500  26.07200 1.000 110.87776 ? 442 PHE A CD1   1 
ATOM 3682 C CD2   . PHE B 2 442 ? -15.38700 63.29900  25.58100 1.000 122.06218 ? 442 PHE A CD2   1 
ATOM 3683 C CE1   . PHE B 2 442 ? -13.78500 65.40400  24.81200 1.000 112.47780 ? 442 PHE A CE1   1 
ATOM 3684 C CE2   . PHE B 2 442 ? -14.80500 63.31200  24.32400 1.000 124.73290 ? 442 PHE A CE2   1 
ATOM 3685 C CZ    . PHE B 2 442 ? -14.00800 64.36400  23.94100 1.000 111.05697 ? 442 PHE A CZ    1 
ATOM 3686 N N     . ASP B 2 443 ? -19.26600 64.38000  29.03300 1.000 123.41005 ? 443 ASP A N     1 
ATOM 3687 C CA    . ASP B 2 443 ? -20.09700 63.99700  30.20900 1.000 115.06949 ? 443 ASP A CA    1 
ATOM 3688 C C     . ASP B 2 443 ? -20.55000 62.53400  30.14100 1.000 107.10826 ? 443 ASP A C     1 
ATOM 3689 O O     . ASP B 2 443 ? -21.27500 62.11000  31.06300 1.000 115.18087 ? 443 ASP A O     1 
ATOM 3690 C CB    . ASP B 2 443 ? -21.26900 64.95200  30.35500 1.000 118.12140 ? 443 ASP A CB    1 
ATOM 3691 C CG    . ASP B 2 443 ? -20.89200 66.41500  30.54400 1.000 136.25823 ? 443 ASP A CG    1 
ATOM 3692 O OD1   . ASP B 2 443 ? -19.67900 66.70800  30.57400 1.000 136.90494 ? 443 ASP A OD1   1 
ATOM 3693 O OD2   . ASP B 2 443 ? -21.81500 67.24800  30.65700 1.000 115.81910 ? 443 ASP A OD2   1 
ATOM 3694 N N     . ASP B 2 444 ? -20.13900 61.78800  29.11400 1.000 110.47494 ? 444 ASP A N     1 
ATOM 3695 C CA    . ASP B 2 444 ? -20.48500 60.34000  29.04500 1.000 108.56096 ? 444 ASP A CA    1 
ATOM 3696 C C     . ASP B 2 444 ? -19.19900 59.51300  28.96900 1.000 103.30305 ? 444 ASP A C     1 
ATOM 3697 O O     . ASP B 2 444 ? -18.32800 59.85700  28.14600 1.000 111.46929 ? 444 ASP A O     1 
ATOM 3698 C CB    . ASP B 2 444 ? -21.42900 60.04400  27.89100 1.000 115.01152 ? 444 ASP A CB    1 
ATOM 3699 C CG    . ASP B 2 444 ? -22.85100 60.56000  28.05700 1.000 136.82968 ? 444 ASP A CG    1 
ATOM 3700 O OD1   . ASP B 2 444 ? -23.13300 61.18600  29.09800 1.000 124.48979 ? 444 ASP A OD1   1 
ATOM 3701 O OD2   . ASP B 2 444 ? -23.66800 60.32900  27.14200 1.000 153.73313 ? 444 ASP A OD2   1 
ATOM 3702 N N     . CYS B 2 445 ? -19.09300 58.46400  29.79000 1.000 94.27461  ? 445 CYS A N     1 
ATOM 3703 C CA    . CYS B 2 445 ? -17.85700 57.64100  29.81900 1.000 103.80166 ? 445 CYS A CA    1 
ATOM 3704 C C     . CYS B 2 445 ? -18.17800 56.16700  30.09200 1.000 109.97895 ? 445 CYS A C     1 
ATOM 3705 O O     . CYS B 2 445 ? -19.11200 55.90300  30.87700 1.000 115.58679 ? 445 CYS A O     1 
ATOM 3706 C CB    . CYS B 2 445 ? -16.91600 58.10300  30.92100 1.000 103.99456 ? 445 CYS A CB    1 
ATOM 3707 S SG    . CYS B 2 445 ? -15.49500 57.00400  31.15900 1.000 120.19812 ? 445 CYS A SG    1 
ATOM 3708 N N     . ILE B 2 446 ? -17.42900 55.25300  29.47100 1.000 94.85884  ? 446 ILE A N     1 
ATOM 3709 C CA    . ILE B 2 446 ? -17.60700 53.79600  29.74700 1.000 90.54208  ? 446 ILE A CA    1 
ATOM 3710 C C     . ILE B 2 446 ? -16.26800 53.26600  30.28200 1.000 91.73836  ? 446 ILE A C     1 
ATOM 3711 O O     . ILE B 2 446 ? -15.26100 53.35000  29.55400 1.000 89.53973  ? 446 ILE A O     1 
ATOM 3712 C CB    . ILE B 2 446 ? -18.09900 53.04200  28.49600 1.000 92.66531  ? 446 ILE A CB    1 
ATOM 3713 C CG1   . ILE B 2 446 ? -17.21600 53.29500  27.28000 1.000 114.15318 ? 446 ILE A CG1   1 
ATOM 3714 C CG2   . ILE B 2 446 ? -19.55500 53.39100  28.19300 1.000 99.62460  ? 446 ILE A CG2   1 
ATOM 3715 C CD1   . ILE B 2 446 ? -17.73500 52.66000  26.00300 1.000 98.16157  ? 446 ILE A CD1   1 
ATOM 3716 N N     . VAL B 2 447 ? -16.25300 52.76500  31.51700 1.000 97.68413  ? 447 VAL A N     1 
ATOM 3717 C CA    . VAL B 2 447 ? -14.96800 52.32800  32.13700 1.000 81.24507  ? 447 VAL A CA    1 
ATOM 3718 C C     . VAL B 2 447 ? -14.79300 50.81800  31.92700 1.000 84.31083  ? 447 VAL A C     1 
ATOM 3719 O O     . VAL B 2 447 ? -15.73500 50.06800  32.24800 1.000 90.07633  ? 447 VAL A O     1 
ATOM 3720 C CB    . VAL B 2 447 ? -14.95900 52.69000  33.63200 1.000 87.01356  ? 447 VAL A CB    1 
ATOM 3721 C CG1   . VAL B 2 447 ? -13.60600 52.42100  34.27300 1.000 85.82642  ? 447 VAL A CG1   1 
ATOM 3722 C CG2   . VAL B 2 447 ? -15.38200 54.13500  33.86500 1.000 83.22328  ? 447 VAL A CG2   1 
ATOM 3723 N N     . ASP B 2 448 ? -13.63600 50.40300  31.40800 1.000 82.73778  ? 448 ASP A N     1 
ATOM 3724 C CA    . ASP B 2 448 ? -13.35400 48.95300  31.22700 1.000 83.80816  ? 448 ASP A CA    1 
ATOM 3725 C C     . ASP B 2 448 ? -12.45200 48.48400  32.37300 1.000 82.89950  ? 448 ASP A C     1 
ATOM 3726 O O     . ASP B 2 448 ? -11.71000 49.32200  32.91700 1.000 87.76803  ? 448 ASP A O     1 
ATOM 3727 C CB    . ASP B 2 448 ? -12.77500 48.66600  29.85200 1.000 71.99101  ? 448 ASP A CB    1 
ATOM 3728 C CG    . ASP B 2 448 ? -12.58400 47.19500  29.51600 1.000 93.96442  ? 448 ASP A CG    1 
ATOM 3729 O OD1   . ASP B 2 448 ? -13.58400 46.45000  29.56300 1.000 99.94569  ? 448 ASP A OD1   1 
ATOM 3730 O OD2   . ASP B 2 448 ? -11.43900 46.81000  29.20400 1.000 97.53806  ? 448 ASP A OD2   1 
ATOM 3731 N N     . GLU B 2 449 ? -12.53900 47.20300  32.73800 1.000 92.55396  ? 449 GLU A N     1 
ATOM 3732 C CA    . GLU B 2 449 ? -11.72000 46.65000  33.84700 1.000 86.86231  ? 449 GLU A CA    1 
ATOM 3733 C C     . GLU B 2 449 ? -11.79000 47.61600  35.03600 1.000 82.66636  ? 449 GLU A C     1 
ATOM 3734 O O     . GLU B 2 449 ? -10.72800 47.92700  35.60500 1.000 87.41121  ? 449 GLU A O     1 
ATOM 3735 C CB    . GLU B 2 449 ? -10.28600 46.41300  33.38100 1.000 85.58004  ? 449 GLU A CB    1 
ATOM 3736 C CG    . GLU B 2 449 ? -10.19900 45.67800  32.04700 1.000 82.65078  ? 449 GLU A CG    1 
ATOM 3737 C CD    . GLU B 2 449 ? -10.88600 44.32500  32.03000 1.000 110.17531 ? 449 GLU A CD    1 
ATOM 3738 O OE1   . GLU B 2 449 ? -10.47200 43.44300  32.80900 1.000 117.44739 ? 449 GLU A OE1   1 
ATOM 3739 O OE2   . GLU B 2 449 ? -11.83600 44.15600  31.23900 1.000 114.89501 ? 449 GLU A OE2   1 
ATOM 3740 N N     . ALA B 2 450 ? -12.99800 48.03600  35.41500 1.000 83.57893  ? 450 ALA A N     1 
ATOM 3741 C CA    . ALA B 2 450 ? -13.16400 49.02300  36.50700 1.000 80.96287  ? 450 ALA A CA    1 
ATOM 3742 C C     . ALA B 2 450 ? -12.83200 48.39500  37.86100 1.000 78.14139  ? 450 ALA A C     1 
ATOM 3743 O O     . ALA B 2 450 ? -12.79100 49.12700  38.86800 1.000 72.98780  ? 450 ALA A O     1 
ATOM 3744 C CB    . ALA B 2 450 ? -14.57200 49.56200  36.48600 1.000 72.22203  ? 450 ALA A CB    1 
ATOM 3745 N N     . HIS B 2 451 ? -12.60500 47.08300  37.88900 1.000 74.43451  ? 451 HIS A N     1 
ATOM 3746 C CA    . HIS B 2 451 ? -12.22700 46.40400  39.15600 1.000 82.92478  ? 451 HIS A CA    1 
ATOM 3747 C C     . HIS B 2 451 ? -10.86600 46.93200  39.61500 1.000 86.29458  ? 451 HIS A C     1 
ATOM 3748 O O     . HIS B 2 451 ? -10.53700 46.79100  40.81000 1.000 91.65652  ? 451 HIS A O     1 
ATOM 3749 C CB    . HIS B 2 451 ? -12.22700 44.88400  38.97100 1.000 79.20228  ? 451 HIS A CB    1 
ATOM 3750 C CG    . HIS B 2 451 ? -11.26600 44.37800  37.95000 1.000 74.61198  ? 451 HIS A CG    1 
ATOM 3751 N ND1   . HIS B 2 451 ? -11.58400 44.27600  36.61300 1.000 100.71063 ? 451 HIS A ND1   1 
ATOM 3752 C CD2   . HIS B 2 451 ? -10.00600 43.94400  38.06600 1.000 81.53696  ? 451 HIS A CD2   1 
ATOM 3753 C CE1   . HIS B 2 451 ? -10.54000 43.79500  35.95400 1.000 106.17211 ? 451 HIS A CE1   1 
ATOM 3754 N NE2   . HIS B 2 451 ? -9.57100  43.58700  36.81700 1.000 94.10352  ? 451 HIS A NE2   1 
ATOM 3755 N N     . ARG B 2 452 ? -10.09800 47.51800  38.69300 1.000 81.78532  ? 452 ARG A N     1 
ATOM 3756 C CA    . ARG B 2 452 ? -8.74100  48.02200  39.02600 1.000 81.59650  ? 452 ARG A CA    1 
ATOM 3757 C C     . ARG B 2 452 ? -8.80700  49.51100  39.39000 1.000 88.78075  ? 452 ARG A C     1 
ATOM 3758 O O     . ARG B 2 452 ? -7.78600  50.04700  39.86400 1.000 104.74113 ? 452 ARG A O     1 
ATOM 3759 C CB    . ARG B 2 452 ? -7.80900  47.81500  37.82900 1.000 80.82880  ? 452 ARG A CB    1 
ATOM 3760 C CG    . ARG B 2 452 ? -7.46100  46.36000  37.55600 1.000 82.17090  ? 452 ARG A CG    1 
ATOM 3761 C CD    . ARG B 2 452 ? -6.61600  45.80000  38.68500 1.000 96.05218  ? 452 ARG A CD    1 
ATOM 3762 N NE    . ARG B 2 452 ? -5.37800  46.56800  38.85000 1.000 123.14736 ? 452 ARG A NE    1 
ATOM 3763 C CZ    . ARG B 2 452 ? -4.45100  46.31800  39.76400 1.000 129.03379 ? 452 ARG A CZ    1 
ATOM 3764 N NH1   . ARG B 2 452 ? -4.62300  45.33200  40.62600 1.000 113.34387 ? 452 ARG A NH1   1 
ATOM 3765 N NH2   . ARG B 2 452 ? -3.35700  47.05700  39.81500 1.000 119.49606 ? 452 ARG A NH2   1 
ATOM 3766 N N     . LEU B 2 453 ? -9.96200  50.14800  39.19200 1.000 78.27507  ? 453 LEU A N     1 
ATOM 3767 C CA    . LEU B 2 453 ? -10.07400 51.60900  39.44600 1.000 70.17572  ? 453 LEU A CA    1 
ATOM 3768 C C     . LEU B 2 453 ? -9.67400  51.92900  40.89700 1.000 81.81396  ? 453 LEU A C     1 
ATOM 3769 O O     . LEU B 2 453 ? -8.89800  52.88700  41.08300 1.000 85.01404  ? 453 LEU A O     1 
ATOM 3770 C CB    . LEU B 2 453 ? -11.48200 52.10000  39.11300 1.000 75.34808  ? 453 LEU A CB    1 
ATOM 3771 C CG    . LEU B 2 453 ? -11.61800 53.59700  38.81900 1.000 72.41374  ? 453 LEU A CG    1 
ATOM 3772 C CD1   . LEU B 2 453 ? -10.51900 54.05400  37.88000 1.000 65.82941  ? 453 LEU A CD1   1 
ATOM 3773 C CD2   . LEU B 2 453 ? -12.98100 53.88600  38.21700 1.000 77.80735  ? 453 LEU A CD2   1 
ATOM 3774 N N     . PRO B 2 454 ? -10.13300 51.19300  41.93400 1.000 85.40120  ? 454 PRO A N     1 
ATOM 3775 C CA    . PRO B 2 454 ? -9.68900  51.46500  43.29400 1.000 83.85939  ? 454 PRO A CA    1 
ATOM 3776 C C     . PRO B 2 454 ? -8.17100  51.45000  43.43700 1.000 84.00586  ? 454 PRO A C     1 
ATOM 3777 O O     . PRO B 2 454 ? -7.62700  52.29300  44.17600 1.000 74.81760  ? 454 PRO A O     1 
ATOM 3778 C CB    . PRO B 2 454 ? -10.35900 50.35200  44.11600 1.000 63.56172  ? 454 PRO A CB    1 
ATOM 3779 C CG    . PRO B 2 454 ? -10.74500 49.31100  43.09400 1.000 82.45667  ? 454 PRO A CG    1 
ATOM 3780 C CD    . PRO B 2 454 ? -11.11900 50.12600  41.87400 1.000 82.45068  ? 454 PRO A CD    1 
ATOM 3781 N N     . ASP B 2 455 ? -7.49800  50.52500  42.75000 1.000 88.97645  ? 455 ASP A N     1 
ATOM 3782 C CA    . ASP B 2 455 ? -6.02000  50.39400  42.88200 1.000 76.49268  ? 455 ASP A CA    1 
ATOM 3783 C C     . ASP B 2 455 ? -5.34500  51.67500  42.38600 1.000 87.06514  ? 455 ASP A C     1 
ATOM 3784 O O     . ASP B 2 455 ? -4.41100  52.16200  43.06100 1.000 87.93557  ? 455 ASP A O     1 
ATOM 3785 C CB    . ASP B 2 455 ? -5.52400  49.14800  42.16900 1.000 73.43796  ? 455 ASP A CB    1 
ATOM 3786 C CG    . ASP B 2 455 ? -6.14000  47.84200  42.64900 1.000 103.35105 ? 455 ASP A CG    1 
ATOM 3787 O OD1   . ASP B 2 455 ? -5.97000  47.51900  43.84300 1.000 104.32025 ? 455 ASP A OD1   1 
ATOM 3788 O OD2   . ASP B 2 455 ? -6.79000  47.16300  41.82900 1.000 123.67734 ? 455 ASP A OD2   1 
ATOM 3789 N N     . TYR B 2 456 ? -5.80600  52.20400  41.25200 1.000 79.58245  ? 456 TYR A N     1 
ATOM 3790 C CA    . TYR B 2 456 ? -5.21400  53.44300  40.68300 1.000 80.17329  ? 456 TYR A CA    1 
ATOM 3791 C C     . TYR B 2 456 ? -5.43000  54.58400  41.66500 1.000 80.96324  ? 456 TYR A C     1 
ATOM 3792 O O     . TYR B 2 456 ? -4.50800  55.39400  41.87500 1.000 91.05567  ? 456 TYR A O     1 
ATOM 3793 C CB    . TYR B 2 456 ? -5.84700  53.66100  39.30800 1.000 69.17719  ? 456 TYR A CB    1 
ATOM 3794 C CG    . TYR B 2 456 ? -5.29300  52.70900  38.25800 1.000 90.83955  ? 456 TYR A CG    1 
ATOM 3795 C CD1   . TYR B 2 456 ? -3.92400  52.52900  38.11200 1.000 116.27012 ? 456 TYR A CD1   1 
ATOM 3796 C CD2   . TYR B 2 456 ? -6.13400  51.95300  37.45400 1.000 90.44580  ? 456 TYR A CD2   1 
ATOM 3797 C CE1   . TYR B 2 456 ? -3.40800  51.65800  37.16800 1.000 119.83461 ? 456 TYR A CE1   1 
ATOM 3798 C CE2   . TYR B 2 456 ? -5.63100  51.07800  36.50700 1.000 98.06807  ? 456 TYR A CE2   1 
ATOM 3799 C CZ    . TYR B 2 456 ? -4.26400  50.92900  36.36400 1.000 123.10341 ? 456 TYR A CZ    1 
ATOM 3800 O OH    . TYR B 2 456 ? -3.76100  50.06600  35.43500 1.000 132.46660 ? 456 TYR A OH    1 
ATOM 3801 N N     . ALA B 2 457 ? -6.61300  54.63200  42.27600 1.000 78.10348  ? 457 ALA A N     1 
ATOM 3802 C CA    . ALA B 2 457 ? -6.92100  55.70700  43.24600 1.000 73.70941  ? 457 ALA A CA    1 
ATOM 3803 C C     . ALA B 2 457 ? -5.89800  55.67400  44.38000 1.000 82.70574  ? 457 ALA A C     1 
ATOM 3804 O O     . ALA B 2 457 ? -5.45700  56.75200  44.81900 1.000 92.50207  ? 457 ALA A O     1 
ATOM 3805 C CB    . ALA B 2 457 ? -8.32200  55.53800  43.77300 1.000 71.54450  ? 457 ALA A CB    1 
ATOM 3806 N N     . LEU B 2 458 ? -5.52500  54.47500  44.83000 1.000 78.39380  ? 458 LEU A N     1 
ATOM 3807 C CA    . LEU B 2 458 ? -4.56400  54.34300  45.95600 1.000 74.69323  ? 458 LEU A CA    1 
ATOM 3808 C C     . LEU B 2 458 ? -3.23700  55.01400  45.57500 1.000 84.02114  ? 458 LEU A C     1 
ATOM 3809 O O     . LEU B 2 458 ? -2.61900  55.64400  46.45500 1.000 102.04534 ? 458 LEU A O     1 
ATOM 3810 C CB    . LEU B 2 458 ? -4.37500  52.86800  46.30100 1.000 65.67833  ? 458 LEU A CB    1 
ATOM 3811 C CG    . LEU B 2 458 ? -5.49900  52.22000  47.11400 1.000 70.51565  ? 458 LEU A CG    1 
ATOM 3812 C CD1   . LEU B 2 458 ? -5.45000  50.71000  46.97600 1.000 60.24159  ? 458 LEU A CD1   1 
ATOM 3813 C CD2   . LEU B 2 458 ? -5.36200  52.62000  48.57100 1.000 82.71312  ? 458 LEU A CD2   1 
ATOM 3814 N N     . ASN B 2 459 ? -2.81800  54.87700  44.31600 1.000 82.32723  ? 459 ASN A N     1 
ATOM 3815 C CA    . ASN B 2 459 ? -1.52800  55.46900  43.86400 1.000 86.31152  ? 459 ASN A CA    1 
ATOM 3816 C C     . ASN B 2 459 ? -1.63100  56.99800  43.83200 1.000 76.49067  ? 459 ASN A C     1 
ATOM 3817 O O     . ASN B 2 459 ? -0.63900  57.65800  44.20000 1.000 98.22547  ? 459 ASN A O     1 
ATOM 3818 C CB    . ASN B 2 459 ? -1.10400  54.90900  42.51200 1.000 79.81512  ? 459 ASN A CB    1 
ATOM 3819 C CG    . ASN B 2 459 ? -1.06100  53.40000  42.51200 1.000 108.65479 ? 459 ASN A CG    1 
ATOM 3820 O OD1   . ASN B 2 459 ? -0.31600  52.80000  43.29400 1.000 105.25842 ? 459 ASN A OD1   1 
ATOM 3821 N ND2   . ASN B 2 459 ? -1.85000  52.77200  41.65300 1.000 136.48701 ? 459 ASN A ND2   1 
ATOM 3822 N N     . GLN B 2 460 ? -2.77500  57.54200  43.41100 1.000 70.11149  ? 460 GLN A N     1 
ATOM 3823 C CA    . GLN B 2 460 ? -2.92200  59.01400  43.27000 1.000 84.69058  ? 460 GLN A CA    1 
ATOM 3824 C C     . GLN B 2 460 ? -3.53000  59.62100  44.54200 1.000 81.98833  ? 460 GLN A C     1 
ATOM 3825 O O     . GLN B 2 460 ? -4.14400  60.70200  44.43500 1.000 83.98016  ? 460 GLN A O     1 
ATOM 3826 C CB    . GLN B 2 460 ? -3.83100  59.35500  42.08900 1.000 80.25035  ? 460 GLN A CB    1 
ATOM 3827 C CG    . GLN B 2 460 ? -3.09700  59.65300  40.78600 1.000 105.19167 ? 460 GLN A CG    1 
ATOM 3828 C CD    . GLN B 2 460 ? -2.71800  58.41400  40.00600 1.000 105.97034 ? 460 GLN A CD    1 
ATOM 3829 O OE1   . GLN B 2 460 ? -2.99700  57.28200  40.41400 1.000 105.65690 ? 460 GLN A OE1   1 
ATOM 3830 N NE2   . GLN B 2 460 ? -2.07600  58.62000  38.86600 1.000 128.75750 ? 460 GLN A NE2   1 
ATOM 3831 N N     . VAL B 2 461 ? -3.37400  58.96000  45.69100 1.000 78.74086  ? 461 VAL A N     1 
ATOM 3832 C CA    . VAL B 2 461 ? -4.01700  59.45000  46.94700 1.000 75.06838  ? 461 VAL A CA    1 
ATOM 3833 C C     . VAL B 2 461 ? -2.93500  59.84800  47.96100 1.000 86.30154  ? 461 VAL A C     1 
ATOM 3834 O O     . VAL B 2 461 ? -3.30300  60.36300  49.03900 1.000 77.70518  ? 461 VAL A O     1 
ATOM 3835 C CB    . VAL B 2 461 ? -4.94400  58.35000  47.49800 1.000 57.41727  ? 461 VAL A CB    1 
ATOM 3836 C CG1   . VAL B 2 461 ? -4.20935  57.33220  48.36190 1.000 67.12374  ? 461 VAL A CG1   1 
ATOM 3837 C CG2   . VAL B 2 461 ? -6.14964  58.92708  48.22447 1.000 74.94117  ? 461 VAL A CG2   1 
ATOM 3838 N N     . THR B 2 462 ? -1.65700  59.67100  47.61400 1.000 67.37380  ? 462 THR A N     1 
ATOM 3839 C CA    . THR B 2 462 ? -0.58200  59.92700  48.59700 1.000 65.37293  ? 462 THR A CA    1 
ATOM 3840 C C     . THR B 2 462 ? 0.43800   60.90500  48.05900 1.000 76.65732  ? 462 THR A C     1 
ATOM 3841 O O     . THR B 2 462 ? 0.55700   61.01300  46.82100 1.000 85.29925  ? 462 THR A O     1 
ATOM 3842 C CB    . THR B 2 462 ? 0.07100   58.59500  48.96000 1.000 63.40543  ? 462 THR A CB    1 
ATOM 3843 O OG1   . THR B 2 462 ? 1.15100   58.94000  49.82000 1.000 86.88555  ? 462 THR A OG1   1 
ATOM 3844 C CG2   . THR B 2 462 ? 0.59300   57.85200  47.74500 1.000 68.29772  ? 462 THR A CG2   1 
ATOM 3845 N N     . ASN B 2 463 ? 1.14700   61.60200  48.95300 1.000 71.99300  ? 463 ASN A N     1 
ATOM 3846 C CA    . ASN B 2 463 ? 2.23500   62.53400  48.54500 1.000 81.98751  ? 463 ASN A CA    1 
ATOM 3847 C C     . ASN B 2 463 ? 3.52500   61.99600  49.16800 1.000 79.51698  ? 463 ASN A C     1 
ATOM 3848 O O     . ASN B 2 463 ? 3.42100   61.27000  50.17500 1.000 64.42564  ? 463 ASN A O     1 
ATOM 3849 C CB    . ASN B 2 463 ? 1.91900   63.97300  48.93500 1.000 80.91026  ? 463 ASN A CB    1 
ATOM 3850 C CG    . ASN B 2 463 ? 2.83500   64.97200  48.26800 1.000 102.27767 ? 463 ASN A CG    1 
ATOM 3851 O OD1   . ASN B 2 463 ? 3.69400   64.59300  47.46500 1.000 111.87234 ? 463 ASN A OD1   1 
ATOM 3852 N ND2   . ASN B 2 463 ? 2.66200   66.24800  48.57800 1.000 128.30148 ? 463 ASN A ND2   1 
ATOM 3853 N N     . GLU B 2 464 ? 4.69200   62.32900  48.61100 1.000 54.51906  ? 464 GLU A N     1 
ATOM 3854 C CA    . GLU B 2 464 ? 5.93500   61.70000  49.12700 1.000 63.06012  ? 464 GLU A CA    1 
ATOM 3855 C C     . GLU B 2 464 ? 7.05700   62.72000  49.35300 1.000 59.37838  ? 464 GLU A C     1 
ATOM 3856 O O     . GLU B 2 464 ? 6.98300   63.82300  48.77400 1.000 76.76793  ? 464 GLU A O     1 
ATOM 3857 C CB    . GLU B 2 464 ? 6.42800   60.64300  48.14000 1.000 76.62023  ? 464 GLU A CB    1 
ATOM 3858 C CG    . GLU B 2 464 ? 6.95000   61.22500  46.83000 1.000 104.43003 ? 464 GLU A CG    1 
ATOM 3859 C CD    . GLU B 2 464 ? 7.50600   60.18200  45.87900 1.000 111.12187 ? 464 GLU A CD    1 
ATOM 3860 O OE1   . GLU B 2 464 ? 7.46300   58.98300  46.22200 1.000 119.00737 ? 464 GLU A OE1   1 
ATOM 3861 O OE2   . GLU B 2 464 ? 7.98900   60.57200  44.79700 1.000 116.18720 ? 464 GLU A OE2   1 
ATOM 3862 N N     . LEU B 2 465 ? 8.04500   62.35900  50.17700 1.000 63.94207  ? 465 LEU A N     1 
ATOM 3863 C CA    . LEU B 2 465 ? 9.23000   63.22400  50.40700 1.000 70.79202  ? 465 LEU A CA    1 
ATOM 3864 C C     . LEU B 2 465 ? 10.46700  62.34200  50.19800 1.000 72.38913  ? 465 LEU A C     1 
ATOM 3865 O O     . LEU B 2 465 ? 10.80300  61.58200  51.12600 1.000 76.66083  ? 465 LEU A O     1 
ATOM 3866 C CB    . LEU B 2 465 ? 9.20200   63.81300  51.81400 1.000 64.03496  ? 465 LEU A CB    1 
ATOM 3867 C CG    . LEU B 2 465 ? 10.28400  64.84800  52.13500 1.000 64.12919  ? 465 LEU A CG    1 
ATOM 3868 C CD1   . LEU B 2 465 ? 10.07500  66.10300  51.30900 1.000 79.01538  ? 465 LEU A CD1   1 
ATOM 3869 C CD2   . LEU B 2 465 ? 10.28000  65.17500  53.61600 1.000 66.59039  ? 465 LEU A CD2   1 
ATOM 3870 N N     . SER B 2 466 ? 11.10100  62.42300  49.02700 1.000 70.32391  ? 466 SER A N     1 
ATOM 3871 C CA    . SER B 2 466 ? 12.24400  61.52500  48.72400 1.000 64.58755  ? 466 SER A CA    1 
ATOM 3872 C C     . SER B 2 466 ? 13.57100  62.26200  48.91700 1.000 73.32642  ? 466 SER A C     1 
ATOM 3873 O O     . SER B 2 466 ? 13.62600  63.47000  48.61600 1.000 87.85405  ? 466 SER A O     1 
ATOM 3874 C CB    . SER B 2 466 ? 12.13900  60.97500  47.33100 1.000 82.62298  ? 466 SER A CB    1 
ATOM 3875 O OG    . SER B 2 466 ? 12.19400  62.02000  46.37200 1.000 95.79750  ? 466 SER A OG    1 
ATOM 3876 N N     . TYR B 2 467 ? 14.59800  61.55100  49.38500 1.000 72.55425  ? 467 TYR A N     1 
ATOM 3877 C CA    . TYR B 2 467 ? 15.94000  62.16200  49.55600 1.000 82.63364  ? 467 TYR A CA    1 
ATOM 3878 C C     . TYR B 2 467 ? 16.41300  62.65900  48.20300 1.000 82.31797  ? 467 TYR A C     1 
ATOM 3879 O O     . TYR B 2 467 ? 16.99600  63.75800  48.12900 1.000 98.51028  ? 467 TYR A O     1 
ATOM 3880 C CB    . TYR B 2 467 ? 16.87100  61.09500  50.13200 1.000 71.33995  ? 467 TYR A CB    1 
ATOM 3881 C CG    . TYR B 2 467 ? 18.27000  61.56000  50.51300 1.000 76.06910  ? 467 TYR A CG    1 
ATOM 3882 C CD1   . TYR B 2 467 ? 18.54800  62.02000  51.79300 1.000 79.76063  ? 467 TYR A CD1   1 
ATOM 3883 C CD2   . TYR B 2 467 ? 19.31300  61.51900  49.59700 1.000 84.18366  ? 467 TYR A CD2   1 
ATOM 3884 C CE1   . TYR B 2 467 ? 19.81900  62.43800  52.14800 1.000 84.33902  ? 467 TYR A CE1   1 
ATOM 3885 C CE2   . TYR B 2 467 ? 20.58900  61.93300  49.94100 1.000 98.77685  ? 467 TYR A CE2   1 
ATOM 3886 C CZ    . TYR B 2 467 ? 20.84200  62.39400  51.21900 1.000 77.15100  ? 467 TYR A CZ    1 
ATOM 3887 O OH    . TYR B 2 467 ? 22.09700  62.80400  51.56000 1.000 90.47830  ? 467 TYR A OH    1 
ATOM 3888 N N     . ALA B 2 468 ? 16.15300  61.88100  47.15100 1.000 61.76571  ? 468 ALA A N     1 
ATOM 3889 C CA    . ALA B 2 468 ? 16.63000  62.25200  45.79900 1.000 80.74789  ? 468 ALA A CA    1 
ATOM 3890 C C     . ALA B 2 468 ? 16.05200  63.60500  45.39300 1.000 85.20112  ? 468 ALA A C     1 
ATOM 3891 O O     . ALA B 2 468 ? 16.81600  64.47200  44.92900 1.000 94.67322  ? 468 ALA A O     1 
ATOM 3892 C CB    . ALA B 2 468 ? 16.23500  61.18700  44.81100 1.000 94.14815  ? 468 ALA A CB    1 
ATOM 3893 N N     . ASP B 2 469 ? 14.74300  63.77900  45.56000 1.000 78.01844  ? 469 ASP A N     1 
ATOM 3894 C CA    . ASP B 2 469 ? 14.10600  65.04400  45.10900 1.000 88.09233  ? 469 ASP A CA    1 
ATOM 3895 C C     . ASP B 2 469 ? 14.75600  66.20300  45.86500 1.000 80.99178  ? 469 ASP A C     1 
ATOM 3896 O O     . ASP B 2 469 ? 15.11900  67.20500  45.21900 1.000 84.13437  ? 469 ASP A O     1 
ATOM 3897 C CB    . ASP B 2 469 ? 12.59700  65.00100  45.27900 1.000 75.96152  ? 469 ASP A CB    1 
ATOM 3898 C CG    . ASP B 2 469 ? 11.81200  65.95200  44.38900 1.000 110.10396 ? 469 ASP A CG    1 
ATOM 3899 O OD1   . ASP B 2 469 ? 12.45300  66.72000  43.64100 1.000 120.53859 ? 469 ASP A OD1   1 
ATOM 3900 O OD2   . ASP B 2 469 ? 10.56600  65.90200  44.43700 1.000 128.88117 ? 469 ASP A OD2   1 
ATOM 3901 N N     . ILE B 2 470 ? 14.91900  66.05300  47.17900 1.000 59.06864  ? 470 ILE A N     1 
ATOM 3902 C CA    . ILE B 2 470 ? 15.50900  67.15000  47.99900 1.000 59.41195  ? 470 ILE A CA    1 
ATOM 3903 C C     . ILE B 2 470 ? 16.95100  67.37700  47.52400 1.000 70.32960  ? 470 ILE A C     1 
ATOM 3904 O O     . ILE B 2 470 ? 17.34500  68.54800  47.36800 1.000 80.45438  ? 470 ILE A O     1 
ATOM 3905 C CB    . ILE B 2 470 ? 15.43500  66.82000  49.49800 1.000 65.77549  ? 470 ILE A CB    1 
ATOM 3906 C CG1   . ILE B 2 470 ? 14.01200  66.47700  49.92300 1.000 67.06052  ? 470 ILE A CG1   1 
ATOM 3907 C CG2   . ILE B 2 470 ? 16.01000  67.96500  50.33000 1.000 56.54290  ? 470 ILE A CG2   1 
ATOM 3908 C CD1   . ILE B 2 470 ? 13.00000  67.56300  49.61200 1.000 79.43450  ? 470 ILE A CD1   1 
ATOM 3909 N N     . LYS B 2 471 ? 17.69000  66.29600  47.27200 1.000 67.17511  ? 471 LYS A N     1 
ATOM 3910 C CA    . LYS B 2 471 ? 19.09200  66.41800  46.80000 1.000 72.46884  ? 471 LYS A CA    1 
ATOM 3911 C C     . LYS B 2 471 ? 19.11700  67.22100  45.49200 1.000 69.73935  ? 471 LYS A C     1 
ATOM 3912 O O     . LYS B 2 471 ? 19.92700  68.16500  45.39000 1.000 66.88378  ? 471 LYS A O     1 
ATOM 3913 C CB    . LYS B 2 471 ? 19.68700  65.02100  46.60000 1.000 64.15994  ? 471 LYS A CB    1 
ATOM 3914 C CG    . LYS B 2 471 ? 21.12100  64.97300  46.10400 1.000 74.80998  ? 471 LYS A CG    1 
ATOM 3915 C CD    . LYS B 2 471 ? 21.63600  63.54500  45.97200 1.000 68.76245  ? 471 LYS A CD    1 
ATOM 3916 C CE    . LYS B 2 471 ? 23.06200  63.48500  45.52800 1.000 66.85189  ? 471 LYS A CE    1 
ATOM 3917 N NZ    . LYS B 2 471 ? 23.54400  62.10400  45.45800 1.000 79.06881  ? 471 LYS A NZ    1 
ATOM 3918 N N     . TYR B 2 472 ? 18.24600  66.87000  44.54300 1.000 65.80550  ? 472 TYR A N     1 
ATOM 3919 C CA    . TYR B 2 472 ? 18.21800  67.56800  43.23100 1.000 70.78403  ? 472 TYR A CA    1 
ATOM 3920 C C     . TYR B 2 472 ? 17.88700  69.03100  43.46100 1.000 75.71753  ? 472 TYR A C     1 
ATOM 3921 O O     . TYR B 2 472 ? 18.59800  69.90400  42.92800 1.000 89.46114  ? 472 TYR A O     1 
ATOM 3922 C CB    . TYR B 2 472 ? 17.19900  66.88000  42.31800 1.000 60.73164  ? 472 TYR A CB    1 
ATOM 3923 C CG    . TYR B 2 472 ? 16.94800  67.56700  40.98300 1.000 74.28816  ? 472 TYR A CG    1 
ATOM 3924 C CD1   . TYR B 2 472 ? 17.78700  67.35300  39.89700 1.000 59.68913  ? 472 TYR A CD1   1 
ATOM 3925 C CD2   . TYR B 2 472 ? 15.85400  68.40300  40.80000 1.000 80.79102  ? 472 TYR A CD2   1 
ATOM 3926 C CE1   . TYR B 2 472 ? 17.56000  67.96900  38.67800 1.000 68.46004  ? 472 TYR A CE1   1 
ATOM 3927 C CE2   . TYR B 2 472 ? 15.61300  69.02000  39.58500 1.000 76.57207  ? 472 TYR A CE2   1 
ATOM 3928 C CZ    . TYR B 2 472 ? 16.47000  68.80400  38.52200 1.000 68.96173  ? 472 TYR A CZ    1 
ATOM 3929 O OH    . TYR B 2 472 ? 16.24000  69.41300  37.32400 1.000 86.78803  ? 472 TYR A OH    1 
ATOM 3930 N N     . GLN B 2 473 ? 16.84700  69.29800  44.25000 1.000 76.33143  ? 473 GLN A N     1 
ATOM 3931 C CA    . GLN B 2 473 ? 16.41500  70.69900  44.48200 1.000 78.12316  ? 473 GLN A CA    1 
ATOM 3932 C C     . GLN B 2 473 ? 17.56800  71.47900  45.13000 1.000 76.38548  ? 473 GLN A C     1 
ATOM 3933 O O     . GLN B 2 473 ? 17.85000  72.60800  44.67800 1.000 86.94668  ? 473 GLN A O     1 
ATOM 3934 C CB    . GLN B 2 473 ? 15.17100  70.73600  45.36600 1.000 69.65902  ? 473 GLN A CB    1 
ATOM 3935 C CG    . GLN B 2 473 ? 13.92500  70.13000  44.73100 1.000 71.14717  ? 473 GLN A CG    1 
ATOM 3936 C CD    . GLN B 2 473 ? 13.58500  70.73800  43.38900 1.000 93.41425  ? 473 GLN A CD    1 
ATOM 3937 O OE1   . GLN B 2 473 ? 13.43700  71.95700  43.25200 1.000 102.33376 ? 473 GLN A OE1   1 
ATOM 3938 N NE2   . GLN B 2 473 ? 13.46900  69.89000  42.37900 1.000 109.71078 ? 473 GLN A NE2   1 
ATOM 3939 N N     . LEU B 2 474 ? 18.21300  70.88900  46.13700 1.000 68.25579  ? 474 LEU A N     1 
ATOM 3940 C CA    . LEU B 2 474 ? 19.33100  71.57200  46.83500 1.000 60.05723  ? 474 LEU A CA    1 
ATOM 3941 C C     . LEU B 2 474 ? 20.44300  71.86000  45.81800 1.000 78.54488  ? 474 LEU A C     1 
ATOM 3942 O O     . LEU B 2 474 ? 21.01600  72.96600  45.86600 1.000 75.97539  ? 474 LEU A O     1 
ATOM 3943 C CB    . LEU B 2 474 ? 19.83800  70.70500  47.98500 1.000 58.21773  ? 474 LEU A CB    1 
ATOM 3944 C CG    . LEU B 2 474 ? 19.03400  70.76800  49.28700 1.000 59.20948  ? 474 LEU A CG    1 
ATOM 3945 C CD1   . LEU B 2 474 ? 19.52600  69.70400  50.25200 1.000 55.53786  ? 474 LEU A CD1   1 
ATOM 3946 C CD2   . LEU B 2 474 ? 19.16600  72.14400  49.91100 1.000 66.05973  ? 474 LEU A CD2   1 
ATOM 3947 N N     . GLY B 2 475 ? 20.72500  70.90100  44.93400 1.000 67.44215  ? 475 GLY A N     1 
ATOM 3948 C CA    . GLY B 2 475 ? 21.78300  71.07800  43.92100 1.000 70.19404  ? 475 GLY A CA    1 
ATOM 3949 C C     . GLY B 2 475 ? 21.45700  72.21200  42.97300 1.000 71.07973  ? 475 GLY A C     1 
ATOM 3950 O O     . GLY B 2 475 ? 22.38600  72.94900  42.59200 1.000 102.06005 ? 475 GLY A O     1 
ATOM 3951 N N     . LEU B 2 476 ? 20.18300  72.35500  42.60600 1.000 71.30127  ? 476 LEU A N     1 
ATOM 3952 C CA    . LEU B 2 476 ? 19.76100  73.45000  41.69700 1.000 76.88662  ? 476 LEU A CA    1 
ATOM 3953 C C     . LEU B 2 476 ? 20.17300  74.79100  42.31700 1.000 83.82048  ? 476 LEU A C     1 
ATOM 3954 O O     . LEU B 2 476 ? 20.57400  75.69400  41.55900 1.000 98.18323  ? 476 LEU A O     1 
ATOM 3955 C CB    . LEU B 2 476 ? 18.25300  73.38900  41.47400 1.000 70.33017  ? 476 LEU A CB    1 
ATOM 3956 C CG    . LEU B 2 476 ? 17.71300  72.12100  40.80800 1.000 71.69403  ? 476 LEU A CG    1 
ATOM 3957 C CD1   . LEU B 2 476 ? 16.21100  72.24600  40.63600 1.000 90.99035  ? 476 LEU A CD1   1 
ATOM 3958 C CD2   . LEU B 2 476 ? 18.38900  71.89600  39.46900 1.000 73.73123  ? 476 LEU A CD2   1 
ATOM 3959 N N     . ILE B 2 477 ? 20.05900  74.91300  43.64000 1.000 73.77652  ? 477 ILE A N     1 
ATOM 3960 C CA    . ILE B 2 477 ? 20.41400  76.18500  44.34000 1.000 80.65382  ? 477 ILE A CA    1 
ATOM 3961 C C     . ILE B 2 477 ? 21.94200  76.35400  44.35100 1.000 82.59345  ? 477 ILE A C     1 
ATOM 3962 O O     . ILE B 2 477 ? 22.41400  77.46900  44.05800 1.000 81.60857  ? 477 ILE A O     1 
ATOM 3963 C CB    . ILE B 2 477 ? 19.82100  76.18800  45.75900 1.000 67.91088  ? 477 ILE A CB    1 
ATOM 3964 C CG1   . ILE B 2 477 ? 18.35800  75.75500  45.73900 1.000 68.80842  ? 477 ILE A CG1   1 
ATOM 3965 C CG2   . ILE B 2 477 ? 20.00200  77.55000  46.42700 1.000 88.08108  ? 477 ILE A CG2   1 
ATOM 3966 C CD1   . ILE B 2 477 ? 17.76400  75.49900  47.11000 1.000 96.40679  ? 477 ILE A CD1   1 
ATOM 3967 N N     . GLY B 2 478 ? 22.68000  75.29000  44.66700 1.000 83.05178  ? 478 GLY A N     1 
ATOM 3968 C CA    . GLY B 2 478 ? 24.15300  75.36100  44.69800 1.000 73.21318  ? 478 GLY A CA    1 
ATOM 3969 C C     . GLY B 2 478 ? 24.67400  75.27800  46.11700 1.000 77.27269  ? 478 GLY A C     1 
ATOM 3970 O O     . GLY B 2 478 ? 23.87500  75.49300  47.04900 1.000 96.81307  ? 478 GLY A O     1 
ATOM 3971 N N     . LYS B 2 479 ? 25.96400  74.97400  46.28300 1.000 76.02754  ? 479 LYS A N     1 
ATOM 3972 C CA    . LYS B 2 479 ? 26.54900  74.82100  47.64000 1.000 81.16725  ? 479 LYS A CA    1 
ATOM 3973 C C     . LYS B 2 479 ? 27.67800  75.84100  47.84600 1.000 103.82530 ? 479 LYS A C     1 
ATOM 3974 O O     . LYS B 2 479 ? 27.93900  76.19600  49.01300 1.000 97.71908  ? 479 LYS A O     1 
ATOM 3975 C CB    . LYS B 2 479 ? 27.09400  73.40400  47.83600 1.000 95.16012  ? 479 LYS A CB    1 
ATOM 3976 C CG    . LYS B 2 479 ? 28.43200  73.11300  47.17300 1.000 104.77470 ? 479 LYS A CG    1 
ATOM 3977 C CD    . LYS B 2 479 ? 28.96300  71.71500  47.46500 1.000 113.43576 ? 479 LYS A CD    1 
ATOM 3978 C CE    . LYS B 2 479 ? 30.32400  71.49000  46.88700 1.000 116.76400 ? 479 LYS A CE    1 
ATOM 3979 N NZ    . LYS B 2 479 ? 30.83300  70.15200  47.19800 1.000 120.86542 ? 479 LYS A NZ    1 
ATOM 3980 N N     . ASN B 2 480 ? 28.31600  76.29100  46.76300 1.000 102.79489 ? 480 ASN A N     1 
ATOM 3981 C CA    . ASN B 2 480 ? 29.47200  77.22200  46.89300 1.000 94.28011  ? 480 ASN A CA    1 
ATOM 3982 C C     . ASN B 2 480 ? 29.25200  78.45200  46.00900 1.000 107.09702 ? 480 ASN A C     1 
ATOM 3983 O O     . ASN B 2 480 ? 28.32200  78.42600  45.17900 1.000 105.31500 ? 480 ASN A O     1 
ATOM 3984 C CB    . ASN B 2 480 ? 30.79600  76.52200  46.60700 1.000 82.51682  ? 480 ASN A CB    1 
ATOM 3985 C CG    . ASN B 2 480 ? 30.82300  75.84900  45.25800 1.000 112.55119 ? 480 ASN A CG    1 
ATOM 3986 O OD1   . ASN B 2 480 ? 30.70200  76.51600  44.22600 1.000 123.80693 ? 480 ASN A OD1   1 
ATOM 3987 N ND2   . ASN B 2 480 ? 30.99800  74.53600  45.24200 1.000 113.21395 ? 480 ASN A ND2   1 
ATOM 3988 N N     . GLU B 2 481 ? 30.09400  79.47500  46.16400 1.000 102.01506 ? 481 GLU A N     1 
ATOM 3989 C CA    . GLU B 2 481 ? 29.92600  80.74200  45.40700 1.000 92.70142  ? 481 GLU A CA    1 
ATOM 3990 C C     . GLU B 2 481 ? 30.23100  80.52000  43.92000 1.000 96.95233  ? 481 GLU A C     1 
ATOM 3991 O O     . GLU B 2 481 ? 30.13900  81.49300  43.14800 1.000 109.54971 ? 481 GLU A O     1 
ATOM 3992 C CB    . GLU B 2 481 ? 30.86700  81.80300  45.97300 1.000 102.76192 ? 481 GLU A CB    1 
ATOM 3993 C CG    . GLU B 2 481 ? 32.34400  81.47200  45.77900 1.000 105.85352 ? 481 GLU A CG    1 
ATOM 3994 C CD    . GLU B 2 481 ? 32.92500  80.50200  46.79200 1.000 126.24900 ? 481 GLU A CD    1 
ATOM 3995 O OE1   . GLU B 2 481 ? 32.18700  80.10200  47.71500 1.000 119.83271 ? 481 GLU A OE1   1 
ATOM 3996 O OE2   . GLU B 2 481 ? 34.11100  80.13800  46.65200 1.000 142.60697 ? 481 GLU A OE2   1 
ATOM 3997 N N     . ASN B 2 482 ? 30.61100  79.29800  43.54800 1.000 93.14371  ? 482 ASN A N     1 
ATOM 3998 C CA    . ASN B 2 482 ? 30.90700  78.98000  42.12700 1.000 94.38710  ? 482 ASN A CA    1 
ATOM 3999 C C     . ASN B 2 482 ? 29.91300  77.92300  41.64600 1.000 99.91059  ? 482 ASN A C     1 
ATOM 4000 O O     . ASN B 2 482 ? 30.23100  77.21900  40.66600 1.000 107.86812 ? 482 ASN A O     1 
ATOM 4001 C CB    . ASN B 2 482 ? 32.34500  78.50700  41.95600 1.000 87.21742  ? 482 ASN A CB    1 
ATOM 4002 C CG    . ASN B 2 482 ? 33.33700  79.44700  42.59700 1.000 111.91959 ? 482 ASN A CG    1 
ATOM 4003 O OD1   . ASN B 2 482 ? 34.07700  79.04800  43.50200 1.000 114.46248 ? 482 ASN A OD1   1 
ATOM 4004 N ND2   . ASN B 2 482 ? 33.36800  80.69300  42.14800 1.000 115.41274 ? 482 ASN A ND2   1 
ATOM 4005 N N     . GLU B 2 483 ? 28.76700  77.79500  42.32200 1.000 108.67218 ? 483 GLU A N     1 
ATOM 4006 C CA    . GLU B 2 483 ? 27.82000  76.70600  41.96500 1.000 91.13478  ? 483 GLU A CA    1 
ATOM 4007 C C     . GLU B 2 483 ? 26.43100  77.25000  41.61100 1.000 85.64054  ? 483 GLU A C     1 
ATOM 4008 O O     . GLU B 2 483 ? 25.72900  77.71600  42.53100 1.000 103.24815 ? 483 GLU A O     1 
ATOM 4009 C CB    . GLU B 2 483 ? 27.67400  75.69600  43.10300 1.000 96.77326  ? 483 GLU A CB    1 
ATOM 4010 C CG    . GLU B 2 483 ? 28.52300  74.44400  42.90900 1.000 100.24497 ? 483 GLU A CG    1 
ATOM 4011 C CD    . GLU B 2 483 ? 27.99700  73.23800  43.66200 1.000 115.02715 ? 483 GLU A CD    1 
ATOM 4012 O OE1   . GLU B 2 483 ? 26.92700  73.35800  44.29400 1.000 98.46575  ? 483 GLU A OE1   1 
ATOM 4013 O OE2   . GLU B 2 483 ? 28.65800  72.18000  43.62300 1.000 124.35003 ? 483 GLU A OE2   1 
ATOM 4014 N N     . LYS B 2 484 ? 26.06400  77.20400  40.33200 1.000 92.27451  ? 484 LYS A N     1 
ATOM 4015 C CA    . LYS B 2 484 ? 24.69600  77.58800  39.89200 1.000 92.35525  ? 484 LYS A CA    1 
ATOM 4016 C C     . LYS B 2 484 ? 24.17900  78.86300  40.57100 1.000 90.39856  ? 484 LYS A C     1 
ATOM 4017 O O     . LYS B 2 484 ? 24.93100  79.85500  40.62900 1.000 102.40691 ? 484 LYS A O     1 
ATOM 4018 C CB    . LYS B 2 484 ? 23.74000  76.42300  40.17000 1.000 91.17442  ? 484 LYS A CB    1 
ATOM 4019 C CG    . LYS B 2 484 ? 24.21500  75.07600  39.64700 1.000 91.97283  ? 484 LYS A CG    1 
ATOM 4020 C CD    . LYS B 2 484 ? 23.07600  74.10400  39.36700 1.000 112.37510 ? 484 LYS A CD    1 
ATOM 4021 C CE    . LYS B 2 484 ? 22.13800  74.64100  38.33300 1.000 109.05379 ? 484 LYS A CE    1 
ATOM 4022 N NZ    . LYS B 2 484 ? 21.12400  73.65700  37.94700 1.000 124.30924 ? 484 LYS A NZ    1 
ATOM 4023 N N     . LEU B 2 485 ? 22.93400  78.83400  41.04800 1.000 71.40015  ? 485 LEU A N     1 
ATOM 4024 C CA    . LEU B 2 485 ? 22.29500  80.04700  41.62300 1.000 78.23761  ? 485 LEU A CA    1 
ATOM 4025 C C     . LEU B 2 485 ? 23.24100  80.79100  42.57800 1.000 97.07901  ? 485 LEU A C     1 
ATOM 4026 O O     . LEU B 2 485 ? 23.30100  82.03400  42.48100 1.000 104.82672 ? 485 LEU A O     1 
ATOM 4027 C CB    . LEU B 2 485 ? 21.00600  79.61600  42.31700 1.000 70.44038  ? 485 LEU A CB    1 
ATOM 4028 C CG    . LEU B 2 485 ? 19.77600  80.49400  42.07100 1.000 87.57749  ? 485 LEU A CG    1 
ATOM 4029 C CD1   . LEU B 2 485 ? 19.69400  80.87600  40.60500 1.000 74.33159  ? 485 LEU A CD1   1 
ATOM 4030 C CD2   . LEU B 2 485 ? 18.53500  79.72400  42.48000 1.000 77.39108  ? 485 LEU A CD2   1 
ATOM 4031 N N     . LEU B 2 486 ? 23.94300  80.08400  43.46500 1.000 85.97438  ? 486 LEU A N     1 
ATOM 4032 C CA    . LEU B 2 486 ? 24.77000  80.80300  44.46900 1.000 75.58989  ? 486 LEU A CA    1 
ATOM 4033 C C     . LEU B 2 486 ? 25.79000  81.67600  43.72200 1.000 87.01935  ? 486 LEU A C     1 
ATOM 4034 O O     . LEU B 2 486 ? 26.05200  82.80900  44.17800 1.000 89.37251  ? 486 LEU A O     1 
ATOM 4035 C CB    . LEU B 2 486 ? 25.46500  79.83900  45.42900 1.000 89.24323  ? 486 LEU A CB    1 
ATOM 4036 C CG    . LEU B 2 486 ? 24.55500  79.00200  46.33200 1.000 91.57268  ? 486 LEU A CG    1 
ATOM 4037 C CD1   . LEU B 2 486 ? 25.29800  78.60700  47.59500 1.000 93.73356  ? 486 LEU A CD1   1 
ATOM 4038 C CD2   . LEU B 2 486 ? 23.27200  79.73400  46.67400 1.000 83.41006  ? 486 LEU A CD2   1 
ATOM 4039 N N     . LYS B 2 487 ? 26.33100  81.16500  42.61500 1.000 82.47313  ? 487 LYS A N     1 
ATOM 4040 C CA    . LYS B 2 487 ? 27.32300  81.93300  41.82000 1.000 83.22346  ? 487 LYS A CA    1 
ATOM 4041 C C     . LYS B 2 487 ? 26.66000  83.20800  41.28500 1.000 83.69196  ? 487 LYS A C     1 
ATOM 4042 O O     . LYS B 2 487 ? 27.28800  84.28200  41.36200 1.000 104.36337 ? 487 LYS A O     1 
ATOM 4043 C CB    . LYS B 2 487 ? 27.86400  81.08000  40.67000 1.000 72.65987  ? 487 LYS A CB    1 
ATOM 4044 C CG    . LYS B 2 487 ? 28.97400  81.72800  39.86000 1.000 90.03329  ? 487 LYS A CG    1 
ATOM 4045 C CD    . LYS B 2 487 ? 29.54800  80.80200  38.79600 1.000 99.76210  ? 487 LYS A CD    1 
ATOM 4046 C CE    . LYS B 2 487 ? 30.63800  81.46400  38.01700 1.000 124.95631 ? 487 LYS A CE    1 
ATOM 4047 N NZ    . LYS B 2 487 ? 30.16200  82.69400  37.38000 1.000 138.57354 ? 487 LYS A NZ    1 
ATOM 4048 N N     . ALA B 2 488 ? 25.43300  83.09000  40.78000 1.000 75.08253  ? 488 ALA A N     1 
ATOM 4049 C CA    . ALA B 2 488 ? 24.71900  84.26700  40.23700 1.000 94.75283  ? 488 ALA A CA    1 
ATOM 4050 C C     . ALA B 2 488 ? 24.62900  85.33800  41.32200 1.000 90.87162  ? 488 ALA A C     1 
ATOM 4051 O O     . ALA B 2 488 ? 24.88600  86.52500  41.03200 1.000 97.90764  ? 488 ALA A O     1 
ATOM 4052 C CB    . ALA B 2 488 ? 23.35000  83.85100  39.76300 1.000 77.10726  ? 488 ALA A CB    1 
ATOM 4053 N N     . ILE B 2 489 ? 24.28800  84.92600  42.54100 1.000 83.58396  ? 489 ILE A N     1 
ATOM 4054 C CA    . ILE B 2 489 ? 24.16100  85.89100  43.67100 1.000 81.59380  ? 489 ILE A CA    1 
ATOM 4055 C C     . ILE B 2 489 ? 25.52100  86.56800  43.89300 1.000 86.55620  ? 489 ILE A C     1 
ATOM 4056 O O     . ILE B 2 489 ? 25.54800  87.80600  44.05600 1.000 93.90449  ? 489 ILE A O     1 
ATOM 4057 C CB    . ILE B 2 489 ? 23.66300  85.16400  44.93200 1.000 89.72260  ? 489 ILE A CB    1 
ATOM 4058 C CG1   . ILE B 2 489 ? 22.20200  84.73900  44.79100 1.000 72.99523  ? 489 ILE A CG1   1 
ATOM 4059 C CG2   . ILE B 2 489 ? 23.88800  86.01000  46.18500 1.000 95.18949  ? 489 ILE A CG2   1 
ATOM 4060 C CD1   . ILE B 2 489 ? 21.24800  85.88700  44.51700 1.000 84.80738  ? 489 ILE A CD1   1 
ATOM 4061 N N     . ASP B 2 490 ? 26.60300  85.78700  43.88000 1.000 84.13748  ? 490 ASP A N     1 
ATOM 4062 C CA    . ASP B 2 490 ? 27.95900  86.35400  44.11600 1.000 82.67311  ? 490 ASP A CA    1 
ATOM 4063 C C     . ASP B 2 490 ? 28.21800  87.44600  43.07800 1.000 87.23578  ? 490 ASP A C     1 
ATOM 4064 O O     . ASP B 2 490 ? 28.68300  88.53600  43.46600 1.000 91.73357  ? 490 ASP A O     1 
ATOM 4065 C CB    . ASP B 2 490 ? 29.03300  85.28200  44.06500 1.000 80.94683  ? 490 ASP A CB    1 
ATOM 4066 C CG    . ASP B 2 490 ? 30.40000  85.69700  44.59100 1.000 101.27777 ? 490 ASP A CG    1 
ATOM 4067 O OD1   . ASP B 2 490 ? 30.52500  86.84600  45.06300 1.000 103.51065 ? 490 ASP A OD1   1 
ATOM 4068 O OD2   . ASP B 2 490 ? 31.32900  84.86600  44.52300 1.000 119.92800 ? 490 ASP A OD2   1 
ATOM 4069 N N     . GLN B 2 491 ? 27.90500  87.16500  41.81300 1.000 88.87235  ? 491 GLN A N     1 
ATOM 4070 C CA    . GLN B 2 491 ? 28.16600  88.14800  40.73100 1.000 95.67674  ? 491 GLN A CA    1 
ATOM 4071 C C     . GLN B 2 491 ? 27.36100  89.42400  41.01100 1.000 96.02734  ? 491 GLN A C     1 
ATOM 4072 O O     . GLN B 2 491 ? 27.92100  90.52200  40.84400 1.000 100.02656 ? 491 GLN A O     1 
ATOM 4073 C CB    . GLN B 2 491 ? 27.80800  87.55700  39.36800 1.000 91.46384  ? 491 GLN A CB    1 
ATOM 4074 C CG    . GLN B 2 491 ? 28.46400  86.20900  39.09200 1.000 102.79294 ? 491 GLN A CG    1 
ATOM 4075 C CD    . GLN B 2 491 ? 29.94700  86.19300  39.38700 1.000 112.64376 ? 491 GLN A CD    1 
ATOM 4076 O OE1   . GLN B 2 491 ? 30.42600  85.43600  40.23800 1.000 125.24954 ? 491 GLN A OE1   1 
ATOM 4077 N NE2   . GLN B 2 491 ? 30.69100  87.03700  38.68700 1.000 105.09862 ? 491 GLN A NE2   1 
ATOM 4078 N N     . LEU B 2 492 ? 26.10300  89.27600  41.42900 1.000 88.09205  ? 492 LEU A N     1 
ATOM 4079 C CA    . LEU B 2 492 ? 25.24600  90.46000  41.69100 1.000 81.19934  ? 492 LEU A CA    1 
ATOM 4080 C C     . LEU B 2 492 ? 25.91900  91.32700  42.76400 1.000 93.13923  ? 492 LEU A C     1 
ATOM 4081 O O     . LEU B 2 492 ? 25.99200  92.55700  42.57500 1.000 112.66814 ? 492 LEU A O     1 
ATOM 4082 C CB    . LEU B 2 492 ? 23.84600  90.03000  42.12200 1.000 82.23516  ? 492 LEU A CB    1 
ATOM 4083 C CG    . LEU B 2 492 ? 22.75200  90.11400  41.05400 1.000 83.62067  ? 492 LEU A CG    1 
ATOM 4084 C CD1   . LEU B 2 492 ? 23.07400  89.22700  39.86400 1.000 98.99263  ? 492 LEU A CD1   1 
ATOM 4085 C CD2   . LEU B 2 492 ? 21.41700  89.73100  41.66500 1.000 99.64823  ? 492 LEU A CD2   1 
ATOM 4086 N N     . GLU B 2 493 ? 26.39300  90.70100  43.84200 1.000 81.40017  ? 493 GLU A N     1 
ATOM 4087 C CA    . GLU B 2 493 ? 27.05600  91.46400  44.93000 1.000 95.90590  ? 493 GLU A CA    1 
ATOM 4088 C C     . GLU B 2 493 ? 28.32700  92.11000  44.36300 1.000 94.43171  ? 493 GLU A C     1 
ATOM 4089 O O     . GLU B 2 493 ? 28.56600  93.29700  44.65100 1.000 98.10252  ? 493 GLU A O     1 
ATOM 4090 C CB    . GLU B 2 493 ? 27.37000  90.57400  46.13000 1.000 82.55606  ? 493 GLU A CB    1 
ATOM 4091 C CG    . GLU B 2 493 ? 28.05900  91.31400  47.27400 1.000 101.35341 ? 493 GLU A CG    1 
ATOM 4092 C CD    . GLU B 2 493 ? 27.20400  92.31400  48.03300 1.000 117.09872 ? 493 GLU A CD    1 
ATOM 4093 O OE1   . GLU B 2 493 ? 26.70500  93.27900  47.41600 1.000 129.75236 ? 493 GLU A OE1   1 
ATOM 4094 O OE2   . GLU B 2 493 ? 27.04500  92.13100  49.25700 1.000 116.31565 ? 493 GLU A OE2   1 
ATOM 4095 N N     . LYS B 2 494 ? 29.09100  91.36100  43.56600 1.000 82.29346  ? 494 LYS A N     1 
ATOM 4096 C CA    . LYS B 2 494 ? 30.32200  91.91500  42.94900 1.000 83.50790  ? 494 LYS A CA    1 
ATOM 4097 C C     . LYS B 2 494 ? 29.94600  93.16400  42.14700 1.000 99.61296  ? 494 LYS A C     1 
ATOM 4098 O O     . LYS B 2 494 ? 30.64600  94.18700  42.27300 1.000 100.13071 ? 494 LYS A O     1 
ATOM 4099 C CB    . LYS B 2 494 ? 30.97800  90.88700  42.02300 1.000 85.08894  ? 494 LYS A CB    1 
ATOM 4100 C CG    . LYS B 2 494 ? 32.02900  91.44600  41.07800 1.000 87.73560  ? 494 LYS A CG    1 
ATOM 4101 C CD    . LYS B 2 494 ? 32.51300  90.42800  40.05400 1.000 90.47046  ? 494 LYS A CD    1 
ATOM 4102 C CE    . LYS B 2 494 ? 33.44000  91.04100  39.05500 1.000 104.23605 ? 494 LYS A CE    1 
ATOM 4103 N NZ    . LYS B 2 494 ? 32.80400  92.16000  38.35600 1.000 123.23252 ? 494 LYS A NZ    1 
ATOM 4104 N N     . GLN B 2 495 ? 28.86800  93.08000  41.37000 1.000 94.70408  ? 495 GLN A N     1 
ATOM 4105 C CA    . GLN B 2 495 ? 28.42900  94.23300  40.54700 1.000 91.78900  ? 495 GLN A CA    1 
ATOM 4106 C C     . GLN B 2 495 ? 28.08400  95.40600  41.47500 1.000 99.91973  ? 495 GLN A C     1 
ATOM 4107 O O     . GLN B 2 495 ? 28.51600  96.53400  41.19000 1.000 103.82943 ? 495 GLN A O     1 
ATOM 4108 C CB    . GLN B 2 495 ? 27.24900  93.80100  39.67800 1.000 98.60466  ? 495 GLN A CB    1 
ATOM 4109 C CG    . GLN B 2 495 ? 27.62400  92.79100  38.59900 1.000 106.28372 ? 495 GLN A CG    1 
ATOM 4110 C CD    . GLN B 2 495 ? 26.44400  91.99900  38.08100 1.000 118.47145 ? 495 GLN A CD    1 
ATOM 4111 O OE1   . GLN B 2 495 ? 25.30600  92.16600  38.53100 1.000 111.65422 ? 495 GLN A OE1   1 
ATOM 4112 N NE2   . GLN B 2 495 ? 26.70900  91.11600  37.12900 1.000 114.26745 ? 495 GLN A NE2   1 
ATOM 4113 N N     . ARG B 2 496 ? 27.35400  95.13700  42.55700 1.000 99.94597  ? 496 ARG A N     1 
ATOM 4114 C CA    . ARG B 2 496 ? 26.96700  96.21500  43.50100 1.000 101.96394 ? 496 ARG A CA    1 
ATOM 4115 C C     . ARG B 2 496 ? 28.24500  96.87300  44.03700 1.000 102.76585 ? 496 ARG A C     1 
ATOM 4116 O O     . ARG B 2 496 ? 28.27300  98.11600  44.13900 1.000 110.97406 ? 496 ARG A O     1 
ATOM 4117 C CB    . ARG B 2 496 ? 26.11600  95.63400  44.63400 1.000 88.14110  ? 496 ARG A CB    1 
ATOM 4118 C CG    . ARG B 2 496 ? 25.35400  96.65200  45.47000 1.000 104.72563 ? 496 ARG A CG    1 
ATOM 4119 C CD    . ARG B 2 496 ? 26.18400  97.24000  46.59700 1.000 108.23432 ? 496 ARG A CD    1 
ATOM 4120 N NE    . ARG B 2 496 ? 26.61700  96.20500  47.54100 1.000 101.22402 ? 496 ARG A NE    1 
ATOM 4121 C CZ    . ARG B 2 496 ? 26.31200  96.20300  48.83000 1.000 116.84133 ? 496 ARG A CZ    1 
ATOM 4122 N NH1   . ARG B 2 496 ? 25.58100  97.18000  49.33500 1.000 128.30760 ? 496 ARG A NH1   1 
ATOM 4123 N NH2   . ARG B 2 496 ? 26.74000  95.22700  49.60900 1.000 116.72843 ? 496 ARG A NH2   1 
ATOM 4124 N N     . ILE B 2 497 ? 29.25900  96.06900  44.36000 1.000 105.58581 ? 497 ILE A N     1 
ATOM 4125 C CA    . ILE B 2 497 ? 30.52000  96.61000  44.95200 1.000 92.49405  ? 497 ILE A CA    1 
ATOM 4126 C C     . ILE B 2 497 ? 31.33000  97.35100  43.87800 1.000 108.26572 ? 497 ILE A C     1 
ATOM 4127 O O     . ILE B 2 497 ? 31.81200  98.46400  44.17400 1.000 123.92348 ? 497 ILE A O     1 
ATOM 4128 C CB    . ILE B 2 497 ? 31.33900  95.47500  45.59200 1.000 91.60812  ? 497 ILE A CB    1 
ATOM 4129 C CG1   . ILE B 2 497 ? 30.53800  94.74400  46.66600 1.000 108.65220 ? 497 ILE A CG1   1 
ATOM 4130 C CG2   . ILE B 2 497 ? 32.66800  95.99600  46.13700 1.000 95.61003  ? 497 ILE A CG2   1 
ATOM 4131 C CD1   . ILE B 2 497 ? 30.03400  95.64300  47.78000 1.000 106.63543 ? 497 ILE A CD1   1 
ATOM 4132 N N     . LEU B 2 498 ? 31.47000  96.77100  42.68300 1.000 103.29787 ? 498 LEU A N     1 
ATOM 4133 C CA    . LEU B 2 498 ? 32.33400  97.39000  41.64300 1.000 97.50292  ? 498 LEU A CA    1 
ATOM 4134 C C     . LEU B 2 498 ? 31.48500  98.17100  40.62700 1.000 108.07009 ? 498 LEU A C     1 
ATOM 4135 O O     . LEU B 2 498 ? 31.64200  99.40600  40.56200 1.000 129.75051 ? 498 LEU A O     1 
ATOM 4136 C CB    . LEU B 2 498 ? 33.15000  96.28900  40.97200 1.000 91.47200  ? 498 LEU A CB    1 
ATOM 4137 C CG    . LEU B 2 498 ? 33.93500  95.37200  41.91400 1.000 93.15020  ? 498 LEU A CG    1 
ATOM 4138 C CD1   . LEU B 2 498 ? 34.67600  94.30600  41.13000 1.000 92.22073  ? 498 LEU A CD1   1 
ATOM 4139 C CD2   . LEU B 2 498 ? 34.90000  96.18000  42.76100 1.000 92.84692  ? 498 LEU A CD2   1 
ATOM 4140 N N     . GLU B 2 499 ? 30.61700  97.48600  39.87700 1.000 103.41379 ? 499 GLU A N     1 
ATOM 4141 C CA    . GLU B 2 499 ? 29.80300  98.15600  38.82600 1.000 98.48868  ? 499 GLU A CA    1 
ATOM 4142 C C     . GLU B 2 499 ? 28.78000  99.09500  39.48300 1.000 96.63254  ? 499 GLU A C     1 
ATOM 4143 O O     . GLU B 2 499 ? 28.06900  99.80200  38.74200 1.000 106.05015 ? 499 GLU A O     1 
ATOM 4144 C CB    . GLU B 2 499 ? 29.09900  97.13100  37.93700 1.000 112.32291 ? 499 GLU A CB    1 
ATOM 4145 C CG    . GLU B 2 499 ? 30.04800  96.35100  37.03100 1.000 117.07849 ? 499 GLU A CG    1 
ATOM 4146 C CD    . GLU B 2 499 ? 30.59700  95.06100  37.61100 1.000 126.92615 ? 499 GLU A CD    1 
ATOM 4147 O OE1   . GLU B 2 499 ? 31.25800  95.11400  38.66700 1.000 138.64409 ? 499 GLU A OE1   1 
ATOM 4148 O OE2   . GLU B 2 499 ? 30.36500  93.99800  36.99800 1.000 107.24197 ? 499 GLU A OE2   1 
ATOM 4149 N N     . LYS B 2 500 ? 28.69400  99.07900  40.81400 1.000 101.60782 ? 500 LYS A N     1 
ATOM 4150 C CA    . LYS B 2 500 ? 27.77500  99.98900  41.54500 1.000 111.70166 ? 500 LYS A CA    1 
ATOM 4151 C C     . LYS B 2 500 ? 26.34900  99.84000  40.99400 1.000 110.38597 ? 500 LYS A C     1 
ATOM 4152 O O     . LYS B 2 500 ? 25.76700  100.86200 40.57800 1.000 101.52710 ? 500 LYS A O     1 
ATOM 4153 C CB    . LYS B 2 500 ? 28.28100  101.43200 41.45200 1.000 114.86858 ? 500 LYS A CB    1 
ATOM 4154 C CG    . LYS B 2 500 ? 28.14700  102.25200 42.73000 1.000 125.69247 ? 500 LYS A CG    1 
ATOM 4155 C CD    . LYS B 2 500 ? 26.75600  102.82100 42.97700 1.000 124.84128 ? 500 LYS A CD    1 
ATOM 4156 C CE    . LYS B 2 500 ? 26.37500  103.83900 41.94900 1.000 130.15990 ? 500 LYS A CE    1 
ATOM 4157 N NZ    . LYS B 2 500 ? 25.02900  104.36800 42.17800 1.000 145.75103 ? 500 LYS A NZ    1 
ATOM 4158 N N     . LEU B 2 501 ? 25.81300  98.61800  40.98600 1.000 103.18814 ? 501 LEU A N     1 
ATOM 4159 C CA    . LEU B 2 501 ? 24.40300  98.42900  40.56300 1.000 116.32711 ? 501 LEU A CA    1 
ATOM 4160 C C     . LEU B 2 501 ? 23.49700  98.97900  41.67200 1.000 117.65364 ? 501 LEU A C     1 
ATOM 4161 O O     . LEU B 2 501 ? 23.90600  98.92300  42.85000 1.000 116.38456 ? 501 LEU A O     1 
ATOM 4162 C CB    . LEU B 2 501 ? 24.10500  96.95900  40.28300 1.000 99.51886  ? 501 LEU A CB    1 
ATOM 4163 C CG    . LEU B 2 501 ? 24.72600  96.38300  39.00900 1.000 128.78769 ? 501 LEU A CG    1 
ATOM 4164 C CD1   . LEU B 2 501 ? 23.99300  95.11600  38.60800 1.000 100.62421 ? 501 LEU A CD1   1 
ATOM 4165 C CD2   . LEU B 2 501 ? 24.68800  97.40300  37.88500 1.000 134.57586 ? 501 LEU A CD2   1 
ATOM 4166 N N     . ASP B 2 502 ? 22.31900  99.48500  41.30500 1.000 103.08695 ? 502 ASP A N     1 
ATOM 4167 C CA    . ASP B 2 502 ? 21.36600  100.01800 42.31600 1.000 96.24173  ? 502 ASP A CA    1 
ATOM 4168 C C     . ASP B 2 502 ? 20.60500  98.84100  42.93100 1.000 121.61873 ? 502 ASP A C     1 
ATOM 4169 O O     . ASP B 2 502 ? 19.37800  98.75000  42.71700 1.000 126.50047 ? 502 ASP A O     1 
ATOM 4170 C CB    . ASP B 2 502 ? 20.44900  101.06900 41.71100 1.000 98.97720  ? 502 ASP A CB    1 
ATOM 4171 C CG    . ASP B 2 502 ? 19.68000  101.92200 42.70900 1.000 116.28458 ? 502 ASP A CG    1 
ATOM 4172 O OD1   . ASP B 2 502 ? 19.86500  101.71300 43.92600 1.000 111.36765 ? 502 ASP A OD1   1 
ATOM 4173 O OD2   . ASP B 2 502 ? 18.90100  102.78900 42.26100 1.000 121.29738 ? 502 ASP A OD2   1 
ATOM 4174 N N     . ILE B 2 503 ? 21.31100  97.97200  43.66100 1.000 120.75091 ? 503 ILE A N     1 
ATOM 4175 C CA    . ILE B 2 503 ? 20.66400  96.79000  44.30600 1.000 103.19276 ? 503 ILE A CA    1 
ATOM 4176 C C     . ILE B 2 503 ? 21.02500  96.79100  45.80000 1.000 102.27400 ? 503 ILE A C     1 
ATOM 4177 O O     . ILE B 2 503 ? 22.15400  97.20100  46.13900 1.000 91.52174  ? 503 ILE A O     1 
ATOM 4178 C CB    . ILE B 2 503 ? 21.07900  95.48300  43.60300 1.000 99.76858  ? 503 ILE A CB    1 
ATOM 4179 C CG1   . ILE B 2 503 ? 20.27800  94.28600  44.11400 1.000 109.87757 ? 503 ILE A CG1   1 
ATOM 4180 C CG2   . ILE B 2 503 ? 22.58500  95.24500  43.71200 1.000 108.08009 ? 503 ILE A CG2   1 
ATOM 4181 C CD1   . ILE B 2 503 ? 18.79300  94.37000  43.81500 1.000 117.62575 ? 503 ILE A CD1   1 
ATOM 4182 N N     . ALA B 2 504 ? 20.09100  96.36700  46.65300 1.000 108.11802 ? 504 ALA A N     1 
ATOM 4183 C CA    . ALA B 2 504 ? 20.33800  96.33200  48.11200 1.000 90.45951  ? 504 ALA A CA    1 
ATOM 4184 C C     . ALA B 2 504 ? 21.40700  95.28400  48.42000 1.000 104.39870 ? 504 ALA A C     1 
ATOM 4185 O O     . ALA B 2 504 ? 21.58700  94.34600  47.61800 1.000 104.15082 ? 504 ALA A O     1 
ATOM 4186 C CB    . ALA B 2 504 ? 19.04700  96.03300  48.83400 1.000 100.21030 ? 504 ALA A CB    1 
ATOM 4187 N N     . PRO B 2 505 ? 22.13400  95.39500  49.55100 1.000 111.40310 ? 505 PRO A N     1 
ATOM 4188 C CA    . PRO B 2 505 ? 23.19700  94.45300  49.86000 1.000 108.99169 ? 505 PRO A CA    1 
ATOM 4189 C C     . PRO B 2 505 ? 22.70100  93.01800  49.81600 1.000 100.04064 ? 505 PRO A C     1 
ATOM 4190 O O     . PRO B 2 505 ? 21.59700  92.73800  50.32300 1.000 113.90068 ? 505 PRO A O     1 
ATOM 4191 C CB    . PRO B 2 505 ? 23.64200  94.86800  51.27000 1.000 115.74589 ? 505 PRO A CB    1 
ATOM 4192 C CG    . PRO B 2 505 ? 22.50800  95.72400  51.78600 1.000 120.70105 ? 505 PRO A CG    1 
ATOM 4193 C CD    . PRO B 2 505 ? 21.97200  96.42900  50.55600 1.000 96.49534  ? 505 PRO A CD    1 
ATOM 4194 N N     . ILE B 2 506 ? 23.49600  92.12700  49.22200 1.000 96.47428  ? 506 ILE A N     1 
ATOM 4195 C CA    . ILE B 2 506 ? 23.12300  90.68200  49.16400 1.000 97.31356  ? 506 ILE A CA    1 
ATOM 4196 C C     . ILE B 2 506 ? 24.15600  89.88600  49.97600 1.000 87.66768  ? 506 ILE A C     1 
ATOM 4197 O O     . ILE B 2 506 ? 25.32400  89.82900  49.54400 1.000 96.29937  ? 506 ILE A O     1 
ATOM 4198 C CB    . ILE B 2 506 ? 23.05400  90.19900  47.70500 1.000 101.85502 ? 506 ILE A CB    1 
ATOM 4199 C CG1   . ILE B 2 506 ? 22.27700  91.17000  46.81800 1.000 86.93754  ? 506 ILE A CG1   1 
ATOM 4200 C CG2   . ILE B 2 506 ? 22.47700  88.78700  47.63100 1.000 80.35553  ? 506 ILE A CG2   1 
ATOM 4201 C CD1   . ILE B 2 506 ? 20.78200  91.18500  47.08100 1.000 107.23374 ? 506 ILE A CD1   1 
ATOM 4202 N N     . ASP B 2 507 ? 23.73800  89.28900  51.09500 1.000 88.57621  ? 507 ASP A N     1 
ATOM 4203 C CA    . ASP B 2 507 ? 24.69400  88.55700  51.97100 1.000 94.13812  ? 507 ASP A CA    1 
ATOM 4204 C C     . ASP B 2 507 ? 24.95200  87.17000  51.38000 1.000 98.56563  ? 507 ASP A C     1 
ATOM 4205 O O     . ASP B 2 507 ? 24.32300  86.19900  51.84500 1.000 104.97384 ? 507 ASP A O     1 
ATOM 4206 C CB    . ASP B 2 507 ? 24.19600  88.48400  53.40400 1.000 82.74646  ? 507 ASP A CB    1 
ATOM 4207 C CG    . ASP B 2 507 ? 25.19000  87.93600  54.41700 1.000 97.61723  ? 507 ASP A CG    1 
ATOM 4208 O OD1   . ASP B 2 507 ? 26.32800  87.61800  54.01300 1.000 100.03464 ? 507 ASP A OD1   1 
ATOM 4209 O OD2   . ASP B 2 507 ? 24.81700  87.82700  55.60300 1.000 122.62302 ? 507 ASP A OD2   1 
ATOM 4210 N N     . ILE B 2 508 ? 25.85100  87.08600  50.39800 1.000 92.07821  ? 508 ILE A N     1 
ATOM 4211 C CA    . ILE B 2 508 ? 26.19500  85.76900  49.78900 1.000 84.19300  ? 508 ILE A CA    1 
ATOM 4212 C C     . ILE B 2 508 ? 26.79400  84.87300  50.88500 1.000 91.17715  ? 508 ILE A C     1 
ATOM 4213 O O     . ILE B 2 508 ? 26.48600  83.66500  50.89500 1.000 100.35056 ? 508 ILE A O     1 
ATOM 4214 C CB    . ILE B 2 508 ? 27.15000  85.94900  48.59700 1.000 78.01692  ? 508 ILE A CB    1 
ATOM 4215 C CG1   . ILE B 2 508 ? 27.55314  84.60455  47.99392 1.000 78.86004  ? 508 ILE A CG1   1 
ATOM 4216 C CG2   . ILE B 2 508 ? 28.36834  86.78323  48.98913 1.000 94.85572  ? 508 ILE A CG2   1 
ATOM 4217 C CD1   . ILE B 2 508 ? 28.38491  84.72051  46.73108 1.000 111.94918 ? 508 ILE A CD1   1 
ATOM 4218 N N     . PHE B 2 509 ? 27.59700  85.45100  51.78100 1.000 90.53863  ? 509 PHE A N     1 
ATOM 4219 C CA    . PHE B 2 509 ? 28.23200  84.66200  52.86800 1.000 88.41124  ? 509 PHE A CA    1 
ATOM 4220 C C     . PHE B 2 509 ? 27.14000  83.95600  53.64200 1.000 108.09942 ? 509 PHE A C     1 
ATOM 4221 O O     . PHE B 2 509 ? 27.18600  82.71500  53.78500 1.000 122.16169 ? 509 PHE A O     1 
ATOM 4222 C CB    . PHE B 2 509 ? 29.00200  85.64200  53.75600 1.000 101.60582 ? 509 PHE A CB    1 
ATOM 4223 C CG    . PHE B 2 509 ? 29.87900  85.05900  54.85700 1.000 117.60784 ? 509 PHE A CG    1 
ATOM 4224 C CD1   . PHE B 2 509 ? 29.57200  83.84900  55.46900 1.000 93.34449  ? 509 PHE A CD1   1 
ATOM 4225 C CD2   . PHE B 2 509 ? 31.01000  85.74100  55.29100 1.000 151.03279 ? 509 PHE A CD2   1 
ATOM 4226 C CE1   . PHE B 2 509 ? 30.37500  83.33500  56.47300 1.000 96.73337  ? 509 PHE A CE1   1 
ATOM 4227 C CE2   . PHE B 2 509 ? 31.81100  85.22300  56.29700 1.000 164.05552 ? 509 PHE A CE2   1 
ATOM 4228 C CZ    . PHE B 2 509 ? 31.49200  84.02200  56.88500 1.000 140.18538 ? 509 PHE A CZ    1 
ATOM 4229 N N     . GLY B 2 510 ? 26.15700  84.72200  54.11600 1.000 94.69047  ? 510 GLY A N     1 
ATOM 4230 C CA    . GLY B 2 510 ? 25.07600  84.13300  54.92400 1.000 85.62370  ? 510 GLY A CA    1 
ATOM 4231 C C     . GLY B 2 510 ? 24.34300  83.06700  54.14100 1.000 85.61336  ? 510 GLY A C     1 
ATOM 4232 O O     . GLY B 2 510 ? 24.11400  81.98200  54.70200 1.000 107.42610 ? 510 GLY A O     1 
ATOM 4233 N N     . LEU B 2 511 ? 24.00800  83.35400  52.88300 1.000 81.41844  ? 511 LEU A N     1 
ATOM 4234 C CA    . LEU B 2 511 ? 23.23900  82.38900  52.05900 1.000 86.93195  ? 511 LEU A CA    1 
ATOM 4235 C C     . LEU B 2 511 ? 24.01400  81.06900  51.98500 1.000 81.32288  ? 511 LEU A C     1 
ATOM 4236 O O     . LEU B 2 511 ? 23.40000  80.01100  52.20500 1.000 93.14671  ? 511 LEU A O     1 
ATOM 4237 C CB    . LEU B 2 511 ? 23.01200  82.98800  50.67400 1.000 75.32357  ? 511 LEU A CB    1 
ATOM 4238 C CG    . LEU B 2 511 ? 22.40700  82.05800  49.61800 1.000 82.64044  ? 511 LEU A CG    1 
ATOM 4239 C CD1   . LEU B 2 511 ? 21.02500  81.59400  50.03200 1.000 87.99522  ? 511 LEU A CD1   1 
ATOM 4240 C CD2   . LEU B 2 511 ? 22.34900  82.77200  48.28000 1.000 82.04299  ? 511 LEU A CD2   1 
ATOM 4241 N N     . LYS B 2 512 ? 25.31600  81.13700  51.70900 1.000 86.89243  ? 512 LYS A N     1 
ATOM 4242 C CA    . LYS B 2 512 ? 26.11500  79.89600  51.55200 1.000 88.44275  ? 512 LYS A CA    1 
ATOM 4243 C C     . LYS B 2 512 ? 26.06300  79.10800  52.86600 1.000 80.39492  ? 512 LYS A C     1 
ATOM 4244 O O     . LYS B 2 512 ? 25.76600  77.89500  52.82300 1.000 96.36765  ? 512 LYS A O     1 
ATOM 4245 C CB    . LYS B 2 512 ? 27.55800  80.23500  51.16500 1.000 89.28390  ? 512 LYS A CB    1 
ATOM 4246 C CG    . LYS B 2 512 ? 28.45500  79.03100  50.92600 1.000 95.11015  ? 512 LYS A CG    1 
ATOM 4247 C CD    . LYS B 2 512 ? 29.86000  79.40000  50.46600 1.000 100.25510 ? 512 LYS A CD    1 
ATOM 4248 C CE    . LYS B 2 512 ? 30.73400  78.19700  50.31000 1.000 112.86797 ? 512 LYS A CE    1 
ATOM 4249 N NZ    . LYS B 2 512 ? 32.08500  78.55400  49.87300 1.000 115.45910 ? 512 LYS A NZ    1 
ATOM 4250 N N     . ALA B 2 513 ? 26.32300  79.78200  53.98600 1.000 79.22806  ? 513 ALA A N     1 
ATOM 4251 C CA    . ALA B 2 513 ? 26.31300  79.10000  55.29900 1.000 77.49031  ? 513 ALA A CA    1 
ATOM 4252 C C     . ALA B 2 513 ? 24.90600  78.57500  55.57000 1.000 92.15719  ? 513 ALA A C     1 
ATOM 4253 O O     . ALA B 2 513 ? 24.76600  77.44600  56.08300 1.000 111.60195 ? 513 ALA A O     1 
ATOM 4254 C CB    . ALA B 2 513 ? 26.76000  80.05600  56.37400 1.000 78.89606  ? 513 ALA A CB    1 
ATOM 4255 N N     . SER B 2 514 ? 23.89400  79.37000  55.22100 1.000 80.22903  ? 514 SER A N     1 
ATOM 4256 C CA    . SER B 2 514 ? 22.48700  78.96000  55.45200 1.000 97.24906  ? 514 SER A CA    1 
ATOM 4257 C C     . SER B 2 514 ? 22.18400  77.68400  54.65800 1.000 103.00479 ? 514 SER A C     1 
ATOM 4258 O O     . SER B 2 514 ? 21.61500  76.74600  55.24800 1.000 94.80463  ? 514 SER A O     1 
ATOM 4259 C CB    . SER B 2 514 ? 21.54100  80.06500  55.08600 1.000 72.20516  ? 514 SER A CB    1 
ATOM 4260 O OG    . SER B 2 514 ? 20.19400  79.64500  55.24400 1.000 125.24250 ? 514 SER A OG    1 
ATOM 4261 N N     . MET B 2 515 ? 22.56200  77.64700  53.37900 1.000 77.88038  ? 515 MET A N     1 
ATOM 4262 C CA    . MET B 2 515 ? 22.24000  76.47000  52.53100 1.000 80.95968  ? 515 MET A CA    1 
ATOM 4263 C C     . MET B 2 515 ? 22.98000  75.24200  53.08000 1.000 74.13061  ? 515 MET A C     1 
ATOM 4264 O O     . MET B 2 515 ? 22.40300  74.13700  53.04500 1.000 72.51505  ? 515 MET A O     1 
ATOM 4265 C CB    . MET B 2 515 ? 22.62900  76.71100  51.06900 1.000 65.75555  ? 515 MET A CB    1 
ATOM 4266 C CG    . MET B 2 515 ? 21.86900  77.84000  50.40500 1.000 72.26682  ? 515 MET A CG    1 
ATOM 4267 S SD    . MET B 2 515 ? 20.08400  77.67000  50.58900 1.000 67.95739  ? 515 MET A SD    1 
ATOM 4268 C CE    . MET B 2 515 ? 19.85200  76.00300  49.95800 1.000 80.45163  ? 515 MET A CE    1 
ATOM 4269 N N     . ASN B 2 516 ? 24.20400  75.43600  53.57200 1.000 77.11101  ? 516 ASN A N     1 
ATOM 4270 C CA    . ASN B 2 516 ? 24.97000  74.30800  54.16500 1.000 85.51729  ? 516 ASN A CA    1 
ATOM 4271 C C     . ASN B 2 516 ? 24.21400  73.78000  55.38500 1.000 84.50680  ? 516 ASN A C     1 
ATOM 4272 O O     . ASN B 2 516 ? 24.09800  72.54600  55.52900 1.000 85.87529  ? 516 ASN A O     1 
ATOM 4273 C CB    . ASN B 2 516 ? 26.38800  74.71700  54.53800 1.000 88.84927  ? 516 ASN A CB    1 
ATOM 4274 C CG    . ASN B 2 516 ? 27.15600  73.57600  55.16000 1.000 107.73299 ? 516 ASN A CG    1 
ATOM 4275 O OD1   . ASN B 2 516 ? 27.58600  73.67100  56.31500 1.000 106.32719 ? 516 ASN A OD1   1 
ATOM 4276 N ND2   . ASN B 2 516 ? 27.32800  72.49100  54.42100 1.000 127.09059 ? 516 ASN A ND2   1 
ATOM 4277 N N     . GLU B 2 517 ? 23.71300  74.68700  56.22500 1.000 74.09835  ? 517 GLU A N     1 
ATOM 4278 C CA    . GLU B 2 517 ? 22.95500  74.27000  57.43100 1.000 82.06075  ? 517 GLU A CA    1 
ATOM 4279 C C     . GLU B 2 517 ? 21.71700  73.48100  56.98400 1.000 79.55322  ? 517 GLU A C     1 
ATOM 4280 O O     . GLU B 2 517 ? 21.46800  72.40200  57.55100 1.000 75.97788  ? 517 GLU A O     1 
ATOM 4281 C CB    . GLU B 2 517 ? 22.58700  75.49700  58.26200 1.000 72.29623  ? 517 GLU A CB    1 
ATOM 4282 C CG    . GLU B 2 517 ? 21.82300  75.15500  59.53700 1.000 110.23599 ? 517 GLU A CG    1 
ATOM 4283 C CD    . GLU B 2 517 ? 21.75000  76.30000  60.53100 1.000 118.62697 ? 517 GLU A CD    1 
ATOM 4284 O OE1   . GLU B 2 517 ? 22.32800  77.36800  60.24400 1.000 107.93668 ? 517 GLU A OE1   1 
ATOM 4285 O OE2   . GLU B 2 517 ? 21.11600  76.12300  61.59100 1.000 127.47128 ? 517 GLU A OE2   1 
ATOM 4286 N N     . ILE B 2 518 ? 20.99800  73.98700  55.98200 1.000 80.95731  ? 518 ILE A N     1 
ATOM 4287 C CA    . ILE B 2 518 ? 19.76300  73.30700  55.49300 1.000 63.59673  ? 518 ILE A CA    1 
ATOM 4288 C C     . ILE B 2 518 ? 20.13100  71.87900  55.06800 1.000 67.75834  ? 518 ILE A C     1 
ATOM 4289 O O     . ILE B 2 518 ? 19.36000  70.95000  55.37600 1.000 78.91956  ? 518 ILE A O     1 
ATOM 4290 C CB    . ILE B 2 518 ? 19.13100  74.11000  54.34200 1.000 71.91813  ? 518 ILE A CB    1 
ATOM 4291 C CG1   . ILE B 2 518 ? 18.68900  75.49400  54.80900 1.000 74.89799  ? 518 ILE A CG1   1 
ATOM 4292 C CG2   . ILE B 2 518 ? 17.98000  73.33800  53.69800 1.000 70.71656  ? 518 ILE A CG2   1 
ATOM 4293 C CD1   . ILE B 2 518 ? 18.24900  76.41800  53.68900 1.000 69.88201  ? 518 ILE A CD1   1 
ATOM 4294 N N     . HIS B 2 519 ? 21.27500  71.71500  54.40500 1.000 82.63251  ? 519 HIS A N     1 
ATOM 4295 C CA    . HIS B 2 519 ? 21.70800  70.37000  53.94400 1.000 75.10987  ? 519 HIS A CA    1 
ATOM 4296 C C     . HIS B 2 519 ? 21.85800  69.45200  55.15800 1.000 75.39298  ? 519 HIS A C     1 
ATOM 4297 O O     . HIS B 2 519 ? 21.36500  68.30900  55.12000 1.000 78.06123  ? 519 HIS A O     1 
ATOM 4298 C CB    . HIS B 2 519 ? 23.01400  70.46400  53.15000 1.000 70.00972  ? 519 HIS A CB    1 
ATOM 4299 C CG    . HIS B 2 519 ? 23.57200  69.14400  52.74200 1.000 76.38884  ? 519 HIS A CG    1 
ATOM 4300 N ND1   . HIS B 2 519 ? 24.47200  68.44300  53.51400 1.000 81.86868  ? 519 HIS A ND1   1 
ATOM 4301 C CD2   . HIS B 2 519 ? 23.36400  68.40200  51.64900 1.000 82.11601  ? 519 HIS A CD2   1 
ATOM 4302 C CE1   . HIS B 2 519 ? 24.78800  67.31300  52.89800 1.000 92.55452  ? 519 HIS A CE1   1 
ATOM 4303 N NE2   . HIS B 2 519 ? 24.12600  67.26800  51.76300 1.000 92.40495  ? 519 HIS A NE2   1 
ATOM 4304 N N     . GLU B 2 520 ? 22.51900  69.94300  56.20700 1.000 64.87709  ? 520 GLU A N     1 
ATOM 4305 C CA    . GLU B 2 520 ? 22.75000  69.10400  57.41000 1.000 73.35824  ? 520 GLU A CA    1 
ATOM 4306 C C     . GLU B 2 520 ? 21.39800  68.78700  58.06500 1.000 82.89722  ? 520 GLU A C     1 
ATOM 4307 O O     . GLU B 2 520 ? 21.21600  67.64300  58.52700 1.000 94.73198  ? 520 GLU A O     1 
ATOM 4308 C CB    . GLU B 2 520 ? 23.70000  69.79700  58.38500 1.000 72.57794  ? 520 GLU A CB    1 
ATOM 4309 C CG    . GLU B 2 520 ? 24.16600  68.88500  59.51600 1.000 113.03414 ? 520 GLU A CG    1 
ATOM 4310 C CD    . GLU B 2 520 ? 25.09600  67.75600  59.10500 1.000 131.24958 ? 520 GLU A CD    1 
ATOM 4311 O OE1   . GLU B 2 520 ? 25.46800  67.67900  57.91500 1.000 105.83674 ? 520 GLU A OE1   1 
ATOM 4312 O OE2   . GLU B 2 520 ? 25.44400  66.94100  59.98400 1.000 142.14696 ? 520 GLU A OE2   1 
ATOM 4313 N N     . LEU B 2 521 ? 20.48700  69.76100  58.09200 1.000 68.62199  ? 521 LEU A N     1 
ATOM 4314 C CA    . LEU B 2 521 ? 19.13700  69.52400  58.66200 1.000 62.51576  ? 521 LEU A CA    1 
ATOM 4315 C C     . LEU B 2 521 ? 18.45100  68.41000  57.85700 1.000 66.34765  ? 521 LEU A C     1 
ATOM 4316 O O     . LEU B 2 521 ? 17.79000  67.55300  58.47600 1.000 74.18775  ? 521 LEU A O     1 
ATOM 4317 C CB    . LEU B 2 521 ? 18.32900  70.81900  58.63600 1.000 69.66778  ? 521 LEU A CB    1 
ATOM 4318 C CG    . LEU B 2 521 ? 18.92900  72.00400  59.39800 1.000 61.18530  ? 521 LEU A CG    1 
ATOM 4319 C CD1   . LEU B 2 521 ? 18.08800  73.25000  59.19900 1.000 66.54900  ? 521 LEU A CD1   1 
ATOM 4320 C CD2   . LEU B 2 521 ? 19.07100  71.68500  60.87400 1.000 59.85889  ? 521 LEU A CD2   1 
ATOM 4321 N N     . ASN B 2 522 ? 18.61300  68.42200  56.53300 1.000 58.28701  ? 522 ASN A N     1 
ATOM 4322 C CA    . ASN B 2 522 ? 18.00500  67.37200  55.67200 1.000 58.78937  ? 522 ASN A CA    1 
ATOM 4323 C C     . ASN B 2 522 ? 18.61200  66.01700  56.03400 1.000 59.89177  ? 522 ASN A C     1 
ATOM 4324 O O     . ASN B 2 522 ? 17.85500  65.03400  56.15000 1.000 68.60677  ? 522 ASN A O     1 
ATOM 4325 C CB    . ASN B 2 522 ? 18.19300  67.67300  54.19100 1.000 58.41672  ? 522 ASN A CB    1 
ATOM 4326 C CG    . ASN B 2 522 ? 17.39700  66.73600  53.31800 1.000 56.55893  ? 522 ASN A CG    1 
ATOM 4327 O OD1   . ASN B 2 522 ? 16.16400  66.71300  53.39600 1.000 65.44566  ? 522 ASN A OD1   1 
ATOM 4328 N ND2   . ASN B 2 522 ? 18.07400  65.96500  52.48100 1.000 90.68185  ? 522 ASN A ND2   1 
ATOM 4329 N N     . GLU B 2 523 ? 19.93100  65.97500  56.21100 1.000 59.83277  ? 523 GLU A N     1 
ATOM 4330 C CA    . GLU B 2 523 ? 20.60600  64.70200  56.56200 1.000 72.60958  ? 523 GLU A CA    1 
ATOM 4331 C C     . GLU B 2 523 ? 20.03500  64.20500  57.89400 1.000 65.14855  ? 523 GLU A C     1 
ATOM 4332 O O     . GLU B 2 523 ? 19.76400  62.99600  58.00600 1.000 79.08275  ? 523 GLU A O     1 
ATOM 4333 C CB    . GLU B 2 523 ? 22.11800  64.89600  56.65500 1.000 81.72738  ? 523 GLU A CB    1 
ATOM 4334 C CG    . GLU B 2 523 ? 22.74000  65.43400  55.37100 1.000 77.28249  ? 523 GLU A CG    1 
ATOM 4335 C CD    . GLU B 2 523 ? 22.42900  64.61300  54.13500 1.000 80.49548  ? 523 GLU A CD    1 
ATOM 4336 O OE1   . GLU B 2 523 ? 22.77200  63.41200  54.11700 1.000 81.78325  ? 523 GLU A OE1   1 
ATOM 4337 O OE2   . GLU B 2 523 ? 21.84600  65.17600  53.18600 1.000 87.32250  ? 523 GLU A OE2   1 
ATOM 4338 N N     . GLN B 2 524 ? 19.84200  65.11400  58.85000 1.000 63.43621  ? 524 GLN A N     1 
ATOM 4339 C CA    . GLN B 2 524 ? 19.29000  64.73100  60.17300 1.000 71.43841  ? 524 GLN A CA    1 
ATOM 4340 C C     . GLN B 2 524 ? 17.89900  64.11300  59.98100 1.000 67.67679  ? 524 GLN A C     1 
ATOM 4341 O O     . GLN B 2 524 ? 17.62100  63.07300  60.60900 1.000 64.30505  ? 524 GLN A O     1 
ATOM 4342 C CB    . GLN B 2 524 ? 19.20200  65.95700  61.08000 1.000 71.33604  ? 524 GLN A CB    1 
ATOM 4343 C CG    . GLN B 2 524 ? 19.06200  65.62200  62.56100 1.000 91.01479  ? 524 GLN A CG    1 
ATOM 4344 C CD    . GLN B 2 524 ? 20.27200  64.90500  63.11800 1.000 109.36894 ? 524 GLN A CD    1 
ATOM 4345 O OE1   . GLN B 2 524 ? 21.39500  65.42100  63.09700 1.000 138.71654 ? 524 GLN A OE1   1 
ATOM 4346 N NE2   . GLN B 2 524 ? 20.05300  63.69900  63.62100 1.000 90.77363  ? 524 GLN A NE2   1 
ATOM 4347 N N     . LEU B 2 525 ? 17.06700  64.72700  59.13900 1.000 65.39240  ? 525 LEU A N     1 
ATOM 4348 C CA    . LEU B 2 525 ? 15.68800  64.22300  58.92600 1.000 58.75057  ? 525 LEU A CA    1 
ATOM 4349 C C     . LEU B 2 525 ? 15.75900  62.77500  58.43300 1.000 69.25139  ? 525 LEU A C     1 
ATOM 4350 O O     . LEU B 2 525 ? 15.09400  61.91100  59.03600 1.000 73.52018  ? 525 LEU A O     1 
ATOM 4351 C CB    . LEU B 2 525 ? 14.96600  65.11600  57.92000 1.000 51.94592  ? 525 LEU A CB    1 
ATOM 4352 C CG    . LEU B 2 525 ? 13.57500  64.65000  57.48200 1.000 58.82880  ? 525 LEU A CG    1 
ATOM 4353 C CD1   . LEU B 2 525 ? 12.60900  64.66200  58.65200 1.000 67.52908  ? 525 LEU A CD1   1 
ATOM 4354 C CD2   . LEU B 2 525 ? 13.06200  65.52200  56.35300 1.000 63.43784  ? 525 LEU A CD2   1 
ATOM 4355 N N     . PHE B 2 526 ? 16.55500  62.52100  57.39600 1.000 66.21822  ? 526 PHE A N     1 
ATOM 4356 C CA    . PHE B 2 526 ? 16.59800  61.15500  56.80600 1.000 70.06567  ? 526 PHE A CA    1 
ATOM 4357 C C     . PHE B 2 526 ? 17.34000  60.21800  57.75600 1.000 60.71031  ? 526 PHE A C     1 
ATOM 4358 O O     . PHE B 2 526 ? 17.02500  59.01200  57.77800 1.000 86.28618  ? 526 PHE A O     1 
ATOM 4359 C CB    . PHE B 2 526 ? 17.15800  61.27000  55.38600 1.000 55.86500  ? 526 PHE A CB    1 
ATOM 4360 C CG    . PHE B 2 526 ? 16.13600  61.83100  54.40700 1.000 63.10635  ? 526 PHE A CG    1 
ATOM 4361 C CD1   . PHE B 2 526 ? 15.26100  60.99000  53.73300 1.000 75.34015  ? 526 PHE A CD1   1 
ATOM 4362 C CD2   . PHE B 2 526 ? 16.03800  63.19800  54.18000 1.000 68.28216  ? 526 PHE A CD2   1 
ATOM 4363 C CE1   . PHE B 2 526 ? 14.32400  61.50100  52.85100 1.000 80.37075  ? 526 PHE A CE1   1 
ATOM 4364 C CE2   . PHE B 2 526 ? 15.10000  63.70300  53.29500 1.000 66.65823  ? 526 PHE A CE2   1 
ATOM 4365 C CZ    . PHE B 2 526 ? 14.24600  62.85500  52.63400 1.000 74.87971  ? 526 PHE A CZ    1 
ATOM 4366 N N     . SER B 2 527 ? 18.28600  60.74800  58.53100 1.000 67.03147  ? 527 SER A N     1 
ATOM 4367 C CA    . SER B 2 527 ? 18.97000  59.90300  59.54300 1.000 69.24267  ? 527 SER A CA    1 
ATOM 4368 C C     . SER B 2 527 ? 17.93800  59.46400  60.58800 1.000 67.13172  ? 527 SER A C     1 
ATOM 4369 O O     . SER B 2 527 ? 17.95900  58.28100  60.98200 1.000 81.28221  ? 527 SER A O     1 
ATOM 4370 C CB    . SER B 2 527 ? 20.11500  60.63200  60.18700 1.000 62.68553  ? 527 SER A CB    1 
ATOM 4371 O OG    . SER B 2 527 ? 21.03500  61.10200  59.21200 1.000 81.95173  ? 527 SER A OG    1 
ATOM 4372 N N     . THR B 2 528 ? 17.06800  60.38400  61.00400 1.000 69.36658  ? 528 THR A N     1 
ATOM 4373 C CA    . THR B 2 528 ? 16.02900  60.05400  61.99800 1.000 76.93224  ? 528 THR A CA    1 
ATOM 4374 C C     . THR B 2 528 ? 15.15100  58.96900  61.42700 1.000 66.86685  ? 528 THR A C     1 
ATOM 4375 O O     . THR B 2 528 ? 14.90800  57.97200  62.13100 1.000 73.83121  ? 528 THR A O     1 
ATOM 4376 C CB    . THR B 2 528 ? 15.22800  61.31100  62.32700 1.000 61.21960  ? 528 THR A CB    1 
ATOM 4377 O OG1   . THR B 2 528 ? 16.17200  62.22900  62.86900 1.000 69.65295  ? 528 THR A OG1   1 
ATOM 4378 C CG2   . THR B 2 528 ? 14.12300  61.05000  63.33300 1.000 86.68451  ? 528 THR A CG2   1 
ATOM 4379 N N     . ILE B 2 529 ? 14.71100  59.13700  60.18100 1.000 66.09899  ? 529 ILE A N     1 
ATOM 4380 C CA    . ILE B 2 529 ? 13.79700  58.14100  59.55000 1.000 68.52914  ? 529 ILE A CA    1 
ATOM 4381 C C     . ILE B 2 529 ? 14.52500  56.79100  59.47600 1.000 74.06723  ? 529 ILE A C     1 
ATOM 4382 O O     . ILE B 2 529 ? 13.88200  55.76100  59.74800 1.000 78.93815  ? 529 ILE A O     1 
ATOM 4383 C CB    . ILE B 2 529 ? 13.33400  58.62900  58.16700 1.000 56.62804  ? 529 ILE A CB    1 
ATOM 4384 C CG1   . ILE B 2 529 ? 12.65800  59.99300  58.25300 1.000 57.40660  ? 529 ILE A CG1   1 
ATOM 4385 C CG2   . ILE B 2 529 ? 12.42900  57.59800  57.49800 1.000 52.89354  ? 529 ILE A CG2   1 
ATOM 4386 C CD1   . ILE B 2 529 ? 12.19500  60.53700  56.91500 1.000 69.12941  ? 529 ILE A CD1   1 
ATOM 4387 N N     . PHE B 2 530 ? 15.81700  56.80100  59.14100 1.000 70.42712  ? 530 PHE A N     1 
ATOM 4388 C CA    . PHE B 2 530 ? 16.58600  55.53500  58.99900 1.000 68.93066  ? 530 PHE A CA    1 
ATOM 4389 C C     . PHE B 2 530 ? 16.66700  54.84900  60.35700 1.000 72.12089  ? 530 PHE A C     1 
ATOM 4390 O O     . PHE B 2 530 ? 16.49500  53.61700  60.43400 1.000 83.09894  ? 530 PHE A O     1 
ATOM 4391 C CB    . PHE B 2 530 ? 17.96000  55.84700  58.40100 1.000 63.78152  ? 530 PHE A CB    1 
ATOM 4392 C CG    . PHE B 2 530 ? 18.75100  54.64300  57.91000 1.000 72.66566  ? 530 PHE A CG    1 
ATOM 4393 C CD1   . PHE B 2 530 ? 18.50500  54.09000  56.66000 1.000 73.87869  ? 530 PHE A CD1   1 
ATOM 4394 C CD2   . PHE B 2 530 ? 19.76300  54.08900  58.68400 1.000 89.64298  ? 530 PHE A CD2   1 
ATOM 4395 C CE1   . PHE B 2 530 ? 19.23200  53.00100  56.21000 1.000 94.34324  ? 530 PHE A CE1   1 
ATOM 4396 C CE2   . PHE B 2 530 ? 20.48700  52.99900  58.22900 1.000 77.94057  ? 530 PHE A CE2   1 
ATOM 4397 C CZ    . PHE B 2 530 ? 20.22100  52.45900  56.99400 1.000 96.16910  ? 530 PHE A CZ    1 
ATOM 4398 N N     . THR B 2 531 ? 16.91100  55.62900  61.41000 1.000 66.09652  ? 531 THR A N     1 
ATOM 4399 C CA    . THR B 2 531 ? 16.98500  55.06000  62.77100 1.000 70.36282  ? 531 THR A CA    1 
ATOM 4400 C C     . THR B 2 531 ? 15.65000  54.43500  63.10000 1.000 73.25377  ? 531 THR A C     1 
ATOM 4401 O O     . THR B 2 531 ? 15.64000  53.31500  63.64500 1.000 84.46862  ? 531 THR A O     1 
ATOM 4402 C CB    . THR B 2 531 ? 17.35800  56.15700  63.76400 1.000 71.39887  ? 531 THR A CB    1 
ATOM 4403 O OG1   . THR B 2 531 ? 18.55200  56.73500  63.24800 1.000 82.77197  ? 531 THR A OG1   1 
ATOM 4404 C CG2   . THR B 2 531 ? 17.60300  55.61700  65.16100 1.000 71.23493  ? 531 THR A CG2   1 
ATOM 4405 N N     . ILE B 2 532 ? 14.55500  55.11900  62.76500 1.000 72.74732  ? 532 ILE A N     1 
ATOM 4406 C CA    . ILE B 2 532 ? 13.18900  54.57200  63.01200 1.000 65.85495  ? 532 ILE A CA    1 
ATOM 4407 C C     . ILE B 2 532 ? 13.05700  53.24300  62.25500 1.000 75.39773  ? 532 ILE A C     1 
ATOM 4408 O O     . ILE B 2 532 ? 12.58900  52.26200  62.86000 1.000 71.39950  ? 532 ILE A O     1 
ATOM 4409 C CB    . ILE B 2 532 ? 12.12100  55.58700  62.57100 1.000 67.29365  ? 532 ILE A CB    1 
ATOM 4410 C CG1   . ILE B 2 532 ? 12.17700  56.85500  63.41600 1.000 70.94681  ? 532 ILE A CG1   1 
ATOM 4411 C CG2   . ILE B 2 532 ? 10.72800  54.96000  62.58900 1.000 77.93522  ? 532 ILE A CG2   1 
ATOM 4412 C CD1   . ILE B 2 532 ? 11.15200  57.90300  63.02500 1.000 64.07961  ? 532 ILE A CD1   1 
ATOM 4413 N N     . ILE B 2 533 ? 13.48900  53.21300  60.99500 1.000 64.74496  ? 533 ILE A N     1 
ATOM 4414 C CA    . ILE B 2 533 ? 13.36100  51.97900  60.16700 1.000 70.73991  ? 533 ILE A CA    1 
ATOM 4415 C C     . ILE B 2 533 ? 14.05400  50.82300  60.90000 1.000 66.72008  ? 533 ILE A C     1 
ATOM 4416 O O     . ILE B 2 533 ? 13.46100  49.72900  60.96500 1.000 97.98457  ? 533 ILE A O     1 
ATOM 4417 C CB    . ILE B 2 533 ? 13.95700  52.20900  58.76800 1.000 76.01040  ? 533 ILE A CB    1 
ATOM 4418 C CG1   . ILE B 2 533 ? 13.14200  53.22800  57.97800 1.000 71.99367  ? 533 ILE A CG1   1 
ATOM 4419 C CG2   . ILE B 2 533 ? 14.10200  50.89300  58.00500 1.000 74.87852  ? 533 ILE A CG2   1 
ATOM 4420 C CD1   . ILE B 2 533 ? 13.72900  53.56700  56.62100 1.000 62.01675  ? 533 ILE A CD1   1 
ATOM 4421 N N     . ASN B 2 534 ? 15.25100  51.06200  61.43700 1.000 67.22737  ? 534 ASN A N     1 
ATOM 4422 C CA    . ASN B 2 534 ? 16.02100  49.98000  62.11100 1.000 71.35164  ? 534 ASN A CA    1 
ATOM 4423 C C     . ASN B 2 534 ? 15.39300  49.65200  63.46700 1.000 78.01255  ? 534 ASN A C     1 
ATOM 4424 O O     . ASN B 2 534 ? 15.46900  48.47800  63.87800 1.000 94.87328  ? 534 ASN A O     1 
ATOM 4425 C CB    . ASN B 2 534 ? 17.48600  50.36100  62.27700 1.000 68.15063  ? 534 ASN A CB    1 
ATOM 4426 C CG    . ASN B 2 534 ? 18.09800  50.83400  60.98100 1.000 96.58786  ? 534 ASN A CG    1 
ATOM 4427 O OD1   . ASN B 2 534 ? 18.13000  50.08700  59.99700 1.000 102.67838 ? 534 ASN A OD1   1 
ATOM 4428 N ND2   . ASN B 2 534 ? 18.58200  52.06600  60.95900 1.000 105.21162 ? 534 ASN A ND2   1 
ATOM 4429 N N     . ASP B 2 535 ? 14.79400  50.64300  64.13000 1.000 87.98478  ? 535 ASP A N     1 
ATOM 4430 C CA    . ASP B 2 535 ? 14.23600  50.43100  65.49400 1.000 75.14698  ? 535 ASP A CA    1 
ATOM 4431 C C     . ASP B 2 535 ? 12.75800  50.03800  65.41200 1.000 74.31269  ? 535 ASP A C     1 
ATOM 4432 O O     . ASP B 2 535 ? 12.10300  49.98400  66.47300 1.000 75.04254  ? 535 ASP A O     1 
ATOM 4433 C CB    . ASP B 2 535 ? 14.43400  51.66400  66.35900 1.000 73.70300  ? 535 ASP A CB    1 
ATOM 4434 C CG    . ASP B 2 535 ? 15.87800  52.09300  66.56900 1.000 101.71704 ? 535 ASP A CG    1 
ATOM 4435 O OD1   . ASP B 2 535 ? 16.77400  51.41400  66.02700 1.000 120.90250 ? 535 ASP A OD1   1 
ATOM 4436 O OD2   . ASP B 2 535 ? 16.09200  53.10200  67.27200 1.000 107.31822 ? 535 ASP A OD2   1 
ATOM 4437 N N     . SER B 2 536 ? 12.25300  49.77500  64.20500 1.000 69.48722  ? 536 SER A N     1 
ATOM 4438 C CA    . SER B 2 536 ? 10.81600  49.44400  64.03400 1.000 73.14956  ? 536 SER A CA    1 
ATOM 4439 C C     . SER B 2 536 ? 10.66300  48.17000  63.19500 1.000 63.86754  ? 536 SER A C     1 
ATOM 4440 O O     . SER B 2 536 ? 11.68000  47.69100  62.65500 1.000 85.65643  ? 536 SER A O     1 
ATOM 4441 C CB    . SER B 2 536 ? 10.07000  50.59000  63.41600 1.000 68.78652  ? 536 SER A CB    1 
ATOM 4442 O OG    . SER B 2 536 ? 10.24500  51.77600  64.17700 1.000 75.12528  ? 536 SER A OG    1 
ATOM 4443 N N     . ASP B 2 537 ? 9.43900   47.64800  63.10100 1.000 62.71204  ? 537 ASP A N     1 
ATOM 4444 C CA    . ASP B 2 537 ? 9.18300   46.40700  62.32200 1.000 72.74416  ? 537 ASP A CA    1 
ATOM 4445 C C     . ASP B 2 537 ? 9.13700   46.75000  60.83200 1.000 65.36314  ? 537 ASP A C     1 
ATOM 4446 O O     . ASP B 2 537 ? 8.42300   47.70600  60.47000 1.000 80.49920  ? 537 ASP A O     1 
ATOM 4447 C CB    . ASP B 2 537 ? 7.91500   45.71800  62.79400 1.000 74.69226  ? 537 ASP A CB    1 
ATOM 4448 C CG    . ASP B 2 537 ? 7.85700   45.41000  64.28300 1.000 106.67820 ? 537 ASP A CG    1 
ATOM 4449 O OD1   . ASP B 2 537 ? 8.73000   44.65500  64.75900 1.000 116.43307 ? 537 ASP A OD1   1 
ATOM 4450 O OD2   . ASP B 2 537 ? 6.94000   45.92900  64.95300 1.000 97.15910  ? 537 ASP A OD2   1 
ATOM 4451 N N     . VAL B 2 538 ? 9.85900   45.99100  60.00600 1.000 65.20160  ? 538 VAL A N     1 
ATOM 4452 C CA    . VAL B 2 538 ? 9.92500   46.28800  58.54400 1.000 59.92883  ? 538 VAL A CA    1 
ATOM 4453 C C     . VAL B 2 538 ? 9.33600   45.10100  57.76900 1.000 56.55480  ? 538 VAL A C     1 
ATOM 4454 O O     . VAL B 2 538 ? 9.67700   43.94900  58.10300 1.000 71.83240  ? 538 VAL A O     1 
ATOM 4455 C CB    . VAL B 2 538 ? 11.36900  46.59400  58.10700 1.000 59.45859  ? 538 VAL A CB    1 
ATOM 4456 C CG1   . VAL B 2 538 ? 12.33514  45.47810  58.48554 1.000 89.66017  ? 538 VAL A CG1   1 
ATOM 4457 C CG2   . VAL B 2 538 ? 11.46460  46.92354  56.62244 1.000 79.62220  ? 538 VAL A CG2   1 
ATOM 4458 N N     . TYR B 2 539 ? 8.47400   45.37900  56.78900 1.000 70.61918  ? 539 TYR A N     1 
ATOM 4459 C CA    . TYR B 2 539 ? 7.82200   44.29900  56.00300 1.000 73.50061  ? 539 TYR A CA    1 
ATOM 4460 C C     . TYR B 2 539 ? 8.18800   44.47000  54.53300 1.000 75.66882  ? 539 TYR A C     1 
ATOM 4461 O O     . TYR B 2 539 ? 8.00700   45.57600  53.98700 1.000 77.21632  ? 539 TYR A O     1 
ATOM 4462 C CB    . TYR B 2 539 ? 6.31200   44.34900  56.24800 1.000 63.67137  ? 539 TYR A CB    1 
ATOM 4463 C CG    . TYR B 2 539 ? 5.90700   44.36400  57.71500 1.000 62.57813  ? 539 TYR A CG    1 
ATOM 4464 C CD1   . TYR B 2 539 ? 5.71500   43.18200  58.41700 1.000 74.68273  ? 539 TYR A CD1   1 
ATOM 4465 C CD2   . TYR B 2 539 ? 5.71300   45.56000  58.39400 1.000 72.83057  ? 539 TYR A CD2   1 
ATOM 4466 C CE1   . TYR B 2 539 ? 5.34800   43.18800  59.75200 1.000 72.82521  ? 539 TYR A CE1   1 
ATOM 4467 C CE2   . TYR B 2 539 ? 5.34600   45.58000  59.72900 1.000 85.54545  ? 539 TYR A CE2   1 
ATOM 4468 C CZ    . TYR B 2 539 ? 5.16400   44.39000  60.40900 1.000 73.92591  ? 539 TYR A CZ    1 
ATOM 4469 O OH    . TYR B 2 539 ? 4.80000   44.40100  61.72400 1.000 104.89492 ? 539 TYR A OH    1 
ATOM 4470 N N     . ASP B 2 540 ? 8.69100   43.40400  53.90900 1.000 83.96634  ? 540 ASP A N     1 
ATOM 4471 C CA    . ASP B 2 540 ? 9.10600   43.46400  52.48100 1.000 85.37330  ? 540 ASP A CA    1 
ATOM 4472 C C     . ASP B 2 540 ? 7.86400   43.45000  51.58700 1.000 86.35792  ? 540 ASP A C     1 
ATOM 4473 O O     . ASP B 2 540 ? 6.83900   42.88200  52.01100 1.000 112.21435 ? 540 ASP A O     1 
ATOM 4474 C CB    . ASP B 2 540 ? 10.07400  42.33800  52.16100 1.000 88.51803  ? 540 ASP A CB    1 
ATOM 4475 C CG    . ASP B 2 540 ? 10.43200  42.17600  50.69200 1.000 134.36060 ? 540 ASP A CG    1 
ATOM 4476 O OD1   . ASP B 2 540 ? 10.92000  43.15900  50.09700 1.000 120.15433 ? 540 ASP A OD1   1 
ATOM 4477 O OD2   . ASP B 2 540 ? 10.22500  41.06600  50.16200 1.000 138.28895 ? 540 ASP A OD2   1 
ATOM 4478 N N     . ASP B 2 541 ? 7.95000   44.05400  50.39900 1.000 78.80404  ? 541 ASP A N     1 
ATOM 4479 C CA    . ASP B 2 541 ? 6.80600   44.01600  49.44600 1.000 82.42806  ? 541 ASP A CA    1 
ATOM 4480 C C     . ASP B 2 541 ? 6.79500   42.65800  48.73900 1.000 111.20527 ? 541 ASP A C     1 
ATOM 4481 O O     . ASP B 2 541 ? 7.83600   41.97100  48.75900 1.000 106.75308 ? 541 ASP A O     1 
ATOM 4482 C CB    . ASP B 2 541 ? 6.81500   45.19600  48.48700 1.000 84.54266  ? 541 ASP A CB    1 
ATOM 4483 C CG    . ASP B 2 541 ? 8.06000   45.34900  47.62800 1.000 125.09335 ? 541 ASP A CG    1 
ATOM 4484 O OD1   . ASP B 2 541 ? 8.98900   44.53800  47.79500 1.000 125.66393 ? 541 ASP A OD1   1 
ATOM 4485 O OD2   . ASP B 2 541 ? 8.09000   46.28300  46.80000 1.000 136.26189 ? 541 ASP A OD2   1 
ATOM 4486 N N     . ASP B 2 542 ? 5.66600   42.29100  48.13100 1.000 132.65668 ? 542 ASP A N     1 
ATOM 4487 C CA    . ASP B 2 542 ? 5.54000   40.95400  47.48600 1.000 136.35146 ? 542 ASP A CA    1 
ATOM 4488 C C     . ASP B 2 542 ? 6.59600   40.79900  46.38800 1.000 136.66375 ? 542 ASP A C     1 
ATOM 4489 O O     . ASP B 2 542 ? 7.20700   39.71400  46.30700 1.000 135.02154 ? 542 ASP A O     1 
ATOM 4490 C CB    . ASP B 2 542 ? 4.12800   40.73700  46.96400 1.000 126.27332 ? 542 ASP A CB    1 
ATOM 4491 C CG    . ASP B 2 542 ? 3.56200   41.86700  46.11700 1.000 147.17533 ? 542 ASP A CG    1 
ATOM 4492 O OD1   . ASP B 2 542 ? 4.27100   42.88000  45.93600 1.000 147.07551 ? 542 ASP A OD1   1 
ATOM 4493 O OD2   . ASP B 2 542 ? 2.41600   41.72500  45.64200 1.000 130.55033 ? 542 ASP A OD2   1 
ATOM 4494 N N     . ILE B 2 543 ? 6.81000   41.84200  45.58400 1.000 123.57029 ? 543 ILE A N     1 
ATOM 4495 C CA    . ILE B 2 543 ? 7.77200   41.75900  44.44500 1.000 113.65823 ? 543 ILE A CA    1 
ATOM 4496 C C     . ILE B 2 543 ? 9.20000   41.84600  45.00500 1.000 112.76980 ? 543 ILE A C     1 
ATOM 4497 O O     . ILE B 2 543 ? 10.15700  41.74800  44.20900 1.000 122.69908 ? 543 ILE A O     1 
ATOM 4498 C CB    . ILE B 2 543 ? 7.47100   42.86300  43.41400 1.000 117.18880 ? 543 ILE A CB    1 
ATOM 4499 C CG1   . ILE B 2 543 ? 8.19100   42.62400  42.08500 1.000 119.13480 ? 543 ILE A CG1   1 
ATOM 4500 C CG2   . ILE B 2 543 ? 7.77400   44.24600  43.98900 1.000 125.03804 ? 543 ILE A CG2   1 
ATOM 4501 C CD1   . ILE B 2 543 ? 7.88100   41.28200  41.44500 1.000 117.21973 ? 543 ILE A CD1   1 
ATOM 4502 N N     . HIS B 2 544 ? 9.33300   42.01400  46.32300 1.000 110.50892 ? 544 HIS A N     1 
ATOM 4503 C CA    . HIS B 2 544 ? 10.67300  42.09800  46.96700 1.000 128.60887 ? 544 HIS A CA    1 
ATOM 4504 C C     . HIS B 2 544 ? 11.47300  43.22000  46.29600 1.000 128.92809 ? 544 HIS A C     1 
ATOM 4505 O O     . HIS B 2 544 ? 12.68200  43.04100  46.03900 1.000 118.94917 ? 544 HIS A O     1 
ATOM 4506 C CB    . HIS B 2 544 ? 11.37400  40.73500  46.93800 1.000 132.14162 ? 544 HIS A CB    1 
ATOM 4507 C CG    . HIS B 2 544 ? 12.37600  40.54500  48.02800 1.000 147.78966 ? 544 HIS A CG    1 
ATOM 4508 N ND1   . HIS B 2 544 ? 12.60400  39.32200  48.61900 1.000 151.25508 ? 544 HIS A ND1   1 
ATOM 4509 C CD2   . HIS B 2 544 ? 13.18700  41.41200  48.64800 1.000 146.22574 ? 544 HIS A CD2   1 
ATOM 4510 C CE1   . HIS B 2 544 ? 13.53400  39.45500  49.55400 1.000 154.65455 ? 544 HIS A CE1   1 
ATOM 4511 N NE2   . HIS B 2 544 ? 13.90100  40.71700  49.58800 1.000 155.14673 ? 544 HIS A NE2   1 
ATOM 4512 N N     . ARG B 2 545 ? 10.81100  44.34600  46.01400 1.000 117.55868 ? 545 ARG A N     1 
ATOM 4513 C CA    . ARG B 2 545 ? 11.50200  45.51100  45.40500 1.000 107.11757 ? 545 ARG A CA    1 
ATOM 4514 C C     . ARG B 2 545 ? 11.82100  46.52200  46.51000 1.000 92.26918  ? 545 ARG A C     1 
ATOM 4515 O O     . ARG B 2 545 ? 12.96100  47.02800  46.54100 1.000 96.55519  ? 545 ARG A O     1 
ATOM 4516 C CB    . ARG B 2 545 ? 10.59900  46.14400  44.34400 1.000 94.58111  ? 545 ARG A CB    1 
ATOM 4517 C CG    . ARG B 2 545 ? 11.12400  47.41700  43.69800 1.000 116.78001 ? 545 ARG A CG    1 
ATOM 4518 C CD    . ARG B 2 545 ? 10.09900  47.97700  42.72600 1.000 128.18397 ? 545 ARG A CD    1 
ATOM 4519 N NE    . ARG B 2 545 ? 10.51500  49.25700  42.14300 1.000 143.77044 ? 545 ARG A NE    1 
ATOM 4520 C CZ    . ARG B 2 545 ? 9.79100   49.95600  41.27900 1.000 150.89998 ? 545 ARG A CZ    1 
ATOM 4521 N NH1   . ARG B 2 545 ? 8.69700   49.43200  40.75700 1.000 140.36312 ? 545 ARG A NH1   1 
ATOM 4522 N NH2   . ARG B 2 545 ? 10.16300  51.17700  40.94100 1.000 139.46365 ? 545 ARG A NH2   1 
ATOM 4523 N N     . PHE B 2 546 ? 10.85400  46.78100  47.39300 1.000 99.51453  ? 546 PHE A N     1 
ATOM 4524 C CA    . PHE B 2 546 ? 11.04500  47.79000  48.46500 1.000 84.37467  ? 546 PHE A CA    1 
ATOM 4525 C C     . PHE B 2 546 ? 10.74700  47.17000  49.81500 1.000 79.35661  ? 546 PHE A C     1 
ATOM 4526 O O     . PHE B 2 546 ? 10.20400  46.05100  49.87000 1.000 79.01224  ? 546 PHE A O     1 
ATOM 4527 C CB    . PHE B 2 546 ? 10.07800  48.96000  48.27700 1.000 83.39203  ? 546 PHE A CB    1 
ATOM 4528 C CG    . PHE B 2 546 ? 10.27100  49.81100  47.02900 1.000 106.71877 ? 546 PHE A CG    1 
ATOM 4529 C CD1   . PHE B 2 546 ? 11.53100  49.99500  46.47300 1.000 117.89671 ? 546 PHE A CD1   1 
ATOM 4530 C CD2   . PHE B 2 546 ? 9.18800   50.43300  46.42100 1.000 102.57593 ? 546 PHE A CD2   1 
ATOM 4531 C CE1   . PHE B 2 546 ? 11.69700  50.77300  45.34000 1.000 119.45088 ? 546 PHE A CE1   1 
ATOM 4532 C CE2   . PHE B 2 546 ? 9.36100   51.21200  45.28900 1.000 122.22645 ? 546 PHE A CE2   1 
ATOM 4533 C CZ    . PHE B 2 546 ? 10.61500  51.38100  44.75100 1.000 117.98662 ? 546 PHE A CZ    1 
ATOM 4534 N N     . HIS B 2 547 ? 11.10900  47.87300  50.88700 1.000 77.78431  ? 547 HIS A N     1 
ATOM 4535 C CA    . HIS B 2 547 ? 10.78400  47.40000  52.25700 1.000 79.16925  ? 547 HIS A CA    1 
ATOM 4536 C C     . HIS B 2 547 ? 10.04500  48.55300  52.93800 1.000 74.25770  ? 547 HIS A C     1 
ATOM 4537 O O     . HIS B 2 547 ? 10.53800  49.69400  52.86200 1.000 83.86370  ? 547 HIS A O     1 
ATOM 4538 C CB    . HIS B 2 547 ? 12.06000  46.94000  52.96100 1.000 84.41130  ? 547 HIS A CB    1 
ATOM 4539 C CG    . HIS B 2 547 ? 12.74000  45.80100  52.27600 1.000 95.81230  ? 547 HIS A CG    1 
ATOM 4540 N ND1   . HIS B 2 547 ? 12.64700  44.49900  52.71700 1.000 131.29870 ? 547 HIS A ND1   1 
ATOM 4541 C CD2   . HIS B 2 547 ? 13.55500  45.77500  51.21400 1.000 89.76972  ? 547 HIS A CD2   1 
ATOM 4542 C CE1   . HIS B 2 547 ? 13.36800  43.71900  51.92500 1.000 127.81197 ? 547 HIS A CE1   1 
ATOM 4543 N NE2   . HIS B 2 547 ? 13.92400  44.47300  51.00400 1.000 121.40928 ? 547 HIS A NE2   1 
ATOM 4544 N N     . ASN B 2 548 ? 8.90100   48.28100  53.56800 1.000 67.64537  ? 548 ASN A N     1 
ATOM 4545 C CA    . ASN B 2 548 ? 8.08700   49.40200  54.11400 1.000 64.89989  ? 548 ASN A CA    1 
ATOM 4546 C C     . ASN B 2 548 ? 7.92800   49.30000  55.63200 1.000 57.90404  ? 548 ASN A C     1 
ATOM 4547 O O     . ASN B 2 548 ? 7.79800   48.17000  56.13800 1.000 58.55052  ? 548 ASN A O     1 
ATOM 4548 C CB    . ASN B 2 548 ? 6.72100   49.46300  53.43900 1.000 56.86582  ? 548 ASN A CB    1 
ATOM 4549 C CG    . ASN B 2 548 ? 6.81600   49.43600  51.93400 1.000 71.87631  ? 548 ASN A CG    1 
ATOM 4550 O OD1   . ASN B 2 548 ? 6.25500   48.54100  51.29100 1.000 73.36993  ? 548 ASN A OD1   1 
ATOM 4551 N ND2   . ASN B 2 548 ? 7.51000   50.40300  51.35400 1.000 77.06121  ? 548 ASN A ND2   1 
ATOM 4552 N N     . VAL B 2 549 ? 7.94300   50.44300  56.32100 1.000 56.75997  ? 549 VAL A N     1 
ATOM 4553 C CA    . VAL B 2 549 ? 7.70300   50.46900  57.79400 1.000 58.99109  ? 549 VAL A CA    1 
ATOM 4554 C C     . VAL B 2 549 ? 6.37700   51.21200  57.99800 1.000 64.92664  ? 549 VAL A C     1 
ATOM 4555 O O     . VAL B 2 549 ? 6.24000   52.32300  57.44900 1.000 61.02956  ? 549 VAL A O     1 
ATOM 4556 C CB    . VAL B 2 549 ? 8.84500   51.14200  58.57800 1.000 56.15151  ? 549 VAL A CB    1 
ATOM 4557 C CG1   . VAL B 2 549 ? 8.49100   51.33900  60.04700 1.000 53.26939  ? 549 VAL A CG1   1 
ATOM 4558 C CG2   . VAL B 2 549 ? 10.15400  50.37800  58.43700 1.000 67.44446  ? 549 VAL A CG2   1 
ATOM 4559 N N     . PHE B 2 550 ? 5.43800   50.62100  58.73800 1.000 58.14602  ? 550 PHE A N     1 
ATOM 4560 C CA    . PHE B 2 550 ? 4.09500   51.24300  58.87300 1.000 61.09639  ? 550 PHE A CA    1 
ATOM 4561 C C     . PHE B 2 550 ? 3.91200   51.82200  60.27400 1.000 69.46650  ? 550 PHE A C     1 
ATOM 4562 O O     . PHE B 2 550 ? 3.39000   52.94800  60.39500 1.000 78.09014  ? 550 PHE A O     1 
ATOM 4563 C CB    . PHE B 2 550 ? 3.05700   50.17400  58.52400 1.000 56.61997  ? 550 PHE A CB    1 
ATOM 4564 C CG    . PHE B 2 550 ? 3.16600   49.61000  57.11500 1.000 59.03837  ? 550 PHE A CG    1 
ATOM 4565 C CD1   . PHE B 2 550 ? 2.54600   50.24400  56.04500 1.000 63.40445  ? 550 PHE A CD1   1 
ATOM 4566 C CD2   . PHE B 2 550 ? 3.87100   48.44000  56.86600 1.000 59.89671  ? 550 PHE A CD2   1 
ATOM 4567 C CE1   . PHE B 2 550 ? 2.64200   49.72900  54.76400 1.000 58.57353  ? 550 PHE A CE1   1 
ATOM 4568 C CE2   . PHE B 2 550 ? 3.96400   47.92900  55.58200 1.000 70.46144  ? 550 PHE A CE2   1 
ATOM 4569 C CZ    . PHE B 2 550 ? 3.34800   48.57200  54.53500 1.000 76.08041  ? 550 PHE A CZ    1 
ATOM 4570 N N     . THR B 2 551 ? 4.31700   51.08200  61.30700 1.000 63.82454  ? 551 THR A N     1 
ATOM 4571 C CA    . THR B 2 551 ? 4.09000   51.55100  62.69100 1.000 57.60463  ? 551 THR A CA    1 
ATOM 4572 C C     . THR B 2 551 ? 5.32100   52.27700  63.17600 1.000 53.96943  ? 551 THR A C     1 
ATOM 4573 O O     . THR B 2 551 ? 6.36300   51.61600  63.35400 1.000 79.57316  ? 551 THR A O     1 
ATOM 4574 C CB    . THR B 2 551 ? 3.73600   50.36800  63.58800 1.000 73.70396  ? 551 THR A CB    1 
ATOM 4575 O OG1   . THR B 2 551 ? 2.53300   49.84000  63.04100 1.000 62.61620  ? 551 THR A OG1   1 
ATOM 4576 C CG2   . THR B 2 551 ? 3.50700   50.78100  65.03000 1.000 58.85573  ? 551 THR A CG2   1 
ATOM 4577 N N     . PHE B 2 552 ? 5.20900   53.59000  63.38800 1.000 58.71489  ? 552 PHE A N     1 
ATOM 4578 C CA    . PHE B 2 552 ? 6.36800   54.40500  63.83700 1.000 64.09370  ? 552 PHE A CA    1 
ATOM 4579 C C     . PHE B 2 552 ? 5.86900   55.68000  64.51100 1.000 60.90088  ? 552 PHE A C     1 
ATOM 4580 O O     . PHE B 2 552 ? 4.66400   55.98500  64.41200 1.000 60.64626  ? 552 PHE A O     1 
ATOM 4581 C CB    . PHE B 2 552 ? 7.28100   54.70500  62.64400 1.000 60.50573  ? 552 PHE A CB    1 
ATOM 4582 C CG    . PHE B 2 552 ? 6.64300   55.43500  61.47000 1.000 65.34215  ? 552 PHE A CG    1 
ATOM 4583 C CD1   . PHE B 2 552 ? 6.04400   54.73000  60.43400 1.000 63.71386  ? 552 PHE A CD1   1 
ATOM 4584 C CD2   . PHE B 2 552 ? 6.66600   56.82200  61.39400 1.000 52.74362  ? 552 PHE A CD2   1 
ATOM 4585 C CE1   . PHE B 2 552 ? 5.46900   55.39500  59.36500 1.000 64.29168  ? 552 PHE A CE1   1 
ATOM 4586 C CE2   . PHE B 2 552 ? 6.09100   57.48100  60.32100 1.000 72.11023  ? 552 PHE A CE2   1 
ATOM 4587 C CZ    . PHE B 2 552 ? 5.49500   56.76700  59.31000 1.000 72.88899  ? 552 PHE A CZ    1 
ATOM 4588 N N     . GLU B 2 553 ? 6.77100   56.40300  65.18000 1.000 64.06060  ? 553 GLU A N     1 
ATOM 4589 C CA    . GLU B 2 553 ? 6.40500   57.67300  65.85800 1.000 59.09913  ? 553 GLU A CA    1 
ATOM 4590 C C     . GLU B 2 553 ? 6.86500   58.84900  64.98500 1.000 67.91557  ? 553 GLU A C     1 
ATOM 4591 O O     . GLU B 2 553 ? 8.03400   58.83500  64.55300 1.000 70.40628  ? 553 GLU A O     1 
ATOM 4592 C CB    . GLU B 2 553 ? 7.05600   57.69700  67.24000 1.000 65.50193  ? 553 GLU A CB    1 
ATOM 4593 C CG    . GLU B 2 553 ? 6.76300   58.96400  68.03700 1.000 105.99170 ? 553 GLU A CG    1 
ATOM 4594 C CD    . GLU B 2 553 ? 7.51800   59.03100  69.35200 1.000 108.10128 ? 553 GLU A CD    1 
ATOM 4595 O OE1   . GLU B 2 553 ? 8.76600   59.01700  69.31600 1.000 113.97062 ? 553 GLU A OE1   1 
ATOM 4596 O OE2   . GLU B 2 553 ? 6.86100   59.09500  70.41200 1.000 110.14637 ? 553 GLU A OE2   1 
ATOM 4597 N N     . THR B 2 554 ? 5.99000   59.82900  64.74700 1.000 61.68259  ? 554 THR A N     1 
ATOM 4598 C CA    . THR B 2 554 ? 6.32400   60.95500  63.84800 1.000 65.49649  ? 554 THR A CA    1 
ATOM 4599 C C     . THR B 2 554 ? 6.81400   62.13600  64.65200 1.000 67.92190  ? 554 THR A C     1 
ATOM 4600 O O     . THR B 2 554 ? 6.98700   63.21400  64.05300 1.000 76.21044  ? 554 THR A O     1 
ATOM 4601 C CB    . THR B 2 554 ? 5.07800   61.31500  63.04500 1.000 51.95616  ? 554 THR A CB    1 
ATOM 4602 O OG1   . THR B 2 554 ? 4.12700   61.72700  64.02000 1.000 72.04731  ? 554 THR A OG1   1 
ATOM 4603 C CG2   . THR B 2 554 ? 4.53600   60.14000  62.25300 1.000 58.55427  ? 554 THR A CG2   1 
ATOM 4604 N N     . LYS B 2 555 ? 7.04100   61.95800  65.95300 1.000 57.60343  ? 555 LYS A N     1 
ATOM 4605 C CA    . LYS B 2 555 ? 7.42800   63.09400  66.82600 1.000 71.85793  ? 555 LYS A CA    1 
ATOM 4606 C C     . LYS B 2 555 ? 8.73400   63.73000  66.34000 1.000 53.56498  ? 555 LYS A C     1 
ATOM 4607 O O     . LYS B 2 555 ? 8.72100   64.93500  66.01600 1.000 62.40548  ? 555 LYS A O     1 
ATOM 4608 C CB    . LYS B 2 555 ? 7.61000   62.57400  68.25500 1.000 61.77774  ? 555 LYS A CB    1 
ATOM 4609 C CG    . LYS B 2 555 ? 8.29200   63.51100  69.23800 1.000 77.53804  ? 555 LYS A CG    1 
ATOM 4610 C CD    . LYS B 2 555 ? 8.74500   62.77600  70.49300 1.000 61.28024  ? 555 LYS A CD    1 
ATOM 4611 C CE    . LYS B 2 555 ? 9.55400   63.64400  71.40300 1.000 138.95223 ? 555 LYS A CE    1 
ATOM 4612 N NZ    . LYS B 2 555 ? 10.08500  62.88500  72.53700 1.000 143.45075 ? 555 LYS A NZ    1 
ATOM 4613 N N     . ASP B 2 556 ? 9.81000   62.94800  66.27500 1.000 64.02266  ? 556 ASP A N     1 
ATOM 4614 C CA    . ASP B 2 556 ? 11.13800  63.51200  65.90600 1.000 67.05583  ? 556 ASP A CA    1 
ATOM 4615 C C     . ASP B 2 556 ? 11.12500  63.95500  64.43900 1.000 76.29701  ? 556 ASP A C     1 
ATOM 4616 O O     . ASP B 2 556 ? 11.74300  64.99200  64.12700 1.000 68.05609  ? 556 ASP A O     1 
ATOM 4617 C CB    . ASP B 2 556 ? 12.24700  62.53600  66.26100 1.000 70.54360  ? 556 ASP A CB    1 
ATOM 4618 C CG    . ASP B 2 556 ? 12.44000  62.29600  67.75100 1.000 77.58397  ? 556 ASP A CG    1 
ATOM 4619 O OD1   . ASP B 2 556 ? 11.70500  62.92000  68.54200 1.000 75.86984  ? 556 ASP A OD1   1 
ATOM 4620 O OD2   . ASP B 2 556 ? 13.32200  61.48700  68.10600 1.000 104.73278 ? 556 ASP A OD2   1 
ATOM 4621 N N     . ILE B 2 557 ? 10.43400  63.20600  63.57900 1.000 70.90633  ? 557 ILE A N     1 
ATOM 4622 C CA    . ILE B 2 557 ? 10.35200  63.57200  62.13500 1.000 65.87302  ? 557 ILE A CA    1 
ATOM 4623 C C     . ILE B 2 557 ? 9.79000   64.99600  62.03300 1.000 55.87779  ? 557 ILE A C     1 
ATOM 4624 O O     . ILE B 2 557 ? 10.39100  65.81600  61.31100 1.000 84.42135  ? 557 ILE A O     1 
ATOM 4625 C CB    . ILE B 2 557 ? 9.48300   62.56400  61.36300 1.000 64.57871  ? 557 ILE A CB    1 
ATOM 4626 C CG1   . ILE B 2 557 ? 10.04200  61.14800  61.46100 1.000 67.61036  ? 557 ILE A CG1   1 
ATOM 4627 C CG2   . ILE B 2 557 ? 9.30100   62.99600  59.90800 1.000 66.10998  ? 557 ILE A CG2   1 
ATOM 4628 C CD1   . ILE B 2 557 ? 9.28500   60.12900  60.62800 1.000 48.50568  ? 557 ILE A CD1   1 
ATOM 4629 N N     . LEU B 2 558 ? 8.70200   65.28100  62.74800 1.000 59.54057  ? 558 LEU A N     1 
ATOM 4630 C CA    . LEU B 2 558 ? 8.05600   66.61700  62.66100 1.000 55.81607  ? 558 LEU A CA    1 
ATOM 4631 C C     . LEU B 2 558 ? 9.01400   67.69100  63.19700 1.000 67.06837  ? 558 LEU A C     1 
ATOM 4632 O O     . LEU B 2 558 ? 9.04400   68.79700  62.62600 1.000 75.44856  ? 558 LEU A O     1 
ATOM 4633 C CB    . LEU B 2 558 ? 6.72900   66.61000  63.41700 1.000 51.46550  ? 558 LEU A CB    1 
ATOM 4634 C CG    . LEU B 2 558 ? 5.53800   66.00800  62.66600 1.000 62.57708  ? 558 LEU A CG    1 
ATOM 4635 C CD1   . LEU B 2 558 ? 4.34400   65.85500  63.58900 1.000 54.90945  ? 558 LEU A CD1   1 
ATOM 4636 C CD2   . LEU B 2 558 ? 5.18700   66.89500  61.48700 1.000 55.35703  ? 558 LEU A CD2   1 
ATOM 4637 N N     . LYS B 2 559 ? 9.76100   67.37200  64.25300 1.000 56.45409  ? 559 LYS A N     1 
ATOM 4638 C CA    . LYS B 2 559 ? 10.70700  68.35200  64.84000 1.000 54.94315  ? 559 LYS A CA    1 
ATOM 4639 C C     . LYS B 2 559 ? 11.75300  68.72600  63.78300 1.000 68.08065  ? 559 LYS A C     1 
ATOM 4640 O O     . LYS B 2 559 ? 12.01400  69.93400  63.60100 1.000 80.90572  ? 559 LYS A O     1 
ATOM 4641 C CB    . LYS B 2 559 ? 11.38100  67.75700  66.07800 1.000 58.59097  ? 559 LYS A CB    1 
ATOM 4642 C CG    . LYS B 2 559 ? 10.45700  67.50000  67.25700 1.000 60.73493  ? 559 LYS A CG    1 
ATOM 4643 C CD    . LYS B 2 559 ? 11.17100  66.83500  68.42700 1.000 83.49443  ? 559 LYS A CD    1 
ATOM 4644 C CE    . LYS B 2 559 ? 10.30100  66.72800  69.63700 1.000 123.35133 ? 559 LYS A CE    1 
ATOM 4645 N NZ    . LYS B 2 559 ? 9.90000   68.04800  70.13000 1.000 141.61505 ? 559 LYS A NZ    1 
ATOM 4646 N N     . ASP B 2 560 ? 12.31500  67.72500  63.10800 1.000 64.24896  ? 560 ASP A N     1 
ATOM 4647 C CA    . ASP B 2 560 ? 13.34600  67.98400  62.06700 1.000 67.30297  ? 560 ASP A CA    1 
ATOM 4648 C C     . ASP B 2 560 ? 12.71600  68.80200  60.93700 1.000 54.29266  ? 560 ASP A C     1 
ATOM 4649 O O     . ASP B 2 560 ? 13.36700  69.75300  60.45700 1.000 76.79592  ? 560 ASP A O     1 
ATOM 4650 C CB    . ASP B 2 560 ? 13.97200  66.68500  61.58900 1.000 76.89993  ? 560 ASP A CB    1 
ATOM 4651 C CG    . ASP B 2 560 ? 14.64900  65.85000  62.66600 1.000 77.89708  ? 560 ASP A CG    1 
ATOM 4652 O OD1   . ASP B 2 560 ? 14.65100  66.29100  63.83300 1.000 96.96140  ? 560 ASP A OD1   1 
ATOM 4653 O OD2   . ASP B 2 560 ? 15.16400  64.76600  62.32900 1.000 82.97719  ? 560 ASP A OD2   1 
ATOM 4654 N N     . LEU B 2 561 ? 11.49200  68.45300  60.54000 1.000 56.46249  ? 561 LEU A N     1 
ATOM 4655 C CA    . LEU B 2 561 ? 10.79900  69.18300  59.44900 1.000 56.69722  ? 561 LEU A CA    1 
ATOM 4656 C C     . LEU B 2 561 ? 10.63400  70.65100  59.85800 1.000 65.20220  ? 561 LEU A C     1 
ATOM 4657 O O     . LEU B 2 561 ? 10.91900  71.53100  59.02900 1.000 66.00687  ? 561 LEU A O     1 
ATOM 4658 C CB    . LEU B 2 561 ? 9.44900   68.52800  59.16800 1.000 58.26171  ? 561 LEU A CB    1 
ATOM 4659 C CG    . LEU B 2 561 ? 9.48700   67.19600  58.41500 1.000 64.87919  ? 561 LEU A CG    1 
ATOM 4660 C CD1   . LEU B 2 561 ? 8.11800   66.54100  58.43800 1.000 55.75104  ? 561 LEU A CD1   1 
ATOM 4661 C CD2   . LEU B 2 561 ? 9.93200   67.43700  56.98600 1.000 63.57659  ? 561 LEU A CD2   1 
ATOM 4662 N N     . HIS B 2 562 ? 10.21500  70.89900  61.09700 1.000 56.57074  ? 562 HIS A N     1 
ATOM 4663 C CA    . HIS B 2 562 ? 9.96700   72.29400  61.54600 1.000 61.03996  ? 562 HIS A CA    1 
ATOM 4664 C C     . HIS B 2 562 ? 11.25600  73.10000  61.40300 1.000 66.68903  ? 562 HIS A C     1 
ATOM 4665 O O     . HIS B 2 562 ? 11.22300  74.21300  60.84400 1.000 77.27611  ? 562 HIS A O     1 
ATOM 4666 C CB    . HIS B 2 562 ? 9.45400   72.30600  62.98800 1.000 64.20698  ? 562 HIS A CB    1 
ATOM 4667 C CG    . HIS B 2 562 ? 9.34200   73.66300  63.59500 1.000 70.52672  ? 562 HIS A CG    1 
ATOM 4668 N ND1   . HIS B 2 562 ? 8.22300   74.45300  63.45100 1.000 100.64606 ? 562 HIS A ND1   1 
ATOM 4669 C CD2   . HIS B 2 562 ? 10.20000  74.36800  64.34100 1.000 64.58433  ? 562 HIS A CD2   1 
ATOM 4670 C CE1   . HIS B 2 562 ? 8.41000   75.59500  64.09600 1.000 94.03587  ? 562 HIS A CE1   1 
ATOM 4671 N NE2   . HIS B 2 562 ? 9.60400   75.56300  64.64500 1.000 92.69693  ? 562 HIS A NE2   1 
ATOM 4672 N N     . ALA B 2 563 ? 12.36900  72.54000  61.87300 1.000 69.20229  ? 563 ALA A N     1 
ATOM 4673 C CA    . ALA B 2 563 ? 13.64700  73.28600  61.83900 1.000 70.58803  ? 563 ALA A CA    1 
ATOM 4674 C C     . ALA B 2 563 ? 14.00600  73.64100  60.39800 1.000 66.28659  ? 563 ALA A C     1 
ATOM 4675 O O     . ALA B 2 563 ? 14.35000  74.80900  60.13700 1.000 72.97666  ? 563 ALA A O     1 
ATOM 4676 C CB    . ALA B 2 563 ? 14.73100  72.46000  62.48300 1.000 59.78466  ? 563 ALA A CB    1 
ATOM 4677 N N     . ILE B 2 564 ? 13.91900  72.67100  59.48800 1.000 63.10596  ? 564 ILE A N     1 
ATOM 4678 C CA    . ILE B 2 564 ? 14.36000  72.93500  58.08500 1.000 65.63185  ? 564 ILE A CA    1 
ATOM 4679 C C     . ILE B 2 564 ? 13.42900  73.98500  57.45600 1.000 63.79650  ? 564 ILE A C     1 
ATOM 4680 O O     . ILE B 2 564 ? 13.94300  74.88600  56.76800 1.000 81.98255  ? 564 ILE A O     1 
ATOM 4681 C CB    . ILE B 2 564 ? 14.45300  71.63100  57.26800 1.000 65.17871  ? 564 ILE A CB    1 
ATOM 4682 C CG1   . ILE B 2 564 ? 15.43100  71.77200  56.10300 1.000 71.35795  ? 564 ILE A CG1   1 
ATOM 4683 C CG2   . ILE B 2 564 ? 13.08100  71.14700  56.79900 1.000 74.19015  ? 564 ILE A CG2   1 
ATOM 4684 C CD1   . ILE B 2 564 ? 15.85200  70.44900  55.49200 1.000 85.69284  ? 564 ILE A CD1   1 
ATOM 4685 N N     . ILE B 2 565 ? 12.12600  73.89200  57.71800 1.000 63.86740  ? 565 ILE A N     1 
ATOM 4686 C CA    . ILE B 2 565 ? 11.15600  74.87600  57.15700 1.000 63.84465  ? 565 ILE A CA    1 
ATOM 4687 C C     . ILE B 2 565 ? 11.52700  76.26200  57.70200 1.000 71.43275  ? 565 ILE A C     1 
ATOM 4688 O O     . ILE B 2 565 ? 11.56400  77.22000  56.90400 1.000 92.19884  ? 565 ILE A O     1 
ATOM 4689 C CB    . ILE B 2 565 ? 9.71000   74.48400  57.50600 1.000 63.20040  ? 565 ILE A CB    1 
ATOM 4690 C CG1   . ILE B 2 565 ? 9.34500   73.12900  56.91300 1.000 70.86873  ? 565 ILE A CG1   1 
ATOM 4691 C CG2   . ILE B 2 565 ? 8.72500   75.56700  57.06800 1.000 55.97050  ? 565 ILE A CG2   1 
ATOM 4692 C CD1   . ILE B 2 565 ? 8.10400   72.50500  57.52200 1.000 56.44867  ? 565 ILE A CD1   1 
ATOM 4693 N N     . ASP B 2 566 ? 11.82100  76.35100  59.00000 1.000 64.53490  ? 566 ASP A N     1 
ATOM 4694 C CA    . ASP B 2 566 ? 12.14000  77.66500  59.62200 1.000 80.23325  ? 566 ASP A CA    1 
ATOM 4695 C C     . ASP B 2 566 ? 13.41200  78.23600  58.99000 1.000 82.21393  ? 566 ASP A C     1 
ATOM 4696 O O     . ASP B 2 566 ? 13.40900  79.43100  58.63600 1.000 76.78402  ? 566 ASP A O     1 
ATOM 4697 C CB    . ASP B 2 566 ? 12.26400  77.55800  61.13200 1.000 73.46228  ? 566 ASP A CB    1 
ATOM 4698 C CG    . ASP B 2 566 ? 10.97200  77.27000  61.88100 1.000 92.08994  ? 566 ASP A CG    1 
ATOM 4699 O OD1   . ASP B 2 566 ? 9.93200   77.09700  61.21300 1.000 115.99225 ? 566 ASP A OD1   1 
ATOM 4700 O OD2   . ASP B 2 566 ? 11.01600  77.23500  63.12800 1.000 90.40377  ? 566 ASP A OD2   1 
ATOM 4701 N N     . LYS B 2 567 ? 14.45500  77.41300  58.85400 1.000 83.19788  ? 567 LYS A N     1 
ATOM 4702 C CA    . LYS B 2 567 ? 15.74100  77.89500  58.29000 1.000 69.04688  ? 567 LYS A CA    1 
ATOM 4703 C C     . LYS B 2 567 ? 15.50000  78.35500  56.84800 1.000 70.72647  ? 567 LYS A C     1 
ATOM 4704 O O     . LYS B 2 567 ? 15.99400  79.43800  56.47900 1.000 65.15722  ? 567 LYS A O     1 
ATOM 4705 C CB    . LYS B 2 567 ? 16.80500  76.79500  58.33300 1.000 65.19091  ? 567 LYS A CB    1 
ATOM 4706 C CG    . LYS B 2 567 ? 18.20800  77.25000  57.96600 1.000 76.47390  ? 567 LYS A CG    1 
ATOM 4707 C CD    . LYS B 2 567 ? 18.68800  78.39600  58.84800 1.000 86.82045  ? 567 LYS A CD    1 
ATOM 4708 C CE    . LYS B 2 567 ? 20.03100  78.90800  58.44500 1.000 71.67549  ? 567 LYS A CE    1 
ATOM 4709 N NZ    . LYS B 2 567 ? 20.45600  80.01900  59.30000 1.000 100.44396 ? 567 LYS A NZ    1 
ATOM 4710 N N     . LEU B 2 568 ? 14.75300  77.56300  56.07700 1.000 64.12912  ? 568 LEU A N     1 
ATOM 4711 C CA    . LEU B 2 568 ? 14.45400  77.93000  54.67100 1.000 59.26888  ? 568 LEU A CA    1 
ATOM 4712 C C     . LEU B 2 568 ? 13.72800  79.27900  54.66700 1.000 74.55850  ? 568 LEU A C     1 
ATOM 4713 O O     . LEU B 2 568 ? 14.06400  80.13400  53.82300 1.000 81.69748  ? 568 LEU A O     1 
ATOM 4714 C CB    . LEU B 2 568 ? 13.61400  76.83400  54.02200 1.000 62.35754  ? 568 LEU A CB    1 
ATOM 4715 C CG    . LEU B 2 568 ? 14.38400  75.63300  53.46600 1.000 68.90687  ? 568 LEU A CG    1 
ATOM 4716 C CD1   . LEU B 2 568 ? 13.45900  74.43700  53.33300 1.000 82.37276  ? 568 LEU A CD1   1 
ATOM 4717 C CD2   . LEU B 2 568 ? 14.97500  75.99000  52.11500 1.000 63.58827  ? 568 LEU A CD2   1 
ATOM 4718 N N     . ASN B 2 569 ? 12.78000  79.46100  55.58700 1.000 71.00130  ? 569 ASN A N     1 
ATOM 4719 C CA    . ASN B 2 569 ? 12.01700  80.73600  55.65800 1.000 70.91227  ? 569 ASN A CA    1 
ATOM 4720 C C     . ASN B 2 569 ? 12.98600  81.88100  55.96000 1.000 69.61285  ? 569 ASN A C     1 
ATOM 4721 O O     . ASN B 2 569 ? 12.90500  82.91500  55.27400 1.000 80.47168  ? 569 ASN A O     1 
ATOM 4722 C CB    . ASN B 2 569 ? 10.88600  80.65900  56.67500 1.000 68.86705  ? 569 ASN A CB    1 
ATOM 4723 C CG    . ASN B 2 569 ? 9.65200   80.01100  56.10000 1.000 71.31397  ? 569 ASN A CG    1 
ATOM 4724 O OD1   . ASN B 2 569 ? 9.09300   80.50900  55.11700 1.000 87.20491  ? 569 ASN A OD1   1 
ATOM 4725 N ND2   . ASN B 2 569 ? 9.21300   78.91100  56.69300 1.000 84.45324  ? 569 ASN A ND2   1 
ATOM 4726 N N     . LYS B 2 570 ? 13.87600  81.69100  56.93500 1.000 63.20070  ? 570 LYS A N     1 
ATOM 4727 C CA    . LYS B 2 570 ? 14.81900  82.76900  57.32500 1.000 70.55602  ? 570 LYS A CA    1 
ATOM 4728 C C     . LYS B 2 570 ? 15.69600  83.12800  56.12000 1.000 71.20002  ? 570 LYS A C     1 
ATOM 4729 O O     . LYS B 2 570 ? 15.92300  84.33400  55.88600 1.000 77.78416  ? 570 LYS A O     1 
ATOM 4730 C CB    . LYS B 2 570 ? 15.70300  82.33100  58.49500 1.000 73.11640  ? 570 LYS A CB    1 
ATOM 4731 C CG    . LYS B 2 570 ? 14.98100  82.12700  59.81600 1.000 91.36707  ? 570 LYS A CG    1 
ATOM 4732 C CD    . LYS B 2 570 ? 15.94900  81.81200  60.95000 1.000 122.69856 ? 570 LYS A CD    1 
ATOM 4733 C CE    . LYS B 2 570 ? 17.00800  82.86000  61.07500 1.000 116.74861 ? 570 LYS A CE    1 
ATOM 4734 N NZ    . LYS B 2 570 ? 17.95400  82.55300  62.15000 1.000 132.21395 ? 570 LYS A NZ    1 
ATOM 4735 N N     . THR B 2 571 ? 16.16300  82.11600  55.38700 1.000 73.47093  ? 571 THR A N     1 
ATOM 4736 C CA    . THR B 2 571 ? 17.00600  82.36300  54.20200 1.000 72.50946  ? 571 THR A CA    1 
ATOM 4737 C C     . THR B 2 571 ? 16.23000  83.22200  53.22900 1.000 78.68524  ? 571 THR A C     1 
ATOM 4738 O O     . THR B 2 571 ? 16.81700  84.17700  52.69000 1.000 91.44057  ? 571 THR A O     1 
ATOM 4739 C CB    . THR B 2 571 ? 17.41200  81.02500  53.59100 1.000 66.98510  ? 571 THR A CB    1 
ATOM 4740 O OG1   . THR B 2 571 ? 17.79200  80.21500  54.69800 1.000 65.98054  ? 571 THR A OG1   1 
ATOM 4741 C CG2   . THR B 2 571 ? 18.56700  81.15700  52.61700 1.000 67.93105  ? 571 THR A CG2   1 
ATOM 4742 N N     . LEU B 2 572 ? 14.94800  82.91600  53.02600 1.000 66.45720  ? 572 LEU A N     1 
ATOM 4743 C CA    . LEU B 2 572 ? 14.09500  83.69600  52.09400 1.000 77.65266  ? 572 LEU A CA    1 
ATOM 4744 C C     . LEU B 2 572 ? 13.97600  85.14800  52.58200 1.000 89.16219  ? 572 LEU A C     1 
ATOM 4745 O O     . LEU B 2 572 ? 13.98500  86.05800  51.72900 1.000 88.88364  ? 572 LEU A O     1 
ATOM 4746 C CB    . LEU B 2 572 ? 12.72500  83.02900  52.00100 1.000 93.17305  ? 572 LEU A CB    1 
ATOM 4747 C CG    . LEU B 2 572 ? 12.64800  81.76300  51.14400 1.000 80.06071  ? 572 LEU A CG    1 
ATOM 4748 C CD1   . LEU B 2 572 ? 11.45200  80.92300  51.55500 1.000 70.99099  ? 572 LEU A CD1   1 
ATOM 4749 C CD2   . LEU B 2 572 ? 12.52700  82.16900  49.68800 1.000 79.23256  ? 572 LEU A CD2   1 
ATOM 4750 N N     . GLU B 2 573 ? 13.86400  85.35400  53.89700 1.000 91.45526  ? 573 GLU A N     1 
ATOM 4751 C CA    . GLU B 2 573 ? 13.67900  86.72500  54.44400 1.000 104.97683 ? 573 GLU A CA    1 
ATOM 4752 C C     . GLU B 2 573 ? 14.86900  87.60600  54.03500 1.000 95.67178  ? 573 GLU A C     1 
ATOM 4753 O O     . GLU B 2 573 ? 14.64200  88.77500  53.66900 1.000 103.41073 ? 573 GLU A O     1 
ATOM 4754 C CB    . GLU B 2 573 ? 13.55200  86.72300  55.96700 1.000 95.85790  ? 573 GLU A CB    1 
ATOM 4755 C CG    . GLU B 2 573 ? 12.57000  85.68500  56.50300 1.000 118.04735 ? 573 GLU A CG    1 
ATOM 4756 C CD    . GLU B 2 573 ? 11.10200  85.88100  56.17100 1.000 141.61162 ? 573 GLU A CD    1 
ATOM 4757 O OE1   . GLU B 2 573 ? 10.75000  86.89600  55.53700 1.000 146.04307 ? 573 GLU A OE1   1 
ATOM 4758 O OE2   . GLU B 2 573 ? 10.30300  85.00000  56.55100 1.000 135.68644 ? 573 GLU A OE2   1 
ATOM 4759 N N     . ILE B 2 574 ? 16.08500  87.05600  54.08200 1.000 88.24615  ? 574 ILE A N     1 
ATOM 4760 C CA    . ILE B 2 574 ? 17.30100  87.84000  53.71700 1.000 88.40459  ? 574 ILE A CA    1 
ATOM 4761 C C     . ILE B 2 574 ? 17.03300  88.54000  52.37900 1.000 89.23825  ? 574 ILE A C     1 
ATOM 4762 O O     . ILE B 2 574 ? 17.48300  89.69200  52.21400 1.000 95.21138  ? 574 ILE A O     1 
ATOM 4763 C CB    . ILE B 2 574 ? 18.53200  86.92100  53.61800 1.000 93.07985  ? 574 ILE A CB    1 
ATOM 4764 C CG1   . ILE B 2 574 ? 18.70400  86.06300  54.86900 1.000 103.00331 ? 574 ILE A CG1   1 
ATOM 4765 C CG2   . ILE B 2 574 ? 19.79600  87.72200  53.30500 1.000 96.43439  ? 574 ILE A CG2   1 
ATOM 4766 C CD1   . ILE B 2 574 ? 19.86400  85.08700  54.78900 1.000 81.81407  ? 574 ILE A CD1   1 
ATOM 4767 N N     . PHE B 2 575 ? 16.31700  87.87500  51.47100 1.000 90.05782  ? 575 PHE A N     1 
ATOM 4768 C CA    . PHE B 2 575 ? 16.09100  88.44400  50.11600 1.000 101.65148 ? 575 PHE A CA    1 
ATOM 4769 C C     . PHE B 2 575 ? 14.66700  88.98000  50.00700 1.000 111.71209 ? 575 PHE A C     1 
ATOM 4770 O O     . PHE B 2 575 ? 14.05700  88.85300  48.92600 1.000 114.55537 ? 575 PHE A O     1 
ATOM 4771 C CB    . PHE B 2 575 ? 16.39500  87.35000  49.08900 1.000 77.73259  ? 575 PHE A CB    1 
ATOM 4772 C CG    . PHE B 2 575 ? 17.71800  86.63400  49.31700 1.000 75.91974  ? 575 PHE A CG    1 
ATOM 4773 C CD1   . PHE B 2 575 ? 18.90400  87.14800  48.80700 1.000 90.98978  ? 575 PHE A CD1   1 
ATOM 4774 C CD2   . PHE B 2 575 ? 17.77200  85.44400  50.03200 1.000 89.89448  ? 575 PHE A CD2   1 
ATOM 4775 C CE1   . PHE B 2 575 ? 20.10700  86.49300  49.01700 1.000 111.41671 ? 575 PHE A CE1   1 
ATOM 4776 C CE2   . PHE B 2 575 ? 18.97700  84.79500  50.24000 1.000 104.57678 ? 575 PHE A CE2   1 
ATOM 4777 C CZ    . PHE B 2 575 ? 20.14100  85.32000  49.73200 1.000 98.62677  ? 575 PHE A CZ    1 
ATOM 4778 N N     . ASN B 2 576 ? 14.13900  89.55200  51.09100 1.000 103.00290 ? 576 ASN A N     1 
ATOM 4779 C CA    . ASN B 2 576 ? 12.79400  90.18700  51.01300 1.000 119.66470 ? 576 ASN A CA    1 
ATOM 4780 C C     . ASN B 2 576 ? 12.95800  91.61500  50.48900 1.000 126.05396 ? 576 ASN A C     1 
ATOM 4781 O O     . ASN B 2 576 ? 14.09800  92.12500  50.50900 1.000 128.81921 ? 576 ASN A O     1 
ATOM 4782 C CB    . ASN B 2 576 ? 12.06200  90.16100  52.34900 1.000 98.16820  ? 576 ASN A CB    1 
ATOM 4783 C CG    . ASN B 2 576 ? 11.40200  88.82900  52.60800 1.000 122.56548 ? 576 ASN A CG    1 
ATOM 4784 O OD1   . ASN B 2 576 ? 11.51500  87.90800  51.79100 1.000 131.68668 ? 576 ASN A OD1   1 
ATOM 4785 N ND2   . ASN B 2 576 ? 10.71000  88.70700  53.73100 1.000 135.20109 ? 576 ASN A ND2   1 
ATOM 4786 N N     . GLY B 2 577 ? 11.86200  92.23300  50.04100 1.000 127.57232 ? 577 GLY A N     1 
ATOM 4787 C CA    . GLY B 2 577 ? 11.92600  93.60600  49.50500 1.000 133.68125 ? 577 GLY A CA    1 
ATOM 4788 C C     . GLY B 2 577 ? 12.93500  93.69700  48.37900 1.000 135.08228 ? 577 GLY A C     1 
ATOM 4789 O O     . GLY B 2 577 ? 13.78300  94.61200  48.41800 1.000 133.75936 ? 577 GLY A O     1 
ATOM 4790 N N     . ILE B 2 578 ? 12.85500  92.78000  47.41200 1.000 116.92059 ? 578 ILE A N     1 
ATOM 4791 C CA    . ILE B 2 578 ? 13.83400  92.75100  46.28600 1.000 95.98404  ? 578 ILE A CA    1 
ATOM 4792 C C     . ILE B 2 578 ? 13.04900  92.53600  44.98300 1.000 115.99590 ? 578 ILE A C     1 
ATOM 4793 O O     . ILE B 2 578 ? 11.85200  92.18900  45.07300 1.000 116.56380 ? 578 ILE A O     1 
ATOM 4794 C CB    . ILE B 2 578 ? 14.87400  91.64500  46.52700 1.000 94.06182  ? 578 ILE A CB    1 
ATOM 4795 C CG1   . ILE B 2 578 ? 16.24000  92.01800  45.95600 1.000 100.13408 ? 578 ILE A CG1   1 
ATOM 4796 C CG2   . ILE B 2 578 ? 14.36800  90.30000  46.00300 1.000 125.63825 ? 578 ILE A CG2   1 
ATOM 4797 C CD1   . ILE B 2 578 ? 16.92100  93.15300  46.69800 1.000 125.97523 ? 578 ILE A CD1   1 
ATOM 4798 N N     . SER B 2 579 ? 13.68400  92.74400  43.82700 1.000 105.38447 ? 579 SER A N     1 
ATOM 4799 C CA    . SER B 2 579 ? 12.94000  92.64100  42.54500 1.000 97.66860  ? 579 SER A CA    1 
ATOM 4800 C C     . SER B 2 579 ? 13.83100  92.06500  41.43600 1.000 101.36807 ? 579 SER A C     1 
ATOM 4801 O O     . SER B 2 579 ? 13.29400  91.76100  40.35200 1.000 101.54752 ? 579 SER A O     1 
ATOM 4802 C CB    . SER B 2 579 ? 12.38000  93.98000  42.14700 1.000 96.41751  ? 579 SER A CB    1 
ATOM 4803 O OG    . SER B 2 579 ? 13.41700  94.94400  42.03300 1.000 142.37262 ? 579 SER A OG    1 
ATOM 4804 N N     . HIS B 2 580 ? 15.13400  91.93000  41.68700 1.000 92.69169  ? 580 HIS A N     1 
ATOM 4805 C CA    . HIS B 2 580 ? 16.05100  91.45200  40.61800 1.000 93.25539  ? 580 HIS A CA    1 
ATOM 4806 C C     . HIS B 2 580 ? 15.62900  90.04400  40.19600 1.000 86.19535  ? 580 HIS A C     1 
ATOM 4807 O O     . HIS B 2 580 ? 15.25400  89.23400  41.06300 1.000 95.49634  ? 580 HIS A O     1 
ATOM 4808 C CB    . HIS B 2 580 ? 17.51100  91.48600  41.07800 1.000 102.28431 ? 580 HIS A CB    1 
ATOM 4809 C CG    . HIS B 2 580 ? 18.48700  91.33900  39.96000 1.000 100.55816 ? 580 HIS A CG    1 
ATOM 4810 N ND1   . HIS B 2 580 ? 18.87100  90.11500  39.45700 1.000 96.27997  ? 580 HIS A ND1   1 
ATOM 4811 C CD2   . HIS B 2 580 ? 19.13400  92.25600  39.23200 1.000 98.31872  ? 580 HIS A CD2   1 
ATOM 4812 C CE1   . HIS B 2 580 ? 19.73200  90.29900  38.46800 1.000 102.51262 ? 580 HIS A CE1   1 
ATOM 4813 N NE2   . HIS B 2 580 ? 19.90800  91.59300  38.31700 1.000 116.63320 ? 580 HIS A NE2   1 
ATOM 4814 N N     . LYS B 2 581 ? 15.70000  89.75700  38.89600 1.000 81.07974  ? 581 LYS A N     1 
ATOM 4815 C CA    . LYS B 2 581 ? 15.25600  88.43400  38.39100 1.000 90.28314  ? 581 LYS A CA    1 
ATOM 4816 C C     . LYS B 2 581 ? 16.05600  87.32700  39.08900 1.000 99.28953  ? 581 LYS A C     1 
ATOM 4817 O O     . LYS B 2 581 ? 15.43400  86.35100  39.55400 1.000 107.87340 ? 581 LYS A O     1 
ATOM 4818 C CB    . LYS B 2 581 ? 15.44400  88.35800  36.87400 1.000 84.66700  ? 581 LYS A CB    1 
ATOM 4819 C CG    . LYS B 2 581 ? 14.54600  89.29400  36.07700 1.000 106.51459 ? 581 LYS A CG    1 
ATOM 4820 C CD    . LYS B 2 581 ? 14.70800  89.14500  34.56900 1.000 120.29010 ? 581 LYS A CD    1 
ATOM 4821 C CE    . LYS B 2 581 ? 13.74600  89.99600  33.80000 1.000 106.84054 ? 581 LYS A CE    1 
ATOM 4822 N NZ    . LYS B 2 581 ? 13.90900  91.41900  34.10900 1.000 116.56884 ? 581 LYS A NZ    1 
ATOM 4823 N N     . THR B 2 582 ? 17.37900  87.47500  39.15800 1.000 92.12942  ? 582 THR A N     1 
ATOM 4824 C CA    . THR B 2 582 ? 18.21800  86.41800  39.75700 1.000 90.55238  ? 582 THR A CA    1 
ATOM 4825 C C     . THR B 2 582 ? 17.70000  86.11300  41.14000 1.000 88.40908  ? 582 THR A C     1 
ATOM 4826 O O     . THR B 2 582 ? 17.46400  84.92400  41.43400 1.000 105.21825 ? 582 THR A O     1 
ATOM 4827 C CB    . THR B 2 582 ? 19.67600  86.86700  39.79100 1.000 93.86647  ? 582 THR A CB    1 
ATOM 4828 O OG1   . THR B 2 582 ? 20.08100  86.91600  38.42800 1.000 107.48983 ? 582 THR A OG1   1 
ATOM 4829 C CG2   . THR B 2 582 ? 20.56100  85.90400  40.56000 1.000 90.88884  ? 582 THR A CG2   1 
ATOM 4830 N N     . VAL B 2 583 ? 17.51900  87.14200  41.96700 1.000 78.33174  ? 583 VAL A N     1 
ATOM 4831 C CA    . VAL B 2 583 ? 17.11000  86.88900  43.37900 1.000 90.48078  ? 583 VAL A CA    1 
ATOM 4832 C C     . VAL B 2 583 ? 15.63400  86.46700  43.38400 1.000 72.37880  ? 583 VAL A C     1 
ATOM 4833 O O     . VAL B 2 583 ? 15.25400  85.66200  44.25400 1.000 79.41748  ? 583 VAL A O     1 
ATOM 4834 C CB    . VAL B 2 583 ? 17.38100  88.09700  44.29500 1.000 74.17838  ? 583 VAL A CB    1 
ATOM 4835 C CG1   . VAL B 2 583 ? 16.77200  89.38200  43.75700 1.000 84.59216  ? 583 VAL A CG1   1 
ATOM 4836 C CG2   . VAL B 2 583 ? 16.95300  87.83700  45.73200 1.000 80.55616  ? 583 VAL A CG2   1 
ATOM 4837 N N     . LYS B 2 584 ? 14.84800  86.96100  42.42900 1.000 79.87611  ? 584 LYS A N     1 
ATOM 4838 C CA    . LYS B 2 584 ? 13.43400  86.52300  42.33300 1.000 78.41601  ? 584 LYS A CA    1 
ATOM 4839 C C     . LYS B 2 584 ? 13.43100  85.01600  42.06000 1.000 84.99335  ? 584 LYS A C     1 
ATOM 4840 O O     . LYS B 2 584 ? 12.61000  84.30200  42.66500 1.000 83.57256  ? 584 LYS A O     1 
ATOM 4841 C CB    . LYS B 2 584 ? 12.71900  87.30600  41.22900 1.000 72.27320  ? 584 LYS A CB    1 
ATOM 4842 C CG    . LYS B 2 584 ? 11.22100  87.08600  41.12200 1.000 91.18852  ? 584 LYS A CG    1 
ATOM 4843 C CD    . LYS B 2 584 ? 10.51600  88.25800  40.45200 1.000 102.71656 ? 584 LYS A CD    1 
ATOM 4844 C CE    . LYS B 2 584 ? 10.71300  89.53200  41.21100 1.000 88.74172  ? 584 LYS A CE    1 
ATOM 4845 N NZ    . LYS B 2 584 ? 9.95900   90.64000  40.62100 1.000 111.49103 ? 584 LYS A NZ    1 
ATOM 4846 N N     . SER B 2 585 ? 14.32800  84.55800  41.18800 1.000 83.33074  ? 585 SER A N     1 
ATOM 4847 C CA    . SER B 2 585 ? 14.43000  83.10900  40.89500 1.000 88.52534  ? 585 SER A CA    1 
ATOM 4848 C C     . SER B 2 585 ? 14.81300  82.37100  42.18000 1.000 86.35280  ? 585 SER A C     1 
ATOM 4849 O O     . SER B 2 585 ? 14.07400  81.45500  42.58500 1.000 85.28523  ? 585 SER A O     1 
ATOM 4850 C CB    . SER B 2 585 ? 15.43100  82.84800  39.81500 1.000 78.97571  ? 585 SER A CB    1 
ATOM 4851 O OG    . SER B 2 585 ? 15.65300  81.45400  39.66200 1.000 112.06051 ? 585 SER A OG    1 
ATOM 4852 N N     . LEU B 2 586 ? 15.93100  82.76100  42.78700 1.000 72.83093  ? 586 LEU A N     1 
ATOM 4853 C CA    . LEU B 2 586 ? 16.36700  82.10100  44.01400 1.000 77.61450  ? 586 LEU A CA    1 
ATOM 4854 C C     . LEU B 2 586 ? 15.24100  82.03900  45.03700 1.000 83.26049  ? 586 LEU A C     1 
ATOM 4855 O O     . LEU B 2 586 ? 15.06100  81.02200  45.71900 1.000 68.84949  ? 586 LEU A O     1 
ATOM 4856 C CB    . LEU B 2 586 ? 17.57600  82.83300  44.59600 1.000 76.32551  ? 586 LEU A CB    1 
ATOM 4857 C CG    . LEU B 2 586 ? 17.95400  82.48200  46.03700 1.000 71.18883  ? 586 LEU A CG    1 
ATOM 4858 C CD1   . LEU B 2 586 ? 18.73400  81.17500  46.10900 1.000 61.04879  ? 586 LEU A CD1   1 
ATOM 4859 C CD2   . LEU B 2 586 ? 18.73300  83.62000  46.66500 1.000 76.30961  ? 586 LEU A CD2   1 
ATOM 4860 N N     . ARG B 2 587 ? 14.46300  83.11900  45.14800 1.000 84.24706  ? 587 ARG A N     1 
ATOM 4861 C CA    . ARG B 2 587 ? 13.31900  83.11600  46.05400 1.000 80.40507  ? 587 ARG A CA    1 
ATOM 4862 C C     . ARG B 2 587 ? 12.29400  82.06600  45.64300 1.000 82.25951  ? 587 ARG A C     1 
ATOM 4863 O O     . ARG B 2 587 ? 11.75500  81.34500  46.49000 1.000 86.56181  ? 587 ARG A O     1 
ATOM 4864 C CB    . ARG B 2 587 ? 12.68400  84.50500  46.10000 1.000 83.84362  ? 587 ARG A CB    1 
ATOM 4865 C CG    . ARG B 2 587 ? 11.39100  84.55700  46.88700 1.000 94.27299  ? 587 ARG A CG    1 
ATOM 4866 C CD    . ARG B 2 587 ? 11.02900  85.98100  47.26500 1.000 104.94174 ? 587 ARG A CD    1 
ATOM 4867 N NE    . ARG B 2 587 ? 11.02800  86.88900  46.12000 1.000 123.00101 ? 587 ARG A NE    1 
ATOM 4868 C CZ    . ARG B 2 587 ? 10.05600  86.95900  45.21700 1.000 134.34036 ? 587 ARG A CZ    1 
ATOM 4869 N NH1   . ARG B 2 587 ? 9.00100   86.16000  45.31000 1.000 152.80119 ? 587 ARG A NH1   1 
ATOM 4870 N NH2   . ARG B 2 587 ? 10.14100  87.82500  44.21800 1.000 99.12420  ? 587 ARG A NH2   1 
ATOM 4871 N N     . LYS B 2 588 ? 12.01200  81.96100  44.34200 1.000 78.96696  ? 588 LYS A N     1 
ATOM 4872 C CA    . LYS B 2 588 ? 11.04100  80.97000  43.88200 1.000 86.47436  ? 588 LYS A CA    1 
ATOM 4873 C C     . LYS B 2 588 ? 11.50400  79.55300  44.20600 1.000 83.56275  ? 588 LYS A C     1 
ATOM 4874 O O     . LYS B 2 588 ? 10.73100  78.73500  44.72300 1.000 83.67387  ? 588 LYS A O     1 
ATOM 4875 C CB    . LYS B 2 588 ? 10.79500  81.13400  42.38300 1.000 66.99220  ? 588 LYS A CB    1 
ATOM 4876 C CG    . LYS B 2 588 ? 10.01200  79.99900  41.74800 1.000 75.17965  ? 588 LYS A CG    1 
ATOM 4877 C CD    . LYS B 2 588 ? 9.71400   80.30900  40.29200 1.000 86.67273  ? 588 LYS A CD    1 
ATOM 4878 C CE    . LYS B 2 588 ? 9.66300   79.04600  39.45200 1.000 81.31906  ? 588 LYS A CE    1 
ATOM 4879 N NZ    . LYS B 2 588 ? 9.51500   79.36300  38.00400 1.000 108.78783 ? 588 LYS A NZ    1 
ATOM 4880 N N     . GLN B 2 589 ? 12.77200  79.24900  43.92200 1.000 77.67356  ? 589 GLN A N     1 
ATOM 4881 C CA    . GLN B 2 589 ? 13.30000  77.91300  44.18500 1.000 74.31739  ? 589 GLN A CA    1 
ATOM 4882 C C     . GLN B 2 589 ? 13.28200  77.58900  45.67600 1.000 70.29626  ? 589 GLN A C     1 
ATOM 4883 O O     . GLN B 2 589 ? 12.79700  76.52600  46.09200 1.000 70.76849  ? 589 GLN A O     1 
ATOM 4884 C CB    . GLN B 2 589 ? 14.71900  77.80400  43.62900 1.000 80.79094  ? 589 GLN A CB    1 
ATOM 4885 C CG    . GLN B 2 589 ? 15.40100  76.49300  43.93800 1.000 76.25900  ? 589 GLN A CG    1 
ATOM 4886 C CD    . GLN B 2 589 ? 14.83200  75.34500  43.13400 1.000 103.67141 ? 589 GLN A CD    1 
ATOM 4887 O OE1   . GLN B 2 589 ? 14.12400  75.55300  42.14600 1.000 119.61169 ? 589 GLN A OE1   1 
ATOM 4888 N NE2   . GLN B 2 589 ? 15.13900  74.12100  43.55300 1.000 87.34641  ? 589 GLN A NE2   1 
ATOM 4889 N N     . LEU B 2 590 ? 13.82500  78.49400  46.49700 1.000 81.54410  ? 590 LEU A N     1 
ATOM 4890 C CA    . LEU B 2 590 ? 13.82600  78.27600  47.94100 1.000 75.36745  ? 590 LEU A CA    1 
ATOM 4891 C C     . LEU B 2 590 ? 12.41300  78.06200  48.46200 1.000 64.29040  ? 590 LEU A C     1 
ATOM 4892 O O     . LEU B 2 590 ? 12.16100  77.14400  49.25100 1.000 81.54116  ? 590 LEU A O     1 
ATOM 4893 C CB    . LEU B 2 590 ? 14.48200  79.45500  48.65900 1.000 89.25447  ? 590 LEU A CB    1 
ATOM 4894 C CG    . LEU B 2 590 ? 16.00800  79.52000  48.70100 1.000 84.31211  ? 590 LEU A CG    1 
ATOM 4895 C CD1   . LEU B 2 590 ? 16.44100  80.65100  49.61600 1.000 75.02909  ? 590 LEU A CD1   1 
ATOM 4896 C CD2   . LEU B 2 590 ? 16.59600  78.19600  49.16300 1.000 83.64655  ? 590 LEU A CD2   1 
ATOM 4897 N N     . LEU B 2 591 ? 11.47400  78.90600  48.02900 1.000 65.08067  ? 591 LEU A N     1 
ATOM 4898 C CA    . LEU B 2 591 ? 10.08500  78.72500  48.43200 1.000 73.72058  ? 591 LEU A CA    1 
ATOM 4899 C C     . LEU B 2 591 ? 9.56000   77.36200  48.00000 1.000 76.35533  ? 591 LEU A C     1 
ATOM 4900 O O     . LEU B 2 591 ? 8.75800   76.74700  48.71400 1.000 85.56526  ? 591 LEU A O     1 
ATOM 4901 C CB    . LEU B 2 591 ? 9.22300   79.84700  47.84800 1.000 76.50325  ? 591 LEU A CB    1 
ATOM 4902 C CG    . LEU B 2 591 ? 7.83600   80.05100  48.45600 1.000 96.37382  ? 591 LEU A CG    1 
ATOM 4903 C CD1   . LEU B 2 591 ? 7.93500   80.48900  49.91300 1.000 93.93820  ? 591 LEU A CD1   1 
ATOM 4904 C CD2   . LEU B 2 591 ? 7.05200   81.06300  47.64200 1.000 82.25063  ? 591 LEU A CD2   1 
ATOM 4905 N N     . TYR B 2 592 ? 10.02500  76.86500  46.85100 1.000 70.37018  ? 592 TYR A N     1 
ATOM 4906 C CA    . TYR B 2 592 ? 9.59300   75.56000  46.36200 1.000 66.46519  ? 592 TYR A CA    1 
ATOM 4907 C C     . TYR B 2 592 ? 10.03900  74.44300  47.30200 1.000 69.52444  ? 592 TYR A C     1 
ATOM 4908 O O     . TYR B 2 592 ? 9.23100   73.60100  47.71500 1.000 86.14238  ? 592 TYR A O     1 
ATOM 4909 C CB    . TYR B 2 592 ? 10.13900  75.35000  44.95000 1.000 73.14405  ? 592 TYR A CB    1 
ATOM 4910 C CG    . TYR B 2 592 ? 9.69400   74.08300  44.27500 1.000 62.43422  ? 592 TYR A CG    1 
ATOM 4911 C CD1   . TYR B 2 592 ? 8.42700   73.97700  43.72500 1.000 79.02138  ? 592 TYR A CD1   1 
ATOM 4912 C CD2   . TYR B 2 592 ? 10.55300  73.00300  44.16000 1.000 80.21559  ? 592 TYR A CD2   1 
ATOM 4913 C CE1   . TYR B 2 592 ? 8.01900   72.82400  43.09800 1.000 87.81945  ? 592 TYR A CE1   1 
ATOM 4914 C CE2   . TYR B 2 592 ? 10.15700  71.84800  43.53300 1.000 89.19872  ? 592 TYR A CE2   1 
ATOM 4915 C CZ    . TYR B 2 592 ? 8.88600   71.76200  43.00400 1.000 88.44056  ? 592 TYR A CZ    1 
ATOM 4916 O OH    . TYR B 2 592 ? 8.48700   70.60400  42.37800 1.000 90.44807  ? 592 TYR A OH    1 
ATOM 4917 N N     . LEU B 2 593 ? 11.33000  74.42100  47.65000 1.000 73.51468  ? 593 LEU A N     1 
ATOM 4918 C CA    . LEU B 2 593 ? 11.81700  73.48100  48.66100 1.000 63.53625  ? 593 LEU A CA    1 
ATOM 4919 C C     . LEU B 2 593 ? 11.02100  73.60400  49.95900 1.000 64.90600  ? 593 LEU A C     1 
ATOM 4920 O O     . LEU B 2 593 ? 10.59000  72.59900  50.55000 1.000 66.38473  ? 593 LEU A O     1 
ATOM 4921 C CB    . LEU B 2 593 ? 13.30400  73.73800  48.92400 1.000 83.19575  ? 593 LEU A CB    1 
ATOM 4922 C CG    . LEU B 2 593 ? 14.33200  72.68200  48.51500 1.000 74.12992  ? 593 LEU A CG    1 
ATOM 4923 C CD1   . LEU B 2 593 ? 15.72200  73.08300  48.99000 1.000 68.71122  ? 593 LEU A CD1   1 
ATOM 4924 C CD2   . LEU B 2 593 ? 13.94900  71.32700  49.08300 1.000 65.56942  ? 593 LEU A CD2   1 
ATOM 4925 N N     . LYS B 2 594 ? 10.81600  74.84500  50.41100 1.000 70.91797  ? 594 LYS A N     1 
ATOM 4926 C CA    . LYS B 2 594 ? 10.10500  75.07800  51.66100 1.000 69.63404  ? 594 LYS A CA    1 
ATOM 4927 C C     . LYS B 2 594 ? 8.71500   74.46600  51.62400 1.000 68.71418  ? 594 LYS A C     1 
ATOM 4928 O O     . LYS B 2 594 ? 8.24900   73.91600  52.62400 1.000 77.88874  ? 594 LYS A O     1 
ATOM 4929 C CB    . LYS B 2 594 ? 10.02000  76.57700  51.95500 1.000 73.78382  ? 594 LYS A CB    1 
ATOM 4930 C CG    . LYS B 2 594 ? 9.10800   76.92300  53.12300 1.000 61.76739  ? 594 LYS A CG    1 
ATOM 4931 C CD    . LYS B 2 594 ? 8.14400   78.04000  52.75600 1.000 77.89755  ? 594 LYS A CD    1 
ATOM 4932 C CE    . LYS B 2 594 ? 7.15000   78.30800  53.87600 1.000 94.51543  ? 594 LYS A CE    1 
ATOM 4933 N NZ    . LYS B 2 594 ? 6.32500   79.52600  53.62000 1.000 109.44487 ? 594 LYS A NZ    1 
ATOM 4934 N N     . ASP B 2 595 ? 8.04200   74.53700  50.47700 1.000 73.63554  ? 595 ASP A N     1 
ATOM 4935 C CA    . ASP B 2 595 ? 6.72300   73.92500  50.38100 1.000 74.52831  ? 595 ASP A CA    1 
ATOM 4936 C C     . ASP B 2 595 ? 6.80200   72.40600  50.29000 1.000 73.19879  ? 595 ASP A C     1 
ATOM 4937 O O     . ASP B 2 595 ? 5.91000   71.71500  50.79900 1.000 87.65517  ? 595 ASP A O     1 
ATOM 4938 C CB    . ASP B 2 595 ? 5.96400   74.49900  49.18700 1.000 61.66161  ? 595 ASP A CB    1 
ATOM 4939 C CG    . ASP B 2 595 ? 5.70300   75.98100  49.33400 1.000 93.45841  ? 595 ASP A CG    1 
ATOM 4940 O OD1   . ASP B 2 595 ? 5.70200   76.46600  50.48900 1.000 102.94735 ? 595 ASP A OD1   1 
ATOM 4941 O OD2   . ASP B 2 595 ? 5.50500   76.66300  48.30400 1.000 113.89169 ? 595 ASP A OD2   1 
ATOM 4942 N N     . LYS B 2 596 ? 7.85000   71.86500  49.65900 1.000 72.29505  ? 596 LYS A N     1 
ATOM 4943 C CA    . LYS B 2 596 ? 8.01200   70.41400  49.65700 1.000 81.84088  ? 596 LYS A CA    1 
ATOM 4944 C C     . LYS B 2 596 ? 8.14600   69.86500  51.07000 1.000 82.97581  ? 596 LYS A C     1 
ATOM 4945 O O     . LYS B 2 596 ? 7.69900   68.74500  51.34200 1.000 85.72699  ? 596 LYS A O     1 
ATOM 4946 C CB    . LYS B 2 596 ? 9.22100   70.00000  48.81900 1.000 90.46670  ? 596 LYS A CB    1 
ATOM 4947 C CG    . LYS B 2 596 ? 8.90400   69.76100  47.35400 1.000 90.27398  ? 596 LYS A CG    1 
ATOM 4948 C CD    . LYS B 2 596 ? 10.02900  69.00000  46.68000 1.000 95.20476  ? 596 LYS A CD    1 
ATOM 4949 C CE    . LYS B 2 596 ? 9.80300   68.87900  45.18300 1.000 107.66642 ? 596 LYS A CE    1 
ATOM 4950 N NZ    . LYS B 2 596 ? 8.57500   68.10900  44.84300 1.000 112.66683 ? 596 LYS A NZ    1 
ATOM 4951 N N     . PHE B 2 597 ? 8.75500   70.62600  51.98400 1.000 81.00823  ? 597 PHE A N     1 
ATOM 4952 C CA    . PHE B 2 597 ? 8.79300   70.16000  53.37100 1.000 62.67755  ? 597 PHE A CA    1 
ATOM 4953 C C     . PHE B 2 597 ? 7.50300   70.49900  54.11600 1.000 66.34699  ? 597 PHE A C     1 
ATOM 4954 O O     . PHE B 2 597 ? 6.93900   69.65300  54.82600 1.000 78.02252  ? 597 PHE A O     1 
ATOM 4955 C CB    . PHE B 2 597 ? 9.99600   70.75700  54.10000 1.000 72.76434  ? 597 PHE A CB    1 
ATOM 4956 C CG    . PHE B 2 597 ? 11.30900  70.14400  53.71100 1.000 64.79108  ? 597 PHE A CG    1 
ATOM 4957 C CD1   . PHE B 2 597 ? 11.57600  68.81200  53.98100 1.000 79.64898  ? 597 PHE A CD1   1 
ATOM 4958 C CD2   . PHE B 2 597 ? 12.28700  70.90600  53.09700 1.000 54.61012  ? 597 PHE A CD2   1 
ATOM 4959 C CE1   . PHE B 2 597 ? 12.79200  68.24900  53.63200 1.000 71.68107  ? 597 PHE A CE1   1 
ATOM 4960 C CE2   . PHE B 2 597 ? 13.50300  70.34900  52.74700 1.000 66.94790  ? 597 PHE A CE2   1 
ATOM 4961 C CZ    . PHE B 2 597 ? 13.75500  69.01800  53.01300 1.000 60.78624  ? 597 PHE A CZ    1 
ATOM 4962 N N     . LYS B 2 598 ? 7.02200   71.73400  53.95800 1.000 64.27815  ? 598 LYS A N     1 
ATOM 4963 C CA    . LYS B 2 598 ? 5.88800   72.21600  54.73800 1.000 64.69359  ? 598 LYS A CA    1 
ATOM 4964 C C     . LYS B 2 598 ? 4.62000   71.43100  54.43500 1.000 62.36686  ? 598 LYS A C     1 
ATOM 4965 O O     . LYS B 2 598 ? 3.75500   71.30400  55.30400 1.000 65.27863  ? 598 LYS A O     1 
ATOM 4966 C CB    . LYS B 2 598 ? 5.66800   73.70700  54.47400 1.000 58.73795  ? 598 LYS A CB    1 
ATOM 4967 C CG    . LYS B 2 598 ? 4.82100   74.43300  55.51300 1.000 74.32685  ? 598 LYS A CG    1 
ATOM 4968 C CD    . LYS B 2 598 ? 4.35100   75.78100  54.97300 1.000 98.80109  ? 598 LYS A CD    1 
ATOM 4969 C CE    . LYS B 2 598 ? 3.75900   76.66400  56.06500 1.000 120.91947 ? 598 LYS A CE    1 
ATOM 4970 N NZ    . LYS B 2 598 ? 4.73600   77.68500  56.55100 1.000 139.09501 ? 598 LYS A NZ    1 
ATOM 4971 N N     . ASN B 2 599 ? 4.49000   70.89300  53.22100 1.000 57.64232  ? 599 ASN A N     1 
ATOM 4972 C CA    . ASN B 2 599 ? 3.30800   70.09800  52.90000 1.000 50.71965  ? 599 ASN A CA    1 
ATOM 4973 C C     . ASN B 2 599 ? 3.28500   68.80000  53.69800 1.000 60.85925  ? 599 ASN A C     1 
ATOM 4974 O O     . ASN B 2 599 ? 2.27400   68.46500  54.32800 1.000 65.89411  ? 599 ASN A O     1 
ATOM 4975 C CB    . ASN B 2 599 ? 3.25400   69.81400  51.40100 1.000 56.00508  ? 599 ASN A CB    1 
ATOM 4976 C CG    . ASN B 2 599 ? 2.84800   71.02900  50.59700 1.000 60.44599  ? 599 ASN A CG    1 
ATOM 4977 O OD1   . ASN B 2 599 ? 2.11000   71.88900  51.08000 1.000 62.30382  ? 599 ASN A OD1   1 
ATOM 4978 N ND2   . ASN B 2 599 ? 3.33100   71.11100  49.36400 1.000 59.40445  ? 599 ASN A ND2   1 
ATOM 4979 N N     . ILE B 2 600 ? 4.39100   68.05200  53.68000 1.000 56.56650  ? 600 ILE A N     1 
ATOM 4980 C CA    . ILE B 2 600 ? 4.45900   66.82100  54.46100 1.000 49.88616  ? 600 ILE A CA    1 
ATOM 4981 C C     . ILE B 2 600 ? 4.28500   67.12300  55.94200 1.000 63.75889  ? 600 ILE A C     1 
ATOM 4982 O O     . ILE B 2 600 ? 3.60900   66.37900  56.66800 1.000 56.96322  ? 600 ILE A O     1 
ATOM 4983 C CB    . ILE B 2 600 ? 5.77900   66.07600  54.19000 1.000 49.55717  ? 600 ILE A CB    1 
ATOM 4984 C CG1   . ILE B 2 600 ? 5.91000   65.74000  52.70400 1.000 52.79528  ? 600 ILE A CG1   1 
ATOM 4985 C CG2   . ILE B 2 600 ? 5.85500   64.80700  55.03100 1.000 54.01014  ? 600 ILE A CG2   1 
ATOM 4986 C CD1   . ILE B 2 600 ? 4.86600   64.77200  52.19500 1.000 56.97708  ? 600 ILE A CD1   1 
ATOM 4987 N N     . GLU B 2 601 ? 4.88000   68.22200  56.41700 1.000 67.62179  ? 601 GLU A N     1 
ATOM 4988 C CA    . GLU B 2 601 ? 4.69600   68.58800  57.81800 1.000 66.26813  ? 601 GLU A CA    1 
ATOM 4989 C C     . GLU B 2 601 ? 3.22500   68.83900  58.12400 1.000 64.38824  ? 601 GLU A C     1 
ATOM 4990 O O     . GLU B 2 601 ? 2.70500   68.37700  59.14500 1.000 68.24409  ? 601 GLU A O     1 
ATOM 4991 C CB    . GLU B 2 601 ? 5.53000   69.81600  58.17300 1.000 60.02492  ? 601 GLU A CB    1 
ATOM 4992 C CG    . GLU B 2 601 ? 5.62700   70.04000  59.67400 1.000 69.33184  ? 601 GLU A CG    1 
ATOM 4993 C CD    . GLU B 2 601 ? 5.73200   71.50000  60.04700 1.000 79.11985  ? 601 GLU A CD    1 
ATOM 4994 O OE1   . GLU B 2 601 ? 5.21100   72.34600  59.28800 1.000 103.02212 ? 601 GLU A OE1   1 
ATOM 4995 O OE2   . GLU B 2 601 ? 6.33700   71.80500  61.10100 1.000 93.52416  ? 601 GLU A OE2   1 
ATOM 4996 N N     . GLN B 2 602 ? 2.53600   69.56700  57.24100 1.000 59.96064  ? 602 GLN A N     1 
ATOM 4997 C CA    . GLN B 2 602 ? 1.11300   69.82500  57.43400 1.000 57.43199  ? 602 GLN A CA    1 
ATOM 4998 C C     . GLN B 2 602 ? 0.31800   68.52700  57.47200 1.000 69.79993  ? 602 GLN A C     1 
ATOM 4999 O O     . GLN B 2 602 ? -0.59300  68.37200  58.29400 1.000 72.76648  ? 602 GLN A O     1 
ATOM 5000 C CB    . GLN B 2 602 ? 0.59000   70.73500  56.32500 1.000 59.74145  ? 602 GLN A CB    1 
ATOM 5001 C CG    . GLN B 2 602 ? 1.04900   72.17500  56.42400 1.000 81.04406  ? 602 GLN A CG    1 
ATOM 5002 C CD    . GLN B 2 602 ? 0.01300   73.07300  57.06200 1.000 117.44424 ? 602 GLN A CD    1 
ATOM 5003 O OE1   . GLN B 2 602 ? -0.22300  73.01000  58.26900 1.000 117.76052 ? 602 GLN A OE1   1 
ATOM 5004 N NE2   . GLN B 2 602 ? -0.61700  73.91600  56.24900 1.000 123.63600 ? 602 GLN A NE2   1 
ATOM 5005 N N     . SER B 2 603 ? 0.65100   67.57900  56.59300 1.000 60.47302  ? 603 SER A N     1 
ATOM 5006 C CA    . SER B 2 603 ? -0.09200  66.32500  56.55200 1.000 52.35118  ? 603 SER A CA    1 
ATOM 5007 C C     . SER B 2 603 ? 0.11800   65.51300  57.82400 1.000 59.94729  ? 603 SER A C     1 
ATOM 5008 O O     . SER B 2 603 ? -0.83500  64.93900  58.36100 1.000 73.17892  ? 603 SER A O     1 
ATOM 5009 C CB    . SER B 2 603 ? 0.30600   65.51800  55.32000 1.000 63.91555  ? 603 SER A CB    1 
ATOM 5010 O OG    . SER B 2 603 ? -0.24500  66.08800  54.14700 1.000 67.99342  ? 603 SER A OG    1 
ATOM 5011 N N     . LEU B 2 604 ? 1.35300   65.45000  58.32700 1.000 61.04400  ? 604 LEU A N     1 
ATOM 5012 C CA    . LEU B 2 604 ? 1.58000   64.73600  59.58100 1.000 51.46488  ? 604 LEU A CA    1 
ATOM 5013 C C     . LEU B 2 604 ? 0.90100   65.44400  60.74900 1.000 54.35607  ? 604 LEU A C     1 
ATOM 5014 O O     . LEU B 2 604 ? 0.32900   64.79000  61.62800 1.000 72.65214  ? 604 LEU A O     1 
ATOM 5015 C CB    . LEU B 2 604 ? 3.07800   64.57900  59.83900 1.000 54.01532  ? 604 LEU A CB    1 
ATOM 5016 C CG    . LEU B 2 604 ? 3.86300   63.77500  58.79700 1.000 56.17115  ? 604 LEU A CG    1 
ATOM 5017 C CD1   . LEU B 2 604 ? 5.34900   63.83000  59.09800 1.000 60.62738  ? 604 LEU A CD1   1 
ATOM 5018 C CD2   . LEU B 2 604 ? 3.37900   62.33900  58.74200 1.000 52.35410  ? 604 LEU A CD2   1 
ATOM 5019 N N     . LYS B 2 605 ? 0.94200   66.77900  60.77400 1.000 57.47272  ? 605 LYS A N     1 
ATOM 5020 C CA    . LYS B 2 605 ? 0.24300   67.52200  61.81700 1.000 61.23576  ? 605 LYS A CA    1 
ATOM 5021 C C     . LYS B 2 605 ? -1.26700  67.36500  61.71400 1.000 71.97351  ? 605 LYS A C     1 
ATOM 5022 O O     . LYS B 2 605 ? -1.96800  67.54300  62.71600 1.000 67.95770  ? 605 LYS A O     1 
ATOM 5023 C CB    . LYS B 2 605 ? 0.60700   69.00800  61.75500 1.000 59.49712  ? 605 LYS A CB    1 
ATOM 5024 C CG    . LYS B 2 605 ? 2.03800   69.33600  62.14400 1.000 61.35585  ? 605 LYS A CG    1 
ATOM 5025 C CD    . LYS B 2 605 ? 2.32800   70.81700  61.93500 1.000 69.21162  ? 605 LYS A CD    1 
ATOM 5026 C CE    . LYS B 2 605 ? 1.45800   71.68700  62.82800 1.000 85.99180  ? 605 LYS A CE    1 
ATOM 5027 N NZ    . LYS B 2 605 ? 1.46700   73.11700  62.39700 1.000 104.45825 ? 605 LYS A NZ    1 
ATOM 5028 N N     . ALA B 2 606 ? -1.78300  67.04200  60.52900 1.000 59.50363  ? 606 ALA A N     1 
ATOM 5029 C CA    . ALA B 2 606 ? -3.21200  66.83300  60.34200 1.000 54.99780  ? 606 ALA A CA    1 
ATOM 5030 C C     . ALA B 2 606 ? -3.66500  65.43800  60.74900 1.000 66.97036  ? 606 ALA A C     1 
ATOM 5031 O O     . ALA B 2 606 ? -4.85600  65.13200  60.62700 1.000 58.81210  ? 606 ALA A O     1 
ATOM 5032 C CB    . ALA B 2 606 ? -3.59300  67.09500  58.88300 1.000 56.43978  ? 606 ALA A CB    1 
ATOM 5033 N N     . GLY B 2 607 ? -2.75600  64.59100  61.22700 1.000 65.48954  ? 607 GLY A N     1 
ATOM 5034 C CA    . GLY B 2 607 ? -3.10400  63.23700  61.60000 1.000 64.34384  ? 607 GLY A CA    1 
ATOM 5035 C C     . GLY B 2 607 ? -3.26800  62.27700  60.44600 1.000 69.31531  ? 607 GLY A C     1 
ATOM 5036 O O     . GLY B 2 607 ? -3.81400  61.18400  60.64500 1.000 66.58578  ? 607 GLY A O     1 
ATOM 5037 N N     . HIS B 2 608 ? -2.81000  62.64400  59.25100 1.000 56.57493  ? 608 HIS A N     1 
ATOM 5038 C CA    . HIS B 2 608 ? -2.97400  61.78700  58.08600 1.000 59.62520  ? 608 HIS A CA    1 
ATOM 5039 C C     . HIS B 2 608 ? -2.18700  60.49100  58.24500 1.000 60.28954  ? 608 HIS A C     1 
ATOM 5040 O O     . HIS B 2 608 ? -1.15300  60.44000  58.91700 1.000 53.67366  ? 608 HIS A O     1 
ATOM 5041 C CB    . HIS B 2 608 ? -2.51900  62.51600  56.82200 1.000 58.95260  ? 608 HIS A CB    1 
ATOM 5042 C CG    . HIS B 2 608 ? -3.41200  63.64800  56.42100 1.000 73.53705  ? 608 HIS A CG    1 
ATOM 5043 N ND1   . HIS B 2 608 ? -3.31100  64.28000  55.19900 1.000 70.62117  ? 608 HIS A ND1   1 
ATOM 5044 C CD2   . HIS B 2 608 ? -4.42600  64.25900  57.07800 1.000 51.84397  ? 608 HIS A CD2   1 
ATOM 5045 C CE1   . HIS B 2 608 ? -4.22500  65.23100  55.12200 1.000 72.11215  ? 608 HIS A CE1   1 
ATOM 5046 N NE2   . HIS B 2 608 ? -4.91300  65.24200  56.25000 1.000 56.67884  ? 608 HIS A NE2   1 
ATOM 5047 N N     . THR B 2 609 ? -2.69700  59.43500  57.61700 1.000 58.50854  ? 609 THR A N     1 
ATOM 5048 C CA    . THR B 2 609 ? -1.98300  58.16700  57.56500 1.000 57.06919  ? 609 THR A CA    1 
ATOM 5049 C C     . THR B 2 609 ? -0.69400  58.32400  56.76600 1.000 64.63359  ? 609 THR A C     1 
ATOM 5050 O O     . THR B 2 609 ? -0.67900  58.92900  55.69100 1.000 62.58598  ? 609 THR A O     1 
ATOM 5051 C CB    . THR B 2 609 ? -2.86500  57.08400  56.93900 1.000 56.28886  ? 609 THR A CB    1 
ATOM 5052 O OG1   . THR B 2 609 ? -4.03700  56.89500  57.74100 1.000 70.97648  ? 609 THR A OG1   1 
ATOM 5053 C CG2   . THR B 2 609 ? -2.11500  55.76100  56.83300 1.000 58.97761  ? 609 THR A CG2   1 
ATOM 5054 N N     . SER B 2 610 ? 0.39400   57.77700  57.30400 1.000 78.62744  ? 610 SER A N     1 
ATOM 5055 C CA    . SER B 2 610 ? 1.70600   57.88300  56.68800 1.000 68.04416  ? 610 SER A CA    1 
ATOM 5056 C C     . SER B 2 610 ? 2.44100   56.55900  56.84100 1.000 60.76837  ? 610 SER A C     1 
ATOM 5057 O O     . SER B 2 610 ? 2.10500   55.73400  57.69400 1.000 74.96398  ? 610 SER A O     1 
ATOM 5058 C CB    . SER B 2 610 ? 2.52900   59.01700  57.31400 1.000 62.36394  ? 610 SER A CB    1 
ATOM 5059 O OG    . SER B 2 610 ? 2.78700   58.76000  58.68200 1.000 83.41834  ? 610 SER A OG    1 
ATOM 5060 N N     . PHE B 2 611 ? 3.45300   56.36500  55.99600 1.000 65.31604  ? 611 PHE A N     1 
ATOM 5061 C CA    . PHE B 2 611 ? 4.31200   55.19200  56.08700 1.000 53.28434  ? 611 PHE A CA    1 
ATOM 5062 C C     . PHE B 2 611 ? 5.62900   55.49900  55.39100 1.000 65.02131  ? 611 PHE A C     1 
ATOM 5063 O O     . PHE B 2 611 ? 5.71800   56.41600  54.57000 1.000 63.75453  ? 611 PHE A O     1 
ATOM 5064 C CB    . PHE B 2 611 ? 3.65100   53.94300  55.48400 1.000 54.48684  ? 611 PHE A CB    1 
ATOM 5065 C CG    . PHE B 2 611 ? 3.44500   54.00800  53.99500 1.000 59.93171  ? 611 PHE A CG    1 
ATOM 5066 C CD1   . PHE B 2 611 ? 2.31500   54.60800  53.46500 1.000 50.63643  ? 611 PHE A CD1   1 
ATOM 5067 C CD2   . PHE B 2 611 ? 4.36700   53.44500  53.12700 1.000 53.75886  ? 611 PHE A CD2   1 
ATOM 5068 C CE1   . PHE B 2 611 ? 2.11600   54.66100  52.09600 1.000 57.26443  ? 611 PHE A CE1   1 
ATOM 5069 C CE2   . PHE B 2 611 ? 4.17500   53.49600  51.75700 1.000 59.86168  ? 611 PHE A CE2   1 
ATOM 5070 C CZ    . PHE B 2 611 ? 3.04800   54.10600  51.24000 1.000 66.18880  ? 611 PHE A CZ    1 
ATOM 5071 N N     . ILE B 2 612 ? 6.65100   54.71700  55.73100 1.000 72.08983  ? 612 ILE A N     1 
ATOM 5072 C CA    . ILE B 2 612 ? 8.00900   54.92000  55.23900 1.000 56.09853  ? 612 ILE A CA    1 
ATOM 5073 C C     . ILE B 2 612 ? 8.35500   53.81000  54.26000 1.000 54.57057  ? 612 ILE A C     1 
ATOM 5074 O O     . ILE B 2 612 ? 8.11800   52.63000  54.53400 1.000 59.25548  ? 612 ILE A O     1 
ATOM 5075 C CB    . ILE B 2 612 ? 9.03300   54.94700  56.38900 1.000 61.77120  ? 612 ILE A CB    1 
ATOM 5076 C CG1   . ILE B 2 612 ? 8.64300   55.99100  57.43400 1.000 50.69797  ? 612 ILE A CG1   1 
ATOM 5077 C CG2   . ILE B 2 612 ? 10.43200  55.20100  55.84800 1.000 52.45900  ? 612 ILE A CG2   1 
ATOM 5078 C CD1   . ILE B 2 612 ? 9.38500   55.83100  58.73800 1.000 52.19170  ? 612 ILE A CD1   1 
ATOM 5079 N N     . SER B 2 613 ? 8.92900   54.18700  53.12700 1.000 66.80936  ? 613 SER A N     1 
ATOM 5080 C CA    . SER B 2 613 ? 9.44300   53.23600  52.15600 1.000 69.39687  ? 613 SER A CA    1 
ATOM 5081 C C     . SER B 2 613 ? 10.95500  53.38000  52.07500 1.000 64.31317  ? 613 SER A C     1 
ATOM 5082 O O     . SER B 2 613 ? 11.48500  54.48800  52.18200 1.000 82.14854  ? 613 SER A O     1 
ATOM 5083 C CB    . SER B 2 613 ? 8.80900   53.46200  50.78100 1.000 77.05175  ? 613 SER A CB    1 
ATOM 5084 O OG    . SER B 2 613 ? 9.37800   52.60500  49.80800 1.000 80.97412  ? 613 SER A OG    1 
ATOM 5085 N N     . ILE B 2 614 ? 11.65300  52.26100  51.91400 1.000 71.68863  ? 614 ILE A N     1 
ATOM 5086 C CA    . ILE B 2 614 ? 13.09500  52.27600  51.70000 1.000 65.48839  ? 614 ILE A CA    1 
ATOM 5087 C C     . ILE B 2 614 ? 13.43200  51.18200  50.69600 1.000 67.72170  ? 614 ILE A C     1 
ATOM 5088 O O     . ILE B 2 614 ? 12.94700  50.05100  50.80800 1.000 71.00303  ? 614 ILE A O     1 
ATOM 5089 C CB    . ILE B 2 614 ? 13.88400  52.11800  53.02100 1.000 56.31634  ? 614 ILE A CB    1 
ATOM 5090 C CG1   . ILE B 2 614 ? 15.37700  52.38000  52.79700 1.000 60.46648  ? 614 ILE A CG1   1 
ATOM 5091 C CG2   . ILE B 2 614 ? 13.65100  50.75500  53.66700 1.000 66.02051  ? 614 ILE A CG2   1 
ATOM 5092 C CD1   . ILE B 2 614 ? 16.19200  52.43700  54.07700 1.000 63.53414  ? 614 ILE A CD1   1 
ATOM 5093 N N     . LYS B 2 615 ? 14.22800  51.53600  49.68400 1.000 73.52102  ? 615 LYS A N     1 
ATOM 5094 C CA    . LYS B 2 615 ? 14.51800  50.61000  48.59500 1.000 84.78997  ? 615 LYS A CA    1 
ATOM 5095 C C     . LYS B 2 615 ? 15.67500  49.68000  48.94200 1.000 82.00637  ? 615 LYS A C     1 
ATOM 5096 O O     . LYS B 2 615 ? 15.66400  48.50300  48.56900 1.000 85.52971  ? 615 LYS A O     1 
ATOM 5097 C CB    . LYS B 2 615 ? 14.81600  51.39800  47.31700 1.000 87.19882  ? 615 LYS A CB    1 
ATOM 5098 C CG    . LYS B 2 615 ? 15.13700  50.55900  46.09200 1.000 90.07673  ? 615 LYS A CG    1 
ATOM 5099 C CD    . LYS B 2 615 ? 15.28900  51.44600  44.86200 1.000 126.89260 ? 615 LYS A CD    1 
ATOM 5100 C CE    . LYS B 2 615 ? 15.77900  50.66000  43.65600 1.000 141.78647 ? 615 LYS A CE    1 
ATOM 5101 N NZ    . LYS B 2 615 ? 15.86300  51.51700  42.44000 1.000 126.08448 ? 615 LYS A NZ    1 
ATOM 5102 N N     . ASN B 2 616 ? 16.67300  50.18800  49.66000 1.000 80.07415  ? 616 ASN A N     1 
ATOM 5103 C CA    . ASN B 2 616 ? 17.82500  49.40600  50.09200 1.000 81.01997  ? 616 ASN A CA    1 
ATOM 5104 C C     . ASN B 2 616 ? 18.01900  49.64900  51.58100 1.000 78.49919  ? 616 ASN A C     1 
ATOM 5105 O O     . ASN B 2 616 ? 18.26700  50.78600  51.99600 1.000 80.88778  ? 616 ASN A O     1 
ATOM 5106 C CB    . ASN B 2 616 ? 19.08100  49.79800  49.30400 1.000 99.90094  ? 616 ASN A CB    1 
ATOM 5107 C CG    . ASN B 2 616 ? 20.20800  48.79200  49.45300 1.000 118.19559 ? 616 ASN A CG    1 
ATOM 5108 O OD1   . ASN B 2 616 ? 20.19100  47.94500  50.34700 1.000 119.86028 ? 616 ASN A OD1   1 
ATOM 5109 N ND2   . ASN B 2 616 ? 21.20100  48.88700  48.57600 1.000 122.14003 ? 616 ASN A ND2   1 
ATOM 5110 N N     . LEU B 2 617 ? 17.92300  48.58300  52.38000 1.000 69.51949  ? 617 LEU A N     1 
ATOM 5111 C CA    . LEU B 2 617 ? 17.91100  48.71600  53.83500 1.000 76.52279  ? 617 LEU A CA    1 
ATOM 5112 C C     . LEU B 2 617 ? 19.21900  49.25700  54.40000 1.000 73.32403  ? 617 LEU A C     1 
ATOM 5113 O O     . LEU B 2 617 ? 19.35200  49.41700  55.61800 1.000 69.18740  ? 617 LEU A O     1 
ATOM 5114 C CB    . LEU B 2 617 ? 17.59900  47.37300  54.49200 1.000 63.88205  ? 617 LEU A CB    1 
ATOM 5115 C CG    . LEU B 2 617 ? 16.14500  47.19100  54.91600 1.000 81.55306  ? 617 LEU A CG    1 
ATOM 5116 C CD1   . LEU B 2 617 ? 15.25000  47.22500  53.69600 1.000 103.65654 ? 617 LEU A CD1   1 
ATOM 5117 C CD2   . LEU B 2 617 ? 15.96600  45.89600  55.68200 1.000 82.66274  ? 617 LEU A CD2   1 
ATOM 5118 N N     . SER B 2 618 ? 20.18800  49.53800  53.52700 1.000 84.16133  ? 618 SER A N     1 
ATOM 5119 C CA    . SER B 2 618 ? 21.48400  50.05300  53.93800 1.000 88.52615  ? 618 SER A CA    1 
ATOM 5120 C C     . SER B 2 618 ? 21.72100  51.49800  53.53700 1.000 89.35389  ? 618 SER A C     1 
ATOM 5121 O O     . SER B 2 618 ? 22.57500  52.15600  54.14100 1.000 94.29515  ? 618 SER A O     1 
ATOM 5122 C CB    . SER B 2 618 ? 22.60500  49.19300  53.34300 1.000 87.14036  ? 618 SER A CB    1 
ATOM 5123 O OG    . SER B 2 618 ? 22.46700  49.10700  51.93300 1.000 98.93646  ? 618 SER A OG    1 
ATOM 5124 N N     . GLN B 2 619 ? 20.99900  52.00500  52.54600 1.000 97.81686  ? 619 GLN A N     1 
ATOM 5125 C CA    . GLN B 2 619 ? 21.23800  53.33200  51.99000 1.000 99.85984  ? 619 GLN A CA    1 
ATOM 5126 C C     . GLN B 2 619 ? 20.06800  54.23300  52.36500 1.000 85.63739  ? 619 GLN A C     1 
ATOM 5127 O O     . GLN B 2 619 ? 18.99000  54.14100  51.77000 1.000 81.61834  ? 619 GLN A O     1 
ATOM 5128 C CB    . GLN B 2 619 ? 21.41400  53.25500  50.47800 1.000 90.36799  ? 619 GLN A CB    1 
ATOM 5129 C CG    . GLN B 2 619 ? 22.31400  52.12300  50.02900 1.000 93.47667  ? 619 GLN A CG    1 
ATOM 5130 C CD    . GLN B 2 619 ? 22.57200  52.14800  48.54000 1.000 111.28878 ? 619 GLN A CD    1 
ATOM 5131 O OE1   . GLN B 2 619 ? 21.71300  52.55200  47.75400 1.000 106.84361 ? 619 GLN A OE1   1 
ATOM 5132 N NE2   . GLN B 2 619 ? 23.76800  51.72500  48.14100 1.000 135.62699 ? 619 GLN A NE2   1 
ATOM 5133 N N     . LYS B 2 620 ? 20.28800  55.11300  53.34600 1.000 80.30501  ? 620 LYS A N     1 
ATOM 5134 C CA    . LYS B 2 620 ? 19.26800  56.09100  53.70600 1.000 76.68685  ? 620 LYS A CA    1 
ATOM 5135 C C     . LYS B 2 620 ? 18.86900  56.96900  52.52900 1.000 78.35254  ? 620 LYS A C     1 
ATOM 5136 O O     . LYS B 2 620 ? 17.82700  57.63000  52.59500 1.000 78.39756  ? 620 LYS A O     1 
ATOM 5137 C CB    . LYS B 2 620 ? 19.75900  56.97300  54.85800 1.000 71.90682  ? 620 LYS A CB    1 
ATOM 5138 C CG    . LYS B 2 620 ? 20.60800  58.14700  54.40400 1.000 74.86038  ? 620 LYS A CG    1 
ATOM 5139 C CD    . LYS B 2 620 ? 20.71700  59.21600  55.47800 1.000 76.68856  ? 620 LYS A CD    1 
ATOM 5140 C CE    . LYS B 2 620 ? 21.92000  59.00000  56.37700 1.000 77.84294  ? 620 LYS A CE    1 
ATOM 5141 N NZ    . LYS B 2 620 ? 22.24400  60.24300  57.13600 1.000 101.06772 ? 620 LYS A NZ    1 
ATOM 5142 N N     . SER B 2 621 ? 19.66300  56.98700  51.46000 1.000 82.39146  ? 621 SER A N     1 
ATOM 5143 C CA    . SER B 2 621 ? 19.36000  57.78600  50.28200 1.000 82.21412  ? 621 SER A CA    1 
ATOM 5144 C C     . SER B 2 621 ? 18.24100  57.19900  49.43500 1.000 78.73634  ? 621 SER A C     1 
ATOM 5145 O O     . SER B 2 621 ? 17.87700  57.80100  48.41900 1.000 94.34241  ? 621 SER A O     1 
ATOM 5146 C CB    . SER B 2 621 ? 20.61700  57.96100  49.42800 1.000 87.46387  ? 621 SER A CB    1 
ATOM 5147 O OG    . SER B 2 621 ? 21.17500  56.70500  49.08800 1.000 98.37712  ? 621 SER A OG    1 
ATOM 5148 N N     . THR B 2 622 ? 17.68900  56.04900  49.81400 1.000 70.74518  ? 622 THR A N     1 
ATOM 5149 C CA    . THR B 2 622 ? 16.53700  55.48400  49.12500 1.000 85.62376  ? 622 THR A CA    1 
ATOM 5150 C C     . THR B 2 622 ? 15.24600  55.68000  49.91300 1.000 79.58598  ? 622 THR A C     1 
ATOM 5151 O O     . THR B 2 622 ? 14.22800  55.06200  49.58500 1.000 82.60892  ? 622 THR A O     1 
ATOM 5152 C CB    . THR B 2 622 ? 16.77200  53.99700  48.83800 1.000 85.02830  ? 622 THR A CB    1 
ATOM 5153 O OG1   . THR B 2 622 ? 16.58600  53.23400  50.03600 1.000 88.02937  ? 622 THR A OG1   1 
ATOM 5154 C CG2   . THR B 2 622 ? 18.19000  53.77500  48.33100 1.000 78.89847  ? 622 THR A CG2   1 
ATOM 5155 N N     . ILE B 2 623 ? 15.26000  56.53900  50.92900 1.000 74.82814  ? 623 ILE A N     1 
ATOM 5156 C CA    . ILE B 2 623 ? 14.12900  56.68300  51.83900 1.000 58.12405  ? 623 ILE A CA    1 
ATOM 5157 C C     . ILE B 2 623 ? 13.07900  57.59200  51.21300 1.000 63.37031  ? 623 ILE A C     1 
ATOM 5158 O O     . ILE B 2 623 ? 13.40100  58.64800  50.65300 1.000 75.49907  ? 623 ILE A O     1 
ATOM 5159 C CB    . ILE B 2 623 ? 14.59800  57.22300  53.20000 1.000 55.73939  ? 623 ILE A CB    1 
ATOM 5160 C CG1   . ILE B 2 623 ? 15.29800  56.12100  53.99500 1.000 64.52384  ? 623 ILE A CG1   1 
ATOM 5161 C CG2   . ILE B 2 623 ? 13.43200  57.80100  53.99000 1.000 71.14157  ? 623 ILE A CG2   1 
ATOM 5162 C CD1   . ILE B 2 623 ? 15.74000  56.54800  55.38600 1.000 70.77798  ? 623 ILE A CD1   1 
ATOM 5163 N N     . ARG B 2 624 ? 11.81700  57.17500  51.29700 1.000 57.21784  ? 624 ARG A N     1 
ATOM 5164 C CA    . ARG B 2 624 ? 10.67700  57.99200  50.92100 1.000 61.01944  ? 624 ARG A CA    1 
ATOM 5165 C C     . ARG B 2 624 ? 9.67400   57.99100  52.06500 1.000 68.93948  ? 624 ARG A C     1 
ATOM 5166 O O     . ARG B 2 624 ? 9.50300   56.98800  52.75900 1.000 64.42273  ? 624 ARG A O     1 
ATOM 5167 C CB    . ARG B 2 624 ? 10.00700  57.48200  49.63700 1.000 73.05329  ? 624 ARG A CB    1 
ATOM 5168 C CG    . ARG B 2 624 ? 10.96700  57.25300  48.48000 1.000 75.78245  ? 624 ARG A CG    1 
ATOM 5169 C CD    . ARG B 2 624 ? 10.24400  57.34800  47.14800 1.000 76.78432  ? 624 ARG A CD    1 
ATOM 5170 N NE    . ARG B 2 624 ? 11.12400  57.07400  46.01600 1.000 124.60583 ? 624 ARG A NE    1 
ATOM 5171 C CZ    . ARG B 2 624 ? 11.02800  55.99900  45.24100 1.000 135.58919 ? 624 ARG A CZ    1 
ATOM 5172 N NH1   . ARG B 2 624 ? 10.08300  55.09800  45.47000 1.000 109.10471 ? 624 ARG A NH1   1 
ATOM 5173 N NH2   . ARG B 2 624 ? 11.87000  55.82900  44.23000 1.000 145.49080 ? 624 ARG A NH2   1 
ATOM 5174 N N     . LEU B 2 625 ? 9.01500   59.12800  52.26200 1.000 64.44378  ? 625 LEU A N     1 
ATOM 5175 C CA    . LEU B 2 625 ? 8.02700   59.29000  53.32200 1.000 57.71788  ? 625 LEU A CA    1 
ATOM 5176 C C     . LEU B 2 625 ? 6.68800   59.62600  52.68000 1.000 60.82627  ? 625 LEU A C     1 
ATOM 5177 O O     . LEU B 2 625 ? 6.52500   60.70600  52.10200 1.000 78.07727  ? 625 LEU A O     1 
ATOM 5178 C CB    . LEU B 2 625 ? 8.45200   60.37600  54.30900 1.000 54.52398  ? 625 LEU A CB    1 
ATOM 5179 C CG    . LEU B 2 625 ? 7.51700   60.58200  55.50300 1.000 59.14121  ? 625 LEU A CG    1 
ATOM 5180 C CD1   . LEU B 2 625 ? 7.42000   59.31300  56.33200 1.000 50.88501  ? 625 LEU A CD1   1 
ATOM 5181 C CD2   . LEU B 2 625 ? 7.97600   61.75400  56.35900 1.000 50.05059  ? 625 LEU A CD2   1 
ATOM 5182 N N     . TYR B 2 626 ? 5.73500   58.70200  52.77900 1.000 62.93194  ? 626 TYR A N     1 
ATOM 5183 C CA    . TYR B 2 626 ? 4.41800   58.86200  52.18300 1.000 56.24689  ? 626 TYR A CA    1 
ATOM 5184 C C     . TYR B 2 626 ? 3.40100   59.28300  53.23400 1.000 64.02390  ? 626 TYR A C     1 
ATOM 5185 O O     . TYR B 2 626 ? 3.43800   58.81000  54.37400 1.000 72.67572  ? 626 TYR A O     1 
ATOM 5186 C CB    . TYR B 2 626 ? 3.95900   57.56100  51.52400 1.000 67.30808  ? 626 TYR A CB    1 
ATOM 5187 C CG    . TYR B 2 626 ? 4.77700   57.14100  50.32700 1.000 66.46416  ? 626 TYR A CG    1 
ATOM 5188 C CD1   . TYR B 2 626 ? 5.88400   56.31700  50.47200 1.000 69.07839  ? 626 TYR A CD1   1 
ATOM 5189 C CD2   . TYR B 2 626 ? 4.43500   57.56000  49.04900 1.000 71.95910  ? 626 TYR A CD2   1 
ATOM 5190 C CE1   . TYR B 2 626 ? 6.63100   55.92900  49.37700 1.000 73.89975  ? 626 TYR A CE1   1 
ATOM 5191 C CE2   . TYR B 2 626 ? 5.17400   57.17700  47.94800 1.000 69.96370  ? 626 TYR A CE2   1 
ATOM 5192 C CZ    . TYR B 2 626 ? 6.27100   56.36300  48.11700 1.000 76.70505  ? 626 TYR A CZ    1 
ATOM 5193 O OH    . TYR B 2 626 ? 7.01000   55.97900  47.02300 1.000 94.38360  ? 626 TYR A OH    1 
ATOM 5194 N N     . VAL B 2 627 ? 2.48900   60.17200  52.83500 1.000 65.55600  ? 627 VAL A N     1 
ATOM 5195 C CA    . VAL B 2 627 ? 1.34600   60.58200  53.64300 1.000 58.36147  ? 627 VAL A CA    1 
ATOM 5196 C C     . VAL B 2 627 ? 0.09100   60.47200  52.78800 1.000 61.35635  ? 627 VAL A C     1 
ATOM 5197 O O     . VAL B 2 627 ? 0.12300   60.74300  51.58300 1.000 59.67500  ? 627 VAL A O     1 
ATOM 5198 C CB    . VAL B 2 627 ? 1.50000   62.01800  54.19100 1.000 51.72863  ? 627 VAL A CB    1 
ATOM 5199 C CG1   . VAL B 2 627 ? 2.64500   62.09500  55.18300 1.000 53.17008  ? 627 VAL A CG1   1 
ATOM 5200 C CG2   . VAL B 2 627 ? 1.69600   63.01300  53.05500 1.000 47.21662  ? 627 VAL A CG2   1 
ATOM 5201 N N     . LYS B 2 628 ? -1.01400  60.07300  53.41200 1.000 56.75093  ? 628 LYS A N     1 
ATOM 5202 C CA    . LYS B 2 628 ? -2.28700  59.91600  52.71600 1.000 54.30000  ? 628 LYS A CA    1 
ATOM 5203 C C     . LYS B 2 628 ? -3.05800  61.23000  52.80800 1.000 66.63483  ? 628 LYS A C     1 
ATOM 5204 O O     . LYS B 2 628 ? -3.56000  61.59000  53.87800 1.000 84.62362  ? 628 LYS A O     1 
ATOM 5205 C CB    . LYS B 2 628 ? -3.08400  58.76000  53.31600 1.000 57.88241  ? 628 LYS A CB    1 
ATOM 5206 C CG    . LYS B 2 628 ? -4.30900  58.36900  52.51000 1.000 50.99909  ? 628 LYS A CG    1 
ATOM 5207 C CD    . LYS B 2 628 ? -5.10000  57.26400  53.19200 1.000 56.37231  ? 628 LYS A CD    1 
ATOM 5208 C CE    . LYS B 2 628 ? -6.37200  56.94900  52.42000 1.000 61.07124  ? 628 LYS A CE    1 
ATOM 5209 N NZ    . LYS B 2 628 ? -7.30800  56.08600  53.19000 1.000 64.13462  ? 628 LYS A NZ    1 
ATOM 5210 N N     . ASP B 2 629 ? -3.15600  61.94500  51.68700 1.000 70.46380  ? 629 ASP A N     1 
ATOM 5211 C CA    . ASP B 2 629 ? -3.78900  63.25800  51.66000 1.000 64.49935  ? 629 ASP A CA    1 
ATOM 5212 C C     . ASP B 2 629 ? -5.22500  63.23500  51.15200 1.000 61.38040  ? 629 ASP A C     1 
ATOM 5213 O O     . ASP B 2 629 ? -5.90300  64.26500  51.22100 1.000 78.66950  ? 629 ASP A O     1 
ATOM 5214 C CB    . ASP B 2 629 ? -2.96500  64.22700  50.80400 1.000 66.28100  ? 629 ASP A CB    1 
ATOM 5215 C CG    . ASP B 2 629 ? -1.70000  64.68800  51.50300 1.000 63.25556  ? 629 ASP A CG    1 
ATOM 5216 O OD1   . ASP B 2 629 ? -1.54400  64.39200  52.70700 1.000 67.85176  ? 629 ASP A OD1   1 
ATOM 5217 O OD2   . ASP B 2 629 ? -0.86200  65.34400  50.84900 1.000 72.52906  ? 629 ASP A OD2   1 
ATOM 5218 N N     . TYR B 2 630 ? -5.70600  62.10300  50.64500 1.000 74.15500  ? 630 TYR A N     1 
ATOM 5219 C CA    . TYR B 2 630 ? -7.09100  61.97300  50.21700 1.000 79.52057  ? 630 TYR A CA    1 
ATOM 5220 C C     . TYR B 2 630 ? -7.58400  60.57200  50.55700 1.000 71.57085  ? 630 TYR A C     1 
ATOM 5221 O O     . TYR B 2 630 ? -6.80500  59.68600  50.91600 1.000 73.33513  ? 630 TYR A O     1 
ATOM 5222 C CB    . TYR B 2 630 ? -7.25100  62.25800  48.71500 1.000 83.64969  ? 630 TYR A CB    1 
ATOM 5223 C CG    . TYR B 2 630 ? -6.74100  63.61800  48.27900 1.000 97.07474  ? 630 TYR A CG    1 
ATOM 5224 C CD1   . TYR B 2 630 ? -7.48300  64.77000  48.51600 1.000 97.12000  ? 630 TYR A CD1   1 
ATOM 5225 C CD2   . TYR B 2 630 ? -5.52100  63.74800  47.62300 1.000 87.08219  ? 630 TYR A CD2   1 
ATOM 5226 C CE1   . TYR B 2 630 ? -7.02100  66.01300  48.11800 1.000 98.97172  ? 630 TYR A CE1   1 
ATOM 5227 C CE2   . TYR B 2 630 ? -5.05100  64.98700  47.22100 1.000 80.66497  ? 630 TYR A CE2   1 
ATOM 5228 C CZ    . TYR B 2 630 ? -5.80500  66.11500  47.47200 1.000 96.82417  ? 630 TYR A CZ    1 
ATOM 5229 O OH    . TYR B 2 630 ? -5.34500  67.35100  47.07600 1.000 109.42608 ? 630 TYR A OH    1 
ATOM 5230 N N     . ALA B 2 631 ? -8.89800  60.38200  50.45200 1.000 86.76843  ? 631 ALA A N     1 
ATOM 5231 C CA    . ALA B 2 631 ? -9.53200  59.08300  50.63300 1.000 84.49251  ? 631 ALA A CA    1 
ATOM 5232 C C     . ALA B 2 631 ? -9.91900  58.51400  49.27400 1.000 83.91496  ? 631 ALA A C     1 
ATOM 5233 O O     . ALA B 2 631 ? -10.37600 59.24800  48.39300 1.000 93.70619  ? 631 ALA A O     1 
ATOM 5234 C CB    . ALA B 2 631 ? -10.76800 59.19200  51.52700 1.000 84.98214  ? 631 ALA A CB    1 
ATOM 5235 N N     . VAL B 2 632 ? -9.74200  57.20200  49.10800 1.000 80.23258  ? 632 VAL A N     1 
ATOM 5236 C CA    . VAL B 2 632 ? -9.93500  56.62900  47.77900 1.000 83.54524  ? 632 VAL A CA    1 
ATOM 5237 C C     . VAL B 2 632 ? -11.42100 56.48600  47.43600 1.000 71.76513  ? 632 VAL A C     1 
ATOM 5238 O O     . VAL B 2 632 ? -11.79700 56.62500  46.26900 1.000 83.55795  ? 632 VAL A O     1 
ATOM 5239 C CB    . VAL B 2 632 ? -9.16900  55.29800  47.64500 1.000 71.52972  ? 632 VAL A CB    1 
ATOM 5240 C CG1   . VAL B 2 632 ? -7.69100  55.48900  47.97900 1.000 88.35753  ? 632 VAL A CG1   1 
ATOM 5241 C CG2   . VAL B 2 632 ? -9.80500  54.19300  48.48200 1.000 84.76380  ? 632 VAL A CG2   1 
ATOM 5242 N N     . LYS B 2 633 ? -12.29400 56.22100  48.41600 1.000 75.25349  ? 633 LYS A N     1 
ATOM 5243 C CA    . LYS B 2 633 ? -13.72700 56.33500  48.14500 1.000 73.24271  ? 633 LYS A CA    1 
ATOM 5244 C C     . LYS B 2 633 ? -14.07800 57.76300  47.75200 1.000 77.06953  ? 633 LYS A C     1 
ATOM 5245 O O     . LYS B 2 633 ? -14.84100 57.99600  46.80400 1.000 84.86366  ? 633 LYS A O     1 
ATOM 5246 C CB    . LYS B 2 633 ? -14.54600 55.90900  49.36700 1.000 64.55553  ? 633 LYS A CB    1 
ATOM 5247 C CG    . LYS B 2 633 ? -14.63700 54.40800  49.61300 1.000 68.99157  ? 633 LYS A CG    1 
ATOM 5248 C CD    . LYS B 2 633 ? -15.09600 54.13500  51.04400 1.000 72.40164  ? 633 LYS A CD    1 
ATOM 5249 C CE    . LYS B 2 633 ? -15.29600 52.65400  51.31700 1.000 71.06273  ? 633 LYS A CE    1 
ATOM 5250 N NZ    . LYS B 2 633 ? -16.72000 52.24700  51.17100 1.000 103.62028 ? 633 LYS A NZ    1 
ATOM 5251 N N     . ASP B 2 634 ? -13.50500 58.73200  48.46800 1.000 91.51622  ? 634 ASP A N     1 
ATOM 5252 C CA    . ASP B 2 634 ? -13.69500 60.14000  48.14400 1.000 98.22665  ? 634 ASP A CA    1 
ATOM 5253 C C     . ASP B 2 634 ? -13.26700 60.44000  46.71400 1.000 91.93785  ? 634 ASP A C     1 
ATOM 5254 O O     . ASP B 2 634 ? -14.00400 61.07600  45.95200 1.000 75.24144  ? 634 ASP A O     1 
ATOM 5255 C CB    . ASP B 2 634 ? -12.90400 60.99900  49.12800 1.000 88.09046  ? 634 ASP A CB    1 
ATOM 5256 C CG    . ASP B 2 634 ? -13.72500 62.11100  49.71400 1.000 115.31537 ? 634 ASP A CG    1 
ATOM 5257 O OD1   . ASP B 2 634 ? -14.95100 62.12500  49.48000 1.000 126.78644 ? 634 ASP A OD1   1 
ATOM 5258 O OD2   . ASP B 2 634 ? -13.14500 62.97300  50.40800 1.000 139.60392 ? 634 ASP A OD2   1 
ATOM 5259 N N     . VAL B 2 635 ? -12.06600 59.99400  46.33400 1.000 87.81645  ? 635 VAL A N     1 
ATOM 5260 C CA    . VAL B 2 635 ? -11.55600 60.27400  44.99400 1.000 87.86356  ? 635 VAL A CA    1 
ATOM 5261 C C     . VAL B 2 635 ? -12.42600 59.59700  43.94300 1.000 93.68097  ? 635 VAL A C     1 
ATOM 5262 O O     . VAL B 2 635 ? -12.79000 60.20500  42.92900 1.000 96.13508  ? 635 VAL A O     1 
ATOM 5263 C CB    . VAL B 2 635 ? -10.08200 59.84400  44.87900 1.000 77.83602  ? 635 VAL A CB    1 
ATOM 5264 C CG1   . VAL B 2 635 ? -9.70800  59.58200  43.42700 1.000 79.27391  ? 635 VAL A CG1   1 
ATOM 5265 C CG2   . VAL B 2 635 ? -9.17800  60.91400  45.46700 1.000 71.07636  ? 635 VAL A CG2   1 
ATOM 5266 N N     . LEU B 2 636 ? -12.78600 58.33200  44.17600 1.000 74.87066  ? 636 LEU A N     1 
ATOM 5267 C CA    . LEU B 2 636 ? -13.61500 57.61300  43.21500 1.000 65.92593  ? 636 LEU A CA    1 
ATOM 5268 C C     . LEU B 2 636 ? -14.96600 58.28900  43.02300 1.000 78.37025  ? 636 LEU A C     1 
ATOM 5269 O O     . LEU B 2 636 ? -15.53100 58.24200  41.92400 1.000 74.90173  ? 636 LEU A O     1 
ATOM 5270 C CB    . LEU B 2 636 ? -13.79400 56.16000  43.65800 1.000 65.24660  ? 636 LEU A CB    1 
ATOM 5271 C CG    . LEU B 2 636 ? -12.55600 55.27300  43.50500 1.000 79.12401  ? 636 LEU A CG    1 
ATOM 5272 C CD1   . LEU B 2 636 ? -12.76600 53.90000  44.13500 1.000 70.51758  ? 636 LEU A CD1   1 
ATOM 5273 C CD2   . LEU B 2 636 ? -12.17100 55.13900  42.03800 1.000 71.36249  ? 636 LEU A CD2   1 
ATOM 5274 N N     . THR B 2 637 ? -15.49200 58.94000  44.06200 1.000 79.02928  ? 637 THR A N     1 
ATOM 5275 C CA    . THR B 2 637 ? -16.78500 59.60400  43.92200 1.000 79.62482  ? 637 THR A CA    1 
ATOM 5276 C C     . THR B 2 637 ? -16.65100 60.97600  43.27200 1.000 76.77879  ? 637 THR A C     1 
ATOM 5277 O O     . THR B 2 637 ? -17.22100 61.22500  42.20500 1.000 84.96535  ? 637 THR A O     1 
ATOM 5278 C CB    . THR B 2 637 ? -17.46200 59.72900  45.28300 1.000 77.20666  ? 637 THR A CB    1 
ATOM 5279 O OG1   . THR B 2 637 ? -16.58500 60.40100  46.19600 1.000 111.79837 ? 637 THR A OG1   1 
ATOM 5280 C CG2   . THR B 2 637 ? -17.76200 58.37100  45.80500 1.000 75.45188  ? 637 THR A CG2   1 
ATOM 5281 N N     . LYS B 2 638 ? -15.90200 61.88000  43.91100 1.000 83.41415  ? 638 LYS A N     1 
ATOM 5282 C CA    . LYS B 2 638 ? -15.83200 63.26100  43.44100 1.000 81.92302  ? 638 LYS A CA    1 
ATOM 5283 C C     . LYS B 2 638 ? -15.21600 63.36200  42.05100 1.000 93.41167  ? 638 LYS A C     1 
ATOM 5284 O O     . LYS B 2 638 ? -15.57400 64.26000  41.28000 1.000 102.62853 ? 638 LYS A O     1 
ATOM 5285 C CB    . LYS B 2 638 ? -15.03300 64.11600  44.42700 1.000 84.92241  ? 638 LYS A CB    1 
ATOM 5286 C CG    . LYS B 2 638 ? -15.68200 64.30300  45.79500 1.000 93.30034  ? 638 LYS A CG    1 
ATOM 5287 C CD    . LYS B 2 638 ? -14.90600 65.32000  46.63000 1.000 99.97348  ? 638 LYS A CD    1 
ATOM 5288 C CE    . LYS B 2 638 ? -15.62600 65.67100  47.92800 1.000 121.56845 ? 638 LYS A CE    1 
ATOM 5289 N NZ    . LYS B 2 638 ? -15.60900 64.56200  48.92100 1.000 104.91265 ? 638 LYS A NZ    1 
ATOM 5290 N N     . GLN B 2 639 ? -14.30300 62.45700  41.70800 1.000 92.44390  ? 639 GLN A N     1 
ATOM 5291 C CA    . GLN B 2 639 ? -13.52600 62.56800  40.48100 1.000 93.49560  ? 639 GLN A CA    1 
ATOM 5292 C C     . GLN B 2 639 ? -14.01300 61.65900  39.36100 1.000 87.53177  ? 639 GLN A C     1 
ATOM 5293 O O     . GLN B 2 639 ? -13.48800 61.74600  38.24700 1.000 98.27568  ? 639 GLN A O     1 
ATOM 5294 C CB    . GLN B 2 639 ? -12.04900 62.27500  40.76700 1.000 101.40956 ? 639 GLN A CB    1 
ATOM 5295 C CG    . GLN B 2 639 ? -11.39100 63.28900  41.68200 1.000 92.09358  ? 639 GLN A CG    1 
ATOM 5296 C CD    . GLN B 2 639 ? -11.35800 64.67100  41.07000 1.000 115.73550 ? 639 GLN A CD    1 
ATOM 5297 O OE1   . GLN B 2 639 ? -10.95500 64.84100  39.92000 1.000 122.08620 ? 639 GLN A OE1   1 
ATOM 5298 N NE2   . GLN B 2 639 ? -11.78800 65.66900  41.83400 1.000 134.94704 ? 639 GLN A NE2   1 
ATOM 5299 N N     . VAL B 2 640 ? -14.98500 60.78400  39.61800 1.000 82.86433  ? 640 VAL A N     1 
ATOM 5300 C CA    . VAL B 2 640 ? -15.48600 59.89000  38.57700 1.000 90.80893  ? 640 VAL A CA    1 
ATOM 5301 C C     . VAL B 2 640 ? -17.00900 59.87700  38.58500 1.000 87.75454  ? 640 VAL A C     1 
ATOM 5302 O O     . VAL B 2 640 ? -17.64900 60.28800  37.61000 1.000 86.73590  ? 640 VAL A O     1 
ATOM 5303 C CB    . VAL B 2 640 ? -14.93200 58.46100  38.74400 1.000 80.78339  ? 640 VAL A CB    1 
ATOM 5304 C CG1   . VAL B 2 640 ? -15.46000 57.56200  37.63900 1.000 77.47221  ? 640 VAL A CG1   1 
ATOM 5305 C CG2   . VAL B 2 640 ? -13.40900 58.46400  38.74500 1.000 83.10728  ? 640 VAL A CG2   1 
ATOM 5306 N N     . LEU B 2 641 ? -17.59600 59.40500  39.68800 1.000 84.18442  ? 641 LEU A N     1 
ATOM 5307 C CA    . LEU B 2 641 ? -19.04400 59.23000  39.75300 1.000 89.12734  ? 641 LEU A CA    1 
ATOM 5308 C C     . LEU B 2 641 ? -19.78200 60.55000  39.56100 1.000 89.02091  ? 641 LEU A C     1 
ATOM 5309 O O     . LEU B 2 641 ? -20.80300 60.60200  38.86500 1.000 105.88767 ? 641 LEU A O     1 
ATOM 5310 C CB    . LEU B 2 641 ? -19.42900 58.59200  41.08800 1.000 88.05641  ? 641 LEU A CB    1 
ATOM 5311 C CG    . LEU B 2 641 ? -20.91700 58.51700  41.43500 1.000 92.29727  ? 641 LEU A CG    1 
ATOM 5312 C CD1   . LEU B 2 641 ? -21.64900 57.56700  40.50000 1.000 95.53837  ? 641 LEU A CD1   1 
ATOM 5313 C CD2   . LEU B 2 641 ? -21.09700 58.09700  42.88500 1.000 86.12852  ? 641 LEU A CD2   1 
ATOM 5314 N N     . GLU B 2 642 ? -19.28400 61.62400  40.16400 1.000 82.08944  ? 642 GLU A N     1 
ATOM 5315 C CA    . GLU B 2 642 ? -19.96000 62.91300  40.12200 1.000 87.63675  ? 642 GLU A CA    1 
ATOM 5316 C C     . GLU B 2 642 ? -19.51700 63.79000  38.95700 1.000 97.21708  ? 642 GLU A C     1 
ATOM 5317 O O     . GLU B 2 642 ? -20.03300 64.90200  38.80900 1.000 112.70038 ? 642 GLU A O     1 
ATOM 5318 C CB    . GLU B 2 642 ? -19.74300 63.66000  41.44400 1.000 86.99839  ? 642 GLU A CB    1 
ATOM 5319 C CG    . GLU B 2 642 ? -20.34500 62.96100  42.65600 1.000 85.12157  ? 642 GLU A CG    1 
ATOM 5320 C CD    . GLU B 2 642 ? -20.13500 63.73200  43.94700 1.000 112.55277 ? 642 GLU A CD    1 
ATOM 5321 O OE1   . GLU B 2 642 ? -19.18000 64.53500  44.01600 1.000 118.95656 ? 642 GLU A OE1   1 
ATOM 5322 O OE2   . GLU B 2 642 ? -20.92800 63.53800  44.89400 1.000 99.00875  ? 642 GLU A OE2   1 
ATOM 5323 N N     . LYS B 2 643 ? -18.58500 63.32200  38.12500 1.000 88.34433  ? 643 LYS A N     1 
ATOM 5324 C CA    . LYS B 2 643 ? -18.07700 64.10200  37.00400 1.000 100.92297 ? 643 LYS A CA    1 
ATOM 5325 C C     . LYS B 2 643 ? -18.72000 63.73800  35.67200 1.000 103.83448 ? 643 LYS A C     1 
ATOM 5326 O O     . LYS B 2 643 ? -18.48500 64.43600  34.68000 1.000 115.64487 ? 643 LYS A O     1 
ATOM 5327 C CB    . LYS B 2 643 ? -16.55700 63.93300  36.88400 1.000 102.99897 ? 643 LYS A CB    1 
ATOM 5328 C CG    . LYS B 2 643 ? -15.74000 65.01800  37.56700 1.000 115.99794 ? 643 LYS A CG    1 
ATOM 5329 C CD    . LYS B 2 643 ? -14.24900 64.76500  37.39800 1.000 121.74903 ? 643 LYS A CD    1 
ATOM 5330 C CE    . LYS B 2 643 ? -13.41900 65.95300  37.86000 1.000 129.56269 ? 643 LYS A CE    1 
ATOM 5331 N NZ    . LYS B 2 643 ? -13.57400 67.12500  36.95400 1.000 136.11532 ? 643 LYS A NZ    1 
ATOM 5332 N N     . PHE B 2 644 ? -19.52600 62.68200  35.62600 1.000 98.57905  ? 644 PHE A N     1 
ATOM 5333 C CA    . PHE B 2 644 ? -20.09300 62.18800  34.38000 1.000 98.65619  ? 644 PHE A CA    1 
ATOM 5334 C C     . PHE B 2 644 ? -21.59900 62.01900  34.51900 1.000 103.35478 ? 644 PHE A C     1 
ATOM 5335 O O     . PHE B 2 644 ? -22.09600 61.61900  35.57600 1.000 105.28579 ? 644 PHE A O     1 
ATOM 5336 C CB    . PHE B 2 644 ? -19.44400 60.86000  33.97500 1.000 91.67759  ? 644 PHE A CB    1 
ATOM 5337 C CG    . PHE B 2 644 ? -18.04100 61.00900  33.46200 1.000 85.11889  ? 644 PHE A CG    1 
ATOM 5338 C CD1   . PHE B 2 644 ? -17.72600 62.02300  32.57600 1.000 93.19550  ? 644 PHE A CD1   1 
ATOM 5339 C CD2   . PHE B 2 644 ? -17.03500 60.14800  33.87300 1.000 84.27985  ? 644 PHE A CD2   1 
ATOM 5340 C CE1   . PHE B 2 644 ? -16.43800 62.17200  32.09900 1.000 113.89671 ? 644 PHE A CE1   1 
ATOM 5341 C CE2   . PHE B 2 644 ? -15.74200 60.29200  33.39900 1.000 100.70541 ? 644 PHE A CE2   1 
ATOM 5342 C CZ    . PHE B 2 644 ? -15.44500 61.30600  32.51200 1.000 111.58695 ? 644 PHE A CZ    1 
ATOM 5343 N N     . LYS B 2 645 ? -22.32000 62.32600  33.43900 1.000 113.33194 ? 645 LYS A N     1 
ATOM 5344 C CA    . LYS B 2 645 ? -23.77400 62.21500  33.44300 1.000 108.78789 ? 645 LYS A CA    1 
ATOM 5345 C C     . LYS B 2 645 ? -24.23700 60.78400  33.21400 1.000 103.53953 ? 645 LYS A C     1 
ATOM 5346 O O     . LYS B 2 645 ? -25.34900 60.42700  33.61500 1.000 134.41686 ? 645 LYS A O     1 
ATOM 5347 C CB    . LYS B 2 645 ? -24.37700 63.13200  32.37400 1.000 102.86466 ? 645 LYS A CB    1 
ATOM 5348 C CG    . LYS B 2 645 ? -23.83900 64.55600  32.39000 1.000 133.94213 ? 645 LYS A CG    1 
ATOM 5349 C CD    . LYS B 2 645 ? -23.92000 65.16400  33.78400 1.000 144.74990 ? 645 LYS A CD    1 
ATOM 5350 C CE    . LYS B 2 645 ? -23.18800 66.49500  33.85300 1.000 126.54457 ? 645 LYS A CE    1 
ATOM 5351 N NZ    . LYS B 2 645 ? -22.95700 66.93500  35.25800 1.000 127.58059 ? 645 LYS A NZ    1 
ATOM 5352 N N     . SER B 2 646 ? -23.39200 59.99000  32.57200 1.000 90.48842  ? 646 SER A N     1 
ATOM 5353 C CA    . SER B 2 646 ? -23.78600 58.60800  32.23000 1.000 109.62418 ? 646 SER A CA    1 
ATOM 5354 C C     . SER B 2 646 ? -22.60800 57.65900  32.42500 1.000 117.14615 ? 646 SER A C     1 
ATOM 5355 O O     . SER B 2 646 ? -22.08400 57.19900  31.42200 1.000 132.57613 ? 646 SER A O     1 
ATOM 5356 C CB    . SER B 2 646 ? -24.26100 58.59200  30.81300 1.000 117.47835 ? 646 SER A CB    1 
ATOM 5357 O OG    . SER B 2 646 ? -24.35500 57.27300  30.30000 1.000 112.58312 ? 646 SER A OG    1 
ATOM 5358 N N     . LEU B 2 647 ? -22.24700 57.35500  33.66500 1.000 107.25919 ? 647 LEU A N     1 
ATOM 5359 C CA    . LEU B 2 647 ? -21.11400 56.43900  33.92500 1.000 103.73431 ? 647 LEU A CA    1 
ATOM 5360 C C     . LEU B 2 647 ? -21.52000 55.01400  33.56900 1.000 105.99499 ? 647 LEU A C     1 
ATOM 5361 O O     . LEU B 2 647 ? -22.64400 54.66000  33.87500 1.000 105.83325 ? 647 LEU A O     1 
ATOM 5362 C CB    . LEU B 2 647 ? -20.82900 56.52900  35.41800 1.000 88.28248  ? 647 LEU A CB    1 
ATOM 5363 C CG    . LEU B 2 647 ? -19.67900 57.45300  35.77200 1.000 95.70618  ? 647 LEU A CG    1 
ATOM 5364 C CD1   . LEU B 2 647 ? -19.43000 57.41300  37.25800 1.000 110.12913 ? 647 LEU A CD1   1 
ATOM 5365 C CD2   . LEU B 2 647 ? -18.43300 57.04700  35.01900 1.000 88.98713  ? 647 LEU A CD2   1 
ATOM 5366 N N     . ILE B 2 648 ? -20.61900 54.21700  33.00000 1.000 98.46955  ? 648 ILE A N     1 
ATOM 5367 C CA    . ILE B 2 648 ? -20.96500 52.79900  32.69700 1.000 100.73567 ? 648 ILE A CA    1 
ATOM 5368 C C     . ILE B 2 648 ? -19.79000 51.90600  33.06100 1.000 98.82335  ? 648 ILE A C     1 
ATOM 5369 O O     . ILE B 2 648 ? -18.85700 51.85000  32.28700 1.000 100.39662 ? 648 ILE A O     1 
ATOM 5370 C CB    . ILE B 2 648 ? -21.27700 52.60100  31.21500 1.000 106.71101 ? 648 ILE A CB    1 
ATOM 5371 C CG1   . ILE B 2 648 ? -22.62300 53.20600  30.83300 1.000 100.64546 ? 648 ILE A CG1   1 
ATOM 5372 C CG2   . ILE B 2 648 ? -21.22000 51.12400  30.89400 1.000 97.11669  ? 648 ILE A CG2   1 
ATOM 5373 C CD1   . ILE B 2 648 ? -23.00300 52.93100  29.41100 1.000 93.30360  ? 648 ILE A CD1   1 
ATOM 5374 N N     . PHE B 2 649 ? -19.87600 51.22800  34.19400 1.000 87.39948  ? 649 PHE A N     1 
ATOM 5375 C CA    . PHE B 2 649 ? -18.82300 50.33800  34.67000 1.000 88.44523  ? 649 PHE A CA    1 
ATOM 5376 C C     . PHE B 2 649 ? -18.91100 48.97400  34.00300 1.000 86.65384  ? 649 PHE A C     1 
ATOM 5377 O O     . PHE B 2 649 ? -19.83500 48.20800  34.29100 1.000 95.17534  ? 649 PHE A O     1 
ATOM 5378 C CB    . PHE B 2 649 ? -18.89700 50.17400  36.19200 1.000 90.17001  ? 649 PHE A CB    1 
ATOM 5379 C CG    . PHE B 2 649 ? -18.53300 51.41500  36.95900 1.000 78.03536  ? 649 PHE A CG    1 
ATOM 5380 C CD1   . PHE B 2 649 ? -17.21500 51.82600  37.04200 1.000 91.15948  ? 649 PHE A CD1   1 
ATOM 5381 C CD2   . PHE B 2 649 ? -19.49800 52.14800  37.62700 1.000 79.92708  ? 649 PHE A CD2   1 
ATOM 5382 C CE1   . PHE B 2 649 ? -16.86300 52.95700  37.74900 1.000 87.35592  ? 649 PHE A CE1   1 
ATOM 5383 C CE2   . PHE B 2 649 ? -19.15100 53.28200  38.34600 1.000 91.32653  ? 649 PHE A CE2   1 
ATOM 5384 C CZ    . PHE B 2 649 ? -17.82900 53.68600  38.40400 1.000 86.09460  ? 649 PHE A CZ    1 
ATOM 5385 N N     . ILE B 2 650 ? -17.92000 48.64900  33.17000 1.000 76.03221  ? 650 ILE A N     1 
ATOM 5386 C CA    . ILE B 2 650 ? -17.89500 47.32200  32.48500 1.000 78.93158  ? 650 ILE A CA    1 
ATOM 5387 C C     . ILE B 2 650 ? -16.64300 46.55100  32.93000 1.000 78.41875  ? 650 ILE A C     1 
ATOM 5388 O O     . ILE B 2 650 ? -15.53100 47.06600  32.71400 1.000 101.88834 ? 650 ILE A O     1 
ATOM 5389 C CB    . ILE B 2 650 ? -17.92500 47.50000  30.95800 1.000 82.49610  ? 650 ILE A CB    1 
ATOM 5390 C CG1   . ILE B 2 650 ? -18.96100 48.53600  30.53700 1.000 97.42832  ? 650 ILE A CG1   1 
ATOM 5391 C CG2   . ILE B 2 650 ? -18.14600 46.15900  30.25800 1.000 84.20846  ? 650 ILE A CG2   1 
ATOM 5392 C CD1   . ILE B 2 650 ? -18.82800 48.99400  29.09700 1.000 108.32717 ? 650 ILE A CD1   1 
ATOM 5393 N N     . SER B 2 651 ? -16.82300 45.36900  33.52100 1.000 78.59178  ? 651 SER A N     1 
ATOM 5394 C CA    . SER B 2 651 ? -15.66700 44.52700  33.92300 1.000 82.95087  ? 651 SER A CA    1 
ATOM 5395 C C     . SER B 2 651 ? -16.10500 43.06200  34.02200 1.000 83.12629  ? 651 SER A C     1 
ATOM 5396 O O     . SER B 2 651 ? -17.28200 42.81700  34.34600 1.000 94.36051  ? 651 SER A O     1 
ATOM 5397 C CB    . SER B 2 651 ? -15.06900 44.99500  35.21700 1.000 96.93848  ? 651 SER A CB    1 
ATOM 5398 O OG    . SER B 2 651 ? -14.15500 44.03500  35.72700 1.000 88.95386  ? 651 SER A OG    1 
ATOM 5399 N N     . GLY B 2 652 ? -15.18600 42.13200  33.76100 1.000 80.25061  ? 652 GLY A N     1 
ATOM 5400 C CA    . GLY B 2 652 ? -15.50700 40.69800  33.85400 1.000 79.11192  ? 652 GLY A CA    1 
ATOM 5401 C C     . GLY B 2 652 ? -15.79300 40.30000  35.28500 1.000 79.46327  ? 652 GLY A C     1 
ATOM 5402 O O     . GLY B 2 652 ? -16.58300 39.35700  35.48600 1.000 91.48709  ? 652 GLY A O     1 
ATOM 5403 N N     . THR B 2 653 ? -15.16600 40.98400  36.24500 1.000 94.82568  ? 653 THR A N     1 
ATOM 5404 C CA    . THR B 2 653 ? -15.34800 40.64700  37.67100 1.000 81.94789  ? 653 THR A CA    1 
ATOM 5405 C C     . THR B 2 653 ? -15.79700 41.88100  38.42000 1.000 84.70971  ? 653 THR A C     1 
ATOM 5406 O O     . THR B 2 653 ? -14.99800 42.82900  38.53000 1.000 85.89025  ? 653 THR A O     1 
ATOM 5407 C CB    . THR B 2 653 ? -14.04500 40.07900  38.22500 1.000 77.70508  ? 653 THR A CB    1 
ATOM 5408 O OG1   . THR B 2 653 ? -13.33100 41.22800  38.66700 1.000 108.58009 ? 653 THR A OG1   1 
ATOM 5409 C CG2   . THR B 2 653 ? -13.23900 39.32400  37.18400 1.000 82.83191  ? 653 THR A CG2   1 
ATOM 5410 N N     . LEU B 2 654 ? -17.03700 41.87900  38.91700 1.000 94.39010  ? 654 LEU A N     1 
ATOM 5411 C CA    . LEU B 2 654 ? -17.58400 43.06200  39.62900 1.000 76.37624  ? 654 LEU A CA    1 
ATOM 5412 C C     . LEU B 2 654 ? -18.49800 42.61300  40.77600 1.000 90.90524  ? 654 LEU A C     1 
ATOM 5413 O O     . LEU B 2 654 ? -19.10200 43.50000  41.41000 1.000 93.06908  ? 654 LEU A O     1 
ATOM 5414 C CB    . LEU B 2 654 ? -18.36100 43.94200  38.65200 1.000 77.39805  ? 654 LEU A CB    1 
ATOM 5415 C CG    . LEU B 2 654 ? -17.54100 44.80900  37.69300 1.000 77.84955  ? 654 LEU A CG    1 
ATOM 5416 C CD1   . LEU B 2 654 ? -18.46500 45.60100  36.78700 1.000 97.06512  ? 654 LEU A CD1   1 
ATOM 5417 C CD2   . LEU B 2 654 ? -16.63500 45.74400  38.46800 1.000 85.87473  ? 654 LEU A CD2   1 
ATOM 5418 N N     . LYS B 2 655 ? -18.56500 41.31200  41.08100 1.000 106.38225 ? 655 LYS A N     1 
ATOM 5419 C CA    . LYS B 2 655 ? -19.55400 40.88900  42.11200 1.000 83.79611  ? 655 LYS A CA    1 
ATOM 5420 C C     . LYS B 2 655 ? -19.00700 39.87400  43.13100 1.000 87.36824  ? 655 LYS A C     1 
ATOM 5421 O O     . LYS B 2 655 ? -18.40700 38.86400  42.70200 1.000 84.60771  ? 655 LYS A O     1 
ATOM 5422 C CB    . LYS B 2 655 ? -20.79400 40.29000  41.43600 1.000 82.78925  ? 655 LYS A CB    1 
ATOM 5423 C CG    . LYS B 2 655 ? -20.54900 39.10300  40.51600 1.000 118.51539 ? 655 LYS A CG    1 
ATOM 5424 C CD    . LYS B 2 655 ? -21.75800 38.18300  40.40100 1.000 137.40139 ? 655 LYS A CD    1 
ATOM 5425 C CE    . LYS B 2 655 ? -22.98600 38.90200  39.94500 1.000 119.30847 ? 655 LYS A CE    1 
ATOM 5426 N NZ    . LYS B 2 655 ? -24.15500 38.01900  39.93200 1.000 124.94078 ? 655 LYS A NZ    1 
ATOM 5427 N N     . PHE B 2 656 ? -19.19100 40.14500  44.42900 1.000 93.44323  ? 656 PHE A N     1 
ATOM 5428 C CA    . PHE B 2 656 ? -18.85100 39.15900  45.49300 1.000 84.33459  ? 656 PHE A CA    1 
ATOM 5429 C C     . PHE B 2 656 ? -20.20300 38.54300  45.82100 1.000 92.21923  ? 656 PHE A C     1 
ATOM 5430 O O     . PHE B 2 656 ? -21.20100 39.12500  45.33700 1.000 90.11379  ? 656 PHE A O     1 
ATOM 5431 C CB    . PHE B 2 656 ? -18.14700 39.98900  46.56800 1.000 77.46866  ? 656 PHE A CB    1 
ATOM 5432 C CG    . PHE B 2 656 ? -17.79600 39.29500  47.87700 1.000 82.89990  ? 656 PHE A CG    1 
ATOM 5433 C CD1   . PHE B 2 656 ? -16.62600 38.55600  48.00000 1.000 87.57073  ? 656 PHE A CD1   1 
ATOM 5434 C CD2   . PHE B 2 656 ? -18.61200 39.42800  48.99400 1.000 83.26293  ? 656 PHE A CD2   1 
ATOM 5435 C CE1   . PHE B 2 656 ? -16.30000 37.94200  49.19700 1.000 92.34503  ? 656 PHE A CE1   1 
ATOM 5436 C CE2   . PHE B 2 656 ? -18.27900 38.81500  50.19000 1.000 85.85288  ? 656 PHE A CE2   1 
ATOM 5437 C CZ    . PHE B 2 656 ? -17.12400 38.07600  50.28900 1.000 87.34089  ? 656 PHE A CZ    1 
ATOM 5438 N N     . ASN B 2 657 ? -20.28900 37.43700  46.57600 1.000 94.42688  ? 657 ASN A N     1 
ATOM 5439 C CA    . ASN B 2 657 ? -21.65700 36.89300  46.73300 1.000 90.45652  ? 657 ASN A CA    1 
ATOM 5440 C C     . ASN B 2 657 ? -22.31000 36.82200  45.36500 1.000 104.45295 ? 657 ASN A C     1 
ATOM 5441 O O     . ASN B 2 657 ? -21.73900 36.21400  44.46400 1.000 114.54909 ? 657 ASN A O     1 
ATOM 5442 C CB    . ASN B 2 657 ? -22.48400 37.70600  47.71200 1.000 99.21472  ? 657 ASN A CB    1 
ATOM 5443 C CG    . ASN B 2 657 ? -22.92600 36.82300  48.84600 1.000 107.50608 ? 657 ASN A CG    1 
ATOM 5444 O OD1   . ASN B 2 657 ? -22.66200 35.63000  48.84700 1.000 89.20689  ? 657 ASN A OD1   1 
ATOM 5445 N ND2   . ASN B 2 657 ? -23.62600 37.40500  49.79800 1.000 150.19979 ? 657 ASN A ND2   1 
ATOM 5446 N N     . HIS B 2 658 ? -23.48700 37.40500  45.22500 1.000 90.21104  ? 658 HIS A N     1 
ATOM 5447 C CA    . HIS B 2 658 ? -24.10500 37.36500  43.88400 1.000 94.67515  ? 658 HIS A CA    1 
ATOM 5448 C C     . HIS B 2 658 ? -24.59300 38.76600  43.53800 1.000 95.24084  ? 658 HIS A C     1 
ATOM 5449 O O     . HIS B 2 658 ? -25.32200 38.89700  42.55300 1.000 110.37798 ? 658 HIS A O     1 
ATOM 5450 C CB    . HIS B 2 658 ? -25.16200 36.25800  43.81200 1.000 99.94678  ? 658 HIS A CB    1 
ATOM 5451 C CG    . HIS B 2 658 ? -24.58400 34.88300  43.78000 1.000 108.94262 ? 658 HIS A CG    1 
ATOM 5452 N ND1   . HIS B 2 658 ? -24.05500 34.33100  42.63300 1.000 127.04583 ? 658 HIS A ND1   1 
ATOM 5453 C CD2   . HIS B 2 658 ? -24.40300 33.97000  44.75400 1.000 90.19501  ? 658 HIS A CD2   1 
ATOM 5454 C CE1   . HIS B 2 658 ? -23.59600 33.12900  42.89600 1.000 111.50342 ? 658 HIS A CE1   1 
ATOM 5455 N NE2   . HIS B 2 658 ? -23.79900 32.88500  44.18900 1.000 105.69883 ? 658 HIS A NE2   1 
ATOM 5456 N N     . SER B 2 659 ? -24.19300 39.76600  44.32500 1.000 81.10043  ? 659 SER A N     1 
ATOM 5457 C CA    . SER B 2 659 ? -24.62500 41.14900  44.02400 1.000 92.48776  ? 659 SER A CA    1 
ATOM 5458 C C     . SER B 2 659 ? -23.39700 42.02200  43.79400 1.000 94.25202  ? 659 SER A C     1 
ATOM 5459 O O     . SER B 2 659 ? -22.27600 41.53400  43.97400 1.000 106.71200 ? 659 SER A O     1 
ATOM 5460 C CB    . SER B 2 659 ? -25.49100 41.71900  45.10500 1.000 105.36878 ? 659 SER A CB    1 
ATOM 5461 O OG    . SER B 2 659 ? -26.38400 42.68200  44.56000 1.000 106.82292 ? 659 SER A OG    1 
ATOM 5462 N N     . PHE B 2 660 ? -23.63600 43.26200  43.38000 1.000 82.94710  ? 660 PHE A N     1 
ATOM 5463 C CA    . PHE B 2 660 ? -22.57300 44.25500  43.10800 1.000 75.33120  ? 660 PHE A CA    1 
ATOM 5464 C C     . PHE B 2 660 ? -22.43700 45.17600  44.31500 1.000 89.93953  ? 660 PHE A C     1 
ATOM 5465 O O     . PHE B 2 660 ? -21.75600 46.19100  44.21600 1.000 96.90789  ? 660 PHE A O     1 
ATOM 5466 C CB    . PHE B 2 660 ? -22.99800 45.12100  41.92900 1.000 75.93778  ? 660 PHE A CB    1 
ATOM 5467 C CG    . PHE B 2 660 ? -23.16200 44.37700  40.63500 1.000 76.67172  ? 660 PHE A CG    1 
ATOM 5468 C CD1   . PHE B 2 660 ? -22.92300 43.02500  40.56800 1.000 100.65519 ? 660 PHE A CD1   1 
ATOM 5469 C CD2   . PHE B 2 660 ? -23.55800 45.03200  39.48900 1.000 88.85310  ? 660 PHE A CD2   1 
ATOM 5470 C CE1   . PHE B 2 660 ? -23.07100 42.34700  39.37400 1.000 117.07597 ? 660 PHE A CE1   1 
ATOM 5471 C CE2   . PHE B 2 660 ? -23.70500 44.35100  38.29800 1.000 92.48822  ? 660 PHE A CE2   1 
ATOM 5472 C CZ    . PHE B 2 660 ? -23.46400 43.00800  38.24400 1.000 97.64240  ? 660 PHE A CZ    1 
ATOM 5473 N N     . GLU B 2 661 ? -23.09800 44.84400  45.41600 1.000 88.36160  ? 661 GLU A N     1 
ATOM 5474 C CA    . GLU B 2 661 ? -23.06100 45.74300  46.59000 1.000 95.69340  ? 661 GLU A CA    1 
ATOM 5475 C C     . GLU B 2 661 ? -21.62500 45.99400  47.03800 1.000 93.94790  ? 661 GLU A C     1 
ATOM 5476 O O     . GLU B 2 661 ? -21.38300 47.04200  47.63300 1.000 92.26016  ? 661 GLU A O     1 
ATOM 5477 C CB    . GLU B 2 661 ? -23.91000 45.16900  47.71400 1.000 91.44384  ? 661 GLU A CB    1 
ATOM 5478 C CG    . GLU B 2 661 ? -25.31600 44.84400  47.27900 1.000 98.64784  ? 661 GLU A CG    1 
ATOM 5479 C CD    . GLU B 2 661 ? -26.08900 44.16600  48.38800 1.000 144.32033 ? 661 GLU A CD    1 
ATOM 5480 O OE1   . GLU B 2 661 ? -25.50000 43.96100  49.46000 1.000 150.58729 ? 661 GLU A OE1   1 
ATOM 5481 O OE2   . GLU B 2 661 ? -27.27000 43.84800  48.17700 1.000 153.36347 ? 661 GLU A OE2   1 
ATOM 5482 N N     . ALA B 2 662 ? -20.71000 45.07200  46.77200 1.000 96.69754  ? 662 ALA A N     1 
ATOM 5483 C CA    . ALA B 2 662 ? -19.35100 45.32500  47.24700 1.000 87.01516  ? 662 ALA A CA    1 
ATOM 5484 C C     . ALA B 2 662 ? -18.65900 46.37700  46.39000 1.000 77.51742  ? 662 ALA A C     1 
ATOM 5485 O O     . ALA B 2 662 ? -18.00500 47.28800  46.91300 1.000 79.94431  ? 662 ALA A O     1 
ATOM 5486 C CB    . ALA B 2 662 ? -18.54400 44.02800  47.26100 1.000 68.96595  ? 662 ALA A CB    1 
ATOM 5487 N N     . PHE B 2 663 ? -18.83200 46.29700  45.07200 1.000 81.38048  ? 663 PHE A N     1 
ATOM 5488 C CA    . PHE B 2 663 ? -18.20600 47.29800  44.16700 1.000 78.63440  ? 663 PHE A CA    1 
ATOM 5489 C C     . PHE B 2 663 ? -18.86500 48.64800  44.39400 1.000 76.89373  ? 663 PHE A C     1 
ATOM 5490 O O     . PHE B 2 663 ? -18.19200 49.68800  44.27900 1.000 87.82669  ? 663 PHE A O     1 
ATOM 5491 C CB    . PHE B 2 663 ? -18.33100 46.85800  42.70700 1.000 74.28725  ? 663 PHE A CB    1 
ATOM 5492 C CG    . PHE B 2 663 ? -17.64100 47.77300  41.70500 1.000 81.54947  ? 663 PHE A CG    1 
ATOM 5493 C CD1   . PHE B 2 663 ? -16.29400 47.61400  41.40600 1.000 80.96402  ? 663 PHE A CD1   1 
ATOM 5494 C CD2   . PHE B 2 663 ? -18.34200 48.78000  41.05300 1.000 94.21644  ? 663 PHE A CD2   1 
ATOM 5495 C CE1   . PHE B 2 663 ? -15.66800 48.44700  40.49300 1.000 78.08407  ? 663 PHE A CE1   1 
ATOM 5496 C CE2   . PHE B 2 663 ? -17.71100 49.60800  40.14100 1.000 84.03245  ? 663 PHE A CE2   1 
ATOM 5497 C CZ    . PHE B 2 663 ? -16.37600 49.44000  39.86300 1.000 71.46082  ? 663 PHE A CZ    1 
ATOM 5498 N N     . LYS B 2 664 ? -20.15500 48.64100  44.71800 1.000 82.97790  ? 664 LYS A N     1 
ATOM 5499 C CA    . LYS B 2 664 ? -20.90200 49.91200  44.87900 1.000 82.78317  ? 664 LYS A CA    1 
ATOM 5500 C C     . LYS B 2 664 ? -20.50000 50.60000  46.18700 1.000 78.38562  ? 664 LYS A C     1 
ATOM 5501 O O     . LYS B 2 664 ? -20.58500 51.84100  46.24600 1.000 78.43189  ? 664 LYS A O     1 
ATOM 5502 C CB    . LYS B 2 664 ? -22.39500 49.57900  44.86100 1.000 75.28490  ? 664 LYS A CB    1 
ATOM 5503 C CG    . LYS B 2 664 ? -23.33900 50.73700  44.58300 1.000 107.06555 ? 664 LYS A CG    1 
ATOM 5504 C CD    . LYS B 2 664 ? -24.76100 50.24300  44.35200 1.000 136.97559 ? 664 LYS A CD    1 
ATOM 5505 C CE    . LYS B 2 664 ? -24.80800 49.17000  43.31000 1.000 118.40419 ? 664 LYS A CE    1 
ATOM 5506 N NZ    . LYS B 2 664 ? -26.16100 48.63800  43.13300 1.000 84.55391  ? 664 LYS A NZ    1 
ATOM 5507 N N     . GLN B 2 665 ? -20.08500 49.82900  47.19300 1.000 78.75640  ? 665 GLN A N     1 
ATOM 5508 C CA    . GLN B 2 665 ? -19.75900 50.41600  48.51900 1.000 85.91740  ? 665 GLN A CA    1 
ATOM 5509 C C     . GLN B 2 665 ? -18.49200 51.27500  48.41300 1.000 74.46021  ? 665 GLN A C     1 
ATOM 5510 O O     . GLN B 2 665 ? -18.25900 52.09300  49.31800 1.000 84.00173  ? 665 GLN A O     1 
ATOM 5511 C CB    . GLN B 2 665 ? -19.58100 49.32500  49.57100 1.000 80.31131  ? 665 GLN A CB    1 
ATOM 5512 C CG    . GLN B 2 665 ? -20.89100 48.81200  50.15700 1.000 98.05566  ? 665 GLN A CG    1 
ATOM 5513 C CD    . GLN B 2 665 ? -20.70100 47.66600  51.12500 1.000 133.63814 ? 665 GLN A CD    1 
ATOM 5514 O OE1   . GLN B 2 665 ? -19.57700 47.22700  51.39300 1.000 113.74162 ? 665 GLN A OE1   1 
ATOM 5515 N NE2   . GLN B 2 665 ? -21.80500 47.16800  51.66200 1.000 127.76033 ? 665 GLN A NE2   1 
ATOM 5516 N N     . LEU B 2 666 ? -17.72600 51.11000  47.33700 1.000 74.97149  ? 666 LEU A N     1 
ATOM 5517 C CA    . LEU B 2 666 ? -16.50500 51.92700  47.12800 1.000 81.17319  ? 666 LEU A CA    1 
ATOM 5518 C C     . LEU B 2 666 ? -16.92300 53.36100  46.77900 1.000 80.34988  ? 666 LEU A C     1 
ATOM 5519 O O     . LEU B 2 666 ? -16.03100 54.20100  46.56100 1.000 84.03786  ? 666 LEU A O     1 
ATOM 5520 C CB    . LEU B 2 666 ? -15.65400 51.31400  46.01900 1.000 78.57329  ? 666 LEU A CB    1 
ATOM 5521 C CG    . LEU B 2 666 ? -15.16800 49.88200  46.25700 1.000 86.67687  ? 666 LEU A CG    1 
ATOM 5522 C CD1   . LEU B 2 666 ? -14.53900 49.32800  44.99300 1.000 83.49212  ? 666 LEU A CD1   1 
ATOM 5523 C CD2   . LEU B 2 666 ? -14.17100 49.85700  47.39800 1.000 69.91509  ? 666 LEU A CD2   1 
ATOM 5524 N N     . PHE B 2 667 ? -18.22900 53.61600  46.70900 1.000 73.68716  ? 667 PHE A N     1 
ATOM 5525 C CA    . PHE B 2 667 ? -18.72300 54.98400  46.40900 1.000 70.52382  ? 667 PHE A CA    1 
ATOM 5526 C C     . PHE B 2 667 ? -19.39300 55.54400  47.65400 1.000 84.05594  ? 667 PHE A C     1 
ATOM 5527 O O     . PHE B 2 667 ? -19.83000 54.75200  48.51000 1.000 87.83680  ? 667 PHE A O     1 
ATOM 5528 C CB    . PHE B 2 667 ? -19.58000 54.92700  45.14400 1.000 70.81583  ? 667 PHE A CB    1 
ATOM 5529 C CG    . PHE B 2 667 ? -18.75800 54.54800  43.92100 1.000 77.06919  ? 667 PHE A CG    1 
ATOM 5530 C CD1   . PHE B 2 667 ? -18.11100 55.52100  43.16900 1.000 71.59433  ? 667 PHE A CD1   1 
ATOM 5531 C CD2   . PHE B 2 667 ? -18.60500 53.21900  43.54700 1.000 89.92375  ? 667 PHE A CD2   1 
ATOM 5532 C CE1   . PHE B 2 667 ? -17.35300 55.17300  42.06400 1.000 72.23355  ? 667 PHE A CE1   1 
ATOM 5533 C CE2   . PHE B 2 667 ? -17.84400 52.87700  42.44200 1.000 87.66635  ? 667 PHE A CE2   1 
ATOM 5534 C CZ    . PHE B 2 667 ? -17.22000 53.85300  41.70500 1.000 69.86519  ? 667 PHE A CZ    1 
ATOM 5535 N N     . ASN B 2 668 ? -19.48100 56.86800  47.75300 1.000 93.38940  ? 668 ASN A N     1 
ATOM 5536 C CA    . ASN B 2 668 ? -20.00300 57.52800  48.95600 1.000 105.64551 ? 668 ASN A CA    1 
ATOM 5537 C C     . ASN B 2 668 ? -21.51100 57.74500  48.86000 1.000 116.00723 ? 668 ASN A C     1 
ATOM 5538 O O     . ASN B 2 668 ? -22.28300 57.10300  49.57400 1.000 134.37765 ? 668 ASN A O     1 
ATOM 5539 C CB    . ASN B 2 668 ? -19.26400 58.84700  49.18900 1.000 105.52957 ? 668 ASN A CB    1 
ATOM 5540 C CG    . ASN B 2 668 ? -17.95100 58.65400  49.91900 1.000 110.14395 ? 668 ASN A CG    1 
ATOM 5541 O OD1   . ASN B 2 668 ? -17.78500 57.69300  50.67200 1.000 104.13489 ? 668 ASN A OD1   1 
ATOM 5542 N ND2   . ASN B 2 668 ? -17.01100 59.57100  49.70600 1.000 87.17008  ? 668 ASN A ND2   1 
ATOM 5543 N N     . LYS B 2 669 ? -21.93300 58.66700  47.99600 1.000 95.63775  ? 669 LYS A N     1 
ATOM 5544 C CA    . LYS B 2 669 ? -23.35800 58.89700  47.80600 1.000 116.64067 ? 669 LYS A CA    1 
ATOM 5545 C C     . LYS B 2 669 ? -24.01600 57.63100  47.27600 1.000 118.83750 ? 669 LYS A C     1 
ATOM 5546 O O     . LYS B 2 669 ? -23.58100 57.06600  46.26700 1.000 119.51397 ? 669 LYS A O     1 
ATOM 5547 C CB    . LYS B 2 669 ? -23.58900 60.05900  46.83800 1.000 125.94638 ? 669 LYS A CB    1 
ATOM 5548 C CG    . LYS B 2 669 ? -22.70200 61.27200  47.07100 1.000 113.99060 ? 669 LYS A CG    1 
ATOM 5549 C CD    . LYS B 2 669 ? -22.86800 61.84400  48.46800 1.000 133.57912 ? 669 LYS A CD    1 
ATOM 5550 C CE    . LYS B 2 669 ? -22.03300 63.10600  48.63700 1.000 126.24084 ? 669 LYS A CE    1 
ATOM 5551 N NZ    . LYS B 2 669 ? -22.02100 63.59200  50.04500 1.000 143.64911 ? 669 LYS A NZ    1 
ATOM 5552 N N     . ASP B 2 670 ? -25.05300 57.17000  47.97000 1.000 102.42157 ? 670 ASP A N     1 
ATOM 5553 C CA    . ASP B 2 670 ? -25.78800 55.98600  47.53400 1.000 107.86156 ? 670 ASP A CA    1 
ATOM 5554 C C     . ASP B 2 670 ? -26.57900 56.34600  46.28400 1.000 119.96624 ? 670 ASP A C     1 
ATOM 5555 O O     . ASP B 2 670 ? -27.66800 56.91800  46.36100 1.000 136.86652 ? 670 ASP A O     1 
ATOM 5556 C CB    . ASP B 2 670 ? -26.69300 55.47500  48.64800 1.000 102.17410 ? 670 ASP A CB    1 
ATOM 5557 C CG    . ASP B 2 670 ? -25.91000 54.89800  49.80800 1.000 145.00171 ? 670 ASP A CG    1 
ATOM 5558 O OD1   . ASP B 2 670 ? -24.68400 55.13500  49.87200 1.000 144.27651 ? 670 ASP A OD1   1 
ATOM 5559 O OD2   . ASP B 2 670 ? -26.51300 54.19900  50.65000 1.000 149.88098 ? 670 ASP A OD2   1 
ATOM 5560 N N     . VAL B 2 671 ? -26.02000 56.01500  45.12500 1.000 121.12037 ? 671 VAL A N     1 
ATOM 5561 C CA    . VAL B 2 671 ? -26.58300 56.36900  43.82900 1.000 112.54131 ? 671 VAL A CA    1 
ATOM 5562 C C     . VAL B 2 671 ? -27.10600 55.10300  43.16700 1.000 100.89632 ? 671 VAL A C     1 
ATOM 5563 O O     . VAL B 2 671 ? -26.46900 54.04500  43.23800 1.000 114.34382 ? 671 VAL A O     1 
ATOM 5564 C CB    . VAL B 2 671 ? -25.53200 57.06600  42.94400 1.000 104.61454 ? 671 VAL A CB    1 
ATOM 5565 C CG1   . VAL B 2 671 ? -26.09200 57.35800  41.56100 1.000 117.80419 ? 671 VAL A CG1   1 
ATOM 5566 C CG2   . VAL B 2 671 ? -25.04800 58.34500  43.60900 1.000 93.08321  ? 671 VAL A CG2   1 
ATOM 5567 N N     . HIS B 2 672 ? -28.26700 55.21100  42.52900 1.000 93.38801  ? 672 HIS A N     1 
ATOM 5568 C CA    . HIS B 2 672 ? -28.85400 54.05800  41.86100 1.000 103.91427 ? 672 HIS A CA    1 
ATOM 5569 C C     . HIS B 2 672 ? -28.07100 53.71600  40.59900 1.000 100.00377 ? 672 HIS A C     1 
ATOM 5570 O O     . HIS B 2 672 ? -27.78800 54.58700  39.77100 1.000 98.20099  ? 672 HIS A O     1 
ATOM 5571 C CB    . HIS B 2 672 ? -30.31700 54.32700  41.51900 1.000 113.67818 ? 672 HIS A CB    1 
ATOM 5572 C CG    . HIS B 2 672 ? -30.95900 53.22900  40.73000 1.000 97.85911  ? 672 HIS A CG    1 
ATOM 5573 N ND1   . HIS B 2 672 ? -31.46400 53.42100  39.46200 1.000 124.94111 ? 672 HIS A ND1   1 
ATOM 5574 C CD2   . HIS B 2 672 ? -31.16700 51.92400  41.02500 1.000 98.11769  ? 672 HIS A CD2   1 
ATOM 5575 C CE1   . HIS B 2 672 ? -31.96100 52.28300  39.01200 1.000 130.47903 ? 672 HIS A CE1   1 
ATOM 5576 N NE2   . HIS B 2 672 ? -31.79200 51.35800  39.94100 1.000 120.56301 ? 672 HIS A NE2   1 
ATOM 5577 N N     . PHE B 2 673 ? -27.71500 52.44300  40.46300 1.000 106.56070 ? 673 PHE A N     1 
ATOM 5578 C CA    . PHE B 2 673 ? -27.07700 51.90200  39.27400 1.000 106.74262 ? 673 PHE A CA    1 
ATOM 5579 C C     . PHE B 2 673 ? -27.98100 50.84800  38.64700 1.000 102.02346 ? 673 PHE A C     1 
ATOM 5580 O O     . PHE B 2 673 ? -28.96200 50.39800  39.24500 1.000 107.51840 ? 673 PHE A O     1 
ATOM 5581 C CB    . PHE B 2 673 ? -25.71000 51.28400  39.60100 1.000 100.97511 ? 673 PHE A CB    1 
ATOM 5582 C CG    . PHE B 2 673 ? -24.62800 52.29100  39.86000 1.000 99.92002  ? 673 PHE A CG    1 
ATOM 5583 C CD1   . PHE B 2 673 ? -23.85100 52.77500  38.82000 1.000 91.00071  ? 673 PHE A CD1   1 
ATOM 5584 C CD2   . PHE B 2 673 ? -24.37800 52.74300  41.14500 1.000 102.65248 ? 673 PHE A CD2   1 
ATOM 5585 C CE1   . PHE B 2 673 ? -22.85300 53.69900  39.05600 1.000 92.42100  ? 673 PHE A CE1   1 
ATOM 5586 C CE2   . PHE B 2 673 ? -23.38100 53.66500  41.38800 1.000 95.86610  ? 673 PHE A CE2   1 
ATOM 5587 C CZ    . PHE B 2 673 ? -22.61700 54.14500  40.34200 1.000 97.89808  ? 673 PHE A CZ    1 
ATOM 5588 N N     . ASN B 2 674 ? -27.63200 50.45200  37.42700 1.000 90.44053  ? 674 ASN A N     1 
ATOM 5589 C CA    . ASN B 2 674 ? -28.29900 49.36500  36.72500 1.000 99.28628  ? 674 ASN A CA    1 
ATOM 5590 C C     . ASN B 2 674 ? -27.31100 48.22200  36.56100 1.000 100.59632 ? 674 ASN A C     1 
ATOM 5591 O O     . ASN B 2 674 ? -26.21800 48.41700  36.02100 1.000 123.10780 ? 674 ASN A O     1 
ATOM 5592 C CB    . ASN B 2 674 ? -28.82000 49.81600  35.35800 1.000 105.55416 ? 674 ASN A CB    1 
ATOM 5593 C CG    . ASN B 2 674 ? -29.87800 50.89400  35.46600 1.000 102.98209 ? 674 ASN A CG    1 
ATOM 5594 O OD1   . ASN B 2 674 ? -30.01700 51.73400  34.57800 1.000 101.42566 ? 674 ASN A OD1   1 
ATOM 5595 N ND2   . ASN B 2 674 ? -30.62300 50.88300  36.56500 1.000 105.90035 ? 674 ASN A ND2   1 
ATOM 5596 N N     . THR B 2 675 ? -27.70100 47.04000  37.04500 1.000 81.95141  ? 675 THR A N     1 
ATOM 5597 C CA    . THR B 2 675 ? -26.80100 45.87100  36.98800 1.000 84.66233  ? 675 THR A CA    1 
ATOM 5598 C C     . THR B 2 675 ? -27.21700 44.97400  35.84700 1.000 92.07215  ? 675 THR A C     1 
ATOM 5599 O O     . THR B 2 675 ? -28.42300 44.67500  35.74000 1.000 104.86620 ? 675 THR A O     1 
ATOM 5600 C CB    . THR B 2 675 ? -26.85200 45.13700  38.32500 1.000 107.95187 ? 675 THR A CB    1 
ATOM 5601 O OG1   . THR B 2 675 ? -25.89300 44.09000  38.20800 1.000 117.21157 ? 675 THR A OG1   1 
ATOM 5602 C CG2   . THR B 2 675 ? -28.22500 44.56100  38.62100 1.000 94.28907  ? 675 THR A CG2   1 
ATOM 5603 N N     . PHE B 2 676 ? -26.25100 44.55700  35.02700 1.000 92.64040  ? 676 PHE A N     1 
ATOM 5604 C CA    . PHE B 2 676 ? -26.53300 43.62800  33.90300 1.000 86.70091  ? 676 PHE A CA    1 
ATOM 5605 C C     . PHE B 2 676 ? -25.42600 42.58300  33.86200 1.000 94.65399  ? 676 PHE A C     1 
ATOM 5606 O O     . PHE B 2 676 ? -24.28400 42.89400  34.25700 1.000 102.88346 ? 676 PHE A O     1 
ATOM 5607 C CB    . PHE B 2 676 ? -26.58700 44.36300  32.56200 1.000 88.32418  ? 676 PHE A CB    1 
ATOM 5608 C CG    . PHE B 2 676 ? -27.44400 45.61900  32.52200 1.000 89.55144  ? 676 PHE A CG    1 
ATOM 5609 C CD1   . PHE B 2 676 ? -28.80400 45.54600  32.24800 1.000 98.24034  ? 676 PHE A CD1   1 
ATOM 5610 C CD2   . PHE B 2 676 ? -26.88200 46.87200  32.73400 1.000 98.36133  ? 676 PHE A CD2   1 
ATOM 5611 C CE1   . PHE B 2 676 ? -29.58000 46.69200  32.20500 1.000 92.09442  ? 676 PHE A CE1   1 
ATOM 5612 C CE2   . PHE B 2 676 ? -27.66200 48.01400  32.68700 1.000 88.90964  ? 676 PHE A CE2   1 
ATOM 5613 C CZ    . PHE B 2 676 ? -29.00800 47.92200  32.42300 1.000 90.64954  ? 676 PHE A CZ    1 
ATOM 5614 N N     . GLU B 2 677 ? -25.73900 41.38600  33.37200 1.000 104.57872 ? 677 GLU A N     1 
ATOM 5615 C CA    . GLU B 2 677 ? -24.72800 40.30300  33.34800 1.000 99.55235  ? 677 GLU A CA    1 
ATOM 5616 C C     . GLU B 2 677 ? -24.76300 39.59200  31.99300 1.000 99.61812  ? 677 GLU A C     1 
ATOM 5617 O O     . GLU B 2 677 ? -25.67500 38.76700  31.78800 1.000 148.20190 ? 677 GLU A O     1 
ATOM 5618 C CB    . GLU B 2 677 ? -24.98900 39.29000  34.45900 1.000 97.45650  ? 677 GLU A CB    1 
ATOM 5619 C CG    . GLU B 2 677 ? -23.94300 38.17900  34.50500 1.000 120.22953 ? 677 GLU A CG    1 
ATOM 5620 C CD    . GLU B 2 677 ? -24.29300 37.02700  35.42700 1.000 141.72568 ? 677 GLU A CD    1 
ATOM 5621 O OE1   . GLU B 2 677 ? -25.33500 36.38000  35.19300 1.000 135.34661 ? 677 GLU A OE1   1 
ATOM 5622 O OE2   . GLU B 2 677 ? -23.52300 36.77500  36.37600 1.000 139.79170 ? 677 GLU A OE2   1 
ATOM 5623 N N     . VAL B 2 678 ? -23.80300 39.87700  31.11200 1.000 115.54247 ? 678 VAL A N     1 
ATOM 5624 C CA    . VAL B 2 678 ? -23.72200 39.11900  29.82600 1.000 118.77852 ? 678 VAL A CA    1 
ATOM 5625 C C     . VAL B 2 678 ? -22.70400 37.98700  30.04500 1.000 132.97330 ? 678 VAL A C     1 
ATOM 5626 O O     . VAL B 2 678 ? -21.49500 38.22500  29.84800 1.000 120.90706 ? 678 VAL A O     1 
ATOM 5627 C CB    . VAL B 2 678 ? -23.38800 40.04400  28.64000 1.000 96.76611  ? 678 VAL A CB    1 
ATOM 5628 C CG1   . VAL B 2 678 ? -22.11800 40.85500  28.85600 1.000 116.08675 ? 678 VAL A CG1   1 
ATOM 5629 C CG2   . VAL B 2 678 ? -23.39000 39.32500  27.29900 1.000 129.67212 ? 678 VAL A CG2   1 
ATOM 5630 N N     . ASN B 2 679 ? -23.17600 36.80900  30.46200 1.000 141.27587 ? 679 ASN A N     1 
ATOM 5631 C CA    . ASN B 2 679 ? -22.25500 35.69400  30.82500 1.000 145.18027 ? 679 ASN A CA    1 
ATOM 5632 C C     . ASN B 2 679 ? -21.42100 35.22900  29.62700 1.000 152.30205 ? 679 ASN A C     1 
ATOM 5633 O O     . ASN B 2 679 ? -20.19000 35.12900  29.78900 1.000 159.49536 ? 679 ASN A O     1 
ATOM 5634 C CB    . ASN B 2 679 ? -23.01800 34.53000  31.44900 1.000 140.80068 ? 679 ASN A CB    1 
ATOM 5635 C CG    . ASN B 2 679 ? -24.14200 34.04500  30.56600 1.000 164.03355 ? 679 ASN A CG    1 
ATOM 5636 O OD1   . ASN B 2 679 ? -25.06100 34.80900  30.25200 1.000 167.11916 ? 679 ASN A OD1   1 
ATOM 5637 N ND2   . ASN B 2 679 ? -24.08600 32.78600  30.15500 1.000 165.57026 ? 679 ASN A ND2   1 
ATOM 5638 N N     . THR B 2 680 ? -22.06200 34.89100  28.50400 1.000 149.37876 ? 680 THR A N     1 
ATOM 5639 C CA    . THR B 2 680 ? -21.33200 34.44600  27.29300 1.000 151.94049 ? 680 THR A CA    1 
ATOM 5640 C C     . THR B 2 680 ? -20.43700 33.27000  27.64100 1.000 152.08966 ? 680 THR A C     1 
ATOM 5641 O O     . THR B 2 680 ? -19.50600 32.98900  26.85800 1.000 150.70512 ? 680 THR A O     1 
ATOM 5642 C CB    . THR B 2 680 ? -20.52800 35.62500  26.74700 1.000 159.29504 ? 680 THR A CB    1 
ATOM 5643 O OG1   . THR B 2 680 ? -21.36100 36.76300  26.93400 1.000 160.54346 ? 680 THR A OG1   1 
ATOM 5644 C CG2   . THR B 2 680 ? -20.17900 35.49100  25.27600 1.000 148.67792 ? 680 THR A CG2   1 
ATOM 5645 N N     . SER B 2 681 ? -20.69900 32.58700  28.76000 1.000 153.62382 ? 681 SER A N     1 
ATOM 5646 C CA    . SER B 2 681 ? -19.81000 31.48300  29.21100 1.000 165.08584 ? 681 SER A CA    1 
ATOM 5647 C C     . SER B 2 681 ? -19.81000 30.35900  28.16800 1.000 161.66429 ? 681 SER A C     1 
ATOM 5648 O O     . SER B 2 681 ? -18.70900 29.89400  27.80300 1.000 151.40071 ? 681 SER A O     1 
ATOM 5649 C CB    . SER B 2 681 ? -20.22500 30.97500  30.56700 1.000 157.94141 ? 681 SER A CB    1 
ATOM 5650 O OG    . SER B 2 681 ? -20.23400 32.03000  31.51900 1.000 150.47653 ? 681 SER A OG    1 
ATOM 5651 N N     . LEU B 2 682 ? -20.99600 29.93500  27.72400 1.000 164.10399 ? 682 LEU A N     1 
ATOM 5652 C CA    . LEU B 2 682 ? -21.10300 28.90200  26.65900 1.000 160.55995 ? 682 LEU A CA    1 
ATOM 5653 C C     . LEU B 2 682 ? -20.35500 27.62000  27.05300 1.000 157.22247 ? 682 LEU A C     1 
ATOM 5654 O O     . LEU B 2 682 ? -20.43400 27.22400  28.23600 1.000 151.39751 ? 682 LEU A O     1 
ATOM 5655 C CB    . LEU B 2 682 ? -20.57100 29.47300  25.34400 1.000 162.13643 ? 682 LEU A CB    1 
ATOM 5656 C CG    . LEU B 2 682 ? -21.61800 29.79400  24.27300 1.000 156.50452 ? 682 LEU A CG    1 
ATOM 5657 C CD1   . LEU B 2 682 ? -21.00600 30.61800  23.15500 1.000 160.09749 ? 682 LEU A CD1   1 
ATOM 5658 C CD2   . LEU B 2 682 ? -22.26400 28.53700  23.71900 1.000 149.66367 ? 682 LEU A CD2   1 
ATOM 5659 N N     . GLN B 2 683 ? -19.65200 27.00700  26.09700 1.000 155.12334 ? 683 GLN A N     1 
ATOM 5660 C CA    . GLN B 2 683 ? -18.96100 25.71300  26.33900 1.000 150.00522 ? 683 GLN A CA    1 
ATOM 5661 C C     . GLN B 2 683 ? -17.86400 25.85500  27.40100 1.000 154.24758 ? 683 GLN A C     1 
ATOM 5662 O O     . GLN B 2 683 ? -17.63700 24.87400  28.13900 1.000 160.03595 ? 683 GLN A O     1 
ATOM 5663 C CB    . GLN B 2 683 ? -18.35800 25.25200  25.01400 1.000 156.66131 ? 683 GLN A CB    1 
ATOM 5664 C CG    . GLN B 2 683 ? -19.38200 25.10500  23.89400 1.000 167.70484 ? 683 GLN A CG    1 
ATOM 5665 C CD    . GLN B 2 683 ? -18.77100 25.17100  22.51200 1.000 170.24642 ? 683 GLN A CD    1 
ATOM 5666 O OE1   . GLN B 2 683 ? -17.87700 24.39200  22.16200 1.000 165.32655 ? 683 GLN A OE1   1 
ATOM 5667 N NE2   . GLN B 2 683 ? -19.24500 26.11500  21.71200 1.000 172.32670 ? 683 GLN A NE2   1 
ATOM 5668 N N     . SER B 2 684 ? -17.20400 27.01200  27.46500 1.000 146.20091 ? 684 SER A N     1 
ATOM 5669 C CA    . SER B 2 684 ? -16.07500 27.19000  28.41400 1.000 143.56693 ? 684 SER A CA    1 
ATOM 5670 C C     . SER B 2 684 ? -16.38000 26.45800  29.72500 1.000 147.32489 ? 684 SER A C     1 
ATOM 5671 O O     . SER B 2 684 ? -15.58700 25.57100  30.10700 1.000 149.32080 ? 684 SER A O     1 
ATOM 5672 C CB    . SER B 2 684 ? -15.82900 28.64800  28.67000 1.000 144.53012 ? 684 SER A CB    1 
ATOM 5673 O OG    . SER B 2 684 ? -15.71700 29.36300  27.44800 1.000 158.30580 ? 684 SER A OG    1 
ATOM 5674 N N     . ALA B 2 685 ? -17.49100 26.80800  30.37200 1.000 151.10545 ? 685 ALA A N     1 
ATOM 5675 C CA    . ALA B 2 685 ? -17.85300 26.20000  31.67400 1.000 143.08614 ? 685 ALA A CA    1 
ATOM 5676 C C     . ALA B 2 685 ? -17.55500 24.70000  31.68700 1.000 137.50538 ? 685 ALA A C     1 
ATOM 5677 O O     . ALA B 2 685 ? -17.10300 24.19400  32.73300 1.000 139.75535 ? 685 ALA A O     1 
ATOM 5678 C CB    . ALA B 2 685 ? -19.31500 26.46000  31.94700 1.000 143.33961 ? 685 ALA A CB    1 
ATOM 5679 N N     . LYS B 2 686 ? -17.80000 24.00500  30.57500 1.000 131.55523 ? 686 LYS A N     1 
ATOM 5680 C CA    . LYS B 2 686 ? -17.64500 22.52700  30.58000 1.000 129.21752 ? 686 LYS A CA    1 
ATOM 5681 C C     . LYS B 2 686 ? -16.30100 22.12700  29.96100 1.000 130.03600 ? 686 LYS A C     1 
ATOM 5682 O O     . LYS B 2 686 ? -15.70700 21.14000  30.43600 1.000 142.15087 ? 686 LYS A O     1 
ATOM 5683 C CB    . LYS B 2 686 ? -18.83300 21.89500  29.85000 1.000 140.27788 ? 686 LYS A CB    1 
ATOM 5684 C CG    . LYS B 2 686 ? -20.15400 22.13200  30.56700 1.000 157.62457 ? 686 LYS A CG    1 
ATOM 5685 C CD    . LYS B 2 686 ? -20.08200 21.72500  32.03500 1.000 150.43022 ? 686 LYS A CD    1 
ATOM 5686 C CE    . LYS B 2 686 ? -21.24000 22.22300  32.83800 1.000 141.93622 ? 686 LYS A CE    1 
ATOM 5687 N NZ    . LYS B 2 686 ? -21.27500 23.68600  32.88700 1.000 127.98552 ? 686 LYS A NZ    1 
ATOM 5688 N N     . ASN B 2 687 ? -15.84600 22.85300  28.94400 1.000 123.59323 ? 687 ASN A N     1 
ATOM 5689 C CA    . ASN B 2 687 ? -14.50300 22.55100  28.38300 1.000 138.89186 ? 687 ASN A CA    1 
ATOM 5690 C C     . ASN B 2 687 ? -13.49600 22.56600  29.53600 1.000 127.09779 ? 687 ASN A C     1 
ATOM 5691 O O     . ASN B 2 687 ? -12.53900 21.76800  29.49600 1.000 113.04218 ? 687 ASN A O     1 
ATOM 5692 C CB    . ASN B 2 687 ? -14.13400 23.52700  27.27300 1.000 147.22432 ? 687 ASN A CB    1 
ATOM 5693 C CG    . ASN B 2 687 ? -13.70200 22.81900  26.01200 1.000 155.87422 ? 687 ASN A CG    1 
ATOM 5694 O OD1   . ASN B 2 687 ? -13.62700 21.58600  25.98500 1.000 159.50836 ? 687 ASN A OD1   1 
ATOM 5695 N ND2   . ASN B 2 687 ? -13.41200 23.57500  24.96400 1.000 157.06928 ? 687 ASN A ND2   1 
ATOM 5696 N N     . THR B 2 688 ? -13.71900 23.42600  30.53300 1.000 119.69770 ? 688 THR A N     1 
ATOM 5697 C CA    . THR B 2 688 ? -12.76700 23.55800  31.65600 1.000 111.57051 ? 688 THR A CA    1 
ATOM 5698 C C     . THR B 2 688 ? -13.09100 22.55800  32.74000 1.000 109.71886 ? 688 THR A C     1 
ATOM 5699 O O     . THR B 2 688 ? -14.24800 22.09800  32.79100 1.000 125.57358 ? 688 THR A O     1 
ATOM 5700 C CB    . THR B 2 688 ? -12.78900 24.98900  32.22500 1.000 114.99895 ? 688 THR A CB    1 
ATOM 5701 O OG1   . THR B 2 688 ? -14.11200 25.30900  32.66900 1.000 137.07585 ? 688 THR A OG1   1 
ATOM 5702 C CG2   . THR B 2 688 ? -12.53400 26.00600  31.12300 1.000 127.88111 ? 688 THR A CG2   1 
ATOM 5703 N N     . SER B 2 689 ? -12.10900 22.23500  33.58500 1.000 103.15401 ? 689 SER A N     1 
ATOM 5704 C CA    . SER B 2 689 ? -12.32800 21.30600  34.72300 1.000 87.95225  ? 689 SER A CA    1 
ATOM 5705 C C     . SER B 2 689 ? -11.52400 21.79300  35.93600 1.000 91.30539  ? 689 SER A C     1 
ATOM 5706 O O     . SER B 2 689 ? -10.53900 22.52500  35.72900 1.000 91.14776  ? 689 SER A O     1 
ATOM 5707 C CB    . SER B 2 689 ? -11.95300 19.90300  34.34600 1.000 88.96068  ? 689 SER A CB    1 
ATOM 5708 O OG    . SER B 2 689 ? -12.65300 19.48600  33.18200 1.000 92.42262  ? 689 SER A OG    1 
ATOM 5709 N N     . VAL B 2 690 ? -11.93400 21.41200  37.14800 1.000 81.92690  ? 690 VAL A N     1 
ATOM 5710 C CA    . VAL B 2 690 ? -11.24600 21.90200  38.37900 1.000 77.03946  ? 690 VAL A CA    1 
ATOM 5711 C C     . VAL B 2 690 ? -10.81000 20.69900  39.22700 1.000 79.16132  ? 690 VAL A C     1 
ATOM 5712 O O     . VAL B 2 690 ? -11.58800 19.72900  39.31400 1.000 88.88000  ? 690 VAL A O     1 
ATOM 5713 C CB    . VAL B 2 690 ? -12.15200 22.85000  39.18600 1.000 78.05294  ? 690 VAL A CB    1 
ATOM 5714 C CG1   . VAL B 2 690 ? -11.53000 23.23700  40.52200 1.000 72.91335  ? 690 VAL A CG1   1 
ATOM 5715 C CG2   . VAL B 2 690 ? -12.51700 24.09600  38.38900 1.000 82.53737  ? 690 VAL A CG2   1 
ATOM 5716 N N     . PHE B 2 691 ? -9.61400  20.76300  39.81700 1.000 89.62139  ? 691 PHE A N     1 
ATOM 5717 C CA    . PHE B 2 691 ? -9.12700  19.67000  40.70200 1.000 76.24597  ? 691 PHE A CA    1 
ATOM 5718 C C     . PHE B 2 691 ? -8.68000  20.28000  42.02100 1.000 79.30226  ? 691 PHE A C     1 
ATOM 5719 O O     . PHE B 2 691 ? -7.88500  21.24000  42.01000 1.000 85.83361  ? 691 PHE A O     1 
ATOM 5720 C CB    . PHE B 2 691 ? -7.98900  18.88400  40.04300 1.000 77.66892  ? 691 PHE A CB    1 
ATOM 5721 C CG    . PHE B 2 691 ? -7.61200  17.59300  40.75700 1.000 78.43227  ? 691 PHE A CG    1 
ATOM 5722 C CD1   . PHE B 2 691 ? -8.25600  16.39900  40.45600 1.000 87.92906  ? 691 PHE A CD1   1 
ATOM 5723 C CD2   . PHE B 2 691 ? -6.62000  17.57600  41.73000 1.000 77.72770  ? 691 PHE A CD2   1 
ATOM 5724 C CE1   . PHE B 2 691 ? -7.91500  15.22500  41.10900 1.000 79.62914  ? 691 PHE A CE1   1 
ATOM 5725 C CE2   . PHE B 2 691 ? -6.28300  16.39900  42.37900 1.000 86.63856  ? 691 PHE A CE2   1 
ATOM 5726 C CZ    . PHE B 2 691 ? -6.93100  15.22800  42.06800 1.000 78.00069  ? 691 PHE A CZ    1 
ATOM 5727 N N     . ILE B 2 692 ? -9.18400  19.74400  43.13100 1.000 71.83349  ? 692 ILE A N     1 
ATOM 5728 C CA    . ILE B 2 692 ? -8.80800  20.24200  44.45400 1.000 80.63031  ? 692 ILE A CA    1 
ATOM 5729 C C     . ILE B 2 692 ? -8.07000  19.14500  45.21600 1.000 78.57015  ? 692 ILE A C     1 
ATOM 5730 O O     . ILE B 2 692 ? -8.69300  18.39700  45.98100 1.000 79.83405  ? 692 ILE A O     1 
ATOM 5731 C CB    . ILE B 2 692 ? -10.03700 20.74700  45.22800 1.000 71.86578  ? 692 ILE A CB    1 
ATOM 5732 C CG1   . ILE B 2 692 ? -10.77900 21.80900  44.41200 1.000 73.81914  ? 692 ILE A CG1   1 
ATOM 5733 C CG2   . ILE B 2 692 ? -9.62800  21.33800  46.56800 1.000 68.86407  ? 692 ILE A CG2   1 
ATOM 5734 C CD1   . ILE B 2 692 ? -12.01300 21.29700  43.70600 1.000 92.40505  ? 692 ILE A CD1   1 
ATOM 5735 N N     . PRO B 2 693 ? -6.74200  19.03100  45.05000 1.000 92.93660  ? 693 PRO A N     1 
ATOM 5736 C CA    . PRO B 2 693 ? -5.98400  17.94000  45.68300 1.000 86.94541  ? 693 PRO A CA    1 
ATOM 5737 C C     . PRO B 2 693 ? -6.28400  17.71300  47.15700 1.000 93.97337  ? 693 PRO A C     1 
ATOM 5738 O O     . PRO B 2 693 ? -6.36300  18.66000  47.94900 1.000 81.24573  ? 693 PRO A O     1 
ATOM 5739 C CB    . PRO B 2 693 ? -4.52400  18.37600  45.48800 1.000 81.23040  ? 693 PRO A CB    1 
ATOM 5740 C CG    . PRO B 2 693 ? -4.57800  19.79600  44.98900 1.000 78.11171  ? 693 PRO A CG    1 
ATOM 5741 C CD    . PRO B 2 693 ? -5.86600  19.90400  44.25800 1.000 87.15997  ? 693 PRO A CD    1 
ATOM 5742 N N     . SER B 2 694 ? -6.45700  16.44200  47.52000 1.000 97.78514  ? 694 SER A N     1 
ATOM 5743 C CA    . SER B 2 694 ? -6.72000  16.02800  48.89000 1.000 94.05577  ? 694 SER A CA    1 
ATOM 5744 C C     . SER B 2 694 ? -5.48300  15.48900  49.59000 1.000 97.61424  ? 694 SER A C     1 
ATOM 5745 O O     . SER B 2 694 ? -5.54500  15.19200  50.78600 1.000 103.40440 ? 694 SER A O     1 
ATOM 5746 C CB    . SER B 2 694 ? -7.81800  14.96100  48.91600 1.000 76.02042  ? 694 SER A CB    1 
ATOM 5747 O OG    . SER B 2 694 ? -7.40200  13.79500  48.22400 1.000 77.27402  ? 694 SER A OG    1 
ATOM 5748 N N     . ASP B 2 695 ? -4.38400  15.34500  48.84800 1.000 100.59911 ? 695 ASP A N     1 
ATOM 5749 C CA    . ASP B 2 695 ? -3.13200  14.79600  49.43600 1.000 79.62828  ? 695 ASP A CA    1 
ATOM 5750 C C     . ASP B 2 695 ? -2.13300  15.93500  49.64100 1.000 90.05223  ? 695 ASP A C     1 
ATOM 5751 O O     . ASP B 2 695 ? -0.93100  15.64500  49.80300 1.000 115.91605 ? 695 ASP A O     1 
ATOM 5752 C CB    . ASP B 2 695 ? -2.57600  13.66200  48.59300 1.000 98.99365  ? 695 ASP A CB    1 
ATOM 5753 C CG    . ASP B 2 695 ? -2.51900  13.92400  47.09700 1.000 89.38944  ? 695 ASP A CG    1 
ATOM 5754 O OD1   . ASP B 2 695 ? -2.85200  15.05200  46.68600 1.000 100.18343 ? 695 ASP A OD1   1 
ATOM 5755 O OD2   . ASP B 2 695 ? -2.16100  12.98600  46.36100 1.000 84.95703  ? 695 ASP A OD2   1 
ATOM 5756 N N     . VAL B 2 696 ? -2.61500  17.17900  49.63000 1.000 97.88252  ? 696 VAL A N     1 
ATOM 5757 C CA    . VAL B 2 696 ? -1.72200  18.34500  49.89800 1.000 101.53270 ? 696 VAL A CA    1 
ATOM 5758 C C     . VAL B 2 696 ? -2.00200  18.82600  51.32800 1.000 101.82696 ? 696 VAL A C     1 
ATOM 5759 O O     . VAL B 2 696 ? -3.17600  18.77600  51.74900 1.000 105.86401 ? 696 VAL A O     1 
ATOM 5760 C CB    . VAL B 2 696 ? -1.89800  19.48200  48.87500 1.000 96.23418  ? 696 VAL A CB    1 
ATOM 5761 C CG1   . VAL B 2 696 ? -1.40300  19.07800  47.49200 1.000 86.38288  ? 696 VAL A CG1   1 
ATOM 5762 C CG2   . VAL B 2 696 ? -3.33900  19.97100  48.80700 1.000 111.84699 ? 696 VAL A CG2   1 
ATOM 5763 N N     . ALA B 2 697 ? -0.96500  19.26000  52.04300 1.000 95.44631  ? 697 ALA A N     1 
ATOM 5764 C CA    . ALA B 2 697 ? -1.14000  19.66700  53.45600 1.000 92.62528  ? 697 ALA A CA    1 
ATOM 5765 C C     . ALA B 2 697 ? -1.70600  21.08400  53.53200 1.000 98.17614  ? 697 ALA A C     1 
ATOM 5766 O O     . ALA B 2 697 ? -1.99400  21.68600  52.47900 1.000 107.80039 ? 697 ALA A O     1 
ATOM 5767 C CB    . ALA B 2 697 ? 0.18000   19.56900  54.18200 1.000 105.60294 ? 697 ALA A CB    1 
ATOM 5768 N N     . SER B 2 698 ? -1.86100  21.59600  54.75300 1.000 96.88650  ? 698 SER A N     1 
ATOM 5769 C CA    . SER B 2 698 ? -2.37700  22.97400  54.93800 1.000 104.54685 ? 698 SER A CA    1 
ATOM 5770 C C     . SER B 2 698 ? -1.24400  23.98000  54.70200 1.000 108.17621 ? 698 SER A C     1 
ATOM 5771 O O     . SER B 2 698 ? -0.15000  23.78100  55.27000 1.000 108.44972 ? 698 SER A O     1 
ATOM 5772 C CB    . SER B 2 698 ? -2.97000  23.13800  56.30600 1.000 117.93955 ? 698 SER A CB    1 
ATOM 5773 O OG    . SER B 2 698 ? -3.99400  22.17800  56.52800 1.000 120.48266 ? 698 SER A OG    1 
ATOM 5774 N N     . TYR B 2 699 ? -1.50200  25.01600  53.90000 1.000 120.23236 ? 699 TYR A N     1 
ATOM 5775 C CA    . TYR B 2 699 ? -0.47600  26.06100  53.64300 1.000 113.05440 ? 699 TYR A CA    1 
ATOM 5776 C C     . TYR B 2 699 ? -0.07900  26.68400  54.96900 1.000 124.10509 ? 699 TYR A C     1 
ATOM 5777 O O     . TYR B 2 699 ? -0.96800  27.08600  55.74900 1.000 128.05349 ? 699 TYR A O     1 
ATOM 5778 C CB    . TYR B 2 699 ? -1.00800  27.12900  52.68400 1.000 116.55107 ? 699 TYR A CB    1 
ATOM 5779 C CG    . TYR B 2 699 ? -0.22100  28.43300  52.68900 1.000 117.05078 ? 699 TYR A CG    1 
ATOM 5780 C CD1   . TYR B 2 699 ? 0.92600   28.58200  51.91900 1.000 123.17113 ? 699 TYR A CD1   1 
ATOM 5781 C CD2   . TYR B 2 699 ? -0.61600  29.50800  53.47500 1.000 124.18157 ? 699 TYR A CD2   1 
ATOM 5782 C CE1   . TYR B 2 699 ? 1.64800   29.76300  51.92300 1.000 117.96589 ? 699 TYR A CE1   1 
ATOM 5783 C CE2   . TYR B 2 699 ? 0.09700   30.69500  53.48800 1.000 125.89830 ? 699 TYR A CE2   1 
ATOM 5784 C CZ    . TYR B 2 699 ? 1.23300   30.82200  52.71000 1.000 135.05126 ? 699 TYR A CZ    1 
ATOM 5785 O OH    . TYR B 2 699 ? 1.94100   31.98800  52.71900 1.000 140.18697 ? 699 TYR A OH    1 
ATOM 5786 N N     . GLN B 2 700 ? 1.22700   26.76400  55.22300 1.000 125.97103 ? 700 GLN A N     1 
ATOM 5787 C CA    . GLN B 2 700 ? 1.71600   27.39700  56.47200 1.000 132.43900 ? 700 GLN A CA    1 
ATOM 5788 C C     . GLN B 2 700 ? 3.06800   28.06700  56.19000 1.000 132.81543 ? 700 GLN A C     1 
ATOM 5789 O O     . GLN B 2 700 ? 3.98000   27.37900  55.68100 1.000 133.81843 ? 700 GLN A O     1 
ATOM 5790 C CB    . GLN B 2 700 ? 1.79800   26.35800  57.59200 1.000 124.65785 ? 700 GLN A CB    1 
ATOM 5791 C CG    . GLN B 2 700 ? 2.52800   25.07600  57.20900 1.000 114.02055 ? 700 GLN A CG    1 
ATOM 5792 C CD    . GLN B 2 700 ? 2.42300   24.00000  58.26600 1.000 145.93219 ? 700 GLN A CD    1 
ATOM 5793 O OE1   . GLN B 2 700 ? 1.32900   23.54300  58.61500 1.000 146.49533 ? 700 GLN A OE1   1 
ATOM 5794 N NE2   . GLN B 2 700 ? 3.56600   23.58600  58.79300 1.000 148.01357 ? 700 GLN A NE2   1 
ATOM 5795 N N     . TYR B 2 701 ? 3.19000   29.35600  56.51400 1.000 123.72875 ? 701 TYR A N     1 
ATOM 5796 C CA    . TYR B 2 701 ? 4.48600   30.06500  56.33600 1.000 132.37937 ? 701 TYR A CA    1 
ATOM 5797 C C     . TYR B 2 701 ? 5.51400   29.40000  57.24900 1.000 140.95618 ? 701 TYR A C     1 
ATOM 5798 O O     . TYR B 2 701 ? 6.73100   29.57900  57.03200 1.000 131.58072 ? 701 TYR A O     1 
ATOM 5799 C CB    . TYR B 2 701 ? 4.30000   31.56300  56.59600 1.000 113.62142 ? 701 TYR A CB    1 
ATOM 5800 C CG    . TYR B 2 701 ? 3.33600   31.90600  57.72300 1.000 144.47541 ? 701 TYR A CG    1 
ATOM 5801 C CD1   . TYR B 2 701 ? 3.77800   32.02900  59.03400 1.000 150.53350 ? 701 TYR A CD1   1 
ATOM 5802 C CD2   . TYR B 2 701 ? 1.98500   32.11600  57.47300 1.000 134.86155 ? 701 TYR A CD2   1 
ATOM 5803 C CE1   . TYR B 2 701 ? 2.90600   32.34300  60.06300 1.000 157.74081 ? 701 TYR A CE1   1 
ATOM 5804 C CE2   . TYR B 2 701 ? 1.10300   32.42700  58.49400 1.000 125.75444 ? 701 TYR A CE2   1 
ATOM 5805 C CZ    . TYR B 2 701 ? 1.56500   32.54400  59.79200 1.000 141.60731 ? 701 TYR A CZ    1 
ATOM 5806 O OH    . TYR B 2 701 ? 0.70300   32.85300  60.80400 1.000 136.88814 ? 701 TYR A OH    1 
ATOM 5807 N N     . LYS B 2 702 ? 5.03900   28.65400  58.25000 1.000 140.83171 ? 702 LYS A N     1 
ATOM 5808 C CA    . LYS B 2 702 ? 5.96000   27.90700  59.14200 1.000 144.94628 ? 702 LYS A CA    1 
ATOM 5809 C C     . LYS B 2 702 ? 6.76700   26.90300  58.31000 1.000 146.39164 ? 702 LYS A C     1 
ATOM 5810 O O     . LYS B 2 702 ? 8.01300   26.97800  58.33800 1.000 149.57099 ? 702 LYS A O     1 
ATOM 5811 C CB    . LYS B 2 702 ? 5.14600   27.16000  60.20100 1.000 136.63983 ? 702 LYS A CB    1 
ATOM 5812 C CG    . LYS B 2 702 ? 5.89700   26.08000  60.96700 1.000 138.97801 ? 702 LYS A CG    1 
ATOM 5813 C CD    . LYS B 2 702 ? 7.09400   26.60400  61.75000 1.000 134.08088 ? 702 LYS A CD    1 
ATOM 5814 C CE    . LYS B 2 702 ? 7.85500   25.50400  62.41800 1.000 144.22369 ? 702 LYS A CE    1 
ATOM 5815 N NZ    . LYS B 2 702 ? 9.00000   26.02200  63.17100 1.000 160.43937 ? 702 LYS A NZ    1 
ATOM 5816 N N     . ASN B 2 703 ? 6.08100   26.02000  57.58200 1.000 146.23510 ? 703 ASN A N     1 
ATOM 5817 C CA    . ASN B 2 703 ? 6.78100   24.96900  56.79300 1.000 149.65813 ? 703 ASN A CA    1 
ATOM 5818 C C     . ASN B 2 703 ? 6.29400   25.01800  55.34400 1.000 141.58577 ? 703 ASN A C     1 
ATOM 5819 O O     . ASN B 2 703 ? 5.49500   24.14100  54.95500 1.000 136.71878 ? 703 ASN A O     1 
ATOM 5820 C CB    . ASN B 2 703 ? 6.58000   23.58400  57.39700 1.000 146.01604 ? 703 ASN A CB    1 
ATOM 5821 C CG    . ASN B 2 703 ? 7.40200   23.36300  58.64400 1.000 149.82292 ? 703 ASN A CG    1 
ATOM 5822 O OD1   . ASN B 2 703 ? 8.19300   24.22800  59.03400 1.000 136.02327 ? 703 ASN A OD1   1 
ATOM 5823 N ND2   . ASN B 2 703 ? 7.24300   22.20700  59.27100 1.000 151.57194 ? 703 ASN A ND2   1 
ATOM 5824 N N     . ILE B 2 704 ? 6.76400   26.00100  54.57800 1.000 113.23149 ? 704 ILE A N     1 
ATOM 5825 C CA    . ILE B 2 704 ? 6.37500   26.12500  53.14200 1.000 115.70595 ? 704 ILE A CA    1 
ATOM 5826 C C     . ILE B 2 704 ? 7.06800   25.00400  52.35400 1.000 113.47255 ? 704 ILE A C     1 
ATOM 5827 O O     . ILE B 2 704 ? 6.65300   24.74000  51.20600 1.000 111.27070 ? 704 ILE A O     1 
ATOM 5828 C CB    . ILE B 2 704 ? 6.76600   27.52400  52.63300 1.000 92.40469  ? 704 ILE A CB    1 
ATOM 5829 C CG1   . ILE B 2 704 ? 6.28700   27.78400  51.20800 1.000 93.24304  ? 704 ILE A CG1   1 
ATOM 5830 C CG2   . ILE B 2 704 ? 8.27200   27.74800  52.77100 1.000 100.46684 ? 704 ILE A CG2   1 
ATOM 5831 C CD1   . ILE B 2 704 ? 6.72800   29.12800  50.65800 1.000 107.22660 ? 704 ILE A CD1   1 
ATOM 5832 N N     . ASP B 2 705 ? 8.05800   24.34500  52.95800 1.000 123.61798 ? 705 ASP A N     1 
ATOM 5833 C CA    . ASP B 2 705 ? 8.85100   23.30900  52.23800 1.000 126.02896 ? 705 ASP A CA    1 
ATOM 5834 C C     . ASP B 2 705 ? 7.95500   22.17200  51.73700 1.000 109.52974 ? 705 ASP A C     1 
ATOM 5835 O O     . ASP B 2 705 ? 8.02600   21.85600  50.53400 1.000 94.11124  ? 705 ASP A O     1 
ATOM 5836 C CB    . ASP B 2 705 ? 9.98500   22.80400  53.11600 1.000 123.61596 ? 705 ASP A CB    1 
ATOM 5837 C CG    . ASP B 2 705 ? 9.59500   22.44300  54.54300 1.000 147.22072 ? 705 ASP A CG    1 
ATOM 5838 O OD1   . ASP B 2 705 ? 8.39400   22.54600  54.86700 1.000 143.11205 ? 705 ASP A OD1   1 
ATOM 5839 O OD2   . ASP B 2 705 ? 10.49800  22.07000  55.32000 1.000 155.89325 ? 705 ASP A OD2   1 
ATOM 5840 N N     . GLU B 2 706 ? 7.15000   21.57200  52.61300 1.000 105.20447 ? 706 GLU A N     1 
ATOM 5841 C CA    . GLU B 2 706 ? 6.34000   20.39900  52.18700 1.000 99.02392  ? 706 GLU A CA    1 
ATOM 5842 C C     . GLU B 2 706 ? 5.29800   20.85500  51.15500 1.000 98.00314  ? 706 GLU A C     1 
ATOM 5843 O O     . GLU B 2 706 ? 4.98400   20.06700  50.24000 1.000 83.94666  ? 706 GLU A O     1 
ATOM 5844 C CB    . GLU B 2 706 ? 5.69100   19.70900  53.38700 1.000 127.82240 ? 706 GLU A CB    1 
ATOM 5845 C CG    . GLU B 2 706 ? 6.58700   19.64800  54.62100 1.000 150.70872 ? 706 GLU A CG    1 
ATOM 5846 C CD    . GLU B 2 706 ? 6.35400   20.76800  55.61600 1.000 153.73078 ? 706 GLU A CD    1 
ATOM 5847 O OE1   . GLU B 2 706 ? 6.15100   21.91900  55.17400 1.000 132.00375 ? 706 GLU A OE1   1 
ATOM 5848 O OE2   . GLU B 2 706 ? 6.38700   20.49000  56.83200 1.000 156.91345 ? 706 GLU A OE2   1 
ATOM 5849 N N     . TYR B 2 707 ? 4.78600   22.07800  51.30300 1.000 98.30039  ? 707 TYR A N     1 
ATOM 5850 C CA    . TYR B 2 707 ? 3.74600   22.59300  50.37600 1.000 88.35918  ? 707 TYR A CA    1 
ATOM 5851 C C     . TYR B 2 707 ? 4.35300   22.72500  48.98300 1.000 85.17958  ? 707 TYR A C     1 
ATOM 5852 O O     . TYR B 2 707 ? 3.75000   22.24600  48.00400 1.000 94.31095  ? 707 TYR A O     1 
ATOM 5853 C CB    . TYR B 2 707 ? 3.21300   23.91100  50.94400 1.000 79.64934  ? 707 TYR A CB    1 
ATOM 5854 C CG    . TYR B 2 707 ? 1.87400   24.37500  50.38700 1.000 78.69499  ? 707 TYR A CG    1 
ATOM 5855 C CD1   . TYR B 2 707 ? 0.67900   23.91000  50.92000 1.000 76.39500  ? 707 TYR A CD1   1 
ATOM 5856 C CD2   . TYR B 2 707 ? 1.80600   25.29900  49.35200 1.000 89.92232  ? 707 TYR A CD2   1 
ATOM 5857 C CE1   . TYR B 2 707 ? -0.54300  24.33200  50.42600 1.000 105.55723 ? 707 TYR A CE1   1 
ATOM 5858 C CE2   . TYR B 2 707 ? 0.59000   25.73100  48.85100 1.000 91.01896  ? 707 TYR A CE2   1 
ATOM 5859 C CZ    . TYR B 2 707 ? -0.58700  25.24700  49.39000 1.000 107.73795 ? 707 TYR A CZ    1 
ATOM 5860 O OH    . TYR B 2 707 ? -1.79000  25.66800  48.90300 1.000 106.85499 ? 707 TYR A OH    1 
ATOM 5861 N N     . VAL B 2 708 ? 5.53200   23.34200  48.89600 1.000 77.84213  ? 708 VAL A N     1 
ATOM 5862 C CA    . VAL B 2 708 ? 6.17800   23.55400  47.56500 1.000 84.96266  ? 708 VAL A CA    1 
ATOM 5863 C C     . VAL B 2 708 ? 6.53800   22.17400  46.99200 1.000 86.26820  ? 708 VAL A C     1 
ATOM 5864 O O     . VAL B 2 708 ? 6.45700   22.00900  45.75900 1.000 93.21867  ? 708 VAL A O     1 
ATOM 5865 C CB    . VAL B 2 708 ? 7.39800   24.49600  47.61700 1.000 86.97155  ? 708 VAL A CB    1 
ATOM 5866 C CG1   . VAL B 2 708 ? 8.57500   23.89700  48.37300 1.000 102.52565 ? 708 VAL A CG1   1 
ATOM 5867 C CG2   . VAL B 2 708 ? 7.83200   24.94200  46.22800 1.000 87.80028  ? 708 VAL A CG2   1 
ATOM 5868 N N     . ALA B 2 709 ? 6.89800   21.22400  47.85700 1.000 91.27747  ? 709 ALA A N     1 
ATOM 5869 C CA    . ALA B 2 709 ? 7.21800   19.85300  47.39600 1.000 95.65682  ? 709 ALA A CA    1 
ATOM 5870 C C     . ALA B 2 709 ? 5.96500   19.22100  46.79500 1.000 88.61767  ? 709 ALA A C     1 
ATOM 5871 O O     . ALA B 2 709 ? 6.06400   18.53500  45.76000 1.000 89.02809  ? 709 ALA A O     1 
ATOM 5872 C CB    . ALA B 2 709 ? 7.74800   19.03000  48.54300 1.000 95.70745  ? 709 ALA A CB    1 
ATOM 5873 N N     . SER B 2 710 ? 4.81500   19.42500  47.43500 1.000 86.45072  ? 710 SER A N     1 
ATOM 5874 C CA    . SER B 2 710 ? 3.58600   18.91500  46.83500 1.000 80.76035  ? 710 SER A CA    1 
ATOM 5875 C C     . SER B 2 710 ? 3.29900   19.60200  45.50600 1.000 80.45699  ? 710 SER A C     1 
ATOM 5876 O O     . SER B 2 710 ? 2.91300   18.94500  44.52600 1.000 82.05031  ? 710 SER A O     1 
ATOM 5877 C CB    . SER B 2 710 ? 2.41800   19.10300  47.80100 1.000 78.34612  ? 710 SER A CB    1 
ATOM 5878 O OG    . SER B 2 710 ? 2.63300   18.38400  49.00500 1.000 102.08209 ? 710 SER A OG    1 
ATOM 5879 N N     . ILE B 2 711 ? 3.49200   20.92300  45.45200 1.000 80.45098  ? 711 ILE A N     1 
ATOM 5880 C CA    . ILE B 2 711 ? 3.24400   21.66200  44.21400 1.000 80.58597  ? 711 ILE A CA    1 
ATOM 5881 C C     . ILE B 2 711 ? 4.13700   21.14100  43.09300 1.000 78.50338  ? 711 ILE A C     1 
ATOM 5882 O O     . ILE B 2 711 ? 3.67700   20.90200  41.96600 1.000 82.06674  ? 711 ILE A O     1 
ATOM 5883 C CB    . ILE B 2 711 ? 3.44400   23.17200  44.43700 1.000 72.51701  ? 711 ILE A CB    1 
ATOM 5884 C CG1   . ILE B 2 711 ? 2.46600   23.69400  45.49300 1.000 93.04890  ? 711 ILE A CG1   1 
ATOM 5885 C CG2   . ILE B 2 711 ? 3.27400   23.92900  43.13000 1.000 73.04202  ? 711 ILE A CG2   1 
ATOM 5886 C CD1   . ILE B 2 711 ? 2.47400   25.20500  45.63400 1.000 82.88469  ? 711 ILE A CD1   1 
ATOM 5887 N N     . VAL B 2 712 ? 5.42600   20.94400  43.38300 1.000 82.36977  ? 712 VAL A N     1 
ATOM 5888 C CA    . VAL B 2 712 ? 6.31300   20.44400  42.33700 1.000 85.98201  ? 712 VAL A CA    1 
ATOM 5889 C C     . VAL B 2 712 ? 5.96500   19.00100  41.98600 1.000 81.03757  ? 712 VAL A C     1 
ATOM 5890 O O     . VAL B 2 712 ? 6.12500   18.58600  40.83200 1.000 85.44310  ? 712 VAL A O     1 
ATOM 5891 C CB    . VAL B 2 712 ? 7.79700   20.60700  42.73500 1.000 83.12900  ? 712 VAL A CB    1 
ATOM 5892 C CG1   . VAL B 2 712 ? 8.09900   19.90400  44.02900 1.000 103.29630 ? 712 VAL A CG1   1 
ATOM 5893 C CG2   . VAL B 2 712 ? 8.70900   20.07100  41.64500 1.000 81.89289  ? 712 VAL A CG2   1 
ATOM 5894 N N     . SER B 2 713 ? 5.45900   18.22300  42.94800 1.000 89.61443  ? 713 SER A N     1 
ATOM 5895 C CA    . SER B 2 713 ? 4.94800   16.89500  42.61200 1.000 91.61421  ? 713 SER A CA    1 
ATOM 5896 C C     . SER B 2 713 ? 3.85000   16.97800  41.55900 1.000 90.49610  ? 713 SER A C     1 
ATOM 5897 O O     . SER B 2 713 ? 3.85600   16.22300  40.57600 1.000 87.40731  ? 713 SER A O     1 
ATOM 5898 C CB    . SER B 2 713 ? 4.43100   16.18900  43.86700 1.000 90.70469  ? 713 SER A CB    1 
ATOM 5899 O OG    . SER B 2 713 ? 5.49200   15.60400  44.60300 1.000 122.21671 ? 713 SER A OG    1 
ATOM 5900 N N     . TYR B 2 714 ? 2.90800   17.90700  41.73500 1.000 97.37836  ? 714 TYR A N     1 
ATOM 5901 C CA    . TYR B 2 714 ? 1.82400   18.03000  40.76500 1.000 90.26599  ? 714 TYR A CA    1 
ATOM 5902 C C     . TYR B 2 714 ? 2.33200   18.51300  39.41000 1.000 84.18051  ? 714 TYR A C     1 
ATOM 5903 O O     . TYR B 2 714 ? 1.90000   18.00400  38.36600 1.000 89.42447  ? 714 TYR A O     1 
ATOM 5904 C CB    . TYR B 2 714 ? 0.73400   18.94900  41.31300 1.000 79.30303  ? 714 TYR A CB    1 
ATOM 5905 C CG    . TYR B 2 714 ? -0.24200  18.18900  42.17200 1.000 83.45036  ? 714 TYR A CG    1 
ATOM 5906 C CD1   . TYR B 2 714 ? 0.08700   17.82000  43.46900 1.000 87.56274  ? 714 TYR A CD1   1 
ATOM 5907 C CD2   . TYR B 2 714 ? -1.48000  17.80600  41.67300 1.000 77.60549  ? 714 TYR A CD2   1 
ATOM 5908 C CE1   . TYR B 2 714 ? -0.79600  17.10700  44.25100 1.000 86.12171  ? 714 TYR A CE1   1 
ATOM 5909 C CE2   . TYR B 2 714 ? -2.37100  17.09400  42.44400 1.000 75.85666  ? 714 TYR A CE2   1 
ATOM 5910 C CZ    . TYR B 2 714 ? -2.02500  16.74600  43.73200 1.000 83.71491  ? 714 TYR A CZ    1 
ATOM 5911 O OH    . TYR B 2 714 ? -2.91300  16.03000  44.49900 1.000 85.04637  ? 714 TYR A OH    1 
ATOM 5912 N N     . ILE B 2 715 ? 3.25400   19.48100  39.40200 1.000 85.48417  ? 715 ILE A N     1 
ATOM 5913 C CA    . ILE B 2 715 ? 3.82900   19.93300  38.13500 1.000 88.00293  ? 715 ILE A CA    1 
ATOM 5914 C C     . ILE B 2 715 ? 4.50900   18.77300  37.41700 1.000 88.38809  ? 715 ILE A C     1 
ATOM 5915 O O     . ILE B 2 715 ? 4.39900   18.62700  36.19100 1.000 93.06982  ? 715 ILE A O     1 
ATOM 5916 C CB    . ILE B 2 715 ? 4.80300   21.10100  38.37600 1.000 89.15454  ? 715 ILE A CB    1 
ATOM 5917 C CG1   . ILE B 2 715 ? 4.10000   22.23700  39.11700 1.000 81.71634  ? 715 ILE A CG1   1 
ATOM 5918 C CG2   . ILE B 2 715 ? 5.37000   21.60500  37.05800 1.000 82.10107  ? 715 ILE A CG2   1 
ATOM 5919 C CD1   . ILE B 2 715 ? 5.00500   23.39700  39.44800 1.000 78.79154  ? 715 ILE A CD1   1 
ATOM 5920 N N     . ILE B 2 716 ? 5.21400   17.92700  38.17400 1.000 98.07062  ? 716 ILE A N     1 
ATOM 5921 C CA    . ILE B 2 716 ? 5.83300   16.72800  37.61100 1.000 98.78678  ? 716 ILE A CA    1 
ATOM 5922 C C     . ILE B 2 716 ? 4.78200   15.85400  36.94200 1.000 102.06025 ? 716 ILE A C     1 
ATOM 5923 O O     . ILE B 2 716 ? 4.87800   15.53700  35.75100 1.000 104.67862 ? 716 ILE A O     1 
ATOM 5924 C CB    . ILE B 2 716 ? 6.58100   15.94100  38.70100 1.000 92.27793  ? 716 ILE A CB    1 
ATOM 5925 C CG1   . ILE B 2 716 ? 7.88400   16.63400  39.08500 1.000 91.47342  ? 716 ILE A CG1   1 
ATOM 5926 C CG2   . ILE B 2 716 ? 6.85200   14.51500  38.23700 1.000 111.76661 ? 716 ILE A CG2   1 
ATOM 5927 C CD1   . ILE B 2 716 ? 8.63900   15.91000  40.16400 1.000 92.27792  ? 716 ILE A CD1   1 
ATOM 5928 N N     . GLU B 2 717 ? 3.76700   15.44300  37.71000 1.000 97.54209  ? 717 GLU A N     1 
ATOM 5929 C CA    . GLU B 2 717 ? 2.75600   14.53200  37.17900 1.000 93.34176  ? 717 GLU A CA    1 
ATOM 5930 C C     . GLU B 2 717 ? 2.12600   15.09200  35.90800 1.000 99.35324  ? 717 GLU A C     1 
ATOM 5931 O O     . GLU B 2 717 ? 2.08700   14.41900  34.86600 1.000 106.78318 ? 717 GLU A O     1 
ATOM 5932 C CB    . GLU B 2 717 ? 1.68800   14.26500  38.24000 1.000 92.50503  ? 717 GLU A CB    1 
ATOM 5933 C CG    . GLU B 2 717 ? 0.73800   13.12900  37.90000 1.000 95.21142  ? 717 GLU A CG    1 
ATOM 5934 C CD    . GLU B 2 717 ? 1.27000   11.77200  38.32200 1.000 101.90257 ? 717 GLU A CD    1 
ATOM 5935 O OE1   . GLU B 2 717 ? 2.42300   11.70100  38.80000 1.000 123.36189 ? 717 GLU A OE1   1 
ATOM 5936 O OE2   . GLU B 2 717 ? 0.53100   10.77500  38.18300 1.000 115.73310 ? 717 GLU A OE2   1 
ATOM 5937 N N     . TYR B 2 718 ? 1.64800   16.34000  35.97300 1.000 103.70878 ? 718 TYR A N     1 
ATOM 5938 C CA    . TYR B 2 718 ? 1.05100   16.96800  34.79800 1.000 98.31943  ? 718 TYR A CA    1 
ATOM 5939 C C     . TYR B 2 718 ? 1.99800   16.92000  33.61000 1.000 96.68564  ? 718 TYR A C     1 
ATOM 5940 O O     . TYR B 2 718 ? 1.62800   16.46600  32.52100 1.000 101.29144 ? 718 TYR A O     1 
ATOM 5941 C CB    . TYR B 2 718 ? 0.66100   18.42000  35.09400 1.000 90.62430  ? 718 TYR A CB    1 
ATOM 5942 C CG    . TYR B 2 718 ? 0.30500   19.20400  33.83900 1.000 91.72702  ? 718 TYR A CG    1 
ATOM 5943 C CD1   . TYR B 2 718 ? -0.98400  19.17900  33.32300 1.000 103.46496 ? 718 TYR A CD1   1 
ATOM 5944 C CD2   . TYR B 2 718 ? 1.26400   19.95700  33.16500 1.000 108.23189 ? 718 TYR A CD2   1 
ATOM 5945 C CE1   . TYR B 2 718 ? -1.31000  19.88100  32.17500 1.000 96.35522  ? 718 TYR A CE1   1 
ATOM 5946 C CE2   . TYR B 2 718 ? 0.94600   20.66000  32.01500 1.000 110.92095 ? 718 TYR A CE2   1 
ATOM 5947 C CZ    . TYR B 2 718 ? -0.34300  20.62000  31.52700 1.000 104.72699 ? 718 TYR A CZ    1 
ATOM 5948 O OH    . TYR B 2 718 ? -0.66600  21.31900  30.38600 1.000 106.60898 ? 718 TYR A OH    1 
ATOM 5949 N N     . THR B 2 719 ? 3.23300   17.38100  33.81000 1.000 95.94616  ? 719 THR A N     1 
ATOM 5950 C CA    . THR B 2 719 ? 4.14700   17.55500  32.68900 1.000 100.10582 ? 719 THR A CA    1 
ATOM 5951 C C     . THR B 2 719 ? 4.55400   16.22100  32.07100 1.000 107.10783 ? 719 THR A C     1 
ATOM 5952 O O     . THR B 2 719 ? 4.70400   16.13000  30.84600 1.000 109.25924 ? 719 THR A O     1 
ATOM 5953 C CB    . THR B 2 719 ? 5.36400   18.36300  33.15200 1.000 94.72467  ? 719 THR A CB    1 
ATOM 5954 O OG1   . THR B 2 719 ? 5.69800   17.99800  34.49800 1.000 112.79759 ? 719 THR A OG1   1 
ATOM 5955 C CG2   . THR B 2 719 ? 5.11000   19.86400  33.06500 1.000 97.94993  ? 719 THR A CG2   1 
ATOM 5956 N N     . THR B 2 720 ? 4.71400   15.17200  32.88400 1.000 103.93654 ? 720 THR A N     1 
ATOM 5957 C CA    . THR B 2 720 ? 5.07700   13.87600  32.32400 1.000 101.85875 ? 720 THR A CA    1 
ATOM 5958 C C     . THR B 2 720 ? 3.90400   13.25300  31.58300 1.000 103.18055 ? 720 THR A C     1 
ATOM 5959 O O     . THR B 2 720 ? 4.09800   12.57400  30.56600 1.000 108.53180 ? 720 THR A O     1 
ATOM 5960 C CB    . THR B 2 720 ? 5.57300   12.93200  33.41900 1.000 100.47508 ? 720 THR A CB    1 
ATOM 5961 O OG1   . THR B 2 720 ? 4.50300   12.64200  34.32600 1.000 104.49575 ? 720 THR A OG1   1 
ATOM 5962 C CG2   . THR B 2 720 ? 6.73300   13.55200  34.17900 1.000 101.73835 ? 720 THR A CG2   1 
ATOM 5963 N N     . ILE B 2 721 ? 2.67900   13.47300  32.06900 1.000 116.00017 ? 721 ILE A N     1 
ATOM 5964 C CA    . ILE B 2 721 ? 1.53300   12.85500  31.40900 1.000 102.03358 ? 721 ILE A CA    1 
ATOM 5965 C C     . ILE B 2 721 ? 1.19700   13.57400  30.10600 1.000 104.91525 ? 721 ILE A C     1 
ATOM 5966 O O     . ILE B 2 721 ? 0.93000   12.93300  29.08300 1.000 112.47450 ? 721 ILE A O     1 
ATOM 5967 C CB    . ILE B 2 721 ? 0.33200   12.80700  32.36700 1.000 99.33089  ? 721 ILE A CB    1 
ATOM 5968 C CG1   . ILE B 2 721 ? 0.66000   11.90100  33.55300 1.000 100.55719 ? 721 ILE A CG1   1 
ATOM 5969 C CG2   . ILE B 2 721 ? -0.90400  12.30000  31.64500 1.000 101.42632 ? 721 ILE A CG2   1 
ATOM 5970 C CD1   . ILE B 2 721 ? -0.37600  11.92000  34.63400 1.000 103.00660 ? 721 ILE A CD1   1 
ATOM 5971 N N     . THR B 2 722 ? 1.21300   14.90500  30.11100 1.000 123.70342 ? 722 THR A N     1 
ATOM 5972 C CA    . THR B 2 722 ? 0.91100   15.69900  28.92400 1.000 117.12317 ? 722 THR A CA    1 
ATOM 5973 C C     . THR B 2 722 ? 1.98400   16.76400  28.74300 1.000 111.75719 ? 722 THR A C     1 
ATOM 5974 O O     . THR B 2 722 ? 2.15300   17.63500  29.60300 1.000 122.29063 ? 722 THR A O     1 
ATOM 5975 C CB    . THR B 2 722 ? -0.47300  16.34800  29.02000 1.000 121.28099 ? 722 THR A CB    1 
ATOM 5976 O OG1   . THR B 2 722 ? -0.73500  17.08800  27.82000 1.000 150.88367 ? 722 THR A OG1   1 
ATOM 5977 C CG2   . THR B 2 722 ? -0.55300  17.28200  30.22100 1.000 107.38865 ? 722 THR A CG2   1 
ATOM 5978 N N     . SER B 2 723 ? 2.69500   16.70600  27.61700 1.000 107.70639 ? 723 SER A N     1 
ATOM 5979 C CA    . SER B 2 723 ? 3.81500   17.61200  27.36300 1.000 111.59354 ? 723 SER A CA    1 
ATOM 5980 C C     . SER B 2 723 ? 3.29200   18.94400  26.82300 1.000 115.71316 ? 723 SER A C     1 
ATOM 5981 O O     . SER B 2 723 ? 3.50900   19.32000  25.66900 1.000 111.93652 ? 723 SER A O     1 
ATOM 5982 C CB    . SER B 2 723 ? 4.80500   16.97000  26.40100 1.000 128.83988 ? 723 SER A CB    1 
ATOM 5983 O OG    . SER B 2 723 ? 5.11600   15.64500  26.79900 1.000 135.15509 ? 723 SER A OG    1 
ATOM 5984 N N     . SER B 2 724 ? 2.59600   19.67300  27.69500 1.000 119.50217 ? 724 SER A N     1 
ATOM 5985 C CA    . SER B 2 724 ? 1.97800   20.94700  27.34800 1.000 106.28758 ? 724 SER A CA    1 
ATOM 5986 C C     . SER B 2 724 ? 2.38100   22.00800  28.36800 1.000 105.82668 ? 724 SER A C     1 
ATOM 5987 O O     . SER B 2 724 ? 3.14800   21.74900  29.30100 1.000 111.53004 ? 724 SER A O     1 
ATOM 5988 C CB    . SER B 2 724 ? 0.45300   20.81200  27.26300 1.000 121.86807 ? 724 SER A CB    1 
ATOM 5989 O OG    . SER B 2 724 ? -0.15700  22.07500  27.05600 1.000 117.72404 ? 724 SER A OG    1 
ATOM 5990 N N     . LYS B 2 725 ? 1.86300   23.22100  28.17600 1.000 112.51402 ? 725 LYS A N     1 
ATOM 5991 C CA    . LYS B 2 725 ? 2.21800   24.33800  29.03800 1.000 104.49375 ? 725 LYS A CA    1 
ATOM 5992 C C     . LYS B 2 725 ? 1.47600   24.25400  30.36700 1.000 98.13607  ? 725 LYS A C     1 
ATOM 5993 O O     . LYS B 2 725 ? 0.45900   23.57000  30.50500 1.000 106.68897 ? 725 LYS A O     1 
ATOM 5994 C CB    . LYS B 2 725 ? 1.89200   25.67500  28.36900 1.000 107.20557 ? 725 LYS A CB    1 
ATOM 5995 C CG    . LYS B 2 725 ? 2.25000   25.76700  26.89300 1.000 111.71681 ? 725 LYS A CG    1 
ATOM 5996 C CD    . LYS B 2 725 ? 2.12100   27.20400  26.38300 1.000 115.64075 ? 725 LYS A CD    1 
ATOM 5997 C CE    . LYS B 2 725 ? 2.38000   27.30600  24.87900 1.000 127.33865 ? 725 LYS A CE    1 
ATOM 5998 N NZ    . LYS B 2 725 ? 1.60100   28.41800  24.23900 1.000 151.06867 ? 725 LYS A NZ    1 
ATOM 5999 N N     . CYS B 2 726 ? 1.99600   24.98500  31.34700 1.000 93.44592  ? 726 CYS A N     1 
ATOM 6000 C CA    . CYS B 2 726 ? 1.42200   25.03800  32.68100 1.000 90.65661  ? 726 CYS A CA    1 
ATOM 6001 C C     . CYS B 2 726 ? 1.68000   26.42800  33.23700 1.000 88.21630  ? 726 CYS A C     1 
ATOM 6002 O O     . CYS B 2 726 ? 2.72100   27.02100  32.95800 1.000 101.28379 ? 726 CYS A O     1 
ATOM 6003 C CB    . CYS B 2 726 ? 2.03400   23.95800  33.58200 1.000 90.12435  ? 726 CYS A CB    1 
ATOM 6004 S SG    . CYS B 2 726 ? 1.73500   24.18100  35.34400 1.000 99.24049  ? 726 CYS A SG    1 
ATOM 6005 N N     . LEU B 2 727 ? 0.74000   26.94300  34.02900 1.000 82.87833  ? 727 LEU A N     1 
ATOM 6006 C CA    . LEU B 2 727 ? 0.89600   28.29200  34.62900 1.000 81.63537  ? 727 LEU A CA    1 
ATOM 6007 C C     . LEU B 2 727 ? 0.59000   28.20900  36.12800 1.000 81.29895  ? 727 LEU A C     1 
ATOM 6008 O O     . LEU B 2 727 ? -0.49500  27.72100  36.48600 1.000 89.56022  ? 727 LEU A O     1 
ATOM 6009 C CB    . LEU B 2 727 ? -0.03900  29.26800  33.92100 1.000 86.71131  ? 727 LEU A CB    1 
ATOM 6010 C CG    . LEU B 2 727 ? -0.17300  30.65700  34.55100 1.000 101.56450 ? 727 LEU A CG    1 
ATOM 6011 C CD1   . LEU B 2 727 ? 1.15800   31.38200  34.56100 1.000 110.34126 ? 727 LEU A CD1   1 
ATOM 6012 C CD2   . LEU B 2 727 ? -1.21100  31.47200  33.80400 1.000 97.60722  ? 727 LEU A CD2   1 
ATOM 6013 N N     . VAL B 2 728 ? 1.52200   28.66200  36.96500 1.000 76.01314  ? 728 VAL A N     1 
ATOM 6014 C CA    . VAL B 2 728 ? 1.31800   28.59600  38.44000 1.000 83.42022  ? 728 VAL A CA    1 
ATOM 6015 C C     . VAL B 2 728 ? 1.29200   30.02800  38.99100 1.000 85.33326  ? 728 VAL A C     1 
ATOM 6016 O O     . VAL B 2 728 ? 2.25900   30.76900  38.74700 1.000 92.09285  ? 728 VAL A O     1 
ATOM 6017 C CB    . VAL B 2 728 ? 2.38600   27.74700  39.15000 1.000 92.02818  ? 728 VAL A CB    1 
ATOM 6018 C CG1   . VAL B 2 728 ? 1.91400   27.30200  40.52900 1.000 86.32078  ? 728 VAL A CG1   1 
ATOM 6019 C CG2   . VAL B 2 728 ? 2.78900   26.53800  38.31600 1.000 81.24985  ? 728 VAL A CG2   1 
ATOM 6020 N N     . LEU B 2 729 ? 0.22200   30.38700  39.70100 1.000 89.28807  ? 729 LEU A N     1 
ATOM 6021 C CA    . LEU B 2 729 ? 0.09400   31.74800  40.27700 1.000 85.88781  ? 729 LEU A CA    1 
ATOM 6022 C C     . LEU B 2 729 ? 0.34900   31.66600  41.78500 1.000 99.16387  ? 729 LEU A C     1 
ATOM 6023 O O     . LEU B 2 729 ? -0.52700  31.14600  42.50200 1.000 107.99827 ? 729 LEU A O     1 
ATOM 6024 C CB    . LEU B 2 729 ? -1.30400  32.27400  39.97200 1.000 91.18921  ? 729 LEU A CB    1 
ATOM 6025 C CG    . LEU B 2 729 ? -1.69200  32.34300  38.49200 1.000 86.12224  ? 729 LEU A CG    1 
ATOM 6026 C CD1   . LEU B 2 729 ? -3.20000  32.29500  38.33600 1.000 85.41749  ? 729 LEU A CD1   1 
ATOM 6027 C CD2   . LEU B 2 729 ? -1.14700  33.61200  37.86600 1.000 121.17000 ? 729 LEU A CD2   1 
ATOM 6028 N N     . PHE B 2 730 ? 1.49900   32.16400  42.24700 1.000 101.27749 ? 730 PHE A N     1 
ATOM 6029 C CA    . PHE B 2 730 ? 1.86100   32.04600  43.68500 1.000 106.81464 ? 730 PHE A CA    1 
ATOM 6030 C C     . PHE B 2 730 ? 1.51800   33.32600  44.41300 1.000 104.44773 ? 730 PHE A C     1 
ATOM 6031 O O     . PHE B 2 730 ? 1.04000   34.28500  43.77700 1.000 116.67608 ? 730 PHE A O     1 
ATOM 6032 C CB    . PHE B 2 730 ? 3.36200   31.81000  43.85400 1.000 90.14947  ? 730 PHE A CB    1 
ATOM 6033 C CG    . PHE B 2 730 ? 3.90900   30.59400  43.12400 1.000 86.66664  ? 730 PHE A CG    1 
ATOM 6034 C CD1   . PHE B 2 730 ? 4.37400   30.69500  41.82000 1.000 97.11241  ? 730 PHE A CD1   1 
ATOM 6035 C CD2   . PHE B 2 730 ? 3.96000   29.35500  43.74900 1.000 101.23822 ? 730 PHE A CD2   1 
ATOM 6036 C CE1   . PHE B 2 730 ? 4.87200   29.58500  41.16100 1.000 130.90543 ? 730 PHE A CE1   1 
ATOM 6037 C CE2   . PHE B 2 730 ? 4.46000   28.24900  43.08500 1.000 126.88942 ? 730 PHE A CE2   1 
ATOM 6038 C CZ    . PHE B 2 730 ? 4.91200   28.36700  41.79300 1.000 132.57843 ? 730 PHE A CZ    1 
ATOM 6039 N N     . THR B 2 731 ? 1.75600   33.34500  45.72500 1.000 114.09757 ? 731 THR A N     1 
ATOM 6040 C CA    . THR B 2 731 ? 1.51900   34.56800  46.51900 1.000 118.96959 ? 731 THR A CA    1 
ATOM 6041 C C     . THR B 2 731 ? 2.77000   34.84900  47.32300 1.000 131.03780 ? 731 THR A C     1 
ATOM 6042 O O     . THR B 2 731 ? 2.80700   35.88300  48.02300 1.000 139.29717 ? 731 THR A O     1 
ATOM 6043 C CB    . THR B 2 731 ? 0.29600   34.37000  47.41300 1.000 118.13455 ? 731 THR A CB    1 
ATOM 6044 O OG1   . THR B 2 731 ? -0.66400  33.70100  46.60300 1.000 135.48905 ? 731 THR A OG1   1 
ATOM 6045 C CG2   . THR B 2 731 ? -0.28800  35.67900  47.91400 1.000 92.91123  ? 731 THR A CG2   1 
ATOM 6046 N N     . SER B 2 732 ? 3.76900   33.96800  47.23100 1.000 122.96036 ? 732 SER A N     1 
ATOM 6047 C CA    . SER B 2 732 ? 5.00200   34.13100  48.04200 1.000 100.97022 ? 732 SER A CA    1 
ATOM 6048 C C     . SER B 2 732 ? 6.23000   34.19900  47.13100 1.000 90.61788  ? 732 SER A C     1 
ATOM 6049 O O     . SER B 2 732 ? 6.54700   33.18000  46.48900 1.000 99.73781  ? 732 SER A O     1 
ATOM 6050 C CB    . SER B 2 732 ? 5.14200   33.02000  49.04000 1.000 118.69821 ? 732 SER A CB    1 
ATOM 6051 O OG    . SER B 2 732 ? 6.41400   33.07200  49.67100 1.000 125.73015 ? 732 SER A OG    1 
ATOM 6052 N N     . TYR B 2 733 ? 6.89300   35.35400  47.08700 1.000 104.46947 ? 733 TYR A N     1 
ATOM 6053 C CA    . TYR B 2 733 ? 8.14600   35.47200  46.29900 1.000 92.22562  ? 733 TYR A CA    1 
ATOM 6054 C C     . TYR B 2 733 ? 9.00500   34.26600  46.61800 1.000 106.99379 ? 733 TYR A C     1 
ATOM 6055 O O     . TYR B 2 733 ? 9.61200   33.67500  45.70300 1.000 115.89447 ? 733 TYR A O     1 
ATOM 6056 C CB    . TYR B 2 733 ? 8.82200   36.78800  46.68600 1.000 98.96799  ? 733 TYR A CB    1 
ATOM 6057 C CG    . TYR B 2 733 ? 10.20700  37.03000  46.10300 1.000 123.23369 ? 733 TYR A CG    1 
ATOM 6058 C CD1   . TYR B 2 733 ? 10.36600  37.63200  44.86100 1.000 130.32756 ? 733 TYR A CD1   1 
ATOM 6059 C CD2   . TYR B 2 733 ? 11.35300  36.68500  46.80700 1.000 103.77425 ? 733 TYR A CD2   1 
ATOM 6060 C CE1   . TYR B 2 733 ? 11.62300  37.86500  44.32900 1.000 129.71981 ? 733 TYR A CE1   1 
ATOM 6061 C CE2   . TYR B 2 733 ? 12.61600  36.91200  46.28700 1.000 102.87238 ? 733 TYR A CE2   1 
ATOM 6062 C CZ    . TYR B 2 733 ? 12.75100  37.50400  45.04400 1.000 127.57094 ? 733 TYR A CZ    1 
ATOM 6063 O OH    . TYR B 2 733 ? 13.99200  37.73200  44.52600 1.000 119.64559 ? 733 TYR A OH    1 
ATOM 6064 N N     . LYS B 2 734 ? 9.04800   33.89700  47.90000 1.000 102.58774 ? 734 LYS A N     1 
ATOM 6065 C CA    . LYS B 2 734 ? 9.89700   32.75500  48.31200 1.000 96.46952  ? 734 LYS A CA    1 
ATOM 6066 C C     . LYS B 2 734 ? 9.42400   31.48600  47.59800 1.000 119.15903 ? 734 LYS A C     1 
ATOM 6067 O O     . LYS B 2 734 ? 10.26700  30.80200  46.98600 1.000 114.25260 ? 734 LYS A O     1 
ATOM 6068 C CB    . LYS B 2 734 ? 9.76900   32.57200  49.82500 1.000 104.04416 ? 734 LYS A CB    1 
ATOM 6069 C CG    . LYS B 2 734 ? 10.46600  31.35300  50.40900 1.000 133.48400 ? 734 LYS A CG    1 
ATOM 6070 C CD    . LYS B 2 734 ? 9.95700   31.03400  51.80900 1.000 137.69974 ? 734 LYS A CD    1 
ATOM 6071 C CE    . LYS B 2 734 ? 9.93400   32.24500  52.68800 1.000 136.02842 ? 734 LYS A CE    1 
ATOM 6072 N NZ    . LYS B 2 734 ? 9.28900   31.97200  53.97400 1.000 148.94928 ? 734 LYS A NZ    1 
ATOM 6073 N N     . MET B 2 735 ? 8.12600   31.19200  47.67500 1.000 105.14844 ? 735 MET A N     1 
ATOM 6074 C CA    . MET B 2 735 ? 7.58600   29.95600  47.05800 1.000 94.03788  ? 735 MET A CA    1 
ATOM 6075 C C     . MET B 2 735 ? 7.95400   29.93800  45.57000 1.000 94.49449  ? 735 MET A C     1 
ATOM 6076 O O     . MET B 2 735 ? 8.42600   28.88800  45.09000 1.000 107.76289 ? 735 MET A O     1 
ATOM 6077 C CB    . MET B 2 735 ? 6.06200   29.90300  47.20900 1.000 93.18108  ? 735 MET A CB    1 
ATOM 6078 C CG    . MET B 2 735 ? 5.45200   28.55300  46.90000 1.000 104.66227 ? 735 MET A CG    1 
ATOM 6079 S SD    . MET B 2 735 ? 3.65700   28.57000  47.09000 1.000 76.47952  ? 735 MET A SD    1 
ATOM 6080 C CE    . MET B 2 735 ? 3.49800   28.97600  48.83300 1.000 71.15022  ? 735 MET A CE    1 
ATOM 6081 N N     . MET B 2 736 ? 7.75600   31.06000  44.87500 1.000 84.35690  ? 736 MET A N     1 
ATOM 6082 C CA    . MET B 2 736 ? 8.01300   31.09400  43.41300 1.000 80.23442  ? 736 MET A CA    1 
ATOM 6083 C C     . MET B 2 736 ? 9.47000   30.68800  43.15900 1.000 85.52950  ? 736 MET A C     1 
ATOM 6084 O O     . MET B 2 736 ? 9.70400   29.80500  42.30800 1.000 88.90955  ? 736 MET A O     1 
ATOM 6085 C CB    . MET B 2 736 ? 7.75600   32.49500  42.84900 1.000 79.47221  ? 736 MET A CB    1 
ATOM 6086 C CG    . MET B 2 736 ? 7.89600   32.59100  41.34500 1.000 98.37566  ? 736 MET A CG    1 
ATOM 6087 S SD    . MET B 2 736 ? 7.51000   34.24700  40.74700 1.000 83.19017  ? 736 MET A SD    1 
ATOM 6088 C CE    . MET B 2 736 ? 8.64100   35.20300  41.76600 1.000 84.11156  ? 736 MET A CE    1 
ATOM 6089 N N     . HIS B 2 737 ? 10.40300  31.30000  43.88800 1.000 98.07420  ? 737 HIS A N     1 
ATOM 6090 C CA    . HIS B 2 737 ? 11.84400  31.00000  43.67700 1.000 102.88468 ? 737 HIS A CA    1 
ATOM 6091 C C     . HIS B 2 737 ? 12.13000  29.56400  44.12500 1.000 102.99227 ? 737 HIS A C     1 
ATOM 6092 O O     . HIS B 2 737 ? 12.86700  28.83900  43.43000 1.000 92.59329  ? 737 HIS A O     1 
ATOM 6093 C CB    . HIS B 2 737 ? 12.71300  32.04600  44.38200 1.000 100.33509 ? 737 HIS A CB    1 
ATOM 6094 C CG    . HIS B 2 737 ? 12.96100  33.24500  43.53400 1.000 108.16737 ? 737 HIS A CG    1 
ATOM 6095 N ND1   . HIS B 2 737 ? 12.10200  34.32100  43.47300 1.000 99.20738  ? 737 HIS A ND1   1 
ATOM 6096 C CD2   . HIS B 2 737 ? 13.95900  33.51900  42.68800 1.000 126.76072 ? 737 HIS A CD2   1 
ATOM 6097 C CE1   . HIS B 2 737 ? 12.58600  35.21500  42.62400 1.000 105.40470 ? 737 HIS A CE1   1 
ATOM 6098 N NE2   . HIS B 2 737 ? 13.71500  34.75000  42.13800 1.000 127.64397 ? 737 HIS A NE2   1 
ATOM 6099 N N     . MET B 2 738 ? 11.54000  29.15900  45.24800 1.000 97.02761  ? 738 MET A N     1 
ATOM 6100 C CA    . MET B 2 738 ? 11.78900  27.79300  45.77100 1.000 96.96888  ? 738 MET A CA    1 
ATOM 6101 C C     . MET B 2 738 ? 11.41700  26.77600  44.68700 1.000 92.42238  ? 738 MET A C     1 
ATOM 6102 O O     . MET B 2 738 ? 12.24800  25.89100  44.39100 1.000 109.58616 ? 738 MET A O     1 
ATOM 6103 C CB    . MET B 2 738 ? 10.94700  27.51700  47.02000 1.000 104.11441 ? 738 MET A CB    1 
ATOM 6104 C CG    . MET B 2 738 ? 11.58100  27.97600  48.31700 1.000 97.33300  ? 738 MET A CG    1 
ATOM 6105 S SD    . MET B 2 738 ? 10.60600  27.49000  49.75400 1.000 101.52037 ? 738 MET A SD    1 
ATOM 6106 C CE    . MET B 2 738 ? 11.76900  27.82500  51.08300 1.000 121.56613 ? 738 MET A CE    1 
ATOM 6107 N N     . VAL B 2 739 ? 10.22700  26.91200  44.10400 1.000 81.51653  ? 739 VAL A N     1 
ATOM 6108 C CA    . VAL B 2 739 ? 9.76900   25.88800  43.11700 1.000 84.27312  ? 739 VAL A CA    1 
ATOM 6109 C C     . VAL B 2 739 ? 10.68300  25.95300  41.88500 1.000 86.54068  ? 739 VAL A C     1 
ATOM 6110 O O     . VAL B 2 739 ? 11.08500  24.87800  41.40900 1.000 103.63732 ? 739 VAL A O     1 
ATOM 6111 C CB    . VAL B 2 739 ? 8.28200   26.01900  42.72800 1.000 87.59545  ? 739 VAL A CB    1 
ATOM 6112 C CG1   . VAL B 2 739 ? 8.01900   27.21500  41.82500 1.000 110.00937 ? 739 VAL A CG1   1 
ATOM 6113 C CG2   . VAL B 2 739 ? 7.75300   24.74300  42.08600 1.000 104.88379 ? 739 VAL A CG2   1 
ATOM 6114 N N     . GLN B 2 740 ? 11.02000  27.15400  41.40900 1.000 90.29907  ? 740 GLN A N     1 
ATOM 6115 C CA    . GLN B 2 740 ? 11.81300  27.24500  40.15500 1.000 91.96487  ? 740 GLN A CA    1 
ATOM 6116 C C     . GLN B 2 740 ? 13.16400  26.55000  40.38200 1.000 93.20565  ? 740 GLN A C     1 
ATOM 6117 O O     . GLN B 2 740 ? 13.61900  25.83000  39.47200 1.000 114.22488 ? 740 GLN A O     1 
ATOM 6118 C CB    . GLN B 2 740 ? 11.99300  28.68100  39.65900 1.000 102.40969 ? 740 GLN A CB    1 
ATOM 6119 C CG    . GLN B 2 740 ? 13.03100  29.50200  40.41700 1.000 112.63038 ? 740 GLN A CG    1 
ATOM 6120 C CD    . GLN B 2 740 ? 13.54500  30.68100  39.62200 1.000 107.76175 ? 740 GLN A CD    1 
ATOM 6121 O OE1   . GLN B 2 740 ? 13.15700  30.89900  38.46900 1.000 102.74504 ? 740 GLN A OE1   1 
ATOM 6122 N NE2   . GLN B 2 740 ? 14.43600  31.45000  40.23000 1.000 114.64997 ? 740 GLN A NE2   1 
ATOM 6123 N N     . ASP B 2 741 ? 13.75600  26.73800  41.56300 1.000 88.97210  ? 741 ASP A N     1 
ATOM 6124 C CA    . ASP B 2 741 ? 15.05100  26.07700  41.86700 1.000 104.78093 ? 741 ASP A CA    1 
ATOM 6125 C C     . ASP B 2 741 ? 14.85300  24.56400  41.74100 1.000 108.22745 ? 741 ASP A C     1 
ATOM 6126 O O     . ASP B 2 741 ? 15.62300  23.92500  40.99500 1.000 105.45880 ? 741 ASP A O     1 
ATOM 6127 C CB    . ASP B 2 741 ? 15.58900  26.51700  43.21700 1.000 115.97362 ? 741 ASP A CB    1 
ATOM 6128 C CG    . ASP B 2 741 ? 15.92000  27.99800  43.32800 1.000 117.75063 ? 741 ASP A CG    1 
ATOM 6129 O OD1   . ASP B 2 741 ? 15.73000  28.71600  42.32400 1.000 123.68500 ? 741 ASP A OD1   1 
ATOM 6130 O OD2   . ASP B 2 741 ? 16.36200  28.42100  44.41600 1.000 114.08219 ? 741 ASP A OD2   1 
ATOM 6131 N N     . MET B 2 742 ? 13.82400  24.02800  42.40100 1.000 97.97324  ? 742 MET A N     1 
ATOM 6132 C CA    . MET B 2 742 ? 13.55800  22.56800  42.34300 1.000 100.18944 ? 742 MET A CA    1 
ATOM 6133 C C     . MET B 2 742 ? 13.30000  22.15500  40.88800 1.000 92.17839  ? 742 MET A C     1 
ATOM 6134 O O     . MET B 2 742 ? 13.92900  21.18200  40.43200 1.000 96.60599  ? 742 MET A O     1 
ATOM 6135 C CB    . MET B 2 742 ? 12.33500  22.19400  43.18700 1.000 90.22891  ? 742 MET A CB    1 
ATOM 6136 C CG    . MET B 2 742 ? 12.53300  22.36100  44.67800 1.000 109.84820 ? 742 MET A CG    1 
ATOM 6137 S SD    . MET B 2 742 ? 11.17500  21.63400  45.61700 1.000 94.78887  ? 742 MET A SD    1 
ATOM 6138 C CE    . MET B 2 742 ? 11.70500  21.97000  47.30100 1.000 113.54351 ? 742 MET A CE    1 
ATOM 6139 N N     . LEU B 2 743 ? 12.43100  22.88000  40.18400 1.000 84.95820  ? 743 LEU A N     1 
ATOM 6140 C CA    . LEU B 2 743 ? 12.07300  22.49500  38.79600 1.000 88.47652  ? 743 LEU A CA    1 
ATOM 6141 C C     . LEU B 2 743 ? 13.35400  22.40000  37.96000 1.000 90.37319  ? 743 LEU A C     1 
ATOM 6142 O O     . LEU B 2 743 ? 13.52100  21.39100  37.24900 1.000 105.61469 ? 743 LEU A O     1 
ATOM 6143 C CB    . LEU B 2 743 ? 11.10500  23.50900  38.19100 1.000 86.10153  ? 743 LEU A CB    1 
ATOM 6144 C CG    . LEU B 2 743 ? 9.74200   23.65300  38.87300 1.000 82.74808  ? 743 LEU A CG    1 
ATOM 6145 C CD1   . LEU B 2 743 ? 8.92800   24.74100  38.19800 1.000 85.74659  ? 743 LEU A CD1   1 
ATOM 6146 C CD2   . LEU B 2 743 ? 8.98500   22.34200  38.85700 1.000 85.28183  ? 743 LEU A CD2   1 
ATOM 6147 N N     . ASN B 2 744 ? 14.22800  23.40300  38.05600 1.000 93.18372  ? 744 ASN A N     1 
ATOM 6148 C CA    . ASN B 2 744 ? 15.45300  23.42300  37.20800 1.000 102.42997 ? 744 ASN A CA    1 
ATOM 6149 C C     . ASN B 2 744 ? 16.31400  22.19200  37.51000 1.000 103.35269 ? 744 ASN A C     1 
ATOM 6150 O O     . ASN B 2 744 ? 16.82900  21.58400  36.54700 1.000 103.28317 ? 744 ASN A O     1 
ATOM 6151 C CB    . ASN B 2 744 ? 16.21700  24.73100  37.37400 1.000 88.26505  ? 744 ASN A CB    1 
ATOM 6152 C CG    . ASN B 2 744 ? 15.54700  25.87200  36.64900 1.000 85.17594  ? 744 ASN A CG    1 
ATOM 6153 O OD1   . ASN B 2 744 ? 15.19700  26.88400  37.26700 1.000 95.53523  ? 744 ASN A OD1   1 
ATOM 6154 N ND2   . ASN B 2 744 ? 15.36900  25.73400  35.34400 1.000 91.67710  ? 744 ASN A ND2   1 
ATOM 6155 N N     . GLU B 2 745 ? 16.45900  21.83800  38.78900 1.000 102.86032 ? 745 GLU A N     1 
ATOM 6156 C CA    . GLU B 2 745 ? 17.32000  20.69200  39.18300 1.000 95.57499  ? 745 GLU A CA    1 
ATOM 6157 C C     . GLU B 2 745 ? 16.69700  19.36500  38.73100 1.000 95.20563  ? 745 GLU A C     1 
ATOM 6158 O O     . GLU B 2 745 ? 17.45200  18.49800  38.24900 1.000 103.19552 ? 745 GLU A O     1 
ATOM 6159 C CB    . GLU B 2 745 ? 17.49400  20.66600  40.70000 1.000 95.98542  ? 745 GLU A CB    1 
ATOM 6160 C CG    . GLU B 2 745 ? 18.06100  21.96500  41.26500 1.000 138.15127 ? 745 GLU A CG    1 
ATOM 6161 C CD    . GLU B 2 745 ? 17.83500  22.12400  42.75700 1.000 151.27652 ? 745 GLU A CD    1 
ATOM 6162 O OE1   . GLU B 2 745 ? 17.24500  21.20600  43.36400 1.000 143.96681 ? 745 GLU A OE1   1 
ATOM 6163 O OE2   . GLU B 2 745 ? 18.24200  23.16800  43.30900 1.000 154.75942 ? 745 GLU A OE2   1 
ATOM 6164 N N     . LEU B 2 746 ? 15.38000  19.21100  38.87900 1.000 100.85722 ? 746 LEU A N     1 
ATOM 6165 C CA    . LEU B 2 746 ? 14.72900  17.91100  38.56100 1.000 99.10979  ? 746 LEU A CA    1 
ATOM 6166 C C     . LEU B 2 746 ? 14.95100  17.55200  37.08500 1.000 95.98592  ? 746 LEU A C     1 
ATOM 6167 O O     . LEU B 2 746 ? 14.76300  18.43000  36.21800 1.000 99.98388  ? 746 LEU A O     1 
ATOM 6168 C CB    . LEU B 2 746 ? 13.24900  17.96800  38.93300 1.000 89.48309  ? 746 LEU A CB    1 
ATOM 6169 C CG    . LEU B 2 746 ? 12.95600  18.09300  40.43000 1.000 86.55094  ? 746 LEU A CG    1 
ATOM 6170 C CD1   . LEU B 2 746 ? 11.46900  18.05300  40.71200 1.000 98.56578  ? 746 LEU A CD1   1 
ATOM 6171 C CD2   . LEU B 2 746 ? 13.67300  17.00500  41.20600 1.000 87.69709  ? 746 LEU A CD2   1 
ATOM 6172 N N     . PRO B 2 747 ? 15.32700  16.29400  36.77200 1.000 101.36362 ? 747 PRO A N     1 
ATOM 6173 C CA    . PRO B 2 747 ? 15.61600  15.90200  35.40000 1.000 98.87198  ? 747 PRO A CA    1 
ATOM 6174 C C     . PRO B 2 747 ? 14.38300  15.85000  34.51900 1.000 105.65520 ? 747 PRO A C     1 
ATOM 6175 O O     . PRO B 2 747 ? 14.51500  15.90700  33.28300 1.000 107.34317 ? 747 PRO A O     1 
ATOM 6176 C CB    . PRO B 2 747 ? 16.22400  14.51000  35.60200 1.000 99.82476  ? 747 PRO A CB    1 
ATOM 6177 C CG    . PRO B 2 747 ? 15.54200  13.99100  36.84200 1.000 98.27120  ? 747 PRO A CG    1 
ATOM 6178 C CD    . PRO B 2 747 ? 15.47500  15.21500  37.73300 1.000 102.68793 ? 747 PRO A CD    1 
ATOM 6179 N N     . GLU B 2 748 ? 13.20600  15.73100  35.13400 1.000 116.19787 ? 748 GLU A N     1 
ATOM 6180 C CA    . GLU B 2 748 ? 11.94400  15.61700  34.35900 1.000 98.28796  ? 748 GLU A CA    1 
ATOM 6181 C C     . GLU B 2 748 ? 11.66100  16.93800  33.63200 1.000 101.02535 ? 748 GLU A C     1 
ATOM 6182 O O     . GLU B 2 748 ? 10.88600  16.91500  32.65500 1.000 99.02574  ? 748 GLU A O     1 
ATOM 6183 C CB    . GLU B 2 748 ? 10.79000  15.25100  35.29000 1.000 94.98278  ? 748 GLU A CB    1 
ATOM 6184 C CG    . GLU B 2 748 ? 11.10346  14.07985  36.21543 1.000 110.16032 ? 748 GLU A CG    1 
ATOM 6185 C CD    . GLU B 2 748 ? 11.59282  14.49066  37.59253 1.000 103.71121 ? 748 GLU A CD    1 
ATOM 6186 O OE1   . GLU B 2 748 ? 11.33940  13.74627  38.56034 1.000 106.20312 ? 748 GLU A OE1   1 
ATOM 6187 O OE2   . GLU B 2 748 ? 12.22220  15.56272  37.69685 1.000 110.00093 ? 748 GLU A OE2   1 
ATOM 6188 N N     . PHE B 2 749 ? 12.26600  18.04000  34.08200 1.000 113.39284 ? 749 PHE A N     1 
ATOM 6189 C CA    . PHE B 2 749 ? 11.95200  19.36700  33.48500 1.000 105.12842 ? 749 PHE A CA    1 
ATOM 6190 C C     . PHE B 2 749 ? 13.00300  19.73300  32.44600 1.000 103.65103 ? 749 PHE A C     1 
ATOM 6191 O O     . PHE B 2 749 ? 13.04800  20.90300  32.01700 1.000 108.40857 ? 749 PHE A O     1 
ATOM 6192 C CB    . PHE B 2 749 ? 11.78200  20.39100  34.60900 1.000 95.34247  ? 749 PHE A CB    1 
ATOM 6193 C CG    . PHE B 2 749 ? 10.65200  20.00500  35.55000 1.000 91.78053  ? 749 PHE A CG    1 
ATOM 6194 C CD1   . PHE B 2 749 ? 9.32700   20.18600  35.17700 1.000 91.95984  ? 749 PHE A CD1   1 
ATOM 6195 C CD2   . PHE B 2 749 ? 10.91600  19.46000  36.80000 1.000 104.57663 ? 749 PHE A CD2   1 
ATOM 6196 C CE1   . PHE B 2 749 ? 8.29600   19.83200  36.02900 1.000 97.18293  ? 749 PHE A CE1   1 
ATOM 6197 C CE2   . PHE B 2 749 ? 9.88100   19.11100  37.64900 1.000 101.91594 ? 749 PHE A CE2   1 
ATOM 6198 C CZ    . PHE B 2 749 ? 8.57500   19.29800  37.26200 1.000 95.05686  ? 749 PHE A CZ    1 
ATOM 6199 N N     . GLU B 2 750 ? 13.84300  18.77400  32.05900 1.000 120.47919 ? 750 GLU A N     1 
ATOM 6200 C CA    . GLU B 2 750 ? 14.79100  19.04300  30.95000 1.000 116.48176 ? 750 GLU A CA    1 
ATOM 6201 C C     . GLU B 2 750 ? 13.92700  19.19700  29.69400 1.000 124.52108 ? 750 GLU A C     1 
ATOM 6202 O O     . GLU B 2 750 ? 12.88100  18.51500  29.62500 1.000 141.32105 ? 750 GLU A O     1 
ATOM 6203 C CB    . GLU B 2 750 ? 15.80300  17.90400  30.83900 1.000 124.22891 ? 750 GLU A CB    1 
ATOM 6204 C CG    . GLU B 2 750 ? 16.92300  18.16200  29.83600 1.000 146.56702 ? 750 GLU A CG    1 
ATOM 6205 C CD    . GLU B 2 750 ? 16.56800  17.87800  28.38800 1.000 155.97026 ? 750 GLU A CD    1 
ATOM 6206 O OE1   . GLU B 2 750 ? 16.21200  16.72000  28.08400 1.000 150.10805 ? 750 GLU A OE1   1 
ATOM 6207 O OE2   . GLU B 2 750 ? 16.64800  18.81400  27.56500 1.000 166.58611 ? 750 GLU A OE2   1 
ATOM 6208 N N     . ASP B 2 751 ? 14.32200  20.06000  28.75800 1.000 122.13435 ? 751 ASP A N     1 
ATOM 6209 C CA    . ASP B 2 751 ? 13.46000  20.32200  27.57200 1.000 138.11179 ? 751 ASP A CA    1 
ATOM 6210 C C     . ASP B 2 751 ? 12.14100  20.92000  28.07200 1.000 122.66004 ? 751 ASP A C     1 
ATOM 6211 O O     . ASP B 2 751 ? 11.08600  20.58300  27.50000 1.000 128.49978 ? 751 ASP A O     1 
ATOM 6212 C CB    . ASP B 2 751 ? 13.28800  19.07300  26.71800 1.000 139.02088 ? 751 ASP A CB    1 
ATOM 6213 C CG    . ASP B 2 751 ? 12.70100  19.29700  25.33200 1.000 149.02033 ? 751 ASP A CG    1 
ATOM 6214 O OD1   . ASP B 2 751 ? 13.32000  20.04400  24.54700 1.000 166.52616 ? 751 ASP A OD1   1 
ATOM 6215 O OD2   . ASP B 2 751 ? 11.63000  18.72300  25.05000 1.000 143.95885 ? 751 ASP A OD2   1 
ATOM 6216 N N     . TYR B 2 752 ? 12.20100  21.74900  29.11900 1.000 115.77639 ? 752 TYR A N     1 
ATOM 6217 C CA    . TYR B 2 752 ? 10.99100  22.41900  29.66800 1.000 111.55114 ? 752 TYR A CA    1 
ATOM 6218 C C     . TYR B 2 752 ? 11.43200  23.74300  30.27900 1.000 122.01672 ? 752 TYR A C     1 
ATOM 6219 O O     . TYR B 2 752 ? 11.59300  23.81100  31.51500 1.000 133.56447 ? 752 TYR A O     1 
ATOM 6220 C CB    . TYR B 2 752 ? 10.28700  21.55600  30.71800 1.000 108.89008 ? 752 TYR A CB    1 
ATOM 6221 C CG    . TYR B 2 752 ? 8.77408   21.46150  30.58414 1.000 116.81650 ? 752 TYR A CG    1 
ATOM 6222 C CD1   . TYR B 2 752 ? 7.94415   22.41990  31.14857 1.000 132.38253 ? 752 TYR A CD1   1 
ATOM 6223 C CD2   . TYR B 2 752 ? 8.17846   20.41213  29.89545 1.000 101.95854 ? 752 TYR A CD2   1 
ATOM 6224 C CE1   . TYR B 2 752 ? 6.56763   22.34359  31.02681 1.000 139.23111 ? 752 TYR A CE1   1 
ATOM 6225 C CE2   . TYR B 2 752 ? 6.80279   20.32141  29.77183 1.000 103.46527 ? 752 TYR A CE2   1 
ATOM 6226 C CZ    . TYR B 2 752 ? 5.99486   21.29028  30.33725 1.000 126.67128 ? 752 TYR A CZ    1 
ATOM 6227 O OH    . TYR B 2 752 ? 4.63915   21.20595  30.21953 1.000 131.50842 ? 752 TYR A OH    1 
ATOM 6228 N N     . VAL B 2 753 ? 11.62800  24.77000  29.44800 1.000 126.94897 ? 753 VAL A N     1 
ATOM 6229 C CA    . VAL B 2 753 ? 12.16000  26.06600  29.97100 1.000 104.90183 ? 753 VAL A CA    1 
ATOM 6230 C C     . VAL B 2 753 ? 11.18700  26.61600  31.02500 1.000 95.93788  ? 753 VAL A C     1 
ATOM 6231 O O     . VAL B 2 753 ? 10.00100  26.81300  30.69500 1.000 100.74840 ? 753 VAL A O     1 
ATOM 6232 C CB    . VAL B 2 753 ? 12.43900  27.10700  28.86700 1.000 105.98003 ? 753 VAL A CB    1 
ATOM 6233 C CG1   . VAL B 2 753 ? 11.18732  27.49943  28.09440 1.000 102.83093 ? 753 VAL A CG1   1 
ATOM 6234 C CG2   . VAL B 2 753 ? 13.15326  28.33781  29.40975 1.000 123.09109 ? 753 VAL A CG2   1 
ATOM 6235 N N     . VAL B 2 754 ? 11.68000  26.83900  32.24300 1.000 97.07692  ? 754 VAL A N     1 
ATOM 6236 C CA    . VAL B 2 754 ? 10.82700  27.43700  33.31000 1.000 89.82936  ? 754 VAL A CA    1 
ATOM 6237 C C     . VAL B 2 754 ? 11.00300  28.96100  33.23700 1.000 90.76928  ? 754 VAL A C     1 
ATOM 6238 O O     . VAL B 2 754 ? 12.14000  29.41700  32.99300 1.000 106.66013 ? 754 VAL A O     1 
ATOM 6239 C CB    . VAL B 2 754 ? 11.16500  26.89100  34.71100 1.000 87.77476  ? 754 VAL A CB    1 
ATOM 6240 C CG1   . VAL B 2 754 ? 11.15200  25.36800  34.74000 1.000 89.36927  ? 754 VAL A CG1   1 
ATOM 6241 C CG2   . VAL B 2 754 ? 12.49000  27.42200  35.23900 1.000 111.81979 ? 754 VAL A CG2   1 
ATOM 6242 N N     . LEU B 2 755 ? 9.91300   29.70800  33.40000 1.000 88.69594  ? 755 LEU A N     1 
ATOM 6243 C CA    . LEU B 2 755 ? 9.98300   31.18900  33.34900 1.000 86.23650  ? 755 LEU A CA    1 
ATOM 6244 C C     . LEU B 2 755 ? 9.43300   31.74600  34.66700 1.000 83.75556  ? 755 LEU A C     1 
ATOM 6245 O O     . LEU B 2 755 ? 8.49500   31.13700  35.21900 1.000 100.49762 ? 755 LEU A O     1 
ATOM 6246 C CB    . LEU B 2 755 ? 9.18700   31.68700  32.14600 1.000 89.75005  ? 755 LEU A CB    1 
ATOM 6247 C CG    . LEU B 2 755 ? 9.65600   31.19500  30.77400 1.000 100.47694 ? 755 LEU A CG    1 
ATOM 6248 C CD1   . LEU B 2 755 ? 8.66600   31.61900  29.70500 1.000 115.17509 ? 755 LEU A CD1   1 
ATOM 6249 C CD2   . LEU B 2 755 ? 11.03800  31.74000  30.46400 1.000 99.47167  ? 755 LEU A CD2   1 
ATOM 6250 N N     . THR B 2 756 ? 10.00100  32.85100  35.14900 1.000 87.80160  ? 756 THR A N     1 
ATOM 6251 C CA    . THR B 2 756 ? 9.54200   33.44600  36.42000 1.000 87.05718  ? 756 THR A CA    1 
ATOM 6252 C C     . THR B 2 756 ? 9.22500   34.90700  36.19800 1.000 102.55930 ? 756 THR A C     1 
ATOM 6253 O O     . THR B 2 756 ? 9.50100   35.41100  35.08900 1.000 95.11696  ? 756 THR A O     1 
ATOM 6254 C CB    . THR B 2 756 ? 10.60300  33.25400  37.50000 1.000 93.19425  ? 756 THR A CB    1 
ATOM 6255 O OG1   . THR B 2 756 ? 10.02600  33.79200  38.68500 1.000 102.59908 ? 756 THR A OG1   1 
ATOM 6256 C CG2   . THR B 2 756 ? 11.89700  33.97900  37.17800 1.000 131.37808 ? 756 THR A CG2   1 
ATOM 6257 N N     . GLN B 2 757 ? 8.65400   35.56400  37.20700 1.000 93.76870  ? 757 GLN A N     1 
ATOM 6258 C CA    . GLN B 2 757 ? 8.25700   36.98800  37.07800 1.000 94.05485  ? 757 GLN A CA    1 
ATOM 6259 C C     . GLN B 2 757 ? 9.40800   37.88200  37.55300 1.000 126.36367 ? 757 GLN A C     1 
ATOM 6260 O O     . GLN B 2 757 ? 10.01300  37.56300  38.59800 1.000 128.74779 ? 757 GLN A O     1 
ATOM 6261 C CB    . GLN B 2 757 ? 7.00100   37.22800  37.91400 1.000 103.04942 ? 757 GLN A CB    1 
ATOM 6262 C CG    . GLN B 2 757 ? 6.47900   38.66000  37.88400 1.000 115.46042 ? 757 GLN A CG    1 
ATOM 6263 C CD    . GLN B 2 757 ? 5.21200   38.84400  38.69100 1.000 119.49354 ? 757 GLN A CD    1 
ATOM 6264 O OE1   . GLN B 2 757 ? 4.18100   38.21700  38.42600 1.000 132.43447 ? 757 GLN A OE1   1 
ATOM 6265 N NE2   . GLN B 2 757 ? 5.27800   39.70900  39.69200 1.000 106.93770 ? 757 GLN A NE2   1 
ATOM 6266 N N     . GLN B 2 758 ? 9.69700   38.95200  36.81000 1.000 134.36243 ? 758 GLN A N     1 
ATOM 6267 C CA    . GLN B 2 758 ? 10.75600  39.90900  37.22600 1.000 140.11867 ? 758 GLN A CA    1 
ATOM 6268 C C     . GLN B 2 758 ? 10.08300  41.21400  37.68000 1.000 141.96945 ? 758 GLN A C     1 
ATOM 6269 O O     . GLN B 2 758 ? 8.91000   41.43100  37.30900 1.000 130.94794 ? 758 GLN A O     1 
ATOM 6270 C CB    . GLN B 2 758 ? 11.76300  40.13800  36.09800 1.000 141.36765 ? 758 GLN A CB    1 
ATOM 6271 C CG    . GLN B 2 758 ? 11.13700  40.36400  34.72600 1.000 143.91773 ? 758 GLN A CG    1 
ATOM 6272 C CD    . GLN B 2 758 ? 10.80000  39.08200  33.99800 1.000 143.19584 ? 758 GLN A CD    1 
ATOM 6273 O OE1   . GLN B 2 758 ? 11.00400  37.97600  34.51200 1.000 137.81790 ? 758 GLN A OE1   1 
ATOM 6274 N NE2   . GLN B 2 758 ? 10.27500  39.21800  32.79000 1.000 155.94516 ? 758 GLN A NE2   1 
ATOM 6275 N N     . GLN B 2 759 ? 10.79400  42.04500  38.44800 1.000 150.88526 ? 759 GLN A N     1 
ATOM 6276 C CA    . GLN B 2 759 ? 10.18600  43.28800  38.99100 1.000 151.72830 ? 759 GLN A CA    1 
ATOM 6277 C C     . GLN B 2 759 ? 9.59200   44.11600  37.84200 1.000 151.08234 ? 759 GLN A C     1 
ATOM 6278 O O     . GLN B 2 759 ? 8.40700   44.49700  37.94100 1.000 143.52496 ? 759 GLN A O     1 
ATOM 6279 C CB    . GLN B 2 759 ? 11.21400  44.12500  39.75400 1.000 129.00018 ? 759 GLN A CB    1 
ATOM 6280 C CG    . GLN B 2 759 ? 11.53000  43.61800  41.15800 1.000 123.40883 ? 759 GLN A CG    1 
ATOM 6281 C CD    . GLN B 2 759 ? 12.21900  42.27200  41.17600 1.000 143.39932 ? 759 GLN A CD    1 
ATOM 6282 O OE1   . GLN B 2 759 ? 13.29800  42.09100  40.60200 1.000 149.92072 ? 759 GLN A OE1   1 
ATOM 6283 N NE2   . GLN B 2 759 ? 11.59700  41.30700  41.83900 1.000 139.80407 ? 759 GLN A NE2   1 
ATOM 6284 N N     . ASN B 2 760 ? 10.38000  44.36800  36.79400 1.000 148.96902 ? 760 ASN A N     1 
ATOM 6285 C CA    . ASN B 2 760 ? 9.90600   45.20200  35.65700 1.000 150.04900 ? 760 ASN A CA    1 
ATOM 6286 C C     . ASN B 2 760 ? 10.13200  44.45100  34.34400 1.000 148.29623 ? 760 ASN A C     1 
ATOM 6287 O O     . ASN B 2 760 ? 10.77900  43.38500  34.38200 1.000 137.84883 ? 760 ASN A O     1 
ATOM 6288 C CB    . ASN B 2 760 ? 10.62000  46.54700  35.60400 1.000 140.34102 ? 760 ASN A CB    1 
ATOM 6289 C CG    . ASN B 2 760 ? 10.21000  47.48100  36.71800 1.000 151.34720 ? 760 ASN A CG    1 
ATOM 6290 O OD1   . ASN B 2 760 ? 9.35400   47.14100  37.54200 1.000 148.72602 ? 760 ASN A OD1   1 
ATOM 6291 N ND2   . ASN B 2 760 ? 10.80100  48.66700  36.75500 1.000 146.48537 ? 760 ASN A ND2   1 
ATOM 6292 N N     . GLN B 2 761 ? 9.62200   44.98900  33.23300 1.000 147.36995 ? 761 GLN A N     1 
ATOM 6293 C CA    . GLN B 2 761 ? 9.85700   44.36900  31.90200 1.000 151.65005 ? 761 GLN A CA    1 
ATOM 6294 C C     . GLN B 2 761 ? 9.43700   42.89300  31.92200 1.000 140.34469 ? 761 GLN A C     1 
ATOM 6295 O O     . GLN B 2 761 ? 10.28700  42.03500  31.60100 1.000 131.88554 ? 761 GLN A O     1 
ATOM 6296 C CB    . GLN B 2 761 ? 11.32700  44.47600  31.49700 1.000 148.83822 ? 761 GLN A CB    1 
ATOM 6297 C CG    . GLN B 2 761 ? 11.82600  45.90700  31.33100 1.000 149.29020 ? 761 GLN A CG    1 
ATOM 6298 C CD    . GLN B 2 761 ? 13.21600  45.98100  30.74000 1.000 152.88644 ? 761 GLN A CD    1 
ATOM 6299 O OE1   . GLN B 2 761 ? 13.83800  44.96100  30.42200 1.000 138.14671 ? 761 GLN A OE1   1 
ATOM 6300 N NE2   . GLN B 2 761 ? 13.71800  47.19700  30.58100 1.000 164.71391 ? 761 GLN A NE2   1 
ATOM 6301 N N     . ASN B 2 762 ? 8.17800   42.61200  32.26500 1.000 141.15682 ? 762 ASN A N     1 
ATOM 6302 C CA    . ASN B 2 762 ? 7.68200   41.20800  32.22200 1.000 125.68673 ? 762 ASN A CA    1 
ATOM 6303 C C     . ASN B 2 762 ? 7.31700   40.86700  30.77400 1.000 130.84291 ? 762 ASN A C     1 
ATOM 6304 O O     . ASN B 2 762 ? 6.11500   40.90800  30.43700 1.000 114.27586 ? 762 ASN A O     1 
ATOM 6305 C CB    . ASN B 2 762 ? 6.54400   40.98500  33.21200 1.000 117.89740 ? 762 ASN A CB    1 
ATOM 6306 C CG    . ASN B 2 762 ? 7.05500   40.83300  34.62500 1.000 130.61236 ? 762 ASN A CG    1 
ATOM 6307 O OD1   . ASN B 2 762 ? 7.81400   39.90200  34.91300 1.000 121.92873 ? 762 ASN A OD1   1 
ATOM 6308 N ND2   . ASN B 2 762 ? 6.65300   41.72700  35.51500 1.000 134.35727 ? 762 ASN A ND2   1 
ATOM 6309 N N     . TYR B 2 763 ? 8.32300   40.55900  29.95100 1.000 133.62351 ? 763 TYR A N     1 
ATOM 6310 C CA    . TYR B 2 763 ? 8.08200   40.22000  28.52300 1.000 127.26849 ? 763 TYR A CA    1 
ATOM 6311 C C     . TYR B 2 763 ? 8.29400   38.72200  28.32500 1.000 137.91548 ? 763 TYR A C     1 
ATOM 6312 O O     . TYR B 2 763 ? 8.27200   38.25300  27.16900 1.000 123.84832 ? 763 TYR A O     1 
ATOM 6313 C CB    . TYR B 2 763 ? 9.02800   41.03800  27.64100 1.000 135.29567 ? 763 TYR A CB    1 
ATOM 6314 C CG    . TYR B 2 763 ? 9.05600   42.53100  27.94200 1.000 156.95534 ? 763 TYR A CG    1 
ATOM 6315 C CD1   . TYR B 2 763 ? 7.91700   43.20200  28.37200 1.000 156.35119 ? 763 TYR A CD1   1 
ATOM 6316 C CD2   . TYR B 2 763 ? 10.22700  43.26500  27.80600 1.000 155.81610 ? 763 TYR A CD2   1 
ATOM 6317 C CE1   . TYR B 2 763 ? 7.94200   44.55800  28.65200 1.000 162.31519 ? 763 TYR A CE1   1 
ATOM 6318 C CE2   . TYR B 2 763 ? 10.26400  44.62200  28.08100 1.000 151.36047 ? 763 TYR A CE2   1 
ATOM 6319 C CZ    . TYR B 2 763 ? 9.11900   45.27000  28.50500 1.000 163.65210 ? 763 TYR A CZ    1 
ATOM 6320 O OH    . TYR B 2 763 ? 9.15200   46.60600  28.77900 1.000 163.97957 ? 763 TYR A OH    1 
ATOM 6321 N N     . LYS B 2 764 ? 8.49100   37.98600  29.42300 1.000 134.74782 ? 764 LYS A N     1 
ATOM 6322 C CA    . LYS B 2 764 ? 8.67000   36.51300  29.34200 1.000 122.01585 ? 764 LYS A CA    1 
ATOM 6323 C C     . LYS B 2 764 ? 7.35600   35.87100  28.88100 1.000 117.48319 ? 764 LYS A C     1 
ATOM 6324 O O     . LYS B 2 764 ? 7.37600   34.69100  28.47100 1.000 113.51709 ? 764 LYS A O     1 
ATOM 6325 C CB    . LYS B 2 764 ? 9.08500   35.94500  30.70200 1.000 123.76445 ? 764 LYS A CB    1 
ATOM 6326 C CG    . LYS B 2 764 ? 10.53800  36.19000  31.07900 1.000 132.14536 ? 764 LYS A CG    1 
ATOM 6327 C CD    . LYS B 2 764 ? 11.00000  35.34400  32.25900 1.000 147.11759 ? 764 LYS A CD    1 
ATOM 6328 C CE    . LYS B 2 764 ? 12.47100  35.45100  32.50600 1.000 157.09387 ? 764 LYS A CE    1 
ATOM 6329 N NZ    . LYS B 2 764 ? 12.88400  36.83600  32.74500 1.000 159.72760 ? 764 LYS A NZ    1 
ATOM 6330 N N     . ILE B 2 765 ? 6.25800   36.62500  28.95500 1.000 120.22252 ? 765 ILE A N     1 
ATOM 6331 C CA    . ILE B 2 765 ? 4.92700   36.08700  28.55300 1.000 118.62272 ? 765 ILE A CA    1 
ATOM 6332 C C     . ILE B 2 765 ? 5.01900   35.63800  27.08900 1.000 117.53273 ? 765 ILE A C     1 
ATOM 6333 O O     . ILE B 2 765 ? 4.46100   34.57300  26.75500 1.000 130.91277 ? 765 ILE A O     1 
ATOM 6334 C CB    . ILE B 2 765 ? 3.82900   37.14600  28.75500 1.000 122.82446 ? 765 ILE A CB    1 
ATOM 6335 C CG1   . ILE B 2 765 ? 4.05100   37.95000  30.03600 1.000 135.59677 ? 765 ILE A CG1   1 
ATOM 6336 C CG2   . ILE B 2 765 ? 2.44000   36.50900  28.71600 1.000 115.73080 ? 765 ILE A CG2   1 
ATOM 6337 C CD1   . ILE B 2 765 ? 4.07500   37.10900  31.30000 1.000 119.99389 ? 765 ILE A CD1   1 
ATOM 6338 N N     . VAL B 2 766 ? 5.70900   36.42200  26.26100 1.000 132.19745 ? 766 VAL A N     1 
ATOM 6339 C CA    . VAL B 2 766 ? 5.84200   36.07000  24.81700 1.000 142.32494 ? 766 VAL A CA    1 
ATOM 6340 C C     . VAL B 2 766 ? 6.57600   34.72200  24.72400 1.000 133.65403 ? 766 VAL A C     1 
ATOM 6341 O O     . VAL B 2 766 ? 6.14100   33.87600  23.92000 1.000 132.05175 ? 766 VAL A O     1 
ATOM 6342 C CB    . VAL B 2 766 ? 6.54100   37.16900  23.99100 1.000 148.16032 ? 766 VAL A CB    1 
ATOM 6343 C CG1   . VAL B 2 766 ? 5.92400   38.54000  24.24400 1.000 134.44878 ? 766 VAL A CG1   1 
ATOM 6344 C CG2   . VAL B 2 766 ? 8.04700   37.21300  24.21900 1.000 138.69203 ? 766 VAL A CG2   1 
ATOM 6345 N N     . GLN B 2 767 ? 7.61100   34.51500  25.54500 1.000 124.66790 ? 767 GLN A N     1 
ATOM 6346 C CA    . GLN B 2 767 ? 8.42300   33.27100  25.46700 1.000 124.50661 ? 767 GLN A CA    1 
ATOM 6347 C C     . GLN B 2 767 ? 7.52600   32.03800  25.65100 1.000 123.87906 ? 767 GLN A C     1 
ATOM 6348 O O     . GLN B 2 767 ? 7.89800   30.95900  25.14500 1.000 135.68022 ? 767 GLN A O     1 
ATOM 6349 C CB    . GLN B 2 767 ? 9.53500   33.29200  26.51600 1.000 117.10338 ? 767 GLN A CB    1 
ATOM 6350 C CG    . GLN B 2 767 ? 10.56800  34.39200  26.30100 1.000 142.48448 ? 767 GLN A CG    1 
ATOM 6351 C CD    . GLN B 2 767 ? 11.62400  34.43600  27.38300 1.000 141.49435 ? 767 GLN A CD    1 
ATOM 6352 O OE1   . GLN B 2 767 ? 12.32000  33.45000  27.64500 1.000 137.04545 ? 767 GLN A OE1   1 
ATOM 6353 N NE2   . GLN B 2 767 ? 11.74700  35.58600  28.02900 1.000 131.18813 ? 767 GLN A NE2   1 
ATOM 6354 N N     . GLN B 2 768 ? 6.38600   32.19100  26.32900 1.000 115.78613 ? 768 GLN A N     1 
ATOM 6355 C CA    . GLN B 2 768 ? 5.51700   31.01800  26.61400 1.000 112.78930 ? 768 GLN A CA    1 
ATOM 6356 C C     . GLN B 2 768 ? 5.17000   30.30600  25.29400 1.000 135.75880 ? 768 GLN A C     1 
ATOM 6357 O O     . GLN B 2 768 ? 5.18700   29.05700  25.27200 1.000 155.44833 ? 768 GLN A O     1 
ATOM 6358 C CB    . GLN B 2 768 ? 4.26600   31.45400  27.37800 1.000 108.09638 ? 768 GLN A CB    1 
ATOM 6359 C CG    . GLN B 2 768 ? 3.29700   30.31800  27.68500 1.000 126.65399 ? 768 GLN A CG    1 
ATOM 6360 C CD    . GLN B 2 768 ? 2.39800   30.60200  28.86800 1.000 138.86299 ? 768 GLN A CD    1 
ATOM 6361 O OE1   . GLN B 2 768 ? 2.49500   31.65100  29.51300 1.000 136.92017 ? 768 GLN A OE1   1 
ATOM 6362 N NE2   . GLN B 2 768 ? 1.51800   29.65900  29.17200 1.000 140.61928 ? 768 GLN A NE2   1 
ATOM 6363 N N     . PHE B 2 769 ? 4.88200   31.07100  24.23700 1.000 129.02370 ? 769 PHE A N     1 
ATOM 6364 C CA    . PHE B 2 769 ? 4.49700   30.46500  22.93200 1.000 159.48402 ? 769 PHE A CA    1 
ATOM 6365 C C     . PHE B 2 769 ? 5.63700   30.65900  21.92400 1.000 157.50456 ? 769 PHE A C     1 
ATOM 6366 O O     . PHE B 2 769 ? 5.41100   30.47800  20.70700 1.000 140.93876 ? 769 PHE A O     1 
ATOM 6367 C CB    . PHE B 2 769 ? 3.16800   31.07900  22.48000 1.000 141.00946 ? 769 PHE A CB    1 
ATOM 6368 C CG    . PHE B 2 769 ? 2.39300   30.26100  21.45400 1.000 159.88094 ? 769 PHE A CG    1 
ATOM 6369 C CD1   . PHE B 2 769 ? 2.57000   28.88500  21.35600 1.000 160.13618 ? 769 PHE A CD1   1 
ATOM 6370 C CD2   . PHE B 2 769 ? 1.47300   30.86700  20.60600 1.000 159.84119 ? 769 PHE A CD2   1 
ATOM 6371 C CE1   . PHE B 2 769 ? 1.85700   28.14300  20.42800 1.000 155.81025 ? 769 PHE A CE1   1 
ATOM 6372 C CE2   . PHE B 2 769 ? 0.76300   30.11900  19.68000 1.000 162.57073 ? 769 PHE A CE2   1 
ATOM 6373 C CZ    . PHE B 2 769 ? 0.95600   28.76000  19.59300 1.000 158.16914 ? 769 PHE A CZ    1 
ATOM 6374 N N     . ASN B 2 770 ? 6.83000   31.01400  22.41300 1.000 151.62545 ? 770 ASN A N     1 
ATOM 6375 C CA    . ASN B 2 770 ? 8.00200   31.21600  21.51500 1.000 160.42626 ? 770 ASN A CA    1 
ATOM 6376 C C     . ASN B 2 770 ? 8.71900   29.88000  21.29700 1.000 168.49728 ? 770 ASN A C     1 
ATOM 6377 O O     . ASN B 2 770 ? 9.78500   29.68100  21.92000 1.000 163.94519 ? 770 ASN A O     1 
ATOM 6378 C CB    . ASN B 2 770 ? 8.95800   32.27500  22.05500 1.000 158.35383 ? 770 ASN A CB    1 
ATOM 6379 C CG    . ASN B 2 770 ? 8.42500   33.67700  21.88000 1.000 151.74504 ? 770 ASN A CG    1 
ATOM 6380 O OD1   . ASN B 2 770 ? 9.08300   34.64400  22.27700 1.000 151.94780 ? 770 ASN A OD1   1 
ATOM 6381 N ND2   . ASN B 2 770 ? 7.24400   33.81100  21.29400 1.000 150.84950 ? 770 ASN A ND2   1 
ATOM 6382 N N     . ASN B 2 771 ? 8.14800   28.99800  20.46800 1.000 183.27719 ? 771 ASN A N     1 
ATOM 6383 C CA    . ASN B 2 771 ? 8.77300   27.67800  20.16100 1.000 174.94636 ? 771 ASN A CA    1 
ATOM 6384 C C     . ASN B 2 771 ? 8.79400   26.82000  21.43200 1.000 175.18233 ? 771 ASN A C     1 
ATOM 6385 O O     . ASN B 2 771 ? 9.46600   25.76500  21.42900 1.000 173.77506 ? 771 ASN A O     1 
ATOM 6386 C CB    . ASN B 2 771 ? 10.15100  27.84400  19.52700 1.000 170.60304 ? 771 ASN A CB    1 
ATOM 6387 C CG    . ASN B 2 771 ? 10.62300  26.58600  18.83700 1.000 178.40291 ? 771 ASN A CG    1 
ATOM 6388 O OD1   . ASN B 2 771 ? 9.96700   26.10300  17.90700 1.000 179.36397 ? 771 ASN A OD1   1 
ATOM 6389 N ND2   . ASN B 2 771 ? 11.74700  26.04000  19.27700 1.000 176.17712 ? 771 ASN A ND2   1 
ATOM 6390 N N     . PHE B 2 772 ? 8.07700   27.25000  22.47400 1.000 164.50802 ? 772 PHE A N     1 
ATOM 6391 C CA    . PHE B 2 772 ? 8.01900   26.48800  23.75100 1.000 152.35030 ? 772 PHE A CA    1 
ATOM 6392 C C     . PHE B 2 772 ? 6.57900   26.03900  23.95900 1.000 144.83547 ? 772 PHE A C     1 
ATOM 6393 O O     . PHE B 2 772 ? 6.12300   25.94900  25.11900 1.000 146.02270 ? 772 PHE A O     1 
ATOM 6394 C CB    . PHE B 2 772 ? 8.54200   27.39100  24.87000 1.000 143.80155 ? 772 PHE A CB    1 
ATOM 6395 C CG    . PHE B 2 772 ? 9.96100   27.90900  24.67500 1.000 140.63631 ? 772 PHE A CG    1 
ATOM 6396 C CD1   . PHE B 2 772 ? 10.92500  27.13500  24.03800 1.000 146.12322 ? 772 PHE A CD1   1 
ATOM 6397 C CD2   . PHE B 2 772 ? 10.32500  29.17300  25.12300 1.000 148.24958 ? 772 PHE A CD2   1 
ATOM 6398 C CE1   . PHE B 2 772 ? 12.21300  27.61400  23.86000 1.000 150.13183 ? 772 PHE A CE1   1 
ATOM 6399 C CE2   . PHE B 2 772 ? 11.61500  29.64700  24.94200 1.000 147.50258 ? 772 PHE A CE2   1 
ATOM 6400 C CZ    . PHE B 2 772 ? 12.55500  28.86600  24.31200 1.000 158.27990 ? 772 PHE A CZ    1 
ATOM 6401 N N     . ASP B 2 773 ? 5.87800   25.75100  22.85900 1.000 157.50431 ? 773 ASP A N     1 
ATOM 6402 C CA    . ASP B 2 773 ? 4.44000   25.37100  22.93600 1.000 165.79186 ? 773 ASP A CA    1 
ATOM 6403 C C     . ASP B 2 773 ? 4.25000   24.11800  23.79700 1.000 155.06668 ? 773 ASP A C     1 
ATOM 6404 O O     . ASP B 2 773 ? 3.19700   24.01800  24.46200 1.000 157.06457 ? 773 ASP A O     1 
ATOM 6405 C CB    . ASP B 2 773 ? 3.85800   25.19900  21.54200 1.000 161.44314 ? 773 ASP A CB    1 
ATOM 6406 C CG    . ASP B 2 773 ? 4.64300   24.28200  20.61400 1.000 159.03278 ? 773 ASP A CG    1 
ATOM 6407 O OD1   . ASP B 2 773 ? 4.77400   23.08400  20.94300 1.000 150.18829 ? 773 ASP A OD1   1 
ATOM 6408 O OD2   . ASP B 2 773 ? 5.12300   24.77700  19.57300 1.000 160.43727 ? 773 ASP A OD2   1 
ATOM 6409 N N     . LYS B 2 774 ? 5.20700   23.18700  23.77200 1.000 144.65979 ? 774 LYS A N     1 
ATOM 6410 C CA    . LYS B 2 774 ? 5.02200   21.90900  24.51000 1.000 152.80500 ? 774 LYS A CA    1 
ATOM 6411 C C     . LYS B 2 774 ? 5.88700   21.89500  25.78200 1.000 154.42951 ? 774 LYS A C     1 
ATOM 6412 O O     . LYS B 2 774 ? 5.86000   20.87100  26.50000 1.000 171.07854 ? 774 LYS A O     1 
ATOM 6413 C CB    . LYS B 2 774 ? 5.37800   20.72900  23.59900 1.000 161.12776 ? 774 LYS A CB    1 
ATOM 6414 C CG    . LYS B 2 774 ? 6.85692   20.37862  23.54329 1.000 155.50238 ? 774 LYS A CG    1 
ATOM 6415 C CD    . LYS B 2 774 ? 7.07893   18.90531  23.22433 1.000 149.17580 ? 774 LYS A CD    1 
ATOM 6416 C CE    . LYS B 2 774 ? 8.49879   18.48801  23.42520 1.000 156.14355 ? 774 LYS A CE    1 
ATOM 6417 N NZ    . LYS B 2 774 ? 8.98120   18.84567  24.76167 1.000 148.05494 ? 774 LYS A NZ    1 
ATOM 6418 N N     . ALA B 2 775 ? 6.60800   22.98400  26.06300 1.000 130.94324 ? 775 ALA A N     1 
ATOM 6419 C CA    . ALA B 2 775 ? 7.53400   22.97400  27.22100 1.000 122.22030 ? 775 ALA A CA    1 
ATOM 6420 C C     . ALA B 2 775 ? 7.61700   24.35900  27.86300 1.000 117.93214 ? 775 ALA A C     1 
ATOM 6421 O O     . ALA B 2 775 ? 8.50400   25.14400  27.46300 1.000 138.73276 ? 775 ALA A O     1 
ATOM 6422 C CB    . ALA B 2 775 ? 8.89400   22.51300  26.75800 1.000 131.50747 ? 775 ALA A CB    1 
ATOM 6423 N N     . ILE B 2 776 ? 6.75000   24.63500  28.84400 1.000 109.11655 ? 776 ILE A N     1 
ATOM 6424 C CA    . ILE B 2 776 ? 6.75000   25.96600  29.52300 1.000 105.25220 ? 776 ILE A CA    1 
ATOM 6425 C C     . ILE B 2 776 ? 6.16400   25.80100  30.93300 1.000 95.49806  ? 776 ILE A C     1 
ATOM 6426 O O     . ILE B 2 776 ? 5.16100   25.07100  31.06700 1.000 112.23603 ? 776 ILE A O     1 
ATOM 6427 C CB    . ILE B 2 776 ? 5.94100   26.99400  28.71700 1.000 125.34153 ? 776 ILE A CB    1 
ATOM 6428 C CG1   . ILE B 2 776 ? 6.54342   27.23457  27.34087 1.000 134.74806 ? 776 ILE A CG1   1 
ATOM 6429 C CG2   . ILE B 2 776 ? 5.80662   28.30193  29.49361 1.000 137.35829 ? 776 ILE A CG2   1 
ATOM 6430 C CD1   . ILE B 2 776 ? 8.03741   26.98058  27.27310 1.000 141.30066 ? 776 ILE A CD1   1 
ATOM 6431 N N     . LEU B 2 777 ? 6.75700   26.45600  31.93300 1.000 91.98695  ? 777 LEU A N     1 
ATOM 6432 C CA    . LEU B 2 777 ? 6.19900   26.42200  33.30900 1.000 87.84064  ? 777 LEU A CA    1 
ATOM 6433 C C     . LEU B 2 777 ? 6.26600   27.84300  33.88100 1.000 96.19109  ? 777 LEU A C     1 
ATOM 6434 O O     . LEU B 2 777 ? 7.16000   28.09800  34.71100 1.000 110.80728 ? 777 LEU A O     1 
ATOM 6435 C CB    . LEU B 2 777 ? 6.98100   25.44300  34.18000 1.000 91.15619  ? 777 LEU A CB    1 
ATOM 6436 C CG    . LEU B 2 777 ? 7.03700   23.99500  33.68700 1.000 96.85521  ? 777 LEU A CG    1 
ATOM 6437 C CD1   . LEU B 2 777 ? 8.03900   23.22000  34.51600 1.000 130.08046 ? 777 LEU A CD1   1 
ATOM 6438 C CD2   . LEU B 2 777 ? 5.66400   23.36100  33.78600 1.000 119.65862 ? 777 LEU A CD2   1 
ATOM 6439 N N     . LEU B 2 778 ? 5.36400   28.73100  33.45400 1.000 90.84324  ? 778 LEU A N     1 
ATOM 6440 C CA    . LEU B 2 778 ? 5.43200   30.14800  33.90000 1.000 94.00784  ? 778 LEU A CA    1 
ATOM 6441 C C     . LEU B 2 778 ? 5.00400   30.26600  35.37100 1.000 83.89086  ? 778 LEU A C     1 
ATOM 6442 O O     . LEU B 2 778 ? 3.86600   29.87100  35.68900 1.000 91.36003  ? 778 LEU A O     1 
ATOM 6443 C CB    . LEU B 2 778 ? 4.56700   31.01700  32.98900 1.000 93.58644  ? 778 LEU A CB    1 
ATOM 6444 C CG    . LEU B 2 778 ? 4.56000   32.51600  33.30400 1.000 99.09136  ? 778 LEU A CG    1 
ATOM 6445 C CD1   . LEU B 2 778 ? 5.97600   33.05400  33.39900 1.000 112.62241 ? 778 LEU A CD1   1 
ATOM 6446 C CD2   . LEU B 2 778 ? 3.77700   33.27500  32.25000 1.000 108.12886 ? 778 LEU A CD2   1 
ATOM 6447 N N     . GLY B 2 779 ? 5.88500   30.79000  36.22700 1.000 78.17336  ? 779 GLY A N     1 
ATOM 6448 C CA    . GLY B 2 779 ? 5.53800   31.00600  37.64500 1.000 78.19772  ? 779 GLY A CA    1 
ATOM 6449 C C     . GLY B 2 779 ? 5.41000   32.48900  37.91400 1.000 99.35869  ? 779 GLY A C     1 
ATOM 6450 O O     . GLY B 2 779 ? 6.38000   33.21500  37.62500 1.000 113.95869 ? 779 GLY A O     1 
ATOM 6451 N N     . THR B 2 780 ? 4.26700   32.93800  38.44000 1.000 122.22819 ? 780 THR A N     1 
ATOM 6452 C CA    . THR B 2 780 ? 4.04300   34.39100  38.62100 1.000 97.22922  ? 780 THR A CA    1 
ATOM 6453 C C     . THR B 2 780 ? 3.45000   34.66900  39.98200 1.000 99.55580  ? 780 THR A C     1 
ATOM 6454 O O     . THR B 2 780 ? 3.02600   33.70500  40.65200 1.000 103.58365 ? 780 THR A O     1 
ATOM 6455 C CB    . THR B 2 780 ? 3.13200   34.89900  37.50900 1.000 130.99922 ? 780 THR A CB    1 
ATOM 6456 O OG1   . THR B 2 780 ? 2.12000   33.90300  37.41800 1.000 158.11865 ? 780 THR A OG1   1 
ATOM 6457 C CG2   . THR B 2 780 ? 3.85200   35.03900  36.18100 1.000 125.70990 ? 780 THR A CG2   1 
ATOM 6458 N N     . SER B 2 781 ? 3.43600   35.94000  40.39200 1.000 111.61902 ? 781 SER A N     1 
ATOM 6459 C CA    . SER B 2 781 ? 2.92100   36.30700  41.73700 1.000 110.61583 ? 781 SER A CA    1 
ATOM 6460 C C     . SER B 2 781 ? 1.63900   37.13900  41.60000 1.000 128.36484 ? 781 SER A C     1 
ATOM 6461 O O     . SER B 2 781 ? 0.62700   36.77000  42.23200 1.000 150.45818 ? 781 SER A O     1 
ATOM 6462 C CB    . SER B 2 781 ? 3.96500   37.04300  42.53700 1.000 96.28607  ? 781 SER A CB    1 
ATOM 6463 O OG    . SER B 2 781 ? 3.45700   37.40900  43.81300 1.000 111.51954 ? 781 SER A OG    1 
ATOM 6464 N N     . THR B 2 782 ? 1.68900   38.22500  40.82200 1.000 122.53220 ? 782 THR A N     1 
ATOM 6465 C CA    . THR B 2 782 ? 0.50900   39.10900  40.68500 1.000 131.31721 ? 782 THR A CA    1 
ATOM 6466 C C     . THR B 2 782 ? 0.30600   39.46300  39.22500 1.000 135.24576 ? 782 THR A C     1 
ATOM 6467 O O     . THR B 2 782 ? 0.43300   40.66100  38.88600 1.000 119.60132 ? 782 THR A O     1 
ATOM 6468 C CB    . THR B 2 782 ? 0.69000   40.35500  41.55400 1.000 127.39274 ? 782 THR A CB    1 
ATOM 6469 O OG1   . THR B 2 782 ? 1.27200   39.91200  42.77600 1.000 134.52444 ? 782 THR A OG1   1 
ATOM 6470 C CG2   . THR B 2 782 ? -0.62600  41.05400  41.84900 1.000 121.04141 ? 782 THR A CG2   1 
ATOM 6471 N N     . PHE B 2 783 ? 0.01300   38.47100  38.38000 1.000 143.16664 ? 783 PHE A N     1 
ATOM 6472 C CA    . PHE B 2 783 ? -0.30100  38.75700  36.95000 1.000 146.21942 ? 783 PHE A CA    1 
ATOM 6473 C C     . PHE B 2 783 ? -1.63400  38.07200  36.62800 1.000 147.42189 ? 783 PHE A C     1 
ATOM 6474 O O     . PHE B 2 783 ? -1.95100  37.85600  35.43500 1.000 146.31354 ? 783 PHE A O     1 
ATOM 6475 C CB    . PHE B 2 783 ? 0.90400   38.39300  36.06800 1.000 136.20202 ? 783 PHE A CB    1 
ATOM 6476 C CG    . PHE B 2 783 ? 1.08825   36.94774  35.62073 1.000 145.76293 ? 783 PHE A CG    1 
ATOM 6477 C CD1   . PHE B 2 783 ? 1.43916   35.94429  36.51729 1.000 152.84294 ? 783 PHE A CD1   1 
ATOM 6478 C CD2   . PHE B 2 783 ? 0.89590   36.59470  34.29039 1.000 133.03752 ? 783 PHE A CD2   1 
ATOM 6479 C CE1   . PHE B 2 783 ? 1.59295   34.63428  36.09350 1.000 160.80020 ? 783 PHE A CE1   1 
ATOM 6480 C CE2   . PHE B 2 783 ? 1.05496   35.28385  33.87155 1.000 133.58073 ? 783 PHE A CE2   1 
ATOM 6481 C CZ    . PHE B 2 783 ? 1.40344   34.30753  34.77250 1.000 148.15598 ? 783 PHE A CZ    1 
ATOM 6482 N N     . PHE B 2 784 ? -2.43000  37.79200  37.66500 1.000 135.85252 ? 784 PHE A N     1 
ATOM 6483 C CA    . PHE B 2 784 ? -3.71500  37.06100  37.47500 1.000 112.22469 ? 784 PHE A CA    1 
ATOM 6484 C C     . PHE B 2 784 ? -4.51900  37.70800  36.34400 1.000 113.24673 ? 784 PHE A C     1 
ATOM 6485 O O     . PHE B 2 784 ? -5.32600  37.00200  35.70500 1.000 135.84768 ? 784 PHE A O     1 
ATOM 6486 C CB    . PHE B 2 784 ? -4.52900  37.03000  38.77400 1.000 116.17058 ? 784 PHE A CB    1 
ATOM 6487 C CG    . PHE B 2 784 ? -3.92900  36.23700  39.92900 1.000 148.56424 ? 784 PHE A CG    1 
ATOM 6488 C CD1   . PHE B 2 784 ? -2.55600  36.20000  40.14500 1.000 138.63965 ? 784 PHE A CD1   1 
ATOM 6489 C CD2   . PHE B 2 784 ? -4.74700  35.54400  40.81400 1.000 135.91906 ? 784 PHE A CD2   1 
ATOM 6490 C CE1   . PHE B 2 784 ? -2.02200  35.48100  41.20200 1.000 124.60002 ? 784 PHE A CE1   1 
ATOM 6491 C CE2   . PHE B 2 784 ? -4.20800  34.82500  41.86800 1.000 123.28897 ? 784 PHE A CE2   1 
ATOM 6492 C CZ    . PHE B 2 784 ? -2.84700  34.79600  42.06200 1.000 135.70428 ? 784 PHE A CZ    1 
ATOM 6493 N N     . GLU B 2 785 ? -4.32500  39.00900  36.11400 1.000 111.68257 ? 785 GLU A N     1 
ATOM 6494 C CA    . GLU B 2 785 ? -5.01800  39.68800  34.98700 1.000 104.61750 ? 785 GLU A CA    1 
ATOM 6495 C C     . GLU B 2 785 ? -3.98800  40.24300  33.99100 1.000 136.98811 ? 785 GLU A C     1 
ATOM 6496 O O     . GLU B 2 785 ? -2.91000  40.69400  34.44000 1.000 144.85667 ? 785 GLU A O     1 
ATOM 6497 C CB    . GLU B 2 785 ? -5.93800  40.79600  35.49900 1.000 119.49483 ? 785 GLU A CB    1 
ATOM 6498 C CG    . GLU B 2 785 ? -5.33100  41.62200  36.62800 1.000 125.20416 ? 785 GLU A CG    1 
ATOM 6499 C CD    . GLU B 2 785 ? -6.35400  42.57000  37.22100 1.000 128.08469 ? 785 GLU A CD    1 
ATOM 6500 O OE1   . GLU B 2 785 ? -6.88300  43.40200  36.45500 1.000 134.63574 ? 785 GLU A OE1   1 
ATOM 6501 O OE2   . GLU B 2 785 ? -6.62900  42.47100  38.43500 1.000 121.15060 ? 785 GLU A OE2   1 
ATOM 6502 N N     . GLY B 2 786 ? -4.31000  40.20400  32.69600 1.000 116.28316 ? 786 GLY A N     1 
ATOM 6503 C CA    . GLY B 2 786 ? -3.41900  40.74600  31.65300 1.000 129.38039 ? 786 GLY A CA    1 
ATOM 6504 C C     . GLY B 2 786 ? -2.65100  39.64800  30.94600 1.000 151.37216 ? 786 GLY A C     1 
ATOM 6505 O O     . GLY B 2 786 ? -1.58400  39.95400  30.37200 1.000 153.07444 ? 786 GLY A O     1 
ATOM 6506 N N     . PHE B 2 787 ? -3.16200  38.41500  30.98000 1.000 147.41586 ? 787 PHE A N     1 
ATOM 6507 C CA    . PHE B 2 787 ? -2.42300  37.27500  30.37300 1.000 133.92705 ? 787 PHE A CA    1 
ATOM 6508 C C     . PHE B 2 787 ? -3.30400  36.54200  29.36400 1.000 129.75709 ? 787 PHE A C     1 
ATOM 6509 O O     . PHE B 2 787 ? -4.46600  36.22300  29.68200 1.000 132.05869 ? 787 PHE A O     1 
ATOM 6510 C CB    . PHE B 2 787 ? -1.92900  36.33000  31.47100 1.000 128.06484 ? 787 PHE A CB    1 
ATOM 6511 C CG    . PHE B 2 787 ? -1.62100  34.93000  30.96200 1.000 138.05167 ? 787 PHE A CG    1 
ATOM 6512 C CD1   . PHE B 2 787 ? -0.43800  34.66600  30.28300 1.000 139.85371 ? 787 PHE A CD1   1 
ATOM 6513 C CD2   . PHE B 2 787 ? -2.50800  33.88200  31.17400 1.000 143.25730 ? 787 PHE A CD2   1 
ATOM 6514 C CE1   . PHE B 2 787 ? -0.16000  33.39300  29.81800 1.000 138.82717 ? 787 PHE A CE1   1 
ATOM 6515 C CE2   . PHE B 2 787 ? -2.22000  32.61000  30.71000 1.000 139.35936 ? 787 PHE A CE2   1 
ATOM 6516 C CZ    . PHE B 2 787 ? -1.04700  32.36700  30.03600 1.000 141.63388 ? 787 PHE A CZ    1 
ATOM 6517 N N     . ASP B 2 788 ? -2.76100  36.26800  28.17500 1.000 129.26668 ? 788 ASP A N     1 
ATOM 6518 C CA    . ASP B 2 788 ? -3.51600  35.49100  27.15400 1.000 133.35737 ? 788 ASP A CA    1 
ATOM 6519 C C     . ASP B 2 788 ? -2.90100  34.09200  27.06400 1.000 136.64110 ? 788 ASP A C     1 
ATOM 6520 O O     . ASP B 2 788 ? -1.68200  33.99500  26.81200 1.000 138.76343 ? 788 ASP A O     1 
ATOM 6521 C CB    . ASP B 2 788 ? -3.53800  36.21000  25.81500 1.000 132.54452 ? 788 ASP A CB    1 
ATOM 6522 C CG    . ASP B 2 788 ? -4.25900  35.48900  24.68500 1.000 145.97702 ? 788 ASP A CG    1 
ATOM 6523 O OD1   . ASP B 2 788 ? -3.79300  34.40000  24.28600 1.000 147.09385 ? 788 ASP A OD1   1 
ATOM 6524 O OD2   . ASP B 2 788 ? -5.27200  36.03200  24.19900 1.000 164.01665 ? 788 ASP A OD2   1 
ATOM 6525 N N     . PHE B 2 789 ? -3.71400  33.05300  27.26800 1.000 132.32321 ? 789 PHE A N     1 
ATOM 6526 C CA    . PHE B 2 789 ? -3.20100  31.65900  27.22900 1.000 129.89471 ? 789 PHE A CA    1 
ATOM 6527 C C     . PHE B 2 789 ? -3.53800  31.04900  25.88200 1.000 138.47403 ? 789 PHE A C     1 
ATOM 6528 O O     . PHE B 2 789 ? -4.66500  30.54200  25.71500 1.000 151.29132 ? 789 PHE A O     1 
ATOM 6529 C CB    . PHE B 2 789 ? -3.82900  30.81000  28.33700 1.000 139.58283 ? 789 PHE A CB    1 
ATOM 6530 C CG    . PHE B 2 789 ? -2.98700  29.62900  28.80400 1.000 133.07995 ? 789 PHE A CG    1 
ATOM 6531 C CD1   . PHE B 2 789 ? -2.07500  29.01700  27.95300 1.000 128.62189 ? 789 PHE A CD1   1 
ATOM 6532 C CD2   . PHE B 2 789 ? -3.11400  29.13300  30.09600 1.000 118.88438 ? 789 PHE A CD2   1 
ATOM 6533 C CE1   . PHE B 2 789 ? -1.31300  27.94400  28.38500 1.000 124.57792 ? 789 PHE A CE1   1 
ATOM 6534 C CE2   . PHE B 2 789 ? -2.35000  28.05900  30.52300 1.000 118.09984 ? 789 PHE A CE2   1 
ATOM 6535 C CZ    . PHE B 2 789 ? -1.45200  27.46700  29.66700 1.000 116.14401 ? 789 PHE A CZ    1 
ATOM 6536 N N     . GLN B 2 790 ? -2.59200  31.08700  24.94300 1.000 133.78396 ? 790 GLN A N     1 
ATOM 6537 C CA    . GLN B 2 790 ? -2.82500  30.41900  23.63800 1.000 142.89906 ? 790 GLN A CA    1 
ATOM 6538 C C     . GLN B 2 790 ? -1.83700  29.25300  23.51700 1.000 145.31782 ? 790 GLN A C     1 
ATOM 6539 O O     . GLN B 2 790 ? -0.61500  29.50900  23.56700 1.000 137.54971 ? 790 GLN A O     1 
ATOM 6540 C CB    . GLN B 2 790 ? -2.68900  31.40200  22.47600 1.000 147.34691 ? 790 GLN A CB    1 
ATOM 6541 C CG    . GLN B 2 790 ? -2.97300  30.78000  21.11400 1.000 158.92002 ? 790 GLN A CG    1 
ATOM 6542 C CD    . GLN B 2 790 ? -4.30800  30.06900  21.05300 1.000 162.38019 ? 790 GLN A CD    1 
ATOM 6543 O OE1   . GLN B 2 790 ? -5.36900  30.67100  21.24700 1.000 158.27206 ? 790 GLN A OE1   1 
ATOM 6544 N NE2   . GLN B 2 790 ? -4.26500  28.77300  20.78100 1.000 157.24796 ? 790 GLN A NE2   1 
ATOM 6545 N N     . ALA B 2 791 ? -2.34900  28.02800  23.37300 1.000 138.23987 ? 791 ALA A N     1 
ATOM 6546 C CA    . ALA B 2 791 ? -1.46600  26.84100  23.31200 1.000 135.15517 ? 791 ALA A CA    1 
ATOM 6547 C C     . ALA B 2 791 ? -2.09700  25.75800  22.43800 1.000 129.21676 ? 791 ALA A C     1 
ATOM 6548 O O     . ALA B 2 791 ? -3.34100  25.68000  22.36900 1.000 127.67056 ? 791 ALA A O     1 
ATOM 6549 C CB    . ALA B 2 791 ? -1.20600  26.32800  24.70800 1.000 126.70188 ? 791 ALA A CB    1 
ATOM 6550 N N     . ASN B 2 792 ? -1.25700  24.94400  21.79800 1.000 140.86925 ? 792 ASN A N     1 
ATOM 6551 C CA    . ASN B 2 792 ? -1.76200  23.83500  20.94500 1.000 142.39014 ? 792 ASN A CA    1 
ATOM 6552 C C     . ASN B 2 792 ? -1.82500  22.56200  21.79300 1.000 141.79675 ? 792 ASN A C     1 
ATOM 6553 O O     . ASN B 2 792 ? -1.13500  21.58000  21.44400 1.000 145.25964 ? 792 ASN A O     1 
ATOM 6554 C CB    . ASN B 2 792 ? -0.90400  23.66700  19.69700 1.000 144.82489 ? 792 ASN A CB    1 
ATOM 6555 C CG    . ASN B 2 792 ? 0.57000   23.79900  20.00000 1.000 151.79556 ? 792 ASN A CG    1 
ATOM 6556 O OD1   . ASN B 2 792 ? 1.01900   24.85600  20.45600 1.000 148.78935 ? 792 ASN A OD1   1 
ATOM 6557 N ND2   . ASN B 2 792 ? 1.33500   22.74500  19.75400 1.000 164.56747 ? 792 ASN A ND2   1 
ATOM 6558 N N     . GLY B 2 793 ? -2.61700  22.58400  22.86900 1.000 139.17086 ? 793 GLY A N     1 
ATOM 6559 C CA    . GLY B 2 793 ? -2.73500  21.40900  23.75300 1.000 140.77086 ? 793 GLY A CA    1 
ATOM 6560 C C     . GLY B 2 793 ? -3.49000  21.73900  25.02500 1.000 125.49989 ? 793 GLY A C     1 
ATOM 6561 O O     . GLY B 2 793 ? -4.02700  22.86100  25.11900 1.000 132.40964 ? 793 GLY A O     1 
ATOM 6562 N N     . ILE B 2 794 ? -3.52400  20.80000  25.97400 1.000 115.82047 ? 794 ILE A N     1 
ATOM 6563 C CA    . ILE B 2 794 ? -4.26200  21.01300  27.25400 1.000 119.29554 ? 794 ILE A CA    1 
ATOM 6564 C C     . ILE B 2 794 ? -3.63000  22.20900  27.98300 1.000 119.12652 ? 794 ILE A C     1 
ATOM 6565 O O     . ILE B 2 794 ? -2.40900  22.41200  27.84300 1.000 114.71352 ? 794 ILE A O     1 
ATOM 6566 C CB    . ILE B 2 794 ? -4.24000  19.73800  28.11600 1.000 115.15893 ? 794 ILE A CB    1 
ATOM 6567 C CG1   . ILE B 2 794 ? -5.15200  19.85500  29.33600 1.000 118.20576 ? 794 ILE A CG1   1 
ATOM 6568 C CG2   . ILE B 2 794 ? -2.81200  19.37900  28.51900 1.000 117.40370 ? 794 ILE A CG2   1 
ATOM 6569 C CD1   . ILE B 2 794 ? -6.62600  19.95800  28.99500 1.000 142.82093 ? 794 ILE A CD1   1 
ATOM 6570 N N     . LYS B 2 795 ? -4.44000  22.97600  28.71300 1.000 112.42237 ? 795 LYS A N     1 
ATOM 6571 C CA    . LYS B 2 795 ? -3.91100  24.13200  29.47900 1.000 103.98763 ? 795 LYS A CA    1 
ATOM 6572 C C     . LYS B 2 795 ? -4.11600  23.85900  30.97300 1.000 101.27964 ? 795 LYS A C     1 
ATOM 6573 O O     . LYS B 2 795 ? -5.16400  23.29200  31.33400 1.000 115.51903 ? 795 LYS A O     1 
ATOM 6574 C CB    . LYS B 2 795 ? -4.61500  25.41400  29.02800 1.000 109.56255 ? 795 LYS A CB    1 
ATOM 6575 C CG    . LYS B 2 795 ? -4.35000  25.79100  27.58100 1.000 121.02169 ? 795 LYS A CG    1 
ATOM 6576 C CD    . LYS B 2 795 ? -5.16700  26.97700  27.08700 1.000 122.81144 ? 795 LYS A CD    1 
ATOM 6577 C CE    . LYS B 2 795 ? -4.78800  27.32300  25.68600 1.000 150.88008 ? 795 LYS A CE    1 
ATOM 6578 N NZ    . LYS B 2 795 ? -4.72000  26.11900  24.85400 1.000 160.43292 ? 795 LYS A NZ    1 
ATOM 6579 N N     . CYS B 2 796 ? -3.13800  24.23000  31.79900 1.000 94.04859  ? 796 CYS A N     1 
ATOM 6580 C CA    . CYS B 2 796 ? -3.24900  23.99700  33.25900 1.000 90.74523  ? 796 CYS A CA    1 
ATOM 6581 C C     . CYS B 2 796 ? -2.91300  25.28000  34.02000 1.000 89.03099  ? 796 CYS A C     1 
ATOM 6582 O O     . CYS B 2 796 ? -1.80500  25.81400  33.81600 1.000 99.11720  ? 796 CYS A O     1 
ATOM 6583 C CB    . CYS B 2 796 ? -2.29400  22.90900  33.72600 1.000 92.30798  ? 796 CYS A CB    1 
ATOM 6584 S SG    . CYS B 2 796 ? -2.34500  22.63900  35.51600 1.000 108.12460 ? 796 CYS A SG    1 
ATOM 6585 N N     . VAL B 2 797 ? -3.83600  25.75000  34.85700 1.000 82.87704  ? 797 VAL A N     1 
ATOM 6586 C CA    . VAL B 2 797 ? -3.55000  26.93900  35.70800 1.000 78.98159  ? 797 VAL A CA    1 
ATOM 6587 C C     . VAL B 2 797 ? -3.57800  26.46100  37.16500 1.000 76.29896  ? 797 VAL A C     1 
ATOM 6588 O O     . VAL B 2 797 ? -4.63600  25.97200  37.60500 1.000 99.50442  ? 797 VAL A O     1 
ATOM 6589 C CB    . VAL B 2 797 ? -4.55600  28.07800  35.46500 1.000 77.90634  ? 797 VAL A CB    1 
ATOM 6590 C CG1   . VAL B 2 797 ? -4.41700  29.18700  36.50000 1.000 76.53381  ? 797 VAL A CG1   1 
ATOM 6591 C CG2   . VAL B 2 797 ? -4.44200  28.64300  34.05500 1.000 86.20544  ? 797 VAL A CG2   1 
ATOM 6592 N N     . MET B 2 798 ? -2.45300  26.57400  37.87100 1.000 76.97824  ? 798 MET A N     1 
ATOM 6593 C CA    . MET B 2 798 ? -2.39000  26.06300  39.26200 1.000 73.99921  ? 798 MET A CA    1 
ATOM 6594 C C     . MET B 2 798 ? -2.42800  27.24300  40.24200 1.000 75.09274  ? 798 MET A C     1 
ATOM 6595 O O     . MET B 2 798 ? -1.50300  28.07500  40.20200 1.000 85.95999  ? 798 MET A O     1 
ATOM 6596 C CB    . MET B 2 798 ? -1.11300  25.24800  39.48600 1.000 84.78894  ? 798 MET A CB    1 
ATOM 6597 C CG    . MET B 2 798 ? -1.06200  23.95500  38.69800 1.000 92.71085  ? 798 MET A CG    1 
ATOM 6598 S SD    . MET B 2 798 ? 0.31000   22.89700  39.19900 1.000 74.68403  ? 798 MET A SD    1 
ATOM 6599 C CE    . MET B 2 798 ? 0.03400   21.46500  38.14800 1.000 80.52183  ? 798 MET A CE    1 
ATOM 6600 N N     . ILE B 2 799 ? -3.45900  27.30400  41.08500 1.000 80.64725  ? 799 ILE A N     1 
ATOM 6601 C CA    . ILE B 2 799 ? -3.54100  28.37700  42.11700 1.000 77.66768  ? 799 ILE A CA    1 
ATOM 6602 C C     . ILE B 2 799 ? -2.82400  27.86600  43.37300 1.000 72.63283  ? 799 ILE A C     1 
ATOM 6603 O O     . ILE B 2 799 ? -3.46500  27.15300  44.16900 1.000 85.99411  ? 799 ILE A O     1 
ATOM 6604 C CB    . ILE B 2 799 ? -5.00600  28.74600  42.40600 1.000 88.69629  ? 799 ILE A CB    1 
ATOM 6605 C CG1   . ILE B 2 799 ? -5.83100  28.82600  41.12200 1.000 76.61937  ? 799 ILE A CG1   1 
ATOM 6606 C CG2   . ILE B 2 799 ? -5.09300  30.03600  43.22200 1.000 79.55172  ? 799 ILE A CG2   1 
ATOM 6607 C CD1   . ILE B 2 799 ? -5.35500  29.88500  40.14600 1.000 89.86914  ? 799 ILE A CD1   1 
ATOM 6608 N N     . ALA B 2 800 ? -1.55400  28.22800  43.54200 1.000 71.01992  ? 800 ALA A N     1 
ATOM 6609 C CA    . ALA B 2 800 ? -0.76400  27.72100  44.68600 1.000 72.89045  ? 800 ALA A CA    1 
ATOM 6610 C C     . ALA B 2 800 ? -1.47800  28.03300  45.99800 1.000 80.73113  ? 800 ALA A C     1 
ATOM 6611 O O     . ALA B 2 800 ? -1.60100  27.12800  46.84600 1.000 94.73949  ? 800 ALA A O     1 
ATOM 6612 C CB    . ALA B 2 800 ? 0.60300   28.35200  44.66100 1.000 78.40807  ? 800 ALA A CB    1 
ATOM 6613 N N     . LYS B 2 801 ? -1.92800  29.27700  46.16100 1.000 85.02477  ? 801 LYS A N     1 
ATOM 6614 C CA    . LYS B 2 801 ? -2.57900  29.68500  47.43100 1.000 83.99956  ? 801 LYS A CA    1 
ATOM 6615 C C     . LYS B 2 801 ? -3.61600  30.77400  47.12600 1.000 83.34963  ? 801 LYS A C     1 
ATOM 6616 O O     . LYS B 2 801 ? -3.40000  31.54300  46.16900 1.000 94.88145  ? 801 LYS A O     1 
ATOM 6617 C CB    . LYS B 2 801 ? -1.48200  30.14100  48.39800 1.000 77.92286  ? 801 LYS A CB    1 
ATOM 6618 C CG    . LYS B 2 801 ? -1.84000  30.09000  49.87300 1.000 112.09041 ? 801 LYS A CG    1 
ATOM 6619 C CD    . LYS B 2 801 ? -2.27300  31.45800  50.37700 1.000 128.20270 ? 801 LYS A CD    1 
ATOM 6620 C CE    . LYS B 2 801 ? -1.23300  32.48000  50.05800 1.000 107.43217 ? 801 LYS A CE    1 
ATOM 6621 N NZ    . LYS B 2 801 ? -1.75900  33.83800  50.21100 1.000 109.37662 ? 801 LYS A NZ    1 
ATOM 6622 N N     . LEU B 2 802 ? -4.69600  30.83000  47.90800 1.000 82.83740  ? 802 LEU A N     1 
ATOM 6623 C CA    . LEU B 2 802 ? -5.77000  31.82500  47.66000 1.000 70.00788  ? 802 LEU A CA    1 
ATOM 6624 C C     . LEU B 2 802 ? -5.14700  33.22600  47.64800 1.000 80.15814  ? 802 LEU A C     1 
ATOM 6625 O O     . LEU B 2 802 ? -4.28400  33.49800  48.50700 1.000 84.79415  ? 802 LEU A O     1 
ATOM 6626 C CB    . LEU B 2 802 ? -6.86500  31.68800  48.71600 1.000 83.81846  ? 802 LEU A CB    1 
ATOM 6627 C CG    . LEU B 2 802 ? -7.71600  30.41600  48.64100 1.000 77.90488  ? 802 LEU A CG    1 
ATOM 6628 C CD1   . LEU B 2 802 ? -8.79200  30.42300  49.71100 1.000 70.85460  ? 802 LEU A CD1   1 
ATOM 6629 C CD2   . LEU B 2 802 ? -8.33400  30.25800  47.26400 1.000 81.31476  ? 802 LEU A CD2   1 
ATOM 6630 N N     . PRO B 2 803 ? -5.54800  34.12600  46.72700 1.000 76.09815  ? 803 PRO A N     1 
ATOM 6631 C CA    . PRO B 2 803 ? -4.90300  35.42800  46.62200 1.000 76.29588  ? 803 PRO A CA    1 
ATOM 6632 C C     . PRO B 2 803 ? -5.35100  36.44600  47.65900 1.000 81.38155  ? 803 PRO A C     1 
ATOM 6633 O O     . PRO B 2 803 ? -6.05900  37.40500  47.30200 1.000 103.13119 ? 803 PRO A O     1 
ATOM 6634 C CB    . PRO B 2 803 ? -5.30200  35.83400  45.19900 1.000 74.69189  ? 803 PRO A CB    1 
ATOM 6635 C CG    . PRO B 2 803 ? -6.66800  35.22300  45.01100 1.000 83.47916  ? 803 PRO A CG    1 
ATOM 6636 C CD    . PRO B 2 803 ? -6.61800  33.91200  45.77000 1.000 71.44730  ? 803 PRO A CD    1 
ATOM 6637 N N     . PHE B 2 804 ? -4.92400  36.26600  48.91000 1.000 73.14449  ? 804 PHE A N     1 
ATOM 6638 C CA    . PHE B 2 804 ? -5.27800  37.22500  49.98900 1.000 70.17488  ? 804 PHE A CA    1 
ATOM 6639 C C     . PHE B 2 804 ? -4.16400  38.25500  50.14800 1.000 74.30240  ? 804 PHE A C     1 
ATOM 6640 O O     . PHE B 2 804 ? -3.06300  38.04600  49.60100 1.000 91.18666  ? 804 PHE A O     1 
ATOM 6641 C CB    . PHE B 2 804 ? -5.50300  36.47600  51.30300 1.000 78.39265  ? 804 PHE A CB    1 
ATOM 6642 C CG    . PHE B 2 804 ? -6.87200  35.83000  51.46100 1.000 81.29344  ? 804 PHE A CG    1 
ATOM 6643 C CD1   . PHE B 2 804 ? -7.93700  36.54600  51.99300 1.000 95.62557  ? 804 PHE A CD1   1 
ATOM 6644 C CD2   . PHE B 2 804 ? -7.08400  34.50800  51.09400 1.000 92.10970  ? 804 PHE A CD2   1 
ATOM 6645 C CE1   . PHE B 2 804 ? -9.18100  35.95700  52.14100 1.000 97.29116  ? 804 PHE A CE1   1 
ATOM 6646 C CE2   . PHE B 2 804 ? -8.33100  33.92400  51.24500 1.000 99.78399  ? 804 PHE A CE2   1 
ATOM 6647 C CZ    . PHE B 2 804 ? -9.37500  34.65000  51.76700 1.000 92.32906  ? 804 PHE A CZ    1 
ATOM 6648 N N     . MET B 2 805 ? -4.44000  39.33800  50.88200 1.000 85.31242  ? 805 MET A N     1 
ATOM 6649 C CA    . MET B 2 805 ? -3.41400  40.38600  51.12700 1.000 70.84107  ? 805 MET A CA    1 
ATOM 6650 C C     . MET B 2 805 ? -3.07900  40.41700  52.62500 1.000 79.30276  ? 805 MET A C     1 
ATOM 6651 O O     . MET B 2 805 ? -3.98700  40.17200  53.44500 1.000 91.56542  ? 805 MET A O     1 
ATOM 6652 C CB    . MET B 2 805 ? -3.90100  41.76800  50.67200 1.000 70.41632  ? 805 MET A CB    1 
ATOM 6653 C CG    . MET B 2 805 ? -5.00500  42.36800  51.51600 1.000 79.11144  ? 805 MET A CG    1 
ATOM 6654 S SD    . MET B 2 805 ? -5.28000  44.10500  51.11500 1.000 82.12591  ? 805 MET A SD    1 
ATOM 6655 C CE    . MET B 2 805 ? -5.76900  43.97400  49.39100 1.000 81.76926  ? 805 MET A CE    1 
ATOM 6656 N N     . ASN B 2 806 ? -1.81600  40.68400  52.95900 1.000 82.25792  ? 806 ASN A N     1 
ATOM 6657 C CA    . ASN B 2 806 ? -1.38900  40.71000  54.38400 1.000 92.86205  ? 806 ASN A CA    1 
ATOM 6658 C C     . ASN B 2 806 ? -1.82800  42.03900  55.00500 1.000 102.88716 ? 806 ASN A C     1 
ATOM 6659 O O     . ASN B 2 806 ? -1.98400  43.02000  54.25200 1.000 112.49482 ? 806 ASN A O     1 
ATOM 6660 C CB    . ASN B 2 806 ? 0.10700   40.45400  54.51800 1.000 80.42815  ? 806 ASN A CB    1 
ATOM 6661 C CG    . ASN B 2 806 ? 0.55800   40.43600  55.95800 1.000 110.95716 ? 806 ASN A CG    1 
ATOM 6662 O OD1   . ASN B 2 806 ? -0.03500  39.73800  56.78700 1.000 116.48318 ? 806 ASN A OD1   1 
ATOM 6663 N ND2   . ASN B 2 806 ? 1.58400   41.21000  56.27800 1.000 124.22036 ? 806 ASN A ND2   1 
ATOM 6664 N N     . LYS B 2 807 ? -2.01200  42.06900  56.32600 1.000 95.58706  ? 807 LYS A N     1 
ATOM 6665 C CA    . LYS B 2 807 ? -2.45700  43.30500  57.01700 1.000 77.30816  ? 807 LYS A CA    1 
ATOM 6666 C C     . LYS B 2 807 ? -1.34100  44.35500  56.94700 1.000 80.12625  ? 807 LYS A C     1 
ATOM 6667 O O     . LYS B 2 807 ? -1.59600  45.51700  57.32000 1.000 87.93166  ? 807 LYS A O     1 
ATOM 6668 C CB    . LYS B 2 807 ? -2.82300  43.00500  58.47300 1.000 68.40984  ? 807 LYS A CB    1 
ATOM 6669 C CG    . LYS B 2 807 ? -4.10400  42.20800  58.65900 1.000 82.45308  ? 807 LYS A CG    1 
ATOM 6670 C CD    . LYS B 2 807 ? -4.53000  42.11100  60.11800 1.000 95.91915  ? 807 LYS A CD    1 
ATOM 6671 C CE    . LYS B 2 807 ? -5.80300  41.34800  60.28800 1.000 126.25142 ? 807 LYS A CE    1 
ATOM 6672 N NZ    . LYS B 2 807 ? -6.21600  41.30000  61.69200 1.000 130.05118 ? 807 LYS A NZ    1 
ATOM 6673 N N     . HIS B 2 808 ? -0.15200  43.95300  56.49700 1.000 83.99907  ? 808 HIS A N     1 
ATOM 6674 C CA    . HIS B 2 808 ? 1.00000   44.88900  56.41700 1.000 90.31915  ? 808 HIS A CA    1 
ATOM 6675 C C     . HIS B 2 808 ? 1.28200   45.20700  54.94700 1.000 83.17259  ? 808 HIS A C     1 
ATOM 6676 O O     . HIS B 2 808 ? 2.46100   45.28800  54.55200 1.000 90.87858  ? 808 HIS A O     1 
ATOM 6677 C CB    . HIS B 2 808 ? 2.20200   44.30700  57.16600 1.000 109.28707 ? 808 HIS A CB    1 
ATOM 6678 C CG    . HIS B 2 808 ? 1.89200   43.97600  58.58600 1.000 107.28125 ? 808 HIS A CG    1 
ATOM 6679 N ND1   . HIS B 2 808 ? 1.49700   42.72100  58.99600 1.000 114.38199 ? 808 HIS A ND1   1 
ATOM 6680 C CD2   . HIS B 2 808 ? 1.92000   44.73300  59.68800 1.000 91.01978  ? 808 HIS A CD2   1 
ATOM 6681 C CE1   . HIS B 2 808 ? 1.29500   42.73300  60.30400 1.000 110.06295 ? 808 HIS A CE1   1 
ATOM 6682 N NE2   . HIS B 2 808 ? 1.54700   43.94500  60.74500 1.000 100.08367 ? 808 HIS A NE2   1 
ATOM 6683 N N     . ASN B 2 809 ? 0.22100   45.36000  54.15500 1.000 86.93839  ? 809 ASN A N     1 
ATOM 6684 C CA    . ASN B 2 809 ? 0.38500   45.74900  52.73000 1.000 77.13047  ? 809 ASN A CA    1 
ATOM 6685 C C     . ASN B 2 809 ? 0.00400   47.22500  52.60900 1.000 92.57170  ? 809 ASN A C     1 
ATOM 6686 O O     . ASN B 2 809 ? -0.96800  47.63400  53.27400 1.000 107.56322 ? 809 ASN A O     1 
ATOM 6687 C CB    . ASN B 2 809 ? -0.46700  44.88500  51.81100 1.000 72.60241  ? 809 ASN A CB    1 
ATOM 6688 C CG    . ASN B 2 809 ? -0.00400  43.44800  51.76900 1.000 123.27115 ? 809 ASN A CG    1 
ATOM 6689 O OD1   . ASN B 2 809 ? -0.63000  42.61400  51.10600 1.000 131.20036 ? 809 ASN A OD1   1 
ATOM 6690 N ND2   . ASN B 2 809 ? 1.07700   43.13400  52.46700 1.000 136.14039 ? 809 ASN A ND2   1 
ATOM 6691 N N     . ALA B 2 810 ? 0.73000   47.99100  51.79500 1.000 80.19441  ? 810 ALA A N     1 
ATOM 6692 C CA    . ALA B 2 810 ? 0.45500   49.44200  51.69300 1.000 65.41582  ? 810 ALA A CA    1 
ATOM 6693 C C     . ALA B 2 810 ? -1.03700  49.65200  51.43200 1.000 74.89897  ? 810 ALA A C     1 
ATOM 6694 O O     . ALA B 2 810 ? -1.62900  50.56500  52.04000 1.000 70.16746  ? 810 ALA A O     1 
ATOM 6695 C CB    . ALA B 2 810 ? 1.30000   50.05800  50.60400 1.000 58.19983  ? 810 ALA A CB    1 
ATOM 6696 N N     . LYS B 2 811 ? -1.63000  48.82100  50.57100 1.000 57.45322  ? 811 LYS A N     1 
ATOM 6697 C CA    . LYS B 2 811 ? -3.06400  48.98200  50.22300 1.000 56.18292  ? 811 LYS A CA    1 
ATOM 6698 C C     . LYS B 2 811 ? -3.91600  48.85500  51.49400 1.000 65.26731  ? 811 LYS A C     1 
ATOM 6699 O O     . LYS B 2 811 ? -4.72900  49.76100  51.75300 1.000 80.75240  ? 811 LYS A O     1 
ATOM 6700 C CB    . LYS B 2 811 ? -3.46800  47.94400  49.17300 1.000 67.45913  ? 811 LYS A CB    1 
ATOM 6701 C CG    . LYS B 2 811 ? -2.79500  48.11300  47.81900 1.000 73.92776  ? 811 LYS A CG    1 
ATOM 6702 C CD    . LYS B 2 811 ? -3.40300  47.23700  46.73100 1.000 89.42374  ? 811 LYS A CD    1 
ATOM 6703 C CE    . LYS B 2 811 ? -3.33700  45.78000  47.05900 1.000 125.80587 ? 811 LYS A CE    1 
ATOM 6704 N NZ    . LYS B 2 811 ? -3.91600  44.96000  45.99200 1.000 120.49977 ? 811 LYS A NZ    1 
ATOM 6705 N N     . TYR B 2 812 ? -3.71500  47.78800  52.26600 1.000 65.57395  ? 812 TYR A N     1 
ATOM 6706 C CA    . TYR B 2 812 ? -4.50700  47.57900  53.50600 1.000 55.86933  ? 812 TYR A CA    1 
ATOM 6707 C C     . TYR B 2 812 ? -4.26000  48.75100  54.43000 1.000 68.75908  ? 812 TYR A C     1 
ATOM 6708 O O     . TYR B 2 812 ? -5.22100  49.26600  55.03500 1.000 67.70583  ? 812 TYR A O     1 
ATOM 6709 C CB    . TYR B 2 812 ? -4.08800  46.28000  54.19500 1.000 56.05671  ? 812 TYR A CB    1 
ATOM 6710 C CG    . TYR B 2 812 ? -4.89600  45.90900  55.43000 1.000 64.72154  ? 812 TYR A CG    1 
ATOM 6711 C CD1   . TYR B 2 812 ? -4.56300  46.40900  56.68200 1.000 68.24588  ? 812 TYR A CD1   1 
ATOM 6712 C CD2   . TYR B 2 812 ? -5.97800  45.04200  55.34700 1.000 56.01364  ? 812 TYR A CD2   1 
ATOM 6713 C CE1   . TYR B 2 812 ? -5.29100  46.07400  57.81100 1.000 75.38993  ? 812 TYR A CE1   1 
ATOM 6714 C CE2   . TYR B 2 812 ? -6.71200  44.69600  56.46900 1.000 56.64260  ? 812 TYR A CE2   1 
ATOM 6715 C CZ    . TYR B 2 812 ? -6.36800  45.21400  57.70400 1.000 60.77422  ? 812 TYR A CZ    1 
ATOM 6716 O OH    . TYR B 2 812 ? -7.08500  44.88000  58.81500 1.000 69.60813  ? 812 TYR A OH    1 
ATOM 6717 N N     . TRP B 2 813 ? -3.00300  49.18000  54.52700 1.000 64.63646  ? 813 TRP A N     1 
ATOM 6718 C CA    . TRP B 2 813 ? -2.63900  50.27200  55.46300 1.000 56.38674  ? 813 TRP A CA    1 
ATOM 6719 C C     . TRP B 2 813 ? -3.39400  51.54700  55.10800 1.000 65.65097  ? 813 TRP A C     1 
ATOM 6720 O O     . TRP B 2 813 ? -3.78100  52.28400  56.03700 1.000 90.33576  ? 813 TRP A O     1 
ATOM 6721 C CB    . TRP B 2 813 ? -1.12200  50.48600  55.42000 1.000 57.15892  ? 813 TRP A CB    1 
ATOM 6722 C CG    . TRP B 2 813 ? -0.61700  51.57000  56.33300 1.000 66.94553  ? 813 TRP A CG    1 
ATOM 6723 C CD1   . TRP B 2 813 ? -0.23600  52.83100  55.98400 1.000 80.00991  ? 813 TRP A CD1   1 
ATOM 6724 C CD2   . TRP B 2 813 ? -0.45500  51.48100  57.76400 1.000 69.35395  ? 813 TRP A CD2   1 
ATOM 6725 N NE1   . TRP B 2 813 ? 0.16600   53.52700  57.09100 1.000 74.09174  ? 813 TRP A NE1   1 
ATOM 6726 C CE2   . TRP B 2 813 ? 0.03800   52.72900  58.19700 1.000 73.11895  ? 813 TRP A CE2   1 
ATOM 6727 C CE3   . TRP B 2 813 ? -0.67500  50.47600  58.71100 1.000 65.65420  ? 813 TRP A CE3   1 
ATOM 6728 C CZ2   . TRP B 2 813 ? 0.31100   52.99400  59.53500 1.000 95.27837  ? 813 TRP A CZ2   1 
ATOM 6729 C CZ3   . TRP B 2 813 ? -0.40500  50.74100  60.03400 1.000 76.79545  ? 813 TRP A CZ3   1 
ATOM 6730 C CH2   . TRP B 2 813 ? 0.08100   51.98200  60.43800 1.000 72.79390  ? 813 TRP A CH2   1 
ATOM 6731 N N     . LEU B 2 814 ? -3.60900  51.79600  53.81600 1.000 66.27729  ? 814 LEU A N     1 
ATOM 6732 C CA    . LEU B 2 814 ? -4.25800  53.06100  53.38700 1.000 72.31436  ? 814 LEU A CA    1 
ATOM 6733 C C     . LEU B 2 814 ? -5.77100  52.86000  53.20900 1.000 64.96689  ? 814 LEU A C     1 
ATOM 6734 O O     . LEU B 2 814 ? -6.43200  53.80200  52.73900 1.000 84.26619  ? 814 LEU A O     1 
ATOM 6735 C CB    . LEU B 2 814 ? -3.60100  53.53100  52.09100 1.000 68.61674  ? 814 LEU A CB    1 
ATOM 6736 C CG    . LEU B 2 814 ? -2.10200  53.83100  52.16500 1.000 66.97866  ? 814 LEU A CG    1 
ATOM 6737 C CD1   . LEU B 2 814 ? -1.58300  54.22600  50.79500 1.000 71.01833  ? 814 LEU A CD1   1 
ATOM 6738 C CD2   . LEU B 2 814 ? -1.82300  54.92600  53.17700 1.000 64.72083  ? 814 LEU A CD2   1 
ATOM 6739 N N     . MET B 2 815 ? -6.29700  51.68500  53.55700 1.000 59.74995  ? 815 MET A N     1 
ATOM 6740 C CA    . MET B 2 815 ? -7.74000  51.40900  53.33000 1.000 68.49669  ? 815 MET A CA    1 
ATOM 6741 C C     . MET B 2 815 ? -8.42600  51.02200  54.64800 1.000 67.12218  ? 815 MET A C     1 
ATOM 6742 O O     . MET B 2 815 ? -9.66100  51.16000  54.72600 1.000 78.35225  ? 815 MET A O     1 
ATOM 6743 C CB    . MET B 2 815 ? -7.91800  50.26100  52.33400 1.000 79.61489  ? 815 MET A CB    1 
ATOM 6744 C CG    . MET B 2 815 ? -7.64800  50.63300  50.89200 1.000 73.64554  ? 815 MET A CG    1 
ATOM 6745 S SD    . MET B 2 815 ? -9.06300  51.46300  50.14600 1.000 75.68935  ? 815 MET A SD    1 
ATOM 6746 C CE    . MET B 2 815 ? -9.08900  50.67700  48.53000 1.000 70.56815  ? 815 MET A CE    1 
ATOM 6747 N N     . ASP B 2 816 ? -7.66200  50.57400  55.64400 1.000 63.10123  ? 816 ASP A N     1 
ATOM 6748 C CA    . ASP B 2 816 ? -8.27400  50.09100  56.91300 1.000 62.15250  ? 816 ASP A CA    1 
ATOM 6749 C C     . ASP B 2 816 ? -9.16400  51.18400  57.50800 1.000 75.16005  ? 816 ASP A C     1 
ATOM 6750 O O     . ASP B 2 816 ? -10.20200 50.83800  58.10700 1.000 98.73581  ? 816 ASP A O     1 
ATOM 6751 C CB    . ASP B 2 816 ? -7.21800  49.62900  57.90400 1.000 59.84568  ? 816 ASP A CB    1 
ATOM 6752 C CG    . ASP B 2 816 ? -7.71400  48.71300  59.01300 1.000 75.10366  ? 816 ASP A CG    1 
ATOM 6753 O OD1   . ASP B 2 816 ? -8.91800  48.38300  59.00900 1.000 100.56280 ? 816 ASP A OD1   1 
ATOM 6754 O OD2   . ASP B 2 816 ? -6.89100  48.33700  59.87300 1.000 90.56325  ? 816 ASP A OD2   1 
ATOM 6755 N N     . SER B 2 817 ? -8.77900  52.45000  57.34900 1.000 59.81686  ? 817 SER A N     1 
ATOM 6756 C CA    . SER B 2 817 ? -9.54500  53.55900  57.97300 1.000 64.98835  ? 817 SER A CA    1 
ATOM 6757 C C     . SER B 2 817 ? -10.72900 53.95500  57.08600 1.000 63.83905  ? 817 SER A C     1 
ATOM 6758 O O     . SER B 2 817 ? -11.44700 54.90600  57.45400 1.000 79.93086  ? 817 SER A O     1 
ATOM 6759 C CB    . SER B 2 817 ? -8.65100  54.73500  58.23000 1.000 88.25066  ? 817 SER A CB    1 
ATOM 6760 O OG    . SER B 2 817 ? -8.01400  55.15100  57.03000 1.000 119.99885 ? 817 SER A OG    1 
ATOM 6761 N N     . GLU B 2 818 ? -10.91800 53.26100  55.96500 1.000 69.76343  ? 818 GLU A N     1 
ATOM 6762 C CA    . GLU B 2 818 ? -11.99800 53.63200  55.01600 1.000 75.19280  ? 818 GLU A CA    1 
ATOM 6763 C C     . GLU B 2 818 ? -13.06200 52.52400  55.00000 1.000 76.81784  ? 818 GLU A C     1 
ATOM 6764 O O     . GLU B 2 818 ? -14.08300 52.69700  54.30400 1.000 71.56381  ? 818 GLU A O     1 
ATOM 6765 C CB    . GLU B 2 818 ? -11.34200 53.86800  53.65700 1.000 68.84930  ? 818 GLU A CB    1 
ATOM 6766 C CG    . GLU B 2 818 ? -12.06500 54.89200  52.79100 1.000 78.17218  ? 818 GLU A CG    1 
ATOM 6767 C CD    . GLU B 2 818 ? -11.15700 55.47900  51.72900 1.000 76.75247  ? 818 GLU A CD    1 
ATOM 6768 O OE1   . GLU B 2 818 ? -9.95400  55.14800  51.72800 1.000 64.34885  ? 818 GLU A OE1   1 
ATOM 6769 O OE2   . GLU B 2 818 ? -11.65500 56.26000  50.89600 1.000 88.07563  ? 818 GLU A OE2   1 
ATOM 6770 N N     . PHE B 2 819 ? -12.83500 51.44100  55.74800 1.000 67.07559  ? 819 PHE A N     1 
ATOM 6771 C CA    . PHE B 2 819 ? -13.79600 50.30700  55.79100 1.000 60.61088  ? 819 PHE A CA    1 
ATOM 6772 C C     . PHE B 2 819 ? -14.01200 49.87800  57.23500 1.000 62.75263  ? 819 PHE A C     1 
ATOM 6773 O O     . PHE B 2 819 ? -13.03000 49.82400  58.00200 1.000 74.88636  ? 819 PHE A O     1 
ATOM 6774 C CB    . PHE B 2 819 ? -13.25700 49.13000  54.97600 1.000 59.70127  ? 819 PHE A CB    1 
ATOM 6775 C CG    . PHE B 2 819 ? -13.14800 49.36500  53.47700 1.000 74.40481  ? 819 PHE A CG    1 
ATOM 6776 C CD1   . PHE B 2 819 ? -14.22100 49.10400  52.63500 1.000 72.55103  ? 819 PHE A CD1   1 
ATOM 6777 C CD2   . PHE B 2 819 ? -11.96700 49.83000  52.91200 1.000 80.34246  ? 819 PHE A CD2   1 
ATOM 6778 C CE1   . PHE B 2 819 ? -14.11800 49.31200  51.27100 1.000 72.77039  ? 819 PHE A CE1   1 
ATOM 6779 C CE2   . PHE B 2 819 ? -11.87000 50.03800  51.54700 1.000 83.94592  ? 819 PHE A CE2   1 
ATOM 6780 C CZ    . PHE B 2 819 ? -12.94400 49.77900  50.73100 1.000 77.26463  ? 819 PHE A CZ    1 
ATOM 6781 N N     . THR B 2 820 ? -15.26200 49.57500  57.60000 1.000 60.08092  ? 820 THR A N     1 
ATOM 6782 C CA    . THR B 2 820 ? -15.56300 49.09500  58.96600 1.000 65.81254  ? 820 THR A CA    1 
ATOM 6783 C C     . THR B 2 820 ? -14.99500 47.70400  59.12400 1.000 71.88689  ? 820 THR A C     1 
ATOM 6784 O O     . THR B 2 820 ? -14.31700 47.45700  60.14100 1.000 105.36693 ? 820 THR A O     1 
ATOM 6785 C CB    . THR B 2 820 ? -17.07100 49.12500  59.20000 1.000 63.79600  ? 820 THR A CB    1 
ATOM 6786 O OG1   . THR B 2 820 ? -17.44000 50.49400  59.07000 1.000 87.36627  ? 820 THR A OG1   1 
ATOM 6787 C CG2   . THR B 2 820 ? -17.45700 48.61900  60.57800 1.000 67.13025  ? 820 THR A CG2   1 
ATOM 6788 N N     . SER B 2 821 ? -15.24700 46.82200  58.15600 1.000 61.78855  ? 821 SER A N     1 
ATOM 6789 C CA    . SER B 2 821 ? -14.64800 45.46400  58.18800 1.000 74.88400  ? 821 SER A CA    1 
ATOM 6790 C C     . SER B 2 821 ? -13.77600 45.29200  56.94300 1.000 72.25766  ? 821 SER A C     1 
ATOM 6791 O O     . SER B 2 821 ? -14.27500 44.73600  55.94700 1.000 78.97331  ? 821 SER A O     1 
ATOM 6792 C CB    . SER B 2 821 ? -15.69600 44.39600  58.26000 1.000 78.62654  ? 821 SER A CB    1 
ATOM 6793 O OG    . SER B 2 821 ? -15.09400 43.11000  58.26700 1.000 75.24500  ? 821 SER A OG    1 
ATOM 6794 N N     . THR B 2 822 ? -12.51900 45.73100  57.01000 1.000 71.46513  ? 822 THR A N     1 
ATOM 6795 C CA    . THR B 2 822 ? -11.65500 45.69000  55.81400 1.000 80.86792  ? 822 THR A CA    1 
ATOM 6796 C C     . THR B 2 822 ? -11.68000 44.29500  55.22900 1.000 79.58289  ? 822 THR A C     1 
ATOM 6797 O O     . THR B 2 822 ? -11.74400 44.18100  53.99200 1.000 80.09970  ? 822 THR A O     1 
ATOM 6798 C CB    . THR B 2 822 ? -10.24600 46.13900  56.19400 1.000 74.32965  ? 822 THR A CB    1 
ATOM 6799 O OG1   . THR B 2 822 ? -10.42800 47.26300  57.04900 1.000 67.17187  ? 822 THR A OG1   1 
ATOM 6800 C CG2   . THR B 2 822 ? -9.42100  46.53800  54.98500 1.000 78.64374  ? 822 THR A CG2   1 
ATOM 6801 N N     . PHE B 2 823 ? -11.65200 43.26200  56.07200 1.000 79.15743  ? 823 PHE A N     1 
ATOM 6802 C CA    . PHE B 2 823 ? -11.58500 41.87200  55.54900 1.000 74.37817  ? 823 PHE A CA    1 
ATOM 6803 C C     . PHE B 2 823 ? -12.83400 41.56900  54.73800 1.000 70.14871  ? 823 PHE A C     1 
ATOM 6804 O O     . PHE B 2 823 ? -12.70000 41.11500  53.58700 1.000 71.78658  ? 823 PHE A O     1 
ATOM 6805 C CB    . PHE B 2 823 ? -11.46400 40.84300  56.67600 1.000 69.94730  ? 823 PHE A CB    1 
ATOM 6806 C CG    . PHE B 2 823 ? -11.30000 39.40800  56.19300 1.000 79.54377  ? 823 PHE A CG    1 
ATOM 6807 C CD1   . PHE B 2 823 ? -12.40700 38.60500  55.94700 1.000 91.18013  ? 823 PHE A CD1   1 
ATOM 6808 C CD2   . PHE B 2 823 ? -10.03700 38.86600  55.98800 1.000 77.87336  ? 823 PHE A CD2   1 
ATOM 6809 C CE1   . PHE B 2 823 ? -12.25200 37.30100  55.50400 1.000 82.31173  ? 823 PHE A CE1   1 
ATOM 6810 C CE2   . PHE B 2 823 ? -9.88900  37.56200  55.54700 1.000 98.73114  ? 823 PHE A CE2   1 
ATOM 6811 C CZ    . PHE B 2 823 ? -10.99500 36.78300  55.30700 1.000 106.93422 ? 823 PHE A CZ    1 
ATOM 6812 N N     . LYS B 2 824 ? -14.01300 41.82800  55.30300 1.000 77.17726  ? 824 LYS A N     1 
ATOM 6813 C CA    . LYS B 2 824 ? -15.27700 41.45200  54.61800 1.000 76.98542  ? 824 LYS A CA    1 
ATOM 6814 C C     . LYS B 2 824 ? -15.65400 42.48000  53.54400 1.000 79.88595  ? 824 LYS A C     1 
ATOM 6815 O O     . LYS B 2 824 ? -16.45500 42.12500  52.65600 1.000 80.15469  ? 824 LYS A O     1 
ATOM 6816 C CB    . LYS B 2 824 ? -16.39600 41.33200  55.65600 1.000 68.91273  ? 824 LYS A CB    1 
ATOM 6817 C CG    . LYS B 2 824 ? -16.16700 40.26200  56.71200 1.000 97.19314  ? 824 LYS A CG    1 
ATOM 6818 C CD    . LYS B 2 824 ? -17.25900 40.22300  57.77300 1.000 80.81581  ? 824 LYS A CD    1 
ATOM 6819 C CE    . LYS B 2 824 ? -17.05700 39.10900  58.74900 1.000 135.25990 ? 824 LYS A CE    1 
ATOM 6820 N NZ    . LYS B 2 824 ? -17.08100 37.80400  58.08400 1.000 121.72500 ? 824 LYS A NZ    1 
ATOM 6821 N N     . GLU B 2 825 ? -15.11300 43.69600  53.61800 1.000 71.85197  ? 825 GLU A N     1 
ATOM 6822 C CA    . GLU B 2 825 ? -15.53500 44.75100  52.66100 1.000 63.56381  ? 825 GLU A CA    1 
ATOM 6823 C C     . GLU B 2 825 ? -14.44700 44.99600  51.60400 1.000 66.86774  ? 825 GLU A C     1 
ATOM 6824 O O     . GLU B 2 825 ? -14.76700 45.64300  50.58700 1.000 82.92229  ? 825 GLU A O     1 
ATOM 6825 C CB    . GLU B 2 825 ? -15.86100 46.03200  53.42800 1.000 70.83535  ? 825 GLU A CB    1 
ATOM 6826 C CG    . GLU B 2 825 ? -16.93800 45.84100  54.49100 1.000 74.92130  ? 825 GLU A CG    1 
ATOM 6827 C CD    . GLU B 2 825 ? -17.23000 47.08300  55.31200 1.000 77.16670  ? 825 GLU A CD    1 
ATOM 6828 O OE1   . GLU B 2 825 ? -16.60000 48.12800  55.04900 1.000 95.36835  ? 825 GLU A OE1   1 
ATOM 6829 O OE2   . GLU B 2 825 ? -18.08400 47.00500  56.21700 1.000 82.30911  ? 825 GLU A OE2   1 
ATOM 6830 N N     . TYR B 2 826 ? -13.22600 44.49600  51.81800 1.000 67.79221  ? 826 TYR A N     1 
ATOM 6831 C CA    . TYR B 2 826 ? -12.12700 44.81400  50.86400 1.000 74.27897  ? 826 TYR A CA    1 
ATOM 6832 C C     . TYR B 2 826 ? -11.28200 43.58300  50.54200 1.000 74.12863  ? 826 TYR A C     1 
ATOM 6833 O O     . TYR B 2 826 ? -11.35700 43.09200  49.39800 1.000 75.47995  ? 826 TYR A O     1 
ATOM 6834 C CB    . TYR B 2 826 ? -11.23200 45.90900  51.45100 1.000 69.28606  ? 826 TYR A CB    1 
ATOM 6835 C CG    . TYR B 2 826 ? -10.07800 46.34900  50.56100 1.000 78.89841  ? 826 TYR A CG    1 
ATOM 6836 C CD1   . TYR B 2 826 ? -10.21400 46.40400  49.18000 1.000 74.09853  ? 826 TYR A CD1   1 
ATOM 6837 C CD2   . TYR B 2 826 ? -8.84700  46.69300  51.10500 1.000 63.06488  ? 826 TYR A CD2   1 
ATOM 6838 C CE1   . TYR B 2 826 ? -9.16500  46.79800  48.36800 1.000 77.33079  ? 826 TYR A CE1   1 
ATOM 6839 C CE2   . TYR B 2 826 ? -7.78900  47.08600  50.30400 1.000 74.76195  ? 826 TYR A CE2   1 
ATOM 6840 C CZ    . TYR B 2 826 ? -7.94900  47.14000  48.93100 1.000 92.44563  ? 826 TYR A CZ    1 
ATOM 6841 O OH    . TYR B 2 826 ? -6.91200  47.52800  48.13300 1.000 106.92832 ? 826 TYR A OH    1 
ATOM 6842 N N     . VAL B 2 827 ? -10.49800 43.09300  51.50400 1.000 69.43899  ? 827 VAL A N     1 
ATOM 6843 C CA    . VAL B 2 827 ? -9.54600  41.97900  51.20000 1.000 64.99849  ? 827 VAL A CA    1 
ATOM 6844 C C     . VAL B 2 827 ? -10.30600 40.76000  50.65200 1.000 74.29015  ? 827 VAL A C     1 
ATOM 6845 O O     . VAL B 2 827 ? -9.85600  40.21400  49.62400 1.000 88.64203  ? 827 VAL A O     1 
ATOM 6846 C CB    . VAL B 2 827 ? -8.65600  41.62000  52.40800 1.000 61.20100  ? 827 VAL A CB    1 
ATOM 6847 C CG1   . VAL B 2 827 ? -7.89790  42.82544  52.94642 1.000 73.06604  ? 827 VAL A CG1   1 
ATOM 6848 C CG2   . VAL B 2 827 ? -9.40787  40.89245  53.51597 1.000 81.13141  ? 827 VAL A CG2   1 
ATOM 6849 N N     . LEU B 2 828 ? -11.40500 40.35000  51.28900 1.000 64.27418  ? 828 LEU A N     1 
ATOM 6850 C CA    . LEU B 2 828 ? -12.09700 39.11500  50.83100 1.000 71.72031  ? 828 LEU A CA    1 
ATOM 6851 C C     . LEU B 2 828 ? -12.66400 39.35000  49.42200 1.000 71.06271  ? 828 LEU A C     1 
ATOM 6852 O O     . LEU B 2 828 ? -12.37500 38.52300  48.53400 1.000 76.97245  ? 828 LEU A O     1 
ATOM 6853 C CB    . LEU B 2 828 ? -13.16900 38.67000  51.82400 1.000 79.12019  ? 828 LEU A CB    1 
ATOM 6854 C CG    . LEU B 2 828 ? -13.79600 37.29500  51.57900 1.000 72.28188  ? 828 LEU A CG    1 
ATOM 6855 C CD1   . LEU B 2 828 ? -12.72700 36.23100  51.42800 1.000 83.82775  ? 828 LEU A CD1   1 
ATOM 6856 C CD2   . LEU B 2 828 ? -14.71900 36.95700  52.73300 1.000 70.76525  ? 828 LEU A CD2   1 
ATOM 6857 N N     . PRO B 2 829 ? -13.43100 40.42900  49.15400 1.000 73.62348  ? 829 PRO A N     1 
ATOM 6858 C CA    . PRO B 2 829 ? -13.88900 40.68800  47.79800 1.000 76.99880  ? 829 PRO A CA    1 
ATOM 6859 C C     . PRO B 2 829 ? -12.72700 40.72700  46.81900 1.000 72.59490  ? 829 PRO A C     1 
ATOM 6860 O O     . PRO B 2 829 ? -12.84100 40.16800  45.71300 1.000 77.15838  ? 829 PRO A O     1 
ATOM 6861 C CB    . PRO B 2 829 ? -14.56900 42.04700  47.94700 1.000 71.76443  ? 829 PRO A CB    1 
ATOM 6862 C CG    . PRO B 2 829 ? -15.08900 42.03300  49.36100 1.000 65.07659  ? 829 PRO A CG    1 
ATOM 6863 C CD    . PRO B 2 829 ? -13.96200 41.37200  50.12800 1.000 61.38311  ? 829 PRO A CD    1 
ATOM 6864 N N     . ASP B 2 830 ? -11.62400 41.36100  47.21900 1.000 62.86487  ? 830 ASP A N     1 
ATOM 6865 C CA    . ASP B 2 830 ? -10.43600 41.47300  46.33000 1.000 70.10800  ? 830 ASP A CA    1 
ATOM 6866 C C     . ASP B 2 830 ? -9.93400  40.07300  45.97600 1.000 79.06166  ? 830 ASP A C     1 
ATOM 6867 O O     . ASP B 2 830 ? -9.68300  39.81500  44.78400 1.000 86.96349  ? 830 ASP A O     1 
ATOM 6868 C CB    . ASP B 2 830 ? -9.33700  42.29700  46.97700 1.000 81.96073  ? 830 ASP A CB    1 
ATOM 6869 C CG    . ASP B 2 830 ? -7.98000  42.23000  46.29300 1.000 92.12510  ? 830 ASP A CG    1 
ATOM 6870 O OD1   . ASP B 2 830 ? -7.89800  42.62100  45.11100 1.000 100.45162 ? 830 ASP A OD1   1 
ATOM 6871 O OD2   . ASP B 2 830 ? -7.01800  41.78200  46.95000 1.000 102.13520 ? 830 ASP A OD2   1 
ATOM 6872 N N     . ALA B 2 831 ? -9.80500  39.20100  46.97700 1.000 77.80576  ? 831 ALA A N     1 
ATOM 6873 C CA    . ALA B 2 831 ? -9.28400  37.83800  46.73400 1.000 68.24443  ? 831 ALA A CA    1 
ATOM 6874 C C     . ALA B 2 831 ? -10.17900 37.13000  45.72000 1.000 78.20702  ? 831 ALA A C     1 
ATOM 6875 O O     . ALA B 2 831 ? -9.65500  36.51700  44.77300 1.000 80.67017  ? 831 ALA A O     1 
ATOM 6876 C CB    . ALA B 2 831 ? -9.22700  37.08000  48.03500 1.000 73.20830  ? 831 ALA A CB    1 
ATOM 6877 N N     . VAL B 2 832 ? -11.49400 37.22700  45.91000 1.000 78.10032  ? 832 VAL A N     1 
ATOM 6878 C CA    . VAL B 2 832 ? -12.44700 36.53400  44.99600 1.000 80.59984  ? 832 VAL A CA    1 
ATOM 6879 C C     . VAL B 2 832 ? -12.21500 37.05200  43.56800 1.000 73.45053  ? 832 VAL A C     1 
ATOM 6880 O O     . VAL B 2 832 ? -12.09900 36.21500  42.65200 1.000 97.23697  ? 832 VAL A O     1 
ATOM 6881 C CB    . VAL B 2 832 ? -13.89700 36.75300  45.46200 1.000 66.83367  ? 832 VAL A CB    1 
ATOM 6882 C CG1   . VAL B 2 832 ? -14.91000 36.28000  44.42800 1.000 69.75116  ? 832 VAL A CG1   1 
ATOM 6883 C CG2   . VAL B 2 832 ? -14.15500 36.10000  46.81400 1.000 75.30561  ? 832 VAL A CG2   1 
ATOM 6884 N N     . THR B 2 833 ? -12.11800 38.37100  43.39500 1.000 71.69816  ? 833 THR A N     1 
ATOM 6885 C CA    . THR B 2 833 ? -11.94500 38.94300  42.04300 1.000 74.93178  ? 833 THR A CA    1 
ATOM 6886 C C     . THR B 2 833 ? -10.62600 38.47400  41.47200 1.000 79.56416  ? 833 THR A C     1 
ATOM 6887 O O     . THR B 2 833 ? -10.59200 38.12500  40.27700 1.000 95.91039  ? 833 THR A O     1 
ATOM 6888 C CB    . THR B 2 833 ? -12.03200 40.46700  42.09400 1.000 82.29440  ? 833 THR A CB    1 
ATOM 6889 O OG1   . THR B 2 833 ? -10.98600 40.87300  42.97000 1.000 99.55629  ? 833 THR A OG1   1 
ATOM 6890 C CG2   . THR B 2 833 ? -13.37300 40.95400  42.61200 1.000 86.29908  ? 833 THR A CG2   1 
ATOM 6891 N N     . ARG B 2 834 ? -9.57100  38.46500  42.28900 1.000 80.70700  ? 834 ARG A N     1 
ATOM 6892 C CA    . ARG B 2 834 ? -8.22800  38.05000  41.80700 1.000 75.29090  ? 834 ARG A CA    1 
ATOM 6893 C C     . ARG B 2 834 ? -8.25900  36.56100  41.43800 1.000 78.38492  ? 834 ARG A C     1 
ATOM 6894 O O     . ARG B 2 834 ? -7.70100  36.19800  40.38400 1.000 80.63136  ? 834 ARG A O     1 
ATOM 6895 C CB    . ARG B 2 834 ? -7.16100  38.32500  42.87100 1.000 73.04764  ? 834 ARG A CB    1 
ATOM 6896 C CG    . ARG B 2 834 ? -6.88200  39.80200  43.10700 1.000 87.67448  ? 834 ARG A CG    1 
ATOM 6897 C CD    . ARG B 2 834 ? -5.41700  40.12900  42.86200 1.000 100.81775 ? 834 ARG A CD    1 
ATOM 6898 N NE    . ARG B 2 834 ? -4.51800  39.50100  43.83700 1.000 127.88156 ? 834 ARG A NE    1 
ATOM 6899 C CZ    . ARG B 2 834 ? -4.48700  39.78000  45.13400 1.000 126.24457 ? 834 ARG A CZ    1 
ATOM 6900 N NH1   . ARG B 2 834 ? -4.97300  40.92400  45.57800 1.000 116.98653 ? 834 ARG A NH1   1 
ATOM 6901 N NH2   . ARG B 2 834 ? -3.95000  38.92300  45.98300 1.000 125.60957 ? 834 ARG A NH2   1 
ATOM 6902 N N     . PHE B 2 835 ? -8.89100  35.73800  42.27400 1.000 77.37745  ? 835 PHE A N     1 
ATOM 6903 C CA    . PHE B 2 835 ? -8.94300  34.27300  42.02400 1.000 84.16640  ? 835 PHE A CA    1 
ATOM 6904 C C     . PHE B 2 835 ? -9.70100  34.01900  40.73800 1.000 82.89652  ? 835 PHE A C     1 
ATOM 6905 O O     . PHE B 2 835 ? -9.20900  33.26000  39.88100 1.000 106.20023 ? 835 PHE A O     1 
ATOM 6906 C CB    . PHE B 2 835 ? -9.61500  33.62000  43.23400 1.000 78.91556  ? 835 PHE A CB    1 
ATOM 6907 C CG    . PHE B 2 835 ? -9.84600  32.11700  43.16000 1.000 73.61719  ? 835 PHE A CG    1 
ATOM 6908 C CD1   . PHE B 2 835 ? -8.83500  31.22400  43.49300 1.000 80.04247  ? 835 PHE A CD1   1 
ATOM 6909 C CD2   . PHE B 2 835 ? -11.08500 31.60200  42.80100 1.000 80.59651  ? 835 PHE A CD2   1 
ATOM 6910 C CE1   . PHE B 2 835 ? -9.05000  29.85700  43.43700 1.000 89.15113  ? 835 PHE A CE1   1 
ATOM 6911 C CE2   . PHE B 2 835 ? -11.29500 30.23300  42.75100 1.000 100.20873 ? 835 PHE A CE2   1 
ATOM 6912 C CZ    . PHE B 2 835 ? -10.27900 29.36500  43.06700 1.000 75.30377  ? 835 PHE A CZ    1 
ATOM 6913 N N     . ARG B 2 836 ? -10.86100 34.65800  40.58700 1.000 85.45483  ? 836 ARG A N     1 
ATOM 6914 C CA    . ARG B 2 836 ? -11.71000 34.40000  39.39500 1.000 98.90879  ? 836 ARG A CA    1 
ATOM 6915 C C     . ARG B 2 836 ? -10.99900 34.94100  38.14400 1.000 84.57384  ? 836 ARG A C     1 
ATOM 6916 O O     . ARG B 2 836 ? -11.26100 34.42200  37.03800 1.000 84.32917  ? 836 ARG A O     1 
ATOM 6917 C CB    . ARG B 2 836 ? -13.11400 34.97700  39.61800 1.000 89.45810  ? 836 ARG A CB    1 
ATOM 6918 C CG    . ARG B 2 836 ? -13.28000 36.48700  39.55700 1.000 100.72696 ? 836 ARG A CG    1 
ATOM 6919 C CD    . ARG B 2 836 ? -14.56400 36.89900  40.25800 1.000 123.33139 ? 836 ARG A CD    1 
ATOM 6920 N NE    . ARG B 2 836 ? -15.71500 36.07700  39.86800 1.000 111.07052 ? 836 ARG A NE    1 
ATOM 6921 C CZ    . ARG B 2 836 ? -16.23000 36.00500  38.64800 1.000 111.67437 ? 836 ARG A CZ    1 
ATOM 6922 N NH1   . ARG B 2 836 ? -16.11700 37.02600  37.81700 1.000 120.29183 ? 836 ARG A NH1   1 
ATOM 6923 N NH2   . ARG B 2 836 ? -16.87100 34.91500  38.26700 1.000 127.27313 ? 836 ARG A NH2   1 
ATOM 6924 N N     . GLN B 2 837 ? -10.12500 35.93200  38.32100 1.000 83.67761  ? 837 GLN A N     1 
ATOM 6925 C CA    . GLN B 2 837 ? -9.39000  36.51100  37.16900 1.000 99.41394  ? 837 GLN A CA    1 
ATOM 6926 C C     . GLN B 2 837 ? -8.46500  35.43500  36.58400 1.000 96.43571  ? 837 GLN A C     1 
ATOM 6927 O O     . GLN B 2 837 ? -8.47200  35.25100  35.34800 1.000 112.42991 ? 837 GLN A O     1 
ATOM 6928 C CB    . GLN B 2 837 ? -8.60200  37.74200  37.60900 1.000 83.42558  ? 837 GLN A CB    1 
ATOM 6929 C CG    . GLN B 2 837 ? -8.44300  38.79000  36.51500 1.000 97.17115  ? 837 GLN A CG    1 
ATOM 6930 C CD    . GLN B 2 837 ? -9.70700  39.57900  36.25900 1.000 109.85904 ? 837 GLN A CD    1 
ATOM 6931 O OE1   . GLN B 2 837 ? -10.22400 40.26800  37.14500 1.000 119.49283 ? 837 GLN A OE1   1 
ATOM 6932 N NE2   . GLN B 2 837 ? -10.21400 39.49100  35.03800 1.000 97.50513  ? 837 GLN A NE2   1 
ATOM 6933 N N     . GLY B 2 838 ? -7.71600  34.74100  37.44400 1.000 94.33011  ? 838 GLY A N     1 
ATOM 6934 C CA    . GLY B 2 838 ? -6.81200  33.67300  36.97900 1.000 104.62978 ? 838 GLY A CA    1 
ATOM 6935 C C     . GLY B 2 838 ? -7.59800  32.53800  36.35700 1.000 100.74272 ? 838 GLY A C     1 
ATOM 6936 O O     . GLY B 2 838 ? -7.12700  31.96900  35.35500 1.000 112.03244 ? 838 GLY A O     1 
ATOM 6937 N N     . LEU B 2 839 ? -8.75900  32.22000  36.92900 1.000 97.44210  ? 839 LEU A N     1 
ATOM 6938 C CA    . LEU B 2 839 ? -9.62100  31.15400  36.36300 1.000 101.51424 ? 839 LEU A CA    1 
ATOM 6939 C C     . LEU B 2 839 ? -9.96500  31.53400  34.91900 1.000 113.52050 ? 839 LEU A C     1 
ATOM 6940 O O     . LEU B 2 839 ? -9.95400  30.63900  34.05100 1.000 130.93390 ? 839 LEU A O     1 
ATOM 6941 C CB    . LEU B 2 839 ? -10.88500 31.02000  37.20700 1.000 95.41102  ? 839 LEU A CB    1 
ATOM 6942 C CG    . LEU B 2 839 ? -10.81700 30.08800  38.42000 1.000 106.44135 ? 839 LEU A CG    1 
ATOM 6943 C CD1   . LEU B 2 839 ? -9.47400  30.12100  39.12800 1.000 118.53217 ? 839 LEU A CD1   1 
ATOM 6944 C CD2   . LEU B 2 839 ? -11.92400 30.49800  39.37100 1.000 93.25043  ? 839 LEU A CD2   1 
ATOM 6945 N N     . GLY B 2 840 ? -10.25100 32.81600  34.67900 1.000 98.37548  ? 840 GLY A N     1 
ATOM 6946 C CA    . GLY B 2 840 ? -10.60300 33.27900  33.32400 1.000 116.21106 ? 840 GLY A CA    1 
ATOM 6947 C C     . GLY B 2 840 ? -9.39200  33.27500  32.41600 1.000 113.51637 ? 840 GLY A C     1 
ATOM 6948 O O     . GLY B 2 840 ? -9.56900  33.44700  31.19200 1.000 124.66140 ? 840 GLY A O     1 
ATOM 6949 N N     . ARG B 2 841 ? -8.20100  33.08800  32.98900 1.000 109.92447 ? 841 ARG A N     1 
ATOM 6950 C CA    . ARG B 2 841 ? -6.95000  33.08100  32.18600 1.000 138.02417 ? 841 ARG A CA    1 
ATOM 6951 C C     . ARG B 2 841 ? -6.68800  31.66600  31.64400 1.000 126.74224 ? 841 ARG A C     1 
ATOM 6952 O O     . ARG B 2 841 ? -5.60800  31.45200  31.05700 1.000 127.06687 ? 841 ARG A O     1 
ATOM 6953 C CB    . ARG B 2 841 ? -5.76300  33.57500  33.02100 1.000 124.28624 ? 841 ARG A CB    1 
ATOM 6954 C CG    . ARG B 2 841 ? -5.87000  35.04300  33.40900 1.000 119.82242 ? 841 ARG A CG    1 
ATOM 6955 C CD    . ARG B 2 841 ? -6.18000  35.89700  32.19200 1.000 131.69896 ? 841 ARG A CD    1 
ATOM 6956 N NE    . ARG B 2 841 ? -6.21900  37.33400  32.48200 1.000 150.50184 ? 841 ARG A NE    1 
ATOM 6957 C CZ    . ARG B 2 841 ? -6.44500  38.27700  31.57700 1.000 152.74625 ? 841 ARG A CZ    1 
ATOM 6958 N NH1   . ARG B 2 841 ? -6.17600  38.05200  30.30300 1.000 160.04649 ? 841 ARG A NH1   1 
ATOM 6959 N NH2   . ARG B 2 841 ? -6.94700  39.44200  31.94400 1.000 145.66389 ? 841 ARG A NH2   1 
ATOM 6960 N N     . LEU B 2 842 ? -7.63500  30.74300  31.83700 1.000 124.16336 ? 842 LEU A N     1 
ATOM 6961 C CA    . LEU B 2 842 ? -7.47400  29.35800  31.32500 1.000 109.19083 ? 842 LEU A CA    1 
ATOM 6962 C C     . LEU B 2 842 ? -8.18900  29.22800  29.97500 1.000 116.33996 ? 842 LEU A C     1 
ATOM 6963 O O     . LEU B 2 842 ? -7.54800  28.76300  29.00900 1.000 128.98776 ? 842 LEU A O     1 
ATOM 6964 C CB    . LEU B 2 842 ? -8.02100  28.33600  32.31900 1.000 104.18110 ? 842 LEU A CB    1 
ATOM 6965 C CG    . LEU B 2 842 ? -7.93800  26.87400  31.87200 1.000 111.06566 ? 842 LEU A CG    1 
ATOM 6966 C CD1   . LEU B 2 842 ? -6.53100  26.33500  32.03600 1.000 128.42637 ? 842 LEU A CD1   1 
ATOM 6967 C CD2   . LEU B 2 842 ? -8.94600  25.99100  32.58300 1.000 115.53068 ? 842 LEU A CD2   1 
ATOM 6968 N N     . ILE B 2 843 ? -9.45800  29.63000  29.90900 1.000 117.08926 ? 843 ILE A N     1 
ATOM 6969 C CA    . ILE B 2 843 ? -10.23600 29.42400  28.65000 1.000 132.46942 ? 843 ILE A CA    1 
ATOM 6970 C C     . ILE B 2 843 ? -10.46400 30.77000  27.94500 1.000 143.04433 ? 843 ILE A C     1 
ATOM 6971 O O     . ILE B 2 843 ? -10.97100 31.70800  28.59700 1.000 136.40124 ? 843 ILE A O     1 
ATOM 6972 C CB    . ILE B 2 843 ? -11.56000 28.69300  28.94500 1.000 140.23796 ? 843 ILE A CB    1 
ATOM 6973 C CG1   . ILE B 2 843 ? -12.34100 28.40100  27.66400 1.000 128.81713 ? 843 ILE A CG1   1 
ATOM 6974 C CG2   . ILE B 2 843 ? -12.40400 29.45500  29.96900 1.000 137.98382 ? 843 ILE A CG2   1 
ATOM 6975 C CD1   . ILE B 2 843 ? -11.72900 27.31000  26.80600 1.000 139.79196 ? 843 ILE A CD1   1 
ATOM 6976 N N     . ARG B 2 844 ? -10.07500 30.86400  26.67200 1.000 153.95453 ? 844 ARG A N     1 
ATOM 6977 C CA    . ARG B 2 844 ? -10.33500 32.09300  25.87600 1.000 156.35121 ? 844 ARG A CA    1 
ATOM 6978 C C     . ARG B 2 844 ? -10.99300 31.65200  24.56400 1.000 160.68624 ? 844 ARG A C     1 
ATOM 6979 O O     . ARG B 2 844 ? -11.83300 32.41100  24.03500 1.000 167.10116 ? 844 ARG A O     1 
ATOM 6980 C CB    . ARG B 2 844 ? -9.03900  32.87300  25.63200 1.000 146.14436 ? 844 ARG A CB    1 
ATOM 6981 C CG    . ARG B 2 844 ? -7.88300  32.02300  25.12800 1.000 155.85714 ? 844 ARG A CG    1 
ATOM 6982 C CD    . ARG B 2 844 ? -6.75400  32.89700  24.61800 1.000 160.93707 ? 844 ARG A CD    1 
ATOM 6983 N NE    . ARG B 2 844 ? -7.21600  33.76900  23.53200 1.000 174.27819 ? 844 ARG A NE    1 
ATOM 6984 C CZ    . ARG B 2 844 ? -6.71800  33.76400  22.30400 1.000 168.54121 ? 844 ARG A CZ    1 
ATOM 6985 N NH1   . ARG B 2 844 ? -5.53700  33.22000  22.07400 1.000 158.26379 ? 844 ARG A NH1   1 
ATOM 6986 N NH2   . ARG B 2 844 ? -7.39800  34.30900  21.31200 1.000 164.52862 ? 844 ARG A NH2   1 
ATOM 6987 N N     . ASN B 2 845 ? -10.62300 30.46800  24.06600 1.000 162.00461 ? 845 ASN A N     1 
ATOM 6988 C CA    . ASN B 2 845 ? -11.25100 29.91300  22.83700 1.000 153.77199 ? 845 ASN A CA    1 
ATOM 6989 C C     . ASN B 2 845 ? -11.88500 28.57000  23.20900 1.000 152.80395 ? 845 ASN A C     1 
ATOM 6990 O O     . ASN B 2 845 ? -11.13900 27.67300  23.64800 1.000 154.92795 ? 845 ASN A O     1 
ATOM 6991 C CB    . ASN B 2 845 ? -10.23800 29.77100  21.70800 1.000 154.89674 ? 845 ASN A CB    1 
ATOM 6992 C CG    . ASN B 2 845 ? -9.25200  30.91400  21.68600 1.000 167.81787 ? 845 ASN A CG    1 
ATOM 6993 O OD1   . ASN B 2 845 ? -9.64900  32.07600  21.54900 1.000 161.57113 ? 845 ASN A OD1   1 
ATOM 6994 N ND2   . ASN B 2 845 ? -7.97000  30.60900  21.82500 1.000 164.09147 ? 845 ASN A ND2   1 
ATOM 6995 N N     . GLU B 2 846 ? -13.20000 28.42600  23.02900 1.000 156.40094 ? 846 GLU A N     1 
ATOM 6996 C CA    . GLU B 2 846 ? -13.89300 27.18200  23.45900 1.000 153.07238 ? 846 GLU A CA    1 
ATOM 6997 C C     . GLU B 2 846 ? -13.48100 26.01100  22.55100 1.000 160.75107 ? 846 GLU A C     1 
ATOM 6998 O O     . GLU B 2 846 ? -13.96900 24.88500  22.78500 1.000 164.07479 ? 846 GLU A O     1 
ATOM 6999 C CB    . GLU B 2 846 ? -15.40600 27.40400  23.47100 1.000 161.03739 ? 846 GLU A CB    1 
ATOM 7000 C CG    . GLU B 2 846 ? -15.93500 28.05000  22.19500 1.000 173.71648 ? 846 GLU A CG    1 
ATOM 7001 C CD    . GLU B 2 846 ? -17.37400 28.51800  22.31100 1.000 175.80010 ? 846 GLU A CD    1 
ATOM 7002 O OE1   . GLU B 2 846 ? -17.96400 28.34700  23.39900 1.000 174.15375 ? 846 GLU A OE1   1 
ATOM 7003 O OE2   . GLU B 2 846 ? -17.90700 29.04900  21.31500 1.000 170.13085 ? 846 GLU A OE2   1 
ATOM 7004 N N     . ASN B 2 847 ? -12.62700 26.26700  21.55700 1.000 157.67107 ? 847 ASN A N     1 
ATOM 7005 C CA    . ASN B 2 847 ? -12.12700 25.17700  20.67600 1.000 166.26132 ? 847 ASN A CA    1 
ATOM 7006 C C     . ASN B 2 847 ? -11.33000 24.17800  21.51900 1.000 168.34822 ? 847 ASN A C     1 
ATOM 7007 O O     . ASN B 2 847 ? -11.57700 22.96000  21.38300 1.000 160.08743 ? 847 ASN A O     1 
ATOM 7008 C CB    . ASN B 2 847 ? -11.28100 25.73100  19.53600 1.000 169.04710 ? 847 ASN A CB    1 
ATOM 7009 C CG    . ASN B 2 847 ? -11.04200 24.71800  18.44100 1.000 172.92756 ? 847 ASN A CG    1 
ATOM 7010 O OD1   . ASN B 2 847 ? -11.55400 23.59500  18.50400 1.000 165.36305 ? 847 ASN A OD1   1 
ATOM 7011 N ND2   . ASN B 2 847 ? -10.28100 25.09800  17.42500 1.000 169.42338 ? 847 ASN A ND2   1 
ATOM 7012 N N     . ASP B 2 848 ? -10.42100 24.67200  22.36400 1.000 153.02266 ? 848 ASP A N     1 
ATOM 7013 C CA    . ASP B 2 848 ? -9.55200  23.76300  23.16400 1.000 142.12394 ? 848 ASP A CA    1 
ATOM 7014 C C     . ASP B 2 848 ? -10.06600 23.68500  24.60600 1.000 136.14078 ? 848 ASP A C     1 
ATOM 7015 O O     . ASP B 2 848 ? -10.97400 24.46700  24.95400 1.000 141.12504 ? 848 ASP A O     1 
ATOM 7016 C CB    . ASP B 2 848 ? -8.08700  24.16200  23.05100 1.000 151.18725 ? 848 ASP A CB    1 
ATOM 7017 C CG    . ASP B 2 848 ? -7.76600  25.61900  23.34900 1.000 161.73664 ? 848 ASP A CG    1 
ATOM 7018 O OD1   . ASP B 2 848 ? -8.68900  26.35800  23.74500 1.000 162.83095 ? 848 ASP A OD1   1 
ATOM 7019 O OD2   . ASP B 2 848 ? -6.59500  26.00700  23.16200 1.000 147.48184 ? 848 ASP A OD2   1 
ATOM 7020 N N     . ARG B 2 849 ? -9.50200  22.77800  25.40800 1.000 138.04966 ? 849 ARG A N     1 
ATOM 7021 C CA    . ARG B 2 849 ? -9.96500  22.58800  26.80700 1.000 133.23187 ? 849 ARG A CA    1 
ATOM 7022 C C     . ARG B 2 849 ? -8.78500  22.75300  27.77600 1.000 131.56970 ? 849 ARG A C     1 
ATOM 7023 O O     . ARG B 2 849 ? -7.63300  22.82200  27.29900 1.000 131.68800 ? 849 ARG A O     1 
ATOM 7024 C CB    . ARG B 2 849 ? -10.59200 21.19800  26.94000 1.000 138.59945 ? 849 ARG A CB    1 
ATOM 7025 C CG    . ARG B 2 849 ? -9.81200  20.11000  26.21700 1.000 141.01643 ? 849 ARG A CG    1 
ATOM 7026 C CD    . ARG B 2 849 ? -10.70300 18.92500  25.87500 1.000 157.75541 ? 849 ARG A CD    1 
ATOM 7027 N NE    . ARG B 2 849 ? -11.88900 19.31300  25.10200 1.000 159.24914 ? 849 ARG A NE    1 
ATOM 7028 C CZ    . ARG B 2 849 ? -11.87800 19.87300  23.89700 1.000 160.01112 ? 849 ARG A CZ    1 
ATOM 7029 N NH1   . ARG B 2 849 ? -10.77900 19.86000  23.16500 1.000 164.26517 ? 849 ARG A NH1   1 
ATOM 7030 N NH2   . ARG B 2 849 ? -12.97500 20.43600  23.42400 1.000 150.99361 ? 849 ARG A NH2   1 
ATOM 7031 N N     . GLY B 2 850 ? -9.06800  22.81600  29.08000 1.000 120.80288 ? 850 GLY A N     1 
ATOM 7032 C CA    . GLY B 2 850 ? -8.00100  23.02600  30.07600 1.000 104.77674 ? 850 GLY A CA    1 
ATOM 7033 C C     . GLY B 2 850 ? -8.41700  22.57200  31.46100 1.000 102.41588 ? 850 GLY A C     1 
ATOM 7034 O O     . GLY B 2 850 ? -9.60300  22.22800  31.63600 1.000 118.10861 ? 850 GLY A O     1 
ATOM 7035 N N     . ILE B 2 851 ? -7.47800  22.57000  32.41200 1.000 98.96019  ? 851 ILE A N     1 
ATOM 7036 C CA    . ILE B 2 851 ? -7.76800  22.12100  33.80200 1.000 92.35480  ? 851 ILE A CA    1 
ATOM 7037 C C     . ILE B 2 851 ? -7.29800  23.19700  34.78100 1.000 87.42906  ? 851 ILE A C     1 
ATOM 7038 O O     . ILE B 2 851 ? -6.35000  23.93200  34.44500 1.000 89.01896  ? 851 ILE A O     1 
ATOM 7039 C CB    . ILE B 2 851 ? -7.07100  20.78600  34.11000 1.000 93.59660  ? 851 ILE A CB    1 
ATOM 7040 C CG1   . ILE B 2 851 ? -5.57600  20.97500  34.32500 1.000 101.10531 ? 851 ILE A CG1   1 
ATOM 7041 C CG2   . ILE B 2 851 ? -7.35200  19.75400  33.02000 1.000 103.76452 ? 851 ILE A CG2   1 
ATOM 7042 C CD1   . ILE B 2 851 ? -4.85100  19.71100  34.74200 1.000 135.13493 ? 851 ILE A CD1   1 
ATOM 7043 N N     . ILE B 2 852 ? -7.95700  23.29400  35.93400 1.000 102.47036 ? 852 ILE A N     1 
ATOM 7044 C CA    . ILE B 2 852 ? -7.48100  24.21300  36.95900 1.000 87.88499  ? 852 ILE A CA    1 
ATOM 7045 C C     . ILE B 2 852 ? -7.22100  23.40100  38.21900 1.000 82.02136  ? 852 ILE A C     1 
ATOM 7046 O O     . ILE B 2 852 ? -8.06700  22.60100  38.63300 1.000 87.78672  ? 852 ILE A O     1 
ATOM 7047 C CB    . ILE B 2 852 ? -8.49600  25.34200  37.21700 1.000 81.63452  ? 852 ILE A CB    1 
ATOM 7048 C CG1   . ILE B 2 852 ? -8.51400  26.31800  36.03800 1.000 82.32806  ? 852 ILE A CG1   1 
ATOM 7049 C CG2   . ILE B 2 852 ? -8.19400  26.06400  38.52500 1.000 86.87109  ? 852 ILE A CG2   1 
ATOM 7050 C CD1   . ILE B 2 852 ? -9.65400  27.30200  36.08300 1.000 87.40952  ? 852 ILE A CD1   1 
ATOM 7051 N N     . VAL B 2 853 ? -6.05200  23.59300  38.81700 1.000 74.82633  ? 853 VAL A N     1 
ATOM 7052 C CA    . VAL B 2 853 ? -5.65300  22.90300  40.03700 1.000 76.48011  ? 853 VAL A CA    1 
ATOM 7053 C C     . VAL B 2 853 ? -5.53100  23.94100  41.14200 1.000 84.68786  ? 853 VAL A C     1 
ATOM 7054 O O     . VAL B 2 853 ? -4.87100  24.97200  40.96300 1.000 95.39151  ? 853 VAL A O     1 
ATOM 7055 C CB    . VAL B 2 853 ? -4.33000  22.14200  39.84300 1.000 82.63175  ? 853 VAL A CB    1 
ATOM 7056 C CG1   . VAL B 2 853 ? -3.87900  21.51400  41.15200 1.000 77.14350  ? 853 VAL A CG1   1 
ATOM 7057 C CG2   . VAL B 2 853 ? -4.47800  21.08500  38.75700 1.000 86.03355  ? 853 VAL A CG2   1 
ATOM 7058 N N     . SER B 2 854 ? -6.17200  23.67800  42.27500 1.000 79.45895  ? 854 SER A N     1 
ATOM 7059 C CA    . SER B 2 854 ? -6.15000  24.58700  43.41400 1.000 82.42987  ? 854 SER A CA    1 
ATOM 7060 C C     . SER B 2 854 ? -5.66500  23.82200  44.63400 1.000 75.38234  ? 854 SER A C     1 
ATOM 7061 O O     . SER B 2 854 ? -6.30900  22.85800  45.06000 1.000 83.13810  ? 854 SER A O     1 
ATOM 7062 C CB    . SER B 2 854 ? -7.53200  25.19200  43.66400 1.000 84.49389  ? 854 SER A CB    1 
ATOM 7063 O OG    . SER B 2 854 ? -7.58300  25.82700  44.92800 1.000 84.52887  ? 854 SER A OG    1 
ATOM 7064 N N     . PHE B 2 855 ? -4.57700  24.28700  45.25200 1.000 83.40409  ? 855 PHE A N     1 
ATOM 7065 C CA    . PHE B 2 855 ? -3.97600  23.52800  46.38400 1.000 83.25428  ? 855 PHE A CA    1 
ATOM 7066 C C     . PHE B 2 855 ? -4.48600  24.02200  47.73700 1.000 80.62993  ? 855 PHE A C     1 
ATOM 7067 O O     . PHE B 2 855 ? -4.52900  23.20800  48.68100 1.000 89.49531  ? 855 PHE A O     1 
ATOM 7068 C CB    . PHE B 2 855 ? -2.45200  23.65700  46.31800 1.000 77.13066  ? 855 PHE A CB    1 
ATOM 7069 C CG    . PHE B 2 855 ? -1.81100  23.14600  45.03600 1.000 83.50655  ? 855 PHE A CG    1 
ATOM 7070 C CD1   . PHE B 2 855 ? -1.63000  23.98500  43.94300 1.000 87.10326  ? 855 PHE A CD1   1 
ATOM 7071 C CD2   . PHE B 2 855 ? -1.38100  21.82900  44.93200 1.000 71.04702  ? 855 PHE A CD2   1 
ATOM 7072 C CE1   . PHE B 2 855 ? -1.04200  23.51600  42.78000 1.000 84.62219  ? 855 PHE A CE1   1 
ATOM 7073 C CE2   . PHE B 2 855 ? -0.79400  21.36600  43.76700 1.000 86.79794  ? 855 PHE A CE2   1 
ATOM 7074 C CZ    . PHE B 2 855 ? -0.62500  22.20900  42.69400 1.000 90.31056  ? 855 PHE A CZ    1 
ATOM 7075 N N     . ASP B 2 856 ? -4.84900  25.30100  47.85200 1.000 77.75027  ? 856 ASP A N     1 
ATOM 7076 C CA    . ASP B 2 856 ? -5.23600  25.83400  49.19000 1.000 88.89873  ? 856 ASP A CA    1 
ATOM 7077 C C     . ASP B 2 856 ? -6.45200  25.06300  49.70900 1.000 81.74902  ? 856 ASP A C     1 
ATOM 7078 O O     . ASP B 2 856 ? -7.45100  24.96800  48.96900 1.000 83.14268  ? 856 ASP A O     1 
ATOM 7079 C CB    . ASP B 2 856 ? -5.43200  27.34100  49.16500 1.000 86.86954  ? 856 ASP A CB    1 
ATOM 7080 C CG    . ASP B 2 856 ? -5.19400  28.04200  50.49400 1.000 100.22954 ? 856 ASP A CG    1 
ATOM 7081 O OD1   . ASP B 2 856 ? -4.95100  27.33400  51.49300 1.000 115.84222 ? 856 ASP A OD1   1 
ATOM 7082 O OD2   . ASP B 2 856 ? -5.22900  29.28800  50.51400 1.000 94.56836  ? 856 ASP A OD2   1 
ATOM 7083 N N     . ASP B 2 857 ? -6.36500  24.54100  50.93600 1.000 108.44435 ? 857 ASP A N     1 
ATOM 7084 C CA    . ASP B 2 857 ? -7.47100  23.73100  51.51800 1.000 100.63579 ? 857 ASP A CA    1 
ATOM 7085 C C     . ASP B 2 857 ? -8.60000  24.64700  51.99300 1.000 111.99185 ? 857 ASP A C     1 
ATOM 7086 O O     . ASP B 2 857 ? -9.73600  24.15800  52.13100 1.000 105.02358 ? 857 ASP A O     1 
ATOM 7087 C CB    . ASP B 2 857 ? -6.97800  22.84900  52.65300 1.000 86.84697  ? 857 ASP A CB    1 
ATOM 7088 C CG    . ASP B 2 857 ? -6.26700  23.57400  53.78600 1.000 125.74056 ? 857 ASP A CG    1 
ATOM 7089 O OD1   . ASP B 2 857 ? -6.06900  24.80100  53.66700 1.000 139.67034 ? 857 ASP A OD1   1 
ATOM 7090 O OD2   . ASP B 2 857 ? -5.93000  22.90600  54.78400 1.000 128.70919 ? 857 ASP A OD2   1 
ATOM 7091 N N     . ARG B 2 858 ? -8.30400  25.92700  52.22500 1.000 109.13348 ? 858 ARG A N     1 
ATOM 7092 C CA    . ARG B 2 858 ? -9.33000  26.85800  52.76100 1.000 92.18972  ? 858 ARG A CA    1 
ATOM 7093 C C     . ARG B 2 858 ? -10.57800 26.80800  51.86600 1.000 91.48471  ? 858 ARG A C     1 
ATOM 7094 O O     . ARG B 2 858 ? -11.69100 27.00200  52.39000 1.000 90.50361  ? 858 ARG A O     1 
ATOM 7095 C CB    . ARG B 2 858 ? -8.74800  28.27100  52.83600 1.000 95.19643  ? 858 ARG A CB    1 
ATOM 7096 C CG    . ARG B 2 858 ? -7.42800  28.38400  53.58400 1.000 70.64369  ? 858 ARG A CG    1 
ATOM 7097 C CD    . ARG B 2 858 ? -6.80500  29.74200  53.31700 1.000 85.63256  ? 858 ARG A CD    1 
ATOM 7098 N NE    . ARG B 2 858 ? -5.42200  29.85100  53.79300 1.000 87.45956  ? 858 ARG A NE    1 
ATOM 7099 C CZ    . ARG B 2 858 ? -4.66100  30.91900  53.60400 1.000 94.78746  ? 858 ARG A CZ    1 
ATOM 7100 N NH1   . ARG B 2 858 ? -5.01400  31.82900  52.71500 1.000 89.34637  ? 858 ARG A NH1   1 
ATOM 7101 N NH2   . ARG B 2 858 ? -3.54700  31.07000  54.29700 1.000 114.93773 ? 858 ARG A NH2   1 
ATOM 7102 N N     . LEU B 2 859 ? -10.39100 26.53200  50.57400 1.000 82.33672  ? 859 LEU A N     1 
ATOM 7103 C CA    . LEU B 2 859 ? -11.53100 26.47100  49.62400 1.000 89.13518  ? 859 LEU A CA    1 
ATOM 7104 C C     . LEU B 2 859 ? -12.51400 25.38400  50.07700 1.000 92.37462  ? 859 LEU A C     1 
ATOM 7105 O O     . LEU B 2 859 ? -13.68400 25.43400  49.65000 1.000 102.60547 ? 859 LEU A O     1 
ATOM 7106 C CB    . LEU B 2 859 ? -11.00600 26.19400  48.21700 1.000 81.91500  ? 859 LEU A CB    1 
ATOM 7107 C CG    . LEU B 2 859 ? -12.02700 26.29600  47.08000 1.000 92.66195  ? 859 LEU A CG    1 
ATOM 7108 C CD1   . LEU B 2 859 ? -11.50800 27.21000  45.98500 1.000 96.67826  ? 859 LEU A CD1   1 
ATOM 7109 C CD2   . LEU B 2 859 ? -12.33900 24.92200  46.51800 1.000 93.10273  ? 859 LEU A CD2   1 
ATOM 7110 N N     . ILE B 2 860 ? -12.06000 24.44500  50.91100 1.000 99.74532  ? 860 ILE A N     1 
ATOM 7111 C CA    . ILE B 2 860 ? -12.94200 23.30900  51.32200 1.000 99.87889  ? 860 ILE A CA    1 
ATOM 7112 C C     . ILE B 2 860 ? -13.07300 23.27500  52.85400 1.000 105.97334 ? 860 ILE A C     1 
ATOM 7113 O O     . ILE B 2 860 ? -14.01000 22.61000  53.34200 1.000 109.51665 ? 860 ILE A O     1 
ATOM 7114 C CB    . ILE B 2 860 ? -12.41200 21.97200  50.77000 1.000 83.05635  ? 860 ILE A CB    1 
ATOM 7115 C CG1   . ILE B 2 860 ? -11.15700 21.50700  51.50600 1.000 95.67826  ? 860 ILE A CG1   1 
ATOM 7116 C CG2   . ILE B 2 860 ? -12.18600 22.05400  49.26000 1.000 84.22024  ? 860 ILE A CG2   1 
ATOM 7117 C CD1   . ILE B 2 860 ? -10.53000 20.25300  50.92800 1.000 100.72050 ? 860 ILE A CD1   1 
ATOM 7118 N N     . ASN B 2 861 ? -12.18200 23.95300  53.58300 1.000 111.65852 ? 861 ASN A N     1 
ATOM 7119 C CA    . ASN B 2 861 ? -12.23000 23.85400  55.07200 1.000 111.40839 ? 861 ASN A CA    1 
ATOM 7120 C C     . ASN B 2 861 ? -12.13100 25.23700  55.73100 1.000 108.24753 ? 861 ASN A C     1 
ATOM 7121 O O     . ASN B 2 861 ? -11.67600 25.29600  56.89300 1.000 115.43979 ? 861 ASN A O     1 
ATOM 7122 C CB    . ASN B 2 861 ? -11.19300 22.86500  55.60000 1.000 98.25953  ? 861 ASN A CB    1 
ATOM 7123 C CG    . ASN B 2 861 ? -9.76400  23.31400  55.39700 1.000 142.70706 ? 861 ASN A CG    1 
ATOM 7124 O OD1   . ASN B 2 861 ? -9.51200  24.42100  54.91200 1.000 147.39872 ? 861 ASN A OD1   1 
ATOM 7125 N ND2   . ASN B 2 861 ? -8.81300  22.47600  55.78100 1.000 116.64213 ? 861 ASN A ND2   1 
ATOM 7126 N N     . SER B 2 862 ? -12.55200 26.30200  55.04200 1.000 116.97946 ? 862 SER A N     1 
ATOM 7127 C CA    . SER B 2 862 ? -12.56400 27.64500  55.68300 1.000 96.97303  ? 862 SER A CA    1 
ATOM 7128 C C     . SER B 2 862 ? -13.99500 28.19400  55.73400 1.000 110.25990 ? 862 SER A C     1 
ATOM 7129 O O     . SER B 2 862 ? -14.84200 27.70600  54.96300 1.000 127.99021 ? 862 SER A O     1 
ATOM 7130 C CB    . SER B 2 862 ? -11.64800 28.60500  54.98800 1.000 106.52778 ? 862 SER A CB    1 
ATOM 7131 O OG    . SER B 2 862 ? -11.55100 29.81300  55.72800 1.000 144.68127 ? 862 SER A OG    1 
ATOM 7132 N N     . ASN B 2 863 ? -14.24700 29.17000  56.60700 1.000 92.45584  ? 863 ASN A N     1 
ATOM 7133 C CA    . ASN B 2 863 ? -15.62600 29.70700  56.77600 1.000 112.90633 ? 863 ASN A CA    1 
ATOM 7134 C C     . ASN B 2 863 ? -16.07000 30.45600  55.51600 1.000 114.66589 ? 863 ASN A C     1 
ATOM 7135 O O     . ASN B 2 863 ? -17.25500 30.32500  55.14700 1.000 114.94762 ? 863 ASN A O     1 
ATOM 7136 C CB    . ASN B 2 863 ? -15.72500 30.58200  58.02000 1.000 107.11153 ? 863 ASN A CB    1 
ATOM 7137 C CG    . ASN B 2 863 ? -14.60700 31.59300  58.09900 1.000 117.76231 ? 863 ASN A CG    1 
ATOM 7138 O OD1   . ASN B 2 863 ? -14.50000 32.47400  57.24000 1.000 135.62634 ? 863 ASN A OD1   1 
ATOM 7139 N ND2   . ASN B 2 863 ? -13.77500 31.49000  59.12500 1.000 129.02042 ? 863 ASN A ND2   1 
ATOM 7140 N N     . TYR B 2 864 ? -15.16600 31.19800  54.87400 1.000 103.77931 ? 864 TYR A N     1 
ATOM 7141 C CA    . TYR B 2 864 ? -15.56600 32.03500  53.71000 1.000 103.18987 ? 864 TYR A CA    1 
ATOM 7142 C C     . TYR B 2 864 ? -15.59000 31.20900  52.43000 1.000 108.00878 ? 864 TYR A C     1 
ATOM 7143 O O     . TYR B 2 864 ? -15.78700 31.79700  51.34700 1.000 97.11034  ? 864 TYR A O     1 
ATOM 7144 C CB    . TYR B 2 864 ? -14.58900 33.20200  53.55900 1.000 81.26638  ? 864 TYR A CB    1 
ATOM 7145 C CG    . TYR B 2 864 ? -13.12100 32.83700  53.72200 1.000 93.18270  ? 864 TYR A CG    1 
ATOM 7146 C CD1   . TYR B 2 864 ? -12.41600 32.22300  52.69400 1.000 97.44033  ? 864 TYR A CD1   1 
ATOM 7147 C CD2   . TYR B 2 864 ? -12.43100 33.14000  54.88900 1.000 85.39582  ? 864 TYR A CD2   1 
ATOM 7148 C CE1   . TYR B 2 864 ? -11.07900 31.89300  52.83400 1.000 93.88491  ? 864 TYR A CE1   1 
ATOM 7149 C CE2   . TYR B 2 864 ? -11.09200 32.82300  55.03800 1.000 79.74194  ? 864 TYR A CE2   1 
ATOM 7150 C CZ    . TYR B 2 864 ? -10.41600 32.19800  54.00800 1.000 83.72041  ? 864 TYR A CZ    1 
ATOM 7151 O OH    . TYR B 2 864 ? -9.09700  31.88100  54.14700 1.000 94.10484  ? 864 TYR A OH    1 
ATOM 7152 N N     . LYS B 2 865 ? -15.39700 29.89400  52.53300 1.000 99.52505  ? 865 LYS A N     1 
ATOM 7153 C CA    . LYS B 2 865 ? -15.30400 29.05900  51.30600 1.000 94.95281  ? 865 LYS A CA    1 
ATOM 7154 C C     . LYS B 2 865 ? -16.45400 29.39900  50.34800 1.000 93.39545  ? 865 LYS A C     1 
ATOM 7155 O O     . LYS B 2 865 ? -16.17900 29.55600  49.14400 1.000 92.94988  ? 865 LYS A O     1 
ATOM 7156 C CB    . LYS B 2 865 ? -15.29300 27.56600  51.65200 1.000 97.77136  ? 865 LYS A CB    1 
ATOM 7157 C CG    . LYS B 2 865 ? -16.49800 27.01900  52.39700 1.000 114.43344 ? 865 LYS A CG    1 
ATOM 7158 C CD    . LYS B 2 865 ? -16.30300 25.55500  52.77000 1.000 107.25728 ? 865 LYS A CD    1 
ATOM 7159 C CE    . LYS B 2 865 ? -17.40800 25.02700  53.62400 1.000 108.77269 ? 865 LYS A CE    1 
ATOM 7160 N NZ    . LYS B 2 865 ? -17.17300 23.62900  53.99000 1.000 126.79745 ? 865 LYS A NZ    1 
ATOM 7161 N N     . ASN B 2 866 ? -17.68000 29.52900  50.85700 1.000 83.87024  ? 866 ASN A N     1 
ATOM 7162 C CA    . ASN B 2 866 ? -18.81900 29.74900  49.97500 1.000 104.05685 ? 866 ASN A CA    1 
ATOM 7163 C C     . ASN B 2 866 ? -18.51100 30.81300  48.93400 1.000 93.03406  ? 866 ASN A C     1 
ATOM 7164 O O     . ASN B 2 866 ? -18.91200 30.68500  47.77000 1.000 85.62609  ? 866 ASN A O     1 
ATOM 7165 C CB    . ASN B 2 866 ? -20.04700 30.17300  50.78600 1.000 108.30440 ? 866 ASN A CB    1 
ATOM 7166 C CG    . ASN B 2 866 ? -20.17900 29.41600  52.08900 1.000 142.81403 ? 866 ASN A CG    1 
ATOM 7167 O OD1   . ASN B 2 866 ? -20.08400 30.00000  53.16600 1.000 144.51403 ? 866 ASN A OD1   1 
ATOM 7168 N ND2   . ASN B 2 866 ? -20.43100 28.11200  51.99800 1.000 123.68476 ? 866 ASN A ND2   1 
ATOM 7169 N N     . PHE B 2 867 ? -17.80800 31.86800  49.35700 1.000 97.79402  ? 867 PHE A N     1 
ATOM 7170 C CA    . PHE B 2 867 ? -17.47600 32.95500  48.44200 1.000 87.32163  ? 867 PHE A CA    1 
ATOM 7171 C C     . PHE B 2 867 ? -16.57800 32.49000  47.30100 1.000 86.48928  ? 867 PHE A C     1 
ATOM 7172 O O     . PHE B 2 867 ? -16.71700 32.95900  46.16500 1.000 83.66551  ? 867 PHE A O     1 
ATOM 7173 C CB    . PHE B 2 867 ? -16.81000 34.09000  49.20700 1.000 84.49888  ? 867 PHE A CB    1 
ATOM 7174 C CG    . PHE B 2 867 ? -17.66400 34.66300  50.31000 1.000 85.10994  ? 867 PHE A CG    1 
ATOM 7175 C CD1   . PHE B 2 867 ? -18.91000 35.20400  50.03700 1.000 89.77658  ? 867 PHE A CD1   1 
ATOM 7176 C CD2   . PHE B 2 867 ? -17.20800 34.68300  51.61400 1.000 94.92300  ? 867 PHE A CD2   1 
ATOM 7177 C CE1   . PHE B 2 867 ? -19.68600 35.73600  51.05100 1.000 92.40234  ? 867 PHE A CE1   1 
ATOM 7178 C CE2   . PHE B 2 867 ? -17.97100 35.21200  52.62700 1.000 91.02197  ? 867 PHE A CE2   1 
ATOM 7179 C CZ    . PHE B 2 867 ? -19.21400 35.74100  52.34800 1.000 73.86037  ? 867 PHE A CZ    1 
ATOM 7180 N N     . PHE B 2 868 ? -15.66500 31.56100  47.57500 1.000 83.92261  ? 868 PHE A N     1 
ATOM 7181 C CA    . PHE B 2 868 ? -14.74700 31.07700  46.55100 1.000 77.43444  ? 868 PHE A CA    1 
ATOM 7182 C C     . PHE B 2 868 ? -15.35600 29.98200  45.68100 1.000 91.23104  ? 868 PHE A C     1 
ATOM 7183 O O     . PHE B 2 868 ? -15.15500 29.98400  44.46200 1.000 95.93239  ? 868 PHE A O     1 
ATOM 7184 C CB    . PHE B 2 868 ? -13.45300 30.58400  47.20300 1.000 76.62947  ? 868 PHE A CB    1 
ATOM 7185 C CG    . PHE B 2 868 ? -12.52100 31.69400  47.59700 1.000 90.50364  ? 868 PHE A CG    1 
ATOM 7186 C CD1   . PHE B 2 868 ? -11.63100 32.21500  46.67400 1.000 76.39810  ? 868 PHE A CD1   1 
ATOM 7187 C CD2   . PHE B 2 868 ? -12.53700 32.22000  48.88200 1.000 84.94641  ? 868 PHE A CD2   1 
ATOM 7188 C CE1   . PHE B 2 868 ? -10.77500 33.23500  47.01600 1.000 80.19012  ? 868 PHE A CE1   1 
ATOM 7189 C CE2   . PHE B 2 868 ? -11.67700 33.24600  49.23200 1.000 85.68093  ? 868 PHE A CE2   1 
ATOM 7190 C CZ    . PHE B 2 868 ? -10.79400 33.75400  48.29700 1.000 86.36044  ? 868 PHE A CZ    1 
ATOM 7191 N N     . GLU B 2 869 ? -16.09400 29.04000  46.27300 1.000 91.45835  ? 869 GLU A N     1 
ATOM 7192 C CA    . GLU B 2 869 ? -16.72500 28.00800  45.45900 1.000 80.18359  ? 869 GLU A CA    1 
ATOM 7193 C C     . GLU B 2 869 ? -17.90500 28.54900  44.66200 1.000 93.35028  ? 869 GLU A C     1 
ATOM 7194 O O     . GLU B 2 869 ? -18.36300 27.88300  43.72600 1.000 110.32830 ? 869 GLU A O     1 
ATOM 7195 C CB    . GLU B 2 869 ? -17.15300 26.82600  46.33200 1.000 90.37876  ? 869 GLU A CB    1 
ATOM 7196 C CG    . GLU B 2 869 ? -17.50400 27.17000  47.76400 1.000 98.39546  ? 869 GLU A CG    1 
ATOM 7197 C CD    . GLU B 2 869 ? -17.56900 25.93500  48.64300 1.000 120.56661 ? 869 GLU A CD    1 
ATOM 7198 O OE1   . GLU B 2 869 ? -16.85600 24.95700  48.33600 1.000 109.47856 ? 869 GLU A OE1   1 
ATOM 7199 O OE2   . GLU B 2 869 ? -18.33700 25.93400  49.62900 1.000 121.81132 ? 869 GLU A OE2   1 
ATOM 7200 N N     . GLN B 2 870 ? -18.40300 29.74100  45.00900 1.000 93.31169  ? 870 GLN A N     1 
ATOM 7201 C CA    . GLN B 2 870 ? -19.32200 30.44200  44.11600 1.000 82.99679  ? 870 GLN A CA    1 
ATOM 7202 C C     . GLN B 2 870 ? -18.67800 30.69800  42.75900 1.000 93.20932  ? 870 GLN A C     1 
ATOM 7203 O O     . GLN B 2 870 ? -19.34700 30.64300  41.72100 1.000 91.95991  ? 870 GLN A O     1 
ATOM 7204 C CB    . GLN B 2 870 ? -19.76600 31.76200  44.74500 1.000 96.40937  ? 870 GLN A CB    1 
ATOM 7205 C CG    . GLN B 2 870 ? -20.97400 31.66400  45.65800 1.000 91.44488  ? 870 GLN A CG    1 
ATOM 7206 C CD    . GLN B 2 870 ? -21.24400 32.96800  46.37900 1.000 96.06681  ? 870 GLN A CD    1 
ATOM 7207 O OE1   . GLN B 2 870 ? -20.43900 33.89700  46.31800 1.000 90.31027  ? 870 GLN A OE1   1 
ATOM 7208 N NE2   . GLN B 2 870 ? -22.37800 33.04700  47.06600 1.000 115.75176 ? 870 GLN A NE2   1 
ATOM 7209 N N     . THR B 2 871 ? -17.37400 30.97700  42.74900 1.000 90.16300  ? 871 THR A N     1 
ATOM 7210 C CA    . THR B 2 871 ? -16.64800 31.27000  41.52000 1.000 86.98396  ? 871 THR A CA    1 
ATOM 7211 C C     . THR B 2 871 ? -16.37800 30.03200  40.67500 1.000 91.58838  ? 871 THR A C     1 
ATOM 7212 O O     . THR B 2 871 ? -15.82900 30.16800  39.57700 1.000 106.14494 ? 871 THR A O     1 
ATOM 7213 C CB    . THR B 2 871 ? -15.32600 31.96400  41.85300 1.000 87.79097  ? 871 THR A CB    1 
ATOM 7214 O OG1   . THR B 2 871 ? -14.43200 31.02700  42.46600 1.000 81.96848  ? 871 THR A OG1   1 
ATOM 7215 C CG2   . THR B 2 871 ? -15.56900 33.11600  42.81500 1.000 95.65009  ? 871 THR A CG2   1 
ATOM 7216 N N     . LEU B 2 872 ? -16.74700 28.84100  41.14700 1.000 83.44773  ? 872 LEU A N     1 
ATOM 7217 C CA    . LEU B 2 872 ? -16.50600 27.59800  40.42300 1.000 94.11426  ? 872 LEU A CA    1 
ATOM 7218 C C     . LEU B 2 872 ? -17.80300 26.83100  40.18400 1.000 95.64252  ? 872 LEU A C     1 
ATOM 7219 O O     . LEU B 2 872 ? -17.79700 25.60300  40.08000 1.000 88.89250  ? 872 LEU A O     1 
ATOM 7220 C CB    . LEU B 2 872 ? -15.49900 26.72600  41.17300 1.000 97.38587  ? 872 LEU A CB    1 
ATOM 7221 C CG    . LEU B 2 872 ? -14.10200 27.30300  41.42000 1.000 99.22125  ? 872 LEU A CG    1 
ATOM 7222 C CD1   . LEU B 2 872 ? -13.32100 26.41000  42.36700 1.000 87.99765  ? 872 LEU A CD1   1 
ATOM 7223 C CD2   . LEU B 2 872 ? -13.34600 27.47700  40.11400 1.000 93.14930  ? 872 LEU A CD2   1 
ATOM 7224 N N     . GLU B 2 873 ? -18.92500 27.54800  40.08200 1.000 106.37665 ? 873 GLU A N     1 
ATOM 7225 C CA    . GLU B 2 873 ? -20.22500 26.88900  39.99400 1.000 103.54757 ? 873 GLU A CA    1 
ATOM 7226 C C     . GLU B 2 873 ? -20.46600 26.26400  38.62500 1.000 90.53664  ? 873 GLU A C     1 
ATOM 7227 O O     . GLU B 2 873 ? -21.15900 25.24500  38.52900 1.000 96.36720  ? 873 GLU A O     1 
ATOM 7228 C CB    . GLU B 2 873 ? -21.33900 27.88200  40.32400 1.000 110.00677 ? 873 GLU A CB    1 
ATOM 7229 C CG    . GLU B 2 873 ? -21.47600 28.17700  41.80800 1.000 109.15234 ? 873 GLU A CG    1 
ATOM 7230 C CD    . GLU B 2 873 ? -22.38800 29.35300  42.09200 1.000 132.67572 ? 873 GLU A CD    1 
ATOM 7231 O OE1   . GLU B 2 873 ? -22.40700 30.30300  41.28200 1.000 131.92991 ? 873 GLU A OE1   1 
ATOM 7232 O OE2   . GLU B 2 873 ? -23.08900 29.32600  43.12500 1.000 142.23540 ? 873 GLU A OE2   1 
ATOM 7233 N N     . ASN B 2 874 ? -19.95200 26.90400  37.57700 1.000 101.25113 ? 874 ASN A N     1 
ATOM 7234 C CA    . ASN B 2 874 ? -20.21500 26.41300  36.19800 1.000 106.32213 ? 874 ASN A CA    1 
ATOM 7235 C C     . ASN B 2 874 ? -19.17900 25.35100  35.84100 1.000 104.02341 ? 874 ASN A C     1 
ATOM 7236 O O     . ASN B 2 874 ? -19.27000 24.78000  34.73800 1.000 121.61151 ? 874 ASN A O     1 
ATOM 7237 C CB    . ASN B 2 874 ? -20.18800 27.55400  35.19200 1.000 106.70635 ? 874 ASN A CB    1 
ATOM 7238 C CG    . ASN B 2 874 ? -21.00000 28.73900  35.65500 1.000 110.01933 ? 874 ASN A CG    1 
ATOM 7239 O OD1   . ASN B 2 874 ? -20.46300 29.84300  35.79500 1.000 111.53184 ? 874 ASN A OD1   1 
ATOM 7240 N ND2   . ASN B 2 874 ? -22.28700 28.53600  35.89700 1.000 98.29264  ? 874 ASN A ND2   1 
ATOM 7241 N N     . TYR B 2 875 ? -18.23300 25.10500  36.74400 1.000 107.73027 ? 875 TYR A N     1 
ATOM 7242 C CA    . TYR B 2 875 ? -17.14500 24.14100  36.44400 1.000 98.10748  ? 875 TYR A CA    1 
ATOM 7243 C C     . TYR B 2 875 ? -17.45200 22.83000  37.13800 1.000 95.77454  ? 875 TYR A C     1 
ATOM 7244 O O     . TYR B 2 875 ? -18.23900 22.82300  38.10500 1.000 99.43387  ? 875 TYR A O     1 
ATOM 7245 C CB    . TYR B 2 875 ? -15.81100 24.72100  36.91500 1.000 93.68235  ? 875 TYR A CB    1 
ATOM 7246 C CG    . TYR B 2 875 ? -15.34600 25.97400  36.18600 1.000 99.05036  ? 875 TYR A CG    1 
ATOM 7247 C CD1   . TYR B 2 875 ? -15.62300 26.16700  34.84000 1.000 111.25435 ? 875 TYR A CD1   1 
ATOM 7248 C CD2   . TYR B 2 875 ? -14.63600 26.96600  36.85000 1.000 88.31071  ? 875 TYR A CD2   1 
ATOM 7249 C CE1   . TYR B 2 875 ? -15.20300 27.30500  34.17300 1.000 124.08494 ? 875 TYR A CE1   1 
ATOM 7250 C CE2   . TYR B 2 875 ? -14.21100 28.10900  36.19600 1.000 85.51421  ? 875 TYR A CE2   1 
ATOM 7251 C CZ    . TYR B 2 875 ? -14.49500 28.27900  34.85400 1.000 106.22833 ? 875 TYR A CZ    1 
ATOM 7252 O OH    . TYR B 2 875 ? -14.07900 29.40300  34.20200 1.000 118.67351 ? 875 TYR A OH    1 
ATOM 7253 N N     . ARG B 2 876 ? -16.84500 21.74600  36.65800 1.000 97.64280  ? 876 ARG A N     1 
ATOM 7254 C CA    . ARG B 2 876 ? -17.04100 20.41900  37.29000 1.000 89.20092  ? 876 ARG A CA    1 
ATOM 7255 C C     . ARG B 2 876 ? -15.83900 20.15400  38.19700 1.000 84.49688  ? 876 ARG A C     1 
ATOM 7256 O O     . ARG B 2 876 ? -14.69900 20.32400  37.73100 1.000 85.31056  ? 876 ARG A O     1 
ATOM 7257 C CB    . ARG B 2 876 ? -17.23100 19.36500  36.19700 1.000 95.87596  ? 876 ARG A CB    1 
ATOM 7258 C CG    . ARG B 2 876 ? -18.27300 19.75900  35.16000 1.000 109.96207 ? 876 ARG A CG    1 
ATOM 7259 C CD    . ARG B 2 876 ? -19.65800 19.87700  35.77700 1.000 147.53259 ? 876 ARG A CD    1 
ATOM 7260 N NE    . ARG B 2 876 ? -20.12600 21.26400  35.86700 1.000 168.66985 ? 876 ARG A NE    1 
ATOM 7261 C CZ    . ARG B 2 876 ? -21.09900 21.67900  36.66700 1.000 132.40192 ? 876 ARG A CZ    1 
ATOM 7262 N NH1   . ARG B 2 876 ? -20.87700 21.80700  37.96300 1.000 130.28087 ? 876 ARG A NH1   1 
ATOM 7263 N NH2   . ARG B 2 876 ? -22.29100 21.96000  36.17200 1.000 119.11568 ? 876 ARG A NH2   1 
ATOM 7264 N N     . GLN B 2 877 ? -16.07600 19.75400  39.44700 1.000 84.13067  ? 877 GLN A N     1 
ATOM 7265 C CA    . GLN B 2 877 ? -14.94600 19.61600  40.40100 1.000 81.51383  ? 877 GLN A CA    1 
ATOM 7266 C C     . GLN B 2 877 ? -14.68000 18.15100  40.76800 1.000 87.96260  ? 877 GLN A C     1 
ATOM 7267 O O     . GLN B 2 877 ? -15.64500 17.36200  40.80500 1.000 95.28511  ? 877 GLN A O     1 
ATOM 7268 C CB    . GLN B 2 877 ? -15.22900 20.42800  41.66500 1.000 81.05518  ? 877 GLN A CB    1 
ATOM 7269 C CG    . GLN B 2 877 ? -15.18900 21.93500  41.44600 1.000 81.10086  ? 877 GLN A CG    1 
ATOM 7270 C CD    . GLN B 2 877 ? -16.42800 22.46800  40.76500 1.000 89.19328  ? 877 GLN A CD    1 
ATOM 7271 O OE1   . GLN B 2 877 ? -17.45300 21.78600  40.66000 1.000 102.91313 ? 877 GLN A OE1   1 
ATOM 7272 N NE2   . GLN B 2 877 ? -16.35000 23.70800  40.30900 1.000 107.99645 ? 877 GLN A NE2   1 
ATOM 7273 N N     . LYS B 2 878 ? -13.41400 17.81500  41.03000 1.000 81.36147  ? 878 LYS A N     1 
ATOM 7274 C CA    . LYS B 2 878 ? -13.03400 16.44800  41.46400 1.000 80.55499  ? 878 LYS A CA    1 
ATOM 7275 C C     . LYS B 2 878 ? -11.89800 16.60200  42.48400 1.000 77.93895  ? 878 LYS A C     1 
ATOM 7276 O O     . LYS B 2 878 ? -10.99300 17.41800  42.23200 1.000 90.16171  ? 878 LYS A O     1 
ATOM 7277 C CB    . LYS B 2 878 ? -12.59800 15.61800  40.25400 1.000 84.38192  ? 878 LYS A CB    1 
ATOM 7278 C CG    . LYS B 2 878 ? -11.53900 14.55200  40.51000 1.000 97.63482  ? 878 LYS A CG    1 
ATOM 7279 C CD    . LYS B 2 878 ? -12.03100 13.32200  41.26200 1.000 92.31954  ? 878 LYS A CD    1 
ATOM 7280 C CE    . LYS B 2 878 ? -12.99900 12.51200  40.46200 1.000 102.14034 ? 878 LYS A CE    1 
ATOM 7281 N NZ    . LYS B 2 878 ? -13.42300 11.31500  41.19300 1.000 107.87823 ? 878 LYS A NZ    1 
ATOM 7282 N N     . LYS B 2 879 ? -11.95700 15.87000  43.59600 1.000 72.67017  ? 879 LYS A N     1 
ATOM 7283 C CA    . LYS B 2 879 ? -10.87300 15.92800  44.60800 1.000 73.07247  ? 879 LYS A CA    1 
ATOM 7284 C C     . LYS B 2 879 ? -10.32500 14.51100  44.82700 1.000 74.08871  ? 879 LYS A C     1 
ATOM 7285 O O     . LYS B 2 879 ? -11.13700 13.56500  44.83500 1.000 97.52897  ? 879 LYS A O     1 
ATOM 7286 C CB    . LYS B 2 879 ? -11.42200 16.54900  45.89500 1.000 75.13965  ? 879 LYS A CB    1 
ATOM 7287 C CG    . LYS B 2 879 ? -12.84500 16.15600  46.24800 1.000 102.76393 ? 879 LYS A CG    1 
ATOM 7288 C CD    . LYS B 2 879 ? -13.60500 17.30000  46.90700 1.000 93.21990  ? 879 LYS A CD    1 
ATOM 7289 C CE    . LYS B 2 879 ? -13.69700 18.49000  46.00600 1.000 85.09321  ? 879 LYS A CE    1 
ATOM 7290 N NZ    . LYS B 2 879 ? -14.44500 19.58600  46.62600 1.000 113.80161 ? 879 LYS A NZ    1 
ATOM 7291 N N     . GLY B 2 880 ? -9.00500  14.37400  44.99500 1.000 79.03922  ? 880 GLY A N     1 
ATOM 7292 C CA    . GLY B 2 880 ? -8.44500  13.03900  45.26100 1.000 100.24118 ? 880 GLY A CA    1 
ATOM 7293 C C     . GLY B 2 880 ? -6.93300  13.03100  45.23800 1.000 98.95468  ? 880 GLY A C     1 
ATOM 7294 O O     . GLY B 2 880 ? -6.33400  14.12300  45.23900 1.000 85.29762  ? 880 GLY A O     1 
ATOM 7295 N N     . ASP B 2 881 ? -6.33900  11.83500  45.22100 1.000 114.21415 ? 881 ASP A N     1 
ATOM 7296 C CA    . ASP B 2 881 ? -4.86000  11.69900  45.22900 1.000 89.96741  ? 881 ASP A CA    1 
ATOM 7297 C C     . ASP B 2 881 ? -4.31300  12.02500  43.84100 1.000 101.11014 ? 881 ASP A C     1 
ATOM 7298 O O     . ASP B 2 881 ? -5.10900  12.10800  42.88400 1.000 106.75958 ? 881 ASP A O     1 
ATOM 7299 C CB    . ASP B 2 881 ? -4.44000  10.30500  45.66000 1.000 93.50807  ? 881 ASP A CB    1 
ATOM 7300 C CG    . ASP B 2 881 ? -5.17300  9.75500   46.87400 1.000 133.99250 ? 881 ASP A CG    1 
ATOM 7301 O OD1   . ASP B 2 881 ? -5.08800  10.38900  47.94600 1.000 151.35624 ? 881 ASP A OD1   1 
ATOM 7302 O OD2   . ASP B 2 881 ? -5.82500  8.70000   46.73500 1.000 136.97434 ? 881 ASP A OD2   1 
ATOM 7303 N N     . ILE B 2 882 ? -2.99600  12.19200  43.74400 1.000 100.83998 ? 882 ILE A N     1 
ATOM 7304 C CA    . ILE B 2 882 ? -2.36800  12.47700  42.42400 1.000 87.33990  ? 882 ILE A CA    1 
ATOM 7305 C C     . ILE B 2 882 ? -2.78900  11.37800  41.43800 1.000 99.00033  ? 882 ILE A C     1 
ATOM 7306 O O     . ILE B 2 882 ? -2.84000  11.67600  40.22800 1.000 97.61203  ? 882 ILE A O     1 
ATOM 7307 C CB    . ILE B 2 882 ? -0.83700  12.58700  42.54600 1.000 87.41131  ? 882 ILE A CB    1 
ATOM 7308 C CG1   . ILE B 2 882 ? -0.42300  13.34400  43.80300 1.000 103.19729 ? 882 ILE A CG1   1 
ATOM 7309 C CG2   . ILE B 2 882 ? -0.23400  13.21800  41.29300 1.000 88.59872  ? 882 ILE A CG2   1 
ATOM 7310 C CD1   . ILE B 2 882 ? 1.07300   13.56500  43.92400 1.000 97.78515  ? 882 ILE A CD1   1 
ATOM 7311 N N     . GLN B 2 883 ? -3.08500  10.16000  41.91200 1.000 99.77036  ? 883 GLN A N     1 
ATOM 7312 C CA    . GLN B 2 883 ? -3.44600  9.16500   40.90600 1.000 94.74190  ? 883 GLN A CA    1 
ATOM 7313 C C     . GLN B 2 883 ? -4.76300  9.51500   40.22100 1.000 98.75382  ? 883 GLN A C     1 
ATOM 7314 O O     . GLN B 2 883 ? -4.88300  9.38900   38.99500 1.000 108.32803 ? 883 GLN A O     1 
ATOM 7315 C CB    . GLN B 2 883 ? -3.51500  7.77700   41.54300 1.000 112.99907 ? 883 GLN A CB    1 
ATOM 7316 C CG    . GLN B 2 883 ? -2.19100  7.01800   41.52800 1.000 121.03775 ? 883 GLN A CG    1 
ATOM 7317 C CD    . GLN B 2 883 ? -1.08600  7.73100   42.28600 1.000 119.98945 ? 883 GLN A CD    1 
ATOM 7318 O OE1   . GLN B 2 883 ? -1.30600  8.26500   43.37400 1.000 110.61036 ? 883 GLN A OE1   1 
ATOM 7319 N NE2   . GLN B 2 883 ? 0.11100   7.74300   41.71100 1.000 130.12071 ? 883 GLN A NE2   1 
ATOM 7320 N N     . GLN B 2 884 ? -5.76400  9.95400   40.99300 1.000 101.59281 ? 884 GLN A N     1 
ATOM 7321 C CA    . GLN B 2 884 ? -6.99200  10.46200  40.38600 1.000 93.74312  ? 884 GLN A CA    1 
ATOM 7322 C C     . GLN B 2 884 ? -6.68800  11.59000  39.41000 1.000 96.97004  ? 884 GLN A C     1 
ATOM 7323 O O     . GLN B 2 884 ? -7.31700  11.69600  38.35000 1.000 97.53423  ? 884 GLN A O     1 
ATOM 7324 C CB    . GLN B 2 884 ? -7.96600  10.95000  41.46300 1.000 90.98512  ? 884 GLN A CB    1 
ATOM 7325 C CG    . GLN B 2 884 ? -8.73100  9.86000   42.19500 1.000 92.25977  ? 884 GLN A CG    1 
ATOM 7326 C CD    . GLN B 2 884 ? -8.15700  9.57000   43.56200 1.000 117.77166 ? 884 GLN A CD    1 
ATOM 7327 O OE1   . GLN B 2 884 ? -6.95900  9.33900   43.70300 1.000 135.38799 ? 884 GLN A OE1   1 
ATOM 7328 N NE2   . GLN B 2 884 ? -9.00900  9.58500   44.58100 1.000 97.83973  ? 884 GLN A NE2   1 
ATOM 7329 N N     . PHE B 2 885 ? -5.71600  12.43900  39.75400 1.000 92.08259  ? 885 PHE A N     1 
ATOM 7330 C CA    . PHE B 2 885 ? -5.30600  13.52000  38.86400 1.000 87.61874  ? 885 PHE A CA    1 
ATOM 7331 C C     . PHE B 2 885 ? -4.67700  12.97400  37.58600 1.000 94.61016  ? 885 PHE A C     1 
ATOM 7332 O O     . PHE B 2 885 ? -4.91000  13.50600  36.49500 1.000 96.86317  ? 885 PHE A O     1 
ATOM 7333 C CB    . PHE B 2 885 ? -4.33400  14.44700  39.59900 1.000 87.44538  ? 885 PHE A CB    1 
ATOM 7334 C CG    . PHE B 2 885 ? -3.84100  15.60900  38.77700 1.000 88.16499  ? 885 PHE A CG    1 
ATOM 7335 C CD1   . PHE B 2 885 ? -4.61000  16.14700  37.75800 1.000 100.33686 ? 885 PHE A CD1   1 
ATOM 7336 C CD2   . PHE B 2 885 ? -2.61000  16.18000  39.04600 1.000 83.64803  ? 885 PHE A CD2   1 
ATOM 7337 C CE1   . PHE B 2 885 ? -4.15000  17.21100  37.01000 1.000 84.67245  ? 885 PHE A CE1   1 
ATOM 7338 C CE2   . PHE B 2 885 ? -2.14800  17.24800  38.30400 1.000 82.05884  ? 885 PHE A CE2   1 
ATOM 7339 C CZ    . PHE B 2 885 ? -2.91900  17.76400  37.28500 1.000 82.35828  ? 885 PHE A CZ    1 
ATOM 7340 N N     . GLY B 2 886 ? -3.86900  11.92200  37.69900 1.000 90.59034  ? 886 GLY A N     1 
ATOM 7341 C CA    . GLY B 2 886 ? -3.30900  11.31200  36.50600 1.000 94.55602  ? 886 GLY A CA    1 
ATOM 7342 C C     . GLY B 2 886 ? -4.38300  10.76000  35.59100 1.000 99.26285  ? 886 GLY A C     1 
ATOM 7343 O O     . GLY B 2 886 ? -4.41300  11.06000  34.39200 1.000 98.64394  ? 886 GLY A O     1 
ATOM 7344 N N     . LYS B 2 887 ? -5.29400  9.99800   36.17900 1.000 109.27697 ? 887 LYS A N     1 
ATOM 7345 C CA    . LYS B 2 887 ? -6.38100  9.38700   35.39100 1.000 116.09065 ? 887 LYS A CA    1 
ATOM 7346 C C     . LYS B 2 887 ? -7.16100  10.49800  34.69800 1.000 111.07563 ? 887 LYS A C     1 
ATOM 7347 O O     . LYS B 2 887 ? -7.39000  10.39000  33.49800 1.000 122.16858 ? 887 LYS A O     1 
ATOM 7348 C CB    . LYS B 2 887 ? -7.31000  8.62900   36.33400 1.000 105.55967 ? 887 LYS A CB    1 
ATOM 7349 C CG    . LYS B 2 887 ? -6.67400  7.47800   37.09500 1.000 108.68334 ? 887 LYS A CG    1 
ATOM 7350 C CD    . LYS B 2 887 ? -7.01900  6.13600   36.50900 1.000 125.23194 ? 887 LYS A CD    1 
ATOM 7351 C CE    . LYS B 2 887 ? -7.06900  5.03400   37.54500 1.000 148.91178 ? 887 LYS A CE    1 
ATOM 7352 N NZ    . LYS B 2 887 ? -8.18400  5.22900   38.50200 1.000 127.25889 ? 887 LYS A NZ    1 
ATOM 7353 N N     . LEU B 2 888 ? -7.47500  11.57100  35.42400 1.000 103.90731 ? 888 LEU A N     1 
ATOM 7354 C CA    . LEU B 2 888 ? -8.22700  12.70600  34.83000 1.000 103.81249 ? 888 LEU A CA    1 
ATOM 7355 C C     . LEU B 2 888 ? -7.48100  13.22600  33.59400 1.000 115.87789 ? 888 LEU A C     1 
ATOM 7356 O O     . LEU B 2 888 ? -8.09200  13.26100  32.50700 1.000 123.85884 ? 888 LEU A O     1 
ATOM 7357 C CB    . LEU B 2 888 ? -8.40800  13.80900  35.86900 1.000 101.83139 ? 888 LEU A CB    1 
ATOM 7358 C CG    . LEU B 2 888 ? -9.06200  15.09900  35.36600 1.000 100.88071 ? 888 LEU A CG    1 
ATOM 7359 C CD1   . LEU B 2 888 ? -10.47900 14.83400  34.89000 1.000 101.52496 ? 888 LEU A CD1   1 
ATOM 7360 C CD2   . LEU B 2 888 ? -9.04700  16.17100  36.44100 1.000 97.84175  ? 888 LEU A CD2   1 
ATOM 7361 N N     . LEU B 2 889 ? -6.21100  13.60100  33.75400 1.000 120.79398 ? 889 LEU A N     1 
ATOM 7362 C CA    . LEU B 2 889 ? -5.44800  14.20100  32.62900 1.000 109.43487 ? 889 LEU A CA    1 
ATOM 7363 C C     . LEU B 2 889 ? -5.51800  13.28100  31.40500 1.000 113.19887 ? 889 LEU A C     1 
ATOM 7364 O O     . LEU B 2 889 ? -5.82700  13.78100  30.30500 1.000 128.00559 ? 889 LEU A O     1 
ATOM 7365 C CB    . LEU B 2 889 ? -4.00300  14.42500  33.06400 1.000 105.51434 ? 889 LEU A CB    1 
ATOM 7366 C CG    . LEU B 2 889 ? -3.71800  15.73200  33.80600 1.000 101.12910 ? 889 LEU A CG    1 
ATOM 7367 C CD1   . LEU B 2 889 ? -2.30100  15.69900  34.34300 1.000 104.82275 ? 889 LEU A CD1   1 
ATOM 7368 C CD2   . LEU B 2 889 ? -3.89200  16.89100  32.84300 1.000 100.95197 ? 889 LEU A CD2   1 
ATOM 7369 N N     . ARG B 2 890 ? -5.24900  11.99100  31.59700 1.000 127.83042 ? 890 ARG A N     1 
ATOM 7370 C CA    . ARG B 2 890 ? -5.22800  11.05400  30.44700 1.000 131.38322 ? 890 ARG A CA    1 
ATOM 7371 C C     . ARG B 2 890 ? -6.57700  11.13800  29.72400 1.000 132.61827 ? 890 ARG A C     1 
ATOM 7372 O O     . ARG B 2 890 ? -6.57900  11.27400  28.48800 1.000 132.88682 ? 890 ARG A O     1 
ATOM 7373 C CB    . ARG B 2 890 ? -4.94300  9.63300   30.94000 1.000 120.53005 ? 890 ARG A CB    1 
ATOM 7374 C CG    . ARG B 2 890 ? -3.60300  9.50800   31.64900 1.000 113.84861 ? 890 ARG A CG    1 
ATOM 7375 C CD    . ARG B 2 890 ? -3.41000  8.13500   32.26700 1.000 119.06904 ? 890 ARG A CD    1 
ATOM 7376 N NE    . ARG B 2 890 ? -2.19600  8.08100   33.08700 1.000 121.41656 ? 890 ARG A NE    1 
ATOM 7377 C CZ    . ARG B 2 890 ? -2.18500  7.82000   34.38700 1.000 128.57783 ? 890 ARG A CZ    1 
ATOM 7378 N NH1   . ARG B 2 890 ? -3.30300  7.47100   34.99900 1.000 122.32226 ? 890 ARG A NH1   1 
ATOM 7379 N NH2   . ARG B 2 890 ? -1.05800  7.90600   35.07000 1.000 140.61815 ? 890 ARG A NH2   1 
ATOM 7380 N N     . GLN B 2 891 ? -7.67600  11.08800  30.47700 1.000 135.22961 ? 891 GLN A N     1 
ATOM 7381 C CA    . GLN B 2 891 ? -9.01800  11.10300  29.84800 1.000 134.26620 ? 891 GLN A CA    1 
ATOM 7382 C C     . GLN B 2 891 ? -9.13200  12.34000  28.95700 1.000 132.45546 ? 891 GLN A C     1 
ATOM 7383 O O     . GLN B 2 891 ? -9.52400  12.19500  27.78100 1.000 144.86191 ? 891 GLN A O     1 
ATOM 7384 C CB    . GLN B 2 891 ? -10.10600 11.16600  30.91700 1.000 144.72402 ? 891 GLN A CB    1 
ATOM 7385 C CG    . GLN B 2 891 ? -10.08000 10.00200  31.90200 1.000 158.34602 ? 891 GLN A CG    1 
ATOM 7386 C CD    . GLN B 2 891 ? -10.96100 10.22800  33.11200 1.000 134.53705 ? 891 GLN A CD    1 
ATOM 7387 O OE1   . GLN B 2 891 ? -11.05600 9.38400   34.00900 1.000 112.61451 ? 891 GLN A OE1   1 
ATOM 7388 N NE2   . GLN B 2 891 ? -11.61600 11.37900  33.14800 1.000 108.58832 ? 891 GLN A NE2   1 
ATOM 7389 N N     . ILE B 2 892 ? -8.78000  13.50600  29.49700 1.000 121.87050 ? 892 ILE A N     1 
ATOM 7390 C CA    . ILE B 2 892 ? -8.93400  14.77300  28.72500 1.000 121.58227 ? 892 ILE A CA    1 
ATOM 7391 C C     . ILE B 2 892 ? -8.03400  14.71200  27.48300 1.000 133.12235 ? 892 ILE A C     1 
ATOM 7392 O O     . ILE B 2 892 ? -8.49000  15.12700  26.39900 1.000 142.52555 ? 892 ILE A O     1 
ATOM 7393 C CB    . ILE B 2 892 ? -8.60300  15.97400  29.62300 1.000 118.29212 ? 892 ILE A CB    1 
ATOM 7394 C CG1   . ILE B 2 892 ? -9.22600  15.80800  31.00400 1.000 121.31926 ? 892 ILE A CG1   1 
ATOM 7395 C CG2   . ILE B 2 892 ? -9.03200  17.28100  28.96200 1.000 130.09369 ? 892 ILE A CG2   1 
ATOM 7396 C CD1   . ILE B 2 892 ? -8.80600  16.86500  32.00500 1.000 115.04482 ? 892 ILE A CD1   1 
ATOM 7397 N N     . GLN B 2 893 ? -6.80900  14.21000  27.64100 1.000 131.00378 ? 893 GLN A N     1 
ATOM 7398 C CA    . GLN B 2 893 ? -5.85800  14.13500  26.50200 1.000 133.17616 ? 893 GLN A CA    1 
ATOM 7399 C C     . GLN B 2 893 ? -6.37200  13.11400  25.47700 1.000 151.59721 ? 893 GLN A C     1 
ATOM 7400 O O     . GLN B 2 893 ? -6.20100  13.35900  24.26500 1.000 164.63110 ? 893 GLN A O     1 
ATOM 7401 C CB    . GLN B 2 893 ? -4.46900  13.75900  27.01800 1.000 140.39199 ? 893 GLN A CB    1 
ATOM 7402 C CG    . GLN B 2 893 ? -3.35500  13.94300  25.99500 1.000 148.05597 ? 893 GLN A CG    1 
ATOM 7403 C CD    . GLN B 2 893 ? -3.23100  15.36800  25.50200 1.000 149.26712 ? 893 GLN A CD    1 
ATOM 7404 O OE1   . GLN B 2 893 ? -3.35800  15.65000  24.30500 1.000 163.49843 ? 893 GLN A OE1   1 
ATOM 7405 N NE2   . GLN B 2 893 ? -2.98100  16.28400  26.42500 1.000 136.69384 ? 893 GLN A NE2   1 
ATOM 7406 N N     . LYS B 2 894 ? -6.98700  12.02400  25.94400 1.000 156.39000 ? 894 LYS A N     1 
ATOM 7407 C CA    . LYS B 2 894 ? -7.45600  10.95000  25.02800 1.000 151.68722 ? 894 LYS A CA    1 
ATOM 7408 C C     . LYS B 2 894 ? -8.89500  11.23500  24.57800 1.000 149.60820 ? 894 LYS A C     1 
ATOM 7409 O O     . LYS B 2 894 ? -9.53800  10.31000  24.04100 1.000 152.36578 ? 894 LYS A O     1 
ATOM 7410 C CB    . LYS B 2 894 ? -7.41000  9.58500   25.72000 1.000 152.70038 ? 894 LYS A CB    1 
ATOM 7411 C CG    . LYS B 2 894 ? -6.03500  9.15000   26.20700 1.000 161.56546 ? 894 LYS A CG    1 
ATOM 7412 C CD    . LYS B 2 894 ? -6.09100  7.94500   27.13800 1.000 172.16434 ? 894 LYS A CD    1 
ATOM 7413 C CE    . LYS B 2 894 ? -4.75000  7.57700   27.69000 1.000 160.71721 ? 894 LYS A CE    1 
ATOM 7414 N NZ    . LYS B 2 894 ? -4.84100  6.45300   28.62500 1.000 154.25357 ? 894 LYS A NZ    1 
ATOM 7415 N N     . LYS B 2 895 ? -9.37500  12.46400  24.78200 1.000 146.00655 ? 895 LYS A N     1 
ATOM 7416 C CA    . LYS B 2 895 ? -10.73900 12.82700  24.31600 1.000 159.25421 ? 895 LYS A CA    1 
ATOM 7417 C C     . LYS B 2 895 ? -10.77300 12.79800  22.77900 1.000 175.40674 ? 895 LYS A C     1 
ATOM 7418 O O     . LYS B 2 895 ? -11.88800 12.84200  22.21600 1.000 186.27677 ? 895 LYS A O     1 
ATOM 7419 C CB    . LYS B 2 895 ? -11.18400 14.18500  24.87200 1.000 140.24606 ? 895 LYS A CB    1 
ATOM 7420 C CG    . LYS B 2 895 ? -11.71600 14.11600  26.29600 1.000 151.69975 ? 895 LYS A CG    1 
ATOM 7421 C CD    . LYS B 2 895 ? -12.32800 15.41500  26.80400 1.000 155.07494 ? 895 LYS A CD    1 
ATOM 7422 C CE    . LYS B 2 895 ? -12.77900 15.31100  28.22600 1.000 156.01454 ? 895 LYS A CE    1 
ATOM 7423 N NZ    . LYS B 2 895 ? -13.32400 16.57800  28.71900 1.000 141.78670 ? 895 LYS A NZ    1 
ATOM 7424 N N     . LYS B 2 896 ? -9.60400  12.73000  22.13400 1.000 166.74124 ? 896 LYS A N     1 
ATOM 7425 C CA    . LYS B 2 896 ? -9.54600  12.64600  20.65100 1.000 163.99155 ? 896 LYS A CA    1 
ATOM 7426 C C     . LYS B 2 896 ? -10.52500 13.66600  20.04700 1.000 165.54754 ? 896 LYS A C     1 
ATOM 7427 O O     . LYS B 2 896 ? -11.41400 13.22200  19.28800 1.000 155.03340 ? 896 LYS A O     1 
ATOM 7428 C CB    . LYS B 2 896 ? -9.89200  11.22800  20.18600 1.000 157.49093 ? 896 LYS A CB    1 
ATOM 7429 C CG    . LYS B 2 896 ? -9.00700  10.12400  20.74500 1.000 154.20668 ? 896 LYS A CG    1 
ATOM 7430 C CD    . LYS B 2 896 ? -9.46600  8.73700   20.31300 1.000 162.46729 ? 896 LYS A CD    1 
ATOM 7431 C CE    . LYS B 2 896 ? -8.61800  7.64400   20.87800 1.000 180.44172 ? 896 LYS A CE    1 
ATOM 7432 N NZ    . LYS B 2 896 ? -9.09100  6.32500   20.45200 1.000 170.44036 ? 896 LYS A NZ    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    P P     . DT  A 1   ? 1.97174 2.03294 2.30470 -0.05360 0.07873  0.11531  2   DT  B P     
2    O OP1   . DT  A 1   ? 1.78941 1.85316 2.14673 -0.05208 0.07632  0.11732  2   DT  B OP1   
3    O OP2   . DT  A 1   ? 1.47838 1.53500 1.78834 -0.05345 0.08889  0.11952  2   DT  B OP2   
4    O "O5'" . DT  A 1   ? 1.72487 1.78762 2.06834 -0.05492 0.07790  0.12256  2   DT  B "O5'" 
5    C "C5'" . DT  A 1   ? 1.26225 1.32779 1.61962 -0.05571 0.06906  0.11766  2   DT  B "C5'" 
6    C "C4'" . DT  A 1   ? 1.27420 1.33880 1.61311 -0.05672 0.06612  0.10823  2   DT  B "C4'" 
7    O "O4'" . DT  A 1   ? 1.60751 1.66875 1.92009 -0.05786 0.07266  0.11122  2   DT  B "O4'" 
8    C "C3'" . DT  A 1   ? 1.46929 1.53598 1.81712 -0.05785 0.06034  0.10629  2   DT  B "C3'" 
9    O "O3'" . DT  A 1   ? 1.34994 1.41656 1.68646 -0.05817 0.05702  0.09551  2   DT  B "O3'" 
10   C "C2'" . DT  A 1   ? 1.47315 1.53863 1.80909 -0.05978 0.06478  0.11612  2   DT  B "C2'" 
11   C "C1'" . DT  A 1   ? 1.61520 1.67658 1.92451 -0.06002 0.07217  0.11669  2   DT  B "C1'" 
12   N N1    . DT  A 1   ? 1.89581 1.95442 2.19779 -0.06099 0.07977  0.12803  2   DT  B N1    
13   C C2    . DT  A 1   ? 1.94373 1.99814 2.22928 -0.06022 0.08798  0.12927  2   DT  B C2    
14   O O2    . DT  A 1   ? 1.68875 1.74187 1.96562 -0.05886 0.08869  0.12202  2   DT  B O2    
15   N N3    . DT  A 1   ? 1.97740 2.02868 2.25627 -0.06127 0.09581  0.13952  2   DT  B N3    
16   C C4    . DT  A 1   ? 1.91357 1.96588 2.19990 -0.06335 0.09562  0.14913  2   DT  B C4    
17   O O4    . DT  A 1   ? 1.73836 1.78707 2.01530 -0.06449 0.10379  0.15784  2   DT  B O4    
18   C C5    . DT  A 1   ? 1.86259 1.91993 2.16782 -0.06408 0.08586  0.14804  2   DT  B C5    
19   C C7    . DT  A 1   ? 1.65262 1.71160 1.96850 -0.06649 0.08436  0.15902  2   DT  B C7    
20   C C6    . DT  A 1   ? 1.73039 1.79040 2.04284 -0.06268 0.07888  0.13736  2   DT  B C6    
21   P P     . DT  A 2   ? 1.19521 1.26409 1.54295 -0.05867 0.05111  0.09038  3   DT  B P     
22   O OP1   . DT  A 2   ? 1.37356 1.44329 1.74298 -0.05749 0.04529  0.08263  3   DT  B OP1   
23   O OP2   . DT  A 2   ? 0.97182 1.04194 1.32483 -0.06014 0.05114  0.09994  3   DT  B OP2   
24   O "O5'" . DT  A 2   ? 1.25358 1.32165 1.57787 -0.05936 0.05179  0.08179  3   DT  B "O5'" 
25   C "C5'" . DT  A 2   ? 0.95497 1.02130 1.26498 -0.05882 0.05317  0.07501  3   DT  B "C5'" 
26   C "C4'" . DT  A 2   ? 1.07128 1.13713 1.35944 -0.05993 0.05426  0.06945  3   DT  B "C4'" 
27   O "O4'" . DT  A 2   ? 1.31059 1.37418 1.57984 -0.06132 0.05923  0.07693  3   DT  B "O4'" 
28   C "C3'" . DT  A 2   ? 1.30386 1.37222 1.59836 -0.06050 0.05103  0.06558  3   DT  B "C3'" 
29   O "O3'" . DT  A 2   ? 1.27746 1.34660 1.58070 -0.05953 0.04754  0.05448  3   DT  B "O3'" 
30   C "C2'" . DT  A 2   ? 1.45706 1.52470 1.72786 -0.06225 0.05366  0.06583  3   DT  B "C2'" 
31   C "C1'" . DT  A 2   ? 1.29691 1.36098 1.55255 -0.06299 0.05856  0.07404  3   DT  B "C1'" 
32   N N1    . DT  A 2   ? 1.44398 1.50701 1.69332 -0.06527 0.06006  0.08387  3   DT  B N1    
33   C C2    . DT  A 2   ? 1.48811 1.55185 1.75284 -0.06544 0.05963  0.09274  3   DT  B C2    
34   O O2    . DT  A 2   ? 1.50481 1.57019 1.79008 -0.06356 0.05810  0.09301  3   DT  B O2    
35   N N3    . DT  A 2   ? 1.44700 1.50926 1.70213 -0.06840 0.06053  0.10181  3   DT  B N3    
36   C C4    . DT  A 2   ? 1.52392 1.58368 1.75618 -0.07131 0.06138  0.10265  3   DT  B C4    
37   O O4    . DT  A 2   ? 1.59869 1.65667 1.82341 -0.07458 0.06125  0.11155  3   DT  B O4    
38   C C5    . DT  A 2   ? 1.64184 1.70109 1.86037 -0.07071 0.06188  0.09301  3   DT  B C5    
39   C C7    . DT  A 2   ? 1.44882 1.50523 1.64344 -0.07400 0.06238  0.09347  3   DT  B C7    
40   C C6    . DT  A 2   ? 1.49869 1.55975 1.72619 -0.06771 0.06141  0.08439  3   DT  B C6    
41   P P     . DT  A 3   ? 1.17966 1.25111 1.49420 -0.05932 0.04502  0.04827  4   DT  B P     
42   O OP1   . DT  A 3   ? 1.12603 1.19655 1.45096 -0.05835 0.04214  0.03660  4   DT  B OP1   
43   O OP2   . DT  A 3   ? 0.99414 1.06757 1.32562 -0.05948 0.04381  0.05712  4   DT  B OP2   
44   O "O5'" . DT  A 3   ? 1.30024 1.37249 1.59241 -0.06061 0.04750  0.04529  4   DT  B "O5'" 
45   C "C5'" . DT  A 3   ? 1.36775 1.44270 1.66610 -0.06060 0.04679  0.04085  4   DT  B "C5'" 
46   C "C4'" . DT  A 3   ? 1.34910 1.42520 1.62938 -0.06255 0.04870  0.04490  4   DT  B "C4'" 
47   O "O4'" . DT  A 3   ? 1.39411 1.46840 1.66556 -0.06409 0.04966  0.05618  4   DT  B "O4'" 
48   C "C3'" . DT  A 3   ? 1.31429 1.39416 1.60611 -0.06288 0.04752  0.04568  4   DT  B "C3'" 
49   O "O3'" . DT  A 3   ? 1.62071 1.70213 1.90183 -0.06314 0.04934  0.03764  4   DT  B "O3'" 
50   C "C2'" . DT  A 3   ? 1.34553 1.42571 1.63203 -0.06541 0.04662  0.05848  4   DT  B "C2'" 
51   C "C1'" . DT  A 3   ? 1.34408 1.41996 1.61174 -0.06635 0.04890  0.06296  4   DT  B "C1'" 
52   N N1    . DT  A 3   ? 1.38478 1.45928 1.65559 -0.06782 0.04836  0.07513  4   DT  B N1    
53   C C2    . DT  A 3   ? 1.47506 1.54939 1.76400 -0.06620 0.04761  0.07827  4   DT  B C2    
54   O O2    . DT  A 3   ? 1.47190 1.54678 1.77515 -0.06372 0.04671  0.07127  4   DT  B O2    
55   N N3    . DT  A 3   ? 1.49126 1.56440 1.78074 -0.06803 0.04771  0.09020  4   DT  B N3    
56   C C4    . DT  A 3   ? 1.53434 1.60569 1.80672 -0.07162 0.04820  0.09874  4   DT  B C4    
57   O O4    . DT  A 3   ? 1.59375 1.66359 1.86695 -0.07342 0.04846  0.10919  4   DT  B O4    
58   C C5    . DT  A 3   ? 1.49732 1.56841 1.75122 -0.07337 0.04825  0.09457  4   DT  B C5    
59   C C7    . DT  A 3   ? 1.60395 1.67216 1.83773 -0.07798 0.04784  0.10307  4   DT  B C7    
60   C C6    . DT  A 3   ? 1.34152 1.41455 1.59637 -0.07125 0.04848  0.08337  4   DT  B C6    
61   P P     . DT  A 4   ? 1.99206 2.07413 2.28259 -0.06108 0.05044  0.02417  5   DT  B P     
62   O OP1   . DT  A 4   ? 1.56816 1.65236 1.84525 -0.06187 0.05329  0.01806  5   DT  B OP1   
63   O OP2   . DT  A 4   ? 1.39377 1.47210 1.68279 -0.06016 0.04978  0.01770  5   DT  B OP2   
64   O "O5'" . DT  A 4   ? 1.71780 1.80211 2.03843 -0.05934 0.04889  0.02498  5   DT  B "O5'" 
65   C "C5'" . DT  A 4   ? 1.56191 1.64983 1.89313 -0.06033 0.04725  0.03525  5   DT  B "C5'" 
66   C "C4'" . DT  A 4   ? 1.67489 1.76622 1.99677 -0.06152 0.04920  0.03391  5   DT  B "C4'" 
67   O "O4'" . DT  A 4   ? 1.68617 1.77646 1.98274 -0.06446 0.04902  0.03999  5   DT  B "O4'" 
68   C "C3'" . DT  A 4   ? 1.62517 1.72121 1.96717 -0.06183 0.04738  0.04079  5   DT  B "C3'" 
69   O "O3'" . DT  A 4   ? 1.65504 1.75281 2.01873 -0.05884 0.04983  0.03206  5   DT  B "O3'" 
70   C "C2'" . DT  A 4   ? 1.54665 1.64513 1.87050 -0.06467 0.04784  0.04417  5   DT  B "C2'" 
71   C "C1'" . DT  A 4   ? 1.79896 1.89303 2.09310 -0.06638 0.04877  0.04360  5   DT  B "C1'" 
72   N N1    . DT  A 4   ? 1.97437 2.06698 2.25352 -0.07008 0.04598  0.05535  5   DT  B N1    
73   C C2    . DT  A 4   ? 1.90181 1.99193 2.18460 -0.07087 0.04348  0.06423  5   DT  B C2    
74   O O2    . DT  A 4   ? 1.82982 1.91950 2.12984 -0.06857 0.04295  0.06365  5   DT  B O2    
75   N N3    . DT  A 4   ? 1.83166 1.91941 2.09706 -0.07482 0.04164  0.07409  5   DT  B N3    
76   C C4    . DT  A 4   ? 1.65870 1.74590 1.90414 -0.07810 0.04142  0.07572  5   DT  B C4    
77   O O4    . DT  A 4   ? 1.48955 1.57316 1.71914 -0.08196 0.03958  0.08442  5   DT  B O4    
78   C C5    . DT  A 4   ? 1.71442 1.80493 1.95886 -0.07694 0.04366  0.06664  5   DT  B C5    
79   C C7    . DT  A 4   ? 1.34437 1.43466 1.56911 -0.08052 0.04323  0.06824  5   DT  B C7    
80   C C6    . DT  A 4   ? 1.77772 1.87086 2.03842 -0.07300 0.04615  0.05709  5   DT  B C6    
81   N N     . MET B 1   ? 2.32567 2.62961 1.79674 -0.29047 0.45492  0.10437  1   MET A N     
82   C CA    . MET B 1   ? 2.46789 2.76802 1.95848 -0.28048 0.46212  0.08670  1   MET A CA    
83   C C     . MET B 1   ? 2.52929 2.81432 1.97809 -0.28256 0.46665  0.06767  1   MET A C     
84   O O     . MET B 1   ? 2.50515 2.77943 1.92210 -0.28856 0.44833  0.06727  1   MET A O     
85   C CB    . MET B 1   ? 2.35122 2.65017 1.87622 -0.27325 0.43895  0.08908  1   MET A CB    
86   C CG    . MET B 1   ? 2.27603 2.58885 1.85191 -0.26759 0.43917  0.10139  1   MET A CG    
87   S SD    . MET B 1   ? 2.25943 2.56853 1.86808 -0.26079 0.41056  0.10426  1   MET A SD    
88   C CE    . MET B 1   ? 2.34923 2.67460 2.01510 -0.25443 0.41824  0.11516  1   MET A CE    
89   N N     . GLY B 2   ? 2.54942 2.83214 2.00168 -0.27596 0.48892  0.05226  2   GLY A N     
90   C CA    . GLY B 2   ? 2.29832 2.56461 1.71850 -0.27504 0.49083  0.03246  2   GLY A CA    
91   C C     . GLY B 2   ? 2.45999 2.71940 1.88867 -0.27208 0.47251  0.02451  2   GLY A C     
92   O O     . GLY B 2   ? 2.43644 2.70222 1.90951 -0.26332 0.46520  0.02790  2   GLY A O     
93   N N     . MET B 3   ? 2.49818 2.74272 1.88749 -0.27723 0.46142  0.01481  3   MET A N     
94   C CA    . MET B 3   ? 2.25526 2.49093 1.65411 -0.27232 0.43971  0.00839  3   MET A CA    
95   C C     . MET B 3   ? 2.23679 2.47173 1.66843 -0.26041 0.45074  -0.00666 3   MET A C     
96   O O     . MET B 3   ? 2.32450 2.55693 1.74947 -0.25822 0.47414  -0.02043 3   MET A O     
97   C CB    . MET B 3   ? 2.15374 2.37357 1.50336 -0.28066 0.42778  0.00022  3   MET A CB    
98   C CG    . MET B 3   ? 2.18741 2.40754 1.50599 -0.29268 0.41361  0.01630  3   MET A CG    
99   S SD    . MET B 3   ? 2.23897 2.44078 1.50576 -0.30222 0.39397  0.00943  3   MET A SD    
100  C CE    . MET B 3   ? 2.12946 2.32890 1.42732 -0.29560 0.36471  0.01288  3   MET A CE    
101  N N     . ALA B 4   ? 2.10339 2.34019 1.57076 -0.25281 0.43390  -0.00373 4   ALA A N     
102  C CA    . ALA B 4   ? 2.05523 2.29389 1.56125 -0.24124 0.44211  -0.01402 4   ALA A CA    
103  C C     . ALA B 4   ? 2.12619 2.35078 1.61217 -0.23904 0.44951  -0.03572 4   ALA A C     
104  O O     . ALA B 4   ? 2.05794 2.26972 1.50847 -0.24465 0.43704  -0.04204 4   ALA A O     
105  C CB    . ALA B 4   ? 1.98548 2.22722 1.52769 -0.23508 0.41974  -0.00591 4   ALA A CB    
106  N N     . THR B 5   ? 2.20046 2.42742 1.71110 -0.23084 0.46978  -0.04682 5   THR A N     
107  C CA    . THR B 5   ? 2.15314 2.36732 1.65361 -0.22695 0.47837  -0.06794 5   THR A CA    
108  C C     . THR B 5   ? 2.05314 2.26821 1.59679 -0.21608 0.46895  -0.07155 5   THR A C     
109  O O     . THR B 5   ? 2.05540 2.28301 1.64319 -0.20911 0.47304  -0.06349 5   THR A O     
110  C CB    . THR B 5   ? 2.19765 2.41245 1.69284 -0.22573 0.51049  -0.07916 5   THR A CB    
111  O OG1   . THR B 5   ? 2.26900 2.48397 1.72425 -0.23628 0.51946  -0.07407 5   THR A OG1   
112  C CG2   . THR B 5   ? 2.13002 2.32931 1.60974 -0.22277 0.51923  -0.10199 5   THR A CG2   
113  N N     . TYR B 6   ? 2.05454 2.25637 1.58549 -0.21509 0.45598  -0.08306 6   TYR A N     
114  C CA    . TYR B 6   ? 2.01786 2.21872 1.58518 -0.20549 0.44607  -0.08739 6   TYR A CA    
115  C C     . TYR B 6   ? 2.06864 2.26314 1.64481 -0.19886 0.46587  -0.10643 6   TYR A C     
116  O O     . TYR B 6   ? 2.23795 2.41928 1.77826 -0.20291 0.47374  -0.12142 6   TYR A O     
117  C CB    . TYR B 6   ? 2.04911 2.23968 1.60041 -0.20808 0.41930  -0.08759 6   TYR A CB    
118  C CG    . TYR B 6   ? 2.08515 2.28057 1.62798 -0.21442 0.39943  -0.06948 6   TYR A CG    
119  C CD1   . TYR B 6   ? 2.03379 2.23839 1.61244 -0.20983 0.38548  -0.05587 6   TYR A CD1   
120  C CD2   . TYR B 6   ? 2.10172 2.29205 1.60055 -0.22532 0.39467  -0.06582 6   TYR A CD2   
121  C CE1   . TYR B 6   ? 1.98096 2.18909 1.55291 -0.21536 0.36812  -0.03990 6   TYR A CE1   
122  C CE2   . TYR B 6   ? 1.95413 2.14885 1.44740 -0.23094 0.37656  -0.04875 6   TYR A CE2   
123  C CZ    . TYR B 6   ? 1.95351 2.15692 1.48396 -0.22567 0.36370  -0.03616 6   TYR A CZ    
124  O OH    . TYR B 6   ? 1.92655 2.13336 1.45238 -0.23102 0.34626  -0.01974 6   TYR A OH    
125  N N     . ALA B 7   ? 1.94782 2.15117 1.57172 -0.18901 0.47349  -0.10563 7   ALA A N     
126  C CA    . ALA B 7   ? 1.94599 2.14378 1.58706 -0.18120 0.48970  -0.12253 7   ALA A CA    
127  C C     . ALA B 7   ? 1.98596 2.17812 1.64728 -0.17531 0.47015  -0.12601 7   ALA A C     
128  O O     . ALA B 7   ? 1.94731 2.14900 1.65067 -0.16871 0.46218  -0.11669 7   ALA A O     
129  C CB    . ALA B 7   ? 1.94705 2.15852 1.62939 -0.17426 0.51159  -0.11894 7   ALA A CB    
130  N N     . VAL B 8   ? 1.97730 2.15377 1.60778 -0.17828 0.46190  -0.13892 8   VAL A N     
131  C CA    . VAL B 8   ? 1.88619 2.05605 1.53277 -0.17317 0.44424  -0.14339 8   VAL A CA    
132  C C     . VAL B 8   ? 1.96151 2.12761 1.63396 -0.16439 0.46071  -0.15841 8   VAL A C     
133  O O     . VAL B 8   ? 2.03820 2.19273 1.68707 -0.16583 0.47554  -0.17513 8   VAL A O     
134  C CB    . VAL B 8   ? 1.89702 2.05215 1.50140 -0.18051 0.42683  -0.14940 8   VAL A CB    
135  C CG1   . VAL B 8   ? 2.05641 2.20619 1.68036 -0.17514 0.40809  -0.15198 8   VAL A CG1   
136  C CG2   . VAL B 8   ? 1.89988 2.05864 1.47783 -0.18967 0.41261  -0.13447 8   VAL A CG2   
137  N N     . VAL B 9   ? 2.05081 2.22595 1.77138 -0.15558 0.45767  -0.15245 9   VAL A N     
138  C CA    . VAL B 9   ? 2.02534 2.20101 1.78020 -0.14648 0.47494  -0.16266 9   VAL A CA    
139  C C     . VAL B 9   ? 2.07696 2.24562 1.85098 -0.14075 0.45984  -0.16824 9   VAL A C     
140  O O     . VAL B 9   ? 2.13867 2.30946 1.91948 -0.14110 0.43698  -0.15791 9   VAL A O     
141  C CB    . VAL B 9   ? 1.90594 2.09948 1.70546 -0.14103 0.48557  -0.14969 9   VAL A CB    
142  C CG1   . VAL B 9   ? 1.89135 2.08624 1.73138 -0.13121 0.50160  -0.15856 9   VAL A CG1   
143  C CG2   . VAL B 9   ? 1.92593 2.12665 1.70751 -0.14667 0.50196  -0.14417 9   VAL A CG2   
144  N N     . ASP B 10  ? 2.01685 2.17670 1.79938 -0.13555 0.47315  -0.18472 10  ASP A N     
145  C CA    . ASP B 10  ? 2.01679 2.17218 1.82727 -0.12856 0.46285  -0.18944 10  ASP A CA    
146  C C     . ASP B 10  ? 2.07100 2.22719 1.91592 -0.11996 0.48477  -0.19952 10  ASP A C     
147  O O     . ASP B 10  ? 2.19803 2.35070 2.03116 -0.12045 0.50820  -0.21026 10  ASP A O     
148  C CB    . ASP B 10  ? 2.03011 2.16835 1.80756 -0.13246 0.44937  -0.20146 10  ASP A CB    
149  C CG    . ASP B 10  ? 2.13537 2.26985 1.94320 -0.12538 0.43752  -0.20464 10  ASP A CG    
150  O OD1   . ASP B 10  ? 2.00802 2.14955 1.83524 -0.12373 0.41825  -0.19121 10  ASP A OD1   
151  O OD2   . ASP B 10  ? 2.22144 2.34526 2.03263 -0.12177 0.44756  -0.22070 10  ASP A OD2   
152  N N     . LEU B 11  ? 2.02826 2.18881 1.91608 -0.11216 0.47705  -0.19575 11  LEU A N     
153  C CA    . LEU B 11  ? 2.05455 2.21808 1.98384 -0.10321 0.49512  -0.20194 11  LEU A CA    
154  C C     . LEU B 11  ? 2.11505 2.26913 2.06163 -0.09783 0.48537  -0.21055 11  LEU A C     
155  O O     . LEU B 11  ? 2.23053 2.38377 2.17823 -0.09858 0.46198  -0.20353 11  LEU A O     
156  C CB    . LEU B 11  ? 1.97366 2.15639 1.94929 -0.09853 0.49708  -0.18437 11  LEU A CB    
157  C CG    . LEU B 11  ? 1.96278 2.15713 1.92814 -0.10352 0.50501  -0.17283 11  LEU A CG    
158  C CD1   . LEU B 11  ? 1.97859 2.19120 1.99175 -0.09927 0.50259  -0.15459 11  LEU A CD1   
159  C CD2   . LEU B 11  ? 1.99608 2.18638 1.94421 -0.10446 0.53358  -0.18556 11  LEU A CD2   
160  N N     . GLU B 12  ? 2.13494 2.28163 2.09519 -0.09242 0.50408  -0.22580 12  GLU A N     
161  C CA    . GLU B 12  ? 2.10025 2.24124 2.09100 -0.08534 0.49924  -0.23222 12  GLU A CA    
162  C C     . GLU B 12  ? 2.21806 2.37097 2.26415 -0.07632 0.51427  -0.22732 12  GLU A C     
163  O O     . GLU B 12  ? 2.28043 2.43689 2.33332 -0.07456 0.53841  -0.23158 12  GLU A O     
164  C CB    . GLU B 12  ? 2.03770 2.15853 2.00117 -0.08633 0.50723  -0.25466 12  GLU A CB    
165  C CG    . GLU B 12  ? 2.04689 2.15510 1.95655 -0.09567 0.49119  -0.25970 12  GLU A CG    
166  C CD    . GLU B 12  ? 2.12839 2.23665 2.04292 -0.09620 0.46234  -0.25045 12  GLU A CD    
167  O OE1   . GLU B 12  ? 2.26272 2.38053 2.22010 -0.08971 0.45434  -0.24003 12  GLU A OE1   
168  O OE2   . GLU B 12  ? 2.08808 2.18667 1.96343 -0.10337 0.44769  -0.25336 12  GLU A OE2   
169  N N     . THR B 13  ? 2.25071 2.40997 2.33652 -0.07090 0.49984  -0.21766 13  THR A N     
170  C CA    . THR B 13  ? 2.29094 2.46352 2.43286 -0.06301 0.50881  -0.20880 13  THR A CA    
171  C C     . THR B 13  ? 2.28920 2.45530 2.46345 -0.05584 0.50579  -0.21560 13  THR A C     
172  O O     . THR B 13  ? 2.22840 2.38141 2.38316 -0.05724 0.49326  -0.22437 13  THR A O     
173  C CB    . THR B 13  ? 2.20185 2.39161 2.36522 -0.06416 0.49261  -0.18578 13  THR A CB    
174  O OG1   . THR B 13  ? 2.22441 2.41100 2.38050 -0.06621 0.46570  -0.17938 13  THR A OG1   
175  C CG2   . THR B 13  ? 2.07202 2.26862 2.20649 -0.07110 0.49619  -0.17835 13  THR A CG2   
176  N N     . THR B 14  ? 2.26931 2.44503 2.49512 -0.04820 0.51736  -0.21082 14  THR A N     
177  C CA    . THR B 14  ? 2.23046 2.40265 2.49431 -0.04107 0.51337  -0.21376 14  THR A CA    
178  C C     . THR B 14  ? 2.06679 2.24456 2.34516 -0.04156 0.48512  -0.19846 14  THR A C     
179  O O     . THR B 14  ? 1.93365 2.10775 2.23907 -0.03669 0.47806  -0.19985 14  THR A O     
180  C CB    . THR B 14  ? 2.18955 2.37152 2.50713 -0.03293 0.53350  -0.21125 14  THR A CB    
181  O OG1   . THR B 14  ? 2.06290 2.26409 2.40626 -0.03336 0.52985  -0.19079 14  THR A OG1   
182  C CG2   . THR B 14  ? 2.13736 2.31172 2.44245 -0.03151 0.56365  -0.22858 14  THR A CG2   
183  N N     . GLY B 15  ? 2.11498 2.30091 2.37564 -0.04741 0.46941  -0.18418 15  GLY A N     
184  C CA    . GLY B 15  ? 2.06142 2.25260 2.33378 -0.04834 0.44372  -0.16927 15  GLY A CA    
185  C C     . GLY B 15  ? 2.11596 2.31706 2.37035 -0.05469 0.43234  -0.15404 15  GLY A C     
186  O O     . GLY B 15  ? 2.20589 2.40910 2.43607 -0.05873 0.44328  -0.15544 15  GLY A O     
187  N N     . ASN B 16  ? 1.98673 2.19345 2.25333 -0.05566 0.41043  -0.13942 16  ASN A N     
188  C CA    . ASN B 16  ? 1.93235 2.14620 2.18054 -0.06190 0.39625  -0.12524 16  ASN A CA    
189  C C     . ASN B 16  ? 2.01755 2.24797 2.30346 -0.06084 0.39468  -0.10711 16  ASN A C     
190  O O     . ASN B 16  ? 1.95407 2.19059 2.22965 -0.06581 0.38156  -0.09410 16  ASN A O     
191  C CB    . ASN B 16  ? 1.75097 1.95781 1.97953 -0.06492 0.37205  -0.12196 16  ASN A CB    
192  C CG    . ASN B 16  ? 1.95939 2.15055 2.14683 -0.06755 0.37111  -0.13785 16  ASN A CG    
193  O OD1   . ASN B 16  ? 1.98019 2.16518 2.14756 -0.06837 0.38757  -0.15112 16  ASN A OD1   
194  N ND2   . ASN B 16  ? 1.87388 2.05831 2.04807 -0.06928 0.35172  -0.13631 16  ASN A ND2   
195  N N     . GLN B 17  ? 2.08513 2.32269 2.41515 -0.05472 0.40744  -0.10571 17  GLN A N     
196  C CA    . GLN B 17  ? 2.00412 2.25772 2.37409 -0.05376 0.40580  -0.08802 17  GLN A CA    
197  C C     . GLN B 17  ? 1.95798 2.22003 2.32944 -0.05458 0.42641  -0.08748 17  GLN A C     
198  O O     . GLN B 17  ? 1.94666 2.20706 2.32864 -0.05020 0.44869  -0.09874 17  GLN A O     
199  C CB    . GLN B 17  ? 2.03091 2.28845 2.45171 -0.04685 0.40621  -0.08460 17  GLN A CB    
200  C CG    . GLN B 17  ? 1.97530 2.22637 2.39702 -0.04666 0.38430  -0.08184 17  GLN A CG    
201  C CD    . GLN B 17  ? 2.01168 2.26842 2.48530 -0.04089 0.38166  -0.07460 17  GLN A CD    
202  O OE1   . GLN B 17  ? 2.09214 2.35316 2.59972 -0.03530 0.39918  -0.07789 17  GLN A OE1   
203  N NE2   . GLN B 17  ? 1.98056 2.23717 2.46079 -0.04233 0.35978  -0.06436 17  GLN A NE2   
204  N N     . LEU B 18  ? 1.77828 2.04913 2.13989 -0.06023 0.41931  -0.07425 18  LEU A N     
205  C CA    . LEU B 18  ? 1.96586 2.24461 2.32368 -0.06213 0.43755  -0.07281 18  LEU A CA    
206  C C     . LEU B 18  ? 2.12556 2.41568 2.53419 -0.05601 0.45587  -0.06907 18  LEU A C     
207  O O     . LEU B 18  ? 2.12742 2.41899 2.53531 -0.05436 0.47955  -0.07689 18  LEU A O     
208  C CB    . LEU B 18  ? 1.84752 2.13421 2.19140 -0.06923 0.42379  -0.05712 18  LEU A CB    
209  C CG    . LEU B 18  ? 1.93490 2.23075 2.27331 -0.07238 0.43981  -0.05286 18  LEU A CG    
210  C CD1   . LEU B 18  ? 1.90746 2.19287 2.20123 -0.07454 0.45498  -0.06932 18  LEU A CD1   
211  C CD2   . LEU B 18  ? 1.91593 2.21955 2.24689 -0.07914 0.42305  -0.03572 18  LEU A CD2   
212  N N     . ASP B 19  ? 2.09453 2.39262 2.54798 -0.05270 0.44555  -0.05698 19  ASP A N     
213  C CA    . ASP B 19  ? 2.07076 2.38155 2.57727 -0.04734 0.46053  -0.05009 19  ASP A CA    
214  C C     . ASP B 19  ? 1.95498 2.25950 2.48362 -0.03923 0.47887  -0.06484 19  ASP A C     
215  O O     . ASP B 19  ? 1.84790 2.16117 2.41439 -0.03437 0.49834  -0.06339 19  ASP A O     
216  C CB    . ASP B 19  ? 2.08380 2.40584 2.63042 -0.04781 0.44096  -0.02994 19  ASP A CB    
217  C CG    . ASP B 19  ? 2.15088 2.48185 2.68670 -0.05533 0.42756  -0.01369 19  ASP A CG    
218  O OD1   . ASP B 19  ? 2.10174 2.43754 2.62332 -0.05816 0.44055  -0.01341 19  ASP A OD1   
219  O OD2   . ASP B 19  ? 2.08620 2.41887 2.62750 -0.05859 0.40420  -0.00122 19  ASP A OD2   
220  N N     . PHE B 20  ? 2.12935 2.41882 2.63666 -0.03762 0.47362  -0.07889 20  PHE A N     
221  C CA    . PHE B 20  ? 2.20217 2.48471 2.73342 -0.02992 0.48821  -0.09221 20  PHE A CA    
222  C C     . PHE B 20  ? 2.26908 2.53566 2.76028 -0.02949 0.50489  -0.11524 20  PHE A C     
223  O O     . PHE B 20  ? 2.20425 2.46512 2.71477 -0.02311 0.52276  -0.12782 20  PHE A O     
224  C CB    . PHE B 20  ? 1.99440 2.27253 2.54448 -0.02744 0.46828  -0.08897 20  PHE A CB    
225  C CG    . PHE B 20  ? 2.02953 2.32180 2.62078 -0.02782 0.45152  -0.06703 20  PHE A CG    
226  C CD1   . PHE B 20  ? 1.99823 2.30168 2.64691 -0.02209 0.46094  -0.05875 20  PHE A CD1   
227  C CD2   . PHE B 20  ? 1.86016 2.15402 2.43274 -0.03417 0.42620  -0.05462 20  PHE A CD2   
228  C CE1   . PHE B 20  ? 1.81084 2.12702 2.49671 -0.02331 0.44420  -0.03790 20  PHE A CE1   
229  C CE2   . PHE B 20  ? 1.94767 2.25330 2.55549 -0.03535 0.41027  -0.03480 20  PHE A CE2   
230  C CZ    . PHE B 20  ? 1.90756 2.22443 2.57160 -0.03022 0.41865  -0.02617 20  PHE A CZ    
231  N N     . ASP B 21  ? 2.22773 2.48657 2.66451 -0.03629 0.49944  -0.12096 21  ASP A N     
232  C CA    . ASP B 21  ? 2.15674 2.39877 2.55071 -0.03731 0.51060  -0.14231 21  ASP A CA    
233  C C     . ASP B 21  ? 2.16675 2.40972 2.53370 -0.04058 0.53178  -0.14835 21  ASP A C     
234  O O     . ASP B 21  ? 2.03599 2.29058 2.39946 -0.04486 0.53011  -0.13525 21  ASP A O     
235  C CB    . ASP B 21  ? 2.03597 2.26664 2.38644 -0.04291 0.48767  -0.14533 21  ASP A CB    
236  C CG    . ASP B 21  ? 2.07660 2.30275 2.44871 -0.03930 0.47044  -0.14392 21  ASP A CG    
237  O OD1   . ASP B 21  ? 2.14639 2.36526 2.53827 -0.03331 0.48079  -0.15552 21  ASP A OD1   
238  O OD2   . ASP B 21  ? 2.10526 2.33485 2.47498 -0.04247 0.44703  -0.13121 21  ASP A OD2   
239  N N     . ASP B 22  ? 2.17348 2.40348 2.52059 -0.03884 0.55175  -0.16845 22  ASP A N     
240  C CA    . ASP B 22  ? 2.21815 2.44640 2.53629 -0.04189 0.57432  -0.17702 22  ASP A CA    
241  C C     . ASP B 22  ? 2.19959 2.41237 2.45303 -0.04949 0.56822  -0.18952 22  ASP A C     
242  O O     . ASP B 22  ? 2.09147 2.29177 2.32637 -0.05045 0.55297  -0.19721 22  ASP A O     
243  C CB    . ASP B 22  ? 2.18131 2.40548 2.52318 -0.03474 0.60444  -0.19136 22  ASP A CB    
244  C CG    . ASP B 22  ? 2.08470 2.32652 2.48822 -0.02822 0.61612  -0.17791 22  ASP A CG    
245  O OD1   . ASP B 22  ? 2.04612 2.30389 2.46651 -0.03073 0.60467  -0.15800 22  ASP A OD1   
246  O OD2   . ASP B 22  ? 2.16538 2.40481 2.60108 -0.02072 0.63685  -0.18724 22  ASP A OD2   
247  N N     . ILE B 23  ? 2.22879 2.44284 2.44884 -0.05519 0.58003  -0.19070 23  ILE A N     
248  C CA    . ILE B 23  ? 2.17903 2.37789 2.33746 -0.06262 0.57888  -0.20400 23  ILE A CA    
249  C C     . ILE B 23  ? 2.25141 2.43392 2.39795 -0.05958 0.60039  -0.22733 23  ILE A C     
250  O O     . ILE B 23  ? 2.12849 2.31364 2.29679 -0.05473 0.62674  -0.23319 23  ILE A O     
251  C CB    . ILE B 23  ? 2.05592 2.26197 2.18422 -0.06993 0.58503  -0.19660 23  ILE A CB    
252  C CG1   . ILE B 23  ? 1.99440 2.21535 2.13435 -0.07317 0.56284  -0.17389 23  ILE A CG1   
253  C CG2   . ILE B 23  ? 2.15792 2.34812 2.22232 -0.07811 0.58485  -0.21018 23  ILE A CG2   
254  C CD1   . ILE B 23  ? 2.25469 2.48457 2.37237 -0.07986 0.56886  -0.16439 23  ILE A CD1   
255  N N     . ILE B 24  ? 2.25483 2.41999 2.36802 -0.06236 0.58950  -0.24083 24  ILE A N     
256  C CA    . ILE B 24  ? 2.34277 2.48979 2.43776 -0.06088 0.60796  -0.26422 24  ILE A CA    
257  C C     . ILE B 24  ? 2.34402 2.47699 2.37310 -0.07048 0.61069  -0.27646 24  ILE A C     
258  O O     . ILE B 24  ? 2.36407 2.48262 2.37244 -0.07062 0.63110  -0.29590 24  ILE A O     
259  C CB    . ILE B 24  ? 2.28581 2.42172 2.39883 -0.05586 0.59675  -0.27297 24  ILE A CB    
260  C CG1   . ILE B 24  ? 2.14107 2.27219 2.22813 -0.06144 0.56547  -0.26763 24  ILE A CG1   
261  C CG2   . ILE B 24  ? 2.30277 2.45106 2.48221 -0.04602 0.59928  -0.26327 24  ILE A CG2   
262  C CD1   . ILE B 24  ? 2.06713 2.18717 2.16949 -0.05721 0.55379  -0.27576 24  ILE A CD1   
263  N N     . GLN B 25  ? 2.32147 2.45762 2.31697 -0.07871 0.59113  -0.26581 25  GLN A N     
264  C CA    . GLN B 25  ? 2.25870 2.38337 2.19286 -0.08851 0.59376  -0.27495 25  GLN A CA    
265  C C     . GLN B 25  ? 2.31973 2.45682 2.23532 -0.09561 0.58029  -0.25661 25  GLN A C     
266  O O     . GLN B 25  ? 2.32538 2.47211 2.25857 -0.09527 0.55757  -0.24068 25  GLN A O     
267  C CB    . GLN B 25  ? 2.27382 2.37899 2.17239 -0.09278 0.57831  -0.28867 25  GLN A CB    
268  C CG    . GLN B 25  ? 2.23383 2.32465 2.06942 -0.10289 0.58432  -0.30110 25  GLN A CG    
269  C CD    . GLN B 25  ? 2.21357 2.28595 2.01421 -0.10810 0.56638  -0.31269 25  GLN A CD    
270  O OE1   . GLN B 25  ? 2.22046 2.29119 2.04339 -0.10417 0.54866  -0.31081 25  GLN A OE1   
271  N NE2   . GLN B 25  ? 2.26315 2.32156 2.00840 -0.11745 0.57056  -0.32422 25  GLN A NE2   
272  N N     . ILE B 26  ? 2.36894 2.50512 2.24830 -0.10225 0.59448  -0.25898 26  ILE A N     
273  C CA    . ILE B 26  ? 2.32790 2.47423 2.18501 -0.10990 0.58285  -0.24266 26  ILE A CA    
274  C C     . ILE B 26  ? 2.30048 2.43246 2.09327 -0.12062 0.58113  -0.25229 26  ILE A C     
275  O O     . ILE B 26  ? 2.36598 2.48588 2.13208 -0.12269 0.60214  -0.26918 26  ILE A O     
276  C CB    . ILE B 26  ? 2.19812 2.36224 2.08091 -0.10787 0.60085  -0.23028 26  ILE A CB    
277  C CG1   . ILE B 26  ? 2.11739 2.29073 1.97445 -0.11648 0.58887  -0.21391 26  ILE A CG1   
278  C CG2   . ILE B 26  ? 2.34044 2.49919 2.21687 -0.10619 0.63449  -0.24523 26  ILE A CG2   
279  C CD1   . ILE B 26  ? 2.09939 2.29270 1.98977 -0.11428 0.59966  -0.19728 26  ILE A CD1   
280  N N     . GLY B 27  ? 2.26152 2.39385 2.02881 -0.12766 0.55614  -0.24204 27  GLY A N     
281  C CA    . GLY B 27  ? 2.24815 2.36968 1.95622 -0.13883 0.55158  -0.24675 27  GLY A CA    
282  C C     . GLY B 27  ? 2.27375 2.40791 1.96968 -0.14536 0.53868  -0.22686 27  GLY A C     
283  O O     . GLY B 27  ? 2.19456 2.33963 1.91726 -0.14291 0.51985  -0.21119 27  GLY A O     
284  N N     . ILE B 28  ? 2.36795 2.49981 2.02338 -0.15374 0.54941  -0.22801 28  ILE A N     
285  C CA    . ILE B 28  ? 2.21047 2.35377 1.85205 -0.16058 0.54017  -0.20969 28  ILE A CA    
286  C C     . ILE B 28  ? 2.15365 2.28422 1.73333 -0.17266 0.53513  -0.21506 28  ILE A C     
287  O O     . ILE B 28  ? 2.18577 2.30415 1.73386 -0.17622 0.55321  -0.23102 28  ILE A O     
288  C CB    . ILE B 28  ? 2.09161 2.25056 1.75573 -0.15822 0.56229  -0.20067 28  ILE A CB    
289  C CG1   . ILE B 28  ? 2.03956 2.20978 1.76568 -0.14627 0.57022  -0.19746 28  ILE A CG1   
290  C CG2   . ILE B 28  ? 2.05185 2.22325 1.70742 -0.16474 0.54969  -0.18011 28  ILE A CG2   
291  C CD1   . ILE B 28  ? 2.05596 2.24138 1.80850 -0.14335 0.59352  -0.18947 28  ILE A CD1   
292  N N     . THR B 29  ? 2.24955 2.38237 1.81186 -0.17916 0.51054  -0.20179 29  THR A N     
293  C CA    . THR B 29  ? 2.23521 2.35848 1.74153 -0.19141 0.50276  -0.20256 29  THR A CA    
294  C C     . THR B 29  ? 2.16932 2.30655 1.67134 -0.19689 0.49660  -0.18206 29  THR A C     
295  O O     . THR B 29  ? 2.18846 2.33653 1.71816 -0.19413 0.47891  -0.16630 29  THR A O     
296  C CB    . THR B 29  ? 2.11536 2.22613 1.60260 -0.19492 0.47664  -0.20624 29  THR A CB    
297  O OG1   . THR B 29  ? 2.15139 2.24755 1.63764 -0.19110 0.48337  -0.22638 29  THR A OG1   
298  C CG2   . THR B 29  ? 2.11248 2.21541 1.54512 -0.20814 0.46578  -0.20348 29  THR A CG2   
299  N N     . PHE B 30  ? 2.18892 2.32527 1.65575 -0.20487 0.51128  -0.18240 30  PHE A N     
300  C CA    . PHE B 30  ? 2.20387 2.35321 1.66508 -0.21059 0.50872  -0.16351 30  PHE A CA    
301  C C     . PHE B 30  ? 2.19163 2.33374 1.60833 -0.22213 0.48669  -0.15711 30  PHE A C     
302  O O     . PHE B 30  ? 2.16064 2.28804 1.53137 -0.23008 0.48853  -0.16889 30  PHE A O     
303  C CB    . PHE B 30  ? 2.16613 2.32003 1.61719 -0.21257 0.53856  -0.16602 30  PHE A CB    
304  C CG    . PHE B 30  ? 2.15932 2.32161 1.65708 -0.20129 0.56097  -0.17068 30  PHE A CG    
305  C CD1   . PHE B 30  ? 2.11127 2.29236 1.65490 -0.19551 0.56195  -0.15414 30  PHE A CD1   
306  C CD2   . PHE B 30  ? 2.23089 2.38190 1.72804 -0.19656 0.58036  -0.19135 30  PHE A CD2   
307  C CE1   . PHE B 30  ? 2.10602 2.29540 1.69496 -0.18536 0.58153  -0.15722 30  PHE A CE1   
308  C CE2   . PHE B 30  ? 2.24635 2.40540 1.78951 -0.18590 0.60091  -0.19490 30  PHE A CE2   
309  C CZ    . PHE B 30  ? 2.17485 2.35354 1.76446 -0.18036 0.60121  -0.17736 30  PHE A CZ    
310  N N     . VAL B 31  ? 2.27205 2.42414 1.70282 -0.22327 0.46588  -0.13832 31  VAL A N     
311  C CA    . VAL B 31  ? 2.25864 2.40568 1.65531 -0.23322 0.44261  -0.12947 31  VAL A CA    
312  C C     . VAL B 31  ? 2.11348 2.27255 1.50264 -0.23963 0.44321  -0.11105 31  VAL A C     
313  O O     . VAL B 31  ? 2.07868 2.25260 1.50470 -0.23427 0.44740  -0.09891 31  VAL A O     
314  C CB    . VAL B 31  ? 2.26342 2.40981 1.68255 -0.22912 0.41528  -0.12354 31  VAL A CB    
315  C CG1   . VAL B 31  ? 2.16916 2.31133 1.55651 -0.23917 0.39164  -0.11292 31  VAL A CG1   
316  C CG2   . VAL B 31  ? 2.25028 2.38467 1.67614 -0.22330 0.41443  -0.14128 31  VAL A CG2   
317  N N     . ARG B 32  ? 2.06114 2.21357 1.40265 -0.25155 0.43842  -0.10857 32  ARG A N     
318  C CA    . ARG B 32  ? 2.05785 2.22031 1.38785 -0.25905 0.43627  -0.09033 32  ARG A CA    
319  C C     . ARG B 32  ? 2.09107 2.24413 1.37745 -0.27084 0.41522  -0.08525 32  ARG A C     
320  O O     . ARG B 32  ? 2.27637 2.41489 1.52289 -0.27725 0.41642  -0.09847 32  ARG A O     
321  C CB    . ARG B 32  ? 2.12325 2.29033 1.44002 -0.26176 0.46537  -0.09285 32  ARG A CB    
322  C CG    . ARG B 32  ? 2.11944 2.29910 1.43143 -0.26839 0.46544  -0.07284 32  ARG A CG    
323  C CD    . ARG B 32  ? 2.22993 2.41162 1.53455 -0.26726 0.49018  -0.07499 32  ARG A CD    
324  N NE    . ARG B 32  ? 2.43428 2.62566 1.78140 -0.25673 0.51253  -0.08003 32  ARG A NE    
325  C CZ    . ARG B 32  ? 2.50960 2.70259 1.86047 -0.25225 0.53627  -0.08473 32  ARG A CZ    
326  N NH1   . ARG B 32  ? 2.51109 2.69632 1.82366 -0.25757 0.54136  -0.08567 32  ARG A NH1   
327  N NH2   . ARG B 32  ? 2.40039 2.60291 1.79412 -0.24247 0.55486  -0.08812 32  ARG A NH2   
328  N N     . ASN B 33  ? 2.10642 2.26740 1.40152 -0.27375 0.39560  -0.06604 33  ASN A N     
329  C CA    . ASN B 33  ? 2.08527 2.23941 1.34560 -0.28457 0.37340  -0.05770 33  ASN A CA    
330  C C     . ASN B 33  ? 2.15564 2.29546 1.40515 -0.28436 0.35652  -0.06926 33  ASN A C     
331  O O     . ASN B 33  ? 2.08572 2.21372 1.29286 -0.29424 0.34838  -0.07351 33  ASN A O     
332  C CB    . ASN B 33  ? 2.11838 2.26895 1.32971 -0.29712 0.38406  -0.05657 33  ASN A CB    
333  C CG    . ASN B 33  ? 2.26882 2.43399 1.49102 -0.29799 0.39843  -0.04270 33  ASN A CG    
334  O OD1   . ASN B 33  ? 2.15270 2.33066 1.41874 -0.28934 0.40340  -0.03572 33  ASN A OD1   
335  N ND2   . ASN B 33  ? 2.40706 2.56838 1.59872 -0.30434 0.40026  -0.03743 33  ASN A ND2   
336  N N     . ASN B 34  ? 2.16548 2.30646 1.45416 -0.27327 0.35111  -0.07398 34  ASN A N     
337  C CA    . ASN B 34  ? 2.15514 2.28402 1.44158 -0.27144 0.33527  -0.08425 34  ASN A CA    
338  C C     . ASN B 34  ? 2.23373 2.34729 1.48340 -0.27595 0.34614  -0.10431 34  ASN A C     
339  O O     . ASN B 34  ? 2.33069 2.43176 1.55505 -0.28166 0.33079  -0.10985 34  ASN A O     
340  C CB    . ASN B 34  ? 2.08691 2.21367 1.36380 -0.27759 0.30679  -0.07073 34  ASN A CB    
341  C CG    . ASN B 34  ? 1.91139 2.05064 1.22890 -0.27137 0.29492  -0.05384 34  ASN A CG    
342  O OD1   . ASN B 34  ? 1.87696 2.02488 1.23228 -0.26157 0.30473  -0.05406 34  ASN A OD1   
343  N ND2   . ASN B 34  ? 1.89836 2.03807 1.20863 -0.27719 0.27361  -0.03918 34  ASN A ND2   
344  N N     . GLN B 35  ? 2.14514 2.25938 1.39275 -0.27342 0.37308  -0.11529 35  GLN A N     
345  C CA    . GLN B 35  ? 2.26433 2.36362 1.47808 -0.27710 0.38755  -0.13575 35  GLN A CA    
346  C C     . GLN B 35  ? 2.36583 2.46806 1.60782 -0.26650 0.41406  -0.14878 35  GLN A C     
347  O O     . GLN B 35  ? 2.25421 2.37038 1.52219 -0.26162 0.42883  -0.14079 35  GLN A O     
348  C CB    . GLN B 35  ? 2.35479 2.44890 1.51529 -0.29075 0.39504  -0.13453 35  GLN A CB    
349  C CG    . GLN B 35  ? 2.31057 2.39688 1.43473 -0.30284 0.36929  -0.12630 35  GLN A CG    
350  C CD    . GLN B 35  ? 2.49146 2.56995 1.57354 -0.31174 0.37195  -0.12474 35  GLN A CD    
351  O OE1   . GLN B 35  ? 2.51701 2.59743 1.59791 -0.30870 0.39328  -0.12802 35  GLN A OE1   
352  N NE2   . GLN B 35  ? 2.54071 2.61029 1.59040 -0.32216 0.34946  -0.11905 35  GLN A NE2   
353  N N     . ILE B 36  ? 2.44464 2.53372 1.68331 -0.26300 0.41944  -0.16835 36  ILE A N     
354  C CA    . ILE B 36  ? 2.32068 2.41028 1.58306 -0.25356 0.44561  -0.18252 36  ILE A CA    
355  C C     . ILE B 36  ? 2.26467 2.35030 1.49129 -0.26014 0.47160  -0.19033 36  ILE A C     
356  O O     . ILE B 36  ? 2.30089 2.37112 1.48495 -0.26750 0.46718  -0.19790 36  ILE A O     
357  C CB    . ILE B 36  ? 2.19342 2.26926 1.46311 -0.24811 0.44266  -0.20092 36  ILE A CB    
358  C CG1   . ILE B 36  ? 2.14302 2.22437 1.45213 -0.24070 0.41900  -0.19223 36  ILE A CG1   
359  C CG2   . ILE B 36  ? 2.27418 2.34878 1.56393 -0.23944 0.47136  -0.21656 36  ILE A CG2   
360  C CD1   . ILE B 36  ? 2.08874 2.15667 1.40435 -0.23627 0.41235  -0.20819 36  ILE A CD1   
361  N N     . ILE B 37  ? 2.31411 2.41286 1.56822 -0.25368 0.49227  -0.18511 37  ILE A N     
362  C CA    . ILE B 37  ? 2.36314 2.45961 1.59944 -0.25429 0.51048  -0.18668 37  ILE A CA    
363  C C     . ILE B 37  ? 2.43296 2.52494 1.68862 -0.24436 0.53672  -0.20381 37  ILE A C     
364  O O     . ILE B 37  ? 2.54950 2.63334 1.78170 -0.24541 0.55130  -0.21110 37  ILE A O     
365  C CB    . ILE B 37  ? 2.30513 2.41976 1.55442 -0.25540 0.51399  -0.16567 37  ILE A CB    
366  C CG1   . ILE B 37  ? 2.24806 2.38075 1.55310 -0.24579 0.52378  -0.15881 37  ILE A CG1   
367  C CG2   . ILE B 37  ? 2.28964 2.40661 1.51506 -0.26599 0.48849  -0.14884 37  ILE A CG2   
368  C CD1   . ILE B 37  ? 2.24357 2.39387 1.56569 -0.24579 0.53112  -0.13987 37  ILE A CD1   
369  N N     . ASP B 38  ? 2.39336 2.49025 1.69119 -0.23486 0.54319  -0.21016 38  ASP A N     
370  C CA    . ASP B 38  ? 2.39803 2.49214 1.72083 -0.22455 0.56810  -0.22480 38  ASP A CA    
371  C C     . ASP B 38  ? 2.42030 2.51633 1.78312 -0.21634 0.56672  -0.23227 38  ASP A C     
372  O O     . ASP B 38  ? 2.49168 2.59595 1.87555 -0.21532 0.54593  -0.22062 38  ASP A O     
373  C CB    . ASP B 38  ? 2.39151 2.50150 1.74111 -0.21906 0.58893  -0.21448 38  ASP A CB    
374  C CG    . ASP B 38  ? 2.50195 2.60652 1.86714 -0.21004 0.61552  -0.22970 38  ASP A CG    
375  O OD1   . ASP B 38  ? 2.54898 2.63531 1.89546 -0.20956 0.61799  -0.24864 38  ASP A OD1   
376  O OD2   . ASP B 38  ? 2.45470 2.57314 1.85175 -0.20353 0.63368  -0.22248 38  ASP A OD2   
377  N N     . THR B 39  ? 2.39194 2.47941 1.77062 -0.20813 0.58422  -0.24957 39  THR A N     
378  C CA    . THR B 39  ? 2.40438 2.49395 1.82602 -0.19886 0.58591  -0.25690 39  THR A CA    
379  C C     . THR B 39  ? 2.45737 2.55056 1.91657 -0.18752 0.61311  -0.26444 39  THR A C     
380  O O     . THR B 39  ? 2.45445 2.54057 1.89681 -0.18701 0.62965  -0.27148 39  THR A O     
381  C CB    . THR B 39  ? 2.33183 2.40206 1.73477 -0.20021 0.57109  -0.27264 39  THR A CB    
382  O OG1   . THR B 39  ? 2.46501 2.51648 1.83234 -0.20306 0.58441  -0.29074 39  THR A OG1   
383  C CG2   . THR B 39  ? 2.33272 2.40002 1.70905 -0.20883 0.53866  -0.26225 39  THR A CG2   
384  N N     . TYR B 40  ? 2.52666 2.63098 2.04007 -0.17751 0.61437  -0.26096 40  TYR A N     
385  C CA    . TYR B 40  ? 2.51786 2.62667 2.07396 -0.16652 0.63974  -0.26828 40  TYR A CA    
386  C C     . TYR B 40  ? 2.50492 2.60951 2.09794 -0.15741 0.62936  -0.27515 40  TYR A C     
387  O O     . TYR B 40  ? 2.44790 2.55738 2.05692 -0.15630 0.60258  -0.26403 40  TYR A O     
388  C CB    . TYR B 40  ? 2.37495 2.50668 1.97170 -0.16199 0.64948  -0.24965 40  TYR A CB    
389  C CG    . TYR B 40  ? 2.29380 2.43254 1.94433 -0.14936 0.67060  -0.25315 40  TYR A CG    
390  C CD1   . TYR B 40  ? 2.35343 2.48902 2.00390 -0.14520 0.69306  -0.25923 40  TYR A CD1   
391  C CD2   . TYR B 40  ? 2.29258 2.44064 1.99716 -0.14023 0.66248  -0.24757 40  TYR A CD2   
392  C CE1   . TYR B 40  ? 2.41277 2.55499 2.11436 -0.13360 0.71178  -0.26162 40  TYR A CE1   
393  C CE2   . TYR B 40  ? 2.23708 2.39215 1.99169 -0.12958 0.68308  -0.25061 40  TYR A CE2   
394  C CZ    . TYR B 40  ? 2.30910 2.46126 2.06282 -0.12614 0.70747  -0.25744 40  TYR A CZ    
395  O OH    . TYR B 40  ? 2.35385 2.51286 2.16047 -0.11471 0.72470  -0.25857 40  TYR A OH    
396  N N     . HIS B 41  ? 2.46313 2.55805 2.06950 -0.15089 0.65024  -0.29329 41  HIS A N     
397  C CA    . HIS B 41  ? 2.40805 2.49822 2.05063 -0.14197 0.64190  -0.30037 41  HIS A CA    
398  C C     . HIS B 41  ? 2.43335 2.52523 2.11591 -0.13161 0.67112  -0.31029 41  HIS A C     
399  O O     . HIS B 41  ? 2.52760 2.61329 2.19514 -0.13125 0.69051  -0.31761 41  HIS A O     
400  C CB    . HIS B 41  ? 2.38107 2.44880 1.98426 -0.14726 0.62927  -0.31732 41  HIS A CB    
401  C CG    . HIS B 41  ? 2.60441 2.65325 2.16800 -0.15118 0.65077  -0.33835 41  HIS A CG    
402  N ND1   . HIS B 41  ? 2.61824 2.65974 2.12943 -0.16097 0.64883  -0.33740 41  HIS A ND1   
403  C CD2   . HIS B 41  ? 2.79002 2.82520 2.36488 -0.14431 0.66598  -0.35594 41  HIS A CD2   
404  C CE1   . HIS B 41  ? 2.72909 2.75310 2.21949 -0.16029 0.66243  -0.35410 41  HIS A CE1   
405  N NE2   . HIS B 41  ? 2.82770 2.84730 2.35583 -0.15026 0.67317  -0.36580 41  HIS A NE2   
406  N N     . SER B 42  ? 2.42055 2.52023 2.15867 -0.12118 0.66542  -0.30570 42  SER A N     
407  C CA    . SER B 42  ? 2.50603 2.60736 2.28709 -0.11077 0.69166  -0.31447 42  SER A CA    
408  C C     . SER B 42  ? 2.42388 2.52623 2.25291 -0.10144 0.67811  -0.31382 42  SER A C     
409  O O     . SER B 42  ? 2.38139 2.49699 2.23820 -0.09946 0.65555  -0.29608 42  SER A O     
410  C CB    . SER B 42  ? 2.48238 2.60414 2.29675 -0.10689 0.70853  -0.29934 42  SER A CB    
411  O OG    . SER B 42  ? 2.53251 2.65453 2.38899 -0.09592 0.72871  -0.30523 42  SER A OG    
412  N N     . MET B 43  ? 2.36578 2.45336 2.20292 -0.09617 0.69166  -0.33323 43  MET A N     
413  C CA    . MET B 43  ? 2.31450 2.40572 2.20814 -0.08542 0.68727  -0.33216 43  MET A CA    
414  C C     . MET B 43  ? 2.41695 2.52751 2.36684 -0.07675 0.70549  -0.32046 43  MET A C     
415  O O     . MET B 43  ? 2.55900 2.67230 2.50529 -0.07650 0.73067  -0.32318 43  MET A O     
416  C CB    . MET B 43  ? 2.35477 2.42439 2.24258 -0.08220 0.69865  -0.35648 43  MET A CB    
417  C CG    . MET B 43  ? 2.42425 2.47292 2.25333 -0.09165 0.68361  -0.37007 43  MET A CG    
418  S SD    . MET B 43  ? 2.35560 2.40660 2.18712 -0.09398 0.64154  -0.35707 43  MET A SD    
419  C CE    . MET B 43  ? 2.28576 2.33172 2.17201 -0.08217 0.64137  -0.36507 43  MET A CE    
420  N N     . ILE B 44  ? 2.37926 2.50338 2.38143 -0.06982 0.69054  -0.30573 44  ILE A N     
421  C CA    . ILE B 44  ? 2.45611 2.60007 2.51566 -0.06207 0.70313  -0.29166 44  ILE A CA    
422  C C     . ILE B 44  ? 2.51577 2.65766 2.62801 -0.05124 0.70892  -0.29765 44  ILE A C     
423  O O     . ILE B 44  ? 2.38247 2.51802 2.50256 -0.04957 0.68828  -0.29894 44  ILE A O     
424  C CB    . ILE B 44  ? 2.25745 2.42126 2.33444 -0.06429 0.67985  -0.26592 44  ILE A CB    
425  C CG1   . ILE B 44  ? 2.21995 2.38502 2.24482 -0.07512 0.67421  -0.26012 44  ILE A CG1   
426  C CG2   . ILE B 44  ? 2.31989 2.50411 2.45652 -0.05701 0.69223  -0.25091 44  ILE A CG2   
427  C CD1   . ILE B 44  ? 2.26541 2.43301 2.27520 -0.07725 0.70410  -0.26433 44  ILE A CD1   
428  N N     . ARG B 45  ? 2.47707 2.62421 2.62597 -0.04392 0.73737  -0.30111 45  ARG A N     
429  C CA    . ARG B 45  ? 2.40732 2.55247 2.60890 -0.03330 0.74579  -0.30700 45  ARG A CA    
430  C C     . ARG B 45  ? 2.47583 2.64249 2.73967 -0.02731 0.73188  -0.28386 45  ARG A C     
431  O O     . ARG B 45  ? 2.45192 2.63702 2.73517 -0.02775 0.73534  -0.26688 45  ARG A O     
432  C CB    . ARG B 45  ? 2.53581 2.67254 2.74583 -0.02752 0.77048  -0.31695 45  ARG A CB    
433  C CG    . ARG B 45  ? 2.54345 2.67903 2.81301 -0.01602 0.77778  -0.31976 45  ARG A CG    
434  C CD    . ARG B 45  ? 2.55429 2.67572 2.82161 -0.01146 0.80121  -0.33400 45  ARG A CD    
435  N NE    . ARG B 45  ? 2.57356 2.69826 2.90520 -0.00026 0.80971  -0.33176 45  ARG A NE    
436  C CZ    . ARG B 45  ? 2.52173 2.63219 2.86122 0.00519  0.82855  -0.34558 45  ARG A CZ    
437  N NH1   . ARG B 45  ? 2.56557 2.65745 2.85162 0.00038  0.84085  -0.36302 45  ARG A NH1   
438  N NH2   . ARG B 45  ? 2.46287 2.57729 2.86342 0.01508  0.83465  -0.34166 45  ARG A NH2   
439  N N     . THR B 46  ? 2.48328 2.64720 2.77789 -0.02217 0.71575  -0.28299 46  THR A N     
440  C CA    . THR B 46  ? 2.40407 2.58601 2.75815 -0.01652 0.70154  -0.26241 46  THR A CA    
441  C C     . THR B 46  ? 2.35171 2.53066 2.75914 -0.00600 0.71433  -0.26938 46  THR A C     
442  O O     . THR B 46  ? 2.34078 2.50120 2.73536 -0.00359 0.72642  -0.29042 46  THR A O     
443  C CB    . THR B 46  ? 2.30354 2.48693 2.64594 -0.02102 0.66518  -0.25065 46  THR A CB    
444  O OG1   . THR B 46  ? 2.18590 2.38602 2.58521 -0.01596 0.65193  -0.23089 46  THR A OG1   
445  C CG2   . THR B 46  ? 2.24482 2.40785 2.56379 -0.02129 0.65507  -0.26748 46  THR A CG2   
446  N N     . ASN B 47  ? 2.30791 2.50515 2.77630 -0.00003 0.71120  -0.25106 47  ASN A N     
447  C CA    . ASN B 47  ? 2.33073 2.52815 2.85734 0.00995  0.71882  -0.25291 47  ASN A CA    
448  C C     . ASN B 47  ? 2.19836 2.39575 2.74429 0.01101  0.68869  -0.24414 47  ASN A C     
449  O O     . ASN B 47  ? 2.20274 2.40115 2.79890 0.01882  0.69069  -0.24309 47  ASN A O     
450  C CB    . ASN B 47  ? 2.18627 2.40351 2.77165 0.01599  0.73388  -0.23734 47  ASN A CB    
451  C CG    . ASN B 47  ? 2.19484 2.40742 2.75957 0.01584  0.75614  -0.24341 47  ASN A CG    
452  O OD1   . ASN B 47  ? 2.23845 2.43127 2.76432 0.01508  0.76954  -0.26397 47  ASN A OD1   
453  N ND2   . ASN B 47  ? 2.31015 2.54087 2.90077 0.01622  0.75970  -0.22518 47  ASN A ND2   
454  N N     . LEU B 48  ? 2.16558 2.36165 2.67326 0.00334  0.66145  -0.23769 48  LEU A N     
455  C CA    . LEU B 48  ? 2.27667 2.47221 2.79675 0.00343  0.63249  -0.22927 48  LEU A CA    
456  C C     . LEU B 48  ? 2.24666 2.42004 2.73467 0.00270  0.62796  -0.24935 48  LEU A C     
457  O O     . LEU B 48  ? 2.26676 2.42545 2.70420 -0.00184 0.63742  -0.26666 48  LEU A O     
458  C CB    . LEU B 48  ? 2.14137 2.34687 2.63830 -0.00435 0.60551  -0.21142 48  LEU A CB    
459  C CG    . LEU B 48  ? 2.05444 2.28136 2.57668 -0.00552 0.60523  -0.19017 48  LEU A CG    
460  C CD1   . LEU B 48  ? 1.95350 2.18550 2.44090 -0.01420 0.57997  -0.17702 48  LEU A CD1   
461  C CD2   . LEU B 48  ? 2.09149 2.33227 2.68251 0.00146  0.60205  -0.17486 48  LEU A CD2   
462  N N     . GLU B 49  ? 2.20802 2.37909 2.72589 0.00675  0.61259  -0.24626 49  GLU A N     
463  C CA    . GLU B 49  ? 2.18954 2.34094 2.67996 0.00555  0.60346  -0.26226 49  GLU A CA    
464  C C     . GLU B 49  ? 2.25061 2.39880 2.69015 -0.00356 0.57795  -0.25802 49  GLU A C     
465  O O     . GLU B 49  ? 2.19938 2.36084 2.64672 -0.00621 0.55719  -0.23858 49  GLU A O     
466  C CB    . GLU B 49  ? 2.10420 2.25554 2.64466 0.01252  0.59416  -0.25813 49  GLU A CB    
467  C CG    . GLU B 49  ? 2.02190 2.15299 2.54132 0.01216  0.58627  -0.27467 49  GLU A CG    
468  C CD    . GLU B 49  ? 2.02511 2.15729 2.59653 0.01898  0.57701  -0.26889 49  GLU A CD    
469  O OE1   . GLU B 49  ? 2.04753 2.19563 2.67214 0.02423  0.57868  -0.25306 49  GLU A OE1   
470  O OE2   . GLU B 49  ? 1.95899 2.07625 2.51857 0.01875  0.56749  -0.27952 49  GLU A OE2   
471  N N     . ILE B 50  ? 2.29172 2.42190 2.67887 -0.00863 0.57958  -0.27616 50  ILE A N     
472  C CA    . ILE B 50  ? 2.23250 2.35809 2.57019 -0.01733 0.55687  -0.27374 50  ILE A CA    
473  C C     . ILE B 50  ? 2.19684 2.31588 2.54439 -0.01620 0.53414  -0.27238 50  ILE A C     
474  O O     . ILE B 50  ? 2.29799 2.40185 2.64820 -0.01316 0.53984  -0.28835 50  ILE A O     
475  C CB    . ILE B 50  ? 2.24011 2.34931 2.51785 -0.02394 0.56740  -0.29283 50  ILE A CB    
476  C CG1   . ILE B 50  ? 2.17962 2.29428 2.45092 -0.02423 0.59375  -0.29572 50  ILE A CG1   
477  C CG2   . ILE B 50  ? 2.30120 2.40813 2.53092 -0.03315 0.54354  -0.28745 50  ILE A CG2   
478  C CD1   . ILE B 50  ? 2.17442 2.27346 2.38467 -0.03158 0.60469  -0.31343 50  ILE A CD1   
479  N N     . PRO B 51  ? 2.09013 2.21952 2.44373 -0.01852 0.50925  -0.25416 51  PRO A N     
480  C CA    . PRO B 51  ? 2.09275 2.21642 2.45576 -0.01759 0.48799  -0.25198 51  PRO A CA    
481  C C     . PRO B 51  ? 2.14147 2.24570 2.45705 -0.02262 0.48213  -0.26900 51  PRO A C     
482  O O     . PRO B 51  ? 2.14957 2.24871 2.41710 -0.02958 0.48306  -0.27473 51  PRO A O     
483  C CB    . PRO B 51  ? 2.09965 2.23783 2.46560 -0.02106 0.46454  -0.22969 51  PRO A CB    
484  C CG    . PRO B 51  ? 2.01011 2.16454 2.39335 -0.02048 0.47572  -0.21791 51  PRO A CG    
485  C CD    . PRO B 51  ? 2.08926 2.23650 2.44573 -0.02170 0.50033  -0.23400 51  PRO A CD    
486  N N     . PRO B 52  ? 2.24497 2.33796 2.57318 -0.01964 0.47562  -0.27693 52  PRO A N     
487  C CA    . PRO B 52  ? 2.27443 2.34810 2.55932 -0.02465 0.46996  -0.29363 52  PRO A CA    
488  C C     . PRO B 52  ? 2.24804 2.32198 2.48991 -0.03308 0.44831  -0.28643 52  PRO A C     
489  O O     . PRO B 52  ? 2.29707 2.35733 2.49311 -0.03929 0.44734  -0.29936 52  PRO A O     
490  C CB    . PRO B 52  ? 2.12635 2.19238 2.44379 -0.01928 0.46299  -0.29739 52  PRO A CB    
491  C CG    . PRO B 52  ? 2.07749 2.15425 2.45223 -0.01058 0.47646  -0.29082 52  PRO A CG    
492  C CD    . PRO B 52  ? 2.16440 2.26104 2.54833 -0.01154 0.47532  -0.27205 52  PRO A CD    
493  N N     . PHE B 53  ? 2.16699 2.25567 2.42231 -0.03372 0.43083  -0.26604 53  PHE A N     
494  C CA    . PHE B 53  ? 2.14711 2.23691 2.36363 -0.04138 0.41164  -0.25828 53  PHE A CA    
495  C C     . PHE B 53  ? 2.23233 2.32298 2.40919 -0.04740 0.42157  -0.26141 53  PHE A C     
496  O O     . PHE B 53  ? 2.27503 2.35738 2.40694 -0.05461 0.41296  -0.26621 53  PHE A O     
497  C CB    . PHE B 53  ? 2.15731 2.26261 2.39881 -0.04042 0.39346  -0.23606 53  PHE A CB    
498  C CG    . PHE B 53  ? 2.05338 2.16172 2.25930 -0.04767 0.37590  -0.22638 53  PHE A CG    
499  C CD1   . PHE B 53  ? 2.04923 2.14853 2.23241 -0.05137 0.35770  -0.22800 53  PHE A CD1   
500  C CD2   . PHE B 53  ? 2.00221 2.12251 2.19919 -0.05071 0.37775  -0.21530 53  PHE A CD2   
501  C CE1   . PHE B 53  ? 2.03290 2.13490 2.18559 -0.05768 0.34216  -0.21889 53  PHE A CE1   
502  C CE2   . PHE B 53  ? 2.01285 2.13542 2.17855 -0.05719 0.36186  -0.20641 53  PHE A CE2   
503  C CZ    . PHE B 53  ? 2.12723 2.24061 2.27112 -0.06052 0.34431  -0.20826 53  PHE A CZ    
504  N N     . ILE B 54  ? 2.28224 2.38303 2.47593 -0.04474 0.43962  -0.25818 54  ILE A N     
505  C CA    . ILE B 54  ? 2.28618 2.38830 2.44405 -0.05034 0.45077  -0.26074 54  ILE A CA    
506  C C     . ILE B 54  ? 2.25848 2.34256 2.38109 -0.05316 0.46620  -0.28330 54  ILE A C     
507  O O     . ILE B 54  ? 2.28323 2.36156 2.35875 -0.06084 0.46587  -0.28812 54  ILE A O     
508  C CB    . ILE B 54  ? 2.12617 2.24458 2.31495 -0.04654 0.46631  -0.25046 54  ILE A CB    
509  C CG1   . ILE B 54  ? 2.12527 2.26061 2.34164 -0.04571 0.44863  -0.22758 54  ILE A CG1   
510  C CG2   . ILE B 54  ? 2.03442 2.15340 2.18704 -0.05206 0.48075  -0.25445 54  ILE A CG2   
511  C CD1   . ILE B 54  ? 1.99961 2.13765 2.17966 -0.05348 0.42944  -0.21747 54  ILE A CD1   
512  N N     . GLN B 55  ? 2.27673 2.35096 2.42097 -0.04738 0.47960  -0.29743 55  GLN A N     
513  C CA    . GLN B 55  ? 2.27025 2.32496 2.38028 -0.05031 0.49346  -0.32024 55  GLN A CA    
514  C C     . GLN B 55  ? 2.27143 2.31238 2.33924 -0.05778 0.47363  -0.32632 55  GLN A C     
515  O O     . GLN B 55  ? 2.25755 2.28591 2.27824 -0.06487 0.47843  -0.33911 55  GLN A O     
516  C CB    . GLN B 55  ? 2.25219 2.29828 2.39758 -0.04221 0.50974  -0.33366 55  GLN A CB    
517  C CG    . GLN B 55  ? 2.24081 2.29933 2.43077 -0.03441 0.53138  -0.32902 55  GLN A CG    
518  C CD    . GLN B 55  ? 2.22880 2.27685 2.45138 -0.02661 0.54894  -0.34397 55  GLN A CD    
519  O OE1   . GLN B 55  ? 2.19910 2.22754 2.39936 -0.02827 0.55189  -0.36279 55  GLN A OE1   
520  N NE2   . GLN B 55  ? 2.22573 2.28661 2.50253 -0.01822 0.56029  -0.33532 55  GLN A NE2   
521  N N     . ALA B 56  ? 2.32779 2.37097 2.41194 -0.05661 0.45113  -0.31685 56  ALA A N     
522  C CA    . ALA B 56  ? 2.33099 2.36254 2.37959 -0.06340 0.43120  -0.32071 56  ALA A CA    
523  C C     . ALA B 56  ? 2.36831 2.40614 2.37925 -0.07157 0.41829  -0.30981 56  ALA A C     
524  O O     . ALA B 56  ? 2.39764 2.42407 2.36673 -0.07919 0.40846  -0.31653 56  ALA A O     
525  C CB    . ALA B 56  ? 2.27157 2.30430 2.35160 -0.05928 0.41236  -0.31316 56  ALA A CB    
526  N N     . LEU B 57  ? 2.33482 2.39042 2.36076 -0.07037 0.41764  -0.29273 57  LEU A N     
527  C CA    . LEU B 57  ? 2.29405 2.35619 2.28764 -0.07773 0.40565  -0.28135 57  LEU A CA    
528  C C     . LEU B 57  ? 2.28117 2.33874 2.23456 -0.08391 0.42118  -0.29018 57  LEU A C     
529  O O     . LEU B 57  ? 2.23424 2.28675 2.14506 -0.09230 0.41118  -0.29019 57  LEU A O     
530  C CB    . LEU B 57  ? 2.29232 2.37414 2.31682 -0.07451 0.39912  -0.26014 57  LEU A CB    
531  C CG    . LEU B 57  ? 2.19949 2.28960 2.19733 -0.08123 0.38635  -0.24621 57  LEU A CG    
532  C CD1   . LEU B 57  ? 2.07090 2.15407 2.04609 -0.08600 0.36285  -0.24360 57  LEU A CD1   
533  C CD2   . LEU B 57  ? 2.28936 2.39793 2.32055 -0.07768 0.38378  -0.22721 57  LEU A CD2   
534  N N     . THR B 58  ? 2.35754 2.41684 2.32417 -0.08003 0.44577  -0.29731 58  THR A N     
535  C CA    . THR B 58  ? 2.37273 2.42997 2.30472 -0.08543 0.46274  -0.30373 58  THR A CA    
536  C C     . THR B 58  ? 2.32246 2.36013 2.22703 -0.08764 0.47925  -0.32724 58  THR A C     
537  O O     . THR B 58  ? 2.33199 2.36469 2.19826 -0.09392 0.49131  -0.33424 58  THR A O     
538  C CB    . THR B 58  ? 2.28189 2.35534 2.24457 -0.08039 0.48083  -0.29468 58  THR A CB    
539  O OG1   . THR B 58  ? 2.19134 2.26257 2.19184 -0.07179 0.49953  -0.30417 58  THR A OG1   
540  C CG2   . THR B 58  ? 2.33188 2.42385 2.32402 -0.07821 0.46456  -0.27184 58  THR A CG2   
541  N N     . SER B 59  ? 2.33143 2.35750 2.25412 -0.08295 0.48017  -0.33943 59  SER A N     
542  C CA    . SER B 59  ? 2.37108 2.37707 2.27217 -0.08426 0.49671  -0.36303 59  SER A CA    
543  C C     . SER B 59  ? 2.39238 2.40005 2.30284 -0.08036 0.52785  -0.37116 59  SER A C     
544  O O     . SER B 59  ? 2.44263 2.43468 2.32091 -0.08406 0.54474  -0.38973 59  SER A O     
545  C CB    . SER B 59  ? 2.38712 2.37782 2.22705 -0.09580 0.48731  -0.37243 59  SER A CB    
546  O OG    . SER B 59  ? 2.45886 2.44748 2.29344 -0.09891 0.45937  -0.36546 59  SER A OG    
547  N N     . ILE B 60  ? 2.44854 2.47486 2.40323 -0.07310 0.53565  -0.35720 60  ILE A N     
548  C CA    . ILE B 60  ? 2.42510 2.45615 2.39745 -0.06830 0.56514  -0.36189 60  ILE A CA    
549  C C     . ILE B 60  ? 2.40016 2.43098 2.42732 -0.05733 0.57589  -0.36661 60  ILE A C     
550  O O     . ILE B 60  ? 2.30372 2.34819 2.37651 -0.05125 0.56422  -0.35127 60  ILE A O     
551  C CB    . ILE B 60  ? 2.40619 2.45902 2.39087 -0.06839 0.56698  -0.34197 60  ILE A CB    
552  C CG1   . ILE B 60  ? 2.43896 2.49160 2.36938 -0.07945 0.55649  -0.33707 60  ILE A CG1   
553  C CG2   . ILE B 60  ? 2.27857 2.33725 2.28738 -0.06269 0.59812  -0.34600 60  ILE A CG2   
554  C CD1   . ILE B 60  ? 2.36899 2.44207 2.30908 -0.08031 0.55729  -0.31755 60  ILE A CD1   
555  N N     . GLU B 61  ? 2.49724 2.51230 2.51997 -0.05503 0.59833  -0.38756 61  GLU A N     
556  C CA    . GLU B 61  ? 2.51180 2.52532 2.58628 -0.04447 0.61276  -0.39386 61  GLU A CA    
557  C C     . GLU B 61  ? 2.65747 2.68275 2.76118 -0.03854 0.64064  -0.39120 61  GLU A C     
558  O O     . GLU B 61  ? 2.74500 2.77386 2.81984 -0.04330 0.65346  -0.39095 61  GLU A O     
559  C CB    . GLU B 61  ? 2.45069 2.43873 2.50601 -0.04498 0.62155  -0.41919 61  GLU A CB    
560  C CG    . GLU B 61  ? 2.65518 2.63158 2.69118 -0.04960 0.59434  -0.42180 61  GLU A CG    
561  C CD    . GLU B 61  ? 2.68099 2.63140 2.69761 -0.05072 0.60284  -0.44714 61  GLU A CD    
562  O OE1   . GLU B 61  ? 2.50882 2.45043 2.53512 -0.04620 0.63026  -0.46255 61  GLU A OE1   
563  O OE2   . GLU B 61  ? 2.64029 2.57872 2.63246 -0.05621 0.58219  -0.45164 61  GLU A OE2   
564  N N     . GLU B 62  ? 2.59108 2.62273 2.75427 -0.02809 0.64989  -0.38845 62  GLU A N     
565  C CA    . GLU B 62  ? 2.51673 2.56089 2.71611 -0.02150 0.67602  -0.38438 62  GLU A CA    
566  C C     . GLU B 62  ? 2.59273 2.62168 2.76239 -0.02279 0.70735  -0.40635 62  GLU A C     
567  O O     . GLU B 62  ? 2.67085 2.70917 2.83951 -0.02281 0.72721  -0.40295 62  GLU A O     
568  C CB    . GLU B 62  ? 2.44649 2.49834 2.71602 -0.01023 0.67899  -0.37826 62  GLU A CB    
569  C CG    . GLU B 62  ? 2.41333 2.48192 2.71580 -0.00876 0.65008  -0.35485 62  GLU A CG    
570  C CD    . GLU B 62  ? 2.25392 2.33177 2.62710 0.00189  0.65407  -0.34687 62  GLU A CD    
571  O OE1   . GLU B 62  ? 2.18336 2.25192 2.57963 0.00843  0.67719  -0.36147 62  GLU A OE1   
572  O OE2   . GLU B 62  ? 2.11248 2.20648 2.51791 0.00348  0.63412  -0.32592 62  GLU A OE2   
573  N N     . ASN B 63  ? 2.57441 2.57935 2.71801 -0.02439 0.71199  -0.42902 63  ASN A N     
574  C CA    . ASN B 63  ? 2.52808 2.51539 2.64023 -0.02608 0.73793  -0.44952 63  ASN A CA    
575  C C     . ASN B 63  ? 2.56262 2.54959 2.61492 -0.03655 0.73920  -0.44835 63  ASN A C     
576  O O     . ASN B 63  ? 2.57958 2.56050 2.61392 -0.03718 0.75658  -0.45365 63  ASN A O     
577  C CB    . ASN B 63  ? 2.50223 2.46259 2.59341 -0.02737 0.73535  -0.47180 63  ASN A CB    
578  C CG    . ASN B 63  ? 2.62875 2.58025 2.67696 -0.03667 0.70954  -0.47503 63  ASN A CG    
579  O OD1   . ASN B 63  ? 2.60843 2.57012 2.62779 -0.04407 0.69201  -0.46112 63  ASN A OD1   
580  N ND2   . ASN B 63  ? 2.62566 2.55784 2.67020 -0.03646 0.70223  -0.49006 63  ASN A ND2   
581  N N     . MET B 64  ? 2.68368 2.67711 2.70528 -0.04482 0.71809  -0.43918 64  MET A N     
582  C CA    . MET B 64  ? 2.62167 2.61613 2.58802 -0.05524 0.71887  -0.43700 64  MET A CA    
583  C C     . MET B 64  ? 2.64182 2.65817 2.63025 -0.05262 0.73094  -0.41942 64  MET A C     
584  O O     . MET B 64  ? 2.64450 2.66021 2.59283 -0.05927 0.73686  -0.41799 64  MET A O     
585  C CB    . MET B 64  ? 2.58355 2.57929 2.51663 -0.06406 0.68411  -0.42601 64  MET A CB    
586  C CG    . MET B 64  ? 2.62417 2.59880 2.53334 -0.06767 0.66746  -0.44047 64  MET A CG    
587  S SD    . MET B 64  ? 2.37877 2.35786 2.26245 -0.07598 0.62598  -0.42461 64  MET A SD    
588  C CE    . MET B 64  ? 2.41006 2.38870 2.22705 -0.08898 0.62728  -0.42269 64  MET A CE    
589  N N     . LEU B 65  ? 2.67044 2.70597 2.72209 -0.04335 0.73265  -0.40471 65  LEU A N     
590  C CA    . LEU B 65  ? 2.61003 2.66812 2.68711 -0.04117 0.74079  -0.38568 65  LEU A CA    
591  C C     . LEU B 65  ? 2.52965 2.58857 2.63874 -0.03296 0.76413  -0.38684 65  LEU A C     
592  O O     . LEU B 65  ? 2.55540 2.63237 2.68744 -0.03079 0.77188  -0.37120 65  LEU A O     
593  C CB    . LEU B 65  ? 2.53398 2.61318 2.66011 -0.03679 0.71832  -0.36185 65  LEU A CB    
594  C CG    . LEU B 65  ? 2.49639 2.57787 2.59788 -0.04374 0.68263  -0.34980 65  LEU A CG    
595  C CD1   . LEU B 65  ? 2.45190 2.55459 2.60385 -0.03905 0.66351  -0.32556 65  LEU A CD1   
596  C CD2   . LEU B 65  ? 2.52017 2.60117 2.56329 -0.05482 0.67821  -0.34728 65  LEU A CD2   
597  N N     . GLN B 66  ? 2.45901 2.49873 2.57082 -0.02855 0.77536  -0.40476 66  GLN A N     
598  C CA    . GLN B 66  ? 2.57059 2.61047 2.71669 -0.02022 0.79787  -0.40631 66  GLN A CA    
599  C C     . GLN B 66  ? 2.64833 2.68654 2.75655 -0.02497 0.81366  -0.40756 66  GLN A C     
600  O O     . GLN B 66  ? 2.63393 2.68331 2.77447 -0.01922 0.82988  -0.39905 66  GLN A O     
601  C CB    . GLN B 66  ? 2.53457 2.55280 2.69058 -0.01504 0.80506  -0.42592 66  GLN A CB    
602  C CG    . GLN B 66  ? 2.45638 2.47732 2.65855 -0.00884 0.79137  -0.42355 66  GLN A CG    
603  C CD    . GLN B 66  ? 2.44145 2.43761 2.63814 -0.00675 0.79370  -0.44491 66  GLN A CD    
604  O OE1   . GLN B 66  ? 2.55814 2.53576 2.72510 -0.00842 0.80832  -0.46112 66  GLN A OE1   
605  N NE2   . GLN B 66  ? 2.40573 2.40138 2.63109 -0.00330 0.77902  -0.44483 66  GLN A NE2   
606  N N     . GLN B 67  ? 2.65619 2.68093 2.69713 -0.03557 0.80866  -0.41728 67  GLN A N     
607  C CA    . GLN B 67  ? 2.67083 2.69345 2.67073 -0.04118 0.82180  -0.41820 67  GLN A CA    
608  C C     . GLN B 67  ? 2.58814 2.62975 2.57112 -0.04789 0.81208  -0.39946 67  GLN A C     
609  O O     . GLN B 67  ? 2.66621 2.70772 2.61354 -0.05336 0.82089  -0.39813 67  GLN A O     
610  C CB    . GLN B 67  ? 2.75114 2.74697 2.68553 -0.04951 0.82229  -0.43942 67  GLN A CB    
611  C CG    . GLN B 67  ? 2.72765 2.70206 2.67177 -0.04413 0.83284  -0.45962 67  GLN A CG    
612  C CD    . GLN B 67  ? 2.69760 2.67398 2.67903 -0.03499 0.85858  -0.46087 67  GLN A CD    
613  O OE1   . GLN B 67  ? 2.75679 2.74293 2.73319 -0.03555 0.87186  -0.45288 67  GLN A OE1   
614  N NE2   . GLN B 67  ? 2.67939 2.64662 2.69982 -0.02651 0.86567  -0.47048 67  GLN A NE2   
615  N N     . ALA B 68  ? 2.59419 2.65136 2.60236 -0.04762 0.79400  -0.38531 68  ALA A N     
616  C CA    . ALA B 68  ? 2.55554 2.63117 2.55063 -0.05419 0.78287  -0.36654 68  ALA A CA    
617  C C     . ALA B 68  ? 2.58646 2.68485 2.63136 -0.04761 0.79440  -0.34807 68  ALA A C     
618  O O     . ALA B 68  ? 2.60709 2.71055 2.70790 -0.03733 0.80382  -0.34640 68  ALA A O     
619  C CB    . ALA B 68  ? 2.43174 2.51330 2.43165 -0.05705 0.75914  -0.36001 68  ALA A CB    
620  N N     . PRO B 69  ? 2.48112 2.59342 2.50889 -0.05336 0.79354  -0.33350 69  PRO A N     
621  C CA    . PRO B 69  ? 2.48639 2.62080 2.56085 -0.04793 0.80290  -0.31497 69  PRO A CA    
622  C C     . PRO B 69  ? 2.53727 2.69272 2.65727 -0.04574 0.78679  -0.29548 69  PRO A C     
623  O O     . PRO B 69  ? 2.44530 2.59968 2.54960 -0.05071 0.76726  -0.29456 69  PRO A O     
624  C CB    . PRO B 69  ? 2.49023 2.62717 2.51737 -0.05661 0.80729  -0.30994 69  PRO A CB    
625  C CG    . PRO B 69  ? 2.42942 2.55675 2.40060 -0.06749 0.78748  -0.31427 69  PRO A CG    
626  C CD    . PRO B 69  ? 2.44074 2.54759 2.40434 -0.06547 0.78319  -0.33398 69  PRO A CD    
627  N N     . TYR B 70  ? 2.55466 2.72871 2.73048 -0.03869 0.79439  -0.27998 70  TYR A N     
628  C CA    . TYR B 70  ? 2.46342 2.65884 2.68367 -0.03733 0.77852  -0.25922 70  TYR A CA    
629  C C     . TYR B 70  ? 2.42559 2.63296 2.61573 -0.04687 0.76913  -0.24475 70  TYR A C     
630  O O     . TYR B 70  ? 2.55001 2.75142 2.69471 -0.05274 0.77771  -0.24907 70  TYR A O     
631  C CB    . TYR B 70  ? 2.43702 2.64732 2.72728 -0.02713 0.78823  -0.24721 70  TYR A CB    
632  C CG    . TYR B 70  ? 2.42432 2.62543 2.75342 -0.01768 0.79228  -0.25766 70  TYR A CG    
633  C CD1   . TYR B 70  ? 2.53070 2.71599 2.85653 -0.01266 0.81209  -0.27435 70  TYR A CD1   
634  C CD2   . TYR B 70  ? 2.40806 2.61618 2.77758 -0.01399 0.77618  -0.25040 70  TYR A CD2   
635  C CE1   . TYR B 70  ? 2.54727 2.72366 2.90936 -0.00426 0.81558  -0.28349 70  TYR A CE1   
636  C CE2   . TYR B 70  ? 2.46621 2.66614 2.87213 -0.00553 0.77908  -0.25894 70  TYR A CE2   
637  C CZ    . TYR B 70  ? 2.53498 2.71886 2.93759 -0.00063 0.79879  -0.27550 70  TYR A CZ    
638  O OH    . TYR B 70  ? 2.50972 2.68492 2.94886 0.00750  0.80156  -0.28366 70  TYR A OH    
639  N N     . PHE B 71  ? 2.21655 2.44022 2.43152 -0.04865 0.75184  -0.22754 71  PHE A N     
640  C CA    . PHE B 71  ? 2.21910 2.45262 2.40371 -0.05840 0.73964  -0.21344 71  PHE A CA    
641  C C     . PHE B 71  ? 2.39001 2.63580 2.58149 -0.05872 0.75493  -0.20230 71  PHE A C     
642  O O     . PHE B 71  ? 2.41693 2.66139 2.56220 -0.06717 0.75459  -0.20045 71  PHE A O     
643  C CB    . PHE B 71  ? 2.18605 2.43105 2.39713 -0.05849 0.70681  -0.19372 71  PHE A CB    
644  C CG    . PHE B 71  ? 2.33964 2.58791 2.51054 -0.06852 0.68471  -0.18164 71  PHE A CG    
645  C CD1   . PHE B 71  ? 2.24805 2.48171 2.37056 -0.07469 0.66441  -0.18908 71  PHE A CD1   
646  C CD2   . PHE B 71  ? 2.35718 2.62304 2.54049 -0.07175 0.68422  -0.16253 71  PHE A CD2   
647  C CE1   . PHE B 71  ? 2.12547 2.36203 2.21373 -0.08352 0.64471  -0.17775 71  PHE A CE1   
648  C CE2   . PHE B 71  ? 2.35262 2.62074 2.50046 -0.08075 0.66427  -0.15168 71  PHE A CE2   
649  C CZ    . PHE B 71  ? 2.27027 2.52376 2.37109 -0.08645 0.64480  -0.15930 71  PHE A CZ    
650  N N     . ASN B 72  ? 2.48833 2.74527 2.73513 -0.04993 0.76659  -0.19455 72  ASN A N     
651  C CA    . ASN B 72  ? 2.44742 2.71827 2.70668 -0.04993 0.77918  -0.18138 72  ASN A CA    
652  C C     . ASN B 72  ? 2.53138 2.79064 2.73052 -0.05612 0.79148  -0.19190 72  ASN A C     
653  O O     . ASN B 72  ? 2.56310 2.83176 2.74043 -0.06336 0.78829  -0.17980 72  ASN A O     
654  C CB    . ASN B 72  ? 2.35232 2.63085 2.67206 -0.03913 0.79383  -0.17757 72  ASN A CB    
655  C CG    . ASN B 72  ? 2.42566 2.68536 2.74534 -0.03219 0.80734  -0.19885 72  ASN A CG    
656  O OD1   . ASN B 72  ? 2.44696 2.68762 2.72083 -0.03563 0.80523  -0.21680 72  ASN A OD1   
657  N ND2   . ASN B 72  ? 2.43014 2.69431 2.80094 -0.02277 0.82066  -0.19693 72  ASN A ND2   
658  N N     . GLN B 73  ? 2.54009 2.77941 2.71310 -0.05381 0.80431  -0.21313 73  GLN A N     
659  C CA    . GLN B 73  ? 2.50310 2.73059 2.61967 -0.05955 0.81702  -0.22346 73  GLN A CA    
660  C C     . GLN B 73  ? 2.61730 2.84141 2.67649 -0.07162 0.80023  -0.22100 73  GLN A C     
661  O O     . GLN B 73  ? 2.55765 2.79054 2.59611 -0.07764 0.80212  -0.20996 73  GLN A O     
662  C CB    . GLN B 73  ? 2.41053 2.61501 2.50883 -0.05565 0.82962  -0.24763 73  GLN A CB    
663  C CG    . GLN B 73  ? 2.42212 2.62842 2.57790 -0.04371 0.84555  -0.25054 73  GLN A CG    
664  C CD    . GLN B 73  ? 2.43621 2.62467 2.59796 -0.03874 0.84416  -0.26863 73  GLN A CD    
665  O OE1   . GLN B 73  ? 2.46836 2.65675 2.64002 -0.03897 0.82621  -0.26766 73  GLN A OE1   
666  N NE2   . GLN B 73  ? 2.50066 2.67365 2.65693 -0.03428 0.86342  -0.28530 73  GLN A NE2   
667  N N     . VAL B 74  ? 2.57059 2.78303 2.60706 -0.07509 0.78382  -0.22998 74  VAL A N     
668  C CA    . VAL B 74  ? 2.45996 2.66717 2.43967 -0.08696 0.76684  -0.22871 74  VAL A CA    
669  C C     . VAL B 74  ? 2.45403 2.68260 2.45112 -0.09125 0.75437  -0.20506 74  VAL A C     
670  O O     . VAL B 74  ? 2.44406 2.67329 2.39886 -0.10074 0.74763  -0.19889 74  VAL A O     
671  C CB    . VAL B 74  ? 2.42706 2.61864 2.38476 -0.08940 0.75105  -0.24220 74  VAL A CB    
672  C CG1   . VAL B 74  ? 2.41583 2.58475 2.35155 -0.08648 0.76257  -0.26582 74  VAL A CG1   
673  C CG2   . VAL B 74  ? 2.43803 2.64006 2.44695 -0.08392 0.73888  -0.23457 74  VAL A CG2   
674  N N     . ALA B 75  ? 2.48079 2.72583 2.53806 -0.08479 0.75120  -0.19185 75  ALA A N     
675  C CA    . ALA B 75  ? 2.45522 2.71981 2.53139 -0.08920 0.73772  -0.16929 75  ALA A CA    
676  C C     . ALA B 75  ? 2.42528 2.69742 2.47826 -0.09495 0.74531  -0.15905 75  ALA A C     
677  O O     . ALA B 75  ? 2.41558 2.69127 2.43836 -0.10438 0.73175  -0.14933 75  ALA A O     
678  C CB    . ALA B 75  ? 2.31493 2.59622 2.46235 -0.08064 0.73767  -0.15637 75  ALA A CB    
679  N N     . GLN B 76  ? 2.50613 2.78042 2.57306 -0.08950 0.76646  -0.16113 76  GLN A N     
680  C CA    . GLN B 76  ? 2.51019 2.79340 2.55972 -0.09435 0.77522  -0.15039 76  GLN A CA    
681  C C     . GLN B 76  ? 2.55596 2.82488 2.53327 -0.10486 0.76964  -0.15832 76  GLN A C     
682  O O     . GLN B 76  ? 2.47422 2.75172 2.43155 -0.11296 0.76119  -0.14428 76  GLN A O     
683  C CB    . GLN B 76  ? 2.48327 2.76829 2.55624 -0.08649 0.80024  -0.15472 76  GLN A CB    
684  C CG    . GLN B 76  ? 2.38219 2.67159 2.51757 -0.07495 0.80671  -0.15621 76  GLN A CG    
685  C CD    . GLN B 76  ? 2.36872 2.68125 2.56416 -0.07192 0.79972  -0.13378 76  GLN A CD    
686  O OE1   . GLN B 76  ? 2.32212 2.64031 2.57155 -0.06335 0.80115  -0.13144 76  GLN A OE1   
687  N NE2   . GLN B 76  ? 2.38695 2.71274 2.57403 -0.07930 0.79109  -0.11649 76  GLN A NE2   
688  N N     . GLU B 77  ? 2.58796 2.83568 2.52865 -0.10501 0.77307  -0.17940 77  GLU A N     
689  C CA    . GLU B 77  ? 2.50758 2.74027 2.37844 -0.11525 0.76734  -0.18751 77  GLU A CA    
690  C C     . GLU B 77  ? 2.46727 2.70020 2.31500 -0.12406 0.74148  -0.18016 77  GLU A C     
691  O O     . GLU B 77  ? 2.43751 2.67259 2.24853 -0.13336 0.73366  -0.17105 77  GLU A O     
692  C CB    . GLU B 77  ? 2.43342 2.64275 2.27481 -0.11333 0.77526  -0.21190 77  GLU A CB    
693  C CG    . GLU B 77  ? 2.45805 2.65057 2.22809 -0.12413 0.76772  -0.22073 77  GLU A CG    
694  C CD    . GLU B 77  ? 2.49828 2.66651 2.23821 -0.12354 0.77071  -0.24465 77  GLU A CD    
695  O OE1   . GLU B 77  ? 2.50199 2.66605 2.27711 -0.11431 0.77952  -0.25500 77  GLU A OE1   
696  O OE2   . GLU B 77  ? 2.52865 2.68199 2.21082 -0.13256 0.76349  -0.25243 77  GLU A OE2   
697  N N     . ILE B 78  ? 2.47593 2.70710 2.34539 -0.12126 0.72873  -0.18338 78  ILE A N     
698  C CA    . ILE B 78  ? 2.45660 2.68636 2.30256 -0.12967 0.70405  -0.17827 78  ILE A CA    
699  C C     . ILE B 78  ? 2.48491 2.73302 2.34231 -0.13455 0.69246  -0.15448 78  ILE A C     
700  O O     . ILE B 78  ? 2.47678 2.72156 2.29236 -0.14396 0.67620  -0.14859 78  ILE A O     
701  C CB    . ILE B 78  ? 2.31480 2.54126 2.19283 -0.12272 0.68716  -0.18186 78  ILE A CB    
702  C CG1   . ILE B 78  ? 2.31298 2.52109 2.18074 -0.11852 0.69971  -0.20586 78  ILE A CG1   
703  C CG2   . ILE B 78  ? 2.31280 2.53735 2.17272 -0.12806 0.65178  -0.17212 78  ILE A CG2   
704  C CD1   . ILE B 78  ? 2.32836 2.53371 2.23242 -0.11055 0.68347  -0.20843 78  ILE A CD1   
705  N N     . TYR B 79  ? 2.48440 2.75053 2.39684 -0.12827 0.69864  -0.14060 79  TYR A N     
706  C CA    . TYR B 79  ? 2.42277 2.70568 2.35066 -0.13219 0.68305  -0.11684 79  TYR A CA    
707  C C     . TYR B 79  ? 2.47251 2.75541 2.35297 -0.14279 0.68829  -0.11212 79  TYR A C     
708  O O     . TYR B 79  ? 2.48206 2.76782 2.34511 -0.14960 0.66514  -0.09890 79  TYR A O     
709  C CB    . TYR B 79  ? 2.30349 2.60529 2.29499 -0.12467 0.69520  -0.10426 79  TYR A CB    
710  C CG    . TYR B 79  ? 2.30997 2.62889 2.32172 -0.12846 0.67968  -0.07997 79  TYR A CG    
711  C CD1   . TYR B 79  ? 2.29892 2.62232 2.33454 -0.12727 0.65056  -0.06796 79  TYR A CD1   
712  C CD2   . TYR B 79  ? 2.21327 2.54335 2.22021 -0.13341 0.69449  -0.06920 79  TYR A CD2   
713  C CE1   . TYR B 79  ? 2.23876 2.57630 2.29200 -0.13104 0.63625  -0.04664 79  TYR A CE1   
714  C CE2   . TYR B 79  ? 2.17449 2.51952 2.20058 -0.13711 0.68002  -0.04719 79  TYR A CE2   
715  C CZ    . TYR B 79  ? 2.15307 2.50141 2.20206 -0.13598 0.65067  -0.03621 79  TYR A CZ    
716  O OH    . TYR B 79  ? 2.11360 2.47528 2.18053 -0.13994 0.63623  -0.01528 79  TYR A OH    
717  N N     . ASP B 80  ? 2.45518 2.73299 2.31598 -0.14186 0.70909  -0.12047 80  ASP A N     
718  C CA    . ASP B 80  ? 2.43468 2.71307 2.25360 -0.15031 0.71051  -0.11319 80  ASP A CA    
719  C C     . ASP B 80  ? 2.44903 2.71469 2.21213 -0.16104 0.69032  -0.11613 80  ASP A C     
720  O O     . ASP B 80  ? 2.43032 2.70236 2.17333 -0.16944 0.68035  -0.10163 80  ASP A O     
721  C CB    . ASP B 80  ? 2.44219 2.71400 2.24524 -0.14692 0.73346  -0.12388 80  ASP A CB    
722  C CG    . ASP B 80  ? 2.51194 2.79333 2.36885 -0.13555 0.75417  -0.12450 80  ASP A CG    
723  O OD1   . ASP B 80  ? 2.58558 2.88635 2.48557 -0.13328 0.75594  -0.10697 80  ASP A OD1   
724  O OD2   . ASP B 80  ? 2.50526 2.77435 2.36093 -0.12934 0.76787  -0.14223 80  ASP A OD2   
725  N N     . LYS B 81  ? 2.47297 2.72140 2.21293 -0.16093 0.68404  -0.13362 81  LYS A N     
726  C CA    . LYS B 81  ? 2.42205 2.65728 2.10734 -0.17129 0.66451  -0.13721 81  LYS A CA    
727  C C     . LYS B 81  ? 2.32322 2.56586 2.02143 -0.17404 0.63534  -0.12177 81  LYS A C     
728  O O     . LYS B 81  ? 2.23515 2.47625 1.89828 -0.18335 0.61942  -0.11291 81  LYS A O     
729  C CB    . LYS B 81  ? 2.46366 2.67863 2.12644 -0.16944 0.66355  -0.15952 81  LYS A CB    
730  C CG    . LYS B 81  ? 2.45909 2.66675 2.13589 -0.16025 0.68679  -0.17538 81  LYS A CG    
731  C CD    . LYS B 81  ? 2.35456 2.54492 2.02489 -0.15701 0.68355  -0.19552 81  LYS A CD    
732  C CE    . LYS B 81  ? 2.47965 2.66198 2.16496 -0.14802 0.70611  -0.21117 81  LYS A CE    
733  N NZ    . LYS B 81  ? 2.55370 2.72686 2.19835 -0.15180 0.71919  -0.21727 81  LYS A NZ    
734  N N     . ILE B 82  ? 2.34765 2.59698 2.09549 -0.16510 0.62498  -0.11739 82  ILE A N     
735  C CA    . ILE B 82  ? 2.21690 2.46998 1.97689 -0.16582 0.59245  -0.10358 82  ILE A CA    
736  C C     . ILE B 82  ? 2.25605 2.52830 2.05057 -0.16584 0.58794  -0.08131 82  ILE A C     
737  O O     . ILE B 82  ? 2.26449 2.53978 2.06491 -0.16776 0.56208  -0.06872 82  ILE A O     
738  C CB    . ILE B 82  ? 2.20719 2.45489 1.99685 -0.15718 0.58092  -0.11144 82  ILE A CB    
739  C CG1   . ILE B 82  ? 2.27461 2.53467 2.12344 -0.14709 0.59469  -0.10825 82  ILE A CG1   
740  C CG2   . ILE B 82  ? 2.16467 2.39291 1.92087 -0.15748 0.58496  -0.13346 82  ILE A CG2   
741  C CD1   . ILE B 82  ? 2.25402 2.50929 2.13383 -0.13863 0.58435  -0.11528 82  ILE A CD1   
742  N N     . LYS B 83  ? 2.31320 2.59746 2.12963 -0.16399 0.61184  -0.07651 83  LYS A N     
743  C CA    . LYS B 83  ? 2.14063 2.44357 1.99498 -0.16371 0.60721  -0.05496 83  LYS A CA    
744  C C     . LYS B 83  ? 2.05883 2.36337 1.88113 -0.17394 0.58984  -0.04094 83  LYS A C     
745  O O     . LYS B 83  ? 2.04588 2.36268 1.89522 -0.17463 0.57678  -0.02279 83  LYS A O     
746  C CB    . LYS B 83  ? 2.21417 2.52974 2.09640 -0.16047 0.63730  -0.05217 83  LYS A CB    
747  C CG    . LYS B 83  ? 2.34081 2.65376 2.18195 -0.16742 0.65999  -0.05679 83  LYS A CG    
748  C CD    . LYS B 83  ? 2.22616 2.55083 2.09950 -0.16181 0.68835  -0.05451 83  LYS A CD    
749  C CE    . LYS B 83  ? 2.24143 2.56154 2.07532 -0.16509 0.70140  -0.05730 83  LYS A CE    
750  N NZ    . LYS B 83  ? 2.28799 2.61861 2.15511 -0.15752 0.72438  -0.05505 83  LYS A NZ    
751  N N     . ASP B 84  ? 2.06724 2.35952 1.83461 -0.18182 0.58948  -0.04886 84  ASP A N     
752  C CA    . ASP B 84  ? 2.15755 2.45049 1.89258 -0.19200 0.57279  -0.03557 84  ASP A CA    
753  C C     . ASP B 84  ? 2.07534 2.35226 1.77214 -0.19613 0.55006  -0.04317 84  ASP A C     
754  O O     . ASP B 84  ? 2.09519 2.36815 1.75267 -0.20557 0.54036  -0.03743 84  ASP A O     
755  C CB    . ASP B 84  ? 2.19565 2.49195 1.90156 -0.19940 0.59375  -0.03297 84  ASP A CB    
756  C CG    . ASP B 84  ? 2.17181 2.48438 1.91571 -0.19551 0.61780  -0.02508 84  ASP A CG    
757  O OD1   . ASP B 84  ? 2.09599 2.42256 1.87857 -0.19376 0.60842  -0.00791 84  ASP A OD1   
758  O OD2   . ASP B 84  ? 2.30006 2.61069 2.03527 -0.19406 0.64513  -0.03606 84  ASP A OD2   
759  N N     . CYS B 85  ? 2.11977 2.38817 1.82908 -0.18945 0.54170  -0.05484 85  CYS A N     
760  C CA    . CYS B 85  ? 2.04258 2.29594 1.71942 -0.19279 0.51978  -0.06212 85  CYS A CA    
761  C C     . CYS B 85  ? 1.98251 2.23802 1.69182 -0.18749 0.49493  -0.05480 85  CYS A C     
762  O O     . CYS B 85  ? 1.99118 2.25308 1.74450 -0.17873 0.49932  -0.05526 85  CYS A O     
763  C CB    . CYS B 85  ? 2.05372 2.29196 1.70851 -0.19079 0.53157  -0.08450 85  CYS A CB    
764  S SG    . CYS B 85  ? 2.32604 2.55889 1.93793 -0.19741 0.56176  -0.09549 85  CYS A SG    
765  N N     . ILE B 86  ? 1.91518 2.16539 1.60369 -0.19277 0.47022  -0.04810 86  ILE A N     
766  C CA    . ILE B 86  ? 1.86413 2.11495 1.57950 -0.18832 0.44622  -0.04140 86  ILE A CA    
767  C C     . ILE B 86  ? 1.82707 2.06947 1.55687 -0.18039 0.44658  -0.05691 86  ILE A C     
768  O O     . ILE B 86  ? 1.99221 2.22155 1.69066 -0.18227 0.44985  -0.07190 86  ILE A O     
769  C CB    . ILE B 86  ? 1.81610 2.06051 1.50207 -0.19556 0.42186  -0.03382 86  ILE A CB    
770  C CG1   . ILE B 86  ? 1.96558 2.21723 1.63444 -0.20400 0.42236  -0.01913 86  ILE A CG1   
771  C CG2   . ILE B 86  ? 1.84462 2.08931 1.55757 -0.19101 0.39894  -0.02705 86  ILE A CG2   
772  C CD1   . ILE B 86  ? 1.81954 2.06598 1.46478 -0.21079 0.39811  -0.00969 86  ILE A CD1   
773  N N     . PHE B 87  ? 1.83678 2.08600 1.61174 -0.17237 0.44272  -0.05309 87  PHE A N     
774  C CA    . PHE B 87  ? 1.95281 2.19509 1.74501 -0.16465 0.44388  -0.06665 87  PHE A CA    
775  C C     . PHE B 87  ? 1.93409 2.16584 1.71387 -0.16517 0.41918  -0.06866 87  PHE A C     
776  O O     . PHE B 87  ? 1.86918 2.10468 1.66059 -0.16576 0.39990  -0.05599 87  PHE A O     
777  C CB    . PHE B 87  ? 2.01673 2.27058 1.86262 -0.15624 0.44938  -0.06113 87  PHE A CB    
778  C CG    . PHE B 87  ? 2.00878 2.25665 1.87462 -0.14815 0.45586  -0.07536 87  PHE A CG    
779  C CD1   . PHE B 87  ? 1.99579 2.24256 1.86563 -0.14471 0.48126  -0.08785 87  PHE A CD1   
780  C CD2   . PHE B 87  ? 1.86203 2.10486 1.74239 -0.14404 0.43710  -0.07639 87  PHE A CD2   
781  C CE1   . PHE B 87  ? 1.96821 2.20895 1.85773 -0.13720 0.48731  -0.10095 87  PHE A CE1   
782  C CE2   . PHE B 87  ? 1.90023 2.13757 1.79967 -0.13680 0.44275  -0.08890 87  PHE A CE2   
783  C CZ    . PHE B 87  ? 2.04565 2.28186 1.95023 -0.13333 0.46760  -0.10117 87  PHE A CZ    
784  N N     . VAL B 88  ? 1.96331 2.18149 1.71973 -0.16505 0.42017  -0.08470 88  VAL A N     
785  C CA    . VAL B 88  ? 1.95421 2.16154 1.69626 -0.16596 0.39829  -0.08786 88  VAL A CA    
786  C C     . VAL B 88  ? 1.98437 2.18418 1.74319 -0.15851 0.40155  -0.10243 88  VAL A C     
787  O O     . VAL B 88  ? 2.05915 2.25664 1.82059 -0.15554 0.42191  -0.11476 88  VAL A O     
788  C CB    . VAL B 88  ? 1.89602 2.09272 1.58662 -0.17534 0.39261  -0.09191 88  VAL A CB    
789  C CG1   . VAL B 88  ? 1.88107 2.06850 1.56068 -0.17656 0.36843  -0.09194 88  VAL A CG1   
790  C CG2   . VAL B 88  ? 1.81221 2.01666 1.48600 -0.18290 0.39328  -0.07812 88  VAL A CG2   
791  N N     . ALA B 89  ? 1.80472 2.00055 1.57564 -0.15545 0.38206  -0.10093 89  ALA A N     
792  C CA    . ALA B 89  ? 1.83722 2.02522 1.62316 -0.14889 0.38229  -0.11379 89  ALA A CA    
793  C C     . ALA B 89  ? 1.87713 2.05977 1.66483 -0.14828 0.35771  -0.10998 89  ALA A C     
794  O O     . ALA B 89  ? 1.82529 2.01195 1.61100 -0.15139 0.34198  -0.09657 89  ALA A O     
795  C CB    . ALA B 89  ? 1.85660 2.05372 1.68866 -0.14026 0.39556  -0.11362 89  ALA A CB    
796  N N     . HIS B 90  ? 1.88947 2.06261 1.68153 -0.14418 0.35516  -0.12209 90  HIS A N     
797  C CA    . HIS B 90  ? 1.68836 1.85637 1.48652 -0.14246 0.33394  -0.11966 90  HIS A CA    
798  C C     . HIS B 90  ? 1.80804 1.98389 1.65221 -0.13432 0.33188  -0.11386 90  HIS A C     
799  O O     . HIS B 90  ? 1.83347 2.00934 1.70046 -0.12831 0.34423  -0.12235 90  HIS A O     
800  C CB    . HIS B 90  ? 1.64053 1.79376 1.41751 -0.14320 0.33137  -0.13524 90  HIS A CB    
801  C CG    . HIS B 90  ? 1.68780 1.83520 1.46460 -0.14299 0.30926  -0.13221 90  HIS A CG    
802  N ND1   . HIS B 90  ? 1.80094 1.94648 1.55469 -0.14917 0.29265  -0.12345 90  HIS A ND1   
803  C CD2   . HIS B 90  ? 1.75830 1.90149 1.55637 -0.13727 0.30150  -0.13632 90  HIS A CD2   
804  C CE1   . HIS B 90  ? 1.69425 1.83472 1.45533 -0.14706 0.27628  -0.12259 90  HIS A CE1   
805  N NE2   . HIS B 90  ? 1.72579 1.86479 1.51299 -0.14001 0.28119  -0.13023 90  HIS A NE2   
806  N N     . ASN B 91  ? 1.88743 2.06941 1.74497 -0.13440 0.31623  -0.09935 91  ASN A N     
807  C CA    . ASN B 91  ? 1.86082 2.05199 1.76016 -0.12835 0.31410  -0.09068 91  ASN A CA    
808  C C     . ASN B 91  ? 1.82711 2.02931 1.74756 -0.12636 0.33316  -0.08814 91  ASN A C     
809  O O     . ASN B 91  ? 1.79233 1.99678 1.73946 -0.12039 0.34536  -0.09422 91  ASN A O     
810  C CB    . ASN B 91  ? 1.76004 1.94542 1.67993 -0.12197 0.30966  -0.09836 91  ASN A CB    
811  C CG    . ASN B 91  ? 1.84734 2.04101 1.80694 -0.11687 0.30294  -0.08779 91  ASN A CG    
812  O OD1   . ASN B 91  ? 1.85311 2.05264 1.81774 -0.11901 0.29204  -0.07423 91  ASN A OD1   
813  N ND2   . ASN B 91  ? 1.85500 2.04857 1.84278 -0.11040 0.30902  -0.09387 91  ASN A ND2   
814  N N     . VAL B 92  ? 1.82999 2.03931 1.73949 -0.13151 0.33546  -0.07831 92  VAL A N     
815  C CA    . VAL B 92  ? 1.75080 1.96891 1.66824 -0.13163 0.35601  -0.07768 92  VAL A CA    
816  C C     . VAL B 92  ? 1.78666 2.01629 1.75124 -0.12539 0.36278  -0.07102 92  VAL A C     
817  O O     . VAL B 92  ? 1.84455 2.08072 1.82277 -0.12347 0.38243  -0.07330 92  VAL A O     
818  C CB    . VAL B 92  ? 1.79897 2.02189 1.69300 -0.13925 0.35463  -0.06719 92  VAL A CB    
819  C CG1   . VAL B 92  ? 1.84799 2.07918 1.76131 -0.14012 0.33933  -0.04985 92  VAL A CG1   
820  C CG2   . VAL B 92  ? 1.83644 2.06604 1.72842 -0.14059 0.37781  -0.06914 92  VAL A CG2   
821  N N     . ASP B 93  ? 1.81199 2.04422 1.80212 -0.12240 0.34715  -0.06250 93  ASP A N     
822  C CA    . ASP B 93  ? 1.77421 2.01748 1.80956 -0.11729 0.35146  -0.05473 93  ASP A CA    
823  C C     . ASP B 93  ? 1.88272 2.12578 1.93956 -0.11081 0.36977  -0.06651 93  ASP A C     
824  O O     . ASP B 93  ? 1.86369 2.11690 1.94797 -0.10816 0.38485  -0.06309 93  ASP A O     
825  C CB    . ASP B 93  ? 1.66357 1.90667 1.71815 -0.11545 0.33079  -0.04598 93  ASP A CB    
826  C CG    . ASP B 93  ? 1.88880 2.13627 1.93773 -0.12077 0.31608  -0.03077 93  ASP A CG    
827  O OD1   . ASP B 93  ? 1.97039 2.22826 2.03130 -0.12292 0.32236  -0.02102 93  ASP A OD1   
828  O OD2   . ASP B 93  ? 1.91929 2.15950 1.95255 -0.12278 0.29852  -0.02861 93  ASP A OD2   
829  N N     . PHE B 94  ? 1.85806 2.08943 1.90383 -0.10822 0.36886  -0.08029 94  PHE A N     
830  C CA    . PHE B 94  ? 1.91424 2.14255 1.97768 -0.10205 0.38518  -0.09336 94  PHE A CA    
831  C C     . PHE B 94  ? 1.93095 2.16205 1.98738 -0.10265 0.40999  -0.10019 94  PHE A C     
832  O O     . PHE B 94  ? 2.02499 2.26575 2.11543 -0.09831 0.42500  -0.09738 94  PHE A O     
833  C CB    . PHE B 94  ? 1.80267 2.01577 1.84395 -0.10141 0.37845  -0.10748 94  PHE A CB    
834  C CG    . PHE B 94  ? 1.77947 1.98716 1.83775 -0.09515 0.39331  -0.12189 94  PHE A CG    
835  C CD1   . PHE B 94  ? 1.79536 2.00583 1.89398 -0.08844 0.38962  -0.11968 94  PHE A CD1   
836  C CD2   . PHE B 94  ? 1.83696 2.03583 1.87008 -0.09627 0.41052  -0.13779 94  PHE A CD2   
837  C CE1   . PHE B 94  ? 1.78707 1.99209 1.90322 -0.08249 0.40300  -0.13275 94  PHE A CE1   
838  C CE2   . PHE B 94  ? 1.85320 2.04573 1.90231 -0.09039 0.42450  -0.15188 94  PHE A CE2   
839  C CZ    . PHE B 94  ? 1.82690 2.02270 1.91869 -0.08328 0.42074  -0.14921 94  PHE A CZ    
840  N N     . ASP B 95  ? 1.83395 2.05652 1.84607 -0.10832 0.41432  -0.10874 95  ASP A N     
841  C CA    . ASP B 95  ? 1.86382 2.08662 1.86221 -0.10965 0.43846  -0.11709 95  ASP A CA    
842  C C     . ASP B 95  ? 1.95513 2.19352 1.97318 -0.11060 0.44847  -0.10344 95  ASP A C     
843  O O     . ASP B 95  ? 2.02360 2.26777 2.06197 -0.10697 0.47043  -0.10680 95  ASP A O     
844  C CB    . ASP B 95  ? 1.79256 2.00386 1.73656 -0.11733 0.43701  -0.12549 95  ASP A CB    
845  C CG    . ASP B 95  ? 1.97278 2.16879 1.89652 -0.11736 0.42476  -0.13758 95  ASP A CG    
846  O OD1   . ASP B 95  ? 2.11986 2.31359 2.03599 -0.11961 0.40244  -0.13057 95  ASP A OD1   
847  O OD2   . ASP B 95  ? 1.94471 2.13080 1.86154 -0.11504 0.43769  -0.15407 95  ASP A OD2   
848  N N     . LEU B 96  ? 1.89597 2.14120 1.90977 -0.11538 0.43279  -0.08781 96  LEU A N     
849  C CA    . LEU B 96  ? 1.86566 2.12537 1.89612 -0.11727 0.44059  -0.07399 96  LEU A CA    
850  C C     . LEU B 96  ? 1.92095 2.19247 2.00565 -0.11033 0.44743  -0.06716 96  LEU A C     
851  O O     . LEU B 96  ? 1.85038 2.13208 1.95439 -0.10913 0.46597  -0.06359 96  LEU A O     
852  C CB    . LEU B 96  ? 1.83599 2.09915 1.85313 -0.12359 0.41998  -0.05878 96  LEU A CB    
853  C CG    . LEU B 96  ? 1.90039 2.17782 1.93164 -0.12680 0.42511  -0.04326 96  LEU A CG    
854  C CD1   . LEU B 96  ? 1.89056 2.16939 1.90040 -0.12991 0.44789  -0.04886 96  LEU A CD1   
855  C CD2   . LEU B 96  ? 1.89606 2.17436 1.91263 -0.13298 0.40329  -0.02967 96  LEU A CD2   
856  N N     . ASN B 97  ? 1.93018 2.20076 2.04077 -0.10590 0.43261  -0.06461 97  ASN A N     
857  C CA    . ASN B 97  ? 2.04646 2.32834 2.20968 -0.09989 0.43650  -0.05658 97  ASN A CA    
858  C C     . ASN B 97  ? 2.04146 2.32242 2.22506 -0.09316 0.46007  -0.06940 97  ASN A C     
859  O O     . ASN B 97  ? 1.95166 2.24439 2.17182 -0.08970 0.47472  -0.06352 97  ASN A O     
860  C CB    . ASN B 97  ? 1.85306 2.13327 2.03526 -0.09772 0.41360  -0.05023 97  ASN A CB    
861  C CG    . ASN B 97  ? 1.64716 1.93141 1.82217 -0.10350 0.39253  -0.03445 97  ASN A CG    
862  O OD1   . ASN B 97  ? 1.76004 2.05376 1.93759 -0.10743 0.39545  -0.02345 97  ASN A OD1   
863  N ND2   . ASN B 97  ? 1.64731 1.92399 1.81385 -0.10404 0.37161  -0.03337 97  ASN A ND2   
864  N N     . PHE B 98  ? 1.99276 2.25957 2.15420 -0.09130 0.46418  -0.08685 98  PHE A N     
865  C CA    . PHE B 98  ? 2.04226 2.30611 2.22056 -0.08501 0.48738  -0.10067 98  PHE A CA    
866  C C     . PHE B 98  ? 2.10829 2.37666 2.27674 -0.08673 0.51282  -0.10396 98  PHE A C     
867  O O     . PHE B 98  ? 2.08910 2.36496 2.29237 -0.08128 0.53286  -0.10467 98  PHE A O     
868  C CB    . PHE B 98  ? 1.95507 2.20127 2.10650 -0.08388 0.48554  -0.11916 98  PHE A CB    
869  C CG    . PHE B 98  ? 1.90135 2.14457 2.08402 -0.07765 0.47442  -0.12041 98  PHE A CG    
870  C CD1   . PHE B 98  ? 1.90475 2.14930 2.12573 -0.06984 0.49021  -0.12682 98  PHE A CD1   
871  C CD2   . PHE B 98  ? 1.83637 2.07549 2.01105 -0.07956 0.44869  -0.11482 98  PHE A CD2   
872  C CE1   . PHE B 98  ? 1.96472 2.20671 2.21518 -0.06435 0.47968  -0.12716 98  PHE A CE1   
873  C CE2   . PHE B 98  ? 1.80958 2.04612 2.01260 -0.07413 0.43876  -0.11540 98  PHE A CE2   
874  C CZ    . PHE B 98  ? 1.91204 2.15012 2.15278 -0.06668 0.45383  -0.12131 98  PHE A CZ    
875  N N     . ILE B 99  ? 2.14463 2.40887 2.26686 -0.09439 0.51246  -0.10522 99  ILE A N     
876  C CA    . ILE B 99  ? 2.13954 2.40777 2.24822 -0.09698 0.53628  -0.10769 99  ILE A CA    
877  C C     . ILE B 99  ? 2.15724 2.44436 2.30365 -0.09636 0.54152  -0.08960 99  ILE A C     
878  O O     . ILE B 99  ? 2.20467 2.49890 2.36913 -0.09370 0.56592  -0.09093 99  ILE A O     
879  C CB    . ILE B 99  ? 2.11079 2.37016 2.16036 -0.10617 0.53168  -0.11154 99  ILE A CB    
880  C CG1   . ILE B 99  ? 2.05955 2.30067 2.07309 -0.10655 0.53946  -0.13317 99  ILE A CG1   
881  C CG2   . ILE B 99  ? 2.17138 2.44037 2.21090 -0.11095 0.54751  -0.10407 99  ILE A CG2   
882  C CD1   . ILE B 99  ? 2.04324 2.27517 1.99845 -0.11600 0.53650  -0.13759 99  ILE A CD1   
883  N N     . LYS B 100 ? 2.08142 2.37663 2.24113 -0.09887 0.51904  -0.07247 100 LYS A N     
884  C CA    . LYS B 100 ? 2.09837 2.41123 2.29615 -0.09872 0.52139  -0.05445 100 LYS A CA    
885  C C     . LYS B 100 ? 2.12808 2.44941 2.38161 -0.09015 0.53405  -0.05339 100 LYS A C     
886  O O     . LYS B 100 ? 2.05844 2.39213 2.33970 -0.08852 0.55214  -0.04686 100 LYS A O     
887  C CB    . LYS B 100 ? 2.07434 2.39167 2.27527 -0.10299 0.49320  -0.03789 100 LYS A CB    
888  C CG    . LYS B 100 ? 1.93505 2.25112 2.09445 -0.11190 0.48490  -0.03185 100 LYS A CG    
889  C CD    . LYS B 100 ? 1.78405 2.10180 1.94570 -0.11555 0.45671  -0.01767 100 LYS A CD    
890  C CE    . LYS B 100 ? 1.81622 2.13296 1.93980 -0.12419 0.44884  -0.01091 100 LYS A CE    
891  N NZ    . LYS B 100 ? 2.02239 2.33645 2.14091 -0.12755 0.42119  -0.00084 100 LYS A NZ    
892  N N     . LYS B 101 ? 2.18208 2.49723 2.45413 -0.08463 0.52492  -0.05915 101 LYS A N     
893  C CA    . LYS B 101 ? 2.13720 2.45984 2.46360 -0.07639 0.53617  -0.05798 101 LYS A CA    
894  C C     . LYS B 101 ? 2.04827 2.36835 2.37738 -0.07187 0.56805  -0.07266 101 LYS A C     
895  O O     . LYS B 101 ? 2.12676 2.45895 2.49680 -0.06762 0.58578  -0.06689 101 LYS A O     
896  C CB    . LYS B 101 ? 2.02776 2.34301 2.36992 -0.07184 0.51970  -0.06175 101 LYS A CB    
897  C CG    . LYS B 101 ? 2.04395 2.36559 2.44157 -0.06314 0.53219  -0.06181 101 LYS A CG    
898  C CD    . LYS B 101 ? 1.99882 2.31056 2.40655 -0.05843 0.52020  -0.06936 101 LYS A CD    
899  C CE    . LYS B 101 ? 1.90193 2.21900 2.36375 -0.04959 0.53535  -0.07089 101 LYS A CE    
900  N NZ    . LYS B 101 ? 1.89980 2.20688 2.37237 -0.04491 0.52471  -0.07852 101 LYS A NZ    
901  N N     . ALA B 102 ? 1.97517 2.27906 2.26125 -0.07286 0.57580  -0.09182 102 ALA A N     
902  C CA    . ALA B 102 ? 2.13179 2.43039 2.41647 -0.06875 0.60634  -0.10803 102 ALA A CA    
903  C C     . ALA B 102 ? 2.25900 2.56766 2.53953 -0.07178 0.62772  -0.10280 102 ALA A C     
904  O O     . ALA B 102 ? 2.19180 2.50492 2.49823 -0.06653 0.65440  -0.10757 102 ALA A O     
905  C CB    . ALA B 102 ? 1.99920 2.27721 2.23297 -0.07091 0.60743  -0.12904 102 ALA A CB    
906  N N     . PHE B 103 ? 2.24758 2.55992 2.49671 -0.08017 0.61689  -0.09274 103 PHE A N     
907  C CA    . PHE B 103 ? 2.25817 2.58219 2.50753 -0.08349 0.63471  -0.08436 103 PHE A CA    
908  C C     . PHE B 103 ? 2.19550 2.53908 2.50681 -0.07917 0.63791  -0.06646 103 PHE A C     
909  O O     . PHE B 103 ? 2.15466 2.50749 2.48882 -0.07649 0.66327  -0.06502 103 PHE A O     
910  C CB    . PHE B 103 ? 2.27900 2.60262 2.48353 -0.09359 0.61933  -0.07603 103 PHE A CB    
911  C CG    . PHE B 103 ? 2.28003 2.58813 2.42302 -0.09924 0.62665  -0.09193 103 PHE A CG    
912  C CD1   . PHE B 103 ? 2.26824 2.56787 2.39848 -0.09654 0.65431  -0.10977 103 PHE A CD1   
913  C CD2   . PHE B 103 ? 2.21397 2.51554 2.31182 -0.10758 0.60579  -0.08881 103 PHE A CD2   
914  C CE1   . PHE B 103 ? 2.25320 2.53779 2.32466 -0.10270 0.66017  -0.12423 103 PHE A CE1   
915  C CE2   . PHE B 103 ? 2.17465 2.46219 2.21614 -0.11351 0.61126  -0.10230 103 PHE A CE2   
916  C CZ    . PHE B 103 ? 2.21605 2.49492 2.24327 -0.11140 0.63804  -0.12003 103 PHE A CZ    
917  N N     . LYS B 104 ? 2.23421 2.58410 2.57337 -0.07872 0.61239  -0.05247 104 LYS A N     
918  C CA    . LYS B 104 ? 2.15194 2.52020 2.54929 -0.07580 0.61159  -0.03392 104 LYS A CA    
919  C C     . LYS B 104 ? 2.16998 2.54248 2.61603 -0.06623 0.63364  -0.03950 104 LYS A C     
920  O O     . LYS B 104 ? 2.27734 2.66504 2.76492 -0.06376 0.64854  -0.02871 104 LYS A O     
921  C CB    . LYS B 104 ? 2.05847 2.42937 2.47123 -0.07751 0.57894  -0.02026 104 LYS A CB    
922  C CG    . LYS B 104 ? 1.95283 2.34164 2.42485 -0.07547 0.57412  -0.00038 104 LYS A CG    
923  C CD    . LYS B 104 ? 1.79304 2.18125 2.27683 -0.07694 0.54233  0.01012  104 LYS A CD    
924  C CE    . LYS B 104 ? 1.77000 2.17488 2.31398 -0.07508 0.53655  0.02934  104 LYS A CE    
925  N NZ    . LYS B 104 ? 1.72260 2.12532 2.27838 -0.07612 0.50690  0.03789  104 LYS A NZ    
926  N N     . ASP B 105 ? 2.02757 2.38679 2.47080 -0.06073 0.63620  -0.05603 105 ASP A N     
927  C CA    . ASP B 105 ? 2.05078 2.41214 2.53875 -0.05134 0.65834  -0.06306 105 ASP A CA    
928  C C     . ASP B 105 ? 2.21298 2.57418 2.69227 -0.04978 0.69358  -0.07372 105 ASP A C     
929  O O     . ASP B 105 ? 2.28027 2.64741 2.80360 -0.04218 0.71517  -0.07543 105 ASP A O     
930  C CB    . ASP B 105 ? 2.03985 2.38544 2.52307 -0.04641 0.65197  -0.07894 105 ASP A CB    
931  C CG    . ASP B 105 ? 2.18779 2.53380 2.68336 -0.04732 0.61882  -0.06826 105 ASP A CG    
932  O OD1   . ASP B 105 ? 2.17481 2.53540 2.70230 -0.04902 0.60449  -0.04803 105 ASP A OD1   
933  O OD2   . ASP B 105 ? 2.16752 2.49888 2.64049 -0.04660 0.60718  -0.08014 105 ASP A OD2   
934  N N     . CYS B 106 ? 2.31010 2.66434 2.73372 -0.05686 0.69948  -0.08049 106 CYS A N     
935  C CA    . CYS B 106 ? 2.31433 2.66805 2.72248 -0.05679 0.72928  -0.08834 106 CYS A CA    
936  C C     . CYS B 106 ? 2.28240 2.65239 2.69667 -0.06167 0.73011  -0.06941 106 CYS A C     
937  O O     . CYS B 106 ? 2.33127 2.69897 2.71751 -0.06362 0.74533  -0.07335 106 CYS A O     
938  C CB    . CYS B 106 ? 2.33929 2.67324 2.67881 -0.06181 0.73514  -0.10859 106 CYS A CB    
939  S SG    . CYS B 106 ? 2.11701 2.42978 2.44285 -0.05721 0.73291  -0.13200 106 CYS A SG    
940  N N     . ASN B 107 ? 2.23005 2.61600 2.68090 -0.06380 0.71334  -0.04886 107 ASN A N     
941  C CA    . ASN B 107 ? 2.27283 2.67525 2.73434 -0.06889 0.71180  -0.02888 107 ASN A CA    
942  C C     . ASN B 107 ? 2.29994 2.69611 2.69873 -0.07901 0.70857  -0.03093 107 ASN A C     
943  O O     . ASN B 107 ? 2.18270 2.58542 2.57090 -0.08203 0.72054  -0.02507 107 ASN A O     
944  C CB    . ASN B 107 ? 2.25097 2.66199 2.74582 -0.06250 0.73072  -0.02481 107 ASN A CB    
945  C CG    . ASN B 107 ? 2.26663 2.68052 2.81902 -0.05229 0.73283  -0.02464 107 ASN A CG    
946  O OD1   . ASN B 107 ? 2.10094 2.52478 2.69508 -0.05148 0.71562  -0.01072 107 ASN A OD1   
947  N ND2   . ASN B 107 ? 2.33622 2.74082 2.89116 -0.04476 0.75305  -0.03966 107 ASN A ND2   
948  N N     . ILE B 108 ? 2.27028 2.65230 2.62621 -0.08319 0.68538  -0.03775 108 ILE A N     
949  C CA    . ILE B 108 ? 2.22992 2.60484 2.52505 -0.09300 0.67711  -0.03855 108 ILE A CA    
950  C C     . ILE B 108 ? 2.16940 2.54525 2.45821 -0.09813 0.64133  -0.02504 108 ILE A C     
951  O O     . ILE B 108 ? 2.03049 2.39959 2.32838 -0.09483 0.62279  -0.02834 108 ILE A O     
952  C CB    . ILE B 108 ? 2.26576 2.62037 2.50697 -0.09412 0.68608  -0.06188 108 ILE A CB    
953  C CG1   . ILE B 108 ? 2.17728 2.52899 2.42570 -0.08854 0.72197  -0.07693 108 ILE A CG1   
954  C CG2   . ILE B 108 ? 2.15970 2.50756 2.34014 -0.10457 0.67706  -0.06149 108 ILE A CG2   
955  C CD1   . ILE B 108 ? 2.25428 2.58449 2.44798 -0.09003 0.72996  -0.10031 108 ILE A CD1   
956  N N     . GLN B 109 ? 2.14999 2.53360 2.42443 -0.10585 0.63269  -0.01041 109 GLN A N     
957  C CA    . GLN B 109 ? 2.13307 2.51679 2.39957 -0.11120 0.59966  0.00243  109 GLN A CA    
958  C C     . GLN B 109 ? 2.18936 2.55925 2.39187 -0.11879 0.58940  -0.00503 109 GLN A C     
959  O O     . GLN B 109 ? 2.12272 2.49601 2.29947 -0.12549 0.59614  0.00040  109 GLN A O     
960  C CB    . GLN B 109 ? 1.97492 2.37620 2.27185 -0.11489 0.59441  0.02488  109 GLN A CB    
961  C CG    . GLN B 109 ? 2.02497 2.42600 2.31507 -0.12059 0.56175  0.03823  109 GLN A CG    
962  C CD    . GLN B 109 ? 2.05218 2.46937 2.37015 -0.12498 0.55681  0.05982  109 GLN A CD    
963  O OE1   . GLN B 109 ? 1.94782 2.37777 2.29199 -0.12388 0.57769  0.06609  109 GLN A OE1   
964  N NE2   . GLN B 109 ? 1.99899 2.41548 2.31203 -0.13011 0.52931  0.07142  109 GLN A NE2   
965  N N     . TYR B 110 ? 2.21046 2.56571 2.38975 -0.11793 0.57355  -0.01626 110 TYR A N     
966  C CA    . TYR B 110 ? 2.20727 2.54896 2.32750 -0.12510 0.56193  -0.02309 110 TYR A CA    
967  C C     . TYR B 110 ? 2.14758 2.49031 2.26421 -0.12980 0.53126  -0.00908 110 TYR A C     
968  O O     . TYR B 110 ? 2.07833 2.41826 2.21403 -0.12618 0.51313  -0.00806 110 TYR A O     
969  C CB    . TYR B 110 ? 2.17087 2.49519 2.26528 -0.12209 0.56269  -0.04377 110 TYR A CB    
970  C CG    . TYR B 110 ? 2.22851 2.53893 2.26273 -0.12970 0.55288  -0.05128 110 TYR A CG    
971  C CD1   . TYR B 110 ? 2.20159 2.51415 2.20257 -0.13780 0.55821  -0.04587 110 TYR A CD1   
972  C CD2   . TYR B 110 ? 2.19100 2.48659 2.20303 -0.12909 0.53762  -0.06274 110 TYR A CD2   
973  C CE1   . TYR B 110 ? 2.24158 2.54187 2.18913 -0.14515 0.54828  -0.05150 110 TYR A CE1   
974  C CE2   . TYR B 110 ? 2.10525 2.38867 2.06476 -0.13626 0.52779  -0.06857 110 TYR A CE2   
975  C CZ    . TYR B 110 ? 2.16729 2.45305 2.09455 -0.14439 0.53285  -0.06280 110 TYR A CZ    
976  O OH    . TYR B 110 ? 2.01686 2.29093 1.89352 -0.15186 0.52234  -0.06747 110 TYR A OH    
977  N N     . ARG B 111 ? 2.17019 2.51637 2.26268 -0.13777 0.52586  0.00143  111 ARG A N     
978  C CA    . ARG B 111 ? 2.10384 2.44962 2.18981 -0.14271 0.49722  0.01431  111 ARG A CA    
979  C C     . ARG B 111 ? 1.98195 2.31816 2.01284 -0.15090 0.49039  0.01180  111 ARG A C     
980  O O     . ARG B 111 ? 2.03177 2.37483 2.05289 -0.15734 0.49046  0.02385  111 ARG A O     
981  C CB    . ARG B 111 ? 2.16020 2.52209 2.28321 -0.14442 0.49330  0.03448  111 ARG A CB    
982  C CG    . ARG B 111 ? 2.08313 2.45344 2.26079 -0.13744 0.49118  0.03975  111 ARG A CG    
983  C CD    . ARG B 111 ? 2.08378 2.46675 2.29255 -0.14071 0.47799  0.06048  111 ARG A CD    
984  N NE    . ARG B 111 ? 2.20683 2.59590 2.46419 -0.13514 0.47032  0.06621  111 ARG A NE    
985  C CZ    . ARG B 111 ? 2.10922 2.50846 2.39935 -0.13728 0.45723  0.08346  111 ARG A CZ    
986  N NH1   . ARG B 111 ? 1.98637 2.39060 2.26685 -0.14456 0.45034  0.09642  111 ARG A NH1   
987  N NH2   . ARG B 111 ? 2.11011 2.51411 2.44247 -0.13253 0.45049  0.08797  111 ARG A NH2   
988  N N     . PRO B 112 ? 1.98957 2.31044 1.98559 -0.15117 0.48388  -0.00255 112 PRO A N     
989  C CA    . PRO B 112 ? 2.11106 2.42280 2.05590 -0.15915 0.47706  -0.00466 112 PRO A CA    
990  C C     . PRO B 112 ? 2.14784 2.46328 2.09110 -0.16468 0.45440  0.01223  112 PRO A C     
991  O O     . PRO B 112 ? 2.22087 2.53535 2.18360 -0.16215 0.43480  0.01727  112 PRO A O     
992  C CB    . PRO B 112 ? 2.09747 2.39304 2.01769 -0.15712 0.46939  -0.02125 112 PRO A CB    
993  C CG    . PRO B 112 ? 2.04137 2.33842 2.00343 -0.14843 0.46440  -0.02351 112 PRO A CG    
994  C CD    . PRO B 112 ? 2.07606 2.38815 2.08202 -0.14421 0.48179  -0.01611 112 PRO A CD    
995  N N     . LYS B 113 ? 2.05300 2.37206 1.97309 -0.17228 0.45724  0.02081  113 LYS A N     
996  C CA    . LYS B 113 ? 1.93585 2.25831 1.85471 -0.17797 0.43675  0.03746  113 LYS A CA    
997  C C     . LYS B 113 ? 2.02708 2.33621 1.92166 -0.17945 0.41294  0.03370  113 LYS A C     
998  O O     . LYS B 113 ? 2.05025 2.36022 1.96059 -0.17953 0.39312  0.04374  113 LYS A O     
999  C CB    . LYS B 113 ? 1.86385 2.19140 1.75865 -0.18604 0.44596  0.04580  113 LYS A CB    
1000 C CG    . LYS B 113 ? 1.85285 2.19269 1.76751 -0.18463 0.47257  0.04776  113 LYS A CG    
1001 C CD    . LYS B 113 ? 1.91155 2.25499 1.79676 -0.19278 0.48445  0.05371  113 LYS A CD    
1002 C CE    . LYS B 113 ? 1.93126 2.28606 1.83581 -0.19072 0.51285  0.05402  113 LYS A CE    
1003 N NZ    . LYS B 113 ? 1.98696 2.34471 1.86068 -0.19885 0.52528  0.05932  113 LYS A NZ    
1004 N N     . LYS B 114 ? 1.98618 2.28319 1.84417 -0.18077 0.41509  0.01976  114 LYS A N     
1005 C CA    . LYS B 114 ? 1.95069 2.23505 1.78497 -0.18244 0.39310  0.01624  114 LYS A CA    
1006 C C     . LYS B 114 ? 2.00479 2.27983 1.84272 -0.17571 0.39351  0.00000  114 LYS A C     
1007 O O     . LYS B 114 ? 2.00523 2.27698 1.83287 -0.17398 0.41190  -0.01326 114 LYS A O     
1008 C CB    . LYS B 114 ? 1.79605 2.07357 1.58288 -0.19113 0.39085  0.01593  114 LYS A CB    
1009 C CG    . LYS B 114 ? 1.91867 2.20414 1.70070 -0.19825 0.38679  0.03304  114 LYS A CG    
1010 C CD    . LYS B 114 ? 1.98324 2.26111 1.71967 -0.20709 0.37959  0.03450  114 LYS A CD    
1011 C CE    . LYS B 114 ? 2.12281 2.40871 1.85749 -0.21389 0.37530  0.05212  114 LYS A CE    
1012 N NZ    . LYS B 114 ? 2.01681 2.29553 1.70936 -0.22257 0.36692  0.05479  114 LYS A NZ    
1013 N N     . VAL B 115 ? 1.90891 2.17944 1.76068 -0.17222 0.37445  0.00099  115 VAL A N     
1014 C CA    . VAL B 115 ? 1.71166 1.97303 1.56770 -0.16599 0.37274  -0.01348 115 VAL A CA    
1015 C C     . VAL B 115 ? 1.68698 1.93598 1.51484 -0.16893 0.35239  -0.01620 115 VAL A C     
1016 O O     . VAL B 115 ? 1.72493 1.97467 1.55051 -0.17242 0.33552  -0.00421 115 VAL A O     
1017 C CB    . VAL B 115 ? 1.60998 1.87747 1.51217 -0.15834 0.37008  -0.01052 115 VAL A CB    
1018 C CG1   . VAL B 115 ? 1.61580 1.87414 1.52327 -0.15211 0.36852  -0.02463 115 VAL A CG1   
1019 C CG2   . VAL B 115 ? 1.75522 2.03607 1.68905 -0.15568 0.38895  -0.00569 115 VAL A CG2   
1020 N N     . ILE B 116 ? 1.65441 1.89228 1.46259 -0.16764 0.35416  -0.03125 116 ILE A N     
1021 C CA    . ILE B 116 ? 1.67610 1.90209 1.45753 -0.17062 0.33533  -0.03417 116 ILE A CA    
1022 C C     . ILE B 116 ? 1.80744 2.02536 1.60019 -0.16405 0.33156  -0.04649 116 ILE A C     
1023 O O     . ILE B 116 ? 1.91666 2.13344 1.71642 -0.16001 0.34779  -0.05841 116 ILE A O     
1024 C CB    . ILE B 116 ? 1.77336 1.99232 1.50961 -0.17844 0.33942  -0.03938 116 ILE A CB    
1025 C CG1   . ILE B 116 ? 1.69133 1.91740 1.41422 -0.18573 0.33946  -0.02553 116 ILE A CG1   
1026 C CG2   . ILE B 116 ? 1.80209 2.00803 1.51325 -0.18069 0.32255  -0.04542 116 ILE A CG2   
1027 C CD1   . ILE B 116 ? 1.77650 1.99571 1.45378 -0.19426 0.34236  -0.02934 116 ILE A CD1   
1028 N N     . ASP B 117 ? 1.58347 1.79581 1.37851 -0.16298 0.31166  -0.04372 117 ASP A N     
1029 C CA    . ASP B 117 ? 1.61119 1.81518 1.41455 -0.15736 0.30702  -0.05512 117 ASP A CA    
1030 C C     . ASP B 117 ? 1.74311 1.93481 1.51192 -0.16187 0.29471  -0.06085 117 ASP A C     
1031 O O     . ASP B 117 ? 1.77979 1.96992 1.54049 -0.16511 0.27775  -0.05135 117 ASP A O     
1032 C CB    . ASP B 117 ? 1.60149 1.80916 1.44008 -0.15154 0.29574  -0.04819 117 ASP A CB    
1033 C CG    . ASP B 117 ? 1.82542 2.02613 1.67742 -0.14532 0.29254  -0.05870 117 ASP A CG    
1034 O OD1   . ASP B 117 ? 1.88509 2.07759 1.71978 -0.14527 0.29932  -0.07232 117 ASP A OD1   
1035 O OD2   . ASP B 117 ? 1.89920 2.10233 1.77828 -0.14095 0.28309  -0.05307 117 ASP A OD2   
1036 N N     . THR B 118 ? 1.72494 1.90794 1.47501 -0.16219 0.30296  -0.07575 118 THR A N     
1037 C CA    . THR B 118 ? 1.68551 1.85655 1.40224 -0.16722 0.29116  -0.08142 118 THR A CA    
1038 C C     . THR B 118 ? 1.69987 1.86683 1.43070 -0.16371 0.27212  -0.07849 118 THR A C     
1039 O O     . THR B 118 ? 1.66512 1.82624 1.37553 -0.16836 0.25688  -0.07468 118 THR A O     
1040 C CB    . THR B 118 ? 1.69189 1.85351 1.38958 -0.16767 0.30366  -0.09904 118 THR A CB    
1041 O OG1   . THR B 118 ? 1.81850 1.97800 1.54457 -0.15953 0.30484  -0.10690 118 THR A OG1   
1042 C CG2   . THR B 118 ? 1.68308 1.84878 1.37120 -0.16976 0.32600  -0.10335 118 THR A CG2   
1043 N N     . LEU B 119 ? 1.73900 1.90884 1.50389 -0.15592 0.27293  -0.07983 119 LEU A N     
1044 C CA    . LEU B 119 ? 1.80586 1.97102 1.58254 -0.15268 0.25582  -0.07789 119 LEU A CA    
1045 C C     . LEU B 119 ? 1.72393 1.89112 1.49617 -0.15620 0.23963  -0.06343 119 LEU A C     
1046 O O     . LEU B 119 ? 1.63277 1.79279 1.39365 -0.15781 0.22486  -0.06251 119 LEU A O     
1047 C CB    . LEU B 119 ? 1.78951 1.95905 1.60478 -0.14441 0.25905  -0.07878 119 LEU A CB    
1048 C CG    . LEU B 119 ? 1.80655 1.97124 1.63660 -0.14031 0.24369  -0.07792 119 LEU A CG    
1049 C CD1   . LEU B 119 ? 1.84491 1.99764 1.65373 -0.14176 0.23797  -0.08896 119 LEU A CD1   
1050 C CD2   . LEU B 119 ? 1.72988 1.89936 1.59712 -0.13279 0.24885  -0.07891 119 LEU A CD2   
1051 N N     . GLU B 120 ? 1.56603 1.74271 1.34800 -0.15747 0.24242  -0.05196 120 GLU A N     
1052 C CA    . GLU B 120 ? 1.48952 1.66745 1.26510 -0.16151 0.22852  -0.03854 120 GLU A CA    
1053 C C     . GLU B 120 ? 1.56488 1.73679 1.30430 -0.16904 0.22318  -0.03854 120 GLU A C     
1054 O O     . GLU B 120 ? 1.54405 1.71088 1.27460 -0.17126 0.20766  -0.03316 120 GLU A O     
1055 C CB    . GLU B 120 ? 1.38269 1.57156 1.17343 -0.16235 0.23410  -0.02708 120 GLU A CB    
1056 C CG    . GLU B 120 ? 1.59999 1.79574 1.42743 -0.15591 0.23836  -0.02501 120 GLU A CG    
1057 C CD    . GLU B 120 ? 1.73039 1.93680 1.57187 -0.15774 0.24283  -0.01298 120 GLU A CD    
1058 O OE1   . GLU B 120 ? 1.83053 2.04147 1.65899 -0.16181 0.25407  -0.01204 120 GLU A OE1   
1059 O OE2   . GLU B 120 ? 1.76527 1.97519 1.62989 -0.15558 0.23494  -0.00426 120 GLU A OE2   
1060 N N     . ILE B 121 ? 1.53863 1.71080 1.25693 -0.17321 0.23613  -0.04440 121 ILE A N     
1061 C CA    . ILE B 121 ? 1.42452 1.59120 1.10652 -0.18143 0.23146  -0.04384 121 ILE A CA    
1062 C C     . ILE B 121 ? 1.64724 1.80264 1.31529 -0.18205 0.21920  -0.05119 121 ILE A C     
1063 O O     . ILE B 121 ? 1.70321 1.85429 1.35342 -0.18722 0.20544  -0.04509 121 ILE A O     
1064 C CB    . ILE B 121 ? 1.53521 1.70328 1.19631 -0.18564 0.24938  -0.05054 121 ILE A CB    
1065 C CG1   . ILE B 121 ? 1.60377 1.78352 1.27520 -0.18679 0.25956  -0.04021 121 ILE A CG1   
1066 C CG2   . ILE B 121 ? 1.57161 1.73180 1.19258 -0.19443 0.24381  -0.05234 121 ILE A CG2   
1067 C CD1   . ILE B 121 ? 1.52870 1.70984 1.17569 -0.19215 0.27666  -0.04477 121 ILE A CD1   
1068 N N     . PHE B 122 ? 1.61173 1.76230 1.28924 -0.17687 0.22380  -0.06389 122 PHE A N     
1069 C CA    . PHE B 122 ? 1.60364 1.74338 1.26874 -0.17762 0.21289  -0.07154 122 PHE A CA    
1070 C C     . PHE B 122 ? 1.60229 1.74088 1.28432 -0.17450 0.19536  -0.06332 122 PHE A C     
1071 O O     . PHE B 122 ? 1.61585 1.74761 1.28326 -0.17796 0.18173  -0.06196 122 PHE A O     
1072 C CB    . PHE B 122 ? 1.68060 1.81529 1.35260 -0.17290 0.22338  -0.08745 122 PHE A CB    
1073 C CG    . PHE B 122 ? 1.72039 1.85407 1.37380 -0.17588 0.24172  -0.09756 122 PHE A CG    
1074 C CD1   . PHE B 122 ? 1.59126 1.72524 1.21375 -0.18423 0.24481  -0.09409 122 PHE A CD1   
1075 C CD2   . PHE B 122 ? 1.75432 1.88653 1.42165 -0.17034 0.25641  -0.11037 122 PHE A CD2   
1076 C CE1   . PHE B 122 ? 1.79795 1.93048 1.40186 -0.18715 0.26280  -0.10361 122 PHE A CE1   
1077 C CE2   . PHE B 122 ? 1.83804 1.96856 1.48841 -0.17282 0.27473  -0.12029 122 PHE A CE2   
1078 C CZ    . PHE B 122 ? 1.86271 1.99326 1.48046 -0.18129 0.27826  -0.11712 122 PHE A CZ    
1079 N N     . LYS B 123 ? 1.56344 1.70892 1.27539 -0.16865 0.19565  -0.05671 123 LYS A N     
1080 C CA    . LYS B 123 ? 1.49984 1.64399 1.22694 -0.16591 0.18001  -0.04831 123 LYS A CA    
1081 C C     . LYS B 123 ? 1.49254 1.63608 1.20194 -0.17228 0.16883  -0.03692 123 LYS A C     
1082 O O     . LYS B 123 ? 1.53193 1.66926 1.23609 -0.17328 0.15516  -0.03465 123 LYS A O     
1083 C CB    . LYS B 123 ? 1.33029 1.48203 1.08870 -0.16013 0.18281  -0.04205 123 LYS A CB    
1084 C CG    . LYS B 123 ? 1.43394 1.58543 1.21662 -0.15283 0.18785  -0.05028 123 LYS A CG    
1085 C CD    . LYS B 123 ? 1.66539 1.82621 1.47530 -0.14884 0.19556  -0.04502 123 LYS A CD    
1086 C CE    . LYS B 123 ? 1.75658 1.91733 1.59277 -0.14182 0.19813  -0.05087 123 LYS A CE    
1087 N NZ    . LYS B 123 ? 1.79611 1.96633 1.65776 -0.13874 0.20703  -0.04639 123 LYS A NZ    
1088 N N     . ILE B 124 ? 1.48348 1.63340 1.18528 -0.17642 0.17473  -0.02967 124 ILE A N     
1089 C CA    . ILE B 124 ? 1.41926 1.56921 1.10681 -0.18250 0.16414  -0.01735 124 ILE A CA    
1090 C C     . ILE B 124 ? 1.47937 1.62237 1.13539 -0.18942 0.15900  -0.02088 124 ILE A C     
1091 O O     . ILE B 124 ? 1.53825 1.67632 1.18891 -0.19156 0.14431  -0.01527 124 ILE A O     
1092 C CB    . ILE B 124 ? 1.29240 1.45129 0.98131 -0.18529 0.17226  -0.00844 124 ILE A CB    
1093 C CG1   . ILE B 124 ? 1.39091 1.55662 1.11109 -0.17906 0.17742  -0.00542 124 ILE A CG1   
1094 C CG2   . ILE B 124 ? 1.29454 1.45332 0.97123 -0.19132 0.16118  0.00480  124 ILE A CG2   
1095 C CD1   . ILE B 124 ? 1.27653 1.45174 1.00036 -0.18091 0.19063  -0.00112 124 ILE A CD1   
1096 N N     . ALA B 125 ? 1.55406 1.69623 1.19046 -0.19285 0.17064  -0.02998 125 ALA A N     
1097 C CA    . ALA B 125 ? 1.58842 1.72362 1.19100 -0.20098 0.16571  -0.03287 125 ALA A CA    
1098 C C     . ALA B 125 ? 1.60200 1.72772 1.20229 -0.19984 0.15445  -0.04006 125 ALA A C     
1099 O O     . ALA B 125 ? 1.53048 1.65086 1.11156 -0.20603 0.14184  -0.03607 125 ALA A O     
1100 C CB    . ALA B 125 ? 1.43366 1.56912 1.01572 -0.20461 0.18220  -0.04225 125 ALA A CB    
1101 N N     . PHE B 126 ? 1.65435 1.77818 1.27419 -0.19251 0.15860  -0.04985 126 PHE A N     
1102 C CA    . PHE B 126 ? 1.57784 1.69249 1.19573 -0.19159 0.14885  -0.05751 126 PHE A CA    
1103 C C     . PHE B 126 ? 1.58870 1.70418 1.23795 -0.18362 0.14130  -0.05420 126 PHE A C     
1104 O O     . PHE B 126 ? 1.52971 1.64357 1.19540 -0.17751 0.14644  -0.06349 126 PHE A O     
1105 C CB    . PHE B 126 ? 1.56923 1.67907 1.17886 -0.19076 0.16150  -0.07403 126 PHE A CB    
1106 C CG    . PHE B 126 ? 1.53632 1.64546 1.11609 -0.19772 0.17359  -0.07923 126 PHE A CG    
1107 C CD1   . PHE B 126 ? 1.50376 1.60692 1.04956 -0.20738 0.16599  -0.07800 126 PHE A CD1   
1108 C CD2   . PHE B 126 ? 1.58479 1.69909 1.17071 -0.19478 0.19270  -0.08512 126 PHE A CD2   
1109 C CE1   . PHE B 126 ? 1.55086 1.65277 1.06721 -0.21420 0.17749  -0.08283 126 PHE A CE1   
1110 C CE2   . PHE B 126 ? 1.52286 1.63618 1.08095 -0.20107 0.20506  -0.09008 126 PHE A CE2   
1111 C CZ    . PHE B 126 ? 1.56086 1.66771 1.08298 -0.21091 0.19760  -0.08915 126 PHE A CZ    
1112 N N     . PRO B 127 ? 1.65174 1.76904 1.31003 -0.18346 0.12930  -0.04140 127 PRO A N     
1113 C CA    . PRO B 127 ? 1.62930 1.74712 1.31606 -0.17607 0.12362  -0.03824 127 PRO A CA    
1114 C C     . PRO B 127 ? 1.62649 1.73662 1.31663 -0.17401 0.11508  -0.04477 127 PRO A C     
1115 O O     . PRO B 127 ? 1.60373 1.71361 1.31612 -0.16711 0.11655  -0.04884 127 PRO A O     
1116 C CB    . PRO B 127 ? 1.39528 1.51561 1.08519 -0.17788 0.11394  -0.02339 127 PRO A CB    
1117 C CG    . PRO B 127 ? 1.47310 1.59144 1.13473 -0.18677 0.10886  -0.01928 127 PRO A CG    
1118 C CD    . PRO B 127 ? 1.61031 1.72849 1.25187 -0.19040 0.12104  -0.02983 127 PRO A CD    
1119 N N     . THR B 128 ? 1.78071 1.88477 1.44975 -0.18019 0.10604  -0.04540 128 THR A N     
1120 C CA    . THR B 128 ? 1.57231 1.66926 1.24617 -0.17868 0.09630  -0.04996 128 THR A CA    
1121 C C     . THR B 128 ? 1.66740 1.76036 1.34409 -0.17559 0.10440  -0.06496 128 THR A C     
1122 O O     . THR B 128 ? 1.76256 1.84997 1.44719 -0.17346 0.09730  -0.06925 128 THR A O     
1123 C CB    . THR B 128 ? 1.73394 1.82537 1.38493 -0.18682 0.08372  -0.04643 128 THR A CB    
1124 O OG1   . THR B 128 ? 2.01521 2.10540 1.63704 -0.19423 0.08994  -0.05140 128 THR A OG1   
1125 C CG2   . THR B 128 ? 1.79343 1.88749 1.44854 -0.18852 0.07290  -0.03098 128 THR A CG2   
1126 N N     . ASP B 129 ? 1.68081 1.77628 1.35236 -0.17526 0.11928  -0.07283 129 ASP A N     
1127 C CA    . ASP B 129 ? 1.75401 1.84482 1.42769 -0.17256 0.12792  -0.08768 129 ASP A CA    
1128 C C     . ASP B 129 ? 1.73194 1.82498 1.43877 -0.16329 0.13001  -0.08933 129 ASP A C     
1129 O O     . ASP B 129 ? 1.51128 1.61174 1.23765 -0.15871 0.13344  -0.08210 129 ASP A O     
1130 C CB    . ASP B 129 ? 1.58419 1.67693 1.24341 -0.17479 0.14455  -0.09544 129 ASP A CB    
1131 C CG    . ASP B 129 ? 1.75294 1.83914 1.37528 -0.18432 0.14344  -0.10003 129 ASP A CG    
1132 O OD1   . ASP B 129 ? 1.91258 1.99022 1.52305 -0.18796 0.13253  -0.10394 129 ASP A OD1   
1133 O OD2   . ASP B 129 ? 1.82245 1.91193 1.42734 -0.18860 0.15308  -0.09938 129 ASP A OD2   
1134 N N     . LYS B 130 ? 1.83447 1.92065 1.54711 -0.16105 0.12737  -0.09868 130 LYS A N     
1135 C CA    . LYS B 130 ? 1.75424 1.84157 1.49747 -0.15282 0.12789  -0.10013 130 LYS A CA    
1136 C C     . LYS B 130 ? 1.71318 1.80535 1.47224 -0.14760 0.14366  -0.10624 130 LYS A C     
1137 O O     . LYS B 130 ? 1.72284 1.81861 1.50927 -0.14090 0.14466  -0.10394 130 LYS A O     
1138 C CB    . LYS B 130 ? 1.46543 1.54383 1.20993 -0.15253 0.12048  -0.10821 130 LYS A CB    
1139 C CG    . LYS B 130 ? 1.82783 1.90163 1.55982 -0.15764 0.10431  -0.10177 130 LYS A CG    
1140 C CD    . LYS B 130 ? 1.92787 1.99232 1.65744 -0.15887 0.09767  -0.11090 130 LYS A CD    
1141 C CE    . LYS B 130 ? 1.78703 1.84774 1.50726 -0.16398 0.08101  -0.10317 130 LYS A CE    
1142 N NZ    . LYS B 130 ? 1.81465 1.86595 1.53048 -0.16645 0.07388  -0.11199 130 LYS A NZ    
1143 N N     . SER B 131 ? 1.61725 1.70955 1.36015 -0.15066 0.15606  -0.11354 131 SER A N     
1144 C CA    . SER B 131 ? 1.51930 1.61642 1.27850 -0.14574 0.17207  -0.11925 131 SER A CA    
1145 C C     . SER B 131 ? 1.66488 1.76614 1.40562 -0.15010 0.18407  -0.11951 131 SER A C     
1146 O O     . SER B 131 ? 1.69317 1.79014 1.40344 -0.15745 0.18230  -0.12107 131 SER A O     
1147 C CB    . SER B 131 ? 1.60858 1.69839 1.37403 -0.14271 0.17846  -0.13410 131 SER A CB    
1148 O OG    . SER B 131 ? 1.97678 2.07132 1.75869 -0.13804 0.19493  -0.13950 131 SER A OG    
1149 N N     . TYR B 132 ? 1.42294 1.53280 1.18313 -0.14575 0.19610  -0.11732 132 TYR A N     
1150 C CA    . TYR B 132 ? 1.65184 1.76690 1.40016 -0.14874 0.21003  -0.11758 132 TYR A CA    
1151 C C     . TYR B 132 ? 1.81419 1.92904 1.57293 -0.14477 0.22819  -0.12995 132 TYR A C     
1152 O O     . TYR B 132 ? 1.84705 1.96825 1.60594 -0.14512 0.24230  -0.12952 132 TYR A O     
1153 C CB    . TYR B 132 ? 1.53600 1.66209 1.29796 -0.14792 0.20886  -0.10278 132 TYR A CB    
1154 C CG    . TYR B 132 ? 1.51668 1.64213 1.26833 -0.15179 0.19206  -0.09101 132 TYR A CG    
1155 C CD1   . TYR B 132 ? 1.66800 1.79082 1.38874 -0.15966 0.18798  -0.08824 132 TYR A CD1   
1156 C CD2   . TYR B 132 ? 1.52585 1.65275 1.29851 -0.14772 0.18047  -0.08270 132 TYR A CD2   
1157 C CE1   . TYR B 132 ? 1.56194 1.68403 1.27545 -0.16298 0.17280  -0.07719 132 TYR A CE1   
1158 C CE2   . TYR B 132 ? 1.49543 1.62102 1.25972 -0.15088 0.16624  -0.07245 132 TYR A CE2   
1159 C CZ    . TYR B 132 ? 1.47679 1.60016 1.21272 -0.15831 0.16245  -0.06962 132 TYR A CZ    
1160 O OH    . TYR B 132 ? 1.53650 1.65860 1.26647 -0.16123 0.14851  -0.05899 132 TYR A OH    
1161 N N     . GLN B 133 ? 1.78851 1.89623 1.55779 -0.14082 0.22839  -0.14061 133 GLN A N     
1162 C CA    . GLN B 133 ? 1.89910 2.00330 1.67207 -0.13820 0.24554  -0.15486 133 GLN A CA    
1163 C C     . GLN B 133 ? 1.83496 1.93113 1.56877 -0.14583 0.25236  -0.16453 133 GLN A C     
1164 O O     . GLN B 133 ? 1.85376 1.94285 1.56024 -0.15234 0.24010  -0.16427 133 GLN A O     
1165 C CB    . GLN B 133 ? 1.83942 1.93648 1.63116 -0.13290 0.24230  -0.16379 133 GLN A CB    
1166 C CG    . GLN B 133 ? 1.74435 1.84918 1.57583 -0.12521 0.23833  -0.15540 133 GLN A CG    
1167 C CD    . GLN B 133 ? 1.88681 1.98516 1.73870 -0.11977 0.23815  -0.16475 133 GLN A CD    
1168 O OE1   . GLN B 133 ? 1.96308 2.05090 1.80098 -0.12203 0.23060  -0.17246 133 GLN A OE1   
1169 N NE2   . GLN B 133 ? 1.77906 1.88378 1.66534 -0.11279 0.24600  -0.16352 133 GLN A NE2   
1170 N N     . LEU B 134 ? 1.65439 1.75159 1.38542 -0.14530 0.27208  -0.17272 134 LEU A N     
1171 C CA    . LEU B 134 ? 1.79641 1.88777 1.48794 -0.15336 0.28005  -0.17944 134 LEU A CA    
1172 C C     . LEU B 134 ? 1.85133 1.92699 1.51484 -0.15834 0.27404  -0.19268 134 LEU A C     
1173 O O     . LEU B 134 ? 1.83762 1.90764 1.46490 -0.16718 0.26731  -0.19226 134 LEU A O     
1174 C CB    . LEU B 134 ? 1.77395 1.86897 1.46991 -0.15117 0.30424  -0.18653 134 LEU A CB    
1175 C CG    . LEU B 134 ? 1.76481 1.85349 1.41699 -0.16015 0.31316  -0.19313 134 LEU A CG    
1176 C CD1   . LEU B 134 ? 1.75512 1.85092 1.38831 -0.16699 0.30287  -0.17744 134 LEU A CD1   
1177 C CD2   . LEU B 134 ? 2.01243 2.10129 1.66525 -0.15811 0.33951  -0.20414 134 LEU A CD2   
1178 N N     . SER B 135 ? 1.85975 1.92796 1.53948 -0.15325 0.27607  -0.20423 135 SER A N     
1179 C CA    . SER B 135 ? 1.98339 2.03583 1.63734 -0.15821 0.27064  -0.21765 135 SER A CA    
1180 C C     . SER B 135 ? 2.02588 2.07517 1.66623 -0.16345 0.24689  -0.20909 135 SER A C     
1181 O O     . SER B 135 ? 1.97164 2.01240 1.57538 -0.17251 0.24016  -0.21211 135 SER A O     
1182 C CB    . SER B 135 ? 2.03594 2.08167 1.71499 -0.15105 0.27675  -0.23044 135 SER A CB    
1183 O OG    . SER B 135 ? 2.08495 2.13914 1.80455 -0.14294 0.26896  -0.22100 135 SER A OG    
1184 N N     . GLU B 136 ? 1.97469 2.03087 1.64434 -0.15808 0.23407  -0.19782 136 GLU A N     
1185 C CA    . GLU B 136 ? 2.05759 2.11119 1.71914 -0.16199 0.21238  -0.18933 136 GLU A CA    
1186 C C     . GLU B 136 ? 1.97837 2.03655 1.61498 -0.16945 0.20529  -0.17735 136 GLU A C     
1187 O O     . GLU B 136 ? 1.90863 1.96136 1.52520 -0.17591 0.18975  -0.17369 136 GLU A O     
1188 C CB    . GLU B 136 ? 1.92327 1.98345 1.62242 -0.15415 0.20269  -0.17996 136 GLU A CB    
1189 C CG    . GLU B 136 ? 1.90373 1.96040 1.63048 -0.14661 0.20917  -0.19007 136 GLU A CG    
1190 C CD    . GLU B 136 ? 1.99451 2.05679 1.75549 -0.13980 0.19857  -0.18051 136 GLU A CD    
1191 O OE1   . GLU B 136 ? 2.05620 2.12683 1.82343 -0.13958 0.19001  -0.16603 136 GLU A OE1   
1192 O OE2   . GLU B 136 ? 2.01818 2.07595 1.79942 -0.13484 0.19898  -0.18762 136 GLU A OE2   
1193 N N     . LEU B 137 ? 1.89870 1.96696 1.53758 -0.16882 0.21608  -0.17054 137 LEU A N     
1194 C CA    . LEU B 137 ? 1.93656 2.00909 1.55177 -0.17614 0.21040  -0.15917 137 LEU A CA    
1195 C C     . LEU B 137 ? 1.83437 1.89789 1.40716 -0.18572 0.21531  -0.16799 137 LEU A C     
1196 O O     . LEU B 137 ? 1.82810 1.88891 1.37453 -0.19399 0.20296  -0.16144 137 LEU A O     
1197 C CB    . LEU B 137 ? 2.06228 2.14834 1.69449 -0.17265 0.22026  -0.14885 137 LEU A CB    
1198 C CG    . LEU B 137 ? 2.03831 2.13050 1.65303 -0.17908 0.21378  -0.13463 137 LEU A CG    
1199 C CD1   . LEU B 137 ? 1.77610 1.86834 1.39650 -0.17979 0.19277  -0.12302 137 LEU A CD1   
1200 C CD2   . LEU B 137 ? 1.75220 1.85703 1.38504 -0.17556 0.22536  -0.12626 137 LEU A CD2   
1201 N N     . ALA B 138 ? 1.93529 1.99366 1.50097 -0.18493 0.23336  -0.18277 138 ALA A N     
1202 C CA    . ALA B 138 ? 2.03408 2.08247 1.55732 -0.19423 0.23981  -0.19277 138 ALA A CA    
1203 C C     . ALA B 138 ? 1.97864 2.01307 1.47939 -0.20059 0.22414  -0.19952 138 ALA A C     
1204 O O     . ALA B 138 ? 1.94350 1.97126 1.40626 -0.21099 0.21797  -0.19955 138 ALA A O     
1205 C CB    . ALA B 138 ? 1.86453 1.90973 1.38857 -0.19089 0.26405  -0.20807 138 ALA A CB    
1206 N N     . GLU B 139 ? 2.02432 2.05354 1.54736 -0.19485 0.21872  -0.20621 139 GLU A N     
1207 C CA    . GLU B 139 ? 2.07286 2.08920 1.57696 -0.20114 0.20195  -0.21131 139 GLU A CA    
1208 C C     . GLU B 139 ? 2.12904 2.15100 1.63261 -0.20481 0.18058  -0.19370 139 GLU A C     
1209 O O     . GLU B 139 ? 2.07092 2.08430 1.55059 -0.21308 0.16551  -0.19349 139 GLU A O     
1210 C CB    . GLU B 139 ? 2.04001 2.05063 1.57172 -0.19394 0.19935  -0.22024 139 GLU A CB    
1211 C CG    . GLU B 139 ? 1.97347 1.97069 1.48719 -0.20056 0.18250  -0.22579 139 GLU A CG    
1212 C CD    . GLU B 139 ? 2.10491 2.08702 1.60982 -0.20115 0.19056  -0.24610 139 GLU A CD    
1213 O OE1   . GLU B 139 ? 2.17430 2.15744 1.70637 -0.19222 0.20423  -0.25417 139 GLU A OE1   
1214 O OE2   . GLU B 139 ? 2.05250 2.02147 1.52336 -0.21085 0.18304  -0.25371 139 GLU A OE2   
1215 N N     . ALA B 140 ? 2.00561 2.04117 1.53619 -0.19872 0.17946  -0.17949 140 ALA A N     
1216 C CA    . ALA B 140 ? 1.81147 1.85282 1.34630 -0.20084 0.16077  -0.16240 140 ALA A CA    
1217 C C     . ALA B 140 ? 1.91680 1.95645 1.41369 -0.21209 0.15555  -0.15653 140 ALA A C     
1218 O O     . ALA B 140 ? 1.86725 1.90322 1.35302 -0.21796 0.13738  -0.14950 140 ALA A O     
1219 C CB    . ALA B 140 ? 2.01506 2.07013 1.58194 -0.19279 0.16436  -0.15040 140 ALA A CB    
1220 N N     . HIS B 141 ? 1.89341 1.93622 1.37280 -0.21493 0.17098  -0.15837 141 HIS A N     
1221 C CA    . HIS B 141 ? 1.89244 1.93501 1.33618 -0.22586 0.16629  -0.15067 141 HIS A CA    
1222 C C     . HIS B 141 ? 2.00735 2.03806 1.41110 -0.23431 0.17572  -0.16543 141 HIS A C     
1223 O O     . HIS B 141 ? 1.95184 1.98473 1.33076 -0.24013 0.18574  -0.16376 141 HIS A O     
1224 C CB    . HIS B 141 ? 2.05591 2.11203 1.50860 -0.22397 0.17415  -0.13782 141 HIS A CB    
1225 C CG    . HIS B 141 ? 2.14824 2.20698 1.57878 -0.23300 0.16182  -0.12331 141 HIS A CG    
1226 N ND1   . HIS B 141 ? 2.07259 2.13626 1.51901 -0.23222 0.14412  -0.10804 141 HIS A ND1   
1227 C CD2   . HIS B 141 ? 2.22436 2.28120 1.61878 -0.24305 0.16459  -0.12143 141 HIS A CD2   
1228 C CE1   . HIS B 141 ? 2.09799 2.16290 1.52023 -0.24131 0.13627  -0.09709 141 HIS A CE1   
1229 N NE2   . HIS B 141 ? 2.24333 2.30432 1.63327 -0.24822 0.14809  -0.10466 141 HIS A NE2   
1230 N N     . GLY B 142 ? 2.07267 2.09069 1.46986 -0.23519 0.17298  -0.17962 142 GLY A N     
1231 C CA    . GLY B 142 ? 2.19399 2.19814 1.54967 -0.24434 0.18012  -0.19458 142 GLY A CA    
1232 C C     . GLY B 142 ? 2.18569 2.19173 1.52933 -0.24370 0.20525  -0.20265 142 GLY A C     
1233 O O     . GLY B 142 ? 2.26452 2.26550 1.56784 -0.25392 0.20928  -0.20442 142 GLY A O     
1234 N N     . ILE B 143 ? 2.10557 2.11856 1.48259 -0.23250 0.22171  -0.20705 143 ILE A N     
1235 C CA    . ILE B 143 ? 2.11540 2.12979 1.48392 -0.23124 0.24766  -0.21601 143 ILE A CA    
1236 C C     . ILE B 143 ? 2.23613 2.23927 1.61125 -0.22628 0.26112  -0.23664 143 ILE A C     
1237 O O     . ILE B 143 ? 2.31531 2.31920 1.72520 -0.21771 0.25587  -0.23846 143 ILE A O     
1238 C CB    . ILE B 143 ? 2.16682 2.19892 1.56833 -0.22305 0.25753  -0.20361 143 ILE A CB    
1239 C CG1   . ILE B 143 ? 2.14582 2.18788 1.54196 -0.22791 0.24334  -0.18345 143 ILE A CG1   
1240 C CG2   . ILE B 143 ? 2.03347 2.06759 1.42962 -0.22140 0.28463  -0.21236 143 ILE A CG2   
1241 C CD1   . ILE B 143 ? 2.07251 2.10991 1.42132 -0.24071 0.24319  -0.18149 143 ILE A CD1   
1242 N N     . THR B 144 ? 2.26698 2.25965 1.60986 -0.23161 0.27793  -0.25149 144 THR A N     
1243 C CA    . THR B 144 ? 2.31206 2.29172 1.65811 -0.22770 0.29115  -0.27253 144 THR A CA    
1244 C C     . THR B 144 ? 2.35365 2.34365 1.74414 -0.21455 0.30980  -0.27429 144 THR A C     
1245 O O     . THR B 144 ? 2.41038 2.40192 1.79485 -0.21349 0.33285  -0.28068 144 THR A O     
1246 C CB    . THR B 144 ? 2.27088 2.23598 1.56749 -0.23765 0.30477  -0.28755 144 THR A CB    
1247 O OG1   . THR B 144 ? 2.21695 2.19273 1.50748 -0.23798 0.32211  -0.28120 144 THR A OG1   
1248 C CG2   . THR B 144 ? 2.37070 2.32444 1.62224 -0.25165 0.28470  -0.28590 144 THR A CG2   
1249 N N     . LEU B 145 ? 2.22699 2.22366 1.66064 -0.20513 0.30040  -0.26865 145 LEU A N     
1250 C CA    . LEU B 145 ? 2.17365 2.18112 1.65336 -0.19260 0.31568  -0.26826 145 LEU A CA    
1251 C C     . LEU B 145 ? 2.33518 2.33077 1.81635 -0.18897 0.33585  -0.28942 145 LEU A C     
1252 O O     . LEU B 145 ? 2.38531 2.38860 1.89765 -0.18007 0.35425  -0.29138 145 LEU A O     
1253 C CB    . LEU B 145 ? 2.32619 2.34143 1.84643 -0.18498 0.29854  -0.25746 145 LEU A CB    
1254 C CG    . LEU B 145 ? 2.28086 2.30759 1.85070 -0.17259 0.30968  -0.25461 145 LEU A CG    
1255 C CD1   . LEU B 145 ? 2.11986 2.13663 1.70678 -0.16648 0.32088  -0.27190 145 LEU A CD1   
1256 C CD2   . LEU B 145 ? 2.18732 2.22683 1.76386 -0.17065 0.32727  -0.24794 145 LEU A CD2   
1257 N N     . ALA B 146 ? 2.42974 2.40696 1.87969 -0.19568 0.33209  -0.30446 146 ALA A N     
1258 C CA    . ALA B 146 ? 2.48976 2.45312 1.93689 -0.19313 0.35184  -0.32624 146 ALA A CA    
1259 C C     . ALA B 146 ? 2.41229 2.38203 1.91375 -0.17958 0.35923  -0.32788 146 ALA A C     
1260 O O     . ALA B 146 ? 2.42564 2.40154 1.95699 -0.17475 0.34169  -0.31803 146 ALA A O     
1261 C CB    . ALA B 146 ? 2.45049 2.41247 1.87102 -0.19678 0.37617  -0.33336 146 ALA A CB    
1262 N N     . ASN B 147 ? 2.38056 2.34874 1.89472 -0.17376 0.38475  -0.33967 147 ASN A N     
1263 C CA    . ASN B 147 ? 2.43429 2.40953 2.00279 -0.16077 0.39297  -0.34021 147 ASN A CA    
1264 C C     . ASN B 147 ? 2.39731 2.39487 2.00043 -0.15479 0.38915  -0.31892 147 ASN A C     
1265 O O     . ASN B 147 ? 2.47502 2.48182 2.06403 -0.15820 0.39646  -0.31049 147 ASN A O     
1266 C CB    . ASN B 147 ? 2.42350 2.39101 1.99774 -0.15620 0.42152  -0.35807 147 ASN A CB    
1267 C CG    . ASN B 147 ? 2.49831 2.47561 2.13054 -0.14303 0.43076  -0.35584 147 ASN A CG    
1268 O OD1   . ASN B 147 ? 2.38101 2.36905 2.03459 -0.13744 0.45030  -0.35294 147 ASN A OD1   
1269 N ND2   . ASN B 147 ? 2.47001 2.44418 2.12912 -0.13819 0.41678  -0.35631 147 ASN A ND2   
1270 N N     . ALA B 148 ? 2.34774 2.35312 1.99334 -0.14675 0.37776  -0.31042 148 ALA A N     
1271 C CA    . ALA B 148 ? 2.21689 2.24227 1.89474 -0.14161 0.37204  -0.29009 148 ALA A CA    
1272 C C     . ALA B 148 ? 2.06988 2.10488 1.78954 -0.13166 0.39229  -0.29048 148 ALA A C     
1273 O O     . ALA B 148 ? 2.13238 2.15858 1.85250 -0.12923 0.41217  -0.30653 148 ALA A O     
1274 C CB    . ALA B 148 ? 2.07713 2.10567 1.77530 -0.13927 0.34784  -0.27948 148 ALA A CB    
1275 N N     . HIS B 149 ? 2.04753 2.09965 1.80128 -0.12636 0.38731  -0.27322 149 HIS A N     
1276 C CA    . HIS B 149 ? 2.09711 2.15981 1.89598 -0.11679 0.40394  -0.27116 149 HIS A CA    
1277 C C     . HIS B 149 ? 2.18561 2.24618 1.97237 -0.11739 0.43109  -0.28196 149 HIS A C     
1278 O O     . HIS B 149 ? 2.14579 2.20684 1.96331 -0.10984 0.44896  -0.28948 149 HIS A O     
1279 C CB    . HIS B 149 ? 2.17015 2.22786 2.00393 -0.10907 0.40076  -0.27745 149 HIS A CB    
1280 C CG    . HIS B 149 ? 2.21877 2.27811 2.06223 -0.10886 0.37522  -0.26708 149 HIS A CG    
1281 N ND1   . HIS B 149 ? 2.30825 2.35703 2.16080 -0.10659 0.36587  -0.27502 149 HIS A ND1   
1282 C CD2   . HIS B 149 ? 1.98242 2.05215 1.82760 -0.11073 0.35776  -0.24968 149 HIS A CD2   
1283 C CE1   . HIS B 149 ? 2.20774 2.26109 2.06746 -0.10699 0.34398  -0.26235 149 HIS A CE1   
1284 N NE2   . HIS B 149 ? 2.05956 2.12524 1.91466 -0.10941 0.33897  -0.24722 149 HIS A NE2   
1285 N N     . ARG B 150 ? 2.23726 2.29577 1.98151 -0.12610 0.43456  -0.28215 150 ARG A N     
1286 C CA    . ARG B 150 ? 2.21610 2.27341 1.94691 -0.12715 0.46157  -0.29126 150 ARG A CA    
1287 C C     . ARG B 150 ? 2.21696 2.29028 1.94429 -0.13013 0.46419  -0.27471 150 ARG A C     
1288 O O     . ARG B 150 ? 2.23705 2.31424 1.94484 -0.13632 0.44490  -0.26232 150 ARG A O     
1289 C CB    . ARG B 150 ? 2.20125 2.23887 1.88061 -0.13551 0.46768  -0.30970 150 ARG A CB    
1290 C CG    . ARG B 150 ? 2.29542 2.32820 1.92724 -0.14699 0.44863  -0.30446 150 ARG A CG    
1291 C CD    . ARG B 150 ? 2.28374 2.29817 1.86381 -0.15591 0.45878  -0.32225 150 ARG A CD    
1292 N NE    . ARG B 150 ? 2.28982 2.28709 1.87214 -0.15306 0.46449  -0.34218 150 ARG A NE    
1293 C CZ    . ARG B 150 ? 2.40604 2.39272 1.98133 -0.15154 0.48956  -0.36014 150 ARG A CZ    
1294 N NH1   . ARG B 150 ? 2.22151 2.21157 1.77963 -0.15406 0.51084  -0.36151 150 ARG A NH1   
1295 N NH2   . ARG B 150 ? 2.42814 2.40068 2.01431 -0.14742 0.49379  -0.37663 150 ARG A NH2   
1296 N N     . ALA B 151 ? 2.22375 2.30626 1.97253 -0.12552 0.48707  -0.27400 151 ALA A N     
1297 C CA    . ALA B 151 ? 2.22074 2.31865 1.96804 -0.12835 0.49158  -0.25851 151 ALA A CA    
1298 C C     . ALA B 151 ? 2.28182 2.37161 1.97199 -0.13955 0.49439  -0.26287 151 ALA A C     
1299 O O     . ALA B 151 ? 2.30213 2.40276 1.98230 -0.14388 0.49598  -0.25017 151 ALA A O     
1300 C CB    . ALA B 151 ? 2.14631 2.25479 1.93021 -0.12094 0.51649  -0.25803 151 ALA A CB    
1301 N N     . ASP B 152 ? 2.28919 2.36011 1.94290 -0.14453 0.49424  -0.27998 152 ASP A N     
1302 C CA    . ASP B 152 ? 2.22453 2.28577 1.82030 -0.15619 0.49688  -0.28535 152 ASP A CA    
1303 C C     . ASP B 152 ? 2.33336 2.39485 1.90463 -0.16405 0.46791  -0.27303 152 ASP A C     
1304 O O     . ASP B 152 ? 2.42476 2.49708 1.98541 -0.16887 0.46343  -0.25800 152 ASP A O     
1305 C CB    . ASP B 152 ? 2.26954 2.30985 1.83581 -0.15883 0.51005  -0.30911 152 ASP A CB    
1306 C CG    . ASP B 152 ? 2.38390 2.42228 1.97920 -0.14984 0.53801  -0.32254 152 ASP A CG    
1307 O OD1   . ASP B 152 ? 2.49738 2.54528 2.10089 -0.14802 0.55962  -0.31946 152 ASP A OD1   
1308 O OD2   . ASP B 152 ? 2.32285 2.35042 1.93399 -0.14463 0.53807  -0.33554 152 ASP A OD2   
1309 N N     . GLU B 153 ? 2.33702 2.38723 1.90184 -0.16510 0.44913  -0.27873 153 GLU A N     
1310 C CA    . GLU B 153 ? 2.41039 2.46031 1.95458 -0.17217 0.42120  -0.26716 153 GLU A CA    
1311 C C     . GLU B 153 ? 2.30857 2.37708 1.88910 -0.16726 0.40857  -0.24587 153 GLU A C     
1312 O O     . GLU B 153 ? 2.25259 2.32707 1.81550 -0.17363 0.39549  -0.23196 153 GLU A O     
1313 C CB    . GLU B 153 ? 2.36073 2.39625 1.89832 -0.17307 0.40399  -0.27656 153 GLU A CB    
1314 C CG    . GLU B 153 ? 2.41473 2.42989 1.90841 -0.18056 0.41119  -0.29648 153 GLU A CG    
1315 C CD    . GLU B 153 ? 2.39861 2.40741 1.83780 -0.19397 0.40374  -0.29431 153 GLU A CD    
1316 O OE1   . GLU B 153 ? 2.26132 2.28195 1.69620 -0.19763 0.39308  -0.27667 153 GLU A OE1   
1317 O OE2   . GLU B 153 ? 2.50305 2.49435 1.90360 -0.20114 0.40823  -0.31033 153 GLU A OE2   
1318 N N     . ASP B 154 ? 2.25213 2.32912 1.88137 -0.15663 0.41289  -0.24337 154 ASP A N     
1319 C CA    . ASP B 154 ? 2.27749 2.37136 1.94162 -0.15213 0.40122  -0.22359 154 ASP A CA    
1320 C C     . ASP B 154 ? 2.25938 2.36525 1.91464 -0.15610 0.40983  -0.21163 154 ASP A C     
1321 O O     . ASP B 154 ? 2.26258 2.38073 1.93456 -0.15553 0.39752  -0.19428 154 ASP A O     
1322 C CB    . ASP B 154 ? 2.26425 2.36477 1.98049 -0.14088 0.40548  -0.22309 154 ASP A CB    
1323 C CG    . ASP B 154 ? 2.21545 2.30754 1.94565 -0.13707 0.39023  -0.22847 154 ASP A CG    
1324 O OD1   . ASP B 154 ? 2.17586 2.25254 1.88418 -0.13947 0.39188  -0.24433 154 ASP A OD1   
1325 O OD2   . ASP B 154 ? 2.33255 2.43319 2.09493 -0.13204 0.37687  -0.21672 154 ASP A OD2   
1326 N N     . ALA B 155 ? 2.11586 2.21810 1.74662 -0.15993 0.43072  -0.22056 155 ALA A N     
1327 C CA    . ALA B 155 ? 2.14432 2.25736 1.76248 -0.16489 0.43861  -0.20889 155 ALA A CA    
1328 C C     . ALA B 155 ? 2.21535 2.31913 1.77885 -0.17698 0.42995  -0.20959 155 ALA A C     
1329 O O     . ALA B 155 ? 2.25601 2.36838 1.80717 -0.18259 0.42387  -0.19499 155 ALA A O     
1330 C CB    . ALA B 155 ? 2.11299 2.23012 1.74250 -0.16120 0.46816  -0.21581 155 ALA A CB    
1331 N N     . ALA B 156 ? 2.23035 2.31684 1.76266 -0.18122 0.42834  -0.22557 156 ALA A N     
1332 C CA    . ALA B 156 ? 2.23667 2.31303 1.71460 -0.19369 0.42014  -0.22706 156 ALA A CA    
1333 C C     . ALA B 156 ? 2.17737 2.25342 1.64988 -0.19754 0.39000  -0.21542 156 ALA A C     
1334 O O     . ALA B 156 ? 2.22918 2.31011 1.68061 -0.20504 0.37989  -0.20218 156 ALA A O     
1335 C CB    . ALA B 156 ? 2.27805 2.33535 1.72401 -0.19738 0.43054  -0.24891 156 ALA A CB    
1336 N N     . THR B 157 ? 2.15112 2.22160 1.64295 -0.19254 0.37646  -0.21987 157 THR A N     
1337 C CA    . THR B 157 ? 2.17958 2.24860 1.66623 -0.19608 0.34851  -0.20987 157 THR A CA    
1338 C C     . THR B 157 ? 2.19803 2.28340 1.70996 -0.19348 0.33860  -0.18917 157 THR A C     
1339 O O     . THR B 157 ? 2.22073 2.30720 1.71409 -0.20028 0.32136  -0.17748 157 THR A O     
1340 C CB    . THR B 157 ? 2.18017 2.24064 1.68588 -0.19051 0.33830  -0.21888 157 THR A CB    
1341 O OG1   . THR B 157 ? 2.25652 2.32428 1.80570 -0.17937 0.35179  -0.22142 157 THR A OG1   
1342 C CG2   . THR B 157 ? 2.25366 2.29532 1.72572 -0.19606 0.34101  -0.23779 157 THR A CG2   
1343 N N     . THR B 158 ? 2.19051 2.28784 1.74352 -0.18433 0.34880  -0.18446 158 THR A N     
1344 C CA    . THR B 158 ? 2.03987 2.15229 1.61650 -0.18230 0.34022  -0.16498 158 THR A CA    
1345 C C     . THR B 158 ? 1.90519 2.02170 1.45141 -0.19128 0.34194  -0.15566 158 THR A C     
1346 O O     . THR B 158 ? 1.80058 1.92134 1.34228 -0.19517 0.32436  -0.14125 158 THR A O     
1347 C CB    . THR B 158 ? 2.06204 2.18610 1.68288 -0.17261 0.35449  -0.16260 158 THR A CB    
1348 O OG1   . THR B 158 ? 2.10889 2.22913 1.72110 -0.17213 0.37863  -0.17632 158 THR A OG1   
1349 C CG2   . THR B 158 ? 1.99168 2.11549 1.64943 -0.16378 0.34576  -0.16429 158 THR A CG2   
1350 N N     . ALA B 159 ? 1.89768 2.01257 1.42369 -0.19454 0.36283  -0.16360 159 ALA A N     
1351 C CA    . ALA B 159 ? 1.93373 2.05270 1.42924 -0.20360 0.36655  -0.15472 159 ALA A CA    
1352 C C     . ALA B 159 ? 1.95103 2.06016 1.40605 -0.21390 0.34717  -0.15248 159 ALA A C     
1353 O O     . ALA B 159 ? 2.04448 2.15979 1.48949 -0.21960 0.33562  -0.13699 159 ALA A O     
1354 C CB    . ALA B 159 ? 1.96964 2.08630 1.44860 -0.20518 0.39342  -0.16615 159 ALA A CB    
1355 N N     . LYS B 160 ? 1.86741 1.96147 1.30107 -0.21637 0.34317  -0.16716 160 LYS A N     
1356 C CA    . LYS B 160 ? 1.95403 2.03799 1.34913 -0.22680 0.32387  -0.16532 160 LYS A CA    
1357 C C     . LYS B 160 ? 2.02105 2.11185 1.43586 -0.22552 0.29952  -0.14845 160 LYS A C     
1358 O O     . LYS B 160 ? 2.06291 2.15432 1.45465 -0.23396 0.28611  -0.13688 160 LYS A O     
1359 C CB    . LYS B 160 ? 2.03999 2.10691 1.41715 -0.22831 0.32142  -0.18357 160 LYS A CB    
1360 C CG    . LYS B 160 ? 2.19840 2.25538 1.55121 -0.23050 0.34489  -0.20207 160 LYS A CG    
1361 C CD    . LYS B 160 ? 2.24189 2.28089 1.57793 -0.23220 0.34079  -0.22019 160 LYS A CD    
1362 C CE    . LYS B 160 ? 2.14724 2.17477 1.45766 -0.23459 0.36446  -0.23940 160 LYS A CE    
1363 N NZ    . LYS B 160 ? 2.14274 2.15178 1.43560 -0.23704 0.35900  -0.25677 160 LYS A NZ    
1364 N N     . LEU B 161 ? 2.00301 2.09844 1.45904 -0.21543 0.29448  -0.14705 161 LEU A N     
1365 C CA    . LEU B 161 ? 1.81381 1.91514 1.29038 -0.21343 0.27285  -0.13182 161 LEU A CA    
1366 C C     . LEU B 161 ? 1.88366 1.99872 1.36974 -0.21427 0.27433  -0.11476 161 LEU A C     
1367 O O     . LEU B 161 ? 1.89498 2.01187 1.37155 -0.21953 0.25795  -0.10148 161 LEU A O     
1368 C CB    . LEU B 161 ? 1.90388 2.00638 1.42066 -0.20262 0.26974  -0.13550 161 LEU A CB    
1369 C CG    . LEU B 161 ? 1.99359 2.08264 1.50468 -0.20164 0.26479  -0.15046 161 LEU A CG    
1370 C CD1   . LEU B 161 ? 1.85529 1.94687 1.40805 -0.19041 0.26750  -0.15489 161 LEU A CD1   
1371 C CD2   . LEU B 161 ? 1.94741 2.02964 1.44111 -0.20772 0.24135  -0.14498 161 LEU A CD2   
1372 N N     . MET B 162 ? 1.85357 1.97783 1.35910 -0.20933 0.29313  -0.11481 162 MET A N     
1373 C CA    . MET B 162 ? 1.72010 1.85705 1.23368 -0.21085 0.29525  -0.09890 162 MET A CA    
1374 C C     . MET B 162 ? 1.76704 1.90167 1.24098 -0.22237 0.28884  -0.09134 162 MET A C     
1375 O O     . MET B 162 ? 1.86736 2.00792 1.34359 -0.22541 0.27579  -0.07548 162 MET A O     
1376 C CB    . MET B 162 ? 1.79261 1.93788 1.32296 -0.20634 0.31954  -0.10240 162 MET A CB    
1377 C CG    . MET B 162 ? 1.71668 1.87628 1.26438 -0.20626 0.32255  -0.08602 162 MET A CG    
1378 S SD    . MET B 162 ? 1.97393 2.14002 1.51212 -0.20853 0.35121  -0.08912 162 MET A SD    
1379 C CE    . MET B 162 ? 2.01964 2.19161 1.60518 -0.19599 0.36763  -0.09734 162 MET A CE    
1380 N N     . ILE B 163 ? 1.80685 1.93208 1.24350 -0.22921 0.29777  -0.10273 163 ILE A N     
1381 C CA    . ILE B 163 ? 1.84509 1.96576 1.23957 -0.24129 0.29001  -0.09698 163 ILE A CA    
1382 C C     . ILE B 163 ? 1.80685 1.92348 1.19832 -0.24442 0.26322  -0.08801 163 ILE A C     
1383 O O     . ILE B 163 ? 1.94377 2.06563 1.33020 -0.24945 0.25149  -0.07219 163 ILE A O     
1384 C CB    . ILE B 163 ? 1.85897 1.96711 1.21332 -0.24786 0.30217  -0.11351 163 ILE A CB    
1385 C CG1   . ILE B 163 ? 1.92178 2.03528 1.27215 -0.24741 0.32929  -0.11811 163 ILE A CG1   
1386 C CG2   . ILE B 163 ? 1.90329 2.00322 1.21334 -0.26077 0.28740  -0.10890 163 ILE A CG2   
1387 C CD1   . ILE B 163 ? 2.09532 2.19577 1.40544 -0.25371 0.34391  -0.13529 163 ILE A CD1   
1388 N N     . LEU B 164 ? 1.75471 1.86222 1.15193 -0.24108 0.25351  -0.09765 164 LEU A N     
1389 C CA    . LEU B 164 ? 1.86182 1.96471 1.25665 -0.24395 0.22880  -0.09023 164 LEU A CA    
1390 C C     . LEU B 164 ? 1.79055 1.90415 1.21561 -0.23975 0.21716  -0.07267 164 LEU A C     
1391 O O     . LEU B 164 ? 1.81558 1.92882 1.23205 -0.24515 0.19962  -0.06044 164 LEU A O     
1392 C CB    . LEU B 164 ? 1.90854 2.00169 1.31299 -0.23907 0.22277  -0.10340 164 LEU A CB    
1393 C CG    . LEU B 164 ? 1.98055 2.06033 1.35328 -0.24399 0.23118  -0.12161 164 LEU A CG    
1394 C CD1   . LEU B 164 ? 2.04707 2.11854 1.43681 -0.23757 0.22683  -0.13432 164 LEU A CD1   
1395 C CD2   . LEU B 164 ? 1.94588 2.01746 1.27401 -0.25732 0.21964  -0.11858 164 LEU A CD2   
1396 N N     . ALA B 165 ? 1.84720 1.96994 1.30797 -0.23038 0.22659  -0.07110 165 ALA A N     
1397 C CA    . ALA B 165 ? 1.71784 1.85041 1.20500 -0.22711 0.21782  -0.05481 165 ALA A CA    
1398 C C     . ALA B 165 ? 1.74849 1.88691 1.21718 -0.23520 0.21778  -0.04130 165 ALA A C     
1399 O O     . ALA B 165 ? 1.79519 1.93460 1.26242 -0.23885 0.20153  -0.02795 165 ALA A O     
1400 C CB    . ALA B 165 ? 1.64170 1.78280 1.16719 -0.21691 0.22961  -0.05609 165 ALA A CB    
1401 N N     . PHE B 166 ? 1.69117 1.83403 1.14857 -0.23761 0.23648  -0.04393 166 PHE A N     
1402 C CA    . PHE B 166 ? 1.61830 1.76750 1.05871 -0.24550 0.23775  -0.03041 166 PHE A CA    
1403 C C     . PHE B 166 ? 1.65533 1.79661 1.06021 -0.25602 0.22210  -0.02577 166 PHE A C     
1404 O O     . PHE B 166 ? 1.68039 1.82552 1.08326 -0.26067 0.20998  -0.01011 166 PHE A O     
1405 C CB    . PHE B 166 ? 1.68610 1.83989 1.11718 -0.24663 0.26187  -0.03619 166 PHE A CB    
1406 C CG    . PHE B 166 ? 1.73446 1.89629 1.20460 -0.23602 0.27540  -0.03980 166 PHE A CG    
1407 C CD1   . PHE B 166 ? 1.69650 1.86181 1.20275 -0.22812 0.26433  -0.03468 166 PHE A CD1   
1408 C CD2   . PHE B 166 ? 1.73855 1.90429 1.20964 -0.23418 0.29890  -0.04772 166 PHE A CD2   
1409 C CE1   . PHE B 166 ? 1.70292 1.87558 1.24513 -0.21903 0.27530  -0.03701 166 PHE A CE1   
1410 C CE2   . PHE B 166 ? 1.81597 1.98958 1.32573 -0.22452 0.31024  -0.04985 166 PHE A CE2   
1411 C CZ    . PHE B 166 ? 1.69178 1.86888 1.23673 -0.21723 0.29777  -0.04423 166 PHE A CZ    
1412 N N     . GLU B 167 ? 1.67690 1.80673 1.05796 -0.25915 0.22045  -0.03897 167 GLU A N     
1413 C CA    . GLU B 167 ? 1.73763 1.85940 1.08578 -0.26963 0.20346  -0.03424 167 GLU A CA    
1414 C C     . GLU B 167 ? 1.73480 1.85749 1.10525 -0.26698 0.18118  -0.02235 167 GLU A C     
1415 O O     . GLU B 167 ? 1.77371 1.89816 1.13374 -0.27382 0.16844  -0.00782 167 GLU A O     
1416 C CB    . GLU B 167 ? 1.92516 2.03361 1.24897 -0.27243 0.20376  -0.05136 167 GLU A CB    
1417 C CG    . GLU B 167 ? 1.86191 1.96762 1.16918 -0.27262 0.22762  -0.06670 167 GLU A CG    
1418 C CD    . GLU B 167 ? 2.06069 2.15199 1.32499 -0.28191 0.22584  -0.07890 167 GLU A CD    
1419 O OE1   . GLU B 167 ? 2.21462 2.30058 1.45739 -0.29055 0.20673  -0.07145 167 GLU A OE1   
1420 O OE2   . GLU B 167 ? 2.25415 2.33926 1.50730 -0.28062 0.24326  -0.09564 167 GLU A OE2   
1421 N N     . LYS B 168 ? 1.78625 1.90865 1.18885 -0.25698 0.17783  -0.02734 168 LYS A N     
1422 C CA    . LYS B 168 ? 1.63143 1.75397 1.05616 -0.25382 0.15792  -0.01698 168 LYS A CA    
1423 C C     . LYS B 168 ? 1.74767 1.88019 1.19019 -0.25304 0.15495  0.00018  168 LYS A C     
1424 O O     . LYS B 168 ? 1.61662 1.74848 1.06131 -0.25595 0.13795  0.01264  168 LYS A O     
1425 C CB    . LYS B 168 ? 1.58968 1.71109 1.04700 -0.24270 0.15803  -0.02550 168 LYS A CB    
1426 C CG    . LYS B 168 ? 1.61558 1.73399 1.09021 -0.23996 0.13828  -0.01872 168 LYS A CG    
1427 C CD    . LYS B 168 ? 1.75447 1.86205 1.21676 -0.24158 0.13008  -0.02961 168 LYS A CD    
1428 C CE    . LYS B 168 ? 2.02090 2.12594 1.49675 -0.23387 0.14209  -0.04568 168 LYS A CE    
1429 N NZ    . LYS B 168 ? 1.80471 1.91460 1.31952 -0.22334 0.14085  -0.04312 168 LYS A NZ    
1430 N N     . PHE B 169 ? 1.82611 1.96729 1.28174 -0.24942 0.17085  0.00099  169 PHE A N     
1431 C CA    . PHE B 169 ? 1.54034 1.69079 1.01654 -0.24805 0.16817  0.01679  169 PHE A CA    
1432 C C     . PHE B 169 ? 1.71447 1.86626 1.16670 -0.25846 0.16085  0.03066  169 PHE A C     
1433 O O     . PHE B 169 ? 1.82177 1.98054 1.28847 -0.25850 0.15816  0.04440  169 PHE A O     
1434 C CB    . PHE B 169 ? 1.60872 1.76813 1.10363 -0.24260 0.18720  0.01417  169 PHE A CB    
1435 C CG    . PHE B 169 ? 1.62970 1.78955 1.15583 -0.23174 0.19221  0.00446  169 PHE A CG    
1436 C CD1   . PHE B 169 ? 1.49405 1.64939 1.03871 -0.22640 0.17801  0.00437  169 PHE A CD1   
1437 C CD2   . PHE B 169 ? 1.63332 1.79831 1.17118 -0.22700 0.21125  -0.00387 169 PHE A CD2   
1438 C CE1   . PHE B 169 ? 1.39702 1.55281 0.96928 -0.21704 0.18225  -0.00367 169 PHE A CE1   
1439 C CE2   . PHE B 169 ? 1.43917 1.60476 1.00646 -0.21747 0.21490  -0.01162 169 PHE A CE2   
1440 C CZ    . PHE B 169 ? 1.40136 1.56229 0.98495 -0.21273 0.20014  -0.01140 169 PHE A CZ    
1441 N N     . GLU B 170 ? 1.83249 1.97742 1.24946 -0.26737 0.15690  0.02769  170 GLU A N     
1442 C CA    . GLU B 170 ? 1.75041 1.89623 1.14377 -0.27810 0.14787  0.04213  170 GLU A CA    
1443 C C     . GLU B 170 ? 1.71122 1.85396 1.11611 -0.27855 0.12525  0.05361  170 GLU A C     
1444 O O     . GLU B 170 ? 1.66380 1.79873 1.04842 -0.28456 0.11256  0.05283  170 GLU A O     
1445 C CB    . GLU B 170 ? 1.81914 1.95822 1.16900 -0.28829 0.15139  0.03517  170 GLU A CB    
1446 C CG    . GLU B 170 ? 2.02646 2.16815 1.36319 -0.28833 0.17539  0.02417  170 GLU A CG    
1447 C CD    . GLU B 170 ? 2.22512 2.35805 1.51673 -0.29823 0.18001  0.01480  170 GLU A CD    
1448 O OE1   . GLU B 170 ? 2.17317 2.30455 1.43629 -0.30923 0.17122  0.02510  170 GLU A OE1   
1449 O OE2   . GLU B 170 ? 2.19102 2.31816 1.47564 -0.29524 0.19224  -0.00273 170 GLU A OE2   
1450 N N     . LYS B 171 ? 1.93235 2.08059 1.36866 -0.27267 0.12058  0.06385  171 LYS A N     
1451 C CA    . LYS B 171 ? 1.86768 2.01278 1.31902 -0.27183 0.10069  0.07444  171 LYS A CA    
1452 C C     . LYS B 171 ? 1.81548 1.96624 1.27200 -0.27602 0.09494  0.09287  171 LYS A C     
1453 O O     . LYS B 171 ? 1.87641 2.03266 1.31777 -0.28166 0.10462  0.09744  171 LYS A O     
1454 C CB    . LYS B 171 ? 1.66304 1.80743 1.14905 -0.26020 0.09960  0.06877  171 LYS A CB    
1455 C CG    . LYS B 171 ? 1.71098 1.86283 1.22003 -0.25296 0.11419  0.06654  171 LYS A CG    
1456 C CD    . LYS B 171 ? 1.75939 1.90971 1.29973 -0.24225 0.11275  0.06036  171 LYS A CD    
1457 C CE    . LYS B 171 ? 1.76241 1.90585 1.29773 -0.23938 0.11227  0.04594  171 LYS A CE    
1458 N NZ    . LYS B 171 ? 1.94168 2.08559 1.45921 -0.24094 0.12785  0.03333  171 LYS A NZ    
1459 N N     . LEU B 172 ? 1.58496 1.73416 1.06275 -0.27328 0.08034  0.10299  172 LEU A N     
1460 C CA    . LEU B 172 ? 1.70071 1.85422 1.18601 -0.27692 0.07398  0.12072  172 LEU A CA    
1461 C C     . LEU B 172 ? 1.78843 1.95024 1.28721 -0.27357 0.08897  0.12187  172 LEU A C     
1462 O O     . LEU B 172 ? 1.75023 1.91351 1.26605 -0.26532 0.09910  0.11107  172 LEU A O     
1463 C CB    . LEU B 172 ? 1.55364 1.70319 1.06377 -0.27268 0.05817  0.12907  172 LEU A CB    
1464 C CG    . LEU B 172 ? 1.83132 1.97466 1.32963 -0.27859 0.04072  0.13539  172 LEU A CG    
1465 C CD1   . LEU B 172 ? 2.05910 2.20462 1.53131 -0.29047 0.03625  0.14774  172 LEU A CD1   
1466 C CD2   . LEU B 172 ? 1.77824 1.91544 1.26456 -0.27782 0.03897  0.12153  172 LEU A CD2   
1467 N N     . PRO B 173 ? 1.72734 1.89482 1.22078 -0.27971 0.09035  0.13513  173 PRO A N     
1468 C CA    . PRO B 173 ? 1.64515 1.82101 1.15026 -0.27743 0.10504  0.13638  173 PRO A CA    
1469 C C     . PRO B 173 ? 1.57629 1.75301 1.11733 -0.26780 0.10455  0.13611  173 PRO A C     
1470 O O     . PRO B 173 ? 1.60660 1.78618 1.16054 -0.26120 0.11649  0.12568  173 PRO A O     
1471 C CB    . PRO B 173 ? 1.75548 1.93600 1.24992 -0.28640 0.10217  0.15325  173 PRO A CB    
1472 C CG    . PRO B 173 ? 1.97504 2.14953 1.44665 -0.29439 0.08712  0.15948  173 PRO A CG    
1473 C CD    . PRO B 173 ? 1.75244 1.91870 1.23131 -0.28886 0.07728  0.15009  173 PRO A CD    
1474 N N     . LEU B 174 ? 1.54877 1.72262 1.10579 -0.26720 0.09094  0.14746  174 LEU A N     
1475 C CA    . LEU B 174 ? 1.75949 1.93304 1.34901 -0.25892 0.09003  0.14804  174 LEU A CA    
1476 C C     . LEU B 174 ? 1.74666 1.91765 1.34695 -0.25027 0.09551  0.13217  174 LEU A C     
1477 O O     . LEU B 174 ? 1.69037 1.86400 1.31262 -0.24405 0.10179  0.12919  174 LEU A O     
1478 C CB    . LEU B 174 ? 1.87005 2.03751 1.47226 -0.25884 0.07368  0.15904  174 LEU A CB    
1479 C CG    . LEU B 174 ? 1.44520 1.61488 1.04100 -0.26700 0.06724  0.17601  174 LEU A CG    
1480 C CD1   . LEU B 174 ? 1.61352 1.77626 1.22559 -0.26566 0.05181  0.18569  174 LEU A CD1   
1481 C CD2   . LEU B 174 ? 1.38837 1.56588 0.99246 -0.26818 0.07750  0.18171  174 LEU A CD2   
1482 N N     . ASP B 175 ? 1.59882 1.76480 1.18433 -0.25033 0.09280  0.12279  175 ASP A N     
1483 C CA    . ASP B 175 ? 1.59328 1.75621 1.19093 -0.24192 0.09675  0.10829  175 ASP A CA    
1484 C C     . ASP B 175 ? 1.57109 1.74056 1.17085 -0.23919 0.11436  0.09903  175 ASP A C     
1485 O O     . ASP B 175 ? 1.45957 1.62980 1.08173 -0.23147 0.11878  0.09288  175 ASP A O     
1486 C CB    . ASP B 175 ? 1.49167 1.64780 1.07326 -0.24303 0.09029  0.10018  175 ASP A CB    
1487 C CG    . ASP B 175 ? 1.75480 1.90540 1.33015 -0.24762 0.07332  0.11015  175 ASP A CG    
1488 O OD1   . ASP B 175 ? 1.85968 2.01070 1.44739 -0.24837 0.06603  0.12287  175 ASP A OD1   
1489 O OD2   . ASP B 175 ? 1.80665 1.95251 1.36461 -0.25092 0.06757  0.10545  175 ASP A OD2   
1490 N N     . THR B 176 ? 1.35553 1.52929 0.93265 -0.24542 0.12419  0.09803  176 THR A N     
1491 C CA    . THR B 176 ? 1.36705 1.54737 0.94700 -0.24288 0.14245  0.08958  176 THR A CA    
1492 C C     . THR B 176 ? 1.50469 1.69174 1.11190 -0.23920 0.14632  0.09699  176 THR A C     
1493 O O     . THR B 176 ? 1.59568 1.78643 1.22081 -0.23297 0.15655  0.08949  176 THR A O     
1494 C CB    . THR B 176 ? 1.47526 1.65870 1.02498 -0.25119 0.15219  0.08957  176 THR A CB    
1495 O OG1   . THR B 176 ? 1.58109 1.75662 1.10687 -0.25413 0.14718  0.08110  176 THR A OG1   
1496 C CG2   . THR B 176 ? 1.50527 1.69596 1.05876 -0.24883 0.17249  0.08201  176 THR A CG2   
1497 N N     . LEU B 177 ? 1.44079 1.62900 1.05214 -0.24308 0.13773  0.11154  177 LEU A N     
1498 C CA    . LEU B 177 ? 1.41005 1.60378 1.04681 -0.24061 0.13986  0.11967  177 LEU A CA    
1499 C C     . LEU B 177 ? 1.38414 1.57367 1.04703 -0.23191 0.13492  0.11433  177 LEU A C     
1500 O O     . LEU B 177 ? 1.26300 1.45757 0.94669 -0.22790 0.14203  0.11357  177 LEU A O     
1501 C CB    . LEU B 177 ? 1.36916 1.56272 1.00372 -0.24676 0.12967  0.13584  177 LEU A CB    
1502 C CG    . LEU B 177 ? 1.57176 1.77075 1.18263 -0.25598 0.13492  0.14364  177 LEU A CG    
1503 C CD1   . LEU B 177 ? 1.67169 1.86844 1.28005 -0.26190 0.12155  0.15944  177 LEU A CD1   
1504 C CD2   . LEU B 177 ? 1.68397 1.89325 1.30299 -0.25625 0.15081  0.14488  177 LEU A CD2   
1505 N N     . LYS B 178 ? 1.41009 1.59084 1.07200 -0.22945 0.12310  0.11131  178 LYS A N     
1506 C CA    . LYS B 178 ? 1.42346 1.59936 1.10823 -0.22149 0.11814  0.10641  178 LYS A CA    
1507 C C     . LYS B 178 ? 1.40286 1.58250 1.09688 -0.21585 0.13030  0.09410  178 LYS A C     
1508 O O     . LYS B 178 ? 1.43308 1.61473 1.14980 -0.21112 0.13239  0.09406  178 LYS A O     
1509 C CB    . LYS B 178 ? 1.35396 1.52046 1.03354 -0.21992 0.10583  0.10362  178 LYS A CB    
1510 C CG    . LYS B 178 ? 1.55448 1.71687 1.22540 -0.22535 0.09335  0.11545  178 LYS A CG    
1511 C CD    . LYS B 178 ? 1.23585 1.38993 0.90197 -0.22403 0.08217  0.11242  178 LYS A CD    
1512 C CE    . LYS B 178 ? 1.67840 1.82929 1.33574 -0.23000 0.07028  0.12458  178 LYS A CE    
1513 N NZ    . LYS B 178 ? 1.59476 1.73859 1.24812 -0.22911 0.05990  0.12191  178 LYS A NZ    
1514 N N     . GLN B 179 ? 1.26242 1.44260 0.93939 -0.21674 0.13783  0.08430  179 GLN A N     
1515 C CA    . GLN B 179 ? 1.26285 1.44580 0.94930 -0.21106 0.14973  0.07183  179 GLN A CA    
1516 C C     . GLN B 179 ? 1.43751 1.63060 1.13596 -0.21125 0.16297  0.07501  179 GLN A C     
1517 O O     . GLN B 179 ? 1.54036 1.73654 1.25993 -0.20537 0.16933  0.06974  179 GLN A O     
1518 C CB    . GLN B 179 ? 1.33452 1.51419 0.99790 -0.21274 0.15437  0.06064  179 GLN A CB    
1519 C CG    . GLN B 179 ? 1.61911 1.78995 1.26647 -0.21543 0.14017  0.06119  179 GLN A CG    
1520 C CD    . GLN B 179 ? 1.78463 1.95032 1.41501 -0.21542 0.14271  0.04803  179 GLN A CD    
1521 O OE1   . GLN B 179 ? 1.86856 2.03645 1.49939 -0.21275 0.15568  0.03725  179 GLN A OE1   
1522 N NE2   . GLN B 179 ? 1.68236 1.84079 1.29887 -0.21843 0.13008  0.04892  179 GLN A NE2   
1523 N N     . LEU B 180 ? 1.40334 1.60166 1.08988 -0.21793 0.16668  0.08402  180 LEU A N     
1524 C CA    . LEU B 180 ? 1.27418 1.48287 0.97370 -0.21857 0.17920  0.08869  180 LEU A CA    
1525 C C     . LEU B 180 ? 1.21491 1.42505 0.94525 -0.21394 0.17415  0.09387  180 LEU A C     
1526 O O     . LEU B 180 ? 1.17856 1.39393 0.92855 -0.20924 0.18311  0.08918  180 LEU A O     
1527 C CB    . LEU B 180 ? 1.29823 1.51118 0.98146 -0.22694 0.18022  0.10037  180 LEU A CB    
1528 C CG    . LEU B 180 ? 1.33706 1.56064 1.03608 -0.22850 0.18999  0.10903  180 LEU A CG    
1529 C CD1   . LEU B 180 ? 1.40556 1.63666 1.10645 -0.22655 0.20928  0.10049  180 LEU A CD1   
1530 C CD2   . LEU B 180 ? 1.31069 1.53698 0.99598 -0.23682 0.18683  0.12285  180 LEU A CD2   
1531 N N     . TYR B 181 ? 1.20882 1.41392 0.94316 -0.21544 0.16014  0.10317  181 TYR A N     
1532 C CA    . TYR B 181 ? 1.15199 1.35684 0.91267 -0.21219 0.15437  0.10855  181 TYR A CA    
1533 C C     . TYR B 181 ? 1.21007 1.41154 0.98580 -0.20463 0.15408  0.09812  181 TYR A C     
1534 O O     . TYR B 181 ? 1.25529 1.46092 1.05340 -0.20151 0.15731  0.09869  181 TYR A O     
1535 C CB    . TYR B 181 ? 1.13583 1.33323 0.89363 -0.21510 0.13951  0.11827  181 TYR A CB    
1536 C CG    . TYR B 181 ? 1.35175 1.55314 1.09872 -0.22274 0.13930  0.13045  181 TYR A CG    
1537 C CD1   . TYR B 181 ? 1.24801 1.45984 0.99945 -0.22591 0.15042  0.13554  181 TYR A CD1   
1538 C CD2   . TYR B 181 ? 1.39938 1.59443 1.13285 -0.22683 0.12816  0.13744  181 TYR A CD2   
1539 C CE1   . TYR B 181 ? 1.23026 1.44599 0.97202 -0.23312 0.15041  0.14725  181 TYR A CE1   
1540 C CE2   . TYR B 181 ? 1.34283 1.54157 1.06698 -0.23405 0.12750  0.14932  181 TYR A CE2   
1541 C CZ    . TYR B 181 ? 1.31683 1.52589 1.04450 -0.23730 0.13867  0.15421  181 TYR A CZ    
1542 O OH    . TYR B 181 ? 1.45139 1.66433 1.17005 -0.24465 0.13818  0.16652  181 TYR A OH    
1543 N N     . TYR B 182 ? 1.19031 1.38455 0.95461 -0.20209 0.14984  0.08938  182 TYR A N     
1544 C CA    . TYR B 182 ? 1.16040 1.35094 0.93837 -0.19497 0.14907  0.07954  182 TYR A CA    
1545 C C     . TYR B 182 ? 1.19960 1.39816 0.98843 -0.19195 0.16342  0.07249  182 TYR A C     
1546 O O     . TYR B 182 ? 1.31394 1.51405 1.12520 -0.18723 0.16416  0.07075  182 TYR A O     
1547 C CB    . TYR B 182 ? 1.16299 1.34556 0.92474 -0.19367 0.14382  0.07132  182 TYR A CB    
1548 C CG    . TYR B 182 ? 1.16559 1.33866 0.92590 -0.19331 0.12887  0.07548  182 TYR A CG    
1549 C CD1   . TYR B 182 ? 1.34268 1.51242 1.12035 -0.19111 0.12157  0.08126  182 TYR A CD1   
1550 C CD2   . TYR B 182 ? 1.20149 1.36855 0.94338 -0.19532 0.12228  0.07355  182 TYR A CD2   
1551 C CE1   . TYR B 182 ? 1.52595 1.68649 1.30287 -0.19043 0.10946  0.08457  182 TYR A CE1   
1552 C CE2   . TYR B 182 ? 1.62684 1.78566 1.36996 -0.19463 0.10947  0.07774  182 TYR A CE2   
1553 C CZ    . TYR B 182 ? 1.78783 1.94331 1.54867 -0.19190 0.10374  0.08301  182 TYR A CZ    
1554 O OH    . TYR B 182 ? 1.83051 1.97733 1.59305 -0.19090 0.09255  0.08668  182 TYR A OH    
1555 N N     . LEU B 183 ? 1.24217 1.44558 1.01576 -0.19484 0.17487  0.06883  183 LEU A N     
1556 C CA    . LEU B 183 ? 1.30424 1.51455 1.08787 -0.19147 0.19033  0.06066  183 LEU A CA    
1557 C C     . LEU B 183 ? 1.35970 1.57857 1.17138 -0.18987 0.19481  0.06754  183 LEU A C     
1558 O O     . LEU B 183 ? 1.54898 1.77129 1.38000 -0.18465 0.20179  0.06149  183 LEU A O     
1559 C CB    . LEU B 183 ? 1.37141 1.58516 1.13184 -0.19614 0.20238  0.05754  183 LEU A CB    
1560 C CG    . LEU B 183 ? 1.91026 2.11643 1.64756 -0.19605 0.20293  0.04550  183 LEU A CG    
1561 C CD1   . LEU B 183 ? 1.75212 1.95767 1.45799 -0.20382 0.20535  0.04777  183 LEU A CD1   
1562 C CD2   . LEU B 183 ? 2.02771 2.23574 1.77456 -0.19064 0.21641  0.03263  183 LEU A CD2   
1563 N N     . SER B 184 ? 1.29224 1.51418 1.10723 -0.19436 0.19025  0.08010  184 SER A N     
1564 C CA    . SER B 184 ? 1.29672 1.52733 1.13829 -0.19393 0.19431  0.08765  184 SER A CA    
1565 C C     . SER B 184 ? 1.55768 1.78641 1.42370 -0.18779 0.18980  0.08394  184 SER A C     
1566 O O     . SER B 184 ? 1.85809 2.09502 1.74787 -0.18622 0.19629  0.08671  184 SER A O     
1567 C CB    . SER B 184 ? 1.51571 1.74673 1.35806 -0.19937 0.18586  0.10136  184 SER A CB    
1568 O OG    . SER B 184 ? 1.78423 2.00483 1.62543 -0.19872 0.16987  0.10351  184 SER A OG    
1569 N N     . LYS B 185 ? 1.41090 1.62955 1.27212 -0.18470 0.17908  0.07862  185 LYS A N     
1570 C CA    . LYS B 185 ? 1.41715 1.63324 1.30019 -0.17951 0.17349  0.07627  185 LYS A CA    
1571 C C     . LYS B 185 ? 1.40643 1.61998 1.28953 -0.17381 0.17820  0.06329  185 LYS A C     
1572 O O     . LYS B 185 ? 1.72067 1.92835 1.61325 -0.16988 0.17019  0.06044  185 LYS A O     
1573 C CB    . LYS B 185 ? 1.57804 1.78387 1.45808 -0.18019 0.15738  0.08093  185 LYS A CB    
1574 C CG    . LYS B 185 ? 1.50495 1.71058 1.38335 -0.18586 0.15094  0.09315  185 LYS A CG    
1575 C CD    . LYS B 185 ? 1.61144 1.80545 1.48716 -0.18592 0.13618  0.09627  185 LYS A CD    
1576 C CE    . LYS B 185 ? 1.70789 1.90068 1.58351 -0.19139 0.12988  0.10790  185 LYS A CE    
1577 N NZ    . LYS B 185 ? 1.65540 1.83592 1.52901 -0.19109 0.11690  0.10998  185 LYS A NZ    
1578 N N     . GLN B 186 ? 1.37668 1.59382 1.24927 -0.17357 0.19075  0.05566  186 GLN A N     
1579 C CA    . GLN B 186 ? 1.79559 2.00885 1.66648 -0.16850 0.19489  0.04257  186 GLN A CA    
1580 C C     . GLN B 186 ? 1.96429 2.18492 1.86195 -0.16366 0.20542  0.03887  186 GLN A C     
1581 O O     . GLN B 186 ? 1.95752 2.17460 1.86916 -0.15852 0.20137  0.03370  186 GLN A O     
1582 C CB    . GLN B 186 ? 1.55329 1.76484 1.39724 -0.17110 0.20278  0.03516  186 GLN A CB    
1583 C CG    . GLN B 186 ? 1.47425 1.67560 1.29402 -0.17339 0.19082  0.03365  186 GLN A CG    
1584 C CD    . GLN B 186 ? 1.72281 1.91923 1.52375 -0.17279 0.19595  0.02116  186 GLN A CD    
1585 O OE1   . GLN B 186 ? 2.05127 2.25130 1.85412 -0.17102 0.20974  0.01292  186 GLN A OE1   
1586 N NE2   . GLN B 186 ? 1.62017 1.80781 1.40324 -0.17440 0.18482  0.01964  186 GLN A NE2   
1587 N N     . LEU B 187 ? 1.75393 1.98449 1.65921 -0.16522 0.21863  0.04170  187 LEU A N     
1588 C CA    . LEU B 187 ? 1.86745 2.10626 1.80115 -0.16068 0.23006  0.03924  187 LEU A CA    
1589 C C     . LEU B 187 ? 1.81051 2.06025 1.74851 -0.16383 0.24424  0.04463  187 LEU A C     
1590 O O     . LEU B 187 ? 1.93207 2.18215 1.85053 -0.16960 0.24322  0.05060  187 LEU A O     
1591 C CB    . LEU B 187 ? 1.91861 2.15349 1.85051 -0.15554 0.23776  0.02488  187 LEU A CB    
1592 C CG    . LEU B 187 ? 1.94908 2.18934 1.91415 -0.14948 0.24423  0.02210  187 LEU A CG    
1593 C CD1   . LEU B 187 ? 1.89685 2.13956 1.88658 -0.14901 0.23203  0.03294  187 LEU A CD1   
1594 C CD2   . LEU B 187 ? 1.89312 2.12603 1.85603 -0.14436 0.24546  0.00884  187 LEU A CD2   
1595 N N     . LYS B 188 ? 1.93859 2.19703 1.90208 -0.16020 0.25720  0.04306  188 LYS A N     
1596 C CA    . LYS B 188 ? 2.16524 2.43465 2.13445 -0.16271 0.27305  0.04766  188 LYS A CA    
1597 C C     . LYS B 188 ? 2.06283 2.32886 1.99864 -0.16545 0.28416  0.03916  188 LYS A C     
1598 O O     . LYS B 188 ? 2.01634 2.28904 1.94472 -0.16982 0.29418  0.04449  188 LYS A O     
1599 C CB    . LYS B 188 ? 2.11734 2.39590 2.12135 -0.15738 0.28595  0.04597  188 LYS A CB    
1600 C CG    . LYS B 188 ? 1.95383 2.22956 1.95433 -0.15235 0.30032  0.03065  188 LYS A CG    
1601 C CD    . LYS B 188 ? 1.76274 2.04474 1.80163 -0.14578 0.30792  0.02864  188 LYS A CD    
1602 C CE    . LYS B 188 ? 1.86279 2.13937 1.91628 -0.14236 0.29159  0.02905  188 LYS A CE    
1603 N NZ    . LYS B 188 ? 1.86574 2.12958 1.89368 -0.14093 0.28516  0.01740  188 LYS A NZ    
1604 N N     . TYR B 189 ? 1.87060 2.12626 1.78621 -0.16357 0.28144  0.02710  189 TYR A N     
1605 C CA    . TYR B 189 ? 1.90143 2.15238 1.78332 -0.16665 0.29123  0.01782  189 TYR A CA    
1606 C C     . TYR B 189 ? 1.91104 2.16232 1.76814 -0.17450 0.28617  0.02741  189 TYR A C     
1607 O O     . TYR B 189 ? 1.87867 2.12427 1.72671 -0.17699 0.26879  0.03350  189 TYR A O     
1608 C CB    . TYR B 189 ? 1.80767 2.04670 1.67498 -0.16373 0.28473  0.00505  189 TYR A CB    
1609 C CG    . TYR B 189 ? 1.92922 2.16860 1.82425 -0.15599 0.28976  -0.00314 189 TYR A CG    
1610 C CD1   . TYR B 189 ? 1.74204 1.99094 1.66383 -0.15243 0.30589  -0.00354 189 TYR A CD1   
1611 C CD2   . TYR B 189 ? 1.96966 2.20018 1.86582 -0.15224 0.27845  -0.00970 189 TYR A CD2   
1612 C CE1   . TYR B 189 ? 1.79116 2.04059 1.74032 -0.14542 0.31007  -0.01007 189 TYR A CE1   
1613 C CE2   . TYR B 189 ? 1.76702 1.99789 1.68904 -0.14544 0.28258  -0.01639 189 TYR A CE2   
1614 C CZ    . TYR B 189 ? 1.85528 2.09555 1.80410 -0.14202 0.29813  -0.01647 189 TYR A CZ    
1615 O OH    . TYR B 189 ? 1.95782 2.19853 1.93392 -0.13534 0.30182  -0.02230 189 TYR A OH    
1616 N N     . ASP B 190 ? 1.89473 2.15229 1.74141 -0.17829 0.30143  0.02880  190 ASP A N     
1617 C CA    . ASP B 190 ? 1.89385 2.15308 1.71874 -0.18623 0.29767  0.03948  190 ASP A CA    
1618 C C     . ASP B 190 ? 1.91717 2.16621 1.70101 -0.19095 0.29392  0.03275  190 ASP A C     
1619 O O     . ASP B 190 ? 2.01788 2.26876 1.77873 -0.19615 0.30536  0.03225  190 ASP A O     
1620 C CB    . ASP B 190 ? 1.87994 2.15101 1.71287 -0.18865 0.31529  0.04554  190 ASP A CB    
1621 C CG    . ASP B 190 ? 2.00802 2.28988 1.88352 -0.18375 0.32168  0.05086  190 ASP A CG    
1622 O OD1   . ASP B 190 ? 2.16888 2.45299 2.06478 -0.18366 0.30785  0.06143  190 ASP A OD1   
1623 O OD2   . ASP B 190 ? 1.99346 2.28088 1.88158 -0.18019 0.34032  0.04430  190 ASP A OD2   
1624 N N     . LEU B 191 ? 1.65397 1.89275 1.42889 -0.18961 0.27836  0.02839  191 LEU A N     
1625 C CA    . LEU B 191 ? 1.67764 1.90670 1.41486 -0.19477 0.27205  0.02370  191 LEU A CA    
1626 C C     . LEU B 191 ? 1.73977 1.96921 1.46391 -0.20166 0.25959  0.03797  191 LEU A C     
1627 O O     . LEU B 191 ? 1.75914 1.98308 1.45145 -0.20780 0.25582  0.03771  191 LEU A O     
1628 C CB    . LEU B 191 ? 1.77432 1.99290 1.50993 -0.19055 0.26067  0.01410  191 LEU A CB    
1629 C CG    . LEU B 191 ? 1.95174 2.16653 1.68710 -0.18589 0.27276  -0.00226 191 LEU A CG    
1630 C CD1   . LEU B 191 ? 1.87115 2.07759 1.61498 -0.18069 0.26038  -0.00907 191 LEU A CD1   
1631 C CD2   . LEU B 191 ? 1.88590 2.09543 1.58376 -0.19192 0.28089  -0.00993 191 LEU A CD2   
1632 N N     . TYR B 192 ? 1.78778 2.02303 1.53586 -0.20098 0.25302  0.05013  192 TYR A N     
1633 C CA    . TYR B 192 ? 1.73288 1.96866 1.47142 -0.20747 0.24206  0.06432  192 TYR A CA    
1634 C C     . TYR B 192 ? 1.72653 1.96811 1.44486 -0.21420 0.25470  0.06819  192 TYR A C     
1635 O O     . TYR B 192 ? 1.72657 1.96444 1.41845 -0.22098 0.24798  0.07346  192 TYR A O     
1636 C CB    . TYR B 192 ? 1.73326 1.97422 1.50236 -0.20567 0.23505  0.07569  192 TYR A CB    
1637 C CG    . TYR B 192 ? 1.78595 2.03738 1.58449 -0.20179 0.24837  0.07608  192 TYR A CG    
1638 C CD1   . TYR B 192 ? 1.93583 2.18733 1.76237 -0.19506 0.24544  0.07262  192 TYR A CD1   
1639 C CD2   . TYR B 192 ? 1.74140 2.00290 1.54078 -0.20510 0.26365  0.08083  192 TYR A CD2   
1640 C CE1   . TYR B 192 ? 2.07765 2.33902 1.93317 -0.19178 0.25653  0.07409  192 TYR A CE1   
1641 C CE2   . TYR B 192 ? 1.86872 2.14035 1.69775 -0.20150 0.27576  0.08210  192 TYR A CE2   
1642 C CZ    . TYR B 192 ? 2.18494 2.45658 2.04272 -0.19485 0.27179  0.07888  192 TYR A CZ    
1643 O OH    . TYR B 192 ? 2.39703 2.67895 2.28602 -0.19150 0.28281  0.08105  192 TYR A OH    
1644 N N     . ASP B 193 ? 1.69846 1.94895 1.42921 -0.21244 0.27306  0.06577  193 ASP A N     
1645 C CA    . ASP B 193 ? 1.74018 1.99672 1.45191 -0.21868 0.28793  0.06898  193 ASP A CA    
1646 C C     . ASP B 193 ? 1.70653 1.95398 1.37808 -0.22317 0.28908  0.05968  193 ASP A C     
1647 O O     . ASP B 193 ? 1.80071 2.04826 1.44633 -0.23120 0.28831  0.06684  193 ASP A O     
1648 C CB    . ASP B 193 ? 1.97042 2.23698 1.70313 -0.21491 0.30902  0.06556  193 ASP A CB    
1649 C CG    . ASP B 193 ? 2.05963 2.33536 1.83400 -0.21064 0.30757  0.07457  193 ASP A CG    
1650 O OD1   . ASP B 193 ? 1.97190 2.24535 1.75727 -0.21082 0.28987  0.08316  193 ASP A OD1   
1651 O OD2   . ASP B 193 ? 2.03319 2.31789 1.82878 -0.20735 0.32414  0.07298  193 ASP A OD2   
1652 N N     . ILE B 194 ? 1.65788 1.89747 1.32465 -0.21859 0.28996  0.04479  194 ILE A N     
1653 C CA    . ILE B 194 ? 1.76340 1.99330 1.39137 -0.22318 0.29096  0.03462  194 ILE A CA    
1654 C C     . ILE B 194 ? 1.65542 1.87915 1.26188 -0.22974 0.27107  0.04377  194 ILE A C     
1655 O O     . ILE B 194 ? 1.89751 2.11915 1.47140 -0.23796 0.27255  0.04616  194 ILE A O     
1656 C CB    . ILE B 194 ? 1.75152 1.97331 1.38261 -0.21670 0.29222  0.01789  194 ILE A CB    
1657 C CG1   . ILE B 194 ? 1.76460 1.99289 1.42303 -0.20944 0.31064  0.01027  194 ILE A CG1   
1658 C CG2   . ILE B 194 ? 1.75980 1.97093 1.35080 -0.22200 0.29301  0.00707  194 ILE A CG2   
1659 C CD1   . ILE B 194 ? 1.85972 2.09452 1.50794 -0.21263 0.33307  0.00884  194 ILE A CD1   
1660 N N     . PHE B 195 ? 1.54941 1.77035 1.17400 -0.22638 0.25353  0.04913  195 PHE A N     
1661 C CA    . PHE B 195 ? 1.61107 1.82588 1.21952 -0.23176 0.23429  0.05813  195 PHE A CA    
1662 C C     . PHE B 195 ? 1.72758 1.94910 1.32911 -0.23907 0.23435  0.07365  195 PHE A C     
1663 O O     . PHE B 195 ? 1.76565 1.98323 1.34031 -0.24669 0.22628  0.07948  195 PHE A O     
1664 C CB    . PHE B 195 ? 1.60871 1.81951 1.24183 -0.22561 0.21850  0.05996  195 PHE A CB    
1665 C CG    . PHE B 195 ? 1.69243 1.89285 1.31721 -0.22255 0.21038  0.04829  195 PHE A CG    
1666 C CD1   . PHE B 195 ? 1.75668 1.95541 1.38968 -0.21635 0.21982  0.03390  195 PHE A CD1   
1667 C CD2   . PHE B 195 ? 1.80189 1.99441 1.41272 -0.22584 0.19320  0.05230  195 PHE A CD2   
1668 C CE1   . PHE B 195 ? 1.56924 1.75851 1.19561 -0.21380 0.21210  0.02372  195 PHE A CE1   
1669 C CE2   . PHE B 195 ? 1.80479 1.98833 1.40969 -0.22322 0.18571  0.04231  195 PHE A CE2   
1670 C CZ    . PHE B 195 ? 1.66176 1.84362 1.27405 -0.21731 0.19503  0.02801  195 PHE A CZ    
1671 N N     . PHE B 196 ? 1.65314 1.88469 1.27902 -0.23716 0.24289  0.08077  196 PHE A N     
1672 C CA    . PHE B 196 ? 1.56015 1.79888 1.18273 -0.24403 0.24350  0.09640  196 PHE A CA    
1673 C C     . PHE B 196 ? 1.62007 1.85978 1.20823 -0.25173 0.25534  0.09499  196 PHE A C     
1674 O O     . PHE B 196 ? 1.64222 1.88130 1.20999 -0.25984 0.24808  0.10582  196 PHE A O     
1675 C CB    . PHE B 196 ? 1.53656 1.78605 1.19312 -0.24025 0.25208  0.10266  196 PHE A CB    
1676 C CG    . PHE B 196 ? 1.54808 1.80609 1.20478 -0.24695 0.25500  0.11840  196 PHE A CG    
1677 C CD1   . PHE B 196 ? 1.46953 1.72637 1.13307 -0.25013 0.23891  0.13234  196 PHE A CD1   
1678 C CD2   . PHE B 196 ? 1.52803 1.79508 1.17957 -0.24986 0.27442  0.11928  196 PHE A CD2   
1679 C CE1   . PHE B 196 ? 1.59878 1.86322 1.26360 -0.25637 0.24124  0.14702  196 PHE A CE1   
1680 C CE2   . PHE B 196 ? 1.55476 1.82998 1.20757 -0.25609 0.27709  0.13432  196 PHE A CE2   
1681 C CZ    . PHE B 196 ? 1.54732 1.82126 1.20688 -0.25943 0.26010  0.14830  196 PHE A CZ    
1682 N N     . GLU B 197 ? 1.67864 1.91932 1.26007 -0.24947 0.27330  0.08193  197 GLU A N     
1683 C CA    . GLU B 197 ? 1.76781 2.00815 1.31353 -0.25695 0.28655  0.07874  197 GLU A CA    
1684 C C     . GLU B 197 ? 1.75145 1.98088 1.26186 -0.26374 0.27158  0.07809  197 GLU A C     
1685 O O     . GLU B 197 ? 1.85509 2.08515 1.33867 -0.27306 0.27073  0.08692  197 GLU A O     
1686 C CB    . GLU B 197 ? 1.83555 2.07530 1.37878 -0.25253 0.30689  0.06183  197 GLU A CB    
1687 C CG    . GLU B 197 ? 2.01444 2.26496 1.59559 -0.24515 0.32188  0.06172  197 GLU A CG    
1688 C CD    . GLU B 197 ? 2.16435 2.41211 1.75268 -0.23801 0.33675  0.04387  197 GLU A CD    
1689 O OE1   . GLU B 197 ? 2.05754 2.29443 1.61994 -0.23900 0.33553  0.03100  197 GLU A OE1   
1690 O OE2   . GLU B 197 ? 2.28456 2.54084 1.90544 -0.23161 0.34904  0.04312  197 GLU A OE2   
1691 N N     . MET B 198 ? 1.70993 1.93001 1.22153 -0.25945 0.25985  0.06875  198 MET A N     
1692 C CA    . MET B 198 ? 1.67380 1.88337 1.15464 -0.26567 0.24440  0.06811  198 MET A CA    
1693 C C     . MET B 198 ? 1.73629 1.94753 1.21698 -0.27138 0.22761  0.08661  198 MET A C     
1694 O O     . MET B 198 ? 1.85364 2.06080 1.30331 -0.28048 0.22046  0.09196  198 MET A O     
1695 C CB    . MET B 198 ? 1.66038 1.86088 1.15014 -0.25915 0.23351  0.05691  198 MET A CB    
1696 C CG    . MET B 198 ? 1.72840 1.92688 1.22360 -0.25256 0.24874  0.03899  198 MET A CG    
1697 S SD    . MET B 198 ? 1.43072 1.61703 0.92758 -0.24724 0.23564  0.02564  198 MET A SD    
1698 C CE    . MET B 198 ? 1.63582 1.82369 1.16430 -0.24274 0.21491  0.03899  198 MET A CE    
1699 N N     . VAL B 199 ? 1.74003 1.95660 1.25407 -0.26654 0.22151  0.09604  199 VAL A N     
1700 C CA    . VAL B 199 ? 1.72091 1.93846 1.23848 -0.27131 0.20580  0.11364  199 VAL A CA    
1701 C C     . VAL B 199 ? 1.68726 1.91111 1.18366 -0.28084 0.21365  0.12443  199 VAL A C     
1702 O O     . VAL B 199 ? 1.65281 1.87350 1.12921 -0.28877 0.20149  0.13472  199 VAL A O     
1703 C CB    . VAL B 199 ? 1.56944 1.79123 1.12617 -0.26462 0.20050  0.12068  199 VAL A CB    
1704 C CG1   . VAL B 199 ? 1.66062 1.88460 1.22175 -0.27002 0.18882  0.13897  199 VAL A CG1   
1705 C CG2   . VAL B 199 ? 1.48348 1.69799 1.05832 -0.25641 0.18999  0.11229  199 VAL A CG2   
1706 N N     . ARG B 200 ? 1.74875 1.98135 1.25026 -0.28013 0.23332  0.12259  200 ARG A N     
1707 C CA    . ARG B 200 ? 1.73647 1.97591 1.21878 -0.28905 0.24297  0.13301  200 ARG A CA    
1708 C C     . ARG B 200 ? 1.77346 2.00598 1.21056 -0.29762 0.24424  0.12790  200 ARG A C     
1709 O O     . ARG B 200 ? 1.91044 2.14265 1.32628 -0.30699 0.23588  0.14061  200 ARG A O     
1710 C CB    . ARG B 200 ? 1.81539 2.06514 1.31226 -0.28585 0.26602  0.12975  200 ARG A CB    
1711 C CG    . ARG B 200 ? 1.71566 1.97283 1.25708 -0.27781 0.26670  0.13387  200 ARG A CG    
1712 C CD    . ARG B 200 ? 1.92887 2.19174 1.48467 -0.27144 0.28812  0.12199  200 ARG A CD    
1713 N NE    . ARG B 200 ? 2.17542 2.44263 1.70639 -0.27714 0.30806  0.12003  200 ARG A NE    
1714 C CZ    . ARG B 200 ? 2.19110 2.46289 1.72849 -0.27299 0.32976  0.10961  200 ARG A CZ    
1715 N NH1   . ARG B 200 ? 2.02089 2.29338 1.58823 -0.26323 0.33333  0.10002  200 ARG A NH1   
1716 N NH2   . ARG B 200 ? 2.08138 2.35680 1.59528 -0.27871 0.34810  0.10896  200 ARG A NH2   
1717 N N     . GLN B 201 ? 1.74432 1.97102 1.16734 -0.29485 0.25377  0.11019  201 GLN A N     
1718 C CA    . GLN B 201 ? 1.78564 2.00448 1.16315 -0.30350 0.25600  0.10356  201 GLN A CA    
1719 C C     . GLN B 201 ? 1.76808 1.97540 1.13445 -0.30453 0.23455  0.10048  201 GLN A C     
1720 O O     . GLN B 201 ? 1.93656 2.13511 1.28255 -0.30459 0.23707  0.08539  201 GLN A O     
1721 C CB    . GLN B 201 ? 1.81355 2.03112 1.18090 -0.30039 0.27853  0.08547  201 GLN A CB    
1722 C CG    . GLN B 201 ? 1.90250 2.13199 1.28660 -0.29787 0.30113  0.08762  201 GLN A CG    
1723 C CD    . GLN B 201 ? 2.25407 2.48874 1.61109 -0.30848 0.31003  0.09877  201 GLN A CD    
1724 O OE1   . GLN B 201 ? 2.35260 2.58160 1.67523 -0.31846 0.29953  0.10475  201 GLN A OE1   
1725 N NE2   . GLN B 201 ? 2.19378 2.43958 1.56664 -0.30667 0.32956  0.10222  201 GLN A NE2   
1726 N N     . TYR B 202 ? 1.77683 1.98396 1.15696 -0.30533 0.21459  0.11425  202 TYR A N     
1727 C CA    . TYR B 202 ? 1.85576 2.05267 1.23096 -0.30535 0.19397  0.11225  202 TYR A CA    
1728 C C     . TYR B 202 ? 1.85724 2.04935 1.19541 -0.31774 0.18274  0.12103  202 TYR A C     
1729 O O     . TYR B 202 ? 1.84171 2.03961 1.17157 -0.32504 0.18264  0.13598  202 TYR A O     
1730 C CB    . TYR B 202 ? 1.76406 1.96200 1.17606 -0.29860 0.17858  0.12099  202 TYR A CB    
1731 C CG    . TYR B 202 ? 1.71770 1.90600 1.12728 -0.29863 0.15777  0.12089  202 TYR A CG    
1732 C CD1   . TYR B 202 ? 1.70192 1.88360 1.11987 -0.29139 0.15558  0.10635  202 TYR A CD1   
1733 C CD2   . TYR B 202 ? 1.67918 1.86534 1.08006 -0.30587 0.14040  0.13599  202 TYR A CD2   
1734 C CE1   . TYR B 202 ? 1.70945 1.88289 1.12682 -0.29139 0.13716  0.10674  202 TYR A CE1   
1735 C CE2   . TYR B 202 ? 1.75101 1.92895 1.15223 -0.30576 0.12183  0.13661  202 TYR A CE2   
1736 C CZ    . TYR B 202 ? 1.76966 1.94135 1.17912 -0.29851 0.12038  0.12194  202 TYR A CZ    
1737 O OH    . TYR B 202 ? 1.63277 1.79688 1.04414 -0.29838 0.10249  0.12308  202 TYR A OH    
1738 N N     . ASP B 203 ? 1.97490 2.15665 1.29180 -0.32045 0.17280  0.11258  203 ASP A N     
1739 C CA    . ASP B 203 ? 1.95523 2.13168 1.23768 -0.33266 0.15941  0.12141  203 ASP A CA    
1740 C C     . ASP B 203 ? 1.86999 2.04101 1.16667 -0.33146 0.13505  0.12858  203 ASP A C     
1741 O O     . ASP B 203 ? 2.05036 2.21543 1.35978 -0.32451 0.12967  0.11756  203 ASP A O     
1742 C CB    . ASP B 203 ? 2.15245 2.32058 1.39396 -0.33899 0.16709  0.10686  203 ASP A CB    
1743 C CG    . ASP B 203 ? 2.21886 2.39115 1.45110 -0.33759 0.19379  0.09592  203 ASP A CG    
1744 O OD1   . ASP B 203 ? 2.08200 2.26089 1.30043 -0.34408 0.20370  0.10522  203 ASP A OD1   
1745 O OD2   . ASP B 203 ? 2.38572 2.55492 1.62638 -0.32975 0.20519  0.07848  203 ASP A OD2   
1746 N N     . ALA B 204 ? 1.92098 2.09407 1.21649 -0.33819 0.12080  0.14729  204 ALA A N     
1747 C CA    . ALA B 204 ? 2.11188 2.28155 1.42843 -0.33604 0.09907  0.15687  204 ALA A CA    
1748 C C     . ALA B 204 ? 2.15398 2.31483 1.44326 -0.34476 0.08216  0.15851  204 ALA A C     
1749 O O     . ALA B 204 ? 2.27060 2.43014 1.52393 -0.35645 0.08159  0.16317  204 ALA A O     
1750 C CB    . ALA B 204 ? 2.08524 2.26170 1.42039 -0.33787 0.09239  0.17695  204 ALA A CB    
1751 N N     . LYS B 205 ? 2.02803 2.18288 1.33488 -0.33932 0.06818  0.15515  205 LYS A N     
1752 C CA    . LYS B 205 ? 1.97845 2.12538 1.26781 -0.34660 0.04907  0.15879  205 LYS A CA    
1753 C C     . LYS B 205 ? 2.27407 2.41763 1.59781 -0.33773 0.03503  0.15935  205 LYS A C     
1754 O O     . LYS B 205 ? 2.32034 2.46545 1.67297 -0.32611 0.04274  0.15075  205 LYS A O     
1755 C CB    . LYS B 205 ? 2.00931 2.14869 1.26235 -0.35195 0.05427  0.14285  205 LYS A CB    
1756 C CG    . LYS B 205 ? 2.14515 2.28155 1.35488 -0.36745 0.04790  0.15088  205 LYS A CG    
1757 C CD    . LYS B 205 ? 2.21263 2.33835 1.38954 -0.37329 0.04488  0.13680  205 LYS A CD    
1758 C CE    . LYS B 205 ? 2.46462 2.58657 1.59745 -0.38979 0.03596  0.14630  205 LYS A CE    
1759 N NZ    . LYS B 205 ? 2.34727 2.45747 1.44648 -0.39674 0.03069  0.13325  205 LYS A NZ    
1760 N N     . PRO B 206 ? 2.41186 2.55091 1.73615 -0.34255 0.01405  0.17015  206 PRO A N     
1761 C CA    . PRO B 206 ? 2.26504 2.40051 1.62167 -0.33391 0.00216  0.16970  206 PRO A CA    
1762 C C     . PRO B 206 ? 2.11524 2.24243 1.46244 -0.33374 -0.00481 0.15719  206 PRO A C     
1763 O O     . PRO B 206 ? 2.21636 2.33911 1.52774 -0.34345 -0.00651 0.15285  206 PRO A O     
1764 C CB    . PRO B 206 ? 2.22084 2.35746 1.58638 -0.33962 -0.01565 0.19130  206 PRO A CB    
1765 C CG    . PRO B 206 ? 1.98549 2.12133 1.31020 -0.35443 -0.02038 0.19845  206 PRO A CG    
1766 C CD    . PRO B 206 ? 2.00937 2.14709 1.30667 -0.35624 0.00046  0.18481  206 PRO A CD    
1767 N N     . LEU B 207 ? 2.02986 2.15451 1.40767 -0.32335 -0.00878 0.15150  207 LEU A N     
1768 C CA    . LEU B 207 ? 2.08063 2.19752 1.45393 -0.32260 -0.01649 0.14042  207 LEU A CA    
1769 C C     . LEU B 207 ? 2.01015 2.12468 1.41165 -0.31945 -0.03504 0.15101  207 LEU A C     
1770 O O     . LEU B 207 ? 2.17649 2.29503 1.60520 -0.31459 -0.03728 0.16240  207 LEU A O     
1771 C CB    . LEU B 207 ? 1.93605 2.05168 1.31822 -0.31262 -0.00112 0.12055  207 LEU A CB    
1772 C CG    . LEU B 207 ? 2.15291 2.27045 1.51062 -0.31449 0.01880  0.10845  207 LEU A CG    
1773 C CD1   . LEU B 207 ? 1.97315 2.08894 1.34393 -0.30422 0.03192  0.08961  207 LEU A CD1   
1774 C CD2   . LEU B 207 ? 1.97608 2.08864 1.28946 -0.32772 0.01615  0.10667  207 LEU A CD2   
1775 N N     . ASP B 208 ? 1.90391 2.01188 1.29974 -0.32219 -0.04750 0.14738  208 ASP A N     
1776 C CA    . ASP B 208 ? 1.95008 2.05599 1.37300 -0.31993 -0.06559 0.15859  208 ASP A CA    
1777 C C     . ASP B 208 ? 2.01494 2.11749 1.46343 -0.30865 -0.06368 0.14618  208 ASP A C     
1778 O O     . ASP B 208 ? 1.98661 2.08782 1.46254 -0.30448 -0.07560 0.15397  208 ASP A O     
1779 C CB    . ASP B 208 ? 2.10722 2.20916 1.50892 -0.33255 -0.08454 0.16863  208 ASP A CB    
1780 C CG    . ASP B 208 ? 2.35746 2.46283 1.73809 -0.34404 -0.08980 0.18471  208 ASP A CG    
1781 O OD1   . ASP B 208 ? 2.38223 2.49342 1.76559 -0.34197 -0.07807 0.18831  208 ASP A OD1   
1782 O OD2   . ASP B 208 ? 2.28841 2.39065 1.65041 -0.35530 -0.10605 0.19406  208 ASP A OD2   
1783 N N     . LYS B 209 ? 2.08137 2.18227 1.52038 -0.30451 -0.04962 0.12787  209 LYS A N     
1784 C CA    . LYS B 209 ? 1.94976 2.04773 1.41280 -0.29371 -0.04669 0.11568  209 LYS A CA    
1785 C C     . LYS B 209 ? 1.77093 1.87240 1.27280 -0.28347 -0.04654 0.12348  209 LYS A C     
1786 O O     . LYS B 209 ? 1.75983 1.85844 1.28619 -0.27691 -0.05307 0.12250  209 LYS A O     
1787 C CB    . LYS B 209 ? 1.93910 2.03688 1.39264 -0.28894 -0.02797 0.09679  209 LYS A CB    
1788 C CG    . LYS B 209 ? 1.97537 2.06860 1.38964 -0.29804 -0.02414 0.08611  209 LYS A CG    
1789 C CD    . LYS B 209 ? 1.80536 1.90192 1.18967 -0.30744 -0.01806 0.09176  209 LYS A CD    
1790 C CE    . LYS B 209 ? 1.96467 2.05504 1.30826 -0.31706 -0.01508 0.08105  209 LYS A CE    
1791 N NZ    . LYS B 209 ? 1.99147 2.08463 1.30452 -0.32728 -0.01084 0.08836  209 LYS A NZ    
1792 N N     . PHE B 210 ? 1.89737 2.00438 1.40382 -0.28253 -0.03911 0.13086  210 PHE A N     
1793 C CA    . PHE B 210 ? 1.78749 1.89674 1.32856 -0.27356 -0.03849 0.13821  210 PHE A CA    
1794 C C     . PHE B 210 ? 2.00098 2.11101 1.54785 -0.27922 -0.05236 0.15760  210 PHE A C     
1795 O O     . PHE B 210 ? 2.05634 2.17053 1.59358 -0.28427 -0.04968 0.16659  210 PHE A O     
1796 C CB    . PHE B 210 ? 1.50239 1.61667 1.04591 -0.26869 -0.02096 0.13247  210 PHE A CB    
1797 C CG    . PHE B 210 ? 1.68022 1.79454 1.20691 -0.26744 -0.00719 0.11494  210 PHE A CG    
1798 C CD1   . PHE B 210 ? 1.93769 2.04863 1.47676 -0.25966 -0.00376 0.10158  210 PHE A CD1   
1799 C CD2   . PHE B 210 ? 1.56109 1.67867 1.06043 -0.27398 0.00284  0.11209  210 PHE A CD2   
1800 C CE1   . PHE B 210 ? 1.97093 2.08149 1.49640 -0.25840 0.00883  0.08581  210 PHE A CE1   
1801 C CE2   . PHE B 210 ? 1.50505 1.62212 0.99063 -0.27245 0.01636  0.09583  210 PHE A CE2   
1802 C CZ    . PHE B 210 ? 1.59496 1.70842 1.09419 -0.26459 0.01916  0.08271  210 PHE A CZ    
1803 N N     . TYR B 211 ? 2.20970 2.31602 1.77331 -0.27843 -0.06678 0.16446  211 TYR A N     
1804 C CA    . TYR B 211 ? 2.08068 2.18742 1.65327 -0.28366 -0.08119 0.18390  211 TYR A CA    
1805 C C     . TYR B 211 ? 2.13699 2.24668 1.72998 -0.27833 -0.07461 0.19147  211 TYR A C     
1806 O O     . TYR B 211 ? 2.18538 2.29703 1.77815 -0.28416 -0.08151 0.20692  211 TYR A O     
1807 C CB    . TYR B 211 ? 1.88273 1.98527 1.47690 -0.28148 -0.09574 0.18912  211 TYR A CB    
1808 C CG    . TYR B 211 ? 2.10302 2.20438 1.73583 -0.27108 -0.09545 0.19438  211 TYR A CG    
1809 C CD1   . TYR B 211 ? 2.20724 2.30657 1.85878 -0.25992 -0.08587 0.18201  211 TYR A CD1   
1810 C CD2   . TYR B 211 ? 2.06547 2.16714 1.71568 -0.27263 -0.10464 0.21174  211 TYR A CD2   
1811 C CE1   . TYR B 211 ? 2.22289 2.32009 1.90700 -0.25091 -0.08492 0.18623  211 TYR A CE1   
1812 C CE2   . TYR B 211 ? 2.16992 2.26923 1.85423 -0.26322 -0.10335 0.21569  211 TYR A CE2   
1813 C CZ    . TYR B 211 ? 2.26178 2.35860 1.96198 -0.25246 -0.09326 0.20264  211 TYR A CZ    
1814 O OH    . TYR B 211 ? 2.09987 2.19336 1.83126 -0.24361 -0.09138 0.20603  211 TYR A OH    
1815 N N     . GLU B 212 ? 1.88930 1.99891 1.49947 -0.26789 -0.06209 0.18114  212 GLU A N     
1816 C CA    . GLU B 212 ? 1.93085 2.04227 1.55979 -0.26282 -0.05536 0.18691  212 GLU A CA    
1817 C C     . GLU B 212 ? 1.70051 1.81329 1.33346 -0.25478 -0.03897 0.17212  212 GLU A C     
1818 O O     . GLU B 212 ? 1.69398 1.80627 1.31648 -0.25308 -0.03352 0.15833  212 GLU A O     
1819 C CB    . GLU B 212 ? 2.01439 2.12153 1.67486 -0.25744 -0.06448 0.19651  212 GLU A CB    
1820 C CG    . GLU B 212 ? 2.14547 2.25310 1.82187 -0.25593 -0.06275 0.20755  212 GLU A CG    
1821 C CD    . GLU B 212 ? 2.19148 2.29378 1.89887 -0.25063 -0.07087 0.21666  212 GLU A CD    
1822 O OE1   . GLU B 212 ? 2.24056 2.34156 1.95180 -0.25496 -0.08429 0.22696  212 GLU A OE1   
1823 O OE2   . GLU B 212 ? 2.01884 2.11796 1.74656 -0.24237 -0.06371 0.21353  212 GLU A OE2   
1824 N N     . LYS B 213 ? 1.57041 1.68460 1.21803 -0.25048 -0.03190 0.17526  213 LYS A N     
1825 C CA    . LYS B 213 ? 1.49541 1.61090 1.15013 -0.24286 -0.01756 0.16279  213 LYS A CA    
1826 C C     . LYS B 213 ? 1.53471 1.64582 1.21928 -0.23445 -0.01774 0.16546  213 LYS A C     
1827 O O     . LYS B 213 ? 1.62719 1.73648 1.32277 -0.23607 -0.02445 0.17839  213 LYS A O     
1828 C CB    . LYS B 213 ? 1.54757 1.66953 1.18694 -0.24706 -0.00696 0.16283  213 LYS A CB    
1829 C CG    . LYS B 213 ? 1.45084 1.57490 1.09383 -0.25160 -0.01015 0.17810  213 LYS A CG    
1830 C CD    . LYS B 213 ? 1.50632 1.63754 1.13182 -0.25689 0.00017  0.17867  213 LYS A CD    
1831 C CE    . LYS B 213 ? 1.61820 1.75218 1.25268 -0.25029 0.01424  0.16821  213 LYS A CE    
1832 N NZ    . LYS B 213 ? 1.75336 1.88466 1.41372 -0.24463 0.01376  0.17310  213 LYS A NZ    
1833 N N     . PHE B 214 ? 1.49585 1.60478 1.19256 -0.22606 -0.01058 0.15372  214 PHE A N     
1834 C CA    . PHE B 214 ? 1.42110 1.52477 1.14368 -0.21820 -0.00972 0.15491  214 PHE A CA    
1835 C C     . PHE B 214 ? 1.52133 1.62754 1.24704 -0.21706 -0.00031 0.15484  214 PHE A C     
1836 O O     . PHE B 214 ? 1.65507 1.76547 1.37389 -0.21557 0.00971  0.14503  214 PHE A O     
1837 C CB    . PHE B 214 ? 1.30064 1.40037 1.03461 -0.21025 -0.00733 0.14342  214 PHE A CB    
1838 C CG    . PHE B 214 ? 1.25378 1.34726 1.01153 -0.20250 -0.00559 0.14374  214 PHE A CG    
1839 C CD1   . PHE B 214 ? 1.27033 1.35751 1.04467 -0.20001 -0.01361 0.15079  214 PHE A CD1   
1840 C CD2   . PHE B 214 ? 1.64010 1.73367 1.40345 -0.19800 0.00416  0.13714  214 PHE A CD2   
1841 C CE1   . PHE B 214 ? 1.24866 1.32901 1.04273 -0.19314 -0.01089 0.15035  214 PHE A CE1   
1842 C CE2   . PHE B 214 ? 1.68719 1.77388 1.46933 -0.19175 0.00550  0.13714  214 PHE A CE2   
1843 C CZ    . PHE B 214 ? 1.66162 1.74134 1.45815 -0.18928 -0.00150 0.14328  214 PHE A CZ    
1844 N N     . GLU B 215 ? 1.44865 1.55222 1.18579 -0.21780 -0.00360 0.16571  215 GLU A N     
1845 C CA    . GLU B 215 ? 1.56918 1.67466 1.31041 -0.21748 0.00402  0.16694  215 GLU A CA    
1846 C C     . GLU B 215 ? 1.73018 1.84484 1.45137 -0.22283 0.01167  0.16401  215 GLU A C     
1847 O O     . GLU B 215 ? 1.79869 1.91730 1.50368 -0.23041 0.00778  0.17111  215 GLU A O     
1848 C CB    . GLU B 215 ? 1.52732 1.62822 1.28430 -0.20918 0.01031  0.15779  215 GLU A CB    
1849 C CG    . GLU B 215 ? 1.57101 1.66206 1.34703 -0.20373 0.00456  0.16013  215 GLU A CG    
1850 C CD    . GLU B 215 ? 1.78664 1.87228 1.57448 -0.20500 0.00040  0.17154  215 GLU A CD    
1851 O OE1   . GLU B 215 ? 1.72024 1.80998 1.50233 -0.21032 0.00142  0.17841  215 GLU A OE1   
1852 O OE2   . GLU B 215 ? 1.93275 2.00973 1.73625 -0.20059 -0.00346 0.17354  215 GLU A OE2   
1853 N N     . GLN B 216 ? 1.51266 1.63046 1.23520 -0.21920 0.02226  0.15429  216 GLN A N     
1854 C CA    . GLN B 216 ? 1.46996 1.59659 1.17556 -0.22343 0.03151  0.15051  216 GLN A CA    
1855 C C     . GLN B 216 ? 1.66901 1.79695 1.36557 -0.22071 0.03646  0.13677  216 GLN A C     
1856 O O     . GLN B 216 ? 1.77218 1.90502 1.46712 -0.21884 0.04730  0.12848  216 GLN A O     
1857 C CB    . GLN B 216 ? 1.77539 1.90561 1.49043 -0.22214 0.03999  0.15101  216 GLN A CB    
1858 C CG    . GLN B 216 ? 1.90904 2.04878 1.60907 -0.22799 0.04868  0.15240  216 GLN A CG    
1859 C CD    . GLN B 216 ? 1.96183 2.10398 1.64472 -0.23662 0.04325  0.16328  216 GLN A CD    
1860 O OE1   . GLN B 216 ? 1.93567 2.08189 1.59746 -0.24128 0.04614  0.16039  216 GLN A OE1   
1861 N NE2   . GLN B 216 ? 1.77086 1.90993 1.46223 -0.23913 0.03520  0.17601  216 GLN A NE2   
1862 N N     . ILE B 217 ? 1.77506 1.89864 1.46777 -0.22044 0.02865  0.13472  217 ILE A N     
1863 C CA    . ILE B 217 ? 1.61214 1.73616 1.29522 -0.21860 0.03240  0.12175  217 ILE A CA    
1864 C C     . ILE B 217 ? 1.35253 1.47575 1.01613 -0.22556 0.02400  0.12492  217 ILE A C     
1865 O O     . ILE B 217 ? 1.44346 1.56303 1.11179 -0.22775 0.01254  0.13520  217 ILE A O     
1866 C CB    . ILE B 217 ? 1.37277 1.49111 1.07422 -0.21006 0.03111  0.11409  217 ILE A CB    
1867 C CG1   . ILE B 217 ? 1.32836 1.44561 1.04932 -0.20418 0.03621  0.11379  217 ILE A CG1   
1868 C CG2   . ILE B 217 ? 1.32482 1.44386 1.01851 -0.20787 0.03605  0.10048  217 ILE A CG2   
1869 C CD1   . ILE B 217 ? 1.63341 1.74451 1.37128 -0.19629 0.03486  0.10733  217 ILE A CD1   
1870 N N     . ILE B 218 ? 1.37101 1.49697 1.01401 -0.22901 0.02937  0.11643  218 ILE A N     
1871 C CA    . ILE B 218 ? 1.50395 1.62793 1.12606 -0.23641 0.02034  0.11865  218 ILE A CA    
1872 C C     . ILE B 218 ? 1.62786 1.74731 1.25111 -0.23240 0.01858  0.10661  218 ILE A C     
1873 O O     . ILE B 218 ? 1.74360 1.86379 1.37394 -0.22616 0.02860  0.09483  218 ILE A O     
1874 C CB    . ILE B 218 ? 1.73197 1.86087 1.32577 -0.24495 0.02669  0.11869  218 ILE A CB    
1875 C CG1   . ILE B 218 ? 1.95017 2.08099 1.53380 -0.24268 0.04041  0.10293  218 ILE A CG1   
1876 C CG2   . ILE B 218 ? 1.46652 1.60069 1.06199 -0.24815 0.03010  0.13020  218 ILE A CG2   
1877 C CD1   . ILE B 218 ? 1.93500 2.06736 1.48584 -0.25159 0.04467  0.09997  218 ILE A CD1   
1878 N N     . TYR B 219 ? 1.47586 1.59097 1.09386 -0.23596 0.00599  0.10995  219 TYR A N     
1879 C CA    . TYR B 219 ? 1.43919 1.54969 1.06181 -0.23182 0.00334  0.09932  219 TYR A CA    
1880 C C     . TYR B 219 ? 1.69858 1.80597 1.30026 -0.23997 -0.00720 0.10003  219 TYR A C     
1881 O O     . TYR B 219 ? 1.79182 1.89918 1.38624 -0.24703 -0.01789 0.11280  219 TYR A O     
1882 C CB    . TYR B 219 ? 1.44826 1.55509 1.10039 -0.22404 -0.00258 0.10318  219 TYR A CB    
1883 C CG    . TYR B 219 ? 1.38903 1.49385 1.05003 -0.22703 -0.01565 0.11869  219 TYR A CG    
1884 C CD1   . TYR B 219 ? 1.41000 1.51127 1.07056 -0.23031 -0.02880 0.12306  219 TYR A CD1   
1885 C CD2   . TYR B 219 ? 1.42397 1.53023 1.09547 -0.22657 -0.01505 0.12925  219 TYR A CD2   
1886 C CE1   . TYR B 219 ? 1.41180 1.51156 1.08315 -0.23283 -0.04064 0.13789  219 TYR A CE1   
1887 C CE2   . TYR B 219 ? 1.50106 1.60509 1.18259 -0.22897 -0.02648 0.14342  219 TYR A CE2   
1888 C CZ    . TYR B 219 ? 1.41205 1.51307 1.09416 -0.23195 -0.03915 0.14796  219 TYR A CZ    
1889 O OH    . TYR B 219 ? 1.72995 1.82910 1.42451 -0.23413 -0.05036 0.16262  219 TYR A OH    
1890 N N     . ARG B 220 ? 1.74844 1.85284 1.34135 -0.23928 -0.00501 0.08697  220 ARG A N     
1891 C CA    . ARG B 220 ? 1.53018 1.63029 1.10281 -0.24737 -0.01607 0.08651  220 ARG A CA    
1892 C C     . ARG B 220 ? 1.50528 1.60176 1.09816 -0.24561 -0.03133 0.09488  220 ARG A C     
1893 O O     . ARG B 220 ? 1.61294 1.70685 1.22545 -0.23788 -0.03076 0.08809  220 ARG A O     
1894 C CB    . ARG B 220 ? 1.66334 1.76023 1.22228 -0.24683 -0.00906 0.06937  220 ARG A CB    
1895 C CG    . ARG B 220 ? 1.92487 2.01615 1.46111 -0.25579 -0.02061 0.06778  220 ARG A CG    
1896 C CD    . ARG B 220 ? 1.90646 1.99378 1.42634 -0.25583 -0.01173 0.04989  220 ARG A CD    
1897 N NE    . ARG B 220 ? 2.10964 2.20039 1.61197 -0.25699 0.00480  0.04292  220 ARG A NE    
1898 C CZ    . ARG B 220 ? 2.03064 2.11860 1.51769 -0.25696 0.01622  0.02730  220 ARG A CZ    
1899 N NH1   . ARG B 220 ? 1.90225 1.98328 1.38685 -0.25667 0.01197  0.01682  220 ARG A NH1   
1900 N NH2   . ARG B 220 ? 2.03281 2.12478 1.50837 -0.25713 0.03213  0.02235  220 ARG A NH2   
1901 N N     . LYS B 221 ? 1.54318 1.63970 1.13256 -0.25253 -0.04419 0.10961  221 LYS A N     
1902 C CA    . LYS B 221 ? 1.64227 1.73586 1.25366 -0.25097 -0.05874 0.11933  221 LYS A CA    
1903 C C     . LYS B 221 ? 1.78562 1.87458 1.39867 -0.24941 -0.06318 0.10914  221 LYS A C     
1904 O O     . LYS B 221 ? 1.61384 1.70049 1.20051 -0.25660 -0.06489 0.10193  221 LYS A O     
1905 C CB    . LYS B 221 ? 1.70058 1.79460 1.30145 -0.26114 -0.07314 0.13540  221 LYS A CB    
1906 C CG    . LYS B 221 ? 1.87414 1.96581 1.49910 -0.26025 -0.08852 0.14738  221 LYS A CG    
1907 C CD    . LYS B 221 ? 1.89732 1.98963 1.51094 -0.27129 -0.10371 0.16364  221 LYS A CD    
1908 C CE    . LYS B 221 ? 1.86342 1.95422 1.50568 -0.26961 -0.11786 0.17704  221 LYS A CE    
1909 N NZ    . LYS B 221 ? 1.97459 2.06659 1.60804 -0.28025 -0.13258 0.19409  221 LYS A NZ    
1910 N N     . GLN B 222 ? 1.69797 1.78513 1.34033 -0.24067 -0.06477 0.10855  222 GLN A N     
1911 C CA    . GLN B 222 ? 1.66312 1.74614 1.31040 -0.23846 -0.06850 0.09905  222 GLN A CA    
1912 C C     . GLN B 222 ? 1.73432 1.81446 1.37181 -0.24791 -0.08610 0.10669  222 GLN A C     
1913 O O     . GLN B 222 ? 1.73843 1.81926 1.39083 -0.24952 -0.09744 0.12173  222 GLN A O     
1914 C CB    . GLN B 222 ? 1.68169 1.76381 1.36313 -0.22724 -0.06603 0.09847  222 GLN A CB    
1915 C CG    . GLN B 222 ? 1.64421 1.72784 1.33294 -0.21839 -0.04955 0.08733  222 GLN A CG    
1916 C CD    . GLN B 222 ? 1.55428 1.63634 1.27414 -0.20810 -0.04734 0.08700  222 GLN A CD    
1917 O OE1   . GLN B 222 ? 1.47712 1.55896 1.21609 -0.20495 -0.05056 0.09764  222 GLN A OE1   
1918 N NE2   . GLN B 222 ? 1.40241 1.48290 1.12743 -0.20283 -0.04136 0.07469  222 GLN A NE2   
1919 N N     . VAL B 223 ? 1.70314 1.77973 1.31708 -0.25404 -0.08837 0.09673  223 VAL A N     
1920 C CA    . VAL B 223 ? 1.64914 1.72210 1.25133 -0.26419 -0.10631 0.10316  223 VAL A CA    
1921 C C     . VAL B 223 ? 1.65093 1.72199 1.28454 -0.25879 -0.11596 0.10676  223 VAL A C     
1922 O O     . VAL B 223 ? 1.72167 1.79071 1.36650 -0.25158 -0.10920 0.09473  223 VAL A O     
1923 C CB    . VAL B 223 ? 1.57656 1.64474 1.14386 -0.27209 -0.10503 0.08971  223 VAL A CB    
1924 C CG1   . VAL B 223 ? 1.81828 1.88174 1.37257 -0.28310 -0.12437 0.09564  223 VAL A CG1   
1925 C CG2   . VAL B 223 ? 1.57578 1.64594 1.11252 -0.27705 -0.09362 0.08581  223 VAL A CG2   
1926 N N     . ASP B 224 ? 1.69613 1.76800 1.34432 -0.26223 -0.13097 0.12313  224 ASP A N     
1927 C CA    . ASP B 224 ? 1.65427 1.72505 1.33606 -0.25663 -0.13948 0.12828  224 ASP A CA    
1928 C C     . ASP B 224 ? 1.71442 1.78039 1.38695 -0.26229 -0.14988 0.12162  224 ASP A C     
1929 O O     . ASP B 224 ? 1.69957 1.76230 1.33889 -0.26970 -0.14864 0.11140  224 ASP A O     
1930 C CB    . ASP B 224 ? 1.64684 1.72017 1.35061 -0.25772 -0.15097 0.14804  224 ASP A CB    
1931 C CG    . ASP B 224 ? 1.82071 1.89734 1.54274 -0.24964 -0.14043 0.15387  224 ASP A CG    
1932 O OD1   . ASP B 224 ? 2.04073 2.11812 1.75768 -0.24344 -0.12443 0.14279  224 ASP A OD1   
1933 O OD2   . ASP B 224 ? 1.81841 1.89649 1.56035 -0.24976 -0.14855 0.16955  224 ASP A OD2   
1934 N N     . PHE B 225 ? 1.77850 1.84363 1.47958 -0.25900 -0.15938 0.12710  225 PHE A N     
1935 C CA    . PHE B 225 ? 1.74688 1.80720 1.44306 -0.26389 -0.16980 0.12089  225 PHE A CA    
1936 C C     . PHE B 225 ? 1.78052 1.84066 1.48489 -0.27253 -0.19134 0.13730  225 PHE A C     
1937 O O     . PHE B 225 ? 1.92452 1.98870 1.65077 -0.27084 -0.19643 0.15332  225 PHE A O     
1938 C CB    . PHE B 225 ? 1.75369 1.81334 1.47831 -0.25249 -0.16227 0.11248  225 PHE A CB    
1939 C CG    . PHE B 225 ? 1.80297 1.85998 1.51271 -0.24817 -0.14712 0.09262  225 PHE A CG    
1940 C CD1   . PHE B 225 ? 1.73599 1.78890 1.40876 -0.25656 -0.14603 0.08148  225 PHE A CD1   
1941 C CD2   . PHE B 225 ? 1.69348 1.75179 1.42638 -0.23591 -0.13383 0.08537  225 PHE A CD2   
1942 C CE1   . PHE B 225 ? 1.62583 1.67624 1.28769 -0.25223 -0.13169 0.06363  225 PHE A CE1   
1943 C CE2   . PHE B 225 ? 1.77313 1.82934 1.49466 -0.23208 -0.12065 0.06828  225 PHE A CE2   
1944 C CZ    . PHE B 225 ? 1.87692 1.92931 1.56418 -0.23997 -0.11943 0.05747  225 PHE A CZ    
1945 N N     . LYS B 226 ? 1.73742 1.79261 1.42554 -0.28174 -0.20402 0.13359  226 LYS A N     
1946 C CA    . LYS B 226 ? 1.90160 1.95645 1.59867 -0.29083 -0.22654 0.14955  226 LYS A CA    
1947 C C     . LYS B 226 ? 2.04464 2.09787 1.77133 -0.28625 -0.23287 0.14804  226 LYS A C     
1948 O O     . LYS B 226 ? 2.03612 2.08958 1.77957 -0.27485 -0.21868 0.13716  226 LYS A O     
1949 C CB    . LYS B 226 ? 1.91384 1.96381 1.56800 -0.30674 -0.23850 0.14848  226 LYS A CB    
1950 C CG    . LYS B 226 ? 2.00304 2.05456 1.65813 -0.31793 -0.26001 0.16903  226 LYS A CG    
1951 C CD    . LYS B 226 ? 1.97362 2.03182 1.64172 -0.31502 -0.25707 0.18422  226 LYS A CD    
1952 C CE    . LYS B 226 ? 1.93780 1.99663 1.57425 -0.31587 -0.24216 0.17668  226 LYS A CE    
1953 N NZ    . LYS B 226 ? 1.99834 2.05228 1.58812 -0.33056 -0.24943 0.17279  226 LYS A NZ    
1954 N N     . LYS B 227 ? 1.96269 2.01448 1.69586 -0.29513 -0.25366 0.15907  227 LYS A N     
1955 C CA    . LYS B 227 ? 2.02421 2.07485 1.78732 -0.29165 -0.26117 0.15923  227 LYS A CA    
1956 C C     . LYS B 227 ? 2.16510 2.20867 1.90350 -0.30483 -0.27767 0.15446  227 LYS A C     
1957 O O     . LYS B 227 ? 2.09543 2.13933 1.84705 -0.31250 -0.29798 0.16882  227 LYS A O     
1958 C CB    . LYS B 227 ? 1.93102 1.98748 1.73700 -0.28811 -0.27097 0.17981  227 LYS A CB    
1959 C CG    . LYS B 227 ? 1.88677 1.94499 1.68619 -0.29998 -0.28967 0.19846  227 LYS A CG    
1960 C CD    . LYS B 227 ? 1.91951 1.98442 1.75644 -0.29319 -0.28960 0.21678  227 LYS A CD    
1961 C CE    . LYS B 227 ? 1.98187 2.04875 1.81468 -0.30501 -0.30883 0.23616  227 LYS A CE    
1962 N NZ    . LYS B 227 ? 2.02441 2.08822 1.80828 -0.31655 -0.31100 0.23155  227 LYS A NZ    
1963 N N     . PRO B 228 ? 2.25046 2.28724 1.95476 -0.30791 -0.27010 0.13511  228 PRO A N     
1964 C CA    . PRO B 228 ? 2.31589 2.34424 1.99260 -0.32116 -0.28513 0.12927  228 PRO A CA    
1965 C C     . PRO B 228 ? 2.34949 2.37440 2.04883 -0.31795 -0.28994 0.12296  228 PRO A C     
1966 O O     . PRO B 228 ? 2.38005 2.40140 2.07528 -0.31115 -0.27551 0.10512  228 PRO A O     
1967 C CB    . PRO B 228 ? 2.25053 2.27312 1.88136 -0.32440 -0.27107 0.11077  228 PRO A CB    
1968 C CG    . PRO B 228 ? 2.09609 2.12538 1.73700 -0.31157 -0.24895 0.10785  228 PRO A CG    
1969 C CD    . PRO B 228 ? 2.12289 2.15929 1.81418 -0.29917 -0.24712 0.11826  228 PRO A CD    
1970 N N     . THR B 229 ? 2.23533 2.26150 1.95942 -0.32278 -0.30985 0.13780  229 THR A N     
1971 C CA    . THR B 229 ? 2.10855 2.13161 1.85569 -0.32089 -0.31650 0.13349  229 THR A CA    
1972 C C     . THR B 229 ? 2.30185 2.32195 2.04920 -0.33498 -0.34368 0.14635  229 THR A C     
1973 O O     . THR B 229 ? 2.36128 2.38726 2.12407 -0.33873 -0.35613 0.16643  229 THR A O     
1974 C CB    . THR B 229 ? 2.04633 2.07725 1.84360 -0.30519 -0.30618 0.13918  229 THR A CB    
1975 O OG1   . THR B 229 ? 2.08091 2.10957 1.90159 -0.30644 -0.31804 0.14029  229 THR A OG1   
1976 C CG2   . THR B 229 ? 2.02047 2.06023 1.84566 -0.30174 -0.30940 0.15997  229 THR A CG2   
1977 N N     . THR B 230 ? 2.42031 2.43129 2.15178 -0.34287 -0.35315 0.13559  230 THR A N     
1978 C CA    . THR B 230 ? 2.32886 2.33614 2.06076 -0.35721 -0.38074 0.14745  230 THR A CA    
1979 C C     . THR B 230 ? 2.16853 2.17696 1.94231 -0.35177 -0.38670 0.14959  230 THR A C     
1980 O O     . THR B 230 ? 2.16877 2.17185 1.94037 -0.34653 -0.37630 0.13203  230 THR A O     
1981 C CB    . THR B 230 ? 2.25760 2.25216 1.93515 -0.37293 -0.38960 0.13464  230 THR A CB    
1982 O OG1   . THR B 230 ? 2.16398 2.15058 1.83793 -0.36978 -0.38259 0.11516  230 THR A OG1   
1983 C CG2   . THR B 230 ? 2.19757 2.19035 1.83153 -0.37554 -0.37649 0.12690  230 THR A CG2   
1984 N N     . ASN B 231 ? 2.02541 2.04076 1.83757 -0.35290 -0.40269 0.17087  231 ASN A N     
1985 C CA    . ASN B 231 ? 2.02292 2.04029 1.87875 -0.34809 -0.40935 0.17526  231 ASN A CA    
1986 C C     . ASN B 231 ? 2.14704 2.15245 1.97829 -0.35808 -0.41955 0.16048  231 ASN A C     
1987 O O     . ASN B 231 ? 2.40442 2.40220 2.20143 -0.37441 -0.43787 0.16163  231 ASN A O     
1988 C CB    . ASN B 231 ? 2.06892 2.09437 1.96430 -0.35125 -0.42840 0.20124  231 ASN A CB    
1989 C CG    . ASN B 231 ? 2.12858 2.15895 2.07631 -0.34262 -0.42972 0.20752  231 ASN A CG    
1990 O OD1   . ASN B 231 ? 2.20531 2.22966 2.15279 -0.34353 -0.43144 0.19577  231 ASN A OD1   
1991 N ND2   . ASN B 231 ? 2.03494 2.07584 2.02815 -0.33427 -0.42852 0.22585  231 ASN A ND2   
1992 N N     . TYR B 232 ? 2.10411 2.10723 1.94975 -0.34879 -0.40734 0.14639  232 TYR A N     
1993 C CA    . TYR B 232 ? 2.12568 2.11664 1.95107 -0.35733 -0.41599 0.13134  232 TYR A CA    
1994 C C     . TYR B 232 ? 2.25263 2.24259 2.09656 -0.36926 -0.44446 0.14701  232 TYR A C     
1995 O O     . TYR B 232 ? 2.19159 2.17007 2.01224 -0.38139 -0.45868 0.13822  232 TYR A O     
1996 C CB    . TYR B 232 ? 1.96425 1.95510 1.81215 -0.34368 -0.39819 0.11723  232 TYR A CB    
1997 C CG    . TYR B 232 ? 2.01425 1.99214 1.84306 -0.35074 -0.40411 0.09998  232 TYR A CG    
1998 C CD1   . TYR B 232 ? 2.07867 2.04431 1.85511 -0.35890 -0.40039 0.08110  232 TYR A CD1   
1999 C CD2   . TYR B 232 ? 2.09919 2.07669 1.96274 -0.34942 -0.41316 0.10268  232 TYR A CD2   
2000 C CE1   . TYR B 232 ? 2.11032 2.06288 1.86911 -0.36541 -0.40537 0.06470  232 TYR A CE1   
2001 C CE2   . TYR B 232 ? 2.12272 2.08768 1.96956 -0.35616 -0.41912 0.08702  232 TYR A CE2   
2002 C CZ    . TYR B 232 ? 2.15408 2.10612 1.94822 -0.36412 -0.41516 0.06763  232 TYR A CZ    
2003 O OH    . TYR B 232 ? 2.08685 2.02527 1.86400 -0.37074 -0.42035 0.05130  232 TYR A OH    
2004 N N     . ASN B 233 ? 2.25166 2.25299 2.13744 -0.36609 -0.45278 0.16985  233 ASN A N     
2005 C CA    . ASN B 233 ? 2.16467 2.16682 2.07663 -0.37641 -0.48017 0.18721  233 ASN A CA    
2006 C C     . ASN B 233 ? 2.23121 2.22705 2.15655 -0.37573 -0.48281 0.17599  233 ASN A C     
2007 O O     . ASN B 233 ? 2.26565 2.25336 2.18011 -0.39028 -0.50569 0.17739  233 ASN A O     
2008 C CB    . ASN B 233 ? 2.28128 2.27708 2.15620 -0.39597 -0.50403 0.19479  233 ASN A CB    
2009 C CG    . ASN B 233 ? 2.21239 2.21222 2.06332 -0.39633 -0.49686 0.20006  233 ASN A CG    
2010 O OD1   . ASN B 233 ? 2.23627 2.24780 2.12037 -0.38844 -0.49325 0.21705  233 ASN A OD1   
2011 N ND2   . ASN B 233 ? 2.30681 2.29687 2.10107 -0.40522 -0.49398 0.18565  233 ASN A ND2   
2012 N N     . GLY B 234 ? 2.24335 2.24241 2.19073 -0.35989 -0.46062 0.16544  234 GLY A N     
2013 C CA    . GLY B 234 ? 2.14271 2.13639 2.10566 -0.35786 -0.46112 0.15481  234 GLY A CA    
2014 C C     . GLY B 234 ? 1.95228 1.95355 1.95011 -0.33877 -0.43681 0.15018  234 GLY A C     
2015 O O     . GLY B 234 ? 1.94786 1.95737 1.95294 -0.32783 -0.41948 0.15369  234 GLY A O     
2016 N N     . SER B 235 ? 1.95295 1.95122 1.97141 -0.33531 -0.43597 0.14288  235 SER A N     
2017 C CA    . SER B 235 ? 2.02031 2.02506 2.07067 -0.31770 -0.41300 0.13792  235 SER A CA    
2018 C C     . SER B 235 ? 1.98284 1.97987 1.99831 -0.31248 -0.39266 0.11331  235 SER A C     
2019 O O     . SER B 235 ? 1.98816 1.97370 1.95850 -0.32332 -0.39836 0.09971  235 SER A O     
2020 C CB    . SER B 235 ? 2.15622 2.16269 2.24889 -0.31594 -0.42123 0.14381  235 SER A CB    
2021 O OG    . SER B 235 ? 2.11180 2.10546 2.18230 -0.32586 -0.43200 0.12944  235 SER A OG    
2022 N N     . LEU B 236 ? 1.82682 1.82960 1.86275 -0.29683 -0.37000 0.10805  236 LEU A N     
2023 C CA    . LEU B 236 ? 1.92783 1.92471 1.93405 -0.29081 -0.34949 0.08609  236 LEU A CA    
2024 C C     . LEU B 236 ? 1.92215 1.90721 1.91653 -0.29613 -0.35429 0.06967  236 LEU A C     
2025 O O     . LEU B 236 ? 1.88903 1.86540 1.84719 -0.29714 -0.34410 0.05056  236 LEU A O     
2026 C CB    . LEU B 236 ? 1.92643 1.93243 1.95832 -0.27342 -0.32549 0.08596  236 LEU A CB    
2027 C CG    . LEU B 236 ? 2.09892 2.10781 2.17090 -0.26423 -0.31975 0.08613  236 LEU A CG    
2028 C CD1   . LEU B 236 ? 1.76026 1.77479 1.84172 -0.24878 -0.29410 0.08032  236 LEU A CD1   
2029 C CD2   . LEU B 236 ? 2.14838 2.16502 2.26517 -0.26455 -0.33335 0.10707  236 LEU A CD2   
2030 N N     . LYS B 237 ? 1.98976 1.97442 2.01467 -0.29924 -0.36872 0.07690  237 LYS A N     
2031 C CA    . LYS B 237 ? 2.03818 2.01030 2.05130 -0.30564 -0.37533 0.06148  237 LYS A CA    
2032 C C     . LYS B 237 ? 1.96750 1.92647 1.92759 -0.32088 -0.38671 0.05040  237 LYS A C     
2033 O O     . LYS B 237 ? 1.92985 1.87771 1.85900 -0.32210 -0.37788 0.02953  237 LYS A O     
2034 C CB    . LYS B 237 ? 1.98358 1.95753 2.03679 -0.30939 -0.39355 0.07430  237 LYS A CB    
2035 C CG    . LYS B 237 ? 2.02881 2.01795 2.13499 -0.29724 -0.38716 0.09285  237 LYS A CG    
2036 C CD    . LYS B 237 ? 2.06667 2.06593 2.17904 -0.29642 -0.38894 0.11048  237 LYS A CD    
2037 C CE    . LYS B 237 ? 2.02310 2.03607 2.18567 -0.28331 -0.37909 0.12648  237 LYS A CE    
2038 N NZ    . LYS B 237 ? 2.07105 2.09269 2.23734 -0.28108 -0.37721 0.14095  237 LYS A NZ    
2039 N N     . SER B 238 ? 1.94548 1.90571 1.89600 -0.33203 -0.40515 0.06439  238 SER A N     
2040 C CA    . SER B 238 ? 1.93040 1.87808 1.82832 -0.34790 -0.41735 0.05573  238 SER A CA    
2041 C C     . SER B 238 ? 1.91805 1.86376 1.77745 -0.34312 -0.39594 0.04115  238 SER A C     
2042 O O     . SER B 238 ? 1.89082 1.82307 1.70784 -0.35031 -0.39378 0.02234  238 SER A O     
2043 C CB    . SER B 238 ? 2.02731 1.97900 1.92641 -0.35929 -0.43976 0.07610  238 SER A CB    
2044 O OG    . SER B 238 ? 2.22137 2.18166 2.17143 -0.35771 -0.45312 0.09501  238 SER A OG    
2045 N N     . LEU B 239 ? 2.00933 1.96770 1.88394 -0.33145 -0.38051 0.04964  239 LEU A N     
2046 C CA    . LEU B 239 ? 1.91068 1.86875 1.75235 -0.32638 -0.35998 0.03773  239 LEU A CA    
2047 C C     . LEU B 239 ? 1.92917 1.87985 1.76095 -0.31927 -0.34177 0.01516  239 LEU A C     
2048 O O     . LEU B 239 ? 1.90857 1.84961 1.69750 -0.32408 -0.33464 -0.00138 239 LEU A O     
2049 C CB    . LEU B 239 ? 1.83814 1.81136 1.70746 -0.31390 -0.34742 0.05196  239 LEU A CB    
2050 C CG    . LEU B 239 ? 1.88738 1.86292 1.73091 -0.30718 -0.32607 0.04321  239 LEU A CG    
2051 C CD1   . LEU B 239 ? 2.04612 2.01497 1.84140 -0.32045 -0.33375 0.04046  239 LEU A CD1   
2052 C CD2   . LEU B 239 ? 1.89626 1.88593 1.77225 -0.29531 -0.31615 0.05858  239 LEU A CD2   
2053 N N     . TYR B 240 ? 1.95097 1.90594 1.82174 -0.30843 -0.33456 0.01503  240 TYR A N     
2054 C CA    . TYR B 240 ? 1.76510 1.71379 1.63170 -0.30094 -0.31746 -0.00505 240 TYR A CA    
2055 C C     . TYR B 240 ? 1.85517 1.78698 1.68781 -0.31386 -0.32808 -0.02100 240 TYR A C     
2056 O O     . TYR B 240 ? 1.85714 1.78018 1.65812 -0.31358 -0.31477 -0.04019 240 TYR A O     
2057 C CB    . TYR B 240 ? 1.69249 1.64798 1.60834 -0.28981 -0.31311 0.00038  240 TYR A CB    
2058 C CG    . TYR B 240 ? 1.74211 1.69156 1.65981 -0.28239 -0.29796 -0.01798 240 TYR A CG    
2059 C CD1   . TYR B 240 ? 1.75155 1.70683 1.67348 -0.26914 -0.27449 -0.02442 240 TYR A CD1   
2060 C CD2   . TYR B 240 ? 1.80553 1.74327 1.72206 -0.28890 -0.30777 -0.02830 240 TYR A CD2   
2061 C CE1   . TYR B 240 ? 1.73190 1.68210 1.65750 -0.26250 -0.26128 -0.04000 240 TYR A CE1   
2062 C CE2   . TYR B 240 ? 1.83091 1.76301 1.75111 -0.28210 -0.29418 -0.04448 240 TYR A CE2   
2063 C CZ    . TYR B 240 ? 1.75084 1.68950 1.67613 -0.26877 -0.27088 -0.05002 240 TYR A CZ    
2064 O OH    . TYR B 240 ? 1.79945 1.73289 1.73006 -0.26222 -0.25809 -0.06496 240 TYR A OH    
2065 N N     . ARG B 241 ? 1.96420 1.89115 1.80321 -0.32538 -0.35185 -0.01303 241 ARG A N     
2066 C CA    . ARG B 241 ? 2.03420 1.94336 1.83998 -0.33930 -0.36450 -0.02791 241 ARG A CA    
2067 C C     . ARG B 241 ? 2.12989 2.03093 1.88040 -0.34863 -0.36224 -0.03742 241 ARG A C     
2068 O O     . ARG B 241 ? 2.16870 2.05701 1.88656 -0.35077 -0.35226 -0.05864 241 ARG A O     
2069 C CB    . ARG B 241 ? 1.95234 1.85956 1.77578 -0.35090 -0.39257 -0.01373 241 ARG A CB    
2070 C CG    . ARG B 241 ? 2.28615 2.17784 2.10376 -0.35985 -0.40498 -0.02632 241 ARG A CG    
2071 C CD    . ARG B 241 ? 2.55299 2.43709 2.36023 -0.37796 -0.43520 -0.01698 241 ARG A CD    
2072 N NE    . ARG B 241 ? 2.62412 2.49543 2.37354 -0.39248 -0.44209 -0.02628 241 ARG A NE    
2073 C CZ    . ARG B 241 ? 2.58106 2.43482 2.28905 -0.39872 -0.43698 -0.04944 241 ARG A CZ    
2074 N NH1   . ARG B 241 ? 2.54924 2.39574 2.26887 -0.39243 -0.42709 -0.06513 241 ARG A NH1   
2075 N NH2   . ARG B 241 ? 2.51683 2.36011 2.17200 -0.41123 -0.44123 -0.05674 241 ARG A NH2   
2076 N N     . LYS B 242 ? 2.11805 2.02647 1.85979 -0.35348 -0.37006 -0.02200 242 LYS A N     
2077 C CA    . LYS B 242 ? 2.18689 2.08788 1.87520 -0.36368 -0.36949 -0.02908 242 LYS A CA    
2078 C C     . LYS B 242 ? 2.11279 2.01333 1.78209 -0.35328 -0.34135 -0.04639 242 LYS A C     
2079 O O     . LYS B 242 ? 2.15875 2.04608 1.78375 -0.36047 -0.33616 -0.06416 242 LYS A O     
2080 C CB    . LYS B 242 ? 2.12147 2.03323 1.81038 -0.36776 -0.37949 -0.00780 242 LYS A CB    
2081 C CG    . LYS B 242 ? 2.08581 1.99023 1.72023 -0.37976 -0.38144 -0.01264 242 LYS A CG    
2082 C CD    . LYS B 242 ? 2.18095 2.06744 1.77755 -0.39808 -0.40066 -0.02185 242 LYS A CD    
2083 C CE    . LYS B 242 ? 2.31772 2.19116 1.85755 -0.40447 -0.38896 -0.04205 242 LYS A CE    
2084 N NZ    . LYS B 242 ? 2.26946 2.13925 1.81048 -0.39219 -0.36390 -0.06295 242 LYS A NZ    
2085 N N     . ALA B 243 ? 2.00131 1.91551 1.70336 -0.33718 -0.32390 -0.04113 243 ALA A N     
2086 C CA    . ALA B 243 ? 1.97551 1.89089 1.66365 -0.32679 -0.29749 -0.05555 243 ALA A CA    
2087 C C     . ALA B 243 ? 2.14236 2.04478 1.82062 -0.32561 -0.28855 -0.07796 243 ALA A C     
2088 O O     . ALA B 243 ? 2.25829 2.15010 1.89584 -0.33039 -0.27957 -0.09485 243 ALA A O     
2089 C CB    . ALA B 243 ? 2.03361 1.96509 1.76231 -0.31054 -0.28331 -0.04487 243 ALA A CB    
2090 N N     . VAL B 244 ? 2.13351 2.03650 1.84857 -0.31958 -0.29079 -0.07789 244 VAL A N     
2091 C CA    . VAL B 244 ? 2.08427 1.97536 1.79485 -0.31710 -0.28119 -0.09891 244 VAL A CA    
2092 C C     . VAL B 244 ? 2.20949 2.08186 1.87302 -0.33318 -0.29190 -0.11319 244 VAL A C     
2093 O O     . VAL B 244 ? 2.29939 2.16037 1.93952 -0.33259 -0.27837 -0.13398 244 VAL A O     
2094 C CB    . VAL B 244 ? 1.90284 1.79594 1.65879 -0.31086 -0.28611 -0.09537 244 VAL A CB    
2095 C CG1   . VAL B 244 ? 2.03822 1.92672 1.80357 -0.32284 -0.31307 -0.08497 244 VAL A CG1   
2096 C CG2   . VAL B 244 ? 1.94188 1.82509 1.69780 -0.30550 -0.27244 -0.11595 244 VAL A CG2   
2097 N N     . ASP B 245 ? 2.09418 1.96344 1.74430 -0.34712 -0.31503 -0.10207 245 ASP A N     
2098 C CA    . ASP B 245 ? 2.22106 2.07131 1.82364 -0.36402 -0.32716 -0.11505 245 ASP A CA    
2099 C C     . ASP B 245 ? 2.23815 2.08338 1.79437 -0.36544 -0.30983 -0.12858 245 ASP A C     
2100 O O     . ASP B 245 ? 2.23352 2.06258 1.75819 -0.37004 -0.30262 -0.14996 245 ASP A O     
2101 C CB    . ASP B 245 ? 2.33803 2.18738 1.93494 -0.37889 -0.35559 -0.09835 245 ASP A CB    
2102 C CG    . ASP B 245 ? 2.36703 2.19645 1.91359 -0.39782 -0.37060 -0.10992 245 ASP A CG    
2103 O OD1   . ASP B 245 ? 2.36919 2.18359 1.90984 -0.40199 -0.37382 -0.12547 245 ASP A OD1   
2104 O OD2   . ASP B 245 ? 2.38381 2.21240 1.89713 -0.40854 -0.37915 -0.10318 245 ASP A OD2   
2105 N N     . GLN B 246 ? 2.23905 2.09757 1.79295 -0.36117 -0.30247 -0.11672 246 GLN A N     
2106 C CA    . GLN B 246 ? 2.23313 2.08808 1.74335 -0.36303 -0.28636 -0.12764 246 GLN A CA    
2107 C C     . GLN B 246 ? 2.22196 2.07910 1.74201 -0.34802 -0.25828 -0.14288 246 GLN A C     
2108 O O     . GLN B 246 ? 2.31373 2.16061 1.79723 -0.35049 -0.24420 -0.16083 246 GLN A O     
2109 C CB    . GLN B 246 ? 2.27646 2.14455 1.78174 -0.36442 -0.28955 -0.10888 246 GLN A CB    
2110 C CG    . GLN B 246 ? 2.41710 2.27597 1.87716 -0.38299 -0.30726 -0.10547 246 GLN A CG    
2111 C CD    . GLN B 246 ? 2.54073 2.41325 2.00517 -0.38519 -0.31605 -0.08276 246 GLN A CD    
2112 O OE1   . GLN B 246 ? 2.58023 2.46382 2.08336 -0.38232 -0.32909 -0.06350 246 GLN A OE1   
2113 N NE2   . GLN B 246 ? 2.41145 2.28309 1.83674 -0.39044 -0.30871 -0.08463 246 GLN A NE2   
2114 N N     . LEU B 247 ? 2.16150 2.03130 1.72910 -0.33336 -0.25052 -0.13571 247 LEU A N     
2115 C CA    . LEU B 247 ? 2.06116 1.93382 1.64217 -0.31897 -0.22520 -0.14854 247 LEU A CA    
2116 C C     . LEU B 247 ? 2.16129 2.01748 1.73507 -0.32089 -0.22209 -0.16951 247 LEU A C     
2117 O O     . LEU B 247 ? 2.01367 1.86643 1.58035 -0.31367 -0.20110 -0.18545 247 LEU A O     
2118 C CB    . LEU B 247 ? 2.15530 2.04463 1.78799 -0.30441 -0.22040 -0.13436 247 LEU A CB    
2119 C CG    . LEU B 247 ? 2.22243 2.12788 1.86523 -0.30027 -0.21966 -0.11515 247 LEU A CG    
2120 C CD1   . LEU B 247 ? 2.12276 2.04231 1.81522 -0.28585 -0.21350 -0.10363 247 LEU A CD1   
2121 C CD2   . LEU B 247 ? 2.18820 2.09541 1.80018 -0.29873 -0.20213 -0.12186 247 LEU A CD2   
2122 N N     . GLY B 248 ? 2.31527 2.16168 1.89235 -0.33029 -0.24240 -0.16906 248 GLY A N     
2123 C CA    . GLY B 248 ? 2.24319 2.07281 1.81527 -0.33275 -0.24126 -0.18862 248 GLY A CA    
2124 C C     . GLY B 248 ? 2.23952 2.07564 1.85645 -0.31745 -0.22847 -0.19112 248 GLY A C     
2125 O O     . GLY B 248 ? 2.29153 2.11817 1.90254 -0.31318 -0.21328 -0.21006 248 GLY A O     
2126 N N     . LEU B 249 ? 2.05769 1.90929 1.71815 -0.30947 -0.23390 -0.17246 249 LEU A N     
2127 C CA    . LEU B 249 ? 1.99751 1.85603 1.70223 -0.29523 -0.22291 -0.17277 249 LEU A CA    
2128 C C     . LEU B 249 ? 2.10396 1.95867 1.83758 -0.29892 -0.24172 -0.16703 249 LEU A C     
2129 O O     . LEU B 249 ? 2.26378 2.10533 1.97589 -0.31285 -0.25968 -0.17076 249 LEU A O     
2130 C CB    . LEU B 249 ? 2.05083 1.92938 1.78297 -0.28267 -0.21238 -0.15676 249 LEU A CB    
2131 C CG    . LEU B 249 ? 2.11040 1.99445 1.81567 -0.28020 -0.19694 -0.15851 249 LEU A CG    
2132 C CD1   . LEU B 249 ? 1.98649 1.88936 1.72155 -0.26832 -0.18870 -0.14199 249 LEU A CD1   
2133 C CD2   . LEU B 249 ? 2.19584 2.07111 1.88179 -0.27640 -0.17681 -0.17990 249 LEU A CD2   
2134 N N     . THR B 250 ? 1.97590 1.84155 1.75585 -0.28735 -0.23793 -0.15798 250 THR A N     
2135 C CA    . THR B 250 ? 1.96553 1.82883 1.77713 -0.28984 -0.25442 -0.15163 250 THR A CA    
2136 C C     . THR B 250 ? 2.02463 1.90366 1.86744 -0.28768 -0.26566 -0.12724 250 THR A C     
2137 O O     . THR B 250 ? 2.08070 1.97399 1.93351 -0.27848 -0.25405 -0.11724 250 THR A O     
2138 C CB    . THR B 250 ? 1.95424 1.81663 1.79561 -0.27885 -0.24147 -0.16055 250 THR A CB    
2139 O OG1   . THR B 250 ? 2.15985 2.03945 2.02724 -0.26484 -0.22621 -0.14997 250 THR A OG1   
2140 C CG2   . THR B 250 ? 1.86751 1.71483 1.68110 -0.27954 -0.22792 -0.18481 250 THR A CG2   
2141 N N     . TYR B 251 ? 1.75787 1.63420 1.61661 -0.29585 -0.28729 -0.11787 251 TYR A N     
2142 C CA    . TYR B 251 ? 1.72324 1.61452 1.61659 -0.29369 -0.29839 -0.09380 251 TYR A CA    
2143 C C     . TYR B 251 ? 1.73158 1.63251 1.67316 -0.28034 -0.28934 -0.08772 251 TYR A C     
2144 O O     . TYR B 251 ? 1.75820 1.65705 1.72731 -0.28283 -0.30212 -0.08276 251 TYR A O     
2145 C CB    . TYR B 251 ? 1.73452 1.61898 1.62607 -0.30851 -0.32579 -0.08575 251 TYR A CB    
2146 C CG    . TYR B 251 ? 1.69333 1.59170 1.61162 -0.30946 -0.33945 -0.06079 251 TYR A CG    
2147 C CD1   . TYR B 251 ? 1.65727 1.56551 1.62542 -0.30304 -0.34406 -0.04618 251 TYR A CD1   
2148 C CD2   . TYR B 251 ? 1.71669 1.61800 1.61096 -0.31709 -0.34778 -0.05158 251 TYR A CD2   
2149 C CE1   . TYR B 251 ? 1.63180 1.55246 1.62622 -0.30357 -0.35550 -0.02355 251 TYR A CE1   
2150 C CE2   . TYR B 251 ? 1.77799 1.69167 1.69859 -0.31786 -0.36017 -0.02861 251 TYR A CE2   
2151 C CZ    . TYR B 251 ? 1.67751 1.60081 1.64876 -0.31090 -0.36370 -0.01477 251 TYR A CZ    
2152 O OH    . TYR B 251 ? 1.71638 1.65172 1.71541 -0.31126 -0.37484 0.00781  251 TYR A OH    
2153 N N     . ARG B 252 ? 1.82595 1.73687 1.77715 -0.26692 -0.26800 -0.08803 252 ARG A N     
2154 C CA    . ARG B 252 ? 1.62256 1.54342 1.61849 -0.25399 -0.25840 -0.08107 252 ARG A CA    
2155 C C     . ARG B 252 ? 1.60188 1.53645 1.63054 -0.25190 -0.26762 -0.05770 252 ARG A C     
2156 O O     . ARG B 252 ? 1.64981 1.59386 1.67305 -0.24919 -0.26321 -0.04780 252 ARG A O     
2157 C CB    . ARG B 252 ? 1.61693 1.54399 1.61211 -0.24112 -0.23383 -0.08775 252 ARG A CB    
2158 C CG    . ARG B 252 ? 1.72278 1.65929 1.76138 -0.22876 -0.22455 -0.08043 252 ARG A CG    
2159 C CD    . ARG B 252 ? 1.71741 1.64467 1.77351 -0.23064 -0.23069 -0.08818 252 ARG A CD    
2160 N NE    . ARG B 252 ? 1.68000 1.61688 1.78152 -0.22182 -0.22838 -0.07598 252 ARG A NE    
2161 C CZ    . ARG B 252 ? 1.99748 1.93422 2.11815 -0.21339 -0.21648 -0.08221 252 ARG A CZ    
2162 N NH1   . ARG B 252 ? 2.03308 1.96366 2.13395 -0.21018 -0.20257 -0.09868 252 ARG A NH1   
2163 N NH2   . ARG B 252 ? 2.06837 2.01139 2.22873 -0.20826 -0.21832 -0.07138 252 ARG A NH2   
2164 N N     . PRO B 253 ? 1.54529 1.48111 1.60850 -0.25308 -0.27990 -0.04842 253 PRO A N     
2165 C CA    . PRO B 253 ? 1.63903 1.58735 1.73461 -0.25154 -0.28871 -0.02617 253 PRO A CA    
2166 C C     . PRO B 253 ? 1.62516 1.58787 1.74291 -0.23710 -0.26994 -0.01696 253 PRO A C     
2167 O O     . PRO B 253 ? 1.53355 1.50626 1.66039 -0.23555 -0.27173 -0.00146 253 PRO A O     
2168 C CB    . PRO B 253 ? 1.55252 1.49777 1.68066 -0.25447 -0.30182 -0.02212 253 PRO A CB    
2169 C CG    . PRO B 253 ? 1.62414 1.55982 1.74722 -0.25088 -0.29115 -0.04092 253 PRO A CG    
2170 C CD    . PRO B 253 ? 1.55064 1.47605 1.62446 -0.25560 -0.28493 -0.05871 253 PRO A CD    
2171 N N     . GLN B 254 ? 1.52282 1.48607 1.64898 -0.22700 -0.25250 -0.02615 254 GLN A N     
2172 C CA    . GLN B 254 ? 1.45821 1.43423 1.60535 -0.21344 -0.23455 -0.01779 254 GLN A CA    
2173 C C     . GLN B 254 ? 1.58427 1.56448 1.70383 -0.21180 -0.22543 -0.01769 254 GLN A C     
2174 O O     . GLN B 254 ? 1.59155 1.58272 1.72711 -0.20560 -0.22021 -0.00368 254 GLN A O     
2175 C CB    . GLN B 254 ? 1.65588 1.63046 1.81411 -0.20441 -0.21912 -0.02837 254 GLN A CB    
2176 C CG    . GLN B 254 ? 1.68971 1.66220 1.88106 -0.20433 -0.22639 -0.02587 254 GLN A CG    
2177 C CD    . GLN B 254 ? 1.80843 1.79328 2.04143 -0.19730 -0.22527 -0.00683 254 GLN A CD    
2178 O OE1   . GLN B 254 ? 1.94025 1.92929 2.19828 -0.18854 -0.21454 -0.00524 254 GLN A OE1   
2179 N NE2   . GLN B 254 ? 1.70995 1.70067 1.95132 -0.20117 -0.23610 0.00819  254 GLN A NE2   
2180 N N     . GLN B 255 ? 1.61462 1.58607 1.69461 -0.21725 -0.22325 -0.03272 255 GLN A N     
2181 C CA    . GLN B 255 ? 1.56274 1.53821 1.61607 -0.21663 -0.21557 -0.03191 255 GLN A CA    
2182 C C     . GLN B 255 ? 1.49695 1.47886 1.55695 -0.22163 -0.22909 -0.01394 255 GLN A C     
2183 O O     . GLN B 255 ? 1.54073 1.53254 1.60840 -0.21504 -0.22077 -0.00346 255 GLN A O     
2184 C CB    . GLN B 255 ? 1.51390 1.47791 1.52320 -0.22448 -0.21505 -0.04936 255 GLN A CB    
2185 C CG    . GLN B 255 ? 1.64076 1.60814 1.62052 -0.22552 -0.20879 -0.04851 255 GLN A CG    
2186 C CD    . GLN B 255 ? 1.61317 1.56882 1.54883 -0.23434 -0.20891 -0.06506 255 GLN A CD    
2187 O OE1   . GLN B 255 ? 1.56758 1.51143 1.49295 -0.23997 -0.21366 -0.07823 255 GLN A OE1   
2188 N NE2   . GLN B 255 ? 1.75867 1.71699 1.66764 -0.23574 -0.20322 -0.06464 255 GLN A NE2   
2189 N N     . LEU B 256 ? 1.44456 1.42069 1.50274 -0.23305 -0.24957 -0.01030 256 LEU A N     
2190 C CA    . LEU B 256 ? 1.54709 1.52904 1.61290 -0.23895 -0.26455 0.00764  256 LEU A CA    
2191 C C     . LEU B 256 ? 1.54644 1.54101 1.65781 -0.22909 -0.26048 0.02518  256 LEU A C     
2192 O O     . LEU B 256 ? 1.54355 1.54650 1.66139 -0.22701 -0.25999 0.03872  256 LEU A O     
2193 C CB    . LEU B 256 ? 1.56137 1.53418 1.62029 -0.25316 -0.28805 0.00800  256 LEU A CB    
2194 C CG    . LEU B 256 ? 1.55365 1.53186 1.62390 -0.26067 -0.30672 0.02742  256 LEU A CG    
2195 C CD1   . LEU B 256 ? 1.65952 1.64197 1.70508 -0.26193 -0.30334 0.03225  256 LEU A CD1   
2196 C CD2   . LEU B 256 ? 1.64573 1.61332 1.70499 -0.27582 -0.33047 0.02593  256 LEU A CD2   
2197 N N     . TYR B 257 ? 1.46391 1.45934 1.60547 -0.22328 -0.25709 0.02477  257 TYR A N     
2198 C CA    . TYR B 257 ? 1.48396 1.49080 1.66928 -0.21387 -0.25205 0.04105  257 TYR A CA    
2199 C C     . TYR B 257 ? 1.53058 1.54557 1.71330 -0.20363 -0.23357 0.04437  257 TYR A C     
2200 O O     . TYR B 257 ? 1.43914 1.46284 1.64239 -0.20013 -0.23346 0.06028  257 TYR A O     
2201 C CB    . TYR B 257 ? 1.46782 1.47326 1.67844 -0.20838 -0.24690 0.03625  257 TYR A CB    
2202 C CG    . TYR B 257 ? 1.29064 1.30688 1.54462 -0.19801 -0.23870 0.05078  257 TYR A CG    
2203 C CD1   . TYR B 257 ? 1.30804 1.33259 1.58758 -0.19808 -0.24586 0.06969  257 TYR A CD1   
2204 C CD2   . TYR B 257 ? 1.39755 1.41550 1.66674 -0.18821 -0.22323 0.04577  257 TYR A CD2   
2205 C CE1   . TYR B 257 ? 1.23624 1.27000 1.55457 -0.18856 -0.23693 0.08244  257 TYR A CE1   
2206 C CE2   . TYR B 257 ? 1.51610 1.54326 1.82235 -0.17917 -0.21497 0.05876  257 TYR A CE2   
2207 C CZ    . TYR B 257 ? 1.26039 1.29527 1.59084 -0.17923 -0.22126 0.07677  257 TYR A CZ    
2208 O OH    . TYR B 257 ? 1.38945 1.43284 1.75587 -0.17025 -0.21179 0.08919  257 TYR A OH    
2209 N N     . LEU B 258 ? 1.42428 1.43613 1.58276 -0.19911 -0.21833 0.02974  258 LEU A N     
2210 C CA    . LEU B 258 ? 1.38709 1.40593 1.54162 -0.18957 -0.20045 0.03179  258 LEU A CA    
2211 C C     . LEU B 258 ? 1.42305 1.44512 1.56312 -0.19411 -0.20640 0.04112  258 LEU A C     
2212 O O     . LEU B 258 ? 1.48413 1.51443 1.64288 -0.18777 -0.20056 0.05401  258 LEU A O     
2213 C CB    . LEU B 258 ? 1.50334 1.51726 1.63135 -0.18632 -0.18619 0.01399  258 LEU A CB    
2214 C CG    . LEU B 258 ? 1.33086 1.35089 1.45266 -0.17705 -0.16781 0.01418  258 LEU A CG    
2215 C CD1   . LEU B 258 ? 1.24875 1.27684 1.40558 -0.16664 -0.15831 0.02521  258 LEU A CD1   
2216 C CD2   . LEU B 258 ? 1.26294 1.27789 1.36121 -0.17480 -0.15555 -0.00328 258 LEU A CD2   
2217 N N     . ALA B 259 ? 1.38162 1.39687 1.48971 -0.20501 -0.21774 0.03497  259 ALA A N     
2218 C CA    . ALA B 259 ? 1.40870 1.42672 1.50066 -0.21015 -0.22391 0.04382  259 ALA A CA    
2219 C C     . ALA B 259 ? 1.35034 1.37569 1.47649 -0.21032 -0.23472 0.06416  259 ALA A C     
2220 O O     . ALA B 259 ? 1.27770 1.30999 1.41076 -0.20618 -0.22985 0.07524  259 ALA A O     
2221 C CB    . ALA B 259 ? 1.43401 1.44275 1.48864 -0.22331 -0.23703 0.03511  259 ALA A CB    
2222 N N     . GLU B 260 ? 1.47359 1.49732 1.62224 -0.21480 -0.24863 0.06904  260 GLU A N     
2223 C CA    . GLU B 260 ? 1.41452 1.44539 1.59880 -0.21565 -0.26019 0.08924  260 GLU A CA    
2224 C C     . GLU B 260 ? 1.33064 1.37097 1.54800 -0.20197 -0.24346 0.09871  260 GLU A C     
2225 O O     . GLU B 260 ? 1.26270 1.30974 1.49600 -0.20008 -0.24461 0.11366  260 GLU A O     
2226 C CB    . GLU B 260 ? 1.44785 1.47480 1.65035 -0.22284 -0.27731 0.09127  260 GLU A CB    
2227 C CG    . GLU B 260 ? 1.52422 1.54118 1.69386 -0.23793 -0.29634 0.08427  260 GLU A CG    
2228 C CD    . GLU B 260 ? 1.93335 1.94408 2.11607 -0.24545 -0.31240 0.08257  260 GLU A CD    
2229 O OE1   . GLU B 260 ? 2.13268 2.14739 2.35135 -0.23850 -0.30816 0.08672  260 GLU A OE1   
2230 O OE2   . GLU B 260 ? 1.85854 1.86009 2.01513 -0.25860 -0.32929 0.07731  260 GLU A OE2   
2231 N N     . THR B 261 ? 1.33384 1.37417 1.56064 -0.19305 -0.22850 0.09037  261 THR A N     
2232 C CA    . THR B 261 ? 1.33093 1.37916 1.58742 -0.18052 -0.21228 0.09880  261 THR A CA    
2233 C C     . THR B 261 ? 1.34062 1.39197 1.58095 -0.17575 -0.20022 0.10014  261 THR A C     
2234 O O     . THR B 261 ? 1.30272 1.36055 1.56609 -0.17051 -0.19611 0.11399  261 THR A O     
2235 C CB    . THR B 261 ? 1.20836 1.25508 1.47239 -0.17309 -0.19913 0.08857  261 THR A CB    
2236 O OG1   . THR B 261 ? 1.55418 1.59433 1.78109 -0.17497 -0.19362 0.07115  261 THR A OG1   
2237 C CG2   . THR B 261 ? 1.22745 1.27224 1.51547 -0.17652 -0.21017 0.09005  261 THR A CG2   
2238 N N     . ILE B 262 ? 1.27795 1.32457 1.48067 -0.17765 -0.19468 0.08640  262 ILE A N     
2239 C CA    . ILE B 262 ? 1.35500 1.40421 1.54013 -0.17367 -0.18337 0.08697  262 ILE A CA    
2240 C C     . ILE B 262 ? 1.29439 1.34686 1.48399 -0.17918 -0.19554 0.10177  262 ILE A C     
2241 O O     . ILE B 262 ? 1.34716 1.40509 1.55286 -0.17264 -0.18756 0.11230  262 ILE A O     
2242 C CB    . ILE B 262 ? 1.25695 1.30042 1.40076 -0.17675 -0.17811 0.07027  262 ILE A CB    
2243 C CG1   . ILE B 262 ? 1.37453 1.41503 1.51642 -0.17106 -0.16602 0.05635  262 ILE A CG1   
2244 C CG2   . ILE B 262 ? 1.17162 1.21781 1.29741 -0.17410 -0.16876 0.07198  262 ILE A CG2   
2245 C CD1   . ILE B 262 ? 1.43051 1.46477 1.53470 -0.17481 -0.16202 0.03949  262 ILE A CD1   
2246 N N     . LEU B 263 ? 1.17028 1.21904 1.34698 -0.19097 -0.21444 0.10281  263 LEU A N     
2247 C CA    . LEU B 263 ? 1.21213 1.26383 1.39094 -0.19746 -0.22771 0.11736  263 LEU A CA    
2248 C C     . LEU B 263 ? 1.26612 1.32515 1.49089 -0.19212 -0.22938 0.13549  263 LEU A C     
2249 O O     . LEU B 263 ? 1.10774 1.17149 1.34209 -0.18984 -0.22778 0.14751  263 LEU A O     
2250 C CB    . LEU B 263 ? 1.27777 1.32347 1.43619 -0.21178 -0.24899 0.11531  263 LEU A CB    
2251 C CG    . LEU B 263 ? 1.33149 1.37947 1.48837 -0.22053 -0.26537 0.13013  263 LEU A CG    
2252 C CD1   . LEU B 263 ? 1.45281 1.50157 1.58186 -0.21995 -0.25713 0.12865  263 LEU A CD1   
2253 C CD2   . LEU B 263 ? 1.38361 1.42494 1.52335 -0.23518 -0.28770 0.12851  263 LEU A CD2   
2254 N N     . ASP B 264 ? 1.28116 1.34096 1.53408 -0.19016 -0.23202 0.13740  264 ASP A N     
2255 C CA    . ASP B 264 ? 1.28863 1.35559 1.58779 -0.18525 -0.23340 0.15505  264 ASP A CA    
2256 C C     . ASP B 264 ? 1.38632 1.45792 1.69785 -0.17269 -0.21232 0.15858  264 ASP A C     
2257 O O     . ASP B 264 ? 1.39308 1.46970 1.72628 -0.17037 -0.21279 0.17339  264 ASP A O     
2258 C CB    . ASP B 264 ? 1.19268 1.25960 1.51850 -0.18459 -0.23735 0.15509  264 ASP A CB    
2259 C CG    . ASP B 264 ? 1.50658 1.58105 1.88159 -0.17992 -0.23871 0.17328  264 ASP A CG    
2260 O OD1   . ASP B 264 ? 1.60290 1.68045 1.99309 -0.18614 -0.25407 0.18764  264 ASP A OD1   
2261 O OD2   . ASP B 264 ? 1.49976 1.57702 1.89778 -0.17023 -0.22424 0.17334  264 ASP A OD2   
2262 N N     . GLN B 265 ? 1.32032 1.38975 1.61815 -0.16525 -0.19482 0.14541  265 GLN A N     
2263 C CA    . GLN B 265 ? 1.35843 1.43098 1.66562 -0.15362 -0.17439 0.14755  265 GLN A CA    
2264 C C     . GLN B 265 ? 1.30390 1.37677 1.59196 -0.15460 -0.17250 0.15058  265 GLN A C     
2265 O O     . GLN B 265 ? 1.29377 1.37016 1.60137 -0.14799 -0.16385 0.16083  265 GLN A O     
2266 C CB    . GLN B 265 ? 1.27682 1.34640 1.56949 -0.14733 -0.15869 0.13240  265 GLN A CB    
2267 C CG    . GLN B 265 ? 1.19326 1.26304 1.50890 -0.14499 -0.15847 0.13089  265 GLN A CG    
2268 C CD    . GLN B 265 ? 1.26741 1.34282 1.62471 -0.13778 -0.15247 0.14518  265 GLN A CD    
2269 O OE1   . GLN B 265 ? 1.31934 1.39666 1.68382 -0.12890 -0.13603 0.14791  265 GLN A OE1   
2270 N NE2   . GLN B 265 ? 1.32102 1.39876 1.70609 -0.14179 -0.16561 0.15447  265 GLN A NE2   
2271 N N     . LEU B 266 ? 1.25532 1.32422 1.50674 -0.16253 -0.17971 0.14185  266 LEU A N     
2272 C CA    . LEU B 266 ? 1.44182 1.51094 1.67264 -0.16417 -0.17821 0.14435  266 LEU A CA    
2273 C C     . LEU B 266 ? 1.49565 1.56867 1.74803 -0.16848 -0.19173 0.16257  266 LEU A C     
2274 O O     . LEU B 266 ? 1.38922 1.46456 1.64696 -0.16441 -0.18511 0.17042  266 LEU A O     
2275 C CB    . LEU B 266 ? 1.31639 1.38045 1.50389 -0.17251 -0.18354 0.13127  266 LEU A CB    
2276 C CG    . LEU B 266 ? 1.14356 1.20430 1.30680 -0.16763 -0.16783 0.11400  266 LEU A CG    
2277 C CD1   . LEU B 266 ? 1.15949 1.21509 1.28280 -0.17683 -0.17450 0.10199  266 LEU A CD1   
2278 C CD2   . LEU B 266 ? 1.17066 1.23358 1.33291 -0.15878 -0.15064 0.11500  266 LEU A CD2   
2279 N N     . MET B 267 ? 1.35366 1.42708 1.61852 -0.17666 -0.21035 0.16924  267 MET A N     
2280 C CA    . MET B 267 ? 1.26300 1.34035 1.54850 -0.18211 -0.22565 0.18755  267 MET A CA    
2281 C C     . MET B 267 ? 1.30041 1.38333 1.62637 -0.17145 -0.21412 0.20080  267 MET A C     
2282 O O     . MET B 267 ? 1.25974 1.34530 1.59423 -0.17155 -0.21620 0.21271  267 MET A O     
2283 C CB    . MET B 267 ? 1.24247 1.31951 1.54036 -0.19183 -0.24696 0.19302  267 MET A CB    
2284 C CG    . MET B 267 ? 1.44838 1.52784 1.75344 -0.20151 -0.26715 0.20910  267 MET A CG    
2285 S SD    . MET B 267 ? 1.25965 1.33441 1.51291 -0.21185 -0.27466 0.20286  267 MET A SD    
2286 C CE    . MET B 267 ? 1.22206 1.28810 1.43652 -0.21968 -0.27965 0.18187  267 MET A CE    
2287 N N     . HIS B 268 ? 1.21035 1.29456 1.55995 -0.16276 -0.20208 0.19877  268 HIS A N     
2288 C CA    . HIS B 268 ? 1.18258 1.27104 1.56879 -0.15194 -0.18817 0.20980  268 HIS A CA    
2289 C C     . HIS B 268 ? 1.49611 1.58187 1.86449 -0.14260 -0.16587 0.19961  268 HIS A C     
2290 O O     . HIS B 268 ? 1.51797 1.59962 1.84922 -0.14466 -0.16239 0.18514  268 HIS A O     
2291 C CB    . HIS B 268 ? 1.19044 1.28189 1.61296 -0.14784 -0.18683 0.21452  268 HIS A CB    
2292 C CG    . HIS B 268 ? 1.54155 1.63403 1.97410 -0.15796 -0.20887 0.21959  268 HIS A CG    
2293 N ND1   . HIS B 268 ? 1.59542 1.68375 2.00786 -0.16366 -0.21597 0.20694  268 HIS A ND1   
2294 C CD2   . HIS B 268 ? 1.58588 1.68262 2.04680 -0.16366 -0.22567 0.23594  268 HIS A CD2   
2295 C CE1   . HIS B 268 ? 1.44431 1.53371 1.87111 -0.17284 -0.23667 0.21504  268 HIS A CE1   
2296 N NE2   . HIS B 268 ? 1.34305 1.43792 1.79958 -0.17315 -0.24328 0.23306  268 HIS A NE2   
2297 N N     . SER B 269 ? 1.51833 1.60597 1.91250 -0.13281 -0.15103 0.20707  269 SER A N     
2298 C CA    . SER B 269 ? 1.45419 1.53843 1.83220 -0.12404 -0.12972 0.19747  269 SER A CA    
2299 C C     . SER B 269 ? 1.49589 1.57945 1.88210 -0.11733 -0.11720 0.18981  269 SER A C     
2300 O O     . SER B 269 ? 1.71951 1.80321 2.12566 -0.10809 -0.10119 0.19347  269 SER A O     
2301 C CB    . SER B 269 ? 1.58192 1.66670 1.97862 -0.11746 -0.11947 0.20786  269 SER A CB    
2302 O OG    . SER B 269 ? 2.08210 2.17058 2.52227 -0.11242 -0.11686 0.22058  269 SER A OG    
2303 N N     . GLU B 270 ? 1.41664 1.49896 1.78767 -0.12197 -0.12398 0.17958  270 GLU A N     
2304 C CA    . GLU B 270 ? 1.51904 1.60116 1.90106 -0.11625 -0.11390 0.17373  270 GLU A CA    
2305 C C     . GLU B 270 ? 1.15913 1.23691 1.50757 -0.11404 -0.10286 0.15695  270 GLU A C     
2306 O O     . GLU B 270 ? 1.16977 1.24498 1.48658 -0.12041 -0.10995 0.14786  270 GLU A O     
2307 C CB    . GLU B 270 ? 1.30853 1.39239 1.70490 -0.12247 -0.12941 0.17547  270 GLU A CB    
2308 C CG    . GLU B 270 ? 1.23912 1.32804 1.67397 -0.12447 -0.14059 0.19305  270 GLU A CG    
2309 C CD    . GLU B 270 ? 1.67966 1.76985 2.12909 -0.13081 -0.15598 0.19450  270 GLU A CD    
2310 O OE1   . GLU B 270 ? 1.71121 1.79813 2.13567 -0.14007 -0.17041 0.18674  270 GLU A OE1   
2311 O OE2   . GLU B 270 ? 1.83515 1.92917 2.32056 -0.12664 -0.15323 0.20321  270 GLU A OE2   
2312 N N     . LYS B 271 ? 1.04543 1.12245 1.40099 -0.10557 -0.08609 0.15352  271 LYS A N     
2313 C CA    . LYS B 271 ? 1.03735 1.11076 1.36475 -0.10341 -0.07606 0.13854  271 LYS A CA    
2314 C C     . LYS B 271 ? 1.03960 1.11326 1.37462 -0.10445 -0.07957 0.13310  271 LYS A C     
2315 O O     . LYS B 271 ? 1.09514 1.17165 1.46167 -0.10163 -0.07914 0.14165  271 LYS A O     
2316 C CB    . LYS B 271 ? 0.97136 1.04300 1.29899 -0.09438 -0.05638 0.13839  271 LYS A CB    
2317 C CG    . LYS B 271 ? 1.24562 1.31594 1.56491 -0.09352 -0.05287 0.14285  271 LYS A CG    
2318 C CD    . LYS B 271 ? 1.28426 1.35128 1.60196 -0.08516 -0.03361 0.14188  271 LYS A CD    
2319 C CE    . LYS B 271 ? 0.99829 1.06310 1.30544 -0.08504 -0.03108 0.14495  271 LYS A CE    
2320 N NZ    . LYS B 271 ? 1.21465 1.27866 1.48970 -0.09147 -0.03910 0.13684  271 LYS A NZ    
2321 N N     . ALA B 272 ? 0.94062 1.01137 1.24948 -0.10828 -0.08263 0.11979  272 ALA A N     
2322 C CA    . ALA B 272 ? 0.96033 1.03064 1.27744 -0.11004 -0.08766 0.11463  272 ALA A CA    
2323 C C     . ALA B 272 ? 0.95595 1.02283 1.24888 -0.10870 -0.07994 0.09964  272 ALA A C     
2324 O O     . ALA B 272 ? 1.07253 1.13733 1.33762 -0.10916 -0.07533 0.09217  272 ALA A O     
2325 C CB    . ALA B 272 ? 0.96326 1.03320 1.28075 -0.11962 -0.10754 0.11597  272 ALA A CB    
2326 N N     . MET B 273 ? 0.91258 0.97914 1.21762 -0.10715 -0.07873 0.09602  273 MET A N     
2327 C CA    . MET B 273 ? 0.89963 0.96306 1.18562 -0.10607 -0.07245 0.08227  273 MET A CA    
2328 C C     . MET B 273 ? 1.01434 1.07531 1.30247 -0.11219 -0.08513 0.07600  273 MET A C     
2329 O O     . MET B 273 ? 1.08609 1.14859 1.40097 -0.11121 -0.08807 0.08156  273 MET A O     
2330 C CB    . MET B 273 ? 0.81515 0.87977 1.11406 -0.09775 -0.05720 0.08361  273 MET A CB    
2331 C CG    . MET B 273 ? 0.98686 1.05231 1.28265 -0.09174 -0.04377 0.08876  273 MET A CG    
2332 S SD    . MET B 273 ? 0.75892 0.82468 1.06736 -0.08324 -0.02682 0.09022  273 MET A SD    
2333 C CE    . MET B 273 ? 1.13081 1.19510 1.42554 -0.07845 -0.01332 0.09328  273 MET A CE    
2334 N N     . ILE B 274 ? 0.96939 1.02627 1.23056 -0.11842 -0.09206 0.06492  274 ILE A N     
2335 C CA    . ILE B 274 ? 0.89398 0.94671 1.15423 -0.12521 -0.10480 0.05780  274 ILE A CA    
2336 C C     . ILE B 274 ? 0.90127 0.95024 1.14786 -0.12321 -0.09711 0.04352  274 ILE A C     
2337 O O     . ILE B 274 ? 1.01981 1.06791 1.24277 -0.12147 -0.08837 0.03602  274 ILE A O     
2338 C CB    . ILE B 274 ? 0.94709 0.99678 1.18688 -0.13477 -0.11927 0.05579  274 ILE A CB    
2339 C CG1   . ILE B 274 ? 0.95085 1.00485 1.20304 -0.13622 -0.12567 0.07067  274 ILE A CG1   
2340 C CG2   . ILE B 274 ? 0.95677 1.00099 1.19596 -0.14249 -0.13332 0.04909  274 ILE A CG2   
2341 C CD1   . ILE B 274 ? 1.08554 1.13688 1.31693 -0.14610 -0.14042 0.07029  274 ILE A CD1   
2342 N N     . GLU B 275 ? 0.96534 1.01232 1.22795 -0.12346 -0.10034 0.04051  275 GLU A N     
2343 C CA    . GLU B 275 ? 0.92663 0.96967 1.17919 -0.12177 -0.09386 0.02714  275 GLU A CA    
2344 C C     . GLU B 275 ? 0.97799 1.01371 1.21747 -0.13011 -0.10626 0.01604  275 GLU A C     
2345 O O     . GLU B 275 ? 1.12889 1.16269 1.38710 -0.13354 -0.11665 0.01857  275 GLU A O     
2346 C CB    . GLU B 275 ? 0.94500 0.99034 1.22417 -0.11538 -0.08651 0.03081  275 GLU A CB    
2347 C CG    . GLU B 275 ? 1.03053 1.07159 1.30322 -0.11435 -0.08202 0.01790  275 GLU A CG    
2348 C CD    . GLU B 275 ? 1.12704 1.17123 1.41911 -0.10684 -0.07076 0.02149  275 GLU A CD    
2349 O OE1   . GLU B 275 ? 1.27240 1.32050 1.56105 -0.10122 -0.05914 0.02593  275 GLU A OE1   
2350 O OE2   . GLU B 275 ? 1.30471 1.34706 1.61467 -0.10697 -0.07387 0.02002  275 GLU A OE2   
2351 N N     . ALA B 276 ? 1.12570 1.15719 1.33409 -0.13336 -0.10478 0.00423  276 ALA A N     
2352 C CA    . ALA B 276 ? 1.08931 1.11245 1.28023 -0.14197 -0.11575 -0.00740 276 ALA A CA    
2353 C C     . ALA B 276 ? 1.21245 1.23050 1.38943 -0.14013 -0.10685 -0.02305 276 ALA A C     
2354 O O     . ALA B 276 ? 1.27919 1.29970 1.44239 -0.13554 -0.09447 -0.02677 276 ALA A O     
2355 C CB    . ALA B 276 ? 1.09559 1.11735 1.26026 -0.14886 -0.12288 -0.00740 276 ALA A CB    
2356 N N     . SER B 277 ? 1.31475 1.32563 1.49598 -0.14380 -0.11320 -0.03183 277 SER A N     
2357 C CA    . SER B 277 ? 1.41525 1.42012 1.58358 -0.14258 -0.10514 -0.04768 277 SER A CA    
2358 C C     . SER B 277 ? 1.60769 1.60234 1.74930 -0.15222 -0.11454 -0.06028 277 SER A C     
2359 O O     . SER B 277 ? 1.72458 1.71122 1.86185 -0.15345 -0.11295 -0.07369 277 SER A O     
2360 C CB    . SER B 277 ? 1.88995 1.89395 2.08514 -0.13806 -0.10231 -0.04876 277 SER A CB    
2361 O OG    . SER B 277 ? 1.98208 1.98086 2.16740 -0.13616 -0.09368 -0.06312 277 SER A OG    
2362 N N     . LEU B 278 ? 1.63016 1.62464 1.75438 -0.15897 -0.12386 -0.05596 278 LEU A N     
2363 C CA    . LEU B 278 ? 1.57172 1.55598 1.66697 -0.16943 -0.13384 -0.06699 278 LEU A CA    
2364 C C     . LEU B 278 ? 1.56803 1.54619 1.63969 -0.16833 -0.12187 -0.08428 278 LEU A C     
2365 O O     . LEU B 278 ? 1.83549 1.81962 1.90083 -0.16196 -0.10809 -0.08440 278 LEU A O     
2366 C CB    . LEU B 278 ? 1.54751 1.53500 1.62512 -0.17493 -0.14123 -0.05839 278 LEU A CB    
2367 C CG    . LEU B 278 ? 1.76996 1.74958 1.83205 -0.18730 -0.15973 -0.05943 278 LEU A CG    
2368 C CD1   . LEU B 278 ? 1.66012 1.64528 1.70989 -0.19106 -0.16552 -0.04794 278 LEU A CD1   
2369 C CD2   . LEU B 278 ? 1.83182 1.79883 1.86232 -0.19416 -0.16004 -0.07827 278 LEU A CD2   
2370 N N     . GLY B 279 ? 1.49580 1.46215 1.55519 -0.17452 -0.12690 -0.09830 279 GLY A N     
2371 C CA    . GLY B 279 ? 1.58315 1.54283 1.62243 -0.17330 -0.11469 -0.11550 279 GLY A CA    
2372 C C     . GLY B 279 ? 1.68036 1.63893 1.68293 -0.17783 -0.11129 -0.12036 279 GLY A C     
2373 O O     . GLY B 279 ? 1.82749 1.77536 1.80339 -0.18717 -0.11838 -0.13063 279 GLY A O     
2374 N N     . SER B 280 ? 1.72350 1.69222 1.72390 -0.17191 -0.10103 -0.11319 280 SER A N     
2375 C CA    . SER B 280 ? 1.73306 1.70170 1.69955 -0.17559 -0.09621 -0.11726 280 SER A CA    
2376 C C     . SER B 280 ? 1.65397 1.61803 1.59894 -0.18694 -0.11223 -0.11378 280 SER A C     
2377 O O     . SER B 280 ? 1.79330 1.74767 1.70727 -0.19475 -0.11385 -0.12600 280 SER A O     
2378 C CB    . SER B 280 ? 1.87194 1.83315 1.81939 -0.17528 -0.08414 -0.13512 280 SER A CB    
2379 O OG    . SER B 280 ? 1.98560 1.95132 1.95522 -0.16512 -0.07054 -0.13722 280 SER A OG    
2380 N N     . GLY B 281 ? 1.46653 1.43704 1.42747 -0.18799 -0.12344 -0.09760 281 GLY A N     
2381 C CA    . GLY B 281 ? 1.49094 1.45846 1.43376 -0.19884 -0.13961 -0.09181 281 GLY A CA    
2382 C C     . GLY B 281 ? 1.73114 1.70995 1.68851 -0.19642 -0.14368 -0.07283 281 GLY A C     
2383 O O     . GLY B 281 ? 1.70003 1.67806 1.65262 -0.20457 -0.15917 -0.06413 281 GLY A O     
2384 N N     . LYS B 282 ? 1.55504 1.54351 1.52956 -0.18593 -0.13052 -0.06648 282 LYS A N     
2385 C CA    . LYS B 282 ? 1.35898 1.35760 1.35034 -0.18250 -0.13266 -0.04866 282 LYS A CA    
2386 C C     . LYS B 282 ? 1.32439 1.32496 1.28862 -0.18745 -0.13403 -0.04490 282 LYS A C     
2387 O O     . LYS B 282 ? 1.21596 1.22110 1.18795 -0.19000 -0.14363 -0.03070 282 LYS A O     
2388 C CB    . LYS B 282 ? 1.33538 1.34187 1.34984 -0.17034 -0.11747 -0.04482 282 LYS A CB    
2389 C CG    . LYS B 282 ? 1.49042 1.49538 1.53099 -0.16521 -0.11487 -0.04832 282 LYS A CG    
2390 C CD    . LYS B 282 ? 1.29341 1.30582 1.35464 -0.15399 -0.10036 -0.04393 282 LYS A CD    
2391 C CE    . LYS B 282 ? 1.47036 1.48101 1.55582 -0.14961 -0.09807 -0.04733 282 LYS A CE    
2392 N NZ    . LYS B 282 ? 1.34799 1.36562 1.45180 -0.13963 -0.08494 -0.04209 282 LYS A NZ    
2393 N N     . SER B 283 ? 1.45486 1.45221 1.38990 -0.18876 -0.12467 -0.05665 283 SER A N     
2394 C CA    . SER B 283 ? 1.46400 1.46382 1.37312 -0.19301 -0.12431 -0.05286 283 SER A CA    
2395 C C     . SER B 283 ? 1.57918 1.57584 1.47718 -0.20424 -0.14325 -0.04523 283 SER A C     
2396 O O     . SER B 283 ? 1.43460 1.43774 1.33743 -0.20483 -0.14819 -0.03098 283 SER A O     
2397 C CB    . SER B 283 ? 1.50426 1.49949 1.38277 -0.19447 -0.11301 -0.06788 283 SER A CB    
2398 O OG    . SER B 283 ? 1.89095 1.88917 1.78175 -0.18450 -0.09656 -0.07442 283 SER A OG    
2399 N N     . LEU B 284 ? 1.59319 1.57983 1.47756 -0.21300 -0.15379 -0.05413 284 LEU A N     
2400 C CA    . LEU B 284 ? 1.63863 1.62122 1.50888 -0.22527 -0.17325 -0.04734 284 LEU A CA    
2401 C C     . LEU B 284 ? 1.55903 1.54913 1.46359 -0.22357 -0.18471 -0.02844 284 LEU A C     
2402 O O     . LEU B 284 ? 1.52047 1.51466 1.42101 -0.22823 -0.19370 -0.01569 284 LEU A O     
2403 C CB    . LEU B 284 ? 1.62677 1.59628 1.48004 -0.23448 -0.18265 -0.06065 284 LEU A CB    
2404 C CG    . LEU B 284 ? 1.58661 1.54961 1.41658 -0.24905 -0.20260 -0.05659 284 LEU A CG    
2405 C CD1   . LEU B 284 ? 1.66001 1.62329 1.45374 -0.25439 -0.19926 -0.05707 284 LEU A CD1   
2406 C CD2   . LEU B 284 ? 1.60272 1.55157 1.41782 -0.25775 -0.21156 -0.07060 284 LEU A CD2   
2407 N N     . ALA B 285 ? 1.51163 1.50377 1.44982 -0.21685 -0.18362 -0.02631 285 ALA A N     
2408 C CA    . ALA B 285 ? 1.51514 1.51424 1.48842 -0.21501 -0.19362 -0.00851 285 ALA A CA    
2409 C C     . ALA B 285 ? 1.53532 1.54449 1.51662 -0.20916 -0.18691 0.00479  285 ALA A C     
2410 O O     . ALA B 285 ? 1.41542 1.42839 1.40587 -0.21335 -0.19901 0.01954  285 ALA A O     
2411 C CB    . ALA B 285 ? 1.37845 1.37895 1.38536 -0.20706 -0.18897 -0.00919 285 ALA A CB    
2412 N N     . TYR B 286 ? 1.46225 1.47523 1.44044 -0.20008 -0.16853 -0.00018 286 TYR A N     
2413 C CA    . TYR B 286 ? 1.30654 1.32821 1.29303 -0.19395 -0.16099 0.01163  286 TYR A CA    
2414 C C     . TYR B 286 ? 1.45193 1.47352 1.41482 -0.20274 -0.17040 0.01783  286 TYR A C     
2415 O O     . TYR B 286 ? 1.50102 1.52782 1.47984 -0.20338 -0.17808 0.03352  286 TYR A O     
2416 C CB    . TYR B 286 ? 1.41319 1.43735 1.39268 -0.18501 -0.14106 0.00343  286 TYR A CB    
2417 C CG    . TYR B 286 ? 1.52734 1.55218 1.52850 -0.17582 -0.13006 -0.00231 286 TYR A CG    
2418 C CD1   . TYR B 286 ? 1.32514 1.35156 1.35858 -0.17276 -0.13504 0.00479  286 TYR A CD1   
2419 C CD2   . TYR B 286 ? 1.52310 1.54743 1.51354 -0.17031 -0.11468 -0.01389 286 TYR A CD2   
2420 C CE1   . TYR B 286 ? 1.22681 1.25394 1.27948 -0.16480 -0.12519 0.00035  286 TYR A CE1   
2421 C CE2   . TYR B 286 ? 1.46310 1.48822 1.47347 -0.16236 -0.10534 -0.01813 286 TYR A CE2   
2422 C CZ    . TYR B 286 ? 1.32582 1.35222 1.36664 -0.15969 -0.11062 -0.01100 286 TYR A CZ    
2423 O OH    . TYR B 286 ? 1.53373 1.56095 1.59374 -0.15226 -0.10165 -0.01447 286 TYR A OH    
2424 N N     . LEU B 287 ? 1.48080 1.49649 1.40703 -0.20951 -0.16965 0.00615  287 LEU A N     
2425 C CA    . LEU B 287 ? 1.56966 1.58546 1.47049 -0.21811 -0.17750 0.01220  287 LEU A CA    
2426 C C     . LEU B 287 ? 1.66028 1.67405 1.56709 -0.22817 -0.19954 0.02313  287 LEU A C     
2427 O O     . LEU B 287 ? 1.67269 1.69127 1.58342 -0.23112 -0.20745 0.03776  287 LEU A O     
2428 C CB    . LEU B 287 ? 1.51647 1.52607 1.37596 -0.22362 -0.17135 -0.00266 287 LEU A CB    
2429 C CG    . LEU B 287 ? 1.71901 1.71783 1.55980 -0.23025 -0.17547 -0.01846 287 LEU A CG    
2430 C CD1   . LEU B 287 ? 1.80195 1.79389 1.61628 -0.24486 -0.19364 -0.01674 287 LEU A CD1   
2431 C CD2   . LEU B 287 ? 1.63079 1.62631 1.44947 -0.22666 -0.15779 -0.03549 287 LEU A CD2   
2432 N N     . LEU B 288 ? 1.57276 1.57962 1.48171 -0.23326 -0.20933 0.01670  288 LEU A N     
2433 C CA    . LEU B 288 ? 1.47385 1.47816 1.38806 -0.24396 -0.23190 0.02692  288 LEU A CA    
2434 C C     . LEU B 288 ? 1.55276 1.56696 1.50580 -0.23884 -0.23664 0.04719  288 LEU A C     
2435 O O     . LEU B 288 ? 1.66816 1.68448 1.62002 -0.24622 -0.25074 0.06059  288 LEU A O     
2436 C CB    . LEU B 288 ? 1.67221 1.66818 1.59067 -0.24816 -0.24024 0.01756  288 LEU A CB    
2437 C CG    . LEU B 288 ? 1.61463 1.59832 1.49199 -0.25693 -0.24095 -0.00115 288 LEU A CG    
2438 C CD1   . LEU B 288 ? 1.56436 1.53933 1.44987 -0.26109 -0.25045 -0.00915 288 LEU A CD1   
2439 C CD2   . LEU B 288 ? 1.61054 1.59030 1.45263 -0.26996 -0.25336 0.00210  288 LEU A CD2   
2440 N N     . ALA B 289 ? 1.39433 1.41410 1.38013 -0.22673 -0.22478 0.04940  289 ALA A N     
2441 C CA    . ALA B 289 ? 1.37456 1.40310 1.39907 -0.22101 -0.22716 0.06789  289 ALA A CA    
2442 C C     . ALA B 289 ? 1.56752 1.60154 1.58488 -0.21974 -0.22318 0.07757  289 ALA A C     
2443 O O     . ALA B 289 ? 1.59102 1.62946 1.62587 -0.22256 -0.23435 0.09412  289 ALA A O     
2444 C CB    . ALA B 289 ? 1.35089 1.38330 1.40572 -0.20834 -0.21253 0.06638  289 ALA A CB    
2445 N N     . ALA B 290 ? 1.58357 1.61724 1.57685 -0.21584 -0.20799 0.06778  290 ALA A N     
2446 C CA    . ALA B 290 ? 1.57968 1.61829 1.56611 -0.21412 -0.20288 0.07628  290 ALA A CA    
2447 C C     . ALA B 290 ? 1.54993 1.58684 1.51620 -0.22683 -0.22029 0.08418  290 ALA A C     
2448 O O     . ALA B 290 ? 1.42576 1.46783 1.40832 -0.22750 -0.22719 0.10053  290 ALA A O     
2449 C CB    . ALA B 290 ? 1.60825 1.64613 1.57090 -0.20896 -0.18475 0.06330  290 ALA A CB    
2450 N N     . LEU B 291 ? 1.50580 1.53526 1.43705 -0.23678 -0.22678 0.07283  291 LEU A N     
2451 C CA    . LEU B 291 ? 1.56419 1.59115 1.47083 -0.25013 -0.24347 0.07968  291 LEU A CA    
2452 C C     . LEU B 291 ? 1.76772 1.79572 1.70009 -0.25631 -0.26434 0.09456  291 LEU A C     
2453 O O     . LEU B 291 ? 1.82943 1.85925 1.75786 -0.26447 -0.27845 0.10811  291 LEU A O     
2454 C CB    . LEU B 291 ? 1.56687 1.58444 1.42869 -0.25958 -0.24473 0.06323  291 LEU A CB    
2455 C CG    . LEU B 291 ? 1.74527 1.75428 1.60351 -0.26365 -0.25070 0.05073  291 LEU A CG    
2456 C CD1   . LEU B 291 ? 2.04093 2.04476 1.89192 -0.27789 -0.27520 0.05802  291 LEU A CD1   
2457 C CD2   . LEU B 291 ? 1.73153 1.73299 1.55414 -0.26437 -0.23776 0.02974  291 LEU A CD2   
2458 N N     . MET B 292 ? 1.61592 1.64304 1.57456 -0.25279 -0.26649 0.09269  292 MET A N     
2459 C CA    . MET B 292 ? 1.65754 1.68676 1.64606 -0.25788 -0.28587 0.10821  292 MET A CA    
2460 C C     . MET B 292 ? 1.68984 1.72911 1.71455 -0.24976 -0.28245 0.12656  292 MET A C     
2461 O O     . MET B 292 ? 1.90652 1.94883 1.94379 -0.25642 -0.29879 0.14317  292 MET A O     
2462 C CB    . MET B 292 ? 1.54810 1.57448 1.55873 -0.25555 -0.28812 0.10250  292 MET A CB    
2463 C CG    . MET B 292 ? 1.61049 1.63692 1.64325 -0.26429 -0.31112 0.11606  292 MET A CG    
2464 S SD    . MET B 292 ? 1.45253 1.47082 1.44400 -0.28396 -0.33480 0.11704  292 MET A SD    
2465 C CE    . MET B 292 ? 1.81860 1.84209 1.85219 -0.29028 -0.35947 0.14060  292 MET A CE    
2466 N N     . TYR B 293 ? 1.55250 1.59622 1.59273 -0.23622 -0.26201 0.12364  293 TYR A N     
2467 C CA    . TYR B 293 ? 1.58741 1.63928 1.65878 -0.22834 -0.25682 0.13976  293 TYR A CA    
2468 C C     . TYR B 293 ? 1.73587 1.78863 1.78658 -0.23607 -0.26500 0.14831  293 TYR A C     
2469 O O     . TYR B 293 ? 1.81872 1.87573 1.89121 -0.23934 -0.27754 0.16609  293 TYR A O     
2470 C CB    . TYR B 293 ? 1.46888 1.52315 1.54761 -0.21435 -0.23280 0.13207  293 TYR A CB    
2471 C CG    . TYR B 293 ? 1.36162 1.42265 1.47786 -0.20398 -0.22414 0.14566  293 TYR A CG    
2472 C CD1   . TYR B 293 ? 1.47843 1.54358 1.63241 -0.20410 -0.23477 0.16174  293 TYR A CD1   
2473 C CD2   . TYR B 293 ? 1.36272 1.42552 1.47691 -0.19415 -0.20492 0.14217  293 TYR A CD2   
2474 C CE1   . TYR B 293 ? 1.66737 1.73789 1.85557 -0.19434 -0.22531 0.17342  293 TYR A CE1   
2475 C CE2   . TYR B 293 ? 1.26705 1.33446 1.41327 -0.18488 -0.19614 0.15337  293 TYR A CE2   
2476 C CZ    . TYR B 293 ? 1.48320 1.55432 1.66645 -0.18476 -0.20573 0.16877  293 TYR A CZ    
2477 O OH    . TYR B 293 ? 1.56447 1.63943 1.77943 -0.17539 -0.19572 0.17928  293 TYR A OH    
2478 N N     . ASN B 294 ? 1.66323 1.71188 1.67272 -0.23978 -0.25907 0.13622  294 ASN A N     
2479 C CA    . ASN B 294 ? 1.87091 1.92018 1.85659 -0.24767 -0.26593 0.14362  294 ASN A CA    
2480 C C     . ASN B 294 ? 1.95389 2.00244 1.94200 -0.26068 -0.29101 0.15727  294 ASN A C     
2481 O O     . ASN B 294 ? 1.94438 1.99845 1.95373 -0.26137 -0.29879 0.17540  294 ASN A O     
2482 C CB    . ASN B 294 ? 1.97720 2.02090 1.91549 -0.25221 -0.25851 0.12721  294 ASN A CB    
2483 C CG    . ASN B 294 ? 2.11844 2.16087 2.02690 -0.26436 -0.27069 0.13394  294 ASN A CG    
2484 O OD1   . ASN B 294 ? 2.07229 2.11999 1.98925 -0.26326 -0.27110 0.14732  294 ASN A OD1   
2485 N ND2   . ASN B 294 ? 2.20698 2.24196 2.08004 -0.27623 -0.28056 0.12491  294 ASN A ND2   
2486 N N     . ILE B 295 ? 1.78160 1.82313 1.74944 -0.27074 -0.30337 0.14893  295 ILE A N     
2487 C CA    . ILE B 295 ? 1.83077 1.87041 1.79588 -0.28512 -0.32922 0.16130  295 ILE A CA    
2488 C C     . ILE B 295 ? 1.82905 1.87640 1.84574 -0.28106 -0.33801 0.18146  295 ILE A C     
2489 O O     . ILE B 295 ? 1.93605 1.98675 1.96040 -0.28827 -0.35350 0.19893  295 ILE A O     
2490 C CB    . ILE B 295 ? 1.91655 1.94660 1.85920 -0.29458 -0.33956 0.14795  295 ILE A CB    
2491 C CG1   . ILE B 295 ? 1.91340 1.93523 1.80295 -0.30034 -0.33228 0.12954  295 ILE A CG1   
2492 C CG2   . ILE B 295 ? 2.16184 2.19022 2.11209 -0.30814 -0.36717 0.16185  295 ILE A CG2   
2493 C CD1   . ILE B 295 ? 2.13790 2.14899 2.00566 -0.30693 -0.33690 0.11251  295 ILE A CD1   
2494 N N     . GLU B 296 ? 1.84601 1.89627 1.89730 -0.26975 -0.32770 0.17956  296 GLU A N     
2495 C CA    . GLU B 296 ? 1.99634 2.05382 2.09905 -0.26545 -0.33475 0.19823  296 GLU A CA    
2496 C C     . GLU B 296 ? 1.99446 2.05928 2.11888 -0.25552 -0.32234 0.20974  296 GLU A C     
2497 O O     . GLU B 296 ? 2.06747 2.13652 2.22490 -0.24265 -0.30756 0.21127  296 GLU A O     
2498 C CB    . GLU B 296 ? 1.88060 1.93799 2.01047 -0.25774 -0.32816 0.19178  296 GLU A CB    
2499 C CG    . GLU B 296 ? 1.90126 1.96511 2.08243 -0.25584 -0.33847 0.21038  296 GLU A CG    
2500 C CD    . GLU B 296 ? 2.05277 2.11631 2.23687 -0.27047 -0.36626 0.22492  296 GLU A CD    
2501 O OE1   . GLU B 296 ? 2.15284 2.20911 2.31241 -0.28182 -0.38052 0.21690  296 GLU A OE1   
2502 O OE2   . GLU B 296 ? 1.98865 2.05879 2.19971 -0.27076 -0.37383 0.24436  296 GLU A OE2   
2503 N N     . THR B 297 ? 1.90404 1.96965 2.00928 -0.26145 -0.32762 0.21708  297 THR A N     
2504 C CA    . THR B 297 ? 2.03738 2.10914 2.16366 -0.25304 -0.31753 0.22897  297 THR A CA    
2505 C C     . THR B 297 ? 1.93448 2.00710 2.06973 -0.23776 -0.29168 0.21787  297 THR A C     
2506 O O     . THR B 297 ? 1.73862 1.81613 1.90950 -0.22770 -0.28243 0.22786  297 THR A O     
2507 C CB    . THR B 297 ? 2.03171 2.10972 2.20504 -0.25318 -0.33057 0.25134  297 THR A CB    
2508 O OG1   . THR B 297 ? 1.99683 2.07681 2.20544 -0.24412 -0.32338 0.25000  297 THR A OG1   
2509 C CG2   . THR B 297 ? 1.96864 2.04559 2.13538 -0.26919 -0.35846 0.26259  297 THR A CG2   
2510 N N     . GLY B 298 ? 1.80555 1.87321 1.90975 -0.23617 -0.28021 0.19801  298 GLY A N     
2511 C CA    . GLY B 298 ? 1.71508 1.78322 1.82606 -0.22238 -0.25646 0.18699  298 GLY A CA    
2512 C C     . GLY B 298 ? 1.91819 1.98665 2.00842 -0.21853 -0.24280 0.18368  298 GLY A C     
2513 O O     . GLY B 298 ? 1.81948 1.88826 1.89244 -0.22643 -0.25201 0.19101  298 GLY A O     
2514 N N     . LYS B 299 ? 1.65626 1.72456 1.74783 -0.20728 -0.22208 0.17342  299 LYS A N     
2515 C CA    . LYS B 299 ? 1.68335 1.75201 1.75841 -0.20295 -0.20842 0.17081  299 LYS A CA    
2516 C C     . LYS B 299 ? 1.75713 1.82237 1.80383 -0.19945 -0.19345 0.15119  299 LYS A C     
2517 O O     . LYS B 299 ? 1.68729 1.74931 1.72218 -0.20268 -0.19642 0.14010  299 LYS A O     
2518 C CB    . LYS B 299 ? 1.80272 1.87470 1.91274 -0.19163 -0.19683 0.18042  299 LYS A CB    
2519 C CG    . LYS B 299 ? 1.94957 2.02131 2.08068 -0.18076 -0.18261 0.17327  299 LYS A CG    
2520 C CD    . LYS B 299 ? 1.93453 2.00793 2.09388 -0.16947 -0.16823 0.18028  299 LYS A CD    
2521 C CE    . LYS B 299 ? 1.83542 1.90769 2.00603 -0.15957 -0.15252 0.17078  299 LYS A CE    
2522 N NZ    . LYS B 299 ? 1.81693 1.88623 1.95492 -0.15871 -0.14231 0.15380  299 LYS A NZ    
2523 N N     . HIS B 300 ? 1.86764 1.93337 1.90520 -0.19322 -0.17825 0.14749  300 HIS A N     
2524 C CA    . HIS B 300 ? 1.78470 1.84793 1.79748 -0.18953 -0.16342 0.13004  300 HIS A CA    
2525 C C     . HIS B 300 ? 1.61467 1.67700 1.64505 -0.18189 -0.15521 0.12172  300 HIS A C     
2526 O O     . HIS B 300 ? 1.54689 1.61130 1.61042 -0.17472 -0.15194 0.12963  300 HIS A O     
2527 C CB    . HIS B 300 ? 1.49332 1.55776 1.50066 -0.18357 -0.14940 0.13049  300 HIS A CB    
2528 C CG    . HIS B 300 ? 1.67359 1.74033 1.71367 -0.17673 -0.14642 0.14405  300 HIS A CG    
2529 N ND1   . HIS B 300 ? 1.75842 1.82526 1.82582 -0.16660 -0.13579 0.14368  300 HIS A ND1   
2530 C CD2   . HIS B 300 ? 1.68429 1.75287 1.73512 -0.17872 -0.15266 0.15849  300 HIS A CD2   
2531 C CE1   . HIS B 300 ? 1.77856 1.84678 1.87140 -0.16240 -0.13465 0.15673  300 HIS A CE1   
2532 N NE2   . HIS B 300 ? 1.88986 1.95920 1.97412 -0.16945 -0.14487 0.16593  300 HIS A NE2   
2533 N N     . VAL B 301 ? 1.41526 1.47443 1.42467 -0.18341 -0.15160 0.10643  301 VAL A N     
2534 C CA    . VAL B 301 ? 1.43493 1.49314 1.45979 -0.17612 -0.14309 0.09787  301 VAL A CA    
2535 C C     . VAL B 301 ? 1.56606 1.62278 1.57008 -0.17147 -0.12707 0.08320  301 VAL A C     
2536 O O     . VAL B 301 ? 1.63147 1.68629 1.60441 -0.17743 -0.12755 0.07550  301 VAL A O     
2537 C CB    . VAL B 301 ? 1.53847 1.59379 1.56425 -0.18243 -0.15574 0.09383  301 VAL A CB    
2538 C CG1   . VAL B 301 ? 1.44810 1.50348 1.49900 -0.17472 -0.14910 0.08993  301 VAL A CG1   
2539 C CG2   . VAL B 301 ? 1.77591 1.83214 1.81176 -0.19089 -0.17515 0.10760  301 VAL A CG2   
2540 N N     . MET B 302 ? 1.50217 1.55974 1.52266 -0.16156 -0.11349 0.07994  302 MET A N     
2541 C CA    . MET B 302 ? 1.43487 1.49151 1.43890 -0.15687 -0.09859 0.06722  302 MET A CA    
2542 C C     . MET B 302 ? 1.42165 1.47600 1.42835 -0.15517 -0.09622 0.05584  302 MET A C     
2543 O O     . MET B 302 ? 1.51031 1.56433 1.53746 -0.15533 -0.10365 0.05961  302 MET A O     
2544 C CB    . MET B 302 ? 1.36316 1.42161 1.38167 -0.14741 -0.08493 0.07124  302 MET A CB    
2545 C CG    . MET B 302 ? 1.53575 1.59397 1.53435 -0.14452 -0.07195 0.06207  302 MET A CG    
2546 S SD    . MET B 302 ? 1.74233 1.80093 1.70890 -0.15270 -0.07581 0.06170  302 MET A SD    
2547 C CE    . MET B 302 ? 1.56395 1.62413 1.54043 -0.14772 -0.06907 0.07292  302 MET A CE    
2548 N N     . ILE B 303 ? 1.18725 1.24019 1.17564 -0.15366 -0.08639 0.04298  303 ILE A N     
2549 C CA    . ILE B 303 ? 1.20397 1.25458 1.19702 -0.15117 -0.08281 0.03204  303 ILE A CA    
2550 C C     . ILE B 303 ? 1.14307 1.19423 1.12710 -0.14529 -0.06730 0.02255  303 ILE A C     
2551 O O     . ILE B 303 ? 1.24193 1.29248 1.20102 -0.14861 -0.06385 0.01557  303 ILE A O     
2552 C CB    . ILE B 303 ? 1.21887 1.26504 1.19548 -0.16003 -0.09382 0.02428  303 ILE A CB    
2553 C CG1   . ILE B 303 ? 1.30717 1.35017 1.28880 -0.15753 -0.08988 0.01252  303 ILE A CG1   
2554 C CG2   . ILE B 303 ? 1.34623 1.39084 1.28907 -0.16696 -0.09439 0.01884  303 ILE A CG2   
2555 C CD1   . ILE B 303 ? 1.67511 1.71218 1.64252 -0.16623 -0.10104 0.00453  303 ILE A CD1   
2556 N N     . SER B 304 ? 1.17082 1.22322 1.17484 -0.13712 -0.05841 0.02308  304 SER A N     
2557 C CA    . SER B 304 ? 1.06124 1.11433 1.05898 -0.13171 -0.04465 0.01523  304 SER A CA    
2558 C C     . SER B 304 ? 1.00672 1.05734 1.00153 -0.13201 -0.04301 0.00287  304 SER A C     
2559 O O     . SER B 304 ? 1.10723 1.15574 1.11314 -0.13377 -0.05056 0.00219  304 SER A O     
2560 C CB    . SER B 304 ? 1.10358 1.15849 1.12063 -0.12369 -0.03596 0.02164  304 SER A CB    
2561 O OG    . SER B 304 ? 1.25423 1.30911 1.27316 -0.11875 -0.02594 0.01383  304 SER A OG    
2562 N N     . THR B 305 ? 1.09792 1.14871 1.08042 -0.13009 -0.03321 -0.00642 305 THR A N     
2563 C CA    . THR B 305 ? 1.04756 1.09554 1.02941 -0.13007 -0.03119 -0.01834 305 THR A CA    
2564 C C     . THR B 305 ? 1.17160 1.22159 1.15858 -0.12339 -0.01833 -0.02291 305 THR A C     
2565 O O     . THR B 305 ? 1.17652 1.22899 1.15254 -0.12228 -0.01138 -0.02238 305 THR A O     
2566 C CB    . THR B 305 ? 1.13925 1.18438 1.09441 -0.13673 -0.03258 -0.02829 305 THR A CB    
2567 O OG1   . THR B 305 ? 1.37007 1.41859 1.31195 -0.13565 -0.02460 -0.02692 305 THR A OG1   
2568 C CG2   . THR B 305 ? 1.17605 1.21830 1.12030 -0.14507 -0.04604 -0.02535 305 THR A CG2   
2569 N N     . ASN B 306 ? 1.16376 1.21261 1.16681 -0.11972 -0.01611 -0.02706 306 ASN A N     
2570 C CA    . ASN B 306 ? 1.13583 1.18668 1.14605 -0.11361 -0.00494 -0.03047 306 ASN A CA    
2571 C C     . ASN B 306 ? 1.19684 1.24767 1.18906 -0.11510 0.00177  -0.04080 306 ASN A C     
2572 O O     . ASN B 306 ? 1.31821 1.37226 1.30773 -0.11198 0.01011  -0.03979 306 ASN A O     
2573 C CB    . ASN B 306 ? 0.91480 0.96399 0.94478 -0.11044 -0.00487 -0.03381 306 ASN A CB    
2574 C CG    . ASN B 306 ? 1.02882 1.07979 1.06385 -0.10546 0.00552  -0.03838 306 ASN A CG    
2575 O OD1   . ASN B 306 ? 1.15179 1.20584 1.18130 -0.10314 0.01240  -0.03555 306 ASN A OD1   
2576 N ND2   . ASN B 306 ? 1.20507 1.25395 1.25140 -0.10407 0.00620  -0.04502 306 ASN A ND2   
2577 N N     . THR B 307 ? 1.31468 1.36160 1.29430 -0.12019 -0.00194 -0.05016 307 THR A N     
2578 C CA    . THR B 307 ? 1.27758 1.32410 1.23893 -0.12196 0.00537  -0.06037 307 THR A CA    
2579 C C     . THR B 307 ? 1.41748 1.46308 1.35421 -0.12886 0.00088  -0.06006 307 THR A C     
2580 O O     . THR B 307 ? 1.36103 1.40708 1.29766 -0.13140 -0.00757 -0.05072 307 THR A O     
2581 C CB    . THR B 307 ? 1.28523 1.32694 1.24959 -0.12237 0.00663  -0.07259 307 THR A CB    
2582 O OG1   . THR B 307 ? 1.62721 1.66336 1.58221 -0.12896 -0.00410 -0.07511 307 THR A OG1   
2583 C CG2   . THR B 307 ? 1.43495 1.47716 1.42588 -0.11631 0.00856  -0.07140 307 THR A CG2   
2584 N N     . LYS B 308 ? 1.59041 1.63479 1.50759 -0.13188 0.00654  -0.06946 308 LYS A N     
2585 C CA    . LYS B 308 ? 1.55947 1.60314 1.45057 -0.13897 0.00315  -0.06899 308 LYS A CA    
2586 C C     . LYS B 308 ? 1.57807 1.61472 1.45093 -0.14533 0.00068  -0.08121 308 LYS A C     
2587 O O     . LYS B 308 ? 1.58561 1.62002 1.43572 -0.15270 -0.00492 -0.08093 308 LYS A O     
2588 C CB    . LYS B 308 ? 1.36734 1.41636 1.24905 -0.13723 0.01334  -0.06753 308 LYS A CB    
2589 C CG    . LYS B 308 ? 1.55067 1.60497 1.44427 -0.13309 0.01368  -0.05483 308 LYS A CG    
2590 C CD    . LYS B 308 ? 1.85518 1.91454 1.74810 -0.12936 0.02484  -0.05429 308 LYS A CD    
2591 C CE    . LYS B 308 ? 1.84738 1.90773 1.75674 -0.12339 0.03291  -0.05996 308 LYS A CE    
2592 N NZ    . LYS B 308 ? 1.92611 1.99160 1.83719 -0.12007 0.04214  -0.05768 308 LYS A NZ    
2593 N N     . LEU B 309 ? 1.52016 1.55291 1.40230 -0.14284 0.00462  -0.09146 309 LEU A N     
2594 C CA    . LEU B 309 ? 1.68448 1.70868 1.54949 -0.14893 0.00245  -0.10433 309 LEU A CA    
2595 C C     . LEU B 309 ? 1.62852 1.64794 1.48801 -0.15588 -0.01349 -0.09993 309 LEU A C     
2596 O O     . LEU B 309 ? 1.81769 1.83195 1.65097 -0.16417 -0.01836 -0.10438 309 LEU A O     
2597 C CB    . LEU B 309 ? 1.74672 1.76730 1.62819 -0.14424 0.00857  -0.11467 309 LEU A CB    
2598 C CG    . LEU B 309 ? 1.77660 1.80200 1.66667 -0.13746 0.02369  -0.11865 309 LEU A CG    
2599 C CD1   . LEU B 309 ? 1.68174 1.70277 1.58875 -0.13349 0.02858  -0.12878 309 LEU A CD1   
2600 C CD2   . LEU B 309 ? 1.49165 1.51777 1.35655 -0.14075 0.03247  -0.12426 309 LEU A CD2   
2601 N N     . LEU B 310 ? 1.55898 1.58018 1.44238 -0.15287 -0.02127 -0.09090 310 LEU A N     
2602 C CA    . LEU B 310 ? 1.82085 1.83864 1.70361 -0.15919 -0.03715 -0.08464 310 LEU A CA    
2603 C C     . LEU B 310 ? 1.74237 1.76318 1.60661 -0.16455 -0.04236 -0.07559 310 LEU A C     
2604 O O     . LEU B 310 ? 1.84587 1.86165 1.69151 -0.17345 -0.05307 -0.07625 310 LEU A O     
2605 C CB    . LEU B 310 ? 1.71900 1.74010 1.63377 -0.15365 -0.04192 -0.07475 310 LEU A CB    
2606 C CG    . LEU B 310 ? 1.78316 1.80399 1.72034 -0.14637 -0.03434 -0.08042 310 LEU A CG    
2607 C CD1   . LEU B 310 ? 1.57458 1.59985 1.54151 -0.14081 -0.03759 -0.06860 310 LEU A CD1   
2608 C CD2   . LEU B 310 ? 1.84094 1.85275 1.77399 -0.15028 -0.03770 -0.09341 310 LEU A CD2   
2609 N N     . GLN B 311 ? 1.61057 1.63887 1.47942 -0.15967 -0.03528 -0.06743 311 GLN A N     
2610 C CA    . GLN B 311 ? 1.66858 1.70013 1.52249 -0.16414 -0.03972 -0.05778 311 GLN A CA    
2611 C C     . GLN B 311 ? 1.61110 1.63784 1.43148 -0.17293 -0.04067 -0.06613 311 GLN A C     
2612 O O     . GLN B 311 ? 1.66793 1.69205 1.47449 -0.18107 -0.05289 -0.06125 311 GLN A O     
2613 C CB    . GLN B 311 ? 1.56307 1.60189 1.42400 -0.15733 -0.02867 -0.05201 311 GLN A CB    
2614 C CG    . GLN B 311 ? 1.53724 1.57966 1.38410 -0.16097 -0.03100 -0.04246 311 GLN A CG    
2615 C CD    . GLN B 311 ? 1.54068 1.58935 1.39738 -0.15417 -0.02127 -0.03618 311 GLN A CD    
2616 O OE1   . GLN B 311 ? 1.52760 1.57826 1.38200 -0.15040 -0.00951 -0.04267 311 GLN A OE1   
2617 N NE2   . GLN B 311 ? 1.54660 1.59805 1.41514 -0.15266 -0.02620 -0.02337 311 GLN A NE2   
2618 N N     . SER B 312 ? 1.54471 1.57014 1.35315 -0.17149 -0.02817 -0.07816 312 SER A N     
2619 C CA    . SER B 312 ? 1.70282 1.72335 1.47771 -0.17958 -0.02653 -0.08699 312 SER A CA    
2620 C C     . SER B 312 ? 1.77691 1.78760 1.54005 -0.18752 -0.03802 -0.09401 312 SER A C     
2621 O O     . SER B 312 ? 1.94143 1.94857 1.67998 -0.19696 -0.04702 -0.09210 312 SER A O     
2622 C CB    . SER B 312 ? 1.82630 1.84725 1.59500 -0.17564 -0.00984 -0.09869 312 SER A CB    
2623 O OG    . SER B 312 ? 1.85978 1.88966 1.63931 -0.16906 -0.00046 -0.09163 312 SER A OG    
2624 N N     . GLN B 313 ? 1.69143 1.69769 1.47186 -0.18422 -0.03856 -0.10109 313 GLN A N     
2625 C CA    . GLN B 313 ? 1.79824 1.79383 1.56744 -0.19200 -0.04929 -0.10926 313 GLN A CA    
2626 C C     . GLN B 313 ? 1.75335 1.74814 1.51407 -0.20064 -0.06719 -0.09772 313 GLN A C     
2627 O O     . GLN B 313 ? 1.77809 1.76550 1.50930 -0.21087 -0.07408 -0.10272 313 GLN A O     
2628 C CB    . GLN B 313 ? 1.82325 1.81620 1.62068 -0.18639 -0.05018 -0.11335 313 GLN A CB    
2629 C CG    . GLN B 313 ? 1.81551 1.79673 1.60399 -0.19396 -0.06084 -0.12265 313 GLN A CG    
2630 C CD    . GLN B 313 ? 1.93029 1.91124 1.73143 -0.19835 -0.07939 -0.11098 313 GLN A CD    
2631 O OE1   . GLN B 313 ? 1.90016 1.88975 1.71807 -0.19531 -0.08381 -0.09573 313 GLN A OE1   
2632 N NE2   . GLN B 313 ? 1.81041 1.78104 1.60447 -0.20563 -0.09031 -0.11807 313 GLN A NE2   
2633 N N     . LEU B 314 ? 1.69160 1.69346 1.47732 -0.19685 -0.07425 -0.08267 314 LEU A N     
2634 C CA    . LEU B 314 ? 1.76085 1.76247 1.54370 -0.20463 -0.09193 -0.07038 314 LEU A CA    
2635 C C     . LEU B 314 ? 1.74758 1.75247 1.50563 -0.20995 -0.09207 -0.06401 314 LEU A C     
2636 O O     . LEU B 314 ? 1.73274 1.73486 1.47620 -0.21956 -0.10648 -0.05762 314 LEU A O     
2637 C CB    . LEU B 314 ? 1.80500 1.81319 1.62422 -0.19825 -0.09759 -0.05637 314 LEU A CB    
2638 C CG    . LEU B 314 ? 1.72076 1.73858 1.55774 -0.18838 -0.08614 -0.04798 314 LEU A CG    
2639 C CD1   . LEU B 314 ? 1.73183 1.75497 1.56416 -0.19122 -0.09178 -0.03369 314 LEU A CD1   
2640 C CD2   . LEU B 314 ? 1.61139 1.63252 1.48426 -0.17954 -0.08442 -0.04329 314 LEU A CD2   
2641 N N     . LEU B 315 ? 1.86628 1.87679 1.62007 -0.20440 -0.07721 -0.06526 315 LEU A N     
2642 C CA    . LEU B 315 ? 1.88579 1.90041 1.61920 -0.20879 -0.07689 -0.05761 315 LEU A CA    
2643 C C     . LEU B 315 ? 1.86962 1.87778 1.56436 -0.21729 -0.07320 -0.06922 315 LEU A C     
2644 O O     . LEU B 315 ? 1.78287 1.79022 1.45485 -0.22629 -0.08166 -0.06295 315 LEU A O     
2645 C CB    . LEU B 315 ? 1.57738 1.60094 1.32553 -0.19917 -0.06331 -0.05268 315 LEU A CB    
2646 C CG    . LEU B 315 ? 1.48462 1.51406 1.22331 -0.20162 -0.06448 -0.04048 315 LEU A CG    
2647 C CD1   . LEU B 315 ? 1.43549 1.46653 1.18728 -0.20475 -0.08050 -0.02508 315 LEU A CD1   
2648 C CD2   . LEU B 315 ? 1.75039 1.78721 1.50328 -0.19216 -0.05041 -0.03783 315 LEU A CD2   
2649 N N     . GLU B 316 ? 1.86790 1.87141 1.55568 -0.21470 -0.06087 -0.08518 316 GLU A N     
2650 C CA    . GLU B 316 ? 1.85388 1.85124 1.50458 -0.22194 -0.05413 -0.09695 316 GLU A CA    
2651 C C     . GLU B 316 ? 1.83310 1.81759 1.46548 -0.23036 -0.06231 -0.10896 316 GLU A C     
2652 O O     . GLU B 316 ? 1.96519 1.94261 1.56464 -0.23706 -0.05669 -0.12017 316 GLU A O     
2653 C CB    . GLU B 316 ? 1.88539 1.88599 1.53894 -0.21384 -0.03340 -0.10677 316 GLU A CB    
2654 C CG    . GLU B 316 ? 1.95066 1.94682 1.62256 -0.20726 -0.02638 -0.11934 316 GLU A CG    
2655 C CD    . GLU B 316 ? 2.15854 2.15960 1.84013 -0.19829 -0.00692 -0.12622 316 GLU A CD    
2656 O OE1   . GLU B 316 ? 2.22058 2.22874 1.89499 -0.19711 0.00114  -0.12109 316 GLU A OE1   
2657 O OE2   . GLU B 316 ? 2.14807 2.14596 1.84546 -0.19269 -0.00024 -0.13616 316 GLU A OE2   
2658 N N     . LYS B 317 ? 1.91380 1.89491 1.56571 -0.23051 -0.07499 -0.10668 317 LYS A N     
2659 C CA    . LYS B 317 ? 2.02006 1.98790 1.65589 -0.23851 -0.08302 -0.11896 317 LYS A CA    
2660 C C     . LYS B 317 ? 1.86892 1.83449 1.51293 -0.24541 -0.10537 -0.10795 317 LYS A C     
2661 O O     . LYS B 317 ? 1.88511 1.84387 1.50020 -0.25766 -0.11763 -0.10731 317 LYS A O     
2662 C CB    . LYS B 317 ? 1.88783 1.85137 1.54261 -0.23079 -0.07318 -0.13254 317 LYS A CB    
2663 C CG    . LYS B 317 ? 1.89692 1.86504 1.55682 -0.22132 -0.05144 -0.14074 317 LYS A CG    
2664 C CD    . LYS B 317 ? 1.83264 1.79788 1.51790 -0.21305 -0.04369 -0.15099 317 LYS A CD    
2665 C CE    . LYS B 317 ? 1.86444 1.83678 1.56221 -0.20283 -0.02420 -0.15481 317 LYS A CE    
2666 N NZ    . LYS B 317 ? 2.05699 2.02695 1.72422 -0.20628 -0.01155 -0.16408 317 LYS A NZ    
2667 N N     . ASP B 318 ? 1.76187 1.73292 1.44370 -0.23821 -0.11049 -0.09922 318 ASP A N     
2668 C CA    . ASP B 318 ? 1.92693 1.89593 1.62117 -0.24425 -0.13142 -0.08889 318 ASP A CA    
2669 C C     . ASP B 318 ? 1.95776 1.93062 1.63848 -0.25242 -0.14426 -0.07373 318 ASP A C     
2670 O O     . ASP B 318 ? 2.05871 2.02418 1.72156 -0.26424 -0.16083 -0.07233 318 ASP A O     
2671 C CB    . ASP B 318 ? 2.01193 1.98772 1.75046 -0.23423 -0.13240 -0.08062 318 ASP A CB    
2672 C CG    . ASP B 318 ? 2.18019 2.15243 1.93544 -0.22652 -0.12180 -0.09367 318 ASP A CG    
2673 O OD1   . ASP B 318 ? 2.31696 2.28128 2.05042 -0.22832 -0.11259 -0.11004 318 ASP A OD1   
2674 O OD2   . ASP B 318 ? 2.20407 2.18131 1.99434 -0.21884 -0.12255 -0.08717 318 ASP A OD2   
2675 N N     . ILE B 319 ? 1.80894 1.79253 1.49831 -0.24676 -0.13764 -0.06244 319 ILE A N     
2676 C CA    . ILE B 319 ? 1.93305 1.92087 1.61412 -0.25402 -0.15055 -0.04620 319 ILE A CA    
2677 C C     . ILE B 319 ? 1.99790 1.97722 1.63344 -0.26748 -0.15586 -0.05266 319 ILE A C     
2678 O O     . ILE B 319 ? 1.97403 1.94950 1.59983 -0.27831 -0.17479 -0.04478 319 ILE A O     
2679 C CB    . ILE B 319 ? 1.92120 1.92065 1.61630 -0.24577 -0.14070 -0.03488 319 ILE A CB    
2680 C CG1   . ILE B 319 ? 1.66727 1.67411 1.40595 -0.23500 -0.14012 -0.02502 319 ILE A CG1   
2681 C CG2   . ILE B 319 ? 1.87793 1.88020 1.55525 -0.25432 -0.15068 -0.02164 319 ILE A CG2   
2682 C CD1   . ILE B 319 ? 1.85634 1.86284 1.61529 -0.23921 -0.15924 -0.01289 319 ILE A CD1   
2683 N N     . PRO B 320 ? 2.05482 2.03072 1.66209 -0.26778 -0.14044 -0.06630 320 PRO A N     
2684 C CA    . PRO B 320 ? 2.05073 2.01742 1.61310 -0.28087 -0.14456 -0.07339 320 PRO A CA    
2685 C C     . PRO B 320 ? 2.02565 1.97970 1.57541 -0.29114 -0.16035 -0.08013 320 PRO A C     
2686 O O     . PRO B 320 ? 2.09254 2.04147 1.61698 -0.30426 -0.17623 -0.07447 320 PRO A O     
2687 C CB    . PRO B 320 ? 2.12041 2.08504 1.66592 -0.27587 -0.12193 -0.09010 320 PRO A CB    
2688 C CG    . PRO B 320 ? 1.98030 1.95766 1.55737 -0.26204 -0.10840 -0.08348 320 PRO A CG    
2689 C CD    . PRO B 320 ? 1.91641 1.89763 1.53341 -0.25612 -0.11872 -0.07398 320 PRO A CD    
2690 N N     . ALA B 321 ? 2.03531 1.98409 1.60234 -0.28581 -0.15679 -0.09159 321 ALA A N     
2691 C CA    . ALA B 321 ? 2.16860 2.10402 1.72419 -0.29550 -0.17127 -0.09972 321 ALA A CA    
2692 C C     . ALA B 321 ? 2.07479 2.01247 1.64447 -0.30264 -0.19560 -0.08193 321 ALA A C     
2693 O O     . ALA B 321 ? 1.99340 1.92070 1.53912 -0.31611 -0.21219 -0.08343 321 ALA A O     
2694 C CB    . ALA B 321 ? 1.99948 1.93080 1.57855 -0.28691 -0.16303 -0.11257 321 ALA A CB    
2695 N N     . MET B 322 ? 2.03069 1.98116 1.63889 -0.29394 -0.19761 -0.06557 322 MET A N     
2696 C CA    . MET B 322 ? 1.97772 1.93181 1.60483 -0.29956 -0.21974 -0.04695 322 MET A CA    
2697 C C     . MET B 322 ? 2.18004 2.13613 1.78080 -0.30997 -0.22964 -0.03501 322 MET A C     
2698 O O     . MET B 322 ? 2.32715 2.28080 1.92617 -0.32057 -0.25117 -0.02395 322 MET A O     
2699 C CB    . MET B 322 ? 2.02224 1.98899 1.69842 -0.28663 -0.21679 -0.03346 322 MET A CB    
2700 C CG    . MET B 322 ? 2.10319 2.06822 1.80977 -0.27849 -0.21310 -0.04069 322 MET A CG    
2701 S SD    . MET B 322 ? 2.23415 2.19016 1.94921 -0.28899 -0.23750 -0.03852 322 MET A SD    
2702 C CE    . MET B 322 ? 1.98361 1.92172 1.65219 -0.29932 -0.23593 -0.06252 322 MET A CE    
2703 N N     . ASN B 323 ? 2.20329 2.16380 1.78532 -0.30731 -0.21496 -0.03654 323 ASN A N     
2704 C CA    . ASN B 323 ? 2.10141 2.06488 1.66014 -0.31665 -0.22353 -0.02381 323 ASN A CA    
2705 C C     . ASN B 323 ? 2.28385 2.23470 1.80440 -0.33397 -0.24088 -0.02751 323 ASN A C     
2706 O O     . ASN B 323 ? 2.35705 2.30944 1.87731 -0.34339 -0.26099 -0.01133 323 ASN A O     
2707 C CB    . ASN B 323 ? 2.04532 2.01327 1.58431 -0.31244 -0.20403 -0.02823 323 ASN A CB    
2708 C CG    . ASN B 323 ? 2.16144 2.14183 1.73632 -0.29698 -0.18950 -0.02205 323 ASN A CG    
2709 O OD1   . ASN B 323 ? 2.24925 2.23377 1.81436 -0.29168 -0.17229 -0.02650 323 ASN A OD1   
2710 N ND2   . ASN B 323 ? 2.17439 2.16041 1.79040 -0.28982 -0.19577 -0.01212 323 ASN A ND2   
2711 N N     . GLU B 324 ? 2.27060 2.20897 1.76073 -0.33815 -0.23354 -0.04796 324 GLU A N     
2712 C CA    . GLU B 324 ? 2.29077 2.21497 1.73891 -0.35553 -0.24893 -0.05364 324 GLU A CA    
2713 C C     . GLU B 324 ? 2.34091 2.26153 1.80959 -0.36193 -0.27327 -0.04497 324 GLU A C     
2714 O O     . GLU B 324 ? 2.46778 2.38449 1.91742 -0.37616 -0.29406 -0.03466 324 GLU A O     
2715 C CB    . GLU B 324 ? 2.22735 2.13799 1.64115 -0.35755 -0.23410 -0.07864 324 GLU A CB    
2716 C CG    . GLU B 324 ? 2.21628 2.12405 1.65726 -0.34626 -0.22292 -0.09284 324 GLU A CG    
2717 C CD    . GLU B 324 ? 2.33923 2.23445 1.78202 -0.35357 -0.23905 -0.09958 324 GLU A CD    
2718 O OE1   . GLU B 324 ? 2.34471 2.23246 1.76560 -0.36841 -0.26011 -0.09378 324 GLU A OE1   
2719 O OE2   . GLU B 324 ? 2.22510 2.11791 1.69170 -0.34474 -0.23113 -0.11017 324 GLU A OE2   
2720 N N     . ALA B 325 ? 2.27965 2.20191 1.78646 -0.35206 -0.27106 -0.04813 325 ALA A N     
2721 C CA    . ALA B 325 ? 2.19038 2.10936 1.71978 -0.35757 -0.29327 -0.04039 325 ALA A CA    
2722 C C     . ALA B 325 ? 2.33054 2.26106 1.88458 -0.35976 -0.31020 -0.01474 325 ALA A C     
2723 O O     . ALA B 325 ? 2.45255 2.37830 2.00067 -0.37280 -0.33391 -0.00536 325 ALA A O     
2724 C CB    . ALA B 325 ? 2.13764 2.05801 1.70552 -0.34505 -0.28480 -0.04761 325 ALA A CB    
2725 N N     . LEU B 326 ? 2.55955 2.50431 2.14043 -0.34773 -0.29866 -0.00366 326 LEU A N     
2726 C CA    . LEU B 326 ? 2.52998 2.48612 2.13903 -0.34808 -0.31261 0.02093  326 LEU A CA    
2727 C C     . LEU B 326 ? 2.56703 2.52203 2.14009 -0.36131 -0.32321 0.03005  326 LEU A C     
2728 O O     . LEU B 326 ? 2.54148 2.50329 2.13234 -0.36560 -0.33982 0.05081  326 LEU A O     
2729 C CB    . LEU B 326 ? 2.27497 2.24494 1.92161 -0.33116 -0.29567 0.02823  326 LEU A CB    
2730 C CG    . LEU B 326 ? 2.22927 2.20448 1.92526 -0.31962 -0.29400 0.03149  326 LEU A CG    
2731 C CD1   . LEU B 326 ? 2.28035 2.24697 1.97419 -0.31597 -0.28515 0.01151  326 LEU A CD1   
2732 C CD2   . LEU B 326 ? 2.13904 2.12709 1.86643 -0.30473 -0.27825 0.04009  326 LEU A CD2   
2733 N N     . ASN B 327 ? 2.63984 2.58707 2.16609 -0.36700 -0.31309 0.01572  327 ASN A N     
2734 C CA    . ASN B 327 ? 2.64975 2.59531 2.13699 -0.38013 -0.32145 0.02333  327 ASN A CA    
2735 C C     . ASN B 327 ? 2.58172 2.54121 2.08379 -0.37164 -0.31089 0.03683  327 ASN A C     
2736 O O     . ASN B 327 ? 2.63470 2.59461 2.10701 -0.38058 -0.31452 0.04375  327 ASN A O     
2737 C CB    . ASN B 327 ? 2.45104 2.39172 1.93126 -0.39626 -0.35109 0.03687  327 ASN A CB    
2738 C CG    . ASN B 327 ? 2.64368 2.56993 2.11055 -0.40457 -0.36171 0.02317  327 ASN A CG    
2739 O OD1   . ASN B 327 ? 2.71222 2.62585 2.13837 -0.40991 -0.35328 0.00327  327 ASN A OD1   
2740 N ND2   . ASN B 327 ? 2.59181 2.51936 2.09315 -0.40568 -0.37964 0.03332  327 ASN A ND2   
2741 N N     . PHE B 328 ? 2.50908 2.47894 2.05426 -0.35548 -0.29831 0.04031  328 PHE A N     
2742 C CA    . PHE B 328 ? 2.28075 2.26289 1.84089 -0.34654 -0.28670 0.05161  328 PHE A CA    
2743 C C     . PHE B 328 ? 2.16027 2.14739 1.74387 -0.32947 -0.26297 0.04086  328 PHE A C     
2744 O O     . PHE B 328 ? 2.33292 2.31580 1.93009 -0.32412 -0.25872 0.02901  328 PHE A O     
2745 C CB    . PHE B 328 ? 2.20620 2.19805 1.80263 -0.34584 -0.30185 0.07598  328 PHE A CB    
2746 C CG    . PHE B 328 ? 2.44172 2.43755 2.08703 -0.33636 -0.30516 0.08058  328 PHE A CG    
2747 C CD1   . PHE B 328 ? 2.34198 2.34750 2.02534 -0.32061 -0.29046 0.08480  328 PHE A CD1   
2748 C CD2   . PHE B 328 ? 2.60833 2.59803 2.26131 -0.34365 -0.32319 0.08126  328 PHE A CD2   
2749 C CE1   . PHE B 328 ? 2.35761 2.36665 2.08449 -0.31218 -0.29263 0.08930  328 PHE A CE1   
2750 C CE2   . PHE B 328 ? 2.46816 2.46205 2.16673 -0.33501 -0.32561 0.08618  328 PHE A CE2   
2751 C CZ    . PHE B 328 ? 2.37212 2.37577 2.10725 -0.31921 -0.30990 0.09022  328 PHE A CZ    
2752 N N     . LYS B 329 ? 2.12522 2.12092 1.71362 -0.32155 -0.24845 0.04534  329 LYS A N     
2753 C CA    . LYS B 329 ? 2.07661 2.07744 1.68678 -0.30567 -0.22615 0.03635  329 LYS A CA    
2754 C C     . LYS B 329 ? 2.17973 2.19190 1.83144 -0.29554 -0.22506 0.05323  329 LYS A C     
2755 O O     . LYS B 329 ? 2.11532 2.13282 1.76369 -0.29841 -0.22862 0.06683  329 LYS A O     
2756 C CB    . LYS B 329 ? 2.26444 2.26425 1.84201 -0.30485 -0.20748 0.02407  329 LYS A CB    
2757 C CG    . LYS B 329 ? 2.29684 2.30499 1.89460 -0.29027 -0.18638 0.02184  329 LYS A CG    
2758 C CD    . LYS B 329 ? 2.09566 2.10442 1.72386 -0.27788 -0.17611 0.01257  329 LYS A CD    
2759 C CE    . LYS B 329 ? 2.11185 2.12619 1.74721 -0.26621 -0.15419 0.00602  329 LYS A CE    
2760 N NZ    . LYS B 329 ? 1.97957 2.00297 1.62682 -0.26234 -0.15157 0.02063  329 LYS A NZ    
2761 N N     . ILE B 330 ? 2.15621 2.17138 1.84524 -0.28446 -0.22034 0.05252  330 ILE A N     
2762 C CA    . ILE B 330 ? 2.10604 2.13100 1.83379 -0.27379 -0.21623 0.06678  330 ILE A CA    
2763 C C     . ILE B 330 ? 2.07488 2.10381 1.79976 -0.26347 -0.19366 0.05880  330 ILE A C     
2764 O O     . ILE B 330 ? 2.06653 2.09313 1.79193 -0.25672 -0.18034 0.04376  330 ILE A O     
2765 C CB    . ILE B 330 ? 1.81225 1.83879 1.58089 -0.26695 -0.22102 0.07090  330 ILE A CB    
2766 C CG1   . ILE B 330 ? 1.78893 1.82428 1.59519 -0.25503 -0.21322 0.08291  330 ILE A CG1   
2767 C CG2   . ILE B 330 ? 1.94919 1.97020 1.71717 -0.26250 -0.21216 0.05279  330 ILE A CG2   
2768 C CD1   . ILE B 330 ? 1.74266 1.78308 1.55699 -0.25906 -0.22383 0.10238  330 ILE A CD1   
2769 N N     . ASN B 331 ? 2.03022 2.06476 1.75235 -0.26277 -0.19013 0.06880  331 ASN A N     
2770 C CA    . ASN B 331 ? 2.00463 2.04273 1.72148 -0.25434 -0.16967 0.06170  331 ASN A CA    
2771 C C     . ASN B 331 ? 1.95523 1.99578 1.70346 -0.24064 -0.15693 0.05615  331 ASN A C     
2772 O O     . ASN B 331 ? 1.92968 1.97335 1.71147 -0.23537 -0.16208 0.06662  331 ASN A O     
2773 C CB    . ASN B 331 ? 2.11633 2.16011 1.83112 -0.25551 -0.16968 0.07544  331 ASN A CB    
2774 C CG    . ASN B 331 ? 1.89416 1.94193 1.63973 -0.25495 -0.18279 0.09440  331 ASN A CG    
2775 O OD1   . ASN B 331 ? 1.73740 1.78291 1.48560 -0.26288 -0.20043 0.10175  331 ASN A OD1   
2776 N ND2   . ASN B 331 ? 1.85667 1.90997 1.62627 -0.24584 -0.17453 0.10253  331 ASN A ND2   
2777 N N     . ALA B 332 ? 1.87757 1.91670 1.61558 -0.23531 -0.14084 0.04067  332 ALA A N     
2778 C CA    . ALA B 332 ? 1.67831 1.71968 1.44364 -0.22271 -0.12817 0.03513  332 ALA A CA    
2779 C C     . ALA B 332 ? 1.79019 1.83526 1.54878 -0.21618 -0.11021 0.02990  332 ALA A C     
2780 O O     . ALA B 332 ? 1.96044 2.00409 1.68905 -0.22138 -0.10504 0.02287  332 ALA A O     
2781 C CB    . ALA B 332 ? 1.68251 1.71806 1.44723 -0.22251 -0.12783 0.02136  332 ALA A CB    
2782 N N     . LEU B 333 ? 1.73034 1.77972 1.51547 -0.20554 -0.10102 0.03336  333 LEU A N     
2783 C CA    . LEU B 333 ? 1.68928 1.74234 1.47019 -0.19957 -0.08516 0.03001  333 LEU A CA    
2784 C C     . LEU B 333 ? 1.63420 1.68841 1.43871 -0.18840 -0.07362 0.02417  333 LEU A C     
2785 O O     . LEU B 333 ? 1.53618 1.59026 1.36641 -0.18407 -0.07819 0.02917  333 LEU A O     
2786 C CB    . LEU B 333 ? 1.53864 1.59588 1.32413 -0.20000 -0.08766 0.04465  333 LEU A CB    
2787 C CG    . LEU B 333 ? 1.56994 1.63042 1.34110 -0.19868 -0.07564 0.04327  333 LEU A CG    
2788 C CD1   . LEU B 333 ? 1.79295 1.85584 1.55910 -0.20391 -0.08299 0.05751  333 LEU A CD1   
2789 C CD2   . LEU B 333 ? 1.75451 1.81745 1.54545 -0.18774 -0.06215 0.04082  333 LEU A CD2   
2790 N N     . LEU B 334 ? 1.55203 1.60752 1.34862 -0.18418 -0.05931 0.01465  334 LEU A N     
2791 C CA    . LEU B 334 ? 1.50866 1.56545 1.32651 -0.17403 -0.04839 0.00985  334 LEU A CA    
2792 C C     . LEU B 334 ? 1.46146 1.52201 1.29608 -0.16807 -0.04427 0.02059  334 LEU A C     
2793 O O     . LEU B 334 ? 1.59340 1.65659 1.41864 -0.16706 -0.03580 0.02050  334 LEU A O     
2794 C CB    . LEU B 334 ? 1.16478 1.22154 0.96887 -0.17238 -0.03560 -0.00372 334 LEU A CB    
2795 C CG    . LEU B 334 ? 1.40024 1.45648 1.22240 -0.16442 -0.02739 -0.01203 334 LEU A CG    
2796 C CD1   . LEU B 334 ? 1.50317 1.55938 1.31142 -0.16381 -0.01561 -0.02491 334 LEU A CD1   
2797 C CD2   . LEU B 334 ? 1.45352 1.51292 1.29993 -0.15596 -0.02234 -0.00480 334 LEU A CD2   
2798 N N     . ILE B 335 ? 1.47196 1.53232 1.33066 -0.16440 -0.04974 0.02936  335 ILE A N     
2799 C CA    . ILE B 335 ? 1.37495 1.43734 1.25002 -0.15871 -0.04559 0.03934  335 ILE A CA    
2800 C C     . ILE B 335 ? 1.35163 1.41486 1.23314 -0.15085 -0.03165 0.03268  335 ILE A C     
2801 O O     . ILE B 335 ? 1.40266 1.46483 1.29161 -0.14737 -0.02816 0.02461  335 ILE A O     
2802 C CB    . ILE B 335 ? 1.49049 1.55201 1.39089 -0.15640 -0.05357 0.04950  335 ILE A CB    
2803 C CG1   . ILE B 335 ? 1.68467 1.74507 1.58103 -0.16447 -0.06877 0.05391  335 ILE A CG1   
2804 C CG2   . ILE B 335 ? 1.19782 1.26023 1.11125 -0.15249 -0.05081 0.06068  335 ILE A CG2   
2805 C CD1   . ILE B 335 ? 1.56013 1.62154 1.43792 -0.17249 -0.07608 0.06098  335 ILE A CD1   
2806 N N     . LYS B 336 ? 1.49189 1.55674 1.37094 -0.14861 -0.02465 0.03633  336 LYS A N     
2807 C CA    . LYS B 336 ? 1.31056 1.37602 1.19552 -0.14183 -0.01243 0.03127  336 LYS A CA    
2808 C C     . LYS B 336 ? 1.33671 1.40132 1.23386 -0.13760 -0.00935 0.04056  336 LYS A C     
2809 O O     . LYS B 336 ? 1.38448 1.44835 1.28562 -0.13986 -0.01622 0.05038  336 LYS A O     
2810 C CB    . LYS B 336 ? 1.11457 1.18247 0.98004 -0.14400 -0.00493 0.02326  336 LYS A CB    
2811 C CG    . LYS B 336 ? 1.10989 1.17756 0.96421 -0.14679 -0.00452 0.01186  336 LYS A CG    
2812 C CD    . LYS B 336 ? 1.42577 1.49606 1.26563 -0.14727 0.00551  0.00376  336 LYS A CD    
2813 C CE    . LYS B 336 ? 1.50469 1.57370 1.33491 -0.14947 0.00717  -0.00817 336 LYS A CE    
2814 N NZ    . LYS B 336 ? 1.31945 1.39127 1.14004 -0.14881 0.01834  -0.01581 336 LYS A NZ    
2815 N N     . SER B 337 ? 1.16381 1.22807 1.06629 -0.13207 0.00040  0.03763  337 SER A N     
2816 C CA    . SER B 337 ? 1.34641 1.40822 1.25885 -0.12813 0.00418  0.04516  337 SER A CA    
2817 C C     . SER B 337 ? 1.28145 1.34434 1.18050 -0.13203 0.00435  0.04986  337 SER A C     
2818 O O     . SER B 337 ? 1.23385 1.30010 1.11556 -0.13683 0.00424  0.04576  337 SER A O     
2819 C CB    . SER B 337 ? 1.44284 1.50315 1.36310 -0.12206 0.01344  0.04073  337 SER A CB    
2820 O OG    . SER B 337 ? 1.48629 1.54517 1.42169 -0.11826 0.01283  0.03890  337 SER A OG    
2821 N N     . LYS B 338 ? 1.27509 1.33486 1.18214 -0.13002 0.00523  0.05799  338 LYS A N     
2822 C CA    . LYS B 338 ? 1.45605 1.51636 1.35251 -0.13383 0.00465  0.06371  338 LYS A CA    
2823 C C     . LYS B 338 ? 1.31393 1.37709 1.19612 -0.13484 0.01197  0.05723  338 LYS A C     
2824 O O     . LYS B 338 ? 1.25418 1.32073 1.12128 -0.14028 0.01034  0.05828  338 LYS A O     
2825 C CB    . LYS B 338 ? 1.25307 1.30806 1.16289 -0.13031 0.00615  0.07200  338 LYS A CB    
2826 C CG    . LYS B 338 ? 1.30618 1.36083 1.20929 -0.13420 0.00381  0.07979  338 LYS A CG    
2827 C CD    . LYS B 338 ? 1.67717 1.72556 1.59590 -0.13083 0.00425  0.08831  338 LYS A CD    
2828 C CE    . LYS B 338 ? 1.45484 1.50294 1.36850 -0.13508 0.00069  0.09670  338 LYS A CE    
2829 N NZ    . LYS B 338 ? 1.37175 1.41301 1.30192 -0.13158 0.00157  0.10454  338 LYS A NZ    
2830 N N     . SER B 339 ? 1.33274 1.39484 1.21999 -0.13007 0.01957  0.05135  339 SER A N     
2831 C CA    . SER B 339 ? 1.29021 1.35534 1.16736 -0.13071 0.02652  0.04606  339 SER A CA    
2832 C C     . SER B 339 ? 1.21056 1.28132 1.07378 -0.13507 0.02607  0.03969  339 SER A C     
2833 O O     . SER B 339 ? 1.28270 1.35699 1.13432 -0.13807 0.02976  0.03868  339 SER A O     
2834 C CB    . SER B 339 ? 1.47301 1.53621 1.35914 -0.12533 0.03316  0.04123  339 SER A CB    
2835 O OG    . SER B 339 ? 1.50162 1.55851 1.39760 -0.12182 0.03453  0.04655  339 SER A OG    
2836 N N     . ASP B 340 ? 1.28523 1.35638 1.14955 -0.13556 0.02201  0.03549  340 ASP A N     
2837 C CA    . ASP B 340 ? 1.30438 1.37930 1.15434 -0.13970 0.02235  0.02785  340 ASP A CA    
2838 C C     . ASP B 340 ? 1.43081 1.50805 1.26330 -0.14655 0.01916  0.03225  340 ASP A C     
2839 O O     . ASP B 340 ? 1.58771 1.66853 1.40617 -0.14959 0.02393  0.02677  340 ASP A O     
2840 C CB    . ASP B 340 ? 1.39192 1.46533 1.24588 -0.13971 0.01718  0.02322  340 ASP A CB    
2841 C CG    . ASP B 340 ? 1.37784 1.44957 1.24833 -0.13337 0.02080  0.01840  340 ASP A CG    
2842 O OD1   . ASP B 340 ? 1.23462 1.30825 1.10544 -0.13090 0.02843  0.01171  340 ASP A OD1   
2843 O OD2   . ASP B 340 ? 1.44104 1.50983 1.32494 -0.13102 0.01598  0.02202  340 ASP A OD2   
2844 N N     . TYR B 341 ? 1.42870 1.50405 1.26277 -0.14891 0.01170  0.04210  341 TYR A N     
2845 C CA    . TYR B 341 ? 1.25908 1.33662 1.07662 -0.15609 0.00737  0.04772  341 TYR A CA    
2846 C C     . TYR B 341 ? 1.33599 1.41537 1.15019 -0.15614 0.01354  0.05148  341 TYR A C     
2847 O O     . TYR B 341 ? 1.54923 1.62626 1.37651 -0.15098 0.01764  0.05324  341 TYR A O     
2848 C CB    . TYR B 341 ? 1.35521 1.43025 1.17807 -0.15875 -0.00389 0.05746  341 TYR A CB    
2849 C CG    . TYR B 341 ? 1.56880 1.64223 1.39557 -0.15932 -0.01072 0.05401  341 TYR A CG    
2850 C CD1   . TYR B 341 ? 1.75334 1.82773 1.56262 -0.16627 -0.01655 0.05089  341 TYR A CD1   
2851 C CD2   . TYR B 341 ? 1.27424 1.34477 1.12156 -0.15327 -0.01125 0.05383  341 TYR A CD2   
2852 C CE1   . TYR B 341 ? 1.72112 1.79335 1.53382 -0.16735 -0.02355 0.04763  341 TYR A CE1   
2853 C CE2   . TYR B 341 ? 1.27021 1.33944 1.12257 -0.15397 -0.01779 0.05117  341 TYR A CE2   
2854 C CZ    . TYR B 341 ? 1.33332 1.40327 1.16862 -0.16111 -0.02438 0.04801  341 TYR A CZ    
2855 O OH    . TYR B 341 ? 1.67042 1.73842 1.51063 -0.16234 -0.03163 0.04533  341 TYR A OH    
2856 N N     . ILE B 342 ? 1.49227 1.57535 1.28886 -0.16219 0.01412  0.05281  342 ILE A N     
2857 C CA    . ILE B 342 ? 1.50900 1.59452 1.30239 -0.16281 0.02014  0.05642  342 ILE A CA    
2858 C C     . ILE B 342 ? 1.32937 1.41312 1.12393 -0.16590 0.01348  0.06894  342 ILE A C     
2859 O O     . ILE B 342 ? 1.38026 1.46341 1.16974 -0.17034 0.00459  0.07426  342 ILE A O     
2860 C CB    . ILE B 342 ? 1.40469 1.49578 1.18006 -0.16713 0.02653  0.05073  342 ILE A CB    
2861 C CG1   . ILE B 342 ? 1.01427 1.10850 0.79016 -0.16679 0.03391  0.05330  342 ILE A CG1   
2862 C CG2   . ILE B 342 ? 1.11670 1.20908 0.87291 -0.17512 0.02022  0.05394  342 ILE A CG2   
2863 C CD1   . ILE B 342 ? 1.26253 1.35467 1.05580 -0.15998 0.03876  0.05129  342 ILE A CD1   
2864 N N     . SER B 343 ? 1.37042 1.45297 1.17195 -0.16390 0.01711  0.07369  343 SER A N     
2865 C CA    . SER B 343 ? 1.41991 1.50024 1.22382 -0.16667 0.01154  0.08558  343 SER A CA    
2866 C C     . SER B 343 ? 1.51607 1.60141 1.30551 -0.17221 0.01467  0.08854  343 SER A C     
2867 O O     . SER B 343 ? 1.34478 1.43470 1.12585 -0.17253 0.02223  0.08101  343 SER A O     
2868 C CB    . SER B 343 ? 1.25053 1.32458 1.07179 -0.16111 0.01311  0.08903  343 SER A CB    
2869 O OG    . SER B 343 ? 1.37500 1.44653 1.19906 -0.16374 0.00865  0.10000  343 SER A OG    
2870 N N     . LEU B 344 ? 1.53707 1.62170 1.32525 -0.17626 0.00949  0.09946  344 LEU A N     
2871 C CA    . LEU B 344 ? 1.30794 1.39747 1.08358 -0.18160 0.01278  0.10331  344 LEU A CA    
2872 C C     . LEU B 344 ? 1.55690 1.64448 1.34280 -0.17809 0.01904  0.10400  344 LEU A C     
2873 O O     . LEU B 344 ? 1.42389 1.51393 1.20489 -0.18208 0.02025  0.11020  344 LEU A O     
2874 C CB    . LEU B 344 ? 1.32239 1.41250 1.09101 -0.18835 0.00403  0.11511  344 LEU A CB    
2875 C CG    . LEU B 344 ? 1.38022 1.47513 1.12781 -0.19543 0.00067  0.11411  344 LEU A CG    
2876 C CD1   . LEU B 344 ? 1.73473 1.83589 1.46637 -0.19820 0.01040  0.10797  344 LEU A CD1   
2877 C CD2   . LEU B 344 ? 1.40655 1.49960 1.15398 -0.19373 -0.00307 0.10683  344 LEU A CD2   
2878 N N     . GLY B 345 ? 1.61235 1.69556 1.41123 -0.17138 0.02264  0.09798  345 GLY A N     
2879 C CA    . GLY B 345 ? 1.17235 1.25305 0.97915 -0.16859 0.02825  0.09760  345 GLY A CA    
2880 C C     . GLY B 345 ? 1.40236 1.49050 1.20085 -0.17038 0.03582  0.09233  345 GLY A C     
2881 O O     . GLY B 345 ? 1.46283 1.55018 1.26722 -0.16887 0.04032  0.09182  345 GLY A O     
2882 N N     . LEU B 346 ? 1.39837 1.49313 1.18378 -0.17371 0.03727  0.08855  346 LEU A N     
2883 C CA    . LEU B 346 ? 1.45852 1.56093 1.23622 -0.17558 0.04573  0.08369  346 LEU A CA    
2884 C C     . LEU B 346 ? 1.47659 1.58122 1.25391 -0.17923 0.04736  0.09185  346 LEU A C     
2885 O O     . LEU B 346 ? 1.42585 1.53510 1.20528 -0.17897 0.05458  0.08921  346 LEU A O     
2886 C CB    . LEU B 346 ? 1.32405 1.43129 1.08475 -0.18000 0.04587  0.08041  346 LEU A CB    
2887 C CG    . LEU B 346 ? 1.55159 1.66455 1.30667 -0.17914 0.05525  0.06982  346 LEU A CG    
2888 C CD1   . LEU B 346 ? 1.36853 1.48303 1.10567 -0.18346 0.05383  0.06587  346 LEU A CD1   
2889 C CD2   . LEU B 346 ? 1.33837 1.45785 1.09232 -0.18113 0.06365  0.07136  346 LEU A CD2   
2890 N N     . ILE B 347 ? 1.39608 1.49758 1.17232 -0.18261 0.04057  0.10195  347 ILE A N     
2891 C CA    . ILE B 347 ? 1.22003 1.32309 0.99656 -0.18655 0.04128  0.11070  347 ILE A CA    
2892 C C     . ILE B 347 ? 1.40568 1.50491 1.19611 -0.18247 0.04470  0.10892  347 ILE A C     
2893 O O     . ILE B 347 ? 1.53961 1.64358 1.33032 -0.18466 0.04962  0.11045  347 ILE A O     
2894 C CB    . ILE B 347 ? 1.13806 1.23699 0.91417 -0.19018 0.03253  0.12209  347 ILE A CB    
2895 C CG1   . ILE B 347 ? 1.49480 1.59608 1.26989 -0.19509 0.03313  0.13144  347 ILE A CG1   
2896 C CG2   . ILE B 347 ? 1.21954 1.30838 1.01007 -0.18518 0.02704  0.12338  347 ILE A CG2   
2897 C CD1   . ILE B 347 ? 1.11347 1.22497 0.87371 -0.20070 0.03870  0.13186  347 ILE A CD1   
2898 N N     . SER B 348 ? 1.37208 1.46307 1.17321 -0.17706 0.04231  0.10584  348 SER A N     
2899 C CA    . SER B 348 ? 1.37935 1.46551 1.19138 -0.17365 0.04513  0.10353  348 SER A CA    
2900 C C     . SER B 348 ? 1.40995 1.50356 1.22189 -0.17259 0.05251  0.09610  348 SER A C     
2901 O O     . SER B 348 ? 1.37455 1.46941 1.19136 -0.17363 0.05541  0.09762  348 SER A O     
2902 C CB    . SER B 348 ? 1.41166 1.48793 1.23277 -0.16816 0.04240  0.10060  348 SER A CB    
2903 O OG    . SER B 348 ? 1.74496 1.81647 1.57362 -0.16541 0.04528  0.09739  348 SER A OG    
2904 N N     . GLN B 349 ? 1.33356 1.43171 1.14111 -0.17080 0.05515  0.08866  349 GLN A N     
2905 C CA    . GLN B 349 ? 1.26203 1.36721 1.07138 -0.16927 0.06274  0.08119  349 GLN A CA    
2906 C C     . GLN B 349 ? 1.33526 1.44923 1.13909 -0.17429 0.06779  0.08498  349 GLN A C     
2907 O O     . GLN B 349 ? 1.36858 1.48701 1.17976 -0.17369 0.07327  0.08328  349 GLN A O     
2908 C CB    . GLN B 349 ? 1.06240 1.16943 0.86728 -0.16684 0.06399  0.07284  349 GLN A CB    
2909 C CG    . GLN B 349 ? 1.20260 1.31363 1.01431 -0.16309 0.07073  0.06398  349 GLN A CG    
2910 C CD    . GLN B 349 ? 1.54036 1.66113 1.34743 -0.16586 0.07886  0.06191  349 GLN A CD    
2911 O OE1   . GLN B 349 ? 1.59138 1.71617 1.38546 -0.16902 0.08097  0.06036  349 GLN A OE1   
2912 N NE2   . GLN B 349 ? 1.65308 1.77750 1.47074 -0.16493 0.08361  0.06206  349 GLN A NE2   
2913 N N     . ILE B 350 ? 1.37013 1.48662 1.16215 -0.17929 0.06581  0.09066  350 ILE A N     
2914 C CA    . ILE B 350 ? 1.21019 1.33527 0.99568 -0.18459 0.07112  0.09517  350 ILE A CA    
2915 C C     . ILE B 350 ? 1.26863 1.39257 1.06486 -0.18583 0.07056  0.10221  350 ILE A C     
2916 O O     . ILE B 350 ? 1.39614 1.52722 1.19682 -0.18697 0.07721  0.10212  350 ILE A O     
2917 C CB    . ILE B 350 ? 1.27489 1.40144 1.04472 -0.19025 0.06750  0.10125  350 ILE A CB    
2918 C CG1   . ILE B 350 ? 1.25040 1.37909 1.00699 -0.19047 0.06903  0.09374  350 ILE A CG1   
2919 C CG2   . ILE B 350 ? 1.55957 1.69316 1.32429 -0.19615 0.07144  0.10902  350 ILE A CG2   
2920 C CD1   . ILE B 350 ? 1.36352 1.49368 1.10237 -0.19706 0.06496  0.09981  350 ILE A CD1   
2921 N N     . LEU B 351 ? 1.37259 1.48751 1.17364 -0.18563 0.06307  0.10797  351 LEU A N     
2922 C CA    . LEU B 351 ? 1.36859 1.48046 1.17865 -0.18748 0.06150  0.11471  351 LEU A CA    
2923 C C     . LEU B 351 ? 1.37255 1.48544 1.19380 -0.18451 0.06561  0.10950  351 LEU A C     
2924 O O     . LEU B 351 ? 1.51646 1.63409 1.34305 -0.18752 0.06829  0.11369  351 LEU A O     
2925 C CB    . LEU B 351 ? 1.27250 1.37234 1.08629 -0.18661 0.05348  0.11940  351 LEU A CB    
2926 C CG    . LEU B 351 ? 1.34126 1.43999 1.14982 -0.19153 0.04847  0.12970  351 LEU A CG    
2927 C CD1   . LEU B 351 ? 1.45967 1.56544 1.25496 -0.19432 0.04861  0.13048  351 LEU A CD1   
2928 C CD2   . LEU B 351 ? 1.42630 1.51237 1.24126 -0.18940 0.04152  0.13296  351 LEU A CD2   
2929 N N     . LYS B 352 ? 1.17501 1.28388 1.00045 -0.17916 0.06567  0.10146  352 LYS A N     
2930 C CA    . LYS B 352 ? 1.35955 1.46857 1.19610 -0.17660 0.06824  0.09738  352 LYS A CA    
2931 C C     . LYS B 352 ? 1.40984 1.53136 1.24947 -0.17845 0.07594  0.09668  352 LYS A C     
2932 O O     . LYS B 352 ? 1.39754 1.52644 1.22976 -0.17867 0.08112  0.09328  352 LYS A O     
2933 C CB    . LYS B 352 ? 1.40180 1.50659 1.24134 -0.17078 0.06812  0.08876  352 LYS A CB    
2934 C CG    . LYS B 352 ? 1.50418 1.60748 1.35487 -0.16852 0.06904  0.08578  352 LYS A CG    
2935 C CD    . LYS B 352 ? 1.40854 1.51680 1.26389 -0.16423 0.07358  0.07737  352 LYS A CD    
2936 C CE    . LYS B 352 ? 1.76833 1.87585 1.63540 -0.16296 0.07365  0.07630  352 LYS A CE    
2937 N NZ    . LYS B 352 ? 1.65909 1.77149 1.53265 -0.15882 0.07785  0.06893  352 LYS A NZ    
2938 N N     . ASP B 353 ? 1.34836 1.47171 1.19873 -0.17989 0.07672  0.09974  353 ASP A N     
2939 C CA    . ASP B 353 ? 1.57208 1.70782 1.42936 -0.18124 0.08464  0.09967  353 ASP A CA    
2940 C C     . ASP B 353 ? 1.61750 1.75458 1.48690 -0.17694 0.08690  0.09321  353 ASP A C     
2941 O O     . ASP B 353 ? 1.69478 1.82461 1.57150 -0.17625 0.08137  0.09423  353 ASP A O     
2942 C CB    . ASP B 353 ? 1.52733 1.66643 1.38992 -0.18664 0.08412  0.10916  353 ASP A CB    
2943 C CG    . ASP B 353 ? 1.81029 1.94628 1.68701 -0.18723 0.08046  0.11174  353 ASP A CG    
2944 O OD1   . ASP B 353 ? 2.07225 2.21442 1.95718 -0.19131 0.08197  0.11839  353 ASP A OD1   
2945 O OD2   . ASP B 353 ? 1.56695 1.69421 1.44610 -0.18397 0.07592  0.10741  353 ASP A OD2   
2946 N N     . ASP B 354 ? 1.55474 1.70013 1.42569 -0.17440 0.09469  0.08680  354 ASP A N     
2947 C CA    . ASP B 354 ? 1.56602 1.71344 1.45028 -0.17012 0.09715  0.08089  354 ASP A CA    
2948 C C     . ASP B 354 ? 1.54113 1.70135 1.43294 -0.17003 0.10780  0.07883  354 ASP A C     
2949 O O     . ASP B 354 ? 1.62533 1.78836 1.51670 -0.16631 0.11344  0.07058  354 ASP A O     
2950 C CB    . ASP B 354 ? 1.45016 1.59074 1.32970 -0.16524 0.09474  0.07295  354 ASP A CB    
2951 C CG    . ASP B 354 ? 1.76731 1.90704 1.66037 -0.16109 0.09453  0.06838  354 ASP A CG    
2952 O OD1   . ASP B 354 ? 1.84861 1.99333 1.75557 -0.16208 0.09590  0.07153  354 ASP A OD1   
2953 O OD2   . ASP B 354 ? 1.69088 1.82513 1.58126 -0.15714 0.09259  0.06238  354 ASP A OD2   
2954 N N     . THR B 355 ? 1.36935 1.53675 1.26878 -0.17396 0.11075  0.08604  355 THR A N     
2955 C CA    . THR B 355 ? 1.58703 1.76708 1.49471 -0.17398 0.12237  0.08483  355 THR A CA    
2956 C C     . THR B 355 ? 1.58362 1.76668 1.50704 -0.16897 0.12614  0.07830  355 THR A C     
2957 O O     . THR B 355 ? 1.64329 1.83281 1.56742 -0.16653 0.13623  0.07172  355 THR A O     
2958 C CB    . THR B 355 ? 1.93699 2.12371 1.85495 -0.17886 0.12347  0.09499  355 THR A CB    
2959 O OG1   . THR B 355 ? 1.87801 2.07682 1.80863 -0.17771 0.13526  0.09324  355 THR A OG1   
2960 C CG2   . THR B 355 ? 1.77007 1.95163 1.70120 -0.18017 0.11386  0.10087  355 THR A CG2   
2961 N N     . SER B 356 ? 1.61047 1.78839 1.54549 -0.16765 0.11841  0.07988  356 SER A N     
2962 C CA    . SER B 356 ? 1.86319 2.04450 1.81596 -0.16332 0.12105  0.07536  356 SER A CA    
2963 C C     . SER B 356 ? 1.94387 2.12358 1.88957 -0.15832 0.12575  0.06448  356 SER A C     
2964 O O     . SER B 356 ? 1.87721 2.06388 1.83594 -0.15509 0.13387  0.05968  356 SER A O     
2965 C CB    . SER B 356 ? 1.62727 1.80114 1.58840 -0.16338 0.11046  0.07875  356 SER A CB    
2966 O OG    . SER B 356 ? 1.66640 1.84332 1.64424 -0.15945 0.11213  0.07508  356 SER A OG    
2967 N N     . ASN B 357 ? 1.59112 1.76167 1.51883 -0.15770 0.12044  0.06104  357 ASN A N     
2968 C CA    . ASN B 357 ? 1.57487 1.74285 1.49632 -0.15329 0.12327  0.05093  357 ASN A CA    
2969 C C     . ASN B 357 ? 1.57254 1.74627 1.48245 -0.15431 0.13303  0.04638  357 ASN A C     
2970 O O     . ASN B 357 ? 1.53051 1.70033 1.42107 -0.15690 0.13060  0.04674  357 ASN A O     
2971 C CB    . ASN B 357 ? 1.56077 1.71718 1.47060 -0.15207 0.11381  0.04941  357 ASN A CB    
2972 C CG    . ASN B 357 ? 1.71871 1.86983 1.64069 -0.14926 0.10764  0.04955  357 ASN A CG    
2973 O OD1   . ASN B 357 ? 1.81457 1.96856 1.74886 -0.14554 0.11085  0.04467  357 ASN A OD1   
2974 N ND2   . ASN B 357 ? 1.74306 1.88600 1.66155 -0.15114 0.09902  0.05507  357 ASN A ND2   
2975 N N     . TYR B 358 ? 1.56869 1.75099 1.49019 -0.15249 0.14375  0.04238  358 TYR A N     
2976 C CA    . TYR B 358 ? 1.36115 1.54819 1.27061 -0.15342 0.15478  0.03666  358 TYR A CA    
2977 C C     . TYR B 358 ? 1.40429 1.58327 1.29425 -0.15241 0.15153  0.02881  358 TYR A C     
2978 O O     . TYR B 358 ? 1.45995 1.63836 1.32958 -0.15590 0.15376  0.02775  358 TYR A O     
2979 C CB    . TYR B 358 ? 1.48904 1.68433 1.41978 -0.14991 0.16564  0.03266  358 TYR A CB    
2980 C CG    . TYR B 358 ? 1.55088 1.74970 1.47559 -0.14842 0.17911  0.02280  358 TYR A CG    
2981 C CD1   . TYR B 358 ? 1.51676 1.71493 1.41710 -0.15219 0.18383  0.02036  358 TYR A CD1   
2982 C CD2   . TYR B 358 ? 1.89008 2.09234 1.83345 -0.14347 0.18719  0.01593  358 TYR A CD2   
2983 C CE1   . TYR B 358 ? 1.65473 1.85488 1.54741 -0.15135 0.19660  0.01070  358 TYR A CE1   
2984 C CE2   . TYR B 358 ? 1.94065 2.14487 1.87851 -0.14203 0.20034  0.00604  358 TYR A CE2   
2985 C CZ    . TYR B 358 ? 1.74801 1.95078 1.65930 -0.14611 0.20524  0.00301  358 TYR A CZ    
2986 O OH    . TYR B 358 ? 1.76804 1.97139 1.67118 -0.14524 0.21852  -0.00745 358 TYR A OH    
2987 N N     . GLU B 359 ? 1.48042 1.65325 1.37646 -0.14820 0.14570  0.02420  359 GLU A N     
2988 C CA    . GLU B 359 ? 1.50441 1.66946 1.38479 -0.14705 0.14163  0.01709  359 GLU A CA    
2989 C C     . GLU B 359 ? 1.46391 1.62277 1.32707 -0.15085 0.13198  0.02323  359 GLU A C     
2990 O O     . GLU B 359 ? 1.67398 1.83082 1.51815 -0.15349 0.13216  0.02054  359 GLU A O     
2991 C CB    . GLU B 359 ? 1.42519 1.58555 1.31893 -0.14181 0.13711  0.01268  359 GLU A CB    
2992 C CG    . GLU B 359 ? 1.44581 1.61239 1.36188 -0.13803 0.14471  0.00940  359 GLU A CG    
2993 C CD    . GLU B 359 ? 1.92552 2.09511 1.86098 -0.13782 0.14104  0.01785  359 GLU A CD    
2994 O OE1   . GLU B 359 ? 1.80504 1.97859 1.74042 -0.14162 0.14107  0.02577  359 GLU A OE1   
2995 O OE2   . GLU B 359 ? 2.04541 2.21314 1.99588 -0.13426 0.13767  0.01684  359 GLU A OE2   
2996 N N     . VAL B 360 ? 1.13118 1.28662 1.00072 -0.15134 0.12377  0.03116  360 VAL A N     
2997 C CA    . VAL B 360 ? 1.18407 1.33258 1.04001 -0.15430 0.11457  0.03707  360 VAL A CA    
2998 C C     . VAL B 360 ? 1.25813 1.41070 1.09841 -0.15974 0.11783  0.04081  360 VAL A C     
2999 O O     . VAL B 360 ? 1.39921 1.54728 1.22353 -0.16201 0.11302  0.04134  360 VAL A O     
3000 C CB    . VAL B 360 ? 1.04306 1.18724 0.90827 -0.15457 0.10720  0.04494  360 VAL A CB    
3001 C CG1   . VAL B 360 ? 1.24061 1.37829 1.09362 -0.15787 0.09952  0.05160  360 VAL A CG1   
3002 C CG2   . VAL B 360 ? 1.14359 1.28247 1.02064 -0.14983 0.10326  0.04160  360 VAL A CG2   
3003 N N     . ASN B 361 ? 1.21877 1.37980 1.06413 -0.16195 0.12566  0.04383  361 ASN A N     
3004 C CA    . ASN B 361 ? 1.33335 1.49895 1.16377 -0.16751 0.12981  0.04809  361 ASN A CA    
3005 C C     . ASN B 361 ? 1.28836 1.45372 1.10105 -0.16828 0.13471  0.03974  361 ASN A C     
3006 O O     . ASN B 361 ? 1.37825 1.54098 1.17210 -0.17265 0.13074  0.04266  361 ASN A O     
3007 C CB    . ASN B 361 ? 1.41700 1.59230 1.25859 -0.16931 0.13842  0.05270  361 ASN A CB    
3008 C CG    . ASN B 361 ? 1.62551 1.80006 1.48143 -0.17018 0.13188  0.06200  361 ASN A CG    
3009 O OD1   . ASN B 361 ? 1.70113 1.87098 1.54976 -0.17351 0.12404  0.06937  361 ASN A OD1   
3010 N ND2   . ASN B 361 ? 1.65817 1.83681 1.53464 -0.16754 0.13462  0.06197  361 ASN A ND2   
3011 N N     . ILE B 362 ? 1.28462 1.45204 1.10325 -0.16445 0.14250  0.02986  362 ILE A N     
3012 C CA    . ILE B 362 ? 1.20823 1.37398 1.00920 -0.16533 0.14743  0.02038  362 ILE A CA    
3013 C C     . ILE B 362 ? 1.26927 1.42579 1.05816 -0.16566 0.13564  0.01935  362 ILE A C     
3014 O O     . ILE B 362 ? 1.35122 1.50542 1.11883 -0.16989 0.13454  0.01769  362 ILE A O     
3015 C CB    . ILE B 362 ? 1.16388 1.33207 0.97677 -0.16042 0.15736  0.00960  362 ILE A CB    
3016 C CG1   . ILE B 362 ? 1.41099 1.58897 1.23762 -0.16012 0.16974  0.01124  362 ILE A CG1   
3017 C CG2   . ILE B 362 ? 1.24753 1.41152 1.04157 -0.16133 0.16100  -0.00119 362 ILE A CG2   
3018 C CD1   . ILE B 362 ? 1.45221 1.63286 1.29088 -0.15547 0.18116  0.00064  362 ILE A CD1   
3019 N N     . LEU B 363 ? 1.16425 1.31572 0.96631 -0.16171 0.12713  0.02090  363 LEU A N     
3020 C CA    . LEU B 363 ? 1.21954 1.36255 1.01373 -0.16146 0.11625  0.02065  363 LEU A CA    
3021 C C     . LEU B 363 ? 1.19472 1.33625 0.97250 -0.16740 0.11008  0.02926  363 LEU A C     
3022 O O     . LEU B 363 ? 1.11217 1.24983 0.87425 -0.17009 0.10546  0.02745  363 LEU A O     
3023 C CB    . LEU B 363 ? 1.23859 1.37691 1.05003 -0.15674 0.10932  0.02298  363 LEU A CB    
3024 C CG    . LEU B 363 ? 1.17066 1.30054 0.97784 -0.15613 0.09842  0.02485  363 LEU A CG    
3025 C CD1   . LEU B 363 ? 1.15729 1.28424 0.95724 -0.15507 0.09787  0.01590  363 LEU A CD1   
3026 C CD2   . LEU B 363 ? 1.09089 1.21608 0.91398 -0.15192 0.09326  0.02788  363 LEU A CD2   
3027 N N     . LYS B 364 ? 1.30203 1.44654 1.08398 -0.16971 0.10965  0.03866  364 LYS A N     
3028 C CA    . LYS B 364 ? 1.31148 1.45469 1.08008 -0.17542 0.10353  0.04809  364 LYS A CA    
3029 C C     . LYS B 364 ? 1.18597 1.33210 0.93280 -0.18068 0.10791  0.04546  364 LYS A C     
3030 O O     . LYS B 364 ? 1.27891 1.42071 1.01122 -0.18423 0.10018  0.04802  364 LYS A O     
3031 C CB    . LYS B 364 ? 1.09351 1.24077 0.87037 -0.17748 0.10493  0.05750  364 LYS A CB    
3032 C CG    . LYS B 364 ? 1.12225 1.26633 0.91857 -0.17346 0.10117  0.06025  364 LYS A CG    
3033 C CD    . LYS B 364 ? 1.47653 1.62621 1.28238 -0.17561 0.10493  0.06726  364 LYS A CD    
3034 C CE    . LYS B 364 ? 1.48484 1.62935 1.30565 -0.17341 0.09896  0.07148  364 LYS A CE    
3035 N NZ    . LYS B 364 ? 1.20835 1.34463 1.02410 -0.17522 0.08945  0.07827  364 LYS A NZ    
3036 N N     . MET B 365 ? 1.17762 1.33055 0.92250 -0.18125 0.12000  0.04054  365 MET A N     
3037 C CA    . MET B 365 ? 1.32188 1.47719 1.04369 -0.18677 0.12601  0.03748  365 MET A CA    
3038 C C     . MET B 365 ? 1.29568 1.44449 1.00455 -0.18653 0.12236  0.02811  365 MET A C     
3039 O O     . MET B 365 ? 1.31905 1.46515 1.00621 -0.19244 0.11761  0.02999  365 MET A O     
3040 C CB    . MET B 365 ? 1.22411 1.38744 0.94956 -0.18622 0.14147  0.03274  365 MET A CB    
3041 C CG    . MET B 365 ? 1.11105 1.28099 0.85531 -0.18530 0.14481  0.04106  365 MET A CG    
3042 S SD    . MET B 365 ? 0.97857 1.15900 0.72971 -0.18485 0.16345  0.03696  365 MET A SD    
3043 C CE    . MET B 365 ? 1.24505 1.42630 0.96287 -0.19282 0.16922  0.03643  365 MET A CE    
3044 N N     . GLN B 366 ? 1.32699 1.47323 1.04909 -0.18035 0.12374  0.01902  366 GLN A N     
3045 C CA    . GLN B 366 ? 1.26985 1.40959 0.98194 -0.17991 0.12008  0.00970  366 GLN A CA    
3046 C C     . GLN B 366 ? 1.13714 1.27068 0.84196 -0.18261 0.10528  0.01654  366 GLN A C     
3047 O O     . GLN B 366 ? 1.22589 1.35581 0.91058 -0.18754 0.10113  0.01434  366 GLN A O     
3048 C CB    . GLN B 366 ? 1.13270 1.27057 0.86476 -0.17238 0.12199  0.00130  366 GLN A CB    
3049 C CG    . GLN B 366 ? 1.30779 1.45097 1.04860 -0.16928 0.13643  -0.00694 366 GLN A CG    
3050 C CD    . GLN B 366 ? 1.50447 1.64600 1.26715 -0.16198 0.13715  -0.01357 366 GLN A CD    
3051 O OE1   . GLN B 366 ? 1.48508 1.62157 1.25611 -0.15914 0.12723  -0.01198 366 GLN A OE1   
3052 N NE2   . GLN B 366 ? 1.42826 1.57415 1.20139 -0.15885 0.14925  -0.02059 366 GLN A NE2   
3053 N N     . LEU B 367 ? 1.14900 1.28105 0.86970 -0.17975 0.09773  0.02469  367 LEU A N     
3054 C CA    . LEU B 367 ? 1.17984 1.30585 0.89798 -0.18133 0.08425  0.03150  367 LEU A CA    
3055 C C     . LEU B 367 ? 1.22051 1.34742 0.91756 -0.18951 0.08029  0.03909  367 LEU A C     
3056 O O     . LEU B 367 ? 1.38999 1.51226 1.07660 -0.19280 0.07075  0.04085  367 LEU A O     
3057 C CB    . LEU B 367 ? 1.07163 1.19579 0.80959 -0.17716 0.07931  0.03902  367 LEU A CB    
3058 C CG    . LEU B 367 ? 1.00530 1.12709 0.76292 -0.16965 0.08057  0.03302  367 LEU A CG    
3059 C CD1   . LEU B 367 ? 1.07536 1.19517 0.84865 -0.16684 0.07723  0.04069  367 LEU A CD1   
3060 C CD2   . LEU B 367 ? 1.11887 1.23475 0.87653 -0.16760 0.07398  0.02791  367 LEU A CD2   
3061 N N     . LEU B 368 ? 1.23278 1.36566 0.92453 -0.19295 0.08700  0.04407  368 LEU A N     
3062 C CA    . LEU B 368 ? 1.22251 1.35666 0.89452 -0.20117 0.08315  0.05287  368 LEU A CA    
3063 C C     . LEU B 368 ? 1.31573 1.44779 0.96304 -0.20639 0.08345  0.04584  368 LEU A C     
3064 O O     . LEU B 368 ? 1.51336 1.64155 1.14772 -0.21163 0.07253  0.05133  368 LEU A O     
3065 C CB    . LEU B 368 ? 1.17294 1.31453 0.84514 -0.20344 0.09231  0.05822  368 LEU A CB    
3066 C CG    . LEU B 368 ? 1.35983 1.50255 1.02777 -0.20898 0.08564  0.07267  368 LEU A CG    
3067 C CD1   . LEU B 368 ? 1.15210 1.28926 0.83752 -0.20551 0.07437  0.07976  368 LEU A CD1   
3068 C CD2   . LEU B 368 ? 1.52532 1.67574 1.19728 -0.21037 0.09557  0.07716  368 LEU A CD2   
3069 N N     . ILE B 369 ? 1.37531 1.50923 1.01698 -0.20509 0.09521  0.03406  369 ILE A N     
3070 C CA    . ILE B 369 ? 1.45378 1.58412 1.07018 -0.21019 0.09647  0.02542  369 ILE A CA    
3071 C C     . ILE B 369 ? 1.35209 1.47471 0.97100 -0.20855 0.08459  0.02167  369 ILE A C     
3072 O O     . ILE B 369 ? 1.39151 1.50974 0.98969 -0.21515 0.07668  0.02216  369 ILE A O     
3073 C CB    . ILE B 369 ? 1.30178 1.43486 0.91520 -0.20799 0.11288  0.01267  369 ILE A CB    
3074 C CG1   . ILE B 369 ? 1.32109 1.46263 0.93550 -0.20930 0.12482  0.01749  369 ILE A CG1   
3075 C CG2   . ILE B 369 ? 1.30225 1.42986 0.88847 -0.21330 0.11470  0.00241  369 ILE A CG2   
3076 C CD1   . ILE B 369 ? 1.49646 1.64050 1.09897 -0.21020 0.14148  0.00653  369 ILE A CD1   
3077 N N     . TRP B 370 ? 1.27969 1.40082 0.92318 -0.20050 0.08300  0.01882  370 TRP A N     
3078 C CA    . TRP B 370 ? 1.37283 1.48714 1.02178 -0.19825 0.07272  0.01519  370 TRP A CA    
3079 C C     . TRP B 370 ? 1.50999 1.62120 1.15477 -0.20275 0.05771  0.02695  370 TRP A C     
3080 O O     . TRP B 370 ? 1.62060 1.72683 1.25326 -0.20677 0.04915  0.02497  370 TRP A O     
3081 C CB    . TRP B 370 ? 1.37527 1.48928 1.05245 -0.18890 0.07421  0.01222  370 TRP A CB    
3082 C CG    . TRP B 370 ? 1.42343 1.53115 1.10904 -0.18597 0.06489  0.00893  370 TRP A CG    
3083 C CD1   . TRP B 370 ? 1.45125 1.55416 1.12553 -0.18818 0.06196  0.00040  370 TRP A CD1   
3084 C CD2   . TRP B 370 ? 1.44669 1.55190 1.15390 -0.18059 0.05731  0.01452  370 TRP A CD2   
3085 N NE1   . TRP B 370 ? 1.43292 1.53132 1.12195 -0.18441 0.05294  0.00074  370 TRP A NE1   
3086 C CE2   . TRP B 370 ? 1.32785 1.42766 1.03697 -0.17961 0.05042  0.00935  370 TRP A CE2   
3087 C CE3   . TRP B 370 ? 1.40539 1.51177 1.12983 -0.17675 0.05605  0.02305  370 TRP A CE3   
3088 C CZ2   . TRP B 370 ? 1.33741 1.43384 1.06587 -0.17467 0.04311  0.01294  370 TRP A CZ2   
3089 C CZ3   . TRP B 370 ? 1.39864 1.50073 1.14039 -0.17196 0.04913  0.02582  370 TRP A CZ3   
3090 C CH2   . TRP B 370 ? 1.40890 1.50647 1.15302 -0.17080 0.04309  0.02106  370 TRP A CH2   
3091 N N     . ILE B 371 ? 1.41418 1.52794 1.06903 -0.20244 0.05438  0.03895  371 ILE A N     
3092 C CA    . ILE B 371 ? 1.24484 1.35541 0.90069 -0.20573 0.04006  0.05094  371 ILE A CA    
3093 C C     . ILE B 371 ? 1.28326 1.39352 0.91151 -0.21585 0.03472  0.05486  371 ILE A C     
3094 O O     . ILE B 371 ? 1.40922 1.51643 1.03586 -0.21971 0.02159  0.06378  371 ILE A O     
3095 C CB    . ILE B 371 ? 1.18909 1.30165 0.86144 -0.20329 0.03884  0.06229  371 ILE A CB    
3096 C CG1   . ILE B 371 ? 1.18661 1.29457 0.86960 -0.20327 0.02537  0.07255  371 ILE A CG1   
3097 C CG2   . ILE B 371 ? 1.42398 1.54211 1.08362 -0.20889 0.04421  0.06878  371 ILE A CG2   
3098 C CD1   . ILE B 371 ? 1.38802 1.49107 1.08882 -0.19653 0.02141  0.06761  371 ILE A CD1   
3099 N N     . THR B 372 ? 1.41501 1.52815 1.02267 -0.22012 0.04467  0.04862  372 THR A N     
3100 C CA    . THR B 372 ? 1.53024 1.64258 1.10790 -0.23057 0.04061  0.05174  372 THR A CA    
3101 C C     . THR B 372 ? 1.52352 1.62974 1.08535 -0.23341 0.03734  0.04085  372 THR A C     
3102 O O     . THR B 372 ? 1.46834 1.57171 1.00587 -0.24260 0.02946  0.04415  372 THR A O     
3103 C CB    . THR B 372 ? 1.62045 1.73876 1.18347 -0.23402 0.05392  0.05132  372 THR A CB    
3104 O OG1   . THR B 372 ? 1.84865 1.96598 1.38351 -0.24465 0.04791  0.05756  372 THR A OG1   
3105 C CG2   . THR B 372 ? 1.44870 1.56790 1.00724 -0.23073 0.06941  0.03583  372 THR A CG2   
3106 N N     . GLU B 373 ? 1.62248 1.72622 1.19744 -0.22629 0.04218  0.02878  373 GLU A N     
3107 C CA    . GLU B 373 ? 1.57791 1.67509 1.13805 -0.22889 0.04010  0.01689  373 GLU A CA    
3108 C C     . GLU B 373 ? 1.53756 1.63006 1.11815 -0.22385 0.02936  0.01594  373 GLU A C     
3109 O O     . GLU B 373 ? 1.55121 1.63768 1.11935 -0.22864 0.02028  0.01239  373 GLU A O     
3110 C CB    . GLU B 373 ? 1.40519 1.50288 0.96166 -0.22529 0.05673  0.00155  373 GLU A CB    
3111 C CG    . GLU B 373 ? 1.41377 1.51642 0.95190 -0.22948 0.06990  0.00118  373 GLU A CG    
3112 C CD    . GLU B 373 ? 1.47971 1.58306 1.01814 -0.22512 0.08726  -0.01373 373 GLU A CD    
3113 O OE1   . GLU B 373 ? 1.50061 1.60044 1.05360 -0.21893 0.08838  -0.02354 373 GLU A OE1   
3114 O OE2   . GLU B 373 ? 1.75407 1.86158 1.27927 -0.22790 0.09990  -0.01514 373 GLU A OE2   
3115 N N     . THR B 374 ? 1.51048 1.60528 1.12052 -0.21500 0.03030  0.01903  374 THR A N     
3116 C CA    . THR B 374 ? 1.51481 1.60542 1.14535 -0.20954 0.02221  0.01741  374 THR A CA    
3117 C C     . THR B 374 ? 1.47515 1.56216 1.10185 -0.21524 0.00549  0.02708  374 THR A C     
3118 O O     . THR B 374 ? 1.40976 1.49906 1.03430 -0.21912 -0.00057 0.03999  374 THR A O     
3119 C CB    . THR B 374 ? 1.54940 1.64282 1.20953 -0.20007 0.02600  0.02080  374 THR A CB    
3120 O OG1   . THR B 374 ? 1.53904 1.62817 1.21616 -0.19556 0.01888  0.01875  374 THR A OG1   
3121 C CG2   . THR B 374 ? 1.52895 1.62526 1.19651 -0.20073 0.02167  0.03527  374 THR A CG2   
3122 N N     . PRO B 375 ? 1.54646 1.62794 1.17292 -0.21631 -0.00271 0.02189  375 PRO A N     
3123 C CA    . PRO B 375 ? 1.39300 1.47147 1.02047 -0.22126 -0.01950 0.03198  375 PRO A CA    
3124 C C     . PRO B 375 ? 1.38076 1.45869 1.04036 -0.21349 -0.02525 0.03746  375 PRO A C     
3125 O O     . PRO B 375 ? 1.29246 1.36914 0.95940 -0.21629 -0.03850 0.04857  375 PRO A O     
3126 C CB    . PRO B 375 ? 1.40284 1.47532 1.01001 -0.22718 -0.02328 0.02129  375 PRO A CB    
3127 C CG    . PRO B 375 ? 1.42598 1.49749 1.04220 -0.21953 -0.01062 0.00623  375 PRO A CG    
3128 C CD    . PRO B 375 ? 1.56591 1.64380 1.19097 -0.21346 0.00360  0.00656  375 PRO A CD    
3129 N N     . SER B 376 ? 1.37382 1.45270 1.05258 -0.20413 -0.01546 0.03043  376 SER A N     
3130 C CA    . SER B 376 ? 1.41752 1.49524 1.12590 -0.19649 -0.01945 0.03441  376 SER A CA    
3131 C C     . SER B 376 ? 1.49958 1.58069 1.22506 -0.18966 -0.01174 0.03968  376 SER A C     
3132 O O     . SER B 376 ? 1.41535 1.49581 1.15798 -0.18717 -0.01772 0.05005  376 SER A O     
3133 C CB    . SER B 376 ? 1.62299 1.69777 1.34013 -0.19174 -0.01633 0.02249  376 SER A CB    
3134 O OG    . SER B 376 ? 1.58005 1.65684 1.29408 -0.18784 -0.00217 0.01170  376 SER A OG    
3135 N N     . GLY B 377 ? 1.60332 1.68747 1.32491 -0.18686 0.00105  0.03269  377 GLY A N     
3136 C CA    . GLY B 377 ? 1.47953 1.56640 1.21612 -0.18104 0.00811  0.03707  377 GLY A CA    
3137 C C     . GLY B 377 ? 1.53427 1.62006 1.29109 -0.17234 0.01407  0.03040  377 GLY A C     
3138 O O     . GLY B 377 ? 1.55377 1.64061 1.32382 -0.16741 0.01905  0.03368  377 GLY A O     
3139 N N     . ASP B 378 ? 1.41065 1.49398 1.16935 -0.17093 0.01327  0.02150  378 ASP A N     
3140 C CA    . ASP B 378 ? 1.37735 1.45988 1.15507 -0.16292 0.01911  0.01505  378 ASP A CA    
3141 C C     . ASP B 378 ? 1.43509 1.52168 1.21256 -0.16008 0.03147  0.01013  378 ASP A C     
3142 O O     . ASP B 378 ? 1.37000 1.45863 1.13306 -0.16300 0.03757  0.00257  378 ASP A O     
3143 C CB    . ASP B 378 ? 1.50173 1.58108 1.28012 -0.16268 0.01647  0.00599  378 ASP A CB    
3144 C CG    . ASP B 378 ? 1.58664 1.66586 1.38080 -0.15551 0.02400  -0.00234 378 ASP A CG    
3145 O OD1   . ASP B 378 ? 1.52766 1.60646 1.34072 -0.14971 0.02447  0.00200  378 ASP A OD1   
3146 O OD2   . ASP B 378 ? 1.62335 1.70248 1.41059 -0.15595 0.02949  -0.01301 378 ASP A OD2   
3147 N N     . ILE B 379 ? 1.31221 1.39952 1.10534 -0.15472 0.03513  0.01414  379 ILE A N     
3148 C CA    . ILE B 379 ? 1.19369 1.28520 0.98863 -0.15241 0.04571  0.01113  379 ILE A CA    
3149 C C     . ILE B 379 ? 1.29169 1.38414 1.09041 -0.14932 0.05262  -0.00058 379 ILE A C     
3150 O O     . ILE B 379 ? 1.33403 1.43067 1.13278 -0.14832 0.06178  -0.00439 379 ILE A O     
3151 C CB    . ILE B 379 ? 1.13093 1.22148 0.94166 -0.14777 0.04664  0.01768  379 ILE A CB    
3152 C CG1   . ILE B 379 ? 1.48974 1.57676 1.31803 -0.14155 0.04598  0.01481  379 ILE A CG1   
3153 C CG2   . ILE B 379 ? 1.25756 1.34601 1.06635 -0.15046 0.03990  0.02887  379 ILE A CG2   
3154 C CD1   . ILE B 379 ? 1.50396 1.58924 1.34540 -0.13720 0.04838  0.01950  379 ILE A CD1   
3155 N N     . GLN B 380 ? 1.38186 1.47058 1.18528 -0.14788 0.04829  -0.00556 380 GLN A N     
3156 C CA    . GLN B 380 ? 1.44878 1.53750 1.25815 -0.14461 0.05435  -0.01663 380 GLN A CA    
3157 C C     . GLN B 380 ? 1.25421 1.34324 1.04424 -0.14968 0.05784  -0.02510 380 GLN A C     
3158 O O     . GLN B 380 ? 1.18983 1.27916 0.98312 -0.14737 0.06514  -0.03500 380 GLN A O     
3159 C CB    . GLN B 380 ? 1.20449 1.28878 1.02798 -0.14104 0.04829  -0.01807 380 GLN A CB    
3160 C CG    . GLN B 380 ? 1.43461 1.51759 1.27511 -0.13645 0.04531  -0.00969 380 GLN A CG    
3161 C CD    . GLN B 380 ? 1.85290 1.93189 1.70753 -0.13314 0.03987  -0.01036 380 GLN A CD    
3162 O OE1   . GLN B 380 ? 1.64933 1.72555 1.50042 -0.13605 0.03195  -0.00953 380 GLN A OE1   
3163 N NE2   . GLN B 380 ? 1.98427 2.06302 1.85539 -0.12736 0.04374  -0.01129 380 GLN A NE2   
3164 N N     . GLU B 381 ? 1.30462 1.39317 1.07522 -0.15646 0.05310  -0.02131 381 GLU A N     
3165 C CA    . GLU B 381 ? 1.36886 1.45705 1.11746 -0.16205 0.05744  -0.02945 381 GLU A CA    
3166 C C     . GLU B 381 ? 1.24516 1.33840 0.99588 -0.15948 0.07142  -0.03492 381 GLU A C     
3167 O O     . GLU B 381 ? 1.51003 1.60213 1.25665 -0.15913 0.07878  -0.04616 381 GLU A O     
3168 C CB    . GLU B 381 ? 1.42401 1.51222 1.15084 -0.17007 0.05146  -0.02241 381 GLU A CB    
3169 C CG    . GLU B 381 ? 1.40968 1.49310 1.13386 -0.17365 0.03703  -0.01683 381 GLU A CG    
3170 C CD    . GLU B 381 ? 1.66397 1.74803 1.36972 -0.18146 0.03006  -0.00738 381 GLU A CD    
3171 O OE1   . GLU B 381 ? 1.50289 1.58705 1.18498 -0.18784 0.03331  -0.01132 381 GLU A OE1   
3172 O OE2   . GLU B 381 ? 1.62988 1.71411 1.34507 -0.18122 0.02173  0.00411  381 GLU A OE2   
3173 N N     . LEU B 382 ? 1.21037 1.30869 0.96846 -0.15777 0.07485  -0.02710 382 LEU A N     
3174 C CA    . LEU B 382 ? 1.43384 1.53782 1.19814 -0.15507 0.08750  -0.03068 382 LEU A CA    
3175 C C     . LEU B 382 ? 1.53006 1.63393 1.31819 -0.14762 0.09039  -0.03495 382 LEU A C     
3176 O O     . LEU B 382 ? 1.50156 1.60302 1.30308 -0.14433 0.08317  -0.02975 382 LEU A O     
3177 C CB    . LEU B 382 ? 1.29309 1.40201 1.05776 -0.15642 0.08853  -0.02007 382 LEU A CB    
3178 C CG    . LEU B 382 ? 1.47167 1.58714 1.24696 -0.15359 0.09986  -0.02089 382 LEU A CG    
3179 C CD1   . LEU B 382 ? 1.24095 1.35902 1.00552 -0.15551 0.11120  -0.03031 382 LEU A CD1   
3180 C CD2   . LEU B 382 ? 1.60842 1.72774 1.38315 -0.15585 0.09886  -0.00965 382 LEU A CD2   
3181 N N     . ASN B 383 ? 1.43063 1.53691 1.22418 -0.14514 0.10090  -0.04375 383 ASN A N     
3182 C CA    . ASN B 383 ? 1.39724 1.50372 1.21430 -0.13834 0.10364  -0.04754 383 ASN A CA    
3183 C C     . ASN B 383 ? 1.47716 1.58861 1.31008 -0.13522 0.10515  -0.03896 383 ASN A C     
3184 O O     . ASN B 383 ? 1.63065 1.74710 1.47476 -0.13272 0.11410  -0.04129 383 ASN A O     
3185 C CB    . ASN B 383 ? 1.79201 1.89920 1.61136 -0.13674 0.11436  -0.05933 383 ASN A CB    
3186 C CG    . ASN B 383 ? 1.81517 1.91730 1.61207 -0.14176 0.11471  -0.06791 383 ASN A CG    
3187 O OD1   . ASN B 383 ? 1.76809 1.87208 1.55135 -0.14483 0.12393  -0.07278 383 ASN A OD1   
3188 N ND2   . ASN B 383 ? 1.41356 1.50906 1.20591 -0.14303 0.10482  -0.06966 383 ASN A ND2   
3189 N N     . LEU B 384 ? 1.44464 1.55436 1.27883 -0.13557 0.09671  -0.02940 384 LEU A N     
3190 C CA    . LEU B 384 ? 1.35259 1.46551 1.19898 -0.13356 0.09732  -0.02122 384 LEU A CA    
3191 C C     . LEU B 384 ? 1.47211 1.58603 1.33972 -0.12792 0.10053  -0.02420 384 LEU A C     
3192 O O     . LEU B 384 ? 1.56523 1.67471 1.44078 -0.12486 0.09600  -0.02651 384 LEU A O     
3193 C CB    . LEU B 384 ? 1.50462 1.61329 1.34926 -0.13438 0.08778  -0.01205 384 LEU A CB    
3194 C CG    . LEU B 384 ? 1.37299 1.48181 1.20026 -0.14003 0.08442  -0.00590 384 LEU A CG    
3195 C CD1   . LEU B 384 ? 1.53830 1.64172 1.36696 -0.13996 0.07487  0.00199  384 LEU A CD1   
3196 C CD2   . LEU B 384 ? 1.06061 1.17520 0.88663 -0.14206 0.09033  -0.00136 384 LEU A CD2   
3197 N N     . LYS B 385 ? 1.43264 1.55246 1.30993 -0.12686 0.10772  -0.02335 385 LYS A N     
3198 C CA    . LYS B 385 ? 1.28957 1.41106 1.18827 -0.12199 0.11042  -0.02506 385 LYS A CA    
3199 C C     . LYS B 385 ? 1.19577 1.32316 1.10424 -0.12225 0.11394  -0.01848 385 LYS A C     
3200 O O     . LYS B 385 ? 1.65786 1.78868 1.55644 -0.12601 0.11641  -0.01473 385 LYS A O     
3201 C CB    . LYS B 385 ? 1.33627 1.45891 1.24019 -0.11987 0.11763  -0.03575 385 LYS A CB    
3202 C CG    . LYS B 385 ? 1.48643 1.61359 1.38049 -0.12261 0.12741  -0.04072 385 LYS A CG    
3203 C CD    . LYS B 385 ? 1.68256 1.80810 1.57812 -0.12086 0.13417  -0.05277 385 LYS A CD    
3204 C CE    . LYS B 385 ? 1.82032 1.94873 1.70221 -0.12403 0.14442  -0.05843 385 LYS A CE    
3205 N NZ    . LYS B 385 ? 1.70418 1.82918 1.58588 -0.12253 0.15113  -0.07105 385 LYS A NZ    
3206 N N     . GLY B 386 ? 1.12174 1.25014 1.04896 -0.11884 0.11349  -0.01651 386 GLY A N     
3207 C CA    . GLY B 386 ? 1.15561 1.28952 1.09391 -0.11948 0.11573  -0.00989 386 GLY A CA    
3208 C C     . GLY B 386 ? 1.40538 1.53698 1.33422 -0.12293 0.10979  -0.00088 386 GLY A C     
3209 O O     . GLY B 386 ? 1.34361 1.46821 1.26354 -0.12316 0.10277  0.00108  386 GLY A O     
3210 N N     . GLY B 387 ? 1.24679 1.38392 1.17860 -0.12551 0.11271  0.00457  387 GLY A N     
3211 C CA    . GLY B 387 ? 1.25728 1.39175 1.18154 -0.12904 0.10706  0.01332  387 GLY A CA    
3212 C C     . GLY B 387 ? 1.30860 1.43900 1.21320 -0.13176 0.10415  0.01376  387 GLY A C     
3213 O O     . GLY B 387 ? 1.38695 1.51103 1.28558 -0.13297 0.09721  0.01923  387 GLY A O     
3214 N N     . GLN B 388 ? 1.17378 1.30721 1.06856 -0.13289 0.10930  0.00828  388 GLN A N     
3215 C CA    . GLN B 388 ? 1.22267 1.35268 1.09813 -0.13628 0.10581  0.00937  388 GLN A CA    
3216 C C     . GLN B 388 ? 1.15076 1.27223 1.02415 -0.13430 0.09735  0.00949  388 GLN A C     
3217 O O     . GLN B 388 ? 1.26147 1.37843 1.12707 -0.13642 0.09127  0.01568  388 GLN A O     
3218 C CB    . GLN B 388 ? 1.17560 1.30894 1.04021 -0.13776 0.11241  0.00196  388 GLN A CB    
3219 C CG    . GLN B 388 ? 1.27923 1.42093 1.14388 -0.14014 0.12196  0.00242  388 GLN A CG    
3220 C CD    . GLN B 388 ? 1.59873 1.74212 1.44702 -0.14282 0.12845  -0.00425 388 GLN A CD    
3221 O OE1   . GLN B 388 ? 1.64831 1.78640 1.48447 -0.14336 0.12491  -0.00940 388 GLN A OE1   
3222 N NE2   . GLN B 388 ? 1.54352 1.69409 1.39099 -0.14489 0.13809  -0.00407 388 GLN A NE2   
3223 N N     . LYS B 389 ? 1.16195 1.28136 1.04375 -0.13027 0.09731  0.00328  389 LYS A N     
3224 C CA    . LYS B 389 ? 1.19735 1.30918 1.07894 -0.12815 0.09003  0.00335  389 LYS A CA    
3225 C C     . LYS B 389 ? 1.16530 1.27246 1.05249 -0.12738 0.08516  0.01085  389 LYS A C     
3226 O O     . LYS B 389 ? 1.11896 1.22027 0.99959 -0.12820 0.07953  0.01503  389 LYS A O     
3227 C CB    . LYS B 389 ? 1.30098 1.41208 1.19312 -0.12396 0.09146  -0.00415 389 LYS A CB    
3228 C CG    . LYS B 389 ? 1.35630 1.46037 1.25116 -0.12146 0.08473  -0.00374 389 LYS A CG    
3229 C CD    . LYS B 389 ? 1.37493 1.47837 1.28100 -0.11758 0.08591  -0.01074 389 LYS A CD    
3230 C CE    . LYS B 389 ? 1.67246 1.76950 1.58346 -0.11504 0.07971  -0.00872 389 LYS A CE    
3231 N NZ    . LYS B 389 ? 1.66313 1.75619 1.56256 -0.11735 0.07416  -0.00597 389 LYS A NZ    
3232 N N     . MET B 390 ? 1.15516 1.26451 1.05399 -0.12616 0.08729  0.01262  390 MET A N     
3233 C CA    . MET B 390 ? 1.23715 1.34081 1.13959 -0.12598 0.08273  0.01903  390 MET A CA    
3234 C C     . MET B 390 ? 1.35367 1.45457 1.24484 -0.12984 0.07985  0.02550  390 MET A C     
3235 O O     . MET B 390 ? 1.44606 1.53900 1.33378 -0.12946 0.07504  0.02893  390 MET A O     
3236 C CB    . MET B 390 ? 1.00108 1.10862 0.91601 -0.12573 0.08499  0.02084  390 MET A CB    
3237 C CG    . MET B 390 ? 1.32769 1.42846 1.24834 -0.12438 0.08049  0.02430  390 MET A CG    
3238 S SD    . MET B 390 ? 1.51018 1.61644 1.44742 -0.12427 0.08212  0.02610  390 MET A SD    
3239 C CE    . MET B 390 ? 0.91952 1.03449 0.86723 -0.12102 0.08897  0.01798  390 MET A CE    
3240 N N     . TYR B 391 ? 1.08756 1.19470 0.97379 -0.13333 0.08318  0.02713  391 TYR A N     
3241 C CA    . TYR B 391 ? 1.11210 1.21715 0.98888 -0.13741 0.08042  0.03410  391 TYR A CA    
3242 C C     . TYR B 391 ? 1.16656 1.26648 1.03297 -0.13788 0.07606  0.03485  391 TYR A C     
3243 O O     . TYR B 391 ? 1.23151 1.32429 1.09556 -0.13848 0.07134  0.04015  391 TYR A O     
3244 C CB    . TYR B 391 ? 1.18286 1.29668 1.05651 -0.14106 0.08566  0.03542  391 TYR A CB    
3245 C CG    . TYR B 391 ? 1.17031 1.28306 1.03361 -0.14566 0.08313  0.04255  391 TYR A CG    
3246 C CD1   . TYR B 391 ? 1.19143 1.30196 1.05790 -0.14800 0.08079  0.04944  391 TYR A CD1   
3247 C CD2   . TYR B 391 ? 1.17673 1.29040 1.02711 -0.14812 0.08257  0.04269  391 TYR A CD2   
3248 C CE1   . TYR B 391 ? 1.47958 1.58886 1.33796 -0.15221 0.07836  0.05620  391 TYR A CE1   
3249 C CE2   . TYR B 391 ? 1.19880 1.31169 1.04076 -0.15249 0.07988  0.05004  391 TYR A CE2   
3250 C CZ    . TYR B 391 ? 1.42663 1.53738 1.27325 -0.15433 0.07800  0.05678  391 TYR A CZ    
3251 O OH    . TYR B 391 ? 1.49339 1.60308 1.33298 -0.15865 0.07525  0.06426  391 TYR A OH    
3252 N N     . PHE B 392 ? 1.06174 1.16466 0.92254 -0.13779 0.07741  0.02976  392 PHE A N     
3253 C CA    . PHE B 392 ? 1.02490 1.12376 0.87592 -0.13923 0.07220  0.03160  392 PHE A CA    
3254 C C     . PHE B 392 ? 1.14969 1.24022 1.00716 -0.13565 0.06718  0.03274  392 PHE A C     
3255 O O     . PHE B 392 ? 1.29492 1.38016 1.14905 -0.13672 0.06241  0.03835  392 PHE A O     
3256 C CB    . PHE B 392 ? 1.05228 1.15507 0.89525 -0.14034 0.07394  0.02533  392 PHE A CB    
3257 C CG    . PHE B 392 ? 1.15252 1.25478 0.98118 -0.14497 0.06970  0.02936  392 PHE A CG    
3258 C CD1   . PHE B 392 ? 1.00571 1.10914 0.82811 -0.14902 0.06887  0.03706  392 PHE A CD1   
3259 C CD2   . PHE B 392 ? 1.32169 1.42213 1.14365 -0.14569 0.06582  0.02608  392 PHE A CD2   
3260 C CE1   . PHE B 392 ? 1.18124 1.28435 0.99111 -0.15359 0.06441  0.04173  392 PHE A CE1   
3261 C CE2   . PHE B 392 ? 1.35625 1.45624 1.16513 -0.15058 0.06085  0.03073  392 PHE A CE2   
3262 C CZ    . PHE B 392 ? 1.31055 1.41201 1.11345 -0.15447 0.06021  0.03874  392 PHE A CZ    
3263 N N     . ASP B 393 ? 0.92396 1.01337 0.79130 -0.13147 0.06858  0.02792  393 ASP A N     
3264 C CA    . ASP B 393 ? 1.09308 1.17474 0.96659 -0.12794 0.06475  0.02884  393 ASP A CA    
3265 C C     . ASP B 393 ? 1.15701 1.23201 1.03114 -0.12833 0.06305  0.03534  393 ASP A C     
3266 O O     . ASP B 393 ? 1.14891 1.21719 1.02261 -0.12756 0.05955  0.03895  393 ASP A O     
3267 C CB    . ASP B 393 ? 1.28289 1.36488 1.16683 -0.12380 0.06677  0.02313  393 ASP A CB    
3268 C CG    . ASP B 393 ? 1.41375 1.49939 1.29787 -0.12292 0.06739  0.01630  393 ASP A CG    
3269 O OD1   . ASP B 393 ? 1.44568 1.52897 1.32549 -0.12352 0.06326  0.01660  393 ASP A OD1   
3270 O OD2   . ASP B 393 ? 1.31703 1.40742 1.20641 -0.12175 0.07174  0.01087  393 ASP A OD2   
3271 N N     . GLN B 394 ? 1.24726 1.32374 1.12288 -0.12966 0.06545  0.03683  394 GLN A N     
3272 C CA    . GLN B 394 ? 1.26063 1.32969 1.13527 -0.13082 0.06366  0.04246  394 GLN A CA    
3273 C C     . GLN B 394 ? 1.25238 1.31894 1.11946 -0.13378 0.06081  0.04794  394 GLN A C     
3274 O O     . GLN B 394 ? 1.28483 1.34244 1.15205 -0.13286 0.05836  0.05137  394 GLN A O     
3275 C CB    . GLN B 394 ? 1.13274 1.20547 1.00974 -0.13307 0.06582  0.04358  394 GLN A CB    
3276 C CG    . GLN B 394 ? 1.27677 1.34278 1.15025 -0.13605 0.06359  0.04955  394 GLN A CG    
3277 C CD    . GLN B 394 ? 1.35843 1.41467 1.23427 -0.13439 0.06225  0.04974  394 GLN A CD    
3278 O OE1   . GLN B 394 ? 1.60071 1.65577 1.48147 -0.13092 0.06304  0.04605  394 GLN A OE1   
3279 N NE2   . GLN B 394 ? 1.21136 1.26004 1.08304 -0.13722 0.06027  0.05406  394 GLN A NE2   
3280 N N     . LYS B 395 ? 1.06746 1.14148 0.92846 -0.13722 0.06148  0.04884  395 LYS A N     
3281 C CA    . LYS B 395 ? 1.18822 1.26071 1.04208 -0.14074 0.05830  0.05516  395 LYS A CA    
3282 C C     . LYS B 395 ? 1.10270 1.17020 0.95686 -0.13893 0.05411  0.05627  395 LYS A C     
3283 O O     . LYS B 395 ? 1.10532 1.16615 0.95971 -0.13956 0.05099  0.06213  395 LYS A O     
3284 C CB    . LYS B 395 ? 0.98380 1.06587 0.82994 -0.14489 0.06036  0.05543  395 LYS A CB    
3285 C CG    . LYS B 395 ? 1.15751 1.24107 1.00012 -0.14936 0.06060  0.06195  395 LYS A CG    
3286 C CD    . LYS B 395 ? 1.08333 1.16591 0.93276 -0.14916 0.06281  0.06231  395 LYS A CD    
3287 C CE    . LYS B 395 ? 1.45630 1.53974 1.30330 -0.15385 0.06227  0.06924  395 LYS A CE    
3288 N NZ    . LYS B 395 ? 1.60013 1.68284 1.45395 -0.15436 0.06345  0.06985  395 LYS A NZ    
3289 N N     . ILE B 396 ? 1.21630 1.28669 1.07181 -0.13680 0.05398  0.05107  396 ILE A N     
3290 C CA    . ILE B 396 ? 1.26857 1.33524 1.12580 -0.13555 0.04920  0.05274  396 ILE A CA    
3291 C C     . ILE B 396 ? 1.20749 1.26475 1.07414 -0.13134 0.04877  0.05447  396 ILE A C     
3292 O O     . ILE B 396 ? 1.09963 1.15200 0.96952 -0.13077 0.04510  0.05916  396 ILE A O     
3293 C CB    . ILE B 396 ? 0.97170 1.04321 0.82821 -0.13472 0.04883  0.04638  396 ILE A CB    
3294 C CG1   . ILE B 396 ? 1.12187 1.19380 0.97328 -0.13750 0.04274  0.04971  396 ILE A CG1   
3295 C CG2   . ILE B 396 ? 1.14544 1.21375 1.01272 -0.12945 0.05020  0.04158  396 ILE A CG2   
3296 C CD1   . ILE B 396 ? 1.26549 1.34240 1.11124 -0.13881 0.04207  0.04327  396 ILE A CD1   
3297 N N     . GLU B 397 ? 1.17404 1.22877 1.04502 -0.12874 0.05253  0.05118  397 GLU A N     
3298 C CA    . GLU B 397 ? 1.25951 1.30451 1.13726 -0.12499 0.05327  0.05215  397 GLU A CA    
3299 C C     . GLU B 397 ? 1.20169 1.23901 1.07672 -0.12676 0.05296  0.05777  397 GLU A C     
3300 O O     . GLU B 397 ? 1.21584 1.24453 1.09527 -0.12452 0.05257  0.06061  397 GLU A O     
3301 C CB    . GLU B 397 ? 1.20077 1.24576 1.08220 -0.12253 0.05682  0.04709  397 GLU A CB    
3302 C CG    . GLU B 397 ? 1.40631 1.44121 1.29263 -0.11899 0.05836  0.04752  397 GLU A CG    
3303 C CD    . GLU B 397 ? 1.50373 1.53883 1.39311 -0.11716 0.06104  0.04338  397 GLU A CD    
3304 O OE1   . GLU B 397 ? 1.34469 1.38807 1.23449 -0.11828 0.06167  0.04026  397 GLU A OE1   
3305 O OE2   . GLU B 397 ? 1.45827 1.48512 1.34985 -0.11471 0.06276  0.04354  397 GLU A OE2   
3306 N N     . THR B 398 ? 1.16717 1.20736 1.03618 -0.13065 0.05341  0.05940  398 THR A N     
3307 C CA    . THR B 398 ? 1.09230 1.12450 0.95879 -0.13278 0.05291  0.06438  398 THR A CA    
3308 C C     . THR B 398 ? 1.18488 1.21816 1.04901 -0.13575 0.04945  0.07060  398 THR A C     
3309 O O     . THR B 398 ? 1.21618 1.24347 1.07866 -0.13804 0.04867  0.07524  398 THR A O     
3310 C CB    . THR B 398 ? 1.05520 1.08982 0.91813 -0.13575 0.05451  0.06362  398 THR A CB    
3311 O OG1   . THR B 398 ? 1.39964 1.44611 1.25969 -0.13853 0.05462  0.06341  398 THR A OG1   
3312 C CG2   . THR B 398 ? 0.93580 0.96895 0.80169 -0.13332 0.05696  0.05866  398 THR A CG2   
3313 N N     . TYR B 399 ? 1.13609 1.17623 0.99977 -0.13618 0.04697  0.07098  399 TYR A N     
3314 C CA    . TYR B 399 ? 1.24569 1.28780 1.10619 -0.13989 0.04270  0.07785  399 TYR A CA    
3315 C C     . TYR B 399 ? 1.34593 1.37810 1.21394 -0.13792 0.04045  0.08322  399 TYR A C     
3316 O O     . TYR B 399 ? 1.44728 1.47489 1.32307 -0.13347 0.04109  0.08122  399 TYR A O     
3317 C CB    . TYR B 399 ? 1.10832 1.15919 0.96498 -0.14138 0.03992  0.07670  399 TYR A CB    
3318 C CG    . TYR B 399 ? 1.36420 1.41754 1.21620 -0.14594 0.03464  0.08432  399 TYR A CG    
3319 C CD1   . TYR B 399 ? 1.26388 1.31671 1.11198 -0.14990 0.03404  0.09055  399 TYR A CD1   
3320 C CD2   . TYR B 399 ? 1.50160 1.55758 1.35342 -0.14674 0.02955  0.08592  399 TYR A CD2   
3321 C CE1   . TYR B 399 ? 1.37272 1.42788 1.21682 -0.15438 0.02887  0.09840  399 TYR A CE1   
3322 C CE2   . TYR B 399 ? 1.51512 1.57329 1.36227 -0.15154 0.02379  0.09375  399 TYR A CE2   
3323 C CZ    . TYR B 399 ? 1.54165 1.59954 1.38490 -0.15530 0.02359  0.10016  399 TYR A CZ    
3324 O OH    . TYR B 399 ? 1.60833 1.66851 1.44717 -0.16034 0.01760  0.10873  399 TYR A OH    
3325 N N     . VAL B 400 ? 1.37511 1.40397 1.24210 -0.14104 0.03828  0.09012  400 VAL A N     
3326 C CA    . VAL B 400 ? 1.35199 1.37124 1.22803 -0.13920 0.03632  0.09598  400 VAL A CA    
3327 C C     . VAL B 400 ? 1.44497 1.46953 1.32077 -0.14305 0.03004  0.10394  400 VAL A C     
3328 O O     . VAL B 400 ? 1.25298 1.27732 1.12548 -0.14716 0.02819  0.10986  400 VAL A O     
3329 C CB    . VAL B 400 ? 1.34330 1.35155 1.22016 -0.13937 0.03892  0.09763  400 VAL A CB    
3330 C CG1   . VAL B 400 ? 1.37963 1.37679 1.26738 -0.13644 0.03866  0.10225  400 VAL A CG1   
3331 C CG2   . VAL B 400 ? 1.23977 1.24380 1.11315 -0.13744 0.04401  0.09027  400 VAL A CG2   
3332 N N     . PRO B 401 ? 1.63725 1.66644 1.51626 -0.14239 0.02610  0.10479  401 PRO A N     
3333 C CA    . PRO B 401 ? 1.73593 1.77053 1.61282 -0.14701 0.01905  0.11262  401 PRO A CA    
3334 C C     . PRO B 401 ? 1.70499 1.73245 1.59133 -0.14762 0.01590  0.12232  401 PRO A C     
3335 O O     . PRO B 401 ? 1.92818 1.94583 1.82674 -0.14284 0.01870  0.12251  401 PRO A O     
3336 C CB    . PRO B 401 ? 1.58646 1.62468 1.46745 -0.14527 0.01552  0.11070  401 PRO A CB    
3337 C CG    . PRO B 401 ? 1.58714 1.61856 1.47869 -0.13850 0.02079  0.10491  401 PRO A CG    
3338 C CD    . PRO B 401 ? 1.49952 1.52861 1.38432 -0.13771 0.02767  0.09884  401 PRO A CD    
3339 N N     . ALA B 402 ? 1.52023 1.55220 1.40123 -0.15342 0.01059  0.13030  402 ALA A N     
3340 C CA    . ALA B 402 ? 1.65459 1.68019 1.54579 -0.15450 0.00689  0.14068  402 ALA A CA    
3341 C C     . ALA B 402 ? 1.76249 1.79580 1.64621 -0.16171 -0.00057 0.14992  402 ALA A C     
3342 O O     . ALA B 402 ? 1.76882 1.81171 1.63805 -0.16565 -0.00193 0.14717  402 ALA A O     
3343 C CB    . ALA B 402 ? 1.73299 1.74978 1.62571 -0.15335 0.01234  0.13957  402 ALA A CB    
3344 N N     . ARG B 403 ? 1.83235 1.86120 1.72554 -0.16349 -0.00501 0.16058  403 ARG A N     
3345 C CA    . ARG B 403 ? 1.87183 1.90751 1.75796 -0.17100 -0.01260 0.17101  403 ARG A CA    
3346 C C     . ARG B 403 ? 1.81629 1.86074 1.69474 -0.17424 -0.01922 0.17190  403 ARG A C     
3347 O O     . ARG B 403 ? 1.75769 1.81056 1.61878 -0.18071 -0.02161 0.17325  403 ARG A O     
3348 C CB    . ARG B 403 ? 1.79261 1.83263 1.66385 -0.17564 -0.00908 0.16993  403 ARG A CB    
3349 C CG    . ARG B 403 ? 1.81980 1.85053 1.69799 -0.17325 -0.00366 0.16905  403 ARG A CG    
3350 C CD    . ARG B 403 ? 1.87072 1.90647 1.73584 -0.17770 -0.00012 0.16766  403 ARG A CD    
3351 N NE    . ARG B 403 ? 2.24844 2.29134 2.10152 -0.17693 0.00524  0.15701  403 ARG A NE    
3352 C CZ    . ARG B 403 ? 2.03440 2.08825 1.87279 -0.18182 0.00565  0.15646  403 ARG A CZ    
3353 N NH1   . ARG B 403 ? 1.76305 1.82205 1.59514 -0.18828 0.00099  0.16611  403 ARG A NH1   
3354 N NH2   . ARG B 403 ? 1.84715 1.90647 1.67741 -0.18028 0.01108  0.14642  403 ARG A NH2   
3355 N N     . HIS B 404 ? 1.72144 1.76360 1.61194 -0.17018 -0.02183 0.17106  404 HIS A N     
3356 C CA    . HIS B 404 ? 1.85286 1.90216 1.73734 -0.17374 -0.02965 0.17253  404 HIS A CA    
3357 C C     . HIS B 404 ? 1.74784 1.80520 1.60911 -0.17733 -0.02670 0.16339  404 HIS A C     
3358 O O     . HIS B 404 ? 1.59230 1.65632 1.43876 -0.18446 -0.03287 0.16735  404 HIS A O     
3359 C CB    . HIS B 404 ? 1.84406 1.89556 1.73162 -0.18002 -0.04076 0.18717  404 HIS A CB    
3360 C CG    . HIS B 404 ? 2.03414 2.09039 1.92033 -0.18328 -0.05036 0.19026  404 HIS A CG    
3361 N ND1   . HIS B 404 ? 2.06477 2.12643 1.94137 -0.19182 -0.06103 0.20050  404 HIS A ND1   
3362 C CD2   . HIS B 404 ? 1.93878 1.99492 1.83153 -0.17967 -0.05139 0.18471  404 HIS A CD2   
3363 C CE1   . HIS B 404 ? 1.88270 1.94695 1.75965 -0.19350 -0.06871 0.20081  404 HIS A CE1   
3364 N NE2   . HIS B 404 ? 1.72061 1.78171 1.60811 -0.18606 -0.06296 0.19130  404 HIS A NE2   
3365 N N     . ASP B 405 ? 1.84928 1.90576 1.70730 -0.17274 -0.01737 0.15162  405 ASP A N     
3366 C CA    . ASP B 405 ? 1.80976 1.87368 1.64856 -0.17528 -0.01363 0.14224  405 ASP A CA    
3367 C C     . ASP B 405 ? 1.66564 1.73266 1.50128 -0.17636 -0.01943 0.13956  405 ASP A C     
3368 O O     . ASP B 405 ? 1.79327 1.85602 1.64455 -0.17144 -0.02134 0.13903  405 ASP A O     
3369 C CB    . ASP B 405 ? 1.65270 1.71502 1.49170 -0.17007 -0.00329 0.13131  405 ASP A CB    
3370 C CG    . ASP B 405 ? 1.70947 1.76561 1.56333 -0.16244 -0.00031 0.12542  405 ASP A CG    
3371 O OD1   . ASP B 405 ? 1.81378 1.86254 1.68322 -0.15910 -0.00165 0.13081  405 ASP A OD1   
3372 O OD2   . ASP B 405 ? 1.67215 1.73075 1.52226 -0.15991 0.00373  0.11564  405 ASP A OD2   
3373 N N     . VAL B 406 ? 1.28525 1.35896 1.10123 -0.18279 -0.02195 0.13797  406 VAL A N     
3374 C CA    . VAL B 406 ? 1.47235 1.54823 1.28265 -0.18502 -0.02838 0.13503  406 VAL A CA    
3375 C C     . VAL B 406 ? 1.46060 1.53665 1.27040 -0.17975 -0.02089 0.12096  406 VAL A C     
3376 O O     . VAL B 406 ? 1.45916 1.53819 1.25825 -0.17946 -0.01220 0.11313  406 VAL A O     
3377 C CB    . VAL B 406 ? 1.53266 1.61418 1.31976 -0.19457 -0.03387 0.13833  406 VAL A CB    
3378 C CG1   . VAL B 406 ? 1.35529 1.44149 1.12411 -0.19711 -0.02456 0.13248  406 VAL A CG1   
3379 C CG2   . VAL B 406 ? 1.53030 1.61293 1.30894 -0.19778 -0.04086 0.13447  406 VAL A CG2   
3380 N N     . HIS B 407 ? 1.34957 1.42270 1.17236 -0.17569 -0.02411 0.11861  407 HIS A N     
3381 C CA    . HIS B 407 ? 1.54233 1.61553 1.36589 -0.17087 -0.01789 0.10589  407 HIS A CA    
3382 C C     . HIS B 407 ? 1.50009 1.57530 1.31522 -0.17482 -0.02505 0.10267  407 HIS A C     
3383 O O     . HIS B 407 ? 1.39829 1.47208 1.22128 -0.17692 -0.03520 0.11052  407 HIS A O     
3384 C CB    . HIS B 407 ? 1.30745 1.37505 1.15300 -0.16241 -0.01388 0.10455  407 HIS A CB    
3385 C CG    . HIS B 407 ? 1.47887 1.54673 1.32516 -0.15754 -0.00640 0.09246  407 HIS A CG    
3386 N ND1   . HIS B 407 ? 1.56563 1.62944 1.42872 -0.15096 -0.00438 0.08956  407 HIS A ND1   
3387 C CD2   . HIS B 407 ? 1.48381 1.55559 1.31698 -0.15833 -0.00019 0.08304  407 HIS A CD2   
3388 C CE1   . HIS B 407 ? 1.67881 1.74416 1.53853 -0.14821 0.00207  0.07907  407 HIS A CE1   
3389 N NE2   . HIS B 407 ? 1.61566 1.68581 1.45809 -0.15244 0.00473  0.07489  407 HIS A NE2   
3390 N N     . TYR B 408 ? 1.46587 1.54389 1.26649 -0.17586 -0.02002 0.09150  408 TYR A N     
3391 C CA    . TYR B 408 ? 1.49782 1.57669 1.28691 -0.18056 -0.02658 0.08708  408 TYR A CA    
3392 C C     . TYR B 408 ? 1.49448 1.56998 1.30240 -0.17590 -0.03114 0.08583  408 TYR A C     
3393 O O     . TYR B 408 ? 1.42213 1.49730 1.22460 -0.17997 -0.03917 0.08438  408 TYR A O     
3394 C CB    . TYR B 408 ? 1.24868 1.33047 1.01895 -0.18208 -0.01808 0.07474  408 TYR A CB    
3395 C CG    . TYR B 408 ? 1.40248 1.48802 1.14963 -0.18948 -0.01647 0.07684  408 TYR A CG    
3396 C CD1   . TYR B 408 ? 1.33753 1.42429 1.08462 -0.19217 -0.01858 0.08824  408 TYR A CD1   
3397 C CD2   . TYR B 408 ? 1.58270 1.67019 1.30820 -0.19384 -0.01228 0.06741  408 TYR A CD2   
3398 C CE1   . TYR B 408 ? 1.45286 1.54337 1.17917 -0.19913 -0.01689 0.09085  408 TYR A CE1   
3399 C CE2   . TYR B 408 ? 1.31867 1.40955 1.02246 -0.20066 -0.00972 0.06936  408 TYR A CE2   
3400 C CZ    . TYR B 408 ? 1.32615 1.41890 1.03035 -0.20341 -0.01218 0.08147  408 TYR A CZ    
3401 O OH    . TYR B 408 ? 1.40638 1.50280 1.08946 -0.21034 -0.00946 0.08411  408 TYR A OH    
3402 N N     . TYR B 409 ? 1.45484 1.52759 1.28366 -0.16798 -0.02616 0.08634  409 TYR A N     
3403 C CA    . TYR B 409 ? 1.40214 1.47185 1.25101 -0.16315 -0.02958 0.08629  409 TYR A CA    
3404 C C     . TYR B 409 ? 1.46443 1.53296 1.32392 -0.16619 -0.04136 0.09893  409 TYR A C     
3405 O O     . TYR B 409 ? 1.59782 1.66559 1.46664 -0.16652 -0.04873 0.09986  409 TYR A O     
3406 C CB    . TYR B 409 ? 1.43708 1.50379 1.30276 -0.15440 -0.02000 0.08355  409 TYR A CB    
3407 C CG    . TYR B 409 ? 1.35092 1.41413 1.23958 -0.14873 -0.02179 0.08561  409 TYR A CG    
3408 C CD1   . TYR B 409 ? 1.25495 1.31824 1.14839 -0.14613 -0.02101 0.07770  409 TYR A CD1   
3409 C CD2   . TYR B 409 ? 1.41201 1.47162 1.31861 -0.14575 -0.02337 0.09548  409 TYR A CD2   
3410 C CE1   . TYR B 409 ? 1.27497 1.33550 1.19001 -0.14104 -0.02207 0.08011  409 TYR A CE1   
3411 C CE2   . TYR B 409 ? 1.44722 1.50379 1.37552 -0.14038 -0.02365 0.09754  409 TYR A CE2   
3412 C CZ    . TYR B 409 ? 1.40458 1.46191 1.33698 -0.13811 -0.02306 0.09009  409 TYR A CZ    
3413 O OH    . TYR B 409 ? 1.42828 1.48303 1.38265 -0.13293 -0.02291 0.09269  409 TYR A OH    
3414 N N     . ASN B 410 ? 1.29927 1.36775 1.15879 -0.16855 -0.04348 0.10899  410 ASN A N     
3415 C CA    . ASN B 410 ? 1.32954 1.39703 1.20228 -0.17125 -0.05479 0.12260  410 ASN A CA    
3416 C C     . ASN B 410 ? 1.41128 1.48141 1.27003 -0.18003 -0.06711 0.12469  410 ASN A C     
3417 O O     . ASN B 410 ? 1.43821 1.50776 1.31086 -0.18201 -0.07809 0.13424  410 ASN A O     
3418 C CB    . ASN B 410 ? 1.46303 1.52964 1.33833 -0.17217 -0.05419 0.13262  410 ASN A CB    
3419 C CG    . ASN B 410 ? 1.65338 1.71589 1.54133 -0.16406 -0.04264 0.12992  410 ASN A CG    
3420 O OD1   . ASN B 410 ? 1.53957 1.60023 1.43397 -0.15791 -0.03528 0.12106  410 ASN A OD1   
3421 N ND2   . ASN B 410 ? 1.51285 1.57336 1.40400 -0.16432 -0.04123 0.13754  410 ASN A ND2   
3422 N N     . PHE B 411 ? 1.55623 1.62876 1.38872 -0.18526 -0.06527 0.11613  411 PHE A N     
3423 C CA    . PHE B 411 ? 1.55667 1.63033 1.37138 -0.19439 -0.07644 0.11633  411 PHE A CA    
3424 C C     . PHE B 411 ? 1.57154 1.64320 1.40105 -0.19253 -0.08303 0.11428  411 PHE A C     
3425 O O     . PHE B 411 ? 1.66598 1.73744 1.49874 -0.19828 -0.09679 0.12287  411 PHE A O     
3426 C CB    . PHE B 411 ? 1.29507 1.37032 1.08124 -0.19800 -0.06920 0.10390  411 PHE A CB    
3427 C CG    . PHE B 411 ? 1.59246 1.66731 1.35561 -0.20747 -0.07840 0.10088  411 PHE A CG    
3428 C CD1   . PHE B 411 ? 1.74244 1.81724 1.50065 -0.21590 -0.09314 0.11277  411 PHE A CD1   
3429 C CD2   . PHE B 411 ? 1.61453 1.68838 1.36124 -0.20815 -0.07254 0.08616  411 PHE A CD2   
3430 C CE1   . PHE B 411 ? 1.74227 1.81565 1.47710 -0.22536 -0.10209 0.10975  411 PHE A CE1   
3431 C CE2   . PHE B 411 ? 1.66742 1.73936 1.39136 -0.21714 -0.08060 0.08247  411 PHE A CE2   
3432 C CZ    . PHE B 411 ? 1.72660 1.79807 1.44355 -0.22599 -0.09557 0.09414  411 PHE A CZ    
3433 N N     . ILE B 412 ? 1.47622 1.54657 1.31562 -0.18492 -0.07392 0.10388  412 ILE A N     
3434 C CA    . ILE B 412 ? 1.34903 1.41761 1.20353 -0.18276 -0.07921 0.10118  412 ILE A CA    
3435 C C     . ILE B 412 ? 1.38503 1.45298 1.26639 -0.18121 -0.08804 0.11531  412 ILE A C     
3436 O O     . ILE B 412 ? 1.70389 1.77163 1.59101 -0.18556 -0.10031 0.11978  412 ILE A O     
3437 C CB    . ILE B 412 ? 1.32893 1.39638 1.19317 -0.17386 -0.06682 0.08977  412 ILE A CB    
3438 C CG1   . ILE B 412 ? 1.30528 1.37396 1.14789 -0.17390 -0.05579 0.07789  412 ILE A CG1   
3439 C CG2   . ILE B 412 ? 1.55825 1.62413 1.43402 -0.17271 -0.07195 0.08548  412 ILE A CG2   
3440 C CD1   . ILE B 412 ? 1.54295 1.61176 1.36009 -0.18158 -0.05953 0.06972  412 ILE A CD1   
3441 N N     . LYS B 413 ? 1.26799 1.33529 1.16541 -0.17551 -0.08209 0.12217  413 LYS A N     
3442 C CA    . LYS B 413 ? 1.47981 1.54601 1.40621 -0.17269 -0.08816 0.13528  413 LYS A CA    
3443 C C     . LYS B 413 ? 1.58487 1.65292 1.50806 -0.18190 -0.10400 0.14801  413 LYS A C     
3444 O O     . LYS B 413 ? 1.76361 1.83178 1.70699 -0.18264 -0.11409 0.15643  413 LYS A O     
3445 C CB    . LYS B 413 ? 1.33372 1.39758 1.27302 -0.16554 -0.07742 0.13863  413 LYS A CB    
3446 C CG    . LYS B 413 ? 1.54579 1.60815 1.47822 -0.15918 -0.06250 0.12585  413 LYS A CG    
3447 C CD    . LYS B 413 ? 1.60625 1.66486 1.55075 -0.15243 -0.05226 0.12844  413 LYS A CD    
3448 C CE    . LYS B 413 ? 1.56550 1.62046 1.53909 -0.14537 -0.05023 0.13334  413 LYS A CE    
3449 N NZ    . LYS B 413 ? 1.59687 1.64663 1.57899 -0.13909 -0.03932 0.13399  413 LYS A NZ    
3450 N N     . ARG B 414 ? 1.46453 1.53420 1.36391 -0.18893 -0.10633 0.15001  414 ARG A N     
3451 C CA    . ARG B 414 ? 1.43904 1.51044 1.33373 -0.19846 -0.12182 0.16339  414 ARG A CA    
3452 C C     . ARG B 414 ? 1.62582 1.69752 1.51060 -0.20598 -0.13464 0.16143  414 ARG A C     
3453 O O     . ARG B 414 ? 1.85129 1.92372 1.74841 -0.21099 -0.14926 0.17409  414 ARG A O     
3454 C CB    . ARG B 414 ? 1.60664 1.67971 1.47491 -0.20464 -0.12025 0.16478  414 ARG A CB    
3455 C CG    . ARG B 414 ? 1.77944 1.85171 1.65733 -0.19829 -0.10915 0.16761  414 ARG A CG    
3456 C CD    . ARG B 414 ? 1.71718 1.79157 1.57031 -0.20464 -0.10779 0.16973  414 ARG A CD    
3457 N NE    . ARG B 414 ? 1.74458 1.82038 1.56861 -0.20710 -0.10014 0.15566  414 ARG A NE    
3458 C CZ    . ARG B 414 ? 1.56721 1.64371 1.38120 -0.20407 -0.08733 0.14873  414 ARG A CZ    
3459 N NH1   . ARG B 414 ? 1.39823 1.47305 1.22949 -0.19731 -0.07988 0.15209  414 ARG A NH1   
3460 N NH2   . ARG B 414 ? 1.55154 1.63004 1.33872 -0.20791 -0.08187 0.13845  414 ARG A NH2   
3461 N N     . ASN B 415 ? 1.52176 1.59256 1.38588 -0.20694 -0.12963 0.14639  415 ASN A N     
3462 C CA    . ASN B 415 ? 1.74415 1.81382 1.59482 -0.21503 -0.14170 0.14295  415 ASN A CA    
3463 C C     . ASN B 415 ? 1.77901 1.84718 1.65342 -0.20912 -0.14226 0.13877  415 ASN A C     
3464 O O     . ASN B 415 ? 1.85754 1.92393 1.72232 -0.21484 -0.15097 0.13380  415 ASN A O     
3465 C CB    . ASN B 415 ? 1.70059 1.76919 1.51435 -0.22043 -0.13659 0.12898  415 ASN A CB    
3466 C CG    . ASN B 415 ? 1.88798 1.95803 1.67509 -0.22940 -0.14015 0.13463  415 ASN A CG    
3467 O OD1   . ASN B 415 ? 1.92110 1.99031 1.67711 -0.23456 -0.13582 0.12459  415 ASN A OD1   
3468 N ND2   . ASN B 415 ? 1.94722 2.01932 1.74632 -0.23143 -0.14763 0.15073  415 ASN A ND2   
3469 N N     . ALA B 416 ? 1.71648 1.78485 1.62021 -0.19859 -0.13357 0.14092  416 ALA A N     
3470 C CA    . ALA B 416 ? 1.67596 1.74316 1.60248 -0.19234 -0.13211 0.13662  416 ALA A CA    
3471 C C     . ALA B 416 ? 1.61997 1.68732 1.55744 -0.19889 -0.14976 0.14503  416 ALA A C     
3472 O O     . ALA B 416 ? 1.68718 1.75293 1.62349 -0.20000 -0.15293 0.13706  416 ALA A O     
3473 C CB    . ALA B 416 ? 1.65983 1.72692 1.61617 -0.18135 -0.12159 0.14089  416 ALA A CB    
3474 N N     . GLN B 417 ? 1.59170 1.66081 1.54057 -0.20333 -0.16141 0.16111  417 GLN A N     
3475 C CA    . GLN B 417 ? 1.60656 1.67630 1.56968 -0.20984 -0.17962 0.17138  417 GLN A CA    
3476 C C     . GLN B 417 ? 1.54660 1.61401 1.47750 -0.22080 -0.18991 0.16308  417 GLN A C     
3477 O O     . GLN B 417 ? 1.60766 1.67381 1.54730 -0.22371 -0.19984 0.16250  417 GLN A O     
3478 C CB    . GLN B 417 ? 1.59899 1.67122 1.57630 -0.21387 -0.19066 0.19044  417 GLN A CB    
3479 C CG    . GLN B 417 ? 1.83123 1.90452 1.84196 -0.20328 -0.18079 0.19896  417 GLN A CG    
3480 C CD    . GLN B 417 ? 2.00271 2.07503 2.00022 -0.19826 -0.16534 0.19364  417 GLN A CD    
3481 O OE1   . GLN B 417 ? 1.79742 1.86921 1.76174 -0.20244 -0.16144 0.18420  417 GLN A OE1   
3482 N NE2   . GLN B 417 ? 1.89896 1.97069 1.92288 -0.18935 -0.15614 0.19971  417 GLN A NE2   
3483 N N     . ASN B 418 ? 1.44542 1.51185 1.34052 -0.22677 -0.18727 0.15683  418 ASN A N     
3484 C CA    . ASN B 418 ? 1.51769 1.58071 1.37826 -0.23799 -0.19621 0.14846  418 ASN A CA    
3485 C C     . ASN B 418 ? 1.43684 1.49644 1.28997 -0.23380 -0.18666 0.12998  418 ASN A C     
3486 O O     . ASN B 418 ? 1.73815 1.79390 1.57848 -0.24112 -0.19672 0.12446  418 ASN A O     
3487 C CB    . ASN B 418 ? 1.85219 1.91521 1.67725 -0.24561 -0.19521 0.14792  418 ASN A CB    
3488 C CG    . ASN B 418 ? 1.84618 1.91196 1.67638 -0.25237 -0.20871 0.16705  418 ASN A CG    
3489 O OD1   . ASN B 418 ? 1.63637 1.70413 1.49843 -0.25092 -0.21855 0.18073  418 ASN A OD1   
3490 N ND2   . ASN B 418 ? 1.85371 1.91986 1.65441 -0.25973 -0.20920 0.16887  418 ASN A ND2   
3491 N N     . ILE B 419 ? 1.49046 1.55098 1.35110 -0.22290 -0.16850 0.12098  419 ILE A N     
3492 C CA    . ILE B 419 ? 1.67065 1.72826 1.52779 -0.21820 -0.15908 0.10418  419 ILE A CA    
3493 C C     . ILE B 419 ? 1.65840 1.71624 1.55071 -0.21218 -0.16238 0.10753  419 ILE A C     
3494 O O     . ILE B 419 ? 1.74076 1.80087 1.65834 -0.20167 -0.15167 0.10967  419 ILE A O     
3495 C CB    . ILE B 419 ? 1.71241 1.77097 1.56165 -0.21004 -0.13924 0.09324  419 ILE A CB    
3496 C CG1   . ILE B 419 ? 1.59293 1.65511 1.46238 -0.20217 -0.13116 0.10271  419 ILE A CG1   
3497 C CG2   . ILE B 419 ? 1.83563 1.89268 1.64607 -0.21694 -0.13536 0.08403  419 ILE A CG2   
3498 C CD1   . ILE B 419 ? 1.64475 1.70777 1.50449 -0.19569 -0.11346 0.09330  419 ILE A CD1   
3499 N N     . GLN B 420 ? 1.58413 1.63930 1.47714 -0.21902 -0.17663 0.10791  420 GLN A N     
3500 C CA    . GLN B 420 ? 1.56723 1.62289 1.49446 -0.21405 -0.18061 0.11159  420 GLN A CA    
3501 C C     . GLN B 420 ? 1.68392 1.73645 1.60842 -0.20902 -0.17049 0.09494  420 GLN A C     
3502 O O     . GLN B 420 ? 1.60411 1.65711 1.55655 -0.20361 -0.17067 0.09614  420 GLN A O     
3503 C CB    . GLN B 420 ? 1.79123 1.84591 1.72437 -0.22406 -0.20214 0.12195  420 GLN A CB    
3504 C CG    . GLN B 420 ? 1.90758 1.96599 1.85013 -0.22838 -0.21299 0.14058  420 GLN A CG    
3505 C CD    . GLN B 420 ? 1.84133 1.90130 1.81291 -0.23224 -0.23055 0.15496  420 GLN A CD    
3506 O OE1   . GLN B 420 ? 1.65660 1.71493 1.64216 -0.23171 -0.23491 0.15130  420 GLN A OE1   
3507 N NE2   . GLN B 420 ? 1.85039 1.91376 1.83328 -0.23614 -0.24095 0.17216  420 GLN A NE2   
3508 N N     . ILE B 421 ? 1.69760 1.74719 1.59099 -0.21077 -0.16188 0.08053  421 ILE A N     
3509 C CA    . ILE B 421 ? 1.66527 1.71201 1.55747 -0.20525 -0.15085 0.06461  421 ILE A CA    
3510 C C     . ILE B 421 ? 1.44164 1.49001 1.32121 -0.19872 -0.13246 0.05609  421 ILE A C     
3511 O O     . ILE B 421 ? 1.50368 1.55049 1.35236 -0.20416 -0.12982 0.04954  421 ILE A O     
3512 C CB    . ILE B 421 ? 1.80106 1.84117 1.67037 -0.21442 -0.15970 0.05364  421 ILE A CB    
3513 C CG1   . ILE B 421 ? 1.57913 1.61596 1.44442 -0.20896 -0.14702 0.03652  421 ILE A CG1   
3514 C CG2   . ILE B 421 ? 1.92714 1.96457 1.75928 -0.22561 -0.16617 0.05269  421 ILE A CG2   
3515 C CD1   . ILE B 421 ? 1.49896 1.52796 1.34555 -0.21716 -0.15517 0.02500  421 ILE A CD1   
3516 N N     . GLY B 422 ? 1.45317 1.50449 1.35583 -0.18783 -0.12039 0.05675  422 GLY A N     
3517 C CA    . GLY B 422 ? 1.48429 1.53731 1.37771 -0.18164 -0.10380 0.04991  422 GLY A CA    
3518 C C     . GLY B 422 ? 1.51213 1.56427 1.41632 -0.17372 -0.09248 0.03902  422 GLY A C     
3519 O O     . GLY B 422 ? 1.57419 1.62614 1.50322 -0.16974 -0.09511 0.04175  422 GLY A O     
3520 N N     . ILE B 423 ? 1.42720 1.47912 1.31466 -0.17160 -0.08036 0.02777  423 ILE A N     
3521 C CA    . ILE B 423 ? 1.41530 1.46638 1.31252 -0.16454 -0.06990 0.01719  423 ILE A CA    
3522 C C     . ILE B 423 ? 1.36448 1.41893 1.26697 -0.15663 -0.05565 0.01743  423 ILE A C     
3523 O O     . ILE B 423 ? 1.39782 1.45430 1.28698 -0.15830 -0.05272 0.02098  423 ILE A O     
3524 C CB    . ILE B 423 ? 1.30322 1.35022 1.17879 -0.16908 -0.06854 0.00249  423 ILE A CB    
3525 C CG1   . ILE B 423 ? 1.68437 1.73238 1.53415 -0.17105 -0.05948 -0.00363 423 ILE A CG1   
3526 C CG2   . ILE B 423 ? 1.38841 1.43082 1.25464 -0.17837 -0.08374 0.00237  423 ILE A CG2   
3527 C CD1   . ILE B 423 ? 1.91958 1.96277 1.74558 -0.17660 -0.05824 -0.01765 423 ILE A CD1   
3528 N N     . THR B 424 ? 1.34370 1.39851 1.26484 -0.14882 -0.04778 0.01436  424 THR A N     
3529 C CA    . THR B 424 ? 1.13533 1.19260 1.06204 -0.14169 -0.03520 0.01497  424 THR A CA    
3530 C C     . THR B 424 ? 1.05030 1.10702 0.98493 -0.13633 -0.02682 0.00545  424 THR A C     
3531 O O     . THR B 424 ? 1.18963 1.24392 1.12176 -0.13876 -0.03014 -0.00264 424 THR A O     
3532 C CB    . THR B 424 ? 1.19053 1.24881 1.13786 -0.13722 -0.03577 0.02735  424 THR A CB    
3533 O OG1   . THR B 424 ? 1.57300 1.63156 1.51622 -0.14285 -0.04586 0.03662  424 THR A OG1   
3534 C CG2   . THR B 424 ? 1.04440 1.10395 0.99280 -0.13164 -0.02437 0.02893  424 THR A CG2   
3535 N N     . ASN B 425 ? 1.24960 1.30796 1.19331 -0.12967 -0.01673 0.00643  425 ASN A N     
3536 C CA    . ASN B 425 ? 1.11583 1.17403 1.06957 -0.12433 -0.00903 -0.00100 425 ASN A CA    
3537 C C     . ASN B 425 ? 1.13275 1.19108 1.10849 -0.11772 -0.00559 0.00642  425 ASN A C     
3538 O O     . ASN B 425 ? 1.13524 1.19393 1.11326 -0.11644 -0.00462 0.01498  425 ASN A O     
3539 C CB    . ASN B 425 ? 1.14861 1.20854 1.08869 -0.12356 0.00064  -0.00872 425 ASN A CB    
3540 C CG    . ASN B 425 ? 1.42529 1.48508 1.37521 -0.11919 0.00711  -0.01668 425 ASN A CG    
3541 O OD1   . ASN B 425 ? 1.63860 1.69866 1.60552 -0.11370 0.01066  -0.01325 425 ASN A OD1   
3542 N ND2   . ASN B 425 ? 1.39414 1.45320 1.33354 -0.12162 0.00911  -0.02720 425 ASN A ND2   
3543 N N     . HIS B 426 ? 1.17299 1.23059 1.16400 -0.11382 -0.00344 0.00319  426 HIS A N     
3544 C CA    . HIS B 426 ? 1.12777 1.18512 1.13877 -0.10768 0.00078  0.00989  426 HIS A CA    
3545 C C     . HIS B 426 ? 1.21037 1.26823 1.21603 -0.10464 0.00927  0.01317  426 HIS A C     
3546 O O     . HIS B 426 ? 1.16417 1.22077 1.17873 -0.10192 0.01080  0.02156  426 HIS A O     
3547 C CB    . HIS B 426 ? 1.20771 1.26477 1.23123 -0.10400 0.00450  0.00437  426 HIS A CB    
3548 C CG    . HIS B 426 ? 0.88056 0.93633 0.91734 -0.10519 -0.00295 0.00344  426 HIS A CG    
3549 N ND1   . HIS B 426 ? 1.21499 1.26996 1.25623 -0.10464 -0.00216 -0.00490 426 HIS A ND1   
3550 C CD2   . HIS B 426 ? 1.01156 1.06665 1.05959 -0.10692 -0.01135 0.00989  426 HIS A CD2   
3551 C CE1   . HIS B 426 ? 1.18846 1.24189 1.24214 -0.10626 -0.01011 -0.00380 426 HIS A CE1   
3552 N NE2   . HIS B 426 ? 1.11375 1.16751 1.17189 -0.10777 -0.01599 0.00536  426 HIS A NE2   
3553 N N     . ALA B 427 ? 1.21086 1.27013 1.20290 -0.10518 0.01487  0.00666  427 ALA A N     
3554 C CA    . ALA B 427 ? 1.15557 1.21508 1.14232 -0.10284 0.02241  0.00941  427 ALA A CA    
3555 C C     . ALA B 427 ? 1.03580 1.09434 1.01675 -0.10478 0.01979  0.01733  427 ALA A C     
3556 O O     . ALA B 427 ? 1.30066 1.35699 1.28693 -0.10163 0.02392  0.02335  427 ALA A O     
3557 C CB    . ALA B 427 ? 1.14232 1.20429 1.11581 -0.10422 0.02727  0.00177  427 ALA A CB    
3558 N N     . HIS B 428 ? 0.98779 1.04739 0.95771 -0.11010 0.01312  0.01734  428 HIS A N     
3559 C CA    . HIS B 428 ? 1.01592 1.07490 0.98089 -0.11249 0.00971  0.02561  428 HIS A CA    
3560 C C     . HIS B 428 ? 1.04312 1.09985 1.02669 -0.11005 0.00594  0.03433  428 HIS A C     
3561 O O     . HIS B 428 ? 1.20135 1.25611 1.18883 -0.10831 0.00808  0.04168  428 HIS A O     
3562 C CB    . HIS B 428 ? 1.15880 1.21952 1.10693 -0.11942 0.00282  0.02400  428 HIS A CB    
3563 C CG    . HIS B 428 ? 1.23097 1.29398 1.16070 -0.12177 0.00798  0.01687  428 HIS A CG    
3564 N ND1   . HIS B 428 ? 1.12715 1.19124 1.05044 -0.12285 0.01001  0.00669  428 HIS A ND1   
3565 C CD2   . HIS B 428 ? 1.08681 1.15119 1.00448 -0.12321 0.01188  0.01867  428 HIS A CD2   
3566 C CE1   . HIS B 428 ? 1.05959 1.12601 0.96802 -0.12466 0.01556  0.00270  428 HIS A CE1   
3567 N NE2   . HIS B 428 ? 1.26854 1.33541 1.17330 -0.12505 0.01648  0.01009  428 HIS A NE2   
3568 N N     . LEU B 429 ? 1.02941 1.08616 1.02539 -0.10977 0.00101  0.03354  429 LEU A N     
3569 C CA    . LEU B 429 ? 0.96034 1.01573 0.97636 -0.10776 -0.00299 0.04260  429 LEU A CA    
3570 C C     . LEU B 429 ? 1.03826 1.09093 1.06574 -0.10140 0.00631  0.04722  429 LEU A C     
3571 O O     . LEU B 429 ? 1.09386 1.14477 1.13221 -0.10001 0.00556  0.05602  429 LEU A O     
3572 C CB    . LEU B 429 ? 1.01483 1.07077 1.04334 -0.10804 -0.00847 0.04001  429 LEU A CB    
3573 C CG    . LEU B 429 ? 0.99595 1.05159 1.04579 -0.10745 -0.01496 0.04947  429 LEU A CG    
3574 C CD1   . LEU B 429 ? 1.10399 1.16043 1.14807 -0.11330 -0.02506 0.05566  429 LEU A CD1   
3575 C CD2   . LEU B 429 ? 1.09705 1.15310 1.15983 -0.10751 -0.01954 0.04630  429 LEU A CD2   
3576 N N     . ILE B 430 ? 0.95564 1.00759 0.98072 -0.09794 0.01472  0.04171  430 ILE A N     
3577 C CA    . ILE B 430 ? 1.02974 1.07800 1.06390 -0.09241 0.02361  0.04559  430 ILE A CA    
3578 C C     . ILE B 430 ? 1.12614 1.17175 1.14758 -0.09259 0.02853  0.04752  430 ILE A C     
3579 O O     . ILE B 430 ? 1.17985 1.22101 1.20518 -0.08873 0.03605  0.05018  430 ILE A O     
3580 C CB    . ILE B 430 ? 1.00372 1.05204 1.04126 -0.08924 0.02938  0.03993  430 ILE A CB    
3581 C CG1   . ILE B 430 ? 1.35400 1.40408 1.37477 -0.09095 0.03235  0.03235  430 ILE A CG1   
3582 C CG2   . ILE B 430 ? 1.09966 1.15013 1.15107 -0.08915 0.02432  0.03824  430 ILE A CG2   
3583 C CD1   . ILE B 430 ? 1.43763 1.48891 1.46307 -0.08878 0.03579  0.02658  430 ILE A CD1   
3584 N N     . HIS B 431 ? 1.15980 1.20753 1.16615 -0.09717 0.02458  0.04627  431 HIS A N     
3585 C CA    . HIS B 431 ? 1.17276 1.21818 1.16697 -0.09779 0.02890  0.04797  431 HIS A CA    
3586 C C     . HIS B 431 ? 1.14779 1.18846 1.15173 -0.09575 0.02996  0.05682  431 HIS A C     
3587 O O     . HIS B 431 ? 1.14950 1.19050 1.16771 -0.09537 0.02508  0.06229  431 HIS A O     
3588 C CB    . HIS B 431 ? 1.13810 1.18732 1.11496 -0.10338 0.02449  0.04540  431 HIS A CB    
3589 C CG    . HIS B 431 ? 1.11066 1.16297 1.07571 -0.10443 0.02796  0.03680  431 HIS A CG    
3590 N ND1   . HIS B 431 ? 1.45884 1.51204 1.42982 -0.10174 0.03108  0.03095  431 HIS A ND1   
3591 C CD2   . HIS B 431 ? 1.26428 1.31920 1.21363 -0.10778 0.02913  0.03361  431 HIS A CD2   
3592 C CE1   . HIS B 431 ? 1.45735 1.51357 1.41740 -0.10327 0.03400  0.02446  431 HIS A CE1   
3593 N NE2   . HIS B 431 ? 1.10058 1.15801 1.04737 -0.10691 0.03315  0.02589  431 HIS A NE2   
3594 N N     . SER B 432 ? 1.20125 1.23741 1.19838 -0.09470 0.03596  0.05829  432 SER A N     
3595 C CA    . SER B 432 ? 1.30194 1.33199 1.30853 -0.09220 0.03880  0.06589  432 SER A CA    
3596 C C     . SER B 432 ? 1.53738 1.56945 1.54807 -0.09543 0.03060  0.07288  432 SER A C     
3597 O O     . SER B 432 ? 1.46113 1.49830 1.46023 -0.10052 0.02381  0.07131  432 SER A O     
3598 C CB    . SER B 432 ? 1.41175 1.43587 1.40752 -0.09148 0.04594  0.06504  432 SER A CB    
3599 O OG    . SER B 432 ? 1.34388 1.37116 1.32357 -0.09612 0.04280  0.06316  432 SER A OG    
3600 N N     . ASP B 433 ? 1.53106 1.55902 1.55771 -0.09268 0.03162  0.08059  433 ASP A N     
3601 C CA    . ASP B 433 ? 1.58600 1.61574 1.61980 -0.09568 0.02325  0.08900  433 ASP A CA    
3602 C C     . ASP B 433 ? 1.61952 1.64911 1.63652 -0.09995 0.02136  0.08977  433 ASP A C     
3603 O O     . ASP B 433 ? 1.68919 1.72357 1.70129 -0.10521 0.01204  0.09303  433 ASP A O     
3604 C CB    . ASP B 433 ? 1.68233 1.70708 1.73827 -0.09121 0.02653  0.09732  433 ASP A CB    
3605 C CG    . ASP B 433 ? 1.98506 2.01147 2.05176 -0.09400 0.01788  0.10740  433 ASP A CG    
3606 O OD1   . ASP B 433 ? 1.85220 1.88491 1.92206 -0.09803 0.00715  0.10989  433 ASP A OD1   
3607 O OD2   . ASP B 433 ? 2.04345 2.06439 2.11529 -0.09243 0.02157  0.11283  433 ASP A OD2   
3608 N N     . VAL B 434 ? 1.58750 1.61157 1.59554 -0.09823 0.02956  0.08714  434 VAL A N     
3609 C CA    . VAL B 434 ? 1.69298 1.71647 1.68666 -0.10222 0.02817  0.08863  434 VAL A CA    
3610 C C     . VAL B 434 ? 1.63502 1.66651 1.61166 -0.10786 0.02216  0.08399  434 VAL A C     
3611 O O     . VAL B 434 ? 1.56754 1.60130 1.53521 -0.11261 0.01716  0.08769  434 VAL A O     
3612 C CB    . VAL B 434 ? 1.39144 1.40736 1.37723 -0.09994 0.03761  0.08547  434 VAL A CB    
3613 C CG1   . VAL B 434 ? 1.48614 1.49267 1.48670 -0.09470 0.04454  0.08949  434 VAL A CG1   
3614 C CG2   . VAL B 434 ? 1.60486 1.62207 1.57983 -0.09915 0.04246  0.07639  434 VAL A CG2   
3615 N N     . GLU B 435 ? 1.40326 1.43854 1.37597 -0.10736 0.02309  0.07633  435 GLU A N     
3616 C CA    . GLU B 435 ? 1.56276 1.60484 1.51936 -0.11227 0.01912  0.07064  435 GLU A CA    
3617 C C     . GLU B 435 ? 1.53115 1.57778 1.49190 -0.11519 0.00994  0.07178  435 GLU A C     
3618 O O     . GLU B 435 ? 1.44336 1.49463 1.38988 -0.12062 0.00484  0.06932  435 GLU A O     
3619 C CB    . GLU B 435 ? 1.57271 1.61582 1.52275 -0.11028 0.02570  0.06141  435 GLU A CB    
3620 C CG    . GLU B 435 ? 1.65824 1.70746 1.59161 -0.11483 0.02423  0.05537  435 GLU A CG    
3621 C CD    . GLU B 435 ? 1.65926 1.70929 1.58662 -0.11314 0.03146  0.04806  435 GLU A CD    
3622 O OE1   . GLU B 435 ? 1.74617 1.79253 1.67131 -0.11187 0.03651  0.04943  435 GLU A OE1   
3623 O OE2   . GLU B 435 ? 1.40123 1.45523 1.32661 -0.11333 0.03174  0.04120  435 GLU A OE2   
3624 N N     . ASN B 436 ? 1.57311 1.61811 1.55237 -0.11201 0.00805  0.07549  436 ASN A N     
3625 C CA    . ASN B 436 ? 1.57558 1.62431 1.56075 -0.11518 -0.00193 0.07746  436 ASN A CA    
3626 C C     . ASN B 436 ? 1.61194 1.65904 1.61427 -0.11507 -0.00759 0.08902  436 ASN A C     
3627 O O     . ASN B 436 ? 1.51106 1.55770 1.53265 -0.11218 -0.00931 0.09225  436 ASN A O     
3628 C CB    . ASN B 436 ? 1.16973 1.21940 1.16316 -0.11227 -0.00055 0.07128  436 ASN A CB    
3629 C CG    . ASN B 436 ? 1.45225 1.50519 1.42885 -0.11482 0.00035  0.06080  436 ASN A CG    
3630 O OD1   . ASN B 436 ? 1.64926 1.70403 1.60791 -0.11865 0.00060  0.05819  436 ASN A OD1   
3631 N ND2   . ASN B 436 ? 1.23169 1.28539 1.21485 -0.11270 0.00124  0.05497  436 ASN A ND2   
3632 N N     . SER B 437 ? 1.53886 1.58531 1.53586 -0.11810 -0.01029 0.09552  437 SER A N     
3633 C CA    . SER B 437 ? 1.49165 1.53659 1.50656 -0.11812 -0.01586 0.10757  437 SER A CA    
3634 C C     . SER B 437 ? 1.52237 1.57226 1.53726 -0.12470 -0.02986 0.11243  437 SER A C     
3635 O O     . SER B 437 ? 1.62935 1.67912 1.66272 -0.12504 -0.03645 0.12305  437 SER A O     
3636 C CB    . SER B 437 ? 1.54415 1.58582 1.55491 -0.11864 -0.01318 0.11290  437 SER A CB    
3637 O OG    . SER B 437 ? 1.66297 1.70823 1.65105 -0.12509 -0.01724 0.11095  437 SER A OG    
3638 N N     . ILE B 438 ? 1.37266 1.42632 1.36771 -0.12991 -0.03414 0.10500  438 ILE A N     
3639 C CA    . ILE B 438 ? 1.37661 1.43387 1.36755 -0.13726 -0.04797 0.10836  438 ILE A CA    
3640 C C     . ILE B 438 ? 1.52819 1.58556 1.54225 -0.13482 -0.05264 0.11123  438 ILE A C     
3641 O O     . ILE B 438 ? 1.39225 1.45145 1.41408 -0.13967 -0.06504 0.11948  438 ILE A O     
3642 C CB    . ILE B 438 ? 1.54792 1.60772 1.51172 -0.14273 -0.04922 0.09777  438 ILE A CB    
3643 C CG1   . ILE B 438 ? 1.28833 1.35031 1.24458 -0.15098 -0.06332 0.10006  438 ILE A CG1   
3644 C CG2   . ILE B 438 ? 1.65519 1.71438 1.61777 -0.13778 -0.03993 0.08564  438 ILE A CG2   
3645 C CD1   . ILE B 438 ? 1.49083 1.55390 1.44542 -0.15717 -0.07367 0.11248  438 ILE A CD1   
3646 N N     . TYR B 439 ? 1.59225 1.64783 1.61754 -0.12789 -0.04344 0.10552  439 TYR A N     
3647 C CA    . TYR B 439 ? 1.53687 1.59294 1.58479 -0.12542 -0.04705 0.10791  439 TYR A CA    
3648 C C     . TYR B 439 ? 1.53297 1.58856 1.60655 -0.12397 -0.05152 0.12187  439 TYR A C     
3649 O O     . TYR B 439 ? 1.61173 1.66897 1.70501 -0.12423 -0.05863 0.12716  439 TYR A O     
3650 C CB    . TYR B 439 ? 1.31000 1.36409 1.36504 -0.11810 -0.03521 0.10017  439 TYR A CB    
3651 C CG    . TYR B 439 ? 1.26447 1.31952 1.29911 -0.11933 -0.03172 0.08704  439 TYR A CG    
3652 C CD1   . TYR B 439 ? 1.28100 1.33844 1.29663 -0.12652 -0.04005 0.08205  439 TYR A CD1   
3653 C CD2   . TYR B 439 ? 1.34793 1.40114 1.38281 -0.11346 -0.02005 0.07985  439 TYR A CD2   
3654 C CE1   . TYR B 439 ? 1.31795 1.37593 1.31689 -0.12723 -0.03585 0.06995  439 TYR A CE1   
3655 C CE2   . TYR B 439 ? 1.22406 1.27844 1.24337 -0.11435 -0.01694 0.06868  439 TYR A CE2   
3656 C CZ    . TYR B 439 ? 1.17040 1.22718 1.17257 -0.12094 -0.02439 0.06354  439 TYR A CZ    
3657 O OH    . TYR B 439 ? 1.39118 1.44877 1.37967 -0.12143 -0.02034 0.05235  439 TYR A OH    
3658 N N     . GLN B 440 ? 1.33239 1.38568 1.40744 -0.12247 -0.04750 0.12804  440 GLN A N     
3659 C CA    . GLN B 440 ? 1.44945 1.50216 1.55037 -0.12120 -0.05177 0.14199  440 GLN A CA    
3660 C C     . GLN B 440 ? 1.42589 1.48304 1.52723 -0.12973 -0.06927 0.14999  440 GLN A C     
3661 O O     . GLN B 440 ? 1.53301 1.59137 1.66061 -0.12937 -0.07601 0.16134  440 GLN A O     
3662 C CB    . GLN B 440 ? 1.38893 1.43756 1.48881 -0.11868 -0.04447 0.14616  440 GLN A CB    
3663 C CG    . GLN B 440 ? 1.53765 1.58069 1.63608 -0.11102 -0.02797 0.13858  440 GLN A CG    
3664 C CD    . GLN B 440 ? 1.71585 1.75377 1.81053 -0.10937 -0.02131 0.14157  440 GLN A CD    
3665 O OE1   . GLN B 440 ? 1.89852 1.93733 1.99323 -0.11355 -0.02859 0.14989  440 GLN A OE1   
3666 N NE2   . GLN B 440 ? 1.72933 1.76140 1.82051 -0.10362 -0.00777 0.13499  440 GLN A NE2   
3667 N N     . LEU B 441 ? 1.34714 1.40643 1.42044 -0.13731 -0.07615 0.14444  441 LEU A N     
3668 C CA    . LEU B 441 ? 1.34318 1.40581 1.41156 -0.14678 -0.09346 0.15118  441 LEU A CA    
3669 C C     . LEU B 441 ? 1.62840 1.69231 1.68906 -0.15012 -0.09923 0.14254  441 LEU A C     
3670 O O     . LEU B 441 ? 1.71777 1.78324 1.76380 -0.15922 -0.11255 0.14364  441 LEU A O     
3671 C CB    . LEU B 441 ? 1.41511 1.47841 1.45641 -0.15367 -0.09715 0.15170  441 LEU A CB    
3672 C CG    . LEU B 441 ? 1.72843 1.79408 1.77203 -0.16206 -0.11337 0.16534  441 LEU A CG    
3673 C CD1   . LEU B 441 ? 1.69136 1.75723 1.77241 -0.15809 -0.11705 0.17934  441 LEU A CD1   
3674 C CD2   . LEU B 441 ? 1.64162 1.70722 1.66590 -0.16586 -0.11250 0.16830  441 LEU A CD2   
3675 N N     . PHE B 442 ? 1.63317 1.69585 1.70189 -0.14344 -0.08953 0.13409  442 PHE A N     
3676 C CA    . PHE B 442 ? 1.47629 1.53958 1.54166 -0.14582 -0.09444 0.12598  442 PHE A CA    
3677 C C     . PHE B 442 ? 1.35933 1.42222 1.45398 -0.13779 -0.08798 0.12731  442 PHE A C     
3678 O O     . PHE B 442 ? 1.37189 1.43300 1.46541 -0.13102 -0.07438 0.11923  442 PHE A O     
3679 C CB    . PHE B 442 ? 1.51516 1.57739 1.55104 -0.14695 -0.08762 0.11064  442 PHE A CB    
3680 C CG    . PHE B 442 ? 1.54895 1.61164 1.55444 -0.15664 -0.09618 0.10718  442 PHE A CG    
3681 C CD1   . PHE B 442 ? 1.38739 1.45048 1.37498 -0.15906 -0.09359 0.10905  442 PHE A CD1   
3682 C CD2   . PHE B 442 ? 1.52723 1.58938 1.52120 -0.16353 -0.10632 0.10170  442 PHE A CD2   
3683 C CE1   . PHE B 442 ? 1.41704 1.48055 1.37605 -0.16807 -0.10048 0.10607  442 PHE A CE1   
3684 C CE2   . PHE B 442 ? 1.57124 1.63286 1.53518 -0.17265 -0.11308 0.09793  442 PHE A CE2   
3685 C CZ    . PHE B 442 ? 1.40355 1.46613 1.34998 -0.17486 -0.10988 0.10033  442 PHE A CZ    
3686 N N     . ASP B 443 ? 1.50129 1.56593 1.62179 -0.13874 -0.09748 0.13767  443 ASP A N     
3687 C CA    . ASP B 443 ? 1.38537 1.44995 1.53680 -0.13060 -0.09006 0.14074  443 ASP A CA    
3688 C C     . ASP B 443 ? 1.28214 1.34772 1.43976 -0.13217 -0.09570 0.13558  443 ASP A C     
3689 O O     . ASP B 443 ? 1.37558 1.44161 1.55916 -0.12602 -0.09023 0.13845  443 ASP A O     
3690 C CB    . ASP B 443 ? 1.41339 1.47926 1.59543 -0.12855 -0.09336 0.15663  443 ASP A CB    
3691 C CG    . ASP B 443 ? 1.64452 1.70842 1.82425 -0.12611 -0.08673 0.16199  443 ASP A CG    
3692 O OD1   . ASP B 443 ? 1.66224 1.72397 1.81555 -0.12621 -0.07966 0.15338  443 ASP A OD1   
3693 O OD2   . ASP B 443 ? 1.37681 1.44131 1.58248 -0.12414 -0.08869 0.17497  443 ASP A OD2   
3694 N N     . ASP B 444 ? 1.33246 1.39788 1.46721 -0.14005 -0.10556 0.12809  444 ASP A N     
3695 C CA    . ASP B 444 ? 1.30685 1.37205 1.44592 -0.14175 -0.11065 0.12168  444 ASP A CA    
3696 C C     . ASP B 444 ? 1.25072 1.31342 1.36091 -0.14241 -0.10409 0.10516  444 ASP A C     
3697 O O     . ASP B 444 ? 1.36396 1.42567 1.44570 -0.14770 -0.10598 0.10012  444 ASP A O     
3698 C CB    . ASP B 444 ? 1.38669 1.45294 1.53028 -0.15104 -0.13017 0.12856  444 ASP A CB    
3699 C CG    . ASP B 444 ? 1.64999 1.71944 1.82947 -0.14995 -0.13739 0.14527  444 ASP A CG    
3700 O OD1   . ASP B 444 ? 1.48604 1.55652 1.68748 -0.14138 -0.12585 0.15132  444 ASP A OD1   
3701 O OD2   . ASP B 444 ? 1.86175 1.93231 2.04709 -0.15791 -0.15448 0.15217  444 ASP A OD2   
3702 N N     . CYS B 445 ? 1.13391 1.19581 1.25229 -0.13727 -0.09652 0.09764  445 CYS A N     
3703 C CA    . CYS B 445 ? 1.26318 1.32287 1.35794 -0.13699 -0.08924 0.08229  445 CYS A CA    
3704 C C     . CYS B 445 ? 1.33823 1.39684 1.44364 -0.13614 -0.09073 0.07581  445 CYS A C     
3705 O O     . CYS B 445 ? 1.39929 1.45934 1.53314 -0.13155 -0.08970 0.08264  445 CYS A O     
3706 C CB    . CYS B 445 ? 1.26695 1.32640 1.35796 -0.12912 -0.07244 0.07851  445 CYS A CB    
3707 S SG    . CYS B 445 ? 1.47973 1.53737 1.54988 -0.12756 -0.06294 0.06147  445 CYS A SG    
3708 N N     . ILE B 446 ? 1.15473 1.21068 1.23880 -0.14031 -0.09248 0.06321  446 ILE A N     
3709 C CA    . ILE B 446 ? 1.09755 1.15168 1.19096 -0.13933 -0.09306 0.05573  446 ILE A CA    
3710 C C     . ILE B 446 ? 1.11796 1.17077 1.19691 -0.13489 -0.07964 0.04296  446 ILE A C     
3711 O O     . ILE B 446 ? 1.09967 1.15080 1.15163 -0.13867 -0.07832 0.03440  446 ILE A O     
3712 C CB    . ILE B 446 ? 1.12830 1.17928 1.21328 -0.14885 -0.10888 0.05249  446 ILE A CB    
3713 C CG1   . ILE B 446 ? 1.41320 1.46130 1.46281 -0.15639 -0.11240 0.04462  446 ILE A CG1   
3714 C CG2   . ILE B 446 ? 1.20843 1.26138 1.31546 -0.15242 -0.12255 0.06664  446 ILE A CG2   
3715 C CD1   . ILE B 446 ? 1.21598 1.25974 1.25397 -0.16685 -0.12859 0.04178  446 ILE A CD1   
3716 N N     . VAL B 447 ? 1.18702 1.24076 1.28377 -0.12729 -0.06989 0.04244  447 VAL A N     
3717 C CA    . VAL B 447 ? 0.98276 1.03581 1.06837 -0.12279 -0.05717 0.03201  447 VAL A CA    
3718 C C     . VAL B 447 ? 1.02240 1.07268 1.10834 -0.12429 -0.05943 0.02151  447 VAL A C     
3719 O O     . VAL B 447 ? 1.08824 1.13834 1.19591 -0.12345 -0.06417 0.02489  447 VAL A O     
3720 C CB    . VAL B 447 ? 1.04963 1.10464 1.15186 -0.11417 -0.04508 0.03756  447 VAL A CB    
3721 C CG1   . VAL B 447 ? 1.03869 1.09335 1.12898 -0.11018 -0.03303 0.02868  447 VAL A CG1   
3722 C CG2   . VAL B 447 ? 0.99970 1.05623 1.10617 -0.11260 -0.04357 0.04864  447 VAL A CG2   
3723 N N     . ASP B 448 ? 1.01055 1.05866 1.07445 -0.12635 -0.05580 0.00948  448 ASP A N     
3724 C CA    . ASP B 448 ? 1.02519 1.06979 1.08935 -0.12730 -0.05644 -0.00169 448 ASP A CA    
3725 C C     . ASP B 448 ? 1.01099 1.05701 1.08180 -0.11989 -0.04315 -0.00617 448 ASP A C     
3726 O O     . ASP B 448 ? 1.07398 1.12267 1.13814 -0.11626 -0.03409 -0.00411 448 ASP A O     
3727 C CB    . ASP B 448 ? 0.88587 0.92617 0.92330 -0.13480 -0.06142 -0.01239 448 ASP A CB    
3728 C CG    . ASP B 448 ? 1.16603 1.20112 1.20307 -0.13664 -0.06305 -0.02444 448 ASP A CG    
3729 O OD1   . ASP B 448 ? 1.23664 1.26975 1.29109 -0.13797 -0.07140 -0.02215 448 ASP A OD1   
3730 O OD2   . ASP B 448 ? 1.21758 1.25049 1.23794 -0.13675 -0.05581 -0.03588 448 ASP A OD2   
3731 N N     . GLU B 449 ? 1.12941 1.17354 1.21368 -0.11806 -0.04272 -0.01138 449 GLU A N     
3732 C CA    . GLU B 449 ? 1.05408 1.09960 1.14669 -0.11142 -0.03122 -0.01478 449 GLU A CA    
3733 C C     . GLU B 449 ? 0.99660 1.04622 1.09812 -0.10565 -0.02359 -0.00437 449 GLU A C     
3734 O O     . GLU B 449 ? 1.05882 1.10993 1.15248 -0.10226 -0.01391 -0.00666 449 GLU A O     
3735 C CB    . GLU B 449 ? 1.04505 1.08923 1.11737 -0.11221 -0.02465 -0.02663 449 GLU A CB    
3736 C CG    . GLU B 449 ? 1.01449 1.05334 1.07252 -0.11878 -0.03147 -0.03752 449 GLU A CG    
3737 C CD    . GLU B 449 ? 1.35895 1.39376 1.43345 -0.11964 -0.03756 -0.04132 449 GLU A CD    
3738 O OE1   . GLU B 449 ? 1.44638 1.48131 1.53477 -0.11487 -0.03124 -0.04472 449 GLU A OE1   
3739 O OE2   . GLU B 449 ? 1.42003 1.45149 1.49396 -0.12541 -0.04918 -0.04040 449 GLU A OE2   
3740 N N     . ALA B 450 ? 1.00217 1.05314 1.12030 -0.10468 -0.02762 0.00655  450 ALA A N     
3741 C CA    . ALA B 450 ? 0.96564 1.01917 1.09141 -0.09947 -0.01993 0.01627  450 ALA A CA    
3742 C C     . ALA B 450 ? 0.92538 0.97962 1.06402 -0.09336 -0.01044 0.01650  450 ALA A C     
3743 O O     . ALA B 450 ? 0.85871 0.91392 1.00057 -0.08905 -0.00252 0.02292  450 ALA A O     
3744 C CB    . ALA B 450 ? 0.84923 0.90374 0.99114 -0.10006 -0.02631 0.02755  450 ALA A CB    
3745 N N     . HIS B 451 ? 0.87653 0.92972 1.02193 -0.09327 -0.01130 0.00979  451 HIS A N     
3746 C CA    . HIS B 451 ? 0.97973 1.03372 1.13732 -0.08798 -0.00297 0.01031  451 HIS A CA    
3747 C C     . HIS B 451 ? 1.02751 1.08226 1.16903 -0.08583 0.00629  0.00694  451 HIS A C     
3748 O O     . HIS B 451 ? 1.09286 1.14840 1.24127 -0.08158 0.01383  0.01005  451 HIS A O     
3749 C CB    . HIS B 451 ? 0.92945 0.98187 1.09800 -0.08879 -0.00663 0.00360  451 HIS A CB    
3750 C CG    . HIS B 451 ? 0.87753 0.92762 1.02977 -0.09230 -0.00848 -0.00883 451 HIS A CG    
3751 N ND1   . HIS B 451 ? 1.21237 1.25958 1.35460 -0.09820 -0.01760 -0.01422 451 HIS A ND1   
3752 C CD2   . HIS B 451 ? 0.96789 1.01784 1.11231 -0.09090 -0.00207 -0.01677 451 HIS A CD2   
3753 C CE1   . HIS B 451 ? 1.28716 1.33207 1.41483 -0.10008 -0.01562 -0.02574 451 HIS A CE1   
3754 N NE2   . HIS B 451 ? 1.13283 1.17971 1.26297 -0.09544 -0.00608 -0.02729 451 HIS A NE2   
3755 N N     . ARG B 452 ? 0.97745 1.03194 1.09808 -0.08910 0.00544  0.00121  452 ARG A N     
3756 C CA    . ARG B 452 ? 0.97965 1.03523 1.08541 -0.08764 0.01359  -0.00206 452 ARG A CA    
3757 C C     . ARG B 452 ? 1.07326 1.12932 1.17069 -0.08678 0.01694  0.00547  452 ARG A C     
3758 O O     . ARG B 452 ? 1.27868 1.33537 1.36564 -0.08539 0.02368  0.00467  452 ARG A O     
3759 C CB    . ARG B 452 ? 0.97592 1.03103 1.06417 -0.09158 0.01201  -0.01253 452 ARG A CB    
3760 C CG    . ARG B 452 ? 0.99117 1.04483 1.08612 -0.09185 0.01117  -0.02161 452 ARG A CG    
3761 C CD    . ARG B 452 ? 1.16332 1.21863 1.26760 -0.08723 0.01912  -0.02195 452 ARG A CD    
3762 N NE    . ARG B 452 ? 1.51056 1.56804 1.60044 -0.08658 0.02597  -0.02309 452 ARG A NE    
3763 C CZ    . ARG B 452 ? 1.58299 1.64232 1.67738 -0.08342 0.03258  -0.02277 452 ARG A CZ    
3764 N NH1   . ARG B 452 ? 1.37829 1.43758 1.49068 -0.08048 0.03356  -0.02105 452 ARG A NH1   
3765 N NH2   . ARG B 452 ? 1.46584 1.52716 1.54731 -0.08354 0.03769  -0.02350 452 ARG A NH2   
3766 N N     . LEU B 453 ? 0.93843 0.99400 1.04167 -0.08764 0.01228  0.01276  453 LEU A N     
3767 C CA    . LEU B 453 ? 0.83831 0.89355 0.93449 -0.08693 0.01531  0.01973  453 LEU A CA    
3768 C C     . LEU B 453 ? 0.98511 1.03942 1.08402 -0.08212 0.02527  0.02354  453 LEU A C     
3769 O O     . LEU B 453 ? 1.03061 1.08421 1.11533 -0.08208 0.02991  0.02372  453 LEU A O     
3770 C CB    . LEU B 453 ? 0.90012 0.95509 1.00767 -0.08797 0.00895  0.02792  453 LEU A CB    
3771 C CG    . LEU B 453 ? 0.86617 0.92063 0.96459 -0.08910 0.00884  0.03368  453 LEU A CG    
3772 C CD1   . LEU B 453 ? 0.79041 0.84541 0.86540 -0.09315 0.00760  0.02730  453 LEU A CD1   
3773 C CD2   . LEU B 453 ? 0.93012 0.98500 1.04121 -0.09122 0.00019  0.04114  453 LEU A CD2   
3774 N N     . PRO B 454 ? 1.02523 1.07913 1.14050 -0.07854 0.02866  0.02669  454 PRO A N     
3775 C CA    . PRO B 454 ? 1.00648 1.05873 1.12107 -0.07490 0.03782  0.02991  454 PRO A CA    
3776 C C     . PRO B 454 ? 1.01322 1.06602 1.11260 -0.07553 0.04164  0.02385  454 PRO A C     
3777 O O     . PRO B 454 ? 0.90073 0.95147 0.99053 -0.07446 0.04758  0.02636  454 PRO A O     
3778 C CB    . PRO B 454 ? 0.74272 0.79523 0.87710 -0.07213 0.03903  0.03285  454 PRO A CB    
3779 C CG    . PRO B 454 ? 0.97846 1.03299 1.12153 -0.07465 0.03035  0.02821  454 PRO A CG    
3780 C CD    . PRO B 454 ? 0.98119 1.03583 1.11572 -0.07825 0.02376  0.02801  454 PRO A CD    
3781 N N     . ASP B 455 ? 1.07596 1.13107 1.17367 -0.07733 0.03845  0.01608  455 ASP A N     
3782 C CA    . ASP B 455 ? 0.92103 0.97745 1.00789 -0.07769 0.04236  0.01062  455 ASP A CA    
3783 C C     . ASP B 455 ? 1.06125 1.11758 1.12926 -0.07990 0.04356  0.01006  455 ASP A C     
3784 O O     . ASP B 455 ? 1.07508 1.13107 1.13501 -0.07928 0.04867  0.01087  455 ASP A O     
3785 C CB    . ASP B 455 ? 0.88036 0.93880 0.97114 -0.07890 0.03943  0.00220  455 ASP A CB    
3786 C CG    . ASP B 455 ? 1.25269 1.31098 1.36319 -0.07690 0.03790  0.00270  455 ASP A CG    
3787 O OD1   . ASP B 455 ? 1.26228 1.32051 1.38090 -0.07412 0.04230  0.00684  455 ASP A OD1   
3788 O OD2   . ASP B 455 ? 1.50803 1.56594 1.62521 -0.07855 0.03194  -0.00075 455 ASP A OD2   
3789 N N     . TYR B 456 ? 0.96860 1.02512 1.03005 -0.08281 0.03844  0.00928  456 TYR A N     
3790 C CA    . TYR B 456 ? 0.98189 1.03853 1.02580 -0.08533 0.03900  0.00937  456 TYR A CA    
3791 C C     . TYR B 456 ? 0.99347 1.04699 1.03578 -0.08328 0.04356  0.01694  456 TYR A C     
3792 O O     . TYR B 456 ? 1.12562 1.17860 1.15548 -0.08399 0.04724  0.01694  456 TYR A O     
3793 C CB    . TYR B 456 ? 0.84407 0.90126 0.88309 -0.08920 0.03154  0.00819  456 TYR A CB    
3794 C CG    . TYR B 456 ? 1.11966 1.17864 1.15319 -0.09213 0.02855  -0.00119 456 TYR A CG    
3795 C CD1   . TYR B 456 ? 1.44439 1.50530 1.46804 -0.09263 0.03331  -0.00757 456 TYR A CD1   
3796 C CD2   . TYR B 456 ? 1.11306 1.17133 1.15215 -0.09442 0.02133  -0.00377 456 TYR A CD2   
3797 C CE1   . TYR B 456 ? 1.49082 1.55262 1.50973 -0.09497 0.03211  -0.01671 456 TYR A CE1   
3798 C CE2   . TYR B 456 ? 1.21173 1.27010 1.24431 -0.09728 0.01928  -0.01328 456 TYR A CE2   
3799 C CZ    . TYR B 456 ? 1.53166 1.59165 1.55406 -0.09733 0.02531  -0.02004 456 TYR A CZ    
3800 O OH    . TYR B 456 ? 1.65250 1.71191 1.66872 -0.09986 0.02471  -0.02997 456 TYR A OH    
3801 N N     . ALA B 457 ? 0.95377 1.00489 1.00892 -0.08083 0.04374  0.02317  457 ALA A N     
3802 C CA    . ALA B 457 ? 0.89994 0.94671 0.95397 -0.07862 0.04923  0.02994  457 ALA A CA    
3803 C C     . ALA B 457 ? 1.01663 1.06156 1.06425 -0.07725 0.05589  0.02903  457 ALA A C     
3804 O O     . ALA B 457 ? 1.14558 1.18698 1.18210 -0.07754 0.05973  0.03121  457 ALA A O     
3805 C CB    . ALA B 457 ? 0.86742 0.91227 0.93868 -0.07578 0.04968  0.03621  457 ALA A CB    
3806 N N     . LEU B 458 ? 0.95900 1.00594 1.01367 -0.07618 0.05661  0.02618  458 LEU A N     
3807 C CA    . LEU B 458 ? 0.91419 0.95965 0.96416 -0.07538 0.06180  0.02634  458 LEU A CA    
3808 C C     . LEU B 458 ? 1.03723 1.08388 1.07131 -0.07808 0.06218  0.02297  458 LEU A C     
3809 O O     . LEU B 458 ? 1.26953 1.31279 1.29494 -0.07831 0.06613  0.02535  458 LEU A O     
3810 C CB    . LEU B 458 ? 0.79493 0.84333 0.85722 -0.07417 0.06115  0.02403  458 LEU A CB    
3811 C CG    . LEU B 458 ? 0.85161 0.89823 0.92944 -0.07135 0.06258  0.02896  458 LEU A CG    
3812 C CD1   . LEU B 458 ? 0.71549 0.76589 0.80753 -0.07078 0.05959  0.02571  458 LEU A CD1   
3813 C CD2   . LEU B 458 ? 1.00920 1.05099 1.08253 -0.07006 0.06907  0.03425  458 LEU A CD2   
3814 N N     . ASN B 459 ? 1.01568 1.06666 1.04572 -0.08037 0.05829  0.01771  459 ASN A N     
3815 C CA    . ASN B 459 ? 1.07006 1.12311 1.08627 -0.08303 0.05910  0.01465  459 ASN A CA    
3816 C C     . ASN B 459 ? 0.95087 1.00022 0.95521 -0.08437 0.06002  0.01878  459 ASN A C     
3817 O O     . ASN B 459 ? 1.22978 1.27822 1.22412 -0.08575 0.06254  0.01927  459 ASN A O     
3818 C CB    . ASN B 459 ? 0.98676 1.04485 1.00100 -0.08519 0.05585  0.00779  459 ASN A CB    
3819 C CG    . ASN B 459 ? 1.34692 1.40752 1.37394 -0.08374 0.05510  0.00320  459 ASN A CG    
3820 O OD1   . ASN B 459 ? 1.30174 1.36342 1.33418 -0.08241 0.05796  0.00283  459 ASN A OD1   
3821 N ND2   . ASN B 459 ? 1.69742 1.75862 1.72984 -0.08430 0.05078  0.00001  459 ASN A ND2   
3822 N N     . GLN B 460 ? 0.87001 0.91727 0.87663 -0.08414 0.05773  0.02202  460 GLN A N     
3823 C CA    . GLN B 460 ? 1.05904 1.10267 1.05614 -0.08540 0.05827  0.02614  460 GLN A CA    
3824 C C     . GLN B 460 ? 1.02630 1.06274 1.02615 -0.08270 0.06325  0.03171  460 GLN A C     
3825 O O     . GLN B 460 ? 1.05346 1.08593 1.05148 -0.08265 0.06366  0.03588  460 GLN A O     
3826 C CB    . GLN B 460 ? 1.00170 1.04683 1.00062 -0.08693 0.05274  0.02755  460 GLN A CB    
3827 C CG    . GLN B 460 ? 1.32023 1.36964 1.30694 -0.09110 0.04907  0.02397  460 GLN A CG    
3828 C CD    . GLN B 460 ? 1.32804 1.38256 1.31579 -0.09243 0.04641  0.01690  460 GLN A CD    
3829 O OE1   . GLN B 460 ? 1.32018 1.37526 1.31905 -0.09022 0.04661  0.01462  460 GLN A OE1   
3830 N NE2   . GLN B 460 ? 1.61946 1.67731 1.59543 -0.09618 0.04428  0.01329  460 GLN A NE2   
3831 N N     . VAL B 461 ? 0.98446 1.01890 0.98844 -0.08068 0.06711  0.03192  461 VAL A N     
3832 C CA    . VAL B 461 ? 0.94008 0.96675 0.94542 -0.07825 0.07287  0.03682  461 VAL A CA    
3833 C C     . VAL B 461 ? 1.08814 1.11030 1.08063 -0.07960 0.07678  0.03663  461 VAL A C     
3834 O O     . VAL B 461 ? 0.98305 0.99723 0.97216 -0.07839 0.08212  0.03989  461 VAL A O     
3835 C CB    . VAL B 461 ? 0.71113 0.73839 0.73207 -0.07516 0.07404  0.03847  461 VAL A CB    
3836 C CG1   . VAL B 461 ? 0.83341 0.86180 0.85519 -0.07497 0.07567  0.03686  461 VAL A CG1   
3837 C CG2   . VAL B 461 ? 0.93323 0.95390 0.96029 -0.07228 0.07921  0.04409  461 VAL A CG2   
3838 N N     . THR B 462 ? 0.84932 0.87592 0.83466 -0.08231 0.07435  0.03311  462 THR A N     
3839 C CA    . THR B 462 ? 0.82867 0.85164 0.80356 -0.08418 0.07669  0.03356  462 THR A CA    
3840 C C     . THR B 462 ? 0.97551 0.99906 0.93807 -0.08760 0.07511  0.03245  462 THR A C     
3841 O O     . THR B 462 ? 1.08286 1.11221 1.04591 -0.08863 0.07193  0.03021  462 THR A O     
3842 C CB    . THR B 462 ? 0.79965 0.82780 0.78166 -0.08406 0.07549  0.03174  462 THR A CB    
3843 O OG1   . THR B 462 ? 1.10151 1.12649 1.07326 -0.08666 0.07644  0.03299  462 THR A OG1   
3844 C CG2   . THR B 462 ? 0.85645 0.89392 0.84463 -0.08468 0.07152  0.02693  462 THR A CG2   
3845 N N     . ASN B 463 ? 0.92227 0.93965 0.87349 -0.08974 0.07708  0.03414  463 ASN A N     
3846 C CA    . ASN B 463 ? 1.05239 1.07025 0.99251 -0.09346 0.07536  0.03367  463 ASN A CA    
3847 C C     . ASN B 463 ? 1.02095 1.04131 0.95903 -0.09587 0.07415  0.03331  463 ASN A C     
3848 O O     . ASN B 463 ? 0.82956 0.84754 0.77078 -0.09496 0.07531  0.03456  463 ASN A O     
3849 C CB    . ASN B 463 ? 1.04574 1.05348 0.97500 -0.09445 0.07779  0.03631  463 ASN A CB    
3850 C CG    . ASN B 463 ? 1.31896 1.32795 1.23918 -0.09810 0.07544  0.03625  463 ASN A CG    
3851 O OD1   . ASN B 463 ? 1.43688 1.45488 1.35888 -0.09981 0.07249  0.03430  463 ASN A OD1   
3852 N ND2   . ASN B 463 ? 1.65464 1.65448 1.56576 -0.09930 0.07719  0.03837  463 ASN A ND2   
3853 N N     . GLU B 464 ? 0.70410 0.72932 0.63806 -0.09899 0.07184  0.03236  464 GLU A N     
3854 C CA    . GLU B 464 ? 0.81026 0.83945 0.74629 -0.10116 0.07017  0.03267  464 GLU A CA    
3855 C C     . GLU B 464 ? 0.76807 0.79475 0.69329 -0.10571 0.06863  0.03477  464 GLU A C     
3856 O O     . GLU B 464 ? 0.99166 1.01598 0.90919 -0.10703 0.06878  0.03498  464 GLU A O     
3857 C CB    . GLU B 464 ? 0.97415 1.01488 0.92219 -0.10009 0.06895  0.02901  464 GLU A CB    
3858 C CG    . GLU B 464 ? 1.32556 1.37207 1.27024 -0.10181 0.06840  0.02681  464 GLU A CG    
3859 C CD    . GLU B 464 ? 1.40347 1.46027 1.35838 -0.10097 0.06849  0.02239  464 GLU A CD    
3860 O OE1   . GLU B 464 ? 1.49870 1.55814 1.46489 -0.09880 0.06862  0.02094  464 GLU A OE1   
3861 O OE2   . GLU B 464 ? 1.46712 1.52888 1.41858 -0.10259 0.06881  0.02039  464 GLU A OE2   
3862 N N     . LEU B 465 ? 0.82562 0.85273 0.75116 -0.10829 0.06665  0.03688  465 LEU A N     
3863 C CA    . LEU B 465 ? 0.91565 0.94123 0.83290 -0.11326 0.06407  0.03941  465 LEU A CA    
3864 C C     . LEU B 465 ? 0.92830 0.96464 0.85751 -0.11449 0.06167  0.03981  465 LEU A C     
3865 O O     . LEU B 465 ? 0.98089 1.01697 0.91490 -0.11518 0.05980  0.04220  465 LEU A O     
3866 C CB    . LEU B 465 ? 0.83857 0.85163 0.74283 -0.11624 0.06336  0.04270  465 LEU A CB    
3867 C CG    . LEU B 465 ? 0.84466 0.85356 0.73839 -0.12201 0.05999  0.04543  465 LEU A CG    
3868 C CD1   . LEU B 465 ? 1.03642 1.04272 0.92308 -0.12252 0.06127  0.04437  465 LEU A CD1   
3869 C CD2   . LEU B 465 ? 0.88463 0.88062 0.76488 -0.12546 0.05879  0.04814  465 LEU A CD2   
3870 N N     . SER B 466 ? 0.89741 0.94280 0.83178 -0.11477 0.06206  0.03786  466 SER A N     
3871 C CA    . SER B 466 ? 0.81645 0.87267 0.76490 -0.11517 0.06129  0.03776  466 SER A CA    
3872 C C     . SER B 466 ? 0.92744 0.98515 0.87348 -0.12021 0.05848  0.04192  466 SER A C     
3873 O O     . SER B 466 ? 1.11649 1.17033 1.05123 -0.12272 0.05824  0.04283  466 SER A O     
3874 C CB    . SER B 466 ? 1.03907 1.10445 0.99578 -0.11221 0.06455  0.03251  466 SER A CB    
3875 O OG    . SER B 466 ? 1.20872 1.27480 1.15635 -0.11383 0.06565  0.03170  466 SER A OG    
3876 N N     . TYR B 467 ? 0.91186 0.97519 0.86969 -0.12171 0.05611  0.04485  467 TYR A N     
3877 C CA    . TYR B 467 ? 1.03826 1.10431 0.99714 -0.12679 0.05276  0.04966  467 TYR A CA    
3878 C C     . TYR B 467 ? 1.03101 1.10487 0.99183 -0.12678 0.05621  0.04739  467 TYR A C     
3879 O O     . TYR B 467 ? 1.23916 1.31126 1.19253 -0.13093 0.05437  0.05052  467 TYR A O     
3880 C CB    . TYR B 467 ? 0.88726 0.96004 0.86329 -0.12748 0.04998  0.05327  467 TYR A CB    
3881 C CG    . TYR B 467 ? 0.94468 1.02047 0.92512 -0.13308 0.04516  0.05974  467 TYR A CG    
3882 C CD1   . TYR B 467 ? 0.99745 1.06449 0.96860 -0.13838 0.03836  0.06565  467 TYR A CD1   
3883 C CD2   . TYR B 467 ? 1.03913 1.12632 1.03314 -0.13335 0.04744  0.06010  467 TYR A CD2   
3884 C CE1   . TYR B 467 ? 1.05302 1.12266 1.02882 -0.14412 0.03276  0.07212  467 TYR A CE1   
3885 C CE2   . TYR B 467 ? 1.22066 1.31128 1.22113 -0.13854 0.04282  0.06681  467 TYR A CE2   
3886 C CZ    . TYR B 467 ? 0.95258 1.03449 0.94432 -0.14408 0.03485  0.07303  467 TYR A CZ    
3887 O OH    . TYR B 467 ? 1.11800 1.20314 1.11662 -0.14980 0.02916  0.08016  467 TYR A OH    
3888 N N     . ALA B 468 ? 0.76517 0.84683 0.73481 -0.12258 0.06111  0.04203  468 ALA A N     
3889 C CA    . ALA B 468 ? 1.00267 1.09212 0.97326 -0.12279 0.06521  0.03958  468 ALA A CA    
3890 C C     . ALA B 468 ? 1.06703 1.15005 1.02018 -0.12471 0.06486  0.03991  468 ALA A C     
3891 O O     . ALA B 468 ? 1.18702 1.27287 1.13726 -0.12810 0.06492  0.04257  468 ALA A O     
3892 C CB    . ALA B 468 ? 1.16740 1.26342 1.14638 -0.11825 0.07038  0.03282  468 ALA A CB    
3893 N N     . ASP B 469 ? 0.98202 1.05685 0.92547 -0.12257 0.06460  0.03780  469 ASP A N     
3894 C CA    . ASP B 469 ? 1.11643 1.18519 1.04549 -0.12393 0.06446  0.03833  469 ASP A CA    
3895 C C     . ASP B 469 ? 1.03126 1.09360 0.95245 -0.12882 0.06081  0.04381  469 ASP A C     
3896 O O     . ASP B 469 ? 1.07264 1.13589 0.98819 -0.13160 0.06085  0.04564  469 ASP A O     
3897 C CB    . ASP B 469 ? 0.96737 1.02838 0.89044 -0.12065 0.06479  0.03602  469 ASP A CB    
3898 C CG    . ASP B 469 ? 1.40388 1.46216 1.31741 -0.12073 0.06548  0.03556  469 ASP A CG    
3899 O OD1   . ASP B 469 ? 1.53608 1.59802 1.44582 -0.12369 0.06563  0.03717  469 ASP A OD1   
3900 O OD2   . ASP B 469 ? 1.64428 1.69722 1.55540 -0.11795 0.06576  0.03418  469 ASP A OD2   
3901 N N     . ILE B 470 ? 0.75599 0.81186 0.67648 -0.13026 0.05749  0.04650  470 ILE A N     
3902 C CA    . ILE B 470 ? 0.76620 0.81392 0.67726 -0.13565 0.05320  0.05134  470 ILE A CA    
3903 C C     . ILE B 470 ? 0.89864 0.95577 0.81779 -0.13942 0.05184  0.05479  470 ILE A C     
3904 O O     . ILE B 470 ? 1.03043 1.08431 0.94216 -0.14339 0.05007  0.05769  470 ILE A O     
3905 C CB    . ILE B 470 ? 0.85091 0.88984 0.75842 -0.13707 0.04967  0.05343  470 ILE A CB    
3906 C CG1   . ILE B 470 ? 0.87172 0.90274 0.77353 -0.13285 0.05235  0.05019  470 ILE A CG1   
3907 C CG2   . ILE B 470 ? 0.74133 0.77024 0.63680 -0.14330 0.04485  0.05771  470 ILE A CG2   
3908 C CD1   . ILE B 470 ? 1.03546 1.05760 0.92509 -0.13188 0.05476  0.04856  470 ILE A CD1   
3909 N N     . LYS B 471 ? 0.84960 0.91801 0.78474 -0.13806 0.05309  0.05459  471 LYS A N     
3910 C CA    . LYS B 471 ? 0.90958 0.98818 0.85573 -0.14118 0.05289  0.05822  471 LYS A CA    
3911 C C     . LYS B 471 ? 0.87514 0.95806 0.81658 -0.14154 0.05686  0.05700  471 LYS A C     
3912 O O     . LYS B 471 ? 0.83926 0.92290 0.77912 -0.14612 0.05479  0.06164  471 LYS A O     
3913 C CB    . LYS B 471 ? 0.79396 0.88400 0.75983 -0.13826 0.05552  0.05703  471 LYS A CB    
3914 C CG    . LYS B 471 ? 0.91986 1.02157 0.90101 -0.14057 0.05676  0.06071  471 LYS A CG    
3915 C CD    . LYS B 471 ? 0.83280 0.94473 0.83513 -0.13708 0.06003  0.05924  471 LYS A CD    
3916 C CE    . LYS B 471 ? 0.79887 0.92244 0.81876 -0.13905 0.06209  0.06333  471 LYS A CE    
3917 N NZ    . LYS B 471 ? 0.94319 1.07579 0.98527 -0.13538 0.06563  0.06197  471 LYS A NZ    
3918 N N     . TYR B 472 ? 0.82536 0.91070 0.76425 -0.13734 0.06178  0.05144  472 TYR A N     
3919 C CA    . TYR B 472 ? 0.88887 0.97853 0.82207 -0.13802 0.06537  0.05053  472 TYR A CA    
3920 C C     . TYR B 472 ? 0.95931 1.03920 0.87840 -0.14152 0.06173  0.05420  472 TYR A C     
3921 O O     . TYR B 472 ? 1.13279 1.21587 1.05046 -0.14522 0.06170  0.05790  472 TYR A O     
3922 C CB    . TYR B 472 ? 0.76149 0.85341 0.69262 -0.13347 0.06969  0.04402  472 TYR A CB    
3923 C CG    . TYR B 472 ? 0.93514 1.03002 0.85745 -0.13447 0.07253  0.04313  472 TYR A CG    
3924 C CD1   . TYR B 472 ? 0.74507 0.85070 0.67215 -0.13534 0.07762  0.04215  472 TYR A CD1   
3925 C CD2   . TYR B 472 ? 1.02440 1.11129 0.93400 -0.13459 0.07040  0.04354  472 TYR A CD2   
3926 C CE1   . TYR B 472 ? 0.85859 0.96671 0.77587 -0.13688 0.08006  0.04179  472 TYR A CE1   
3927 C CE2   . TYR B 472 ? 0.97267 1.06235 0.87437 -0.13600 0.07205  0.04371  472 TYR A CE2   
3928 C CZ    . TYR B 472 ? 0.87185 0.97207 0.77631 -0.13741 0.07668  0.04288  472 TYR A CZ    
3929 O OH    . TYR B 472 ? 1.09995 1.20270 0.99489 -0.13942 0.07816  0.04352  472 TYR A OH    
3930 N N     . GLN B 473 ? 0.97415 1.04220 0.88390 -0.14038 0.05917  0.05334  473 GLN A N     
3931 C CA    . GLN B 473 ? 1.00483 1.06196 0.90153 -0.14316 0.05649  0.05611  473 GLN A CA    
3932 C C     . GLN B 473 ? 0.98381 1.03838 0.88011 -0.14897 0.05213  0.06161  473 GLN A C     
3933 O O     . GLN B 473 ? 1.11976 1.17284 1.01098 -0.15237 0.05115  0.06483  473 GLN A O     
3934 C CB    . GLN B 473 ? 0.90453 0.94902 0.79317 -0.14065 0.05561  0.05405  473 GLN A CB    
3935 C CG    . GLN B 473 ? 0.92265 0.96863 0.81199 -0.13542 0.05897  0.04960  473 GLN A CG    
3936 C CD    . GLN B 473 ? 1.20437 1.25449 1.09046 -0.13551 0.06055  0.04968  473 GLN A CD    
3937 O OE1   . GLN B 473 ? 1.32181 1.36598 1.20043 -0.13797 0.05911  0.05284  473 GLN A OE1   
3938 N NE2   . GLN B 473 ? 1.40575 1.46569 1.29708 -0.13316 0.06336  0.04630  473 GLN A NE2   
3939 N N     . LEU B 474 ? 0.87906 0.93324 0.78111 -0.15041 0.04905  0.06316  474 LEU A N     
3940 C CA    . LEU B 474 ? 0.77617 0.82748 0.67825 -0.15668 0.04349  0.06889  474 LEU A CA    
3941 C C     . LEU B 474 ? 1.00285 1.06665 0.91484 -0.15913 0.04499  0.07238  474 LEU A C     
3942 O O     . LEU B 474 ? 0.97278 1.03314 0.88080 -0.16424 0.04158  0.07696  474 LEU A O     
3943 C CB    . LEU B 474 ? 0.75094 0.80167 0.65939 -0.15784 0.03951  0.07052  474 LEU A CB    
3944 C CG    . LEU B 474 ? 0.77300 0.80850 0.66819 -0.15823 0.03644  0.06926  474 LEU A CG    
3945 C CD1   . LEU B 474 ? 0.72316 0.76068 0.62634 -0.15904 0.03283  0.07126  474 LEU A CD1   
3946 C CD2   . LEU B 474 ? 0.86921 0.89110 0.74966 -0.16400 0.03182  0.07195  474 LEU A CD2   
3947 N N     . GLY B 475 ? 0.85364 0.93089 0.77797 -0.15569 0.05035  0.07014  475 GLY A N     
3948 C CA    . GLY B 475 ? 0.88099 0.97080 0.81527 -0.15760 0.05359  0.07309  475 GLY A CA    
3949 C C     . GLY B 475 ? 0.89618 0.98460 0.81993 -0.15912 0.05538  0.07395  475 GLY A C     
3950 O O     . GLY B 475 ? 1.28579 1.37888 1.21315 -0.16340 0.05485  0.07920  475 GLY A O     
3951 N N     . LEU B 476 ? 0.90479 0.98723 0.81710 -0.15595 0.05709  0.06970  476 LEU A N     
3952 C CA    . LEU B 476 ? 0.97943 1.06004 0.88187 -0.15746 0.05804  0.07123  476 LEU A CA    
3953 C C     . LEU B 476 ? 1.07206 1.14367 0.96907 -0.16295 0.05240  0.07705  476 LEU A C     
3954 O O     . LEU B 476 ? 1.25342 1.32812 1.14897 -0.16620 0.05280  0.08118  476 LEU A O     
3955 C CB    . LEU B 476 ? 0.90193 0.97569 0.79461 -0.15341 0.05904  0.06670  476 LEU A CB    
3956 C CG    . LEU B 476 ? 0.91547 0.99659 0.81199 -0.14843 0.06380  0.06064  476 LEU A CG    
3957 C CD1   . LEU B 476 ? 1.16536 1.23893 1.05293 -0.14534 0.06335  0.05772  476 LEU A CD1   
3958 C CD2   . LEU B 476 ? 0.93572 1.02975 0.83598 -0.14922 0.06899  0.06042  476 LEU A CD2   
3959 N N     . ILE B 477 ? 0.94985 1.01015 0.84317 -0.16421 0.04739  0.07729  477 ILE A N     
3960 C CA    . ILE B 477 ? 1.04297 1.09216 0.92935 -0.16987 0.04155  0.08192  477 ILE A CA    
3961 C C     . ILE B 477 ? 1.06117 1.11858 0.95843 -0.17518 0.03878  0.08797  477 ILE A C     
3962 O O     . ILE B 477 ? 1.04985 1.10563 0.94527 -0.17978 0.03652  0.09280  477 ILE A O     
3963 C CB    . ILE B 477 ? 0.88980 0.92358 0.76692 -0.16993 0.03764  0.07961  477 ILE A CB    
3964 C CG1   . ILE B 477 ? 0.90509 0.93350 0.77581 -0.16387 0.04152  0.07385  477 ILE A CG1   
3965 C CG2   . ILE B 477 ? 1.15332 1.17301 1.02035 -0.17559 0.03230  0.08286  477 ILE A CG2   
3966 C CD1   . ILE B 477 ? 1.26169 1.27682 1.12450 -0.16312 0.03953  0.07115  477 ILE A CD1   
3967 N N     . GLY B 478 ? 1.05991 1.12602 0.96966 -0.17458 0.03886  0.08825  478 GLY A N     
3968 C CA    . GLY B 478 ? 0.92770 1.00278 0.85129 -0.17940 0.03626  0.09475  478 GLY A CA    
3969 C C     . GLY B 478 ? 0.98137 1.04873 0.90591 -0.18362 0.02801  0.09773  478 GLY A C     
3970 O O     . GLY B 478 ? 1.23854 1.29113 1.14879 -0.18378 0.02444  0.09486  478 GLY A O     
3971 N N     . LYS B 479 ? 0.95700 1.03383 0.89787 -0.18715 0.02515  0.10358  479 LYS A N     
3972 C CA    . LYS B 479 ? 1.02362 1.09397 0.96639 -0.19207 0.01593  0.10753  479 LYS A CA    
3973 C C     . LYS B 479 ? 1.30936 1.37895 1.25658 -0.20026 0.00876  0.11571  479 LYS A C     
3974 O O     . LYS B 479 ? 1.23814 1.29630 1.17844 -0.20614 -0.00067 0.11861  479 LYS A O     
3975 C CB    . LYS B 479 ? 1.19071 1.27280 1.15215 -0.18939 0.01702  0.10835  479 LYS A CB    
3976 C CG    . LYS B 479 ? 1.29866 1.39797 1.28433 -0.19073 0.01917  0.11449  479 LYS A CG    
3977 C CD    . LYS B 479 ? 1.39811 1.50785 1.40409 -0.18802 0.01995  0.11562  479 LYS A CD    
3978 C CE    . LYS B 479 ? 1.42619 1.55229 1.45802 -0.18951 0.02234  0.12232  479 LYS A CE    
3979 N NZ    . LYS B 479 ? 1.46773 1.60339 1.52122 -0.18674 0.02307  0.12378  479 LYS A NZ    
3980 N N     . ASN B 480 ? 1.28906 1.36995 1.24673 -0.20103 0.01294  0.11941  480 ASN A N     
3981 C CA    . ASN B 480 ? 1.17833 1.26028 1.14360 -0.20896 0.00623  0.12817  480 ASN A CA    
3982 C C     . ASN B 480 ? 1.34415 1.42387 1.30119 -0.21036 0.00907  0.12902  480 ASN A C     
3983 O O     . ASN B 480 ? 1.32413 1.40461 1.27275 -0.20486 0.01683  0.12344  480 ASN A O     
3984 C CB    . ASN B 480 ? 1.01443 1.11419 1.00664 -0.20998 0.00721  0.13484  480 ASN A CB    
3985 C CG    . ASN B 480 ? 1.38534 1.50151 1.38958 -0.20344 0.01985  0.13216  480 ASN A CG    
3986 O OD1   . ASN B 480 ? 1.52806 1.64772 1.52832 -0.20295 0.02566  0.13206  480 ASN A OD1   
3987 N ND2   . ASN B 480 ? 1.38566 1.51160 1.40435 -0.19872 0.02421  0.13010  480 ASN A ND2   
3988 N N     . GLU B 481 ? 1.27946 1.35684 1.23981 -0.21777 0.00251  0.13635  481 GLU A N     
3989 C CA    . GLU B 481 ? 1.16505 1.23913 1.11806 -0.21998 0.00399  0.13827  481 GLU A CA    
3990 C C     . GLU B 481 ? 1.20875 1.30096 1.17404 -0.21643 0.01441  0.13997  481 GLU A C     
3991 O O     . GLU B 481 ? 1.36988 1.46183 1.33068 -0.21815 0.01642  0.14249  481 GLU A O     
3992 C CB    . GLU B 481 ? 1.29353 1.36139 1.24956 -0.22928 -0.00613 0.14629  481 GLU A CB    
3993 C CG    . GLU B 481 ? 1.31877 1.40305 1.30013 -0.23301 -0.00768 0.15530  481 GLU A CG    
3994 C CD    . GLU B 481 ? 1.57289 1.65922 1.56478 -0.23449 -0.01386 0.15713  481 GLU A CD    
3995 O OE1   . GLU B 481 ? 1.50055 1.57458 1.47797 -0.23314 -0.01745 0.15134  481 GLU A OE1   
3996 O OE2   . GLU B 481 ? 1.76750 1.86800 1.78291 -0.23699 -0.01490 0.16482  481 GLU A OE2   
3997 N N     . ASN B 482 ? 1.15066 1.25753 1.13085 -0.21201 0.02083  0.13884  482 ASN A N     
3998 C CA    . ASN B 482 ? 1.15741 1.28104 1.14783 -0.20853 0.03212  0.13936  482 ASN A CA    
3999 C C     . ASN B 482 ? 1.22874 1.35488 1.21252 -0.20040 0.04049  0.12995  482 ASN A C     
4000 O O     . ASN B 482 ? 1.32137 1.46172 1.31540 -0.19680 0.05019  0.12873  482 ASN A O     
4001 C CB    . ASN B 482 ? 1.05263 1.19227 1.06896 -0.21064 0.03397  0.14654  482 ASN A CB    
4002 C CG    . ASN B 482 ? 1.36376 1.50037 1.38831 -0.21918 0.02382  0.15627  482 ASN A CG    
4003 O OD1   . ASN B 482 ? 1.39131 1.52882 1.42893 -0.22228 0.01670  0.16052  482 ASN A OD1   
4004 N ND2   . ASN B 482 ? 1.41161 1.54440 1.42916 -0.22344 0.02234  0.16034  482 ASN A ND2   
4005 N N     . GLU B 483 ? 1.34962 1.46219 1.31723 -0.19777 0.03717  0.12347  483 GLU A N     
4006 C CA    . GLU B 483 ? 1.12833 1.24305 1.09133 -0.19027 0.04408  0.11482  483 GLU A CA    
4007 C C     . GLU B 483 ? 1.06898 1.17326 1.01171 -0.18773 0.04527  0.10965  483 GLU A C     
4008 O O     . GLU B 483 ? 1.30113 1.39030 1.23153 -0.18866 0.03907  0.10798  483 GLU A O     
4009 C CB    . GLU B 483 ? 1.19998 1.31054 1.16642 -0.18816 0.04018  0.11167  483 GLU A CB    
4010 C CG    . GLU B 483 ? 1.23182 1.35729 1.21974 -0.18553 0.04498  0.11223  483 GLU A CG    
4011 C CD    . GLU B 483 ? 1.41952 1.54213 1.40886 -0.18110 0.04415  0.10693  483 GLU A CD    
4012 O OE1   . GLU B 483 ? 1.21972 1.32912 1.19240 -0.17987 0.04060  0.10256  483 GLU A OE1   
4013 O OE2   . GLU B 483 ? 1.52769 1.66125 1.53580 -0.17884 0.04738  0.10746  483 GLU A OE2   
4014 N N     . LYS B 484 ? 1.15156 1.26334 1.09111 -0.18495 0.05297  0.10751  484 LYS A N     
4015 C CA    . LYS B 484 ? 1.16102 1.26451 1.08355 -0.18219 0.05408  0.10305  484 LYS A CA    
4016 C C     . LYS B 484 ? 1.14546 1.23308 1.05619 -0.18566 0.04667  0.10553  484 LYS A C     
4017 O O     . LYS B 484 ? 1.29708 1.38352 1.21039 -0.19130 0.04287  0.11222  484 LYS A O     
4018 C CB    . LYS B 484 ? 1.14795 1.24908 1.06719 -0.17595 0.05633  0.09485  484 LYS A CB    
4019 C CG    . LYS B 484 ? 1.14943 1.26418 1.08094 -0.17224 0.06339  0.09137  484 LYS A CG    
4020 C CD    . LYS B 484 ? 1.41023 1.52383 1.33568 -0.16617 0.06720  0.08309  484 LYS A CD    
4021 C CE    . LYS B 484 ? 1.37333 1.48510 1.28511 -0.16547 0.06955  0.08146  484 LYS A CE    
4022 N NZ    . LYS B 484 ? 1.56794 1.67993 1.47531 -0.16020 0.07301  0.07389  484 LYS A NZ    
4023 N N     . LEU B 485 ? 0.91270 0.98841 0.81177 -0.18235 0.04516  0.10031  485 LEU A N     
4024 C CA    . LEU B 485 ? 1.00859 1.06802 0.89606 -0.18480 0.03977  0.10162  485 LEU A CA    
4025 C C     . LEU B 485 ? 1.24883 1.30120 1.13852 -0.19124 0.03267  0.10667  485 LEU A C     
4026 O O     . LEU B 485 ? 1.35083 1.39608 1.23602 -0.19540 0.02944  0.11088  485 LEU A O     
4027 C CB    . LEU B 485 ? 0.91664 0.96480 0.79498 -0.17999 0.03971  0.09495  485 LEU A CB    
4028 C CG    . LEU B 485 ? 1.14090 1.17817 1.00847 -0.17849 0.03972  0.09402  485 LEU A CG    
4029 C CD1   . LEU B 485 ? 0.96960 1.01661 0.83805 -0.17866 0.04301  0.09720  485 LEU A CD1   
4030 C CD2   . LEU B 485 ? 1.01540 1.04691 0.87820 -0.17253 0.04192  0.08739  485 LEU A CD2   
4031 N N     . LEU B 486 ? 1.10545 1.15921 1.00198 -0.19245 0.02968  0.10666  486 LEU A N     
4032 C CA    . LEU B 486 ? 0.97676 1.02182 0.87349 -0.19940 0.02135  0.11143  486 LEU A CA    
4033 C C     . LEU B 486 ? 1.11597 1.16894 1.02143 -0.20471 0.02040  0.11933  486 LEU A C     
4034 O O     . LEU B 486 ? 1.15098 1.19313 1.05164 -0.21048 0.01406  0.12315  486 LEU A O     
4035 C CB    . LEU B 486 ? 1.14614 1.19380 1.05090 -0.20047 0.01765  0.11168  486 LEU A CB    
4036 C CG    . LEU B 486 ? 1.18142 1.22037 1.07756 -0.19627 0.01762  0.10497  486 LEU A CG    
4037 C CD1   . LEU B 486 ? 1.20917 1.24404 1.10825 -0.20070 0.01003  0.10744  486 LEU A CD1   
4038 C CD2   . LEU B 486 ? 1.08987 1.11164 0.96769 -0.19470 0.01779  0.10028  486 LEU A CD2   
4039 N N     . LYS B 487 ? 1.04847 1.11911 0.96602 -0.20290 0.02690  0.12149  487 LYS A N     
4040 C CA    . LYS B 487 ? 1.05174 1.13165 0.97872 -0.20775 0.02740  0.12953  487 LYS A CA    
4041 C C     . LYS B 487 ? 1.06435 1.13583 0.97973 -0.20937 0.02677  0.13122  487 LYS A C     
4042 O O     . LYS B 487 ? 1.32657 1.39448 1.24429 -0.21554 0.02181  0.13786  487 LYS A O     
4043 C CB    . LYS B 487 ? 0.90714 1.00676 0.84684 -0.20466 0.03664  0.13021  487 LYS A CB    
4044 C CG    . LYS B 487 ? 1.11953 1.23051 1.07081 -0.20944 0.03860  0.13885  487 LYS A CG    
4045 C CD    . LYS B 487 ? 1.23236 1.36214 1.19600 -0.20623 0.04913  0.13873  487 LYS A CD    
4046 C CE    . LYS B 487 ? 1.54388 1.68483 1.51906 -0.21102 0.05195  0.14769  487 LYS A CE    
4047 N NZ    . LYS B 487 ? 1.72230 1.85776 1.68511 -0.21390 0.05089  0.15104  487 LYS A NZ    
4048 N N     . ALA B 488 ? 0.96002 1.02825 0.86452 -0.20424 0.03108  0.12589  488 ALA A N     
4049 C CA    . ALA B 488 ? 1.21489 1.27537 1.10992 -0.20540 0.03037  0.12803  488 ALA A CA    
4050 C C     . ALA B 488 ? 1.17406 1.21608 1.06257 -0.20979 0.02227  0.12929  488 ALA A C     
4051 O O     . ALA B 488 ? 1.26450 1.30256 1.15298 -0.21448 0.01927  0.13519  488 ALA A O     
4052 C CB    . ALA B 488 ? 0.99527 1.05365 0.88080 -0.19914 0.03481  0.12192  488 ALA A CB    
4053 N N     . ILE B 489 ? 1.08750 1.11809 0.97021 -0.20860 0.01899  0.12387  489 ILE A N     
4054 C CA    . ILE B 489 ? 1.07196 1.08267 0.94557 -0.21296 0.01179  0.12363  489 ILE A CA    
4055 C C     . ILE B 489 ? 1.13155 1.14377 1.01343 -0.22107 0.00532  0.13123  489 ILE A C     
4056 O O     . ILE B 489 ? 1.23002 1.23047 1.10745 -0.22577 0.00076  0.13429  489 ILE A O     
4057 C CB    . ILE B 489 ? 1.18131 1.18112 1.04662 -0.21063 0.01015  0.11662  489 ILE A CB    
4058 C CG1   . ILE B 489 ? 0.97375 0.96902 0.83071 -0.20317 0.01592  0.10971  489 ILE A CG1   
4059 C CG2   . ILE B 489 ? 1.26009 1.24063 1.11605 -0.21675 0.00232  0.11662  489 ILE A CG2   
4060 C CD1   . ILE B 489 ? 1.13008 1.11310 0.97911 -0.20252 0.01663  0.10955  489 ILE A CD1   
4061 N N     . ASP B 490 ? 1.09188 1.11813 0.98683 -0.22262 0.00498  0.13445  490 ASP A N     
4062 C CA    . ASP B 490 ? 1.06881 1.09786 0.97453 -0.23058 -0.00169 0.14263  490 ASP A CA    
4063 C C     . ASP B 490 ? 1.12371 1.15715 1.03370 -0.23360 -0.00041 0.14942  490 ASP A C     
4064 O O     . ASP B 490 ? 1.18406 1.20779 1.09361 -0.24037 -0.00757 0.15419  490 ASP A O     
4065 C CB    . ASP B 490 ? 1.03551 1.08174 0.95836 -0.23073 -0.00061 0.14582  490 ASP A CB    
4066 C CG    . ASP B 490 ? 1.28834 1.33622 1.22353 -0.23905 -0.00906 0.15413  490 ASP A CG    
4067 O OD1   . ASP B 490 ? 1.32339 1.35757 1.25198 -0.24532 -0.01659 0.15694  490 ASP A OD1   
4068 O OD2   . ASP B 490 ? 1.51392 1.57657 1.46622 -0.23929 -0.00815 0.15788  490 ASP A OD2   
4069 N N     . GLN B 491 ? 1.13897 1.18577 1.05200 -0.22910 0.00811  0.14984  491 GLN A N     
4070 C CA    . GLN B 491 ? 1.22190 1.27451 1.13887 -0.23215 0.00984  0.15722  491 GLN A CA    
4071 C C     . GLN B 491 ? 1.23661 1.27042 1.14157 -0.23415 0.00512  0.15694  491 GLN A C     
4072 O O     . GLN B 491 ? 1.28676 1.31780 1.19600 -0.24021 0.00083  0.16418  491 GLN A O     
4073 C CB    . GLN B 491 ? 1.16295 1.23116 1.08109 -0.22698 0.01981  0.15658  491 GLN A CB    
4074 C CG    . GLN B 491 ? 1.29709 1.38227 1.22630 -0.22391 0.02600  0.15502  491 GLN A CG    
4075 C CD    . GLN B 491 ? 1.41318 1.50705 1.35972 -0.22925 0.02314  0.16213  491 GLN A CD    
4076 O OE1   . GLN B 491 ? 1.57020 1.66482 1.52389 -0.22916 0.02031  0.16041  491 GLN A OE1   
4077 N NE2   . GLN B 491 ? 1.31267 1.41343 1.26718 -0.23423 0.02350  0.17099  491 GLN A NE2   
4078 N N     . LEU B 492 ? 1.14462 1.16598 1.03649 -0.22919 0.00617  0.14909  492 LEU A N     
4079 C CA    . LEU B 492 ? 1.06685 1.06971 0.94864 -0.23019 0.00297  0.14828  492 LEU A CA    
4080 C C     . LEU B 492 ? 1.22347 1.21134 1.10406 -0.23754 -0.00592 0.15032  492 LEU A C     
4081 O O     . LEU B 492 ? 1.47337 1.45322 1.35429 -0.24191 -0.00941 0.15517  492 LEU A O     
4082 C CB    . LEU B 492 ? 1.08753 1.07958 0.95746 -0.22345 0.00604  0.13927  492 LEU A CB    
4083 C CG    . LEU B 492 ? 1.10454 1.10060 0.97207 -0.21827 0.01164  0.13905  492 LEU A CG    
4084 C CD1   . LEU B 492 ? 1.28974 1.30758 1.16395 -0.21587 0.01756  0.14124  492 LEU A CD1   
4085 C CD2   . LEU B 492 ? 1.31479 1.29875 1.17264 -0.21213 0.01387  0.13060  492 LEU A CD2   
4086 N N     . GLU B 493 ? 1.07656 1.06055 0.95573 -0.23921 -0.00990 0.14700  493 GLU A N     
4087 C CA    . GLU B 493 ? 1.26642 1.23510 1.14247 -0.24712 -0.01947 0.14860  493 GLU A CA    
4088 C C     . GLU B 493 ? 1.23932 1.21837 1.13028 -0.25414 -0.02352 0.15922  493 GLU A C     
4089 O O     . GLU B 493 ? 1.29079 1.25687 1.17978 -0.26036 -0.02988 0.16255  493 GLU A O     
4090 C CB    . GLU B 493 ? 1.10017 1.06459 0.97199 -0.24812 -0.02350 0.14413  493 GLU A CB    
4091 C CG    . GLU B 493 ? 1.34554 1.29344 1.21199 -0.25717 -0.03433 0.14567  493 GLU A CG    
4092 C CD    . GLU B 493 ? 1.55977 1.48145 1.40799 -0.25869 -0.03674 0.13970  493 GLU A CD    
4093 O OE1   . GLU B 493 ? 1.72192 1.63838 1.56970 -0.25790 -0.03433 0.14097  493 GLU A OE1   
4094 O OE2   . GLU B 493 ? 1.55969 1.46568 1.39409 -0.26085 -0.04090 0.13389  493 GLU A OE2   
4095 N N     . LYS B 494 ? 1.07322 1.07454 0.97902 -0.25306 -0.01934 0.16426  494 LYS A N     
4096 C CA    . LYS B 494 ? 1.07915 1.09251 1.00126 -0.25935 -0.02173 0.17511  494 LYS A CA    
4097 C C     . LYS B 494 ? 1.28518 1.29420 1.20547 -0.26097 -0.02091 0.17965  494 LYS A C     
4098 O O     . LYS B 494 ? 1.29157 1.29536 1.21758 -0.26839 -0.02766 0.18657  494 LYS A O     
4099 C CB    . LYS B 494 ? 1.08577 1.12409 1.02314 -0.25618 -0.01397 0.17873  494 LYS A CB    
4100 C CG    . LYS B 494 ? 1.10891 1.16193 1.06272 -0.26096 -0.01273 0.18988  494 LYS A CG    
4101 C CD    . LYS B 494 ? 1.13142 1.20808 1.09797 -0.25680 -0.00243 0.19206  494 LYS A CD    
4102 C CE    . LYS B 494 ? 1.29628 1.38688 1.27733 -0.26124 0.00038  0.20300  494 LYS A CE    
4103 N NZ    . LYS B 494 ? 1.54201 1.62626 1.51400 -0.26243 0.00083  0.20581  494 LYS A NZ    
4104 N N     . GLN B 495 ? 1.22481 1.23558 1.13793 -0.25457 -0.01360 0.17627  495 GLN A N     
4105 C CA    . GLN B 495 ? 1.18942 1.19671 1.10143 -0.25582 -0.01290 0.18133  495 GLN A CA    
4106 C C     . GLN B 495 ? 1.30326 1.28617 1.20707 -0.26001 -0.02078 0.17963  495 GLN A C     
4107 O O     . GLN B 495 ? 1.35204 1.33142 1.26159 -0.26580 -0.02498 0.18713  495 GLN A O     
4108 C CB    . GLN B 495 ? 1.27636 1.28883 1.18133 -0.24818 -0.00475 0.17743  495 GLN A CB    
4109 C CG    . GLN B 495 ? 1.36353 1.39927 1.27549 -0.24500 0.00340  0.17951  495 GLN A CG    
4110 C CD    . GLN B 495 ? 1.51988 1.55881 1.42269 -0.23718 0.01024  0.17270  495 GLN A CD    
4111 O OE1   . GLN B 495 ? 1.44167 1.46638 1.33430 -0.23364 0.00914  0.16677  495 GLN A OE1   
4112 N NE2   . GLN B 495 ? 1.45915 1.51659 1.36590 -0.23452 0.01763  0.17341  495 GLN A NE2   
4113 N N     . ARG B 496 ? 1.31343 1.27979 1.20428 -0.25735 -0.02233 0.17004  496 ARG A N     
4114 C CA    . ARG B 496 ? 1.35075 1.29175 1.23167 -0.26105 -0.02858 0.16679  496 ARG A CA    
4115 C C     . ARG B 496 ? 1.36017 1.29688 1.24759 -0.27085 -0.03808 0.17285  496 ARG A C     
4116 O O     . ARG B 496 ? 1.46894 1.39180 1.35577 -0.27585 -0.04297 0.17583  496 ARG A O     
4117 C CB    . ARG B 496 ? 1.18593 1.11157 1.05146 -0.25689 -0.02771 0.15536  496 ARG A CB    
4118 C CG    . ARG B 496 ? 1.40924 1.30788 1.26198 -0.25823 -0.03042 0.14981  496 ARG A CG    
4119 C CD    . ARG B 496 ? 1.46084 1.34328 1.30828 -0.26716 -0.04004 0.14946  496 ARG A CD    
4120 N NE    . ARG B 496 ? 1.37378 1.25707 1.21520 -0.26821 -0.04280 0.14507  496 ARG A NE    
4121 C CZ    . ARG B 496 ? 1.58403 1.44670 1.40870 -0.27010 -0.04597 0.13700  496 ARG A CZ    
4122 N NH1   . ARG B 496 ? 1.74120 1.58030 1.55360 -0.27084 -0.04592 0.13165  496 ARG A NH1   
4123 N NH2   . ARG B 496 ? 1.58319 1.44853 1.40343 -0.27138 -0.04892 0.13444  496 ARG A NH2   
4124 N N     . ILE B 497 ? 1.38968 1.33777 1.28434 -0.27359 -0.04087 0.17496  497 ILE A N     
4125 C CA    . ILE B 497 ? 1.22262 1.16702 1.12472 -0.28351 -0.05119 0.18124  497 ILE A CA    
4126 C C     . ILE B 497 ? 1.41208 1.37007 1.33146 -0.28789 -0.05153 0.19328  497 ILE A C     
4127 O O     . ILE B 497 ? 1.61348 1.55988 1.53517 -0.29560 -0.05957 0.19798  497 ILE A O     
4128 C CB    . ILE B 497 ? 1.20658 1.16037 1.11374 -0.28491 -0.05420 0.18094  497 ILE A CB    
4129 C CG1   . ILE B 497 ? 1.43282 1.37314 1.32233 -0.28100 -0.05397 0.16973  497 ILE A CG1   
4130 C CG2   . ILE B 497 ? 1.25460 1.20639 1.17176 -0.29550 -0.06559 0.18875  497 ILE A CG2   
4131 C CD1   . ILE B 497 ? 1.42313 1.33455 1.29398 -0.28527 -0.06046 0.16342  497 ILE A CD1   
4132 N N     . LEU B 498 ? 1.33787 1.31876 1.26822 -0.28347 -0.04301 0.19800  498 LEU A N     
4133 C CA    . LEU B 498 ? 1.25397 1.24964 1.20106 -0.28794 -0.04239 0.21020  498 LEU A CA    
4134 C C     . LEU B 498 ? 1.38936 1.38397 1.33284 -0.28517 -0.03731 0.21255  498 LEU A C     
4135 O O     . LEU B 498 ? 1.66619 1.65116 1.61258 -0.29083 -0.04273 0.21836  498 LEU A O     
4136 C CB    . LEU B 498 ? 1.16411 1.18554 1.12587 -0.28578 -0.03584 0.21458  498 LEU A CB    
4137 C CG    . LEU B 498 ? 1.18233 1.20691 1.15004 -0.28756 -0.04029 0.21280  498 LEU A CG    
4138 C CD1   . LEU B 498 ? 1.15645 1.20681 1.14070 -0.28448 -0.03202 0.21711  498 LEU A CD1   
4139 C CD2   . LEU B 498 ? 1.17962 1.19404 1.15410 -0.29771 -0.05292 0.21876  498 LEU A CD2   
4140 N N     . GLU B 499 ? 1.32930 1.33292 1.26704 -0.27720 -0.02799 0.20854  499 GLU A N     
4141 C CA    . GLU B 499 ? 1.26759 1.27202 1.20252 -0.27481 -0.02361 0.21192  499 GLU A CA    
4142 C C     . GLU B 499 ? 1.25611 1.23567 1.17982 -0.27450 -0.02818 0.20682  499 GLU A C     
4143 O O     . GLU B 499 ? 1.37649 1.35374 1.29920 -0.27314 -0.02621 0.21024  499 GLU A O     
4144 C CB    . GLU B 499 ? 1.43953 1.45844 1.36979 -0.26689 -0.01361 0.20831  499 GLU A CB    
4145 C CG    . GLU B 499 ? 1.48782 1.53141 1.42922 -0.26709 -0.00707 0.21400  499 GLU A CG    
4146 C CD    . GLU B 499 ? 1.60864 1.66032 1.55366 -0.26470 -0.00509 0.20852  499 GLU A CD    
4147 O OE1   . GLU B 499 ? 1.75807 1.80233 1.70745 -0.26882 -0.01230 0.20807  499 GLU A OE1   
4148 O OE2   . GLU B 499 ? 1.35533 1.42048 1.29890 -0.25901 0.00335  0.20491  499 GLU A OE2   
4149 N N     . LYS B 500 ? 1.32785 1.28943 1.24335 -0.27573 -0.03369 0.19902  500 LYS A N     
4150 C CA    . LYS B 500 ? 1.46792 1.40380 1.37243 -0.27567 -0.03719 0.19323  500 LYS A CA    
4151 C C     . LYS B 500 ? 1.45403 1.38851 1.35163 -0.26735 -0.02988 0.18887  500 LYS A C     
4152 O O     . LYS B 500 ? 1.34422 1.27013 1.24322 -0.26765 -0.03037 0.19237  500 LYS A O     
4153 C CB    . LYS B 500 ? 1.50877 1.43510 1.42061 -0.28348 -0.04406 0.20135  500 LYS A CB    
4154 C CG    . LYS B 500 ? 1.65827 1.55670 1.56077 -0.28791 -0.05154 0.19525  500 LYS A CG    
4155 C CD    . LYS B 500 ? 1.65765 1.53610 1.54965 -0.28289 -0.04844 0.18804  500 LYS A CD    
4156 C CE    . LYS B 500 ? 1.72142 1.60127 1.62280 -0.28295 -0.04726 0.19639  500 LYS A CE    
4157 N NZ    . LYS B 500 ? 1.92747 1.78870 1.82171 -0.27775 -0.04404 0.19009  500 LYS A NZ    
4158 N N     . LEU B 501 ? 1.36208 1.30474 1.25386 -0.26040 -0.02381 0.18209  501 LEU A N     
4159 C CA    . LEU B 501 ? 1.53139 1.47165 1.41686 -0.25263 -0.01770 0.17763  501 LEU A CA    
4160 C C     . LEU B 501 ? 1.56031 1.47453 1.43546 -0.25107 -0.01946 0.16924  501 LEU A C     
4161 O O     . LEU B 501 ? 1.55069 1.45221 1.41918 -0.25421 -0.02359 0.16372  501 LEU A O     
4162 C CB    . LEU B 501 ? 1.31441 1.26989 1.19697 -0.24607 -0.01115 0.17255  501 LEU A CB    
4163 C CG    . LEU B 501 ? 1.67392 1.65447 1.56496 -0.24608 -0.00684 0.17960  501 LEU A CG    
4164 C CD1   . LEU B 501 ? 1.31536 1.30648 1.20143 -0.23849 0.00022  0.17350  501 LEU A CD1   
4165 C CD2   . LEU B 501 ? 1.74371 1.72883 1.64073 -0.24898 -0.00709 0.18974  501 LEU A CD2   
4166 N N     . ASP B 502 ? 1.37876 1.28529 1.25279 -0.24661 -0.01634 0.16858  502 ASP A N     
4167 C CA    . ASP B 502 ? 1.30332 1.18473 1.16870 -0.24427 -0.01612 0.16032  502 ASP A CA    
4168 C C     . ASP B 502 ? 1.62836 1.50864 1.48396 -0.23730 -0.01078 0.15006  502 ASP A C     
4169 O O     . ASP B 502 ? 1.69165 1.56849 1.54631 -0.23068 -0.00566 0.14708  502 ASP A O     
4170 C CB    . ASP B 502 ? 1.33865 1.21212 1.20992 -0.24238 -0.01498 0.16460  502 ASP A CB    
4171 C CG    . ASP B 502 ? 1.56895 1.41479 1.43454 -0.24150 -0.01494 0.15769  502 ASP A CG    
4172 O OD1   . ASP B 502 ? 1.51521 1.34672 1.36953 -0.24287 -0.01586 0.14893  502 ASP A OD1   
4173 O OD2   . ASP B 502 ? 1.63259 1.47111 1.50505 -0.23960 -0.01381 0.16126  502 ASP A OD2   
4174 N N     . ILE B 503 ? 1.61822 1.50166 1.46811 -0.23895 -0.01227 0.14563  503 ILE A N     
4175 C CA    . ILE B 503 ? 1.39912 1.28185 1.23989 -0.23280 -0.00756 0.13628  503 ILE A CA    
4176 C C     . ILE B 503 ? 1.39762 1.26211 1.22622 -0.23669 -0.01142 0.12909  503 ILE A C     
4177 O O     . ILE B 503 ? 1.26177 1.12420 1.09145 -0.24449 -0.01846 0.13264  503 ILE A O     
4178 C CB    . ILE B 503 ? 1.34574 1.25322 1.19179 -0.23009 -0.00476 0.13817  503 ILE A CB    
4179 C CG1   . ILE B 503 ? 1.47621 1.38380 1.31484 -0.22317 0.00039  0.12937  503 ILE A CG1   
4180 C CG2   . ILE B 503 ? 1.44583 1.36364 1.29708 -0.23676 -0.00992 0.14277  503 ILE A CG2   
4181 C CD1   . ILE B 503 ? 1.57671 1.47866 1.41387 -0.21603 0.00605  0.12624  503 ILE A CD1   
4182 N N     . ALA B 504 ? 1.47973 1.33125 1.29701 -0.23183 -0.00712 0.11977  504 ALA A N     
4183 C CA    . ALA B 504 ? 1.26728 1.10006 1.06971 -0.23568 -0.01026 0.11239  504 ALA A CA    
4184 C C     . ALA B 504 ? 1.43928 1.28560 1.24179 -0.23901 -0.01457 0.11354  504 ALA A C     
4185 O O     . ALA B 504 ? 1.42548 1.29406 1.23772 -0.23539 -0.01193 0.11692  504 ALA A O     
4186 C CB    . ALA B 504 ? 1.39936 1.21760 1.19057 -0.22910 -0.00313 0.10287  504 ALA A CB    
4187 N N     . PRO B 505 ? 1.53569 1.36917 1.32795 -0.24603 -0.02133 0.11101  505 PRO A N     
4188 C CA    . PRO B 505 ? 1.50005 1.34634 1.29480 -0.24977 -0.02650 0.11345  505 PRO A CA    
4189 C C     . PRO B 505 ? 1.38223 1.24167 1.17719 -0.24233 -0.02038 0.10968  505 PRO A C     
4190 O O     . PRO B 505 ? 1.56504 1.41357 1.34909 -0.23682 -0.01454 0.10198  505 PRO A O     
4191 C CB    . PRO B 505 ? 1.59837 1.42243 1.37702 -0.25774 -0.03409 0.10921  505 PRO A CB    
4192 C CG    . PRO B 505 ? 1.67415 1.47326 1.43867 -0.25546 -0.02938 0.10140  505 PRO A CG    
4193 C CD    . PRO B 505 ? 1.36076 1.16668 1.13894 -0.25096 -0.02448 0.10595  505 PRO A CD    
4194 N N     . ILE B 506 ? 1.32512 1.20731 1.13315 -0.24212 -0.02125 0.11503  506 ILE A N     
4195 C CA    . ILE B 506 ? 1.33073 1.22622 1.14053 -0.23535 -0.01585 0.11162  506 ILE A CA    
4196 C C     . ILE B 506 ? 1.20698 1.10672 1.01727 -0.24026 -0.02237 0.11285  506 ILE A C     
4197 O O     . ILE B 506 ? 1.30701 1.22085 1.13107 -0.24476 -0.02691 0.12040  506 ILE A O     
4198 C CB    . ILE B 506 ? 1.37544 1.29409 1.20049 -0.22991 -0.00990 0.11604  506 ILE A CB    
4199 C CG1   . ILE B 506 ? 1.18704 1.10252 1.01367 -0.22736 -0.00609 0.11774  506 ILE A CG1   
4200 C CG2   . ILE B 506 ? 1.09931 1.02874 0.92510 -0.22246 -0.00381 0.11131  506 ILE A CG2   
4201 C CD1   . ILE B 506 ? 1.45151 1.35428 1.26860 -0.22063 -0.00007 0.11051  506 ILE A CD1   
4202 N N     . ASP B 507 ? 1.22679 1.11519 1.02351 -0.23950 -0.02267 0.10634  507 ASP A N     
4203 C CA    . ASP B 507 ? 1.29657 1.18737 1.09288 -0.24494 -0.03014 0.10816  507 ASP A CA    
4204 C C     . ASP B 507 ? 1.33957 1.25411 1.15137 -0.23960 -0.02635 0.11041  507 ASP A C     
4205 O O     . ASP B 507 ? 1.42273 1.33693 1.22886 -0.23473 -0.02264 0.10522  507 ASP A O     
4206 C CB    . ASP B 507 ? 1.16684 1.03584 0.94131 -0.24713 -0.03232 0.10100  507 ASP A CB    
4207 C CG    . ASP B 507 ? 1.35663 1.22445 1.12792 -0.25464 -0.04214 0.10368  507 ASP A CG    
4208 O OD1   . ASP B 507 ? 1.37582 1.26048 1.16456 -0.25813 -0.04758 0.11163  507 ASP A OD1   
4209 O OD2   . ASP B 507 ? 1.68579 1.53589 1.43744 -0.25710 -0.04415 0.09815  507 ASP A OD2   
4210 N N     . ILE B 508 ? 1.24456 1.17854 1.07545 -0.24057 -0.02681 0.11786  508 ILE A N     
4211 C CA    . ILE B 508 ? 1.13183 1.08838 0.97875 -0.23568 -0.02252 0.11983  508 ILE A CA    
4212 C C     . ILE B 508 ? 1.22048 1.17654 1.06730 -0.23899 -0.02885 0.12025  508 ILE A C     
4213 O O     . ILE B 508 ? 1.33226 1.29743 1.18317 -0.23328 -0.02444 0.11743  508 ILE A O     
4214 C CB    . ILE B 508 ? 1.04055 1.01645 0.90728 -0.23709 -0.02147 0.12797  508 ILE A CB    
4215 C CG1   . ILE B 508 ? 1.03842 1.03627 0.92163 -0.23223 -0.01622 0.12934  508 ILE A CG1   
4216 C CG2   . ILE B 508 ? 1.25322 1.22560 1.12526 -0.24704 -0.03148 0.13552  508 ILE A CG2   
4217 C CD1   . ILE B 508 ? 1.44495 1.46206 1.34655 -0.23264 -0.01257 0.13642  508 ILE A CD1   
4218 N N     . PHE B 509 ? 1.21757 1.16280 1.05969 -0.24821 -0.03936 0.12385  509 PHE A N     
4219 C CA    . PHE B 509 ? 1.19112 1.13526 1.03284 -0.25276 -0.04724 0.12564  509 PHE A CA    
4220 C C     . PHE B 509 ? 1.44956 1.38316 1.27456 -0.24790 -0.04333 0.11734  509 PHE A C     
4221 O O     . PHE B 509 ? 1.62142 1.56597 1.45421 -0.24428 -0.04176 0.11737  509 PHE A O     
4222 C CB    . PHE B 509 ? 1.36635 1.29486 1.19935 -0.26411 -0.05956 0.12942  509 PHE A CB    
4223 C CG    . PHE B 509 ? 1.56941 1.49631 1.40285 -0.27154 -0.07078 0.13375  509 PHE A CG    
4224 C CD1   . PHE B 509 ? 1.26224 1.19159 1.09284 -0.26824 -0.06979 0.13112  509 PHE A CD1   
4225 C CD2   . PHE B 509 ? 1.99297 1.91557 1.83002 -0.28237 -0.08313 0.14112  509 PHE A CD2   
4226 C CE1   . PHE B 509 ? 1.30542 1.23329 1.13672 -0.27556 -0.08090 0.13612  509 PHE A CE1   
4227 C CE2   . PHE B 509 ? 2.15819 2.07924 1.99594 -0.28986 -0.09462 0.14600  509 PHE A CE2   
4228 C CZ    . PHE B 509 ? 1.85597 1.77973 1.69071 -0.28648 -0.09355 0.14366  509 PHE A CZ    
4229 N N     . GLY B 510 ? 1.29381 1.20663 1.09737 -0.24753 -0.04114 0.11048  510 GLY A N     
4230 C CA    . GLY B 510 ? 1.18852 1.08967 0.97512 -0.24323 -0.03677 0.10265  510 GLY A CA    
4231 C C     . GLY B 510 ? 1.17946 1.09651 0.97695 -0.23276 -0.02665 0.09995  510 GLY A C     
4232 O O     . GLY B 510 ? 1.45537 1.37486 1.25147 -0.23024 -0.02587 0.09801  510 GLY A O     
4233 N N     . LEU B 511 ? 1.11940 1.04684 0.92729 -0.22736 -0.01969 0.10020  511 LEU A N     
4234 C CA    . LEU B 511 ? 1.18156 1.12306 0.99840 -0.21771 -0.01023 0.09714  511 LEU A CA    
4235 C C     . LEU B 511 ? 1.09909 1.05870 0.93211 -0.21675 -0.01155 0.10059  511 LEU A C     
4236 O O     . LEU B 511 ? 1.24787 1.21057 1.08071 -0.21126 -0.00743 0.09667  511 LEU A O     
4237 C CB    . LEU B 511 ? 1.02858 0.97916 0.85422 -0.21426 -0.00469 0.09865  511 LEU A CB    
4238 C CG    . LEU B 511 ? 1.11233 1.07924 0.94838 -0.20565 0.00395  0.09655  511 LEU A CG    
4239 C CD1   . LEU B 511 ? 1.18674 1.14461 1.01207 -0.19928 0.00945  0.08926  511 LEU A CD1   
4240 C CD2   . LEU B 511 ? 1.09977 1.07483 0.94266 -0.20432 0.00769  0.09942  511 LEU A CD2   
4241 N N     . LYS B 512 ? 1.16097 1.13183 1.00871 -0.22194 -0.01703 0.10797  512 LYS A N     
4242 C CA    . LYS B 512 ? 1.16811 1.15731 1.03500 -0.22066 -0.01751 0.11185  512 LYS A CA    
4243 C C     . LYS B 512 ? 1.07131 1.05265 0.93069 -0.22255 -0.02279 0.11063  512 LYS A C     
4244 O O     . LYS B 512 ? 1.26806 1.25854 1.13493 -0.21687 -0.01857 0.10855  512 LYS A O     
4245 C CB    . LYS B 512 ? 1.16905 1.16981 1.05353 -0.22680 -0.02298 0.12082  512 LYS A CB    
4246 C CG    . LYS B 512 ? 1.22861 1.24890 1.13625 -0.22535 -0.02262 0.12548  512 LYS A CG    
4247 C CD    . LYS B 512 ? 1.28301 1.31570 1.21052 -0.23094 -0.02671 0.13486  512 LYS A CD    
4248 C CE    . LYS B 512 ? 1.42846 1.47955 1.38047 -0.22927 -0.02586 0.13949  512 LYS A CE    
4249 N NZ    . LYS B 512 ? 1.45008 1.51357 1.42327 -0.23447 -0.02906 0.14905  512 LYS A NZ    
4250 N N     . ALA B 513 ? 1.06726 1.03156 0.91149 -0.23056 -0.03178 0.11183  513 ALA A N     
4251 C CA    . ALA B 513 ? 1.05150 1.00696 0.88581 -0.23374 -0.03777 0.11141  513 ALA A CA    
4252 C C     . ALA B 513 ? 1.24445 1.19214 1.06497 -0.22639 -0.02956 0.10303  513 ALA A C     
4253 O O     . ALA B 513 ? 1.48858 1.44018 1.31161 -0.22417 -0.02959 0.10273  513 ALA A O     
4254 C CB    . ALA B 513 ? 1.08151 1.01789 0.89828 -0.24420 -0.04846 0.11332  513 ALA A CB    
4255 N N     . SER B 514 ? 1.10093 1.03836 0.90904 -0.22270 -0.02277 0.09706  514 SER A N     
4256 C CA    . SER B 514 ? 1.32302 1.25269 1.11931 -0.21556 -0.01443 0.08944  514 SER A CA    
4257 C C     . SER B 514 ? 1.38364 1.33243 1.19765 -0.20709 -0.00764 0.08871  514 SER A C     
4258 O O     . SER B 514 ? 1.28141 1.22875 1.09198 -0.20384 -0.00555 0.08597  514 SER A O     
4259 C CB    . SER B 514 ? 1.01374 0.93119 0.79853 -0.21299 -0.00847 0.08448  514 SER A CB    
4260 O OG    . SER B 514 ? 1.69006 1.60169 1.46689 -0.20579 -0.00010 0.07798  514 SER A OG    
4261 N N     . MET B 515 ? 1.05398 1.01948 0.88564 -0.20402 -0.00427 0.09104  515 MET A N     
4262 C CA    . MET B 515 ? 1.08212 1.06468 0.92930 -0.19605 0.00281  0.08930  515 MET A CA    
4263 C C     . MET B 515 ? 0.98849 0.98036 0.84778 -0.19713 -0.00131 0.09274  515 MET A C     
4264 O O     . MET B 515 ? 0.96440 0.96202 0.82882 -0.19116 0.00330  0.08959  515 MET A O     
4265 C CB    . MET B 515 ? 0.87958 0.87744 0.74139 -0.19379 0.00704  0.09135  515 MET A CB    
4266 C CG    . MET B 515 ? 0.96760 0.95825 0.81996 -0.19233 0.01103  0.08892  515 MET A CG    
4267 S SD    . MET B 515 ? 0.92124 0.90064 0.76019 -0.18508 0.01804  0.08097  515 MET A SD    
4268 C CE    . MET B 515 ? 1.06839 1.06575 0.92266 -0.17772 0.02361  0.07867  515 MET A CE    
4269 N N     . ASN B 516 ? 1.02397 1.01715 0.88875 -0.20469 -0.01014 0.09946  516 ASN A N     
4270 C CA    . ASN B 516 ? 1.12317 1.12489 1.00121 -0.20647 -0.01535 0.10414  516 ASN A CA    
4271 C C     . ASN B 516 ? 1.12004 1.10872 0.98211 -0.20650 -0.01717 0.10107  516 ASN A C     
4272 O O     . ASN B 516 ? 1.13115 1.12812 1.00360 -0.20256 -0.01553 0.10111  516 ASN A O     
4273 C CB    . ASN B 516 ? 1.16170 1.16588 1.04829 -0.21544 -0.02573 0.11284  516 ASN A CB    
4274 C CG    . ASN B 516 ? 1.39283 1.40578 1.29476 -0.21742 -0.03171 0.11863  516 ASN A CG    
4275 O OD1   . ASN B 516 ? 1.38110 1.38431 1.27453 -0.22503 -0.04201 0.12292  516 ASN A OD1   
4276 N ND2   . ASN B 516 ? 1.62469 1.65529 1.54888 -0.21095 -0.02561 0.11889  516 ASN A ND2   
4277 N N     . GLU B 517 ? 1.00304 0.97163 0.84073 -0.21084 -0.01993 0.09842  517 GLU A N     
4278 C CA    . GLU B 517 ? 1.11467 1.06912 0.93415 -0.21135 -0.02069 0.09530  517 GLU A CA    
4279 C C     . GLU B 517 ? 1.08066 1.03941 0.90259 -0.20132 -0.01001 0.08904  517 GLU A C     
4280 O O     . GLU B 517 ? 1.03390 0.99480 0.85811 -0.19936 -0.00999 0.08926  517 GLU A O     
4281 C CB    . GLU B 517 ? 1.00784 0.93909 0.79999 -0.21726 -0.02338 0.09230  517 GLU A CB    
4282 C CG    . GLU B 517 ? 1.50087 1.41603 1.27157 -0.21846 -0.02326 0.08891  517 GLU A CG    
4283 C CD    . GLU B 517 ? 1.62439 1.51561 1.36729 -0.22645 -0.02764 0.08669  517 GLU A CD    
4284 O OE1   . GLU B 517 ? 1.49086 1.37797 1.23227 -0.23131 -0.03174 0.08810  517 GLU A OE1   
4285 O OE2   . GLU B 517 ? 1.74822 1.62446 1.47065 -0.22797 -0.02666 0.08346  517 GLU A OE2   
4286 N N     . ILE B 518 ? 1.09762 1.05809 0.92031 -0.19558 -0.00192 0.08441  518 ILE A N     
4287 C CA    . ILE B 518 ? 0.87563 0.83981 0.70094 -0.18637 0.00765  0.07867  518 ILE A CA    
4288 C C     . ILE B 518 ? 0.91505 0.89752 0.76194 -0.18224 0.00861  0.08059  518 ILE A C     
4289 O O     . ILE B 518 ? 1.05623 1.03885 0.90350 -0.17754 0.01225  0.07783  518 ILE A O     
4290 C CB    . ILE B 518 ? 0.98046 0.94589 0.80622 -0.18197 0.01436  0.07515  518 ILE A CB    
4291 C CG1   . ILE B 518 ? 1.03124 0.97748 0.83707 -0.18550 0.01402  0.07302  518 ILE A CG1   
4292 C CG2   . ILE B 518 ? 0.96108 0.93290 0.79293 -0.17305 0.02286  0.07032  518 ILE A CG2   
4293 C CD1   . ILE B 518 ? 0.96659 0.91414 0.77447 -0.18255 0.01881  0.07143  518 ILE A CD1   
4294 N N     . HIS B 519 ? 1.09259 1.08955 0.95752 -0.18397 0.00579  0.08527  519 HIS A N     
4295 C CA    . HIS B 519 ? 0.98400 0.99835 0.87149 -0.17990 0.00751  0.08685  519 HIS A CA    
4296 C C     . HIS B 519 ? 0.98856 0.99983 0.87619 -0.18218 0.00202  0.08986  519 HIS A C     
4297 O O     . HIS B 519 ? 1.01741 1.03472 0.91384 -0.17667 0.00586  0.08776  519 HIS A O     
4298 C CB    . HIS B 519 ? 0.90816 0.93712 0.81477 -0.18226 0.00560  0.09203  519 HIS A CB    
4299 C CG    . HIS B 519 ? 0.97537 1.02102 0.90604 -0.17858 0.00763  0.09379  519 HIS A CG    
4300 N ND1   . HIS B 519 ? 1.03917 1.08915 0.98231 -0.18232 0.00062  0.10021  519 HIS A ND1   
4301 C CD2   . HIS B 519 ? 1.03898 1.09736 0.98369 -0.17172 0.01580  0.08996  519 HIS A CD2   
4302 C CE1   . HIS B 519 ? 1.16199 1.22703 1.12763 -0.17730 0.00511  0.10014  519 HIS A CE1   
4303 N NE2   . HIS B 519 ? 1.15836 1.22826 1.12435 -0.17089 0.01456  0.09347  519 HIS A NE2   
4304 N N     . GLU B 520 ? 0.86185 0.86356 0.73962 -0.19054 -0.00724 0.09494  520 GLU A N     
4305 C CA    . GLU B 520 ? 0.97064 0.96916 0.84747 -0.19406 -0.01393 0.09918  520 GLU A CA    
4306 C C     . GLU B 520 ? 1.10129 1.08781 0.96061 -0.19040 -0.00902 0.09361  520 GLU A C     
4307 O O     . GLU B 520 ? 1.24749 1.23800 1.11389 -0.18828 -0.00935 0.09505  520 GLU A O     
4308 C CB    . GLU B 520 ? 0.96720 0.95636 0.83407 -0.20481 -0.02568 0.10576  520 GLU A CB    
4309 C CG    . GLU B 520 ? 1.47883 1.46759 1.34836 -0.20950 -0.03428 0.11220  520 GLU A CG    
4310 C CD    . GLU B 520 ? 1.69222 1.70090 1.59376 -0.20764 -0.03656 0.11861  520 GLU A CD    
4311 O OE1   . GLU B 520 ? 1.35879 1.38197 1.28055 -0.20290 -0.03100 0.11780  520 GLU A OE1   
4312 O OE2   . GLU B 520 ? 1.82840 1.83781 1.73472 -0.21101 -0.04363 0.12455  520 GLU A OE2   
4313 N N     . LEU B 521 ? 0.93195 0.90455 0.77082 -0.18956 -0.00431 0.08788  521 LEU A N     
4314 C CA    . LEU B 521 ? 0.86353 0.82477 0.68702 -0.18554 0.00188  0.08253  521 LEU A CA    
4315 C C     . LEU B 521 ? 0.90168 0.87635 0.74288 -0.17621 0.00954  0.07944  521 LEU A C     
4316 O O     . LEU B 521 ? 1.00240 0.97470 0.84170 -0.17368 0.01149  0.07872  521 LEU A O     
4317 C CB    . LEU B 521 ? 0.96605 0.91174 0.76927 -0.18546 0.00667  0.07705  521 LEU A CB    
4318 C CG    . LEU B 521 ? 0.87017 0.80036 0.65423 -0.19472 -0.00036 0.07886  521 LEU A CG    
4319 C CD1   . LEU B 521 ? 0.94814 0.86418 0.71624 -0.19332 0.00579  0.07296  521 LEU A CD1   
4320 C CD2   . LEU B 521 ? 0.86303 0.78090 0.63043 -0.20129 -0.00652 0.08142  521 LEU A CD2   
4321 N N     . ASN B 522 ? 0.78991 0.77772 0.64701 -0.17174 0.01357  0.07779  522 ASN A N     
4322 C CA    . ASN B 522 ? 0.78669 0.78693 0.66011 -0.16340 0.02046  0.07428  522 ASN A CA    
4323 C C     . ASN B 522 ? 0.79151 0.80199 0.68211 -0.16324 0.01692  0.07839  522 ASN A C     
4324 O O     . ASN B 522 ? 0.89954 0.91204 0.79516 -0.15824 0.02062  0.07615  522 ASN A O     
4325 C CB    . ASN B 522 ? 0.77429 0.78599 0.65929 -0.15995 0.02482  0.07202  522 ASN A CB    
4326 C CG    . ASN B 522 ? 0.74373 0.76478 0.64048 -0.15200 0.03190  0.06723  522 ASN A CG    
4327 O OD1   . ASN B 522 ? 0.86135 0.87551 0.74978 -0.14799 0.03643  0.06307  522 ASN A OD1   
4328 N ND2   . ASN B 522 ? 1.16432 1.20056 1.08062 -0.14975 0.03313  0.06766  522 ASN A ND2   
4329 N N     . GLU B 523 ? 0.78530 0.80205 0.68602 -0.16862 0.00977  0.08471  523 GLU A N     
4330 C CA    . GLU B 523 ? 0.93723 0.96425 0.85736 -0.16875 0.00578  0.08978  523 GLU A CA    
4331 C C     . GLU B 523 ? 0.85049 0.86672 0.75813 -0.17074 0.00252  0.09157  523 GLU A C     
4332 O O     . GLU B 523 ? 1.02053 1.04316 0.94110 -0.16675 0.00405  0.09201  523 GLU A O     
4333 C CB    . GLU B 523 ? 1.04626 1.08024 0.97876 -0.17519 -0.00229 0.09751  523 GLU A CB    
4334 C CG    . GLU B 523 ? 0.98245 1.02705 0.92689 -0.17376 0.00142  0.09648  523 GLU A CG    
4335 C CD    . GLU B 523 ? 1.01282 1.07080 0.97484 -0.16531 0.01080  0.09119  523 GLU A CD    
4336 O OE1   . GLU B 523 ? 1.01908 1.08710 1.00121 -0.16257 0.01116  0.09296  523 GLU A OE1   
4337 O OE2   . GLU B 523 ? 1.10149 1.15940 1.05697 -0.16176 0.01752  0.08539  523 GLU A OE2   
4338 N N     . GLN B 524 ? 0.84253 0.84241 0.72535 -0.17678 -0.00134 0.09232  524 GLN A N     
4339 C CA    . GLN B 524 ? 0.95314 0.94105 0.82015 -0.17952 -0.00386 0.09398  524 GLN A CA    
4340 C C     . GLN B 524 ? 0.90606 0.89305 0.77230 -0.17135 0.00568  0.08797  524 GLN A C     
4341 O O     . GLN B 524 ? 0.86144 0.84966 0.73220 -0.17031 0.00491  0.09047  524 GLN A O     
4342 C CB    . GLN B 524 ? 0.96810 0.93676 0.80559 -0.18691 -0.00743 0.09369  524 GLN A CB    
4343 C CG    . GLN B 524 ? 1.22730 1.18362 1.04723 -0.19279 -0.01274 0.09752  524 GLN A CG    
4344 C CD    . GLN B 524 ? 1.45283 1.41687 1.28581 -0.19911 -0.02427 0.10721  524 GLN A CD    
4345 O OE1   . GLN B 524 ? 1.82249 1.78871 1.65939 -0.20554 -0.03266 0.11214  524 GLN A OE1   
4346 N NE2   . GLN B 524 ? 1.21300 1.18156 1.05443 -0.19744 -0.02510 0.11072  524 GLN A NE2   
4347 N N     . LEU B 525 ? 0.87918 0.86437 0.74106 -0.16605 0.01383  0.08106  525 LEU A N     
4348 C CA    . LEU B 525 ? 0.79550 0.77948 0.65727 -0.15854 0.02254  0.07570  525 LEU A CA    
4349 C C     . LEU B 525 ? 0.91505 0.91441 0.80177 -0.15330 0.02358  0.07655  525 LEU A C     
4350 O O     . LEU B 525 ? 0.96943 0.96697 0.85703 -0.15109 0.02514  0.07713  525 LEU A O     
4351 C CB    . LEU B 525 ? 0.71125 0.69354 0.56892 -0.15415 0.02958  0.06944  525 LEU A CB    
4352 C CG    . LEU B 525 ? 0.79702 0.78000 0.65821 -0.14630 0.03801  0.06433  525 LEU A CG    
4353 C CD1   . LEU B 525 ? 0.91759 0.88621 0.76199 -0.14665 0.04095  0.06393  525 LEU A CD1   
4354 C CD2   . LEU B 525 ? 0.85542 0.83909 0.71585 -0.14278 0.04308  0.05964  525 LEU A CD2   
4355 N N     . PHE B 526 ? 0.86542 0.87891 0.77166 -0.15159 0.02305  0.07668  526 PHE A N     
4356 C CA    . PHE B 526 ? 0.90138 0.92885 0.83195 -0.14607 0.02526  0.07613  526 PHE A CA    
4357 C C     . PHE B 526 ? 0.77844 0.80901 0.71926 -0.14966 0.01823  0.08350  526 PHE A C     
4358 O O     . PHE B 526 ? 1.09541 1.13207 1.05101 -0.14555 0.01980  0.08364  526 PHE A O     
4359 C CB    . PHE B 526 ? 0.71245 0.75231 0.65785 -0.14323 0.02835  0.07313  526 PHE A CB    
4360 C CG    . PHE B 526 ? 0.80732 0.84525 0.74519 -0.13840 0.03568  0.06589  526 PHE A CG    
4361 C CD1   . PHE B 526 ? 0.95740 1.00050 0.90468 -0.13176 0.04132  0.06084  526 PHE A CD1   
4362 C CD2   . PHE B 526 ? 0.88066 0.91122 0.80253 -0.14089 0.03623  0.06464  526 PHE A CD2   
4363 C CE1   . PHE B 526 ? 1.02385 1.06523 0.96465 -0.12804 0.04677  0.05520  526 PHE A CE1   
4364 C CE2   . PHE B 526 ? 0.86240 0.89149 0.77882 -0.13676 0.04214  0.05914  526 PHE A CE2   
4365 C CZ    . PHE B 526 ? 0.96156 0.99621 0.88732 -0.13050 0.04711  0.05468  526 PHE A CZ    
4366 N N     . SER B 527 ? 0.86236 0.88856 0.79597 -0.15745 0.01008  0.08988  527 SER A N     
4367 C CA    . SER B 527 ? 0.88694 0.91505 0.82892 -0.16193 0.00191  0.09826  527 SER A CA    
4368 C C     . SER B 527 ? 0.86861 0.88609 0.79600 -0.16182 0.00285  0.09858  527 SER A C     
4369 O O     . SER B 527 ? 1.04119 1.06424 0.98292 -0.16056 0.00083  0.10265  527 SER A O     
4370 C CB    . SER B 527 ? 0.80750 0.83174 0.74252 -0.17113 -0.00792 0.10530  527 SER A CB    
4371 O OG    . SER B 527 ? 1.04371 1.07774 0.99234 -0.17122 -0.00803 0.10531  527 SER A OG    
4372 N N     . THR B 528 ? 0.91064 0.91341 0.81156 -0.16294 0.00637  0.09457  528 THR A N     
4373 C CA    . THR B 528 ? 1.01526 1.00707 0.90075 -0.16275 0.00892  0.09457  528 THR A CA    
4374 C C     . THR B 528 ? 0.87911 0.87943 0.78210 -0.15418 0.01590  0.09115  528 THR A C     
4375 O O     . THR B 528 ? 0.96536 0.96633 0.87356 -0.15407 0.01438  0.09528  528 THR A O     
4376 C CB    . THR B 528 ? 0.83137 0.80654 0.68816 -0.16421 0.01370  0.08952  528 THR A CB    
4377 O OG1   . THR B 528 ? 0.94564 0.91310 0.78775 -0.17292 0.00589  0.09305  528 THR A OG1   
4378 C CG2   . THR B 528 ? 1.16342 1.12666 1.00354 -0.16381 0.01811  0.08912  528 THR A CG2   
4379 N N     . ILE B 529 ? 0.86425 0.87093 0.77628 -0.14765 0.02271  0.08425  529 ILE A N     
4380 C CA    . ILE B 529 ? 0.88730 0.90127 0.81522 -0.13966 0.02915  0.08020  529 ILE A CA    
4381 C C     . ILE B 529 ? 0.94454 0.97132 0.89836 -0.13863 0.02507  0.08455  529 ILE A C     
4382 O O     . ILE B 529 ? 1.00263 1.03117 0.96549 -0.13524 0.02688  0.08524  529 ILE A O     
4383 C CB    . ILE B 529 ? 0.73374 0.75221 0.66565 -0.13415 0.03565  0.07252  529 ILE A CB    
4384 C CG1   . ILE B 529 ? 0.75557 0.76140 0.66422 -0.13524 0.03929  0.06910  529 ILE A CG1   
4385 C CG2   . ILE B 529 ? 0.67880 0.70427 0.62664 -0.12677 0.04109  0.06838  529 ILE A CG2   
4386 C CD1   . ILE B 529 ? 0.90157 0.91150 0.81354 -0.13055 0.04468  0.06276  529 ILE A CD1   
4387 N N     . PHE B 530 ? 0.89138 0.92664 0.85789 -0.14146 0.01992  0.08777  530 PHE A N     
4388 C CA    . PHE B 530 ? 0.85886 0.90684 0.85335 -0.14009 0.01665  0.09195  530 PHE A CA    
4389 C C     . PHE B 530 ? 0.90105 0.94485 0.89436 -0.14438 0.01010  0.10043  530 PHE A C     
4390 O O     . PHE B 530 ? 1.03176 1.08184 1.04377 -0.14105 0.01029  0.10238  530 PHE A O     
4391 C CB    . PHE B 530 ? 0.78622 0.84335 0.79384 -0.14259 0.01315  0.09418  530 PHE A CB    
4392 C CG    . PHE B 530 ? 0.88321 0.95470 0.92305 -0.13957 0.01254  0.09646  530 PHE A CG    
4393 C CD1   . PHE B 530 ? 0.89023 0.97055 0.94627 -0.13237 0.02032  0.08889  530 PHE A CD1   
4394 C CD2   . PHE B 530 ? 1.09209 1.16780 1.14613 -0.14423 0.00411  0.10622  530 PHE A CD2   
4395 C CE1   . PHE B 530 ? 1.13564 1.22792 1.22105 -0.12945 0.02083  0.09017  530 PHE A CE1   
4396 C CE2   . PHE B 530 ? 0.92900 1.01763 1.01475 -0.14107 0.00424  0.10838  530 PHE A CE2   
4397 C CZ    . PHE B 530 ? 1.15203 1.24862 1.25334 -0.13348 0.01315  0.09993  530 PHE A CZ    
4398 N N     . THR B 531 ? 0.83586 0.86863 0.80688 -0.15198 0.00427  0.10540  531 THR A N     
4399 C CA    . THR B 531 ? 0.89353 0.92086 0.85907 -0.15737 -0.00258 0.11407  531 THR A CA    
4400 C C     . THR B 531 ? 0.93331 0.95592 0.89409 -0.15278 0.00378  0.11153  531 THR A C     
4401 O O     . THR B 531 ? 1.06970 1.09615 1.04356 -0.15272 0.00074  0.11741  531 THR A O     
4402 C CB    . THR B 531 ? 0.92057 0.93448 0.85778 -0.16665 -0.00899 0.11803  531 THR A CB    
4403 O OG1   . THR B 531 ? 1.05983 1.07983 1.00530 -0.16990 -0.01409 0.11973  531 THR A OG1   
4404 C CG2   . THR B 531 ? 0.92280 0.93108 0.85272 -0.17376 -0.01756 0.12790  531 THR A CG2   
4405 N N     . ILE B 532 ? 0.93482 0.94983 0.87942 -0.14900 0.01228  0.10364  532 ILE A N     
4406 C CA    . ILE B 532 ? 0.84994 0.86075 0.79149 -0.14414 0.01930  0.10113  532 ILE A CA    
4407 C C     . ILE B 532 ? 0.95606 0.98043 0.92828 -0.13736 0.02122  0.10004  532 ILE A C     
4408 O O     . ILE B 532 ? 0.90294 0.92766 0.88225 -0.13638 0.02096  0.10410  532 ILE A O     
4409 C CB    . ILE B 532 ? 0.87686 0.87913 0.80086 -0.14064 0.02814  0.09284  532 ILE A CB    
4410 C CG1   . ILE B 532 ? 0.93849 0.92543 0.83173 -0.14727 0.02702  0.09350  532 ILE A CG1   
4411 C CG2   . ILE B 532 ? 1.01104 1.01184 0.93831 -0.13458 0.03578  0.09016  532 ILE A CG2   
4412 C CD1   . ILE B 532 ? 0.85980 0.83769 0.73724 -0.14386 0.03586  0.08587  532 ILE A CD1   
4413 N N     . ILE B 533 ? 0.81206 0.84667 0.80128 -0.13327 0.02307  0.09486  533 ILE A N     
4414 C CA    . ILE B 533 ? 0.87465 0.92103 0.89211 -0.12673 0.02568  0.09218  533 ILE A CA    
4415 C C     . ILE B 533 ? 0.81575 0.86769 0.85162 -0.12909 0.01889  0.10104  533 ILE A C     
4416 O O     . ILE B 533 ? 1.20585 1.26087 1.25625 -0.12521 0.02066  0.10155  533 ILE A O     
4417 C CB    . ILE B 533 ? 0.93405 0.98975 0.96424 -0.12352 0.02824  0.08581  533 ILE A CB    
4418 C CG1   . ILE B 533 ? 0.89015 0.94100 0.90428 -0.12079 0.03477  0.07758  533 ILE A CG1   
4419 C CG2   . ILE B 533 ? 0.90609 0.97329 0.96566 -0.11804 0.03006  0.08349  533 ILE A CG2   
4420 C CD1   . ILE B 533 ? 0.75815 0.81726 0.78095 -0.11856 0.03729  0.07180  533 ILE A CD1   
4421 N N     . ASN B 534 ? 0.82168 0.87480 0.85785 -0.13547 0.01093  0.10830  534 ASN A N     
4422 C CA    . ASN B 534 ? 0.86511 0.92443 0.92150 -0.13819 0.00328  0.11808  534 ASN A CA    
4423 C C     . ASN B 534 ? 0.95728 1.00750 0.99934 -0.14211 0.00012  0.12514  534 ASN A C     
4424 O O     . ASN B 534 ? 1.16281 1.21812 1.22383 -0.14157 -0.00320 0.13142  534 ASN A O     
4425 C CB    . ASN B 534 ? 0.82121 0.88480 0.88340 -0.14430 -0.00504 0.12471  534 ASN A CB    
4426 C CG    . ASN B 534 ? 1.17510 1.24673 1.24807 -0.14103 -0.00099 0.11799  534 ASN A CG    
4427 O OD1   . ASN B 534 ? 1.24118 1.32253 1.33760 -0.13451 0.00424  0.11299  534 ASN A OD1   
4428 N ND2   . ASN B 534 ? 1.29158 1.35878 1.34720 -0.14568 -0.00308 0.11768  534 ASN A ND2   
4429 N N     . ASP B 535 ? 1.09864 1.13563 1.10875 -0.14591 0.00159  0.12417  535 ASP A N     
4430 C CA    . ASP B 535 ? 0.94535 0.97221 0.93768 -0.15060 -0.00074 0.13100  535 ASP A CA    
4431 C C     . ASP B 535 ? 0.93676 0.96022 0.92657 -0.14431 0.00873  0.12599  535 ASP A C     
4432 O O     . ASP B 535 ? 0.95503 0.96899 0.92726 -0.14742 0.00947  0.13025  535 ASP A O     
4433 C CB    . ASP B 535 ? 0.94293 0.95602 0.90143 -0.15880 -0.00406 0.13294  535 ASP A CB    
4434 C CG    . ASP B 535 ? 1.29666 1.31196 1.25616 -0.16629 -0.01477 0.13912  535 ASP A CG    
4435 O OD1   . ASP B 535 ? 1.52545 1.55408 1.51422 -0.16475 -0.01921 0.14240  535 ASP A OD1   
4436 O OD2   . ASP B 535 ? 1.38088 1.38424 1.31249 -0.17366 -0.01840 0.14057  535 ASP A OD2   
4437 N N     . SER B 536 ? 0.86771 0.89840 0.87409 -0.13618 0.01563  0.11754  536 SER A N     
4438 C CA    . SER B 536 ? 0.91521 0.94313 0.92100 -0.13018 0.02421  0.11276  536 SER A CA    
4439 C C     . SER B 536 ? 0.78295 0.82278 0.82095 -0.12349 0.02561  0.11053  536 SER A C     
4440 O O     . SER B 536 ? 1.04868 1.09825 1.10762 -0.12306 0.02133  0.11127  536 SER A O     
4441 C CB    . SER B 536 ? 0.86785 0.88945 0.85627 -0.12736 0.03182  0.10376  536 SER A CB    
4442 O OG    . SER B 536 ? 0.96185 0.97151 0.92106 -0.13354 0.03078  0.10518  536 SER A OG    
4443 N N     . ASP B 537 ? 0.76731 0.80593 0.80953 -0.11858 0.03160  0.10791  537 ASP A N     
4444 C CA    . ASP B 537 ? 0.88120 0.92960 0.95315 -0.11244 0.03290  0.10522  537 ASP A CA    
4445 C C     . ASP B 537 ? 0.78371 0.83719 0.86259 -0.10732 0.03724  0.09437  537 ASP A C     
4446 O O     . ASP B 537 ? 0.98304 1.03087 1.04469 -0.10601 0.04239  0.08864  537 ASP A O     
4447 C CB    . ASP B 537 ? 0.90606 0.95128 0.98063 -0.10975 0.03687  0.10720  537 ASP A CB    
4448 C CG    . ASP B 537 ? 1.31637 1.35576 1.38116 -0.11510 0.03354  0.11810  537 ASP A CG    
4449 O OD1   . ASP B 537 ? 1.43379 1.47802 1.51212 -0.11826 0.02624  0.12583  537 ASP A OD1   
4450 O OD2   . ASP B 537 ? 1.20592 1.23585 1.24983 -0.11619 0.03849  0.11901  537 ASP A OD2   
4451 N N     . VAL B 538 ? 0.77025 0.83364 0.87348 -0.10465 0.03552  0.09184  538 VAL A N     
4452 C CA    . VAL B 538 ? 0.70006 0.76828 0.80868 -0.10045 0.03967  0.08143  538 VAL A CA    
4453 C C     . VAL B 538 ? 0.64790 0.72148 0.77945 -0.09461 0.04240  0.07626  538 VAL A C     
4454 O O     . VAL B 538 ? 0.83283 0.91092 0.98555 -0.09408 0.03934  0.08076  538 VAL A O     
4455 C CB    . VAL B 538 ? 0.69001 0.76441 0.80473 -0.10268 0.03662  0.08144  538 VAL A CB    
4456 C CG1   . VAL B 538 ? 1.06174 1.14341 1.20153 -0.10361 0.03139  0.08815  538 VAL A CG1   
4457 C CG2   . VAL B 538 ? 0.94273 1.02175 1.06079 -0.09891 0.04149  0.07109  538 VAL A CG2   
4458 N N     . TYR B 539 ? 0.82770 0.90030 0.95521 -0.09077 0.04742  0.06753  539 TYR A N     
4459 C CA    . TYR B 539 ? 0.85643 0.93273 1.00353 -0.08577 0.04956  0.06183  539 TYR A CA    
4460 C C     . TYR B 539 ? 0.88109 0.96196 1.03201 -0.08333 0.05236  0.05169  539 TYR A C     
4461 O O     . TYR B 539 ? 0.90751 0.98588 1.04048 -0.08392 0.05468  0.04743  539 TYR A O     
4462 C CB    . TYR B 539 ? 0.73642 0.80683 0.87598 -0.08397 0.05231  0.06173  539 TYR A CB    
4463 C CG    . TYR B 539 ? 0.72733 0.79205 0.85830 -0.08678 0.05114  0.07152  539 TYR A CG    
4464 C CD1   . TYR B 539 ? 0.87458 0.94085 1.02218 -0.08642 0.04889  0.07776  539 TYR A CD1   
4465 C CD2   . TYR B 539 ? 0.86812 0.92533 0.97378 -0.09001 0.05260  0.07443  539 TYR A CD2   
4466 C CE1   . TYR B 539 ? 0.85599 0.91688 0.99416 -0.08944 0.04819  0.08700  539 TYR A CE1   
4467 C CE2   . TYR B 539 ? 1.03466 1.08562 1.13005 -0.09295 0.05239  0.08276  539 TYR A CE2   
4468 C CZ    . TYR B 539 ? 0.88158 0.93458 0.99269 -0.09279 0.05021  0.08924  539 TYR A CZ    
4469 O OH    . TYR B 539 ? 1.27978 1.32646 1.37928 -0.09611 0.05034  0.09777  539 TYR A OH    
4470 N N     . ASP B 540 ? 0.97663 1.06357 1.15014 -0.08077 0.05246  0.04797  540 ASP A N     
4471 C CA    . ASP B 540 ? 0.99193 1.08290 1.16896 -0.07865 0.05600  0.03777  540 ASP A CA    
4472 C C     . ASP B 540 ? 1.00724 1.09509 1.17888 -0.07593 0.05869  0.02971  540 ASP A C     
4473 O O     . ASP B 540 ? 1.33406 1.41886 1.51072 -0.07456 0.05768  0.03179  540 ASP A O     
4474 C CB    . ASP B 540 ? 1.02099 1.11844 1.22385 -0.07686 0.05614  0.03627  540 ASP A CB    
4475 C CG    . ASP B 540 ? 1.59876 1.69955 1.80678 -0.07435 0.06104  0.02494  540 ASP A CG    
4476 O OD1   . ASP B 540 ? 1.42316 1.52509 1.61706 -0.07581 0.06334  0.02180  540 ASP A OD1   
4477 O OD2   . ASP B 540 ? 1.64231 1.74407 1.86796 -0.07119 0.06266  0.01935  540 ASP A OD2   
4478 N N     . ASP B 541 ? 0.91450 1.00318 1.07652 -0.07555 0.06165  0.02149  541 ASP A N     
4479 C CA    . ASP B 541 ? 0.96292 1.04881 1.12016 -0.07363 0.06311  0.01391  541 ASP A CA    
4480 C C     . ASP B 541 ? 1.31984 1.40796 1.49749 -0.07082 0.06390  0.00708  541 ASP A C     
4481 O O     . ASP B 541 ? 1.25676 1.34916 1.45021 -0.07015 0.06478  0.00678  541 ASP A O     
4482 C CB    . ASP B 541 ? 0.99643 1.08167 1.13414 -0.07496 0.06520  0.00870  541 ASP A CB    
4483 C CG    . ASP B 541 ? 1.50807 1.59836 1.64654 -0.07558 0.06809  0.00352  541 ASP A CG    
4484 O OD1   . ASP B 541 ? 1.50812 1.60269 1.66385 -0.07474 0.06877  0.00400  541 ASP A OD1   
4485 O OD2   . ASP B 541 ? 1.65487 1.74491 1.77755 -0.07691 0.06986  -0.00047 541 ASP A OD2   
4486 N N     . ASP B 542 ? 1.59240 1.67742 1.77052 -0.06938 0.06347  0.00187  542 ASP A N     
4487 C CA    . ASP B 542 ? 1.63275 1.71820 1.82978 -0.06703 0.06374  -0.00514 542 ASP A CA    
4488 C C     . ASP B 542 ? 1.63500 1.72352 1.83408 -0.06672 0.06784  -0.01422 542 ASP A C     
4489 O O     . ASP B 542 ? 1.60683 1.69736 1.82602 -0.06484 0.06931  -0.01698 542 ASP A O     
4490 C CB    . ASP B 542 ? 1.50736 1.58844 1.70201 -0.06644 0.06171  -0.00904 542 ASP A CB    
4491 C CG    . ASP B 542 ? 1.78012 1.85902 1.95285 -0.06816 0.06188  -0.01290 542 ASP A CG    
4492 O OD1   . ASP B 542 ? 1.78317 1.86376 1.94128 -0.06977 0.06400  -0.01268 542 ASP A OD1   
4493 O OD2   . ASP B 542 ? 1.57109 1.64672 1.74251 -0.06811 0.05944  -0.01553 542 ASP A OD2   
4494 N N     . ILE B 543 ? 1.47553 1.56430 1.65528 -0.06846 0.07006  -0.01840 543 ILE A N     
4495 C CA    . ILE B 543 ? 1.34923 1.44069 1.52858 -0.06840 0.07515  -0.02747 543 ILE A CA    
4496 C C     . ILE B 543 ? 1.33292 1.43010 1.52172 -0.06844 0.07752  -0.02241 543 ILE A C     
4497 O O     . ILE B 543 ? 1.45653 1.55694 1.64853 -0.06807 0.08277  -0.02852 543 ILE A O     
4498 C CB    . ILE B 543 ? 1.40254 1.49247 1.55763 -0.07072 0.07632  -0.03250 543 ILE A CB    
4499 C CG1   . ILE B 543 ? 1.42747 1.51870 1.58041 -0.07083 0.08199  -0.04338 543 ILE A CG1   
4500 C CG2   . ILE B 543 ? 1.50666 1.59805 1.64617 -0.07298 0.07552  -0.02456 543 ILE A CG2   
4501 C CD1   . ILE B 543 ? 1.39983 1.48789 1.56610 -0.06896 0.08316  -0.05268 543 ILE A CD1   
4502 N N     . HIS B 544 ? 1.30252 1.40069 1.49562 -0.06917 0.07383  -0.01145 544 HIS A N     
4503 C CA    . HIS B 544 ? 1.52666 1.63022 1.72967 -0.06998 0.07430  -0.00492 544 HIS A CA    
4504 C C     . HIS B 544 ? 1.53481 1.64122 1.72264 -0.07205 0.07777  -0.00721 544 HIS A C     
4505 O O     . HIS B 544 ? 1.40278 1.51461 1.60214 -0.07174 0.08132  -0.00797 544 HIS A O     
4506 C CB    . HIS B 544 ? 1.56083 1.66780 1.79215 -0.06723 0.07626  -0.00682 544 HIS A CB    
4507 C CG    . HIS B 544 ? 1.75224 1.86389 1.99920 -0.06812 0.07359  0.00372  544 HIS A CG    
4508 N ND1   . HIS B 544 ? 1.78686 1.90017 2.05998 -0.06621 0.07177  0.00758  544 HIS A ND1   
4509 C CD2   . HIS B 544 ? 1.73356 1.84829 1.97407 -0.07115 0.07157  0.01178  544 HIS A CD2   
4510 C CE1   . HIS B 544 ? 1.82551 1.94313 2.10752 -0.06821 0.06848  0.01805  544 HIS A CE1   
4511 N NE2   . HIS B 544 ? 1.83814 1.95650 2.10023 -0.07135 0.06817  0.02056  544 HIS A NE2   
4512 N N     . ARG B 545 ? 1.39986 1.50288 1.56395 -0.07405 0.07693  -0.00783 545 ARG A N     
4513 C CA    . ARG B 545 ? 1.27205 1.37744 1.42049 -0.07643 0.07971  -0.00905 545 ARG A CA    
4514 C C     . ARG B 545 ? 1.08727 1.19222 1.22633 -0.07948 0.07577  0.00136  545 ARG A C     
4515 O O     . ARG B 545 ? 1.13981 1.24917 1.27967 -0.08135 0.07691  0.00428  545 ARG A O     
4516 C CB    . ARG B 545 ? 1.12117 1.22281 1.24967 -0.07713 0.08081  -0.01597 545 ARG A CB    
4517 C CG    . ARG B 545 ? 1.40774 1.51112 1.51824 -0.07988 0.08313  -0.01661 545 ARG A CG    
4518 C CD    . ARG B 545 ? 1.55974 1.65905 1.65161 -0.08085 0.08285  -0.02210 545 ARG A CD    
4519 N NE    . ARG B 545 ? 1.76263 1.86327 1.83673 -0.08378 0.08447  -0.02163 545 ARG A NE    
4520 C CZ    . ARG B 545 ? 1.85967 1.95752 1.91633 -0.08545 0.08386  -0.02483 545 ARG A CZ    
4521 N NH1   . ARG B 545 ? 1.72805 1.82206 1.78305 -0.08461 0.08195  -0.02981 545 ARG A NH1   
4522 N NH2   . ARG B 545 ? 1.71946 1.81836 1.76116 -0.08826 0.08459  -0.02248 545 ARG A NH2   
4523 N N     . PHE B 546 ? 1.18356 1.28303 1.31451 -0.08011 0.07154  0.00670  546 PHE A N     
4524 C CA    . PHE B 546 ? 0.99683 1.09369 1.11534 -0.08343 0.06807  0.01571  546 PHE A CA    
4525 C C     . PHE B 546 ? 0.93131 1.02563 1.05826 -0.08352 0.06401  0.02350  546 PHE A C     
4526 O O     . PHE B 546 ? 0.92213 1.01647 1.06350 -0.08076 0.06383  0.02198  546 PHE A O     
4527 C CB    . PHE B 546 ? 0.99399 1.08489 1.08964 -0.08465 0.06789  0.01497  546 PHE A CB    
4528 C CG    . PHE B 546 ? 1.29309 1.38557 1.37617 -0.08555 0.07094  0.00902  546 PHE A CG    
4529 C CD1   . PHE B 546 ? 1.43152 1.53000 1.51802 -0.08673 0.07353  0.00751  546 PHE A CD1   
4530 C CD2   . PHE B 546 ? 1.24685 1.33506 1.31550 -0.08540 0.07117  0.00572  546 PHE A CD2   
4531 C CE1   . PHE B 546 ? 1.45481 1.55475 1.52903 -0.08787 0.07661  0.00263  546 PHE A CE1   
4532 C CE2   . PHE B 546 ? 1.49924 1.58889 1.55592 -0.08674 0.07337  0.00119  546 PHE A CE2   
4533 C CZ    . PHE B 546 ? 1.44296 1.53837 1.50162 -0.08804 0.07625  -0.00044 546 PHE A CZ    
4534 N N     . HIS B 547 ? 0.91533 1.00711 1.03301 -0.08703 0.06064  0.03182  547 HIS A N     
4535 C CA    . HIS B 547 ? 0.93285 1.02108 1.05414 -0.08806 0.05667  0.04006  547 HIS A CA    
4536 C C     . HIS B 547 ? 0.88148 0.96129 0.97868 -0.09058 0.05593  0.04353  547 HIS A C     
4537 O O     . HIS B 547 ? 1.00867 1.08690 1.09087 -0.09353 0.05577  0.04412  547 HIS A O     
4538 C CB    . HIS B 547 ? 0.99282 1.08587 1.12856 -0.09040 0.05294  0.04719  547 HIS A CB    
4539 C CG    . HIS B 547 ? 1.12603 1.22688 1.28752 -0.08731 0.05483  0.04347  547 HIS A CG    
4540 N ND1   . HIS B 547 ? 1.56775 1.67046 1.75054 -0.08529 0.05315  0.04616  547 HIS A ND1   
4541 C CD2   . HIS B 547 ? 1.04473 1.15160 1.21451 -0.08598 0.05875  0.03750  547 HIS A CD2   
4542 C CE1   . HIS B 547 ? 1.51447 1.62363 1.71817 -0.08256 0.05615  0.04135  547 HIS A CE1   
4543 N NE2   . HIS B 547 ? 1.43519 1.54692 1.63089 -0.08291 0.05999  0.03586  547 HIS A NE2   
4544 N N     . ASN B 548 ? 0.80055 0.87490 0.89477 -0.08942 0.05601  0.04570  548 ASN A N     
4545 C CA    . ASN B 548 ? 0.77619 0.84179 0.84792 -0.09111 0.05710  0.04782  548 ASN A CA    
4546 C C     . ASN B 548 ? 0.69146 0.75119 0.75744 -0.09386 0.05482  0.05648  548 ASN A C     
4547 O O     . ASN B 548 ? 0.69393 0.75580 0.77492 -0.09280 0.05323  0.06004  548 ASN A O     
4548 C CB    . ASN B 548 ? 0.67609 0.73913 0.74542 -0.08753 0.06060  0.04252  548 ASN A CB    
4549 C CG    . ASN B 548 ? 0.86285 0.93116 0.93696 -0.08540 0.06223  0.03407  548 ASN A CG    
4550 O OD1   . ASN B 548 ? 0.87660 0.94756 0.96356 -0.08230 0.06289  0.02957  548 ASN A OD1   
4551 N ND2   . ASN B 548 ? 0.93175 1.00119 0.99503 -0.08739 0.06279  0.03187  548 ASN A ND2   
4552 N N     . VAL B 549 ? 0.68671 0.73876 0.73115 -0.09753 0.05475  0.05965  549 VAL A N     
4553 C CA    . VAL B 549 ? 0.72109 0.76545 0.75485 -0.10083 0.05336  0.06736  549 VAL A CA    
4554 C C     . VAL B 549 ? 0.80463 0.83993 0.82236 -0.09934 0.05886  0.06567  549 VAL A C     
4555 O O     . VAL B 549 ? 0.76065 0.79266 0.76554 -0.09937 0.06124  0.06151  549 VAL A O     
4556 C CB    . VAL B 549 ? 0.69046 0.73165 0.71139 -0.10715 0.04858  0.07280  549 VAL A CB    
4557 C CG1   . VAL B 549 ? 0.66296 0.69398 0.66705 -0.11124 0.04776  0.07968  549 VAL A CG1   
4558 C CG2   . VAL B 549 ? 0.82396 0.87468 0.86395 -0.10858 0.04307  0.07580  549 VAL A CG2   
4559 N N     . PHE B 550 ? 0.71924 0.75092 0.73913 -0.09799 0.06109  0.06917  550 PHE A N     
4560 C CA    . PHE B 550 ? 0.76292 0.78682 0.77164 -0.09575 0.06744  0.06769  550 PHE A CA    
4561 C C     . PHE B 550 ? 0.87966 0.89228 0.86746 -0.09976 0.06949  0.07327  550 PHE A C     
4562 O O     . PHE B 550 ? 0.99761 1.00155 0.96791 -0.10006 0.07422  0.07127  550 PHE A O     
4563 C CB    . PHE B 550 ? 0.69833 0.72666 0.72630 -0.09084 0.06952  0.06684  550 PHE A CB    
4564 C CG    . PHE B 550 ? 0.71978 0.75749 0.76592 -0.08733 0.06772  0.06033  550 PHE A CG    
4565 C CD1   . PHE B 550 ? 0.77580 0.81369 0.81958 -0.08479 0.07017  0.05422  550 PHE A CD1   
4566 C CD2   . PHE B 550 ? 0.72158 0.76731 0.78691 -0.08680 0.06367  0.06039  550 PHE A CD2   
4567 C CE1   . PHE B 550 ? 0.70756 0.75293 0.76504 -0.08235 0.06845  0.04803  550 PHE A CE1   
4568 C CE2   . PHE B 550 ? 0.84814 0.90097 0.92809 -0.08382 0.06291  0.05351  550 PHE A CE2   
4569 C CZ    . PHE B 550 ? 0.92119 0.97359 0.99593 -0.08185 0.06524  0.04719  550 PHE A CZ    
4570 N N     . THR B 551 ? 0.80793 0.82006 0.79706 -0.10294 0.06618  0.08012  551 THR A N     
4571 C CA    . THR B 551 ? 0.74041 0.74083 0.70747 -0.10734 0.06840  0.08549  551 THR A CA    
4572 C C     . THR B 551 ? 0.70143 0.69759 0.65158 -0.11401 0.06280  0.08763  551 THR A C     
4573 O O     . THR B 551 ? 1.02033 1.02283 0.98026 -0.11706 0.05526  0.09204  551 THR A O     
4574 C CB    . THR B 551 ? 0.94100 0.94241 0.91700 -0.10772 0.06789  0.09261  551 THR A CB    
4575 O OG1   . THR B 551 ? 0.79421 0.79909 0.78582 -0.10148 0.07328  0.09004  551 THR A OG1   
4576 C CG2   . THR B 551 ? 0.76522 0.75421 0.71682 -0.11278 0.07055  0.09831  551 THR A CG2   
4577 N N     . PHE B 552 ? 0.77282 0.75843 0.69965 -0.11633 0.06613  0.08491  552 PHE A N     
4578 C CA    . PHE B 552 ? 0.84862 0.82887 0.75778 -0.12331 0.06036  0.08662  552 PHE A CA    
4579 C C     . PHE B 552 ? 0.82314 0.78747 0.70335 -0.12609 0.06604  0.08469  552 PHE A C     
4580 O O     . PHE B 552 ? 0.82259 0.78185 0.69984 -0.12160 0.07495  0.08134  552 PHE A O     
4581 C CB    . PHE B 552 ? 0.79629 0.78588 0.71677 -0.12245 0.05600  0.08253  552 PHE A CB    
4582 C CG    . PHE B 552 ? 0.85656 0.84728 0.77886 -0.11730 0.06168  0.07478  552 PHE A CG    
4583 C CD1   . PHE B 552 ? 0.82573 0.82608 0.76902 -0.11088 0.06415  0.07103  552 PHE A CD1   
4584 C CD2   . PHE B 552 ? 0.70635 0.68820 0.60947 -0.11935 0.06385  0.07153  552 PHE A CD2   
4585 C CE1   . PHE B 552 ? 0.83242 0.83373 0.77664 -0.10697 0.06823  0.06482  552 PHE A CE1   
4586 C CE2   . PHE B 552 ? 0.95029 0.93351 0.85606 -0.11497 0.06831  0.06552  552 PHE A CE2   
4587 C CZ    . PHE B 552 ? 0.95012 0.94324 0.87609 -0.10897 0.07024  0.06246  552 PHE A CZ    
4588 N N     . GLU B 553 ? 0.87249 0.82880 0.73272 -0.13342 0.06100  0.08683  553 GLU A N     
4589 C CA    . GLU B 553 ? 0.82518 0.76446 0.65586 -0.13685 0.06619  0.08429  553 GLU A CA    
4590 C C     . GLU B 553 ? 0.93842 0.87696 0.76511 -0.13691 0.06527  0.07865  553 GLU A C     
4591 O O     . GLU B 553 ? 0.96488 0.91114 0.79910 -0.13986 0.05681  0.08005  553 GLU A O     
4592 C CB    . GLU B 553 ? 0.91697 0.84607 0.72574 -0.14587 0.06073  0.09042  553 GLU A CB    
4593 C CG    . GLU B 553 ? 1.44727 1.35692 1.22302 -0.15040 0.06587  0.08739  553 GLU A CG    
4594 C CD    . GLU B 553 ? 1.48562 1.38448 1.23725 -0.16061 0.05892  0.09320  553 GLU A CD    
4595 O OE1   . GLU B 553 ? 1.55752 1.46113 1.31170 -0.16627 0.04744  0.09690  553 GLU A OE1   
4596 O OE2   . GLU B 553 ? 1.52304 1.40868 1.25334 -0.16319 0.06496  0.09431  553 GLU A OE2   
4597 N N     . THR B 554 ? 0.86583 0.79555 0.68228 -0.13383 0.07377  0.07311  554 THR A N     
4598 C CA    . THR B 554 ? 0.91501 0.84430 0.72927 -0.13344 0.07328  0.06811  554 THR A CA    
4599 C C     . THR B 554 ? 0.96034 0.87370 0.74668 -0.14060 0.07204  0.06753  554 THR A C     
4600 O O     . THR B 554 ? 1.06801 0.97809 0.84954 -0.14070 0.07258  0.06349  554 THR A O     
4601 C CB    . THR B 554 ? 0.74069 0.67034 0.56306 -0.12587 0.08244  0.06308  554 THR A CB    
4602 O OG1   . THR B 554 ? 1.00589 0.92068 0.81090 -0.12592 0.09115  0.06261  554 THR A OG1   
4603 C CG2   . THR B 554 ? 0.81052 0.75480 0.65948 -0.11934 0.08314  0.06338  554 THR A CG2   
4604 N N     . LYS B 555 ? 0.83918 0.74244 0.60705 -0.14684 0.07007  0.07152  555 LYS A N     
4605 C CA    . LYS B 555 ? 1.03580 0.92108 0.77339 -0.15444 0.06918  0.07035  555 LYS A CA    
4606 C C     . LYS B 555 ? 0.80291 0.69157 0.54074 -0.15949 0.05918  0.07066  555 LYS A C     
4607 O O     . LYS B 555 ? 0.92107 0.80148 0.64857 -0.16007 0.06158  0.06589  555 LYS A O     
4608 C CB    . LYS B 555 ? 0.91731 0.79351 0.63645 -0.16133 0.06644  0.07579  555 LYS A CB    
4609 C CG    . LYS B 555 ? 1.13333 0.99198 0.82078 -0.17136 0.06191  0.07593  555 LYS A CG    
4610 C CD    . LYS B 555 ? 0.93359 0.78766 0.60712 -0.17926 0.05530  0.08329  555 LYS A CD    
4611 C CE    . LYS B 555 ? 1.93311 1.77064 1.57580 -0.19035 0.04836  0.08394  555 LYS A CE    
4612 N NZ    . LYS B 555 ? 1.99500 1.82970 1.62578 -0.19873 0.03990  0.09226  555 LYS A NZ    
4613 N N     . ASP B 556 ? 0.92696 0.82761 0.67800 -0.16283 0.04864  0.07646  556 ASP A N     
4614 C CA    . ASP B 556 ? 0.96373 0.86798 0.71611 -0.16836 0.03873  0.07803  556 ASP A CA    
4615 C C     . ASP B 556 ? 1.07133 0.98609 0.84152 -0.16224 0.04141  0.07331  556 ASP A C     
4616 O O     . ASP B 556 ? 0.97062 0.88154 0.73366 -0.16575 0.03825  0.07170  556 ASP A O     
4617 C CB    . ASP B 556 ? 1.00067 0.91502 0.76464 -0.17330 0.02742  0.08620  556 ASP A CB    
4618 C CG    . ASP B 556 ? 1.10103 1.00341 0.84340 -0.18161 0.02248  0.09189  556 ASP A CG    
4619 O OD1   . ASP B 556 ? 1.09400 0.97896 0.80975 -0.18369 0.02880  0.08864  556 ASP A OD1   
4620 O OD2   . ASP B 556 ? 1.43889 1.34921 1.19127 -0.18607 0.01254  0.09969  556 ASP A OD2   
4621 N N     . ILE B 557 ? 0.99180 0.91879 0.78353 -0.15386 0.04676  0.07136  557 ILE A N     
4622 C CA    . ILE B 557 ? 0.91944 0.85644 0.72699 -0.14826 0.04935  0.06695  557 ILE A CA    
4623 C C     . ILE B 557 ? 0.80307 0.72670 0.59333 -0.14820 0.05506  0.06191  557 ILE A C     
4624 O O     . ILE B 557 ? 1.16348 1.08925 0.95490 -0.14962 0.05231  0.06053  557 ILE A O     
4625 C CB    . ILE B 557 ? 0.89187 0.84076 0.72107 -0.13980 0.05470  0.06513  557 ILE A CB    
4626 C CG1   . ILE B 557 ? 0.91997 0.88134 0.76757 -0.13968 0.04935  0.06985  557 ILE A CG1   
4627 C CG2   . ILE B 557 ? 0.90428 0.86163 0.74597 -0.13477 0.05741  0.06052  557 ILE A CG2   
4628 C CD1   . ILE B 557 ? 0.66670 0.63975 0.53654 -0.13184 0.05370  0.06760  557 ILE A CD1   
4629 N N     . LEU B 558 ? 0.85883 0.76904 0.63439 -0.14672 0.06300  0.05962  558 LEU A N     
4630 C CA    . LEU B 558 ? 0.82090 0.71766 0.58219 -0.14583 0.06976  0.05464  558 LEU A CA    
4631 C C     . LEU B 558 ? 0.97430 0.85896 0.71503 -0.15428 0.06398  0.05478  558 LEU A C     
4632 O O     . LEU B 558 ? 1.08298 0.96328 0.82044 -0.15419 0.06526  0.05159  558 LEU A O     
4633 C CB    . LEU B 558 ? 0.77325 0.65795 0.52426 -0.14255 0.08029  0.05257  558 LEU A CB    
4634 C CG    . LEU B 558 ? 0.90405 0.79814 0.67545 -0.13345 0.08762  0.05122  558 LEU A CG    
4635 C CD1   . LEU B 558 ? 0.81374 0.69657 0.57600 -0.13100 0.09768  0.05066  558 LEU A CD1   
4636 C CD2   . LEU B 558 ? 0.80886 0.70561 0.58885 -0.12931 0.09026  0.04760  558 LEU A CD2   
4637 N N     . LYS B 559 ? 0.84600 0.72530 0.57370 -0.16167 0.05727  0.05877  559 LYS A N     
4638 C CA    . LYS B 559 ? 0.83784 0.70475 0.54500 -0.17084 0.05036  0.05933  559 LYS A CA    
4639 C C     . LYS B 559 ? 0.99512 0.87420 0.71743 -0.17199 0.04289  0.06070  559 LYS A C     
4640 O O     . LYS B 559 ? 1.16395 1.03417 0.87593 -0.17499 0.04222  0.05813  559 LYS A O     
4641 C CB    . LYS B 559 ? 0.89023 0.75204 0.58392 -0.17896 0.04258  0.06482  559 LYS A CB    
4642 C CG    . LYS B 559 ? 0.92886 0.77628 0.60251 -0.17959 0.04976  0.06388  559 LYS A CG    
4643 C CD    . LYS B 559 ? 1.22256 1.06634 0.88351 -0.18822 0.04079  0.07049  559 LYS A CD    
4644 C CE    . LYS B 559 ? 1.74095 1.56832 1.37753 -0.19001 0.04834  0.06938  559 LYS A CE    
4645 N NZ    . LYS B 559 ? 1.98910 1.79433 1.59729 -0.19304 0.05495  0.06261  559 LYS A NZ    
4646 N N     . ASP B 560 ? 0.93216 0.83049 0.67852 -0.16959 0.03813  0.06455  560 ASP A N     
4647 C CA    . ASP B 560 ? 0.96118 0.87245 0.72357 -0.17043 0.03206  0.06619  560 ASP A CA    
4648 C C     . ASP B 560 ? 0.79424 0.70688 0.56175 -0.16466 0.03899  0.06094  560 ASP A C     
4649 O O     . ASP B 560 ? 1.08010 0.99191 0.84588 -0.16784 0.03565  0.06085  560 ASP A O     
4650 C CB    . ASP B 560 ? 1.06788 0.99858 0.85538 -0.16826 0.02755  0.07063  560 ASP A CB    
4651 C CG    . ASP B 560 ? 1.08118 1.01179 0.86676 -0.17414 0.01962  0.07719  560 ASP A CG    
4652 O OD1   . ASP B 560 ? 1.33584 1.25057 1.09768 -0.18073 0.01705  0.07836  560 ASP A OD1   
4653 O OD2   . ASP B 560 ? 1.13307 1.07901 0.94068 -0.17228 0.01611  0.08112  560 ASP A OD2   
4654 N N     . LEU B 561 ? 0.81888 0.73350 0.59295 -0.15687 0.04780  0.05740  561 LEU A N     
4655 C CA    . LEU B 561 ? 0.81931 0.73558 0.59935 -0.15140 0.05388  0.05326  561 LEU A CA    
4656 C C     . LEU B 561 ? 0.93981 0.83806 0.69952 -0.15500 0.05594  0.05060  561 LEU A C     
4657 O O     . LEU B 561 ? 0.94835 0.84838 0.71123 -0.15526 0.05495  0.04981  561 LEU A O     
4658 C CB    . LEU B 561 ? 0.83495 0.75443 0.62430 -0.14334 0.06221  0.05076  561 LEU A CB    
4659 C CG    . LEU B 561 ? 0.90499 0.84289 0.71724 -0.13866 0.06098  0.05204  561 LEU A CG    
4660 C CD1   . LEU B 561 ? 0.78724 0.72523 0.60582 -0.13199 0.06844  0.05018  561 LEU A CD1   
4661 C CD2   . LEU B 561 ? 0.87956 0.83021 0.70585 -0.13677 0.05917  0.05117  561 LEU A CD2   
4662 N N     . HIS B 562 ? 0.84304 0.72413 0.58226 -0.15796 0.05885  0.04931  562 HIS A N     
4663 C CA    . HIS B 562 ? 0.91292 0.77453 0.63178 -0.16111 0.06215  0.04568  562 HIS A CA    
4664 C C     . HIS B 562 ? 0.98658 0.84689 0.70041 -0.16859 0.05284  0.04766  562 HIS A C     
4665 O O     . HIS B 562 ? 1.12277 0.97820 0.83517 -0.16857 0.05418  0.04554  562 HIS A O     
4666 C CB    . HIS B 562 ? 0.96700 0.81002 0.66256 -0.16412 0.06659  0.04389  562 HIS A CB    
4667 C CG    . HIS B 562 ? 1.06208 0.88323 0.73438 -0.16852 0.06957  0.03969  562 HIS A CG    
4668 N ND1   . HIS B 562 ? 1.44811 1.25851 1.11747 -0.16334 0.08044  0.03474  562 HIS A ND1   
4669 C CD2   . HIS B 562 ? 0.99823 0.80579 0.64989 -0.17767 0.06305  0.03965  562 HIS A CD2   
4670 C CE1   . HIS B 562 ? 1.37837 1.16880 1.02577 -0.16896 0.08112  0.03128  562 HIS A CE1   
4671 N NE2   . HIS B 562 ? 1.36618 1.15426 1.00162 -0.17794 0.07036  0.03400  562 HIS A NE2   
4672 N N     . ALA B 563 ? 1.01701 0.88221 0.73014 -0.17488 0.04329  0.05233  563 ALA A N     
4673 C CA    . ALA B 563 ? 1.03647 0.90016 0.74539 -0.18284 0.03360  0.05513  563 ALA A CA    
4674 C C     . ALA B 563 ? 0.97045 0.84883 0.69932 -0.17949 0.03287  0.05590  563 ALA A C     
4675 O O     . ALA B 563 ? 1.05953 0.93089 0.78236 -0.18287 0.03104  0.05512  563 ALA A O     
4676 C CB    . ALA B 563 ? 0.89721 0.76684 0.60749 -0.18929 0.02332  0.06126  563 ALA A CB    
4677 N N     . ILE B 564 ? 0.91634 0.81384 0.66755 -0.17329 0.03443  0.05728  564 ILE A N     
4678 C CA    . ILE B 564 ? 0.93746 0.84970 0.70656 -0.17082 0.03362  0.05831  564 ILE A CA    
4679 C C     . ILE B 564 ? 0.91785 0.82290 0.68322 -0.16684 0.04061  0.05415  564 ILE A C     
4680 O O     . ILE B 564 ? 1.14689 1.05345 0.91463 -0.16904 0.03821  0.05521  564 ILE A O     
4681 C CB    . ILE B 564 ? 0.91724 0.85003 0.70922 -0.16533 0.03432  0.05983  564 ILE A CB    
4682 C CG1   . ILE B 564 ? 0.98510 0.93306 0.79312 -0.16600 0.03089  0.06251  564 ILE A CG1   
4683 C CG2   . ILE B 564 ? 1.02855 0.96386 0.82648 -0.15681 0.04311  0.05575  564 ILE A CG2   
4684 C CD1   . ILE B 564 ? 1.15328 1.12009 0.98258 -0.16249 0.03041  0.06429  564 ILE A CD1   
4685 N N     . ILE B 565 ? 0.92292 0.82026 0.68349 -0.16148 0.04879  0.05028  565 ILE A N     
4686 C CA    . ILE B 565 ? 0.92544 0.81568 0.68469 -0.15735 0.05561  0.04701  565 ILE A CA    
4687 C C     . ILE B 565 ? 1.03328 0.90586 0.77498 -0.16361 0.05365  0.04600  565 ILE A C     
4688 O O     . ILE B 565 ? 1.29499 1.16757 1.04058 -0.16341 0.05376  0.04616  565 ILE A O     
4689 C CB    . ILE B 565 ? 0.91960 0.80394 0.67779 -0.15086 0.06480  0.04372  565 ILE A CB    
4690 C CG1   . ILE B 565 ? 1.00491 0.90647 0.78130 -0.14502 0.06601  0.04471  565 ILE A CG1   
4691 C CG2   . ILE B 565 ? 0.83129 0.70663 0.58870 -0.14711 0.07160  0.04109  565 ILE A CG2   
4692 C CD1   . ILE B 565 ? 0.82439 0.72066 0.59974 -0.13995 0.07360  0.04267  565 ILE A CD1   
4693 N N     . ASP B 566 ? 0.95711 0.81505 0.67988 -0.16944 0.05141  0.04523  566 ASP A N     
4694 C CA    . ASP B 566 ? 1.16887 1.00727 0.87236 -0.17602 0.04955  0.04333  566 ASP A CA    
4695 C C     . ASP B 566 ? 1.18935 1.03513 0.89928 -0.18163 0.04029  0.04743  566 ASP A C     
4696 O O     . ASP B 566 ? 1.12435 0.96201 0.83108 -0.18306 0.04080  0.04632  566 ASP A O     
4697 C CB    . ASP B 566 ? 1.09659 0.91795 0.77669 -0.18210 0.04817  0.04174  566 ASP A CB    
4698 C CG    . ASP B 566 ? 1.33986 1.14955 1.00958 -0.17742 0.05886  0.03723  566 ASP A CG    
4699 O OD1   . ASP B 566 ? 1.63603 1.45188 1.31927 -0.16892 0.06719  0.03567  566 ASP A OD1   
4700 O OD2   . ASP B 566 ? 1.33089 1.12518 0.97886 -0.18265 0.05872  0.03561  566 ASP A OD2   
4701 N N     . LYS B 567 ? 1.19345 1.05415 0.91355 -0.18460 0.03243  0.05238  567 LYS A N     
4702 C CA    . LYS B 567 ? 1.00888 0.87767 0.73692 -0.19020 0.02378  0.05713  567 LYS A CA    
4703 C C     . LYS B 567 ? 1.02106 0.90118 0.76505 -0.18501 0.02756  0.05748  567 LYS A C     
4704 O O     . LYS B 567 ? 0.95225 0.82847 0.69496 -0.18891 0.02446  0.05893  567 LYS A O     
4705 C CB    . LYS B 567 ? 0.95062 0.83532 0.69101 -0.19292 0.01624  0.06270  567 LYS A CB    
4706 C CG    . LYS B 567 ? 1.08846 0.98038 0.83681 -0.19965 0.00702  0.06839  567 LYS A CG    
4707 C CD    . LYS B 567 ? 1.23273 1.10504 0.96101 -0.20884 0.00068  0.06840  567 LYS A CD    
4708 C CE    . LYS B 567 ? 1.03533 0.91487 0.77315 -0.21552 -0.00846 0.07455  567 LYS A CE    
4709 N NZ    . LYS B 567 ? 1.41297 1.27247 1.13097 -0.22478 -0.01515 0.07426  567 LYS A NZ    
4710 N N     . LEU B 568 ? 0.92858 0.82164 0.68640 -0.17696 0.03365  0.05642  568 LEU A N     
4711 C CA    . LEU B 568 ? 0.85877 0.76275 0.63044 -0.17231 0.03698  0.05699  568 LEU A CA    
4712 C C     . LEU B 568 ? 1.06097 0.94900 0.82291 -0.17207 0.04086  0.05444  568 LEU A C     
4713 O O     . LEU B 568 ? 1.14853 1.03972 0.91589 -0.17346 0.03915  0.05683  568 LEU A O     
4714 C CB    . LEU B 568 ? 0.88921 0.80621 0.67388 -0.16424 0.04267  0.05547  568 LEU A CB    
4715 C CG    . LEU B 568 ? 0.96029 0.89709 0.76076 -0.16336 0.03967  0.05818  568 LEU A CG    
4716 C CD1   . LEU B 568 ? 1.12591 1.06970 0.93418 -0.15639 0.04486  0.05556  568 LEU A CD1   
4717 C CD2   . LEU B 568 ? 0.88438 0.83470 0.69698 -0.16345 0.03851  0.06092  568 LEU A CD2   
4718 N N     . ASN B 569 ? 1.02591 0.89726 0.77456 -0.17042 0.04630  0.05000  569 ASN A N     
4719 C CA    . ASN B 569 ? 1.03309 0.88769 0.77356 -0.16963 0.05125  0.04711  569 ASN A CA    
4720 C C     . ASN B 569 ? 1.02374 0.86728 0.75394 -0.17788 0.04478  0.04836  569 ASN A C     
4721 O O     . ASN B 569 ? 1.16071 1.00179 0.89506 -0.17788 0.04522  0.04941  569 ASN A O     
4722 C CB    . ASN B 569 ? 1.01675 0.85505 0.74483 -0.16649 0.05932  0.04191  569 ASN A CB    
4723 C CG    . ASN B 569 ? 1.04041 0.88734 0.78186 -0.15748 0.06700  0.04103  569 ASN A CG    
4724 O OD1   . ASN B 569 ? 1.23624 1.08780 0.98934 -0.15339 0.06964  0.04212  569 ASN A OD1   
4725 N ND2   . ASN B 569 ? 1.20641 1.05557 0.94686 -0.15470 0.07005  0.03965  569 ASN A ND2   
4726 N N     . LYS B 570 ? 0.94867 0.78602 0.66665 -0.18500 0.03831  0.04885  570 LYS A N     
4727 C CA    . LYS B 570 ? 1.04945 0.87478 0.75658 -0.19384 0.03107  0.05005  570 LYS A CA    
4728 C C     . LYS B 570 ? 1.04661 0.88793 0.77073 -0.19543 0.02559  0.05596  570 LYS A C     
4729 O O     . LYS B 570 ? 1.13374 0.96638 0.85532 -0.19890 0.02369  0.05667  570 LYS A O     
4730 C CB    . LYS B 570 ? 1.08856 0.90766 0.78186 -0.20176 0.02330  0.05095  570 LYS A CB    
4731 C CG    . LYS B 570 ? 1.33317 1.13345 1.00491 -0.20232 0.02793  0.04536  570 LYS A CG    
4732 C CD    . LYS B 570 ? 1.73745 1.53070 1.39384 -0.21178 0.01842  0.04725  570 LYS A CD    
4733 C CE    . LYS B 570 ? 1.66721 1.45189 1.31681 -0.22117 0.00889  0.04949  570 LYS A CE    
4734 N NZ    . LYS B 570 ? 1.86997 1.64816 1.50539 -0.23100 -0.00166 0.05215  570 LYS A NZ    
4735 N N     . THR B 571 ? 1.06244 0.92582 0.80330 -0.19299 0.02368  0.05998  571 THR A N     
4736 C CA    . THR B 571 ? 1.03938 0.91916 0.79649 -0.19426 0.01981  0.06564  571 THR A CA    
4737 C C     . THR B 571 ? 1.11608 0.99517 0.87843 -0.18991 0.02520  0.06517  571 THR A C     
4738 O O     . THR B 571 ? 1.27643 1.15571 1.04219 -0.19386 0.02160  0.06883  571 THR A O     
4739 C CB    . THR B 571 ? 0.95647 0.85868 0.72998 -0.19090 0.01953  0.06844  571 THR A CB    
4740 O OG1   . THR B 571 ? 0.94700 0.84605 0.71391 -0.19392 0.01571  0.06816  571 THR A OG1   
4741 C CG2   . THR B 571 ? 0.95800 0.87652 0.74654 -0.19391 0.01498  0.07462  571 THR A CG2   
4742 N N     . LEU B 572 ? 0.96107 0.83920 0.72480 -0.18236 0.03314  0.06147  572 LEU A N     
4743 C CA    . LEU B 572 ? 1.10087 0.97852 0.87105 -0.17798 0.03795  0.06178  572 LEU A CA    
4744 C C     . LEU B 572 ? 1.25721 1.11407 1.01647 -0.18186 0.03765  0.06047  572 LEU A C     
4745 O O     . LEU B 572 ? 1.25082 1.10923 1.01712 -0.18225 0.03705  0.06380  572 LEU A O     
4746 C CB    . LEU B 572 ? 1.29591 1.17475 1.06950 -0.16971 0.04583  0.05823  572 LEU A CB    
4747 C CG    . LEU B 572 ? 1.11817 1.01823 0.90554 -0.16497 0.04676  0.05964  572 LEU A CG    
4748 C CD1   . LEU B 572 ? 1.00405 0.90190 0.79138 -0.15846 0.05314  0.05554  572 LEU A CD1   
4749 C CD2   . LEU B 572 ? 1.09966 1.01170 0.89911 -0.16306 0.04690  0.06350  572 LEU A CD2   
4750 N N     . GLU B 573 ? 1.29834 1.13597 1.04057 -0.18485 0.03818  0.05579  573 GLU A N     
4751 C CA    . GLU B 573 ? 1.48112 1.29620 1.21133 -0.18843 0.03893  0.05311  573 GLU A CA    
4752 C C     . GLU B 573 ? 1.36185 1.17847 1.09477 -0.19590 0.03038  0.05818  573 GLU A C     
4753 O O     . GLU B 573 ? 1.46229 1.26999 1.19686 -0.19653 0.03128  0.05889  573 GLU A O     
4754 C CB    . GLU B 573 ? 1.37990 1.17389 1.08837 -0.19188 0.04020  0.04698  573 GLU A CB    
4755 C CG    . GLU B 573 ? 1.66207 1.45597 1.36721 -0.18562 0.04786  0.04282  573 GLU A CG    
4756 C CD    . GLU B 573 ? 1.95960 1.74956 1.67144 -0.17696 0.05859  0.04001  573 GLU A CD    
4757 O OE1   . GLU B 573 ? 2.01475 1.80058 1.73364 -0.17547 0.06054  0.04108  573 GLU A OE1   
4758 O OE2   . GLU B 573 ? 1.88425 1.67565 1.59557 -0.17176 0.06479  0.03735  573 GLU A OE2   
4759 N N     . ILE B 574 ? 1.26326 1.09124 0.99845 -0.20124 0.02246  0.06212  574 ILE A N     
4760 C CA    . ILE B 574 ? 1.26292 1.09362 1.00243 -0.20881 0.01396  0.06784  574 ILE A CA    
4761 C C     . ILE B 574 ? 1.26562 1.10527 1.01976 -0.20561 0.01637  0.07205  574 ILE A C     
4762 O O     . ILE B 574 ? 1.34389 1.17581 1.09790 -0.21066 0.01244  0.07480  574 ILE A O     
4763 C CB    . ILE B 574 ? 1.31344 1.16200 1.06117 -0.21264 0.00684  0.07300  574 ILE A CB    
4764 C CG1   . ILE B 574 ? 1.44543 1.28757 1.18065 -0.21513 0.00434  0.06988  574 ILE A CG1   
4765 C CG2   . ILE B 574 ? 1.35313 1.20444 1.10650 -0.22069 -0.00178 0.07946  574 ILE A CG2   
4766 C CD1   . ILE B 574 ? 1.16740 1.02760 0.91357 -0.21830 -0.00246 0.07550  574 ILE A CD1   
4767 N N     . PHE B 575 ? 1.26707 1.12183 1.03288 -0.19797 0.02212  0.07276  575 PHE A N     
4768 C CA    . PHE B 575 ? 1.40592 1.27110 1.18527 -0.19547 0.02361  0.07775  575 PHE A CA    
4769 C C     . PHE B 575 ? 1.53720 1.39128 1.31607 -0.18945 0.03073  0.07462  575 PHE A C     
4770 O O     . PHE B 575 ? 1.56535 1.43144 1.35580 -0.18444 0.03381  0.07755  575 PHE A O     
4771 C CB    . PHE B 575 ? 1.09021 0.98044 0.88283 -0.19227 0.02410  0.08135  575 PHE A CB    
4772 C CG    . PHE B 575 ? 1.06272 0.96401 0.85788 -0.19709 0.01846  0.08393  575 PHE A CG    
4773 C CD1   . PHE B 575 ? 1.24857 1.15773 1.05090 -0.20312 0.01284  0.09045  575 PHE A CD1   
4774 C CD2   . PHE B 575 ? 1.23973 1.14399 1.03186 -0.19557 0.01881  0.08055  575 PHE A CD2   
4775 C CE1   . PHE B 575 ? 1.50206 1.42180 1.30947 -0.20733 0.00789  0.09349  575 PHE A CE1   
4776 C CE2   . PHE B 575 ? 1.42065 1.33522 1.21757 -0.19990 0.01338  0.08372  575 PHE A CE2   
4777 C CZ    . PHE B 575 ? 1.33995 1.26235 1.14507 -0.20567 0.00803  0.09019  575 PHE A CZ    
4778 N N     . ASN B 576 ? 1.43870 1.27027 1.20467 -0.19004 0.03341  0.06894  576 ASN A N     
4779 C CA    . ASN B 576 ? 1.65305 1.47277 1.42089 -0.18428 0.04086  0.06638  576 ASN A CA    
4780 C C     . ASN B 576 ? 1.73479 1.54709 1.50759 -0.18751 0.03836  0.07051  576 ASN A C     
4781 O O     . ASN B 576 ? 1.77076 1.58257 1.54121 -0.19486 0.03116  0.07367  576 ASN A O     
4782 C CB    . ASN B 576 ? 1.39278 1.19152 1.14565 -0.18266 0.04687  0.05819  576 ASN A CB    
4783 C CG    . ASN B 576 ? 1.69902 1.50587 1.45205 -0.17673 0.05192  0.05507  576 ASN A CG    
4784 O OD1   . ASN B 576 ? 1.80379 1.63157 1.56813 -0.17393 0.05050  0.05860  576 ASN A OD1   
4785 N ND2   . ASN B 576 ? 1.86881 1.65899 1.60922 -0.17490 0.05818  0.04841  576 ASN A ND2   
4786 N N     . GLY B 577 ? 1.75313 1.56005 1.53398 -0.18235 0.04378  0.07110  577 GLY A N     
4787 C CA    . GLY B 577 ? 1.83064 1.63040 1.61824 -0.18498 0.04158  0.07570  577 GLY A CA    
4788 C C     . GLY B 577 ? 1.83885 1.65755 1.63611 -0.18928 0.03422  0.08440  577 GLY A C     
4789 O O     . GLY B 577 ? 1.82471 1.63704 1.62050 -0.19596 0.02869  0.08737  577 GLY A O     
4790 N N     . ILE B 578 ? 1.59839 1.43915 1.40490 -0.18584 0.03439  0.08824  578 ILE A N     
4791 C CA    . ILE B 578 ? 1.32394 1.18415 1.13887 -0.18975 0.02875  0.09632  578 ILE A CA    
4792 C C     . ILE B 578 ? 1.56840 1.44353 1.39538 -0.18473 0.03104  0.10139  578 ILE A C     
4793 O O     . ILE B 578 ? 1.57601 1.44794 1.40495 -0.17831 0.03623  0.09817  578 ILE A O     
4794 C CB    . ILE B 578 ? 1.29664 1.16962 1.10766 -0.19237 0.02586  0.09520  578 ILE A CB    
4795 C CG1   . ILE B 578 ? 1.36842 1.25190 1.18431 -0.19936 0.01942  0.10224  578 ILE A CG1   
4796 C CG2   . ILE B 578 ? 1.68945 1.57925 1.50498 -0.18623 0.02972  0.09384  578 ILE A CG2   
4797 C CD1   . ILE B 578 ? 1.70336 1.56972 1.51341 -0.20652 0.01429  0.10270  578 ILE A CD1   
4798 N N     . SER B 579 ? 1.42641 1.31684 1.26088 -0.18786 0.02726  0.10930  579 SER A N     
4799 C CA    . SER B 579 ? 1.32121 1.22460 1.16515 -0.18425 0.02849  0.11477  579 SER A CA    
4800 C C     . SER B 579 ? 1.35967 1.28520 1.20666 -0.18705 0.02608  0.12019  579 SER A C     
4801 O O     . SER B 579 ? 1.35620 1.29399 1.20815 -0.18461 0.02692  0.12400  579 SER A O     
4802 C CB    . SER B 579 ? 1.30626 1.19990 1.15726 -0.18490 0.02741  0.12041  579 SER A CB    
4803 O OG    . SER B 579 ? 1.88898 1.78001 1.74053 -0.19187 0.02253  0.12559  579 SER A OG    
4804 N N     . HIS B 580 ? 1.24913 1.17931 1.09342 -0.19220 0.02327  0.12072  580 HIS A N     
4805 C CA    . HIS B 580 ? 1.24798 1.19896 1.09634 -0.19497 0.02223  0.12614  580 HIS A CA    
4806 C C     . HIS B 580 ? 1.15416 1.11879 1.00209 -0.18977 0.02622  0.12215  580 HIS A C     
4807 O O     . HIS B 580 ? 1.27489 1.23467 1.11887 -0.18600 0.02848  0.11477  580 HIS A O     
4808 C CB    . HIS B 580 ? 1.36170 1.31503 1.20960 -0.20103 0.01886  0.12736  580 HIS A CB    
4809 C CG    . HIS B 580 ? 1.33143 1.30386 1.18547 -0.20456 0.01841  0.13440  580 HIS A CG    
4810 N ND1   . HIS B 580 ? 1.27101 1.26058 1.12661 -0.20260 0.02175  0.13286  580 HIS A ND1   
4811 C CD2   . HIS B 580 ? 1.29987 1.27675 1.15904 -0.20983 0.01578  0.14298  580 HIS A CD2   
4812 C CE1   . HIS B 580 ? 1.34352 1.34710 1.20439 -0.20651 0.02181  0.13996  580 HIS A CE1   
4813 N NE2   . HIS B 580 ? 1.52397 1.52049 1.38706 -0.21105 0.01806  0.14652  580 HIS A NE2   
4814 N N     . LYS B 581 ? 1.08288 1.06371 0.93407 -0.18993 0.02707  0.12691  581 LYS A N     
4815 C CA    . LYS B 581 ? 1.19563 1.18880 1.04592 -0.18531 0.03072  0.12286  581 LYS A CA    
4816 C C     . LYS B 581 ? 1.30843 1.30663 1.15749 -0.18480 0.03238  0.11700  581 LYS A C     
4817 O O     . LYS B 581 ? 1.41803 1.41532 1.26534 -0.17988 0.03490  0.11039  581 LYS A O     
4818 C CB    . LYS B 581 ? 1.11870 1.12797 0.97029 -0.18719 0.03122  0.12893  581 LYS A CB    
4819 C CG    . LYS B 581 ? 1.39593 1.40204 1.24911 -0.18759 0.02894  0.13553  581 LYS A CG    
4820 C CD    . LYS B 581 ? 1.56565 1.58752 1.41731 -0.19007 0.02922  0.14150  581 LYS A CD    
4821 C CE    . LYS B 581 ? 1.39570 1.41459 1.24916 -0.19064 0.02593  0.14868  581 LYS A CE    
4822 N NZ    . LYS B 581 ? 1.52092 1.52874 1.37943 -0.19400 0.02241  0.15497  581 LYS A NZ    
4823 N N     . THR B 582 ? 1.21518 1.21875 1.06657 -0.18980 0.03077  0.12000  582 THR A N     
4824 C CA    . THR B 582 ? 1.19264 1.20244 1.04550 -0.18968 0.03182  0.11580  582 THR A CA    
4825 C C     . THR B 582 ? 1.17187 1.16739 1.01987 -0.18701 0.03111  0.10903  582 THR A C     
4826 O O     . THR B 582 ? 1.38335 1.38326 1.23120 -0.18295 0.03377  0.10352  582 THR A O     
4827 C CB    . THR B 582 ? 1.23128 1.24599 1.08923 -0.19609 0.02903  0.12128  582 THR A CB    
4828 O OG1   . THR B 582 ? 1.39741 1.42736 1.25936 -0.19768 0.03159  0.12688  582 THR A OG1   
4829 C CG2   . THR B 582 ? 1.19088 1.21016 1.05233 -0.19654 0.02882  0.11807  582 THR A CG2   
4830 N N     . VAL B 583 ? 1.05138 1.02979 0.89509 -0.18934 0.02796  0.10927  583 VAL A N     
4831 C CA    . VAL B 583 ? 1.21264 1.17594 1.04928 -0.18766 0.02773  0.10260  583 VAL A CA    
4832 C C     . VAL B 583 ? 0.98555 0.94443 0.82008 -0.18068 0.03220  0.09786  583 VAL A C     
4833 O O     . VAL B 583 ? 1.07759 1.03177 0.90815 -0.17752 0.03410  0.09190  583 VAL A O     
4834 C CB    . VAL B 583 ? 1.01426 0.95905 0.84514 -0.19265 0.02355  0.10331  583 VAL A CB    
4835 C CG1   . VAL B 583 ? 1.14842 1.08509 0.98061 -0.19313 0.02334  0.10722  583 VAL A CG1   
4836 C CG2   . VAL B 583 ? 1.10383 1.03226 0.92468 -0.19143 0.02396  0.09615  583 VAL A CG2   
4837 N N     . LYS B 584 ? 1.07864 1.03971 0.91658 -0.17863 0.03349  0.10113  584 LYS A N     
4838 C CA    . LYS B 584 ? 1.06076 1.01938 0.89931 -0.17212 0.03721  0.09772  584 LYS A CA    
4839 C C     . LYS B 584 ? 1.13883 1.11147 0.97906 -0.16861 0.03968  0.09396  584 LYS A C     
4840 O O     . LYS B 584 ? 1.12275 1.09089 0.96173 -0.16385 0.04246  0.08862  584 LYS A O     
4841 C CB    . LYS B 584 ? 0.98062 0.94130 0.82413 -0.17156 0.03672  0.10357  584 LYS A CB    
4842 C CG    . LYS B 584 ? 1.22048 1.17726 1.06702 -0.16552 0.03949  0.10173  584 LYS A CG    
4843 C CD    . LYS B 584 ? 1.36628 1.31813 1.21835 -0.16591 0.03787  0.10825  584 LYS A CD    
4844 C CE    . LYS B 584 ? 1.19535 1.13021 1.04622 -0.16869 0.03688  0.10926  584 LYS A CE    
4845 N NZ    . LYS B 584 ? 1.48282 1.41211 1.34122 -0.16848 0.03561  0.11564  584 LYS A NZ    
4846 N N     . SER B 585 ? 1.11138 1.10003 0.95478 -0.17093 0.03918  0.09664  585 SER A N     
4847 C CA    . SER B 585 ? 1.17204 1.17380 1.01771 -0.16782 0.04193  0.09265  585 SER A CA    
4848 C C     . SER B 585 ? 1.14667 1.14356 0.99078 -0.16711 0.04205  0.08755  585 SER A C     
4849 O O     . SER B 585 ? 1.13358 1.12940 0.97747 -0.16237 0.04448  0.08246  585 SER A O     
4850 C CB    . SER B 585 ? 1.04449 1.06258 0.89365 -0.17082 0.04240  0.09618  585 SER A CB    
4851 O OG    . SER B 585 ? 1.45891 1.48805 1.31083 -0.16800 0.04549  0.09160  585 SER A OG    
4852 N N     . LEU B 586 ? 0.97656 0.97072 0.81997 -0.17209 0.03898  0.08952  586 LEU A N     
4853 C CA    . LEU B 586 ? 1.03938 1.02885 0.88077 -0.17250 0.03783  0.08582  586 LEU A CA    
4854 C C     . LEU B 586 ? 1.11836 1.09260 0.95256 -0.16887 0.03941  0.08071  586 LEU A C     
4855 O O     . LEU B 586 ? 0.93606 0.91037 0.76954 -0.16619 0.04075  0.07650  586 LEU A O     
4856 C CB    . LEU B 586 ? 1.02496 1.00978 0.86529 -0.17938 0.03278  0.08958  586 LEU A CB    
4857 C CG    . LEU B 586 ? 0.96492 0.94000 0.79994 -0.18146 0.02972  0.08671  586 LEU A CG    
4858 C CD1   . LEU B 586 ? 0.82921 0.81804 0.67232 -0.18092 0.02968  0.08630  586 LEU A CD1   
4859 C CD2   . LEU B 586 ? 1.03518 0.99891 0.86533 -0.18864 0.02390  0.09010  586 LEU A CD2   
4860 N N     . ARG B 587 ? 1.13676 1.09781 0.96643 -0.16864 0.03976  0.08128  587 ARG A N     
4861 C CA    . ARG B 587 ? 1.09495 1.04134 0.91875 -0.16474 0.04283  0.07650  587 ARG A CA    
4862 C C     . ARG B 587 ? 1.11416 1.06828 0.94305 -0.15810 0.04701  0.07362  587 ARG A C     
4863 O O     . ARG B 587 ? 1.17131 1.12019 0.99745 -0.15489 0.04957  0.06911  587 ARG A O     
4864 C CB    . ARG B 587 ? 1.14435 1.07608 0.96525 -0.16537 0.04324  0.07809  587 ARG A CB    
4865 C CG    . ARG B 587 ? 1.28260 1.19974 1.09960 -0.16056 0.04812  0.07347  587 ARG A CG    
4866 C CD    . ARG B 587 ? 1.42508 1.32419 1.23804 -0.16224 0.04867  0.07411  587 ARG A CD    
4867 N NE    . ARG B 587 ? 1.64952 1.55360 1.47036 -0.16355 0.04648  0.08039  587 ARG A NE    
4868 C CZ    . ARG B 587 ? 1.78830 1.69787 1.61815 -0.15931 0.04841  0.08318  587 ARG A CZ    
4869 N NH1   . ARG B 587 ? 2.02048 1.93162 1.85365 -0.15330 0.05263  0.08008  587 ARG A NH1   
4870 N NH2   . ARG B 587 ? 1.33888 1.25253 1.17486 -0.16147 0.04560  0.08971  587 ARG A NH2   
4871 N N     . LYS B 588 ? 1.06606 1.03242 0.90190 -0.15642 0.04746  0.07640  588 LYS A N     
4872 C CA    . LYS B 588 ? 1.15710 1.13071 0.99783 -0.15078 0.05044  0.07384  588 LYS A CA    
4873 C C     . LYS B 588 ? 1.11670 1.09915 0.95915 -0.14936 0.05130  0.06991  588 LYS A C     
4874 O O     . LYS B 588 ? 1.11856 1.09872 0.96194 -0.14503 0.05386  0.06597  588 LYS A O     
4875 C CB    . LYS B 588 ? 0.90488 0.88990 0.75062 -0.15067 0.04964  0.07786  588 LYS A CB    
4876 C CG    . LYS B 588 ? 1.00384 0.99848 0.85417 -0.14615 0.05145  0.07529  588 LYS A CG    
4877 C CD    . LYS B 588 ? 1.14566 1.14928 0.99823 -0.14711 0.04982  0.07972  588 LYS A CD    
4878 C CE    . LYS B 588 ? 1.07265 1.08995 0.92715 -0.14538 0.05073  0.07689  588 LYS A CE    
4879 N NZ    . LYS B 588 ? 1.41801 1.44387 1.27156 -0.14763 0.04877  0.08129  588 LYS A NZ    
4880 N N     . GLN B 589 ? 1.03808 1.03073 0.88243 -0.15294 0.04936  0.07137  589 GLN A N     
4881 C CA    . GLN B 589 ? 0.99122 0.99285 0.83965 -0.15167 0.05013  0.06827  589 GLN A CA    
4882 C C     . GLN B 589 ? 0.94543 0.93621 0.78930 -0.15155 0.04964  0.06544  589 GLN A C     
4883 O O     . GLN B 589 ? 0.95021 0.94236 0.79631 -0.14774 0.05167  0.06183  589 GLN A O     
4884 C CB    . GLN B 589 ? 1.06758 1.08140 0.92071 -0.15580 0.04858  0.07126  589 GLN A CB    
4885 C CG    . GLN B 589 ? 1.00495 1.02784 0.86471 -0.15480 0.04930  0.06880  589 GLN A CG    
4886 C CD    . GLN B 589 ? 1.34686 1.38010 1.21208 -0.14992 0.05309  0.06498  589 GLN A CD    
4887 O OE1   . GLN B 589 ? 1.54826 1.58431 1.41212 -0.14830 0.05461  0.06495  589 GLN A OE1   
4888 N NE2   . GLN B 589 ? 1.13620 1.17480 1.00777 -0.14789 0.05411  0.06198  589 GLN A NE2   
4889 N N     . LEU B 590 ? 1.09398 1.07353 0.93079 -0.15619 0.04668  0.06720  590 LEU A N     
4890 C CA    . LEU B 590 ? 1.02224 0.98983 0.85155 -0.15717 0.04580  0.06470  590 LEU A CA    
4891 C C     . LEU B 590 ? 0.88652 0.84429 0.71193 -0.15192 0.05038  0.06071  590 LEU A C     
4892 O O     . LEU B 590 ? 1.10596 1.06208 0.93015 -0.14988 0.05170  0.05790  590 LEU A O     
4893 C CB    . LEU B 590 ? 1.20555 1.16010 1.02560 -0.16347 0.04175  0.06683  590 LEU A CB    
4894 C CG    . LEU B 590 ? 1.13972 1.10091 0.96284 -0.16977 0.03605  0.07090  590 LEU A CG    
4895 C CD1   . LEU B 590 ? 1.03143 0.97612 0.84321 -0.17607 0.03160  0.07206  590 LEU A CD1   
4896 C CD2   . LEU B 590 ? 1.12646 1.09657 0.95515 -0.16948 0.03473  0.07029  590 LEU A CD2   
4897 N N     . LEU B 591 ? 0.89890 0.85029 0.72359 -0.14972 0.05292  0.06105  591 LEU A N     
4898 C CA    . LEU B 591 ? 1.01131 0.95444 0.83530 -0.14433 0.05792  0.05798  591 LEU A CA    
4899 C C     . LEU B 591 ? 1.03755 0.99304 0.87056 -0.13932 0.05994  0.05614  591 LEU A C     
4900 O O     . LEU B 591 ? 1.15608 1.10644 0.98856 -0.13566 0.06340  0.05326  591 LEU A O     
4901 C CB    . LEU B 591 ? 1.04807 0.98481 0.87389 -0.14276 0.05978  0.05993  591 LEU A CB    
4902 C CG    . LEU B 591 ? 1.30425 1.22816 1.12936 -0.13798 0.06548  0.05751  591 LEU A CG    
4903 C CD1   . LEU B 591 ? 1.28388 1.18953 1.09582 -0.14019 0.06764  0.05426  591 LEU A CD1   
4904 C CD2   . LEU B 591 ? 1.12412 1.04540 0.95563 -0.13630 0.06644  0.06083  591 LEU A CD2   
4905 N N     . TYR B 592 ? 0.95382 0.92516 0.79477 -0.13936 0.05810  0.05761  592 TYR A N     
4906 C CA    . TYR B 592 ? 0.89779 0.88054 0.74704 -0.13511 0.05966  0.05533  592 TYR A CA    
4907 C C     . TYR B 592 ? 0.93597 0.92002 0.78563 -0.13480 0.05968  0.05280  592 TYR A C     
4908 O O     . TYR B 592 ? 1.14579 1.12884 0.99839 -0.13071 0.06225  0.05024  592 TYR A O     
4909 C CB    . TYR B 592 ? 0.97538 0.97327 0.83049 -0.13617 0.05809  0.05694  592 TYR A CB    
4910 C CG    . TYR B 592 ? 0.83350 0.84249 0.69622 -0.13231 0.05954  0.05408  592 TYR A CG    
4911 C CD1   . TYR B 592 ? 1.04256 1.05137 0.90853 -0.12862 0.06067  0.05359  592 TYR A CD1   
4912 C CD2   . TYR B 592 ? 1.05356 1.07304 0.92122 -0.13258 0.05952  0.05207  592 TYR A CD2   
4913 C CE1   . TYR B 592 ? 1.14878 1.16686 1.02110 -0.12568 0.06129  0.05075  592 TYR A CE1   
4914 C CE2   . TYR B 592 ? 1.16209 1.19058 1.03647 -0.12922 0.06098  0.04881  592 TYR A CE2   
4915 C CZ    . TYR B 592 ? 1.15234 1.17979 1.02821 -0.12598 0.06163  0.04795  592 TYR A CZ    
4916 O OH    . TYR B 592 ? 1.17302 1.20859 1.05500 -0.12318 0.06242  0.04445  592 TYR A OH    
4917 N N     . LEU B 593 ? 0.98623 0.97283 0.83416 -0.13933 0.05644  0.05421  593 LEU A N     
4918 C CA    . LEU B 593 ? 0.85980 0.84631 0.70798 -0.13995 0.05534  0.05308  593 LEU A CA    
4919 C C     . LEU B 593 ? 0.88546 0.85651 0.72416 -0.13900 0.05732  0.05133  593 LEU A C     
4920 O O     . LEU B 593 ? 0.90335 0.87466 0.74430 -0.13618 0.05902  0.04948  593 LEU A O     
4921 C CB    . LEU B 593 ? 1.10818 1.09731 0.95557 -0.14598 0.05057  0.05623  593 LEU A CB    
4922 C CG    . LEU B 593 ? 0.98416 0.98874 0.84370 -0.14642 0.04909  0.05715  593 LEU A CG    
4923 C CD1   . LEU B 593 ? 0.91560 0.92035 0.77476 -0.15283 0.04386  0.06134  593 LEU A CD1   
4924 C CD2   . LEU B 593 ? 0.87311 0.88016 0.73807 -0.14276 0.05043  0.05462  593 LEU A CD2   
4925 N N     . LYS B 594 ? 0.96988 0.92687 0.79781 -0.14142 0.05759  0.05185  594 LYS A N     
4926 C CA    . LYS B 594 ? 0.96281 0.90336 0.77961 -0.14098 0.06062  0.04969  594 LYS A CA    
4927 C C     . LYS B 594 ? 0.94938 0.88974 0.77170 -0.13430 0.06646  0.04738  594 LYS A C     
4928 O O     . LYS B 594 ? 1.06937 1.00289 0.88715 -0.13292 0.06925  0.04565  594 LYS A O     
4929 C CB    . LYS B 594 ? 1.02417 0.94938 0.82990 -0.14406 0.06101  0.04994  594 LYS A CB    
4930 C CG    . LYS B 594 ? 0.88205 0.78888 0.67596 -0.14284 0.06630  0.04682  594 LYS A CG    
4931 C CD    . LYS B 594 ? 1.08935 0.98680 0.88360 -0.14011 0.07101  0.04631  594 LYS A CD    
4932 C CE    . LYS B 594 ? 1.30909 1.18862 1.09344 -0.13793 0.07824  0.04278  594 LYS A CE    
4933 N NZ    . LYS B 594 ? 1.50153 1.37000 1.28688 -0.13577 0.08297  0.04248  594 LYS A NZ    
4934 N N     . ASP B 595 ? 1.00584 0.95385 0.83812 -0.13048 0.06803  0.04783  595 ASP A N     
4935 C CA    . ASP B 595 ? 1.01439 0.96324 0.85410 -0.12443 0.07266  0.04635  595 ASP A CA    
4936 C C     . ASP B 595 ? 0.99061 0.95146 0.83915 -0.12209 0.07192  0.04515  595 ASP A C     
4937 O O     . ASP B 595 ? 1.17342 1.13188 1.02519 -0.11825 0.07553  0.04381  595 ASP A O     
4938 C CB    . ASP B 595 ? 0.84748 0.80026 0.69512 -0.12183 0.07330  0.04797  595 ASP A CB    
4939 C CG    . ASP B 595 ? 1.25663 1.19642 1.09795 -0.12331 0.07477  0.04940  595 ASP A CG    
4940 O OD1   . ASP B 595 ? 1.38520 1.31039 1.21594 -0.12476 0.07744  0.04782  595 ASP A OD1   
4941 O OD2   . ASP B 595 ? 1.51245 1.45601 1.35890 -0.12329 0.07321  0.05211  595 ASP A OD2   
4942 N N     . LYS B 596 ? 0.97329 0.94680 0.82679 -0.12425 0.06778  0.04568  596 LYS A N     
4943 C CA    . LYS B 596 ? 1.08778 1.07153 0.95027 -0.12219 0.06728  0.04427  596 LYS A CA    
4944 C C     . LYS B 596 ? 1.10626 1.08285 0.96359 -0.12311 0.06765  0.04413  596 LYS A C     
4945 O O     . LYS B 596 ? 1.13754 1.11786 1.00184 -0.11994 0.06906  0.04306  596 LYS A O     
4946 C CB    . LYS B 596 ? 1.19037 1.18773 1.05922 -0.12455 0.06376  0.04479  596 LYS A CB    
4947 C CG    . LYS B 596 ? 1.18155 1.18994 1.05851 -0.12217 0.06427  0.04366  596 LYS A CG    
4948 C CD    . LYS B 596 ? 1.23705 1.25883 1.12146 -0.12354 0.06273  0.04300  596 LYS A CD    
4949 C CE    . LYS B 596 ? 1.39023 1.42165 1.27896 -0.12226 0.06349  0.04152  596 LYS A CE    
4950 N NZ    . LYS B 596 ? 1.45136 1.48399 1.34547 -0.11773 0.06496  0.03869  596 LYS A NZ    
4951 N N     . PHE B 597 ? 1.08911 1.05505 0.93378 -0.12784 0.06600  0.04541  597 PHE A N     
4952 C CA    . PHE B 597 ? 0.86235 0.81986 0.69925 -0.12938 0.06620  0.04556  597 PHE A CA    
4953 C C     . PHE B 597 ? 0.91602 0.85975 0.74512 -0.12646 0.07257  0.04389  597 PHE A C     
4954 O O     . PHE B 597 ? 1.06418 1.00612 0.89420 -0.12416 0.07534  0.04348  597 PHE A O     
4955 C CB    . PHE B 597 ? 0.99610 0.94718 0.82143 -0.13649 0.06104  0.04769  597 PHE A CB    
4956 C CG    . PHE B 597 ? 0.88740 0.85195 0.72241 -0.13941 0.05512  0.05024  597 PHE A CG    
4957 C CD1   . PHE B 597 ? 1.06944 1.04263 0.91423 -0.13820 0.05366  0.05109  597 PHE A CD1   
4958 C CD2   . PHE B 597 ? 0.75695 0.72541 0.59257 -0.14335 0.05131  0.05220  597 PHE A CD2   
4959 C CE1   . PHE B 597 ? 0.96071 0.94618 0.81666 -0.14056 0.04891  0.05364  597 PHE A CE1   
4960 C CE2   . PHE B 597 ? 0.90543 0.88653 0.75176 -0.14582 0.04680  0.05491  597 PHE A CE2   
4961 C CZ    . PHE B 597 ? 0.82103 0.81060 0.67797 -0.14427 0.04580  0.05552  597 PHE A CZ    
4962 N N     . LYS B 598 ? 0.89528 0.82922 0.71778 -0.12642 0.07539  0.04320  598 LYS A N     
4963 C CA    . LYS B 598 ? 0.90810 0.82715 0.72282 -0.12399 0.08244  0.04156  598 LYS A CA    
4964 C C     . LYS B 598 ? 0.87247 0.79685 0.70034 -0.11723 0.08751  0.04109  598 LYS A C     
4965 O O     . LYS B 598 ? 0.91387 0.82870 0.73773 -0.11490 0.09371  0.04020  598 LYS A O     
4966 C CB    . LYS B 598 ? 0.83820 0.74682 0.64675 -0.12497 0.08432  0.04116  598 LYS A CB    
4967 C CG    . LYS B 598 ? 1.04610 0.93545 0.84253 -0.12418 0.09183  0.03893  598 LYS A CG    
4968 C CD    . LYS B 598 ? 1.35830 1.24003 1.15566 -0.12317 0.09452  0.03886  598 LYS A CD    
4969 C CE    . LYS B 598 ? 1.65030 1.51059 1.43350 -0.12349 0.10212  0.03592  598 LYS A CE    
4970 N NZ    . LYS B 598 ? 1.89030 1.73820 1.65648 -0.13045 0.09848  0.03471  598 LYS A NZ    
4971 N N     . ASN B 599 ? 0.80259 0.74174 0.64581 -0.11431 0.08508  0.04171  599 ASN A N     
4972 C CA    . ASN B 599 ? 0.70868 0.65321 0.56523 -0.10848 0.08862  0.04154  599 ASN A CA    
4973 C C     . ASN B 599 ? 0.83545 0.78258 0.69434 -0.10753 0.08930  0.04132  599 ASN A C     
4974 O O     . ASN B 599 ? 0.90037 0.84204 0.76127 -0.10415 0.09490  0.04137  599 ASN A O     
4975 C CB    . ASN B 599 ? 0.76634 0.72522 0.63638 -0.10669 0.08488  0.04195  599 ASN A CB    
4976 C CG    . ASN B 599 ? 0.82338 0.77942 0.69387 -0.10648 0.08513  0.04327  599 ASN A CG    
4977 O OD1   . ASN B 599 ? 0.85209 0.79618 0.71898 -0.10519 0.08984  0.04379  599 ASN A OD1   
4978 N ND2   . ASN B 599 ? 0.80509 0.77183 0.68018 -0.10783 0.08041  0.04398  599 ASN A ND2   
4979 N N     . ILE B 600 ? 0.77785 0.73355 0.63788 -0.11043 0.08384  0.04161  600 ILE A N     
4980 C CA    . ILE B 600 ? 0.69138 0.64962 0.55445 -0.11000 0.08369  0.04221  600 ILE A CA    
4981 C C     . ILE B 600 ? 0.87731 0.82053 0.72471 -0.11224 0.08736  0.04287  600 ILE A C     
4982 O O     . ILE B 600 ? 0.79149 0.73226 0.64059 -0.11000 0.09113  0.04353  600 ILE A O     
4983 C CB    . ILE B 600 ? 0.68173 0.65128 0.54994 -0.11305 0.07706  0.04296  600 ILE A CB    
4984 C CG1   . ILE B 600 ? 0.71343 0.69696 0.59559 -0.11080 0.07482  0.04148  600 ILE A CG1   
4985 C CG2   . ILE B 600 ? 0.73585 0.70776 0.60853 -0.11276 0.07642  0.04439  600 ILE A CG2   
4986 C CD1   . ILE B 600 ? 0.75954 0.74959 0.65574 -0.10545 0.07703  0.04011  600 ILE A CD1   
4987 N N     . GLU B 601 ? 0.93527 0.86763 0.76642 -0.11700 0.08645  0.04267  601 GLU A N     
4988 C CA    . GLU B 601 ? 0.92959 0.84565 0.74265 -0.11975 0.09031  0.04252  601 GLU A CA    
4989 C C     . GLU B 601 ? 0.90869 0.81574 0.72203 -0.11465 0.10005  0.04116  601 GLU A C     
4990 O O     . GLU B 601 ? 0.96198 0.86185 0.76913 -0.11413 0.10499  0.04152  601 GLU A O     
4991 C CB    . GLU B 601 ? 0.86013 0.76492 0.65563 -0.12592 0.08750  0.04189  601 GLU A CB    
4992 C CG    . GLU B 601 ? 0.99078 0.87890 0.76461 -0.13060 0.08951  0.04158  601 GLU A CG    
4993 C CD    . GLU B 601 ? 1.12645 0.99757 0.88218 -0.13437 0.09148  0.03908  601 GLU A CD    
4994 O OE1   . GLU B 601 ? 1.42773 1.29747 1.18917 -0.13111 0.09497  0.03745  601 GLU A OE1   
4995 O OE2   . GLU B 601 ? 1.31970 1.17836 1.05544 -0.14092 0.08912  0.03892  601 GLU A OE2   
4996 N N     . GLN B 602 ? 0.84973 0.75733 0.67117 -0.11095 0.10302  0.04018  602 GLN A N     
4997 C CA    . GLN B 602 ? 0.81869 0.71895 0.64451 -0.10566 0.11231  0.03966  602 GLN A CA    
4998 C C     . GLN B 602 ? 0.96756 0.87650 0.80802 -0.10104 0.11468  0.04120  602 GLN A C     
4999 O O     . GLN B 602 ? 1.00846 0.90924 0.84710 -0.09849 0.12272  0.04144  602 GLN A O     
5000 C CB    . GLN B 602 ? 0.84400 0.74612 0.67979 -0.10275 0.11303  0.03966  602 GLN A CB    
5001 C CG    . GLN B 602 ? 1.12238 1.01240 0.94453 -0.10638 0.11319  0.03829  602 GLN A CG    
5002 C CD    . GLN B 602 ? 1.59056 1.46410 1.40769 -0.10374 0.12337  0.03687  602 GLN A CD    
5003 O OE1   . GLN B 602 ? 1.60308 1.46414 1.40715 -0.10452 0.12976  0.03515  602 GLN A OE1   
5004 N NE2   . GLN B 602 ? 1.66557 1.53876 1.49327 -0.10068 0.12523  0.03781  602 GLN A NE2   
5005 N N     . SER B 603 ? 0.83914 0.76424 0.69432 -0.10001 0.10818  0.04215  603 SER A N     
5006 C CA    . SER B 603 ? 0.72838 0.66186 0.59886 -0.09582 0.10961  0.04351  603 SER A CA    
5007 C C     . SER B 603 ? 0.82865 0.75792 0.69115 -0.09776 0.11116  0.04478  603 SER A C     
5008 O O     . SER B 603 ? 0.99505 0.92232 0.86309 -0.09444 0.11707  0.04618  603 SER A O     
5009 C CB    . SER B 603 ? 0.86402 0.81426 0.75022 -0.09488 0.10225  0.04336  603 SER A CB    
5010 O OG    . SER B 603 ? 0.91121 0.86559 0.80664 -0.09239 0.10170  0.04299  603 SER A OG    
5011 N N     . LEU B 604 ? 0.84707 0.77514 0.69718 -0.10338 0.10565  0.04504  604 LEU A N     
5012 C CA    . LEU B 604 ? 0.73040 0.65368 0.57135 -0.10612 0.10626  0.04715  604 LEU A CA    
5013 C C     . LEU B 604 ? 0.77896 0.68441 0.60191 -0.10687 0.11524  0.04658  604 LEU A C     
5014 O O     . LEU B 604 ? 1.01262 0.91428 0.83355 -0.10597 0.12023  0.04845  604 LEU A O     
5015 C CB    . LEU B 604 ? 0.76461 0.69050 0.59723 -0.11254 0.09738  0.04841  604 LEU A CB    
5016 C CG    . LEU B 604 ? 0.78019 0.72339 0.63066 -0.11199 0.08954  0.04894  604 LEU A CG    
5017 C CD1   . LEU B 604 ? 0.83879 0.78328 0.68150 -0.11851 0.08154  0.05077  604 LEU A CD1   
5018 C CD2   . LEU B 604 ? 0.72276 0.67583 0.59063 -0.10813 0.08975  0.05059  604 LEU A CD2   
5019 N N     . LYS B 605 ? 0.82668 0.72058 0.63643 -0.10854 0.11797  0.04392  605 LYS A N     
5020 C CA    . LYS B 605 ? 0.88611 0.76173 0.67884 -0.10883 0.12795  0.04230  605 LYS A CA    
5021 C C     . LYS B 605 ? 1.01755 0.89281 0.82431 -0.10159 0.13818  0.04268  605 LYS A C     
5022 O O     . LYS B 605 ? 0.97456 0.83693 0.77059 -0.10096 0.14801  0.04222  605 LYS A O     
5023 C CB    . LYS B 605 ? 0.87309 0.73640 0.65113 -0.11186 0.12854  0.03901  605 LYS A CB    
5024 C CG    . LYS B 605 ? 0.90390 0.76319 0.66416 -0.12003 0.11966  0.03882  605 LYS A CG    
5025 C CD    . LYS B 605 ? 1.01091 0.85889 0.75992 -0.12258 0.11997  0.03566  605 LYS A CD    
5026 C CE    . LYS B 605 ? 1.23563 1.06302 0.96865 -0.12185 0.13167  0.03217  605 LYS A CE    
5027 N NZ    . LYS B 605 ? 1.47409 1.29185 1.20300 -0.12224 0.13335  0.02911  605 LYS A NZ    
5028 N N     . ALA B 606 ? 0.84725 0.73606 0.67756 -0.09643 0.13616  0.04367  606 ALA A N     
5029 C CA    . ALA B 606 ? 0.78408 0.67433 0.63125 -0.08976 0.14435  0.04505  606 ALA A CA    
5030 C C     . ALA B 606 ? 0.92970 0.82740 0.78747 -0.08766 0.14546  0.04819  606 ALA A C     
5031 O O     . ALA B 606 ? 0.82029 0.72027 0.69403 -0.08228 0.15182  0.05009  606 ALA A O     
5032 C CB    . ALA B 606 ? 0.79201 0.69312 0.65932 -0.08596 0.14050  0.04535  606 ALA A CB    
5033 N N     . GLY B 607 ? 0.91192 0.81360 0.76279 -0.09183 0.13921  0.04937  607 GLY A N     
5034 C CA    . GLY B 607 ? 0.89131 0.80038 0.75308 -0.09022 0.13935  0.05283  607 GLY A CA    
5035 C C     . GLY B 607 ? 0.93998 0.86639 0.82730 -0.08662 0.13285  0.05391  607 GLY A C     
5036 O O     . GLY B 607 ? 0.89902 0.83146 0.79947 -0.08418 0.13396  0.05681  607 GLY A O     
5037 N N     . HIS B 608 ? 0.77382 0.70790 0.66787 -0.08653 0.12619  0.05164  608 HIS A N     
5038 C CA    . HIS B 608 ? 0.80007 0.74930 0.71611 -0.08356 0.12022  0.05177  608 HIS A CA    
5039 C C     . HIS B 608 ? 0.80378 0.76202 0.72493 -0.08554 0.11373  0.05294  608 HIS A C     
5040 O O     . HIS B 608 ? 0.72540 0.68074 0.63321 -0.09018 0.11058  0.05345  608 HIS A O     
5041 C CB    . HIS B 608 ? 0.78915 0.74355 0.70724 -0.08409 0.11466  0.04903  608 HIS A CB    
5042 C CG    . HIS B 608 ? 0.97540 0.92372 0.89495 -0.08141 0.11974  0.04878  608 HIS A CG    
5043 N ND1   . HIS B 608 ? 0.93511 0.88853 0.85965 -0.08121 0.11528  0.04751  608 HIS A ND1   
5044 C CD2   . HIS B 608 ? 0.70489 0.64243 0.62252 -0.07881 0.12918  0.05001  608 HIS A CD2   
5045 C CE1   . HIS B 608 ? 0.95566 0.90195 0.88232 -0.07865 0.12096  0.04846  608 HIS A CE1   
5046 N NE2   . HIS B 608 ? 0.76463 0.70113 0.68778 -0.07692 0.12984  0.04974  608 HIS A NE2   
5047 N N     . THR B 609 ? 0.77083 0.73978 0.71245 -0.08214 0.11140  0.05364  609 THR A N     
5048 C CA    . THR B 609 ? 0.74646 0.72493 0.69698 -0.08335 0.10503  0.05430  609 THR A CA    
5049 C C     . THR B 609 ? 0.84096 0.82592 0.78891 -0.08633 0.09745  0.05126  609 THR A C     
5050 O O     . THR B 609 ? 0.81327 0.80149 0.76322 -0.08558 0.09560  0.04829  609 THR A O     
5051 C CB    . THR B 609 ? 0.72587 0.71349 0.69936 -0.07904 0.10415  0.05487  609 THR A CB    
5052 O OG1   . THR B 609 ? 0.91237 0.89456 0.88985 -0.07637 0.11155  0.05858  609 THR A OG1   
5053 C CG2   . THR B 609 ? 0.75322 0.75020 0.73746 -0.08004 0.09780  0.05502  609 THR A CG2   
5054 N N     . SER B 610 ? 1.01881 1.00579 0.96289 -0.08990 0.09313  0.05264  610 SER A N     
5055 C CA    . SER B 610 ? 0.88316 0.87632 0.82589 -0.09294 0.08663  0.05062  610 SER A CA    
5056 C C     . SER B 610 ? 0.78408 0.78580 0.73904 -0.09377 0.08168  0.05232  610 SER A C     
5057 O O     . SER B 610 ? 0.96286 0.96338 0.92205 -0.09341 0.08275  0.05596  610 SER A O     
5058 C CB    . SER B 610 ? 0.82127 0.80535 0.74293 -0.09796 0.08610  0.05128  610 SER A CB    
5059 O OG    . SER B 610 ? 1.09384 1.07078 1.00490 -0.10133 0.08648  0.05527  610 SER A OG    
5060 N N     . PHE B 611 ? 0.83662 0.84701 0.79808 -0.09485 0.07664  0.04991  611 PHE A N     
5061 C CA    . PHE B 611 ? 0.67718 0.69574 0.65164 -0.09571 0.07204  0.05143  611 PHE A CA    
5062 C C     . PHE B 611 ? 0.82372 0.84838 0.79841 -0.09828 0.06788  0.04945  611 PHE A C     
5063 O O     . PHE B 611 ? 0.80982 0.83452 0.77804 -0.09844 0.06859  0.04607  611 PHE A O     
5064 C CB    . PHE B 611 ? 0.68290 0.70918 0.67817 -0.09122 0.07219  0.04955  611 PHE A CB    
5065 C CG    . PHE B 611 ? 0.74718 0.77983 0.75012 -0.08858 0.07197  0.04345  611 PHE A CG    
5066 C CD1   . PHE B 611 ? 0.63144 0.66094 0.63157 -0.08617 0.07500  0.04144  611 PHE A CD1   
5067 C CD2   . PHE B 611 ? 0.66258 0.70417 0.67585 -0.08868 0.06886  0.03998  611 PHE A CD2   
5068 C CE1   . PHE B 611 ? 0.71170 0.74670 0.71739 -0.08457 0.07386  0.03641  611 PHE A CE1   
5069 C CE2   . PHE B 611 ? 0.73675 0.78331 0.75442 -0.08687 0.06891  0.03411  611 PHE A CE2   
5070 C CZ    . PHE B 611 ? 0.81954 0.86274 0.83259 -0.08512 0.07087  0.03248  611 PHE A CZ    
5071 N N     . ILE B 612 ? 0.90851 0.93862 0.89196 -0.10035 0.06363  0.05223  612 ILE A N     
5072 C CA    . ILE B 612 ? 0.70305 0.73936 0.68907 -0.10307 0.05989  0.05172  612 ILE A CA    
5073 C C     . ILE B 612 ? 0.67268 0.72045 0.68031 -0.09986 0.05928  0.04819  612 ILE A C     
5074 O O     . ILE B 612 ? 0.72611 0.77704 0.74829 -0.09777 0.05871  0.04945  612 ILE A O     
5075 C CB    . ILE B 612 ? 0.77759 0.81124 0.75819 -0.10850 0.05505  0.05834  612 ILE A CB    
5076 C CG1   . ILE B 612 ? 0.64968 0.67001 0.60660 -0.11212 0.05605  0.06111  612 ILE A CG1   
5077 C CG2   . ILE B 612 ? 0.65564 0.69633 0.64123 -0.11128 0.05131  0.05846  612 ILE A CG2   
5078 C CD1   . ILE B 612 ? 0.67243 0.68832 0.62229 -0.11786 0.05090  0.06817  612 ILE A CD1   
5079 N N     . SER B 613 ? 0.82517 0.87865 0.83463 -0.09964 0.05974  0.04373  613 SER A N     
5080 C CA    . SER B 613 ? 0.84844 0.91202 0.87630 -0.09719 0.06003  0.03959  613 SER A CA    
5081 C C     . SER B 613 ? 0.78058 0.84994 0.81309 -0.10029 0.05773  0.04167  613 SER A C     
5082 O O     . SER B 613 ? 1.01176 1.07840 1.03111 -0.10388 0.05659  0.04363  613 SER A O     
5083 C CB    . SER B 613 ? 0.94510 1.01087 0.97164 -0.09436 0.06329  0.03226  613 SER A CB    
5084 O OG    . SER B 613 ? 0.98690 1.06124 1.02850 -0.09250 0.06433  0.02732  613 SER A OG    
5085 N N     . ILE B 614 ? 0.86469 0.94186 0.91729 -0.09896 0.05703  0.04163  614 ILE A N     
5086 C CA    . ILE B 614 ? 0.78070 0.86497 0.84259 -0.10119 0.05567  0.04351  614 ILE A CA    
5087 C C     . ILE B 614 ? 0.79912 0.89217 0.88183 -0.09727 0.05914  0.03777  614 ILE A C     
5088 O O     . ILE B 614 ? 0.83589 0.92983 0.93208 -0.09416 0.05948  0.03648  614 ILE A O     
5089 C CB    . ILE B 614 ? 0.66362 0.74692 0.72922 -0.10531 0.04977  0.05287  614 ILE A CB    
5090 C CG1   . ILE B 614 ? 0.71094 0.80131 0.78520 -0.10829 0.04785  0.05584  614 ILE A CG1   
5091 C CG2   . ILE B 614 ? 0.78027 0.86520 0.86300 -0.10332 0.04797  0.05593  614 ILE A CG2   
5092 C CD1   . ILE B 614 ? 0.74999 0.83875 0.82527 -0.11368 0.04049  0.06591  614 ILE A CD1   
5093 N N     . LYS B 615 ? 0.86994 0.96886 0.95467 -0.09746 0.06227  0.03396  615 LYS A N     
5094 C CA    . LYS B 615 ? 1.00482 1.11078 1.10603 -0.09382 0.06719  0.02690  615 LYS A CA    
5095 C C     . LYS B 615 ? 0.95906 1.07214 1.08467 -0.09353 0.06648  0.03072  615 LYS A C     
5096 O O     . LYS B 615 ? 0.99645 1.11298 1.14031 -0.08989 0.06924  0.02658  615 LYS A O     
5097 C CB    . LYS B 615 ? 1.03765 1.14644 1.12907 -0.09424 0.07191  0.02101  615 LYS A CB    
5098 C CG    . LYS B 615 ? 1.06777 1.18266 1.17207 -0.09102 0.07822  0.01259  615 LYS A CG    
5099 C CD    . LYS B 615 ? 1.53828 1.65477 1.62829 -0.09218 0.08272  0.00732  615 LYS A CD    
5100 C CE    . LYS B 615 ? 1.72134 1.84350 1.82241 -0.08966 0.09002  -0.00114 615 LYS A CE    
5101 N NZ    . LYS B 615 ? 1.52751 1.65080 1.61232 -0.09129 0.09447  -0.00603 615 LYS A NZ    
5102 N N     . ASN B 616 ? 0.93343 1.04845 1.06058 -0.09750 0.06245  0.03884  616 ASN A N     
5103 C CA    . ASN B 616 ? 0.93488 1.05696 1.08655 -0.09791 0.06053  0.04454  616 ASN A CA    
5104 C C     . ASN B 616 ? 0.90557 1.02366 1.05339 -0.10259 0.05187  0.05562  616 ASN A C     
5105 O O     . ASN B 616 ? 0.94276 1.05713 1.07348 -0.10725 0.04831  0.05991  616 ASN A O     
5106 C CB    . ASN B 616 ? 1.16851 1.29865 1.32862 -0.09880 0.06438  0.04384  616 ASN A CB    
5107 C CG    . ASN B 616 ? 1.38702 1.52579 1.57809 -0.09763 0.06467  0.04786  616 ASN A CG    
5108 O OD1   . ASN B 616 ? 1.40346 1.54201 1.60868 -0.09744 0.05986  0.05354  616 ASN A OD1   
5109 N ND2   . ASN B 616 ? 1.43053 1.57708 1.63315 -0.09688 0.07060  0.04543  616 ASN A ND2   
5110 N N     . LEU B 617 ? 0.78661 0.90499 0.94983 -0.10175 0.04830  0.06035  617 LEU A N     
5111 C CA    . LEU B 617 ? 0.87927 0.99243 1.03582 -0.10648 0.03997  0.07067  617 LEU A CA    
5112 C C     . LEU B 617 ? 0.83645 0.95287 0.99666 -0.11222 0.03383  0.07978  617 LEU A C     
5113 O O     . LEU B 617 ? 0.78788 0.89967 0.94126 -0.11733 0.02594  0.08890  617 LEU A O     
5114 C CB    . LEU B 617 ? 0.71285 0.82676 0.88762 -0.10445 0.03748  0.07442  617 LEU A CB    
5115 C CG    . LEU B 617 ? 0.94413 1.04969 1.10483 -0.10285 0.03801  0.07241  617 LEU A CG    
5116 C CD1   . LEU B 617 ? 1.22607 1.33088 1.38153 -0.09778 0.04561  0.06066  617 LEU A CD1   
5117 C CD2   . LEU B 617 ? 0.95153 1.05819 1.13109 -0.10178 0.03460  0.07808  617 LEU A CD2   
5118 N N     . SER B 618 ? 0.96763 1.09180 1.13832 -0.11180 0.03728  0.07766  618 SER A N     
5119 C CA    . SER B 618 ? 1.01926 1.14774 1.19659 -0.11716 0.03164  0.08642  618 SER A CA    
5120 C C     . SER B 618 ? 1.03750 1.16347 1.19407 -0.12059 0.03239  0.08478  618 SER A C     
5121 O O     . SER B 618 ? 1.10079 1.22679 1.25521 -0.12661 0.02558  0.09297  618 SER A O     
5122 C CB    . SER B 618 ? 0.98632 1.12704 1.19757 -0.11435 0.03490  0.08740  618 SER A CB    
5123 O OG    . SER B 618 ? 1.13327 1.27808 1.34778 -0.10891 0.04569  0.07616  618 SER A OG    
5124 N N     . GLN B 619 ? 1.15037 1.27402 1.29220 -0.11734 0.03976  0.07502  619 GLN A N     
5125 C CA    . GLN B 619 ? 1.18239 1.30468 1.30716 -0.12001 0.04140  0.07309  619 GLN A CA    
5126 C C     . GLN B 619 ? 1.01641 1.12648 1.11094 -0.12152 0.04007  0.07073  619 GLN A C     
5127 O O     . GLN B 619 ? 0.96949 1.07638 1.05525 -0.11730 0.04544  0.06294  619 GLN A O     
5128 C CB    . GLN B 619 ? 1.05720 1.18692 1.18945 -0.11555 0.05112  0.06441  619 GLN A CB    
5129 C CG    . GLN B 619 ? 1.08248 1.22317 1.24604 -0.11224 0.05512  0.06436  619 GLN A CG    
5130 C CD    . GLN B 619 ? 1.30447 1.45157 1.47242 -0.10863 0.06552  0.05562  619 GLN A CD    
5131 O OE1   . GLN B 619 ? 1.25567 1.39866 1.40524 -0.10682 0.07023  0.04746  619 GLN A OE1   
5132 N NE2   . GLN B 619 ? 1.60118 1.75834 1.79368 -0.10783 0.06929  0.05766  619 GLN A NE2   
5133 N N     . LYS B 620 ? 0.95643 1.05928 1.03551 -0.12773 0.03290  0.07749  620 LYS A N     
5134 C CA    . LYS B 620 ? 0.92422 1.01473 0.97480 -0.12935 0.03253  0.07520  620 LYS A CA    
5135 C C     . LYS B 620 ? 0.94924 1.03951 0.98829 -0.12719 0.03894  0.06778  620 LYS A C     
5136 O O     . LYS B 620 ? 0.95956 1.04058 0.97862 -0.12672 0.04049  0.06439  620 LYS A O     
5137 C CB    . LYS B 620 ? 0.87136 0.95377 0.90700 -0.13708 0.02412  0.08307  620 LYS A CB    
5138 C CG    . LYS B 620 ? 0.91014 0.99390 0.94031 -0.14115 0.02293  0.08436  620 LYS A CG    
5139 C CD    . LYS B 620 ? 0.94475 1.01636 0.95271 -0.14862 0.01552  0.08954  620 LYS A CD    
5140 C CE    . LYS B 620 ? 0.95505 1.02924 0.97339 -0.15518 0.00574  0.09973  620 LYS A CE    
5141 N NZ    . LYS B 620 ? 1.26016 1.32321 1.25674 -0.16330 -0.00140 0.10389  620 LYS A NZ    
5142 N N     . SER B 621 ? 0.99289 1.09309 1.04452 -0.12596 0.04292  0.06558  621 SER A N     
5143 C CA    . SER B 621 ? 0.99396 1.09478 1.03502 -0.12444 0.04877  0.05928  621 SER A CA    
5144 C C     . SER B 621 ? 0.95023 1.05117 0.99022 -0.11848 0.05521  0.05059  621 SER A C     
5145 O O     . SER B 621 ? 1.15099 1.25217 1.18142 -0.11733 0.05964  0.04541  621 SER A O     
5146 C CB    . SER B 621 ? 1.05232 1.16389 1.10702 -0.12544 0.05151  0.06024  621 SER A CB    
5147 O OG    . SER B 621 ? 1.17893 1.30037 1.25858 -0.12190 0.05488  0.05921  621 SER A OG    
5148 N N     . THR B 622 ? 0.84586 0.94659 0.89555 -0.11509 0.05529  0.04932  622 THR A N     
5149 C CA    . THR B 622 ? 1.03516 1.13474 1.08341 -0.11003 0.06008  0.04160  622 THR A CA    
5150 C C     . THR B 622 ? 0.96712 1.05616 1.00063 -0.10968 0.05786  0.04216  622 THR A C     
5151 O O     . THR B 622 ? 1.00533 1.09306 1.04037 -0.10569 0.06049  0.03732  622 THR A O     
5152 C CB    . THR B 622 ? 1.01742 1.12434 1.08893 -0.10599 0.06273  0.03884  622 THR A CB    
5153 O OG1   . THR B 622 ? 1.05375 1.15788 1.13309 -0.10611 0.05801  0.04412  622 THR A OG1   
5154 C CG2   . THR B 622 ? 0.93059 1.04761 1.01959 -0.10663 0.06501  0.04004  622 THR A CG2   
5155 N N     . ILE B 623 ? 0.91426 0.99537 0.93350 -0.11391 0.05339  0.04782  623 ILE A N     
5156 C CA    . ILE B 623 ? 0.71059 0.78120 0.71666 -0.11378 0.05214  0.04903  623 ILE A CA    
5157 C C     . ILE B 623 ? 0.78426 0.84907 0.77445 -0.11223 0.05572  0.04431  623 ILE A C     
5158 O O     . ILE B 623 ? 0.94116 1.00552 0.92194 -0.11432 0.05628  0.04359  623 ILE A O     
5159 C CB    . ILE B 623 ? 0.68631 0.74955 0.68199 -0.11942 0.04631  0.05653  623 ILE A CB    
5160 C CG1   . ILE B 623 ? 0.79060 0.85838 0.80263 -0.12061 0.04190  0.06225  623 ILE A CG1   
5161 C CG2   . ILE B 623 ? 0.89219 0.94260 0.86826 -0.11984 0.04695  0.05668  623 ILE A CG2   
5162 C CD1   . ILE B 623 ? 0.87618 0.93619 0.87688 -0.12701 0.03505  0.07018  623 ILE A CD1   
5163 N N     . ARG B 624 ? 0.70820 0.76888 0.69694 -0.10865 0.05792  0.04173  624 ARG A N     
5164 C CA    . ARG B 624 ? 0.76299 0.81712 0.73835 -0.10719 0.06066  0.03878  624 ARG A CA    
5165 C C     . ARG B 624 ? 0.86919 0.91341 0.83678 -0.10672 0.06086  0.04146  624 ARG A C     
5166 O O     . ARG B 624 ? 0.80894 0.85364 0.78520 -0.10558 0.06003  0.04349  624 ARG A O     
5167 C CB    . ARG B 624 ? 0.91097 0.97076 0.89396 -0.10297 0.06386  0.03248  624 ARG A CB    
5168 C CG    . ARG B 624 ? 0.93946 1.00916 0.93077 -0.10308 0.06504  0.02899  624 ARG A CG    
5169 C CD    . ARG B 624 ? 0.95226 1.02411 0.94108 -0.10084 0.06778  0.02299  624 ARG A CD    
5170 N NE    . ARG B 624 ? 1.55290 1.63355 1.54800 -0.10101 0.07007  0.01897  624 ARG A NE    
5171 C CZ    . ARG B 624 ? 1.68660 1.77254 1.69263 -0.09827 0.07239  0.01327  624 ARG A CZ    
5172 N NH1   . ARG B 624 ? 1.34964 1.43334 1.36250 -0.09526 0.07181  0.01134  624 ARG A NH1   
5173 N NH2   . ARG B 624 ? 1.80833 1.90135 1.81831 -0.09866 0.07565  0.00934  624 ARG A NH2   
5174 N N     . LEU B 625 ? 0.82063 0.85566 0.77228 -0.10760 0.06245  0.04165  625 LEU A N     
5175 C CA    . LEU B 625 ? 0.74201 0.76646 0.68455 -0.10711 0.06432  0.04379  625 LEU A CA    
5176 C C     . LEU B 625 ? 0.78259 0.80443 0.72410 -0.10312 0.06845  0.04059  625 LEU A C     
5177 O O     . LEU B 625 ? 1.00484 1.02386 0.93788 -0.10370 0.06949  0.03924  625 LEU A O     
5178 C CB    . LEU B 625 ? 0.71119 0.72500 0.63547 -0.11210 0.06297  0.04722  625 LEU A CB    
5179 C CG    . LEU B 625 ? 0.77781 0.77918 0.69011 -0.11215 0.06602  0.04917  625 LEU A CG    
5180 C CD1   . LEU B 625 ? 0.66983 0.67309 0.59049 -0.11153 0.06504  0.05223  625 LEU A CD1   
5181 C CD2   . LEU B 625 ? 0.67343 0.66290 0.56537 -0.11760 0.06485  0.05126  625 LEU A CD2   
5182 N N     . TYR B 626 ? 0.80558 0.82856 0.75699 -0.09931 0.07034  0.04003  626 TYR A N     
5183 C CA    . TYR B 626 ? 0.72053 0.74205 0.67454 -0.09553 0.07345  0.03787  626 TYR A CA    
5184 C C     . TYR B 626 ? 0.82532 0.83587 0.77142 -0.09463 0.07761  0.04072  626 TYR A C     
5185 O O     . TYR B 626 ? 0.93692 0.94338 0.88105 -0.09552 0.07831  0.04380  626 TYR A O     
5186 C CB    . TYR B 626 ? 0.85198 0.88187 0.82355 -0.09196 0.07279  0.03530  626 TYR A CB    
5187 C CG    . TYR B 626 ? 0.83545 0.87529 0.81460 -0.09224 0.07031  0.03113  626 TYR A CG    
5188 C CD1   . TYR B 626 ? 0.86373 0.90972 0.85122 -0.09336 0.06830  0.03114  626 TYR A CD1   
5189 C CD2   . TYR B 626 ? 0.90434 0.94724 0.88254 -0.09152 0.07028  0.02744  626 TYR A CD2   
5190 C CE1   . TYR B 626 ? 0.91948 0.97409 0.91429 -0.09333 0.06754  0.02690  626 TYR A CE1   
5191 C CE2   . TYR B 626 ? 0.87467 0.92587 0.85776 -0.09204 0.06904  0.02319  626 TYR A CE2   
5192 C CZ    . TYR B 626 ? 0.95536 1.01225 0.94683 -0.09272 0.06830  0.02259  626 TYR A CZ    
5193 O OH    . TYR B 626 ? 1.17491 1.23960 1.17163 -0.09296 0.06852  0.01795  626 TYR A OH    
5194 N N     . VAL B 627 ? 0.84770 0.85347 0.78966 -0.09293 0.08063  0.03997  627 VAL A N     
5195 C CA    . VAL B 627 ? 0.76138 0.75718 0.69891 -0.09102 0.08617  0.04213  627 VAL A CA    
5196 C C     . VAL B 627 ? 0.79417 0.79309 0.74401 -0.08675 0.08771  0.04129  627 VAL A C     
5197 O O     . VAL B 627 ? 0.76973 0.77440 0.72325 -0.08655 0.08477  0.03910  627 VAL A O     
5198 C CB    . VAL B 627 ? 0.68729 0.67143 0.60673 -0.09368 0.08891  0.04287  627 VAL A CB    
5199 C CG1   . VAL B 627 ? 0.71140 0.69098 0.61784 -0.09859 0.08673  0.04435  627 VAL A CG1   
5200 C CG2   . VAL B 627 ? 0.63014 0.61641 0.54746 -0.09434 0.08697  0.04103  627 VAL A CG2   
5201 N N     . LYS B 628 ? 0.73496 0.73013 0.69118 -0.08370 0.09211  0.04353  628 LYS A N     
5202 C CA    . LYS B 628 ? 0.69837 0.69632 0.66847 -0.07981 0.09321  0.04389  628 LYS A CA    
5203 C C     . LYS B 628 ? 0.85956 0.84860 0.82367 -0.07875 0.09815  0.04547  628 LYS A C     
5204 O O     . LYS B 628 ? 1.09247 1.07192 1.05093 -0.07786 0.10486  0.04768  628 LYS A O     
5205 C CB    . LYS B 628 ? 0.73894 0.73831 0.72202 -0.07699 0.09545  0.04617  628 LYS A CB    
5206 C CG    . LYS B 628 ? 0.64432 0.64848 0.64493 -0.07348 0.09472  0.04677  628 LYS A CG    
5207 C CD    . LYS B 628 ? 0.70758 0.71268 0.72163 -0.07088 0.09728  0.04974  628 LYS A CD    
5208 C CE    . LYS B 628 ? 0.75958 0.76889 0.79196 -0.06777 0.09608  0.05105  628 LYS A CE    
5209 N NZ    . LYS B 628 ? 0.79400 0.80285 0.83997 -0.06504 0.10002  0.05515  628 LYS A NZ    
5210 N N     . ASP B 629 ? 0.90669 0.89853 0.87209 -0.07894 0.09517  0.04446  629 ASP A N     
5211 C CA    . ASP B 629 ? 0.83519 0.81902 0.79647 -0.07811 0.09909  0.04624  629 ASP A CA    
5212 C C     . ASP B 629 ? 0.78961 0.77504 0.76753 -0.07423 0.10041  0.04906  629 ASP A C     
5213 O O     . ASP B 629 ? 1.01083 0.98931 0.98894 -0.07281 0.10460  0.05137  629 ASP A O     
5214 C CB    . ASP B 629 ? 0.86049 0.84553 0.81235 -0.08131 0.09480  0.04468  629 ASP A CB    
5215 C CG    . ASP B 629 ? 0.82967 0.80948 0.76427 -0.08527 0.09495  0.04324  629 ASP A CG    
5216 O OD1   . ASP B 629 ? 0.89211 0.86571 0.82023 -0.08573 0.09858  0.04365  629 ASP A OD1   
5217 O OD2   . ASP B 629 ? 0.94879 0.93071 0.87627 -0.08831 0.09112  0.04214  629 ASP A OD2   
5218 N N     . TYR B 630 ? 0.94353 0.93761 0.93641 -0.07262 0.09674  0.04917  630 TYR A N     
5219 C CA    . TYR B 630 ? 1.00496 1.00096 1.01550 -0.06934 0.09708  0.05262  630 TYR A CA    
5220 C C     . TYR B 630 ? 0.89815 0.89889 0.92233 -0.06733 0.09698  0.05331  630 TYR A C     
5221 O O     . TYR B 630 ? 0.92072 0.92439 0.94129 -0.06862 0.09548  0.05080  630 TYR A O     
5222 C CB    . TYR B 630 ? 1.05322 1.05605 1.06904 -0.07068 0.08933  0.05243  630 TYR A CB    
5223 C CG    . TYR B 630 ? 1.22860 1.22771 1.23209 -0.07298 0.08865  0.05240  630 TYR A CG    
5224 C CD1   . TYR B 630 ? 1.23105 1.22245 1.23662 -0.07125 0.09339  0.05633  630 TYR A CD1   
5225 C CD2   . TYR B 630 ? 1.10476 1.10807 1.09590 -0.07682 0.08363  0.04872  630 TYR A CD2   
5226 C CE1   . TYR B 630 ? 1.25913 1.24681 1.25454 -0.07345 0.09249  0.05662  630 TYR A CE1   
5227 C CE2   . TYR B 630 ? 1.02803 1.02819 1.00868 -0.07916 0.08286  0.04928  630 TYR A CE2   
5228 C CZ    . TYR B 630 ? 1.23464 1.22686 1.21737 -0.07755 0.08695  0.05326  630 TYR A CZ    
5229 O OH    . TYR B 630 ? 1.39853 1.38727 1.37190 -0.07995 0.08595  0.05413  630 TYR A OH    
5230 N N     . ALA B 631 ? 1.08457 1.08610 1.12614 -0.06419 0.09846  0.05736  631 ALA A N     
5231 C CA    . ALA B 631 ? 1.04868 1.05520 1.10646 -0.06228 0.09762  0.05883  631 ALA A CA    
5232 C C     . ALA B 631 ? 1.03407 1.04950 1.10481 -0.06310 0.08816  0.05803  631 ALA A C     
5233 O O     . ALA B 631 ? 1.15675 1.17308 1.23057 -0.06362 0.08462  0.05965  631 ALA A O     
5234 C CB    . ALA B 631 ? 1.05268 1.05388 1.12238 -0.05838 0.10624  0.06448  631 ALA A CB    
5235 N N     . VAL B 632 ? 0.98295 1.00443 1.06109 -0.06354 0.08380  0.05565  632 VAL A N     
5236 C CA    . VAL B 632 ? 1.01972 1.04848 1.10614 -0.06527 0.07436  0.05330  632 VAL A CA    
5237 C C     . VAL B 632 ? 0.86316 0.89351 0.97008 -0.06341 0.07222  0.05876  632 VAL A C     
5238 O O     . VAL B 632 ? 1.00990 1.04386 1.12106 -0.06537 0.06454  0.05876  632 VAL A O     
5239 C CB    . VAL B 632 ? 0.86559 0.89943 0.95279 -0.06656 0.07043  0.04800  632 VAL A CB    
5240 C CG1   . VAL B 632 ? 1.08499 1.11785 1.15434 -0.06845 0.07233  0.04369  632 VAL A CG1   
5241 C CG2   . VAL B 632 ? 1.02775 1.06211 1.13077 -0.06400 0.07298  0.05093  632 VAL A CG2   
5242 N N     . LYS B 633 ? 0.90380 0.93160 1.02389 -0.05999 0.07870  0.06399  633 LYS A N     
5243 C CA    . LYS B 633 ? 0.87107 0.89997 1.01185 -0.05803 0.07775  0.07053  633 LYS A CA    
5244 C C     . LYS B 633 ? 0.92162 0.94714 1.05953 -0.05792 0.07880  0.07381  633 LYS A C     
5245 O O     . LYS B 633 ? 1.01532 1.04414 1.16498 -0.05884 0.07198  0.07723  633 LYS A O     
5246 C CB    . LYS B 633 ? 0.75726 0.78356 0.91199 -0.05412 0.08663  0.07596  633 LYS A CB    
5247 C CG    . LYS B 633 ? 0.80807 0.83890 0.97440 -0.05397 0.08407  0.07536  633 LYS A CG    
5248 C CD    . LYS B 633 ? 0.85049 0.87739 1.02305 -0.05061 0.09499  0.08023  633 LYS A CD    
5249 C CE    . LYS B 633 ? 0.82722 0.85876 1.01408 -0.05037 0.09248  0.08103  633 LYS A CE    
5250 N NZ    . LYS B 633 ? 1.22952 1.26433 1.44325 -0.04831 0.09159  0.08792  633 LYS A NZ    
5251 N N     . ASP B 634 ? 1.11213 1.13069 1.23438 -0.05719 0.08674  0.07299  634 ASP A N     
5252 C CA    . ASP B 634 ? 1.19987 1.21421 1.31809 -0.05717 0.08821  0.07557  634 ASP A CA    
5253 C C     . ASP B 634 ? 1.12064 1.14006 1.23252 -0.06130 0.07723  0.07327  634 ASP A C     
5254 O O     . ASP B 634 ? 0.90555 0.92620 1.02708 -0.06172 0.07288  0.07799  634 ASP A O     
5255 C CB    . ASP B 634 ? 1.08094 1.08638 1.17972 -0.05673 0.09745  0.07324  634 ASP A CB    
5256 C CG    . ASP B 634 ? 1.42652 1.42387 1.53107 -0.05343 0.10667  0.07830  634 ASP A CG    
5257 O OD1   . ASP B 634 ? 1.56390 1.56321 1.69020 -0.05087 0.10690  0.08438  634 ASP A OD1   
5258 O OD2   . ASP B 634 ? 1.74254 1.73122 1.83056 -0.05351 0.11371  0.07622  634 ASP A OD2   
5259 N N     . VAL B 635 ? 1.07279 1.09520 1.16864 -0.06455 0.07283  0.06643  635 VAL A N     
5260 C CA    . VAL B 635 ? 1.07489 1.10171 1.16182 -0.06879 0.06363  0.06369  635 VAL A CA    
5261 C C     . VAL B 635 ? 1.14154 1.17454 1.24337 -0.07037 0.05398  0.06559  635 VAL A C     
5262 O O     . VAL B 635 ? 1.17165 1.20647 1.27458 -0.07291 0.04717  0.06843  635 VAL A O     
5263 C CB    . VAL B 635 ? 0.95335 0.98219 1.02188 -0.07153 0.06243  0.05592  635 VAL A CB    
5264 C CG1   . VAL B 635 ? 0.97134 1.00634 1.03437 -0.07583 0.05272  0.05216  635 VAL A CG1   
5265 C CG2   . VAL B 635 ? 0.87536 0.89841 0.92681 -0.07189 0.06844  0.05496  635 VAL A CG2   
5266 N N     . LEU B 636 ? 0.89838 0.93437 1.01200 -0.06931 0.05272  0.06449  636 LEU A N     
5267 C CA    . LEU B 636 ? 0.77869 0.81976 0.90643 -0.07132 0.04289  0.06596  636 LEU A CA    
5268 C C     . LEU B 636 ? 0.93034 0.97101 1.07637 -0.07011 0.04112  0.07526  636 LEU A C     
5269 O O     . LEU B 636 ? 0.88307 0.92731 1.03555 -0.07346 0.03081  0.07760  636 LEU A O     
5270 C CB    . LEU B 636 ? 0.76554 0.80894 0.90459 -0.07000 0.04281  0.06369  636 LEU A CB    
5271 C CG    . LEU B 636 ? 0.94525 0.99053 1.07057 -0.07197 0.04147  0.05451  636 LEU A CG    
5272 C CD1   . LEU B 636 ? 0.83131 0.87805 0.96999 -0.07004 0.04261  0.05341  636 LEU A CD1   
5273 C CD2   . LEU B 636 ? 0.84916 0.89770 0.96459 -0.07702 0.03160  0.04924  636 LEU A CD2   
5274 N N     . THR B 637 ? 0.93741 0.97344 1.09190 -0.06563 0.05100  0.08078  637 THR A N     
5275 C CA    . THR B 637 ? 0.93826 0.97397 1.11315 -0.06390 0.05045  0.09015  637 THR A CA    
5276 C C     . THR B 637 ? 0.90555 0.93925 1.07245 -0.06575 0.04811  0.09282  637 THR A C     
5277 O O     . THR B 637 ? 1.00539 1.04273 1.18018 -0.06884 0.03804  0.09731  637 THR A O     
5278 C CB    . THR B 637 ? 0.90463 0.93573 1.09314 -0.05810 0.06324  0.09494  637 THR A CB    
5279 O OG1   . THR B 637 ? 1.35142 1.37551 1.52090 -0.05642 0.07376  0.09109  637 THR A OG1   
5280 C CG2   . THR B 637 ? 0.87766 0.91168 1.07749 -0.05671 0.06412  0.09419  637 THR A CG2   
5281 N N     . LYS B 638 ? 0.99683 1.02444 1.14809 -0.06429 0.05683  0.09050  638 LYS A N     
5282 C CA    . LYS B 638 ? 0.98071 1.00539 1.12660 -0.06546 0.05598  0.09384  638 LYS A CA    
5283 C C     . LYS B 638 ? 1.12912 1.15873 1.26137 -0.07153 0.04395  0.09128  638 LYS A C     
5284 O O     . LYS B 638 ? 1.24462 1.27469 1.38011 -0.07361 0.03845  0.09682  638 LYS A O     
5285 C CB    . LYS B 638 ? 1.02686 1.04325 1.15655 -0.06332 0.06731  0.09065  638 LYS A CB    
5286 C CG    . LYS B 638 ? 1.13176 1.14110 1.27213 -0.05766 0.08055  0.09361  638 LYS A CG    
5287 C CD    . LYS B 638 ? 1.22561 1.22524 1.34769 -0.05666 0.09037  0.09041  638 LYS A CD    
5288 C CE    . LYS B 638 ? 1.49900 1.48990 1.63015 -0.05134 0.10435  0.09335  638 LYS A CE    
5289 N NZ    . LYS B 638 ? 1.28825 1.27896 1.41900 -0.04946 0.11037  0.09074  638 LYS A NZ    
5290 N N     . GLN B 639 ? 1.12061 1.15378 1.23805 -0.07451 0.04004  0.08327  639 GLN A N     
5291 C CA    . GLN B 639 ? 1.13841 1.17526 1.23873 -0.08024 0.03109  0.07941  639 GLN A CA    
5292 C C     . GLN B 639 ? 1.05901 1.10182 1.16497 -0.08435 0.01912  0.07906  639 GLN A C     
5293 O O     . GLN B 639 ? 1.19902 1.24454 1.29046 -0.08964 0.01137  0.07623  639 GLN A O     
5294 C CB    . GLN B 639 ? 1.24610 1.28242 1.32459 -0.08118 0.03539  0.07024  639 GLN A CB    
5295 C CG    . GLN B 639 ? 1.13363 1.16363 1.20187 -0.07893 0.04500  0.07012  639 GLN A CG    
5296 C CD    . GLN B 639 ? 1.43553 1.46360 1.49829 -0.08109 0.04267  0.07461  639 GLN A CD    
5297 O OE1   . GLN B 639 ? 1.51788 1.55006 1.57078 -0.08584 0.03479  0.07374  639 GLN A OE1   
5298 N NE2   . GLN B 639 ? 1.67901 1.70037 1.74800 -0.07773 0.04985  0.07949  639 GLN A NE2   
5299 N N     . VAL B 640 ? 0.99273 1.03724 1.11850 -0.08245 0.01742  0.08174  640 VAL A N     
5300 C CA    . VAL B 640 ? 1.08998 1.13912 1.22123 -0.08685 0.00532  0.08123  640 VAL A CA    
5301 C C     . VAL B 640 ? 1.04163 1.09208 1.20057 -0.08554 0.00103  0.09130  640 VAL A C     
5302 O O     . VAL B 640 ? 1.02616 1.07874 1.19067 -0.08957 -0.00932 0.09737  640 VAL A O     
5303 C CB    . VAL B 640 ? 0.96406 1.01472 1.09063 -0.08701 0.00567  0.07215  640 VAL A CB    
5304 C CG1   . VAL B 640 ? 0.91954 0.97350 1.05055 -0.09205 -0.00704 0.07090  640 VAL A CG1   
5305 C CG2   . VAL B 640 ? 1.00194 1.05188 1.10387 -0.08812 0.01020  0.06287  640 VAL A CG2   
5306 N N     . LEU B 641 ? 0.99076 1.04015 1.16771 -0.08014 0.00885  0.09376  641 LEU A N     
5307 C CA    . LEU B 641 ? 1.04298 1.09437 1.24908 -0.07860 0.00549  0.10334  641 LEU A CA    
5308 C C     . LEU B 641 ? 1.03798 1.08835 1.25606 -0.07783 0.00506  0.11360  641 LEU A C     
5309 O O     . LEU B 641 ? 1.24437 1.29805 1.48082 -0.08027 -0.00485 0.12183  641 LEU A O     
5310 C CB    . LEU B 641 ? 1.02477 1.07478 1.24619 -0.07252 0.01650  0.10417  641 LEU A CB    
5311 C CG    . LEU B 641 ? 1.06701 1.11873 1.32114 -0.06943 0.01700  0.11495  641 LEU A CG    
5312 C CD1   . LEU B 641 ? 1.10158 1.15863 1.36982 -0.07403 0.00249  0.11726  641 LEU A CD1   
5313 C CD2   . LEU B 641 ? 0.98649 1.03565 1.25035 -0.06315 0.03105  0.11529  641 LEU A CD2   
5314 N N     . GLU B 642 ? 0.95491 1.00042 1.16370 -0.07470 0.01523  0.11355  642 GLU A N     
5315 C CA    . GLU B 642 ? 1.02154 1.06495 1.24331 -0.07306 0.01681  0.12308  642 GLU A CA    
5316 C C     . GLU B 642 ? 1.14747 1.19180 1.35454 -0.07866 0.00730  0.12428  642 GLU A C     
5317 O O     . GLU B 642 ? 1.34050 1.38324 1.55836 -0.07789 0.00729  0.13265  642 GLU A O     
5318 C CB    . GLU B 642 ? 1.01627 1.05242 1.23685 -0.06667 0.03351  0.12257  642 GLU A CB    
5319 C CG    . GLU B 642 ? 0.98754 1.02216 1.22453 -0.06096 0.04416  0.12349  642 GLU A CG    
5320 C CD    . GLU B 642 ? 1.33921 1.36529 1.57199 -0.05537 0.06083  0.12258  642 GLU A CD    
5321 O OE1   . GLU B 642 ? 1.42923 1.45039 1.64019 -0.05632 0.06415  0.11788  642 GLU A OE1   
5322 O OE2   . GLU B 642 ? 1.16237 1.18625 1.41326 -0.05029 0.07075  0.12655  642 GLU A OE2   
5323 N N     . LYS B 643 ? 1.04215 1.08890 1.22563 -0.08427 -0.00035 0.11646  643 LYS A N     
5324 C CA    . LYS B 643 ? 1.20671 1.25446 1.37344 -0.09011 -0.00886 0.11721  643 LYS A CA    
5325 C C     . LYS B 643 ? 1.24035 1.29317 1.41172 -0.09697 -0.02546 0.12176  643 LYS A C     
5326 O O     . LYS B 643 ? 1.39348 1.44733 1.55317 -0.10238 -0.03366 0.12453  643 LYS A O     
5327 C CB    . LYS B 643 ? 1.24362 1.29047 1.37941 -0.09237 -0.00586 0.10582  643 LYS A CB    
5328 C CG    . LYS B 643 ? 1.41397 1.45566 1.53776 -0.08943 0.00488  0.10434  643 LYS A CG    
5329 C CD    . LYS B 643 ? 1.49607 1.53799 1.59185 -0.09206 0.00686  0.09386  643 LYS A CD    
5330 C CE    . LYS B 643 ? 1.60090 1.63797 1.68392 -0.09074 0.01480  0.09338  643 LYS A CE    
5331 N NZ    . LYS B 643 ? 1.68442 1.72179 1.76555 -0.09449 0.00823  0.10050  643 LYS A NZ    
5332 N N     . PHE B 644 ? 1.16740 1.22308 1.35507 -0.09733 -0.03096 0.12299  644 PHE A N     
5333 C CA    . PHE B 644 ? 1.16634 1.22595 1.35619 -0.10469 -0.04760 0.12610  644 PHE A CA    
5334 C C     . PHE B 644 ? 1.21350 1.27558 1.43793 -0.10320 -0.05274 0.13758  644 PHE A C     
5335 O O     . PHE B 644 ? 1.23159 1.29315 1.47564 -0.09679 -0.04350 0.13888  644 PHE A O     
5336 C CB    . PHE B 644 ? 1.08361 1.14403 1.25570 -0.10842 -0.05166 0.11428  644 PHE A CB    
5337 C CG    . PHE B 644 ? 1.01205 1.07124 1.15084 -0.11186 -0.05011 0.10426  644 PHE A CG    
5338 C CD1   . PHE B 644 ? 1.11915 1.17855 1.24331 -0.11678 -0.05574 0.10773  644 PHE A CD1   
5339 C CD2   . PHE B 644 ? 1.00685 1.06497 1.13043 -0.11017 -0.04280 0.09210  644 PHE A CD2   
5340 C CE1   . PHE B 644 ? 1.39142 1.45013 1.48601 -0.11996 -0.05365 0.09907  644 PHE A CE1   
5341 C CE2   . PHE B 644 ? 1.22453 1.28202 1.31980 -0.11315 -0.04078 0.08345  644 PHE A CE2   
5342 C CZ    . PHE B 644 ? 1.36711 1.42496 1.44772 -0.11801 -0.04590 0.08686  644 PHE A CZ    
5343 N N     . LYS B 645 ? 1.33639 1.40132 1.56839 -0.10949 -0.06772 0.14646  645 LYS A N     
5344 C CA    . LYS B 645 ? 1.26619 1.33424 1.53301 -0.10898 -0.07458 0.15887  645 LYS A CA    
5345 C C     . LYS B 645 ? 1.19658 1.26689 1.47056 -0.11202 -0.08302 0.15570  645 LYS A C     
5346 O O     . LYS B 645 ? 1.57642 1.64917 1.88164 -0.10941 -0.08424 0.16389  645 LYS A O     
5347 C CB    . LYS B 645 ? 1.18817 1.25849 1.46173 -0.11510 -0.08860 0.17094  645 LYS A CB    
5348 C CG    . LYS B 645 ? 1.58585 1.65372 1.84962 -0.11359 -0.08257 0.17390  645 LYS A CG    
5349 C CD    . LYS B 645 ? 1.71859 1.78299 1.99826 -0.10330 -0.06390 0.17523  645 LYS A CD    
5350 C CE    . LYS B 645 ? 1.49405 1.55457 1.75950 -0.10196 -0.05699 0.17544  645 LYS A CE    
5351 N NZ    . LYS B 645 ? 1.50717 1.56223 1.77808 -0.09267 -0.03753 0.17230  645 LYS A NZ    
5352 N N     . SER B 646 ? 1.04091 1.11017 1.28707 -0.11745 -0.08840 0.14402  646 SER A N     
5353 C CA    . SER B 646 ? 1.28140 1.35167 1.53215 -0.12133 -0.09772 0.14002  646 SER A CA    
5354 C C     . SER B 646 ? 1.38609 1.45360 1.61132 -0.12084 -0.09103 0.12391  646 SER A C     
5355 O O     . SER B 646 ? 1.58975 1.65593 1.79161 -0.12806 -0.10019 0.11632  646 SER A O     
5356 C CB    . SER B 646 ? 1.38216 1.45364 1.62784 -0.13163 -0.11752 0.14477  646 SER A CB    
5357 O OG    . SER B 646 ? 1.32228 1.39283 1.56253 -0.13699 -0.12715 0.13765  646 SER A OG    
5358 N N     . LEU B 647 ? 1.25948 1.32596 1.48992 -0.11286 -0.07583 0.11933  647 LEU A N     
5359 C CA    . LEU B 647 ? 1.22266 1.28690 1.43187 -0.11198 -0.06922 0.10492  647 LEU A CA    
5360 C C     . LEU B 647 ? 1.24898 1.31343 1.46492 -0.11557 -0.07823 0.10058  647 LEU A C     
5361 O O     . LEU B 647 ? 1.23686 1.30337 1.48094 -0.11423 -0.08181 0.10881  647 LEU A O     
5362 C CB    . LEU B 647 ? 1.02454 1.08776 1.24204 -0.10282 -0.05188 0.10400  647 LEU A CB    
5363 C CG    . LEU B 647 ? 1.12673 1.18753 1.32213 -0.10024 -0.04111 0.09939  647 LEU A CG    
5364 C CD1   . LEU B 647 ? 1.30775 1.36663 1.51003 -0.09218 -0.02519 0.09811  647 LEU A CD1   
5365 C CD2   . LEU B 647 ? 1.05218 1.11199 1.21693 -0.10503 -0.04384 0.08730  647 LEU A CD2   
5366 N N     . ILE B 648 ? 1.16238 1.22449 1.35452 -0.11959 -0.08074 0.08797  648 ILE A N     
5367 C CA    . ILE B 648 ? 1.18935 1.25038 1.38776 -0.12289 -0.08874 0.08264  648 ILE A CA    
5368 C C     . ILE B 648 ? 1.17148 1.22999 1.35337 -0.12057 -0.07979 0.06856  648 ILE A C     
5369 O O     . ILE B 648 ? 1.20119 1.25733 1.35609 -0.12486 -0.08137 0.05903  648 ILE A O     
5370 C CB    . ILE B 648 ? 1.26964 1.32903 1.45586 -0.13320 -0.10624 0.08171  648 ILE A CB    
5371 C CG1   . ILE B 648 ? 1.18440 1.24669 1.39298 -0.13637 -0.11813 0.09685  648 ILE A CG1   
5372 C CG2   . ILE B 648 ? 1.15006 1.20621 1.33373 -0.13664 -0.11191 0.07174  648 ILE A CG2   
5373 C CD1   . ILE B 648 ? 1.09595 1.15617 1.29299 -0.14739 -0.13687 0.09669  648 ILE A CD1   
5374 N N     . PHE B 649 ? 1.02089 1.08004 1.21985 -0.11415 -0.07082 0.06808  649 PHE A N     
5375 C CA    . PHE B 649 ? 1.03840 1.09564 1.22648 -0.11139 -0.06226 0.05633  649 PHE A CA    
5376 C C     . PHE B 649 ? 1.01677 1.07133 1.20435 -0.11625 -0.07145 0.04820  649 PHE A C     
5377 O O     . PHE B 649 ? 1.11663 1.17179 1.32780 -0.11580 -0.07600 0.05250  649 PHE A O     
5378 C CB    . PHE B 649 ? 1.05365 1.11240 1.25999 -0.10298 -0.04925 0.06006  649 PHE A CB    
5379 C CG    . PHE B 649 ? 0.90129 0.96071 1.10299 -0.09796 -0.03784 0.06480  649 PHE A CG    
5380 C CD1   . PHE B 649 ? 1.07604 1.13409 1.25351 -0.09711 -0.03026 0.05720  649 PHE A CD1   
5381 C CD2   . PHE B 649 ? 0.91782 0.97882 1.14023 -0.09405 -0.03421 0.07667  649 PHE A CD2   
5382 C CE1   . PHE B 649 ? 1.02963 1.08735 1.20215 -0.09303 -0.02038 0.06114  649 PHE A CE1   
5383 C CE2   . PHE B 649 ? 1.06424 1.12439 1.28137 -0.08958 -0.02326 0.08007  649 PHE A CE2   
5384 C CZ    . PHE B 649 ? 1.00714 1.06539 1.19867 -0.08931 -0.01682 0.07217  649 PHE A CZ    
5385 N N     . ILE B 650 ? 0.89208 0.94335 1.05345 -0.12058 -0.07311 0.03620  650 ILE A N     
5386 C CA    . ILE B 650 ? 0.93136 0.97837 1.08932 -0.12545 -0.08097 0.02639  650 ILE A CA    
5387 C C     . ILE B 650 ? 0.92885 0.97400 1.07670 -0.12174 -0.07009 0.01419  650 ILE A C     
5388 O O     . ILE B 650 ? 1.23369 1.27860 1.35900 -0.12154 -0.06339 0.00808  650 ILE A O     
5389 C CB    . ILE B 650 ? 0.98509 1.02851 1.12087 -0.13501 -0.09364 0.02235  650 ILE A CB    
5390 C CG1   . ILE B 650 ? 1.17080 1.21696 1.31407 -0.13850 -0.10340 0.03572  650 ILE A CG1   
5391 C CG2   . ILE B 650 ? 1.00905 1.04678 1.14371 -0.14067 -0.10316 0.01336  650 ILE A CG2   
5392 C CD1   . ILE B 650 ? 1.31855 1.36175 1.43564 -0.14791 -0.11448 0.03320  650 ILE A CD1   
5393 N N     . SER B 651 ? 0.92555 0.96969 1.09089 -0.11904 -0.06866 0.01148  651 SER A N     
5394 C CA    . SER B 651 ? 0.98352 1.02584 1.14240 -0.11574 -0.05932 0.00037  651 SER A CA    
5395 C C     . SER B 651 ? 0.98089 1.02012 1.15740 -0.11630 -0.06393 -0.00369 651 SER A C     
5396 O O     . SER B 651 ? 1.11488 1.15555 1.31484 -0.11615 -0.06993 0.00524  651 SER A O     
5397 C CB    . SER B 651 ? 1.15770 1.20404 1.32148 -0.10803 -0.04563 0.00440  651 SER A CB    
5398 O OG    . SER B 651 ? 1.05667 1.10185 1.22132 -0.10479 -0.03823 -0.00395 651 SER A OG    
5399 N N     . GLY B 652 ? 0.94901 0.98414 1.11600 -0.11678 -0.06085 -0.01642 652 GLY A N     
5400 C CA    . GLY B 652 ? 0.93027 0.96161 1.11402 -0.11722 -0.06474 -0.02122 652 GLY A CA    
5401 C C     . GLY B 652 ? 0.92430 0.95997 1.13497 -0.11013 -0.05783 -0.01319 652 GLY A C     
5402 O O     . GLY B 652 ? 1.06986 1.10416 1.30207 -0.11062 -0.06349 -0.01100 652 GLY A O     
5403 N N     . THR B 653 ? 1.11793 1.15823 1.32679 -0.10420 -0.04620 -0.00887 653 THR A N     
5404 C CA    . THR B 653 ? 0.94617 0.99015 1.17733 -0.09772 -0.03856 -0.00119 653 THR A CA    
5405 C C     . THR B 653 ? 0.97848 1.02720 1.21290 -0.09429 -0.03342 0.01092  653 THR A C     
5406 O O     . THR B 653 ? 0.99898 1.04896 1.21550 -0.09281 -0.02661 0.01006  653 THR A O     
5407 C CB    . THR B 653 ? 0.89417 0.93780 1.12046 -0.09399 -0.02887 -0.00872 653 THR A CB    
5408 O OG1   . THR B 653 ? 1.28906 1.33589 1.50059 -0.09120 -0.02028 -0.00590 653 THR A OG1   
5409 C CG2   . THR B 653 ? 0.96555 1.00386 1.17782 -0.09776 -0.03160 -0.02319 653 THR A CG2   
5410 N N     . LEU B 654 ? 1.09271 1.14372 1.34996 -0.09308 -0.03623 0.02188  654 LEU A N     
5411 C CA    . LEU B 654 ? 0.86158 0.91633 1.12404 -0.08961 -0.03064 0.03362  654 LEU A CA    
5412 C C     . LEU B 654 ? 1.03530 1.09268 1.32600 -0.08532 -0.02678 0.04386  654 LEU A C     
5413 O O     . LEU B 654 ? 1.05931 1.11922 1.35767 -0.08223 -0.02152 0.05395  654 LEU A O     
5414 C CB    . LEU B 654 ? 0.87571 0.93069 1.13438 -0.09412 -0.03991 0.03805  654 LEU A CB    
5415 C CG    . LEU B 654 ? 0.89164 0.94503 1.12126 -0.09772 -0.04147 0.03154  654 LEU A CG    
5416 C CD1   . LEU B 654 ? 1.13477 1.18869 1.36457 -0.10252 -0.05193 0.03804  654 LEU A CD1   
5417 C CD2   . LEU B 654 ? 0.99716 1.05203 1.21366 -0.09300 -0.02891 0.03226  654 LEU A CD2   
5418 N N     . LYS B 655 ? 1.22659 1.28319 1.53226 -0.08489 -0.02820 0.04152  655 LYS A N     
5419 C CA    . LYS B 655 ? 0.93015 0.98964 1.26407 -0.08137 -0.02510 0.05248  655 LYS A CA    
5420 C C     . LYS B 655 ? 0.97255 1.03211 1.31494 -0.07775 -0.01787 0.05107  655 LYS A C     
5421 O O     . LYS B 655 ? 0.93929 0.99609 1.27933 -0.07978 -0.02199 0.04173  655 LYS A O     
5422 C CB    . LYS B 655 ? 0.91041 0.96991 1.26530 -0.08549 -0.03770 0.05637  655 LYS A CB    
5423 C CG    . LYS B 655 ? 1.36494 1.42001 1.71810 -0.09053 -0.04812 0.04574  655 LYS A CG    
5424 C CD    . LYS B 655 ? 1.59465 1.64989 1.97609 -0.09302 -0.05778 0.05139  655 LYS A CD    
5425 C CE    . LYS B 655 ? 1.36082 1.41861 1.75375 -0.09574 -0.06573 0.06145  655 LYS A CE    
5426 N NZ    . LYS B 655 ? 1.42192 1.48054 1.84473 -0.09797 -0.07470 0.06816  655 LYS A NZ    
5427 N N     . PHE B 656 ? 1.04566 1.10780 1.39696 -0.07275 -0.00726 0.06000  656 PHE A N     
5428 C CA    . PHE B 656 ? 0.92640 0.98908 1.28885 -0.06968 -0.00107 0.06135  656 PHE A CA    
5429 C C     . PHE B 656 ? 1.01543 1.08041 1.40807 -0.06937 -0.00427 0.07117  656 PHE A C     
5430 O O     . PHE B 656 ? 0.98561 1.05191 1.38639 -0.07081 -0.00908 0.07679  656 PHE A O     
5431 C CB    . PHE B 656 ? 0.84410 0.90729 1.19207 -0.06562 0.01175  0.06434  656 PHE A CB    
5432 C CG    . PHE B 656 ? 0.91001 0.97395 1.26586 -0.06236 0.01994  0.06837  656 PHE A CG    
5433 C CD1   . PHE B 656 ? 0.97203 1.03483 1.32043 -0.06254 0.02047  0.06107  656 PHE A CD1   
5434 C CD2   . PHE B 656 ? 0.90924 0.97494 1.27943 -0.05923 0.02757  0.07987  656 PHE A CD2   
5435 C CE1   . PHE B 656 ? 1.02980 1.09344 1.38544 -0.06008 0.02703  0.06581  656 PHE A CE1   
5436 C CE2   . PHE B 656 ? 0.94022 1.00635 1.31545 -0.05691 0.03481  0.08406  656 PHE A CE2   
5437 C CZ    . PHE B 656 ? 0.96182 1.02701 1.32973 -0.05753 0.03393  0.07734  656 PHE A CZ    
5438 N N     . ASN B 657 ? 1.03723 1.10299 1.44757 -0.06779 -0.00226 0.07408  657 ASN A N     
5439 C CA    . ASN B 657 ? 0.97611 1.04436 1.41647 -0.06813 -0.00649 0.08376  657 ASN A CA    
5440 C C     . ASN B 657 ? 1.15234 1.21924 1.59715 -0.07337 -0.02064 0.08037  657 ASN A C     
5441 O O     . ASN B 657 ? 1.28464 1.34766 1.72004 -0.07714 -0.02887 0.06931  657 ASN A O     
5442 C CB    . ASN B 657 ? 1.08250 1.15422 1.53298 -0.06416 0.00347  0.09674  657 ASN A CB    
5443 C CG    . ASN B 657 ? 1.17926 1.25330 1.65217 -0.06151 0.00930  0.10534  657 ASN A CG    
5444 O OD1   . ASN B 657 ? 0.94463 1.01792 1.42691 -0.06281 0.00474  0.10207  657 ASN A OD1   
5445 N ND2   . ASN B 657 ? 1.71606 1.79264 2.19821 -0.05790 0.01963  0.11651  657 ASN A ND2   
5446 N N     . HIS B 658 ? 0.96618 1.03589 1.42554 -0.07380 -0.02336 0.08988  658 HIS A N     
5447 C CA    . HIS B 658 ? 1.02216 1.09038 1.48468 -0.07975 -0.03842 0.08729  658 HIS A CA    
5448 C C     . HIS B 658 ? 1.03074 1.10095 1.48703 -0.07985 -0.03821 0.09302  658 HIS A C     
5449 O O     . HIS B 658 ? 1.22043 1.29051 1.68292 -0.08468 -0.05050 0.09460  658 HIS A O     
5450 C CB    . HIS B 658 ? 1.07818 1.14739 1.57195 -0.08215 -0.04739 0.09294  658 HIS A CB    
5451 C CG    . HIS B 658 ? 1.19247 1.25798 1.68888 -0.08359 -0.05087 0.08446  658 HIS A CG    
5452 N ND1   . HIS B 658 ? 1.42839 1.48789 1.91089 -0.08894 -0.06157 0.07139  658 HIS A ND1   
5453 C CD2   . HIS B 658 ? 0.95001 1.01648 1.46051 -0.08037 -0.04452 0.08694  658 HIS A CD2   
5454 C CE1   . HIS B 658 ? 1.23008 1.28682 1.71972 -0.08865 -0.06153 0.06598  658 HIS A CE1   
5455 N NE2   . HIS B 658 ? 1.14916 1.21043 1.65649 -0.08351 -0.05165 0.07577  658 HIS A NE2   
5456 N N     . SER B 659 ? 0.85516 0.92667 1.29962 -0.07500 -0.02513 0.09611  659 SER A N     
5457 C CA    . SER B 659 ? 1.00068 1.07356 1.43987 -0.07472 -0.02418 0.10157  659 SER A CA    
5458 C C     . SER B 659 ? 1.03517 1.10519 1.44079 -0.07444 -0.01940 0.09272  659 SER A C     
5459 O O     . SER B 659 ? 1.19923 1.26686 1.58847 -0.07400 -0.01598 0.08352  659 SER A O     
5460 C CB    . SER B 659 ? 1.15609 1.23258 1.61487 -0.06940 -0.01301 0.11477  659 SER A CB    
5461 O OG    . SER B 659 ? 1.17084 1.24936 1.63858 -0.07050 -0.01737 0.12232  659 SER A OG    
5462 N N     . PHE B 660 ? 0.89442 0.96490 1.29230 -0.07487 -0.01974 0.09609  660 PHE A N     
5463 C CA    . PHE B 660 ? 0.80893 0.87700 1.17631 -0.07489 -0.01564 0.08920  660 PHE A CA    
5464 C C     . PHE B 660 ? 0.99488 1.06311 1.35930 -0.06883 -0.00011 0.09495  660 PHE A C     
5465 O O     . PHE B 660 ? 1.09089 1.15726 1.43391 -0.06836 0.00416  0.09185  660 PHE A O     
5466 C CB    . PHE B 660 ? 0.81837 0.88659 1.18033 -0.07934 -0.02579 0.09071  660 PHE A CB    
5467 C CG    . PHE B 660 ? 0.82855 0.89539 1.18924 -0.08645 -0.04195 0.08497  660 PHE A CG    
5468 C CD1   . PHE B 660 ? 1.13151 1.19658 1.49635 -0.08814 -0.04605 0.07817  660 PHE A CD1   
5469 C CD2   . PHE B 660 ? 0.98481 1.05149 1.33971 -0.09177 -0.05318 0.08646  660 PHE A CD2   
5470 C CE1   . PHE B 660 ? 1.34139 1.40369 1.70327 -0.09505 -0.06063 0.07196  660 PHE A CE1   
5471 C CE2   . PHE B 660 ? 1.03298 1.09725 1.38391 -0.09910 -0.06828 0.08082  660 PHE A CE2   
5472 C CZ    . PHE B 660 ? 1.09812 1.15979 1.45205 -0.10073 -0.07175 0.07314  660 PHE A CZ    
5473 N N     . GLU B 661 ? 0.96740 1.03735 1.35259 -0.06462 0.00817  0.10327  661 GLU A N     
5474 C CA    . GLU B 661 ? 1.06181 1.13066 1.44344 -0.05918 0.02362  0.10879  661 GLU A CA    
5475 C C     . GLU B 661 ? 1.05064 1.11593 1.40302 -0.05816 0.03103  0.10015  661 GLU A C     
5476 O O     . GLU B 661 ? 1.03403 1.09685 1.37459 -0.05535 0.04102  0.10204  661 GLU A O     
5477 C CB    . GLU B 661 ? 0.99897 1.06983 1.40565 -0.05531 0.03180  0.11817  661 GLU A CB    
5478 C CG    . GLU B 661 ? 1.07826 1.15328 1.51662 -0.05649 0.02402  0.12729  661 GLU A CG    
5479 C CD    . GLU B 661 ? 1.64752 1.72495 2.11104 -0.05285 0.03245  0.13642  661 GLU A CD    
5480 O OE1   . GLU B 661 ? 1.73077 1.80621 2.18465 -0.04979 0.04387  0.13524  661 GLU A OE1   
5481 O OE2   . GLU B 661 ? 1.75104 1.83239 2.24368 -0.05341 0.02733  0.14513  661 GLU A OE2   
5482 N N     . ALA B 662 ? 1.08907 1.15381 1.43118 -0.06043 0.02639  0.09119  662 ALA A N     
5483 C CA    . ALA B 662 ? 0.97576 1.03773 1.29269 -0.05944 0.03345  0.08425  662 ALA A CA    
5484 C C     . ALA B 662 ? 0.86386 0.92413 1.15732 -0.06171 0.03064  0.07829  662 ALA A C     
5485 O O     . ALA B 662 ? 0.90121 0.95900 1.17730 -0.05993 0.03894  0.07761  662 ALA A O     
5486 C CB    . ALA B 662 ? 0.74763 0.80978 1.06298 -0.06076 0.03017  0.07704  662 ALA A CB    
5487 N N     . PHE B 663 ? 0.91281 0.97403 1.20525 -0.06604 0.01880  0.07441  663 PHE A N     
5488 C CA    . PHE B 663 ? 0.88596 0.94587 1.15592 -0.06880 0.01554  0.06933  663 PHE A CA    
5489 C C     . PHE B 663 ? 0.86328 0.92274 1.13560 -0.06677 0.02023  0.07770  663 PHE A C     
5490 O O     . PHE B 663 ? 1.00893 1.06639 1.26170 -0.06686 0.02370  0.07536  663 PHE A O     
5491 C CB    . PHE B 663 ? 0.83141 0.89186 1.09930 -0.07453 0.00159  0.06385  663 PHE A CB    
5492 C CG    . PHE B 663 ? 0.93186 0.99112 1.17552 -0.07806 -0.00217 0.05840  663 PHE A CG    
5493 C CD1   . PHE B 663 ? 0.93237 0.99022 1.15367 -0.07944 -0.00061 0.04801  663 PHE A CD1   
5494 C CD2   . PHE B 663 ? 1.09179 1.15163 1.33637 -0.08010 -0.00728 0.06431  663 PHE A CD2   
5495 C CE1   . PHE B 663 ? 0.90341 0.96048 1.10295 -0.08277 -0.00348 0.04357  663 PHE A CE1   
5496 C CE2   . PHE B 663 ? 0.97051 1.02941 1.19293 -0.08363 -0.01082 0.06003  663 PHE A CE2   
5497 C CZ    . PHE B 663 ? 0.81941 0.87693 1.01885 -0.08499 -0.00868 0.04959  663 PHE A CZ    
5498 N N     . LYS B 664 ? 0.93148 0.99268 1.22862 -0.06488 0.02066  0.08752  664 LYS A N     
5499 C CA    . LYS B 664 ? 0.92703 0.98774 1.23061 -0.06269 0.02516  0.09611  664 LYS A CA    
5500 C C     . LYS B 664 ? 0.87549 0.93251 1.17029 -0.05768 0.04084  0.09781  664 LYS A C     
5501 O O     . LYS B 664 ? 0.87891 0.93348 1.16767 -0.05630 0.04567  0.10083  664 LYS A O     
5502 C CB    . LYS B 664 ? 0.82023 0.88433 1.15592 -0.06205 0.02132  0.10636  664 LYS A CB    
5503 C CG    . LYS B 664 ? 1.21836 1.28319 1.56645 -0.06126 0.02101  0.11565  664 LYS A CG    
5504 C CD    . LYS B 664 ? 1.58457 1.65378 1.96610 -0.06183 0.01413  0.12549  664 LYS A CD    
5505 C CE    . LYS B 664 ? 1.34784 1.41920 1.73177 -0.06786 -0.00182 0.12103  664 LYS A CE    
5506 N NZ    . LYS B 664 ? 0.90674 0.98219 1.32373 -0.06886 -0.00917 0.13080  664 LYS A NZ    
5507 N N     . GLN B 665 ? 0.88079 0.93690 1.17469 -0.05541 0.04814  0.09611  665 GLN A N     
5508 C CA    . GLN B 665 ? 0.97605 1.02773 1.26069 -0.05130 0.06291  0.09812  665 GLN A CA    
5509 C C     . GLN B 665 ? 0.84210 0.88995 1.09710 -0.05254 0.06513  0.09091  665 GLN A C     
5510 O O     . GLN B 665 ? 0.96808 1.01098 1.21263 -0.04996 0.07610  0.09247  665 GLN A O     
5511 C CB    . GLN B 665 ? 0.90331 0.95511 1.19305 -0.04955 0.06866  0.09854  665 GLN A CB    
5512 C CG    . GLN B 665 ? 1.11773 1.17184 1.43610 -0.04681 0.07250  0.10820  665 GLN A CG    
5513 C CD    . GLN B 665 ? 1.56647 1.62111 1.89007 -0.04570 0.07705  0.10906  665 GLN A CD    
5514 O OE1   . GLN B 665 ? 1.32062 1.37390 1.62714 -0.04693 0.07712  0.10262  665 GLN A OE1   
5515 N NE2   . GLN B 665 ? 1.48289 1.53985 1.83157 -0.04346 0.08083  0.11777  665 GLN A NE2   
5516 N N     . LEU B 666 ? 0.85229 0.90196 1.09432 -0.05656 0.05529  0.08336  666 LEU A N     
5517 C CA    . LEU B 666 ? 0.94071 0.98758 1.15592 -0.05811 0.05672  0.07689  666 LEU A CA    
5518 C C     . LEU B 666 ? 0.93206 0.97667 1.14421 -0.05783 0.05797  0.08099  666 LEU A C     
5519 O O     . LEU B 666 ? 0.98650 1.02861 1.17795 -0.05920 0.05903  0.07684  666 LEU A O     
5520 C CB    . LEU B 666 ? 0.91050 0.96021 1.11472 -0.06242 0.04658  0.06808  666 LEU A CB    
5521 C CG    . LEU B 666 ? 1.01118 1.06279 1.21936 -0.06277 0.04487  0.06330  666 LEU A CG    
5522 C CD1   . LEU B 666 ? 0.97293 1.02665 1.17274 -0.06704 0.03491  0.05460  666 LEU A CD1   
5523 C CD2   . LEU B 666 ? 0.80387 0.85295 0.99963 -0.06081 0.05404  0.06151  666 LEU A CD2   
5524 N N     . PHE B 667 ? 0.84013 0.88583 1.07382 -0.05621 0.05757  0.08928  667 PHE A N     
5525 C CA    . PHE B 667 ? 0.80042 0.84395 1.03522 -0.05555 0.05899  0.09440  667 PHE A CA    
5526 C C     . PHE B 667 ? 0.96991 1.00893 1.21490 -0.05027 0.07283  0.10114  667 PHE A C     
5527 O O     . PHE B 667 ? 1.01347 1.05292 1.27100 -0.04768 0.07861  0.10391  667 PHE A O     
5528 C CB    . PHE B 667 ? 0.79743 0.84578 1.04747 -0.05877 0.04603  0.09833  667 PHE A CB    
5529 C CG    . PHE B 667 ? 0.88141 0.93225 1.11462 -0.06446 0.03400  0.09026  667 PHE A CG    
5530 C CD1   . PHE B 667 ? 0.81881 0.86845 1.03300 -0.06733 0.03073  0.08746  667 PHE A CD1   
5531 C CD2   . PHE B 667 ? 1.04230 1.09614 1.27826 -0.06693 0.02682  0.08523  667 PHE A CD2   
5532 C CE1   . PHE B 667 ? 0.83170 0.88333 1.02952 -0.07256 0.02107  0.07999  667 PHE A CE1   
5533 C CE2   . PHE B 667 ? 1.01876 1.07384 1.23833 -0.07201 0.01732  0.07709  667 PHE A CE2   
5534 C CZ    . PHE B 667 ? 0.80012 0.85421 1.00023 -0.07482 0.01480  0.07450  667 PHE A CZ    
5535 N N     . ASN B 668 ? 1.09137 1.12577 1.33123 -0.04880 0.07842  0.10373  668 ASN A N     
5536 C CA    . ASN B 668 ? 1.24676 1.27490 1.49239 -0.04380 0.09333  0.10868  668 ASN A CA    
5537 C C     . ASN B 668 ? 1.36685 1.39728 1.64362 -0.04094 0.09455  0.11895  668 ASN A C     
5538 O O     . ASN B 668 ? 1.59297 1.62456 1.88821 -0.03793 0.10070  0.12385  668 ASN A O     
5539 C CB    . ASN B 668 ? 1.25509 1.27569 1.47886 -0.04360 0.09969  0.10549  668 ASN A CB    
5540 C CG    . ASN B 668 ? 1.32397 1.34018 1.52081 -0.04472 0.10446  0.09759  668 ASN A CG    
5541 O OD1   . ASN B 668 ? 1.24779 1.26449 1.44436 -0.04401 0.10797  0.09632  668 ASN A OD1   
5542 N ND2   . ASN B 668 ? 1.04167 1.05371 1.21669 -0.04673 0.10417  0.09296  668 ASN A ND2   
5543 N N     . LYS B 669 ? 1.10627 1.13753 1.39000 -0.04192 0.08887  0.12294  669 LYS A N     
5544 C CA    . LYS B 669 ? 1.36056 1.39482 1.67644 -0.03956 0.08857  0.13364  669 LYS A CA    
5545 C C     . LYS B 669 ? 1.37882 1.42136 1.71511 -0.04175 0.07759  0.13681  669 LYS A C     
5546 O O     . LYS B 669 ? 1.38864 1.43554 1.71680 -0.04696 0.06348  0.13240  669 LYS A O     
5547 C CB    . LYS B 669 ? 1.47735 1.51172 1.79632 -0.04129 0.08173  0.13759  669 LYS A CB    
5548 C CG    . LYS B 669 ? 1.33668 1.36320 1.63124 -0.04083 0.08863  0.13277  669 LYS A CG    
5549 C CD    . LYS B 669 ? 1.58783 1.60547 1.88210 -0.03502 0.10753  0.13351  669 LYS A CD    
5550 C CE    . LYS B 669 ? 1.50553 1.51453 1.77651 -0.03510 0.11323  0.12890  669 LYS A CE    
5551 N NZ    . LYS B 669 ? 1.73173 1.73023 1.99605 -0.03038 0.13162  0.12742  669 LYS A NZ    
5552 N N     . ASP B 670 ? 1.16165 1.20585 1.52405 -0.03794 0.08450  0.14422  670 ASP A N     
5553 C CA    . ASP B 670 ? 1.22043 1.27218 1.60563 -0.03992 0.07437  0.14837  670 ASP A CA    
5554 C C     . ASP B 670 ? 1.36585 1.42271 1.76961 -0.04325 0.06014  0.15530  670 ASP A C     
5555 O O     . ASP B 670 ? 1.57058 1.62871 2.00102 -0.04039 0.06337  0.16568  670 ASP A O     
5556 C CB    . ASP B 670 ? 1.14027 1.19253 1.54935 -0.03491 0.08645  0.15541  670 ASP A CB    
5557 C CG    . ASP B 670 ? 1.69039 1.73836 2.08065 -0.03301 0.09778  0.14901  670 ASP A CG    
5558 O OD1   . ASP B 670 ? 1.69298 1.73657 2.05230 -0.03472 0.09841  0.13975  670 ASP A OD1   
5559 O OD2   . ASP B 670 ? 1.74624 1.79547 2.15309 -0.03012 0.10564  0.15380  670 ASP A OD2   
5560 N N     . VAL B 671 ? 1.38431 1.44390 1.77381 -0.04952 0.04442  0.14974  671 VAL A N     
5561 C CA    . VAL B 671 ? 1.27074 1.33443 1.67089 -0.05428 0.02890  0.15520  671 VAL A CA    
5562 C C     . VAL B 671 ? 1.11642 1.18586 1.53133 -0.05880 0.01468  0.15643  671 VAL A C     
5563 O O     . VAL B 671 ? 1.29098 1.36042 1.69314 -0.06057 0.01251  0.14802  671 VAL A O     
5564 C CB    . VAL B 671 ? 1.18130 1.24267 1.55091 -0.05880 0.02186  0.14789  671 VAL A CB    
5565 C CG1   . VAL B 671 ? 1.34408 1.40959 1.72235 -0.06478 0.00459  0.15372  671 VAL A CG1   
5566 C CG2   . VAL B 671 ? 1.04170 1.09683 1.39821 -0.05457 0.03546  0.14708  671 VAL A CG2   
5567 N N     . HIS B 672 ? 1.01053 1.08455 1.45324 -0.06081 0.00472  0.16714  672 HIS A N     
5568 C CA    . HIS B 672 ? 1.13706 1.21594 1.59527 -0.06579 -0.01009 0.16910  672 HIS A CA    
5569 C C     . HIS B 672 ? 1.09652 1.17485 1.52831 -0.07387 -0.02611 0.15988  672 HIS A C     
5570 O O     . HIS B 672 ? 1.07868 1.15611 1.49640 -0.07744 -0.03282 0.15977  672 HIS A O     
5571 C CB    . HIS B 672 ? 1.24638 1.33034 1.74253 -0.06623 -0.01711 0.18407  672 HIS A CB    
5572 C CG    . HIS B 672 ? 1.03921 1.12768 1.55131 -0.07248 -0.03451 0.18677  672 HIS A CG    
5573 N ND1   . HIS B 672 ? 1.37923 1.47038 1.89758 -0.07976 -0.05335 0.19217  672 HIS A ND1   
5574 C CD2   . HIS B 672 ? 1.03847 1.12864 1.56091 -0.07302 -0.03648 0.18483  672 HIS A CD2   
5575 C CE1   . HIS B 672 ? 1.44421 1.53802 1.97538 -0.08468 -0.06627 0.19300  672 HIS A CE1   
5576 N NE2   . HIS B 672 ? 1.31764 1.41097 1.85224 -0.08053 -0.05622 0.18852  672 HIS A NE2   
5577 N N     . PHE B 673 ? 1.18176 1.26026 1.60680 -0.07676 -0.03164 0.15211  673 PHE A N     
5578 C CA    . PHE B 673 ? 1.19192 1.26935 1.59446 -0.08457 -0.04650 0.14284  673 PHE A CA    
5579 C C     . PHE B 673 ? 1.12418 1.20452 1.54772 -0.08981 -0.06159 0.14662  673 PHE A C     
5580 O O     . PHE B 673 ? 1.18230 1.26587 1.63705 -0.08687 -0.05938 0.15537  673 PHE A O     
5581 C CB    . PHE B 673 ? 1.12975 1.20352 1.50333 -0.08380 -0.03979 0.12845  673 PHE A CB    
5582 C CG    . PHE B 673 ? 1.12648 1.19694 1.47309 -0.08134 -0.02966 0.12289  673 PHE A CG    
5583 C CD1   . PHE B 673 ? 1.02291 1.09176 1.34295 -0.08663 -0.03727 0.11654  673 PHE A CD1   
5584 C CD2   . PHE B 673 ? 1.16156 1.23013 1.50864 -0.07416 -0.01259 0.12403  673 PHE A CD2   
5585 C CE1   . PHE B 673 ? 1.04964 1.11567 1.34627 -0.08459 -0.02829 0.11194  673 PHE A CE1   
5586 C CE2   . PHE B 673 ? 1.08503 1.14998 1.40747 -0.07243 -0.00410 0.11896  673 PHE A CE2   
5587 C CZ    . PHE B 673 ? 1.11916 1.18316 1.41736 -0.07754 -0.01208 0.11312  673 PHE A CZ    
5588 N N     . ASN B 674 ? 0.98404 1.06277 1.38951 -0.09793 -0.07689 0.13979  674 ASN A N     
5589 C CA    . ASN B 674 ? 1.09140 1.17096 1.51006 -0.10429 -0.09263 0.14050  674 ASN A CA    
5590 C C     . ASN B 674 ? 1.11694 1.19228 1.51299 -0.10663 -0.09356 0.12534  674 ASN A C     
5591 O O     . ASN B 674 ? 1.41407 1.48578 1.77769 -0.10924 -0.09365 0.11445  674 ASN A O     
5592 C CB    . ASN B 674 ? 1.17128 1.25131 1.58799 -0.11301 -0.11127 0.14552  674 ASN A CB    
5593 C CG    . ASN B 674 ? 1.12816 1.21280 1.57189 -0.11097 -0.11178 0.16182  674 ASN A CG    
5594 O OD1   . ASN B 674 ? 1.11063 1.19559 1.54750 -0.11594 -0.12164 0.16642  674 ASN A OD1   
5595 N ND2   . ASN B 674 ? 1.15351 1.24166 1.62856 -0.10360 -0.10061 0.17092  674 ASN A ND2   
5596 N N     . THR B 675 ? 0.87436 0.95028 1.28914 -0.10549 -0.09367 0.12510  675 THR A N     
5597 C CA    . THR B 675 ? 0.91582 0.98756 1.31341 -0.10700 -0.09363 0.11114  675 THR A CA    
5598 C C     . THR B 675 ? 1.01020 1.07929 1.40884 -0.11594 -0.11228 0.10770  675 THR A C     
5599 O O     . THR B 675 ? 1.16167 1.23356 1.58921 -0.11824 -0.12165 0.11803  675 THR A O     
5600 C CB    . THR B 675 ? 1.20417 1.27752 1.61998 -0.09989 -0.08081 0.11260  675 THR A CB    
5601 O OG1   . THR B 675 ? 1.32864 1.39779 1.72707 -0.10142 -0.08100 0.09905  675 THR A OG1   
5602 C CG2   . THR B 675 ? 1.01703 1.09433 1.47119 -0.09977 -0.08599 0.12448  675 THR A CG2   
5603 N N     . PHE B 676 ? 1.02937 1.09285 1.39769 -0.12099 -0.11723 0.09364  676 PHE A N     
5604 C CA    . PHE B 676 ? 0.95705 1.01583 1.32136 -0.13020 -0.13459 0.08784  676 PHE A CA    
5605 C C     . PHE B 676 ? 1.06639 1.11930 1.41073 -0.13037 -0.13050 0.07146  676 PHE A C     
5606 O O     . PHE B 676 ? 1.17762 1.22991 1.50157 -0.12582 -0.11765 0.06385  676 PHE A O     
5607 C CB    . PHE B 676 ? 0.98524 1.04178 1.32890 -0.13873 -0.14810 0.08769  676 PHE A CB    
5608 C CG    . PHE B 676 ? 0.99392 1.05612 1.35250 -0.13839 -0.15109 0.10325  676 PHE A CG    
5609 C CD1   . PHE B 676 ? 1.09313 1.15842 1.48114 -0.14231 -0.16434 0.11628  676 PHE A CD1   
5610 C CD2   . PHE B 676 ? 1.10960 1.17382 1.45386 -0.13438 -0.14104 0.10506  676 PHE A CD2   
5611 C CE1   . PHE B 676 ? 1.00818 1.07877 1.41222 -0.14177 -0.16686 0.13096  676 PHE A CE1   
5612 C CE2   . PHE B 676 ? 0.98334 1.05216 1.34267 -0.13392 -0.14357 0.11919  676 PHE A CE2   
5613 C CZ    . PHE B 676 ? 0.99416 1.06628 1.38383 -0.13745 -0.15626 0.13220  676 PHE A CZ    
5614 N N     . GLU B 677 ? 1.19158 1.23994 1.54199 -0.13573 -0.14140 0.06616  677 GLU A N     
5615 C CA    . GLU B 677 ? 1.13511 1.17734 1.47008 -0.13560 -0.13723 0.05053  677 GLU A CA    
5616 C C     . GLU B 677 ? 1.14411 1.17789 1.46303 -0.14591 -0.15323 0.04047  677 GLU A C     
5617 O O     . GLU B 677 ? 1.75330 1.78512 2.09258 -0.15020 -0.16495 0.04365  677 GLU A O     
5618 C CB    . GLU B 677 ? 1.09864 1.14277 1.46149 -0.12985 -0.13058 0.05306  677 GLU A CB    
5619 C CG    . GLU B 677 ? 1.39325 1.43137 1.74355 -0.12912 -0.12575 0.03794  677 GLU A CG    
5620 C CD    . GLU B 677 ? 1.65566 1.69471 2.03456 -0.12521 -0.12258 0.04054  677 GLU A CD    
5621 O OE1   . GLU B 677 ? 1.56770 1.60595 1.96890 -0.12932 -0.13423 0.04582  677 GLU A OE1   
5622 O OE2   . GLU B 677 ? 1.63052 1.67116 2.00976 -0.11843 -0.10897 0.03782  677 GLU A OE2   
5623 N N     . VAL B 678 ? 1.35933 1.38785 1.64290 -0.14998 -0.15346 0.02864  678 VAL A N     
5624 C CA    . VAL B 678 ? 1.41012 1.42876 1.67416 -0.16001 -0.16707 0.01678  678 VAL A CA    
5625 C C     . VAL B 678 ? 1.59475 1.60729 1.85035 -0.15727 -0.15828 0.00115  678 VAL A C     
5626 O O     . VAL B 678 ? 1.45161 1.46190 1.68041 -0.15566 -0.14862 -0.00959 678 VAL A O     
5627 C CB    . VAL B 678 ? 1.14335 1.15915 1.37417 -0.16721 -0.17356 0.01363  678 VAL A CB    
5628 C CG1   . VAL B 678 ? 1.39541 1.41346 1.60190 -0.16191 -0.15821 0.00797  678 VAL A CG1   
5629 C CG2   . VAL B 678 ? 1.57115 1.57595 1.77985 -0.17842 -0.18793 0.00205  678 VAL A CG2   
5630 N N     . ASN B 679 ? 1.69263 1.70295 1.97227 -0.15656 -0.16126 0.00063  679 ASN A N     
5631 C CA    . ASN B 679 ? 1.74445 1.74968 2.02206 -0.15288 -0.15214 -0.01256 679 ASN A CA    
5632 C C     . ASN B 679 ? 1.84939 1.84341 2.09398 -0.15968 -0.15562 -0.03063 679 ASN A C     
5633 O O     . ASN B 679 ? 1.94639 1.93890 2.17481 -0.15538 -0.14277 -0.04120 679 ASN A O     
5634 C CB    . ASN B 679 ? 1.67789 1.68269 1.98921 -0.15156 -0.15610 -0.00852 679 ASN A CB    
5635 C CG    . ASN B 679 ? 1.97126 1.97050 2.29077 -0.16123 -0.17557 -0.00644 679 ASN A CG    
5636 O OD1   . ASN B 679 ? 2.00694 2.01032 2.33251 -0.16504 -0.18529 0.00532  679 ASN A OD1   
5637 N ND2   . ASN B 679 ? 1.99361 1.98318 2.31413 -0.16551 -0.18183 -0.01748 679 ASN A ND2   
5638 N N     . THR B 680 ? 1.81790 1.80393 2.05388 -0.16994 -0.17208 -0.03414 680 THR A N     
5639 C CA    . THR B 680 ? 1.86577 1.83956 2.06772 -0.17739 -0.17556 -0.05195 680 THR A CA    
5640 C C     . THR B 680 ? 1.86902 1.83673 2.07296 -0.17299 -0.16524 -0.06601 680 THR A C     
5641 O O     . THR B 680 ? 1.86403 1.82281 2.03927 -0.17614 -0.16158 -0.08196 680 THR A O     
5642 C CB    . THR B 680 ? 1.96931 1.94500 2.13818 -0.17822 -0.16963 -0.05458 680 THR A CB    
5643 O OG1   . THR B 680 ? 1.97864 1.96354 2.15774 -0.17826 -0.17507 -0.03756 680 THR A OG1   
5644 C CG2   . THR B 680 ? 1.85106 1.81494 1.98308 -0.18875 -0.17776 -0.06827 680 THR A CG2   
5645 N N     . SER B 681 ? 1.87599 1.84808 2.11293 -0.16609 -0.16040 -0.06028 681 SER A N     
5646 C CA    . SER B 681 ? 2.02090 1.98828 2.26333 -0.16104 -0.14984 -0.07207 681 SER A CA    
5647 C C     . SER B 681 ? 1.98641 1.93872 2.21738 -0.16928 -0.15930 -0.08766 681 SER A C     
5648 O O     . SER B 681 ? 1.86519 1.81004 2.07731 -0.16856 -0.15060 -0.10341 681 SER A O     
5649 C CB    . SER B 681 ? 1.91529 1.89013 2.19564 -0.15330 -0.14489 -0.06127 681 SER A CB    
5650 O OG    . SER B 681 ? 1.81388 1.80123 2.10232 -0.14616 -0.13575 -0.04764 681 SER A OG    
5651 N N     . LEU B 682 ? 2.01488 1.96263 2.25769 -0.17682 -0.17619 -0.08336 682 LEU A N     
5652 C CA    . LEU B 682 ? 1.97964 1.91139 2.20951 -0.18616 -0.18722 -0.09823 682 LEU A CA    
5653 C C     . LEU B 682 ? 1.93628 1.86097 2.17648 -0.18144 -0.17776 -0.11100 682 LEU A C     
5654 O O     . LEU B 682 ? 1.84931 1.78166 2.12144 -0.17324 -0.17090 -0.10278 682 LEU A O     
5655 C CB    . LEU B 682 ? 2.01699 1.94057 2.20288 -0.19408 -0.18993 -0.10970 682 LEU A CB    
5656 C CG    . LEU B 682 ? 1.95174 1.86988 2.12483 -0.20650 -0.21039 -0.10576 682 LEU A CG    
5657 C CD1   . LEU B 682 ? 2.01352 1.92689 2.14257 -0.21287 -0.21034 -0.11385 682 LEU A CD1   
5658 C CD2   . LEU B 682 ? 1.86751 1.77181 2.04722 -0.21483 -0.22470 -0.11378 682 LEU A CD2   
5659 N N     . GLN B 683 ? 1.92320 1.83357 2.13721 -0.18650 -0.17704 -0.13019 683 GLN A N     
5660 C CA    . GLN B 683 ? 1.85790 1.75954 2.08207 -0.18281 -0.16893 -0.14368 683 GLN A CA    
5661 C C     . GLN B 683 ? 1.90499 1.81644 2.13928 -0.17070 -0.14920 -0.14227 683 GLN A C     
5662 O O     . GLN B 683 ? 1.97003 1.88064 2.22996 -0.16514 -0.14361 -0.14393 683 GLN A O     
5663 C CB    . GLN B 683 ? 1.95978 1.84403 2.14861 -0.19074 -0.17028 -0.16492 683 GLN A CB    
5664 C CG    . GLN B 683 ? 2.10827 1.98116 2.28259 -0.20405 -0.19065 -0.16737 683 GLN A CG    
5665 C CD    . GLN B 683 ? 2.16047 2.01873 2.28939 -0.21268 -0.19117 -0.18553 683 GLN A CD    
5666 O OE1   . GLN B 683 ? 2.10626 1.95270 2.22270 -0.21195 -0.18161 -0.20363 683 GLN A OE1   
5667 N NE2   . GLN B 683 ? 2.19497 2.05382 2.29884 -0.22101 -0.20193 -0.18056 683 GLN A NE2   
5668 N N     . SER B 684 ? 1.80656 1.72660 2.02182 -0.16720 -0.13972 -0.13910 684 SER A N     
5669 C CA    . SER B 684 ? 1.76805 1.69677 1.99007 -0.15653 -0.12148 -0.13831 684 SER A CA    
5670 C C     . SER B 684 ? 1.80012 1.73518 2.06237 -0.14926 -0.11866 -0.12854 684 SER A C     
5671 O O     . SER B 684 ? 1.82300 1.75463 2.09588 -0.14441 -0.10946 -0.13663 684 SER A O     
5672 C CB    . SER B 684 ? 1.78066 1.72145 1.98938 -0.15346 -0.11567 -0.12815 684 SER A CB    
5673 O OG    . SER B 684 ? 1.96877 1.90429 2.14184 -0.16109 -0.12033 -0.13482 684 SER A OG    
5674 N N     . ALA B 685 ? 1.83773 1.78159 2.12201 -0.14870 -0.12613 -0.11152 685 ALA A N     
5675 C CA    . ALA B 685 ? 1.72118 1.67210 2.04334 -0.14197 -0.12310 -0.10027 685 ALA A CA    
5676 C C     . ALA B 685 ? 1.64872 1.58956 1.98630 -0.14171 -0.12273 -0.11129 685 ALA A C     
5677 O O     . ALA B 685 ? 1.66812 1.61396 2.02799 -0.13419 -0.11333 -0.10743 685 ALA A O     
5678 C CB    . ALA B 685 ? 1.71564 1.67221 2.05840 -0.14477 -0.13526 -0.08432 685 ALA A CB    
5679 N N     . LYS B 686 ? 1.58191 1.50851 1.90808 -0.14991 -0.13281 -0.12440 686 LYS A N     
5680 C CA    . LYS B 686 ? 1.55010 1.46583 1.89375 -0.15010 -0.13362 -0.13469 686 LYS A CA    
5681 C C     . LYS B 686 ? 1.57122 1.47687 1.89269 -0.14917 -0.12275 -0.15432 686 LYS A C     
5682 O O     . LYS B 686 ? 1.71963 1.62185 2.05960 -0.14427 -0.11535 -0.15998 686 LYS A O     
5683 C CB    . LYS B 686 ? 1.69171 1.59710 2.04111 -0.15974 -0.15192 -0.13634 686 LYS A CB    
5684 C CG    . LYS B 686 ? 1.89824 1.81412 2.27665 -0.15978 -0.16160 -0.11615 686 LYS A CG    
5685 C CD    . LYS B 686 ? 1.79177 1.71822 2.20567 -0.15021 -0.15230 -0.10422 686 LYS A CD    
5686 C CE    . LYS B 686 ? 1.67163 1.61073 2.11056 -0.14877 -0.15760 -0.08326 686 LYS A CE    
5687 N NZ    . LYS B 686 ? 1.49727 1.44673 1.91887 -0.14730 -0.15409 -0.07442 686 LYS A NZ    
5688 N N     . ASN B 687 ? 1.50343 1.40461 1.78795 -0.15370 -0.12158 -0.16386 687 ASN A N     
5689 C CA    . ASN B 687 ? 1.70708 1.59969 1.97048 -0.15215 -0.10897 -0.18207 687 ASN A CA    
5690 C C     . ASN B 687 ? 1.54806 1.45159 1.82949 -0.14096 -0.09277 -0.17701 687 ASN A C     
5691 O O     . ASN B 687 ? 1.37115 1.26795 1.65599 -0.13756 -0.08291 -0.18932 687 ASN A O     
5692 C CB    . ASN B 687 ? 1.82772 1.71712 2.04901 -0.15778 -0.10837 -0.18980 687 ASN A CB    
5693 C CG    . ASN B 687 ? 1.95199 1.82268 2.14784 -0.16466 -0.10876 -0.21149 687 ASN A CG    
5694 O OD1   . ASN B 687 ? 1.99673 1.85646 2.20739 -0.16467 -0.10875 -0.22150 687 ASN A OD1   
5695 N ND2   . ASN B 687 ? 1.98141 1.84770 2.13880 -0.17067 -0.10875 -0.21907 687 ASN A ND2   
5696 N N     . THR B 688 ? 1.44518 1.36444 1.73835 -0.13569 -0.09033 -0.15940 688 THR A N     
5697 C CA    . THR B 688 ? 1.33389 1.26387 1.64141 -0.12588 -0.07588 -0.15333 688 THR A CA    
5698 C C     . THR B 688 ? 1.29665 1.22925 1.64292 -0.12119 -0.07642 -0.14531 688 THR A C     
5699 O O     . THR B 688 ? 1.49264 1.42289 1.85570 -0.12497 -0.08841 -0.13943 688 THR A O     
5700 C CB    . THR B 688 ? 1.37531 1.31975 1.67437 -0.12273 -0.07225 -0.13899 688 THR A CB    
5701 O OG1   . THR B 688 ? 1.64785 1.59833 1.96207 -0.12453 -0.08287 -0.12373 688 THR A OG1   
5702 C CG2   . THR B 688 ? 1.55185 1.49387 1.81318 -0.12793 -0.07278 -0.14579 688 THR A CG2   
5703 N N     . SER B 689 ? 1.20697 1.14459 1.56783 -0.11351 -0.06429 -0.14425 689 SER A N     
5704 C CA    . SER B 689 ? 1.00073 0.94196 1.39910 -0.10868 -0.06396 -0.13505 689 SER A CA    
5705 C C     . SER B 689 ? 1.03574 0.99020 1.44325 -0.10053 -0.05218 -0.12398 689 SER A C     
5706 O O     . SER B 689 ? 1.03977 0.99719 1.42624 -0.09847 -0.04308 -0.12853 689 SER A O     
5707 C CB    . SER B 689 ? 1.01338 0.94181 1.42491 -0.10926 -0.06359 -0.14885 689 SER A CB    
5708 O OG    . SER B 689 ? 1.06578 0.98056 1.46529 -0.11757 -0.07467 -0.16019 689 SER A OG    
5709 N N     . VAL B 690 ? 0.90465 0.86654 1.34166 -0.09654 -0.05261 -0.10969 690 VAL A N     
5710 C CA    . VAL B 690 ? 0.83612 0.81033 1.28070 -0.08963 -0.04252 -0.09776 690 VAL A CA    
5711 C C     . VAL B 690 ? 0.85259 0.82660 1.32858 -0.08519 -0.03897 -0.09524 690 VAL A C     
5712 O O     . VAL B 690 ? 0.96973 0.93891 1.46840 -0.08702 -0.04649 -0.09365 690 VAL A O     
5713 C CB    . VAL B 690 ? 0.84461 0.82978 1.29127 -0.08896 -0.04514 -0.08003 690 VAL A CB    
5714 C CG1   . VAL B 690 ? 0.77304 0.76925 1.22809 -0.08261 -0.03564 -0.06764 690 VAL A CG1   
5715 C CG2   . VAL B 690 ? 0.91094 0.89695 1.32816 -0.09293 -0.04826 -0.08149 690 VAL A CG2   
5716 N N     . PHE B 691 ? 0.98267 0.96178 1.46076 -0.07990 -0.02850 -0.09436 691 PHE A N     
5717 C CA    . PHE B 691 ? 0.80261 0.78267 1.31172 -0.07556 -0.02511 -0.09013 691 PHE A CA    
5718 C C     . PHE B 691 ? 0.83532 0.82829 1.34951 -0.07077 -0.01864 -0.07444 691 PHE A C     
5719 O O     . PHE B 691 ? 0.92329 0.92128 1.41672 -0.06918 -0.01178 -0.07514 691 PHE A O     
5720 C CB    . PHE B 691 ? 0.82298 0.79431 1.33377 -0.07420 -0.01905 -0.10627 691 PHE A CB    
5721 C CG    . PHE B 691 ? 0.82149 0.79138 1.36720 -0.07057 -0.01744 -0.10352 691 PHE A CG    
5722 C CD1   . PHE B 691 ? 0.93822 0.89818 1.50450 -0.07293 -0.02454 -0.10863 691 PHE A CD1   
5723 C CD2   . PHE B 691 ? 0.80548 0.78376 1.36406 -0.06520 -0.00955 -0.09529 691 PHE A CD2   
5724 C CE1   . PHE B 691 ? 0.82250 0.78108 1.42197 -0.06964 -0.02326 -0.10555 691 PHE A CE1   
5725 C CE2   . PHE B 691 ? 0.90770 0.88488 1.49929 -0.06216 -0.00877 -0.09177 691 PHE A CE2   
5726 C CZ    . PHE B 691 ? 0.79464 0.76205 1.40697 -0.06420 -0.01538 -0.09687 691 PHE A CZ    
5727 N N     . ILE B 692 ? 0.73036 0.72823 1.27076 -0.06896 -0.02094 -0.06043 692 ILE A N     
5728 C CA    . ILE B 692 ? 0.83650 0.84557 1.38151 -0.06512 -0.01532 -0.04499 692 ILE A CA    
5729 C C     . ILE B 692 ? 0.80086 0.81056 1.37389 -0.06168 -0.01239 -0.04136 692 ILE A C     
5730 O O     . ILE B 692 ? 0.80797 0.81912 1.40624 -0.06138 -0.01630 -0.03093 692 ILE A O     
5731 C CB    . ILE B 692 ? 0.72215 0.73772 1.27070 -0.06607 -0.01931 -0.02930 692 ILE A CB    
5732 C CG1   . ILE B 692 ? 0.75554 0.77026 1.27899 -0.06953 -0.02280 -0.03275 692 ILE A CG1   
5733 C CG2   . ILE B 692 ? 0.68075 0.70653 1.22924 -0.06271 -0.01288 -0.01439 692 ILE A CG2   
5734 C CD1   . ILE B 692 ? 0.99021 0.99843 1.52234 -0.07392 -0.03299 -0.03582 692 ILE A CD1   
5735 N N     . PRO B 693 ? 0.98378 0.99288 1.55451 -0.05908 -0.00550 -0.04880 693 PRO A N     
5736 C CA    . PRO B 693 ? 0.89822 0.90744 1.49786 -0.05586 -0.00308 -0.04585 693 PRO A CA    
5737 C C     . PRO B 693 ? 0.97767 0.99528 1.59761 -0.05434 -0.00447 -0.02629 693 PRO A C     
5738 O O     . PRO B 693 ? 0.81799 0.84408 1.42490 -0.05401 -0.00237 -0.01445 693 PRO A O     
5739 C CB    . PRO B 693 ? 0.82900 0.84049 1.41689 -0.05319 0.00562  -0.05222 693 PRO A CB    
5740 C CG    . PRO B 693 ? 0.80037 0.81467 1.35286 -0.05494 0.00773  -0.05525 693 PRO A CG    
5741 C CD    . PRO B 693 ? 0.92010 0.92867 1.46291 -0.05900 0.00050  -0.05974 693 PRO A CD    
5742 N N     . SER B 694 ? 1.01644 1.03099 1.66797 -0.05368 -0.00790 -0.02304 694 SER A N     
5743 C CA    . SER B 694 ? 0.95945 0.98102 1.63322 -0.05261 -0.00950 -0.00458 694 SER A CA    
5744 C C     . SER B 694 ? 0.99736 1.02245 1.68909 -0.04943 -0.00532 0.00040  694 SER A C     
5745 O O     . SER B 694 ? 1.06310 1.09449 1.77131 -0.04884 -0.00640 0.01661  694 SER A O     
5746 C CB    . SER B 694 ? 0.72408 0.74071 1.42365 -0.05442 -0.01701 -0.00174 694 SER A CB    
5747 O OG    . SER B 694 ? 0.73657 0.74364 1.45585 -0.05388 -0.01836 -0.01416 694 SER A OG    
5748 N N     . ASP B 695 ? 1.03732 1.05831 1.72668 -0.04761 -0.00062 -0.01297 695 ASP A N     
5749 C CA    . ASP B 695 ? 0.76383 0.78819 1.47349 -0.04441 0.00331  -0.00857 695 ASP A CA    
5750 C C     . ASP B 695 ? 0.90110 0.93279 1.58768 -0.04332 0.00949  -0.00670 695 ASP A C     
5751 O O     . ASP B 695 ? 1.22390 1.25766 1.92272 -0.04079 0.01363  -0.00698 695 ASP A O     
5752 C CB    . ASP B 695 ? 1.00529 1.01996 1.73606 -0.04267 0.00476  -0.02318 695 ASP A CB    
5753 C CG    . ASP B 695 ? 0.89393 0.89916 1.60330 -0.04363 0.00768  -0.04441 695 ASP A CG    
5754 O OD1   . ASP B 695 ? 1.04066 1.04773 1.71812 -0.04567 0.00830  -0.04741 695 ASP A OD1   
5755 O OD2   . ASP B 695 ? 0.83587 0.83148 1.56063 -0.04255 0.00932  -0.05764 695 ASP A OD2   
5756 N N     . VAL B 696 ? 1.00926 1.04463 1.66520 -0.04522 0.00993  -0.00458 696 VAL A N     
5757 C CA    . VAL B 696 ? 1.06083 1.10318 1.69378 -0.04465 0.01523  -0.00166 696 VAL A CA    
5758 C C     . VAL B 696 ? 1.06243 1.11330 1.69323 -0.04561 0.01350  0.01800  696 VAL A C     
5759 O O     . VAL B 696 ? 1.11298 1.16396 1.74541 -0.04726 0.00951  0.02571  696 VAL A O     
5760 C CB    . VAL B 696 ? 1.00586 1.04600 1.60459 -0.04612 0.01778  -0.01342 696 VAL A CB    
5761 C CG1   . VAL B 696 ? 0.88441 0.91615 1.48159 -0.04548 0.02089  -0.03295 696 VAL A CG1   
5762 C CG2   . VAL B 696 ? 1.20850 1.24756 1.79362 -0.04888 0.01303  -0.01048 696 VAL A CG2   
5763 N N     . ALA B 697 ? 0.98057 1.03793 1.60803 -0.04488 0.01647  0.02585  697 ALA A N     
5764 C CA    . ALA B 697 ? 0.94358 1.00795 1.56780 -0.04639 0.01488  0.04451  697 ALA A CA    
5765 C C     . ALA B 697 ? 1.02461 1.09104 1.61460 -0.04826 0.01672  0.04623  697 ALA A C     
5766 O O     . ALA B 697 ? 1.15391 1.21679 1.72522 -0.04841 0.01835  0.03371  697 ALA A O     
5767 C CB    . ALA B 697 ? 1.10296 1.17277 1.73670 -0.04568 0.01613  0.05248  697 ALA A CB    
5768 N N     . SER B 698 ? 1.00930 1.08080 1.59114 -0.04987 0.01651  0.06147  698 SER A N     
5769 C CA    . SER B 698 ? 1.11645 1.18942 1.66643 -0.05149 0.01903  0.06388  698 SER A CA    
5770 C C     . SER B 698 ? 1.16892 1.24412 1.69716 -0.05153 0.02279  0.05918  698 SER A C     
5771 O O     . SER B 698 ? 1.16856 1.24727 1.70477 -0.05152 0.02282  0.06486  698 SER A O     
5772 C CB    . SER B 698 ? 1.28562 1.36183 1.83372 -0.05334 0.01844  0.08082  698 SER A CB    
5773 O OG    . SER B 698 ? 1.31097 1.38569 1.88113 -0.05333 0.01520  0.08589  698 SER A OG    
5774 N N     . TYR B 699 ? 1.33062 1.40406 1.83360 -0.05183 0.02535  0.04997  699 TYR A N     
5775 C CA    . TYR B 699 ? 1.24627 1.32185 1.72743 -0.05212 0.02902  0.04569  699 TYR A CA    
5776 C C     . TYR B 699 ? 1.38823 1.46811 1.85908 -0.05403 0.02940  0.05997  699 TYR A C     
5777 O O     . TYR B 699 ? 1.44143 1.52123 1.90279 -0.05551 0.02926  0.06917  699 TYR A O     
5778 C CB    . TYR B 699 ? 1.30013 1.37312 1.75516 -0.05264 0.03112  0.03579  699 TYR A CB    
5779 C CG    . TYR B 699 ? 1.31429 1.38980 1.74331 -0.05361 0.03469  0.03512  699 TYR A CG    
5780 C CD1   . TYR B 699 ? 1.39258 1.46886 1.81850 -0.05283 0.03736  0.02577  699 TYR A CD1   
5781 C CD2   . TYR B 699 ? 1.41112 1.48788 1.81934 -0.05536 0.03583  0.04389  699 TYR A CD2   
5782 C CE1   . TYR B 699 ? 1.33328 1.41205 1.73684 -0.05395 0.04029  0.02570  699 TYR A CE1   
5783 C CE2   . TYR B 699 ? 1.44007 1.51840 1.82509 -0.05651 0.03866  0.04324  699 TYR A CE2   
5784 C CZ    . TYR B 699 ? 1.55621 1.63585 1.93927 -0.05591 0.04050  0.03444  699 TYR A CZ    
5785 O OH    . TYR B 699 ? 1.62790 1.70928 1.98929 -0.05726 0.04298  0.03430  699 TYR A OH    
5786 N N     . GLN B 700 ? 1.41015 1.49338 1.88280 -0.05424 0.03000  0.06189  700 GLN A N     
5787 C CA    . GLN B 700 ? 1.49494 1.58156 1.95559 -0.05698 0.02942  0.07526  700 GLN A CA    
5788 C C     . GLN B 700 ? 1.50209 1.59151 1.95279 -0.05740 0.03117  0.07151  700 GLN A C     
5789 O O     . GLN B 700 ? 1.50770 1.59881 1.97799 -0.05554 0.03126  0.06642  700 GLN A O     
5790 C CB    . GLN B 700 ? 1.38787 1.47662 1.87195 -0.05793 0.02533  0.08889  700 GLN A CB    
5791 C CG    . GLN B 700 ? 1.24176 1.33169 1.75881 -0.05562 0.02327  0.08581  700 GLN A CG    
5792 C CD    . GLN B 700 ? 1.63706 1.72873 2.17897 -0.05661 0.01866  0.09973  700 GLN A CD    
5793 O OE1   . GLN B 700 ? 1.64274 1.73253 2.19089 -0.05688 0.01730  0.10457  700 GLN A OE1   
5794 N NE2   . GLN B 700 ? 1.65693 1.75256 2.21435 -0.05736 0.01599  0.10711  700 GLN A NE2   
5795 N N     . TYR B 701 ? 1.39633 1.48600 1.81880 -0.05973 0.03283  0.07405  701 TYR A N     
5796 C CA    . TYR B 701 ? 1.50816 1.60080 1.92086 -0.06071 0.03401  0.07199  701 TYR A CA    
5797 C C     . TYR B 701 ? 1.60888 1.70576 2.04105 -0.06215 0.03001  0.08317  701 TYR A C     
5798 O O     . TYR B 701 ? 1.48768 1.58812 1.92367 -0.06232 0.03025  0.08180  701 TYR A O     
5799 C CB    . TYR B 701 ? 1.28234 1.37343 1.66133 -0.06332 0.03596  0.07341  701 TYR A CB    
5800 C CG    . TYR B 701 ? 1.67841 1.76677 2.04423 -0.06571 0.03519  0.08413  701 TYR A CG    
5801 C CD1   . TYR B 701 ? 1.75641 1.84562 2.11755 -0.06939 0.03239  0.09739  701 TYR A CD1   
5802 C CD2   . TYR B 701 ? 1.56052 1.64520 1.91840 -0.06455 0.03745  0.08118  701 TYR A CD2   
5803 C CE1   . TYR B 701 ? 1.85338 1.93928 2.20077 -0.07173 0.03291  0.10667  701 TYR A CE1   
5804 C CE2   . TYR B 701 ? 1.44967 1.53181 1.79662 -0.06639 0.03821  0.09084  701 TYR A CE2   
5805 C CZ    . TYR B 701 ? 1.65241 1.73486 1.99316 -0.06994 0.03648  0.10323  701 TYR A CZ    
5806 O OH    . TYR B 701 ? 1.59792 1.67708 1.92613 -0.07193 0.03836  0.11231  701 TYR A OH    
5807 N N     . LYS B 702 ? 1.60303 1.69987 2.04806 -0.06337 0.02626  0.09472  702 LYS A N     
5808 C CA    . LYS B 702 ? 1.64669 1.74764 2.11297 -0.06512 0.02127  0.10677  702 LYS A CA    
5809 C C     . LYS B 702 ? 1.65374 1.75720 2.15127 -0.06141 0.02171  0.09950  702 LYS A C     
5810 O O     . LYS B 702 ? 1.68997 1.79764 2.19541 -0.06195 0.02081  0.10152  702 LYS A O     
5811 C CB    . LYS B 702 ? 1.53848 1.63844 2.01478 -0.06676 0.01764  0.11932  702 LYS A CB    
5812 C CG    . LYS B 702 ? 1.55713 1.66103 2.06237 -0.06797 0.01183  0.13131  702 LYS A CG    
5813 C CD    . LYS B 702 ? 1.49634 1.60388 1.99424 -0.07227 0.00780  0.14137  702 LYS A CD    
5814 C CE    . LYS B 702 ? 1.61285 1.72473 2.14226 -0.07345 0.00139  0.15345  702 LYS A CE    
5815 N NZ    . LYS B 702 ? 1.81931 1.93476 2.34190 -0.07826 -0.00368 0.16392  702 LYS A NZ    
5816 N N     . ASN B 703 ? 1.64701 1.74757 2.16169 -0.05788 0.02327  0.09112  703 ASN A N     
5817 C CA    . ASN B 703 ? 1.67981 1.78116 2.22535 -0.05416 0.02453  0.08331  703 ASN A CA    
5818 C C     . ASN B 703 ? 1.58119 1.67777 2.12065 -0.05095 0.02991  0.06497  703 ASN A C     
5819 O O     . ASN B 703 ? 1.51605 1.60849 2.07015 -0.04906 0.02944  0.06001  703 ASN A O     
5820 C CB    . ASN B 703 ? 1.62265 1.72425 2.20104 -0.05348 0.02008  0.09200  703 ASN A CB    
5821 C CG    . ASN B 703 ? 1.66508 1.77202 2.25549 -0.05657 0.01443  0.10926  703 ASN A CG    
5822 O OD1   . ASN B 703 ? 1.49437 1.60469 2.06920 -0.05931 0.01362  0.11424  703 ASN A OD1   
5823 N ND2   . ASN B 703 ? 1.67767 1.78527 2.29610 -0.05657 0.00989  0.11888  703 ASN A ND2   
5824 N N     . ILE B 704 ? 1.22899 1.32588 1.74741 -0.05081 0.03437  0.05566  704 ILE A N     
5825 C CA    . ILE B 704 ? 1.26493 1.35708 1.77429 -0.04852 0.03937  0.03810  704 ILE A CA    
5826 C C     . ILE B 704 ? 1.22750 1.31840 1.76554 -0.04498 0.04241  0.02870  704 ILE A C     
5827 O O     . ILE B 704 ? 1.20214 1.28747 1.73817 -0.04321 0.04582  0.01413  704 ILE A O     
5828 C CB    . ILE B 704 ? 0.97956 1.07295 1.45845 -0.04982 0.04318  0.03257  704 ILE A CB    
5829 C CG1   . ILE B 704 ? 0.99650 1.08494 1.46138 -0.04848 0.04758  0.01594  704 ILE A CG1   
5830 C CG2   . ILE B 704 ? 1.07741 1.17652 1.56335 -0.04986 0.04495  0.03551  704 ILE A CG2   
5831 C CD1   . ILE B 704 ? 1.18254 1.27246 1.61912 -0.04981 0.05139  0.01082  704 ILE A CD1   
5832 N N     . ASP B 705 ? 1.34579 1.44113 1.91001 -0.04420 0.04106  0.03693  705 ASP A N     
5833 C CA    . ASP B 705 ? 1.36679 1.46104 1.96069 -0.04040 0.04517  0.02824  705 ASP A CA    
5834 C C     . ASP B 705 ? 1.15465 1.24161 1.76538 -0.03833 0.04468  0.02030  705 ASP A C     
5835 O O     . ASP B 705 ? 0.96061 1.04210 1.57309 -0.03594 0.05031  0.00416  705 ASP A O     
5836 C CB    . ASP B 705 ? 1.32481 1.42566 1.94637 -0.04023 0.04259  0.04115  705 ASP A CB    
5837 C CG    . ASP B 705 ? 1.61969 1.72326 2.25076 -0.04304 0.03406  0.05958  705 ASP A CG    
5838 O OD1   . ASP B 705 ? 1.57340 1.67364 2.19057 -0.04474 0.03100  0.06215  705 ASP A OD1   
5839 O OD2   . ASP B 705 ? 1.72056 1.82967 2.37301 -0.04374 0.03058  0.07171  705 ASP A OD2   
5840 N N     . GLU B 706 ? 1.09620 1.18262 1.71847 -0.03950 0.03829  0.03109  706 GLU A N     
5841 C CA    . GLU B 706 ? 1.01356 1.09306 1.65584 -0.03774 0.03704  0.02454  706 GLU A CA    
5842 C C     . GLU B 706 ? 1.01126 1.08398 1.62844 -0.03835 0.03881  0.01064  706 GLU A C     
5843 O O     . GLU B 706 ? 0.83202 0.89740 1.46017 -0.03666 0.04046  -0.00221 706 GLU A O     
5844 C CB    . GLU B 706 ? 1.37193 1.45300 2.03174 -0.03923 0.02976  0.04044  706 GLU A CB    
5845 C CG    . GLU B 706 ? 1.65458 1.74343 2.32824 -0.04055 0.02618  0.05791  706 GLU A CG    
5846 C CD    . GLU B 706 ? 1.70062 1.79412 2.34632 -0.04468 0.02307  0.07079  706 GLU A CD    
5847 O OE1   . GLU B 706 ? 1.43626 1.52910 2.05018 -0.04570 0.02624  0.06417  706 GLU A OE1   
5848 O OE2   . GLU B 706 ? 1.73645 1.83373 2.39181 -0.04710 0.01757  0.08742  706 GLU A OE2   
5849 N N     . TYR B 707 ? 1.02508 1.09973 1.61016 -0.04095 0.03817  0.01333  707 TYR A N     
5850 C CA    . TYR B 707 ? 0.90904 0.97797 1.47024 -0.04203 0.03878  0.00209  707 TYR A CA    
5851 C C     . TYR B 707 ? 0.87290 0.93776 1.42578 -0.04060 0.04516  -0.01568 707 TYR A C     
5852 O O     . TYR B 707 ? 0.99119 1.04833 1.54387 -0.04042 0.04551  -0.02846 707 TYR A O     
5853 C CB    . TYR B 707 ? 0.80747 0.88002 1.33883 -0.04482 0.03729  0.01041  707 TYR A CB    
5854 C CG    . TYR B 707 ? 0.80342 0.87134 1.31529 -0.04637 0.03563  0.00492  707 TYR A CG    
5855 C CD1   . TYR B 707 ? 0.77193 0.83821 1.29253 -0.04725 0.03080  0.01214  707 TYR A CD1   
5856 C CD2   . TYR B 707 ? 0.95510 1.02079 1.44075 -0.04719 0.03867  -0.00636 707 TYR A CD2   
5857 C CE1   . TYR B 707 ? 1.14750 1.21016 1.65303 -0.04873 0.02890  0.00821  707 TYR A CE1   
5858 C CE2   . TYR B 707 ? 0.97566 1.03751 1.44513 -0.04891 0.03627  -0.01021 707 TYR A CE2   
5859 C CZ    . TYR B 707 ? 1.18432 1.24477 1.66446 -0.04962 0.03130  -0.00285 707 TYR A CZ    
5860 O OH    . TYR B 707 ? 1.17866 1.23587 1.64547 -0.05136 0.02859  -0.00572 707 TYR A OH    
5861 N N     . VAL B 708 ? 0.78059 0.85023 1.32682 -0.03995 0.05007  -0.01631 708 VAL A N     
5862 C CA    . VAL B 708 ? 0.87520 0.94146 1.41154 -0.03872 0.05752  -0.03292 708 VAL A CA    
5863 C C     . VAL B 708 ? 0.88389 0.94429 1.44962 -0.03567 0.06066  -0.04268 708 VAL A C     
5864 O O     . VAL B 708 ? 0.97715 1.03015 1.53458 -0.03528 0.06529  -0.05915 708 VAL A O     
5865 C CB    . VAL B 708 ? 0.90197 0.97520 1.42735 -0.03865 0.06246  -0.03065 708 VAL A CB    
5866 C CG1   . VAL B 708 ? 1.08706 1.16627 1.64217 -0.03658 0.06326  -0.02146 708 VAL A CG1   
5867 C CG2   . VAL B 708 ? 0.91946 0.98922 1.42733 -0.03821 0.07024  -0.04712 708 VAL A CG2   
5868 N N     . ALA B 709 ? 0.93564 0.99865 1.53384 -0.03388 0.05811  -0.03282 709 ALA A N     
5869 C CA    . ALA B 709 ? 0.98264 1.03957 1.61231 -0.03072 0.06098  -0.04126 709 ALA A CA    
5870 C C     . ALA B 709 ? 0.89737 0.94425 1.52544 -0.03177 0.05752  -0.05060 709 ALA A C     
5871 O O     . ALA B 709 ? 0.90330 0.94132 1.53804 -0.03032 0.06214  -0.06640 709 ALA A O     
5872 C CB    . ALA B 709 ? 0.96981 1.03213 1.63451 -0.02914 0.05743  -0.02639 709 ALA A CB    
5873 N N     . SER B 710 ? 0.87228 0.92009 1.49237 -0.03441 0.04972  -0.04103 710 SER A N     
5874 C CA    . SER B 710 ? 0.80400 0.84275 1.42178 -0.03595 0.04568  -0.04929 710 SER A CA    
5875 C C     . SER B 710 ? 0.81259 0.84517 1.39925 -0.03778 0.04900  -0.06563 710 SER A C     
5876 O O     . SER B 710 ? 0.83559 0.85799 1.42396 -0.03823 0.04945  -0.07992 710 SER A O     
5877 C CB    . SER B 710 ? 0.77318 0.81523 1.38838 -0.03839 0.03747  -0.03476 710 SER A CB    
5878 O OG    . SER B 710 ? 1.06268 1.10964 1.70633 -0.03727 0.03409  -0.01961 710 SER A OG    
5879 N N     . ILE B 711 ? 0.82037 0.85846 1.37794 -0.03924 0.05105  -0.06366 711 ILE A N     
5880 C CA    . ILE B 711 ? 0.83407 0.86708 1.36075 -0.04142 0.05382  -0.07770 711 ILE A CA    
5881 C C     . ILE B 711 ? 0.80863 0.83501 1.33913 -0.03963 0.06221  -0.09469 711 ILE A C     
5882 O O     . ILE B 711 ? 0.86102 0.87756 1.37959 -0.04145 0.06287  -0.10961 711 ILE A O     
5883 C CB    . ILE B 711 ? 0.73890 0.77965 1.23677 -0.04298 0.05506  -0.07134 711 ILE A CB    
5884 C CG1   . ILE B 711 ? 0.99914 1.04476 1.49154 -0.04481 0.04780  -0.05591 711 ILE A CG1   
5885 C CG2   . ILE B 711 ? 0.75752 0.79335 1.22440 -0.04538 0.05800  -0.08527 711 ILE A CG2   
5886 C CD1   . ILE B 711 ? 0.87859 0.92978 1.34088 -0.04669 0.04865  -0.05097 711 ILE A CD1   
5887 N N     . VAL B 712 ? 0.85032 0.88160 1.39775 -0.03626 0.06886  -0.09263 712 VAL A N     
5888 C CA    . VAL B 712 ? 0.89639 0.92142 1.44911 -0.03408 0.07852  -0.10874 712 VAL A CA    
5889 C C     . VAL B 712 ? 0.82908 0.84334 1.40663 -0.03281 0.07778  -0.11778 712 VAL A C     
5890 O O     . VAL B 712 ? 0.89009 0.89415 1.46221 -0.03278 0.08390  -0.13539 712 VAL A O     
5891 C CB    . VAL B 712 ? 0.85248 0.88611 1.41993 -0.03063 0.08611  -0.10349 712 VAL A CB    
5892 C CG1   . VAL B 712 ? 1.09423 1.13417 1.69639 -0.02832 0.08172  -0.08767 712 VAL A CG1   
5893 C CG2   . VAL B 712 ? 0.83665 0.86369 1.41121 -0.02796 0.09765  -0.12032 712 VAL A CG2   
5894 N N     . SER B 713 ? 0.92853 0.94409 1.53232 -0.03213 0.07038  -0.10629 713 SER A N     
5895 C CA    . SER B 713 ? 0.95015 0.95469 1.57608 -0.03162 0.06815  -0.11450 713 SER A CA    
5896 C C     . SER B 713 ? 0.94799 0.94158 1.54887 -0.03582 0.06456  -0.12797 713 SER A C     
5897 O O     . SER B 713 ? 0.91208 0.89337 1.51563 -0.03597 0.06809  -0.14461 713 SER A O     
5898 C CB    . SER B 713 ? 0.92759 0.93628 1.58249 -0.03105 0.05953  -0.09787 713 SER A CB    
5899 O OG    . SER B 713 ? 1.31406 1.32848 2.00114 -0.02709 0.06287  -0.08945 713 SER A OG    
5900 N N     . TYR B 714 ? 1.04214 1.03958 1.61822 -0.03951 0.05755  -0.12109 714 TYR A N     
5901 C CA    . TYR B 714 ? 0.96291 0.95076 1.51603 -0.04407 0.05266  -0.13209 714 TYR A CA    
5902 C C     . TYR B 714 ? 0.89742 0.87868 1.42238 -0.04558 0.06041  -0.14985 714 TYR A C     
5903 O O     . TYR B 714 ? 0.97090 0.93941 1.48741 -0.04832 0.05978  -0.16522 714 TYR A O     
5904 C CB    . TYR B 714 ? 0.82762 0.82204 1.36350 -0.04728 0.04391  -0.11930 714 TYR A CB    
5905 C CG    . TYR B 714 ? 0.87201 0.86662 1.43210 -0.04764 0.03493  -0.10801 714 TYR A CG    
5906 C CD1   . TYR B 714 ? 0.91255 0.91545 1.49898 -0.04458 0.03423  -0.09232 714 TYR A CD1   
5907 C CD2   . TYR B 714 ? 0.80167 0.78798 1.35900 -0.05142 0.02688  -0.11274 714 TYR A CD2   
5908 C CE1   . TYR B 714 ? 0.88682 0.88997 1.49544 -0.04508 0.02655  -0.08159 714 TYR A CE1   
5909 C CE2   . TYR B 714 ? 0.77149 0.75824 1.35247 -0.05180 0.01902  -0.10208 714 TYR A CE2   
5910 C CZ    . TYR B 714 ? 0.85972 0.85496 1.46611 -0.04851 0.01929  -0.08656 714 TYR A CZ    
5911 O OH    . TYR B 714 ? 0.86860 0.86440 1.49837 -0.04908 0.01190  -0.07547 714 TYR A OH    
5912 N N     . ILE B 715 ? 0.91631 0.90564 1.42606 -0.04423 0.06767  -0.14798 715 ILE A N     
5913 C CA    . ILE B 715 ? 0.95872 0.94243 1.44256 -0.04554 0.07625  -0.16418 715 ILE A CA    
5914 C C     . ILE B 715 ? 0.96154 0.93430 1.46250 -0.04314 0.08476  -0.18008 715 ILE A C     
5915 O O     . ILE B 715 ? 1.03123 0.99221 1.51279 -0.04593 0.08835  -0.19748 715 ILE A O     
5916 C CB    . ILE B 715 ? 0.97401 0.96932 1.44413 -0.04402 0.08294  -0.15768 715 ILE A CB    
5917 C CG1   . ILE B 715 ? 0.88217 0.88699 1.33569 -0.04638 0.07480  -0.14241 715 ILE A CG1   
5918 C CG2   . ILE B 715 ? 0.89567 0.88565 1.33815 -0.04567 0.09212  -0.17367 715 ILE A CG2   
5919 C CD1   . ILE B 715 ? 0.84571 0.86152 1.28649 -0.04529 0.08013  -0.13500 715 ILE A CD1   
5920 N N     . ILE B 716 ? 1.07094 1.04688 1.60843 -0.03815 0.08811  -0.17424 716 ILE A N     
5921 C CA    . ILE B 716 ? 1.07620 1.04149 1.63576 -0.03519 0.09632  -0.18825 716 ILE A CA    
5922 C C     . ILE B 716 ? 1.12332 1.07317 1.68134 -0.03868 0.09015  -0.20030 716 ILE A C     
5923 O O     . ILE B 716 ? 1.16575 1.10239 1.70918 -0.04046 0.09615  -0.21942 716 ILE A O     
5924 C CB    . ILE B 716 ? 0.97697 0.94915 1.58002 -0.02960 0.09807  -0.17646 716 ILE A CB    
5925 C CG1   . ILE B 716 ? 0.96146 0.94607 1.56804 -0.02612 0.10662  -0.16908 716 ILE A CG1   
5926 C CG2   . ILE B 716 ? 1.21882 1.17812 1.84969 -0.02690 0.10340  -0.18957 716 ILE A CG2   
5927 C CD1   . ILE B 716 ? 0.95500 0.94701 1.60414 -0.02128 0.10722  -0.15613 716 ILE A CD1   
5928 N N     . GLU B 717 ? 1.06071 1.01170 1.63374 -0.04003 0.07810  -0.18911 717 GLU A N     
5929 C CA    . GLU B 717 ? 1.01114 0.94786 1.58756 -0.04346 0.07100  -0.19888 717 GLU A CA    
5930 C C     . GLU B 717 ? 1.10403 1.03093 1.64000 -0.04964 0.06917  -0.21344 717 GLU A C     
5931 O O     . GLU B 717 ? 1.20545 1.11676 1.73507 -0.05178 0.07226  -0.23190 717 GLU A O     
5932 C CB    . GLU B 717 ? 0.99272 0.93476 1.58728 -0.04455 0.05789  -0.18200 717 GLU A CB    
5933 C CG    . GLU B 717 ? 1.02695 0.95531 1.63534 -0.04733 0.05014  -0.18946 717 GLU A CG    
5934 C CD    . GLU B 717 ? 1.09925 1.02302 1.74956 -0.04278 0.05340  -0.19010 717 GLU A CD    
5935 O OE1   . GLU B 717 ? 1.36259 1.29353 2.03107 -0.03744 0.06217  -0.18562 717 GLU A OE1   
5936 O OE2   . GLU B 717 ? 1.27261 1.18568 1.93904 -0.04471 0.04675  -0.19451 717 GLU A OE2   
5937 N N     . TYR B 718 ? 1.16577 1.10120 1.67349 -0.05283 0.06422  -0.20533 718 TYR A N     
5938 C CA    . TYR B 718 ? 1.11316 1.04057 1.58196 -0.05915 0.06150  -0.21709 718 TYR A CA    
5939 C C     . TYR B 718 ? 1.10157 1.01953 1.55251 -0.05921 0.07429  -0.23657 718 TYR A C     
5940 O O     . TYR B 718 ? 1.17036 1.07290 1.60536 -0.06369 0.07369  -0.25335 718 TYR A O     
5941 C CB    . TYR B 718 ? 1.02006 0.95974 1.46350 -0.06140 0.05681  -0.20458 718 TYR A CB    
5942 C CG    . TYR B 718 ? 1.05003 0.98299 1.45219 -0.06759 0.05583  -0.21618 718 TYR A CG    
5943 C CD1   . TYR B 718 ? 1.20606 1.13125 1.59389 -0.07405 0.04378  -0.21880 718 TYR A CD1   
5944 C CD2   . TYR B 718 ? 1.26648 1.20101 1.64483 -0.06730 0.06664  -0.22387 718 TYR A CD2   
5945 C CE1   . TYR B 718 ? 1.13062 1.04958 1.48086 -0.08032 0.04187  -0.22853 718 TYR A CE1   
5946 C CE2   . TYR B 718 ? 1.31534 1.24365 1.65551 -0.07340 0.06553  -0.23383 718 TYR A CE2   
5947 C CZ    . TYR B 718 ? 1.24427 1.16473 1.57016 -0.08002 0.05280  -0.23599 718 TYR A CZ    
5948 O OH    . TYR B 718 ? 1.28284 1.19714 1.57068 -0.08670 0.05065  -0.24494 718 TYR A OH    
5949 N N     . THR B 719 ? 1.08846 1.01527 1.54179 -0.05452 0.08610  -0.23445 719 THR A N     
5950 C CA    . THR B 719 ? 1.15025 1.07019 1.58313 -0.05468 0.09941  -0.25138 719 THR A CA    
5951 C C     . THR B 719 ? 1.23843 1.14270 1.68848 -0.05294 0.10734  -0.26883 719 THR A C     
5952 O O     . THR B 719 ? 1.27824 1.16935 1.70376 -0.05622 0.11405  -0.28750 719 THR A O     
5953 C CB    . THR B 719 ? 1.07638 1.01084 1.51189 -0.04991 0.10964  -0.24290 719 THR A CB    
5954 O OG1   . THR B 719 ? 1.28910 1.23461 1.76208 -0.04446 0.10774  -0.22654 719 THR A OG1   
5955 C CG2   . THR B 719 ? 1.12541 1.06934 1.52690 -0.05354 0.10599  -0.23524 719 THR A CG2   
5956 N N     . THR B 720 ? 1.18443 1.08902 1.67567 -0.04813 0.10671  -0.26331 720 THR A N     
5957 C CA    . THR B 720 ? 1.15710 1.04599 1.66708 -0.04623 0.11428  -0.27987 720 THR A CA    
5958 C C     . THR B 720 ? 1.18407 1.05567 1.68066 -0.05276 0.10461  -0.29211 720 THR A C     
5959 O O     . THR B 720 ? 1.26019 1.11458 1.74894 -0.05437 0.11174  -0.31235 720 THR A O     
5960 C CB    . THR B 720 ? 1.12119 1.01553 1.68088 -0.03940 0.11559  -0.26938 720 THR A CB    
5961 O OG1   . THR B 720 ? 1.16538 1.06362 1.74136 -0.04098 0.10017  -0.25480 720 THR A OG1   
5962 C CG2   . THR B 720 ? 1.12686 1.03843 1.70030 -0.03366 0.12370  -0.25621 720 THR A CG2   
5963 N N     . ILE B 721 ? 1.34611 1.22153 1.83983 -0.05683 0.08853  -0.28024 721 ILE A N     
5964 C CA    . ILE B 721 ? 1.17782 1.03728 1.66172 -0.06344 0.07789  -0.29048 721 ILE A CA    
5965 C C     . ILE B 721 ? 1.23342 1.08365 1.66923 -0.07093 0.07741  -0.30442 721 ILE A C     
5966 O O     . ILE B 721 ? 1.34000 1.17152 1.76200 -0.07565 0.07757  -0.32294 721 ILE A O     
5967 C CB    . ILE B 721 ? 1.13575 1.00266 1.63572 -0.06521 0.06126  -0.27250 721 ILE A CB    
5968 C CG1   . ILE B 721 ? 1.13331 1.00632 1.68108 -0.05858 0.06183  -0.26072 721 ILE A CG1   
5969 C CG2   . ILE B 721 ? 1.17148 1.02293 1.65933 -0.07291 0.04895  -0.28190 721 ILE A CG2   
5970 C CD1   . ILE B 721 ? 1.15536 1.03806 1.72037 -0.05947 0.04772  -0.24090 721 ILE A CD1   
5971 N N     . THR B 722 ? 1.47621 1.33864 1.88531 -0.07251 0.07667  -0.29592 722 THR A N     
5972 C CA    . THR B 722 ? 1.41053 1.26607 1.77355 -0.07984 0.07562  -0.30673 722 THR A CA    
5973 C C     . THR B 722 ? 1.34546 1.21137 1.68944 -0.07714 0.08837  -0.30579 722 THR A C     
5974 O O     . THR B 722 ? 1.47138 1.35470 1.82041 -0.07400 0.08710  -0.28856 722 THR A O     
5975 C CB    . THR B 722 ? 1.46742 1.32666 1.81405 -0.08644 0.05795  -0.29591 722 THR A CB    
5976 O OG1   . THR B 722 ? 1.85958 1.71156 2.16176 -0.09403 0.05648  -0.30635 722 THR A OG1   
5977 C CG2   . THR B 722 ? 1.28089 1.16112 1.63827 -0.08256 0.05418  -0.27300 722 THR A CG2   
5978 N N     . SER B 723 ? 1.30543 1.16019 1.62673 -0.07870 0.10076  -0.32439 723 SER A N     
5979 C CA    . SER B 723 ? 1.35710 1.22064 1.66231 -0.07597 0.11470  -0.32500 723 SER A CA    
5980 C C     . SER B 723 ? 1.42172 1.28987 1.68498 -0.08274 0.10803  -0.32126 723 SER A C     
5981 O O     . SER B 723 ? 1.38852 1.24803 1.61652 -0.08765 0.11400  -0.33481 723 SER A O     
5982 C CB    . SER B 723 ? 1.58187 1.43161 1.88185 -0.07455 0.13208  -0.34616 723 SER A CB    
5983 O OG    . SER B 723 ? 1.65128 1.49395 1.99005 -0.06916 0.13663  -0.35099 723 SER A OG    
5984 N N     . SER B 724 ? 1.46361 1.34557 1.73136 -0.08297 0.09575  -0.30208 724 SER A N     
5985 C CA    . SER B 724 ? 1.30577 1.19340 1.53927 -0.08895 0.08757  -0.29555 724 SER A CA    
5986 C C     . SER B 724 ? 1.29050 1.19828 1.53216 -0.08418 0.08868  -0.27642 724 SER A C     
5987 O O     . SER B 724 ? 1.34961 1.26654 1.62148 -0.07687 0.09537  -0.26860 724 SER A O     
5988 C CB    . SER B 724 ? 1.50719 1.38890 1.73435 -0.09570 0.06912  -0.29209 724 SER A CB    
5989 O OG    . SER B 724 ? 1.46170 1.35058 1.66069 -0.10078 0.06076  -0.28325 724 SER A OG    
5990 N N     . LYS B 725 ? 1.38221 1.29642 1.59640 -0.08873 0.08173  -0.26877 725 LYS A N     
5991 C CA    . LYS B 725 ? 1.27390 1.20563 1.49076 -0.08515 0.08273  -0.25187 725 LYS A CA    
5992 C C     . LYS B 725 ? 1.18116 1.12211 1.42545 -0.08230 0.07202  -0.23414 725 LYS A C     
5993 O O     . LYS B 725 ? 1.28791 1.22264 1.54314 -0.08456 0.06141  -0.23340 725 LYS A O     
5994 C CB    . LYS B 725 ? 1.31988 1.25469 1.49874 -0.09104 0.07900  -0.24968 725 LYS A CB    
5995 C CG    . LYS B 725 ? 1.39229 1.31547 1.53698 -0.09650 0.08591  -0.26738 725 LYS A CG    
5996 C CD    . LYS B 725 ? 1.45142 1.38066 1.56173 -0.10138 0.08344  -0.26223 725 LYS A CD    
5997 C CE    . LYS B 725 ? 1.61600 1.53307 1.68922 -0.10798 0.08923  -0.27924 725 LYS A CE    
5998 N NZ    . LYS B 725 ? 1.92770 1.84559 1.96662 -0.11594 0.07885  -0.27465 725 LYS A NZ    
5999 N N     . CYS B 726 ? 1.11345 1.06917 1.36790 -0.07767 0.07496  -0.21958 726 CYS A N     
6000 C CA    . CYS B 726 ? 1.06709 1.03251 1.34494 -0.07481 0.06671  -0.20187 726 CYS A CA    
6001 C C     . CYS B 726 ? 1.03570 1.01468 1.30144 -0.07389 0.06743  -0.18840 726 CYS A C     
6002 O O     . CYS B 726 ? 1.20350 1.18674 1.45808 -0.07249 0.07724  -0.19108 726 CYS A O     
6003 C CB    . CYS B 726 ? 1.04692 1.01421 1.36319 -0.06844 0.07137  -0.19885 726 CYS A CB    
6004 S SG    . CYS B 726 ? 1.14871 1.13028 1.49170 -0.06430 0.06493  -0.17568 726 CYS A SG    
6005 N N     . LEU B 727 ? 0.96496 0.95040 1.23363 -0.07464 0.05749  -0.17398 727 LEU A N     
6006 C CA    . LEU B 727 ? 0.94904 0.94640 1.20633 -0.07390 0.05767  -0.16082 727 LEU A CA    
6007 C C     . LEU B 727 ? 0.93353 0.93946 1.21599 -0.07008 0.05346  -0.14421 727 LEU A C     
6008 O O     . LEU B 727 ? 1.03509 1.03847 1.32932 -0.07117 0.04463  -0.13950 727 LEU A O     
6009 C CB    . LEU B 727 ? 1.02371 1.01936 1.25156 -0.07983 0.05009  -0.16041 727 LEU A CB    
6010 C CG    . LEU B 727 ? 1.21189 1.21828 1.42882 -0.07959 0.04825  -0.14627 727 LEU A CG    
6011 C CD1   . LEU B 727 ? 1.32379 1.33683 1.53185 -0.07722 0.05887  -0.14636 727 LEU A CD1   
6012 C CD2   . LEU B 727 ? 1.17103 1.17466 1.36294 -0.08558 0.03971  -0.14594 727 LEU A CD2   
6013 N N     . VAL B 728 ? 0.86086 0.87636 1.15093 -0.06614 0.05953  -0.13553 728 VAL A N     
6014 C CA    . VAL B 728 ? 0.94481 0.96808 1.25670 -0.06296 0.05603  -0.11947 728 VAL A CA    
6015 C C     . VAL B 728 ? 0.97183 1.00381 1.26664 -0.06356 0.05530  -0.10784 728 VAL A C     
6016 O O     . VAL B 728 ? 1.06047 1.09647 1.34218 -0.06317 0.06195  -0.10947 728 VAL A O     
6017 C CB    . VAL B 728 ? 1.04343 1.06984 1.38338 -0.05812 0.06217  -0.11740 728 VAL A CB    
6018 C CG1   . VAL B 728 ? 0.96149 0.99253 1.32578 -0.05599 0.05658  -0.10278 728 VAL A CG1   
6019 C CG2   . VAL B 728 ? 0.90604 0.92321 1.25787 -0.05729 0.06671  -0.13248 728 VAL A CG2   
6020 N N     . LEU B 729 ? 1.02079 1.05516 1.31659 -0.06445 0.04791  -0.09666 729 LEU A N     
6021 C CA    . LEU B 729 ? 0.98063 1.02200 1.26071 -0.06498 0.04729  -0.08563 729 LEU A CA    
6022 C C     . LEU B 729 ? 1.14047 1.18853 1.43877 -0.06173 0.04781  -0.07174 729 LEU A C     
6023 O O     . LEU B 729 ? 1.24742 1.29505 1.56098 -0.06122 0.04268  -0.06432 729 LEU A O     
6024 C CB    . LEU B 729 ? 1.05281 1.09162 1.32035 -0.06840 0.03946  -0.08300 729 LEU A CB    
6025 C CG    . LEU B 729 ? 0.99740 1.02899 1.24586 -0.07275 0.03684  -0.09555 729 LEU A CG    
6026 C CD1   . LEU B 729 ? 0.98951 1.01758 1.23839 -0.07582 0.02700  -0.09227 729 LEU A CD1   
6027 C CD2   . LEU B 729 ? 1.44954 1.48374 1.67063 -0.07471 0.04065  -0.09771 729 LEU A CD2   
6028 N N     . PHE B 730 ? 1.16591 1.21982 1.46236 -0.06005 0.05351  -0.06797 730 PHE A N     
6029 C CA    . PHE B 730 ? 1.22866 1.28841 1.54140 -0.05771 0.05358  -0.05479 730 PHE A CA    
6030 C C     . PHE B 730 ? 1.20290 1.26677 1.49887 -0.05892 0.05215  -0.04392 730 PHE A C     
6031 O O     . PHE B 730 ? 1.36552 1.42812 1.63952 -0.06115 0.05132  -0.04660 730 PHE A O     
6032 C CB    . PHE B 730 ? 1.01289 1.07665 1.33573 -0.05555 0.05980  -0.05580 730 PHE A CB    
6033 C CG    . PHE B 730 ? 0.96433 1.02394 1.30466 -0.05377 0.06338  -0.06726 730 PHE A CG    
6034 C CD1   . PHE B 730 ? 1.10219 1.15809 1.42955 -0.05458 0.06865  -0.08118 730 PHE A CD1   
6035 C CD2   . PHE B 730 ? 1.13936 1.19828 1.50894 -0.05140 0.06191  -0.06406 730 PHE A CD2   
6036 C CE1   . PHE B 730 ? 1.52670 1.57764 1.86947 -0.05286 0.07307  -0.09243 730 PHE A CE1   
6037 C CE2   . PHE B 730 ? 1.46012 1.51437 1.84673 -0.04955 0.06573  -0.07493 730 PHE A CE2   
6038 C CZ    . PHE B 730 ? 1.53818 1.58812 1.91108 -0.05020 0.07166  -0.08950 730 PHE A CZ    
6039 N N     . THR B 731 ? 1.32042 1.38858 1.62619 -0.05773 0.05181  -0.03178 731 THR A N     
6040 C CA    . THR B 731 ? 1.38669 1.45773 1.67588 -0.05894 0.05137  -0.02161 731 THR A CA    
6041 C C     . THR B 731 ? 1.53718 1.61324 1.82842 -0.05847 0.05429  -0.01516 731 THR A C     
6042 O O     . THR B 731 ? 1.64605 1.72398 1.92263 -0.05978 0.05441  -0.00721 731 THR A O     
6043 C CB    . THR B 731 ? 1.37412 1.44402 1.67044 -0.05890 0.04728  -0.01205 731 THR A CB    
6044 O OG1   . THR B 731 ? 1.59319 1.65865 1.89613 -0.05916 0.04390  -0.01893 731 THR A OG1   
6045 C CG2   . THR B 731 ? 1.06114 1.13157 1.33750 -0.06026 0.04735  -0.00463 731 THR A CG2   
6046 N N     . SER B 732 ? 1.42824 1.50605 1.73765 -0.05683 0.05646  -0.01832 732 SER A N     
6047 C CA    . SER B 732 ? 1.14594 1.22911 1.46136 -0.05666 0.05817  -0.01087 732 SER A CA    
6048 C C     . SER B 732 ? 1.01411 1.09946 1.32949 -0.05597 0.06359  -0.01982 732 SER A C     
6049 O O     . SER B 732 ? 1.12447 1.20826 1.45686 -0.05396 0.06601  -0.02808 732 SER A O     
6050 C CB    . SER B 732 ? 1.36124 1.44590 1.70285 -0.05535 0.05550  -0.00262 732 SER A CB    
6051 O OG    . SER B 732 ? 1.44584 1.53570 1.79563 -0.05549 0.05648  0.00384  732 SER A OG    
6052 N N     . TYR B 733 ? 1.19447 1.28295 1.49195 -0.05761 0.06583  -0.01820 733 TYR A N     
6053 C CA    . TYR B 733 ? 1.03801 1.12959 1.33655 -0.05702 0.07172  -0.02525 733 TYR A CA    
6054 C C     . TYR B 733 ? 1.21404 1.30824 1.54300 -0.05447 0.07318  -0.02406 733 TYR A C     
6055 O O     . TYR B 733 ? 1.32353 1.41724 1.66268 -0.05253 0.07878  -0.03419 733 TYR A O     
6056 C CB    . TYR B 733 ? 1.12778 1.22353 1.40902 -0.05937 0.07225  -0.01873 733 TYR A CB    
6057 C CG    . TYR B 733 ? 1.43268 1.53314 1.71650 -0.05909 0.07809  -0.02274 733 TYR A CG    
6058 C CD1   . TYR B 733 ? 1.52849 1.62809 1.79527 -0.05975 0.08319  -0.03290 733 TYR A CD1   
6059 C CD2   . TYR B 733 ? 1.17780 1.28383 1.48131 -0.05850 0.07836  -0.01551 733 TYR A CD2   
6060 C CE1   . TYR B 733 ? 1.51833 1.62254 1.78789 -0.05948 0.08942  -0.03616 733 TYR A CE1   
6061 C CE2   . TYR B 733 ? 1.16317 1.27412 1.47139 -0.05815 0.08403  -0.01840 733 TYR A CE2   
6062 C CZ    . TYR B 733 ? 1.48194 1.59202 1.77315 -0.05849 0.09009  -0.02891 733 TYR A CZ    
6063 O OH    . TYR B 733 ? 1.37815 1.49336 1.67447 -0.05811 0.09657  -0.03145 733 TYR A OH    
6064 N N     . LYS B 734 ? 1.15263 1.24922 1.49602 -0.05459 0.06846  -0.01171 734 LYS A N     
6065 C CA    . LYS B 734 ? 1.06358 1.16328 1.43854 -0.05237 0.06887  -0.00842 734 LYS A CA    
6066 C C     . LYS B 734 ? 1.34666 1.44138 1.73946 -0.04950 0.07061  -0.01844 734 LYS A C     
6067 O O     . LYS B 734 ? 1.27841 1.37377 1.68890 -0.04703 0.07597  -0.02563 734 LYS A O     
6068 C CB    . LYS B 734 ? 1.15566 1.25763 1.53991 -0.05382 0.06214  0.00723  734 LYS A CB    
6069 C CG    . LYS B 734 ? 1.51617 1.62123 1.93438 -0.05202 0.06061  0.01325  734 LYS A CG    
6070 C CD    . LYS B 734 ? 1.56724 1.67262 1.99210 -0.05386 0.05332  0.02776  734 LYS A CD    
6071 C CE    . LYS B 734 ? 1.55380 1.66049 1.95417 -0.05791 0.04997  0.03773  734 LYS A CE    
6072 N NZ    . LYS B 734 ? 1.71716 1.82274 2.11949 -0.05999 0.04399  0.05053  734 LYS A NZ    
6073 N N     . MET B 735 ? 1.17221 1.26185 1.56109 -0.04990 0.06646  -0.01890 735 MET A N     
6074 C CA    . MET B 735 ? 1.02766 1.11161 1.43373 -0.04777 0.06681  -0.02793 735 MET A CA    
6075 C C     . MET B 735 ? 1.03723 1.11754 1.43560 -0.04691 0.07371  -0.04440 735 MET A C     
6076 O O     . MET B 735 ? 1.19907 1.27691 1.61852 -0.04436 0.07761  -0.05208 735 MET A O     
6077 C CB    . MET B 735 ? 1.02114 1.10029 1.41903 -0.04909 0.06124  -0.02646 735 MET A CB    
6078 C CG    . MET B 735 ? 1.16125 1.23482 1.58062 -0.04745 0.05948  -0.03212 735 MET A CG    
6079 S SD    . MET B 735 ? 0.80865 0.87760 1.21962 -0.04933 0.05263  -0.02901 735 MET A SD    
6080 C CE    . MET B 735 ? 0.73849 0.81339 1.15150 -0.05029 0.04862  -0.00920 735 MET A CE    
6081 N N     . MET B 736 ? 0.91879 0.99842 1.28797 -0.04910 0.07545  -0.04948 736 MET A N     
6082 C CA    . MET B 736 ? 0.87180 0.94725 1.22950 -0.04910 0.08191  -0.06517 736 MET A CA    
6083 C C     . MET B 736 ? 0.93197 1.01094 1.30682 -0.04652 0.08994  -0.06890 736 MET A C     
6084 O O     . MET B 736 ? 0.97285 1.04677 1.35854 -0.04465 0.09535  -0.08100 736 MET A O     
6085 C CB    . MET B 736 ? 0.87312 0.94902 1.19744 -0.05219 0.08232  -0.06714 736 MET A CB    
6086 C CG    . MET B 736 ? 1.11936 1.19050 1.42797 -0.05313 0.08820  -0.08250 736 MET A CG    
6087 S SD    . MET B 736 ? 0.93944 1.01139 1.21002 -0.05718 0.08730  -0.08276 736 MET A SD    
6088 C CE    . MET B 736 ? 0.94742 1.02919 1.21925 -0.05679 0.08906  -0.06980 736 MET A CE    
6089 N N     . HIS B 737 ? 1.08716 1.17412 1.46509 -0.04656 0.09067  -0.05873 737 HIS A N     
6090 C CA    . HIS B 737 ? 1.14045 1.23204 1.53665 -0.04415 0.09835  -0.06073 737 HIS A CA    
6091 C C     . HIS B 737 ? 1.12989 1.22080 1.56255 -0.04077 0.09827  -0.05912 737 HIS A C     
6092 O O     . HIS B 737 ? 0.99305 1.08243 1.44264 -0.03787 0.10628  -0.06845 737 HIS A O     
6093 C CB    . HIS B 737 ? 1.10714 1.20738 1.49776 -0.04576 0.09756  -0.04913 737 HIS A CB    
6094 C CG    . HIS B 737 ? 1.21540 1.31660 1.57787 -0.04789 0.10221  -0.05490 737 HIS A CG    
6095 N ND1   . HIS B 737 ? 1.11259 1.21186 1.44498 -0.05114 0.09794  -0.05355 737 HIS A ND1   
6096 C CD2   . HIS B 737 ? 1.45058 1.55438 1.81137 -0.04719 0.11112  -0.06190 737 HIS A CD2   
6097 C CE1   . HIS B 737 ? 1.19697 1.29771 1.51022 -0.05256 0.10347  -0.05918 737 HIS A CE1   
6098 N NE2   . HIS B 737 ? 1.47227 1.57589 1.80173 -0.05028 0.11168  -0.06429 737 HIS A NE2   
6099 N N     . MET B 738 ? 1.05017 1.14176 1.49468 -0.04116 0.08988  -0.04760 738 MET A N     
6100 C CA    . MET B 738 ? 1.03743 1.12875 1.51820 -0.03823 0.08872  -0.04411 738 MET A CA    
6101 C C     . MET B 738 ? 0.98003 1.06237 1.46924 -0.03592 0.09359  -0.06012 738 MET A C     
6102 O O     . MET B 738 ? 1.18886 1.27071 1.70420 -0.03256 0.09979  -0.06516 738 MET A O     
6103 C CB    . MET B 738 ? 1.12553 1.21740 1.61295 -0.03965 0.07877  -0.03047 738 MET A CB    
6104 C CG    . MET B 738 ? 1.03511 1.13515 1.52795 -0.04135 0.07387  -0.01326 738 MET A CG    
6105 S SD    . MET B 738 ? 1.08534 1.18504 1.58693 -0.04310 0.06349  0.00215  738 MET A SD    
6106 C CE    . MET B 738 ? 1.33255 1.44138 1.84504 -0.04523 0.05912  0.02030  738 MET A CE    
6107 N N     . VAL B 739 ? 0.85134 0.92647 1.31945 -0.03785 0.09090  -0.06785 739 VAL A N     
6108 C CA    . VAL B 739 ? 0.88726 0.95233 1.36240 -0.03654 0.09395  -0.08301 739 VAL A CA    
6109 C C     . VAL B 739 ? 0.91877 0.98136 1.38801 -0.03522 0.10543  -0.09781 739 VAL A C     
6110 O O     . VAL B 739 ? 1.12988 1.18718 1.62068 -0.03228 0.11130  -0.10717 739 VAL A O     
6111 C CB    . VAL B 739 ? 0.93874 0.99655 1.39294 -0.03957 0.08756  -0.08763 739 VAL A CB    
6112 C CG1   . VAL B 739 ? 1.23534 1.29188 1.65263 -0.04273 0.08948  -0.09478 739 VAL A CG1   
6113 C CG2   . VAL B 739 ? 1.15625 1.20373 1.62513 -0.03856 0.08771  -0.09937 739 VAL A CG2   
6114 N N     . GLN B 740 ? 0.97426 1.04034 1.41635 -0.03725 0.10902  -0.09960 740 GLN A N     
6115 C CA    . GLN B 740 ? 0.99921 1.06240 1.43264 -0.03644 0.12071  -0.11423 740 GLN A CA    
6116 C C     . GLN B 740 ? 1.00228 1.06999 1.46912 -0.03200 0.12882  -0.11295 740 GLN A C     
6117 O O     . GLN B 740 ? 1.26758 1.32907 1.74338 -0.02965 0.13858  -0.12682 740 GLN A O     
6118 C CB    . GLN B 740 ? 1.14132 1.20839 1.54139 -0.03955 0.12302  -0.11474 740 GLN A CB    
6119 C CG    . GLN B 740 ? 1.26527 1.34393 1.67024 -0.03911 0.12417  -0.10194 740 GLN A CG    
6120 C CD    . GLN B 740 ? 1.21164 1.29314 1.58967 -0.04126 0.13046  -0.10634 740 GLN A CD    
6121 O OE1   . GLN B 740 ? 1.15813 1.23306 1.51265 -0.04317 0.13441  -0.11904 740 GLN A OE1   
6122 N NE2   . GLN B 740 ? 1.29463 1.38579 1.67575 -0.04141 0.13103  -0.09549 740 GLN A NE2   
6123 N N     . ASP B 741 ? 0.93932 1.01695 1.42426 -0.03112 0.12475  -0.09675 741 ASP A N     
6124 C CA    . ASP B 741 ? 1.12592 1.20895 1.64632 -0.02708 0.13116  -0.09322 741 ASP A CA    
6125 C C     . ASP B 741 ? 1.16235 1.23763 1.71217 -0.02367 0.13279  -0.10010 741 ASP A C     
6126 O O     . ASP B 741 ? 1.12294 1.19495 1.68907 -0.02025 0.14398  -0.11112 741 ASP A O     
6127 C CB    . ASP B 741 ? 1.25963 1.35383 1.79301 -0.02784 0.12399  -0.07351 741 ASP A CB    
6128 C CG    . ASP B 741 ? 1.28875 1.39001 1.79522 -0.03116 0.12308  -0.06724 741 ASP A CG    
6129 O OD1   . ASP B 741 ? 1.37456 1.47261 1.85230 -0.03273 0.12827  -0.07793 741 ASP A OD1   
6130 O OD2   . ASP B 741 ? 1.23705 1.34648 1.75108 -0.03254 0.11681  -0.05159 741 ASP A OD2   
6131 N N     . MET B 742 ? 1.03171 1.10355 1.58729 -0.02465 0.12261  -0.09442 742 MET A N     
6132 C CA    . MET B 742 ? 1.05267 1.11672 1.63735 -0.02174 0.12290  -0.10005 742 MET A CA    
6133 C C     . MET B 742 ? 0.95961 1.01130 1.53145 -0.02132 0.13159  -0.12177 742 MET A C     
6134 O O     . MET B 742 ? 1.00905 1.05580 1.60573 -0.01751 0.14028  -0.13096 742 MET A O     
6135 C CB    . MET B 742 ? 0.92636 0.98828 1.51365 -0.02371 0.11030  -0.09093 742 MET A CB    
6136 C CG    . MET B 742 ? 1.16636 1.23851 1.76886 -0.02431 0.10170  -0.06983 742 MET A CG    
6137 S SD    . MET B 742 ? 0.97348 1.04220 1.58587 -0.02587 0.08924  -0.06011 742 MET A SD    
6138 C CE    . MET B 742 ? 1.20222 1.28334 1.82857 -0.02710 0.08135  -0.03574 742 MET A CE    
6139 N N     . LEU B 743 ? 0.88234 0.92893 1.41676 -0.02529 0.12943  -0.12954 743 LEU A N     
6140 C CA    . LEU B 743 ? 0.93662 0.97022 1.45486 -0.02616 0.13604  -0.15007 743 LEU A CA    
6141 C C     . LEU B 743 ? 0.95888 0.99191 1.48298 -0.02311 0.15153  -0.16119 743 LEU A C     
6142 O O     . LEU B 743 ? 1.15098 1.17373 1.68816 -0.02084 0.15929  -0.17541 743 LEU A O     
6143 C CB    . LEU B 743 ? 0.92181 0.95232 1.39734 -0.03148 0.13111  -0.15428 743 LEU A CB    
6144 C CG    . LEU B 743 ? 0.88201 0.91223 1.34980 -0.03460 0.11695  -0.14473 743 LEU A CG    
6145 C CD1   . LEU B 743 ? 0.93427 0.96227 1.36144 -0.03961 0.11328  -0.14870 743 LEU A CD1   
6146 C CD2   . LEU B 743 ? 0.91084 0.93114 1.39834 -0.03399 0.11251  -0.15004 743 LEU A CD2   
6147 N N     . ASN B 744 ? 0.99385 1.03721 1.50950 -0.02307 0.15617  -0.15488 744 ASN A N     
6148 C CA    . ASN B 744 ? 1.10955 1.15319 1.62913 -0.02037 0.17197  -0.16512 744 ASN A CA    
6149 C C     . ASN B 744 ? 1.10611 1.14951 1.67131 -0.01456 0.17889  -0.16532 744 ASN A C     
6150 O O     . ASN B 744 ? 1.10590 1.14121 1.67718 -0.01198 0.19219  -0.18111 744 ASN A O     
6151 C CB    . ASN B 744 ? 0.93085 0.98667 1.43615 -0.02160 0.17433  -0.15604 744 ASN A CB    
6152 C CG    . ASN B 744 ? 0.90776 0.96122 1.36731 -0.02682 0.17224  -0.16127 744 ASN A CG    
6153 O OD1   . ASN B 744 ? 1.04199 1.10275 1.48516 -0.02982 0.16321  -0.14905 744 ASN A OD1   
6154 N ND2   . ASN B 744 ? 1.00069 1.04361 1.43902 -0.02821 0.18049  -0.17919 744 ASN A ND2   
6155 N N     . GLU B 745 ? 1.08700 1.13846 1.68277 -0.01277 0.17042  -0.14843 745 GLU A N     
6156 C CA    . GLU B 745 ? 0.97860 1.03124 1.62157 -0.00728 0.17579  -0.14588 745 GLU A CA    
6157 C C     . GLU B 745 ? 0.97401 1.01227 1.63110 -0.00552 0.17715  -0.15901 745 GLU A C     
6158 O O     . GLU B 745 ? 1.06814 1.10141 1.75141 -0.00097 0.18906  -0.16865 745 GLU A O     
6159 C CB    . GLU B 745 ? 0.97129 1.03557 1.64015 -0.00702 0.16411  -0.12335 745 GLU A CB    
6160 C CG    . GLU B 745 ? 1.50547 1.58315 2.16050 -0.00946 0.16091  -0.10937 745 GLU A CG    
6161 C CD    . GLU B 745 ? 1.66503 1.75154 2.33125 -0.01147 0.14634  -0.08793 745 GLU A CD    
6162 O OE1   . GLU B 745 ? 1.56705 1.65005 2.25298 -0.01079 0.13896  -0.08321 745 GLU A OE1   
6163 O OE2   . GLU B 745 ? 1.70979 1.80619 2.36417 -0.01403 0.14241  -0.07602 745 GLU A OE2   
6164 N N     . LEU B 746 ? 1.05297 1.08459 1.69455 -0.00898 0.16570  -0.15934 746 LEU A N     
6165 C CA    . LEU B 746 ? 1.03017 1.04807 1.68748 -0.00780 0.16496  -0.17020 746 LEU A CA    
6166 C C     . LEU B 746 ? 0.99954 1.00378 1.64370 -0.00707 0.17908  -0.19399 746 LEU A C     
6167 O O     . LEU B 746 ? 1.06411 1.06579 1.66903 -0.01065 0.18266  -0.20320 746 LEU A O     
6168 C CB    . LEU B 746 ? 0.91536 0.92949 1.55510 -0.01232 0.15000  -0.16571 746 LEU A CB    
6169 C CG    . LEU B 746 ? 0.86910 0.89448 1.52496 -0.01287 0.13685  -0.14310 746 LEU A CG    
6170 C CD1   . LEU B 746 ? 1.02788 1.04854 1.66864 -0.01691 0.12392  -0.14003 746 LEU A CD1   
6171 C CD2   . LEU B 746 ? 0.86637 0.89492 1.57080 -0.00816 0.13768  -0.13451 746 LEU A CD2   
6172 N N     . PRO B 747 ? 1.06056 1.05533 1.73547 -0.00283 0.18721  -0.20422 747 PRO A N     
6173 C CA    . PRO B 747 ? 1.03756 1.01827 1.70086 -0.00201 0.20208  -0.22741 747 PRO A CA    
6174 C C     . PRO B 747 ? 1.14062 1.10622 1.76757 -0.00759 0.19713  -0.24245 747 PRO A C     
6175 O O     . PRO B 747 ? 1.17397 1.12847 1.77611 -0.00908 0.20819  -0.26146 747 PRO A O     
6176 C CB    . PRO B 747 ? 1.03523 1.01059 1.74707 0.00412  0.20908  -0.23047 747 PRO A CB    
6177 C CG    . PRO B 747 ? 1.00568 0.98561 1.74256 0.00390  0.19273  -0.21351 747 PRO A CG    
6178 C CD    . PRO B 747 ? 1.06120 1.05792 1.78255 0.00107  0.18242  -0.19371 747 PRO A CD    
6179 N N     . GLU B 748 ? 1.27536 1.24031 1.89932 -0.01091 0.18086  -0.23394 748 GLU A N     
6180 C CA    . GLU B 748 ? 1.06364 1.01435 1.65650 -0.01668 0.17397  -0.24668 748 GLU A CA    
6181 C C     . GLU B 748 ? 1.11402 1.06655 1.65793 -0.02205 0.17388  -0.25064 748 GLU A C     
6182 O O     . GLU B 748 ? 1.10315 1.04251 1.61687 -0.02707 0.17218  -0.26515 748 GLU A O     
6183 C CB    . GLU B 748 ? 1.01750 0.96947 1.62195 -0.01871 0.15664  -0.23392 748 GLU A CB    
6184 C CG    . GLU B 748 ? 1.19255 1.14605 1.84700 -0.01359 0.15506  -0.22525 748 GLU A CG    
6185 C CD    . GLU B 748 ? 1.09723 1.06907 1.77426 -0.01099 0.14965  -0.20165 748 GLU A CD    
6186 O OE1   . GLU B 748 ? 1.11722 1.09173 1.82629 -0.00933 0.14150  -0.18954 748 GLU A OE1   
6187 O OE2   . GLU B 748 ? 1.17822 1.16135 1.83997 -0.01107 0.15324  -0.19519 748 GLU A OE2   
6188 N N     . PHE B 749 ? 1.26802 1.23583 1.80456 -0.02143 0.17511  -0.23805 749 PHE A N     
6189 C CA    . PHE B 749 ? 1.17754 1.14813 1.66873 -0.02669 0.17366  -0.23955 749 PHE A CA    
6190 C C     . PHE B 749 ? 1.16449 1.13309 1.64069 -0.02573 0.19075  -0.25262 749 PHE A C     
6191 O O     . PHE B 749 ? 1.23414 1.20769 1.67720 -0.02922 0.19179  -0.25191 749 PHE A O     
6192 C CB    . PHE B 749 ? 1.04892 1.03588 1.53778 -0.02753 0.16300  -0.21797 749 PHE A CB    
6193 C CG    . PHE B 749 ? 0.99966 0.98713 1.50045 -0.02889 0.14723  -0.20640 749 PHE A CG    
6194 C CD1   . PHE B 749 ? 1.01303 0.99308 1.48794 -0.03432 0.13690  -0.21010 749 PHE A CD1   
6195 C CD2   . PHE B 749 ? 1.14654 1.14205 1.68485 -0.02500 0.14273  -0.19127 749 PHE A CD2   
6196 C CE1   . PHE B 749 ? 1.07481 1.05571 1.56199 -0.03544 0.12340  -0.19919 749 PHE A CE1   
6197 C CE2   . PHE B 749 ? 1.10934 1.10531 1.65769 -0.02643 0.12918  -0.18052 749 PHE A CE2   
6198 C CZ    . PHE B 749 ? 1.03322 1.02203 1.55648 -0.03144 0.12001  -0.18460 749 PHE A CZ    
6199 N N     . GLU B 750 ? 1.37170 1.33340 1.87256 -0.02102 0.20438  -0.26386 750 GLU A N     
6200 C CA    . GLU B 750 ? 1.32763 1.28541 1.81274 -0.02026 0.22248  -0.27849 750 GLU A CA    
6201 C C     . GLU B 750 ? 1.44956 1.39183 1.88985 -0.02708 0.22177  -0.29614 750 GLU A C     
6202 O O     . GLU B 750 ? 1.66688 1.59772 2.10495 -0.02998 0.21170  -0.30138 750 GLU A O     
6203 C CB    . GLU B 750 ? 1.41452 1.36721 1.93840 -0.01346 0.23749  -0.28688 750 GLU A CB    
6204 C CG    . GLU B 750 ? 1.70140 1.65205 2.21543 -0.01156 0.25814  -0.29992 750 GLU A CG    
6205 C CD    . GLU B 750 ? 1.83850 1.76961 2.31805 -0.01563 0.26716  -0.32425 750 GLU A CD    
6206 O OE1   . GLU B 750 ? 1.76551 1.68097 2.25694 -0.01487 0.26867  -0.33716 750 GLU A OE1   
6207 O OE2   . GLU B 750 ? 1.98604 1.91711 2.42636 -0.01992 0.27239  -0.33018 750 GLU A OE2   
6208 N N     . ASP B 751 ? 1.43081 1.37279 1.83695 -0.03002 0.23116  -0.30410 751 ASP A N     
6209 C CA    . ASP B 751 ? 1.65334 1.58123 2.01306 -0.03772 0.22867  -0.31916 751 ASP A CA    
6210 C C     . ASP B 751 ? 1.46220 1.39400 1.80432 -0.04318 0.20778  -0.30706 751 ASP A C     
6211 O O     . ASP B 751 ? 1.54747 1.46587 1.86907 -0.04875 0.19936  -0.31652 751 ASP A O     
6212 C CB    . ASP B 751 ? 1.67133 1.57836 2.03247 -0.03816 0.23586  -0.34052 751 ASP A CB    
6213 C CG    . ASP B 751 ? 1.81956 1.71065 2.13188 -0.04619 0.23730  -0.35864 751 ASP A CG    
6214 O OD1   . ASP B 751 ? 2.04987 1.94223 2.33513 -0.04797 0.24892  -0.36468 751 ASP A OD1   
6215 O OD2   . ASP B 751 ? 1.76350 1.64103 2.06525 -0.05098 0.22639  -0.36609 751 ASP A OD2   
6216 N N     . TYR B 752 ? 1.36626 1.31534 1.71738 -0.04170 0.19982  -0.28683 752 TYR A N     
6217 C CA    . TYR B 752 ? 1.31624 1.27029 1.65190 -0.04633 0.18128  -0.27402 752 TYR A CA    
6218 C C     . TYR B 752 ? 1.44531 1.41670 1.77407 -0.04587 0.17978  -0.25764 752 TYR A C     
6219 O O     . TYR B 752 ? 1.57876 1.56198 1.93410 -0.04224 0.17405  -0.24100 752 TYR A O     
6220 C CB    . TYR B 752 ? 1.27185 1.22603 1.63945 -0.04416 0.16918  -0.26466 752 TYR A CB    
6221 C CG    . TYR B 752 ? 1.38072 1.32676 1.73101 -0.05009 0.15357  -0.26539 752 TYR A CG    
6222 C CD1   . TYR B 752 ? 1.57962 1.53475 1.91556 -0.05334 0.14036  -0.25076 752 TYR A CD1   
6223 C CD2   . TYR B 752 ? 1.19852 1.12750 1.54793 -0.05252 0.15215  -0.28062 752 TYR A CD2   
6224 C CE1   . TYR B 752 ? 1.67298 1.62144 1.99573 -0.05861 0.12638  -0.25057 752 TYR A CE1   
6225 C CE2   . TYR B 752 ? 1.22460 1.14655 1.56006 -0.05827 0.13723  -0.28052 752 TYR A CE2   
6226 C CZ    . TYR B 752 ? 1.51927 1.45146 1.84220 -0.06121 0.12439  -0.26510 752 TYR A CZ    
6227 O OH    . TYR B 752 ? 1.58632 1.51229 1.89811 -0.06672 0.10990  -0.26416 752 TYR A OH    
6228 N N     . VAL B 753 ? 1.51913 1.49160 1.81275 -0.04979 0.18457  -0.26196 753 VAL A N     
6229 C CA    . VAL B 753 ? 1.23671 1.22520 1.52388 -0.04937 0.18435  -0.24711 753 VAL A CA    
6230 C C     . VAL B 753 ? 1.12034 1.11665 1.40821 -0.05106 0.16713  -0.22991 753 VAL A C     
6231 O O     . VAL B 753 ? 1.19094 1.18086 1.45618 -0.05626 0.15643  -0.23180 753 VAL A O     
6232 C CB    . VAL B 753 ? 1.26364 1.25155 1.51156 -0.05393 0.19145  -0.25418 753 VAL A CB    
6233 C CG1   . VAL B 753 ? 1.23952 1.21812 1.44947 -0.06163 0.18107  -0.26003 753 VAL A CG1   
6234 C CG2   . VAL B 753 ? 1.47555 1.47954 1.72181 -0.05286 0.19287  -0.23957 753 VAL A CG2   
6235 N N     . VAL B 754 ? 1.12200 1.13126 1.43522 -0.04700 0.16480  -0.21373 754 VAL A N     
6236 C CA    . VAL B 754 ? 1.02780 1.04468 1.34063 -0.04848 0.14995  -0.19690 754 VAL A CA    
6237 C C     . VAL B 754 ? 1.04582 1.07157 1.33143 -0.05143 0.14928  -0.18938 754 VAL A C     
6238 O O     . VAL B 754 ? 1.24526 1.27692 1.53042 -0.04983 0.15991  -0.19000 754 VAL A O     
6239 C CB    . VAL B 754 ? 0.98618 1.01121 1.33765 -0.04356 0.14639  -0.18283 754 VAL A CB    
6240 C CG1   . VAL B 754 ? 0.99925 1.01580 1.38057 -0.04024 0.14853  -0.19033 754 VAL A CG1   
6241 C CG2   . VAL B 754 ? 1.28202 1.31941 1.64721 -0.04028 0.15376  -0.17365 754 VAL A CG2   
6242 N N     . LEU B 755 ? 1.02637 1.05264 1.29103 -0.05560 0.13758  -0.18277 755 LEU A N     
6243 C CA    . LEU B 755 ? 1.00124 1.03517 1.24018 -0.05860 0.13602  -0.17520 755 LEU A CA    
6244 C C     . LEU B 755 ? 0.96451 1.00668 1.21114 -0.05820 0.12489  -0.15750 755 LEU A C     
6245 O O     . LEU B 755 ? 1.17383 1.21264 1.43199 -0.05803 0.11602  -0.15395 755 LEU A O     
6246 C CB    . LEU B 755 ? 1.06054 1.08634 1.26321 -0.06464 0.13335  -0.18481 755 LEU A CB    
6247 C CG    . LEU B 755 ? 1.20419 1.22022 1.39325 -0.06616 0.14439  -0.20317 755 LEU A CG    
6248 C CD1   . LEU B 755 ? 1.40524 1.41245 1.55844 -0.07318 0.13830  -0.21087 755 LEU A CD1   
6249 C CD2   . LEU B 755 ? 1.18988 1.21279 1.37680 -0.06424 0.15805  -0.20432 755 LEU A CD2   
6250 N N     . THR B 756 ? 1.01456 1.06660 1.25491 -0.05823 0.12570  -0.14702 756 THR A N     
6251 C CA    . THR B 756 ? 1.00116 1.06016 1.24645 -0.05811 0.11620  -0.13066 756 THR A CA    
6252 C C     . THR B 756 ? 1.20634 1.26851 1.42194 -0.06200 0.11298  -0.12587 756 THR A C     
6253 O O     . THR B 756 ? 1.12007 1.18017 1.31378 -0.06458 0.11849  -0.13446 756 THR A O     
6254 C CB    . THR B 756 ? 1.06690 1.13462 1.33943 -0.05413 0.11914  -0.12051 756 THR A CB    
6255 O OG1   . THR B 756 ? 1.18419 1.25653 1.45758 -0.05481 0.10965  -0.10589 756 THR A OG1   
6256 C CG2   . THR B 756 ? 1.54983 1.62430 1.81763 -0.05378 0.12834  -0.12048 756 THR A CG2   
6257 N N     . GLN B 757 ? 1.09392 1.16044 1.30843 -0.06256 0.10471  -0.11267 757 GLN A N     
6258 C CA    . GLN B 757 ? 1.10563 1.17460 1.29343 -0.06611 0.10105  -0.10726 757 GLN A CA    
6259 C C     . GLN B 757 ? 1.51199 1.58970 1.69955 -0.06544 0.10564  -0.09948 757 GLN A C     
6260 O O     . GLN B 757 ? 1.53325 1.61602 1.74256 -0.06263 0.10576  -0.09133 757 GLN A O     
6261 C CB    . GLN B 757 ? 1.22002 1.28814 1.40725 -0.06694 0.09062  -0.09763 757 GLN A CB    
6262 C CG    . GLN B 757 ? 1.38471 1.45467 1.54759 -0.07017 0.08647  -0.09128 757 GLN A CG    
6263 C CD    . GLN B 757 ? 1.43576 1.50441 1.60005 -0.07056 0.07754  -0.08225 757 GLN A CD    
6264 O OE1   . GLN B 757 ? 1.60052 1.66371 1.76767 -0.07129 0.07247  -0.08561 757 GLN A OE1   
6265 N NE2   . GLN B 757 ? 1.27578 1.34909 1.43828 -0.07023 0.07577  -0.07067 757 GLN A NE2   
6266 N N     . GLN B 758 ? 1.62058 1.69987 1.78471 -0.06833 0.10870  -0.10143 758 GLN A N     
6267 C CA    . GLN B 758 ? 1.69127 1.77871 1.85389 -0.06833 0.11234  -0.09359 758 GLN A CA    
6268 C C     . GLN B 758 ? 1.72053 1.80934 1.86432 -0.07119 0.10507  -0.08395 758 GLN A C     
6269 O O     . GLN B 758 ? 1.58757 1.67120 1.71665 -0.07340 0.09934  -0.08573 758 GLN A O     
6270 C CB    . GLN B 758 ? 1.70966 1.79863 1.86304 -0.06916 0.12270  -0.10228 758 GLN A CB    
6271 C CG    . GLN B 758 ? 1.75300 1.83536 1.87986 -0.07285 0.12374  -0.11307 758 GLN A CG    
6272 C CD    . GLN B 758 ? 1.74480 1.81892 1.87707 -0.07207 0.12643  -0.12613 758 GLN A CD    
6273 O OE1   . GLN B 758 ? 1.66850 1.74174 1.82622 -0.06831 0.12776  -0.12736 758 GLN A OE1   
6274 N NE2   . GLN B 758 ? 1.91656 1.98402 2.02463 -0.07600 0.12682  -0.13587 758 GLN A NE2   
6275 N N     . GLN B 759 ? 1.83095 1.92606 1.97595 -0.07130 0.10516  -0.07409 759 GLN A N     
6276 C CA    . GLN B 759 ? 1.84700 1.94248 1.97550 -0.07377 0.09874  -0.06482 759 GLN A CA    
6277 C C     . GLN B 759 ? 1.84870 1.94100 1.95074 -0.07730 0.09829  -0.07005 759 GLN A C     
6278 O O     . GLN B 759 ? 1.75771 1.84609 1.84949 -0.07875 0.09153  -0.06731 759 GLN A O     
6279 C CB    . GLN B 759 ? 1.55630 1.65819 1.68693 -0.07423 0.09991  -0.05544 759 GLN A CB    
6280 C CG    . GLN B 759 ? 1.47753 1.58194 1.62950 -0.07216 0.09673  -0.04629 759 GLN A CG    
6281 C CD    . GLN B 759 ? 1.72143 1.82775 1.89934 -0.06889 0.10095  -0.05021 759 GLN A CD    
6282 O OE1   . GLN B 759 ? 1.80026 1.91050 1.98554 -0.06809 0.10822  -0.05457 759 GLN A OE1   
6283 N NE2   . GLN B 759 ? 1.67169 1.77525 1.86497 -0.06688 0.09681  -0.04839 759 GLN A NE2   
6284 N N     . ASN B 760 ? 1.82463 1.91865 1.91687 -0.07873 0.10535  -0.07683 760 ASN A N     
6285 C CA    . ASN B 760 ? 1.84806 1.93940 1.91372 -0.08281 0.10486  -0.08107 760 ASN A CA    
6286 C C     . ASN B 760 ? 1.82890 1.91668 1.88900 -0.08363 0.11137  -0.09453 760 ASN A C     
6287 O O     . ASN B 760 ? 1.69040 1.77844 1.76879 -0.08052 0.11733  -0.10008 760 ASN A O     
6288 C CB    . ASN B 760 ? 1.72770 1.82422 1.78039 -0.08509 0.10705  -0.07501 760 ASN A CB    
6289 C CG    . ASN B 760 ? 1.86723 1.96485 1.91843 -0.08545 0.10014  -0.06301 760 ASN A CG    
6290 O OD1   . ASN B 760 ? 1.83237 1.92703 1.89150 -0.08393 0.09414  -0.05896 760 ASN A OD1   
6291 N ND2   . ASN B 760 ? 1.80787 1.90921 1.84869 -0.08758 0.10126  -0.05734 760 ASN A ND2   
6292 N N     . GLN B 761 ? 1.82652 1.91066 1.86221 -0.08787 0.11030  -0.09944 761 GLN A N     
6293 C CA    . GLN B 761 ? 1.88570 1.96531 1.91099 -0.08968 0.11696  -0.11287 761 GLN A CA    
6294 C C     . GLN B 761 ? 1.73940 1.81279 1.78027 -0.08726 0.11650  -0.12112 761 GLN A C     
6295 O O     . GLN B 761 ? 1.62874 1.70161 1.68071 -0.08493 0.12578  -0.12945 761 GLN A O     
6296 C CB    . GLN B 761 ? 1.84759 1.93253 1.87505 -0.08878 0.12916  -0.11614 761 GLN A CB    
6297 C CG    . GLN B 761 ? 1.85662 1.94747 1.86826 -0.09167 0.13038  -0.10886 761 GLN A CG    
6298 C CD    . GLN B 761 ? 1.90024 1.99605 1.91270 -0.09134 0.14307  -0.11293 761 GLN A CD    
6299 O OE1   . GLN B 761 ? 1.70978 1.80446 1.73471 -0.08872 0.15192  -0.12173 761 GLN A OE1   
6300 N NE2   . GLN B 761 ? 2.05231 2.15357 2.05250 -0.09396 0.14449  -0.10641 761 GLN A NE2   
6301 N N     . ASN B 762 ? 1.75064 1.81938 1.79329 -0.08778 0.10647  -0.11883 762 ASN A N     
6302 C CA    . ASN B 762 ? 1.55220 1.61424 1.60908 -0.08609 0.10504  -0.12673 762 ASN A CA    
6303 C C     . ASN B 762 ? 1.62731 1.68084 1.66329 -0.09056 0.10613  -0.13990 762 ASN A C     
6304 O O     . ASN B 762 ? 1.42309 1.47105 1.44782 -0.09414 0.09663  -0.14024 762 ASN A O     
6305 C CB    . ASN B 762 ? 1.44969 1.51061 1.51927 -0.08478 0.09451  -0.11851 762 ASN A CB    
6306 C CG    . ASN B 762 ? 1.60052 1.66777 1.69439 -0.08003 0.09532  -0.10872 762 ASN A CG    
6307 O OD1   . ASN B 762 ? 1.48348 1.55172 1.59754 -0.07653 0.10099  -0.11197 762 ASN A OD1   
6308 N ND2   . ASN B 762 ? 1.64721 1.71828 1.73948 -0.08006 0.08974  -0.09670 762 ASN A ND2   
6309 N N     . TYR B 763 ? 1.66461 1.71702 1.69545 -0.09065 0.11740  -0.15005 763 TYR A N     
6310 C CA    . TYR B 763 ? 1.59488 1.63804 1.60270 -0.09548 0.11981  -0.16378 763 TYR A CA    
6311 C C     . TYR B 763 ? 1.72688 1.76268 1.75059 -0.09281 0.12544  -0.17611 763 TYR A C     
6312 O O     . TYR B 763 ? 1.55742 1.58421 1.56404 -0.09633 0.12968  -0.18957 763 TYR A O     
6313 C CB    . TYR B 763 ? 1.70252 1.74877 1.68933 -0.09814 0.12955  -0.16683 763 TYR A CB    
6314 C CG    . TYR B 763 ? 1.97786 2.03238 1.95335 -0.09996 0.12559  -0.15394 763 TYR A CG    
6315 C CD1   . TYR B 763 ? 1.97195 2.02673 1.94196 -0.10208 0.11261  -0.14424 763 TYR A CD1   
6316 C CD2   . TYR B 763 ? 1.96220 2.02408 1.93403 -0.09947 0.13514  -0.15134 763 TYR A CD2   
6317 C CE1   . TYR B 763 ? 2.04844 2.10976 2.00904 -0.10358 0.10943  -0.13295 763 TYR A CE1   
6318 C CE2   . TYR B 763 ? 1.90675 1.97543 1.86883 -0.10131 0.13135  -0.13979 763 TYR A CE2   
6319 C CZ    . TYR B 763 ? 2.06461 2.13263 2.02079 -0.10332 0.11854  -0.13087 763 TYR A CZ    
6320 O OH    . TYR B 763 ? 2.06979 2.14356 2.01713 -0.10499 0.11519  -0.11992 763 TYR A OH    
6321 N N     . LYS B 764 ? 1.67525 1.71416 1.73038 -0.08704 0.12542  -0.17163 764 LYS A N     
6322 C CA    . LYS B 764 ? 1.50987 1.54175 1.58443 -0.08399 0.13025  -0.18237 764 LYS A CA    
6323 C C     . LYS B 764 ? 1.45895 1.47976 1.52512 -0.08780 0.12027  -0.18890 764 LYS A C     
6324 O O     . LYS B 764 ? 1.40900 1.42083 1.48330 -0.08708 0.12389  -0.20089 764 LYS A O     
6325 C CB    . LYS B 764 ? 1.51782 1.55622 1.62845 -0.07750 0.13046  -0.17363 764 LYS A CB    
6326 C CG    . LYS B 764 ? 1.61608 1.66371 1.74113 -0.07345 0.14152  -0.16984 764 LYS A CG    
6327 C CD    . LYS B 764 ? 1.79186 1.84388 1.95406 -0.06751 0.14215  -0.16358 764 LYS A CD    
6328 C CE    . LYS B 764 ? 1.90998 1.97037 2.08851 -0.06386 0.15318  -0.16090 764 LYS A CE    
6329 N NZ    . LYS B 764 ? 1.94480 2.01429 2.10983 -0.06568 0.15247  -0.15056 764 LYS A NZ    
6330 N N     . ILE B 765 ? 1.49830 1.51957 1.55005 -0.09177 0.10809  -0.18103 765 ILE A N     
6331 C CA    . ILE B 765 ? 1.48349 1.49505 1.52858 -0.09594 0.09686  -0.18533 765 ILE A CA    
6332 C C     . ILE B 765 ? 1.48142 1.48150 1.50278 -0.10106 0.10143  -0.20214 765 ILE A C     
6333 O O     . ILE B 765 ? 1.65294 1.64260 1.67855 -0.10248 0.09799  -0.21150 765 ILE A O     
6334 C CB    . ILE B 765 ? 1.53992 1.55481 1.57203 -0.09965 0.08423  -0.17352 765 ILE A CB    
6335 C CG1   . ILE B 765 ? 1.69291 1.71947 1.73968 -0.09525 0.08343  -0.15779 765 ILE A CG1   
6336 C CG2   . ILE B 765 ? 1.45132 1.45865 1.48727 -0.10250 0.07165  -0.17416 765 ILE A CG2   
6337 C CD1   . ILE B 765 ? 1.48332 1.51272 1.56318 -0.08928 0.08288  -0.15221 765 ILE A CD1   
6338 N N     . VAL B 766 ? 1.67481 1.67636 1.67173 -0.10397 0.10907  -0.20573 766 VAL A N     
6339 C CA    . VAL B 766 ? 1.81590 1.80596 1.78584 -0.10957 0.11450  -0.22198 766 VAL A CA    
6340 C C     . VAL B 766 ? 1.70226 1.68551 1.69048 -0.10526 0.12603  -0.23532 766 VAL A C     
6341 O O     . VAL B 766 ? 1.68994 1.65980 1.66763 -0.10906 0.12495  -0.24880 766 VAL A O     
6342 C CB    . VAL B 766 ? 1.89811 1.89185 1.83945 -0.11323 0.12204  -0.22255 766 VAL A CB    
6343 C CG1   . VAL B 766 ? 1.72598 1.72771 1.65475 -0.11633 0.11136  -0.20772 766 VAL A CG1   
6344 C CG2   . VAL B 766 ? 1.77138 1.77258 1.72571 -0.10749 0.13860  -0.22364 766 VAL A CG2   
6345 N N     . GLN B 767 ? 1.57647 1.56815 1.59220 -0.09781 0.13587  -0.23129 767 GLN A N     
6346 C CA    . GLN B 767 ? 1.56944 1.55550 1.60574 -0.09309 0.14819  -0.24323 767 GLN A CA    
6347 C C     . GLN B 767 ? 1.55992 1.53557 1.61135 -0.09298 0.14002  -0.24895 767 GLN A C     
6348 O O     . GLN B 767 ? 1.71073 1.67613 1.76837 -0.09181 0.14857  -0.26343 767 GLN A O     
6349 C CB    . GLN B 767 ? 1.46094 1.45937 1.52908 -0.08523 0.15660  -0.23415 767 GLN A CB    
6350 C CG    . GLN B 767 ? 1.78302 1.79126 1.83948 -0.08510 0.16618  -0.22962 767 GLN A CG    
6351 C CD    . GLN B 767 ? 1.75560 1.77621 1.84433 -0.07806 0.17250  -0.21934 767 GLN A CD    
6352 O OE1   . GLN B 767 ? 1.69055 1.71017 1.80638 -0.07283 0.18107  -0.22417 767 GLN A OE1   
6353 N NE2   . GLN B 767 ? 1.62198 1.65401 1.70856 -0.07815 0.16782  -0.20474 767 GLN A NE2   
6354 N N     . GLN B 768 ? 1.45470 1.43246 1.51218 -0.09420 0.12456  -0.23819 768 GLN A N     
6355 C CA    . GLN B 768 ? 1.41363 1.38268 1.48918 -0.09388 0.11618  -0.24177 768 GLN A CA    
6356 C C     . GLN B 768 ? 1.71762 1.66978 1.77082 -0.09987 0.11704  -0.26024 768 GLN A C     
6357 O O     . GLN B 768 ? 1.96430 1.90705 2.03497 -0.09784 0.11968  -0.27016 768 GLN A O     
6358 C CB    . GLN B 768 ? 1.35106 1.32486 1.43125 -0.09545 0.09968  -0.22733 768 GLN A CB    
6359 C CG    . GLN B 768 ? 1.58251 1.54823 1.68154 -0.09560 0.09013  -0.22940 768 GLN A CG    
6360 C CD    . GLN B 768 ? 1.72833 1.70236 1.84547 -0.09382 0.07810  -0.21239 768 GLN A CD    
6361 O OE1   . GLN B 768 ? 1.70040 1.68581 1.81614 -0.09228 0.07694  -0.19916 768 GLN A OE1   
6362 N NE2   . GLN B 768 ? 1.74678 1.71473 1.88138 -0.09407 0.06949  -0.21272 768 GLN A NE2   
6363 N N     . PHE B 769 ? 1.64623 1.59419 1.66189 -0.10728 0.11480  -0.26460 769 PHE A N     
6364 C CA    . PHE B 769 ? 2.04655 1.97731 2.03581 -0.11446 0.11439  -0.28211 769 PHE A CA    
6365 C C     . PHE B 769 ? 2.03034 1.95736 1.99676 -0.11560 0.13139  -0.29473 769 PHE A C     
6366 O O     . PHE B 769 ? 1.83557 1.74905 1.77041 -0.12294 0.13218  -0.30861 769 PHE A O     
6367 C CB    . PHE B 769 ? 1.82205 1.74951 1.78616 -0.12309 0.09700  -0.27714 769 PHE A CB    
6368 C CG    . PHE B 769 ? 2.07356 1.98282 2.01836 -0.13091 0.09014  -0.29188 769 PHE A CG    
6369 C CD1   . PHE B 769 ? 2.07563 1.97285 2.03597 -0.12878 0.09543  -0.30566 769 PHE A CD1   
6370 C CD2   . PHE B 769 ? 2.08583 1.98967 1.99774 -0.14071 0.07765  -0.29148 769 PHE A CD2   
6371 C CE1   . PHE B 769 ? 2.03292 1.91242 1.97474 -0.13646 0.08860  -0.31948 769 PHE A CE1   
6372 C CE2   . PHE B 769 ? 2.13226 2.01891 2.02578 -0.14865 0.07021  -0.30462 769 PHE A CE2   
6373 C CZ    . PHE B 769 ? 2.07592 1.95008 1.98371 -0.14661 0.07572  -0.31895 769 PHE A CZ    
6374 N N     . ASN B 770 ? 1.94697 1.88545 1.92866 -0.10889 0.14465  -0.28986 770 ASN A N     
6375 C CA    . ASN B 770 ? 2.06514 2.00163 2.02870 -0.10919 0.16260  -0.30077 770 ASN A CA    
6376 C C     . ASN B 770 ? 2.16472 2.09101 2.14639 -0.10471 0.17673  -0.31662 770 ASN A C     
6377 O O     . ASN B 770 ? 2.09461 2.02946 2.10510 -0.09676 0.18889  -0.31359 770 ASN A O     
6378 C CB    . ASN B 770 ? 2.03083 1.98428 2.00161 -0.10479 0.17017  -0.28801 770 ASN A CB    
6379 C CG    . ASN B 770 ? 1.95372 1.91427 1.89763 -0.11051 0.16012  -0.27652 770 ASN A CG    
6380 O OD1   . ASN B 770 ? 1.95108 1.92466 1.89758 -0.10806 0.16433  -0.26565 770 ASN A OD1   
6381 N ND2   . ASN B 770 ? 1.95343 1.90555 1.87262 -0.11829 0.14646  -0.27831 770 ASN A ND2   
6382 N N     . ASN B 771 ? 2.36288 2.27133 2.32949 -0.10975 0.17471  -0.33248 771 ASN A N     
6383 C CA    . ASN B 771 ? 2.25637 2.15241 2.23839 -0.10596 0.18858  -0.34960 771 ASN A CA    
6384 C C     . ASN B 771 ? 2.24135 2.14272 2.27206 -0.09753 0.18567  -0.34215 771 ASN A C     
6385 O O     . ASN B 771 ? 2.21831 2.11285 2.27151 -0.09234 0.19800  -0.35295 771 ASN A O     
6386 C CB    . ASN B 771 ? 2.20372 2.10052 2.17790 -0.10336 0.21084  -0.35876 771 ASN A CB    
6387 C CG    . ASN B 771 ? 2.30718 2.18683 2.28449 -0.10208 0.22532  -0.37997 771 ASN A CG    
6388 O OD1   . ASN B 771 ? 2.33453 2.19634 2.28415 -0.10939 0.22175  -0.39464 771 ASN A OD1   
6389 N ND2   . ASN B 771 ? 2.26620 2.15044 2.27729 -0.09310 0.24144  -0.38183 771 ASN A ND2   
6390 N N     . PHE B 772 ? 2.09715 2.00985 2.14355 -0.09634 0.17025  -0.32430 772 PHE A N     
6391 C CA    . PHE B 772 ? 1.92626 1.84471 2.01764 -0.08901 0.16602  -0.31523 772 PHE A CA    
6392 C C     . PHE B 772 ? 1.83312 1.74443 1.92553 -0.09326 0.14753  -0.31289 772 PHE A C     
6393 O O     . PHE B 772 ? 1.83599 1.75612 1.95609 -0.08958 0.13772  -0.29849 772 PHE A O     
6394 C CB    . PHE B 772 ? 1.80509 1.74354 1.91517 -0.08362 0.16575  -0.29571 772 PHE A CB    
6395 C CG    . PHE B 772 ? 1.76232 1.70890 1.87232 -0.07988 0.18302  -0.29651 772 PHE A CG    
6396 C CD1   . PHE B 772 ? 1.83244 1.77104 1.94854 -0.07699 0.20047  -0.31186 772 PHE A CD1   
6397 C CD2   . PHE B 772 ? 1.85544 1.81731 1.96005 -0.07932 0.18208  -0.28190 772 PHE A CD2   
6398 C CE1   . PHE B 772 ? 1.87988 1.82658 1.99787 -0.07354 0.21658  -0.31183 772 PHE A CE1   
6399 C CE2   . PHE B 772 ? 1.84299 1.81257 1.94886 -0.07622 0.19736  -0.28200 772 PHE A CE2   
6400 C CZ    . PHE B 772 ? 1.97945 1.94189 2.09258 -0.07329 0.21462  -0.29662 772 PHE A CZ    
6401 N N     . ASP B 773 ? 2.00875 1.90416 2.07154 -0.10121 0.14284  -0.32658 773 ASP A N     
6402 C CA    . ASP B 773 ? 2.11661 2.00465 2.17807 -0.10651 0.12406  -0.32442 773 ASP A CA    
6403 C C     . ASP B 773 ? 1.96797 1.85318 2.07067 -0.10089 0.12142  -0.32367 773 ASP A C     
6404 O O     . ASP B 773 ? 1.98797 1.87591 2.10386 -0.10198 0.10589  -0.31284 773 ASP A O     
6405 C CB    . ASP B 773 ? 2.08051 1.95066 2.10293 -0.11648 0.12035  -0.34059 773 ASP A CB    
6406 C CG    . ASP B 773 ? 2.05816 1.91210 2.07227 -0.11660 0.13628  -0.36272 773 ASP A CG    
6407 O OD1   . ASP B 773 ? 1.93910 1.78552 1.98186 -0.11213 0.13984  -0.36978 773 ASP A OD1   
6408 O OD2   . ASP B 773 ? 2.08928 1.93805 2.06856 -0.12117 0.14548  -0.37262 773 ASP A OD2   
6409 N N     . LYS B 774 ? 1.83118 1.71091 1.95431 -0.09523 0.13608  -0.33450 774 LYS A N     
6410 C CA    . LYS B 774 ? 1.92259 1.79798 2.08532 -0.09033 0.13350  -0.33475 774 LYS A CA    
6411 C C     . LYS B 774 ? 1.92449 1.81610 2.12703 -0.08056 0.14008  -0.32066 774 LYS A C     
6412 O O     . LYS B 774 ? 2.12383 2.01387 2.36251 -0.07579 0.13876  -0.31876 774 LYS A O     
6413 C CB    . LYS B 774 ? 2.03525 1.89084 2.19602 -0.09117 0.14397  -0.35729 774 LYS A CB    
6414 C CG    . LYS B 774 ? 1.95802 1.81482 2.13554 -0.08375 0.16539  -0.36502 774 LYS A CG    
6415 C CD    . LYS B 774 ? 1.87721 1.71670 2.07410 -0.08149 0.17324  -0.38214 774 LYS A CD    
6416 C CE    . LYS B 774 ? 1.95507 1.79820 2.17948 -0.07265 0.19332  -0.38613 774 LYS A CE    
6417 N NZ    . LYS B 774 ? 1.83380 1.69788 2.09373 -0.06508 0.19198  -0.36515 774 LYS A NZ    
6418 N N     . ALA B 775 ? 1.62412 1.53052 1.82061 -0.07814 0.14603  -0.31058 775 ALA A N     
6419 C CA    . ALA B 775 ? 1.49655 1.41772 1.72955 -0.06951 0.15254  -0.29771 775 ALA A CA    
6420 C C     . ALA B 775 ? 1.43923 1.37786 1.66380 -0.06931 0.14811  -0.27982 775 ALA A C     
6421 O O     . ALA B 775 ? 1.70577 1.65020 1.91523 -0.06888 0.15870  -0.28088 775 ALA A O     
6422 C CB    . ALA B 775 ? 1.61195 1.53000 1.85474 -0.06478 0.17224  -0.30964 775 ALA A CB    
6423 N N     . ILE B 776 ? 1.32147 1.26794 1.55652 -0.06947 0.13368  -0.26394 776 ILE A N     
6424 C CA    . ILE B 776 ? 1.27002 1.23204 1.49705 -0.06941 0.12891  -0.24676 776 ILE A CA    
6425 C C     . ILE B 776 ? 1.13426 1.10477 1.38947 -0.06634 0.11782  -0.22968 776 ILE A C     
6426 O O     . ILE B 776 ? 1.34576 1.30908 1.60962 -0.06806 0.10800  -0.23050 776 ILE A O     
6427 C CB    . ILE B 776 ? 1.53874 1.49839 1.72528 -0.07701 0.12134  -0.24781 776 ILE A CB    
6428 C CG1   . ILE B 776 ? 1.67071 1.62248 1.82662 -0.08065 0.13244  -0.26357 776 ILE A CG1   
6429 C CG2   . ILE B 776 ? 1.68781 1.66223 1.86895 -0.07680 0.11537  -0.22985 776 ILE A CG2   
6430 C CD1   . ILE B 776 ? 1.74798 1.70281 1.91800 -0.07493 0.15038  -0.26922 776 ILE A CD1   
6431 N N     . LEU B 777 ? 1.08074 1.06552 1.34883 -0.06242 0.11923  -0.21479 777 LEU A N     
6432 C CA    . LEU B 777 ? 1.01791 1.01094 1.30870 -0.06013 0.10899  -0.19768 777 LEU A CA    
6433 C C     . LEU B 777 ? 1.12425 1.12979 1.40079 -0.06084 0.10609  -0.18335 777 LEU A C     
6434 O O     . LEU B 777 ? 1.30059 1.31627 1.59331 -0.05680 0.11060  -0.17370 777 LEU A O     
6435 C CB    . LEU B 777 ? 1.04562 1.04201 1.37589 -0.05383 0.11397  -0.19364 777 LEU A CB    
6436 C CG    . LEU B 777 ? 1.11578 1.09970 1.46457 -0.05230 0.11809  -0.20761 777 LEU A CG    
6437 C CD1   . LEU B 777 ? 1.52179 1.51106 1.90962 -0.04574 0.12468  -0.20235 777 LEU A CD1   
6438 C CD2   . LEU B 777 ? 1.40618 1.38211 1.75820 -0.05533 0.10545  -0.20762 777 LEU A CD2   
6439 N N     . LEU B 778 ? 1.06634 1.07086 1.31443 -0.06599 0.09853  -0.18185 778 LEU A N     
6440 C CA    . LEU B 778 ? 1.10800 1.12319 1.34067 -0.06688 0.09644  -0.16940 778 LEU A CA    
6441 C C     . LEU B 778 ? 0.97050 0.99389 1.22308 -0.06429 0.08885  -0.15224 778 LEU A C     
6442 O O     . LEU B 778 ? 1.06422 1.08414 1.32291 -0.06557 0.07938  -0.14870 778 LEU A O     
6443 C CB    . LEU B 778 ? 1.11539 1.12655 1.31391 -0.07314 0.09046  -0.17264 778 LEU A CB    
6444 C CG    . LEU B 778 ? 1.18792 1.20848 1.36863 -0.07454 0.08823  -0.16107 778 LEU A CG    
6445 C CD1   . LEU B 778 ? 1.35663 1.38491 1.53759 -0.07176 0.09932  -0.15976 778 LEU A CD1   
6446 C CD2   . LEU B 778 ? 1.31485 1.33054 1.46301 -0.08095 0.08285  -0.16548 778 LEU A CD2   
6447 N N     . GLY B 779 ? 0.89161 0.92518 1.15345 -0.06115 0.09288  -0.14193 779 GLY A N     
6448 C CA    . GLY B 779 ? 0.88451 0.92546 1.16119 -0.05935 0.08623  -0.12544 779 GLY A CA    
6449 C C     . GLY B 779 ? 1.15767 1.20521 1.41230 -0.06149 0.08381  -0.11611 779 GLY A C     
6450 O O     . GLY B 779 ? 1.34464 1.39668 1.58859 -0.06147 0.09055  -0.11706 779 GLY A O     
6451 N N     . THR B 780 ? 1.44908 1.49708 1.69795 -0.06322 0.07498  -0.10734 780 THR A N     
6452 C CA    . THR B 780 ? 1.13817 1.19103 1.36507 -0.06541 0.07274  -0.09930 780 THR A CA    
6453 C C     . THR B 780 ? 1.16302 1.22026 1.39939 -0.06425 0.06700  -0.08450 780 THR A C     
6454 O O     . THR B 780 ? 1.20725 1.26319 1.46526 -0.06240 0.06373  -0.08097 780 THR A O     
6455 C CB    . THR B 780 ? 1.57598 1.62322 1.77817 -0.06992 0.06858  -0.10596 780 THR A CB    
6456 O OG1   . THR B 780 ? 1.91780 1.95851 2.13149 -0.07051 0.06233  -0.10908 780 THR A OG1   
6457 C CG2   . THR B 780 ? 1.51602 1.56001 1.70037 -0.07201 0.07535  -0.11898 780 THR A CG2   
6458 N N     . SER B 781 ? 1.31949 1.38134 1.54018 -0.06540 0.06623  -0.07611 781 SER A N     
6459 C CA    . SER B 781 ? 1.30356 1.36888 1.53046 -0.06449 0.06205  -0.06212 781 SER A CA    
6460 C C     . SER B 781 ? 1.53445 1.59764 1.74520 -0.06698 0.05644  -0.05848 781 SER A C     
6461 O O     . SER B 781 ? 1.81121 1.87301 2.03250 -0.06646 0.05155  -0.05234 781 SER A O     
6462 C CB    . SER B 781 ? 1.12056 1.19225 1.34561 -0.06363 0.06572  -0.05420 781 SER A CB    
6463 O OG    . SER B 781 ? 1.31189 1.38552 1.53983 -0.06330 0.06210  -0.04154 781 SER A OG    
6464 N N     . THR B 782 ? 1.46831 1.53156 1.65580 -0.06956 0.05729  -0.06140 782 THR A N     
6465 C CA    . THR B 782 ? 1.58482 1.64647 1.75816 -0.07191 0.05196  -0.05699 782 THR A CA    
6466 C C     . THR B 782 ? 1.64215 1.70028 1.79630 -0.07555 0.05074  -0.06650 782 THR A C     
6467 O O     . THR B 782 ? 1.44986 1.50973 1.58472 -0.07756 0.05146  -0.06466 782 THR A O     
6468 C CB    . THR B 782 ? 1.53693 1.60268 1.70073 -0.07163 0.05334  -0.04657 782 THR A CB    
6469 O OG1   . THR B 782 ? 1.62097 1.68976 1.80058 -0.06891 0.05556  -0.03982 782 THR A OG1   
6470 C CG2   . THR B 782 ? 1.45890 1.52309 1.61703 -0.07261 0.04845  -0.03925 782 THR A CG2   
6471 N N     . PHE B 783 ? 1.74282 1.79566 1.90120 -0.07677 0.04877  -0.07630 783 PHE A N     
6472 C CA    . PHE B 783 ? 1.78988 1.83807 1.92772 -0.08130 0.04643  -0.08544 783 PHE A CA    
6473 C C     . PHE B 783 ? 1.80489 1.84729 1.94918 -0.08344 0.03775  -0.08702 783 PHE A C     
6474 O O     . PHE B 783 ? 1.79701 1.83354 1.92869 -0.08759 0.03451  -0.09635 783 PHE A O     
6475 C CB    . PHE B 783 ? 1.66581 1.71257 1.79667 -0.08168 0.05404  -0.09741 783 PHE A CB    
6476 C CG    . PHE B 783 ? 1.78450 1.82530 1.92853 -0.08095 0.05578  -0.10852 783 PHE A CG    
6477 C CD1   . PHE B 783 ? 1.86493 1.90698 2.03543 -0.07658 0.05805  -0.10647 783 PHE A CD1   
6478 C CD2   . PHE B 783 ? 1.63075 1.66396 1.76011 -0.08500 0.05492  -0.12106 783 PHE A CD2   
6479 C CE1   . PHE B 783 ? 1.96337 1.99928 2.14702 -0.07583 0.05975  -0.11677 783 PHE A CE1   
6480 C CE2   . PHE B 783 ? 1.63616 1.66251 1.77679 -0.08447 0.05690  -0.13209 783 PHE A CE2   
6481 C CZ    . PHE B 783 ? 1.81096 1.83869 1.97960 -0.07965 0.05947  -0.13000 783 PHE A CZ    
6482 N N     . PHE B 784 ? 1.65182 1.69571 1.81425 -0.08118 0.03378  -0.07754 784 PHE A N     
6483 C CA    . PHE B 784 ? 1.35064 1.38968 1.52370 -0.08296 0.02532  -0.07769 784 PHE A CA    
6484 C C     . PHE B 784 ? 1.37133 1.40683 1.52470 -0.08840 0.01848  -0.08047 784 PHE A C     
6485 O O     . PHE B 784 ? 1.65844 1.68803 1.81512 -0.09157 0.01134  -0.08536 784 PHE A O     
6486 C CB    . PHE B 784 ? 1.39323 1.43571 1.58502 -0.08008 0.02272  -0.06462 784 PHE A CB    
6487 C CG    . PHE B 784 ? 1.79547 1.84075 2.00854 -0.07553 0.02742  -0.06064 784 PHE A CG    
6488 C CD1   . PHE B 784 ? 1.66910 1.71718 1.88139 -0.07330 0.03496  -0.06350 784 PHE A CD1   
6489 C CD2   . PHE B 784 ? 1.62803 1.67352 1.86275 -0.07374 0.02401  -0.05302 784 PHE A CD2   
6490 C CE1   . PHE B 784 ? 1.48364 1.53445 1.71615 -0.06967 0.03813  -0.05873 784 PHE A CE1   
6491 C CE2   . PHE B 784 ? 1.46091 1.50898 1.71453 -0.07013 0.02768  -0.04848 784 PHE A CE2   
6492 C CZ    . PHE B 784 ? 1.61768 1.66835 1.87012 -0.06822 0.03433  -0.05119 784 PHE A CZ    
6493 N N     . GLU B 785 ? 1.35686 1.39564 1.49093 -0.08983 0.01988  -0.07687 785 GLU A N     
6494 C CA    . GLU B 785 ? 1.27495 1.31069 1.38934 -0.09551 0.01302  -0.07878 785 GLU A CA    
6495 C C     . GLU B 785 ? 1.69332 1.72849 1.78311 -0.09821 0.01818  -0.08721 785 GLU A C     
6496 O O     . GLU B 785 ? 1.79224 1.83218 1.87947 -0.09516 0.02667  -0.08597 785 GLU A O     
6497 C CB    . GLU B 785 ? 1.46216 1.50177 1.57633 -0.09551 0.00873  -0.06582 785 GLU A CB    
6498 C CG    . GLU B 785 ? 1.53175 1.57758 1.64787 -0.09101 0.01615  -0.05716 785 GLU A CG    
6499 C CD    . GLU B 785 ? 1.56640 1.61463 1.68560 -0.09049 0.01264  -0.04485 785 GLU A CD    
6500 O OE1   . GLU B 785 ? 1.65410 1.70158 1.75987 -0.09425 0.00765  -0.04330 785 GLU A OE1   
6501 O OE2   . GLU B 785 ? 1.47250 1.52308 1.60759 -0.08649 0.01507  -0.03670 785 GLU A OE2   
6502 N N     . GLY B 786 ? 1.43883 1.46827 1.51112 -0.10409 0.01305  -0.09509 786 GLY A N     
6503 C CA    . GLY B 786 ? 1.61358 1.64200 1.66029 -0.10745 0.01791  -0.10299 786 GLY A CA    
6504 C C     . GLY B 786 ? 1.89512 1.91742 1.93891 -0.10816 0.02338  -0.11783 786 GLY A C     
6505 O O     . GLY B 786 ? 1.92173 1.94460 1.94980 -0.10882 0.03164  -0.12439 786 GLY A O     
6506 N N     . PHE B 787 ? 1.84190 1.85830 1.90093 -0.10802 0.01948  -0.12299 787 PHE A N     
6507 C CA    . PHE B 787 ? 1.67341 1.68281 1.73240 -0.10811 0.02560  -0.13786 787 PHE A CA    
6508 C C     . PHE B 787 ? 1.62696 1.62555 1.67766 -0.11439 0.01653  -0.14686 787 PHE A C     
6509 O O     . PHE B 787 ? 1.65224 1.64926 1.71613 -0.11552 0.00617  -0.14104 787 PHE A O     
6510 C CB    . PHE B 787 ? 1.58852 1.60041 1.67695 -0.10124 0.03139  -0.13672 787 PHE A CB    
6511 C CG    . PHE B 787 ? 1.71545 1.71838 1.81151 -0.10133 0.03436  -0.15071 787 PHE A CG    
6512 C CD1   . PHE B 787 ? 1.74253 1.74254 1.82873 -0.10098 0.04522  -0.16276 787 PHE A CD1   
6513 C CD2   . PHE B 787 ? 1.77723 1.77447 1.89142 -0.10165 0.02684  -0.15171 787 PHE A CD2   
6514 C CE1   . PHE B 787 ? 1.73010 1.72094 1.82377 -0.10083 0.04883  -0.17612 787 PHE A CE1   
6515 C CE2   . PHE B 787 ? 1.72846 1.71655 1.85001 -0.10177 0.02965  -0.16488 787 PHE A CE2   
6516 C CZ    . PHE B 787 ? 1.76189 1.74648 1.87307 -0.10125 0.04086  -0.17735 787 PHE A CZ    
6517 N N     . ASP B 788 ? 1.63048 1.62138 1.65968 -0.11867 0.02048  -0.16080 788 ASP A N     
6518 C CA    . ASP B 788 ? 1.68991 1.66855 1.70851 -0.12549 0.01199  -0.17121 788 ASP A CA    
6519 C C     . ASP B 788 ? 1.73006 1.70076 1.76092 -0.12293 0.01935  -0.18490 788 ASP A C     
6520 O O     . ASP B 788 ? 1.75897 1.72958 1.78383 -0.12041 0.03237  -0.19331 788 ASP A O     
6521 C CB    . ASP B 788 ? 1.69328 1.66712 1.67569 -0.13359 0.00939  -0.17685 788 ASP A CB    
6522 C CG    . ASP B 788 ? 1.87322 1.83342 1.83982 -0.14192 0.00017  -0.18798 788 ASP A CG    
6523 O OD1   . ASP B 788 ? 1.89037 1.84110 1.85744 -0.14193 0.00593  -0.20234 788 ASP A OD1   
6524 O OD2   . ASP B 788 ? 2.10644 2.06515 2.06030 -0.14860 -0.01284 -0.18218 788 ASP A OD2   
6525 N N     . PHE B 789 ? 1.67147 1.63580 1.72041 -0.12347 0.01150  -0.18668 789 PHE A N     
6526 C CA    . PHE B 789 ? 1.63856 1.59451 1.70234 -0.12087 0.01787  -0.19942 789 PHE A CA    
6527 C C     . PHE B 789 ? 1.75977 1.70040 1.80120 -0.12891 0.01338  -0.21503 789 PHE A C     
6528 O O     . PHE B 789 ? 1.92282 1.85673 1.96882 -0.13346 0.00043  -0.21470 789 PHE A O     
6529 C CB    . PHE B 789 ? 1.74875 1.70660 1.84816 -0.11640 0.01249  -0.19187 789 PHE A CB    
6530 C CG    . PHE B 789 ? 1.65922 1.61441 1.78280 -0.11033 0.02227  -0.19918 789 PHE A CG    
6531 C CD1   . PHE B 789 ? 1.60935 1.55534 1.72236 -0.11095 0.03225  -0.21600 789 PHE A CD1   
6532 C CD2   . PHE B 789 ? 1.46602 1.42773 1.62331 -0.10410 0.02176  -0.18887 789 PHE A CD2   
6533 C CE1   . PHE B 789 ? 1.55066 1.49431 1.68842 -0.10513 0.04129  -0.22210 789 PHE A CE1   
6534 C CE2   . PHE B 789 ? 1.44895 1.40848 1.62982 -0.09877 0.02995  -0.19449 789 PHE A CE2   
6535 C CZ    . PHE B 789 ? 1.43006 1.38066 1.60223 -0.09912 0.03962  -0.21100 789 PHE A CZ    
6536 N N     . GLN B 790 ? 1.71023 1.64507 1.72788 -0.13094 0.02384  -0.22835 790 GLN A N     
6537 C CA    . GLN B 790 ? 1.83912 1.75734 1.83305 -0.13891 0.02102  -0.24520 790 GLN A CA    
6538 C C     . GLN B 790 ? 1.86897 1.77887 1.87357 -0.13465 0.03478  -0.26073 790 GLN A C     
6539 O O     . GLN B 790 ? 1.76934 1.68432 1.77259 -0.12979 0.04997  -0.26377 790 GLN A O     
6540 C CB    . GLN B 790 ? 1.90993 1.82576 1.86282 -0.14649 0.02101  -0.24898 790 GLN A CB    
6541 C CG    . GLN B 790 ? 2.07202 1.96992 1.99630 -0.15589 0.01727  -0.26595 790 GLN A CG    
6542 C CD    . GLN B 790 ? 2.11597 2.00508 2.04865 -0.16127 0.00002  -0.26546 790 GLN A CD    
6543 O OE1   . GLN B 790 ? 2.06168 1.95610 1.99584 -0.16481 -0.01472 -0.25216 790 GLN A OE1   
6544 N NE2   . GLN B 790 ? 2.05322 1.92861 1.99288 -0.16193 0.00186  -0.27988 790 GLN A NE2   
6545 N N     . ALA B 791 ? 1.77948 1.67712 1.79588 -0.13638 0.02962  -0.26976 791 ALA A N     
6546 C CA    . ALA B 791 ? 1.73857 1.62748 1.76923 -0.13188 0.04255  -0.28441 791 ALA A CA    
6547 C C     . ALA B 791 ? 1.67295 1.54240 1.69430 -0.13884 0.03577  -0.30002 791 ALA A C     
6548 O O     . ALA B 791 ? 1.65494 1.52067 1.67529 -0.14474 0.01892  -0.29505 791 ALA A O     
6549 C CB    . ALA B 791 ? 1.61382 1.51255 1.68773 -0.12219 0.04578  -0.27436 791 ALA A CB    
6550 N N     . ASN B 792 ? 1.82656 1.68366 1.84217 -0.13819 0.04876  -0.31834 792 ASN A N     
6551 C CA    . ASN B 792 ? 1.85599 1.69227 1.86192 -0.14484 0.04374  -0.33542 792 ASN A CA    
6552 C C     . ASN B 792 ? 1.83536 1.66875 1.88352 -0.13841 0.04398  -0.33616 792 ASN A C     
6553 O O     . ASN B 792 ? 1.88139 1.70261 1.93520 -0.13620 0.05560  -0.35235 792 ASN A O     
6554 C CB    . ASN B 792 ? 1.90246 1.72479 1.87543 -0.14866 0.05765  -0.35595 792 ASN A CB    
6555 C CG    . ASN B 792 ? 1.98433 1.81492 1.96829 -0.13952 0.07897  -0.35818 792 ASN A CG    
6556 O OD1   . ASN B 792 ? 1.94074 1.78786 1.92472 -0.13579 0.08288  -0.34520 792 ASN A OD1   
6557 N ND2   . ASN B 792 ? 2.14641 1.96558 2.14083 -0.13590 0.09283  -0.37428 792 ASN A ND2   
6558 N N     . GLY B 793 ? 1.78889 1.63294 1.86603 -0.13549 0.03217  -0.31906 793 GLY A N     
6559 C CA    . GLY B 793 ? 1.79576 1.63836 1.91453 -0.12958 0.03133  -0.31741 793 GLY A CA    
6560 C C     . GLY B 793 ? 1.58767 1.44585 1.73490 -0.12583 0.02049  -0.29549 793 GLY A C     
6561 O O     . GLY B 793 ? 1.67662 1.54486 1.80948 -0.12858 0.01271  -0.28295 793 GLY A O     
6562 N N     . ILE B 794 ? 1.45146 1.31136 1.63783 -0.11979 0.02045  -0.29087 794 ILE A N     
6563 C CA    . ILE B 794 ? 1.48119 1.35529 1.69621 -0.11614 0.01089  -0.26991 794 ILE A CA    
6564 C C     . ILE B 794 ? 1.47335 1.36580 1.68712 -0.11059 0.01805  -0.25580 794 ILE A C     
6565 O O     . ILE B 794 ? 1.41858 1.31343 1.62659 -0.10652 0.03251  -0.26172 794 ILE A O     
6566 C CB    . ILE B 794 ? 1.41552 1.28773 1.67226 -0.11051 0.01154  -0.26828 794 ILE A CB    
6567 C CG1   . ILE B 794 ? 1.44095 1.32545 1.72488 -0.10817 0.00076  -0.24772 794 ILE A CG1   
6568 C CG2   . ILE B 794 ? 1.43713 1.31283 1.71085 -0.10207 0.02873  -0.27238 794 ILE A CG2   
6569 C CD1   . ILE B 794 ? 1.75685 1.63697 2.03273 -0.11609 -0.01667 -0.24352 794 ILE A CD1   
6570 N N     . LYS B 795 ? 1.38271 1.28710 1.60173 -0.11066 0.00844  -0.23803 795 LYS A N     
6571 C CA    . LYS B 795 ? 1.27062 1.19169 1.48874 -0.10569 0.01437  -0.22409 795 LYS A CA    
6572 C C     . LYS B 795 ? 1.22050 1.15255 1.47512 -0.09915 0.01258  -0.20781 795 LYS A C     
6573 O O     . LYS B 795 ? 1.39578 1.32552 1.66790 -0.10080 0.00176  -0.20220 795 LYS A O     
6574 C CB    . LYS B 795 ? 1.34932 1.27471 1.53885 -0.11148 0.00614  -0.21732 795 LYS A CB    
6575 C CG    . LYS B 795 ? 1.51054 1.42617 1.66156 -0.11833 0.00813  -0.23187 795 LYS A CG    
6576 C CD    . LYS B 795 ? 1.54094 1.45990 1.66543 -0.12495 -0.00217 -0.22454 795 LYS A CD    
6577 C CE    . LYS B 795 ? 1.91246 1.82194 1.99835 -0.13177 0.00078  -0.23863 795 LYS A CE    
6578 N NZ    . LYS B 795 ? 2.04083 1.93297 2.12192 -0.13557 0.00163  -0.25704 795 LYS A NZ    
6579 N N     . CYS B 796 ? 1.12156 1.06483 1.38703 -0.09241 0.02272  -0.20042 796 CYS A N     
6580 C CA    . CYS B 796 ? 1.06543 1.01907 1.36341 -0.08657 0.02155  -0.18453 796 CYS A CA    
6581 C C     . CYS B 796 ? 1.04118 1.00935 1.33224 -0.08366 0.02483  -0.17033 796 CYS A C     
6582 O O     . CYS B 796 ? 1.17169 1.14352 1.45080 -0.08158 0.03499  -0.17396 796 CYS A O     
6583 C CB    . CYS B 796 ? 1.07646 1.02852 1.40230 -0.08074 0.03041  -0.18873 796 CYS A CB    
6584 S SG    . CYS B 796 ? 1.26004 1.22480 1.62340 -0.07433 0.02893  -0.16856 796 CYS A SG    
6585 N N     . VAL B 797 ? 0.95821 0.93390 1.25684 -0.08363 0.01689  -0.15496 797 VAL A N     
6586 C CA    . VAL B 797 ? 0.90623 0.89487 1.19984 -0.08071 0.02010  -0.14103 797 VAL A CA    
6587 C C     . VAL B 797 ? 0.85951 0.85538 1.18413 -0.07558 0.02020  -0.12750 797 VAL A C     
6588 O O     . VAL B 797 ? 1.14843 1.14323 1.48905 -0.07646 0.01202  -0.12081 797 VAL A O     
6589 C CB    . VAL B 797 ? 0.89852 0.88998 1.17159 -0.08502 0.01221  -0.13400 797 VAL A CB    
6590 C CG1   . VAL B 797 ? 0.87741 0.88098 1.14954 -0.08178 0.01490  -0.11886 797 VAL A CG1   
6591 C CG2   . VAL B 797 ? 1.01654 1.00172 1.25716 -0.09049 0.01208  -0.14596 797 VAL A CG2   
6592 N N     . MET B 798 ? 0.86298 0.86580 1.19604 -0.07081 0.02885  -0.12334 798 MET A N     
6593 C CA    . MET B 798 ? 0.81353 0.82276 1.17534 -0.06647 0.02885  -0.11037 798 MET A CA    
6594 C C     . MET B 798 ? 0.82633 0.84628 1.18057 -0.06519 0.02936  -0.09521 798 MET A C     
6595 O O     . MET B 798 ? 0.96726 0.99198 1.30685 -0.06420 0.03580  -0.09539 798 MET A O     
6596 C CB    . MET B 798 ? 0.94390 0.95317 1.32452 -0.06225 0.03711  -0.11483 798 MET A CB    
6597 C CG    . MET B 798 ? 1.04385 1.04182 1.43693 -0.06273 0.03750  -0.12915 798 MET A CG    
6598 S SD    . MET B 798 ? 0.80496 0.80390 1.22879 -0.05694 0.04659  -0.13107 798 MET A SD    
6599 C CE    . MET B 798 ? 0.88063 0.86361 1.31522 -0.05852 0.04572  -0.14912 798 MET A CE    
6600 N N     . ILE B 799 ? 0.89234 0.91548 1.25640 -0.06533 0.02318  -0.08276 799 ILE A N     
6601 C CA    . ILE B 799 ? 0.85378 0.88593 1.21131 -0.06405 0.02432  -0.06830 799 ILE A CA    
6602 C C     . ILE B 799 ? 0.78098 0.81857 1.16016 -0.06013 0.02802  -0.05889 799 ILE A C     
6603 O O     . ILE B 799 ? 0.94299 0.98110 1.34329 -0.05926 0.02420  -0.05051 799 ILE A O     
6604 C CB    . ILE B 799 ? 0.99346 1.02621 1.35038 -0.06608 0.01708  -0.05937 799 ILE A CB    
6605 C CG1   . ILE B 799 ? 0.84729 0.87313 1.19077 -0.07058 0.01085  -0.06886 799 ILE A CG1   
6606 C CG2   . ILE B 799 ? 0.87952 0.91963 1.22345 -0.06527 0.01942  -0.04735 799 ILE A CG2   
6607 C CD1   . ILE B 799 ? 1.02529 1.05055 1.33879 -0.07292 0.01350  -0.07657 799 ILE A CD1   
6608 N N     . ALA B 800 ? 0.76078 0.80247 1.13519 -0.05823 0.03476  -0.05952 800 ALA A N     
6609 C CA    . ALA B 800 ? 0.77580 0.82262 1.17109 -0.05509 0.03751  -0.05046 800 ALA A CA    
6610 C C     . ALA B 800 ? 0.87188 0.92362 1.27191 -0.05496 0.03422  -0.03421 800 ALA A C     
6611 O O     . ALA B 800 ? 1.04106 1.09378 1.46483 -0.05356 0.03227  -0.02658 800 ALA A O     
6612 C CB    . ALA B 800 ? 0.84742 0.89877 1.23297 -0.05390 0.04432  -0.05195 800 ALA A CB    
6613 N N     . LYS B 801 ? 0.93268 0.98706 1.31082 -0.05644 0.03406  -0.02902 801 LYS A N     
6614 C CA    . LYS B 801 ? 0.91780 0.97620 1.29760 -0.05632 0.03258  -0.01394 801 LYS A CA    
6615 C C     . LYS B 801 ? 0.91657 0.97427 1.27607 -0.05829 0.03080  -0.01258 801 LYS A C     
6616 O O     . LYS B 801 ? 1.06977 1.12615 1.40914 -0.05969 0.03191  -0.02084 801 LYS A O     
6617 C CB    . LYS B 801 ? 0.83996 0.90390 1.21686 -0.05528 0.03671  -0.00590 801 LYS A CB    
6618 C CG    . LYS B 801 ? 1.26883 1.33602 1.65407 -0.05504 0.03574  0.00947  801 LYS A CG    
6619 C CD    . LYS B 801 ? 1.48016 1.54892 1.84203 -0.05633 0.03740  0.01643  801 LYS A CD    
6620 C CE    . LYS B 801 ? 1.22332 1.29389 1.56472 -0.05693 0.04099  0.01243  801 LYS A CE    
6621 N NZ    . LYS B 801 ? 1.25587 1.32628 1.57366 -0.05824 0.04241  0.01594  801 LYS A NZ    
6622 N N     . LEU B 802 ? 0.90773 0.96637 1.27334 -0.05839 0.02844  -0.00210 802 LEU A N     
6623 C CA    . LEU B 802 ? 0.75050 0.80860 1.10088 -0.05992 0.02687  0.00027  802 LEU A CA    
6624 C C     . LEU B 802 ? 0.88687 0.94721 1.21157 -0.06033 0.03126  0.00045  802 LEU A C     
6625 O O     . LEU B 802 ? 0.94553 1.00899 1.26727 -0.05933 0.03527  0.00598  802 LEU A O     
6626 C CB    . LEU B 802 ? 0.92078 0.98040 1.28354 -0.05934 0.02581  0.01311  802 LEU A CB    
6627 C CG    . LEU B 802 ? 0.83820 0.89553 1.22630 -0.05946 0.02056  0.01371  802 LEU A CG    
6628 C CD1   . LEU B 802 ? 0.74455 0.80415 1.14345 -0.05889 0.02079  0.02740  802 LEU A CD1   
6629 C CD2   . LEU B 802 ? 0.88371 0.93634 1.26955 -0.06174 0.01488  0.00301  802 LEU A CD2   
6630 N N     . PRO B 803 ? 0.84207 0.90082 1.14850 -0.06214 0.03007  -0.00478 803 PRO A N     
6631 C CA    . PRO B 803 ? 0.85183 0.91235 1.13472 -0.06270 0.03400  -0.00526 803 PRO A CA    
6632 C C     . PRO B 803 ? 0.91848 0.98090 1.19275 -0.06219 0.03677  0.00611  803 PRO A C     
6633 O O     . PRO B 803 ? 1.19846 1.26002 1.46003 -0.06324 0.03611  0.00707  803 PRO A O     
6634 C CB    . PRO B 803 ? 0.83696 0.89446 1.10653 -0.06522 0.03063  -0.01475 803 PRO A CB    
6635 C CG    . PRO B 803 ? 0.94440 0.99934 1.22809 -0.06608 0.02453  -0.01296 803 PRO A CG    
6636 C CD    . PRO B 803 ? 0.78370 0.83882 1.09216 -0.06413 0.02423  -0.00972 803 PRO A CD    
6637 N N     . PHE B 804 ? 0.81142 0.87593 1.09181 -0.06085 0.03989  0.01456  804 PHE A N     
6638 C CA    . PHE B 804 ? 0.77708 0.84210 1.04715 -0.06064 0.04355  0.02495  804 PHE A CA    
6639 C C     . PHE B 804 ? 0.83581 0.90177 1.08557 -0.06142 0.04725  0.02425  804 PHE A C     
6640 O O     . PHE B 804 ? 1.04975 1.11711 1.29782 -0.06176 0.04725  0.01740  804 PHE A O     
6641 C CB    . PHE B 804 ? 0.87563 0.94156 1.16137 -0.05959 0.04460  0.03519  804 PHE A CB    
6642 C CG    . PHE B 804 ? 0.90682 0.97193 1.21004 -0.05890 0.04231  0.03989  804 PHE A CG    
6643 C CD1   . PHE B 804 ? 1.09009 1.15436 1.38888 -0.05858 0.04498  0.04754  804 PHE A CD1   
6644 C CD2   . PHE B 804 ? 1.03651 1.10149 1.36174 -0.05856 0.03784  0.03685  804 PHE A CD2   
6645 C CE1   . PHE B 804 ? 1.10523 1.16941 1.42198 -0.05794 0.04318  0.05258  804 PHE A CE1   
6646 C CE2   . PHE B 804 ? 1.12819 1.19263 1.47052 -0.05824 0.03531  0.04174  804 PHE A CE2   
6647 C CZ    . PHE B 804 ? 1.03504 1.09952 1.37352 -0.05793 0.03797  0.04990  804 PHE A CZ    
6648 N N     . MET B 805 ? 0.98041 1.04530 1.21578 -0.06174 0.05068  0.03113  805 MET A N     
6649 C CA    . MET B 805 ? 0.80368 0.86873 1.01923 -0.06295 0.05380  0.03126  805 MET A CA    
6650 C C     . MET B 805 ? 0.91147 0.97604 1.12564 -0.06332 0.05655  0.04114  805 MET A C     
6651 O O     . MET B 805 ? 1.06507 1.12809 1.28592 -0.06262 0.05787  0.04858  805 MET A O     
6652 C CB    . MET B 805 ? 0.80536 0.86819 1.00195 -0.06368 0.05539  0.03014  805 MET A CB    
6653 C CG    . MET B 805 ? 0.91746 0.97730 1.11111 -0.06298 0.05847  0.03850  805 MET A CG    
6654 S SD    . MET B 805 ? 0.96413 1.02100 1.13527 -0.06381 0.06111  0.03771  805 MET A SD    
6655 C CE    . MET B 805 ? 0.95780 1.01632 1.13274 -0.06436 0.05540  0.02896  805 MET A CE    
6656 N N     . ASN B 806 ? 0.95119 1.01702 1.15722 -0.06472 0.05722  0.04147  806 ASN A N     
6657 C CA    . ASN B 806 ? 1.08689 1.15179 1.28966 -0.06613 0.05864  0.05106  806 ASN A CA    
6658 C C     . ASN B 806 ? 1.22275 1.28283 1.40366 -0.06733 0.06270  0.05541  806 ASN A C     
6659 O O     . ASN B 806 ? 1.34923 1.40796 1.51710 -0.06732 0.06387  0.05032  806 ASN A O     
6660 C CB    . ASN B 806 ? 0.92776 0.99589 1.13225 -0.06760 0.05682  0.05063  806 ASN A CB    
6661 C CG    . ASN B 806 ? 1.31599 1.38298 1.51690 -0.06993 0.05675  0.06100  806 ASN A CG    
6662 O OD1   . ASN B 806 ? 1.38296 1.44909 1.59377 -0.06972 0.05658  0.06810  806 ASN A OD1   
6663 N ND2   . ASN B 806 ? 1.48898 1.55566 1.67517 -0.07262 0.05660  0.06242  806 ASN A ND2   
6664 N N     . LYS B 807 ? 1.13270 1.18978 1.30939 -0.06852 0.06496  0.06448  807 LYS A N     
6665 C CA    . LYS B 807 ? 0.91036 0.96129 1.06571 -0.06968 0.06997  0.06836  807 LYS A CA    
6666 C C     . LYS B 807 ? 0.95319 1.00261 1.08863 -0.07234 0.06971  0.06576  807 LYS A C     
6667 O O     . LYS B 807 ? 1.06039 1.10400 1.17661 -0.07342 0.07364  0.06702  807 LYS A O     
6668 C CB    . LYS B 807 ? 0.79928 0.84668 0.95331 -0.07092 0.07282  0.07836  807 LYS A CB    
6669 C CG    . LYS B 807 ? 0.97116 1.01915 1.14254 -0.06839 0.07464  0.08228  807 LYS A CG    
6670 C CD    . LYS B 807 ? 1.14496 1.18860 1.31094 -0.06987 0.07916  0.09239  807 LYS A CD    
6671 C CE    . LYS B 807 ? 1.52261 1.56737 1.70700 -0.06735 0.08148  0.09684  807 LYS A CE    
6672 N NZ    . LYS B 807 ? 1.57451 1.61485 1.75199 -0.06895 0.08698  0.10669  807 LYS A NZ    
6673 N N     . HIS B 808 ? 0.99876 1.05301 1.13981 -0.07332 0.06555  0.06242  808 HIS A N     
6674 C CA    . HIS B 808 ? 1.08444 1.13818 1.20909 -0.07610 0.06480  0.06060  808 HIS A CA    
6675 C C     . HIS B 808 ? 0.99251 1.04993 1.11774 -0.07478 0.06400  0.05113  808 HIS A C     
6676 O O     . HIS B 808 ? 1.08912 1.15013 1.21372 -0.07616 0.06206  0.04829  808 HIS A O     
6677 C CB    . HIS B 808 ? 1.32209 1.37844 1.45188 -0.07884 0.06108  0.06577  808 HIS A CB    
6678 C CG    . HIS B 808 ? 1.29872 1.35116 1.42632 -0.08080 0.06142  0.07549  808 HIS A CG    
6679 N ND1   . HIS B 808 ? 1.38138 1.43633 1.52829 -0.07952 0.06001  0.08005  808 HIS A ND1   
6680 C CD2   . HIS B 808 ? 1.10175 1.14739 1.20920 -0.08430 0.06312  0.08149  808 HIS A CD2   
6681 C CE1   . HIS B 808 ? 1.33112 1.38144 1.46933 -0.08225 0.06096  0.08903  808 HIS A CE1   
6682 N NE2   . HIS B 808 ? 1.21501 1.25927 1.32844 -0.08527 0.06297  0.08971  808 HIS A NE2   
6683 N N     . ASN B 809 ? 1.03988 1.09655 1.16684 -0.07243 0.06537  0.04686  809 ASN A N     
6684 C CA    . ASN B 809 ? 0.91568 0.97497 1.03995 -0.07186 0.06449  0.03817  809 ASN A CA    
6685 C C     . ASN B 809 ? 1.11943 1.17412 1.22375 -0.07280 0.06710  0.03813  809 ASN A C     
6686 O O     . ASN B 809 ? 1.31243 1.36218 1.41230 -0.07215 0.06996  0.04282  809 ASN A O     
6687 C CB    . ASN B 809 ? 0.85240 0.91389 0.99227 -0.06943 0.06274  0.03325  809 ASN A CB    
6688 C CG    . ASN B 809 ? 1.48602 1.55154 1.64619 -0.06845 0.06026  0.03181  809 ASN A CG    
6689 O OD1   . ASN B 809 ? 1.58150 1.64807 1.75545 -0.06683 0.05840  0.02774  809 ASN A OD1   
6690 N ND2   . ASN B 809 ? 1.64735 1.71483 1.81053 -0.06962 0.05980  0.03534  809 ASN A ND2   
6691 N N     . ALA B 810 ? 0.96574 1.02188 1.05941 -0.07419 0.06663  0.03327  810 ALA A N     
6692 C CA    . ALA B 810 ? 0.78625 0.83779 0.86147 -0.07531 0.06883  0.03366  810 ALA A CA    
6693 C C     . ALA B 810 ? 0.90643 0.95509 0.98430 -0.07315 0.07014  0.03424  810 ALA A C     
6694 O O     . ALA B 810 ? 0.85185 0.89462 0.91957 -0.07317 0.07357  0.03828  810 ALA A O     
6695 C CB    . ALA B 810 ? 0.69651 0.75122 0.76360 -0.07683 0.06766  0.02791  810 ALA A CB    
6696 N N     . LYS B 811 ? 0.67963 0.73190 0.77143 -0.07147 0.06752  0.03045  811 LYS A N     
6697 C CA    . LYS B 811 ? 0.66249 0.71283 0.75937 -0.06977 0.06755  0.03153  811 LYS A CA    
6698 C C     . LYS B 811 ? 0.77730 0.82356 0.87900 -0.06822 0.07140  0.03914  811 LYS A C     
6699 O O     . LYS B 811 ? 0.97698 1.01873 1.07252 -0.06751 0.07483  0.04250  811 LYS A O     
6700 C CB    . LYS B 811 ? 0.79900 0.85348 0.91066 -0.06901 0.06302  0.02631  811 LYS A CB    
6701 C CG    . LYS B 811 ? 0.88214 0.93966 0.98711 -0.07075 0.06011  0.01832  811 LYS A CG    
6702 C CD    . LYS B 811 ? 1.07402 1.13350 1.19017 -0.07064 0.05553  0.01282  811 LYS A CD    
6703 C CE    . LYS B 811 ? 1.52827 1.58942 1.66237 -0.06926 0.05438  0.01184  811 LYS A CE    
6704 N NZ    . LYS B 811 ? 1.45769 1.51943 1.60132 -0.06965 0.04966  0.00582  811 LYS A NZ    
6705 N N     . TYR B 812 ? 0.77716 0.82475 0.88961 -0.06776 0.07129  0.04200  812 TYR A N     
6706 C CA    . TYR B 812 ? 0.65407 0.69793 0.77078 -0.06660 0.07544  0.04969  812 TYR A CA    
6707 C C     . TYR B 812 ? 0.82615 0.86343 0.92295 -0.06806 0.08057  0.05341  812 TYR A C     
6708 O O     . TYR B 812 ? 0.81546 0.84758 0.90947 -0.06682 0.08588  0.05782  812 TYR A O     
6709 C CB    . TYR B 812 ? 0.65125 0.69782 0.78082 -0.06670 0.07382  0.05258  812 TYR A CB    
6710 C CG    . TYR B 812 ? 0.76025 0.80364 0.89523 -0.06583 0.07795  0.06085  812 TYR A CG    
6711 C CD1   . TYR B 812 ? 0.81159 0.84969 0.93175 -0.06768 0.08224  0.06648  812 TYR A CD1   
6712 C CD2   . TYR B 812 ? 0.64283 0.68820 0.79723 -0.06358 0.07750  0.06315  812 TYR A CD2   
6713 C CE1   . TYR B 812 ? 0.90216 0.93695 1.02536 -0.06723 0.08681  0.07402  812 TYR A CE1   
6714 C CE2   . TYR B 812 ? 0.64983 0.69270 0.80963 -0.06284 0.08197  0.07118  812 TYR A CE2   
6715 C CZ    . TYR B 812 ? 0.70934 0.74689 0.85291 -0.06462 0.08704  0.07658  812 TYR A CZ    
6716 O OH    . TYR B 812 ? 0.82105 0.85569 0.96805 -0.06422 0.09224  0.08450  812 TYR A OH    
6717 N N     . TRP B 813 ? 0.77840 0.81546 0.86203 -0.07073 0.07927  0.05158  813 TRP A N     
6718 C CA    . TRP B 813 ? 0.68319 0.71292 0.74632 -0.07299 0.08330  0.05479  813 TRP A CA    
6719 C C     . TRP B 813 ? 0.80554 0.83019 0.85871 -0.07202 0.08712  0.05373  813 TRP A C     
6720 O O     . TRP B 813 ? 1.12478 1.14142 1.16614 -0.07237 0.09291  0.05745  813 TRP A O     
6721 C CB    . TRP B 813 ? 0.69560 0.72713 0.74905 -0.07633 0.07972  0.05275  813 TRP A CB    
6722 C CG    . TRP B 813 ? 0.82934 0.85303 0.86125 -0.07956 0.08233  0.05559  813 TRP A CG    
6723 C CD1   . TRP B 813 ? 1.00122 1.02132 1.01747 -0.08122 0.08298  0.05294  813 TRP A CD1   
6724 C CD2   . TRP B 813 ? 0.86490 0.88252 0.88771 -0.08202 0.08436  0.06170  813 TRP A CD2   
6725 N NE1   . TRP B 813 ? 0.93501 0.94682 0.93332 -0.08454 0.08513  0.05643  813 TRP A NE1   
6726 C CE2   . TRP B 813 ? 0.92249 0.93239 0.92331 -0.08529 0.08600  0.06173  813 TRP A CE2   
6727 C CE3   . TRP B 813 ? 0.81549 0.83313 0.84595 -0.08220 0.08470  0.06733  813 TRP A CE3   
6728 C CZ2   . TRP B 813 ? 1.21125 1.21280 1.19609 -0.08898 0.08784  0.06661  813 TRP A CZ2   
6729 C CZ3   . TRP B 813 ? 0.96441 0.97443 0.97904 -0.08584 0.08663  0.07279  813 TRP A CZ3   
6730 C CH2   . TRP B 813 ? 0.92424 0.92600 0.91560 -0.08933 0.08812  0.07215  813 TRP A CH2   
6731 N N     . LEU B 814 ? 0.81065 0.83929 0.86830 -0.07103 0.08415  0.04896  814 LEU A N     
6732 C CA    . LEU B 814 ? 0.89130 0.91564 0.94068 -0.07038 0.08683  0.04851  814 LEU A CA    
6733 C C     . LEU B 814 ? 0.79340 0.81764 0.85740 -0.06711 0.08882  0.05119  814 LEU A C     
6734 O O     . LEU B 814 ? 1.03943 1.06114 1.10117 -0.06622 0.09034  0.05142  814 LEU A O     
6735 C CB    . LEU B 814 ? 0.84463 0.87325 0.88924 -0.07189 0.08205  0.04287  814 LEU A CB    
6736 C CG    . LEU B 814 ? 0.82787 0.85728 0.85973 -0.07511 0.08028  0.04061  814 LEU A CG    
6737 C CD1   . LEU B 814 ? 0.87841 0.91269 0.90727 -0.07633 0.07642  0.03528  814 LEU A CD1   
6738 C CD2   . LEU B 814 ? 0.80803 0.82879 0.82227 -0.07697 0.08452  0.04380  814 LEU A CD2   
6739 N N     . MET B 815 ? 0.72107 0.74819 0.80097 -0.06551 0.08851  0.05370  815 MET A N     
6740 C CA    . MET B 815 ? 0.82591 0.85394 0.92272 -0.06261 0.08960  0.05677  815 MET A CA    
6741 C C     . MET B 815 ? 0.80800 0.83215 0.91018 -0.06096 0.09643  0.06348  815 MET A C     
6742 O O     . MET B 815 ? 0.94698 0.96984 1.06022 -0.05841 0.10019  0.06747  815 MET A O     
6743 C CB    . MET B 815 ? 0.95838 0.99394 1.07268 -0.06231 0.08219  0.05351  815 MET A CB    
6744 C CG    . MET B 815 ? 0.88278 0.92173 0.99368 -0.06375 0.07606  0.04741  815 MET A CG    
6745 S SD    . MET B 815 ? 0.90678 0.94467 1.02440 -0.06248 0.07539  0.05012  815 MET A SD    
6746 C CE    . MET B 815 ? 0.83683 0.88121 0.96322 -0.06439 0.06504  0.04379  815 MET A CE    
6747 N N     . ASP B 816 ? 0.76007 0.78249 0.85500 -0.06258 0.09800  0.06524  816 ASP A N     
6748 C CA    . ASP B 816 ? 0.74782 0.76675 0.84694 -0.06160 0.10435  0.07204  816 ASP A CA    
6749 C C     . ASP B 816 ? 0.91794 0.92873 1.00907 -0.06000 0.11382  0.07541  816 ASP A C     
6750 O O     . ASP B 816 ? 1.21325 1.22274 1.31552 -0.05770 0.11968  0.08087  816 ASP A O     
6751 C CB    . ASP B 816 ? 0.72263 0.73997 0.81126 -0.06458 0.10398  0.07389  816 ASP A CB    
6752 C CG    . ASP B 816 ? 0.91338 0.92989 1.01032 -0.06418 0.10775  0.08091  816 ASP A CG    
6753 O OD1   . ASP B 816 ? 1.23024 1.24784 1.34284 -0.06122 0.11116  0.08432  816 ASP A OD1   
6754 O OD2   . ASP B 816 ? 1.11259 1.12757 1.20083 -0.06709 0.10695  0.08356  816 ASP A OD2   
6755 N N     . SER B 817 ? 0.73128 0.73663 0.80486 -0.06107 0.11571  0.07238  817 SER A N     
6756 C CA    . SER B 817 ? 0.80276 0.79881 0.86770 -0.05954 0.12570  0.07497  817 SER A CA    
6757 C C     . SER B 817 ? 0.78178 0.78032 0.86349 -0.05604 0.12630  0.07576  817 SER A C     
6758 O O     . SER B 817 ? 0.98902 0.98044 1.06755 -0.05411 0.13472  0.07791  817 SER A O     
6759 C CB    . SER B 817 ? 1.10827 1.09654 1.14832 -0.06237 0.12735  0.07168  817 SER A CB    
6760 O OG    . SER B 817 ? 1.50930 1.50233 1.54777 -0.06351 0.11961  0.06659  817 SER A OG    
6761 N N     . GLU B 818 ? 0.84802 0.85577 0.94690 -0.05549 0.11764  0.07413  818 GLU A N     
6762 C CA    . GLU B 818 ? 0.91049 0.92112 1.02537 -0.05311 0.11599  0.07535  818 GLU A CA    
6763 C C     . GLU B 818 ? 0.92078 0.93694 1.06101 -0.05085 0.11503  0.08002  818 GLU A C     
6764 O O     . GLU B 818 ? 0.84776 0.86670 1.00464 -0.04903 0.11325  0.08249  818 GLU A O     
6765 C CB    . GLU B 818 ? 0.82976 0.84539 0.94081 -0.05531 0.10611  0.06949  818 GLU A CB    
6766 C CG    . GLU B 818 ? 0.94657 0.96165 1.06197 -0.05432 0.10513  0.07033  818 GLU A CG    
6767 C CD    . GLU B 818 ? 0.93224 0.94935 1.03465 -0.05729 0.09797  0.06470  818 GLU A CD    
6768 O OE1   . GLU B 818 ? 0.77878 0.79737 0.86881 -0.05980 0.09493  0.06005  818 GLU A OE1   
6769 O OE2   . GLU B 818 ? 1.07444 1.09195 1.18009 -0.05719 0.09543  0.06553  818 GLU A OE2   
6770 N N     . PHE B 819 ? 0.79567 0.81337 0.93953 -0.05124 0.11574  0.08185  819 PHE A N     
6771 C CA    . PHE B 819 ? 0.70373 0.72670 0.87251 -0.04939 0.11460  0.08668  819 PHE A CA    
6772 C C     . PHE B 819 ? 0.73246 0.75153 0.90033 -0.04858 0.12381  0.09257  819 PHE A C     
6773 O O     . PHE B 819 ? 0.89337 0.90883 1.04314 -0.05087 0.12555  0.09134  819 PHE A O     
6774 C CB    . PHE B 819 ? 0.68658 0.71713 0.86466 -0.05122 0.10340  0.08244  819 PHE A CB    
6775 C CG    . PHE B 819 ? 0.87080 0.90545 1.05080 -0.05246 0.09398  0.07667  819 PHE A CG    
6776 C CD1   . PHE B 819 ? 0.83932 0.87800 1.03929 -0.05159 0.08892  0.07853  819 PHE A CD1   
6777 C CD2   . PHE B 819 ? 0.95217 0.98663 1.11385 -0.05494 0.08994  0.06982  819 PHE A CD2   
6778 C CE1   . PHE B 819 ? 0.84127 0.88303 1.04064 -0.05354 0.07987  0.07347  819 PHE A CE1   
6779 C CE2   . PHE B 819 ? 0.99661 1.03453 1.15842 -0.05646 0.08192  0.06477  819 PHE A CE2   
6780 C CZ    . PHE B 819 ? 0.90497 0.94622 1.08452 -0.05595 0.07678  0.06648  819 PHE A CZ    
6781 N N     . THR B 820 ? 0.69196 0.71181 0.87903 -0.04574 0.12938  0.09934  820 THR A N     
6782 C CA    . THR B 820 ? 0.76562 0.78211 0.95284 -0.04509 0.13878  0.10573  820 THR A CA    
6783 C C     . THR B 820 ? 0.83849 0.86042 1.03247 -0.04708 0.13188  0.10616  820 THR A C     
6784 O O     . THR B 820 ? 1.26855 1.28683 1.44808 -0.04908 0.13539  0.10776  820 THR A O     
6785 C CB    . THR B 820 ? 0.73271 0.74964 0.94161 -0.04136 0.14660  0.11314  820 THR A CB    
6786 O OG1   . THR B 820 ? 1.03573 1.04681 1.23698 -0.03958 0.15316  0.11222  820 THR A OG1   
6787 C CG2   . THR B 820 ? 0.77580 0.78947 0.98537 -0.04071 0.15724  0.12020  820 THR A CG2   
6788 N N     . SER B 821 ? 0.70095 0.73079 0.91594 -0.04688 0.12204  0.10484  821 SER A N     
6789 C CA    . SER B 821 ? 0.86239 0.89722 1.08564 -0.04867 0.11476  0.10432  821 SER A CA    
6790 C C     . SER B 821 ? 0.82862 0.86745 1.04939 -0.05052 0.10335  0.09542  821 SER A C     
6791 O O     . SER B 821 ? 0.90596 0.94982 1.14485 -0.05015 0.09584  0.09346  821 SER A O     
6792 C CB    . SER B 821 ? 0.89888 0.93854 1.15003 -0.04708 0.11391  0.11061  821 SER A CB    
6793 O OG    . SER B 821 ? 0.85180 0.89564 1.11153 -0.04878 0.10678  0.10985  821 SER A OG    
6794 N N     . THR B 822 ? 0.82661 0.86302 1.02572 -0.05273 0.10220  0.09038  822 THR A N     
6795 C CA    . THR B 822 ? 0.94583 0.98574 1.14104 -0.05438 0.09299  0.08175  822 THR A CA    
6796 C C     . THR B 822 ? 0.92071 0.96663 1.13644 -0.05460 0.08495  0.07990  822 THR A C     
6797 O O     . THR B 822 ? 0.92431 0.97325 1.14587 -0.05504 0.07780  0.07396  822 THR A O     
6798 C CB    . THR B 822 ? 0.87153 0.90867 1.04398 -0.05684 0.09342  0.07834  822 THR A CB    
6799 O OG1   . THR B 822 ? 0.78891 0.81891 0.94441 -0.05668 0.10220  0.08173  822 THR A OG1   
6800 C CG2   . THR B 822 ? 0.92815 0.96763 1.09233 -0.05829 0.08686  0.06981  822 THR A CG2   
6801 N N     . PHE B 823 ? 0.91147 0.95856 1.13760 -0.05457 0.08592  0.08485  823 PHE A N     
6802 C CA    . PHE B 823 ? 0.84249 0.89458 1.08896 -0.05486 0.07816  0.08273  823 PHE A CA    
6803 C C     . PHE B 823 ? 0.78143 0.83596 1.04794 -0.05362 0.07437  0.08313  823 PHE A C     
6804 O O     . PHE B 823 ? 0.79909 0.85607 1.07240 -0.05460 0.06617  0.07613  823 PHE A O     
6805 C CB    . PHE B 823 ? 0.78290 0.83570 1.03908 -0.05504 0.08012  0.08970  823 PHE A CB    
6806 C CG    . PHE B 823 ? 0.89585 0.95302 1.17343 -0.05532 0.07233  0.08740  823 PHE A CG    
6807 C CD1   . PHE B 823 ? 1.03447 1.09397 1.33599 -0.05419 0.06974  0.09053  823 PHE A CD1   
6808 C CD2   . PHE B 823 ? 0.87508 0.93374 1.15002 -0.05673 0.06775  0.08221  823 PHE A CD2   
6809 C CE1   . PHE B 823 ? 0.91474 0.97710 1.23563 -0.05464 0.06258  0.08788  823 PHE A CE1   
6810 C CE2   . PHE B 823 ? 1.13145 1.19316 1.42672 -0.05675 0.06140  0.07961  823 PHE A CE2   
6811 C CZ    . PHE B 823 ? 1.22745 1.29058 1.54498 -0.05579 0.05874  0.08215  823 PHE A CZ    
6812 N N     . LYS B 824 ? 0.86776 0.92133 1.14329 -0.05180 0.08022  0.09107  824 LYS A N     
6813 C CA    . LYS B 824 ? 0.85671 0.91319 1.15520 -0.05088 0.07601  0.09326  824 LYS A CA    
6814 C C     . LYS B 824 ? 0.89557 0.95157 1.18815 -0.05109 0.07302  0.08918  824 LYS A C     
6815 O O     . LYS B 824 ? 0.89251 0.95116 1.20185 -0.05158 0.06593  0.08873  824 LYS A O     
6816 C CB    . LYS B 824 ? 0.74981 0.80607 1.06249 -0.04871 0.08413  0.10426  824 LYS A CB    
6817 C CG    . LYS B 824 ? 1.10512 1.16220 1.42558 -0.04889 0.08666  0.10983  824 LYS A CG    
6818 C CD    . LYS B 824 ? 0.89394 0.95054 1.22615 -0.04691 0.09619  0.12103  824 LYS A CD    
6819 C CE    . LYS B 824 ? 1.58027 1.63807 1.92092 -0.04761 0.09771  0.12718  824 LYS A CE    
6820 N NZ    . LYS B 824 ? 1.39977 1.46221 1.76302 -0.04853 0.08718  0.12520  824 LYS A NZ    
6821 N N     . GLU B 825 ? 0.80246 0.85501 1.07258 -0.05112 0.07757  0.08676  825 GLU A N     
6822 C CA    . GLU B 825 ? 0.69927 0.75127 0.96460 -0.05132 0.07514  0.08438  825 GLU A CA    
6823 C C     . GLU B 825 ? 0.74651 0.79890 0.99526 -0.05397 0.06807  0.07436  825 GLU A C     
6824 O O     . GLU B 825 ? 0.95047 1.00328 1.19692 -0.05502 0.06337  0.07180  825 GLU A O     
6825 C CB    . GLU B 825 ? 0.79665 0.84397 1.05080 -0.04932 0.08575  0.08930  825 GLU A CB    
6826 C CG    . GLU B 825 ? 0.84355 0.89002 1.11309 -0.04655 0.09462  0.09910  825 GLU A CG    
6827 C CD    . GLU B 825 ? 0.87805 0.91846 1.13547 -0.04445 0.10670  0.10312  825 GLU A CD    
6828 O OE1   . GLU B 825 ? 1.11651 1.15322 1.35383 -0.04524 0.10750  0.09842  825 GLU A OE1   
6829 O OE2   . GLU B 825 ? 0.94009 0.97907 1.20821 -0.04207 0.11576  0.11086  825 GLU A OE2   
6830 N N     . TYR B 826 ? 0.76157 0.81405 1.00018 -0.05516 0.06731  0.06948  826 TYR A N     
6831 C CA    . TYR B 826 ? 0.84906 0.90193 1.07127 -0.05748 0.06234  0.06021  826 TYR A CA    
6832 C C     . TYR B 826 ? 0.84455 0.89996 1.07204 -0.05875 0.05701  0.05419  826 TYR A C     
6833 O O     . TYR B 826 ? 0.85922 0.91630 1.09238 -0.06031 0.04955  0.04798  826 TYR A O     
6834 C CB    . TYR B 826 ? 0.79469 0.84412 0.99375 -0.05767 0.06868  0.05988  826 TYR A CB    
6835 C CG    . TYR B 826 ? 0.92183 0.97193 1.10403 -0.05998 0.06482  0.05151  826 TYR A CG    
6836 C CD1   . TYR B 826 ? 0.86021 0.91235 1.04285 -0.06162 0.05782  0.04570  826 TYR A CD1   
6837 C CD2   . TYR B 826 ? 0.72724 0.77588 0.89306 -0.06091 0.06806  0.04981  826 TYR A CD2   
6838 C CE1   . TYR B 826 ? 0.90614 0.95899 1.07309 -0.06381 0.05527  0.03834  826 TYR A CE1   
6839 C CE2   . TYR B 826 ? 0.87955 0.92937 1.03169 -0.06295 0.06514  0.04280  826 TYR A CE2   
6840 C CZ    . TYR B 826 ? 1.10265 1.15464 1.25522 -0.06424 0.05928  0.03697  826 TYR A CZ    
6841 O OH    . TYR B 826 ? 1.29030 1.34351 1.42898 -0.06634 0.05730  0.03028  826 TYR A OH    
6842 N N     . VAL B 827 ? 0.78580 0.84106 1.01151 -0.05836 0.06058  0.05594  827 VAL A N     
6843 C CA    . VAL B 827 ? 0.72691 0.78451 0.95822 -0.05935 0.05606  0.05010  827 VAL A CA    
6844 C C     . VAL B 827 ? 0.83639 0.89579 1.09051 -0.05926 0.04996  0.04889  827 VAL A C     
6845 O O     . VAL B 827 ? 1.01732 1.07749 1.27318 -0.06065 0.04422  0.04027  827 VAL A O     
6846 C CB    . VAL B 827 ? 0.67980 0.73723 0.90833 -0.05918 0.06015  0.05413  827 VAL A CB    
6847 C CG1   . VAL B 827 ? 0.83871 0.89348 1.04399 -0.06000 0.06522  0.05515  827 VAL A CG1   
6848 C CG2   . VAL B 827 ? 0.92706 0.98442 1.17114 -0.05787 0.06300  0.06336  827 VAL A CG2   
6849 N N     . LEU B 828 ? 0.70391 0.76356 0.97466 -0.05788 0.05135  0.05694  828 LEU A N     
6850 C CA    . LEU B 828 ? 0.78993 0.85109 1.08402 -0.05814 0.04496  0.05627  828 LEU A CA    
6851 C C     . LEU B 828 ? 0.78166 0.84249 1.07591 -0.05998 0.03773  0.05009  828 LEU A C     
6852 O O     . LEU B 828 ? 0.85482 0.91540 1.15439 -0.06170 0.03106  0.04212  828 LEU A O     
6853 C CB    . LEU B 828 ? 0.87721 0.93916 1.18983 -0.05644 0.04828  0.06713  828 LEU A CB    
6854 C CG    . LEU B 828 ? 0.78143 0.84490 1.12005 -0.05679 0.04204  0.06786  828 LEU A CG    
6855 C CD1   . LEU B 828 ? 0.92636 0.98997 1.26874 -0.05755 0.03849  0.06145  828 LEU A CD1   
6856 C CD2   . LEU B 828 ? 0.75636 0.82102 1.11137 -0.05504 0.04713  0.07988  828 LEU A CD2   
6857 N N     . PRO B 829 ? 0.81622 0.87655 1.10459 -0.06000 0.03855  0.05324  829 PRO A N     
6858 C CA    . PRO B 829 ? 0.85961 0.91962 1.14637 -0.06254 0.03066  0.04796  829 PRO A CA    
6859 C C     . PRO B 829 ? 0.81001 0.86904 1.07923 -0.06489 0.02727  0.03649  829 PRO A C     
6860 O O     . PRO B 829 ? 0.86717 0.92529 1.13920 -0.06762 0.01941  0.02942  829 PRO A O     
6861 C CB    . PRO B 829 ? 0.79573 0.85540 1.07559 -0.06162 0.03457  0.05428  829 PRO A CB    
6862 C CG    . PRO B 829 ? 0.70756 0.76742 0.99764 -0.05837 0.04315  0.06447  829 PRO A CG    
6863 C CD    . PRO B 829 ? 0.66262 0.72225 0.94741 -0.05780 0.04679  0.06231  829 PRO A CD    
6864 N N     . ASP B 830 ? 0.69281 0.75165 0.94412 -0.06414 0.03321  0.03464  830 ASP A N     
6865 C CA    . ASP B 830 ? 0.79023 0.84868 1.02487 -0.06615 0.03143  0.02427  830 ASP A CA    
6866 C C     . ASP B 830 ? 0.90000 0.95831 1.14568 -0.06675 0.02780  0.01720  830 ASP A C     
6867 O O     . ASP B 830 ? 1.00235 1.05926 1.24260 -0.06930 0.02279  0.00791  830 ASP A O     
6868 C CB    . ASP B 830 ? 0.94610 1.00475 1.16328 -0.06519 0.03841  0.02492  830 ASP A CB    
6869 C CG    . ASP B 830 ? 1.07899 1.13816 1.28318 -0.06669 0.03807  0.01546  830 ASP A CG    
6870 O OD1   . ASP B 830 ? 1.18821 1.24685 1.38165 -0.06908 0.03445  0.00893  830 ASP A OD1   
6871 O OD2   . ASP B 830 ? 1.20501 1.26523 1.41044 -0.06563 0.04147  0.01519  830 ASP A OD2   
6872 N N     . ALA B 831 ? 0.87886 0.93808 1.13932 -0.06466 0.03043  0.02155  831 ALA A N     
6873 C CA    . ALA B 831 ? 0.75358 0.81238 1.02702 -0.06483 0.02754  0.01537  831 ALA A CA    
6874 C C     . ALA B 831 ? 0.87673 0.93326 1.16152 -0.06701 0.01946  0.01062  831 ALA A C     
6875 O O     . ALA B 831 ? 0.90934 0.96353 1.19222 -0.06880 0.01599  0.00010  831 ALA A O     
6876 C CB    . ALA B 831 ? 0.81060 0.87089 1.10009 -0.06251 0.03088  0.02324  831 ALA A CB    
6877 N N     . VAL B 832 ? 0.87147 0.92830 1.16768 -0.06708 0.01670  0.01817  832 VAL A N     
6878 C CA    . VAL B 832 ? 0.89967 0.95422 1.20854 -0.06979 0.00764  0.01497  832 VAL A CA    
6879 C C     . VAL B 832 ? 0.81636 0.86827 1.10615 -0.07353 0.00261  0.00504  832 VAL A C     
6880 O O     . VAL B 832 ? 1.11818 1.16642 1.40996 -0.07624 -0.00325 -0.00433 832 VAL A O     
6881 C CB    . VAL B 832 ? 0.71959 0.77584 1.04394 -0.06924 0.00603  0.02628  832 VAL A CB    
6882 C CG1   . VAL B 832 ? 0.75370 0.80775 1.08877 -0.07289 -0.00458 0.02381  832 VAL A CG1   
6883 C CG2   . VAL B 832 ? 0.81977 0.87822 1.16328 -0.06605 0.01102  0.03576  832 VAL A CG2   
6884 N N     . THR B 833 ? 0.79992 0.85307 1.07122 -0.07388 0.00509  0.00687  833 THR A N     
6885 C CA    . THR B 833 ? 0.84799 0.89892 1.10015 -0.07790 0.00017  -0.00122 833 THR A CA    
6886 C C     . THR B 833 ? 0.91133 0.96026 1.15149 -0.07872 0.00223  -0.01322 833 THR A C     
6887 O O     . THR B 833 ? 1.12212 1.16722 1.35482 -0.08260 -0.00355 -0.02267 833 THR A O     
6888 C CB    . THR B 833 ? 0.94586 0.99877 1.18218 -0.07771 0.00321  0.00418  833 THR A CB    
6889 O OG1   . THR B 833 ? 1.16672 1.22147 1.39449 -0.07455 0.01241  0.00532  833 THR A OG1   
6890 C CG2   . THR B 833 ? 0.99150 1.04609 1.24138 -0.07662 0.00202  0.01594  833 THR A CG2   
6891 N N     . ARG B 834 ? 0.92569 0.97684 1.16397 -0.07547 0.01022  -0.01278 834 ARG A N     
6892 C CA    . ARG B 834 ? 0.86049 0.91051 1.08971 -0.07571 0.01343  -0.02344 834 ARG A CA    
6893 C C     . ARG B 834 ? 0.89559 0.94191 1.14077 -0.07632 0.00972  -0.03074 834 ARG A C     
6894 O O     . ARG B 834 ? 0.92837 0.97097 1.16429 -0.07870 0.00858  -0.04241 834 ARG A O     
6895 C CB    . ARG B 834 ? 0.83144 0.88509 1.05895 -0.07228 0.02178  -0.01946 834 ARG A CB    
6896 C CG    . ARG B 834 ? 1.02221 1.07819 1.23083 -0.07218 0.02582  -0.01475 834 ARG A CG    
6897 C CD    . ARG B 834 ? 1.19301 1.25034 1.38727 -0.07220 0.03095  -0.02088 834 ARG A CD    
6898 N NE    . ARG B 834 ? 1.53145 1.59092 1.73655 -0.06945 0.03565  -0.01877 834 ARG A NE    
6899 C CZ    . ARG B 834 ? 1.50866 1.57015 1.71791 -0.06739 0.03896  -0.00900 834 ARG A CZ    
6900 N NH1   . ARG B 834 ? 1.39494 1.45658 1.59344 -0.06747 0.04040  -0.00198 834 ARG A NH1   
6901 N NH2   . ARG B 834 ? 1.49534 1.55823 1.71903 -0.06548 0.04091  -0.00626 834 ARG A NH2   
6902 N N     . PHE B 835 ? 0.87502 0.92188 1.14309 -0.07437 0.00832  -0.02415 835 PHE A N     
6903 C CA    . PHE B 835 ? 0.95629 0.99926 1.24239 -0.07476 0.00470  -0.03032 835 PHE A CA    
6904 C C     . PHE B 835 ? 0.94348 0.98086 1.22535 -0.07949 -0.00403 -0.03794 835 PHE A C     
6905 O O     . PHE B 835 ? 1.24130 1.27330 1.52053 -0.08143 -0.00551 -0.05002 835 PHE A O     
6906 C CB    . PHE B 835 ? 0.88070 0.92604 1.19168 -0.07207 0.00459  -0.01934 835 PHE A CB    
6907 C CG    . PHE B 835 ? 0.80725 0.84891 1.14096 -0.07229 0.00034  -0.02301 835 PHE A CG    
6908 C CD1   . PHE B 835 ? 0.88546 0.92662 1.22917 -0.07004 0.00433  -0.02706 835 PHE A CD1   
6909 C CD2   . PHE B 835 ? 0.89217 0.93096 1.23917 -0.07477 -0.00786 -0.02155 835 PHE A CD2   
6910 C CE1   . PHE B 835 ? 0.99478 1.03206 1.36050 -0.07014 0.00054  -0.03028 835 PHE A CE1   
6911 C CE2   . PHE B 835 ? 1.13476 1.16963 1.50309 -0.07517 -0.01199 -0.02482 835 PHE A CE2   
6912 C CZ    . PHE B 835 ? 0.81661 0.85049 1.19410 -0.07276 -0.00761 -0.02940 835 PHE A CZ    
6913 N N     . ARG B 836 ? 0.97595 1.01415 1.25679 -0.08157 -0.00966 -0.03112 836 ARG A N     
6914 C CA    . ARG B 836 ? 1.14902 1.18184 1.42722 -0.08697 -0.01996 -0.03673 836 ARG A CA    
6915 C C     . ARG B 836 ? 0.97793 1.00725 1.22824 -0.09071 -0.02022 -0.04813 836 ARG A C     
6916 O O     . ARG B 836 ? 0.97898 1.00166 1.22348 -0.09562 -0.02740 -0.05741 836 ARG A O     
6917 C CB    . ARG B 836 ? 1.02548 1.06102 1.31250 -0.08806 -0.02583 -0.02490 836 ARG A CB    
6918 C CG    . ARG B 836 ? 1.17252 1.21184 1.44281 -0.08829 -0.02408 -0.01877 836 ARG A CG    
6919 C CD    . ARG B 836 ? 1.45182 1.49502 1.73919 -0.08696 -0.02611 -0.00474 836 ARG A CD    
6920 N NE    . ARG B 836 ? 1.29103 1.33175 1.59740 -0.09016 -0.03640 -0.00304 836 ARG A NE    
6921 C CZ    . ARG B 836 ? 1.30226 1.33868 1.60217 -0.09615 -0.04718 -0.00820 836 ARG A CZ    
6922 N NH1   . ARG B 836 ? 1.41892 1.45491 1.69671 -0.09937 -0.04961 -0.01035 836 ARG A NH1   
6923 N NH2   . ARG B 836 ? 1.49604 1.52828 1.81148 -0.09934 -0.05601 -0.01079 836 ARG A NH2   
6924 N N     . GLN B 837 ? 0.97096 1.00418 1.20423 -0.08882 -0.01265 -0.04741 837 GLN A N     
6925 C CA    . GLN B 837 ? 1.18009 1.21074 1.38645 -0.09228 -0.01179 -0.05736 837 GLN A CA    
6926 C C     . GLN B 837 ? 1.14467 1.16982 1.34964 -0.09279 -0.00897 -0.07131 837 GLN A C     
6927 O O     . GLN B 837 ? 1.35440 1.37317 1.54425 -0.09781 -0.01325 -0.08182 837 GLN A O     
6928 C CB    . GLN B 837 ? 0.98058 1.01690 1.17230 -0.08975 -0.00380 -0.05279 837 GLN A CB    
6929 C CG    . GLN B 837 ? 1.16384 1.19923 1.32899 -0.09409 -0.00564 -0.05662 837 GLN A CG    
6930 C CD    . GLN B 837 ? 1.32488 1.36091 1.48835 -0.09710 -0.01387 -0.04819 837 GLN A CD    
6931 O OE1   . GLN B 837 ? 1.44261 1.48313 1.61444 -0.09421 -0.01235 -0.03664 837 GLN A OE1   
6932 N NE2   . GLN B 837 ? 1.17367 1.20483 1.32625 -0.10316 -0.02261 -0.05379 837 GLN A NE2   
6933 N N     . GLY B 838 ? 1.11219 1.13931 1.33261 -0.08801 -0.00205 -0.07121 838 GLY A N     
6934 C CA    . GLY B 838 ? 1.24339 1.26539 1.46667 -0.08767 0.00171  -0.08392 838 GLY A CA    
6935 C C     . GLY B 838 ? 1.19345 1.20728 1.42704 -0.09103 -0.00643 -0.09073 838 GLY A C     
6936 O O     . GLY B 838 ? 1.34216 1.34855 1.56602 -0.09377 -0.00590 -0.10451 838 GLY A O     
6937 N N     . LEU B 839 ? 1.14501 1.15976 1.39759 -0.09102 -0.01344 -0.08148 839 LEU A N     
6938 C CA    . LEU B 839 ? 1.19538 1.20225 1.45945 -0.09481 -0.02272 -0.08679 839 LEU A CA    
6939 C C     . LEU B 839 ? 1.35795 1.35810 1.59721 -0.10188 -0.02977 -0.09574 839 LEU A C     
6940 O O     . LEU B 839 ? 1.58260 1.57318 1.81911 -0.10567 -0.03356 -0.10804 839 LEU A O     
6941 C CB    . LEU B 839 ? 1.10920 1.11981 1.39618 -0.09398 -0.02910 -0.07307 839 LEU A CB    
6942 C CG    . LEU B 839 ? 1.23828 1.25171 1.55430 -0.08896 -0.02559 -0.06661 839 LEU A CG    
6943 C CD1   . LEU B 839 ? 1.39004 1.40773 1.70591 -0.08377 -0.01431 -0.06706 839 LEU A CD1   
6944 C CD2   . LEU B 839 ? 1.06397 1.08388 1.39524 -0.08748 -0.02843 -0.05046 839 LEU A CD2   
6945 N N     . GLY B 840 ? 1.17063 1.17509 1.39210 -0.10383 -0.03149 -0.08972 840 GLY A N     
6946 C CA    . GLY B 840 ? 1.40669 1.40543 1.60337 -0.11116 -0.03901 -0.09641 840 GLY A CA    
6947 C C     . GLY B 840 ? 1.38230 1.37610 1.55470 -0.11276 -0.03201 -0.11093 840 GLY A C     
6948 O O     . GLY B 840 ? 1.53324 1.52029 1.68304 -0.11953 -0.03771 -0.11900 840 GLY A O     
6949 N N     . ARG B 841 ? 1.33422 1.33125 1.51116 -0.10703 -0.02008 -0.11376 841 ARG A N     
6950 C CA    . ARG B 841 ? 1.69821 1.69143 1.85465 -0.10774 -0.01140 -0.12719 841 ARG A CA    
6951 C C     . ARG B 841 ? 1.55665 1.53930 1.71968 -0.10894 -0.01078 -0.14157 841 ARG A C     
6952 O O     . ARG B 841 ? 1.56620 1.54496 1.71680 -0.10866 -0.00187 -0.15361 841 ARG A O     
6953 C CB    . ARG B 841 ? 1.52034 1.52217 1.67979 -0.10132 0.00086  -0.12304 841 ARG A CB    
6954 C CG    . ARG B 841 ? 1.46465 1.47513 1.61293 -0.10072 0.00129  -0.11122 841 ARG A CG    
6955 C CD    . ARG B 841 ? 1.62566 1.63306 1.74525 -0.10734 -0.00383 -0.11476 841 ARG A CD    
6956 N NE    . ARG B 841 ? 1.86492 1.87996 1.97350 -0.10687 -0.00304 -0.10410 841 ARG A NE    
6957 C CZ    . ARG B 841 ? 1.90152 1.91579 1.98635 -0.11211 -0.00713 -0.10419 841 ARG A CZ    
6958 N NH1   . ARG B 841 ? 2.00345 2.01053 2.06705 -0.11769 -0.00831 -0.11621 841 ARG A NH1   
6959 N NH2   . ARG B 841 ? 1.81076 1.83094 1.89286 -0.11194 -0.00989 -0.09221 841 ARG A NH2   
6960 N N     . LEU B 842 ? 1.51897 1.49699 1.70167 -0.11018 -0.01943 -0.14030 842 LEU A N     
6961 C CA    . LEU B 842 ? 1.33062 1.29723 1.52091 -0.11164 -0.01969 -0.15417 842 LEU A CA    
6962 C C     . LEU B 842 ? 1.43221 1.38737 1.60081 -0.12074 -0.03001 -0.16391 842 LEU A C     
6963 O O     . LEU B 842 ? 1.60146 1.54659 1.75290 -0.12371 -0.02571 -0.17986 842 LEU A O     
6964 C CB    . LEU B 842 ? 1.25520 1.22258 1.48062 -0.10799 -0.02314 -0.14759 842 LEU A CB    
6965 C CG    . LEU B 842 ? 1.34264 1.29784 1.57950 -0.10935 -0.02416 -0.16096 842 LEU A CG    
6966 C CD1   . LEU B 842 ? 1.56085 1.51522 1.80354 -0.10389 -0.01042 -0.16978 842 LEU A CD1   
6967 C CD2   . LEU B 842 ? 1.38910 1.34366 1.65688 -0.10874 -0.03285 -0.15317 842 LEU A CD2   
6968 N N     . ILE B 843 ? 1.44108 1.39747 1.61031 -0.12520 -0.04293 -0.15454 843 ILE A N     
6969 C CA    . ILE B 843 ? 1.64595 1.59091 1.79638 -0.13486 -0.05513 -0.16273 843 ILE A CA    
6970 C C     . ILE B 843 ? 1.78850 1.73669 1.90985 -0.14008 -0.05943 -0.15848 843 ILE A C     
6971 O O     . ILE B 843 ? 1.69837 1.65731 1.82695 -0.13788 -0.06196 -0.14311 843 ILE A O     
6972 C CB    . ILE B 843 ? 1.73715 1.67929 1.91196 -0.13740 -0.06862 -0.15624 843 ILE A CB    
6973 C CG1   . ILE B 843 ? 1.60288 1.53239 1.75920 -0.14801 -0.08234 -0.16479 843 ILE A CG1   
6974 C CG2   . ILE B 843 ? 1.69796 1.65303 1.89177 -0.13405 -0.07275 -0.13626 843 ILE A CG2   
6975 C CD1   . ILE B 843 ? 1.75087 1.66501 1.89558 -0.15129 -0.07924 -0.18493 843 ILE A CD1   
6976 N N     . ARG B 844 ? 1.94039 1.87929 2.02990 -0.14671 -0.05955 -0.17162 844 ARG A N     
6977 C CA    . ARG B 844 ? 1.97984 1.92066 2.04014 -0.15297 -0.06512 -0.16777 844 ARG A CA    
6978 C C     . ARG B 844 ? 2.04654 1.97335 2.08545 -0.16405 -0.07781 -0.17784 844 ARG A C     
6979 O O     . ARG B 844 ? 2.13188 2.05960 2.15760 -0.17088 -0.09002 -0.17030 844 ARG A O     
6980 C CB    . ARG B 844 ? 1.85670 1.80155 1.89457 -0.15037 -0.05111 -0.17244 844 ARG A CB    
6981 C CG    . ARG B 844 ? 1.98594 1.92181 2.01411 -0.14931 -0.03907 -0.19048 844 ARG A CG    
6982 C CD    . ARG B 844 ? 2.05819 1.99716 2.05953 -0.14904 -0.02736 -0.19495 844 ARG A CD    
6983 N NE    . ARG B 844 ? 2.23901 2.17493 2.20784 -0.15820 -0.03602 -0.19448 844 ARG A NE    
6984 C CZ    . ARG B 844 ? 2.18049 2.10685 2.11645 -0.16472 -0.03293 -0.20792 844 ARG A CZ    
6985 N NH1   . ARG B 844 ? 2.05374 1.97552 1.98405 -0.16153 -0.01796 -0.22161 844 ARG A NH1   
6986 N NH2   . ARG B 844 ? 2.14029 2.06169 2.04936 -0.17453 -0.04460 -0.20724 844 ARG A NH2   
6987 N N     . ASN B 845 ? 2.06854 1.98242 2.10447 -0.16595 -0.07519 -0.19412 845 ASN A N     
6988 C CA    . ASN B 845 ? 1.97641 1.87470 1.99152 -0.17710 -0.08763 -0.20517 845 ASN A CA    
6989 C C     . ASN B 845 ? 1.95725 1.84805 2.00055 -0.17682 -0.09441 -0.20819 845 ASN A C     
6990 O O     . ASN B 845 ? 1.98000 1.86779 2.03876 -0.17051 -0.08321 -0.21676 845 ASN A O     
6991 C CB    . ASN B 845 ? 2.00629 1.89317 1.98591 -0.18128 -0.07831 -0.22391 845 ASN A CB    
6992 C CG    . ASN B 845 ? 2.17278 2.06938 2.13415 -0.17771 -0.06570 -0.22116 845 ASN A CG    
6993 O OD1   . ASN B 845 ? 2.09509 1.99952 2.04436 -0.18065 -0.07190 -0.20957 845 ASN A OD1   
6994 N ND2   . ASN B 845 ? 2.12583 2.02221 2.08669 -0.17138 -0.04818 -0.23112 845 ASN A ND2   
6995 N N     . GLU B 846 ? 2.00122 1.88912 2.05218 -0.18355 -0.11225 -0.20109 846 GLU A N     
6996 C CA    . GLU B 846 ? 1.95099 1.83288 2.03219 -0.18331 -0.11973 -0.20183 846 GLU A CA    
6997 C C     . GLU B 846 ? 2.05974 1.92233 2.12574 -0.18855 -0.11859 -0.22347 846 GLU A C     
6998 O O     . GLU B 846 ? 2.09669 1.95183 2.18558 -0.18905 -0.12452 -0.22665 846 GLU A O     
6999 C CB    . GLU B 846 ? 2.04680 1.93127 2.14062 -0.18948 -0.13925 -0.18769 846 GLU A CB    
7000 C CG    . GLU B 846 ? 2.22113 2.09878 2.28053 -0.20157 -0.15263 -0.18952 846 GLU A CG    
7001 C CD    . GLU B 846 ? 2.24036 2.12422 2.31503 -0.20654 -0.17091 -0.17200 846 GLU A CD    
7002 O OE1   . GLU B 846 ? 2.20384 2.09739 2.31582 -0.20021 -0.17208 -0.15869 846 GLU A OE1   
7003 O OE2   . GLU B 846 ? 2.17845 2.05751 2.22824 -0.21688 -0.18389 -0.17122 846 GLU A OE2   
7004 N N     . ASN B 847 ? 2.03576 1.89021 2.06481 -0.19240 -0.11089 -0.23775 847 ASN A N     
7005 C CA    . ASN B 847 ? 2.15669 1.99163 2.16885 -0.19696 -0.10706 -0.26001 847 ASN A CA    
7006 C C     . ASN B 847 ? 2.17313 2.00806 2.21527 -0.18658 -0.09269 -0.26608 847 ASN A C     
7007 O O     . ASN B 847 ? 2.06887 1.89059 2.12314 -0.18867 -0.09650 -0.27625 847 ASN A O     
7008 C CB    . ASN B 847 ? 2.20937 2.03716 2.17649 -0.20206 -0.09883 -0.27311 847 ASN A CB    
7009 C CG    . ASN B 847 ? 2.27386 2.07925 2.21735 -0.20964 -0.09831 -0.29569 847 ASN A CG    
7010 O OD1   . ASN B 847 ? 2.17586 1.97039 2.13679 -0.21157 -0.10544 -0.30169 847 ASN A OD1   
7011 N ND2   . ASN B 847 ? 2.24541 2.04309 2.14882 -0.21428 -0.08979 -0.30847 847 ASN A ND2   
7012 N N     . ASP B 848 ? 1.97025 1.81924 2.02468 -0.17616 -0.07752 -0.25959 848 ASP A N     
7013 C CA    . ASP B 848 ? 1.82249 1.67219 1.90538 -0.16626 -0.06336 -0.26466 848 ASP A CA    
7014 C C     . ASP B 848 ? 1.72798 1.59195 1.85280 -0.15862 -0.06655 -0.24614 848 ASP A C     
7015 O O     . ASP B 848 ? 1.78639 1.66033 1.91538 -0.16031 -0.07718 -0.23009 848 ASP A O     
7016 C CB    . ASP B 848 ? 1.94095 1.79409 2.00938 -0.16055 -0.04383 -0.27233 848 ASP A CB    
7017 C CG    . ASP B 848 ? 2.07301 1.94243 2.12982 -0.15774 -0.03954 -0.25922 848 ASP A CG    
7018 O OD1   . ASP B 848 ? 2.08191 1.96089 2.14403 -0.15931 -0.05106 -0.24316 848 ASP A OD1   
7019 O OD2   . ASP B 848 ? 1.89619 1.76826 1.93919 -0.15411 -0.02450 -0.26526 848 ASP A OD2   
7020 N N     . ARG B 849 ? 1.74192 1.60662 1.89672 -0.15062 -0.05735 -0.24809 849 ARG A N     
7021 C CA    . ARG B 849 ? 1.66341 1.54065 1.85814 -0.14364 -0.05987 -0.23087 849 ARG A CA    
7022 C C     . ARG B 849 ? 1.63319 1.52212 1.84374 -0.13295 -0.04341 -0.22633 849 ARG A C     
7023 O O     . ARG B 849 ? 1.64129 1.52695 1.83531 -0.13109 -0.03046 -0.23814 849 ARG A O     
7024 C CB    . ARG B 849 ? 1.72627 1.59284 1.94704 -0.14519 -0.06776 -0.23523 849 ARG A CB    
7025 C CG    . ARG B 849 ? 1.76458 1.61417 1.97923 -0.14611 -0.05994 -0.25674 849 ARG A CG    
7026 C CD    . ARG B 849 ? 1.97738 1.81199 2.20462 -0.15215 -0.07259 -0.26365 849 ARG A CD    
7027 N NE    . ARG B 849 ? 2.00475 1.83396 2.21203 -0.16291 -0.09018 -0.26160 849 ARG A NE    
7028 C CZ    . ARG B 849 ? 2.03078 1.85148 2.19744 -0.17131 -0.09333 -0.27145 849 ARG A CZ    
7029 N NH1   . ARG B 849 ? 2.09617 1.90846 2.23669 -0.17118 -0.08000 -0.28812 849 ARG A NH1   
7030 N NH2   . ARG B 849 ? 1.92117 1.74181 2.07409 -0.18002 -0.10986 -0.26411 849 ARG A NH2   
7031 N N     . GLY B 850 ? 1.48232 1.38420 1.72344 -0.12659 -0.04398 -0.20957 850 GLY A N     
7032 C CA    . GLY B 850 ? 1.27047 1.18400 1.52657 -0.11718 -0.03008 -0.20330 850 GLY A CA    
7033 C C     . GLY B 850 ? 1.22490 1.14741 1.51903 -0.11141 -0.03228 -0.18812 850 GLY A C     
7034 O O     . GLY B 850 ? 1.41957 1.34049 1.72753 -0.11469 -0.04454 -0.18134 850 GLY A O     
7035 N N     . ILE B 851 ? 1.17261 1.10426 1.48317 -0.10349 -0.02107 -0.18243 851 ILE A N     
7036 C CA    . ILE B 851 ? 1.07423 1.01460 1.42023 -0.09797 -0.02214 -0.16744 851 ILE A CA    
7037 C C     . ILE B 851 ? 1.00696 0.96274 1.35220 -0.09271 -0.01542 -0.15309 851 ILE A C     
7038 O O     . ILE B 851 ? 1.03303 0.99158 1.35771 -0.09152 -0.00672 -0.15772 851 ILE A O     
7039 C CB    . ILE B 851 ? 1.08308 1.01770 1.45547 -0.09372 -0.01606 -0.17442 851 ILE A CB    
7040 C CG1   . ILE B 851 ? 1.17713 1.11649 1.54792 -0.08785 -0.00144 -0.17801 851 ILE A CG1   
7041 C CG2   . ILE B 851 ? 1.21878 1.13598 1.58783 -0.09903 -0.02078 -0.19172 851 ILE A CG2   
7042 C CD1   . ILE B 851 ? 1.59950 1.53482 2.00019 -0.08296 0.00490  -0.18261 851 ILE A CD1   
7043 N N     . ILE B 852 ? 1.18747 1.15236 1.55358 -0.09007 -0.01930 -0.13640 852 ILE A N     
7044 C CA    . ILE B 852 ? 0.99822 0.97635 1.36465 -0.08515 -0.01263 -0.12315 852 ILE A CA    
7045 C C     . ILE B 852 ? 0.91144 0.89445 1.31055 -0.07967 -0.00954 -0.11385 852 ILE A C     
7046 O O     . ILE B 852 ? 0.97749 0.95858 1.39942 -0.08021 -0.01636 -0.10849 852 ILE A O     
7047 C CB    . ILE B 852 ? 0.92013 0.90536 1.27625 -0.08729 -0.01890 -0.11043 852 ILE A CB    
7048 C CG1   . ILE B 852 ? 0.94125 0.92345 1.26339 -0.09223 -0.02055 -0.11820 852 ILE A CG1   
7049 C CG2   . ILE B 852 ? 0.98004 0.97770 1.34296 -0.08206 -0.01288 -0.09518 852 ILE A CG2   
7050 C CD1   . ILE B 852 ? 1.00671 0.99374 1.32071 -0.09527 -0.02852 -0.10713 852 ILE A CD1   
7051 N N     . VAL B 853 ? 0.81728 0.80660 1.21918 -0.07479 0.00024  -0.11146 853 VAL A N     
7052 C CA    . VAL B 853 ? 0.82672 0.82137 1.25781 -0.06985 0.00343  -0.10177 853 VAL A CA    
7053 C C     . VAL B 853 ? 0.92798 0.93483 1.35494 -0.06723 0.00645  -0.08604 853 VAL A C     
7054 O O     . VAL B 853 ? 1.06943 1.08047 1.47455 -0.06685 0.01182  -0.08705 853 VAL A O     
7055 C CB    . VAL B 853 ? 0.90247 0.89362 1.34354 -0.06658 0.01190  -0.11186 853 VAL A CB    
7056 C CG1   . VAL B 853 ? 0.82072 0.81845 1.29193 -0.06179 0.01445  -0.09994 853 VAL A CG1   
7057 C CG2   . VAL B 853 ? 0.94895 0.92634 1.39359 -0.06926 0.00961  -0.12842 853 VAL A CG2   
7058 N N     . SER B 854 ? 0.85332 0.86532 1.30045 -0.06573 0.00318  -0.07166 854 SER A N     
7059 C CA    . SER B 854 ? 0.88874 0.91096 1.33226 -0.06361 0.00600  -0.05646 854 SER A CA    
7060 C C     . SER B 854 ? 0.78930 0.81592 1.25897 -0.05999 0.00855  -0.04653 854 SER A C     
7061 O O     . SER B 854 ? 0.88011 0.90496 1.37380 -0.05992 0.00400  -0.04165 854 SER A O     
7062 C CB    . SER B 854 ? 0.91548 0.94007 1.35484 -0.06585 -0.00003 -0.04679 854 SER A CB    
7063 O OG    . SER B 854 ? 0.91259 0.94571 1.35341 -0.06354 0.00322  -0.03162 854 SER A OG    
7064 N N     . PHE B 855 ? 0.89029 0.92305 1.35563 -0.05739 0.01512  -0.04206 855 PHE A N     
7065 C CA    . PHE B 855 ? 0.87874 0.91561 1.36894 -0.05443 0.01704  -0.03248 855 PHE A CA    
7066 C C     . PHE B 855 ? 0.84251 0.88671 1.33436 -0.05411 0.01625  -0.01470 855 PHE A C     
7067 O O     . PHE B 855 ? 0.94625 0.99256 1.46160 -0.05289 0.01490  -0.00489 855 PHE A O     
7068 C CB    . PHE B 855 ? 0.80134 0.84060 1.28868 -0.05219 0.02401  -0.03701 855 PHE A CB    
7069 C CG    . PHE B 855 ? 0.88490 0.91681 1.37115 -0.05203 0.02704  -0.05475 855 PHE A CG    
7070 C CD1   . PHE B 855 ? 0.94059 0.96988 1.39905 -0.05386 0.02973  -0.06604 855 PHE A CD1   
7071 C CD2   . PHE B 855 ? 0.71979 0.74700 1.23267 -0.05014 0.02772  -0.06005 855 PHE A CD2   
7072 C CE1   . PHE B 855 ? 0.91256 0.93450 1.36820 -0.05399 0.03351  -0.08249 855 PHE A CE1   
7073 C CE2   . PHE B 855 ? 0.92247 0.94192 1.43354 -0.04992 0.03178  -0.07700 855 PHE A CE2   
7074 C CZ    . PHE B 855 ? 0.97769 0.99441 1.45929 -0.05193 0.03494  -0.08834 855 PHE A CZ    
7075 N N     . ASP B 856 ? 0.81289 0.86047 1.28079 -0.05526 0.01740  -0.01046 856 ASP A N     
7076 C CA    . ASP B 856 ? 0.95233 1.00605 1.41937 -0.05490 0.01832  0.00590  856 ASP A CA    
7077 C C     . ASP B 856 ? 0.85503 0.90799 1.34307 -0.05537 0.01358  0.01429  856 ASP A C     
7078 O O     . ASP B 856 ? 0.87387 0.92290 1.36228 -0.05705 0.00915  0.00944  856 ASP A O     
7079 C CB    . ASP B 856 ? 0.93536 0.99161 1.37367 -0.05592 0.02093  0.00789  856 ASP A CB    
7080 C CG    . ASP B 856 ? 1.10512 1.16689 1.53626 -0.05535 0.02463  0.02154  856 ASP A CG    
7081 O OD1   . ASP B 856 ? 1.29631 1.36038 1.74479 -0.05452 0.02461  0.03075  856 ASP A OD1   
7082 O OD2   . ASP B 856 ? 1.04072 1.10393 1.44852 -0.05604 0.02737  0.02279  856 ASP A OD2   
7083 N N     . ASP B 857 ? 1.18627 1.24297 1.69115 -0.05433 0.01415  0.02702  857 ASP A N     
7084 C CA    . ASP B 857 ? 1.07994 1.13651 1.60725 -0.05476 0.01019  0.03636  857 ASP A CA    
7085 C C     . ASP B 857 ? 1.22694 1.28614 1.74210 -0.05572 0.01112  0.04561  857 ASP A C     
7086 O O     . ASP B 857 ? 1.13369 1.19224 1.66449 -0.05644 0.00764  0.05094  857 ASP A O     
7087 C CB    . ASP B 857 ? 0.89699 0.95663 1.44618 -0.05368 0.01052  0.04736  857 ASP A CB    
7088 C CG    . ASP B 857 ? 1.39207 1.45732 1.92818 -0.05347 0.01515  0.05827  857 ASP A CG    
7089 O OD1   . ASP B 857 ? 1.57697 1.64345 2.08641 -0.05388 0.01869  0.05629  857 ASP A OD1   
7090 O OD2   . ASP B 857 ? 1.42328 1.49126 1.97582 -0.05330 0.01472  0.06898  857 ASP A OD2   
7091 N N     . ARG B 858 ? 1.19842 1.26026 1.68789 -0.05571 0.01586  0.04748  858 ARG A N     
7092 C CA    . ARG B 858 ? 0.98689 1.05086 1.46504 -0.05621 0.01821  0.05662  858 ARG A CA    
7093 C C     . ARG B 858 ? 0.97714 1.03831 1.46055 -0.05740 0.01336  0.05226  858 ARG A C     
7094 O O     . ARG B 858 ? 0.96221 1.02513 1.45138 -0.05756 0.01384  0.06193  858 ARG A O     
7095 C CB    . ARG B 858 ? 1.03439 1.09983 1.48281 -0.05620 0.02344  0.05555  858 ARG A CB    
7096 C CG    . ARG B 858 ? 0.72485 0.79270 1.16659 -0.05575 0.02700  0.05878  858 ARG A CG    
7097 C CD    . ARG B 858 ? 0.92422 0.99241 1.33702 -0.05614 0.03083  0.05437  858 ARG A CD    
7098 N NE    . ARG B 858 ? 0.94870 1.01897 1.35539 -0.05614 0.03305  0.05541  858 ARG A NE    
7099 C CZ    . ARG B 858 ? 1.04892 1.11973 1.43285 -0.05667 0.03601  0.05178  858 ARG A CZ    
7100 N NH1   . ARG B 858 ? 0.98634 1.05546 1.35295 -0.05700 0.03674  0.04434  858 ARG A NH1   
7101 N NH2   . ARG B 858 ? 1.30490 1.37799 1.68422 -0.05719 0.03766  0.05613  858 ARG A NH2   
7102 N N     . LEU B 859 ? 0.86325 0.92000 1.34517 -0.05846 0.00891  0.03850  859 LEU A N     
7103 C CA    . LEU B 859 ? 0.94926 1.00260 1.43487 -0.06058 0.00267  0.03375  859 LEU A CA    
7104 C C     . LEU B 859 ? 0.98053 1.03373 1.49555 -0.06093 -0.00172 0.04171  859 LEU A C     
7105 O O     . LEU B 859 ? 1.10845 1.16056 1.62953 -0.06271 -0.00657 0.04305  859 LEU A O     
7106 C CB    . LEU B 859 ? 0.86219 0.90962 1.34059 -0.06222 -0.00128 0.01708  859 LEU A CB    
7107 C CG    . LEU B 859 ? 1.00072 1.04374 1.47627 -0.06551 -0.00861 0.01060  859 LEU A CG    
7108 C CD1   . LEU B 859 ? 1.06175 1.10234 1.50925 -0.06714 -0.00810 -0.00096 859 LEU A CD1   
7109 C CD2   . LEU B 859 ? 1.00108 1.03796 1.49844 -0.06724 -0.01570 0.00407  859 LEU A CD2   
7110 N N     . ILE B 860 ? 1.06725 1.12176 1.60086 -0.05953 -0.00049 0.04753  860 ILE A N     
7111 C CA    . ILE B 860 ? 1.05898 1.11321 1.62275 -0.06003 -0.00497 0.05517  860 ILE A CA    
7112 C C     . ILE B 860 ? 1.13142 1.19150 1.70359 -0.05856 0.00035  0.07201  860 ILE A C     
7113 O O     . ILE B 860 ? 1.16847 1.22977 1.76289 -0.05902 -0.00190 0.08145  860 ILE A O     
7114 C CB    . ILE B 860 ? 0.84126 0.89011 1.42439 -0.06035 -0.00992 0.04601  860 ILE A CB    
7115 C CG1   . ILE B 860 ? 0.99855 1.04942 1.58737 -0.05815 -0.00566 0.04856  860 ILE A CG1   
7116 C CG2   . ILE B 860 ? 0.86253 0.90452 1.43293 -0.06218 -0.01394 0.02837  860 ILE A CG2   
7117 C CD1   . ILE B 860 ? 1.05790 1.10306 1.66596 -0.05792 -0.00929 0.03868  860 ILE A CD1   
7118 N N     . ASN B 861 ? 1.20814 1.27140 1.76298 -0.05728 0.00692  0.07589  861 ASN A N     
7119 C CA    . ASN B 861 ? 1.20145 1.26926 1.76230 -0.05665 0.01170  0.09180  861 ASN A CA    
7120 C C     . ASN B 861 ? 1.16969 1.24016 1.70307 -0.05629 0.01925  0.09740  861 ASN A C     
7121 O O     . ASN B 861 ? 1.26117 1.33420 1.79082 -0.05625 0.02369  0.10749  861 ASN A O     
7122 C CB    . ASN B 861 ? 1.02988 1.09819 1.60534 -0.05619 0.01073  0.09409  861 ASN A CB    
7123 C CG    . ASN B 861 ? 1.59871 1.66688 2.15663 -0.05554 0.01303  0.08661  861 ASN A CG    
7124 O OD1   . ASN B 861 ? 1.66665 1.73442 2.19941 -0.05551 0.01579  0.07994  861 ASN A OD1   
7125 N ND2   . ASN B 861 ? 1.26360 1.33242 1.83585 -0.05506 0.01188  0.08841  861 ASN A ND2   
7126 N N     . SER B 862 ? 1.28680 1.35622 1.80167 -0.05639 0.02038  0.09153  862 SER A N     
7127 C CA    . SER B 862 ? 1.04120 1.11225 1.53108 -0.05598 0.02794  0.09696  862 SER A CA    
7128 C C     . SER B 862 ? 1.20849 1.28029 1.70059 -0.05580 0.03001  0.10300  862 SER A C     
7129 O O     . SER B 862 ? 1.42780 1.49874 1.93650 -0.05639 0.02410  0.10001  862 SER A O     
7130 C CB    . SER B 862 ? 1.17124 1.24083 1.63550 -0.05602 0.02901  0.08630  862 SER A CB    
7131 O OG    . SER B 862 ? 1.66181 1.73223 2.10319 -0.05581 0.03619  0.09199  862 SER A OG    
7132 N N     . ASN B 863 ? 0.98785 1.06078 1.46427 -0.05518 0.03812  0.11115  863 ASN A N     
7133 C CA    . ASN B 863 ? 1.24504 1.31896 1.72593 -0.05450 0.04178  0.11826  863 ASN A CA    
7134 C C     . ASN B 863 ? 1.27027 1.34277 1.74374 -0.05470 0.03798  0.10910  863 ASN A C     
7135 O O     . ASN B 863 ? 1.26808 1.34150 1.75791 -0.05483 0.03521  0.11212  863 ASN A O     
7136 C CB    . ASN B 863 ? 1.17701 1.25123 1.64151 -0.05374 0.05254  0.12819  863 ASN A CB    
7137 C CG    . ASN B 863 ? 1.32274 1.39476 1.75693 -0.05400 0.05606  0.12260  863 ASN A CG    
7138 O OD1   . ASN B 863 ? 1.55433 1.62490 1.97395 -0.05379 0.05506  0.11413  863 ASN A OD1   
7139 N ND2   . ASN B 863 ? 1.46862 1.54036 1.89321 -0.05486 0.05968  0.12783  863 ASN A ND2   
7140 N N     . TYR B 864 ? 1.14061 1.21120 1.59133 -0.05504 0.03742  0.09904  864 TYR A N     
7141 C CA    . TYR B 864 ? 1.13693 1.20616 1.57765 -0.05565 0.03409  0.09130  864 TYR A CA    
7142 C C     . TYR B 864 ? 1.19466 1.26208 1.64710 -0.05755 0.02365  0.08110  864 TYR A C     
7143 O O     . TYR B 864 ? 1.06042 1.12623 1.50310 -0.05890 0.01941  0.07357  864 TYR A O     
7144 C CB    . TYR B 864 ? 0.86967 0.93749 1.28059 -0.05553 0.03808  0.08524  864 TYR A CB    
7145 C CG    . TYR B 864 ? 1.02379 1.09111 1.42563 -0.05585 0.03809  0.07996  864 TYR A CG    
7146 C CD1   . TYR B 864 ? 1.07735 1.14337 1.48156 -0.05689 0.03158  0.06861  864 TYR A CD1   
7147 C CD2   . TYR B 864 ? 0.92879 0.99658 1.31928 -0.05535 0.04474  0.08632  864 TYR A CD2   
7148 C CE1   . TYR B 864 ? 1.03415 1.10018 1.43287 -0.05686 0.03217  0.06430  864 TYR A CE1   
7149 C CE2   . TYR B 864 ? 0.85922 0.92712 1.24350 -0.05588 0.04404  0.08257  864 TYR A CE2   
7150 C CZ    . TYR B 864 ? 0.90795 0.97536 1.29768 -0.05635 0.03800  0.07175  864 TYR A CZ    
7151 O OH    . TYR B 864 ? 1.04041 1.10837 1.42678 -0.05656 0.03786  0.06852  864 TYR A OH    
7152 N N     . LYS B 865 ? 1.08076 1.14784 1.55290 -0.05795 0.01950  0.08076  865 LYS A N     
7153 C CA    . LYS B 865 ? 1.02089 1.08454 1.50235 -0.06000 0.01000  0.06938  865 LYS A CA    
7154 C C     . LYS B 865 ? 1.00041 1.06291 1.48529 -0.06205 0.00371  0.06744  865 LYS A C     
7155 O O     . LYS B 865 ? 0.99969 1.05869 1.47329 -0.06423 -0.00199 0.05574  865 LYS A O     
7156 C CB    . LYS B 865 ? 1.04791 1.11105 1.55591 -0.06009 0.00638  0.07176  865 LYS A CB    
7157 C CG    . LYS B 865 ? 1.24974 1.31558 1.78263 -0.05988 0.00620  0.08477  865 LYS A CG    
7158 C CD    . LYS B 865 ? 1.15069 1.21588 1.70872 -0.06002 0.00279  0.08704  865 LYS A CD    
7159 C CE    . LYS B 865 ? 1.16068 1.22918 1.74301 -0.05981 0.00365  0.10122  865 LYS A CE    
7160 N NZ    . LYS B 865 ? 1.38105 1.44887 1.98780 -0.06008 0.00014  0.10383  865 LYS A NZ    
7161 N N     . ASN B 866 ? 0.87390 0.93928 1.37351 -0.06159 0.00481  0.07881  866 ASN A N     
7162 C CA    . ASN B 866 ? 1.12717 1.19197 1.63455 -0.06386 -0.00242 0.07849  866 ASN A CA    
7163 C C     . ASN B 866 ? 0.99662 1.05931 1.47894 -0.06542 -0.00464 0.06921  866 ASN A C     
7164 O O     . ASN B 866 ? 0.90345 0.96319 1.38676 -0.06884 -0.01414 0.06234  866 ASN A O     
7165 C CB    . ASN B 866 ? 1.17480 1.24404 1.69623 -0.06225 0.00249  0.09310  866 ASN A CB    
7166 C CG    . ASN B 866 ? 1.60498 1.67705 2.14425 -0.06017 0.00853  0.10410  866 ASN A CG    
7167 O OD1   . ASN B 866 ? 1.62841 1.70284 2.15962 -0.05763 0.01902  0.11227  866 ASN A OD1   
7168 N ND2   . ASN B 866 ? 1.35493 1.42626 1.91828 -0.06160 0.00183  0.10460  866 ASN A ND2   
7169 N N     . PHE B 867 ? 1.06415 1.12801 1.52357 -0.06335 0.00374  0.06936  867 PHE A N     
7170 C CA    . PHE B 867 ? 0.94011 1.00237 1.37534 -0.06473 0.00242  0.06164  867 PHE A CA    
7171 C C     . PHE B 867 ? 0.93465 0.99261 1.35894 -0.06741 -0.00405 0.04697  867 PHE A C     
7172 O O     . PHE B 867 ? 0.90363 0.95923 1.31605 -0.07038 -0.01002 0.03994  867 PHE A O     
7173 C CB    . PHE B 867 ? 0.91093 0.97475 1.32489 -0.06207 0.01285  0.06468  867 PHE A CB    
7174 C CG    . PHE B 867 ? 0.91534 0.98206 1.33638 -0.05946 0.02080  0.07800  867 PHE A CG    
7175 C CD1   . PHE B 867 ? 0.97082 1.03889 1.40139 -0.05973 0.01909  0.08405  867 PHE A CD1   
7176 C CD2   . PHE B 867 ? 1.04039 1.10815 1.45810 -0.05697 0.03021  0.08455  867 PHE A CD2   
7177 C CE1   . PHE B 867 ? 1.00091 1.07128 1.43868 -0.05697 0.02791  0.09593  867 PHE A CE1   
7178 C CE2   . PHE B 867 ? 0.98902 1.05839 1.41101 -0.05476 0.03869  0.09599  867 PHE A CE2   
7179 C CZ    . PHE B 867 ? 0.76775 0.83840 1.20021 -0.05446 0.03822  0.10146  867 PHE A CZ    
7180 N N     . PHE B 868 ? 0.90117 0.95783 1.32967 -0.06656 -0.00278 0.04242  868 PHE A N     
7181 C CA    . PHE B 868 ? 0.82363 0.87577 1.24275 -0.06858 -0.00701 0.02811  868 PHE A CA    
7182 C C     . PHE B 868 ? 0.99443 1.04190 1.43004 -0.07187 -0.01715 0.02214  868 PHE A C     
7183 O O     . PHE B 868 ? 1.05966 1.10230 1.48304 -0.07520 -0.02286 0.01057  868 PHE A O     
7184 C CB    . PHE B 868 ? 0.81364 0.86632 1.23160 -0.06609 -0.00094 0.02587  868 PHE A CB    
7185 C CG    . PHE B 868 ? 0.99631 1.05148 1.39094 -0.06438 0.00690  0.02631  868 PHE A CG    
7186 C CD1   . PHE B 868 ? 0.82544 0.87859 1.19875 -0.06562 0.00703  0.01522  868 PHE A CD1   
7187 C CD2   . PHE B 868 ? 0.92507 0.98409 1.31842 -0.06191 0.01417  0.03776  868 PHE A CD2   
7188 C CE1   . PHE B 868 ? 0.87948 0.93490 1.23248 -0.06437 0.01366  0.01588  868 PHE A CE1   
7189 C CE2   . PHE B 868 ? 0.94126 1.00162 1.31260 -0.06091 0.02060  0.03784  868 PHE A CE2   
7190 C CZ    . PHE B 868 ? 0.95681 1.01563 1.30886 -0.06210 0.02006  0.02709  868 PHE A CZ    
7191 N N     . GLU B 869 ? 0.98808 1.03637 1.45054 -0.07142 -0.01962 0.02972  869 GLU A N     
7192 C CA    . GLU B 869 ? 0.84153 0.88471 1.32037 -0.07501 -0.03001 0.02433  869 GLU A CA    
7193 C C     . GLU B 869 ? 1.00880 1.05130 1.48678 -0.07878 -0.03818 0.02603  869 GLU A C     
7194 O O     . GLU B 869 ? 1.22346 1.26039 1.70812 -0.08310 -0.04836 0.01933  869 GLU A O     
7195 C CB    . GLU B 869 ? 0.96009 1.00447 1.46942 -0.07362 -0.03059 0.03256  869 GLU A CB    
7196 C CG    . GLU B 869 ? 1.05614 1.10767 1.57477 -0.06993 -0.02233 0.04835  869 GLU A CG    
7197 C CD    . GLU B 869 ? 1.32770 1.38018 1.87309 -0.06854 -0.02180 0.05521  869 GLU A CD    
7198 O OE1   . GLU B 869 ? 1.18658 1.23474 1.73836 -0.06903 -0.02465 0.04678  869 GLU A OE1   
7199 O OE2   . GLU B 869 ? 1.33679 1.39412 1.89736 -0.06700 -0.01824 0.06910  869 GLU A OE2   
7200 N N     . GLN B 870 ? 1.00921 1.05677 1.47944 -0.07748 -0.03421 0.03493  870 GLN A N     
7201 C CA    . GLN B 870 ? 0.88038 0.92738 1.34573 -0.08120 -0.04192 0.03558  870 GLN A CA    
7202 C C     . GLN B 870 ? 1.02003 1.06116 1.46034 -0.08529 -0.04746 0.02096  870 GLN A C     
7203 O O     . GLN B 870 ? 1.00570 1.04306 1.44529 -0.09048 -0.05826 0.01731  870 GLN A O     
7204 C CB    . GLN B 870 ? 1.05019 1.10320 1.50973 -0.07841 -0.03483 0.04666  870 GLN A CB    
7205 C CG    . GLN B 870 ? 0.97678 1.03478 1.46293 -0.07641 -0.03290 0.06190  870 GLN A CG    
7206 C CD    . GLN B 870 ? 1.03623 1.09905 1.51482 -0.07292 -0.02323 0.07156  870 GLN A CD    
7207 O OE1   . GLN B 870 ? 0.97177 1.03419 1.42542 -0.07175 -0.01770 0.06711  870 GLN A OE1   
7208 N NE2   . GLN B 870 ? 1.27679 1.34385 1.77741 -0.07123 -0.02072 0.08479  870 GLN A NE2   
7209 N N     . THR B 871 ? 0.98871 1.02895 1.40812 -0.08338 -0.04026 0.01281  871 THR A N     
7210 C CA    . THR B 871 ? 0.95867 0.99371 1.35261 -0.08687 -0.04332 -0.00098 871 THR A CA    
7211 C C     . THR B 871 ? 1.01846 1.04537 1.41611 -0.09037 -0.05007 -0.01375 871 THR A C     
7212 O O     . THR B 871 ? 1.21178 1.23319 1.58805 -0.09387 -0.05268 -0.02613 871 THR A O     
7213 C CB    . THR B 871 ? 0.97516 1.01248 1.34802 -0.08344 -0.03262 -0.00458 871 THR A CB    
7214 O OG1   . THR B 871 ? 0.89851 0.93523 1.28069 -0.08035 -0.02715 -0.00779 871 THR A OG1   
7215 C CG2   . THR B 871 ? 1.07342 1.11752 1.44332 -0.07989 -0.02530 0.00783  871 THR A CG2   
7216 N N     . LEU B 872 ? 0.90715 0.93266 1.33083 -0.08968 -0.05260 -0.01124 872 LEU A N     
7217 C CA    . LEU B 872 ? 1.04318 1.05995 1.47278 -0.09275 -0.05854 -0.02345 872 LEU A CA    
7218 C C     . LEU B 872 ? 1.05595 1.06962 1.50842 -0.09677 -0.07022 -0.01940 872 LEU A C     
7219 O O     . LEU B 872 ? 0.96704 0.97484 1.43564 -0.09793 -0.07415 -0.02475 872 LEU A O     
7220 C CB    . LEU B 872 ? 1.08091 1.09764 1.52167 -0.08818 -0.05055 -0.02601 872 LEU A CB    
7221 C CG    . LEU B 872 ? 1.10967 1.12910 1.53118 -0.08443 -0.03956 -0.03041 872 LEU A CG    
7222 C CD1   . LEU B 872 ? 0.96108 0.98201 1.40042 -0.07995 -0.03301 -0.02863 872 LEU A CD1   
7223 C CD2   . LEU B 872 ? 1.04354 1.05610 1.43961 -0.08771 -0.04035 -0.04660 872 LEU A CD2   
7224 N N     . GLU B 873 ? 1.18968 1.20712 1.64503 -0.09905 -0.07607 -0.00972 873 GLU A N     
7225 C CA    . GLU B 873 ? 1.14581 1.16199 1.62653 -0.10262 -0.08701 -0.00308 873 GLU A CA    
7226 C C     . GLU B 873 ? 0.98695 0.99232 1.46070 -0.11027 -0.10008 -0.01573 873 GLU A C     
7227 O O     . GLU B 873 ? 1.05486 1.05595 1.55071 -0.11328 -0.10878 -0.01508 873 GLU A O     
7228 C CB    . GLU B 873 ? 1.22259 1.24661 1.71056 -0.10245 -0.08865 0.01195  873 GLU A CB    
7229 C CG    . GLU B 873 ? 1.20336 1.23672 1.70722 -0.09563 -0.07725 0.02644  873 GLU A CG    
7230 C CD    . GLU B 873 ? 1.49816 1.53863 2.00428 -0.09472 -0.07601 0.03950  873 GLU A CD    
7231 O OE1   . GLU B 873 ? 1.49576 1.53543 1.98155 -0.09749 -0.07945 0.03627  873 GLU A OE1   
7232 O OE2   . GLU B 873 ? 1.60962 1.65634 2.13834 -0.09125 -0.07121 0.05319  873 GLU A OE2   
7233 N N     . ASN B 874 ? 1.13447 1.13525 1.57736 -0.11387 -0.10181 -0.02652 874 ASN A N     
7234 C CA    . ASN B 874 ? 1.20632 1.19576 1.63767 -0.12226 -0.11468 -0.03887 874 ASN A CA    
7235 C C     . ASN B 874 ? 1.18246 1.16209 1.60787 -0.12222 -0.11122 -0.05536 874 ASN A C     
7236 O O     . ASN B 874 ? 1.41247 1.38065 1.82756 -0.12901 -0.12041 -0.06782 874 ASN A O     
7237 C CB    . ASN B 874 ? 1.22187 1.21027 1.62222 -0.12694 -0.11859 -0.04255 874 ASN A CB    
7238 C CG    . ASN B 874 ? 1.25852 1.25743 1.66428 -0.12539 -0.11884 -0.02623 874 ASN A CG    
7239 O OD1   . ASN B 874 ? 1.28204 1.28626 1.66940 -0.12237 -0.11070 -0.02432 874 ASN A OD1   
7240 N ND2   . ASN B 874 ? 1.10031 1.10218 1.53218 -0.12734 -0.12777 -0.01425 874 ASN A ND2   
7241 N N     . TYR B 875 ? 1.22595 1.20955 1.65776 -0.11504 -0.09846 -0.05524 875 TYR A N     
7242 C CA    . TYR B 875 ? 1.10827 1.08318 1.53619 -0.11412 -0.09356 -0.07058 875 TYR A CA    
7243 C C     . TYR B 875 ? 1.06805 1.04114 1.52980 -0.11221 -0.09535 -0.06717 875 TYR A C     
7244 O O     . TYR B 875 ? 1.10357 1.08480 1.58966 -0.10970 -0.09623 -0.05154 875 TYR A O     
7245 C CB    . TYR B 875 ? 1.05527 1.03564 1.46858 -0.10789 -0.07895 -0.07277 875 TYR A CB    
7246 C CG    . TYR B 875 ? 1.13426 1.11582 1.51338 -0.10972 -0.07625 -0.07742 875 TYR A CG    
7247 C CD1   . TYR B 875 ? 1.29912 1.27226 1.65577 -0.11720 -0.08496 -0.08746 875 TYR A CD1   
7248 C CD2   . TYR B 875 ? 0.99856 0.98932 1.36752 -0.10443 -0.06542 -0.07137 875 TYR A CD2   
7249 C CE1   . TYR B 875 ? 1.47150 1.44591 1.79725 -0.11915 -0.08264 -0.09091 875 TYR A CE1   
7250 C CE2   . TYR B 875 ? 0.97271 0.96463 1.31180 -0.10617 -0.06306 -0.07506 875 TYR A CE2   
7251 C CZ    . TYR B 875 ? 1.24479 1.22883 1.56257 -0.11343 -0.07152 -0.08459 875 TYR A CZ    
7252 O OH    . TYR B 875 ? 1.41175 1.39709 1.70022 -0.11544 -0.06935 -0.08753 875 TYR A OH    
7253 N N     . ARG B 876 ? 1.09465 1.05704 1.55829 -0.11336 -0.09533 -0.08138 876 ARG A N     
7254 C CA    . ARG B 876 ? 0.97754 0.93723 1.47445 -0.11151 -0.09689 -0.07899 876 ARG A CA    
7255 C C     . ARG B 876 ? 0.91379 0.87820 1.41851 -0.10382 -0.08326 -0.07848 876 ARG A C     
7256 O O     . ARG B 876 ? 0.93200 0.89289 1.41652 -0.10244 -0.07556 -0.09060 876 ARG A O     
7257 C CB    . ARG B 876 ? 1.06748 1.01142 1.56395 -0.11806 -0.10646 -0.09443 876 ARG A CB    
7258 C CG    . ARG B 876 ? 1.25244 1.19101 1.73461 -0.12677 -0.12049 -0.09620 876 ARG A CG    
7259 C CD    . ARG B 876 ? 1.71711 1.66378 2.22468 -0.12793 -0.12945 -0.07797 876 ARG A CD    
7260 N NE    . ARG B 876 ? 1.98571 1.94278 2.48019 -0.12789 -0.12953 -0.06671 876 ARG A NE    
7261 C CZ    . ARG B 876 ? 1.51590 1.48373 2.03104 -0.12613 -0.13163 -0.04859 876 ARG A CZ    
7262 N NH1   . ARG B 876 ? 1.48000 1.45843 2.01166 -0.11846 -0.12072 -0.03670 876 ARG A NH1   
7263 N NH2   . ARG B 876 ? 1.34625 1.31397 1.86563 -0.13225 -0.14453 -0.04219 876 ARG A NH2   
7264 N N     . GLN B 877 ? 0.89705 0.86927 1.43026 -0.09924 -0.08043 -0.06444 877 GLN A N     
7265 C CA    . GLN B 877 ? 0.85970 0.83771 1.39975 -0.09230 -0.06820 -0.06150 877 GLN A CA    
7266 C C     . GLN B 877 ? 0.93344 0.90604 1.50270 -0.09062 -0.06842 -0.06393 877 GLN A C     
7267 O O     . GLN B 877 ? 1.01987 0.98892 1.61161 -0.09350 -0.07741 -0.06003 877 GLN A O     
7268 C CB    . GLN B 877 ? 0.84732 0.83907 1.39334 -0.08804 -0.06281 -0.04279 877 GLN A CB    
7269 C CG    . GLN B 877 ? 0.85563 0.85313 1.37270 -0.08822 -0.05957 -0.04067 877 GLN A CG    
7270 C CD    . GLN B 877 ? 0.96054 0.95695 1.47145 -0.09357 -0.06967 -0.03815 877 GLN A CD    
7271 O OE1   . GLN B 877 ? 1.12860 1.12199 1.65964 -0.09684 -0.07909 -0.03461 877 GLN A OE1   
7272 N NE2   . GLN B 877 ? 1.20664 1.20580 1.69093 -0.09466 -0.06819 -0.03911 877 GLN A NE2   
7273 N N     . LYS B 878 ? 0.84966 0.82184 1.41987 -0.08619 -0.05905 -0.06957 878 LYS A N     
7274 C CA    . LYS B 878 ? 0.83101 0.79879 1.43093 -0.08384 -0.05814 -0.07090 878 LYS A CA    
7275 C C     . LYS B 878 ? 0.79322 0.76984 1.39827 -0.07739 -0.04692 -0.06393 878 LYS A C     
7276 O O     . LYS B 878 ? 0.95514 0.93423 1.53637 -0.07568 -0.03949 -0.06939 878 LYS A O     
7277 C CB    . LYS B 878 ? 0.88619 0.83869 1.48125 -0.08682 -0.06019 -0.09146 878 LYS A CB    
7278 C CG    . LYS B 878 ? 1.04897 0.99691 1.66379 -0.08265 -0.05349 -0.09781 878 LYS A CG    
7279 C CD    . LYS B 878 ? 0.96908 0.91591 1.62274 -0.08175 -0.05834 -0.08924 878 LYS A CD    
7280 C CE    . LYS B 878 ? 1.09483 1.02913 1.75691 -0.08774 -0.06981 -0.09727 878 LYS A CE    
7281 N NZ    . LYS B 878 ? 1.15495 1.08819 1.85574 -0.08681 -0.07422 -0.08879 878 LYS A NZ    
7282 N N     . LYS B 879 ? 0.71499 0.69636 1.34979 -0.07439 -0.04626 -0.05157 879 LYS A N     
7283 C CA    . LYS B 879 ? 0.71519 0.70461 1.35662 -0.06898 -0.03696 -0.04390 879 LYS A CA    
7284 C C     . LYS B 879 ? 0.71979 0.70364 1.39161 -0.06696 -0.03662 -0.04693 879 LYS A C     
7285 O O     . LYS B 879 ? 1.01059 0.98934 1.70573 -0.06906 -0.04402 -0.04511 879 LYS A O     
7286 C CB    . LYS B 879 ? 0.73573 0.73750 1.38173 -0.06738 -0.03572 -0.02350 879 LYS A CB    
7287 C CG    . LYS B 879 ? 1.07882 1.08150 1.74424 -0.06990 -0.04366 -0.01271 879 LYS A CG    
7288 C CD    . LYS B 879 ? 0.95856 0.97109 1.61228 -0.06987 -0.04221 0.00146  879 LYS A CD    
7289 C CE    . LYS B 879 ? 0.86666 0.87831 1.48818 -0.07191 -0.04219 -0.00670 879 LYS A CE    
7290 N NZ    . LYS B 879 ? 1.23047 1.25086 1.84261 -0.07162 -0.04037 0.00665  879 LYS A NZ    
7291 N N     . GLY B 880 ? 0.78174 0.76659 1.45480 -0.06310 -0.02854 -0.05092 880 GLY A N     
7292 C CA    . GLY B 880 ? 1.04129 1.02140 1.74601 -0.06075 -0.02782 -0.05260 880 GLY A CA    
7293 C C     . GLY B 880 ? 1.02527 1.00618 1.72837 -0.05668 -0.01844 -0.05892 880 GLY A C     
7294 O O     . GLY B 880 ? 0.85846 0.84574 1.53672 -0.05556 -0.01257 -0.05872 880 GLY A O     
7295 N N     . ASP B 881 ? 1.21152 1.18617 1.94192 -0.05453 -0.01709 -0.06399 881 ASP A N     
7296 C CA    . ASP B 881 ? 0.90258 0.87812 1.63765 -0.05025 -0.00789 -0.06925 881 ASP A CA    
7297 C C     . ASP B 881 ? 1.05518 1.02150 1.76505 -0.05104 -0.00251 -0.09060 881 ASP A C     
7298 O O     . ASP B 881 ? 1.13526 1.09272 1.82839 -0.05529 -0.00728 -0.10164 881 ASP A O     
7299 C CB    . ASP B 881 ? 0.93544 0.90713 1.71031 -0.04757 -0.00809 -0.06716 881 ASP A CB    
7300 C CG    . ASP B 881 ? 1.43702 1.41505 2.23903 -0.04787 -0.01487 -0.04754 881 ASP A CG    
7301 O OD1   . ASP B 881 ? 1.65387 1.64432 2.45266 -0.04693 -0.01397 -0.03060 881 ASP A OD1   
7302 O OD2   . ASP B 881 ? 1.46963 1.43968 2.29510 -0.04934 -0.02092 -0.04943 881 ASP A OD2   
7303 N N     . ILE B 882 ? 1.05176 1.02017 1.75953 -0.04738 0.00696  -0.09566 882 ILE A N     
7304 C CA    . ILE B 882 ? 0.89157 0.85124 1.57571 -0.04787 0.01388  -0.11616 882 ILE A CA    
7305 C C     . ILE B 882 ? 1.04185 0.98470 1.73502 -0.05019 0.01103  -0.13299 882 ILE A C     
7306 O O     . ILE B 882 ? 1.03637 0.96970 1.70275 -0.05323 0.01285  -0.14991 882 ILE A O     
7307 C CB    . ILE B 882 ? 0.88919 0.85347 1.57856 -0.04300 0.02505  -0.11817 882 ILE A CB    
7308 C CG1   . ILE B 882 ? 1.08318 1.06354 1.77430 -0.04080 0.02584  -0.09843 882 ILE A CG1   
7309 C CG2   . ILE B 882 ? 0.91646 0.87490 1.57499 -0.04380 0.03308  -0.13628 882 ILE A CG2   
7310 C CD1   . ILE B 882 ? 1.01139 0.99730 1.70670 -0.03664 0.03578  -0.09913 882 ILE A CD1   
7311 N N     . GLN B 883 ? 1.04129 0.97988 1.76965 -0.04926 0.00650  -0.12877 883 GLN A N     
7312 C CA    . GLN B 883 ? 0.98141 0.90254 1.71581 -0.05186 0.00401  -0.14634 883 GLN A CA    
7313 C C     . GLN B 883 ? 1.04210 0.95701 1.75308 -0.05857 -0.00592 -0.15097 883 GLN A C     
7314 O O     . GLN B 883 ? 1.17435 1.07549 1.86613 -0.06223 -0.00588 -0.16974 883 GLN A O     
7315 C CB    . GLN B 883 ? 1.19926 1.11659 1.97760 -0.04969 0.00070  -0.14069 883 GLN A CB    
7316 C CG    . GLN B 883 ? 1.29432 1.20801 2.09655 -0.04417 0.01099  -0.14757 883 GLN A CG    
7317 C CD    . GLN B 883 ? 1.27595 1.20471 2.07839 -0.03943 0.01897  -0.13613 883 GLN A CD    
7318 O OE1   . GLN B 883 ? 1.15166 1.09450 1.95653 -0.03909 0.01497  -0.11651 883 GLN A OE1   
7319 N NE2   . GLN B 883 ? 1.40625 1.33175 2.20600 -0.03601 0.03047  -0.14843 883 GLN A NE2   
7320 N N     . GLN B 884 ? 1.07438 0.99902 1.78666 -0.06051 -0.01446 -0.13386 884 GLN A N     
7321 C CA    . GLN B 884 ? 0.98367 0.90473 1.67341 -0.06675 -0.02380 -0.13609 884 GLN A CA    
7322 C C     . GLN B 884 ? 1.03885 0.95866 1.68692 -0.06898 -0.01949 -0.14758 884 GLN A C     
7323 O O     . GLN B 884 ? 1.05648 0.96594 1.68344 -0.07466 -0.02503 -0.15967 884 GLN A O     
7324 C CB    . GLN B 884 ? 0.94198 0.87617 1.63886 -0.06739 -0.03084 -0.11437 884 GLN A CB    
7325 C CG    . GLN B 884 ? 0.94614 0.87947 1.67984 -0.06773 -0.03859 -0.10359 884 GLN A CG    
7326 C CD    . GLN B 884 ? 1.25649 1.20120 2.01710 -0.06242 -0.03423 -0.08668 884 GLN A CD    
7327 O OE1   . GLN B 884 ? 1.47692 1.42231 2.24490 -0.05813 -0.02590 -0.09011 884 GLN A OE1   
7328 N NE2   . GLN B 884 ? 0.99602 0.94981 1.77163 -0.06293 -0.03979 -0.06782 884 GLN A NE2   
7329 N N     . PHE B 885 ? 0.97757 0.90772 1.61342 -0.06498 -0.01007 -0.14352 885 PHE A N     
7330 C CA    . PHE B 885 ? 0.93394 0.86364 1.53153 -0.06672 -0.00493 -0.15374 885 PHE A CA    
7331 C C     . PHE B 885 ? 1.03121 0.94538 1.61817 -0.06798 0.00085  -0.17674 885 PHE A C     
7332 O O     . PHE B 885 ? 1.07284 0.97980 1.62772 -0.07277 -0.00021 -0.18898 885 PHE A O     
7333 C CB    . PHE B 885 ? 0.92905 0.87311 1.52036 -0.06196 0.00393  -0.14361 885 PHE A CB    
7334 C CG    . PHE B 885 ? 0.95036 0.89542 1.50409 -0.06338 0.00978  -0.15233 885 PHE A CG    
7335 C CD1   . PHE B 885 ? 1.11656 1.05496 1.64083 -0.06933 0.00419  -0.16105 885 PHE A CD1   
7336 C CD2   . PHE B 885 ? 0.89217 0.84528 1.44079 -0.05910 0.02029  -0.15069 885 PHE A CD2   
7337 C CE1   . PHE B 885 ? 0.92919 0.86868 1.41930 -0.07087 0.00943  -0.16824 885 PHE A CE1   
7338 C CE2   . PHE B 885 ? 0.88278 0.83713 1.39795 -0.06049 0.02577  -0.15802 885 PHE A CE2   
7339 C CZ    . PHE B 885 ? 0.89869 0.84622 1.38432 -0.06633 0.02051  -0.16678 885 PHE A CZ    
7340 N N     . GLY B 886 ? 0.97341 0.88195 1.58666 -0.06387 0.00736  -0.18278 886 GLY A N     
7341 C CA    . GLY B 886 ? 1.03178 0.92406 1.63686 -0.06490 0.01383  -0.20533 886 GLY A CA    
7342 C C     . GLY B 886 ? 1.09977 0.97606 1.69570 -0.07194 0.00375  -0.21735 886 GLY A C     
7343 O O     . GLY B 886 ? 1.10613 0.97163 1.67026 -0.07667 0.00485  -0.23364 886 GLY A O     
7344 N N     . LYS B 887 ? 1.21798 1.09318 1.84087 -0.07317 -0.00673 -0.20824 887 LYS A N     
7345 C CA    . LYS B 887 ? 1.31082 1.17077 1.92932 -0.08033 -0.01809 -0.21814 887 LYS A CA    
7346 C C     . LYS B 887 ? 1.25988 1.12082 1.83967 -0.08697 -0.02523 -0.21917 887 LYS A C     
7347 O O     . LYS B 887 ? 1.41335 1.25940 1.96909 -0.09299 -0.02790 -0.23628 887 LYS A O     
7348 C CB    . LYS B 887 ? 1.16443 1.02771 1.81864 -0.08042 -0.02884 -0.20295 887 LYS A CB    
7349 C CG    . LYS B 887 ? 1.19030 1.05298 1.88619 -0.07444 -0.02391 -0.19943 887 LYS A CG    
7350 C CD    . LYS B 887 ? 1.40017 1.24389 2.11419 -0.07741 -0.02873 -0.21310 887 LYS A CD    
7351 C CE    . LYS B 887 ? 1.68351 1.52973 2.44473 -0.07350 -0.03120 -0.20107 887 LYS A CE    
7352 N NZ    . LYS B 887 ? 1.40060 1.25901 2.17565 -0.07524 -0.04256 -0.17945 887 LYS A NZ    
7353 N N     . LEU B 888 ? 1.16581 1.04354 1.73866 -0.08584 -0.02738 -0.20166 888 LEU A N     
7354 C CA    . LEU B 888 ? 1.17535 1.05543 1.71362 -0.09177 -0.03425 -0.20064 888 LEU A CA    
7355 C C     . LEU B 888 ? 1.34340 1.21504 1.84439 -0.09418 -0.02654 -0.21914 888 LEU A C     
7356 O O     . LEU B 888 ? 1.45651 1.31601 1.93355 -0.10173 -0.03386 -0.23084 888 LEU A O     
7357 C CB    . LEU B 888 ? 1.14396 1.04351 1.68165 -0.08860 -0.03404 -0.17988 888 LEU A CB    
7358 C CG    . LEU B 888 ? 1.14161 1.04558 1.64582 -0.09354 -0.03948 -0.17701 888 LEU A CG    
7359 C CD1   . LEU B 888 ? 1.15229 1.04887 1.65634 -0.10099 -0.05468 -0.17669 888 LEU A CD1   
7360 C CD2   . LEU B 888 ? 1.09694 1.01920 1.60140 -0.08938 -0.03657 -0.15788 888 LEU A CD2   
7361 N N     . LEU B 889 ? 1.40513 1.28284 1.90166 -0.08838 -0.01258 -0.22127 889 LEU A N     
7362 C CA    . LEU B 889 ? 1.27534 1.14684 1.73585 -0.09032 -0.00379 -0.23736 889 LEU A CA    
7363 C C     . LEU B 889 ? 1.33356 1.18340 1.78408 -0.09553 -0.00458 -0.25958 889 LEU A C     
7364 O O     . LEU B 889 ? 1.53583 1.37724 1.95056 -0.10246 -0.00783 -0.27046 889 LEU A O     
7365 C CB    . LEU B 889 ? 1.22061 1.10064 1.68781 -0.08260 0.01190  -0.23662 889 LEU A CB    
7366 C CG    . LEU B 889 ? 1.16200 1.06073 1.61972 -0.07951 0.01476  -0.22044 889 LEU A CG    
7367 C CD1   . LEU B 889 ? 1.20137 1.10763 1.67379 -0.07197 0.02877  -0.21884 889 LEU A CD1   
7368 C CD2   . LEU B 889 ? 1.17428 1.07216 1.58927 -0.08492 0.01391  -0.22639 889 LEU A CD2   
7369 N N     . ARG B 890 ? 1.51186 1.35258 1.99253 -0.09263 -0.00193 -0.26582 890 ARG A N     
7370 C CA    . ARG B 890 ? 1.56730 1.38559 2.03907 -0.09727 -0.00119 -0.28853 890 ARG A CA    
7371 C C     . ARG B 890 ? 1.59309 1.40176 2.04404 -0.10742 -0.01768 -0.29165 890 ARG A C     
7372 O O     . ARG B 890 ? 1.61264 1.40724 2.02921 -0.11398 -0.01750 -0.30882 890 ARG A O     
7373 C CB    . ARG B 890 ? 1.41843 1.22939 1.93177 -0.09263 0.00160  -0.29130 890 ARG A CB    
7374 C CG    . ARG B 890 ? 1.32290 1.14337 1.85945 -0.08290 0.01702  -0.28741 890 ARG A CG    
7375 C CD    . ARG B 890 ? 1.37574 1.19091 1.95742 -0.07827 0.01810  -0.28662 890 ARG A CD    
7376 N NE    . ARG B 890 ? 1.39311 1.21999 2.00018 -0.06916 0.03083  -0.27890 890 ARG A NE    
7377 C CZ    . ARG B 890 ? 1.46747 1.30769 2.11021 -0.06414 0.02799  -0.25953 890 ARG A CZ    
7378 N NH1   . ARG B 890 ? 1.38185 1.22427 2.04156 -0.06682 0.01421  -0.24716 890 ARG A NH1   
7379 N NH2   . ARG B 890 ? 1.61004 1.46135 2.27145 -0.05681 0.03877  -0.25215 890 ARG A NH2   
7380 N N     . GLN B 891 ? 1.61698 1.43334 2.08779 -0.10889 -0.03134 -0.27493 891 GLN A N     
7381 C CA    . GLN B 891 ? 1.61244 1.42028 2.06879 -0.11868 -0.04837 -0.27615 891 GLN A CA    
7382 C C     . GLN B 891 ? 1.60430 1.41319 2.01521 -0.12449 -0.04990 -0.28006 891 GLN A C     
7383 O O     . GLN B 891 ? 1.77587 1.56853 2.15969 -0.13317 -0.05631 -0.29510 891 GLN A O     
7384 C CB    . GLN B 891 ? 1.73137 1.55233 2.21515 -0.11821 -0.06065 -0.25382 891 GLN A CB    
7385 C CG    . GLN B 891 ? 1.88821 1.71009 2.41812 -0.11277 -0.06027 -0.24672 891 GLN A CG    
7386 C CD    . GLN B 891 ? 1.57257 1.41076 2.12846 -0.11084 -0.06869 -0.22253 891 GLN A CD    
7387 O OE1   . GLN B 891 ? 1.28150 1.12260 1.87474 -0.10687 -0.06956 -0.21345 891 GLN A OE1   
7388 N NE2   . GLN B 891 ? 1.24684 1.09569 1.78333 -0.11367 -0.07456 -0.21162 891 GLN A NE2   
7389 N N     . ILE B 892 ? 1.46708 1.29383 1.86962 -0.12018 -0.04433 -0.26704 892 ILE A N     
7390 C CA    . ILE B 892 ? 1.47633 1.30580 1.83744 -0.12558 -0.04647 -0.26823 892 ILE A CA    
7391 C C     . ILE B 892 ? 1.63819 1.45304 1.96681 -0.12839 -0.03623 -0.29080 892 ILE A C     
7392 O O     . ILE B 892 ? 1.77203 1.57753 2.06576 -0.13724 -0.04320 -0.29958 892 ILE A O     
7393 C CB    . ILE B 892 ? 1.42740 1.27827 1.78890 -0.11950 -0.04077 -0.25042 892 ILE A CB    
7394 C CG1   . ILE B 892 ? 1.44895 1.31317 1.84745 -0.11485 -0.04641 -0.22970 892 ILE A CG1   
7395 C CG2   . ILE B 892 ? 1.58785 1.44272 1.91240 -0.12546 -0.04621 -0.24782 892 ILE A CG2   
7396 C CD1   . ILE B 892 ? 1.36202 1.24589 1.76326 -0.10835 -0.03950 -0.21289 892 ILE A CD1   
7397 N N     . GLN B 893 ? 1.60811 1.42111 1.94832 -0.12132 -0.02025 -0.29932 893 GLN A N     
7398 C CA    . GLN B 893 ? 1.64983 1.44927 1.96099 -0.12304 -0.00773 -0.32097 893 GLN A CA    
7399 C C     . GLN B 893 ? 1.89450 1.66995 2.19555 -0.13111 -0.01454 -0.34004 893 GLN A C     
7400 O O     . GLN B 893 ? 2.07683 1.83936 2.33904 -0.13780 -0.01213 -0.35623 893 GLN A O     
7401 C CB    . GLN B 893 ? 1.73248 1.53639 2.06539 -0.11295 0.01079  -0.32389 893 GLN A CB    
7402 C CG    . GLN B 893 ? 1.84224 1.63710 2.14611 -0.11309 0.02670  -0.34270 893 GLN A CG    
7403 C CD    . GLN B 893 ? 1.86768 1.67110 2.13269 -0.11643 0.02806  -0.33950 893 GLN A CD    
7404 O OE1   . GLN B 893 ? 2.06481 1.85611 2.29127 -0.12424 0.02724  -0.35320 893 GLN A OE1   
7405 N NE2   . GLN B 893 ? 1.69851 1.52248 1.97275 -0.11091 0.02994  -0.32118 893 GLN A NE2   
7406 N N     . LYS B 894 ? 1.94634 1.71568 2.28009 -0.13095 -0.02296 -0.33799 894 LYS A N     
7407 C CA    . LYS B 894 ? 1.89699 1.64211 2.22432 -0.13857 -0.02967 -0.35658 894 LYS A CA    
7408 C C     . LYS B 894 ? 1.87764 1.61865 2.18813 -0.14952 -0.05083 -0.35174 894 LYS A C     
7409 O O     . LYS B 894 ? 1.91811 1.64094 2.23016 -0.15641 -0.06084 -0.36252 894 LYS A O     
7410 C CB    . LYS B 894 ? 1.89662 1.63611 2.26919 -0.13341 -0.02885 -0.35703 894 LYS A CB    
7411 C CG    . LYS B 894 ? 2.00010 1.74291 2.39574 -0.12267 -0.00927 -0.36098 894 LYS A CG    
7412 C CD    . LYS B 894 ? 2.11784 1.86006 2.56357 -0.11695 -0.01056 -0.35508 894 LYS A CD    
7413 C CE    . LYS B 894 ? 1.96259 1.71008 2.43385 -0.10633 0.00763  -0.35623 894 LYS A CE    
7414 N NZ    . LYS B 894 ? 1.86423 1.61214 2.38456 -0.10117 0.00523  -0.34856 894 LYS A NZ    
7415 N N     . LYS B 895 ? 1.83159 1.58848 2.12752 -0.15119 -0.05753 -0.33609 895 LYS A N     
7416 C CA    . LYS B 895 ? 2.00559 1.75962 2.28572 -0.16177 -0.07784 -0.33034 895 LYS A CA    
7417 C C     . LYS B 895 ? 2.23216 1.96519 2.46730 -0.17274 -0.08094 -0.35143 895 LYS A C     
7418 O O     . LYS B 895 ? 2.37686 2.10241 2.59840 -0.18318 -0.09901 -0.35049 895 LYS A O     
7419 C CB    . LYS B 895 ? 1.75922 1.53482 2.03467 -0.16054 -0.08283 -0.30906 895 LYS A CB    
7420 C CG    . LYS B 895 ? 1.88429 1.67705 2.20256 -0.15378 -0.08723 -0.28689 895 LYS A CG    
7421 C CD    . LYS B 895 ? 1.92219 1.73399 2.23596 -0.15354 -0.09342 -0.26645 895 LYS A CD    
7422 C CE    . LYS B 895 ? 1.91517 1.74285 2.26982 -0.14662 -0.09552 -0.24570 895 LYS A CE    
7423 N NZ    . LYS B 895 ? 1.73079 1.57585 2.08061 -0.14595 -0.09968 -0.22702 895 LYS A NZ    
7424 N N     . LYS B 896 ? 2.13278 1.85671 2.34592 -0.17073 -0.06403 -0.36923 896 LYS A N     
7425 C CA    . LYS B 896 ? 2.12029 1.82254 2.28810 -0.18126 -0.06489 -0.39098 896 LYS A CA    
7426 C C     . LYS B 896 ? 2.14983 1.85509 2.28514 -0.19190 -0.08180 -0.38294 896 LYS A C     
7427 O O     . LYS B 896 ? 2.02704 1.71590 2.14762 -0.20313 -0.09754 -0.39050 896 LYS A O     
7428 C CB    . LYS B 896 ? 2.04305 1.72136 2.21953 -0.18646 -0.07055 -0.40773 896 LYS A CB    
7429 C CG    . LYS B 896 ? 1.99137 1.66494 2.20285 -0.17651 -0.05519 -0.41588 896 LYS A CG    
7430 C CD    . LYS B 896 ? 2.10059 1.75009 2.32234 -0.18214 -0.06255 -0.43141 896 LYS A CD    
7431 C CE    . LYS B 896 ? 2.31737 1.96226 2.57634 -0.17220 -0.04780 -0.43857 896 LYS A CE    
7432 N NZ    . LYS B 896 ? 2.19536 1.81626 2.46434 -0.17792 -0.05534 -0.45361 896 LYS A NZ    
# 
