data_8Y9T
# 
_entry.id   8Y9T 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8Y9T         pdb_00008y9t 10.2210/pdb8y9t/pdb 
WWPDB D_1300045100 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        8Y9T 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-07 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yuding@fudan.edu.cn 
_pdbx_contact_author.name_first         Yu 
_pdbx_contact_author.name_last          Ding 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7772-6449 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ding, Y.'    1 0000-0001-7772-6449 
'Zhong, P.Y.' 2 0000-0002-3250-7645 
# 
_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                     'Crystal structure of nanobody MY632X bound to human serum albumin (HSA)' 
_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 'Ding, Y.'    1 0000-0001-7772-6449 
primary 'Zhong, P.Y.' 2 0000-0002-3250-7645 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man Albumin           67346.156 1  ? ? ? ? 
2 polymer man 'nanobody MY6322' 13829.351 1  ? ? ? ? 
3 water   nat water             18.015    53 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        HSA 
# 
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 'polypeptide(L)' no no 
;RGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKL
CTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPEL
LFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKL
VTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD
VCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCEL
FEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVT
KCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAF
VEKCCKADDKETCFAEEGKKLVAASQAALGL
;
;RGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKL
CTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPEL
LFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKL
VTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD
VCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCEL
FEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVT
KCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAF
VEKCCKADDKETCFAEEGKKLVAASQAALGL
;
A ? 
2 'polypeptide(L)' no no 
;EVQLQESGGGLVQPGGSLRLSCAASGFTFSRYWMFWVRQAPGKGLEWISDINSGGTYTRYADSVKGRFTISRDNAKNTLY
LQMNSLRAEDTAVYYCATNSGDGKRYCSGGYCYRSRGQGTLVTVSS
;
;EVQLQESGGGLVQPGGSLRLSCAASGFTFSRYWMFWVRQAPGKGLEWISDINSGGTYTRYADSVKGRFTISRDNAKNTLY
LQMNSLRAEDTAVYYCATNSGDGKRYCSGGYCYRSRGQGTLVTVSS
;
B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   GLY n 
1 3   VAL n 
1 4   PHE n 
1 5   ARG n 
1 6   ARG n 
1 7   ASP n 
1 8   ALA n 
1 9   HIS n 
1 10  LYS n 
1 11  SER n 
1 12  GLU n 
1 13  VAL n 
1 14  ALA n 
1 15  HIS n 
1 16  ARG n 
1 17  PHE n 
1 18  LYS n 
1 19  ASP n 
1 20  LEU n 
1 21  GLY n 
1 22  GLU n 
1 23  GLU n 
1 24  ASN n 
1 25  PHE n 
1 26  LYS n 
1 27  ALA n 
1 28  LEU n 
1 29  VAL n 
1 30  LEU n 
1 31  ILE n 
1 32  ALA n 
1 33  PHE n 
1 34  ALA n 
1 35  GLN n 
1 36  TYR n 
1 37  LEU n 
1 38  GLN n 
1 39  GLN n 
1 40  CYS n 
1 41  PRO n 
1 42  PHE n 
1 43  GLU n 
1 44  ASP n 
1 45  HIS n 
1 46  VAL n 
1 47  LYS n 
1 48  LEU n 
1 49  VAL n 
1 50  ASN n 
1 51  GLU n 
1 52  VAL n 
1 53  THR n 
1 54  GLU n 
1 55  PHE n 
1 56  ALA n 
1 57  LYS n 
1 58  THR n 
1 59  CYS n 
1 60  VAL n 
1 61  ALA n 
1 62  ASP n 
1 63  GLU n 
1 64  SER n 
1 65  ALA n 
1 66  GLU n 
1 67  ASN n 
1 68  CYS n 
1 69  ASP n 
1 70  LYS n 
1 71  SER n 
1 72  LEU n 
1 73  HIS n 
1 74  THR n 
1 75  LEU n 
1 76  PHE n 
1 77  GLY n 
1 78  ASP n 
1 79  LYS n 
1 80  LEU n 
1 81  CYS n 
1 82  THR n 
1 83  VAL n 
1 84  ALA n 
1 85  THR n 
1 86  LEU n 
1 87  ARG n 
1 88  GLU n 
1 89  THR n 
1 90  TYR n 
1 91  GLY n 
1 92  GLU n 
1 93  MET n 
1 94  ALA n 
1 95  ASP n 
1 96  CYS n 
1 97  CYS n 
1 98  ALA n 
1 99  LYS n 
1 100 GLN n 
1 101 GLU n 
1 102 PRO n 
1 103 GLU n 
1 104 ARG n 
1 105 ASN n 
1 106 GLU n 
1 107 CYS n 
1 108 PHE n 
1 109 LEU n 
1 110 GLN n 
1 111 HIS n 
1 112 LYS n 
1 113 ASP n 
1 114 ASP n 
1 115 ASN n 
1 116 PRO n 
1 117 ASN n 
1 118 LEU n 
1 119 PRO n 
1 120 ARG n 
1 121 LEU n 
1 122 VAL n 
1 123 ARG n 
1 124 PRO n 
1 125 GLU n 
1 126 VAL n 
1 127 ASP n 
1 128 VAL n 
1 129 MET n 
1 130 CYS n 
1 131 THR n 
1 132 ALA n 
1 133 PHE n 
1 134 HIS n 
1 135 ASP n 
1 136 ASN n 
1 137 GLU n 
1 138 GLU n 
1 139 THR n 
1 140 PHE n 
1 141 LEU n 
1 142 LYS n 
1 143 LYS n 
1 144 TYR n 
1 145 LEU n 
1 146 TYR n 
1 147 GLU n 
1 148 ILE n 
1 149 ALA n 
1 150 ARG n 
1 151 ARG n 
1 152 HIS n 
1 153 PRO n 
1 154 TYR n 
1 155 PHE n 
1 156 TYR n 
1 157 ALA n 
1 158 PRO n 
1 159 GLU n 
1 160 LEU n 
1 161 LEU n 
1 162 PHE n 
1 163 PHE n 
1 164 ALA n 
1 165 LYS n 
1 166 ARG n 
1 167 TYR n 
1 168 LYS n 
1 169 ALA n 
1 170 ALA n 
1 171 PHE n 
1 172 THR n 
1 173 GLU n 
1 174 CYS n 
1 175 CYS n 
1 176 GLN n 
1 177 ALA n 
1 178 ALA n 
1 179 ASP n 
1 180 LYS n 
1 181 ALA n 
1 182 ALA n 
1 183 CYS n 
1 184 LEU n 
1 185 LEU n 
1 186 PRO n 
1 187 LYS n 
1 188 LEU n 
1 189 ASP n 
1 190 GLU n 
1 191 LEU n 
1 192 ARG n 
1 193 ASP n 
1 194 GLU n 
1 195 GLY n 
1 196 LYS n 
1 197 ALA n 
1 198 SER n 
1 199 SER n 
1 200 ALA n 
1 201 LYS n 
1 202 GLN n 
1 203 ARG n 
1 204 LEU n 
1 205 LYS n 
1 206 CYS n 
1 207 ALA n 
1 208 SER n 
1 209 LEU n 
1 210 GLN n 
1 211 LYS n 
1 212 PHE n 
1 213 GLY n 
1 214 GLU n 
1 215 ARG n 
1 216 ALA n 
1 217 PHE n 
1 218 LYS n 
1 219 ALA n 
1 220 TRP n 
1 221 ALA n 
1 222 VAL n 
1 223 ALA n 
1 224 ARG n 
1 225 LEU n 
1 226 SER n 
1 227 GLN n 
1 228 ARG n 
1 229 PHE n 
1 230 PRO n 
1 231 LYS n 
1 232 ALA n 
1 233 GLU n 
1 234 PHE n 
1 235 ALA n 
1 236 GLU n 
1 237 VAL n 
1 238 SER n 
1 239 LYS n 
1 240 LEU n 
1 241 VAL n 
1 242 THR n 
1 243 ASP n 
1 244 LEU n 
1 245 THR n 
1 246 LYS n 
1 247 VAL n 
1 248 HIS n 
1 249 THR n 
1 250 GLU n 
1 251 CYS n 
1 252 CYS n 
1 253 HIS n 
1 254 GLY n 
1 255 ASP n 
1 256 LEU n 
1 257 LEU n 
1 258 GLU n 
1 259 CYS n 
1 260 ALA n 
1 261 ASP n 
1 262 ASP n 
1 263 ARG n 
1 264 ALA n 
1 265 ASP n 
1 266 LEU n 
1 267 ALA n 
1 268 LYS n 
1 269 TYR n 
1 270 ILE n 
1 271 CYS n 
1 272 GLU n 
1 273 ASN n 
1 274 GLN n 
1 275 ASP n 
1 276 SER n 
1 277 ILE n 
1 278 SER n 
1 279 SER n 
1 280 LYS n 
1 281 LEU n 
1 282 LYS n 
1 283 GLU n 
1 284 CYS n 
1 285 CYS n 
1 286 GLU n 
1 287 LYS n 
1 288 PRO n 
1 289 LEU n 
1 290 LEU n 
1 291 GLU n 
1 292 LYS n 
1 293 SER n 
1 294 HIS n 
1 295 CYS n 
1 296 ILE n 
1 297 ALA n 
1 298 GLU n 
1 299 VAL n 
1 300 GLU n 
1 301 ASN n 
1 302 ASP n 
1 303 GLU n 
1 304 MET n 
1 305 PRO n 
1 306 ALA n 
1 307 ASP n 
1 308 LEU n 
1 309 PRO n 
1 310 SER n 
1 311 LEU n 
1 312 ALA n 
1 313 ALA n 
1 314 ASP n 
1 315 PHE n 
1 316 VAL n 
1 317 GLU n 
1 318 SER n 
1 319 LYS n 
1 320 ASP n 
1 321 VAL n 
1 322 CYS n 
1 323 LYS n 
1 324 ASN n 
1 325 TYR n 
1 326 ALA n 
1 327 GLU n 
1 328 ALA n 
1 329 LYS n 
1 330 ASP n 
1 331 VAL n 
1 332 PHE n 
1 333 LEU n 
1 334 GLY n 
1 335 MET n 
1 336 PHE n 
1 337 LEU n 
1 338 TYR n 
1 339 GLU n 
1 340 TYR n 
1 341 ALA n 
1 342 ARG n 
1 343 ARG n 
1 344 HIS n 
1 345 PRO n 
1 346 ASP n 
1 347 TYR n 
1 348 SER n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 LEU n 
1 353 LEU n 
1 354 ARG n 
1 355 LEU n 
1 356 ALA n 
1 357 LYS n 
1 358 THR n 
1 359 TYR n 
1 360 GLU n 
1 361 THR n 
1 362 THR n 
1 363 LEU n 
1 364 GLU n 
1 365 LYS n 
1 366 CYS n 
1 367 CYS n 
1 368 ALA n 
1 369 ALA n 
1 370 ALA n 
1 371 ASP n 
1 372 PRO n 
1 373 HIS n 
1 374 GLU n 
1 375 CYS n 
1 376 TYR n 
1 377 ALA n 
1 378 LYS n 
1 379 VAL n 
1 380 PHE n 
1 381 ASP n 
1 382 GLU n 
1 383 PHE n 
1 384 LYS n 
1 385 PRO n 
1 386 LEU n 
1 387 VAL n 
1 388 GLU n 
1 389 GLU n 
1 390 PRO n 
1 391 GLN n 
1 392 ASN n 
1 393 LEU n 
1 394 ILE n 
1 395 LYS n 
1 396 GLN n 
1 397 ASN n 
1 398 CYS n 
1 399 GLU n 
1 400 LEU n 
1 401 PHE n 
1 402 GLU n 
1 403 GLN n 
1 404 LEU n 
1 405 GLY n 
1 406 GLU n 
1 407 TYR n 
1 408 LYS n 
1 409 PHE n 
1 410 GLN n 
1 411 ASN n 
1 412 ALA n 
1 413 LEU n 
1 414 LEU n 
1 415 VAL n 
1 416 ARG n 
1 417 TYR n 
1 418 THR n 
1 419 LYS n 
1 420 LYS n 
1 421 VAL n 
1 422 PRO n 
1 423 GLN n 
1 424 VAL n 
1 425 SER n 
1 426 THR n 
1 427 PRO n 
1 428 THR n 
1 429 LEU n 
1 430 VAL n 
1 431 GLU n 
1 432 VAL n 
1 433 SER n 
1 434 ARG n 
1 435 ASN n 
1 436 LEU n 
1 437 GLY n 
1 438 LYS n 
1 439 VAL n 
1 440 GLY n 
1 441 SER n 
1 442 LYS n 
1 443 CYS n 
1 444 CYS n 
1 445 LYS n 
1 446 HIS n 
1 447 PRO n 
1 448 GLU n 
1 449 ALA n 
1 450 LYS n 
1 451 ARG n 
1 452 MET n 
1 453 PRO n 
1 454 CYS n 
1 455 ALA n 
1 456 GLU n 
1 457 ASP n 
1 458 TYR n 
1 459 LEU n 
1 460 SER n 
1 461 VAL n 
1 462 VAL n 
1 463 LEU n 
1 464 ASN n 
1 465 GLN n 
1 466 LEU n 
1 467 CYS n 
1 468 VAL n 
1 469 LEU n 
1 470 HIS n 
1 471 GLU n 
1 472 LYS n 
1 473 THR n 
1 474 PRO n 
1 475 VAL n 
1 476 SER n 
1 477 ASP n 
1 478 ARG n 
1 479 VAL n 
1 480 THR n 
1 481 LYS n 
1 482 CYS n 
1 483 CYS n 
1 484 THR n 
1 485 GLU n 
1 486 SER n 
1 487 LEU n 
1 488 VAL n 
1 489 ASN n 
1 490 ARG n 
1 491 ARG n 
1 492 PRO n 
1 493 CYS n 
1 494 PHE n 
1 495 SER n 
1 496 ALA n 
1 497 LEU n 
1 498 GLU n 
1 499 VAL n 
1 500 ASP n 
1 501 GLU n 
1 502 THR n 
1 503 TYR n 
1 504 VAL n 
1 505 PRO n 
1 506 LYS n 
1 507 GLU n 
1 508 PHE n 
1 509 ASN n 
1 510 ALA n 
1 511 GLU n 
1 512 THR n 
1 513 PHE n 
1 514 THR n 
1 515 PHE n 
1 516 HIS n 
1 517 ALA n 
1 518 ASP n 
1 519 ILE n 
1 520 CYS n 
1 521 THR n 
1 522 LEU n 
1 523 SER n 
1 524 GLU n 
1 525 LYS n 
1 526 GLU n 
1 527 ARG n 
1 528 GLN n 
1 529 ILE n 
1 530 LYS n 
1 531 LYS n 
1 532 GLN n 
1 533 THR n 
1 534 ALA n 
1 535 LEU n 
1 536 VAL n 
1 537 GLU n 
1 538 LEU n 
1 539 VAL n 
1 540 LYS n 
1 541 HIS n 
1 542 LYS n 
1 543 PRO n 
1 544 LYS n 
1 545 ALA n 
1 546 THR n 
1 547 LYS n 
1 548 GLU n 
1 549 GLN n 
1 550 LEU n 
1 551 LYS n 
1 552 ALA n 
1 553 VAL n 
1 554 MET n 
1 555 ASP n 
1 556 ASP n 
1 557 PHE n 
1 558 ALA n 
1 559 ALA n 
1 560 PHE n 
1 561 VAL n 
1 562 GLU n 
1 563 LYS n 
1 564 CYS n 
1 565 CYS n 
1 566 LYS n 
1 567 ALA n 
1 568 ASP n 
1 569 ASP n 
1 570 LYS n 
1 571 GLU n 
1 572 THR n 
1 573 CYS n 
1 574 PHE n 
1 575 ALA n 
1 576 GLU n 
1 577 GLU n 
1 578 GLY n 
1 579 LYS n 
1 580 LYS n 
1 581 LEU n 
1 582 VAL n 
1 583 ALA n 
1 584 ALA n 
1 585 SER n 
1 586 GLN n 
1 587 ALA n 
1 588 ALA n 
1 589 LEU n 
1 590 GLY n 
1 591 LEU n 
2 1   GLU n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   GLN n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  ALA n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  THR n 
2 29  PHE n 
2 30  SER n 
2 31  ARG n 
2 32  TYR n 
2 33  TRP n 
2 34  MET n 
2 35  PHE n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  ILE n 
2 49  SER n 
2 50  ASP n 
2 51  ILE n 
2 52  ASN n 
2 53  SER n 
2 54  GLY n 
2 55  GLY n 
2 56  THR n 
2 57  TYR n 
2 58  THR n 
2 59  ARG n 
2 60  TYR n 
2 61  ALA n 
2 62  ASP n 
2 63  SER n 
2 64  VAL n 
2 65  LYS n 
2 66  GLY n 
2 67  ARG n 
2 68  PHE n 
2 69  THR n 
2 70  ILE n 
2 71  SER n 
2 72  ARG n 
2 73  ASP n 
2 74  ASN n 
2 75  ALA n 
2 76  LYS n 
2 77  ASN n 
2 78  THR n 
2 79  LEU n 
2 80  TYR n 
2 81  LEU n 
2 82  GLN n 
2 83  MET n 
2 84  ASN n 
2 85  SER n 
2 86  LEU n 
2 87  ARG n 
2 88  ALA n 
2 89  GLU n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  THR n 
2 99  ASN n 
2 100 SER n 
2 101 GLY n 
2 102 ASP n 
2 103 GLY n 
2 104 LYS n 
2 105 ARG n 
2 106 TYR n 
2 107 CYS n 
2 108 SER n 
2 109 GLY n 
2 110 GLY n 
2 111 TYR n 
2 112 CYS n 
2 113 TYR n 
2 114 ARG n 
2 115 SER n 
2 116 ARG n 
2 117 GLY n 
2 118 GLN n 
2 119 GLY n 
2 120 THR n 
2 121 LEU n 
2 122 VAL n 
2 123 THR n 
2 124 VAL n 
2 125 SER n 
2 126 SER n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 591 human ? 'ALB, GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696/PRO1341' ? 
? ? ? ? ? 'Homo sapiens'  9606  ? ? ? ? ? ? ? ? 'Oryza sativa'             4530 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 126 ?     ? ?                                                                                ? 
? ? ? ? ? 'Vicugna pacos' 30538 ? ? ? ? ? ? ? ? 'Saccharomyces cerevisiae' 4932 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
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   ARG 1   -5  ?   ?   ?   A . n 
A 1 2   GLY 2   -4  ?   ?   ?   A . n 
A 1 3   VAL 3   -3  ?   ?   ?   A . n 
A 1 4   PHE 4   -2  ?   ?   ?   A . n 
A 1 5   ARG 5   -1  ?   ?   ?   A . n 
A 1 6   ARG 6   0   ?   ?   ?   A . n 
A 1 7   ASP 7   1   ?   ?   ?   A . n 
A 1 8   ALA 8   2   ?   ?   ?   A . n 
A 1 9   HIS 9   3   ?   ?   ?   A . n 
A 1 10  LYS 10  4   ?   ?   ?   A . n 
A 1 11  SER 11  5   5   SER SER A . n 
A 1 12  GLU 12  6   6   GLU GLU A . n 
A 1 13  VAL 13  7   7   VAL VAL A . n 
A 1 14  ALA 14  8   8   ALA ALA A . n 
A 1 15  HIS 15  9   9   HIS HIS A . n 
A 1 16  ARG 16  10  10  ARG ARG A . n 
A 1 17  PHE 17  11  11  PHE PHE A . n 
A 1 18  LYS 18  12  12  LYS LYS A . n 
A 1 19  ASP 19  13  13  ASP ASP A . n 
A 1 20  LEU 20  14  14  LEU LEU A . n 
A 1 21  GLY 21  15  15  GLY GLY A . n 
A 1 22  GLU 22  16  16  GLU GLU A . n 
A 1 23  GLU 23  17  17  GLU GLU A . n 
A 1 24  ASN 24  18  18  ASN ASN A . n 
A 1 25  PHE 25  19  19  PHE PHE A . n 
A 1 26  LYS 26  20  20  LYS LYS A . n 
A 1 27  ALA 27  21  21  ALA ALA A . n 
A 1 28  LEU 28  22  22  LEU LEU A . n 
A 1 29  VAL 29  23  23  VAL VAL A . n 
A 1 30  LEU 30  24  24  LEU LEU A . n 
A 1 31  ILE 31  25  25  ILE ILE A . n 
A 1 32  ALA 32  26  26  ALA ALA A . n 
A 1 33  PHE 33  27  27  PHE PHE A . n 
A 1 34  ALA 34  28  28  ALA ALA A . n 
A 1 35  GLN 35  29  29  GLN GLN A . n 
A 1 36  TYR 36  30  30  TYR TYR A . n 
A 1 37  LEU 37  31  31  LEU LEU A . n 
A 1 38  GLN 38  32  32  GLN GLN A . n 
A 1 39  GLN 39  33  ?   ?   ?   A . n 
A 1 40  CYS 40  34  ?   ?   ?   A . n 
A 1 41  PRO 41  35  ?   ?   ?   A . n 
A 1 42  PHE 42  36  ?   ?   ?   A . n 
A 1 43  GLU 43  37  37  GLU GLU A . n 
A 1 44  ASP 44  38  38  ASP ASP A . n 
A 1 45  HIS 45  39  39  HIS HIS A . n 
A 1 46  VAL 46  40  40  VAL VAL A . n 
A 1 47  LYS 47  41  41  LYS LYS A . n 
A 1 48  LEU 48  42  42  LEU LEU A . n 
A 1 49  VAL 49  43  43  VAL VAL A . n 
A 1 50  ASN 50  44  44  ASN ASN A . n 
A 1 51  GLU 51  45  45  GLU GLU A . n 
A 1 52  VAL 52  46  46  VAL VAL A . n 
A 1 53  THR 53  47  47  THR THR A . n 
A 1 54  GLU 54  48  48  GLU GLU A . n 
A 1 55  PHE 55  49  49  PHE PHE A . n 
A 1 56  ALA 56  50  50  ALA ALA A . n 
A 1 57  LYS 57  51  51  LYS LYS A . n 
A 1 58  THR 58  52  52  THR THR A . n 
A 1 59  CYS 59  53  53  CYS CYS A . n 
A 1 60  VAL 60  54  54  VAL VAL A . n 
A 1 61  ALA 61  55  ?   ?   ?   A . n 
A 1 62  ASP 62  56  ?   ?   ?   A . n 
A 1 63  GLU 63  57  ?   ?   ?   A . n 
A 1 64  SER 64  58  58  SER SER A . n 
A 1 65  ALA 65  59  59  ALA ALA A . n 
A 1 66  GLU 66  60  60  GLU GLU A . n 
A 1 67  ASN 67  61  61  ASN ASN A . n 
A 1 68  CYS 68  62  62  CYS CYS A . n 
A 1 69  ASP 69  63  63  ASP ASP A . n 
A 1 70  LYS 70  64  64  LYS LYS A . n 
A 1 71  SER 71  65  65  SER SER A . n 
A 1 72  LEU 72  66  66  LEU LEU A . n 
A 1 73  HIS 73  67  67  HIS HIS A . n 
A 1 74  THR 74  68  68  THR THR A . n 
A 1 75  LEU 75  69  69  LEU LEU A . n 
A 1 76  PHE 76  70  70  PHE PHE A . n 
A 1 77  GLY 77  71  71  GLY GLY A . n 
A 1 78  ASP 78  72  72  ASP ASP A . n 
A 1 79  LYS 79  73  73  LYS LYS A . n 
A 1 80  LEU 80  74  74  LEU LEU A . n 
A 1 81  CYS 81  75  75  CYS CYS A . n 
A 1 82  THR 82  76  76  THR THR A . n 
A 1 83  VAL 83  77  ?   ?   ?   A . n 
A 1 84  ALA 84  78  ?   ?   ?   A . n 
A 1 85  THR 85  79  ?   ?   ?   A . n 
A 1 86  LEU 86  80  ?   ?   ?   A . n 
A 1 87  ARG 87  81  ?   ?   ?   A . n 
A 1 88  GLU 88  82  ?   ?   ?   A . n 
A 1 89  THR 89  83  ?   ?   ?   A . n 
A 1 90  TYR 90  84  ?   ?   ?   A . n 
A 1 91  GLY 91  85  ?   ?   ?   A . n 
A 1 92  GLU 92  86  ?   ?   ?   A . n 
A 1 93  MET 93  87  ?   ?   ?   A . n 
A 1 94  ALA 94  88  ?   ?   ?   A . n 
A 1 95  ASP 95  89  89  ASP ASP A . n 
A 1 96  CYS 96  90  90  CYS CYS A . n 
A 1 97  CYS 97  91  91  CYS CYS A . n 
A 1 98  ALA 98  92  92  ALA ALA A . n 
A 1 99  LYS 99  93  93  LYS LYS A . n 
A 1 100 GLN 100 94  94  GLN GLN A . n 
A 1 101 GLU 101 95  95  GLU GLU A . n 
A 1 102 PRO 102 96  96  PRO PRO A . n 
A 1 103 GLU 103 97  97  GLU GLU A . n 
A 1 104 ARG 104 98  98  ARG ARG A . n 
A 1 105 ASN 105 99  99  ASN ASN A . n 
A 1 106 GLU 106 100 100 GLU GLU A . n 
A 1 107 CYS 107 101 101 CYS CYS A . n 
A 1 108 PHE 108 102 102 PHE PHE A . n 
A 1 109 LEU 109 103 103 LEU LEU A . n 
A 1 110 GLN 110 104 104 GLN GLN A . n 
A 1 111 HIS 111 105 105 HIS HIS A . n 
A 1 112 LYS 112 106 ?   ?   ?   A . n 
A 1 113 ASP 113 107 ?   ?   ?   A . n 
A 1 114 ASP 114 108 ?   ?   ?   A . n 
A 1 115 ASN 115 109 ?   ?   ?   A . n 
A 1 116 PRO 116 110 ?   ?   ?   A . n 
A 1 117 ASN 117 111 ?   ?   ?   A . n 
A 1 118 LEU 118 112 ?   ?   ?   A . n 
A 1 119 PRO 119 113 ?   ?   ?   A . n 
A 1 120 ARG 120 114 ?   ?   ?   A . n 
A 1 121 LEU 121 115 ?   ?   ?   A . n 
A 1 122 VAL 122 116 ?   ?   ?   A . n 
A 1 123 ARG 123 117 ?   ?   ?   A . n 
A 1 124 PRO 124 118 ?   ?   ?   A . n 
A 1 125 GLU 125 119 119 GLU GLU A . n 
A 1 126 VAL 126 120 120 VAL VAL A . n 
A 1 127 ASP 127 121 121 ASP ASP A . n 
A 1 128 VAL 128 122 122 VAL VAL A . n 
A 1 129 MET 129 123 123 MET MET A . n 
A 1 130 CYS 130 124 124 CYS CYS A . n 
A 1 131 THR 131 125 125 THR THR A . n 
A 1 132 ALA 132 126 126 ALA ALA A . n 
A 1 133 PHE 133 127 127 PHE PHE A . n 
A 1 134 HIS 134 128 ?   ?   ?   A . n 
A 1 135 ASP 135 129 ?   ?   ?   A . n 
A 1 136 ASN 136 130 130 ASN ASN A . n 
A 1 137 GLU 137 131 131 GLU GLU A . n 
A 1 138 GLU 138 132 132 GLU GLU A . n 
A 1 139 THR 139 133 133 THR THR A . n 
A 1 140 PHE 140 134 134 PHE PHE A . n 
A 1 141 LEU 141 135 135 LEU LEU A . n 
A 1 142 LYS 142 136 136 LYS LYS A . n 
A 1 143 LYS 143 137 137 LYS LYS A . n 
A 1 144 TYR 144 138 138 TYR TYR A . n 
A 1 145 LEU 145 139 139 LEU LEU A . n 
A 1 146 TYR 146 140 140 TYR TYR A . n 
A 1 147 GLU 147 141 141 GLU GLU A . n 
A 1 148 ILE 148 142 142 ILE ILE A . n 
A 1 149 ALA 149 143 143 ALA ALA A . n 
A 1 150 ARG 150 144 144 ARG ARG A . n 
A 1 151 ARG 151 145 145 ARG ARG A . n 
A 1 152 HIS 152 146 146 HIS HIS A . n 
A 1 153 PRO 153 147 147 PRO PRO A . n 
A 1 154 TYR 154 148 148 TYR TYR A . n 
A 1 155 PHE 155 149 149 PHE PHE A . n 
A 1 156 TYR 156 150 150 TYR TYR A . n 
A 1 157 ALA 157 151 151 ALA ALA A . n 
A 1 158 PRO 158 152 152 PRO PRO A . n 
A 1 159 GLU 159 153 153 GLU GLU A . n 
A 1 160 LEU 160 154 154 LEU LEU A . n 
A 1 161 LEU 161 155 155 LEU LEU A . n 
A 1 162 PHE 162 156 156 PHE PHE A . n 
A 1 163 PHE 163 157 157 PHE PHE A . n 
A 1 164 ALA 164 158 158 ALA ALA A . n 
A 1 165 LYS 165 159 159 LYS LYS A . n 
A 1 166 ARG 166 160 160 ARG ARG A . n 
A 1 167 TYR 167 161 161 TYR TYR A . n 
A 1 168 LYS 168 162 162 LYS LYS A . n 
A 1 169 ALA 169 163 163 ALA ALA A . n 
A 1 170 ALA 170 164 164 ALA ALA A . n 
A 1 171 PHE 171 165 165 PHE PHE A . n 
A 1 172 THR 172 166 166 THR THR A . n 
A 1 173 GLU 173 167 167 GLU GLU A . n 
A 1 174 CYS 174 168 168 CYS CYS A . n 
A 1 175 CYS 175 169 169 CYS CYS A . n 
A 1 176 GLN 176 170 170 GLN GLN A . n 
A 1 177 ALA 177 171 171 ALA ALA A . n 
A 1 178 ALA 178 172 172 ALA ALA A . n 
A 1 179 ASP 179 173 173 ASP ASP A . n 
A 1 180 LYS 180 174 ?   ?   ?   A . n 
A 1 181 ALA 181 175 ?   ?   ?   A . n 
A 1 182 ALA 182 176 ?   ?   ?   A . n 
A 1 183 CYS 183 177 177 CYS CYS A . n 
A 1 184 LEU 184 178 178 LEU LEU A . n 
A 1 185 LEU 185 179 179 LEU LEU A . n 
A 1 186 PRO 186 180 180 PRO PRO A . n 
A 1 187 LYS 187 181 181 LYS LYS A . n 
A 1 188 LEU 188 182 182 LEU LEU A . n 
A 1 189 ASP 189 183 183 ASP ASP A . n 
A 1 190 GLU 190 184 184 GLU GLU A . n 
A 1 191 LEU 191 185 185 LEU LEU A . n 
A 1 192 ARG 192 186 186 ARG ARG A . n 
A 1 193 ASP 193 187 187 ASP ASP A . n 
A 1 194 GLU 194 188 188 GLU GLU A . n 
A 1 195 GLY 195 189 189 GLY GLY A . n 
A 1 196 LYS 196 190 190 LYS LYS A . n 
A 1 197 ALA 197 191 191 ALA ALA A . n 
A 1 198 SER 198 192 192 SER SER A . n 
A 1 199 SER 199 193 193 SER SER A . n 
A 1 200 ALA 200 194 194 ALA ALA A . n 
A 1 201 LYS 201 195 195 LYS LYS A . n 
A 1 202 GLN 202 196 196 GLN GLN A . n 
A 1 203 ARG 203 197 197 ARG ARG A . n 
A 1 204 LEU 204 198 198 LEU LEU A . n 
A 1 205 LYS 205 199 199 LYS LYS A . n 
A 1 206 CYS 206 200 200 CYS CYS A . n 
A 1 207 ALA 207 201 201 ALA ALA A . n 
A 1 208 SER 208 202 202 SER SER A . n 
A 1 209 LEU 209 203 203 LEU LEU A . n 
A 1 210 GLN 210 204 204 GLN GLN A . n 
A 1 211 LYS 211 205 205 LYS LYS A . n 
A 1 212 PHE 212 206 206 PHE PHE A . n 
A 1 213 GLY 213 207 207 GLY GLY A . n 
A 1 214 GLU 214 208 208 GLU GLU A . n 
A 1 215 ARG 215 209 209 ARG ARG A . n 
A 1 216 ALA 216 210 210 ALA ALA A . n 
A 1 217 PHE 217 211 211 PHE PHE A . n 
A 1 218 LYS 218 212 212 LYS LYS A . n 
A 1 219 ALA 219 213 213 ALA ALA A . n 
A 1 220 TRP 220 214 214 TRP TRP A . n 
A 1 221 ALA 221 215 215 ALA ALA A . n 
A 1 222 VAL 222 216 216 VAL VAL A . n 
A 1 223 ALA 223 217 217 ALA ALA A . n 
A 1 224 ARG 224 218 218 ARG ARG A . n 
A 1 225 LEU 225 219 219 LEU LEU A . n 
A 1 226 SER 226 220 220 SER SER A . n 
A 1 227 GLN 227 221 221 GLN GLN A . n 
A 1 228 ARG 228 222 222 ARG ARG A . n 
A 1 229 PHE 229 223 223 PHE PHE A . n 
A 1 230 PRO 230 224 224 PRO PRO A . n 
A 1 231 LYS 231 225 225 LYS LYS A . n 
A 1 232 ALA 232 226 226 ALA ALA A . n 
A 1 233 GLU 233 227 227 GLU GLU A . n 
A 1 234 PHE 234 228 228 PHE PHE A . n 
A 1 235 ALA 235 229 229 ALA ALA A . n 
A 1 236 GLU 236 230 230 GLU GLU A . n 
A 1 237 VAL 237 231 231 VAL VAL A . n 
A 1 238 SER 238 232 232 SER SER A . n 
A 1 239 LYS 239 233 233 LYS LYS A . n 
A 1 240 LEU 240 234 234 LEU LEU A . n 
A 1 241 VAL 241 235 235 VAL VAL A . n 
A 1 242 THR 242 236 236 THR THR A . n 
A 1 243 ASP 243 237 237 ASP ASP A . n 
A 1 244 LEU 244 238 238 LEU LEU A . n 
A 1 245 THR 245 239 239 THR THR A . n 
A 1 246 LYS 246 240 240 LYS LYS A . n 
A 1 247 VAL 247 241 241 VAL VAL A . n 
A 1 248 HIS 248 242 242 HIS HIS A . n 
A 1 249 THR 249 243 243 THR THR A . n 
A 1 250 GLU 250 244 244 GLU GLU A . n 
A 1 251 CYS 251 245 245 CYS CYS A . n 
A 1 252 CYS 252 246 246 CYS CYS A . n 
A 1 253 HIS 253 247 247 HIS HIS A . n 
A 1 254 GLY 254 248 248 GLY GLY A . n 
A 1 255 ASP 255 249 249 ASP ASP A . n 
A 1 256 LEU 256 250 250 LEU LEU A . n 
A 1 257 LEU 257 251 251 LEU LEU A . n 
A 1 258 GLU 258 252 252 GLU GLU A . n 
A 1 259 CYS 259 253 253 CYS CYS A . n 
A 1 260 ALA 260 254 254 ALA ALA A . n 
A 1 261 ASP 261 255 255 ASP ASP A . n 
A 1 262 ASP 262 256 256 ASP ASP A . n 
A 1 263 ARG 263 257 257 ARG ARG A . n 
A 1 264 ALA 264 258 258 ALA ALA A . n 
A 1 265 ASP 265 259 259 ASP ASP A . n 
A 1 266 LEU 266 260 260 LEU LEU A . n 
A 1 267 ALA 267 261 261 ALA ALA A . n 
A 1 268 LYS 268 262 262 LYS LYS A . n 
A 1 269 TYR 269 263 263 TYR TYR A . n 
A 1 270 ILE 270 264 264 ILE ILE A . n 
A 1 271 CYS 271 265 265 CYS CYS A . n 
A 1 272 GLU 272 266 266 GLU GLU A . n 
A 1 273 ASN 273 267 267 ASN ASN A . n 
A 1 274 GLN 274 268 268 GLN GLN A . n 
A 1 275 ASP 275 269 269 ASP ASP A . n 
A 1 276 SER 276 270 270 SER SER A . n 
A 1 277 ILE 277 271 271 ILE ILE A . n 
A 1 278 SER 278 272 272 SER SER A . n 
A 1 279 SER 279 273 273 SER SER A . n 
A 1 280 LYS 280 274 274 LYS LYS A . n 
A 1 281 LEU 281 275 275 LEU LEU A . n 
A 1 282 LYS 282 276 276 LYS LYS A . n 
A 1 283 GLU 283 277 277 GLU GLU A . n 
A 1 284 CYS 284 278 278 CYS CYS A . n 
A 1 285 CYS 285 279 279 CYS CYS A . n 
A 1 286 GLU 286 280 280 GLU GLU A . n 
A 1 287 LYS 287 281 281 LYS LYS A . n 
A 1 288 PRO 288 282 282 PRO PRO A . n 
A 1 289 LEU 289 283 283 LEU LEU A . n 
A 1 290 LEU 290 284 284 LEU LEU A . n 
A 1 291 GLU 291 285 285 GLU GLU A . n 
A 1 292 LYS 292 286 286 LYS LYS A . n 
A 1 293 SER 293 287 287 SER SER A . n 
A 1 294 HIS 294 288 288 HIS HIS A . n 
A 1 295 CYS 295 289 289 CYS CYS A . n 
A 1 296 ILE 296 290 290 ILE ILE A . n 
A 1 297 ALA 297 291 291 ALA ALA A . n 
A 1 298 GLU 298 292 292 GLU GLU A . n 
A 1 299 VAL 299 293 293 VAL VAL A . n 
A 1 300 GLU 300 294 294 GLU GLU A . n 
A 1 301 ASN 301 295 295 ASN ASN A . n 
A 1 302 ASP 302 296 296 ASP ASP A . n 
A 1 303 GLU 303 297 297 GLU GLU A . n 
A 1 304 MET 304 298 298 MET MET A . n 
A 1 305 PRO 305 299 299 PRO PRO A . n 
A 1 306 ALA 306 300 300 ALA ALA A . n 
A 1 307 ASP 307 301 301 ASP ASP A . n 
A 1 308 LEU 308 302 302 LEU LEU A . n 
A 1 309 PRO 309 303 303 PRO PRO A . n 
A 1 310 SER 310 304 304 SER SER A . n 
A 1 311 LEU 311 305 305 LEU LEU A . n 
A 1 312 ALA 312 306 306 ALA ALA A . n 
A 1 313 ALA 313 307 307 ALA ALA A . n 
A 1 314 ASP 314 308 308 ASP ASP A . n 
A 1 315 PHE 315 309 309 PHE PHE A . n 
A 1 316 VAL 316 310 310 VAL VAL A . n 
A 1 317 GLU 317 311 311 GLU GLU A . n 
A 1 318 SER 318 312 312 SER SER A . n 
A 1 319 LYS 319 313 313 LYS LYS A . n 
A 1 320 ASP 320 314 314 ASP ASP A . n 
A 1 321 VAL 321 315 315 VAL VAL A . n 
A 1 322 CYS 322 316 316 CYS CYS A . n 
A 1 323 LYS 323 317 317 LYS LYS A . n 
A 1 324 ASN 324 318 318 ASN ASN A . n 
A 1 325 TYR 325 319 319 TYR TYR A . n 
A 1 326 ALA 326 320 320 ALA ALA A . n 
A 1 327 GLU 327 321 321 GLU GLU A . n 
A 1 328 ALA 328 322 322 ALA ALA A . n 
A 1 329 LYS 329 323 323 LYS LYS A . n 
A 1 330 ASP 330 324 324 ASP ASP A . n 
A 1 331 VAL 331 325 325 VAL VAL A . n 
A 1 332 PHE 332 326 326 PHE PHE A . n 
A 1 333 LEU 333 327 327 LEU LEU A . n 
A 1 334 GLY 334 328 328 GLY GLY A . n 
A 1 335 MET 335 329 329 MET MET A . n 
A 1 336 PHE 336 330 330 PHE PHE A . n 
A 1 337 LEU 337 331 331 LEU LEU A . n 
A 1 338 TYR 338 332 332 TYR TYR A . n 
A 1 339 GLU 339 333 333 GLU GLU A . n 
A 1 340 TYR 340 334 334 TYR TYR A . n 
A 1 341 ALA 341 335 335 ALA ALA A . n 
A 1 342 ARG 342 336 336 ARG ARG A . n 
A 1 343 ARG 343 337 337 ARG ARG A . n 
A 1 344 HIS 344 338 338 HIS HIS A . n 
A 1 345 PRO 345 339 339 PRO PRO A . n 
A 1 346 ASP 346 340 340 ASP ASP A . n 
A 1 347 TYR 347 341 341 TYR TYR A . n 
A 1 348 SER 348 342 342 SER SER A . n 
A 1 349 VAL 349 343 343 VAL VAL A . n 
A 1 350 VAL 350 344 344 VAL VAL A . n 
A 1 351 LEU 351 345 345 LEU LEU A . n 
A 1 352 LEU 352 346 346 LEU LEU A . n 
A 1 353 LEU 353 347 347 LEU LEU A . n 
A 1 354 ARG 354 348 348 ARG ARG A . n 
A 1 355 LEU 355 349 349 LEU LEU A . n 
A 1 356 ALA 356 350 350 ALA ALA A . n 
A 1 357 LYS 357 351 351 LYS LYS A . n 
A 1 358 THR 358 352 352 THR THR A . n 
A 1 359 TYR 359 353 353 TYR TYR A . n 
A 1 360 GLU 360 354 354 GLU GLU A . n 
A 1 361 THR 361 355 355 THR THR A . n 
A 1 362 THR 362 356 356 THR THR A . n 
A 1 363 LEU 363 357 357 LEU LEU A . n 
A 1 364 GLU 364 358 358 GLU GLU A . n 
A 1 365 LYS 365 359 359 LYS LYS A . n 
A 1 366 CYS 366 360 360 CYS CYS A . n 
A 1 367 CYS 367 361 361 CYS CYS A . n 
A 1 368 ALA 368 362 362 ALA ALA A . n 
A 1 369 ALA 369 363 363 ALA ALA A . n 
A 1 370 ALA 370 364 364 ALA ALA A . n 
A 1 371 ASP 371 365 365 ASP ASP A . n 
A 1 372 PRO 372 366 366 PRO PRO A . n 
A 1 373 HIS 373 367 367 HIS HIS A . n 
A 1 374 GLU 374 368 368 GLU GLU A . n 
A 1 375 CYS 375 369 369 CYS CYS A . n 
A 1 376 TYR 376 370 370 TYR TYR A . n 
A 1 377 ALA 377 371 371 ALA ALA A . n 
A 1 378 LYS 378 372 372 LYS LYS A . n 
A 1 379 VAL 379 373 373 VAL VAL A . n 
A 1 380 PHE 380 374 374 PHE PHE A . n 
A 1 381 ASP 381 375 375 ASP ASP A . n 
A 1 382 GLU 382 376 376 GLU GLU A . n 
A 1 383 PHE 383 377 377 PHE PHE A . n 
A 1 384 LYS 384 378 378 LYS LYS A . n 
A 1 385 PRO 385 379 379 PRO PRO A . n 
A 1 386 LEU 386 380 380 LEU LEU A . n 
A 1 387 VAL 387 381 381 VAL VAL A . n 
A 1 388 GLU 388 382 382 GLU GLU A . n 
A 1 389 GLU 389 383 383 GLU GLU A . n 
A 1 390 PRO 390 384 384 PRO PRO A . n 
A 1 391 GLN 391 385 385 GLN GLN A . n 
A 1 392 ASN 392 386 386 ASN ASN A . n 
A 1 393 LEU 393 387 387 LEU LEU A . n 
A 1 394 ILE 394 388 388 ILE ILE A . n 
A 1 395 LYS 395 389 389 LYS LYS A . n 
A 1 396 GLN 396 390 390 GLN GLN A . n 
A 1 397 ASN 397 391 391 ASN ASN A . n 
A 1 398 CYS 398 392 392 CYS CYS A . n 
A 1 399 GLU 399 393 393 GLU GLU A . n 
A 1 400 LEU 400 394 394 LEU LEU A . n 
A 1 401 PHE 401 395 395 PHE PHE A . n 
A 1 402 GLU 402 396 396 GLU GLU A . n 
A 1 403 GLN 403 397 397 GLN GLN A . n 
A 1 404 LEU 404 398 398 LEU LEU A . n 
A 1 405 GLY 405 399 399 GLY GLY A . n 
A 1 406 GLU 406 400 400 GLU GLU A . n 
A 1 407 TYR 407 401 401 TYR TYR A . n 
A 1 408 LYS 408 402 402 LYS LYS A . n 
A 1 409 PHE 409 403 403 PHE PHE A . n 
A 1 410 GLN 410 404 404 GLN GLN A . n 
A 1 411 ASN 411 405 405 ASN ASN A . n 
A 1 412 ALA 412 406 406 ALA ALA A . n 
A 1 413 LEU 413 407 407 LEU LEU A . n 
A 1 414 LEU 414 408 408 LEU LEU A . n 
A 1 415 VAL 415 409 409 VAL VAL A . n 
A 1 416 ARG 416 410 410 ARG ARG A . n 
A 1 417 TYR 417 411 411 TYR TYR A . n 
A 1 418 THR 418 412 412 THR THR A . n 
A 1 419 LYS 419 413 413 LYS LYS A . n 
A 1 420 LYS 420 414 414 LYS LYS A . n 
A 1 421 VAL 421 415 415 VAL VAL A . n 
A 1 422 PRO 422 416 416 PRO PRO A . n 
A 1 423 GLN 423 417 417 GLN GLN A . n 
A 1 424 VAL 424 418 418 VAL VAL A . n 
A 1 425 SER 425 419 419 SER SER A . n 
A 1 426 THR 426 420 420 THR THR A . n 
A 1 427 PRO 427 421 421 PRO PRO A . n 
A 1 428 THR 428 422 422 THR THR A . n 
A 1 429 LEU 429 423 423 LEU LEU A . n 
A 1 430 VAL 430 424 424 VAL VAL A . n 
A 1 431 GLU 431 425 425 GLU GLU A . n 
A 1 432 VAL 432 426 426 VAL VAL A . n 
A 1 433 SER 433 427 427 SER SER A . n 
A 1 434 ARG 434 428 428 ARG ARG A . n 
A 1 435 ASN 435 429 429 ASN ASN A . n 
A 1 436 LEU 436 430 430 LEU LEU A . n 
A 1 437 GLY 437 431 431 GLY GLY A . n 
A 1 438 LYS 438 432 432 LYS LYS A . n 
A 1 439 VAL 439 433 433 VAL VAL A . n 
A 1 440 GLY 440 434 434 GLY GLY A . n 
A 1 441 SER 441 435 435 SER SER A . n 
A 1 442 LYS 442 436 436 LYS LYS A . n 
A 1 443 CYS 443 437 437 CYS CYS A . n 
A 1 444 CYS 444 438 438 CYS CYS A . n 
A 1 445 LYS 445 439 439 LYS LYS A . n 
A 1 446 HIS 446 440 440 HIS HIS A . n 
A 1 447 PRO 447 441 441 PRO PRO A . n 
A 1 448 GLU 448 442 442 GLU GLU A . n 
A 1 449 ALA 449 443 443 ALA ALA A . n 
A 1 450 LYS 450 444 444 LYS LYS A . n 
A 1 451 ARG 451 445 445 ARG ARG A . n 
A 1 452 MET 452 446 446 MET MET A . n 
A 1 453 PRO 453 447 447 PRO PRO A . n 
A 1 454 CYS 454 448 448 CYS CYS A . n 
A 1 455 ALA 455 449 449 ALA ALA A . n 
A 1 456 GLU 456 450 450 GLU GLU A . n 
A 1 457 ASP 457 451 451 ASP ASP A . n 
A 1 458 TYR 458 452 452 TYR TYR A . n 
A 1 459 LEU 459 453 453 LEU LEU A . n 
A 1 460 SER 460 454 454 SER SER A . n 
A 1 461 VAL 461 455 455 VAL VAL A . n 
A 1 462 VAL 462 456 456 VAL VAL A . n 
A 1 463 LEU 463 457 457 LEU LEU A . n 
A 1 464 ASN 464 458 458 ASN ASN A . n 
A 1 465 GLN 465 459 459 GLN GLN A . n 
A 1 466 LEU 466 460 460 LEU LEU A . n 
A 1 467 CYS 467 461 461 CYS CYS A . n 
A 1 468 VAL 468 462 462 VAL VAL A . n 
A 1 469 LEU 469 463 463 LEU LEU A . n 
A 1 470 HIS 470 464 464 HIS HIS A . n 
A 1 471 GLU 471 465 465 GLU GLU A . n 
A 1 472 LYS 472 466 466 LYS LYS A . n 
A 1 473 THR 473 467 467 THR THR A . n 
A 1 474 PRO 474 468 468 PRO PRO A . n 
A 1 475 VAL 475 469 469 VAL VAL A . n 
A 1 476 SER 476 470 470 SER SER A . n 
A 1 477 ASP 477 471 471 ASP ASP A . n 
A 1 478 ARG 478 472 472 ARG ARG A . n 
A 1 479 VAL 479 473 473 VAL VAL A . n 
A 1 480 THR 480 474 474 THR THR A . n 
A 1 481 LYS 481 475 475 LYS LYS A . n 
A 1 482 CYS 482 476 476 CYS CYS A . n 
A 1 483 CYS 483 477 477 CYS CYS A . n 
A 1 484 THR 484 478 478 THR THR A . n 
A 1 485 GLU 485 479 479 GLU GLU A . n 
A 1 486 SER 486 480 480 SER SER A . n 
A 1 487 LEU 487 481 481 LEU LEU A . n 
A 1 488 VAL 488 482 482 VAL VAL A . n 
A 1 489 ASN 489 483 483 ASN ASN A . n 
A 1 490 ARG 490 484 484 ARG ARG A . n 
A 1 491 ARG 491 485 485 ARG ARG A . n 
A 1 492 PRO 492 486 486 PRO PRO A . n 
A 1 493 CYS 493 487 487 CYS CYS A . n 
A 1 494 PHE 494 488 488 PHE PHE A . n 
A 1 495 SER 495 489 489 SER SER A . n 
A 1 496 ALA 496 490 490 ALA ALA A . n 
A 1 497 LEU 497 491 491 LEU LEU A . n 
A 1 498 GLU 498 492 492 GLU GLU A . n 
A 1 499 VAL 499 493 493 VAL VAL A . n 
A 1 500 ASP 500 494 494 ASP ASP A . n 
A 1 501 GLU 501 495 495 GLU GLU A . n 
A 1 502 THR 502 496 496 THR THR A . n 
A 1 503 TYR 503 497 497 TYR TYR A . n 
A 1 504 VAL 504 498 498 VAL VAL A . n 
A 1 505 PRO 505 499 499 PRO PRO A . n 
A 1 506 LYS 506 500 500 LYS LYS A . n 
A 1 507 GLU 507 501 501 GLU GLU A . n 
A 1 508 PHE 508 502 502 PHE PHE A . n 
A 1 509 ASN 509 503 503 ASN ASN A . n 
A 1 510 ALA 510 504 504 ALA ALA A . n 
A 1 511 GLU 511 505 505 GLU GLU A . n 
A 1 512 THR 512 506 506 THR THR A . n 
A 1 513 PHE 513 507 507 PHE PHE A . n 
A 1 514 THR 514 508 508 THR THR A . n 
A 1 515 PHE 515 509 509 PHE PHE A . n 
A 1 516 HIS 516 510 510 HIS HIS A . n 
A 1 517 ALA 517 511 511 ALA ALA A . n 
A 1 518 ASP 518 512 512 ASP ASP A . n 
A 1 519 ILE 519 513 513 ILE ILE A . n 
A 1 520 CYS 520 514 514 CYS CYS A . n 
A 1 521 THR 521 515 515 THR THR A . n 
A 1 522 LEU 522 516 516 LEU LEU A . n 
A 1 523 SER 523 517 517 SER SER A . n 
A 1 524 GLU 524 518 518 GLU GLU A . n 
A 1 525 LYS 525 519 519 LYS LYS A . n 
A 1 526 GLU 526 520 520 GLU GLU A . n 
A 1 527 ARG 527 521 521 ARG ARG A . n 
A 1 528 GLN 528 522 522 GLN GLN A . n 
A 1 529 ILE 529 523 523 ILE ILE A . n 
A 1 530 LYS 530 524 524 LYS LYS A . n 
A 1 531 LYS 531 525 525 LYS LYS A . n 
A 1 532 GLN 532 526 526 GLN GLN A . n 
A 1 533 THR 533 527 527 THR THR A . n 
A 1 534 ALA 534 528 528 ALA ALA A . n 
A 1 535 LEU 535 529 529 LEU LEU A . n 
A 1 536 VAL 536 530 530 VAL VAL A . n 
A 1 537 GLU 537 531 531 GLU GLU A . n 
A 1 538 LEU 538 532 532 LEU LEU A . n 
A 1 539 VAL 539 533 533 VAL VAL A . n 
A 1 540 LYS 540 534 534 LYS LYS A . n 
A 1 541 HIS 541 535 535 HIS HIS A . n 
A 1 542 LYS 542 536 536 LYS LYS A . n 
A 1 543 PRO 543 537 537 PRO PRO A . n 
A 1 544 LYS 544 538 538 LYS LYS A . n 
A 1 545 ALA 545 539 539 ALA ALA A . n 
A 1 546 THR 546 540 540 THR THR A . n 
A 1 547 LYS 547 541 541 LYS LYS A . n 
A 1 548 GLU 548 542 542 GLU GLU A . n 
A 1 549 GLN 549 543 543 GLN GLN A . n 
A 1 550 LEU 550 544 544 LEU LEU A . n 
A 1 551 LYS 551 545 545 LYS LYS A . n 
A 1 552 ALA 552 546 546 ALA ALA A . n 
A 1 553 VAL 553 547 547 VAL VAL A . n 
A 1 554 MET 554 548 548 MET MET A . n 
A 1 555 ASP 555 549 549 ASP ASP A . n 
A 1 556 ASP 556 550 550 ASP ASP A . n 
A 1 557 PHE 557 551 551 PHE PHE A . n 
A 1 558 ALA 558 552 552 ALA ALA A . n 
A 1 559 ALA 559 553 553 ALA ALA A . n 
A 1 560 PHE 560 554 554 PHE PHE A . n 
A 1 561 VAL 561 555 555 VAL VAL A . n 
A 1 562 GLU 562 556 556 GLU GLU A . n 
A 1 563 LYS 563 557 557 LYS LYS A . n 
A 1 564 CYS 564 558 558 CYS CYS A . n 
A 1 565 CYS 565 559 559 CYS CYS A . n 
A 1 566 LYS 566 560 560 LYS LYS A . n 
A 1 567 ALA 567 561 561 ALA ALA A . n 
A 1 568 ASP 568 562 562 ASP ASP A . n 
A 1 569 ASP 569 563 563 ASP ASP A . n 
A 1 570 LYS 570 564 564 LYS LYS A . n 
A 1 571 GLU 571 565 565 GLU GLU A . n 
A 1 572 THR 572 566 566 THR THR A . n 
A 1 573 CYS 573 567 567 CYS CYS A . n 
A 1 574 PHE 574 568 568 PHE PHE A . n 
A 1 575 ALA 575 569 569 ALA ALA A . n 
A 1 576 GLU 576 570 570 GLU GLU A . n 
A 1 577 GLU 577 571 571 GLU GLU A . n 
A 1 578 GLY 578 572 572 GLY GLY A . n 
A 1 579 LYS 579 573 573 LYS LYS A . n 
A 1 580 LYS 580 574 574 LYS LYS A . n 
A 1 581 LEU 581 575 575 LEU LEU A . n 
A 1 582 VAL 582 576 576 VAL VAL A . n 
A 1 583 ALA 583 577 577 ALA ALA A . n 
A 1 584 ALA 584 578 578 ALA ALA A . n 
A 1 585 SER 585 579 579 SER SER A . n 
A 1 586 GLN 586 580 580 GLN GLN A . n 
A 1 587 ALA 587 581 581 ALA ALA A . n 
A 1 588 ALA 588 582 582 ALA ALA A . n 
A 1 589 LEU 589 583 583 LEU LEU A . n 
A 1 590 GLY 590 584 584 GLY GLY A . n 
A 1 591 LEU 591 585 ?   ?   ?   A . n 
B 2 1   GLU 1   1   1   GLU GLU B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   GLN 5   5   5   GLN GLN B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   GLY 9   9   9   GLY GLY B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  VAL 12  12  12  VAL VAL B . n 
B 2 13  GLN 13  13  13  GLN GLN B . n 
B 2 14  PRO 14  14  14  PRO PRO B . n 
B 2 15  GLY 15  15  15  GLY GLY B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  SER 17  17  17  SER SER B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  ARG 19  19  19  ARG ARG B . n 
B 2 20  LEU 20  20  20  LEU LEU B . n 
B 2 21  SER 21  21  21  SER SER B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  ALA 23  23  23  ALA ALA B . n 
B 2 24  ALA 24  24  24  ALA ALA B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  PHE 27  27  27  PHE PHE B . n 
B 2 28  THR 28  28  28  THR THR B . n 
B 2 29  PHE 29  29  29  PHE PHE B . n 
B 2 30  SER 30  30  30  SER SER B . n 
B 2 31  ARG 31  31  31  ARG ARG B . n 
B 2 32  TYR 32  32  32  TYR TYR B . n 
B 2 33  TRP 33  33  33  TRP TRP B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  PHE 35  35  35  PHE PHE B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  VAL 37  37  37  VAL VAL B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  TRP 47  47  47  TRP TRP B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  SER 49  49  49  SER SER B . n 
B 2 50  ASP 50  50  50  ASP ASP B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  ASN 52  52  52  ASN ASN B . n 
B 2 53  SER 53  53  53  SER SER B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  THR 56  56  56  THR THR B . n 
B 2 57  TYR 57  57  57  TYR TYR B . n 
B 2 58  THR 58  58  58  THR THR B . n 
B 2 59  ARG 59  59  59  ARG ARG B . n 
B 2 60  TYR 60  60  60  TYR TYR B . n 
B 2 61  ALA 61  61  61  ALA ALA B . n 
B 2 62  ASP 62  62  62  ASP ASP B . n 
B 2 63  SER 63  63  63  SER SER B . n 
B 2 64  VAL 64  64  64  VAL VAL B . n 
B 2 65  LYS 65  65  65  LYS LYS B . n 
B 2 66  GLY 66  66  66  GLY GLY B . n 
B 2 67  ARG 67  67  67  ARG ARG B . n 
B 2 68  PHE 68  68  68  PHE PHE B . n 
B 2 69  THR 69  69  69  THR THR B . n 
B 2 70  ILE 70  70  70  ILE ILE B . n 
B 2 71  SER 71  71  71  SER SER B . n 
B 2 72  ARG 72  72  72  ARG ARG B . n 
B 2 73  ASP 73  73  73  ASP ASP B . n 
B 2 74  ASN 74  74  74  ASN ASN B . n 
B 2 75  ALA 75  75  75  ALA ALA B . n 
B 2 76  LYS 76  76  76  LYS LYS B . n 
B 2 77  ASN 77  77  77  ASN ASN B . n 
B 2 78  THR 78  78  78  THR THR B . n 
B 2 79  LEU 79  79  79  LEU LEU B . n 
B 2 80  TYR 80  80  80  TYR TYR B . n 
B 2 81  LEU 81  81  81  LEU LEU B . n 
B 2 82  GLN 82  82  82  GLN GLN B . n 
B 2 83  MET 83  83  83  MET MET B . n 
B 2 84  ASN 84  84  84  ASN ASN B . n 
B 2 85  SER 85  85  85  SER SER B . n 
B 2 86  LEU 86  86  86  LEU LEU B . n 
B 2 87  ARG 87  87  87  ARG ARG B . n 
B 2 88  ALA 88  88  88  ALA ALA B . n 
B 2 89  GLU 89  89  89  GLU GLU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  THR 91  91  91  THR THR B . n 
B 2 92  ALA 92  92  92  ALA ALA B . n 
B 2 93  VAL 93  93  93  VAL VAL B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  TYR 95  95  95  TYR TYR B . n 
B 2 96  CYS 96  96  96  CYS CYS B . n 
B 2 97  ALA 97  97  97  ALA ALA B . n 
B 2 98  THR 98  98  98  THR THR B . n 
B 2 99  ASN 99  99  99  ASN ASN B . n 
B 2 100 SER 100 100 100 SER SER B . n 
B 2 101 GLY 101 101 101 GLY GLY B . n 
B 2 102 ASP 102 102 102 ASP ASP B . n 
B 2 103 GLY 103 103 103 GLY GLY B . n 
B 2 104 LYS 104 104 104 LYS LYS B . n 
B 2 105 ARG 105 105 105 ARG ARG B . n 
B 2 106 TYR 106 106 106 TYR TYR B . n 
B 2 107 CYS 107 107 107 CYS CYS B . n 
B 2 108 SER 108 108 108 SER SER B . n 
B 2 109 GLY 109 109 109 GLY GLY B . n 
B 2 110 GLY 110 110 110 GLY GLY B . n 
B 2 111 TYR 111 111 111 TYR TYR B . n 
B 2 112 CYS 112 112 112 CYS CYS B . n 
B 2 113 TYR 113 113 113 TYR TYR B . n 
B 2 114 ARG 114 114 114 ARG ARG B . n 
B 2 115 SER 115 115 115 SER SER B . n 
B 2 116 ARG 116 116 116 ARG ARG B . n 
B 2 117 GLY 117 117 117 GLY GLY B . n 
B 2 118 GLN 118 118 118 GLN GLN B . n 
B 2 119 GLY 119 119 119 GLY GLY B . n 
B 2 120 THR 120 120 120 THR THR B . n 
B 2 121 LEU 121 121 121 LEU LEU B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 THR 123 123 123 THR THR B . n 
B 2 124 VAL 124 124 124 VAL VAL B . n 
B 2 125 SER 125 125 125 SER SER B . n 
B 2 126 SER 126 126 126 SER SER B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 HOH 1  601 20  HOH HOH A . 
C 3 HOH 2  602 14  HOH HOH A . 
C 3 HOH 3  603 2   HOH HOH A . 
C 3 HOH 4  604 137 HOH HOH A . 
C 3 HOH 5  605 81  HOH HOH A . 
C 3 HOH 6  606 1   HOH HOH A . 
C 3 HOH 7  607 18  HOH HOH A . 
C 3 HOH 8  608 131 HOH HOH A . 
C 3 HOH 9  609 133 HOH HOH A . 
C 3 HOH 10 610 10  HOH HOH A . 
C 3 HOH 11 611 44  HOH HOH A . 
C 3 HOH 12 612 12  HOH HOH A . 
C 3 HOH 13 613 6   HOH HOH A . 
C 3 HOH 14 614 45  HOH HOH A . 
C 3 HOH 15 615 93  HOH HOH A . 
C 3 HOH 16 616 53  HOH HOH A . 
C 3 HOH 17 617 30  HOH HOH A . 
C 3 HOH 18 618 21  HOH HOH A . 
C 3 HOH 19 619 140 HOH HOH A . 
C 3 HOH 20 620 43  HOH HOH A . 
C 3 HOH 21 621 68  HOH HOH A . 
C 3 HOH 22 622 55  HOH HOH A . 
C 3 HOH 23 623 39  HOH HOH A . 
C 3 HOH 24 624 36  HOH HOH A . 
C 3 HOH 25 625 118 HOH HOH A . 
C 3 HOH 26 626 31  HOH HOH A . 
C 3 HOH 27 627 13  HOH HOH A . 
C 3 HOH 28 628 188 HOH HOH A . 
C 3 HOH 29 629 48  HOH HOH A . 
C 3 HOH 30 630 116 HOH HOH A . 
C 3 HOH 31 631 69  HOH HOH A . 
C 3 HOH 32 632 130 HOH HOH A . 
C 3 HOH 33 633 128 HOH HOH A . 
C 3 HOH 34 634 11  HOH HOH A . 
C 3 HOH 35 635 57  HOH HOH A . 
C 3 HOH 36 636 59  HOH HOH A . 
C 3 HOH 37 637 67  HOH HOH A . 
C 3 HOH 38 638 124 HOH HOH A . 
C 3 HOH 39 639 16  HOH HOH A . 
C 3 HOH 40 640 63  HOH HOH A . 
C 3 HOH 41 641 23  HOH HOH A . 
C 3 HOH 42 642 52  HOH HOH A . 
C 3 HOH 43 643 98  HOH HOH A . 
C 3 HOH 44 644 25  HOH HOH A . 
C 3 HOH 45 645 4   HOH HOH A . 
C 3 HOH 46 646 35  HOH HOH A . 
C 3 HOH 47 647 85  HOH HOH A . 
C 3 HOH 48 648 95  HOH HOH A . 
D 3 HOH 1  201 61  HOH HOH B . 
D 3 HOH 2  202 70  HOH HOH B . 
D 3 HOH 3  203 136 HOH HOH B . 
D 3 HOH 4  204 169 HOH HOH B . 
D 3 HOH 5  205 28  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0425 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? 0.7.7    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? 0.7.7    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? 2.8.3    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   118.74 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y9T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     167.951 
_cell.length_a_esd                 ? 
_cell.length_b                     73.699 
_cell.length_b_esd                 ? 
_cell.length_c                     86.008 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Y9T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Y9T 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.87 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.21 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Sodium acetate trihydrate pH 4.6, 1.8 M Ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-06 
_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   0.979183 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y9T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.40 
_reflns.d_resolution_low                               75.41 
_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                                     35902 
_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                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.4 
_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                                0.052 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.991 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.40 
_reflns_shell.d_res_low                                     2.46 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2440 
_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                               3.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.434 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.780 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          91.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.508 
_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]                            -0.10 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.01 
_refine.aniso_B[2][2]                            0.30 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.12 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               85.961 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 8Y9T 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.40 
_refine.ls_d_res_low                             75.41 
_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                     34089 
_refine.ls_number_reflns_R_free                  1807 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.11 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.26628 
_refine.ls_R_factor_R_free                       0.32447 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.26334 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.454 
_refine.pdbx_overall_ESU_R_Free                  0.324 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             15.659 
_refine.overall_SU_ML                            0.332 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        75.41 
_refine_hist.number_atoms_solvent             53 
_refine_hist.number_atoms_total               5345 
_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        5292 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_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         ? 
# 
_refine_ls_shell.R_factor_R_free                  0.3151 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2497 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.d_res_high                       2.40 
_refine_ls_shell.d_res_low                        2.46 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                2440 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.percent_reflns_obs               91.6 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
# 
_struct.entry_id                     8Y9T 
_struct.title                        'Crystal structure of nanobody MY6322 bound to human serum albumin (HSA)' 
_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        8Y9T 
_struct_keywords.text            'human serum albumin, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP ALBU_HUMAN P02768 ? 1 
;RGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKL
CTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPEL
LFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKL
VTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKD
VCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCEL
FEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVT
KCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAF
VEKCCKADDKETCFAEEGKKLVAASQAALGL
;
19 
2 PDB 8Y9T       8Y9T   ? 2 ? 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 8Y9T A 1 ? 591 ? P02768 19 ? 609 ? -5 585 
2 2 8Y9T B 1 ? 126 ? 8Y9T   1  ? 126 ? 1  126 
# 
_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)' 1710  ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  33710 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration'                   ? 
2 1 'isothermal titration calorimetry' ? 
3 1 'surface plasmon resonance'        ? 
# 
_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 SER A 11  ? GLY A 21  ? SER A 5   GLY A 15  1 ? 11 
HELX_P HELX_P2  AA2 GLU A 22  ? LEU A 37  ? GLU A 16  LEU A 31  1 ? 16 
HELX_P HELX_P3  AA3 HIS A 45  ? VAL A 60  ? HIS A 39  VAL A 54  1 ? 16 
HELX_P HELX_P4  AA4 SER A 71  ? CYS A 81  ? SER A 65  CYS A 75  1 ? 11 
HELX_P HELX_P5  AA5 GLU A 101 ? HIS A 111 ? GLU A 95  HIS A 105 1 ? 11 
HELX_P HELX_P6  AA6 VAL A 126 ? PHE A 133 ? VAL A 120 PHE A 127 1 ? 8  
HELX_P HELX_P7  AA7 GLU A 137 ? HIS A 152 ? GLU A 131 HIS A 146 1 ? 16 
HELX_P HELX_P8  AA8 TYR A 156 ? ALA A 177 ? TYR A 150 ALA A 171 1 ? 22 
HELX_P HELX_P9  AA9 LEU A 184 ? PHE A 212 ? LEU A 178 PHE A 206 1 ? 29 
HELX_P HELX_P10 AB1 GLY A 213 ? PHE A 229 ? GLY A 207 PHE A 223 1 ? 17 
HELX_P HELX_P11 AB2 GLU A 233 ? GLY A 254 ? GLU A 227 GLY A 248 1 ? 22 
HELX_P HELX_P12 AB3 LEU A 257 ? ASN A 273 ? LEU A 251 ASN A 267 1 ? 17 
HELX_P HELX_P13 AB4 GLN A 274 ? ILE A 277 ? GLN A 268 ILE A 271 5 ? 4  
HELX_P HELX_P14 AB5 GLU A 283 ? LYS A 287 ? GLU A 277 LYS A 281 5 ? 5  
HELX_P HELX_P15 AB6 PRO A 288 ? VAL A 299 ? PRO A 282 VAL A 293 1 ? 12 
HELX_P HELX_P16 AB7 ASP A 320 ? ARG A 343 ? ASP A 314 ARG A 337 1 ? 24 
HELX_P HELX_P17 AB8 SER A 348 ? CYS A 367 ? SER A 342 CYS A 361 1 ? 20 
HELX_P HELX_P18 AB9 ASP A 371 ? TYR A 376 ? ASP A 365 TYR A 370 1 ? 6  
HELX_P HELX_P19 AC1 LYS A 378 ? VAL A 421 ? LYS A 372 VAL A 415 1 ? 44 
HELX_P HELX_P20 AC2 SER A 425 ? CYS A 444 ? SER A 419 CYS A 438 1 ? 20 
HELX_P HELX_P21 AC3 PRO A 447 ? ALA A 449 ? PRO A 441 ALA A 443 5 ? 3  
HELX_P HELX_P22 AC4 LYS A 450 ? LYS A 472 ? LYS A 444 LYS A 466 1 ? 23 
HELX_P HELX_P23 AC5 SER A 476 ? GLU A 485 ? SER A 470 GLU A 479 1 ? 10 
HELX_P HELX_P24 AC6 SER A 486 ? ALA A 496 ? SER A 480 ALA A 490 1 ? 11 
HELX_P HELX_P25 AC7 ALA A 510 ? THR A 514 ? ALA A 504 THR A 508 5 ? 5  
HELX_P HELX_P26 AC8 HIS A 516 ? LEU A 522 ? HIS A 510 LEU A 516 5 ? 7  
HELX_P HELX_P27 AC9 SER A 523 ? LYS A 542 ? SER A 517 LYS A 536 1 ? 20 
HELX_P HELX_P28 AD1 THR A 546 ? CYS A 565 ? THR A 540 CYS A 559 1 ? 20 
HELX_P HELX_P29 AD2 ASP A 569 ? GLY A 590 ? ASP A 563 GLY A 584 1 ? 22 
HELX_P HELX_P30 AD3 THR B 28  ? TYR B 32  ? THR B 28  TYR B 32  5 ? 5  
HELX_P HELX_P31 AD4 ARG B 87  ? THR B 91  ? ARG B 87  THR B 91  5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 81  SG ? ? ? 1_555 A CYS 97  SG ? ? A CYS 75  A CYS 91  1_555 ? ? ? ? ? ? ? 2.959 ? ? 
disulf2  disulf ? ? A CYS 206 SG ? ? ? 1_555 A CYS 252 SG ? ? A CYS 200 A CYS 246 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3  disulf ? ? A CYS 251 SG ? ? ? 1_555 A CYS 259 SG ? ? A CYS 245 A CYS 253 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
disulf4  disulf ? ? A CYS 322 SG ? ? ? 1_555 A CYS 367 SG ? ? A CYS 316 A CYS 361 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
disulf5  disulf ? ? A CYS 366 SG ? ? ? 1_555 A CYS 375 SG ? ? A CYS 360 A CYS 369 1_555 ? ? ? ? ? ? ? 2.458 ? ? 
disulf6  disulf ? ? A CYS 398 SG ? ? ? 1_555 A CYS 444 SG ? ? A CYS 392 A CYS 438 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
disulf7  disulf ? ? A CYS 443 SG ? ? ? 1_555 A CYS 454 SG ? ? A CYS 437 A CYS 448 1_555 ? ? ? ? ? ? ? 2.569 ? ? 
disulf8  disulf ? ? A CYS 467 SG ? ? ? 1_555 A CYS 483 SG ? ? A CYS 461 A CYS 477 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
disulf9  disulf ? ? A CYS 482 SG ? ? ? 1_555 A CYS 493 SG ? ? A CYS 476 A CYS 487 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
disulf10 disulf ? ? A CYS 520 SG ? ? ? 1_555 A CYS 565 SG ? ? A CYS 514 A CYS 559 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
disulf11 disulf ? ? A CYS 564 SG ? ? ? 1_555 A CYS 573 SG ? ? A CYS 558 A CYS 567 1_555 ? ? ? ? ? ? ? 2.854 ? ? 
disulf12 disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 96  SG ? ? B CYS 22  B CYS 96  1_555 ? ? ? ? ? ? ? 2.455 ? ? 
disulf13 disulf ? ? B CYS 107 SG ? ? ? 1_555 B CYS 112 SG ? ? B CYS 107 B CYS 112 1_555 ? ? ? ? ? ? ? 2.215 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 81  ? CYS A 97  ? CYS A 75  ? 1_555 CYS A 91  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 206 ? CYS A 252 ? CYS A 200 ? 1_555 CYS A 246 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS A 251 ? CYS A 259 ? CYS A 245 ? 1_555 CYS A 253 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS A 322 ? CYS A 367 ? CYS A 316 ? 1_555 CYS A 361 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS A 366 ? CYS A 375 ? CYS A 360 ? 1_555 CYS A 369 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS A 398 ? CYS A 444 ? CYS A 392 ? 1_555 CYS A 438 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS A 443 ? CYS A 454 ? CYS A 437 ? 1_555 CYS A 448 ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS A 467 ? CYS A 483 ? CYS A 461 ? 1_555 CYS A 477 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS A 482 ? CYS A 493 ? CYS A 476 ? 1_555 CYS A 487 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS A 520 ? CYS A 565 ? CYS A 514 ? 1_555 CYS A 559 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS A 564 ? CYS A 573 ? CYS A 558 ? 1_555 CYS A 567 ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS B 22  ? CYS B 96  ? CYS B 22  ? 1_555 CYS B 96  ? 1_555 SG SG . . . None 'Disulfide bridge' 
13 CYS B 107 ? CYS B 112 ? CYS B 107 ? 1_555 CYS B 112 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLN B 3   ? SER B 7   ? GLN B 3   SER B 7   
AA1 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AA1 3 THR B 78  ? MET B 83  ? THR B 78  MET B 83  
AA1 4 PHE B 68  ? ASP B 73  ? PHE B 68  ASP B 73  
AA2 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA2 2 THR B 120 ? VAL B 124 ? THR B 120 VAL B 124 
AA2 3 ALA B 92  ? THR B 98  ? ALA B 92  THR B 98  
AA2 4 MET B 34  ? GLN B 39  ? MET B 34  GLN B 39  
AA2 5 LEU B 45  ? ILE B 51  ? LEU B 45  ILE B 51  
AA2 6 THR B 58  ? TYR B 60  ? THR B 58  TYR B 60  
AA3 1 LEU B 11  ? VAL B 12  ? LEU B 11  VAL B 12  
AA3 2 THR B 120 ? VAL B 124 ? THR B 120 VAL B 124 
AA3 3 ALA B 92  ? THR B 98  ? ALA B 92  THR B 98  
AA3 4 SER B 115 ? ARG B 116 ? SER B 115 ARG B 116 
AA4 1 TYR B 106 ? SER B 108 ? TYR B 106 SER B 108 
AA4 2 TYR B 111 ? TYR B 113 ? TYR B 111 TYR B 113 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N SER B 7   ? N SER B 7   O SER B 21  ? O SER B 21  
AA1 2 3 N LEU B 20  ? N LEU B 20  O LEU B 81  ? O LEU B 81  
AA1 3 4 O GLN B 82  ? O GLN B 82  N THR B 69  ? N THR B 69  
AA2 1 2 N VAL B 12  ? N VAL B 12  O THR B 123 ? O THR B 123 
AA2 2 3 O THR B 120 ? O THR B 120 N TYR B 94  ? N TYR B 94  
AA2 3 4 O TYR B 95  ? O TYR B 95  N VAL B 37  ? N VAL B 37  
AA2 4 5 N ARG B 38  ? N ARG B 38  O GLU B 46  ? O GLU B 46  
AA2 5 6 N ASP B 50  ? N ASP B 50  O ARG B 59  ? O ARG B 59  
AA3 1 2 N VAL B 12  ? N VAL B 12  O THR B 123 ? O THR B 123 
AA3 2 3 O THR B 120 ? O THR B 120 N TYR B 94  ? N TYR B 94  
AA3 3 4 O THR B 98  ? O THR B 98  N SER B 115 ? N SER B 115 
AA4 1 2 N TYR B 106 ? N TYR B 106 O TYR B 113 ? O TYR B 113 
# 
_pdbx_entry_details.entry_id                   8Y9T 
_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   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A CYS 253 ? ? CA A CYS 253 ? ? C  A CYS 253 ? ? 87.14  110.40 -23.26 2.00 N 
2 1 CB A CYS 476 ? ? CA A CYS 476 ? ? C  A CYS 476 ? ? 120.51 111.50 9.01   1.20 N 
3 1 N  A LEU 481 ? ? CA A LEU 481 ? ? CB A LEU 481 ? ? 98.23  110.40 -12.17 2.00 N 
4 1 N  B TYR 32  ? ? CA B TYR 32  ? ? CB B TYR 32  ? ? 97.27  110.60 -13.33 1.80 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 61  ? ? 83.69   -1.94   
2  1 ASP A 63  ? ? 82.89   4.04    
3  1 LYS A 73  ? ? -73.93  -71.84  
4  1 LEU A 250 ? ? 59.18   -130.25 
5  1 LEU A 251 ? ? 60.52   -118.22 
6  1 ILE A 271 ? ? -125.54 -69.20  
7  1 ASP A 308 ? ? 83.86   -1.32   
8  1 PHE A 309 ? ? -142.48 -21.23  
9  1 ALA A 322 ? ? -153.27 55.02   
10 1 PRO A 441 ? ? -59.40  173.91  
11 1 THR A 467 ? ? -161.98 65.52   
12 1 SER B 85  ? ? 39.57   58.19   
13 1 ALA B 92  ? ? 177.13  159.42  
# 
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 144 ? ? 0.265 'SIDE CHAIN' 
2  1 ARG A 145 ? ? 0.195 'SIDE CHAIN' 
3  1 ARG A 160 ? ? 0.195 'SIDE CHAIN' 
4  1 ARG A 186 ? ? 0.285 'SIDE CHAIN' 
5  1 ARG A 218 ? ? 0.113 'SIDE CHAIN' 
6  1 ARG A 348 ? ? 0.124 'SIDE CHAIN' 
7  1 ARG A 445 ? ? 0.150 'SIDE CHAIN' 
8  1 ARG A 472 ? ? 0.081 'SIDE CHAIN' 
9  1 ARG A 521 ? ? 0.209 'SIDE CHAIN' 
10 1 ARG B 31  ? ? 0.078 'SIDE CHAIN' 
11 1 ARG B 59  ? ? 0.280 'SIDE CHAIN' 
12 1 ARG B 67  ? ? 0.096 'SIDE CHAIN' 
13 1 ARG B 72  ? ? 0.076 'SIDE CHAIN' 
14 1 ARG B 87  ? ? 0.087 'SIDE CHAIN' 
15 1 ARG B 105 ? ? 0.094 'SIDE CHAIN' 
16 1 ARG B 116 ? ? 0.091 'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     202 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 644 ? 5.89 . 
2 1 O ? A HOH 645 ? 6.66 . 
3 1 O ? A HOH 646 ? 7.14 . 
4 1 O ? A HOH 647 ? 7.91 . 
5 1 O ? A HOH 648 ? 9.25 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ARG -5  ? A ARG 1   
2  1 Y 1 A GLY -4  ? A GLY 2   
3  1 Y 1 A VAL -3  ? A VAL 3   
4  1 Y 1 A PHE -2  ? A PHE 4   
5  1 Y 1 A ARG -1  ? A ARG 5   
6  1 Y 1 A ARG 0   ? A ARG 6   
7  1 Y 1 A ASP 1   ? A ASP 7   
8  1 Y 1 A ALA 2   ? A ALA 8   
9  1 Y 1 A HIS 3   ? A HIS 9   
10 1 Y 1 A LYS 4   ? A LYS 10  
11 1 Y 1 A GLN 33  ? A GLN 39  
12 1 Y 1 A CYS 34  ? A CYS 40  
13 1 Y 1 A PRO 35  ? A PRO 41  
14 1 Y 1 A PHE 36  ? A PHE 42  
15 1 Y 1 A ALA 55  ? A ALA 61  
16 1 Y 1 A ASP 56  ? A ASP 62  
17 1 Y 1 A GLU 57  ? A GLU 63  
18 1 Y 1 A VAL 77  ? A VAL 83  
19 1 Y 1 A ALA 78  ? A ALA 84  
20 1 Y 1 A THR 79  ? A THR 85  
21 1 Y 1 A LEU 80  ? A LEU 86  
22 1 Y 1 A ARG 81  ? A ARG 87  
23 1 Y 1 A GLU 82  ? A GLU 88  
24 1 Y 1 A THR 83  ? A THR 89  
25 1 Y 1 A TYR 84  ? A TYR 90  
26 1 Y 1 A GLY 85  ? A GLY 91  
27 1 Y 1 A GLU 86  ? A GLU 92  
28 1 Y 1 A MET 87  ? A MET 93  
29 1 Y 1 A ALA 88  ? A ALA 94  
30 1 Y 1 A LYS 106 ? A LYS 112 
31 1 Y 1 A ASP 107 ? A ASP 113 
32 1 Y 1 A ASP 108 ? A ASP 114 
33 1 Y 1 A ASN 109 ? A ASN 115 
34 1 Y 1 A PRO 110 ? A PRO 116 
35 1 Y 1 A ASN 111 ? A ASN 117 
36 1 Y 1 A LEU 112 ? A LEU 118 
37 1 Y 1 A PRO 113 ? A PRO 119 
38 1 Y 1 A ARG 114 ? A ARG 120 
39 1 Y 1 A LEU 115 ? A LEU 121 
40 1 Y 1 A VAL 116 ? A VAL 122 
41 1 Y 1 A ARG 117 ? A ARG 123 
42 1 Y 1 A PRO 118 ? A PRO 124 
43 1 Y 1 A HIS 128 ? A HIS 134 
44 1 Y 1 A ASP 129 ? A ASP 135 
45 1 Y 1 A LYS 174 ? A LYS 180 
46 1 Y 1 A ALA 175 ? A ALA 181 
47 1 Y 1 A ALA 176 ? A ALA 182 
48 1 Y 1 A LEU 585 ? A LEU 591 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, China)'         China 32070939       1 
'National Science Foundation (NSF, China)'         China 82030106       2 
'Ministry of Science and Technology (MoST, China)' China 2021YFA0805200 3 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 1n5u ? 
2 ? 'experimental model' PDB 1e7a ? 
# 
_atom_sites.entry_id                    8Y9T 
_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]   0.005954 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003265 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013569 
_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]   0.013260 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 11  ? 23.107  -28.170 23.556  1.00 133.72 ? 5   SER A N   1 
ATOM   2    C CA  . SER A 1 11  ? 22.206  -27.686 22.472  1.00 133.79 ? 5   SER A CA  1 
ATOM   3    C C   . SER A 1 11  ? 22.030  -26.158 22.507  1.00 129.65 ? 5   SER A C   1 
ATOM   4    O O   . SER A 1 11  ? 21.450  -25.648 23.485  1.00 125.11 ? 5   SER A O   1 
ATOM   5    C CB  . SER A 1 11  ? 20.876  -28.376 22.527  1.00 135.14 ? 5   SER A CB  1 
ATOM   6    O OG  . SER A 1 11  ? 20.395  -28.641 21.216  1.00 135.59 ? 5   SER A OG  1 
ATOM   7    N N   . GLU A 1 12  ? 22.477  -25.469 21.458  1.00 125.66 ? 6   GLU A N   1 
ATOM   8    C CA  . GLU A 1 12  ? 22.395  -23.988 21.370  1.00 123.04 ? 6   GLU A CA  1 
ATOM   9    C C   . GLU A 1 12  ? 20.932  -23.561 21.372  1.00 119.43 ? 6   GLU A C   1 
ATOM   10   O O   . GLU A 1 12  ? 20.600  -22.566 22.038  1.00 117.55 ? 6   GLU A O   1 
ATOM   11   C CB  . GLU A 1 12  ? 23.117  -23.523 20.110  1.00 125.15 ? 6   GLU A CB  1 
ATOM   12   C CG  . GLU A 1 12  ? 24.494  -22.932 20.397  1.00 124.50 ? 6   GLU A CG  1 
ATOM   13   C CD  . GLU A 1 12  ? 24.809  -21.633 19.677  1.00 124.18 ? 6   GLU A CD  1 
ATOM   14   O OE1 . GLU A 1 12  ? 24.423  -20.563 20.189  1.00 122.02 ? 6   GLU A OE1 1 
ATOM   15   O OE2 . GLU A 1 12  ? 25.447  -21.689 18.605  1.00 122.97 ? 6   GLU A OE2 1 
ATOM   16   N N   . VAL A 1 13  ? 20.088  -24.318 20.686  1.00 117.57 ? 7   VAL A N   1 
ATOM   17   C CA  . VAL A 1 13  ? 18.673  -23.898 20.529  1.00 117.02 ? 7   VAL A CA  1 
ATOM   18   C C   . VAL A 1 13  ? 18.115  -23.848 21.943  1.00 120.18 ? 7   VAL A C   1 
ATOM   19   O O   . VAL A 1 13  ? 17.338  -22.924 22.235  1.00 119.33 ? 7   VAL A O   1 
ATOM   20   C CB  . VAL A 1 13  ? 17.939  -24.931 19.662  1.00 115.60 ? 7   VAL A CB  1 
ATOM   21   C CG1 . VAL A 1 13  ? 18.393  -26.355 19.953  1.00 114.11 ? 7   VAL A CG1 1 
ATOM   22   C CG2 . VAL A 1 13  ? 16.426  -24.795 19.758  1.00 116.41 ? 7   VAL A CG2 1 
ATOM   23   N N   . ALA A 1 14  ? 18.492  -24.810 22.774  1.00 126.50 ? 8   ALA A N   1 
ATOM   24   C CA  . ALA A 1 14  ? 18.084  -24.758 24.194  1.00 131.75 ? 8   ALA A CA  1 
ATOM   25   C C   . ALA A 1 14  ? 18.692  -23.551 24.890  1.00 134.55 ? 8   ALA A C   1 
ATOM   26   O O   . ALA A 1 14  ? 17.945  -22.828 25.575  1.00 135.50 ? 8   ALA A O   1 
ATOM   27   C CB  . ALA A 1 14  ? 18.587  -25.981 24.872  1.00 134.50 ? 8   ALA A CB  1 
ATOM   28   N N   . HIS A 1 15  ? 19.999  -23.343 24.727  1.00 138.12 ? 9   HIS A N   1 
ATOM   29   C CA  . HIS A 1 15  ? 20.674  -22.270 25.504  1.00 138.60 ? 9   HIS A CA  1 
ATOM   30   C C   . HIS A 1 15  ? 19.886  -20.990 25.290  1.00 137.56 ? 9   HIS A C   1 
ATOM   31   O O   . HIS A 1 15  ? 19.428  -20.351 26.254  1.00 142.73 ? 9   HIS A O   1 
ATOM   32   C CB  . HIS A 1 15  ? 22.096  -22.076 24.972  1.00 139.59 ? 9   HIS A CB  1 
ATOM   33   C CG  . HIS A 1 15  ? 23.047  -21.304 25.819  1.00 138.90 ? 9   HIS A CG  1 
ATOM   34   N ND1 . HIS A 1 15  ? 22.991  -19.939 25.990  1.00 139.35 ? 9   HIS A ND1 1 
ATOM   35   C CD2 . HIS A 1 15  ? 24.117  -21.720 26.504  1.00 138.13 ? 9   HIS A CD2 1 
ATOM   36   C CE1 . HIS A 1 15  ? 23.989  -19.558 26.774  1.00 139.49 ? 9   HIS A CE1 1 
ATOM   37   N NE2 . HIS A 1 15  ? 24.683  -20.625 27.099  1.00 140.26 ? 9   HIS A NE2 1 
ATOM   38   N N   . ARG A 1 16  ? 19.699  -20.652 24.027  1.00 131.75 ? 10  ARG A N   1 
ATOM   39   C CA  . ARG A 1 16  ? 19.010  -19.424 23.673  1.00 128.58 ? 10  ARG A CA  1 
ATOM   40   C C   . ARG A 1 16  ? 17.526  -19.432 24.042  1.00 127.57 ? 10  ARG A C   1 
ATOM   41   O O   . ARG A 1 16  ? 16.977  -18.375 24.338  1.00 123.42 ? 10  ARG A O   1 
ATOM   42   C CB  . ARG A 1 16  ? 19.206  -19.140 22.173  1.00 128.16 ? 10  ARG A CB  1 
ATOM   43   C CG  . ARG A 1 16  ? 20.681  -19.094 21.729  1.00 126.00 ? 10  ARG A CG  1 
ATOM   44   C CD  . ARG A 1 16  ? 21.549  -18.223 22.620  1.00 124.37 ? 10  ARG A CD  1 
ATOM   45   N NE  . ARG A 1 16  ? 22.792  -17.847 21.956  1.00 126.61 ? 10  ARG A NE  1 
ATOM   46   C CZ  . ARG A 1 16  ? 24.009  -18.221 22.336  1.00 129.22 ? 10  ARG A CZ  1 
ATOM   47   N NH1 . ARG A 1 16  ? 24.197  -19.225 23.177  1.00 134.10 ? 10  ARG A NH1 1 
ATOM   48   N NH2 . ARG A 1 16  ? 25.066  -17.587 21.837  1.00 127.27 ? 10  ARG A NH2 1 
ATOM   49   N N   . PHE A 1 17  ? 16.872  -20.605 24.039  1.00 128.43 ? 11  PHE A N   1 
ATOM   50   C CA  . PHE A 1 17  ? 15.531  -20.696 24.598  1.00 126.32 ? 11  PHE A CA  1 
ATOM   51   C C   . PHE A 1 17  ? 15.573  -20.264 26.060  1.00 128.82 ? 11  PHE A C   1 
ATOM   52   O O   . PHE A 1 17  ? 14.794  -19.412 26.482  1.00 130.01 ? 11  PHE A O   1 
ATOM   53   C CB  . PHE A 1 17  ? 14.892  -22.098 24.536  1.00 126.36 ? 11  PHE A CB  1 
ATOM   54   C CG  . PHE A 1 17  ? 13.737  -22.219 25.523  1.00 129.10 ? 11  PHE A CG  1 
ATOM   55   C CD1 . PHE A 1 17  ? 13.966  -22.545 26.854  1.00 128.70 ? 11  PHE A CD1 1 
ATOM   56   C CD2 . PHE A 1 17  ? 12.436  -21.929 25.138  1.00 126.15 ? 11  PHE A CD2 1 
ATOM   57   C CE1 . PHE A 1 17  ? 12.911  -22.619 27.765  1.00 126.26 ? 11  PHE A CE1 1 
ATOM   58   C CE2 . PHE A 1 17  ? 11.385  -22.007 26.055  1.00 124.13 ? 11  PHE A CE2 1 
ATOM   59   C CZ  . PHE A 1 17  ? 11.631  -22.353 27.360  1.00 124.18 ? 11  PHE A CZ  1 
ATOM   60   N N   . LYS A 1 18  ? 16.486  -20.876 26.823  1.00 130.78 ? 12  LYS A N   1 
ATOM   61   C CA  . LYS A 1 18  ? 16.548  -20.675 28.262  1.00 133.57 ? 12  LYS A CA  1 
ATOM   62   C C   . LYS A 1 18  ? 16.910  -19.225 28.583  1.00 133.99 ? 12  LYS A C   1 
ATOM   63   O O   . LYS A 1 18  ? 16.405  -18.662 29.553  1.00 137.72 ? 12  LYS A O   1 
ATOM   64   C CB  . LYS A 1 18  ? 17.575  -21.626 28.913  1.00 134.36 ? 12  LYS A CB  1 
ATOM   65   C CG  . LYS A 1 18  ? 17.450  -23.132 28.568  1.00 136.65 ? 12  LYS A CG  1 
ATOM   66   C CD  . LYS A 1 18  ? 16.711  -24.018 29.609  1.00 138.37 ? 12  LYS A CD  1 
ATOM   67   C CE  . LYS A 1 18  ? 15.330  -24.470 29.187  1.00 137.67 ? 12  LYS A CE  1 
ATOM   68   N NZ  . LYS A 1 18  ? 14.857  -25.644 29.976  1.00 136.39 ? 12  LYS A NZ  1 
ATOM   69   N N   . ASP A 1 19  ? 17.780  -18.626 27.756  1.00 131.48 ? 13  ASP A N   1 
ATOM   70   C CA  . ASP A 1 19  ? 18.243  -17.260 27.956  1.00 126.78 ? 13  ASP A CA  1 
ATOM   71   C C   . ASP A 1 19  ? 17.269  -16.198 27.450  1.00 123.46 ? 13  ASP A C   1 
ATOM   72   O O   . ASP A 1 19  ? 16.816  -15.364 28.231  1.00 123.87 ? 13  ASP A O   1 
ATOM   73   C CB  . ASP A 1 19  ? 19.590  -17.045 27.259  1.00 125.86 ? 13  ASP A CB  1 
ATOM   74   C CG  . ASP A 1 19  ? 20.757  -17.794 27.851  1.00 125.49 ? 13  ASP A CG  1 
ATOM   75   O OD1 . ASP A 1 19  ? 20.544  -18.558 28.816  1.00 125.50 ? 13  ASP A OD1 1 
ATOM   76   O OD2 . ASP A 1 19  ? 21.886  -17.621 27.344  1.00 126.25 ? 13  ASP A OD2 1 
ATOM   77   N N   . LEU A 1 20  ? 16.981  -16.225 26.138  1.00 119.07 ? 14  LEU A N   1 
ATOM   78   C CA  . LEU A 1 20  ? 16.119  -15.237 25.502  1.00 116.41 ? 14  LEU A CA  1 
ATOM   79   C C   . LEU A 1 20  ? 14.764  -15.176 26.206  1.00 118.43 ? 14  LEU A C   1 
ATOM   80   O O   . LEU A 1 20  ? 14.255  -14.095 26.495  1.00 116.13 ? 14  LEU A O   1 
ATOM   81   C CB  . LEU A 1 20  ? 15.900  -15.564 24.002  1.00 112.76 ? 14  LEU A CB  1 
ATOM   82   C CG  . LEU A 1 20  ? 17.153  -15.627 23.107  1.00 111.40 ? 14  LEU A CG  1 
ATOM   83   C CD1 . LEU A 1 20  ? 16.789  -15.932 21.655  1.00 107.84 ? 14  LEU A CD1 1 
ATOM   84   C CD2 . LEU A 1 20  ? 17.945  -14.349 23.181  1.00 111.38 ? 14  LEU A CD2 1 
ATOM   85   N N   . GLY A 1 21  ? 14.208  -16.360 26.488  1.00 123.56 ? 15  GLY A N   1 
ATOM   86   C CA  . GLY A 1 21  ? 12.897  -16.502 27.100  1.00 125.08 ? 15  GLY A CA  1 
ATOM   87   C C   . GLY A 1 21  ? 11.966  -17.312 26.200  1.00 128.80 ? 15  GLY A C   1 
ATOM   88   O O   . GLY A 1 21  ? 12.367  -18.328 25.635  1.00 128.30 ? 15  GLY A O   1 
ATOM   89   N N   . GLU A 1 22  ? 10.718  -16.846 26.085  1.00 131.28 ? 16  GLU A N   1 
ATOM   90   C CA  . GLU A 1 22  ? 9.753   -17.417 25.160  1.00 130.68 ? 16  GLU A CA  1 
ATOM   91   C C   . GLU A 1 22  ? 9.166   -16.326 24.265  1.00 124.80 ? 16  GLU A C   1 
ATOM   92   O O   . GLU A 1 22  ? 9.140   -16.477 23.046  1.00 117.34 ? 16  GLU A O   1 
ATOM   93   C CB  . GLU A 1 22  ? 8.653   -18.150 25.938  1.00 134.56 ? 16  GLU A CB  1 
ATOM   94   C CG  . GLU A 1 22  ? 7.642   -18.865 25.058  1.00 137.83 ? 16  GLU A CG  1 
ATOM   95   C CD  . GLU A 1 22  ? 6.414   -19.375 25.788  1.00 140.11 ? 16  GLU A CD  1 
ATOM   96   O OE1 . GLU A 1 22  ? 6.379   -19.299 27.038  1.00 141.75 ? 16  GLU A OE1 1 
ATOM   97   O OE2 . GLU A 1 22  ? 5.473   -19.834 25.101  1.00 141.50 ? 16  GLU A OE2 1 
ATOM   98   N N   . GLU A 1 23  ? 8.704   -15.232 24.887  1.00 122.21 ? 17  GLU A N   1 
ATOM   99   C CA  . GLU A 1 23  ? 8.160   -14.086 24.172  1.00 123.41 ? 17  GLU A CA  1 
ATOM   100  C C   . GLU A 1 23  ? 9.181   -13.449 23.229  1.00 120.26 ? 17  GLU A C   1 
ATOM   101  O O   . GLU A 1 23  ? 8.830   -12.999 22.140  1.00 118.61 ? 17  GLU A O   1 
ATOM   102  C CB  . GLU A 1 23  ? 7.653   -13.023 25.180  1.00 123.55 ? 17  GLU A CB  1 
ATOM   103  C CG  . GLU A 1 23  ? 6.837   -11.894 24.556  1.00 121.07 ? 17  GLU A CG  1 
ATOM   104  C CD  . GLU A 1 23  ? 6.433   -10.784 25.512  1.00 118.33 ? 17  GLU A CD  1 
ATOM   105  O OE1 . GLU A 1 23  ? 5.830   -11.090 26.565  1.00 113.80 ? 17  GLU A OE1 1 
ATOM   106  O OE2 . GLU A 1 23  ? 6.713   -9.603  25.203  1.00 117.11 ? 17  GLU A OE2 1 
ATOM   107  N N   . ASN A 1 24  ? 10.448  -13.427 23.661  1.00 116.14 ? 18  ASN A N   1 
ATOM   108  C CA  . ASN A 1 24  ? 11.514  -12.771 22.921  1.00 114.30 ? 18  ASN A CA  1 
ATOM   109  C C   . ASN A 1 24  ? 12.014  -13.712 21.828  1.00 113.51 ? 18  ASN A C   1 
ATOM   110  O O   . ASN A 1 24  ? 12.227  -13.297 20.690  1.00 108.18 ? 18  ASN A O   1 
ATOM   111  C CB  . ASN A 1 24  ? 12.669  -12.359 23.843  1.00 113.66 ? 18  ASN A CB  1 
ATOM   112  C CG  . ASN A 1 24  ? 12.245  -11.912 25.221  1.00 114.42 ? 18  ASN A CG  1 
ATOM   113  O OD1 . ASN A 1 24  ? 12.224  -10.720 25.531  1.00 116.44 ? 18  ASN A OD1 1 
ATOM   114  N ND2 . ASN A 1 24  ? 11.893  -12.860 26.081  1.00 114.06 ? 18  ASN A ND2 1 
ATOM   115  N N   . PHE A 1 25  ? 12.204  -14.983 22.205  1.00 114.80 ? 19  PHE A N   1 
ATOM   116  C CA  . PHE A 1 25  ? 12.529  -16.045 21.268  1.00 113.96 ? 19  PHE A CA  1 
ATOM   117  C C   . PHE A 1 25  ? 11.589  -16.011 20.066  1.00 115.20 ? 19  PHE A C   1 
ATOM   118  O O   . PHE A 1 25  ? 12.047  -16.042 18.925  1.00 108.37 ? 19  PHE A O   1 
ATOM   119  C CB  . PHE A 1 25  ? 12.453  -17.414 21.969  1.00 112.36 ? 19  PHE A CB  1 
ATOM   120  C CG  . PHE A 1 25  ? 12.863  -18.586 21.107  1.00 114.78 ? 19  PHE A CG  1 
ATOM   121  C CD1 . PHE A 1 25  ? 12.069  -19.006 20.049  1.00 116.70 ? 19  PHE A CD1 1 
ATOM   122  C CD2 . PHE A 1 25  ? 14.044  -19.266 21.349  1.00 116.61 ? 19  PHE A CD2 1 
ATOM   123  C CE1 . PHE A 1 25  ? 12.450  -20.082 19.254  1.00 116.19 ? 19  PHE A CE1 1 
ATOM   124  C CE2 . PHE A 1 25  ? 14.422  -20.342 20.551  1.00 118.19 ? 19  PHE A CE2 1 
ATOM   125  C CZ  . PHE A 1 25  ? 13.623  -20.743 19.508  1.00 118.03 ? 19  PHE A CZ  1 
ATOM   126  N N   . LYS A 1 26  ? 10.277  -15.952 20.347  1.00 121.10 ? 20  LYS A N   1 
ATOM   127  C CA  . LYS A 1 26  ? 9.256   -16.009 19.312  1.00 123.98 ? 20  LYS A CA  1 
ATOM   128  C C   . LYS A 1 26  ? 9.282   -14.770 18.424  1.00 122.82 ? 20  LYS A C   1 
ATOM   129  O O   . LYS A 1 26  ? 9.095   -14.872 17.215  1.00 125.71 ? 20  LYS A O   1 
ATOM   130  C CB  . LYS A 1 26  ? 7.843   -16.168 19.889  1.00 128.29 ? 20  LYS A CB  1 
ATOM   131  C CG  . LYS A 1 26  ? 7.646   -17.407 20.762  1.00 130.97 ? 20  LYS A CG  1 
ATOM   132  C CD  . LYS A 1 26  ? 6.392   -18.225 20.424  1.00 133.74 ? 20  LYS A CD  1 
ATOM   133  C CE  . LYS A 1 26  ? 5.136   -17.408 20.202  1.00 135.67 ? 20  LYS A CE  1 
ATOM   134  N NZ  . LYS A 1 26  ? 3.949   -18.279 19.986  1.00 137.38 ? 20  LYS A NZ  1 
ATOM   135  N N   . ALA A 1 27  ? 9.503   -13.602 19.036  1.00 119.25 ? 21  ALA A N   1 
ATOM   136  C CA  . ALA A 1 27  ? 9.707   -12.376 18.282  1.00 115.78 ? 21  ALA A CA  1 
ATOM   137  C C   . ALA A 1 27  ? 10.908  -12.512 17.348  1.00 114.45 ? 21  ALA A C   1 
ATOM   138  O O   . ALA A 1 27  ? 10.805  -12.208 16.164  1.00 110.98 ? 21  ALA A O   1 
ATOM   139  C CB  . ALA A 1 27  ? 9.890   -11.198 19.221  1.00 115.20 ? 21  ALA A CB  1 
ATOM   140  N N   . LEU A 1 28  ? 12.034  -13.006 17.881  1.00 115.43 ? 22  LEU A N   1 
ATOM   141  C CA  . LEU A 1 28  ? 13.265  -13.117 17.113  1.00 117.81 ? 22  LEU A CA  1 
ATOM   142  C C   . LEU A 1 28  ? 13.089  -14.013 15.887  1.00 115.59 ? 22  LEU A C   1 
ATOM   143  O O   . LEU A 1 28  ? 13.518  -13.654 14.791  1.00 110.14 ? 22  LEU A O   1 
ATOM   144  C CB  . LEU A 1 28  ? 14.407  -13.634 18.017  1.00 121.21 ? 22  LEU A CB  1 
ATOM   145  C CG  . LEU A 1 28  ? 15.836  -13.657 17.416  1.00 123.20 ? 22  LEU A CG  1 
ATOM   146  C CD1 . LEU A 1 28  ? 16.032  -14.815 16.442  1.00 124.32 ? 22  LEU A CD1 1 
ATOM   147  C CD2 . LEU A 1 28  ? 16.180  -12.334 16.727  1.00 122.28 ? 22  LEU A CD2 1 
ATOM   148  N N   . VAL A 1 29  ? 12.454  -15.176 16.071  1.00 116.11 ? 23  VAL A N   1 
ATOM   149  C CA  . VAL A 1 29  ? 12.179  -16.063 14.952  1.00 114.33 ? 23  VAL A CA  1 
ATOM   150  C C   . VAL A 1 29  ? 11.225  -15.378 13.971  1.00 109.13 ? 23  VAL A C   1 
ATOM   151  O O   . VAL A 1 29  ? 11.364  -15.551 12.766  1.00 103.18 ? 23  VAL A O   1 
ATOM   152  C CB  . VAL A 1 29  ? 11.677  -17.462 15.407  1.00 114.44 ? 23  VAL A CB  1 
ATOM   153  C CG1 . VAL A 1 29  ? 12.751  -18.189 16.210  1.00 114.30 ? 23  VAL A CG1 1 
ATOM   154  C CG2 . VAL A 1 29  ? 10.384  -17.381 16.199  1.00 114.06 ? 23  VAL A CG2 1 
ATOM   155  N N   . LEU A 1 30  ? 10.292  -14.563 14.485  1.00 108.21 ? 24  LEU A N   1 
ATOM   156  C CA  . LEU A 1 30  ? 9.414   -13.777 13.628  1.00 111.05 ? 24  LEU A CA  1 
ATOM   157  C C   . LEU A 1 30  ? 10.181  -12.878 12.655  1.00 111.70 ? 24  LEU A C   1 
ATOM   158  O O   . LEU A 1 30  ? 9.753   -12.710 11.517  1.00 116.59 ? 24  LEU A O   1 
ATOM   159  C CB  . LEU A 1 30  ? 8.423   -12.894 14.442  1.00 112.31 ? 24  LEU A CB  1 
ATOM   160  C CG  . LEU A 1 30  ? 6.934   -13.341 14.603  1.00 112.45 ? 24  LEU A CG  1 
ATOM   161  C CD1 . LEU A 1 30  ? 6.477   -14.246 13.478  1.00 112.93 ? 24  LEU A CD1 1 
ATOM   162  C CD2 . LEU A 1 30  ? 6.669   -13.979 15.966  1.00 111.42 ? 24  LEU A CD2 1 
ATOM   163  N N   . ILE A 1 31  ? 11.332  -12.361 13.052  1.00 107.87 ? 25  ILE A N   1 
ATOM   164  C CA  . ILE A 1 31  ? 11.979  -11.375 12.135  1.00 105.73 ? 25  ILE A CA  1 
ATOM   165  C C   . ILE A 1 31  ? 12.763  -12.081 11.028  1.00 105.10 ? 25  ILE A C   1 
ATOM   166  O O   . ILE A 1 31  ? 12.493  -11.837 9.844   1.00 96.78  ? 25  ILE A O   1 
ATOM   167  C CB  . ILE A 1 31  ? 12.877  -10.414 12.929  1.00 106.00 ? 25  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 31  ? 12.055  -9.373  13.667  1.00 103.87 ? 25  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 31  ? 13.919  -9.764  12.020  1.00 106.57 ? 25  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 31  ? 12.074  -9.537  15.171  1.00 103.26 ? 25  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 32  ? 13.684  -12.946 11.404  1.00 111.90 ? 26  ALA A N   1 
ATOM   172  C CA  . ALA A 1 32  ? 14.557  -13.504 10.361  1.00 113.87 ? 26  ALA A CA  1 
ATOM   173  C C   . ALA A 1 32  ? 13.706  -14.280 9.389   1.00 114.64 ? 26  ALA A C   1 
ATOM   174  O O   . ALA A 1 32  ? 13.875  -14.141 8.166   1.00 111.99 ? 26  ALA A O   1 
ATOM   175  C CB  . ALA A 1 32  ? 15.526  -14.444 11.020  1.00 112.32 ? 26  ALA A CB  1 
ATOM   176  N N   . PHE A 1 33  ? 12.765  -15.025 9.943   1.00 117.82 ? 27  PHE A N   1 
ATOM   177  C CA  . PHE A 1 33  ? 12.017  -15.864 8.995   1.00 122.38 ? 27  PHE A CA  1 
ATOM   178  C C   . PHE A 1 33  ? 11.314  -14.930 8.077   1.00 123.01 ? 27  PHE A C   1 
ATOM   179  O O   . PHE A 1 33  ? 11.337  -15.104 6.848   1.00 118.45 ? 27  PHE A O   1 
ATOM   180  C CB  . PHE A 1 33  ? 11.044  -16.682 9.839   1.00 123.92 ? 27  PHE A CB  1 
ATOM   181  C CG  . PHE A 1 33  ? 11.677  -17.922 10.454  1.00 124.32 ? 27  PHE A CG  1 
ATOM   182  C CD1 . PHE A 1 33  ? 12.829  -17.827 11.225  1.00 123.71 ? 27  PHE A CD1 1 
ATOM   183  C CD2 . PHE A 1 33  ? 11.126  -19.180 10.250  1.00 123.08 ? 27  PHE A CD2 1 
ATOM   184  C CE1 . PHE A 1 33  ? 13.407  -18.956 11.779  1.00 122.86 ? 27  PHE A CE1 1 
ATOM   185  C CE2 . PHE A 1 33  ? 11.708  -20.305 10.806  1.00 122.25 ? 27  PHE A CE2 1 
ATOM   186  C CZ  . PHE A 1 33  ? 12.846  -20.192 11.567  1.00 122.92 ? 27  PHE A CZ  1 
ATOM   187  N N   . ALA A 1 34  ? 10.766  -13.872 8.665   1.00 127.93 ? 28  ALA A N   1 
ATOM   188  C CA  . ALA A 1 34  ? 9.937   -13.007 7.806   1.00 129.89 ? 28  ALA A CA  1 
ATOM   189  C C   . ALA A 1 34  ? 10.789  -12.391 6.717   1.00 130.65 ? 28  ALA A C   1 
ATOM   190  O O   . ALA A 1 34  ? 10.361  -12.309 5.555   1.00 130.33 ? 28  ALA A O   1 
ATOM   191  C CB  . ALA A 1 34  ? 9.303   -11.922 8.638   1.00 129.62 ? 28  ALA A CB  1 
ATOM   192  N N   . GLN A 1 35  ? 11.951  -11.887 7.094   1.00 133.65 ? 29  GLN A N   1 
ATOM   193  C CA  . GLN A 1 35  ? 12.800  -11.183 6.112   1.00 134.44 ? 29  GLN A CA  1 
ATOM   194  C C   . GLN A 1 35  ? 13.119  -12.133 4.966   1.00 136.90 ? 29  GLN A C   1 
ATOM   195  O O   . GLN A 1 35  ? 12.979  -11.735 3.795   1.00 139.42 ? 29  GLN A O   1 
ATOM   196  C CB  . GLN A 1 35  ? 14.057  -10.773 6.873   1.00 134.63 ? 29  GLN A CB  1 
ATOM   197  C CG  . GLN A 1 35  ? 15.341  -10.774 6.052   1.00 134.72 ? 29  GLN A CG  1 
ATOM   198  C CD  . GLN A 1 35  ? 16.585  -10.666 6.906   1.00 134.53 ? 29  GLN A CD  1 
ATOM   199  O OE1 . GLN A 1 35  ? 16.686  -11.274 7.977   1.00 135.19 ? 29  GLN A OE1 1 
ATOM   200  N NE2 . GLN A 1 35  ? 17.549  -9.888  6.437   1.00 134.08 ? 29  GLN A NE2 1 
ATOM   201  N N   . TYR A 1 36  ? 13.521  -13.350 5.296   1.00 138.44 ? 30  TYR A N   1 
ATOM   202  C CA  . TYR A 1 36  ? 13.971  -14.287 4.239   1.00 139.72 ? 30  TYR A CA  1 
ATOM   203  C C   . TYR A 1 36  ? 12.848  -14.611 3.277   1.00 142.93 ? 30  TYR A C   1 
ATOM   204  O O   . TYR A 1 36  ? 13.115  -14.670 2.065   1.00 143.89 ? 30  TYR A O   1 
ATOM   205  C CB  . TYR A 1 36  ? 14.515  -15.509 4.978   1.00 138.90 ? 30  TYR A CB  1 
ATOM   206  C CG  . TYR A 1 36  ? 15.702  -15.204 5.881   1.00 137.78 ? 30  TYR A CG  1 
ATOM   207  C CD1 . TYR A 1 36  ? 16.598  -14.192 5.567   1.00 137.56 ? 30  TYR A CD1 1 
ATOM   208  C CD2 . TYR A 1 36  ? 15.923  -15.924 7.047   1.00 136.36 ? 30  TYR A CD2 1 
ATOM   209  C CE1 . TYR A 1 36  ? 17.679  -13.908 6.383   1.00 137.83 ? 30  TYR A CE1 1 
ATOM   210  C CE2 . TYR A 1 36  ? 16.995  -15.643 7.875   1.00 134.55 ? 30  TYR A CE2 1 
ATOM   211  C CZ  . TYR A 1 36  ? 17.879  -14.636 7.540   1.00 135.27 ? 30  TYR A CZ  1 
ATOM   212  O OH  . TYR A 1 36  ? 18.941  -14.360 8.349   1.00 133.01 ? 30  TYR A OH  1 
ATOM   213  N N   . LEU A 1 37  ? 11.627  -14.800 3.773   1.00 148.04 ? 31  LEU A N   1 
ATOM   214  C CA  . LEU A 1 37  ? 10.534  -15.275 2.884   1.00 152.00 ? 31  LEU A CA  1 
ATOM   215  C C   . LEU A 1 37  ? 9.450   -14.207 2.758   1.00 158.02 ? 31  LEU A C   1 
ATOM   216  O O   . LEU A 1 37  ? 9.023   -13.670 3.794   1.00 163.51 ? 31  LEU A O   1 
ATOM   217  C CB  . LEU A 1 37  ? 9.955   -16.563 3.460   1.00 149.46 ? 31  LEU A CB  1 
ATOM   218  C CG  . LEU A 1 37  ? 8.501   -16.507 3.941   1.00 147.07 ? 31  LEU A CG  1 
ATOM   219  C CD1 . LEU A 1 37  ? 7.558   -17.346 3.095   1.00 147.79 ? 31  LEU A CD1 1 
ATOM   220  C CD2 . LEU A 1 37  ? 8.384   -16.871 5.408   1.00 146.52 ? 31  LEU A CD2 1 
ATOM   221  N N   . GLN A 1 38  ? 9.047   -13.896 1.524   1.00 159.37 ? 32  GLN A N   1 
ATOM   222  C CA  . GLN A 1 38  ? 8.020   -12.845 1.299   1.00 158.80 ? 32  GLN A CA  1 
ATOM   223  C C   . GLN A 1 38  ? 6.919   -13.374 0.361   1.00 155.77 ? 32  GLN A C   1 
ATOM   224  O O   . GLN A 1 38  ? 5.761   -13.471 0.829   1.00 149.08 ? 32  GLN A O   1 
ATOM   225  C CB  . GLN A 1 38  ? 8.707   -11.596 0.753   1.00 161.59 ? 32  GLN A CB  1 
ATOM   226  C CG  . GLN A 1 38  ? 10.103  -11.359 1.321   1.00 163.10 ? 32  GLN A CG  1 
ATOM   227  C CD  . GLN A 1 38  ? 10.308  -9.962  1.865   1.00 162.79 ? 32  GLN A CD  1 
ATOM   228  O OE1 . GLN A 1 38  ? 9.678   -9.551  2.845   1.00 159.94 ? 32  GLN A OE1 1 
ATOM   229  N NE2 . GLN A 1 38  ? 11.202  -9.216  1.232   1.00 164.11 ? 32  GLN A NE2 1 
ATOM   230  N N   . GLU A 1 43  ? 3.687   -15.097 6.737   1.00 168.08 ? 37  GLU A N   1 
ATOM   231  C CA  . GLU A 1 43  ? 2.270   -15.034 7.176   1.00 159.82 ? 37  GLU A CA  1 
ATOM   232  C C   . GLU A 1 43  ? 1.738   -16.473 7.169   1.00 162.72 ? 37  GLU A C   1 
ATOM   233  O O   . GLU A 1 43  ? 1.195   -16.915 8.203   1.00 162.91 ? 37  GLU A O   1 
ATOM   234  C CB  . GLU A 1 43  ? 1.526   -14.034 6.291   1.00 152.50 ? 37  GLU A CB  1 
ATOM   235  C CG  . GLU A 1 43  ? 1.567   -14.351 4.799   1.00 149.60 ? 37  GLU A CG  1 
ATOM   236  C CD  . GLU A 1 43  ? 2.912   -14.182 4.118   1.00 147.42 ? 37  GLU A CD  1 
ATOM   237  O OE1 . GLU A 1 43  ? 3.687   -15.158 4.141   1.00 148.45 ? 37  GLU A OE1 1 
ATOM   238  O OE2 . GLU A 1 43  ? 3.188   -13.095 3.571   1.00 141.34 ? 37  GLU A OE2 1 
ATOM   239  N N   . ASP A 1 44  ? 1.895   -17.176 6.051   1.00 161.98 ? 38  ASP A N   1 
ATOM   240  C CA  . ASP A 1 44  ? 1.485   -18.602 5.938   1.00 157.90 ? 38  ASP A CA  1 
ATOM   241  C C   . ASP A 1 44  ? 2.304   -19.460 6.905   1.00 160.34 ? 38  ASP A C   1 
ATOM   242  O O   . ASP A 1 44  ? 1.716   -20.381 7.500   1.00 166.76 ? 38  ASP A O   1 
ATOM   243  C CB  . ASP A 1 44  ? 1.590   -19.064 4.500   1.00 152.76 ? 38  ASP A CB  1 
ATOM   244  C CG  . ASP A 1 44  ? 2.759   -18.451 3.757   1.00 149.90 ? 38  ASP A CG  1 
ATOM   245  O OD1 . ASP A 1 44  ? 3.896   -18.885 4.028   1.00 145.78 ? 38  ASP A OD1 1 
ATOM   246  O OD2 . ASP A 1 44  ? 2.513   -17.530 2.953   1.00 146.08 ? 38  ASP A OD2 1 
ATOM   247  N N   . HIS A 1 45  ? 3.593   -19.180 7.070   1.00 157.30 ? 39  HIS A N   1 
ATOM   248  C CA  . HIS A 1 45  ? 4.530   -20.056 7.843   1.00 155.05 ? 39  HIS A CA  1 
ATOM   249  C C   . HIS A 1 45  ? 4.678   -19.543 9.286   1.00 151.20 ? 39  HIS A C   1 
ATOM   250  O O   . HIS A 1 45  ? 5.619   -19.949 9.986   1.00 150.48 ? 39  HIS A O   1 
ATOM   251  C CB  . HIS A 1 45  ? 5.749   -20.480 7.014   1.00 155.23 ? 39  HIS A CB  1 
ATOM   252  C CG  . HIS A 1 45  ? 5.605   -21.859 6.461   1.00 156.99 ? 39  HIS A CG  1 
ATOM   253  N ND1 . HIS A 1 45  ? 6.659   -22.731 6.301   1.00 156.01 ? 39  HIS A ND1 1 
ATOM   254  C CD2 . HIS A 1 45  ? 4.515   -22.516 6.042   1.00 156.68 ? 39  HIS A CD2 1 
ATOM   255  C CE1 . HIS A 1 45  ? 6.210   -23.871 5.794   1.00 153.96 ? 39  HIS A CE1 1 
ATOM   256  N NE2 . HIS A 1 45  ? 4.910   -23.762 5.629   1.00 155.70 ? 39  HIS A NE2 1 
ATOM   257  N N   . VAL A 1 46  ? 3.809   -18.624 9.692   1.00 147.16 ? 40  VAL A N   1 
ATOM   258  C CA  . VAL A 1 46  ? 3.813   -18.074 11.083  1.00 143.21 ? 40  VAL A CA  1 
ATOM   259  C C   . VAL A 1 46  ? 3.570   -19.288 11.991  1.00 141.88 ? 40  VAL A C   1 
ATOM   260  O O   . VAL A 1 46  ? 4.178   -19.357 13.078  1.00 142.37 ? 40  VAL A O   1 
ATOM   261  C CB  . VAL A 1 46  ? 2.732   -17.010 11.331  1.00 139.66 ? 40  VAL A CB  1 
ATOM   262  C CG1 . VAL A 1 46  ? 2.335   -16.920 12.799  1.00 134.61 ? 40  VAL A CG1 1 
ATOM   263  C CG2 . VAL A 1 46  ? 3.152   -15.647 10.797  1.00 141.01 ? 40  VAL A CG2 1 
ATOM   264  N N   . LYS A 1 47  ? 2.733   -20.217 11.554  1.00 138.10 ? 41  LYS A N   1 
ATOM   265  C CA  . LYS A 1 47  ? 2.465   -21.431 12.353  1.00 136.39 ? 41  LYS A CA  1 
ATOM   266  C C   . LYS A 1 47  ? 3.820   -22.131 12.495  1.00 139.04 ? 41  LYS A C   1 
ATOM   267  O O   . LYS A 1 47  ? 4.083   -22.673 13.582  1.00 140.18 ? 41  LYS A O   1 
ATOM   268  C CB  . LYS A 1 47  ? 1.468   -22.354 11.649  1.00 132.96 ? 41  LYS A CB  1 
ATOM   269  C CG  . LYS A 1 47  ? 0.418   -23.006 12.537  1.00 129.61 ? 41  LYS A CG  1 
ATOM   270  C CD  . LYS A 1 47  ? -0.022  -22.124 13.699  1.00 129.28 ? 41  LYS A CD  1 
ATOM   271  C CE  . LYS A 1 47  ? -1.336  -21.456 13.458  1.00 128.08 ? 41  LYS A CE  1 
ATOM   272  N NZ  . LYS A 1 47  ? -1.253  -20.016 13.713  1.00 127.23 ? 41  LYS A NZ  1 
ATOM   273  N N   . LEU A 1 48  ? 4.645   -22.121 11.452  1.00 142.12 ? 42  LEU A N   1 
ATOM   274  C CA  . LEU A 1 48  ? 5.958   -22.818 11.492  1.00 144.64 ? 42  LEU A CA  1 
ATOM   275  C C   . LEU A 1 48  ? 6.807   -22.178 12.604  1.00 146.76 ? 42  LEU A C   1 
ATOM   276  O O   . LEU A 1 48  ? 7.517   -22.917 13.300  1.00 147.57 ? 42  LEU A O   1 
ATOM   277  C CB  . LEU A 1 48  ? 6.655   -22.700 10.138  1.00 143.96 ? 42  LEU A CB  1 
ATOM   278  C CG  . LEU A 1 48  ? 8.107   -22.210 10.170  1.00 146.61 ? 42  LEU A CG  1 
ATOM   279  C CD1 . LEU A 1 48  ? 9.080   -23.345 10.427  1.00 148.16 ? 42  LEU A CD1 1 
ATOM   280  C CD2 . LEU A 1 48  ? 8.471   -21.480 8.895   1.00 146.87 ? 42  LEU A CD2 1 
ATOM   281  N N   . VAL A 1 49  ? 6.760   -20.860 12.758  1.00 147.98 ? 43  VAL A N   1 
ATOM   282  C CA  . VAL A 1 49  ? 7.479   -20.216 13.899  1.00 145.31 ? 43  VAL A CA  1 
ATOM   283  C C   . VAL A 1 49  ? 6.897   -20.701 15.238  1.00 146.13 ? 43  VAL A C   1 
ATOM   284  O O   . VAL A 1 49  ? 7.686   -20.970 16.147  1.00 145.53 ? 43  VAL A O   1 
ATOM   285  C CB  . VAL A 1 49  ? 7.388   -18.682 13.785  1.00 141.76 ? 43  VAL A CB  1 
ATOM   286  C CG1 . VAL A 1 49  ? 7.128   -18.003 15.125  1.00 139.46 ? 43  VAL A CG1 1 
ATOM   287  C CG2 . VAL A 1 49  ? 8.606   -18.095 13.085  1.00 141.13 ? 43  VAL A CG2 1 
ATOM   288  N N   . ASN A 1 50  ? 5.581   -20.840 15.365  1.00 148.66 ? 44  ASN A N   1 
ATOM   289  C CA  . ASN A 1 50  ? 5.038   -21.409 16.629  1.00 151.47 ? 44  ASN A CA  1 
ATOM   290  C C   . ASN A 1 50  ? 5.453   -22.884 16.680  1.00 158.76 ? 44  ASN A C   1 
ATOM   291  O O   . ASN A 1 50  ? 5.684   -23.392 17.795  1.00 166.12 ? 44  ASN A O   1 
ATOM   292  C CB  . ASN A 1 50  ? 3.543   -21.144 16.745  1.00 148.27 ? 44  ASN A CB  1 
ATOM   293  C CG  . ASN A 1 50  ? 3.184   -19.768 16.240  1.00 145.69 ? 44  ASN A CG  1 
ATOM   294  O OD1 . ASN A 1 50  ? 3.723   -18.769 16.726  1.00 146.08 ? 44  ASN A OD1 1 
ATOM   295  N ND2 . ASN A 1 50  ? 2.292   -19.693 15.264  1.00 143.23 ? 44  ASN A ND2 1 
ATOM   296  N N   . GLU A 1 51  ? 5.548   -23.549 15.523  1.00 159.01 ? 45  GLU A N   1 
ATOM   297  C CA  . GLU A 1 51  ? 6.022   -24.953 15.441  1.00 157.26 ? 45  GLU A CA  1 
ATOM   298  C C   . GLU A 1 51  ? 7.457   -25.039 15.968  1.00 161.36 ? 45  GLU A C   1 
ATOM   299  O O   . GLU A 1 51  ? 7.766   -26.002 16.698  1.00 163.21 ? 45  GLU A O   1 
ATOM   300  C CB  . GLU A 1 51  ? 6.029   -25.401 13.983  1.00 153.01 ? 45  GLU A CB  1 
ATOM   301  C CG  . GLU A 1 51  ? 6.662   -26.771 13.758  1.00 151.56 ? 45  GLU A CG  1 
ATOM   302  C CD  . GLU A 1 51  ? 8.176   -26.778 13.643  1.00 149.58 ? 45  GLU A CD  1 
ATOM   303  O OE1 . GLU A 1 51  ? 8.724   -25.837 13.032  1.00 150.48 ? 45  GLU A OE1 1 
ATOM   304  O OE2 . GLU A 1 51  ? 8.806   -27.713 14.184  1.00 142.78 ? 45  GLU A OE2 1 
ATOM   305  N N   . VAL A 1 52  ? 8.295   -24.056 15.644  1.00 162.65 ? 46  VAL A N   1 
ATOM   306  C CA  . VAL A 1 52  ? 9.732   -24.129 16.046  1.00 159.58 ? 46  VAL A CA  1 
ATOM   307  C C   . VAL A 1 52  ? 9.775   -24.149 17.580  1.00 161.01 ? 46  VAL A C   1 
ATOM   308  O O   . VAL A 1 52  ? 10.587  -24.907 18.127  1.00 164.60 ? 46  VAL A O   1 
ATOM   309  C CB  . VAL A 1 52  ? 10.634  -23.015 15.475  1.00 157.04 ? 46  VAL A CB  1 
ATOM   310  C CG1 . VAL A 1 52  ? 10.471  -22.828 13.974  1.00 153.74 ? 46  VAL A CG1 1 
ATOM   311  C CG2 . VAL A 1 52  ? 10.519  -21.695 16.223  1.00 158.67 ? 46  VAL A CG2 1 
ATOM   312  N N   . THR A 1 53  ? 8.929   -23.362 18.239  1.00 161.35 ? 47  THR A N   1 
ATOM   313  C CA  . THR A 1 53  ? 8.976   -23.288 19.713  1.00 159.57 ? 47  THR A CA  1 
ATOM   314  C C   . THR A 1 53  ? 8.661   -24.647 20.279  1.00 158.91 ? 47  THR A C   1 
ATOM   315  O O   . THR A 1 53  ? 9.339   -25.051 21.242  1.00 164.35 ? 47  THR A O   1 
ATOM   316  C CB  . THR A 1 53  ? 7.962   -22.261 20.202  1.00 159.33 ? 47  THR A CB  1 
ATOM   317  O OG1 . THR A 1 53  ? 6.716   -22.951 20.197  1.00 159.84 ? 47  THR A OG1 1 
ATOM   318  C CG2 . THR A 1 53  ? 7.893   -21.044 19.301  1.00 158.12 ? 47  THR A CG2 1 
ATOM   319  N N   . GLU A 1 54  ? 7.688   -25.344 19.690  1.00 151.87 ? 48  GLU A N   1 
ATOM   320  C CA  . GLU A 1 54  ? 7.337   -26.707 20.164  1.00 147.44 ? 48  GLU A CA  1 
ATOM   321  C C   . GLU A 1 54  ? 8.557   -27.626 19.967  1.00 146.51 ? 48  GLU A C   1 
ATOM   322  O O   . GLU A 1 54  ? 8.860   -28.404 20.894  1.00 148.58 ? 48  GLU A O   1 
ATOM   323  C CB  . GLU A 1 54  ? 6.045   -27.170 19.494  1.00 144.19 ? 48  GLU A CB  1 
ATOM   324  C CG  . GLU A 1 54  ? 6.231   -28.271 18.454  1.00 141.59 ? 48  GLU A CG  1 
ATOM   325  C CD  . GLU A 1 54  ? 5.001   -28.471 17.587  1.00 136.49 ? 48  GLU A CD  1 
ATOM   326  O OE1 . GLU A 1 54  ? 4.211   -29.384 17.900  1.00 133.38 ? 48  GLU A OE1 1 
ATOM   327  O OE2 . GLU A 1 54  ? 4.825   -27.713 16.610  1.00 131.33 ? 48  GLU A OE2 1 
ATOM   328  N N   . PHE A 1 55  ? 9.269   -27.489 18.848  1.00 141.43 ? 49  PHE A N   1 
ATOM   329  C CA  . PHE A 1 55  ? 10.497  -28.293 18.620  1.00 138.09 ? 49  PHE A CA  1 
ATOM   330  C C   . PHE A 1 55  ? 11.489  -27.925 19.692  1.00 143.68 ? 49  PHE A C   1 
ATOM   331  O O   . PHE A 1 55  ? 12.211  -28.798 20.175  1.00 147.74 ? 49  PHE A O   1 
ATOM   332  C CB  . PHE A 1 55  ? 11.152  -28.014 17.271  1.00 133.72 ? 49  PHE A CB  1 
ATOM   333  C CG  . PHE A 1 55  ? 12.491  -28.700 17.044  1.00 130.31 ? 49  PHE A CG  1 
ATOM   334  C CD1 . PHE A 1 55  ? 12.754  -29.955 17.581  1.00 128.10 ? 49  PHE A CD1 1 
ATOM   335  C CD2 . PHE A 1 55  ? 13.477  -28.094 16.278  1.00 128.58 ? 49  PHE A CD2 1 
ATOM   336  C CE1 . PHE A 1 55  ? 13.975  -30.573 17.374  1.00 128.87 ? 49  PHE A CE1 1 
ATOM   337  C CE2 . PHE A 1 55  ? 14.694  -28.721 16.067  1.00 128.86 ? 49  PHE A CE2 1 
ATOM   338  C CZ  . PHE A 1 55  ? 14.939  -29.957 16.615  1.00 130.09 ? 49  PHE A CZ  1 
ATOM   339  N N   . ALA A 1 56  ? 11.568  -26.643 20.036  1.00 148.52 ? 50  ALA A N   1 
ATOM   340  C CA  . ALA A 1 56  ? 12.592  -26.201 21.007  1.00 149.15 ? 50  ALA A CA  1 
ATOM   341  C C   . ALA A 1 56  ? 12.358  -26.871 22.359  1.00 151.04 ? 50  ALA A C   1 
ATOM   342  O O   . ALA A 1 56  ? 13.324  -27.336 22.989  1.00 151.31 ? 50  ALA A O   1 
ATOM   343  C CB  . ALA A 1 56  ? 12.509  -24.702 21.144  1.00 147.18 ? 50  ALA A CB  1 
ATOM   344  N N   . LYS A 1 57  ? 11.098  -26.971 22.769  1.00 151.35 ? 51  LYS A N   1 
ATOM   345  C CA  . LYS A 1 57  ? 10.787  -27.643 24.048  1.00 150.46 ? 51  LYS A CA  1 
ATOM   346  C C   . LYS A 1 57  ? 11.243  -29.085 23.861  1.00 155.19 ? 51  LYS A C   1 
ATOM   347  O O   . LYS A 1 57  ? 11.788  -29.675 24.808  1.00 154.09 ? 51  LYS A O   1 
ATOM   348  C CB  . LYS A 1 57  ? 9.291   -27.480 24.309  1.00 148.69 ? 51  LYS A CB  1 
ATOM   349  C CG  . LYS A 1 57  ? 8.776   -26.053 24.211  1.00 146.35 ? 51  LYS A CG  1 
ATOM   350  C CD  . LYS A 1 57  ? 7.313   -25.975 23.791  1.00 144.82 ? 51  LYS A CD  1 
ATOM   351  C CE  . LYS A 1 57  ? 6.834   -24.567 23.625  1.00 141.75 ? 51  LYS A CE  1 
ATOM   352  N NZ  . LYS A 1 57  ? 5.389   -24.452 23.839  1.00 141.20 ? 51  LYS A NZ  1 
ATOM   353  N N   . THR A 1 58  ? 10.998  -29.627 22.673  1.00 162.45 ? 52  THR A N   1 
ATOM   354  C CA  . THR A 1 58  ? 11.454  -30.989 22.342  1.00 165.36 ? 52  THR A CA  1 
ATOM   355  C C   . THR A 1 58  ? 12.959  -30.974 22.399  1.00 165.58 ? 52  THR A C   1 
ATOM   356  O O   . THR A 1 58  ? 13.545  -31.952 22.910  1.00 167.37 ? 52  THR A O   1 
ATOM   357  C CB  . THR A 1 58  ? 10.938  -31.377 20.957  1.00 165.49 ? 52  THR A CB  1 
ATOM   358  O OG1 . THR A 1 58  ? 9.548   -31.068 20.982  1.00 165.88 ? 52  THR A OG1 1 
ATOM   359  C CG2 . THR A 1 58  ? 11.158  -32.846 20.646  1.00 164.37 ? 52  THR A CG2 1 
ATOM   360  N N   . CYS A 1 59  ? 13.571  -29.893 21.921  1.00 161.72 ? 53  CYS A N   1 
ATOM   361  C CA  . CYS A 1 59  ? 15.044  -29.870 21.824  1.00 158.07 ? 53  CYS A CA  1 
ATOM   362  C C   . CYS A 1 59  ? 15.559  -30.014 23.256  1.00 158.84 ? 53  CYS A C   1 
ATOM   363  O O   . CYS A 1 59  ? 16.570  -30.714 23.440  1.00 159.91 ? 53  CYS A O   1 
ATOM   364  C CB  . CYS A 1 59  ? 15.507  -28.611 21.116  1.00 156.53 ? 53  CYS A CB  1 
ATOM   365  S SG  . CYS A 1 59  ? 15.805  -27.241 22.259  1.00 159.44 ? 53  CYS A SG  1 
ATOM   366  N N   . VAL A 1 60  ? 14.920  -29.366 24.223  1.00 159.57 ? 54  VAL A N   1 
ATOM   367  C CA  . VAL A 1 60  ? 15.332  -29.636 25.635  1.00 164.42 ? 54  VAL A CA  1 
ATOM   368  C C   . VAL A 1 60  ? 14.090  -29.804 26.522  1.00 165.70 ? 54  VAL A C   1 
ATOM   369  O O   . VAL A 1 60  ? 14.152  -30.659 27.431  1.00 168.19 ? 54  VAL A O   1 
ATOM   370  C CB  . VAL A 1 60  ? 16.229  -28.535 26.200  1.00 169.46 ? 54  VAL A CB  1 
ATOM   371  C CG1 . VAL A 1 60  ? 17.694  -28.784 25.864  1.00 171.46 ? 54  VAL A CG1 1 
ATOM   372  C CG2 . VAL A 1 60  ? 15.771  -27.157 25.741  1.00 169.81 ? 54  VAL A CG2 1 
ATOM   373  N N   A SER A 1 64  ? 18.677  -35.699 24.168  0.42 168.46 ? 58  SER A N   1 
ATOM   374  N N   B SER A 1 64  ? 18.664  -35.606 24.129  0.58 168.24 ? 58  SER A N   1 
ATOM   375  C CA  A SER A 1 64  ? 19.582  -36.062 23.046  0.42 165.50 ? 58  SER A CA  1 
ATOM   376  C CA  B SER A 1 64  ? 19.576  -36.071 23.053  0.58 164.40 ? 58  SER A CA  1 
ATOM   377  C C   A SER A 1 64  ? 18.745  -36.457 21.825  0.42 161.98 ? 58  SER A C   1 
ATOM   378  C C   B SER A 1 64  ? 18.750  -36.451 21.820  0.58 160.86 ? 58  SER A C   1 
ATOM   379  O O   A SER A 1 64  ? 19.308  -37.143 20.942  0.42 160.35 ? 58  SER A O   1 
ATOM   380  O O   B SER A 1 64  ? 19.320  -37.122 20.931  0.58 158.71 ? 58  SER A O   1 
ATOM   381  C CB  A SER A 1 64  ? 20.520  -37.167 23.445  0.42 166.01 ? 58  SER A CB  1 
ATOM   382  C CB  B SER A 1 64  ? 20.416  -37.224 23.523  0.58 164.36 ? 58  SER A CB  1 
ATOM   383  O OG  A SER A 1 64  ? 19.819  -38.207 24.112  0.42 167.08 ? 58  SER A OG  1 
ATOM   384  O OG  B SER A 1 64  ? 21.371  -37.592 22.537  0.58 164.43 ? 58  SER A OG  1 
ATOM   385  N N   . ALA A 1 65  ? 17.623  -35.763 21.615  1.00 160.41 ? 59  ALA A N   1 
ATOM   386  C CA  . ALA A 1 65  ? 16.736  -36.077 20.465  1.00 161.24 ? 59  ALA A CA  1 
ATOM   387  C C   . ALA A 1 65  ? 17.436  -35.786 19.136  1.00 163.52 ? 59  ALA A C   1 
ATOM   388  O O   . ALA A 1 65  ? 18.216  -34.819 19.061  1.00 163.54 ? 59  ALA A O   1 
ATOM   389  C CB  . ALA A 1 65  ? 15.443  -35.308 20.595  1.00 159.66 ? 59  ALA A CB  1 
ATOM   390  N N   . GLU A 1 66  ? 17.194  -36.625 18.126  1.00 165.06 ? 60  GLU A N   1 
ATOM   391  C CA  . GLU A 1 66  ? 17.777  -36.405 16.776  1.00 166.35 ? 60  GLU A CA  1 
ATOM   392  C C   . GLU A 1 66  ? 17.183  -35.124 16.175  1.00 167.32 ? 60  GLU A C   1 
ATOM   393  O O   . GLU A 1 66  ? 16.008  -34.827 16.485  1.00 170.10 ? 60  GLU A O   1 
ATOM   394  C CB  . GLU A 1 66  ? 17.531  -37.587 15.842  1.00 167.91 ? 60  GLU A CB  1 
ATOM   395  C CG  . GLU A 1 66  ? 18.563  -37.686 14.722  1.00 168.84 ? 60  GLU A CG  1 
ATOM   396  C CD  . GLU A 1 66  ? 19.978  -37.312 15.131  1.00 170.99 ? 60  GLU A CD  1 
ATOM   397  O OE1 . GLU A 1 66  ? 20.705  -38.202 15.619  1.00 172.23 ? 60  GLU A OE1 1 
ATOM   398  O OE2 . GLU A 1 66  ? 20.357  -36.135 14.960  1.00 173.76 ? 60  GLU A OE2 1 
ATOM   399  N N   . ASN A 1 67  ? 17.987  -34.373 15.418  1.00 164.34 ? 61  ASN A N   1 
ATOM   400  C CA  . ASN A 1 67  ? 17.532  -33.087 14.821  1.00 159.64 ? 61  ASN A CA  1 
ATOM   401  C C   . ASN A 1 67  ? 17.703  -32.010 15.894  1.00 166.95 ? 61  ASN A C   1 
ATOM   402  O O   . ASN A 1 67  ? 17.467  -30.828 15.583  1.00 172.03 ? 61  ASN A O   1 
ATOM   403  C CB  . ASN A 1 67  ? 16.134  -33.187 14.218  1.00 151.61 ? 61  ASN A CB  1 
ATOM   404  C CG  . ASN A 1 67  ? 15.925  -32.199 13.097  1.00 146.88 ? 61  ASN A CG  1 
ATOM   405  O OD1 . ASN A 1 67  ? 14.782  -31.863 12.768  1.00 143.55 ? 61  ASN A OD1 1 
ATOM   406  N ND2 . ASN A 1 67  ? 17.008  -31.724 12.501  1.00 142.22 ? 61  ASN A ND2 1 
ATOM   407  N N   . CYS A 1 68  ? 18.154  -32.406 17.087  1.00 171.42 ? 62  CYS A N   1 
ATOM   408  C CA  . CYS A 1 68  ? 18.359  -31.445 18.205  1.00 173.08 ? 62  CYS A CA  1 
ATOM   409  C C   . CYS A 1 68  ? 19.869  -31.336 18.448  1.00 172.32 ? 62  CYS A C   1 
ATOM   410  O O   . CYS A 1 68  ? 20.522  -32.394 18.442  1.00 179.12 ? 62  CYS A O   1 
ATOM   411  C CB  . CYS A 1 68  ? 17.658  -31.878 19.484  1.00 174.07 ? 62  CYS A CB  1 
ATOM   412  S SG  . CYS A 1 68  ? 15.906  -32.276 19.260  1.00 176.21 ? 62  CYS A SG  1 
ATOM   413  N N   . ASP A 1 69  ? 20.397  -30.122 18.576  1.00 165.83 ? 63  ASP A N   1 
ATOM   414  C CA  . ASP A 1 69  ? 21.865  -29.907 18.679  1.00 162.57 ? 63  ASP A CA  1 
ATOM   415  C C   . ASP A 1 69  ? 22.364  -29.914 17.233  1.00 162.17 ? 63  ASP A C   1 
ATOM   416  O O   . ASP A 1 69  ? 23.592  -29.808 17.009  1.00 164.70 ? 63  ASP A O   1 
ATOM   417  C CB  . ASP A 1 69  ? 22.521  -30.858 19.668  1.00 163.08 ? 63  ASP A CB  1 
ATOM   418  C CG  . ASP A 1 69  ? 24.022  -30.696 19.842  1.00 161.97 ? 63  ASP A CG  1 
ATOM   419  O OD1 . ASP A 1 69  ? 24.482  -29.543 19.966  1.00 157.13 ? 63  ASP A OD1 1 
ATOM   420  O OD2 . ASP A 1 69  ? 24.718  -31.727 19.844  1.00 161.25 ? 63  ASP A OD2 1 
ATOM   421  N N   . LYS A 1 70  ? 21.434  -30.013 16.281  1.00 158.73 ? 64  LYS A N   1 
ATOM   422  C CA  . LYS A 1 70  ? 21.795  -29.850 14.848  1.00 156.52 ? 64  LYS A CA  1 
ATOM   423  C C   . LYS A 1 70  ? 22.121  -28.354 14.696  1.00 155.60 ? 64  LYS A C   1 
ATOM   424  O O   . LYS A 1 70  ? 21.589  -27.570 15.507  1.00 155.83 ? 64  LYS A O   1 
ATOM   425  C CB  . LYS A 1 70  ? 20.691  -30.451 13.977  1.00 154.09 ? 64  LYS A CB  1 
ATOM   426  C CG  . LYS A 1 70  ? 20.685  -31.971 13.969  1.00 152.91 ? 64  LYS A CG  1 
ATOM   427  C CD  . LYS A 1 70  ? 20.542  -32.554 12.568  1.00 152.39 ? 64  LYS A CD  1 
ATOM   428  C CE  . LYS A 1 70  ? 20.092  -33.982 12.554  1.00 149.87 ? 64  LYS A CE  1 
ATOM   429  N NZ  . LYS A 1 70  ? 18.724  -34.131 12.047  1.00 148.19 ? 64  LYS A NZ  1 
ATOM   430  N N   . SER A 1 71  ? 22.982  -27.958 13.753  1.00 153.48 ? 65  SER A N   1 
ATOM   431  C CA  . SER A 1 71  ? 23.427  -26.536 13.729  1.00 150.60 ? 65  SER A CA  1 
ATOM   432  C C   . SER A 1 71  ? 22.239  -25.606 13.468  1.00 149.51 ? 65  SER A C   1 
ATOM   433  O O   . SER A 1 71  ? 21.361  -25.972 12.674  1.00 149.96 ? 65  SER A O   1 
ATOM   434  C CB  . SER A 1 71  ? 24.492  -26.316 12.706  1.00 148.22 ? 65  SER A CB  1 
ATOM   435  O OG  . SER A 1 71  ? 24.372  -25.022 12.131  1.00 147.18 ? 65  SER A OG  1 
ATOM   436  N N   . LEU A 1 72  ? 22.174  -24.500 14.215  1.00 146.27 ? 66  LEU A N   1 
ATOM   437  C CA  . LEU A 1 72  ? 21.030  -23.558 14.119  1.00 141.23 ? 66  LEU A CA  1 
ATOM   438  C C   . LEU A 1 72  ? 20.828  -23.137 12.667  1.00 134.63 ? 66  LEU A C   1 
ATOM   439  O O   . LEU A 1 72  ? 19.707  -23.296 12.146  1.00 129.12 ? 66  LEU A O   1 
ATOM   440  C CB  . LEU A 1 72  ? 21.317  -22.341 14.992  1.00 142.74 ? 66  LEU A CB  1 
ATOM   441  C CG  . LEU A 1 72  ? 22.738  -22.223 15.549  1.00 145.90 ? 66  LEU A CG  1 
ATOM   442  C CD1 . LEU A 1 72  ? 23.649  -21.483 14.583  1.00 145.68 ? 66  LEU A CD1 1 
ATOM   443  C CD2 . LEU A 1 72  ? 22.684  -21.503 16.882  1.00 147.82 ? 66  LEU A CD2 1 
ATOM   444  N N   . HIS A 1 73  ? 21.869  -22.588 12.058  1.00 134.04 ? 67  HIS A N   1 
ATOM   445  C CA  . HIS A 1 73  ? 21.653  -22.094 10.683  1.00 138.02 ? 67  HIS A CA  1 
ATOM   446  C C   . HIS A 1 73  ? 21.289  -23.295 9.823   1.00 137.16 ? 67  HIS A C   1 
ATOM   447  O O   . HIS A 1 73  ? 20.383  -23.190 8.987   1.00 135.73 ? 67  HIS A O   1 
ATOM   448  C CB  . HIS A 1 73  ? 22.906  -21.414 10.122  1.00 141.87 ? 67  HIS A CB  1 
ATOM   449  C CG  . HIS A 1 73  ? 23.614  -22.233 9.092   1.00 144.66 ? 67  HIS A CG  1 
ATOM   450  N ND1 . HIS A 1 73  ? 23.136  -22.421 7.813   1.00 144.92 ? 67  HIS A ND1 1 
ATOM   451  C CD2 . HIS A 1 73  ? 24.752  -22.932 9.167   1.00 145.31 ? 67  HIS A CD2 1 
ATOM   452  C CE1 . HIS A 1 73  ? 23.966  -23.209 7.148   1.00 144.37 ? 67  HIS A CE1 1 
ATOM   453  N NE2 . HIS A 1 73  ? 24.957  -23.525 7.949   1.00 145.90 ? 67  HIS A NE2 1 
ATOM   454  N N   . THR A 1 74  ? 21.969  -24.420 10.036  1.00 138.59 ? 68  THR A N   1 
ATOM   455  C CA  . THR A 1 74  ? 21.672  -25.518 9.110   1.00 138.54 ? 68  THR A CA  1 
ATOM   456  C C   . THR A 1 74  ? 20.232  -25.893 9.290   1.00 140.70 ? 68  THR A C   1 
ATOM   457  O O   . THR A 1 74  ? 19.553  -26.113 8.271   1.00 137.47 ? 68  THR A O   1 
ATOM   458  C CB  . THR A 1 74  ? 22.574  -26.713 9.406   1.00 136.56 ? 68  THR A CB  1 
ATOM   459  O OG1 . THR A 1 74  ? 22.264  -27.101 10.740  1.00 132.22 ? 68  THR A OG1 1 
ATOM   460  C CG2 . THR A 1 74  ? 24.049  -26.386 9.260   1.00 136.22 ? 68  THR A CG2 1 
ATOM   461  N N   . LEU A 1 75  ? 19.761  -25.956 10.535  1.00 144.38 ? 69  LEU A N   1 
ATOM   462  C CA  . LEU A 1 75  ? 18.351  -26.384 10.631  1.00 146.10 ? 69  LEU A CA  1 
ATOM   463  C C   . LEU A 1 75  ? 17.446  -25.358 9.952   1.00 146.47 ? 69  LEU A C   1 
ATOM   464  O O   . LEU A 1 75  ? 16.536  -25.781 9.212   1.00 145.44 ? 69  LEU A O   1 
ATOM   465  C CB  . LEU A 1 75  ? 18.028  -26.499 12.116  1.00 145.63 ? 69  LEU A CB  1 
ATOM   466  C CG  . LEU A 1 75  ? 18.644  -27.703 12.829  1.00 146.05 ? 69  LEU A CG  1 
ATOM   467  C CD1 . LEU A 1 75  ? 18.015  -27.884 14.198  1.00 145.26 ? 69  LEU A CD1 1 
ATOM   468  C CD2 . LEU A 1 75  ? 18.425  -28.925 11.960  1.00 145.88 ? 69  LEU A CD2 1 
ATOM   469  N N   . PHE A 1 76  ? 17.687  -24.061 10.182  1.00 148.54 ? 70  PHE A N   1 
ATOM   470  C CA  . PHE A 1 76  ? 16.902  -23.057 9.419   1.00 151.50 ? 70  PHE A CA  1 
ATOM   471  C C   . PHE A 1 76  ? 17.216  -23.138 7.921   1.00 150.29 ? 70  PHE A C   1 
ATOM   472  O O   . PHE A 1 76  ? 16.285  -23.096 7.091   1.00 149.41 ? 70  PHE A O   1 
ATOM   473  C CB  . PHE A 1 76  ? 17.207  -21.693 10.044  1.00 156.67 ? 70  PHE A CB  1 
ATOM   474  C CG  . PHE A 1 76  ? 17.730  -20.644 9.071   1.00 163.86 ? 70  PHE A CG  1 
ATOM   475  C CD1 . PHE A 1 76  ? 16.875  -20.002 8.183   1.00 167.62 ? 70  PHE A CD1 1 
ATOM   476  C CD2 . PHE A 1 76  ? 19.076  -20.303 9.048   1.00 166.22 ? 70  PHE A CD2 1 
ATOM   477  C CE1 . PHE A 1 76  ? 17.357  -19.058 7.293   1.00 168.36 ? 70  PHE A CE1 1 
ATOM   478  C CE2 . PHE A 1 76  ? 19.553  -19.355 8.158   1.00 168.12 ? 70  PHE A CE2 1 
ATOM   479  C CZ  . PHE A 1 76  ? 18.693  -18.734 7.284   1.00 168.93 ? 70  PHE A CZ  1 
ATOM   480  N N   . GLY A 1 77  ? 18.508  -23.273 7.586   1.00 145.85 ? 71  GLY A N   1 
ATOM   481  C CA  . GLY A 1 77  ? 18.896  -23.297 6.163   1.00 141.09 ? 71  GLY A CA  1 
ATOM   482  C C   . GLY A 1 77  ? 18.342  -24.485 5.425   1.00 137.98 ? 71  GLY A C   1 
ATOM   483  O O   . GLY A 1 77  ? 17.878  -24.316 4.282   1.00 131.21 ? 71  GLY A O   1 
ATOM   484  N N   . ASP A 1 78  ? 18.401  -25.650 6.066   1.00 139.46 ? 72  ASP A N   1 
ATOM   485  C CA  . ASP A 1 78  ? 17.859  -26.894 5.462   1.00 143.22 ? 72  ASP A CA  1 
ATOM   486  C C   . ASP A 1 78  ? 16.350  -26.793 5.275   1.00 144.59 ? 72  ASP A C   1 
ATOM   487  O O   . ASP A 1 78  ? 15.849  -27.206 4.206   1.00 143.49 ? 72  ASP A O   1 
ATOM   488  C CB  . ASP A 1 78  ? 18.241  -28.116 6.283   1.00 144.51 ? 72  ASP A CB  1 
ATOM   489  C CG  . ASP A 1 78  ? 17.080  -28.876 6.908   1.00 146.85 ? 72  ASP A CG  1 
ATOM   490  O OD1 . ASP A 1 78  ? 16.625  -28.462 7.995   1.00 148.41 ? 72  ASP A OD1 1 
ATOM   491  O OD2 . ASP A 1 78  ? 16.640  -29.873 6.299   1.00 147.26 ? 72  ASP A OD2 1 
ATOM   492  N N   . LYS A 1 79  ? 15.662  -26.221 6.259   1.00 143.65 ? 73  LYS A N   1 
ATOM   493  C CA  . LYS A 1 79  ? 14.182  -26.279 6.250   1.00 142.17 ? 73  LYS A CA  1 
ATOM   494  C C   . LYS A 1 79  ? 13.511  -25.369 5.233   1.00 145.04 ? 73  LYS A C   1 
ATOM   495  O O   . LYS A 1 79  ? 12.988  -25.882 4.223   1.00 149.24 ? 73  LYS A O   1 
ATOM   496  C CB  . LYS A 1 79  ? 13.699  -25.785 7.616   1.00 137.89 ? 73  LYS A CB  1 
ATOM   497  C CG  . LYS A 1 79  ? 12.232  -26.050 7.926   1.00 136.11 ? 73  LYS A CG  1 
ATOM   498  C CD  . LYS A 1 79  ? 11.381  -24.789 7.998   1.00 134.26 ? 73  LYS A CD  1 
ATOM   499  C CE  . LYS A 1 79  ? 10.157  -24.886 7.143   1.00 133.27 ? 73  LYS A CE  1 
ATOM   500  N NZ  . LYS A 1 79  ? 9.798   -23.594 6.554   1.00 132.76 ? 73  LYS A NZ  1 
ATOM   501  N N   . LEU A 1 80  ? 13.542  -24.072 5.485   1.00 144.84 ? 74  LEU A N   1 
ATOM   502  C CA  . LEU A 1 80  ? 12.735  -23.158 4.696   1.00 146.07 ? 74  LEU A CA  1 
ATOM   503  C C   . LEU A 1 80  ? 12.902  -23.458 3.208   1.00 151.67 ? 74  LEU A C   1 
ATOM   504  O O   . LEU A 1 80  ? 11.919  -23.489 2.471   1.00 156.82 ? 74  LEU A O   1 
ATOM   505  C CB  . LEU A 1 80  ? 13.098  -21.696 5.026   1.00 143.58 ? 74  LEU A CB  1 
ATOM   506  C CG  . LEU A 1 80  ? 12.548  -21.155 6.362   1.00 141.01 ? 74  LEU A CG  1 
ATOM   507  C CD1 . LEU A 1 80  ? 13.331  -21.680 7.553   1.00 142.59 ? 74  LEU A CD1 1 
ATOM   508  C CD2 . LEU A 1 80  ? 12.541  -19.627 6.385   1.00 138.16 ? 74  LEU A CD2 1 
ATOM   509  N N   . CYS A 1 81  ? 14.140  -23.785 2.837   1.00 155.31 ? 75  CYS A N   1 
ATOM   510  C CA  . CYS A 1 81  ? 14.412  -24.191 1.442   1.00 159.98 ? 75  CYS A CA  1 
ATOM   511  C C   . CYS A 1 81  ? 14.149  -25.696 1.343   1.00 165.14 ? 75  CYS A C   1 
ATOM   512  O O   . CYS A 1 81  ? 15.127  -26.469 1.388   1.00 167.62 ? 75  CYS A O   1 
ATOM   513  C CB  . CYS A 1 81  ? 15.858  -23.894 1.084   1.00 161.31 ? 75  CYS A CB  1 
ATOM   514  S SG  . CYS A 1 81  ? 16.127  -22.171 0.595   1.00 167.66 ? 75  CYS A SG  1 
ATOM   515  N N   . THR A 1 82  ? 12.875  -26.086 1.243   1.00 169.16 ? 76  THR A N   1 
ATOM   516  C CA  . THR A 1 82  ? 12.525  -27.517 1.140   1.00 170.82 ? 76  THR A CA  1 
ATOM   517  C C   . THR A 1 82  ? 13.407  -28.165 0.088   1.00 178.13 ? 76  THR A C   1 
ATOM   518  O O   . THR A 1 82  ? 13.507  -27.588 -1.016  1.00 185.09 ? 76  THR A O   1 
ATOM   519  C CB  . THR A 1 82  ? 11.038  -27.658 0.822   1.00 165.69 ? 76  THR A CB  1 
ATOM   520  O OG1 . THR A 1 82  ? 10.911  -28.884 0.109   1.00 161.97 ? 76  THR A OG1 1 
ATOM   521  C CG2 . THR A 1 82  ? 10.513  -26.503 -0.012  1.00 163.56 ? 76  THR A CG2 1 
ATOM   522  N N   . ASP A 1 95  ? 16.709  -17.664 -2.714  1.00 187.41 ? 89  ASP A N   1 
ATOM   523  C CA  . ASP A 1 95  ? 15.936  -18.937 -2.776  1.00 187.24 ? 89  ASP A CA  1 
ATOM   524  C C   . ASP A 1 95  ? 16.654  -19.957 -3.670  1.00 182.73 ? 89  ASP A C   1 
ATOM   525  O O   . ASP A 1 95  ? 15.956  -20.771 -4.311  1.00 183.26 ? 89  ASP A O   1 
ATOM   526  C CB  . ASP A 1 95  ? 14.500  -18.682 -3.205  1.00 190.00 ? 89  ASP A CB  1 
ATOM   527  C CG  . ASP A 1 95  ? 13.500  -19.773 -2.846  1.00 190.60 ? 89  ASP A CG  1 
ATOM   528  O OD1 . ASP A 1 95  ? 12.517  -19.939 -3.600  1.00 188.29 ? 89  ASP A OD1 1 
ATOM   529  O OD2 . ASP A 1 95  ? 13.713  -20.450 -1.819  1.00 191.70 ? 89  ASP A OD2 1 
ATOM   530  N N   . CYS A 1 96  ? 17.994  -19.956 -3.678  1.00 175.46 ? 90  CYS A N   1 
ATOM   531  C CA  . CYS A 1 96  ? 18.791  -20.929 -4.477  1.00 170.16 ? 90  CYS A CA  1 
ATOM   532  C C   . CYS A 1 96  ? 18.706  -22.327 -3.844  1.00 163.50 ? 90  CYS A C   1 
ATOM   533  O O   . CYS A 1 96  ? 18.179  -23.225 -4.531  1.00 162.06 ? 90  CYS A O   1 
ATOM   534  C CB  . CYS A 1 96  ? 20.246  -20.487 -4.555  1.00 172.38 ? 90  CYS A CB  1 
ATOM   535  S SG  . CYS A 1 96  ? 20.885  -19.827 -2.994  1.00 175.08 ? 90  CYS A SG  1 
ATOM   536  N N   . CYS A 1 97  ? 19.235  -22.521 -2.627  1.00 156.32 ? 91  CYS A N   1 
ATOM   537  C CA  . CYS A 1 97  ? 19.112  -23.807 -1.875  1.00 152.08 ? 91  CYS A CA  1 
ATOM   538  C C   . CYS A 1 97  ? 20.094  -24.880 -2.381  1.00 149.09 ? 91  CYS A C   1 
ATOM   539  O O   . CYS A 1 97  ? 19.945  -26.043 -1.950  1.00 145.94 ? 91  CYS A O   1 
ATOM   540  C CB  . CYS A 1 97  ? 17.702  -24.390 -1.923  1.00 148.81 ? 91  CYS A CB  1 
ATOM   541  S SG  . CYS A 1 97  ? 16.377  -23.179 -2.176  1.00 144.64 ? 91  CYS A SG  1 
ATOM   542  N N   . ALA A 1 98  ? 21.059  -24.528 -3.233  1.00 146.79 ? 92  ALA A N   1 
ATOM   543  C CA  . ALA A 1 98  ? 21.930  -25.564 -3.852  1.00 145.81 ? 92  ALA A CA  1 
ATOM   544  C C   . ALA A 1 98  ? 22.794  -26.366 -2.874  1.00 147.72 ? 92  ALA A C   1 
ATOM   545  O O   . ALA A 1 98  ? 22.897  -27.589 -3.087  1.00 146.13 ? 92  ALA A O   1 
ATOM   546  C CB  . ALA A 1 98  ? 22.816  -24.918 -4.893  1.00 143.75 ? 92  ALA A CB  1 
ATOM   547  N N   . LYS A 1 99  ? 23.393  -25.750 -1.851  1.00 151.49 ? 93  LYS A N   1 
ATOM   548  C CA  . LYS A 1 99  ? 24.361  -26.516 -1.014  1.00 156.49 ? 93  LYS A CA  1 
ATOM   549  C C   . LYS A 1 99  ? 23.890  -26.642 0.440   1.00 168.66 ? 93  LYS A C   1 
ATOM   550  O O   . LYS A 1 99  ? 24.488  -27.466 1.154   1.00 173.62 ? 93  LYS A O   1 
ATOM   551  C CB  . LYS A 1 99  ? 25.742  -25.851 -1.081  1.00 150.33 ? 93  LYS A CB  1 
ATOM   552  C CG  . LYS A 1 99  ? 26.592  -26.254 -2.276  1.00 145.47 ? 93  LYS A CG  1 
ATOM   553  C CD  . LYS A 1 99  ? 26.323  -25.426 -3.526  1.00 141.32 ? 93  LYS A CD  1 
ATOM   554  C CE  . LYS A 1 99  ? 26.288  -26.265 -4.762  1.00 138.66 ? 93  LYS A CE  1 
ATOM   555  N NZ  . LYS A 1 99  ? 26.575  -25.475 -5.961  1.00 139.13 ? 93  LYS A NZ  1 
ATOM   556  N N   . GLN A 1 100 ? 22.897  -25.861 0.860   1.00 175.20 ? 94  GLN A N   1 
ATOM   557  C CA  . GLN A 1 100 ? 22.333  -25.887 2.208   1.00 176.70 ? 94  GLN A CA  1 
ATOM   558  C C   . GLN A 1 100 ? 23.348  -25.862 3.361   1.00 177.79 ? 94  GLN A C   1 
ATOM   559  O O   . GLN A 1 100 ? 23.081  -26.409 4.430   1.00 179.44 ? 94  GLN A O   1 
ATOM   560  C CB  . GLN A 1 100 ? 21.321  -27.077 2.360   1.00 176.27 ? 94  GLN A CB  1 
ATOM   561  C CG  . GLN A 1 100 ? 21.787  -28.491 1.943   1.00 175.60 ? 94  GLN A CG  1 
ATOM   562  C CD  . GLN A 1 100 ? 22.769  -29.108 2.907   1.00 176.78 ? 94  GLN A CD  1 
ATOM   563  O OE1 . GLN A 1 100 ? 22.476  -29.274 4.094   1.00 179.79 ? 94  GLN A OE1 1 
ATOM   564  N NE2 . GLN A 1 100 ? 23.956  -29.469 2.422   1.00 177.12 ? 94  GLN A NE2 1 
ATOM   565  N N   . GLU A 1 101 ? 24.476  -25.159 3.158   1.00 173.99 ? 95  GLU A N   1 
ATOM   566  C CA  . GLU A 1 101 ? 25.566  -25.078 4.126   1.00 166.82 ? 95  GLU A CA  1 
ATOM   567  C C   . GLU A 1 101 ? 25.863  -23.626 4.508   1.00 163.00 ? 95  GLU A C   1 
ATOM   568  O O   . GLU A 1 101 ? 25.186  -22.722 4.030   1.00 160.03 ? 95  GLU A O   1 
ATOM   569  C CB  . GLU A 1 101 ? 26.823  -25.743 3.530   1.00 162.08 ? 95  GLU A CB  1 
ATOM   570  C CG  . GLU A 1 101 ? 26.630  -27.195 3.141   1.00 157.30 ? 95  GLU A CG  1 
ATOM   571  C CD  . GLU A 1 101 ? 27.892  -28.030 3.083   1.00 152.29 ? 95  GLU A CD  1 
ATOM   572  O OE1 . GLU A 1 101 ? 28.968  -27.517 3.465   1.00 152.18 ? 95  GLU A OE1 1 
ATOM   573  O OE2 . GLU A 1 101 ? 27.805  -29.204 2.658   1.00 145.63 ? 95  GLU A OE2 1 
ATOM   574  N N   . PRO A 1 102 ? 26.849  -23.328 5.393   1.00 161.72 ? 96  PRO A N   1 
ATOM   575  C CA  . PRO A 1 102 ? 27.225  -21.935 5.658   1.00 161.57 ? 96  PRO A CA  1 
ATOM   576  C C   . PRO A 1 102 ? 27.929  -21.217 4.505   1.00 162.49 ? 96  PRO A C   1 
ATOM   577  O O   . PRO A 1 102 ? 28.040  -19.992 4.529   1.00 164.43 ? 96  PRO A O   1 
ATOM   578  C CB  . PRO A 1 102 ? 28.132  -22.044 6.892   1.00 160.79 ? 96  PRO A CB  1 
ATOM   579  C CG  . PRO A 1 102 ? 28.667  -23.433 6.859   1.00 160.92 ? 96  PRO A CG  1 
ATOM   580  C CD  . PRO A 1 102 ? 27.591  -24.281 6.239   1.00 161.52 ? 96  PRO A CD  1 
ATOM   581  N N   . GLU A 1 103 ? 28.408  -21.974 3.505   1.00 159.15 ? 97  GLU A N   1 
ATOM   582  C CA  . GLU A 1 103 ? 28.937  -21.380 2.284   1.00 152.92 ? 97  GLU A CA  1 
ATOM   583  C C   . GLU A 1 103 ? 27.837  -21.077 1.267   1.00 150.75 ? 97  GLU A C   1 
ATOM   584  O O   . GLU A 1 103 ? 28.098  -20.409 0.266   1.00 146.45 ? 97  GLU A O   1 
ATOM   585  C CB  . GLU A 1 103 ? 30.020  -22.261 1.622   1.00 150.86 ? 97  GLU A CB  1 
ATOM   586  C CG  . GLU A 1 103 ? 29.567  -23.637 1.162   1.00 148.79 ? 97  GLU A CG  1 
ATOM   587  C CD  . GLU A 1 103 ? 29.946  -24.771 2.091   1.00 146.74 ? 97  GLU A CD  1 
ATOM   588  O OE1 . GLU A 1 103 ? 29.664  -24.667 3.306   1.00 146.63 ? 97  GLU A OE1 1 
ATOM   589  O OE2 . GLU A 1 103 ? 30.529  -25.766 1.603   1.00 142.78 ? 97  GLU A OE2 1 
ATOM   590  N N   . ARG A 1 104 ? 26.620  -21.581 1.518   1.00 149.39 ? 98  ARG A N   1 
ATOM   591  C CA  . ARG A 1 104 ? 25.454  -21.182 0.744   1.00 148.44 ? 98  ARG A CA  1 
ATOM   592  C C   . ARG A 1 104 ? 24.929  -19.849 1.270   1.00 145.95 ? 98  ARG A C   1 
ATOM   593  O O   . ARG A 1 104 ? 24.473  -19.017 0.490   1.00 143.06 ? 98  ARG A O   1 
ATOM   594  C CB  . ARG A 1 104 ? 24.339  -22.261 0.758   1.00 149.87 ? 98  ARG A CB  1 
ATOM   595  C CG  . ARG A 1 104 ? 23.354  -22.231 1.949   1.00 152.84 ? 98  ARG A CG  1 
ATOM   596  C CD  . ARG A 1 104 ? 22.265  -21.170 1.843   1.00 152.26 ? 98  ARG A CD  1 
ATOM   597  N NE  . ARG A 1 104 ? 21.364  -21.187 2.990   1.00 149.29 ? 98  ARG A NE  1 
ATOM   598  C CZ  . ARG A 1 104 ? 20.087  -20.832 2.943   1.00 148.16 ? 98  ARG A CZ  1 
ATOM   599  N NH1 . ARG A 1 104 ? 19.557  -20.301 1.852   1.00 145.68 ? 98  ARG A NH1 1 
ATOM   600  N NH2 . ARG A 1 104 ? 19.330  -20.984 4.026   1.00 147.41 ? 98  ARG A NH2 1 
ATOM   601  N N   . ASN A 1 105 ? 25.078  -19.618 2.570   1.00 146.48 ? 99  ASN A N   1 
ATOM   602  C CA  . ASN A 1 105 ? 24.509  -18.378 3.162   1.00 144.18 ? 99  ASN A CA  1 
ATOM   603  C C   . ASN A 1 105 ? 25.168  -17.158 2.508   1.00 138.98 ? 99  ASN A C   1 
ATOM   604  O O   . ASN A 1 105 ? 24.457  -16.169 2.276   1.00 135.61 ? 99  ASN A O   1 
ATOM   605  C CB  . ASN A 1 105 ? 24.571  -18.430 4.683   1.00 143.98 ? 99  ASN A CB  1 
ATOM   606  C CG  . ASN A 1 105 ? 23.663  -19.511 5.216   1.00 146.73 ? 99  ASN A CG  1 
ATOM   607  O OD1 . ASN A 1 105 ? 22.443  -19.324 5.279   1.00 145.86 ? 99  ASN A OD1 1 
ATOM   608  N ND2 . ASN A 1 105 ? 24.227  -20.654 5.577   1.00 148.14 ? 99  ASN A ND2 1 
ATOM   609  N N   . GLU A 1 106 ? 26.465  -17.227 2.214   1.00 136.21 ? 100 GLU A N   1 
ATOM   610  C CA  . GLU A 1 106 ? 27.123  -16.102 1.502   1.00 135.35 ? 100 GLU A CA  1 
ATOM   611  C C   . GLU A 1 106 ? 26.503  -15.924 0.107   1.00 136.47 ? 100 GLU A C   1 
ATOM   612  O O   . GLU A 1 106 ? 26.289  -14.763 -0.300  1.00 132.14 ? 100 GLU A O   1 
ATOM   613  C CB  . GLU A 1 106 ? 28.623  -16.378 1.416   1.00 133.70 ? 100 GLU A CB  1 
ATOM   614  C CG  . GLU A 1 106 ? 29.140  -17.254 2.554   1.00 130.20 ? 100 GLU A CG  1 
ATOM   615  C CD  . GLU A 1 106 ? 30.610  -17.615 2.446   1.00 128.09 ? 100 GLU A CD  1 
ATOM   616  O OE1 . GLU A 1 106 ? 31.012  -18.154 1.394   1.00 125.39 ? 100 GLU A OE1 1 
ATOM   617  O OE2 . GLU A 1 106 ? 31.354  -17.356 3.415   1.00 126.43 ? 100 GLU A OE2 1 
ATOM   618  N N   . CYS A 1 107 ? 26.224  -17.021 -0.602  1.00 140.52 ? 101 CYS A N   1 
ATOM   619  C CA  . CYS A 1 107 ? 25.517  -16.916 -1.907  1.00 141.50 ? 101 CYS A CA  1 
ATOM   620  C C   . CYS A 1 107 ? 24.122  -16.337 -1.650  1.00 142.21 ? 101 CYS A C   1 
ATOM   621  O O   . CYS A 1 107 ? 23.682  -15.474 -2.438  1.00 137.52 ? 101 CYS A O   1 
ATOM   622  C CB  . CYS A 1 107 ? 25.397  -18.275 -2.580  1.00 142.02 ? 101 CYS A CB  1 
ATOM   623  S SG  . CYS A 1 107 ? 23.887  -18.464 -3.564  1.00 144.39 ? 101 CYS A SG  1 
ATOM   624  N N   . PHE A 1 108 ? 23.482  -16.778 -0.565  1.00 144.29 ? 102 PHE A N   1 
ATOM   625  C CA  . PHE A 1 108 ? 22.100  -16.344 -0.229  1.00 145.10 ? 102 PHE A CA  1 
ATOM   626  C C   . PHE A 1 108 ? 22.096  -14.842 0.021   1.00 152.01 ? 102 PHE A C   1 
ATOM   627  O O   . PHE A 1 108 ? 21.144  -14.154 -0.384  1.00 153.86 ? 102 PHE A O   1 
ATOM   628  C CB  . PHE A 1 108 ? 21.649  -17.206 0.952   1.00 140.69 ? 102 PHE A CB  1 
ATOM   629  C CG  . PHE A 1 108 ? 20.768  -16.514 1.979   1.00 139.75 ? 102 PHE A CG  1 
ATOM   630  C CD1 . PHE A 1 108 ? 19.472  -16.128 1.662   1.00 139.45 ? 102 PHE A CD1 1 
ATOM   631  C CD2 . PHE A 1 108 ? 21.237  -16.264 3.263   1.00 138.06 ? 102 PHE A CD2 1 
ATOM   632  C CE1 . PHE A 1 108 ? 18.674  -15.499 2.602   1.00 138.37 ? 102 PHE A CE1 1 
ATOM   633  C CE2 . PHE A 1 108 ? 20.433  -15.638 4.199   1.00 134.86 ? 102 PHE A CE2 1 
ATOM   634  C CZ  . PHE A 1 108 ? 19.156  -15.258 3.864   1.00 136.01 ? 102 PHE A CZ  1 
ATOM   635  N N   . LEU A 1 109 ? 23.130  -14.341 0.691   1.00 157.53 ? 103 LEU A N   1 
ATOM   636  C CA  . LEU A 1 109 ? 23.206  -12.892 1.002   1.00 158.34 ? 103 LEU A CA  1 
ATOM   637  C C   . LEU A 1 109 ? 23.265  -12.119 -0.322  1.00 159.67 ? 103 LEU A C   1 
ATOM   638  O O   . LEU A 1 109 ? 22.595  -11.070 -0.429  1.00 156.82 ? 103 LEU A O   1 
ATOM   639  C CB  . LEU A 1 109 ? 24.419  -12.618 1.885   1.00 158.34 ? 103 LEU A CB  1 
ATOM   640  C CG  . LEU A 1 109 ? 24.386  -13.281 3.265   1.00 157.12 ? 103 LEU A CG  1 
ATOM   641  C CD1 . LEU A 1 109 ? 25.732  -13.214 3.961   1.00 155.72 ? 103 LEU A CD1 1 
ATOM   642  C CD2 . LEU A 1 109 ? 23.286  -12.711 4.145   1.00 155.10 ? 103 LEU A CD2 1 
ATOM   643  N N   . GLN A 1 110 ? 24.012  -12.636 -1.299  1.00 162.40 ? 104 GLN A N   1 
ATOM   644  C CA  . GLN A 1 110 ? 24.066  -11.979 -2.628  1.00 162.82 ? 104 GLN A CA  1 
ATOM   645  C C   . GLN A 1 110 ? 22.657  -11.995 -3.236  1.00 163.48 ? 104 GLN A C   1 
ATOM   646  O O   . GLN A 1 110 ? 22.250  -10.965 -3.815  1.00 165.56 ? 104 GLN A O   1 
ATOM   647  C CB  . GLN A 1 110 ? 25.023  -12.744 -3.537  1.00 161.93 ? 104 GLN A CB  1 
ATOM   648  C CG  . GLN A 1 110 ? 25.334  -12.041 -4.853  1.00 161.34 ? 104 GLN A CG  1 
ATOM   649  C CD  . GLN A 1 110 ? 26.810  -12.043 -5.182  1.00 161.73 ? 104 GLN A CD  1 
ATOM   650  O OE1 . GLN A 1 110 ? 27.664  -11.866 -4.307  1.00 163.92 ? 104 GLN A OE1 1 
ATOM   651  N NE2 . GLN A 1 110 ? 27.126  -12.248 -6.453  1.00 159.55 ? 104 GLN A NE2 1 
ATOM   652  N N   . HIS A 1 111 ? 21.928  -13.104 -3.082  1.00 163.04 ? 105 HIS A N   1 
ATOM   653  C CA  . HIS A 1 111 ? 20.528  -13.171 -3.580  1.00 159.55 ? 105 HIS A CA  1 
ATOM   654  C C   . HIS A 1 111 ? 19.576  -12.835 -2.428  1.00 154.77 ? 105 HIS A C   1 
ATOM   655  O O   . HIS A 1 111 ? 19.904  -11.876 -1.696  1.00 150.39 ? 105 HIS A O   1 
ATOM   656  C CB  . HIS A 1 111 ? 20.247  -14.543 -4.199  1.00 159.61 ? 105 HIS A CB  1 
ATOM   657  C CG  . HIS A 1 111 ? 21.304  -15.009 -5.146  1.00 160.95 ? 105 HIS A CG  1 
ATOM   658  N ND1 . HIS A 1 111 ? 22.580  -15.356 -4.757  1.00 161.73 ? 105 HIS A ND1 1 
ATOM   659  C CD2 . HIS A 1 111 ? 21.262  -15.195 -6.471  1.00 159.00 ? 105 HIS A CD2 1 
ATOM   660  C CE1 . HIS A 1 111 ? 23.276  -15.730 -5.819  1.00 160.45 ? 105 HIS A CE1 1 
ATOM   661  N NE2 . HIS A 1 111 ? 22.494  -15.642 -6.871  1.00 159.08 ? 105 HIS A NE2 1 
ATOM   662  N N   . GLU A 1 125 ? -7.078  4.838   11.805  1.00 141.36 ? 119 GLU A N   1 
ATOM   663  C CA  . GLU A 1 125 ? -8.373  4.314   12.304  1.00 137.28 ? 119 GLU A CA  1 
ATOM   664  C C   . GLU A 1 125 ? -8.291  4.116   13.818  1.00 136.99 ? 119 GLU A C   1 
ATOM   665  O O   . GLU A 1 125 ? -8.102  2.961   14.255  1.00 138.87 ? 119 GLU A O   1 
ATOM   666  C CB  . GLU A 1 125 ? -8.662  2.969   11.651  1.00 134.93 ? 119 GLU A CB  1 
ATOM   667  C CG  . GLU A 1 125 ? -10.072 2.878   11.080  1.00 131.96 ? 119 GLU A CG  1 
ATOM   668  C CD  . GLU A 1 125 ? -10.001 2.440   9.634   1.00 125.79 ? 119 GLU A CD  1 
ATOM   669  O OE1 . GLU A 1 125 ? -9.887  1.218   9.407   1.00 122.74 ? 119 GLU A OE1 1 
ATOM   670  O OE2 . GLU A 1 125 ? -10.040 3.316   8.746   1.00 120.91 ? 119 GLU A OE2 1 
ATOM   671  N N   . VAL A 1 126 ? -8.471  5.183   14.595  1.00 134.47 ? 120 VAL A N   1 
ATOM   672  C CA  . VAL A 1 126 ? -8.264  5.024   16.058  1.00 130.79 ? 120 VAL A CA  1 
ATOM   673  C C   . VAL A 1 126 ? -9.265  4.024   16.651  1.00 134.57 ? 120 VAL A C   1 
ATOM   674  O O   . VAL A 1 126 ? -8.836  3.231   17.510  1.00 130.13 ? 120 VAL A O   1 
ATOM   675  C CB  . VAL A 1 126 ? -8.477  6.421   16.660  1.00 126.23 ? 120 VAL A CB  1 
ATOM   676  C CG1 . VAL A 1 126 ? -8.074  6.490   18.130  1.00 125.18 ? 120 VAL A CG1 1 
ATOM   677  C CG2 . VAL A 1 126 ? -7.786  7.504   15.841  1.00 124.08 ? 120 VAL A CG2 1 
ATOM   678  N N   . ASP A 1 127 ? -10.540 4.072   16.250  1.00 141.59 ? 121 ASP A N   1 
ATOM   679  C CA  . ASP A 1 127 ? -11.522 3.155   16.907  1.00 143.55 ? 121 ASP A CA  1 
ATOM   680  C C   . ASP A 1 127 ? -11.234 1.668   16.650  1.00 146.57 ? 121 ASP A C   1 
ATOM   681  O O   . ASP A 1 127 ? -11.386 0.867   17.595  1.00 145.11 ? 121 ASP A O   1 
ATOM   682  C CB  . ASP A 1 127 ? -12.958 3.466   16.494  1.00 138.48 ? 121 ASP A CB  1 
ATOM   683  C CG  . ASP A 1 127 ? -13.262 4.908   16.112  1.00 132.88 ? 121 ASP A CG  1 
ATOM   684  O OD1 . ASP A 1 127 ? -12.843 5.329   15.012  1.00 125.74 ? 121 ASP A OD1 1 
ATOM   685  O OD2 . ASP A 1 127 ? -13.929 5.595   16.911  1.00 129.67 ? 121 ASP A OD2 1 
ATOM   686  N N   . VAL A 1 128 ? -10.892 1.302   15.411  1.00 148.07 ? 122 VAL A N   1 
ATOM   687  C CA  . VAL A 1 128 ? -10.540 -0.113  15.065  1.00 147.06 ? 122 VAL A CA  1 
ATOM   688  C C   . VAL A 1 128 ? -9.263  -0.577  15.782  1.00 152.34 ? 122 VAL A C   1 
ATOM   689  O O   . VAL A 1 128 ? -9.231  -1.743  16.240  1.00 151.96 ? 122 VAL A O   1 
ATOM   690  C CB  . VAL A 1 128 ? -10.481 -0.335  13.541  1.00 142.27 ? 122 VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 128 ? -9.052  -0.436  13.020  1.00 141.13 ? 122 VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 128 ? -11.286 -1.564  13.136  1.00 139.67 ? 122 VAL A CG2 1 
ATOM   693  N N   . MET A 1 129 ? -8.248  0.299   15.859  1.00 154.65 ? 123 MET A N   1 
ATOM   694  C CA  . MET A 1 129 ? -6.942  -0.150  16.420  1.00 153.72 ? 123 MET A CA  1 
ATOM   695  C C   . MET A 1 129 ? -7.163  -0.552  17.885  1.00 153.60 ? 123 MET A C   1 
ATOM   696  O O   . MET A 1 129 ? -6.655  -1.622  18.294  1.00 151.52 ? 123 MET A O   1 
ATOM   697  C CB  . MET A 1 129 ? -5.883  0.945   16.254  1.00 151.36 ? 123 MET A CB  1 
ATOM   698  C CG  . MET A 1 129 ? -5.554  1.265   14.810  1.00 149.91 ? 123 MET A CG  1 
ATOM   699  S SD  . MET A 1 129 ? -3.939  2.044   14.618  1.00 152.29 ? 123 MET A SD  1 
ATOM   700  C CE  . MET A 1 129 ? -4.325  3.781   14.875  1.00 150.62 ? 123 MET A CE  1 
ATOM   701  N N   . CYS A 1 130 ? -7.967  0.227   18.607  1.00 151.20 ? 124 CYS A N   1 
ATOM   702  C CA  . CYS A 1 130 ? -8.323  -0.100  20.012  1.00 145.92 ? 124 CYS A CA  1 
ATOM   703  C C   . CYS A 1 130 ? -9.097  -1.435  20.025  1.00 146.70 ? 124 CYS A C   1 
ATOM   704  O O   . CYS A 1 130 ? -8.934  -2.183  21.008  1.00 144.91 ? 124 CYS A O   1 
ATOM   705  C CB  . CYS A 1 130 ? -9.056  1.073   20.645  1.00 141.20 ? 124 CYS A CB  1 
ATOM   706  S SG  . CYS A 1 130 ? -8.225  2.653   20.354  1.00 137.33 ? 124 CYS A SG  1 
ATOM   707  N N   . THR A 1 131 ? -9.980  -1.678  19.048  1.00 143.94 ? 125 THR A N   1 
ATOM   708  C CA  . THR A 1 131 ? -10.811 -2.902  19.101  1.00 141.39 ? 125 THR A CA  1 
ATOM   709  C C   . THR A 1 131 ? -9.906  -4.100  19.040  1.00 142.24 ? 125 THR A C   1 
ATOM   710  O O   . THR A 1 131 ? -10.164 -5.057  19.792  1.00 140.97 ? 125 THR A O   1 
ATOM   711  C CB  . THR A 1 131 ? -11.837 -2.929  17.968  1.00 139.38 ? 125 THR A CB  1 
ATOM   712  O OG1 . THR A 1 131 ? -13.104 -3.089  18.595  1.00 133.71 ? 125 THR A OG1 1 
ATOM   713  C CG2 . THR A 1 131 ? -11.649 -4.087  17.006  1.00 139.11 ? 125 THR A CG2 1 
ATOM   714  N N   . ALA A 1 132 ? -8.870  -4.062  18.205  1.00 144.46 ? 126 ALA A N   1 
ATOM   715  C CA  . ALA A 1 132 ? -7.922  -5.196  18.241  1.00 145.79 ? 126 ALA A CA  1 
ATOM   716  C C   . ALA A 1 132 ? -7.302  -5.203  19.631  1.00 150.12 ? 126 ALA A C   1 
ATOM   717  O O   . ALA A 1 132 ? -7.166  -6.278  20.231  1.00 154.63 ? 126 ALA A O   1 
ATOM   718  C CB  . ALA A 1 132 ? -6.885  -5.070  17.163  1.00 143.35 ? 126 ALA A CB  1 
ATOM   719  N N   . PHE A 1 133 ? -6.984  -4.020  20.152  1.00 152.48 ? 127 PHE A N   1 
ATOM   720  C CA  . PHE A 1 133 ? -6.487  -3.959  21.547  1.00 154.72 ? 127 PHE A CA  1 
ATOM   721  C C   . PHE A 1 133 ? -7.593  -4.448  22.470  1.00 158.81 ? 127 PHE A C   1 
ATOM   722  O O   . PHE A 1 133 ? -7.583  -4.001  23.642  1.00 163.71 ? 127 PHE A O   1 
ATOM   723  C CB  . PHE A 1 133 ? -6.085  -2.524  21.889  1.00 153.88 ? 127 PHE A CB  1 
ATOM   724  C CG  . PHE A 1 133 ? -4.754  -2.399  22.611  1.00 153.09 ? 127 PHE A CG  1 
ATOM   725  C CD1 . PHE A 1 133 ? -3.562  -2.695  21.961  1.00 152.50 ? 127 PHE A CD1 1 
ATOM   726  C CD2 . PHE A 1 133 ? -4.704  -2.000  23.941  1.00 150.28 ? 127 PHE A CD2 1 
ATOM   727  C CE1 . PHE A 1 133 ? -2.352  -2.585  22.623  1.00 150.77 ? 127 PHE A CE1 1 
ATOM   728  C CE2 . PHE A 1 133 ? -3.492  -1.891  24.597  1.00 149.19 ? 127 PHE A CE2 1 
ATOM   729  C CZ  . PHE A 1 133 ? -2.320  -2.184  23.940  1.00 150.61 ? 127 PHE A CZ  1 
ATOM   730  N N   . ASN A 1 136 ? -7.570  -9.878  20.945  1.00 151.31 ? 130 ASN A N   1 
ATOM   731  C CA  . ASN A 1 136 ? -6.245  -10.362 21.413  1.00 145.18 ? 130 ASN A CA  1 
ATOM   732  C C   . ASN A 1 136 ? -5.193  -9.307  21.091  1.00 144.25 ? 130 ASN A C   1 
ATOM   733  O O   . ASN A 1 136 ? -4.852  -9.135  19.903  1.00 140.56 ? 130 ASN A O   1 
ATOM   734  C CB  . ASN A 1 136 ? -5.865  -11.715 20.827  1.00 141.42 ? 130 ASN A CB  1 
ATOM   735  C CG  . ASN A 1 136 ? -4.975  -12.498 21.759  1.00 138.08 ? 130 ASN A CG  1 
ATOM   736  O OD1 . ASN A 1 136 ? -3.964  -13.063 21.329  1.00 133.84 ? 130 ASN A OD1 1 
ATOM   737  N ND2 . ASN A 1 136 ? -5.332  -12.541 23.034  1.00 138.40 ? 130 ASN A ND2 1 
ATOM   738  N N   . GLU A 1 137 ? -4.697  -8.638  22.125  1.00 145.17 ? 131 GLU A N   1 
ATOM   739  C CA  . GLU A 1 137 ? -3.632  -7.625  21.947  1.00 143.62 ? 131 GLU A CA  1 
ATOM   740  C C   . GLU A 1 137 ? -2.402  -8.339  21.400  1.00 138.10 ? 131 GLU A C   1 
ATOM   741  O O   . GLU A 1 137 ? -1.715  -7.769  20.542  1.00 136.10 ? 131 GLU A O   1 
ATOM   742  C CB  . GLU A 1 137 ? -3.281  -6.957  23.275  1.00 144.47 ? 131 GLU A CB  1 
ATOM   743  C CG  . GLU A 1 137 ? -3.085  -7.931  24.436  1.00 144.48 ? 131 GLU A CG  1 
ATOM   744  C CD  . GLU A 1 137 ? -4.289  -8.739  24.896  1.00 142.73 ? 131 GLU A CD  1 
ATOM   745  O OE1 . GLU A 1 137 ? -5.419  -8.217  24.819  1.00 140.66 ? 131 GLU A OE1 1 
ATOM   746  O OE2 . GLU A 1 137 ? -4.101  -9.901  25.311  1.00 141.33 ? 131 GLU A OE2 1 
ATOM   747  N N   . GLU A 1 138 ? -2.126  -9.533  21.904  1.00 135.80 ? 132 GLU A N   1 
ATOM   748  C CA  . GLU A 1 138 ? -0.880  -10.180 21.456  1.00 136.63 ? 132 GLU A CA  1 
ATOM   749  C C   . GLU A 1 138 ? -0.976  -10.424 19.950  1.00 138.95 ? 132 GLU A C   1 
ATOM   750  O O   . GLU A 1 138 ? 0.020   -10.155 19.256  1.00 142.87 ? 132 GLU A O   1 
ATOM   751  C CB  . GLU A 1 138 ? -0.721  -11.512 22.182  1.00 136.25 ? 132 GLU A CB  1 
ATOM   752  C CG  . GLU A 1 138 ? 0.725   -11.993 22.255  1.00 136.04 ? 132 GLU A CG  1 
ATOM   753  C CD  . GLU A 1 138 ? 1.643   -11.179 23.150  1.00 137.74 ? 132 GLU A CD  1 
ATOM   754  O OE1 . GLU A 1 138 ? 1.161   -10.616 24.154  1.00 139.98 ? 132 GLU A OE1 1 
ATOM   755  O OE2 . GLU A 1 138 ? 2.851   -11.116 22.843  1.00 136.40 ? 132 GLU A OE2 1 
ATOM   756  N N   . THR A 1 139 ? -2.132  -10.864 19.452  1.00 138.33 ? 133 THR A N   1 
ATOM   757  C CA  . THR A 1 139 ? -2.254  -11.017 17.991  1.00 133.85 ? 133 THR A CA  1 
ATOM   758  C C   . THR A 1 139 ? -2.120  -9.670  17.331  1.00 133.02 ? 133 THR A C   1 
ATOM   759  O O   . THR A 1 139 ? -1.442  -9.589  16.293  1.00 135.90 ? 133 THR A O   1 
ATOM   760  C CB  . THR A 1 139 ? -3.577  -11.693 17.644  1.00 129.22 ? 133 THR A CB  1 
ATOM   761  O OG1 . THR A 1 139 ? -3.728  -12.727 18.611  1.00 127.90 ? 133 THR A OG1 1 
ATOM   762  C CG2 . THR A 1 139 ? -3.566  -12.289 16.249  1.00 125.05 ? 133 THR A CG2 1 
ATOM   763  N N   . PHE A 1 140 ? -2.733  -8.641  17.908  1.00 132.42 ? 134 PHE A N   1 
ATOM   764  C CA  . PHE A 1 140 ? -2.702  -7.335  17.216  1.00 136.22 ? 134 PHE A CA  1 
ATOM   765  C C   . PHE A 1 140 ? -1.285  -6.827  17.103  1.00 140.68 ? 134 PHE A C   1 
ATOM   766  O O   . PHE A 1 140 ? -0.887  -6.320  16.033  1.00 143.61 ? 134 PHE A O   1 
ATOM   767  C CB  . PHE A 1 140 ? -3.517  -6.425  18.131  1.00 137.29 ? 134 PHE A CB  1 
ATOM   768  C CG  . PHE A 1 140 ? -3.276  -4.932  17.968  1.00 138.34 ? 134 PHE A CG  1 
ATOM   769  C CD1 . PHE A 1 140 ? -3.838  -4.231  16.910  1.00 139.33 ? 134 PHE A CD1 1 
ATOM   770  C CD2 . PHE A 1 140 ? -2.499  -4.232  18.882  1.00 138.36 ? 134 PHE A CD2 1 
ATOM   771  C CE1 . PHE A 1 140 ? -3.623  -2.871  16.767  1.00 140.20 ? 134 PHE A CE1 1 
ATOM   772  C CE2 . PHE A 1 140 ? -2.284  -2.873  18.731  1.00 139.78 ? 134 PHE A CE2 1 
ATOM   773  C CZ  . PHE A 1 140 ? -2.847  -2.196  17.677  1.00 140.19 ? 134 PHE A CZ  1 
ATOM   774  N N   . LEU A 1 141 ? -0.511  -6.972  18.179  1.00 143.16 ? 135 LEU A N   1 
ATOM   775  C CA  . LEU A 1 141 ? 0.912   -6.550  18.153  1.00 140.88 ? 135 LEU A CA  1 
ATOM   776  C C   . LEU A 1 141 ? 1.694   -7.387  17.140  1.00 141.62 ? 135 LEU A C   1 
ATOM   777  O O   . LEU A 1 141 ? 2.515   -6.821  16.404  1.00 139.16 ? 135 LEU A O   1 
ATOM   778  C CB  . LEU A 1 141 ? 1.472   -6.714  19.562  1.00 137.65 ? 135 LEU A CB  1 
ATOM   779  C CG  . LEU A 1 141 ? 1.280   -5.518  20.498  1.00 135.77 ? 135 LEU A CG  1 
ATOM   780  C CD1 . LEU A 1 141 ? 1.486   -5.938  21.942  1.00 134.76 ? 135 LEU A CD1 1 
ATOM   781  C CD2 . LEU A 1 141 ? 2.231   -4.395  20.123  1.00 133.94 ? 135 LEU A CD2 1 
ATOM   782  N N   . LYS A 1 142 ? 1.421   -8.688  17.108  1.00 144.33 ? 136 LYS A N   1 
ATOM   783  C CA  . LYS A 1 142 ? 2.188   -9.596  16.229  1.00 144.88 ? 136 LYS A CA  1 
ATOM   784  C C   . LYS A 1 142 ? 1.983   -9.244  14.755  1.00 146.73 ? 136 LYS A C   1 
ATOM   785  O O   . LYS A 1 142 ? 2.972   -9.253  13.995  1.00 147.43 ? 136 LYS A O   1 
ATOM   786  C CB  . LYS A 1 142 ? 1.694   -11.009 16.533  1.00 147.26 ? 136 LYS A CB  1 
ATOM   787  C CG  . LYS A 1 142 ? 2.315   -11.662 17.760  1.00 147.25 ? 136 LYS A CG  1 
ATOM   788  C CD  . LYS A 1 142 ? 1.483   -12.814 18.311  1.00 147.00 ? 136 LYS A CD  1 
ATOM   789  C CE  . LYS A 1 142 ? 2.321   -13.884 18.931  1.00 147.57 ? 136 LYS A CE  1 
ATOM   790  N NZ  . LYS A 1 142 ? 1.693   -14.441 20.131  1.00 148.05 ? 136 LYS A NZ  1 
ATOM   791  N N   . LYS A 1 143 ? 0.754   -8.920  14.368  1.00 149.47 ? 137 LYS A N   1 
ATOM   792  C CA  . LYS A 1 143 ? 0.575   -8.505  12.959  1.00 149.14 ? 137 LYS A CA  1 
ATOM   793  C C   . LYS A 1 143 ? 1.387   -7.224  12.746  1.00 148.89 ? 137 LYS A C   1 
ATOM   794  O O   . LYS A 1 143 ? 2.046   -7.101  11.698  1.00 149.68 ? 137 LYS A O   1 
ATOM   795  C CB  . LYS A 1 143 ? -0.908  -8.344  12.608  1.00 149.11 ? 137 LYS A CB  1 
ATOM   796  C CG  . LYS A 1 143 ? -1.623  -7.112  13.136  1.00 148.74 ? 137 LYS A CG  1 
ATOM   797  C CD  . LYS A 1 143 ? -3.066  -7.403  13.534  1.00 149.41 ? 137 LYS A CD  1 
ATOM   798  C CE  . LYS A 1 143 ? -3.341  -8.868  13.664  1.00 150.49 ? 137 LYS A CE  1 
ATOM   799  N NZ  . LYS A 1 143 ? -4.578  -9.257  12.982  1.00 150.16 ? 137 LYS A NZ  1 
ATOM   800  N N   . TYR A 1 144 ? 1.352   -6.320  13.722  1.00 147.80 ? 138 TYR A N   1 
ATOM   801  C CA  . TYR A 1 144 ? 2.058   -5.030  13.531  1.00 146.53 ? 138 TYR A CA  1 
ATOM   802  C C   . TYR A 1 144 ? 3.537   -5.326  13.386  1.00 147.97 ? 138 TYR A C   1 
ATOM   803  O O   . TYR A 1 144 ? 4.222   -4.749  12.527  1.00 149.86 ? 138 TYR A O   1 
ATOM   804  C CB  . TYR A 1 144 ? 1.724   -4.114  14.713  1.00 141.16 ? 138 TYR A CB  1 
ATOM   805  C CG  . TYR A 1 144 ? 2.828   -3.179  15.190  1.00 133.57 ? 138 TYR A CG  1 
ATOM   806  C CD1 . TYR A 1 144 ? 3.136   -2.017  14.495  1.00 128.77 ? 138 TYR A CD1 1 
ATOM   807  C CD2 . TYR A 1 144 ? 3.545   -3.446  16.348  1.00 129.66 ? 138 TYR A CD2 1 
ATOM   808  C CE1 . TYR A 1 144 ? 4.134   -1.160  14.926  1.00 124.96 ? 138 TYR A CE1 1 
ATOM   809  C CE2 . TYR A 1 144 ? 4.546   -2.598  16.790  1.00 128.86 ? 138 TYR A CE2 1 
ATOM   810  C CZ  . TYR A 1 144 ? 4.841   -1.451  16.077  1.00 126.02 ? 138 TYR A CZ  1 
ATOM   811  O OH  . TYR A 1 144 ? 5.825   -0.611  16.512  1.00 121.14 ? 138 TYR A OH  1 
ATOM   812  N N   . LEU A 1 145 ? 4.024   -6.249  14.205  1.00 146.20 ? 139 LEU A N   1 
ATOM   813  C CA  . LEU A 1 145 ? 5.467   -6.587  14.160  1.00 144.14 ? 139 LEU A CA  1 
ATOM   814  C C   . LEU A 1 145 ? 5.839   -7.182  12.801  1.00 139.51 ? 139 LEU A C   1 
ATOM   815  O O   . LEU A 1 145 ? 6.890   -6.804  12.251  1.00 135.70 ? 139 LEU A O   1 
ATOM   816  C CB  . LEU A 1 145 ? 5.777   -7.568  15.288  1.00 145.17 ? 139 LEU A CB  1 
ATOM   817  C CG  . LEU A 1 145 ? 6.387   -8.912  14.874  1.00 146.19 ? 139 LEU A CG  1 
ATOM   818  C CD1 . LEU A 1 145 ? 7.895   -8.919  15.060  1.00 146.73 ? 139 LEU A CD1 1 
ATOM   819  C CD2 . LEU A 1 145 ? 5.748   -10.057 15.637  1.00 145.06 ? 139 LEU A CD2 1 
ATOM   820  N N   . TYR A 1 146 ? 4.984   -8.044  12.257  1.00 136.98 ? 140 TYR A N   1 
ATOM   821  C CA  . TYR A 1 146 ? 5.417   -8.718  11.010  1.00 135.83 ? 140 TYR A CA  1 
ATOM   822  C C   . TYR A 1 146 ? 5.590   -7.637  9.995   1.00 130.58 ? 140 TYR A C   1 
ATOM   823  O O   . TYR A 1 146 ? 6.561   -7.620  9.227   1.00 127.32 ? 140 TYR A O   1 
ATOM   824  C CB  . TYR A 1 146 ? 4.474   -9.861  10.599  1.00 140.86 ? 140 TYR A CB  1 
ATOM   825  C CG  . TYR A 1 146 ? 3.043   -9.613  10.141  1.00 146.64 ? 140 TYR A CG  1 
ATOM   826  C CD1 . TYR A 1 146 ? 2.731   -8.675  9.165   1.00 150.01 ? 140 TYR A CD1 1 
ATOM   827  C CD2 . TYR A 1 146 ? 2.006   -10.388 10.643  1.00 149.45 ? 140 TYR A CD2 1 
ATOM   828  C CE1 . TYR A 1 146 ? 1.426   -8.472  8.749   1.00 152.63 ? 140 TYR A CE1 1 
ATOM   829  C CE2 . TYR A 1 146 ? 0.698   -10.208 10.226  1.00 150.79 ? 140 TYR A CE2 1 
ATOM   830  C CZ  . TYR A 1 146 ? 0.406   -9.242  9.281   1.00 151.60 ? 140 TYR A CZ  1 
ATOM   831  O OH  . TYR A 1 146 ? -0.885  -9.061  8.876   1.00 149.25 ? 140 TYR A OH  1 
ATOM   832  N N   . GLU A 1 147 ? 4.663   -6.701  10.024  1.00 130.47 ? 141 GLU A N   1 
ATOM   833  C CA  . GLU A 1 147 ? 4.731   -5.718  8.937   1.00 136.81 ? 141 GLU A CA  1 
ATOM   834  C C   . GLU A 1 147 ? 6.033   -4.929  9.005   1.00 138.01 ? 141 GLU A C   1 
ATOM   835  O O   . GLU A 1 147 ? 6.659   -4.750  7.943   1.00 140.63 ? 141 GLU A O   1 
ATOM   836  C CB  . GLU A 1 147 ? 3.490   -4.854  9.155   1.00 139.27 ? 141 GLU A CB  1 
ATOM   837  C CG  . GLU A 1 147 ? 3.755   -3.427  9.623   1.00 138.28 ? 141 GLU A CG  1 
ATOM   838  C CD  . GLU A 1 147 ? 2.662   -2.881  10.525  1.00 134.70 ? 141 GLU A CD  1 
ATOM   839  O OE1 . GLU A 1 147 ? 1.477   -3.181  10.277  1.00 130.98 ? 141 GLU A OE1 1 
ATOM   840  O OE2 . GLU A 1 147 ? 2.995   -2.150  11.479  1.00 131.63 ? 141 GLU A OE2 1 
ATOM   841  N N   . ILE A 1 148 ? 6.461   -4.511  10.191  1.00 136.20 ? 142 ILE A N   1 
ATOM   842  C CA  . ILE A 1 148 ? 7.757   -3.781  10.170  1.00 135.48 ? 142 ILE A CA  1 
ATOM   843  C C   . ILE A 1 148 ? 8.847   -4.754  9.699   1.00 135.85 ? 142 ILE A C   1 
ATOM   844  O O   . ILE A 1 148 ? 9.706   -4.363  8.892   1.00 137.79 ? 142 ILE A O   1 
ATOM   845  C CB  . ILE A 1 148 ? 8.054   -3.134  11.531  1.00 133.06 ? 142 ILE A CB  1 
ATOM   846  C CG1 . ILE A 1 148 ? 6.784   -2.918  12.341  1.00 130.17 ? 142 ILE A CG1 1 
ATOM   847  C CG2 . ILE A 1 148 ? 8.824   -1.827  11.344  1.00 133.22 ? 142 ILE A CG2 1 
ATOM   848  C CD1 . ILE A 1 148 ? 6.167   -1.546  12.157  1.00 128.25 ? 142 ILE A CD1 1 
ATOM   849  N N   . ALA A 1 149 ? 8.792   -5.991  10.190  1.00 134.67 ? 143 ALA A N   1 
ATOM   850  C CA  . ALA A 1 149 ? 9.863   -6.954  9.849   1.00 132.37 ? 143 ALA A CA  1 
ATOM   851  C C   . ALA A 1 149 ? 9.858   -7.222  8.350   1.00 133.09 ? 143 ALA A C   1 
ATOM   852  O O   . ALA A 1 149 ? 10.928  -7.261  7.704   1.00 127.05 ? 143 ALA A O   1 
ATOM   853  C CB  . ALA A 1 149 ? 9.664   -8.218  10.642  1.00 130.44 ? 143 ALA A CB  1 
ATOM   854  N N   . ARG A 1 150 ? 8.655   -7.352  7.806   1.00 133.47 ? 144 ARG A N   1 
ATOM   855  C CA  . ARG A 1 150 ? 8.545   -7.657  6.371   1.00 134.38 ? 144 ARG A CA  1 
ATOM   856  C C   . ARG A 1 150 ? 9.148   -6.499  5.581   1.00 137.07 ? 144 ARG A C   1 
ATOM   857  O O   . ARG A 1 150 ? 9.863   -6.773  4.598   1.00 139.11 ? 144 ARG A O   1 
ATOM   858  C CB  . ARG A 1 150 ? 7.055   -7.797  6.071   1.00 135.08 ? 144 ARG A CB  1 
ATOM   859  C CG  . ARG A 1 150 ? 6.554   -9.225  5.918   1.00 138.47 ? 144 ARG A CG  1 
ATOM   860  C CD  . ARG A 1 150 ? 6.129   -9.866  7.227   1.00 141.77 ? 144 ARG A CD  1 
ATOM   861  N NE  . ARG A 1 150 ? 5.366   -11.105 7.040   1.00 144.49 ? 144 ARG A NE  1 
ATOM   862  C CZ  . ARG A 1 150 ? 4.044   -11.184 6.954   1.00 147.58 ? 144 ARG A CZ  1 
ATOM   863  N NH1 . ARG A 1 150 ? 3.415   -10.656 5.921   1.00 150.02 ? 144 ARG A NH1 1 
ATOM   864  N NH2 . ARG A 1 150 ? 3.356   -11.802 7.897   1.00 145.57 ? 144 ARG A NH2 1 
ATOM   865  N N   . ARG A 1 151 ? 8.893   -5.260  6.003   1.00 137.42 ? 145 ARG A N   1 
ATOM   866  C CA  . ARG A 1 151 ? 9.325   -4.125  5.147   1.00 140.00 ? 145 ARG A CA  1 
ATOM   867  C C   . ARG A 1 151 ? 10.840  -3.985  4.929   1.00 142.26 ? 145 ARG A C   1 
ATOM   868  O O   . ARG A 1 151 ? 11.232  -3.714  3.777   1.00 144.21 ? 145 ARG A O   1 
ATOM   869  C CB  . ARG A 1 151 ? 8.822   -2.789  5.708   1.00 142.69 ? 145 ARG A CB  1 
ATOM   870  C CG  . ARG A 1 151 ? 9.230   -2.269  7.079   1.00 145.13 ? 145 ARG A CG  1 
ATOM   871  C CD  . ARG A 1 151 ? 10.422  -1.323  7.105   1.00 148.85 ? 145 ARG A CD  1 
ATOM   872  N NE  . ARG A 1 151 ? 10.235  -0.090  6.331   1.00 153.62 ? 145 ARG A NE  1 
ATOM   873  C CZ  . ARG A 1 151 ? 11.230  0.611   5.801   1.00 156.90 ? 145 ARG A CZ  1 
ATOM   874  N NH1 . ARG A 1 151 ? 11.113  1.110   4.584   1.00 158.96 ? 145 ARG A NH1 1 
ATOM   875  N NH2 . ARG A 1 151 ? 12.341  0.806   6.488   1.00 156.13 ? 145 ARG A NH2 1 
ATOM   876  N N   . HIS A 1 152 ? 11.672  -4.161  5.954   1.00 141.69 ? 146 HIS A N   1 
ATOM   877  C CA  . HIS A 1 152 ? 13.113  -3.895  5.675   1.00 139.87 ? 146 HIS A CA  1 
ATOM   878  C C   . HIS A 1 152 ? 14.024  -5.073  6.022   1.00 139.54 ? 146 HIS A C   1 
ATOM   879  O O   . HIS A 1 152 ? 13.926  -5.620  7.133   1.00 137.62 ? 146 HIS A O   1 
ATOM   880  C CB  . HIS A 1 152 ? 13.541  -2.552  6.267   1.00 140.98 ? 146 HIS A CB  1 
ATOM   881  C CG  . HIS A 1 152 ? 14.305  -1.802  5.236   1.00 143.93 ? 146 HIS A CG  1 
ATOM   882  N ND1 . HIS A 1 152 ? 15.657  -1.979  5.039   1.00 144.62 ? 146 HIS A ND1 1 
ATOM   883  C CD2 . HIS A 1 152 ? 13.899  -0.945  4.296   1.00 142.72 ? 146 HIS A CD2 1 
ATOM   884  C CE1 . HIS A 1 152 ? 16.051  -1.215  4.033   1.00 142.90 ? 146 HIS A CE1 1 
ATOM   885  N NE2 . HIS A 1 152 ? 14.997  -0.582  3.566   1.00 144.20 ? 146 HIS A NE2 1 
ATOM   886  N N   . PRO A 1 153 ? 14.926  -5.472  5.104   1.00 140.16 ? 147 PRO A N   1 
ATOM   887  C CA  . PRO A 1 153 ? 15.877  -6.544  5.382   1.00 139.31 ? 147 PRO A CA  1 
ATOM   888  C C   . PRO A 1 153 ? 16.942  -6.428  6.467   1.00 137.51 ? 147 PRO A C   1 
ATOM   889  O O   . PRO A 1 153 ? 17.120  -7.392  7.226   1.00 135.29 ? 147 PRO A O   1 
ATOM   890  C CB  . PRO A 1 153 ? 16.556  -6.620  3.998   1.00 139.04 ? 147 PRO A CB  1 
ATOM   891  C CG  . PRO A 1 153 ? 16.522  -5.204  3.496   1.00 138.38 ? 147 PRO A CG  1 
ATOM   892  C CD  . PRO A 1 153 ? 15.078  -4.871  3.790   1.00 140.07 ? 147 PRO A CD  1 
ATOM   893  N N   . TYR A 1 154 ? 17.701  -5.327  6.472   1.00 135.33 ? 148 TYR A N   1 
ATOM   894  C CA  . TYR A 1 154 ? 18.867  -5.219  7.389   1.00 132.17 ? 148 TYR A CA  1 
ATOM   895  C C   . TYR A 1 154 ? 18.516  -4.537  8.695   1.00 127.63 ? 148 TYR A C   1 
ATOM   896  O O   . TYR A 1 154 ? 19.439  -4.024  9.346   1.00 123.34 ? 148 TYR A O   1 
ATOM   897  C CB  . TYR A 1 154 ? 19.955  -4.375  6.722   1.00 133.60 ? 148 TYR A CB  1 
ATOM   898  C CG  . TYR A 1 154 ? 20.803  -5.059  5.658   1.00 136.54 ? 148 TYR A CG  1 
ATOM   899  C CD1 . TYR A 1 154 ? 20.231  -5.605  4.516   1.00 136.47 ? 148 TYR A CD1 1 
ATOM   900  C CD2 . TYR A 1 154 ? 22.184  -5.134  5.788   1.00 138.22 ? 148 TYR A CD2 1 
ATOM   901  C CE1 . TYR A 1 154 ? 21.005  -6.216  3.543   1.00 137.54 ? 148 TYR A CE1 1 
ATOM   902  C CE2 . TYR A 1 154 ? 22.970  -5.742  4.823   1.00 136.99 ? 148 TYR A CE2 1 
ATOM   903  C CZ  . TYR A 1 154 ? 22.379  -6.284  3.697   1.00 136.17 ? 148 TYR A CZ  1 
ATOM   904  O OH  . TYR A 1 154 ? 23.155  -6.883  2.747   1.00 129.37 ? 148 TYR A OH  1 
ATOM   905  N N   . PHE A 1 155 ? 17.252  -4.548  9.105   1.00 124.68 ? 149 PHE A N   1 
ATOM   906  C CA  . PHE A 1 155 ? 16.969  -3.949  10.430  1.00 123.25 ? 149 PHE A CA  1 
ATOM   907  C C   . PHE A 1 155 ? 17.689  -4.793  11.460  1.00 124.73 ? 149 PHE A C   1 
ATOM   908  O O   . PHE A 1 155 ? 17.708  -6.036  11.334  1.00 128.77 ? 149 PHE A O   1 
ATOM   909  C CB  . PHE A 1 155 ? 15.461  -3.985  10.653  1.00 122.34 ? 149 PHE A CB  1 
ATOM   910  C CG  . PHE A 1 155 ? 14.767  -2.662  10.935  1.00 123.86 ? 149 PHE A CG  1 
ATOM   911  C CD1 . PHE A 1 155 ? 14.478  -2.276  12.237  1.00 126.89 ? 149 PHE A CD1 1 
ATOM   912  C CD2 . PHE A 1 155 ? 14.373  -1.828  9.898   1.00 125.63 ? 149 PHE A CD2 1 
ATOM   913  C CE1 . PHE A 1 155 ? 13.829  -1.083  12.498  1.00 127.58 ? 149 PHE A CE1 1 
ATOM   914  C CE2 . PHE A 1 155 ? 13.725  -0.633  10.163  1.00 126.47 ? 149 PHE A CE2 1 
ATOM   915  C CZ  . PHE A 1 155 ? 13.450  -0.269  11.460  1.00 126.28 ? 149 PHE A CZ  1 
ATOM   916  N N   . TYR A 1 156 ? 18.267  -4.145  12.469  1.00 123.27 ? 150 TYR A N   1 
ATOM   917  C CA  . TYR A 1 156 ? 19.009  -4.886  13.519  1.00 119.24 ? 150 TYR A CA  1 
ATOM   918  C C   . TYR A 1 156 ? 17.975  -5.582  14.364  1.00 117.01 ? 150 TYR A C   1 
ATOM   919  O O   . TYR A 1 156 ? 17.223  -4.908  15.088  1.00 117.34 ? 150 TYR A O   1 
ATOM   920  C CB  . TYR A 1 156 ? 19.852  -3.894  14.317  1.00 117.04 ? 150 TYR A CB  1 
ATOM   921  C CG  . TYR A 1 156 ? 21.038  -4.500  15.047  1.00 116.15 ? 150 TYR A CG  1 
ATOM   922  C CD1 . TYR A 1 156 ? 21.974  -5.265  14.369  1.00 115.51 ? 150 TYR A CD1 1 
ATOM   923  C CD2 . TYR A 1 156 ? 21.222  -4.294  16.407  1.00 117.74 ? 150 TYR A CD2 1 
ATOM   924  C CE1 . TYR A 1 156 ? 23.062  -5.809  15.025  1.00 117.12 ? 150 TYR A CE1 1 
ATOM   925  C CE2 . TYR A 1 156 ? 22.304  -4.838  17.077  1.00 117.17 ? 150 TYR A CE2 1 
ATOM   926  C CZ  . TYR A 1 156 ? 23.222  -5.602  16.382  1.00 117.32 ? 150 TYR A CZ  1 
ATOM   927  O OH  . TYR A 1 156 ? 24.298  -6.140  17.017  1.00 122.39 ? 150 TYR A OH  1 
ATOM   928  N N   . ALA A 1 157 ? 17.953  -6.912  14.325  1.00 111.71 ? 151 ALA A N   1 
ATOM   929  C CA  . ALA A 1 157 ? 16.844  -7.585  15.036  1.00 109.15 ? 151 ALA A CA  1 
ATOM   930  C C   . ALA A 1 157 ? 16.605  -7.036  16.444  1.00 111.05 ? 151 ALA A C   1 
ATOM   931  O O   . ALA A 1 157 ? 15.448  -6.701  16.756  1.00 111.74 ? 151 ALA A O   1 
ATOM   932  C CB  . ALA A 1 157 ? 17.120  -9.065  15.064  1.00 109.23 ? 151 ALA A CB  1 
ATOM   933  N N   . PRO A 1 158 ? 17.621  -6.883  17.317  1.00 114.96 ? 152 PRO A N   1 
ATOM   934  C CA  . PRO A 1 158 ? 17.379  -6.537  18.716  1.00 115.35 ? 152 PRO A CA  1 
ATOM   935  C C   . PRO A 1 158 ? 16.587  -5.265  18.919  1.00 116.00 ? 152 PRO A C   1 
ATOM   936  O O   . PRO A 1 158 ? 15.768  -5.203  19.842  1.00 117.21 ? 152 PRO A O   1 
ATOM   937  C CB  . PRO A 1 158 ? 18.804  -6.437  19.280  1.00 113.81 ? 152 PRO A CB  1 
ATOM   938  C CG  . PRO A 1 158 ? 19.616  -7.330  18.378  1.00 113.88 ? 152 PRO A CG  1 
ATOM   939  C CD  . PRO A 1 158 ? 19.037  -7.014  17.017  1.00 115.08 ? 152 PRO A CD  1 
ATOM   940  N N   . GLU A 1 159 ? 16.867  -4.250  18.122  1.00 116.30 ? 153 GLU A N   1 
ATOM   941  C CA  . GLU A 1 159 ? 16.171  -2.939  18.211  1.00 119.04 ? 153 GLU A CA  1 
ATOM   942  C C   . GLU A 1 159 ? 14.678  -3.132  17.897  1.00 119.15 ? 153 GLU A C   1 
ATOM   943  O O   . GLU A 1 159 ? 13.848  -2.492  18.578  1.00 119.55 ? 153 GLU A O   1 
ATOM   944  C CB  . GLU A 1 159 ? 16.953  -1.883  17.429  1.00 121.17 ? 153 GLU A CB  1 
ATOM   945  C CG  . GLU A 1 159 ? 16.176  -1.229  16.295  1.00 123.62 ? 153 GLU A CG  1 
ATOM   946  C CD  . GLU A 1 159 ? 16.324  -2.153  15.110  1.00 124.31 ? 153 GLU A CD  1 
ATOM   947  O OE1 . GLU A 1 159 ? 15.439  -3.016  14.989  1.00 119.42 ? 153 GLU A OE1 1 
ATOM   948  O OE2 . GLU A 1 159 ? 17.302  -2.033  14.343  1.00 123.80 ? 153 GLU A OE2 1 
ATOM   949  N N   . LEU A 1 160 ? 14.339  -3.998  16.947  1.00 115.75 ? 154 LEU A N   1 
ATOM   950  C CA  . LEU A 1 160 ? 12.942  -4.093  16.468  1.00 113.77 ? 154 LEU A CA  1 
ATOM   951  C C   . LEU A 1 160 ? 12.054  -4.482  17.638  1.00 110.56 ? 154 LEU A C   1 
ATOM   952  O O   . LEU A 1 160 ? 10.965  -3.908  17.781  1.00 105.80 ? 154 LEU A O   1 
ATOM   953  C CB  . LEU A 1 160 ? 12.994  -5.240  15.468  1.00 114.89 ? 154 LEU A CB  1 
ATOM   954  C CG  . LEU A 1 160 ? 12.973  -4.897  13.975  1.00 114.69 ? 154 LEU A CG  1 
ATOM   955  C CD1 . LEU A 1 160 ? 14.133  -5.594  13.300  1.00 115.79 ? 154 LEU A CD1 1 
ATOM   956  C CD2 . LEU A 1 160 ? 11.673  -5.363  13.350  1.00 111.70 ? 154 LEU A CD2 1 
ATOM   957  N N   . LEU A 1 161 ? 12.534  -5.374  18.481  1.00 112.65 ? 155 LEU A N   1 
ATOM   958  C CA  . LEU A 1 161 ? 11.705  -5.863  19.600  1.00 117.58 ? 155 LEU A CA  1 
ATOM   959  C C   . LEU A 1 161 ? 11.386  -4.663  20.485  1.00 118.59 ? 155 LEU A C   1 
ATOM   960  O O   . LEU A 1 161 ? 10.257  -4.580  20.995  1.00 121.02 ? 155 LEU A O   1 
ATOM   961  C CB  . LEU A 1 161 ? 12.477  -6.919  20.387  1.00 118.41 ? 155 LEU A CB  1 
ATOM   962  C CG  . LEU A 1 161 ? 12.943  -8.164  19.621  1.00 119.08 ? 155 LEU A CG  1 
ATOM   963  C CD1 . LEU A 1 161 ? 12.396  -8.326  18.212  1.00 116.40 ? 155 LEU A CD1 1 
ATOM   964  C CD2 . LEU A 1 161 ? 14.449  -8.302  19.618  1.00 119.22 ? 155 LEU A CD2 1 
ATOM   965  N N   . PHE A 1 162 ? 12.353  -3.782  20.681  1.00 120.28 ? 156 PHE A N   1 
ATOM   966  C CA  . PHE A 1 162 ? 12.131  -2.662  21.620  1.00 121.06 ? 156 PHE A CA  1 
ATOM   967  C C   . PHE A 1 162 ? 11.000  -1.762  21.157  1.00 124.44 ? 156 PHE A C   1 
ATOM   968  O O   . PHE A 1 162 ? 10.173  -1.388  22.011  1.00 122.22 ? 156 PHE A O   1 
ATOM   969  C CB  . PHE A 1 162 ? 13.421  -1.850  21.633  1.00 119.80 ? 156 PHE A CB  1 
ATOM   970  C CG  . PHE A 1 162 ? 13.237  -0.441  22.177  1.00 121.37 ? 156 PHE A CG  1 
ATOM   971  C CD1 . PHE A 1 162 ? 13.149  -0.213  23.545  1.00 119.11 ? 156 PHE A CD1 1 
ATOM   972  C CD2 . PHE A 1 162 ? 13.132  0.648   21.320  1.00 119.08 ? 156 PHE A CD2 1 
ATOM   973  C CE1 . PHE A 1 162 ? 12.973  1.068   24.038  1.00 116.58 ? 156 PHE A CE1 1 
ATOM   974  C CE2 . PHE A 1 162 ? 12.951  1.925   21.820  1.00 116.56 ? 156 PHE A CE2 1 
ATOM   975  C CZ  . PHE A 1 162 ? 12.875  2.132   23.176  1.00 116.75 ? 156 PHE A CZ  1 
ATOM   976  N N   . PHE A 1 163 ? 10.928  -1.420  19.870  1.00 127.10 ? 157 PHE A N   1 
ATOM   977  C CA  . PHE A 1 163 ? 9.920   -0.404  19.444  1.00 128.00 ? 157 PHE A CA  1 
ATOM   978  C C   . PHE A 1 163 ? 8.510   -0.906  19.701  1.00 126.33 ? 157 PHE A C   1 
ATOM   979  O O   . PHE A 1 163 ? 7.589   -0.129  20.014  1.00 119.53 ? 157 PHE A O   1 
ATOM   980  C CB  . PHE A 1 163 ? 10.149  0.036   17.995  1.00 130.82 ? 157 PHE A CB  1 
ATOM   981  C CG  . PHE A 1 163 ? 10.087  -0.990  16.874  1.00 133.30 ? 157 PHE A CG  1 
ATOM   982  C CD1 . PHE A 1 163 ? 8.988   -1.824  16.715  1.00 134.20 ? 157 PHE A CD1 1 
ATOM   983  C CD2 . PHE A 1 163 ? 11.114  -1.073  15.942  1.00 133.91 ? 157 PHE A CD2 1 
ATOM   984  C CE1 . PHE A 1 163 ? 8.939   -2.744  15.683  1.00 133.87 ? 157 PHE A CE1 1 
ATOM   985  C CE2 . PHE A 1 163 ? 11.053  -1.984  14.903  1.00 133.62 ? 157 PHE A CE2 1 
ATOM   986  C CZ  . PHE A 1 163 ? 9.970   -2.820  14.780  1.00 132.90 ? 157 PHE A CZ  1 
ATOM   987  N N   . ALA A 1 164 ? 8.346   -2.212  19.591  1.00 127.71 ? 158 ALA A N   1 
ATOM   988  C CA  . ALA A 1 164 ? 6.994   -2.767  19.745  1.00 127.38 ? 158 ALA A CA  1 
ATOM   989  C C   . ALA A 1 164 ? 6.510   -2.471  21.162  1.00 136.04 ? 158 ALA A C   1 
ATOM   990  O O   . ALA A 1 164 ? 5.334   -2.108  21.343  1.00 142.67 ? 158 ALA A O   1 
ATOM   991  C CB  . ALA A 1 164 ? 7.074   -4.237  19.459  1.00 121.88 ? 158 ALA A CB  1 
ATOM   992  N N   . LYS A 1 165 ? 7.394   -2.603  22.148  1.00 140.94 ? 159 LYS A N   1 
ATOM   993  C CA  . LYS A 1 165 ? 6.973   -2.429  23.563  1.00 144.61 ? 159 LYS A CA  1 
ATOM   994  C C   . LYS A 1 165 ? 6.484   -0.992  23.770  1.00 144.87 ? 159 LYS A C   1 
ATOM   995  O O   . LYS A 1 165 ? 5.502   -0.778  24.504  1.00 142.65 ? 159 LYS A O   1 
ATOM   996  C CB  . LYS A 1 165 ? 8.140   -2.772  24.495  1.00 145.41 ? 159 LYS A CB  1 
ATOM   997  C CG  . LYS A 1 165 ? 7.770   -3.136  25.923  1.00 144.74 ? 159 LYS A CG  1 
ATOM   998  C CD  . LYS A 1 165 ? 9.000   -3.380  26.787  1.00 143.90 ? 159 LYS A CD  1 
ATOM   999  C CE  . LYS A 1 165 ? 10.263  -3.413  25.986  1.00 143.87 ? 159 LYS A CE  1 
ATOM   1000 N NZ  . LYS A 1 165 ? 10.570  -4.759  25.496  1.00 143.01 ? 159 LYS A NZ  1 
ATOM   1001 N N   . ARG A 1 166 ? 7.179   -0.044  23.166  1.00 145.84 ? 160 ARG A N   1 
ATOM   1002 C CA  . ARG A 1 166 ? 6.739   1.365   23.257  1.00 147.77 ? 160 ARG A CA  1 
ATOM   1003 C C   . ARG A 1 166 ? 5.361   1.484   22.592  1.00 145.76 ? 160 ARG A C   1 
ATOM   1004 O O   . ARG A 1 166 ? 4.516   2.231   23.124  1.00 146.58 ? 160 ARG A O   1 
ATOM   1005 C CB  . ARG A 1 166 ? 7.838   2.234   22.644  1.00 149.59 ? 160 ARG A CB  1 
ATOM   1006 C CG  . ARG A 1 166 ? 9.187   1.951   23.290  1.00 149.61 ? 160 ARG A CG  1 
ATOM   1007 C CD  . ARG A 1 166 ? 9.221   2.335   24.764  1.00 150.47 ? 160 ARG A CD  1 
ATOM   1008 N NE  . ARG A 1 166 ? 8.793   1.259   25.666  1.00 152.49 ? 160 ARG A NE  1 
ATOM   1009 C CZ  . ARG A 1 166 ? 7.803   1.368   26.544  1.00 153.58 ? 160 ARG A CZ  1 
ATOM   1010 N NH1 . ARG A 1 166 ? 7.675   2.466   27.266  1.00 152.33 ? 160 ARG A NH1 1 
ATOM   1011 N NH2 . ARG A 1 166 ? 6.944   0.378   26.699  1.00 155.82 ? 160 ARG A NH2 1 
ATOM   1012 N N   . TYR A 1 167 ? 5.157   0.793   21.472  1.00 141.61 ? 161 TYR A N   1 
ATOM   1013 C CA  . TYR A 1 167 ? 3.872   0.907   20.740  1.00 138.68 ? 161 TYR A CA  1 
ATOM   1014 C C   . TYR A 1 167 ? 2.744   0.405   21.628  1.00 137.99 ? 161 TYR A C   1 
ATOM   1015 O O   . TYR A 1 167 ? 1.673   1.042   21.699  1.00 134.14 ? 161 TYR A O   1 
ATOM   1016 C CB  . TYR A 1 167 ? 4.075   0.064   19.480  1.00 135.28 ? 161 TYR A CB  1 
ATOM   1017 C CG  . TYR A 1 167 ? 2.869   -0.160  18.579  1.00 132.08 ? 161 TYR A CG  1 
ATOM   1018 C CD1 . TYR A 1 167 ? 2.004   -1.223  18.791  1.00 130.13 ? 161 TYR A CD1 1 
ATOM   1019 C CD2 . TYR A 1 167 ? 2.621   0.668   17.494  1.00 128.95 ? 161 TYR A CD2 1 
ATOM   1020 C CE1 . TYR A 1 167 ? 0.919   -1.447  17.961  1.00 130.69 ? 161 TYR A CE1 1 
ATOM   1021 C CE2 . TYR A 1 167 ? 1.540   0.455   16.656  1.00 126.80 ? 161 TYR A CE2 1 
ATOM   1022 C CZ  . TYR A 1 167 ? 0.686   -0.606  16.890  1.00 127.25 ? 161 TYR A CZ  1 
ATOM   1023 O OH  . TYR A 1 167 ? -0.384  -0.817  16.071  1.00 122.29 ? 161 TYR A OH  1 
ATOM   1024 N N   . LYS A 1 168 ? 2.994   -0.688  22.343  1.00 138.20 ? 162 LYS A N   1 
ATOM   1025 C CA  . LYS A 1 168 ? 1.976   -1.210  23.285  1.00 136.68 ? 162 LYS A CA  1 
ATOM   1026 C C   . LYS A 1 168 ? 1.732   -0.166  24.375  1.00 137.76 ? 162 LYS A C   1 
ATOM   1027 O O   . LYS A 1 168 ? 0.566   0.045   24.753  1.00 137.32 ? 162 LYS A O   1 
ATOM   1028 C CB  . LYS A 1 168 ? 2.372   -2.549  23.916  1.00 134.39 ? 162 LYS A CB  1 
ATOM   1029 C CG  . LYS A 1 168 ? 3.271   -2.537  25.144  1.00 132.33 ? 162 LYS A CG  1 
ATOM   1030 C CD  . LYS A 1 168 ? 2.570   -2.685  26.488  1.00 130.30 ? 162 LYS A CD  1 
ATOM   1031 C CE  . LYS A 1 168 ? 3.488   -2.344  27.620  1.00 127.35 ? 162 LYS A CE  1 
ATOM   1032 N NZ  . LYS A 1 168 ? 2.808   -1.585  28.672  1.00 123.53 ? 162 LYS A NZ  1 
ATOM   1033 N N   . ALA A 1 169 ? 2.792   0.480   24.847  1.00 136.70 ? 163 ALA A N   1 
ATOM   1034 C CA  . ALA A 1 169 ? 2.569   1.376   25.995  1.00 135.55 ? 163 ALA A CA  1 
ATOM   1035 C C   . ALA A 1 169 ? 1.618   2.480   25.565  1.00 134.64 ? 163 ALA A C   1 
ATOM   1036 O O   . ALA A 1 169 ? 0.714   2.856   26.334  1.00 131.63 ? 163 ALA A O   1 
ATOM   1037 C CB  . ALA A 1 169 ? 3.886   1.946   26.436  1.00 135.39 ? 163 ALA A CB  1 
ATOM   1038 N N   . ALA A 1 170 ? 1.826   2.987   24.358  1.00 139.09 ? 164 ALA A N   1 
ATOM   1039 C CA  . ALA A 1 170 ? 0.963   4.105   23.941  1.00 140.19 ? 164 ALA A CA  1 
ATOM   1040 C C   . ALA A 1 170 ? -0.477  3.617   23.867  1.00 138.46 ? 164 ALA A C   1 
ATOM   1041 O O   . ALA A 1 170 ? -1.383  4.332   24.305  1.00 140.20 ? 164 ALA A O   1 
ATOM   1042 C CB  . ALA A 1 170 ? 1.418   4.624   22.602  1.00 140.54 ? 164 ALA A CB  1 
ATOM   1043 N N   . PHE A 1 171 ? -0.688  2.423   23.324  1.00 135.77 ? 165 PHE A N   1 
ATOM   1044 C CA  . PHE A 1 171 ? -2.111  2.021   23.221  1.00 133.74 ? 165 PHE A CA  1 
ATOM   1045 C C   . PHE A 1 171 ? -2.672  1.894   24.637  1.00 137.66 ? 165 PHE A C   1 
ATOM   1046 O O   . PHE A 1 171 ? -3.815  2.318   24.886  1.00 137.64 ? 165 PHE A O   1 
ATOM   1047 C CB  . PHE A 1 171 ? -2.324  0.781   22.354  1.00 128.27 ? 165 PHE A CB  1 
ATOM   1048 C CG  . PHE A 1 171 ? -2.231  0.972   20.850  1.00 124.23 ? 165 PHE A CG  1 
ATOM   1049 C CD1 . PHE A 1 171 ? -1.010  1.211   20.237  1.00 123.12 ? 165 PHE A CD1 1 
ATOM   1050 C CD2 . PHE A 1 171 ? -3.363  0.883   20.052  1.00 124.29 ? 165 PHE A CD2 1 
ATOM   1051 C CE1 . PHE A 1 171 ? -0.930  1.377   18.868  1.00 122.13 ? 165 PHE A CE1 1 
ATOM   1052 C CE2 . PHE A 1 171 ? -3.274  1.048   18.681  1.00 124.11 ? 165 PHE A CE2 1 
ATOM   1053 C CZ  . PHE A 1 171 ? -2.059  1.292   18.093  1.00 121.18 ? 165 PHE A CZ  1 
ATOM   1054 N N   . THR A 1 172 ? -1.890  1.319   25.555  1.00 141.16 ? 166 THR A N   1 
ATOM   1055 C CA  . THR A 1 172 ? -2.496  1.096   26.878  1.00 141.50 ? 166 THR A CA  1 
ATOM   1056 C C   . THR A 1 172 ? -2.851  2.412   27.501  1.00 145.93 ? 166 THR A C   1 
ATOM   1057 O O   . THR A 1 172 ? -3.936  2.491   28.101  1.00 145.08 ? 166 THR A O   1 
ATOM   1058 C CB  . THR A 1 172 ? -1.508  0.357   27.775  1.00 140.31 ? 166 THR A CB  1 
ATOM   1059 O OG1 . THR A 1 172 ? -0.420  1.258   27.946  1.00 141.50 ? 166 THR A OG1 1 
ATOM   1060 C CG2 . THR A 1 172 ? -1.024  -0.947  27.167  1.00 139.29 ? 166 THR A CG2 1 
ATOM   1061 N N   . GLU A 1 173 ? -1.972  3.412   27.408  1.00 152.71 ? 167 GLU A N   1 
ATOM   1062 C CA  . GLU A 1 173 ? -2.353  4.763   27.903  1.00 158.15 ? 167 GLU A CA  1 
ATOM   1063 C C   . GLU A 1 173 ? -3.508  5.389   27.102  1.00 161.09 ? 167 GLU A C   1 
ATOM   1064 O O   . GLU A 1 173 ? -4.402  5.994   27.719  1.00 156.82 ? 167 GLU A O   1 
ATOM   1065 C CB  . GLU A 1 173 ? -1.113  5.657   27.951  1.00 160.50 ? 167 GLU A CB  1 
ATOM   1066 C CG  . GLU A 1 173 ? -0.509  5.987   26.590  1.00 163.31 ? 167 GLU A CG  1 
ATOM   1067 C CD  . GLU A 1 173 ? -0.673  7.414   26.095  1.00 164.26 ? 167 GLU A CD  1 
ATOM   1068 O OE1 . GLU A 1 173 ? -1.815  7.921   26.081  1.00 162.47 ? 167 GLU A OE1 1 
ATOM   1069 O OE2 . GLU A 1 173 ? 0.347   8.015   25.700  1.00 164.02 ? 167 GLU A OE2 1 
ATOM   1070 N N   . CYS A 1 174 ? -3.478  5.248   25.778  1.00 165.67 ? 168 CYS A N   1 
ATOM   1071 C CA  . CYS A 1 174 ? -4.458  5.953   24.903  1.00 168.65 ? 168 CYS A CA  1 
ATOM   1072 C C   . CYS A 1 174 ? -5.931  5.535   25.101  1.00 167.39 ? 168 CYS A C   1 
ATOM   1073 O O   . CYS A 1 174 ? -6.790  6.427   25.017  1.00 164.60 ? 168 CYS A O   1 
ATOM   1074 C CB  . CYS A 1 174 ? -3.934  5.909   23.474  1.00 171.05 ? 168 CYS A CB  1 
ATOM   1075 S SG  . CYS A 1 174 ? -2.300  6.682   23.369  1.00 176.01 ? 168 CYS A SG  1 
ATOM   1076 N N   . CYS A 1 175 ? -6.226  4.249   25.277  1.00 166.70 ? 169 CYS A N   1 
ATOM   1077 C CA  . CYS A 1 175 ? -7.653  3.846   25.376  1.00 168.56 ? 169 CYS A CA  1 
ATOM   1078 C C   . CYS A 1 175 ? -8.279  4.499   26.619  1.00 163.45 ? 169 CYS A C   1 
ATOM   1079 O O   . CYS A 1 175 ? -9.442  4.941   26.533  1.00 160.67 ? 169 CYS A O   1 
ATOM   1080 C CB  . CYS A 1 175 ? -7.770  2.329   25.436  1.00 174.78 ? 169 CYS A CB  1 
ATOM   1081 S SG  . CYS A 1 175 ? -9.083  1.752   26.546  1.00 184.83 ? 169 CYS A SG  1 
ATOM   1082 N N   . GLN A 1 176 ? -7.538  4.533   27.728  1.00 159.28 ? 170 GLN A N   1 
ATOM   1083 C CA  . GLN A 1 176 ? -8.000  5.211   28.968  1.00 155.03 ? 170 GLN A CA  1 
ATOM   1084 C C   . GLN A 1 176 ? -8.143  6.700   28.606  1.00 155.15 ? 170 GLN A C   1 
ATOM   1085 O O   . GLN A 1 176 ? -9.098  7.341   29.089  1.00 154.63 ? 170 GLN A O   1 
ATOM   1086 C CB  . GLN A 1 176 ? -7.113  4.811   30.151  1.00 150.63 ? 170 GLN A CB  1 
ATOM   1087 C CG  . GLN A 1 176 ? -5.996  5.795   30.479  1.00 149.66 ? 170 GLN A CG  1 
ATOM   1088 C CD  . GLN A 1 176 ? -4.772  5.124   31.062  1.00 146.40 ? 170 GLN A CD  1 
ATOM   1089 O OE1 . GLN A 1 176 ? -4.857  4.062   31.688  1.00 145.76 ? 170 GLN A OE1 1 
ATOM   1090 N NE2 . GLN A 1 176 ? -3.617  5.740   30.858  1.00 145.34 ? 170 GLN A NE2 1 
ATOM   1091 N N   . ALA A 1 177 ? -7.215  7.218   27.801  1.00 152.05 ? 171 ALA A N   1 
ATOM   1092 C CA  . ALA A 1 177 ? -7.243  8.636   27.379  1.00 147.40 ? 171 ALA A CA  1 
ATOM   1093 C C   . ALA A 1 177 ? -8.491  8.871   26.540  1.00 144.52 ? 171 ALA A C   1 
ATOM   1094 O O   . ALA A 1 177 ? -8.891  7.964   25.787  1.00 140.77 ? 171 ALA A O   1 
ATOM   1095 C CB  . ALA A 1 177 ? -5.999  8.947   26.596  1.00 147.17 ? 171 ALA A CB  1 
ATOM   1096 N N   . ALA A 1 178 ? -9.090  10.053  26.660  1.00 144.38 ? 172 ALA A N   1 
ATOM   1097 C CA  . ALA A 1 178 ? -10.389 10.285  25.989  1.00 146.35 ? 172 ALA A CA  1 
ATOM   1098 C C   . ALA A 1 178 ? -10.220 10.152  24.477  1.00 149.76 ? 172 ALA A C   1 
ATOM   1099 O O   . ALA A 1 178 ? -11.128 9.592   23.832  1.00 146.90 ? 172 ALA A O   1 
ATOM   1100 C CB  . ALA A 1 178 ? -10.934 11.631  26.392  1.00 143.55 ? 172 ALA A CB  1 
ATOM   1101 N N   . ASP A 1 179 ? -9.121  10.657  23.922  1.00 155.73 ? 173 ASP A N   1 
ATOM   1102 C CA  . ASP A 1 179 ? -8.864  10.439  22.475  1.00 158.68 ? 173 ASP A CA  1 
ATOM   1103 C C   . ASP A 1 179 ? -8.248  9.048   22.295  1.00 160.06 ? 173 ASP A C   1 
ATOM   1104 O O   . ASP A 1 179 ? -9.016  8.064   22.374  1.00 162.39 ? 173 ASP A O   1 
ATOM   1105 C CB  . ASP A 1 179 ? -8.013  11.559  21.909  1.00 158.34 ? 173 ASP A CB  1 
ATOM   1106 C CG  . ASP A 1 179 ? -8.054  12.857  22.699  1.00 158.86 ? 173 ASP A CG  1 
ATOM   1107 O OD1 . ASP A 1 179 ? -9.132  13.483  22.736  1.00 160.45 ? 173 ASP A OD1 1 
ATOM   1108 O OD2 . ASP A 1 179 ? -7.010  13.222  23.274  1.00 160.18 ? 173 ASP A OD2 1 
ATOM   1109 N N   . CYS A 1 183 ? -3.400  11.100  22.909  1.00 168.22 ? 177 CYS A N   1 
ATOM   1110 C CA  . CYS A 1 183 ? -2.750  11.416  21.613  1.00 171.10 ? 177 CYS A CA  1 
ATOM   1111 C C   . CYS A 1 183 ? -1.890  10.221  21.170  1.00 170.27 ? 177 CYS A C   1 
ATOM   1112 O O   . CYS A 1 183 ? -0.650  10.340  21.207  1.00 173.06 ? 177 CYS A O   1 
ATOM   1113 C CB  . CYS A 1 183 ? -1.907  12.675  21.735  1.00 172.63 ? 177 CYS A CB  1 
ATOM   1114 S SG  . CYS A 1 183 ? -0.880  12.697  23.225  1.00 169.74 ? 177 CYS A SG  1 
ATOM   1115 N N   . LEU A 1 184 ? -2.528  9.102   20.823  1.00 164.99 ? 178 LEU A N   1 
ATOM   1116 C CA  . LEU A 1 184 ? -1.800  7.892   20.368  1.00 159.92 ? 178 LEU A CA  1 
ATOM   1117 C C   . LEU A 1 184 ? -1.043  8.156   19.079  1.00 159.11 ? 178 LEU A C   1 
ATOM   1118 O O   . LEU A 1 184 ? 0.132   7.759   18.995  1.00 158.41 ? 178 LEU A O   1 
ATOM   1119 C CB  . LEU A 1 184 ? -2.850  6.817   20.111  1.00 157.91 ? 178 LEU A CB  1 
ATOM   1120 C CG  . LEU A 1 184 ? -2.336  5.497   19.532  1.00 155.58 ? 178 LEU A CG  1 
ATOM   1121 C CD1 . LEU A 1 184 ? -2.314  4.470   20.645  1.00 152.77 ? 178 LEU A CD1 1 
ATOM   1122 C CD2 . LEU A 1 184 ? -3.252  5.046   18.410  1.00 155.94 ? 178 LEU A CD2 1 
ATOM   1123 N N   . LEU A 1 185 ? -1.662  8.883   18.156  1.00 157.68 ? 179 LEU A N   1 
ATOM   1124 C CA  . LEU A 1 185 ? -1.048  9.017   16.815  1.00 154.77 ? 179 LEU A CA  1 
ATOM   1125 C C   . LEU A 1 185 ? 0.308   9.717   16.892  1.00 152.81 ? 179 LEU A C   1 
ATOM   1126 O O   . LEU A 1 185 ? 1.224   9.259   16.182  1.00 150.09 ? 179 LEU A O   1 
ATOM   1127 C CB  . LEU A 1 185 ? -2.041  9.809   15.969  1.00 151.78 ? 179 LEU A CB  1 
ATOM   1128 C CG  . LEU A 1 185 ? -3.415  9.157   15.792  1.00 148.44 ? 179 LEU A CG  1 
ATOM   1129 C CD1 . LEU A 1 185 ? -4.247  9.928   14.783  1.00 147.75 ? 179 LEU A CD1 1 
ATOM   1130 C CD2 . LEU A 1 185 ? -3.260  7.705   15.372  1.00 146.18 ? 179 LEU A CD2 1 
ATOM   1131 N N   . PRO A 1 186 ? 0.500   10.781  17.700  1.00 149.65 ? 180 PRO A N   1 
ATOM   1132 C CA  . PRO A 1 186 ? 1.822   11.364  17.817  1.00 144.59 ? 180 PRO A CA  1 
ATOM   1133 C C   . PRO A 1 186 ? 2.793   10.359  18.405  1.00 137.86 ? 180 PRO A C   1 
ATOM   1134 O O   . PRO A 1 186 ? 3.932   10.297  17.910  1.00 135.20 ? 180 PRO A O   1 
ATOM   1135 C CB  . PRO A 1 186 ? 1.580   12.537  18.771  1.00 146.20 ? 180 PRO A CB  1 
ATOM   1136 C CG  . PRO A 1 186 ? 0.129   12.890  18.581  1.00 145.83 ? 180 PRO A CG  1 
ATOM   1137 C CD  . PRO A 1 186 ? -0.530  11.543  18.388  1.00 149.29 ? 180 PRO A CD  1 
ATOM   1138 N N   . LYS A 1 187 ? 2.388   9.588   19.416  1.00 132.18 ? 181 LYS A N   1 
ATOM   1139 C CA  . LYS A 1 187 ? 3.393   8.629   19.926  1.00 129.61 ? 181 LYS A CA  1 
ATOM   1140 C C   . LYS A 1 187 ? 3.765   7.617   18.834  1.00 130.09 ? 181 LYS A C   1 
ATOM   1141 O O   . LYS A 1 187 ? 4.971   7.368   18.639  1.00 132.51 ? 181 LYS A O   1 
ATOM   1142 C CB  . LYS A 1 187 ? 2.811   7.874   21.122  1.00 125.83 ? 181 LYS A CB  1 
ATOM   1143 C CG  . LYS A 1 187 ? 3.836   7.205   22.030  1.00 123.65 ? 181 LYS A CG  1 
ATOM   1144 C CD  . LYS A 1 187 ? 4.127   7.985   23.306  1.00 121.40 ? 181 LYS A CD  1 
ATOM   1145 C CE  . LYS A 1 187 ? 5.545   7.856   23.764  1.00 119.70 ? 181 LYS A CE  1 
ATOM   1146 N NZ  . LYS A 1 187 ? 6.101   9.135   24.213  1.00 118.70 ? 181 LYS A NZ  1 
ATOM   1147 N N   . LEU A 1 188 ? 2.768   7.126   18.099  1.00 127.63 ? 182 LEU A N   1 
ATOM   1148 C CA  . LEU A 1 188 ? 3.043   6.150   17.018  1.00 126.97 ? 182 LEU A CA  1 
ATOM   1149 C C   . LEU A 1 188 ? 3.898   6.811   15.934  1.00 126.16 ? 182 LEU A C   1 
ATOM   1150 O O   . LEU A 1 188 ? 4.787   6.145   15.387  1.00 128.16 ? 182 LEU A O   1 
ATOM   1151 C CB  . LEU A 1 188 ? 1.768   5.542   16.441  1.00 129.07 ? 182 LEU A CB  1 
ATOM   1152 C CG  . LEU A 1 188 ? 0.921   4.705   17.404  1.00 131.77 ? 182 LEU A CG  1 
ATOM   1153 C CD1 . LEU A 1 188 ? 0.125   3.681   16.621  1.00 130.90 ? 182 LEU A CD1 1 
ATOM   1154 C CD2 . LEU A 1 188 ? 1.765   4.022   18.462  1.00 133.95 ? 182 LEU A CD2 1 
ATOM   1155 N N   . ASP A 1 189 ? 3.593   8.060   15.604  1.00 124.62 ? 183 ASP A N   1 
ATOM   1156 C CA  . ASP A 1 189 ? 4.359   8.686   14.505  1.00 124.83 ? 183 ASP A CA  1 
ATOM   1157 C C   . ASP A 1 189 ? 5.816   8.762   14.956  1.00 125.80 ? 183 ASP A C   1 
ATOM   1158 O O   . ASP A 1 189 ? 6.716   8.473   14.136  1.00 123.32 ? 183 ASP A O   1 
ATOM   1159 C CB  . ASP A 1 189 ? 3.819   10.060  14.152  1.00 124.92 ? 183 ASP A CB  1 
ATOM   1160 C CG  . ASP A 1 189 ? 2.479   10.108  13.432  1.00 124.29 ? 183 ASP A CG  1 
ATOM   1161 O OD1 . ASP A 1 189 ? 2.272   9.290   12.512  1.00 129.54 ? 183 ASP A OD1 1 
ATOM   1162 O OD2 . ASP A 1 189 ? 1.659   10.977  13.791  1.00 118.83 ? 183 ASP A OD2 1 
ATOM   1163 N N   . GLU A 1 190 ? 6.015   9.172   16.211  1.00 123.63 ? 184 GLU A N   1 
ATOM   1164 C CA  . GLU A 1 190 ? 7.377   9.286   16.776  1.00 121.54 ? 184 GLU A CA  1 
ATOM   1165 C C   . GLU A 1 190 ? 8.132   8.000   16.476  1.00 122.87 ? 184 GLU A C   1 
ATOM   1166 O O   . GLU A 1 190 ? 9.169   8.043   15.790  1.00 120.69 ? 184 GLU A O   1 
ATOM   1167 C CB  . GLU A 1 190 ? 7.199   9.439   18.282  1.00 118.91 ? 184 GLU A CB  1 
ATOM   1168 C CG  . GLU A 1 190 ? 8.434   9.093   19.109  1.00 117.57 ? 184 GLU A CG  1 
ATOM   1169 C CD  . GLU A 1 190 ? 8.160   9.021   20.601  1.00 116.11 ? 184 GLU A CD  1 
ATOM   1170 O OE1 . GLU A 1 190 ? 7.490   8.059   21.033  1.00 112.82 ? 184 GLU A OE1 1 
ATOM   1171 O OE2 . GLU A 1 190 ? 8.616   9.924   21.334  1.00 110.07 ? 184 GLU A OE2 1 
ATOM   1172 N N   . LEU A 1 191 ? 7.578   6.889   16.935  1.00 124.99 ? 185 LEU A N   1 
ATOM   1173 C CA  . LEU A 1 191 ? 8.317   5.620   16.788  1.00 126.68 ? 185 LEU A CA  1 
ATOM   1174 C C   . LEU A 1 191 ? 8.539   5.262   15.315  1.00 127.35 ? 185 LEU A C   1 
ATOM   1175 O O   . LEU A 1 191 ? 9.669   4.868   14.980  1.00 128.40 ? 185 LEU A O   1 
ATOM   1176 C CB  . LEU A 1 191 ? 7.426   4.600   17.488  1.00 125.28 ? 185 LEU A CB  1 
ATOM   1177 C CG  . LEU A 1 191 ? 7.013   4.941   18.923  1.00 124.77 ? 185 LEU A CG  1 
ATOM   1178 C CD1 . LEU A 1 191 ? 5.771   4.167   19.333  1.00 122.99 ? 185 LEU A CD1 1 
ATOM   1179 C CD2 . LEU A 1 191 ? 8.156   4.659   19.877  1.00 124.95 ? 185 LEU A CD2 1 
ATOM   1180 N N   . ARG A 1 192 ? 7.545   5.455   14.455  1.00 127.11 ? 186 ARG A N   1 
ATOM   1181 C CA  . ARG A 1 192 ? 7.703   4.989   13.053  1.00 129.02 ? 186 ARG A CA  1 
ATOM   1182 C C   . ARG A 1 192 ? 8.850   5.741   12.385  1.00 129.52 ? 186 ARG A C   1 
ATOM   1183 O O   . ARG A 1 192 ? 9.652   5.103   11.676  1.00 122.59 ? 186 ARG A O   1 
ATOM   1184 C CB  . ARG A 1 192 ? 6.404   5.228   12.280  1.00 129.63 ? 186 ARG A CB  1 
ATOM   1185 C CG  . ARG A 1 192 ? 6.508   5.020   10.778  1.00 129.25 ? 186 ARG A CG  1 
ATOM   1186 C CD  . ARG A 1 192 ? 6.362   6.327   10.024  1.00 129.36 ? 186 ARG A CD  1 
ATOM   1187 N NE  . ARG A 1 192 ? 5.527   7.306   10.726  1.00 127.35 ? 186 ARG A NE  1 
ATOM   1188 C CZ  . ARG A 1 192 ? 4.818   8.236   10.105  1.00 126.75 ? 186 ARG A CZ  1 
ATOM   1189 N NH1 . ARG A 1 192 ? 3.503   8.138   10.049  1.00 126.08 ? 186 ARG A NH1 1 
ATOM   1190 N NH2 . ARG A 1 192 ? 5.432   9.252   9.529   1.00 127.66 ? 186 ARG A NH2 1 
ATOM   1191 N N   . ASP A 1 193 ? 8.940   7.038   12.647  1.00 132.02 ? 187 ASP A N   1 
ATOM   1192 C CA  . ASP A 1 193 ? 9.956   7.872   11.951  1.00 135.71 ? 187 ASP A CA  1 
ATOM   1193 C C   . ASP A 1 193 ? 11.368  7.392   12.314  1.00 135.63 ? 187 ASP A C   1 
ATOM   1194 O O   . ASP A 1 193 ? 12.226  7.350   11.409  1.00 141.73 ? 187 ASP A O   1 
ATOM   1195 C CB  . ASP A 1 193 ? 9.669   9.351   12.166  1.00 135.75 ? 187 ASP A CB  1 
ATOM   1196 C CG  . ASP A 1 193 ? 8.674   9.952   11.186  1.00 133.02 ? 187 ASP A CG  1 
ATOM   1197 O OD1 . ASP A 1 193 ? 7.760   9.216   10.767  1.00 129.37 ? 187 ASP A OD1 1 
ATOM   1198 O OD2 . ASP A 1 193 ? 8.825   11.143  10.845  1.00 132.47 ? 187 ASP A OD2 1 
ATOM   1199 N N   . GLU A 1 194 ? 11.598  7.032   13.569  1.00 128.89 ? 188 GLU A N   1 
ATOM   1200 C CA  . GLU A 1 194 ? 12.952  6.643   14.039  1.00 124.02 ? 188 GLU A CA  1 
ATOM   1201 C C   . GLU A 1 194 ? 13.471  5.384   13.310  1.00 120.93 ? 188 GLU A C   1 
ATOM   1202 O O   . GLU A 1 194 ? 14.671  5.360   12.980  1.00 121.09 ? 188 GLU A O   1 
ATOM   1203 C CB  . GLU A 1 194 ? 12.823  6.530   15.558  1.00 120.83 ? 188 GLU A CB  1 
ATOM   1204 C CG  . GLU A 1 194 ? 12.419  7.843   16.219  1.00 117.38 ? 188 GLU A CG  1 
ATOM   1205 C CD  . GLU A 1 194 ? 11.706  7.636   17.541  1.00 118.11 ? 188 GLU A CD  1 
ATOM   1206 O OE1 . GLU A 1 194 ? 11.214  6.512   17.756  1.00 119.19 ? 188 GLU A OE1 1 
ATOM   1207 O OE2 . GLU A 1 194 ? 11.645  8.586   18.349  1.00 116.04 ? 188 GLU A OE2 1 
ATOM   1208 N N   . GLY A 1 195 ? 12.630  4.393   13.042  1.00 116.16 ? 189 GLY A N   1 
ATOM   1209 C CA  . GLY A 1 195 ? 13.068  3.088   12.507  1.00 115.70 ? 189 GLY A CA  1 
ATOM   1210 C C   . GLY A 1 195 ? 13.739  3.092   11.149  1.00 117.51 ? 189 GLY A C   1 
ATOM   1211 O O   . GLY A 1 195 ? 14.697  2.323   10.983  1.00 121.84 ? 189 GLY A O   1 
ATOM   1212 N N   . LYS A 1 196 ? 13.298  3.894   10.192  1.00 115.80 ? 190 LYS A N   1 
ATOM   1213 C CA  . LYS A 1 196 ? 13.798  3.790   8.791   1.00 113.19 ? 190 LYS A CA  1 
ATOM   1214 C C   . LYS A 1 196 ? 15.307  4.065   8.739   1.00 108.95 ? 190 LYS A C   1 
ATOM   1215 O O   . LYS A 1 196 ? 15.992  3.428   7.925   1.00 108.36 ? 190 LYS A O   1 
ATOM   1216 C CB  . LYS A 1 196 ? 12.950  4.713   7.912   1.00 112.85 ? 190 LYS A CB  1 
ATOM   1217 C CG  . LYS A 1 196 ? 11.460  4.413   7.967   1.00 111.07 ? 190 LYS A CG  1 
ATOM   1218 C CD  . LYS A 1 196 ? 10.703  5.375   8.871   1.00 109.16 ? 190 LYS A CD  1 
ATOM   1219 C CE  . LYS A 1 196 ? 9.321   5.627   8.375   1.00 109.74 ? 190 LYS A CE  1 
ATOM   1220 N NZ  . LYS A 1 196 ? 8.630   4.371   8.077   1.00 111.74 ? 190 LYS A NZ  1 
ATOM   1221 N N   . ALA A 1 197 ? 15.789  5.008   9.525   1.00 107.04 ? 191 ALA A N   1 
ATOM   1222 C CA  . ALA A 1 197 ? 17.214  5.401   9.533   1.00 107.09 ? 191 ALA A CA  1 
ATOM   1223 C C   . ALA A 1 197 ? 18.092  4.223   9.948   1.00 104.40 ? 191 ALA A C   1 
ATOM   1224 O O   . ALA A 1 197 ? 19.195  4.062   9.396   1.00 102.06 ? 191 ALA A O   1 
ATOM   1225 C CB  . ALA A 1 197 ? 17.368  6.546   10.488  1.00 108.92 ? 191 ALA A CB  1 
ATOM   1226 N N   . SER A 1 198 ? 17.640  3.423   10.901  1.00 102.51 ? 192 SER A N   1 
ATOM   1227 C CA  . SER A 1 198 ? 18.506  2.344   11.423  1.00 102.73 ? 192 SER A CA  1 
ATOM   1228 C C   . SER A 1 198 ? 18.857  1.366   10.295  1.00 105.78 ? 192 SER A C   1 
ATOM   1229 O O   . SER A 1 198 ? 19.997  0.887   10.269  1.00 107.61 ? 192 SER A O   1 
ATOM   1230 C CB  . SER A 1 198 ? 17.791  1.636   12.514  1.00 100.07 ? 192 SER A CB  1 
ATOM   1231 O OG  . SER A 1 198 ? 16.513  1.205   12.079  1.00 97.65  ? 192 SER A OG  1 
ATOM   1232 N N   . SER A 1 199 ? 17.911  1.041   9.424   1.00 108.65 ? 193 SER A N   1 
ATOM   1233 C CA  . SER A 1 199 ? 18.171  0.060   8.340   1.00 109.32 ? 193 SER A CA  1 
ATOM   1234 C C   . SER A 1 199 ? 19.274  0.580   7.416   1.00 109.09 ? 193 SER A C   1 
ATOM   1235 O O   . SER A 1 199 ? 19.943  -0.244  6.768   1.00 105.36 ? 193 SER A O   1 
ATOM   1236 C CB  . SER A 1 199 ? 16.917  -0.220  7.561   1.00 109.05 ? 193 SER A CB  1 
ATOM   1237 O OG  . SER A 1 199 ? 16.731  -1.618  7.394   1.00 108.96 ? 193 SER A OG  1 
ATOM   1238 N N   . ALA A 1 200 ? 19.453  1.896   7.363   1.00 111.36 ? 194 ALA A N   1 
ATOM   1239 C CA  . ALA A 1 200 ? 20.424  2.484   6.455   1.00 109.67 ? 194 ALA A CA  1 
ATOM   1240 C C   . ALA A 1 200 ? 21.822  2.496   7.067   1.00 108.10 ? 194 ALA A C   1 
ATOM   1241 O O   . ALA A 1 200 ? 22.807  2.326   6.353   1.00 108.45 ? 194 ALA A O   1 
ATOM   1242 C CB  . ALA A 1 200 ? 19.992  3.891   6.088   1.00 107.82 ? 194 ALA A CB  1 
ATOM   1243 N N   . LYS A 1 201 ? 21.894  2.702   8.391   1.00 107.68 ? 195 LYS A N   1 
ATOM   1244 C CA  . LYS A 1 201 ? 23.156  2.679   9.116   1.00 108.14 ? 195 LYS A CA  1 
ATOM   1245 C C   . LYS A 1 201 ? 23.739  1.269   9.195   1.00 105.49 ? 195 LYS A C   1 
ATOM   1246 O O   . LYS A 1 201 ? 24.956  1.099   9.192   1.00 102.28 ? 195 LYS A O   1 
ATOM   1247 C CB  . LYS A 1 201 ? 22.978  3.258   10.541  1.00 108.79 ? 195 LYS A CB  1 
ATOM   1248 C CG  . LYS A 1 201 ? 22.148  2.395   11.504  1.00 112.74 ? 195 LYS A CG  1 
ATOM   1249 C CD  . LYS A 1 201 ? 22.957  1.338   12.305  1.00 114.56 ? 195 LYS A CD  1 
ATOM   1250 C CE  . LYS A 1 201 ? 22.078  0.408   13.120  1.00 115.00 ? 195 LYS A CE  1 
ATOM   1251 N NZ  . LYS A 1 201 ? 22.879  -0.614  13.851  1.00 115.23 ? 195 LYS A NZ  1 
ATOM   1252 N N   . GLN A 1 202 ? 22.852  0.269   9.291   1.00 102.77 ? 196 GLN A N   1 
ATOM   1253 C CA  . GLN A 1 202 ? 23.251  -1.113  9.492   1.00 101.61 ? 196 GLN A CA  1 
ATOM   1254 C C   . GLN A 1 202 ? 23.881  -1.656  8.213   1.00 101.22 ? 196 GLN A C   1 
ATOM   1255 O O   . GLN A 1 202 ? 24.940  -2.285  8.256   1.00 103.53 ? 196 GLN A O   1 
ATOM   1256 C CB  . GLN A 1 202 ? 22.040  -1.953  9.925   1.00 101.40 ? 196 GLN A CB  1 
ATOM   1257 C CG  . GLN A 1 202 ? 22.344  -3.427  10.225  1.00 102.93 ? 196 GLN A CG  1 
ATOM   1258 C CD  . GLN A 1 202 ? 23.332  -3.624  11.352  1.00 102.05 ? 196 GLN A CD  1 
ATOM   1259 O OE1 . GLN A 1 202 ? 23.237  -2.990  12.413  1.00 100.76 ? 196 GLN A OE1 1 
ATOM   1260 N NE2 . GLN A 1 202 ? 24.312  -4.507  11.145  1.00 100.70 ? 196 GLN A NE2 1 
ATOM   1261 N N   . ARG A 1 203 ? 23.210  -1.398  7.084   1.00 94.20  ? 197 ARG A N   1 
ATOM   1262 C CA  . ARG A 1 203 ? 23.765  -1.648  5.764   1.00 94.23  ? 197 ARG A CA  1 
ATOM   1263 C C   . ARG A 1 203 ? 25.205  -1.148  5.656   1.00 90.52  ? 197 ARG A C   1 
ATOM   1264 O O   . ARG A 1 203 ? 26.072  -1.820  5.098   1.00 83.67  ? 197 ARG A O   1 
ATOM   1265 C CB  . ARG A 1 203 ? 22.881  -0.942  4.726   1.00 97.76  ? 197 ARG A CB  1 
ATOM   1266 C CG  . ARG A 1 203 ? 23.345  -1.069  3.280   1.00 98.17  ? 197 ARG A CG  1 
ATOM   1267 C CD  . ARG A 1 203 ? 23.374  -2.503  2.825   1.00 98.57  ? 197 ARG A CD  1 
ATOM   1268 N NE  . ARG A 1 203 ? 23.135  -2.618  1.393   1.00 102.23 ? 197 ARG A NE  1 
ATOM   1269 C CZ  . ARG A 1 203 ? 21.972  -2.366  0.803   1.00 105.22 ? 197 ARG A CZ  1 
ATOM   1270 N NH1 . ARG A 1 203 ? 20.981  -1.775  1.452   1.00 107.17 ? 197 ARG A NH1 1 
ATOM   1271 N NH2 . ARG A 1 203 ? 21.799  -2.715  -0.471  1.00 102.26 ? 197 ARG A NH2 1 
ATOM   1272 N N   . LEU A 1 204 ? 25.428  0.057   6.192   1.00 89.85  ? 198 LEU A N   1 
ATOM   1273 C CA  . LEU A 1 204 ? 26.741  0.676   6.249   1.00 88.55  ? 198 LEU A CA  1 
ATOM   1274 C C   . LEU A 1 204 ? 27.702  -0.210  7.040   1.00 84.02  ? 198 LEU A C   1 
ATOM   1275 O O   . LEU A 1 204 ? 28.706  -0.676  6.506   1.00 76.99  ? 198 LEU A O   1 
ATOM   1276 C CB  . LEU A 1 204 ? 26.596  2.087   6.887   1.00 86.55  ? 198 LEU A CB  1 
ATOM   1277 C CG  . LEU A 1 204 ? 27.763  3.043   6.741   1.00 85.00  ? 198 LEU A CG  1 
ATOM   1278 C CD1 . LEU A 1 204 ? 27.958  3.446   5.324   1.00 83.59  ? 198 LEU A CD1 1 
ATOM   1279 C CD2 . LEU A 1 204 ? 27.554  4.285   7.587   1.00 83.85  ? 198 LEU A CD2 1 
ATOM   1280 N N   . LYS A 1 205 ? 27.347  -0.472  8.302   1.00 87.70  ? 199 LYS A N   1 
ATOM   1281 C CA  . LYS A 1 205 ? 28.198  -1.219  9.216   1.00 91.01  ? 199 LYS A CA  1 
ATOM   1282 C C   . LYS A 1 205 ? 28.650  -2.547  8.612   1.00 91.66  ? 199 LYS A C   1 
ATOM   1283 O O   . LYS A 1 205 ? 29.826  -2.900  8.700   1.00 89.06  ? 199 LYS A O   1 
ATOM   1284 C CB  . LYS A 1 205 ? 27.461  -1.454  10.538  1.00 90.53  ? 199 LYS A CB  1 
ATOM   1285 C CG  . LYS A 1 205 ? 27.180  -0.161  11.301  1.00 93.41  ? 199 LYS A CG  1 
ATOM   1286 C CD  . LYS A 1 205 ? 26.063  -0.305  12.325  1.00 94.34  ? 199 LYS A CD  1 
ATOM   1287 C CE  . LYS A 1 205 ? 26.448  -1.161  13.501  1.00 94.24  ? 199 LYS A CE  1 
ATOM   1288 N NZ  . LYS A 1 205 ? 27.448  -0.486  14.366  1.00 94.74  ? 199 LYS A NZ  1 
ATOM   1289 N N   . CYS A 1 206 ? 27.702  -3.266  8.017   1.00 89.45  ? 200 CYS A N   1 
ATOM   1290 C CA  . CYS A 1 206 ? 28.025  -4.622  7.521   1.00 88.37  ? 200 CYS A CA  1 
ATOM   1291 C C   . CYS A 1 206 ? 28.912  -4.507  6.288   1.00 87.79  ? 200 CYS A C   1 
ATOM   1292 O O   . CYS A 1 206 ? 29.854  -5.296  6.156   1.00 87.92  ? 200 CYS A O   1 
ATOM   1293 C CB  . CYS A 1 206 ? 26.754  -5.382  7.182   1.00 90.47  ? 200 CYS A CB  1 
ATOM   1294 S SG  . CYS A 1 206 ? 25.514  -5.387  8.498   1.00 97.83  ? 200 CYS A SG  1 
ATOM   1295 N N   . ALA A 1 207 ? 28.573  -3.585  5.402   1.00 88.72  ? 201 ALA A N   1 
ATOM   1296 C CA  . ALA A 1 207 ? 29.356  -3.461  4.161   1.00 93.01  ? 201 ALA A CA  1 
ATOM   1297 C C   . ALA A 1 207 ? 30.778  -3.066  4.532   1.00 97.02  ? 201 ALA A C   1 
ATOM   1298 O O   . ALA A 1 207 ? 31.747  -3.577  3.949   1.00 97.08  ? 201 ALA A O   1 
ATOM   1299 C CB  . ALA A 1 207 ? 28.733  -2.446  3.262   1.00 93.95  ? 201 ALA A CB  1 
ATOM   1300 N N   . SER A 1 208 ? 30.886  -2.168  5.506   1.00 97.30  ? 202 SER A N   1 
ATOM   1301 C CA  . SER A 1 208 ? 32.235  -1.728  5.907   1.00 94.41  ? 202 SER A CA  1 
ATOM   1302 C C   . SER A 1 208 ? 32.995  -2.937  6.451   1.00 91.20  ? 202 SER A C   1 
ATOM   1303 O O   . SER A 1 208 ? 34.167  -3.090  6.095   1.00 87.76  ? 202 SER A O   1 
ATOM   1304 C CB  . SER A 1 208 ? 32.119  -0.665  6.933   1.00 94.52  ? 202 SER A CB  1 
ATOM   1305 O OG  . SER A 1 208 ? 30.981  0.146   6.688   1.00 96.26  ? 202 SER A OG  1 
ATOM   1306 N N   . LEU A 1 209 ? 32.331  -3.781  7.245   1.00 90.62  ? 203 LEU A N   1 
ATOM   1307 C CA  . LEU A 1 209 ? 33.002  -5.007  7.726   1.00 87.53  ? 203 LEU A CA  1 
ATOM   1308 C C   . LEU A 1 209 ? 33.360  -5.933  6.572   1.00 90.42  ? 203 LEU A C   1 
ATOM   1309 O O   . LEU A 1 209 ? 34.403  -6.587  6.659   1.00 91.57  ? 203 LEU A O   1 
ATOM   1310 C CB  . LEU A 1 209 ? 32.011  -5.710  8.645   1.00 85.89  ? 203 LEU A CB  1 
ATOM   1311 C CG  . LEU A 1 209 ? 32.570  -6.396  9.893   1.00 82.98  ? 203 LEU A CG  1 
ATOM   1312 C CD1 . LEU A 1 209 ? 31.414  -6.650  10.839  1.00 80.60  ? 203 LEU A CD1 1 
ATOM   1313 C CD2 . LEU A 1 209 ? 33.246  -7.701  9.529   1.00 84.57  ? 203 LEU A CD2 1 
ATOM   1314 N N   . GLN A 1 210 ? 32.469  -6.129  5.603   1.00 94.96  ? 204 GLN A N   1 
ATOM   1315 C CA  . GLN A 1 210 ? 32.917  -6.941  4.448   1.00 94.98  ? 204 GLN A CA  1 
ATOM   1316 C C   . GLN A 1 210 ? 34.023  -6.224  3.690   1.00 92.55  ? 204 GLN A C   1 
ATOM   1317 O O   . GLN A 1 210 ? 35.021  -6.864  3.333   1.00 93.21  ? 204 GLN A O   1 
ATOM   1318 C CB  . GLN A 1 210 ? 31.769  -7.231  3.488   1.00 99.89  ? 204 GLN A CB  1 
ATOM   1319 C CG  . GLN A 1 210 ? 32.204  -7.842  2.161   1.00 102.16 ? 204 GLN A CG  1 
ATOM   1320 C CD  . GLN A 1 210 ? 32.708  -9.261  2.299   1.00 102.56 ? 204 GLN A CD  1 
ATOM   1321 O OE1 . GLN A 1 210 ? 31.981  -10.164 2.726   1.00 102.54 ? 204 GLN A OE1 1 
ATOM   1322 N NE2 . GLN A 1 210 ? 33.966  -9.470  1.939   1.00 103.39 ? 204 GLN A NE2 1 
ATOM   1323 N N   . LYS A 1 211 ? 33.841  -4.919  3.497   1.00 93.49  ? 205 LYS A N   1 
ATOM   1324 C CA  . LYS A 1 211 ? 34.812  -4.168  2.662   1.00 94.81  ? 205 LYS A CA  1 
ATOM   1325 C C   . LYS A 1 211 ? 36.178  -4.177  3.329   1.00 93.17  ? 205 LYS A C   1 
ATOM   1326 O O   . LYS A 1 211 ? 37.183  -4.459  2.656   1.00 84.69  ? 205 LYS A O   1 
ATOM   1327 C CB  . LYS A 1 211 ? 34.305  -2.743  2.449   1.00 94.87  ? 205 LYS A CB  1 
ATOM   1328 C CG  . LYS A 1 211 ? 33.962  -2.422  1.006   1.00 96.05  ? 205 LYS A CG  1 
ATOM   1329 C CD  . LYS A 1 211 ? 33.133  -3.518  0.349   1.00 96.65  ? 205 LYS A CD  1 
ATOM   1330 C CE  . LYS A 1 211 ? 33.601  -3.847  -1.032  1.00 98.06  ? 205 LYS A CE  1 
ATOM   1331 N NZ  . LYS A 1 211 ? 32.496  -3.850  -1.993  1.00 97.62  ? 205 LYS A NZ  1 
ATOM   1332 N N   . PHE A 1 212 ? 36.161  -4.001  4.640   1.00 94.53  ? 206 PHE A N   1 
ATOM   1333 C CA  . PHE A 1 212 ? 37.421  -3.860  5.395   1.00 93.01  ? 206 PHE A CA  1 
ATOM   1334 C C   . PHE A 1 212 ? 37.318  -4.782  6.558   1.00 91.38  ? 206 PHE A C   1 
ATOM   1335 O O   . PHE A 1 212 ? 36.219  -4.937  7.072   1.00 92.71  ? 206 PHE A O   1 
ATOM   1336 C CB  . PHE A 1 212 ? 37.622  -2.427  5.882   1.00 92.63  ? 206 PHE A CB  1 
ATOM   1337 C CG  . PHE A 1 212 ? 36.970  -1.333  5.051   1.00 97.10  ? 206 PHE A CG  1 
ATOM   1338 C CD1 . PHE A 1 212 ? 37.434  -1.030  3.777   1.00 97.03  ? 206 PHE A CD1 1 
ATOM   1339 C CD2 . PHE A 1 212 ? 35.906  -0.596  5.556   1.00 100.63 ? 206 PHE A CD2 1 
ATOM   1340 C CE1 . PHE A 1 212 ? 36.838  -0.030  3.028   1.00 99.16  ? 206 PHE A CE1 1 
ATOM   1341 C CE2 . PHE A 1 212 ? 35.314  0.403   4.802   1.00 100.38 ? 206 PHE A CE2 1 
ATOM   1342 C CZ  . PHE A 1 212 ? 35.782  0.684   3.542   1.00 100.46 ? 206 PHE A CZ  1 
ATOM   1343 N N   . GLY A 1 213 ? 38.428  -5.223  7.089   1.00 85.95  ? 207 GLY A N   1 
ATOM   1344 C CA  . GLY A 1 213 ? 38.508  -6.243  8.142   1.00 80.37  ? 207 GLY A CA  1 
ATOM   1345 C C   . GLY A 1 213 ? 38.068  -5.750  9.492   1.00 75.13  ? 207 GLY A C   1 
ATOM   1346 O O   . GLY A 1 213 ? 37.787  -4.551  9.624   1.00 74.77  ? 207 GLY A O   1 
ATOM   1347 N N   . GLU A 1 214 ? 37.887  -6.693  10.416  1.00 72.63  ? 208 GLU A N   1 
ATOM   1348 C CA  . GLU A 1 214 ? 37.465  -6.381  11.796  1.00 70.56  ? 208 GLU A CA  1 
ATOM   1349 C C   . GLU A 1 214 ? 38.437  -5.410  12.448  1.00 66.22  ? 208 GLU A C   1 
ATOM   1350 O O   . GLU A 1 214 ? 38.003  -4.663  13.327  1.00 68.67  ? 208 GLU A O   1 
ATOM   1351 C CB  . GLU A 1 214 ? 37.477  -7.671  12.604  1.00 74.87  ? 208 GLU A CB  1 
ATOM   1352 C CG  . GLU A 1 214 ? 38.787  -8.448  12.513  1.00 82.76  ? 208 GLU A CG  1 
ATOM   1353 C CD  . GLU A 1 214 ? 39.303  -9.013  13.827  1.00 86.89  ? 208 GLU A CD  1 
ATOM   1354 O OE1 . GLU A 1 214 ? 38.587  -9.830  14.444  1.00 84.61  ? 208 GLU A OE1 1 
ATOM   1355 O OE2 . GLU A 1 214 ? 40.427  -8.643  14.230  1.00 87.47  ? 208 GLU A OE2 1 
ATOM   1356 N N   . ARG A 1 215 ? 39.697  -5.445  12.033  1.00 61.10  ? 209 ARG A N   1 
ATOM   1357 C CA  . ARG A 1 215 ? 40.700  -4.530  12.614  1.00 57.81  ? 209 ARG A CA  1 
ATOM   1358 C C   . ARG A 1 215 ? 40.154  -3.121  12.440  1.00 59.17  ? 209 ARG A C   1 
ATOM   1359 O O   . ARG A 1 215 ? 40.223  -2.331  13.385  1.00 59.36  ? 209 ARG A O   1 
ATOM   1360 C CB  . ARG A 1 215 ? 42.067  -4.689  11.948  1.00 56.26  ? 209 ARG A CB  1 
ATOM   1361 C CG  . ARG A 1 215 ? 43.177  -3.914  12.638  1.00 55.43  ? 209 ARG A CG  1 
ATOM   1362 C CD  . ARG A 1 215 ? 44.499  -4.173  11.958  1.00 55.06  ? 209 ARG A CD  1 
ATOM   1363 N NE  . ARG A 1 215 ? 45.496  -3.183  12.366  1.00 54.42  ? 209 ARG A NE  1 
ATOM   1364 C CZ  . ARG A 1 215 ? 45.696  -2.036  11.747  1.00 51.70  ? 209 ARG A CZ  1 
ATOM   1365 N NH1 . ARG A 1 215 ? 44.831  -1.611  10.848  1.00 51.28  ? 209 ARG A NH1 1 
ATOM   1366 N NH2 . ARG A 1 215 ? 46.765  -1.319  12.027  1.00 51.54  ? 209 ARG A NH2 1 
ATOM   1367 N N   . ALA A 1 216 ? 39.596  -2.861  11.266  1.00 61.08  ? 210 ALA A N   1 
ATOM   1368 C CA  . ALA A 1 216 ? 39.040  -1.545  11.009  1.00 62.26  ? 210 ALA A CA  1 
ATOM   1369 C C   . ALA A 1 216 ? 37.777  -1.278  11.828  1.00 60.93  ? 210 ALA A C   1 
ATOM   1370 O O   . ALA A 1 216 ? 37.543  -0.150  12.249  1.00 59.19  ? 210 ALA A O   1 
ATOM   1371 C CB  . ALA A 1 216 ? 38.758  -1.409  9.524   1.00 62.91  ? 210 ALA A CB  1 
ATOM   1372 N N   . PHE A 1 217 ? 36.972  -2.322  12.060  1.00 63.33  ? 211 PHE A N   1 
ATOM   1373 C CA  . PHE A 1 217 ? 35.742  -2.194  12.828  1.00 69.00  ? 211 PHE A CA  1 
ATOM   1374 C C   . PHE A 1 217 ? 35.987  -2.050  14.331  1.00 66.51  ? 211 PHE A C   1 
ATOM   1375 O O   . PHE A 1 217 ? 35.316  -1.260  15.000  1.00 62.77  ? 211 PHE A O   1 
ATOM   1376 C CB  . PHE A 1 217 ? 34.810  -3.401  12.562  1.00 75.52  ? 211 PHE A CB  1 
ATOM   1377 C CG  . PHE A 1 217 ? 33.437  -3.239  13.178  1.00 82.20  ? 211 PHE A CG  1 
ATOM   1378 C CD1 . PHE A 1 217 ? 33.235  -3.461  14.533  1.00 88.02  ? 211 PHE A CD1 1 
ATOM   1379 C CD2 . PHE A 1 217 ? 32.363  -2.820  12.413  1.00 84.75  ? 211 PHE A CD2 1 
ATOM   1380 C CE1 . PHE A 1 217 ? 31.975  -3.293  15.101  1.00 92.35  ? 211 PHE A CE1 1 
ATOM   1381 C CE2 . PHE A 1 217 ? 31.106  -2.649  12.984  1.00 90.55  ? 211 PHE A CE2 1 
ATOM   1382 C CZ  . PHE A 1 217 ? 30.918  -2.886  14.324  1.00 93.21  ? 211 PHE A CZ  1 
ATOM   1383 N N   . LYS A 1 218 ? 36.928  -2.848  14.855  1.00 65.27  ? 212 LYS A N   1 
ATOM   1384 C CA  . LYS A 1 218 ? 37.376  -2.702  16.232  1.00 63.55  ? 212 LYS A CA  1 
ATOM   1385 C C   . LYS A 1 218 ? 37.921  -1.298  16.479  1.00 58.49  ? 212 LYS A C   1 
ATOM   1386 O O   . LYS A 1 218 ? 37.639  -0.701  17.513  1.00 61.04  ? 212 LYS A O   1 
ATOM   1387 C CB  . LYS A 1 218 ? 38.473  -3.708  16.592  1.00 67.45  ? 212 LYS A CB  1 
ATOM   1388 C CG  . LYS A 1 218 ? 38.070  -5.181  16.595  1.00 71.64  ? 212 LYS A CG  1 
ATOM   1389 C CD  . LYS A 1 218 ? 39.005  -5.996  17.522  1.00 75.43  ? 212 LYS A CD  1 
ATOM   1390 C CE  . LYS A 1 218 ? 38.940  -7.493  17.327  1.00 78.21  ? 212 LYS A CE  1 
ATOM   1391 N NZ  . LYS A 1 218 ? 37.618  -8.063  17.727  1.00 78.66  ? 212 LYS A NZ  1 
ATOM   1392 N N   . ALA A 1 219 ? 38.723  -0.791  15.537  1.00 55.08  ? 213 ALA A N   1 
ATOM   1393 C CA  . ALA A 1 219 ? 39.344  0.513   15.690  1.00 53.96  ? 213 ALA A CA  1 
ATOM   1394 C C   . ALA A 1 219 ? 38.263  1.584   15.726  1.00 54.98  ? 213 ALA A C   1 
ATOM   1395 O O   . ALA A 1 219 ? 38.338  2.504   16.538  1.00 52.67  ? 213 ALA A O   1 
ATOM   1396 C CB  . ALA A 1 219 ? 40.327  0.795   14.564  1.00 53.88  ? 213 ALA A CB  1 
ATOM   1397 N N   . TRP A 1 220 ? 37.266  1.450   14.837  1.00 55.41  ? 214 TRP A N   1 
ATOM   1398 C CA  . TRP A 1 220 ? 36.130  2.355   14.835  1.00 56.57  ? 214 TRP A CA  1 
ATOM   1399 C C   . TRP A 1 220 ? 35.480  2.345   16.215  1.00 55.34  ? 214 TRP A C   1 
ATOM   1400 O O   . TRP A 1 220 ? 35.294  3.391   16.830  1.00 52.47  ? 214 TRP A O   1 
ATOM   1401 C CB  . TRP A 1 220 ? 35.096  1.983   13.757  1.00 60.44  ? 214 TRP A CB  1 
ATOM   1402 C CG  . TRP A 1 220 ? 34.047  3.040   13.594  1.00 63.02  ? 214 TRP A CG  1 
ATOM   1403 C CD1 . TRP A 1 220 ? 34.082  4.092   12.727  1.00 66.12  ? 214 TRP A CD1 1 
ATOM   1404 C CD2 . TRP A 1 220 ? 32.816  3.154   14.314  1.00 67.68  ? 214 TRP A CD2 1 
ATOM   1405 N NE1 . TRP A 1 220 ? 32.963  4.870   12.880  1.00 68.48  ? 214 TRP A NE1 1 
ATOM   1406 C CE2 . TRP A 1 220 ? 32.163  4.317   13.847  1.00 70.11  ? 214 TRP A CE2 1 
ATOM   1407 C CE3 . TRP A 1 220 ? 32.195  2.388   15.315  1.00 69.62  ? 214 TRP A CE3 1 
ATOM   1408 C CZ2 . TRP A 1 220 ? 30.921  4.730   14.342  1.00 70.59  ? 214 TRP A CZ2 1 
ATOM   1409 C CZ3 . TRP A 1 220 ? 30.965  2.797   15.805  1.00 70.07  ? 214 TRP A CZ3 1 
ATOM   1410 C CH2 . TRP A 1 220 ? 30.340  3.953   15.321  1.00 70.82  ? 214 TRP A CH2 1 
ATOM   1411 N N   . ALA A 1 221 ? 35.161  1.136   16.690  1.00 55.21  ? 215 ALA A N   1 
ATOM   1412 C CA  . ALA A 1 221 ? 34.543  0.943   17.991  1.00 55.41  ? 215 ALA A CA  1 
ATOM   1413 C C   . ALA A 1 221 ? 35.374  1.545   19.124  1.00 55.36  ? 215 ALA A C   1 
ATOM   1414 O O   . ALA A 1 221 ? 34.851  2.314   19.924  1.00 58.38  ? 215 ALA A O   1 
ATOM   1415 C CB  . ALA A 1 221 ? 34.297  -0.538  18.233  1.00 55.75  ? 215 ALA A CB  1 
ATOM   1416 N N   . VAL A 1 222 ? 36.672  1.229   19.174  1.00 51.87  ? 216 VAL A N   1 
ATOM   1417 C CA  . VAL A 1 222 ? 37.532  1.821   20.187  1.00 51.92  ? 216 VAL A CA  1 
ATOM   1418 C C   . VAL A 1 222 ? 37.383  3.339   20.209  1.00 52.56  ? 216 VAL A C   1 
ATOM   1419 O O   . VAL A 1 222 ? 37.273  3.930   21.278  1.00 54.93  ? 216 VAL A O   1 
ATOM   1420 C CB  . VAL A 1 222 ? 39.017  1.408   20.028  1.00 50.94  ? 216 VAL A CB  1 
ATOM   1421 C CG1 . VAL A 1 222 ? 39.956  2.414   20.679  1.00 51.40  ? 216 VAL A CG1 1 
ATOM   1422 C CG2 . VAL A 1 222 ? 39.263  0.016   20.585  1.00 50.05  ? 216 VAL A CG2 1 
ATOM   1423 N N   . ALA A 1 223 ? 37.396  3.966   19.032  1.00 54.11  ? 217 ALA A N   1 
ATOM   1424 C CA  . ALA A 1 223 ? 37.277  5.413   18.950  1.00 57.05  ? 217 ALA A CA  1 
ATOM   1425 C C   . ALA A 1 223 ? 35.987  5.930   19.585  1.00 59.23  ? 217 ALA A C   1 
ATOM   1426 O O   . ALA A 1 223 ? 36.009  6.939   20.288  1.00 56.20  ? 217 ALA A O   1 
ATOM   1427 C CB  . ALA A 1 223 ? 37.363  5.882   17.508  1.00 57.22  ? 217 ALA A CB  1 
ATOM   1428 N N   . ARG A 1 224 ? 34.872  5.236   19.335  1.00 61.37  ? 218 ARG A N   1 
ATOM   1429 C CA  . ARG A 1 224 ? 33.564  5.714   19.759  1.00 64.62  ? 218 ARG A CA  1 
ATOM   1430 C C   . ARG A 1 224 ? 33.344  5.521   21.261  1.00 60.97  ? 218 ARG A C   1 
ATOM   1431 O O   . ARG A 1 224 ? 33.001  6.465   21.972  1.00 61.72  ? 218 ARG A O   1 
ATOM   1432 C CB  . ARG A 1 224 ? 32.461  5.004   18.937  1.00 69.01  ? 218 ARG A CB  1 
ATOM   1433 C CG  . ARG A 1 224 ? 31.039  5.457   19.241  1.00 70.77  ? 218 ARG A CG  1 
ATOM   1434 C CD  . ARG A 1 224 ? 30.863  6.941   19.040  1.00 72.52  ? 218 ARG A CD  1 
ATOM   1435 N NE  . ARG A 1 224 ? 29.582  7.398   19.564  1.00 76.71  ? 218 ARG A NE  1 
ATOM   1436 C CZ  . ARG A 1 224 ? 29.441  8.322   20.503  1.00 76.52  ? 218 ARG A CZ  1 
ATOM   1437 N NH1 . ARG A 1 224 ? 30.404  8.579   21.369  1.00 78.75  ? 218 ARG A NH1 1 
ATOM   1438 N NH2 . ARG A 1 224 ? 28.296  8.994   20.585  1.00 76.41  ? 218 ARG A NH2 1 
ATOM   1439 N N   . LEU A 1 225 ? 33.574  4.302   21.751  1.00 55.56  ? 219 LEU A N   1 
ATOM   1440 C CA  . LEU A 1 225 ? 33.455  4.031   23.174  1.00 55.13  ? 219 LEU A CA  1 
ATOM   1441 C C   . LEU A 1 225 ? 34.399  4.850   24.064  1.00 54.82  ? 219 LEU A C   1 
ATOM   1442 O O   . LEU A 1 225 ? 34.078  5.121   25.213  1.00 56.64  ? 219 LEU A O   1 
ATOM   1443 C CB  . LEU A 1 225 ? 33.643  2.533   23.409  1.00 54.17  ? 219 LEU A CB  1 
ATOM   1444 C CG  . LEU A 1 225 ? 32.622  1.647   22.691  1.00 57.36  ? 219 LEU A CG  1 
ATOM   1445 C CD1 . LEU A 1 225 ? 32.756  0.212   23.073  1.00 58.94  ? 219 LEU A CD1 1 
ATOM   1446 C CD2 . LEU A 1 225 ? 31.211  2.088   22.981  1.00 60.87  ? 219 LEU A CD2 1 
ATOM   1447 N N   . SER A 1 226 ? 35.554  5.276   23.549  1.00 53.83  ? 220 SER A N   1 
ATOM   1448 C CA  . SER A 1 226 ? 36.449  6.117   24.330  1.00 53.29  ? 220 SER A CA  1 
ATOM   1449 C C   . SER A 1 226 ? 35.834  7.497   24.518  1.00 56.18  ? 220 SER A C   1 
ATOM   1450 O O   . SER A 1 226 ? 35.926  8.074   25.600  1.00 58.94  ? 220 SER A O   1 
ATOM   1451 C CB  . SER A 1 226 ? 37.825  6.244   23.676  1.00 51.05  ? 220 SER A CB  1 
ATOM   1452 O OG  . SER A 1 226 ? 38.463  4.982   23.609  1.00 50.02  ? 220 SER A OG  1 
ATOM   1453 N N   . GLN A 1 227 ? 35.227  8.010   23.438  1.00 57.78  ? 221 GLN A N   1 
ATOM   1454 C CA  . GLN A 1 227 ? 34.464  9.247   23.465  1.00 57.26  ? 221 GLN A CA  1 
ATOM   1455 C C   . GLN A 1 227 ? 33.329  9.152   24.479  1.00 56.62  ? 221 GLN A C   1 
ATOM   1456 O O   . GLN A 1 227 ? 33.138  10.069  25.282  1.00 52.00  ? 221 GLN A O   1 
ATOM   1457 C CB  . GLN A 1 227 ? 33.862  9.555   22.090  1.00 57.35  ? 221 GLN A CB  1 
ATOM   1458 C CG  . GLN A 1 227 ? 34.910  9.873   21.024  1.00 57.99  ? 221 GLN A CG  1 
ATOM   1459 C CD  . GLN A 1 227 ? 34.279  10.214  19.711  1.00 53.56  ? 221 GLN A CD  1 
ATOM   1460 O OE1 . GLN A 1 227 ? 33.550  9.412   19.120  1.00 51.10  ? 221 GLN A OE1 1 
ATOM   1461 N NE2 . GLN A 1 227 ? 34.542  11.421  19.247  1.00 53.04  ? 221 GLN A NE2 1 
ATOM   1462 N N   . ARG A 1 228 ? 32.622  8.018   24.420  1.00 56.81  ? 222 ARG A N   1 
ATOM   1463 C CA  . ARG A 1 228 ? 31.407  7.795   25.176  1.00 61.91  ? 222 ARG A CA  1 
ATOM   1464 C C   . ARG A 1 228 ? 31.712  7.514   26.646  1.00 65.13  ? 222 ARG A C   1 
ATOM   1465 O O   . ARG A 1 228 ? 30.937  7.925   27.513  1.00 72.21  ? 222 ARG A O   1 
ATOM   1466 C CB  . ARG A 1 228 ? 30.608  6.623   24.561  1.00 66.71  ? 222 ARG A CB  1 
ATOM   1467 C CG  . ARG A 1 228 ? 29.098  6.895   24.504  1.00 73.58  ? 222 ARG A CG  1 
ATOM   1468 C CD  . ARG A 1 228 ? 28.270  5.663   24.172  1.00 78.07  ? 222 ARG A CD  1 
ATOM   1469 N NE  . ARG A 1 228 ? 28.252  5.366   22.744  1.00 86.10  ? 222 ARG A NE  1 
ATOM   1470 C CZ  . ARG A 1 228 ? 27.752  4.258   22.211  1.00 90.62  ? 222 ARG A CZ  1 
ATOM   1471 N NH1 . ARG A 1 228 ? 27.282  3.276   22.966  1.00 90.49  ? 222 ARG A NH1 1 
ATOM   1472 N NH2 . ARG A 1 228 ? 27.739  4.125   20.888  1.00 93.51  ? 222 ARG A NH2 1 
ATOM   1473 N N   . PHE A 1 229 ? 32.845  6.837   26.912  1.00 60.35  ? 223 PHE A N   1 
ATOM   1474 C CA  . PHE A 1 229 ? 33.191  6.363   28.243  1.00 55.41  ? 223 PHE A CA  1 
ATOM   1475 C C   . PHE A 1 229 ? 34.610  6.750   28.659  1.00 56.90  ? 223 PHE A C   1 
ATOM   1476 O O   . PHE A 1 229 ? 35.409  5.883   29.015  1.00 57.33  ? 223 PHE A O   1 
ATOM   1477 C CB  . PHE A 1 229 ? 33.030  4.830   28.294  1.00 54.39  ? 223 PHE A CB  1 
ATOM   1478 C CG  . PHE A 1 229 ? 31.663  4.288   27.910  1.00 55.29  ? 223 PHE A CG  1 
ATOM   1479 C CD1 . PHE A 1 229 ? 30.498  4.951   28.285  1.00 56.31  ? 223 PHE A CD1 1 
ATOM   1480 C CD2 . PHE A 1 229 ? 31.540  3.077   27.240  1.00 54.35  ? 223 PHE A CD2 1 
ATOM   1481 C CE1 . PHE A 1 229 ? 29.241  4.439   27.950  1.00 55.98  ? 223 PHE A CE1 1 
ATOM   1482 C CE2 . PHE A 1 229 ? 30.281  2.558   26.914  1.00 54.27  ? 223 PHE A CE2 1 
ATOM   1483 C CZ  . PHE A 1 229 ? 29.141  3.238   27.276  1.00 55.70  ? 223 PHE A CZ  1 
ATOM   1484 N N   . PRO A 1 230 ? 34.953  8.060   28.692  1.00 58.03  ? 224 PRO A N   1 
ATOM   1485 C CA  . PRO A 1 230 ? 36.336  8.504   28.895  1.00 62.30  ? 224 PRO A CA  1 
ATOM   1486 C C   . PRO A 1 230 ? 36.996  8.091   30.209  1.00 68.37  ? 224 PRO A C   1 
ATOM   1487 O O   . PRO A 1 230 ? 38.187  7.797   30.238  1.00 77.10  ? 224 PRO A O   1 
ATOM   1488 C CB  . PRO A 1 230 ? 36.240  10.045  28.856  1.00 61.53  ? 224 PRO A CB  1 
ATOM   1489 C CG  . PRO A 1 230 ? 34.890  10.368  28.375  1.00 60.32  ? 224 PRO A CG  1 
ATOM   1490 C CD  . PRO A 1 230 ? 34.009  9.184   28.623  1.00 58.68  ? 224 PRO A CD  1 
ATOM   1491 N N   . LYS A 1 231 ? 36.228  8.104   31.304  1.00 73.43  ? 225 LYS A N   1 
ATOM   1492 C CA  . LYS A 1 231 ? 36.756  7.769   32.619  1.00 74.34  ? 225 LYS A CA  1 
ATOM   1493 C C   . LYS A 1 231 ? 37.204  6.312   32.733  1.00 71.38  ? 225 LYS A C   1 
ATOM   1494 O O   . LYS A 1 231 ? 38.086  6.010   33.533  1.00 75.39  ? 225 LYS A O   1 
ATOM   1495 C CB  . LYS A 1 231 ? 35.719  8.086   33.710  1.00 76.24  ? 225 LYS A CB  1 
ATOM   1496 C CG  . LYS A 1 231 ? 35.409  9.581   33.855  1.00 79.56  ? 225 LYS A CG  1 
ATOM   1497 C CD  . LYS A 1 231 ? 34.472  9.867   35.048  1.00 81.44  ? 225 LYS A CD  1 
ATOM   1498 C CE  . LYS A 1 231 ? 34.059  11.318  35.155  1.00 82.73  ? 225 LYS A CE  1 
ATOM   1499 N NZ  . LYS A 1 231 ? 35.212  12.205  35.467  1.00 83.56  ? 225 LYS A NZ  1 
ATOM   1500 N N   . ALA A 1 232 ? 36.602  5.414   31.941  1.00 67.00  ? 226 ALA A N   1 
ATOM   1501 C CA  . ALA A 1 232 ? 37.052  4.033   31.881  1.00 64.89  ? 226 ALA A CA  1 
ATOM   1502 C C   . ALA A 1 232 ? 38.486  3.960   31.355  1.00 64.87  ? 226 ALA A C   1 
ATOM   1503 O O   . ALA A 1 232 ? 38.900  4.771   30.525  1.00 61.58  ? 226 ALA A O   1 
ATOM   1504 C CB  . ALA A 1 232 ? 36.130  3.188   31.013  1.00 64.34  ? 226 ALA A CB  1 
ATOM   1505 N N   . GLU A 1 233 ? 39.243  2.989   31.880  1.00 65.71  ? 227 GLU A N   1 
ATOM   1506 C CA  . GLU A 1 233 ? 40.601  2.727   31.432  1.00 63.80  ? 227 GLU A CA  1 
ATOM   1507 C C   . GLU A 1 233 ? 40.517  1.995   30.094  1.00 61.29  ? 227 GLU A C   1 
ATOM   1508 O O   . GLU A 1 233 ? 39.426  1.722   29.608  1.00 64.64  ? 227 GLU A O   1 
ATOM   1509 C CB  . GLU A 1 233 ? 41.406  1.932   32.498  1.00 62.99  ? 227 GLU A CB  1 
ATOM   1510 C CG  . GLU A 1 233 ? 40.929  0.515   32.790  1.00 65.33  ? 227 GLU A CG  1 
ATOM   1511 C CD  . GLU A 1 233 ? 41.774  -0.202  33.831  1.00 70.88  ? 227 GLU A CD  1 
ATOM   1512 O OE1 . GLU A 1 233 ? 42.948  -0.506  33.521  1.00 76.45  ? 227 GLU A OE1 1 
ATOM   1513 O OE2 . GLU A 1 233 ? 41.281  -0.443  34.960  1.00 73.70  ? 227 GLU A OE2 1 
ATOM   1514 N N   . PHE A 1 234 ? 41.679  1.684   29.517  1.00 61.11  ? 228 PHE A N   1 
ATOM   1515 C CA  . PHE A 1 234 ? 41.769  1.055   28.209  1.00 59.20  ? 228 PHE A CA  1 
ATOM   1516 C C   . PHE A 1 234 ? 41.317  -0.407  28.183  1.00 56.65  ? 228 PHE A C   1 
ATOM   1517 O O   . PHE A 1 234 ? 40.766  -0.865  27.184  1.00 57.60  ? 228 PHE A O   1 
ATOM   1518 C CB  . PHE A 1 234 ? 43.222  1.178   27.672  1.00 55.79  ? 228 PHE A CB  1 
ATOM   1519 C CG  . PHE A 1 234 ? 43.416  0.483   26.347  1.00 56.53  ? 228 PHE A CG  1 
ATOM   1520 C CD1 . PHE A 1 234 ? 43.669  -0.873  26.287  1.00 55.27  ? 228 PHE A CD1 1 
ATOM   1521 C CD2 . PHE A 1 234 ? 43.279  1.178   25.155  1.00 56.60  ? 228 PHE A CD2 1 
ATOM   1522 C CE1 . PHE A 1 234 ? 43.811  -1.513  25.062  1.00 55.79  ? 228 PHE A CE1 1 
ATOM   1523 C CE2 . PHE A 1 234 ? 43.412  0.533   23.941  1.00 56.47  ? 228 PHE A CE2 1 
ATOM   1524 C CZ  . PHE A 1 234 ? 43.683  -0.807  23.900  1.00 55.68  ? 228 PHE A CZ  1 
ATOM   1525 N N   . ALA A 1 235 ? 41.578  -1.152  29.259  1.00 56.33  ? 229 ALA A N   1 
ATOM   1526 C CA  . ALA A 1 235 ? 41.330  -2.586  29.261  1.00 57.88  ? 229 ALA A CA  1 
ATOM   1527 C C   . ALA A 1 235 ? 39.829  -2.866  29.280  1.00 58.31  ? 229 ALA A C   1 
ATOM   1528 O O   . ALA A 1 235 ? 39.376  -3.874  28.733  1.00 57.89  ? 229 ALA A O   1 
ATOM   1529 C CB  . ALA A 1 235 ? 42.021  -3.247  30.447  1.00 57.69  ? 229 ALA A CB  1 
ATOM   1530 N N   . GLU A 1 236 ? 39.082  -1.942  29.900  1.00 56.35  ? 230 GLU A N   1 
ATOM   1531 C CA  . GLU A 1 236 ? 37.630  -2.002  29.960  1.00 58.97  ? 230 GLU A CA  1 
ATOM   1532 C C   . GLU A 1 236 ? 36.968  -1.725  28.608  1.00 57.50  ? 230 GLU A C   1 
ATOM   1533 O O   . GLU A 1 236 ? 36.117  -2.499  28.159  1.00 55.98  ? 230 GLU A O   1 
ATOM   1534 C CB  . GLU A 1 236 ? 37.126  -0.979  31.001  1.00 62.44  ? 230 GLU A CB  1 
ATOM   1535 C CG  . GLU A 1 236 ? 35.669  -1.159  31.375  1.00 63.41  ? 230 GLU A CG  1 
ATOM   1536 C CD  . GLU A 1 236 ? 35.384  -2.589  31.758  1.00 62.68  ? 230 GLU A CD  1 
ATOM   1537 O OE1 . GLU A 1 236 ? 36.155  -3.125  32.580  1.00 66.30  ? 230 GLU A OE1 1 
ATOM   1538 O OE2 . GLU A 1 236 ? 34.430  -3.186  31.219  1.00 61.01  ? 230 GLU A OE2 1 
ATOM   1539 N N   . VAL A 1 237 ? 37.371  -0.610  27.977  1.00 55.56  ? 231 VAL A N   1 
ATOM   1540 C CA  . VAL A 1 237 ? 36.964  -0.264  26.622  1.00 54.07  ? 231 VAL A CA  1 
ATOM   1541 C C   . VAL A 1 237 ? 37.218  -1.421  25.660  1.00 51.91  ? 231 VAL A C   1 
ATOM   1542 O O   . VAL A 1 237 ? 36.313  -1.842  24.957  1.00 55.56  ? 231 VAL A O   1 
ATOM   1543 C CB  . VAL A 1 237 ? 37.666  1.030   26.145  1.00 55.24  ? 231 VAL A CB  1 
ATOM   1544 C CG1 . VAL A 1 237 ? 37.513  1.236   24.637  1.00 54.47  ? 231 VAL A CG1 1 
ATOM   1545 C CG2 . VAL A 1 237 ? 37.141  2.240   26.910  1.00 56.26  ? 231 VAL A CG2 1 
ATOM   1546 N N   . SER A 1 238 ? 38.442  -1.955  25.654  1.00 51.79  ? 232 SER A N   1 
ATOM   1547 C CA  . SER A 1 238 ? 38.770  -3.093  24.809  1.00 50.18  ? 232 SER A CA  1 
ATOM   1548 C C   . SER A 1 238 ? 37.826  -4.274  24.999  1.00 49.34  ? 232 SER A C   1 
ATOM   1549 O O   . SER A 1 238 ? 37.563  -5.001  24.054  1.00 50.12  ? 232 SER A O   1 
ATOM   1550 C CB  . SER A 1 238 ? 40.208  -3.560  25.048  1.00 49.55  ? 232 SER A CB  1 
ATOM   1551 O OG  . SER A 1 238 ? 40.428  -4.835  24.454  1.00 49.21  ? 232 SER A OG  1 
ATOM   1552 N N   . LYS A 1 239 ? 37.383  -4.498  26.239  1.00 56.93  ? 233 LYS A N   1 
ATOM   1553 C CA  . LYS A 1 239 ? 36.489  -5.600  26.560  1.00 62.29  ? 233 LYS A CA  1 
ATOM   1554 C C   . LYS A 1 239 ? 35.123  -5.420  25.905  1.00 62.49  ? 233 LYS A C   1 
ATOM   1555 O O   . LYS A 1 239 ? 34.581  -6.355  25.308  1.00 60.31  ? 233 LYS A O   1 
ATOM   1556 C CB  . LYS A 1 239 ? 36.263  -5.700  28.072  1.00 69.20  ? 233 LYS A CB  1 
ATOM   1557 C CG  . LYS A 1 239 ? 35.469  -6.950  28.457  1.00 73.58  ? 233 LYS A CG  1 
ATOM   1558 C CD  . LYS A 1 239 ? 34.211  -6.644  29.256  1.00 74.83  ? 233 LYS A CD  1 
ATOM   1559 C CE  . LYS A 1 239 ? 33.473  -7.904  29.672  1.00 76.37  ? 233 LYS A CE  1 
ATOM   1560 N NZ  . LYS A 1 239 ? 33.295  -8.863  28.542  1.00 76.73  ? 233 LYS A NZ  1 
ATOM   1561 N N   . LEU A 1 240 ? 34.600  -4.210  26.015  1.00 59.78  ? 234 LEU A N   1 
ATOM   1562 C CA  . LEU A 1 240 ? 33.294  -3.909  25.393  1.00 59.61  ? 234 LEU A CA  1 
ATOM   1563 C C   . LEU A 1 240 ? 33.397  -4.068  23.871  1.00 61.24  ? 234 LEU A C   1 
ATOM   1564 O O   . LEU A 1 240 ? 32.514  -4.719  23.304  1.00 65.32  ? 234 LEU A O   1 
ATOM   1565 C CB  . LEU A 1 240 ? 32.912  -2.495  25.820  1.00 55.83  ? 234 LEU A CB  1 
ATOM   1566 C CG  . LEU A 1 240 ? 32.759  -2.255  27.323  1.00 55.75  ? 234 LEU A CG  1 
ATOM   1567 C CD1 . LEU A 1 240 ? 32.486  -0.790  27.583  1.00 56.18  ? 234 LEU A CD1 1 
ATOM   1568 C CD2 . LEU A 1 240 ? 31.644  -3.109  27.883  1.00 55.50  ? 234 LEU A CD2 1 
ATOM   1569 N N   . VAL A 1 241 ? 34.466  -3.571  23.249  1.00 58.80  ? 235 VAL A N   1 
ATOM   1570 C CA  . VAL A 1 241 ? 34.558  -3.580  21.763  1.00 57.04  ? 235 VAL A CA  1 
ATOM   1571 C C   . VAL A 1 241 ? 34.551  -5.027  21.271  1.00 57.59  ? 235 VAL A C   1 
ATOM   1572 O O   . VAL A 1 241 ? 33.869  -5.319  20.292  1.00 59.15  ? 235 VAL A O   1 
ATOM   1573 C CB  . VAL A 1 241 ? 35.836  -2.853  21.325  1.00 54.75  ? 235 VAL A CB  1 
ATOM   1574 C CG1 . VAL A 1 241 ? 36.341  -3.326  19.971  1.00 54.26  ? 235 VAL A CG1 1 
ATOM   1575 C CG2 . VAL A 1 241 ? 35.685  -1.342  21.377  1.00 54.50  ? 235 VAL A CG2 1 
ATOM   1576 N N   . THR A 1 242 ? 35.256  -5.898  21.956  1.00 58.11  ? 236 THR A N   1 
ATOM   1577 C CA  . THR A 1 242 ? 35.265  -7.258  21.456  1.00 60.59  ? 236 THR A CA  1 
ATOM   1578 C C   . THR A 1 242 ? 33.858  -7.779  21.521  1.00 62.10  ? 236 THR A C   1 
ATOM   1579 O O   . THR A 1 242 ? 33.437  -8.474  20.587  1.00 61.59  ? 236 THR A O   1 
ATOM   1580 C CB  . THR A 1 242 ? 36.212  -8.049  22.356  1.00 58.53  ? 236 THR A CB  1 
ATOM   1581 O OG1 . THR A 1 242 ? 37.298  -7.177  22.647  1.00 58.14  ? 236 THR A OG1 1 
ATOM   1582 C CG2 . THR A 1 242 ? 36.738  -9.307  21.692  1.00 56.47  ? 236 THR A CG2 1 
ATOM   1583 N N   . ASP A 1 243 ? 33.162  -7.485  22.613  1.00 65.07  ? 237 ASP A N   1 
ATOM   1584 C CA  . ASP A 1 243 ? 31.749  -7.915  22.743  1.00 69.00  ? 237 ASP A CA  1 
ATOM   1585 C C   . ASP A 1 243 ? 30.817  -7.275  21.716  1.00 70.52  ? 237 ASP A C   1 
ATOM   1586 O O   . ASP A 1 243 ? 30.054  -7.995  21.078  1.00 64.17  ? 237 ASP A O   1 
ATOM   1587 C CB  . ASP A 1 243 ? 31.246  -7.564  24.134  1.00 66.44  ? 237 ASP A CB  1 
ATOM   1588 C CG  . ASP A 1 243 ? 31.677  -8.499  25.250  1.00 67.97  ? 237 ASP A CG  1 
ATOM   1589 O OD1 . ASP A 1 243 ? 32.029  -9.653  24.941  1.00 69.28  ? 237 ASP A OD1 1 
ATOM   1590 O OD2 . ASP A 1 243 ? 31.652  -8.062  26.416  1.00 67.11  ? 237 ASP A OD2 1 
ATOM   1591 N N   . LEU A 1 244 ? 30.977  -5.976  21.489  1.00 72.05  ? 238 LEU A N   1 
ATOM   1592 C CA  . LEU A 1 244 ? 30.120  -5.270  20.520  1.00 74.85  ? 238 LEU A CA  1 
ATOM   1593 C C   . LEU A 1 244 ? 30.376  -5.846  19.148  1.00 72.41  ? 238 LEU A C   1 
ATOM   1594 O O   . LEU A 1 244 ? 29.434  -6.065  18.392  1.00 74.87  ? 238 LEU A O   1 
ATOM   1595 C CB  . LEU A 1 244 ? 30.548  -3.814  20.573  1.00 80.09  ? 238 LEU A CB  1 
ATOM   1596 C CG  . LEU A 1 244 ? 29.542  -2.782  20.061  1.00 84.18  ? 238 LEU A CG  1 
ATOM   1597 C CD1 . LEU A 1 244 ? 29.758  -2.525  18.582  1.00 86.30  ? 238 LEU A CD1 1 
ATOM   1598 C CD2 . LEU A 1 244 ? 28.119  -3.222  20.341  1.00 85.13  ? 238 LEU A CD2 1 
ATOM   1599 N N   . THR A 1 245 ? 31.645  -6.088  18.872  1.00 74.81  ? 239 THR A N   1 
ATOM   1600 C CA  . THR A 1 245 ? 31.954  -6.540  17.523  1.00 77.58  ? 239 THR A CA  1 
ATOM   1601 C C   . THR A 1 245 ? 31.286  -7.859  17.307  1.00 77.78  ? 239 THR A C   1 
ATOM   1602 O O   . THR A 1 245 ? 30.685  -8.046  16.250  1.00 78.28  ? 239 THR A O   1 
ATOM   1603 C CB  . THR A 1 245 ? 33.473  -6.655  17.415  1.00 78.29  ? 239 THR A CB  1 
ATOM   1604 O OG1 . THR A 1 245 ? 33.963  -5.363  17.754  1.00 79.24  ? 239 THR A OG1 1 
ATOM   1605 C CG2 . THR A 1 245 ? 33.938  -7.041  16.024  1.00 77.31  ? 239 THR A CG2 1 
ATOM   1606 N N   . LYS A 1 246 ? 31.342  -8.735  18.301  1.00 81.95  ? 240 LYS A N   1 
ATOM   1607 C CA  . LYS A 1 246 ? 30.760  -10.065 18.022  1.00 82.23  ? 240 LYS A CA  1 
ATOM   1608 C C   . LYS A 1 246 ? 29.264  -9.891  17.777  1.00 80.73  ? 240 LYS A C   1 
ATOM   1609 O O   . LYS A 1 246 ? 28.740  -10.543 16.869  1.00 74.63  ? 240 LYS A O   1 
ATOM   1610 C CB  . LYS A 1 246 ? 31.046  -11.075 19.139  1.00 82.41  ? 240 LYS A CB  1 
ATOM   1611 C CG  . LYS A 1 246 ? 30.496  -10.777 20.517  1.00 84.88  ? 240 LYS A CG  1 
ATOM   1612 C CD  . LYS A 1 246 ? 29.776  -11.944 21.178  1.00 86.85  ? 240 LYS A CD  1 
ATOM   1613 C CE  . LYS A 1 246 ? 29.629  -11.731 22.650  1.00 89.11  ? 240 LYS A CE  1 
ATOM   1614 N NZ  . LYS A 1 246 ? 28.957  -10.467 22.954  1.00 87.60  ? 240 LYS A NZ  1 
ATOM   1615 N N   . VAL A 1 247 ? 28.614  -9.053  18.586  1.00 82.20  ? 241 VAL A N   1 
ATOM   1616 C CA  . VAL A 1 247 ? 27.144  -8.978  18.413  1.00 84.97  ? 241 VAL A CA  1 
ATOM   1617 C C   . VAL A 1 247 ? 26.823  -8.433  17.026  1.00 89.51  ? 241 VAL A C   1 
ATOM   1618 O O   . VAL A 1 247 ? 25.949  -9.003  16.354  1.00 94.67  ? 241 VAL A O   1 
ATOM   1619 C CB  . VAL A 1 247 ? 26.640  -8.010  19.491  1.00 86.56  ? 241 VAL A CB  1 
ATOM   1620 C CG1 . VAL A 1 247 ? 25.152  -7.735  19.351  1.00 89.19  ? 241 VAL A CG1 1 
ATOM   1621 C CG2 . VAL A 1 247 ? 26.951  -8.504  20.895  1.00 86.71  ? 241 VAL A CG2 1 
ATOM   1622 N N   . HIS A 1 248 ? 27.541  -7.394  16.610  1.00 86.67  ? 242 HIS A N   1 
ATOM   1623 C CA  . HIS A 1 248 ? 27.367  -6.832  15.245  1.00 82.39  ? 242 HIS A CA  1 
ATOM   1624 C C   . HIS A 1 248 ? 27.784  -7.824  14.158  1.00 79.00  ? 242 HIS A C   1 
ATOM   1625 O O   . HIS A 1 248 ? 27.096  -7.950  13.141  1.00 81.87  ? 242 HIS A O   1 
ATOM   1626 C CB  . HIS A 1 248 ? 27.941  -5.413  15.234  1.00 81.02  ? 242 HIS A CB  1 
ATOM   1627 C CG  . HIS A 1 248 ? 27.024  -4.453  15.909  1.00 78.34  ? 242 HIS A CG  1 
ATOM   1628 N ND1 . HIS A 1 248 ? 25.868  -3.995  15.320  1.00 79.15  ? 242 HIS A ND1 1 
ATOM   1629 C CD2 . HIS A 1 248 ? 27.067  -3.892  17.116  1.00 78.10  ? 242 HIS A CD2 1 
ATOM   1630 C CE1 . HIS A 1 248 ? 25.253  -3.169  16.150  1.00 79.74  ? 242 HIS A CE1 1 
ATOM   1631 N NE2 . HIS A 1 248 ? 25.965  -3.093  17.248  1.00 78.23  ? 242 HIS A NE2 1 
ATOM   1632 N N   . THR A 1 249 ? 28.882  -8.532  14.387  1.00 78.97  ? 243 THR A N   1 
ATOM   1633 C CA  . THR A 1 249 ? 29.414  -9.403  13.327  1.00 77.93  ? 243 THR A CA  1 
ATOM   1634 C C   . THR A 1 249 ? 28.383  -10.448 13.059  1.00 82.25  ? 243 THR A C   1 
ATOM   1635 O O   . THR A 1 249 ? 28.191  -10.808 11.896  1.00 81.21  ? 243 THR A O   1 
ATOM   1636 C CB  . THR A 1 249 ? 30.740  -10.014 13.762  1.00 72.36  ? 243 THR A CB  1 
ATOM   1637 O OG1 . THR A 1 249 ? 31.579  -8.906  14.058  1.00 72.82  ? 243 THR A OG1 1 
ATOM   1638 C CG2 . THR A 1 249 ? 31.377  -10.864 12.679  1.00 71.29  ? 243 THR A CG2 1 
ATOM   1639 N N   . GLU A 1 250 ? 27.732  -10.907 14.117  1.00 87.42  ? 244 GLU A N   1 
ATOM   1640 C CA  . GLU A 1 250 ? 26.738  -11.990 13.951  1.00 91.62  ? 244 GLU A CA  1 
ATOM   1641 C C   . GLU A 1 250 ? 25.437  -11.568 13.271  1.00 96.78  ? 244 GLU A C   1 
ATOM   1642 O O   . GLU A 1 250 ? 24.961  -12.327 12.409  1.00 95.86  ? 244 GLU A O   1 
ATOM   1643 C CB  . GLU A 1 250 ? 26.347  -12.381 15.372  1.00 91.44  ? 244 GLU A CB  1 
ATOM   1644 C CG  . GLU A 1 250 ? 27.301  -13.378 16.021  1.00 89.60  ? 244 GLU A CG  1 
ATOM   1645 C CD  . GLU A 1 250 ? 27.223  -13.413 17.535  1.00 88.31  ? 244 GLU A CD  1 
ATOM   1646 O OE1 . GLU A 1 250 ? 26.477  -12.598 18.111  1.00 86.24  ? 244 GLU A OE1 1 
ATOM   1647 O OE2 . GLU A 1 250 ? 27.918  -14.254 18.136  1.00 86.16  ? 244 GLU A OE2 1 
ATOM   1648 N N   . CYS A 1 251 ? 24.881  -10.423 13.663  1.00 99.63  ? 245 CYS A N   1 
ATOM   1649 C CA  . CYS A 1 251 ? 23.613  -9.938  13.060  1.00 96.59  ? 245 CYS A CA  1 
ATOM   1650 C C   . CYS A 1 251 ? 23.899  -9.528  11.600  1.00 96.38  ? 245 CYS A C   1 
ATOM   1651 O O   . CYS A 1 251 ? 23.021  -9.759  10.757  1.00 98.88  ? 245 CYS A O   1 
ATOM   1652 C CB  . CYS A 1 251 ? 23.004  -8.888  13.979  1.00 95.57  ? 245 CYS A CB  1 
ATOM   1653 S SG  . CYS A 1 251 ? 22.139  -9.589  15.409  1.00 92.68  ? 245 CYS A SG  1 
ATOM   1654 N N   . CYS A 1 252 ? 25.074  -8.965  11.306  1.00 99.29  ? 246 CYS A N   1 
ATOM   1655 C CA  . CYS A 1 252 ? 25.485  -8.666  9.901   1.00 103.24 ? 246 CYS A CA  1 
ATOM   1656 C C   . CYS A 1 252 ? 25.557  -10.034 9.229   1.00 98.52  ? 246 CYS A C   1 
ATOM   1657 O O   . CYS A 1 252 ? 25.197  -10.143 8.045   1.00 98.53  ? 246 CYS A O   1 
ATOM   1658 C CB  . CYS A 1 252 ? 26.772  -7.851  9.838   1.00 107.28 ? 246 CYS A CB  1 
ATOM   1659 S SG  . CYS A 1 252 ? 26.511  -6.082  10.136  1.00 112.78 ? 246 CYS A SG  1 
ATOM   1660 N N   . HIS A 1 253 ? 26.046  -11.014 9.968   1.00 98.75  ? 247 HIS A N   1 
ATOM   1661 C CA  . HIS A 1 253 ? 26.081  -12.425 9.508   1.00 101.71 ? 247 HIS A CA  1 
ATOM   1662 C C   . HIS A 1 253 ? 24.606  -12.782 9.318   1.00 103.97 ? 247 HIS A C   1 
ATOM   1663 O O   . HIS A 1 253 ? 24.304  -13.574 8.408   1.00 107.82 ? 247 HIS A O   1 
ATOM   1664 C CB  . HIS A 1 253 ? 26.949  -13.290 10.425  1.00 103.08 ? 247 HIS A CB  1 
ATOM   1665 C CG  . HIS A 1 253 ? 28.385  -13.203 10.034  1.00 104.85 ? 247 HIS A CG  1 
ATOM   1666 N ND1 . HIS A 1 253 ? 28.805  -12.315 9.067   1.00 103.64 ? 247 HIS A ND1 1 
ATOM   1667 C CD2 . HIS A 1 253 ? 29.481  -13.851 10.441  1.00 103.99 ? 247 HIS A CD2 1 
ATOM   1668 C CE1 . HIS A 1 253 ? 30.113  -12.432 8.902   1.00 105.09 ? 247 HIS A CE1 1 
ATOM   1669 N NE2 . HIS A 1 253 ? 30.544  -13.359 9.726   1.00 103.31 ? 247 HIS A NE2 1 
ATOM   1670 N N   . GLY A 1 254 ? 23.727  -12.269 10.182  1.00 102.85 ? 248 GLY A N   1 
ATOM   1671 C CA  . GLY A 1 254 ? 22.311  -12.658 10.076  1.00 103.93 ? 248 GLY A CA  1 
ATOM   1672 C C   . GLY A 1 254 ? 21.974  -13.900 10.850  1.00 108.72 ? 248 GLY A C   1 
ATOM   1673 O O   . GLY A 1 254 ? 20.837  -14.393 10.724  1.00 109.26 ? 248 GLY A O   1 
ATOM   1674 N N   . ASP A 1 255 ? 22.911  -14.375 11.653  1.00 112.38 ? 249 ASP A N   1 
ATOM   1675 C CA  . ASP A 1 255 ? 22.551  -15.511 12.532  1.00 112.42 ? 249 ASP A CA  1 
ATOM   1676 C C   . ASP A 1 255 ? 21.429  -15.023 13.460  1.00 115.01 ? 249 ASP A C   1 
ATOM   1677 O O   . ASP A 1 255 ? 20.502  -15.820 13.675  1.00 118.83 ? 249 ASP A O   1 
ATOM   1678 C CB  . ASP A 1 255 ? 23.767  -16.089 13.235  1.00 110.65 ? 249 ASP A CB  1 
ATOM   1679 C CG  . ASP A 1 255 ? 24.625  -15.101 14.003  1.00 109.45 ? 249 ASP A CG  1 
ATOM   1680 O OD1 . ASP A 1 255 ? 24.045  -14.260 14.716  1.00 114.20 ? 249 ASP A OD1 1 
ATOM   1681 O OD2 . ASP A 1 255 ? 25.862  -15.195 13.883  1.00 105.24 ? 249 ASP A OD2 1 
ATOM   1682 N N   . LEU A 1 256 ? 21.469  -13.783 13.966  1.00 114.56 ? 250 LEU A N   1 
ATOM   1683 C CA  . LEU A 1 256 ? 20.448  -13.366 14.968  1.00 115.96 ? 250 LEU A CA  1 
ATOM   1684 C C   . LEU A 1 256 ? 20.703  -14.391 16.049  1.00 115.58 ? 250 LEU A C   1 
ATOM   1685 O O   . LEU A 1 256 ? 21.881  -14.495 16.449  1.00 112.79 ? 250 LEU A O   1 
ATOM   1686 C CB  . LEU A 1 256 ? 19.019  -13.398 14.438  1.00 30.00  ? 250 LEU A CB  1 
ATOM   1687 C CG  . LEU A 1 256 ? 18.581  -12.187 13.607  1.00 30.00  ? 250 LEU A CG  1 
ATOM   1688 C CD1 . LEU A 1 256 ? 19.368  -12.029 12.319  1.00 30.00  ? 250 LEU A CD1 1 
ATOM   1689 C CD2 . LEU A 1 256 ? 17.095  -12.235 13.309  1.00 30.00  ? 250 LEU A CD2 1 
ATOM   1690 N N   . LEU A 1 257 ? 19.668  -15.072 16.554  1.00 116.34 ? 251 LEU A N   1 
ATOM   1691 C CA  . LEU A 1 257 ? 20.157  -16.147 17.438  1.00 115.44 ? 251 LEU A CA  1 
ATOM   1692 C C   . LEU A 1 257 ? 20.932  -15.437 18.543  1.00 112.24 ? 251 LEU A C   1 
ATOM   1693 O O   . LEU A 1 257 ? 20.305  -14.677 19.305  1.00 105.10 ? 251 LEU A O   1 
ATOM   1694 C CB  . LEU A 1 257 ? 20.983  -17.159 16.649  1.00 30.00  ? 251 LEU A CB  1 
ATOM   1695 C CG  . LEU A 1 257 ? 20.179  -18.019 15.671  1.00 30.00  ? 251 LEU A CG  1 
ATOM   1696 C CD1 . LEU A 1 257 ? 21.052  -18.698 14.632  1.00 30.00  ? 251 LEU A CD1 1 
ATOM   1697 C CD2 . LEU A 1 257 ? 19.304  -19.024 16.395  1.00 30.00  ? 251 LEU A CD2 1 
ATOM   1698 N N   . GLU A 1 258 ? 22.219  -15.705 18.665  1.00 110.69 ? 252 GLU A N   1 
ATOM   1699 C CA  . GLU A 1 258 ? 23.078  -15.285 19.790  1.00 109.61 ? 252 GLU A CA  1 
ATOM   1700 C C   . GLU A 1 258 ? 23.156  -13.767 19.990  1.00 106.18 ? 252 GLU A C   1 
ATOM   1701 O O   . GLU A 1 258 ? 23.237  -13.377 21.166  1.00 101.90 ? 252 GLU A O   1 
ATOM   1702 C CB  . GLU A 1 258 ? 24.420  -15.822 19.314  1.00 109.01 ? 252 GLU A CB  1 
ATOM   1703 C CG  . GLU A 1 258 ? 24.302  -17.189 18.646  1.00 109.17 ? 252 GLU A CG  1 
ATOM   1704 C CD  . GLU A 1 258 ? 24.836  -17.263 17.229  1.00 109.79 ? 252 GLU A CD  1 
ATOM   1705 O OE1 . GLU A 1 258 ? 24.015  -17.287 16.292  1.00 106.28 ? 252 GLU A OE1 1 
ATOM   1706 O OE2 . GLU A 1 258 ? 26.072  -17.306 17.064  1.00 110.63 ? 252 GLU A OE2 1 
ATOM   1707 N N   . CYS A 1 259 ? 23.156  -12.921 18.963  1.00 103.96 ? 253 CYS A N   1 
ATOM   1708 C CA  . CYS A 1 259 ? 23.427  -11.487 19.217  1.00 103.29 ? 253 CYS A CA  1 
ATOM   1709 C C   . CYS A 1 259 ? 22.382  -10.924 20.174  1.00 100.25 ? 253 CYS A C   1 
ATOM   1710 O O   . CYS A 1 259 ? 22.786  -10.130 21.039  1.00 98.18  ? 253 CYS A O   1 
ATOM   1711 C CB  . CYS A 1 259 ? 22.837  -10.571 18.155  1.00 106.15 ? 253 CYS A CB  1 
ATOM   1712 S SG  . CYS A 1 259 ? 23.501  -10.673 16.471  1.00 106.28 ? 253 CYS A SG  1 
ATOM   1713 N N   . ALA A 1 260 ? 21.108  -11.282 20.052  1.00 97.34  ? 254 ALA A N   1 
ATOM   1714 C CA  . ALA A 1 260 ? 20.132  -10.822 21.072  1.00 97.64  ? 254 ALA A CA  1 
ATOM   1715 C C   . ALA A 1 260 ? 20.565  -11.262 22.478  1.00 95.91  ? 254 ALA A C   1 
ATOM   1716 O O   . ALA A 1 260 ? 20.442  -10.445 23.406  1.00 94.87  ? 254 ALA A O   1 
ATOM   1717 C CB  . ALA A 1 260 ? 18.759  -11.331 20.721  1.00 99.72  ? 254 ALA A CB  1 
ATOM   1718 N N   . ASP A 1 261 ? 21.030  -12.504 22.646  1.00 97.09  ? 255 ASP A N   1 
ATOM   1719 C CA  . ASP A 1 261 ? 21.530  -13.026 23.945  1.00 96.01  ? 255 ASP A CA  1 
ATOM   1720 C C   . ASP A 1 261 ? 22.825  -12.290 24.271  1.00 93.03  ? 255 ASP A C   1 
ATOM   1721 O O   . ASP A 1 261 ? 22.998  -11.860 25.425  1.00 89.81  ? 255 ASP A O   1 
ATOM   1722 C CB  . ASP A 1 261 ? 21.743  -14.530 23.876  1.00 97.21  ? 255 ASP A CB  1 
ATOM   1723 C CG  . ASP A 1 261 ? 22.185  -15.205 25.164  1.00 99.02  ? 255 ASP A CG  1 
ATOM   1724 O OD1 . ASP A 1 261 ? 21.724  -14.774 26.240  1.00 100.46 ? 255 ASP A OD1 1 
ATOM   1725 O OD2 . ASP A 1 261 ? 22.981  -16.161 25.078  1.00 103.03 ? 255 ASP A OD2 1 
ATOM   1726 N N   . ASP A 1 262 ? 23.656  -12.087 23.255  1.00 92.87  ? 256 ASP A N   1 
ATOM   1727 C CA  . ASP A 1 262 ? 24.967  -11.427 23.470  1.00 91.71  ? 256 ASP A CA  1 
ATOM   1728 C C   . ASP A 1 262 ? 24.717  -9.950  23.780  1.00 91.59  ? 256 ASP A C   1 
ATOM   1729 O O   . ASP A 1 262 ? 25.460  -9.389  24.607  1.00 92.05  ? 256 ASP A O   1 
ATOM   1730 C CB  . ASP A 1 262 ? 25.884  -11.688 22.288  1.00 90.76  ? 256 ASP A CB  1 
ATOM   1731 C CG  . ASP A 1 262 ? 26.336  -13.129 22.119  1.00 89.36  ? 256 ASP A CG  1 
ATOM   1732 O OD1 . ASP A 1 262 ? 26.708  -13.748 23.135  1.00 87.56  ? 256 ASP A OD1 1 
ATOM   1733 O OD2 . ASP A 1 262 ? 26.315  -13.614 20.971  1.00 86.85  ? 256 ASP A OD2 1 
ATOM   1734 N N   . ARG A 1 263 ? 23.692  -9.356  23.169  1.00 87.55  ? 257 ARG A N   1 
ATOM   1735 C CA  . ARG A 1 263 ? 23.364  -7.955  23.500  1.00 88.22  ? 257 ARG A CA  1 
ATOM   1736 C C   . ARG A 1 263 ? 22.867  -7.915  24.944  1.00 87.55  ? 257 ARG A C   1 
ATOM   1737 O O   . ARG A 1 263 ? 23.225  -6.979  25.679  1.00 86.15  ? 257 ARG A O   1 
ATOM   1738 C CB  . ARG A 1 263 ? 22.342  -7.429  22.494  1.00 92.72  ? 257 ARG A CB  1 
ATOM   1739 C CG  . ARG A 1 263 ? 21.545  -6.223  22.967  1.00 98.37  ? 257 ARG A CG  1 
ATOM   1740 C CD  . ARG A 1 263 ? 20.052  -6.438  22.789  1.00 104.80 ? 257 ARG A CD  1 
ATOM   1741 N NE  . ARG A 1 263 ? 19.288  -5.204  22.992  1.00 109.59 ? 257 ARG A NE  1 
ATOM   1742 C CZ  . ARG A 1 263 ? 19.255  -4.177  22.155  1.00 114.33 ? 257 ARG A CZ  1 
ATOM   1743 N NH1 . ARG A 1 263 ? 19.992  -4.181  21.058  1.00 114.82 ? 257 ARG A NH1 1 
ATOM   1744 N NH2 . ARG A 1 263 ? 18.475  -3.146  22.415  1.00 116.64 ? 257 ARG A NH2 1 
ATOM   1745 N N   . ALA A 1 264 ? 22.061  -8.900  25.324  1.00 87.38  ? 258 ALA A N   1 
ATOM   1746 C CA  . ALA A 1 264 ? 21.486  -8.932  26.686  1.00 84.78  ? 258 ALA A CA  1 
ATOM   1747 C C   . ALA A 1 264 ? 22.594  -9.062  27.723  1.00 81.98  ? 258 ALA A C   1 
ATOM   1748 O O   . ALA A 1 264 ? 22.550  -8.392  28.763  1.00 74.99  ? 258 ALA A O   1 
ATOM   1749 C CB  . ALA A 1 264 ? 20.514  -10.070 26.759  1.00 84.66  ? 258 ALA A CB  1 
ATOM   1750 N N   . ASP A 1 265 ? 23.576  -9.897  27.416  1.00 84.30  ? 259 ASP A N   1 
ATOM   1751 C CA  . ASP A 1 265 ? 24.703  -10.126 28.354  1.00 83.12  ? 259 ASP A CA  1 
ATOM   1752 C C   . ASP A 1 265 ? 25.561  -8.863  28.421  1.00 78.32  ? 259 ASP A C   1 
ATOM   1753 O O   . ASP A 1 265 ? 25.998  -8.501  29.524  1.00 72.92  ? 259 ASP A O   1 
ATOM   1754 C CB  . ASP A 1 265 ? 25.449  -11.375 27.928  1.00 84.23  ? 259 ASP A CB  1 
ATOM   1755 C CG  . ASP A 1 265 ? 24.618  -12.648 27.925  1.00 88.30  ? 259 ASP A CG  1 
ATOM   1756 O OD1 . ASP A 1 265 ? 23.606  -12.684 28.654  1.00 85.97  ? 259 ASP A OD1 1 
ATOM   1757 O OD2 . ASP A 1 265 ? 24.989  -13.589 27.195  1.00 90.34  ? 259 ASP A OD2 1 
ATOM   1758 N N   . LEU A 1 266 ? 25.770  -8.214  27.281  1.00 73.64  ? 260 LEU A N   1 
ATOM   1759 C CA  . LEU A 1 266 ? 26.572  -7.005  27.243  1.00 75.72  ? 260 LEU A CA  1 
ATOM   1760 C C   . LEU A 1 266 ? 25.912  -5.911  28.078  1.00 78.04  ? 260 LEU A C   1 
ATOM   1761 O O   . LEU A 1 266 ? 26.569  -5.249  28.881  1.00 74.36  ? 260 LEU A O   1 
ATOM   1762 C CB  . LEU A 1 266 ? 26.764  -6.570  25.785  1.00 78.45  ? 260 LEU A CB  1 
ATOM   1763 C CG  . LEU A 1 266 ? 27.793  -5.463  25.534  1.00 77.51  ? 260 LEU A CG  1 
ATOM   1764 C CD1 . LEU A 1 266 ? 28.153  -5.375  24.057  1.00 77.82  ? 260 LEU A CD1 1 
ATOM   1765 C CD2 . LEU A 1 266 ? 27.290  -4.127  25.993  1.00 74.47  ? 260 LEU A CD2 1 
ATOM   1766 N N   . ALA A 1 267 ? 24.599  -5.744  27.885  1.00 84.13  ? 261 ALA A N   1 
ATOM   1767 C CA  . ALA A 1 267 ? 23.806  -4.818  28.677  1.00 84.55  ? 261 ALA A CA  1 
ATOM   1768 C C   . ALA A 1 267 ? 23.809  -5.214  30.151  1.00 86.19  ? 261 ALA A C   1 
ATOM   1769 O O   . ALA A 1 267 ? 23.806  -4.352  31.028  1.00 85.36  ? 261 ALA A O   1 
ATOM   1770 C CB  . ALA A 1 267 ? 22.385  -4.767  28.142  1.00 84.74  ? 261 ALA A CB  1 
ATOM   1771 N N   . LYS A 1 268 ? 23.812  -6.528  30.413  1.00 89.26  ? 262 LYS A N   1 
ATOM   1772 C CA  . LYS A 1 268 ? 23.947  -7.036  31.770  1.00 92.45  ? 262 LYS A CA  1 
ATOM   1773 C C   . LYS A 1 268 ? 25.220  -6.436  32.355  1.00 90.90  ? 262 LYS A C   1 
ATOM   1774 O O   . LYS A 1 268 ? 25.165  -5.706  33.342  1.00 93.95  ? 262 LYS A O   1 
ATOM   1775 C CB  . LYS A 1 268 ? 24.014  -8.583  31.813  1.00 96.06  ? 262 LYS A CB  1 
ATOM   1776 C CG  . LYS A 1 268 ? 23.214  -9.233  32.955  1.00 98.45  ? 262 LYS A CG  1 
ATOM   1777 C CD  . LYS A 1 268 ? 21.746  -9.537  32.587  1.00 101.54 ? 262 LYS A CD  1 
ATOM   1778 C CE  . LYS A 1 268 ? 21.605  -10.623 31.528  1.00 103.09 ? 262 LYS A CE  1 
ATOM   1779 N NZ  . LYS A 1 268 ? 20.184  -10.855 31.152  1.00 101.95 ? 262 LYS A NZ  1 
ATOM   1780 N N   . TYR A 1 269 ? 26.344  -6.715  31.677  1.00 87.59  ? 263 TYR A N   1 
ATOM   1781 C CA  . TYR A 1 269 ? 27.680  -6.363  32.132  1.00 80.17  ? 263 TYR A CA  1 
ATOM   1782 C C   . TYR A 1 269 ? 27.845  -4.899  32.551  1.00 80.34  ? 263 TYR A C   1 
ATOM   1783 O O   . TYR A 1 269 ? 28.372  -4.624  33.632  1.00 77.43  ? 263 TYR A O   1 
ATOM   1784 C CB  . TYR A 1 269 ? 28.697  -6.724  31.021  1.00 77.09  ? 263 TYR A CB  1 
ATOM   1785 C CG  . TYR A 1 269 ? 30.101  -6.306  31.362  1.00 73.60  ? 263 TYR A CG  1 
ATOM   1786 C CD1 . TYR A 1 269 ? 30.909  -7.103  32.161  1.00 73.94  ? 263 TYR A CD1 1 
ATOM   1787 C CD2 . TYR A 1 269 ? 30.593  -5.076  30.957  1.00 71.34  ? 263 TYR A CD2 1 
ATOM   1788 C CE1 . TYR A 1 269 ? 32.188  -6.703  32.516  1.00 74.41  ? 263 TYR A CE1 1 
ATOM   1789 C CE2 . TYR A 1 269 ? 31.863  -4.657  31.314  1.00 73.84  ? 263 TYR A CE2 1 
ATOM   1790 C CZ  . TYR A 1 269 ? 32.664  -5.476  32.090  1.00 76.37  ? 263 TYR A CZ  1 
ATOM   1791 O OH  . TYR A 1 269 ? 33.929  -5.069  32.438  1.00 78.07  ? 263 TYR A OH  1 
ATOM   1792 N N   . ILE A 1 270 ? 27.396  -3.967  31.694  1.00 80.36  ? 264 ILE A N   1 
ATOM   1793 C CA  . ILE A 1 270 ? 27.588  -2.539  31.928  1.00 82.33  ? 264 ILE A CA  1 
ATOM   1794 C C   . ILE A 1 270 ? 26.982  -2.104  33.263  1.00 83.86  ? 264 ILE A C   1 
ATOM   1795 O O   . ILE A 1 270 ? 27.672  -1.569  34.132  1.00 80.49  ? 264 ILE A O   1 
ATOM   1796 C CB  . ILE A 1 270 ? 27.011  -1.658  30.752  1.00 80.58  ? 264 ILE A CB  1 
ATOM   1797 C CG1 . ILE A 1 270 ? 27.982  -1.570  29.568  1.00 78.53  ? 264 ILE A CG1 1 
ATOM   1798 C CG2 . ILE A 1 270 ? 26.633  -0.232  31.207  1.00 80.63  ? 264 ILE A CG2 1 
ATOM   1799 C CD1 . ILE A 1 270 ? 27.995  -2.657  28.783  1.00 79.54  ? 264 ILE A CD1 1 
ATOM   1800 N N   . CYS A 1 271 ? 25.676  -2.348  33.404  1.00 87.73  ? 265 CYS A N   1 
ATOM   1801 C CA  . CYS A 1 271 ? 24.911  -1.889  34.551  1.00 91.55  ? 265 CYS A CA  1 
ATOM   1802 C C   . CYS A 1 271 ? 25.509  -2.429  35.847  1.00 91.34  ? 265 CYS A C   1 
ATOM   1803 O O   . CYS A 1 271 ? 25.523  -1.734  36.860  1.00 92.89  ? 265 CYS A O   1 
ATOM   1804 C CB  . CYS A 1 271 ? 23.445  -2.281  34.391  1.00 94.98  ? 265 CYS A CB  1 
ATOM   1805 S SG  . CYS A 1 271 ? 22.743  -1.891  32.756  1.00 95.17  ? 265 CYS A SG  1 
ATOM   1806 N N   . GLU A 1 272 ? 26.027  -3.664  35.789  1.00 90.14  ? 266 GLU A N   1 
ATOM   1807 C CA  . GLU A 1 272 ? 26.701  -4.283  36.920  1.00 89.01  ? 266 GLU A CA  1 
ATOM   1808 C C   . GLU A 1 272 ? 28.003  -3.571  37.278  1.00 85.49  ? 266 GLU A C   1 
ATOM   1809 O O   . GLU A 1 272 ? 28.394  -3.528  38.443  1.00 76.85  ? 266 GLU A O   1 
ATOM   1810 C CB  . GLU A 1 272 ? 27.029  -5.740  36.605  1.00 91.59  ? 266 GLU A CB  1 
ATOM   1811 C CG  . GLU A 1 272 ? 25.831  -6.599  36.260  1.00 96.78  ? 266 GLU A CG  1 
ATOM   1812 C CD  . GLU A 1 272 ? 26.200  -7.847  35.485  1.00 103.59 ? 266 GLU A CD  1 
ATOM   1813 O OE1 . GLU A 1 272 ? 27.413  -8.142  35.379  1.00 110.10 ? 266 GLU A OE1 1 
ATOM   1814 O OE2 . GLU A 1 272 ? 25.281  -8.523  34.970  1.00 105.65 ? 266 GLU A OE2 1 
ATOM   1815 N N   . ASN A 1 273 ? 28.679  -3.033  36.256  1.00 83.44  ? 267 ASN A N   1 
ATOM   1816 C CA  . ASN A 1 273 ? 30.022  -2.507  36.426  1.00 82.61  ? 267 ASN A CA  1 
ATOM   1817 C C   . ASN A 1 273 ? 30.134  -1.009  36.155  1.00 81.93  ? 267 ASN A C   1 
ATOM   1818 O O   . ASN A 1 273 ? 31.230  -0.516  35.892  1.00 81.74  ? 267 ASN A O   1 
ATOM   1819 C CB  . ASN A 1 273 ? 30.959  -3.309  35.538  1.00 79.20  ? 267 ASN A CB  1 
ATOM   1820 C CG  . ASN A 1 273 ? 31.117  -4.720  36.031  1.00 77.81  ? 267 ASN A CG  1 
ATOM   1821 O OD1 . ASN A 1 273 ? 31.835  -4.979  37.008  1.00 79.28  ? 267 ASN A OD1 1 
ATOM   1822 N ND2 . ASN A 1 273 ? 30.463  -5.669  35.372  1.00 76.86  ? 267 ASN A ND2 1 
ATOM   1823 N N   . GLN A 1 274 ? 29.004  -0.294  36.276  1.00 81.73  ? 268 GLN A N   1 
ATOM   1824 C CA  . GLN A 1 274 ? 28.942  1.150   36.083  1.00 83.32  ? 268 GLN A CA  1 
ATOM   1825 C C   . GLN A 1 274 ? 30.105  1.932   36.686  1.00 84.00  ? 268 GLN A C   1 
ATOM   1826 O O   . GLN A 1 274 ? 30.568  2.902   36.091  1.00 80.70  ? 268 GLN A O   1 
ATOM   1827 C CB  . GLN A 1 274 ? 27.665  1.709   36.706  1.00 85.64  ? 268 GLN A CB  1 
ATOM   1828 C CG  . GLN A 1 274 ? 26.420  1.417   35.899  1.00 88.51  ? 268 GLN A CG  1 
ATOM   1829 C CD  . GLN A 1 274 ? 25.185  1.832   36.646  1.00 87.69  ? 268 GLN A CD  1 
ATOM   1830 O OE1 . GLN A 1 274 ? 25.088  2.952   37.161  1.00 85.05  ? 268 GLN A OE1 1 
ATOM   1831 N NE2 . GLN A 1 274 ? 24.225  0.932   36.740  1.00 89.98  ? 268 GLN A NE2 1 
ATOM   1832 N N   . ASP A 1 275 ? 30.542  1.505   37.879  1.00 88.76  ? 269 ASP A N   1 
ATOM   1833 C CA  . ASP A 1 275 ? 31.666  2.105   38.587  1.00 91.31  ? 269 ASP A CA  1 
ATOM   1834 C C   . ASP A 1 275 ? 32.843  2.426   37.668  1.00 87.39  ? 269 ASP A C   1 
ATOM   1835 O O   . ASP A 1 275 ? 33.514  3.441   37.853  1.00 83.45  ? 269 ASP A O   1 
ATOM   1836 C CB  . ASP A 1 275 ? 32.176  1.163   39.707  1.00 96.97  ? 269 ASP A CB  1 
ATOM   1837 C CG  . ASP A 1 275 ? 31.106  0.467   40.544  1.00 103.74 ? 269 ASP A CG  1 
ATOM   1838 O OD1 . ASP A 1 275 ? 29.901  0.770   40.349  1.00 104.39 ? 269 ASP A OD1 1 
ATOM   1839 O OD2 . ASP A 1 275 ? 31.473  -0.400  41.378  1.00 106.76 ? 269 ASP A OD2 1 
ATOM   1840 N N   . SER A 1 276 ? 33.080  1.544   36.685  1.00 84.59  ? 270 SER A N   1 
ATOM   1841 C CA  . SER A 1 276 ? 34.251  1.617   35.826  1.00 82.12  ? 270 SER A CA  1 
ATOM   1842 C C   . SER A 1 276 ? 33.954  2.027   34.382  1.00 77.12  ? 270 SER A C   1 
ATOM   1843 O O   . SER A 1 276 ? 34.816  1.879   33.519  1.00 75.08  ? 270 SER A O   1 
ATOM   1844 C CB  . SER A 1 276 ? 34.959  0.261   35.835  1.00 85.20  ? 270 SER A CB  1 
ATOM   1845 O OG  . SER A 1 276 ? 34.193  -0.741  35.181  1.00 87.30  ? 270 SER A OG  1 
ATOM   1846 N N   . ILE A 1 277 ? 32.751  2.559   34.120  1.00 73.96  ? 271 ILE A N   1 
ATOM   1847 C CA  . ILE A 1 277 ? 32.319  2.823   32.752  1.00 70.48  ? 271 ILE A CA  1 
ATOM   1848 C C   . ILE A 1 277 ? 31.883  4.274   32.539  1.00 70.99  ? 271 ILE A C   1 
ATOM   1849 O O   . ILE A 1 277 ? 32.571  5.034   31.854  1.00 67.23  ? 271 ILE A O   1 
ATOM   1850 C CB  . ILE A 1 277 ? 31.234  1.780   32.358  1.00 65.08  ? 271 ILE A CB  1 
ATOM   1851 C CG1 . ILE A 1 277 ? 31.775  0.334   32.643  1.00 63.02  ? 271 ILE A CG1 1 
ATOM   1852 C CG2 . ILE A 1 277 ? 30.783  1.977   30.913  1.00 65.01  ? 271 ILE A CG2 1 
ATOM   1853 C CD1 . ILE A 1 277 ? 31.047  -0.811  32.003  1.00 61.80  ? 271 ILE A CD1 1 
ATOM   1854 N N   . SER A 1 278 ? 30.748  4.654   33.142  1.00 73.31  ? 272 SER A N   1 
ATOM   1855 C CA  . SER A 1 278 ? 30.193  5.987   32.969  1.00 74.38  ? 272 SER A CA  1 
ATOM   1856 C C   . SER A 1 278 ? 29.234  6.372   34.092  1.00 77.42  ? 272 SER A C   1 
ATOM   1857 O O   . SER A 1 278 ? 28.445  5.543   34.548  1.00 78.29  ? 272 SER A O   1 
ATOM   1858 C CB  . SER A 1 278 ? 29.454  6.086   31.640  1.00 74.62  ? 272 SER A CB  1 
ATOM   1859 O OG  . SER A 1 278 ? 29.048  7.421   31.389  1.00 72.96  ? 272 SER A OG  1 
ATOM   1860 N N   . SER A 1 279 ? 29.287  7.656   34.483  1.00 79.07  ? 273 SER A N   1 
ATOM   1861 C CA  . SER A 1 279 ? 28.406  8.220   35.495  1.00 78.13  ? 273 SER A CA  1 
ATOM   1862 C C   . SER A 1 279 ? 27.076  8.688   34.906  1.00 79.75  ? 273 SER A C   1 
ATOM   1863 O O   . SER A 1 279 ? 26.327  9.409   35.562  1.00 81.06  ? 273 SER A O   1 
ATOM   1864 C CB  . SER A 1 279 ? 29.101  9.373   36.221  1.00 77.78  ? 273 SER A CB  1 
ATOM   1865 O OG  . SER A 1 279 ? 29.464  10.430  35.348  1.00 77.59  ? 273 SER A OG  1 
ATOM   1866 N N   . LYS A 1 280 ? 26.793  8.246   33.673  1.00 81.94  ? 274 LYS A N   1 
ATOM   1867 C CA  . LYS A 1 280 ? 25.564  8.553   32.959  1.00 81.51  ? 274 LYS A CA  1 
ATOM   1868 C C   . LYS A 1 280 ? 24.689  7.318   32.744  1.00 79.01  ? 274 LYS A C   1 
ATOM   1869 O O   . LYS A 1 280 ? 23.773  7.343   31.928  1.00 77.94  ? 274 LYS A O   1 
ATOM   1870 C CB  . LYS A 1 280 ? 25.916  9.140   31.583  1.00 80.18  ? 274 LYS A CB  1 
ATOM   1871 C CG  . LYS A 1 280 ? 26.758  10.399  31.625  1.00 78.78  ? 274 LYS A CG  1 
ATOM   1872 C CD  . LYS A 1 280 ? 26.010  11.565  32.181  1.00 79.76  ? 274 LYS A CD  1 
ATOM   1873 C CE  . LYS A 1 280 ? 26.611  12.881  31.763  1.00 82.80  ? 274 LYS A CE  1 
ATOM   1874 N NZ  . LYS A 1 280 ? 27.918  13.143  32.417  1.00 83.59  ? 274 LYS A NZ  1 
ATOM   1875 N N   . LEU A 1 281 ? 24.979  6.237   33.471  1.00 78.82  ? 275 LEU A N   1 
ATOM   1876 C CA  . LEU A 1 281 ? 24.382  4.947   33.170  1.00 83.92  ? 275 LEU A CA  1 
ATOM   1877 C C   . LEU A 1 281 ? 23.235  4.589   34.109  1.00 89.01  ? 275 LEU A C   1 
ATOM   1878 O O   . LEU A 1 281 ? 22.518  3.626   33.844  1.00 88.55  ? 275 LEU A O   1 
ATOM   1879 C CB  . LEU A 1 281 ? 25.467  3.869   33.246  1.00 85.48  ? 275 LEU A CB  1 
ATOM   1880 C CG  . LEU A 1 281 ? 26.311  3.692   31.992  1.00 87.14  ? 275 LEU A CG  1 
ATOM   1881 C CD1 . LEU A 1 281 ? 27.555  2.857   32.292  1.00 86.93  ? 275 LEU A CD1 1 
ATOM   1882 C CD2 . LEU A 1 281 ? 25.494  3.062   30.877  1.00 85.07  ? 275 LEU A CD2 1 
ATOM   1883 N N   . LYS A 1 282 ? 23.055  5.376   35.180  1.00 88.97  ? 276 LYS A N   1 
ATOM   1884 C CA  . LYS A 1 282 ? 22.176  4.992   36.273  1.00 93.48  ? 276 LYS A CA  1 
ATOM   1885 C C   . LYS A 1 282 ? 20.739  4.751   35.825  1.00 99.39  ? 276 LYS A C   1 
ATOM   1886 O O   . LYS A 1 282 ? 20.197  3.672   36.055  1.00 99.35  ? 276 LYS A O   1 
ATOM   1887 C CB  . LYS A 1 282 ? 22.175  6.051   37.373  1.00 93.90  ? 276 LYS A CB  1 
ATOM   1888 C CG  . LYS A 1 282 ? 21.395  5.608   38.600  1.00 94.55  ? 276 LYS A CG  1 
ATOM   1889 C CD  . LYS A 1 282 ? 21.508  6.584   39.737  1.00 95.83  ? 276 LYS A CD  1 
ATOM   1890 C CE  . LYS A 1 282 ? 20.746  6.117   40.944  1.00 96.79  ? 276 LYS A CE  1 
ATOM   1891 N NZ  . LYS A 1 282 ? 20.780  7.131   42.023  1.00 97.43  ? 276 LYS A NZ  1 
ATOM   1892 N N   . GLU A 1 283 ? 20.144  5.772   35.192  1.00 107.40 ? 277 GLU A N   1 
ATOM   1893 C CA  . GLU A 1 283 ? 18.758  5.735   34.749  1.00 111.07 ? 277 GLU A CA  1 
ATOM   1894 C C   . GLU A 1 283 ? 18.559  4.658   33.685  1.00 110.84 ? 277 GLU A C   1 
ATOM   1895 O O   . GLU A 1 283 ? 17.710  3.781   33.836  1.00 109.92 ? 277 GLU A O   1 
ATOM   1896 C CB  . GLU A 1 283 ? 18.330  7.124   34.222  1.00 115.67 ? 277 GLU A CB  1 
ATOM   1897 C CG  . GLU A 1 283 ? 16.851  7.230   33.873  1.00 119.94 ? 277 GLU A CG  1 
ATOM   1898 C CD  . GLU A 1 283 ? 16.333  8.632   33.598  1.00 124.35 ? 277 GLU A CD  1 
ATOM   1899 O OE1 . GLU A 1 283 ? 17.148  9.583   33.564  1.00 127.76 ? 277 GLU A OE1 1 
ATOM   1900 O OE2 . GLU A 1 283 ? 15.100  8.777   33.427  1.00 123.38 ? 277 GLU A OE2 1 
ATOM   1901 N N   . CYS A 1 284 ? 19.364  4.718   32.618  1.00 111.34 ? 278 CYS A N   1 
ATOM   1902 C CA  . CYS A 1 284 ? 19.395  3.662   31.619  1.00 111.81 ? 278 CYS A CA  1 
ATOM   1903 C C   . CYS A 1 284 ? 19.281  2.306   32.307  1.00 113.01 ? 278 CYS A C   1 
ATOM   1904 O O   . CYS A 1 284 ? 18.494  1.460   31.890  1.00 112.80 ? 278 CYS A O   1 
ATOM   1905 C CB  . CYS A 1 284 ? 20.672  3.739   30.789  1.00 113.88 ? 278 CYS A CB  1 
ATOM   1906 S SG  . CYS A 1 284 ? 21.047  5.391   30.158  1.00 120.31 ? 278 CYS A SG  1 
ATOM   1907 N N   . CYS A 1 285 ? 20.063  2.150   33.384  1.00 112.38 ? 279 CYS A N   1 
ATOM   1908 C CA  . CYS A 1 285 ? 20.250  0.887   34.077  1.00 110.23 ? 279 CYS A CA  1 
ATOM   1909 C C   . CYS A 1 285 ? 19.276  0.642   35.229  1.00 111.32 ? 279 CYS A C   1 
ATOM   1910 O O   . CYS A 1 285 ? 19.593  -0.120  36.144  1.00 112.00 ? 279 CYS A O   1 
ATOM   1911 C CB  . CYS A 1 285 ? 21.693  0.812   34.566  1.00 107.77 ? 279 CYS A CB  1 
ATOM   1912 S SG  . CYS A 1 285 ? 22.924  1.068   33.265  1.00 103.73 ? 279 CYS A SG  1 
ATOM   1913 N N   . GLU A 1 286 ? 18.094  1.271   35.177  1.00 111.42 ? 280 GLU A N   1 
ATOM   1914 C CA  . GLU A 1 286 ? 16.980  0.898   36.041  1.00 110.37 ? 280 GLU A CA  1 
ATOM   1915 C C   . GLU A 1 286 ? 15.737  0.490   35.244  1.00 108.46 ? 280 GLU A C   1 
ATOM   1916 O O   . GLU A 1 286 ? 14.713  0.148   35.829  1.00 105.59 ? 280 GLU A O   1 
ATOM   1917 C CB  . GLU A 1 286 ? 16.655  2.050   37.017  1.00 108.00 ? 280 GLU A CB  1 
ATOM   1918 C CG  . GLU A 1 286 ? 17.750  2.282   38.049  1.00 107.58 ? 280 GLU A CG  1 
ATOM   1919 C CD  . GLU A 1 286 ? 17.569  3.489   38.951  1.00 108.48 ? 280 GLU A CD  1 
ATOM   1920 O OE1 . GLU A 1 286 ? 17.428  4.614   38.420  1.00 108.78 ? 280 GLU A OE1 1 
ATOM   1921 O OE2 . GLU A 1 286 ? 17.591  3.314   40.190  1.00 109.66 ? 280 GLU A OE2 1 
ATOM   1922 N N   . LYS A 1 287 ? 15.853  0.489   33.909  1.00 109.51 ? 281 LYS A N   1 
ATOM   1923 C CA  . LYS A 1 287 ? 14.741  0.211   33.016  1.00 112.30 ? 281 LYS A CA  1 
ATOM   1924 C C   . LYS A 1 287 ? 14.576  -1.287  32.771  1.00 112.22 ? 281 LYS A C   1 
ATOM   1925 O O   . LYS A 1 287 ? 15.382  -2.077  33.249  1.00 110.32 ? 281 LYS A O   1 
ATOM   1926 C CB  . LYS A 1 287 ? 14.968  0.951   31.681  1.00 116.55 ? 281 LYS A CB  1 
ATOM   1927 C CG  . LYS A 1 287 ? 15.096  2.474   31.830  1.00 117.43 ? 281 LYS A CG  1 
ATOM   1928 C CD  . LYS A 1 287 ? 14.672  3.243   30.562  1.00 116.96 ? 281 LYS A CD  1 
ATOM   1929 C CE  . LYS A 1 287 ? 14.470  4.720   30.811  1.00 115.51 ? 281 LYS A CE  1 
ATOM   1930 N NZ  . LYS A 1 287 ? 13.664  5.353   29.733  1.00 115.26 ? 281 LYS A NZ  1 
ATOM   1931 N N   . PRO A 1 288 ? 13.505  -1.729  32.066  1.00 118.95 ? 282 PRO A N   1 
ATOM   1932 C CA  . PRO A 1 288 ? 13.419  -3.102  31.555  1.00 120.73 ? 282 PRO A CA  1 
ATOM   1933 C C   . PRO A 1 288 ? 14.388  -3.382  30.409  1.00 117.87 ? 282 PRO A C   1 
ATOM   1934 O O   . PRO A 1 288 ? 14.924  -2.452  29.813  1.00 115.75 ? 282 PRO A O   1 
ATOM   1935 C CB  . PRO A 1 288 ? 11.958  -3.222  31.086  1.00 124.42 ? 282 PRO A CB  1 
ATOM   1936 C CG  . PRO A 1 288 ? 11.240  -2.022  31.676  1.00 124.49 ? 282 PRO A CG  1 
ATOM   1937 C CD  . PRO A 1 288 ? 12.280  -0.956  31.802  1.00 123.11 ? 282 PRO A CD  1 
ATOM   1938 N N   . LEU A 1 289 ? 14.557  -4.669  30.078  1.00 118.46 ? 283 LEU A N   1 
ATOM   1939 C CA  . LEU A 1 289 ? 15.725  -5.133  29.342  1.00 120.49 ? 283 LEU A CA  1 
ATOM   1940 C C   . LEU A 1 289 ? 15.877  -4.494  27.961  1.00 120.51 ? 283 LEU A C   1 
ATOM   1941 O O   . LEU A 1 289 ? 16.933  -3.939  27.663  1.00 122.27 ? 283 LEU A O   1 
ATOM   1942 C CB  . LEU A 1 289 ? 15.743  -6.690  29.247  1.00 120.86 ? 283 LEU A CB  1 
ATOM   1943 C CG  . LEU A 1 289 ? 14.627  -7.398  28.457  1.00 121.43 ? 283 LEU A CG  1 
ATOM   1944 C CD1 . LEU A 1 289 ? 14.935  -7.463  26.980  1.00 120.81 ? 283 LEU A CD1 1 
ATOM   1945 C CD2 . LEU A 1 289 ? 14.383  -8.808  28.976  1.00 121.84 ? 283 LEU A CD2 1 
ATOM   1946 N N   . LEU A 1 290 ? 14.827  -4.550  27.131  1.00 119.43 ? 284 LEU A N   1 
ATOM   1947 C CA  . LEU A 1 290 ? 14.918  -4.059  25.762  1.00 114.97 ? 284 LEU A CA  1 
ATOM   1948 C C   . LEU A 1 290 ? 15.030  -2.538  25.736  1.00 110.22 ? 284 LEU A C   1 
ATOM   1949 O O   . LEU A 1 290 ? 15.586  -1.976  24.795  1.00 105.28 ? 284 LEU A O   1 
ATOM   1950 C CB  . LEU A 1 290 ? 13.715  -4.493  24.903  1.00 114.19 ? 284 LEU A CB  1 
ATOM   1951 C CG  . LEU A 1 290 ? 13.984  -5.398  23.683  1.00 113.08 ? 284 LEU A CG  1 
ATOM   1952 C CD1 . LEU A 1 290 ? 15.299  -5.047  23.008  1.00 112.64 ? 284 LEU A CD1 1 
ATOM   1953 C CD2 . LEU A 1 290 ? 13.928  -6.878  24.034  1.00 110.05 ? 284 LEU A CD2 1 
ATOM   1954 N N   . GLU A 1 291 ? 14.482  -1.895  26.774  1.00 109.04 ? 285 GLU A N   1 
ATOM   1955 C CA  . GLU A 1 291 ? 14.581  -0.456  26.945  1.00 108.81 ? 285 GLU A CA  1 
ATOM   1956 C C   . GLU A 1 291 ? 15.958  -0.089  27.490  1.00 108.29 ? 285 GLU A C   1 
ATOM   1957 O O   . GLU A 1 291 ? 16.618  0.805   26.965  1.00 107.66 ? 285 GLU A O   1 
ATOM   1958 C CB  . GLU A 1 291 ? 13.476  0.057   27.884  1.00 110.02 ? 285 GLU A CB  1 
ATOM   1959 C CG  . GLU A 1 291 ? 12.067  -0.295  27.428  1.00 110.85 ? 285 GLU A CG  1 
ATOM   1960 C CD  . GLU A 1 291 ? 10.949  0.325   28.246  1.00 111.44 ? 285 GLU A CD  1 
ATOM   1961 O OE1 . GLU A 1 291 ? 11.211  1.287   29.004  1.00 109.11 ? 285 GLU A OE1 1 
ATOM   1962 O OE2 . GLU A 1 291 ? 9.806   -0.172  28.141  1.00 113.65 ? 285 GLU A OE2 1 
ATOM   1963 N N   . LYS A 1 292 ? 16.379  -0.794  28.548  1.00 107.05 ? 286 LYS A N   1 
ATOM   1964 C CA  . LYS A 1 292 ? 17.689  -0.605  29.150  1.00 101.61 ? 286 LYS A CA  1 
ATOM   1965 C C   . LYS A 1 292 ? 18.803  -0.704  28.108  1.00 101.03 ? 286 LYS A C   1 
ATOM   1966 O O   . LYS A 1 292 ? 19.705  0.132   28.088  1.00 101.59 ? 286 LYS A O   1 
ATOM   1967 C CB  . LYS A 1 292 ? 17.912  -1.647  30.256  1.00 98.11  ? 286 LYS A CB  1 
ATOM   1968 C CG  . LYS A 1 292 ? 19.222  -1.499  31.018  1.00 96.90  ? 286 LYS A CG  1 
ATOM   1969 C CD  . LYS A 1 292 ? 19.518  -2.676  31.947  1.00 96.56  ? 286 LYS A CD  1 
ATOM   1970 C CE  . LYS A 1 292 ? 18.450  -2.957  32.969  1.00 96.17  ? 286 LYS A CE  1 
ATOM   1971 N NZ  . LYS A 1 292 ? 18.213  -1.795  33.850  1.00 95.68  ? 286 LYS A NZ  1 
ATOM   1972 N N   . SER A 1 293 ? 18.722  -1.727  27.247  1.00 97.85  ? 287 SER A N   1 
ATOM   1973 C CA  . SER A 1 293 ? 19.753  -1.985  26.255  1.00 96.17  ? 287 SER A CA  1 
ATOM   1974 C C   . SER A 1 293 ? 19.796  -0.895  25.186  1.00 99.39  ? 287 SER A C   1 
ATOM   1975 O O   . SER A 1 293 ? 20.784  -0.168  25.077  1.00 100.00 ? 287 SER A O   1 
ATOM   1976 C CB  . SER A 1 293 ? 19.573  -3.361  25.628  1.00 93.93  ? 287 SER A CB  1 
ATOM   1977 O OG  . SER A 1 293 ? 18.233  -3.583  25.226  1.00 94.59  ? 287 SER A OG  1 
ATOM   1978 N N   . HIS A 1 294 ? 18.700  -0.775  24.422  1.00 102.33 ? 288 HIS A N   1 
ATOM   1979 C CA  . HIS A 1 294 ? 18.531  0.286   23.440  1.00 96.44  ? 288 HIS A CA  1 
ATOM   1980 C C   . HIS A 1 294 ? 18.964  1.629   24.028  1.00 95.91  ? 288 HIS A C   1 
ATOM   1981 O O   . HIS A 1 294 ? 19.504  2.475   23.318  1.00 101.55 ? 288 HIS A O   1 
ATOM   1982 C CB  . HIS A 1 294 ? 17.058  0.341   22.967  1.00 95.10  ? 288 HIS A CB  1 
ATOM   1983 C CG  . HIS A 1 294 ? 16.819  1.142   21.720  1.00 93.38  ? 288 HIS A CG  1 
ATOM   1984 N ND1 . HIS A 1 294 ? 16.273  2.419   21.767  1.00 89.51  ? 288 HIS A ND1 1 
ATOM   1985 C CD2 . HIS A 1 294 ? 17.066  0.827   20.429  1.00 93.08  ? 288 HIS A CD2 1 
ATOM   1986 C CE1 . HIS A 1 294 ? 16.206  2.841   20.511  1.00 88.92  ? 288 HIS A CE1 1 
ATOM   1987 N NE2 . HIS A 1 294 ? 16.674  1.910   19.669  1.00 91.46  ? 288 HIS A NE2 1 
ATOM   1988 N N   . CYS A 1 295 ? 18.737  1.807   25.335  1.00 92.31  ? 289 CYS A N   1 
ATOM   1989 C CA  . CYS A 1 295 ? 19.062  3.047   26.017  1.00 92.76  ? 289 CYS A CA  1 
ATOM   1990 C C   . CYS A 1 295 ? 20.562  3.310   26.145  1.00 92.92  ? 289 CYS A C   1 
ATOM   1991 O O   . CYS A 1 295 ? 20.973  4.469   26.114  1.00 94.12  ? 289 CYS A O   1 
ATOM   1992 C CB  . CYS A 1 295 ? 18.384  3.093   27.383  1.00 91.68  ? 289 CYS A CB  1 
ATOM   1993 S SG  . CYS A 1 295 ? 18.561  4.678   28.230  1.00 98.50  ? 289 CYS A SG  1 
ATOM   1994 N N   . ILE A 1 296 ? 21.374  2.254   26.314  1.00 91.21  ? 290 ILE A N   1 
ATOM   1995 C CA  . ILE A 1 296 ? 22.813  2.446   26.442  1.00 88.74  ? 290 ILE A CA  1 
ATOM   1996 C C   . ILE A 1 296 ? 23.416  2.760   25.072  1.00 83.49  ? 290 ILE A C   1 
ATOM   1997 O O   . ILE A 1 296 ? 24.414  3.467   24.981  1.00 77.43  ? 290 ILE A O   1 
ATOM   1998 C CB  . ILE A 1 296 ? 23.595  1.296   27.163  1.00 87.79  ? 290 ILE A CB  1 
ATOM   1999 C CG1 . ILE A 1 296 ? 23.688  -0.011  26.328  1.00 88.65  ? 290 ILE A CG1 1 
ATOM   2000 C CG2 . ILE A 1 296 ? 23.029  1.071   28.586  1.00 86.54  ? 290 ILE A CG2 1 
ATOM   2001 C CD1 . ILE A 1 296 ? 22.941  -1.178  26.854  1.00 88.73  ? 290 ILE A CD1 1 
ATOM   2002 N N   . ALA A 1 297 ? 22.789  2.259   24.003  1.00 82.42  ? 291 ALA A N   1 
ATOM   2003 C CA  . ALA A 1 297 ? 23.154  2.685   22.664  1.00 82.42  ? 291 ALA A CA  1 
ATOM   2004 C C   . ALA A 1 297 ? 23.055  4.207   22.547  1.00 86.48  ? 291 ALA A C   1 
ATOM   2005 O O   . ALA A 1 297 ? 23.937  4.835   21.961  1.00 88.77  ? 291 ALA A O   1 
ATOM   2006 C CB  . ALA A 1 297 ? 22.282  2.003   21.627  1.00 79.20  ? 291 ALA A CB  1 
ATOM   2007 N N   . GLU A 1 298 ? 22.001  4.786   23.144  1.00 88.22  ? 292 GLU A N   1 
ATOM   2008 C CA  . GLU A 1 298 ? 21.710  6.210   23.030  1.00 91.30  ? 292 GLU A CA  1 
ATOM   2009 C C   . GLU A 1 298 ? 22.313  7.109   24.112  1.00 90.23  ? 292 GLU A C   1 
ATOM   2010 O O   . GLU A 1 298 ? 22.240  8.330   23.977  1.00 92.77  ? 292 GLU A O   1 
ATOM   2011 C CB  . GLU A 1 298 ? 20.166  6.458   23.021  1.00 96.45  ? 292 GLU A CB  1 
ATOM   2012 C CG  . GLU A 1 298 ? 19.448  6.203   21.693  1.00 98.95  ? 292 GLU A CG  1 
ATOM   2013 C CD  . GLU A 1 298 ? 18.093  6.895   21.548  1.00 100.12 ? 292 GLU A CD  1 
ATOM   2014 O OE1 . GLU A 1 298 ? 17.248  6.757   22.463  1.00 100.78 ? 292 GLU A OE1 1 
ATOM   2015 O OE2 . GLU A 1 298 ? 17.874  7.572   20.515  1.00 95.59  ? 292 GLU A OE2 1 
ATOM   2016 N N   . VAL A 1 299 ? 22.890  6.531   25.179  1.00 87.85  ? 293 VAL A N   1 
ATOM   2017 C CA  . VAL A 1 299 ? 23.406  7.325   26.292  1.00 87.42  ? 293 VAL A CA  1 
ATOM   2018 C C   . VAL A 1 299 ? 24.431  8.355   25.816  1.00 84.45  ? 293 VAL A C   1 
ATOM   2019 O O   . VAL A 1 299 ? 25.260  8.055   24.962  1.00 85.86  ? 293 VAL A O   1 
ATOM   2020 C CB  . VAL A 1 299 ? 24.006  6.446   27.425  1.00 88.47  ? 293 VAL A CB  1 
ATOM   2021 C CG1 . VAL A 1 299 ? 25.083  5.500   26.904  1.00 90.12  ? 293 VAL A CG1 1 
ATOM   2022 C CG2 . VAL A 1 299 ? 24.551  7.296   28.570  1.00 86.12  ? 293 VAL A CG2 1 
ATOM   2023 N N   . GLU A 1 300 ? 24.370  9.570   26.374  1.00 82.88  ? 294 GLU A N   1 
ATOM   2024 C CA  . GLU A 1 300 ? 25.243  10.647  25.937  1.00 85.08  ? 294 GLU A CA  1 
ATOM   2025 C C   . GLU A 1 300 ? 26.654  10.482  26.504  1.00 85.39  ? 294 GLU A C   1 
ATOM   2026 O O   . GLU A 1 300 ? 26.916  9.599   27.323  1.00 84.14  ? 294 GLU A O   1 
ATOM   2027 C CB  . GLU A 1 300 ? 24.656  12.041  26.290  1.00 86.22  ? 294 GLU A CB  1 
ATOM   2028 C CG  . GLU A 1 300 ? 24.746  12.475  27.746  1.00 90.24  ? 294 GLU A CG  1 
ATOM   2029 C CD  . GLU A 1 300 ? 23.728  11.861  28.690  1.00 95.41  ? 294 GLU A CD  1 
ATOM   2030 O OE1 . GLU A 1 300 ? 22.999  10.934  28.265  1.00 95.77  ? 294 GLU A OE1 1 
ATOM   2031 O OE2 . GLU A 1 300 ? 23.652  12.319  29.855  1.00 96.97  ? 294 GLU A OE2 1 
ATOM   2032 N N   . ASN A 1 301 ? 27.564  11.342  26.033  1.00 82.12  ? 295 ASN A N   1 
ATOM   2033 C CA  . ASN A 1 301 ? 28.962  11.299  26.427  1.00 77.89  ? 295 ASN A CA  1 
ATOM   2034 C C   . ASN A 1 301 ? 29.165  11.724  27.878  1.00 80.40  ? 295 ASN A C   1 
ATOM   2035 O O   . ASN A 1 301 ? 28.620  12.739  28.308  1.00 82.52  ? 295 ASN A O   1 
ATOM   2036 C CB  . ASN A 1 301 ? 29.789  12.201  25.514  1.00 72.89  ? 295 ASN A CB  1 
ATOM   2037 C CG  . ASN A 1 301 ? 29.958  11.667  24.111  1.00 68.63  ? 295 ASN A CG  1 
ATOM   2038 O OD1 . ASN A 1 301 ? 29.491  10.563  23.741  1.00 65.09  ? 295 ASN A OD1 1 
ATOM   2039 N ND2 . ASN A 1 301 ? 30.652  12.446  23.308  1.00 64.52  ? 295 ASN A ND2 1 
ATOM   2040 N N   . ASP A 1 302 ? 29.966  10.941  28.616  1.00 79.30  ? 296 ASP A N   1 
ATOM   2041 C CA  . ASP A 1 302 ? 30.341  11.279  29.978  1.00 75.79  ? 296 ASP A CA  1 
ATOM   2042 C C   . ASP A 1 302 ? 31.433  12.343  29.939  1.00 76.18  ? 296 ASP A C   1 
ATOM   2043 O O   . ASP A 1 302 ? 32.114  12.500  28.922  1.00 75.24  ? 296 ASP A O   1 
ATOM   2044 C CB  . ASP A 1 302 ? 30.803  10.026  30.722  1.00 75.87  ? 296 ASP A CB  1 
ATOM   2045 C CG  . ASP A 1 302 ? 31.124  10.250  32.179  1.00 77.45  ? 296 ASP A CG  1 
ATOM   2046 O OD1 . ASP A 1 302 ? 30.245  10.743  32.907  1.00 80.39  ? 296 ASP A OD1 1 
ATOM   2047 O OD2 . ASP A 1 302 ? 32.255  9.942   32.588  1.00 78.06  ? 296 ASP A OD2 1 
ATOM   2048 N N   . GLU A 1 303 ? 31.578  13.080  31.045  1.00 78.42  ? 297 GLU A N   1 
ATOM   2049 C CA  . GLU A 1 303 ? 32.622  14.086  31.146  1.00 84.76  ? 297 GLU A CA  1 
ATOM   2050 C C   . GLU A 1 303 ? 33.969  13.380  31.253  1.00 85.29  ? 297 GLU A C   1 
ATOM   2051 O O   . GLU A 1 303 ? 34.047  12.244  31.721  1.00 80.52  ? 297 GLU A O   1 
ATOM   2052 C CB  . GLU A 1 303 ? 32.477  15.034  32.358  1.00 88.59  ? 297 GLU A CB  1 
ATOM   2053 C CG  . GLU A 1 303 ? 31.065  15.453  32.726  1.00 91.79  ? 297 GLU A CG  1 
ATOM   2054 C CD  . GLU A 1 303 ? 30.365  14.551  33.728  1.00 94.37  ? 297 GLU A CD  1 
ATOM   2055 O OE1 . GLU A 1 303 ? 30.777  13.377  33.886  1.00 92.49  ? 297 GLU A OE1 1 
ATOM   2056 O OE2 . GLU A 1 303 ? 29.406  15.034  34.372  1.00 99.51  ? 297 GLU A OE2 1 
ATOM   2057 N N   . MET A 1 304 ? 35.000  14.069  30.777  1.00 88.77  ? 298 MET A N   1 
ATOM   2058 C CA  . MET A 1 304 ? 36.361  13.499  30.794  1.00 91.42  ? 298 MET A CA  1 
ATOM   2059 C C   . MET A 1 304 ? 36.954  13.773  32.171  1.00 96.79  ? 298 MET A C   1 
ATOM   2060 O O   . MET A 1 304 ? 36.474  14.692  32.850  1.00 103.41 ? 298 MET A O   1 
ATOM   2061 C CB  . MET A 1 304 ? 37.247  14.175  29.746  1.00 90.83  ? 298 MET A CB  1 
ATOM   2062 C CG  . MET A 1 304 ? 36.511  14.819  28.598  1.00 91.47  ? 298 MET A CG  1 
ATOM   2063 S SD  . MET A 1 304 ? 37.677  15.773  27.609  1.00 92.17  ? 298 MET A SD  1 
ATOM   2064 C CE  . MET A 1 304 ? 39.151  15.632  28.626  1.00 91.97  ? 298 MET A CE  1 
ATOM   2065 N N   . PRO A 1 305 ? 37.979  13.026  32.608  1.00 97.02  ? 299 PRO A N   1 
ATOM   2066 C CA  . PRO A 1 305 ? 38.616  13.336  33.868  1.00 97.46  ? 299 PRO A CA  1 
ATOM   2067 C C   . PRO A 1 305 ? 39.275  14.687  33.796  1.00 100.02 ? 299 PRO A C   1 
ATOM   2068 O O   . PRO A 1 305 ? 39.804  15.046  32.733  1.00 101.03 ? 299 PRO A O   1 
ATOM   2069 C CB  . PRO A 1 305 ? 39.641  12.222  33.953  1.00 96.94  ? 299 PRO A CB  1 
ATOM   2070 C CG  . PRO A 1 305 ? 39.022  11.100  33.165  1.00 99.00  ? 299 PRO A CG  1 
ATOM   2071 C CD  . PRO A 1 305 ? 38.477  11.833  31.961  1.00 99.37  ? 299 PRO A CD  1 
ATOM   2072 N N   . ALA A 1 306 ? 39.206  15.451  34.883  1.00 102.61 ? 300 ALA A N   1 
ATOM   2073 C CA  . ALA A 1 306 ? 39.846  16.787  34.967  1.00 101.82 ? 300 ALA A CA  1 
ATOM   2074 C C   . ALA A 1 306 ? 41.367  16.677  35.007  1.00 102.25 ? 300 ALA A C   1 
ATOM   2075 O O   . ALA A 1 306 ? 41.870  15.651  35.497  1.00 95.86  ? 300 ALA A O   1 
ATOM   2076 C CB  . ALA A 1 306 ? 39.318  17.542  36.166  1.00 101.16 ? 300 ALA A CB  1 
ATOM   2077 N N   . ASP A 1 307 ? 42.065  17.684  34.478  1.00 108.08 ? 301 ASP A N   1 
ATOM   2078 C CA  . ASP A 1 307 ? 43.554  17.729  34.554  1.00 112.22 ? 301 ASP A CA  1 
ATOM   2079 C C   . ASP A 1 307 ? 44.204  16.501  33.906  1.00 110.69 ? 301 ASP A C   1 
ATOM   2080 O O   . ASP A 1 307 ? 45.219  16.010  34.437  1.00 113.31 ? 301 ASP A O   1 
ATOM   2081 C CB  . ASP A 1 307 ? 43.992  17.916  35.996  1.00 117.27 ? 301 ASP A CB  1 
ATOM   2082 C CG  . ASP A 1 307 ? 43.079  18.799  36.833  1.00 121.30 ? 301 ASP A CG  1 
ATOM   2083 O OD1 . ASP A 1 307 ? 42.603  19.819  36.294  1.00 123.75 ? 301 ASP A OD1 1 
ATOM   2084 O OD2 . ASP A 1 307 ? 42.846  18.455  38.009  1.00 125.24 ? 301 ASP A OD2 1 
ATOM   2085 N N   . LEU A 1 308 ? 43.646  16.035  32.791  1.00 103.42 ? 302 LEU A N   1 
ATOM   2086 C CA  . LEU A 1 308 ? 44.236  14.879  32.080  1.00 94.91  ? 302 LEU A CA  1 
ATOM   2087 C C   . LEU A 1 308 ? 45.619  15.276  31.557  1.00 90.02  ? 302 LEU A C   1 
ATOM   2088 O O   . LEU A 1 308 ? 45.810  16.432  31.147  1.00 87.75  ? 302 LEU A O   1 
ATOM   2089 C CB  . LEU A 1 308 ? 43.313  14.392  30.964  1.00 91.57  ? 302 LEU A CB  1 
ATOM   2090 C CG  . LEU A 1 308 ? 43.034  12.888  30.913  1.00 88.14  ? 302 LEU A CG  1 
ATOM   2091 C CD1 . LEU A 1 308 ? 43.021  12.277  32.296  1.00 86.60  ? 302 LEU A CD1 1 
ATOM   2092 C CD2 . LEU A 1 308 ? 41.716  12.634  30.213  1.00 87.43  ? 302 LEU A CD2 1 
ATOM   2093 N N   . PRO A 1 309 ? 46.634  14.386  31.539  1.00 86.96  ? 303 PRO A N   1 
ATOM   2094 C CA  . PRO A 1 309 ? 47.918  14.762  30.976  1.00 85.30  ? 303 PRO A CA  1 
ATOM   2095 C C   . PRO A 1 309 ? 47.908  14.889  29.473  1.00 86.73  ? 303 PRO A C   1 
ATOM   2096 O O   . PRO A 1 309 ? 47.000  14.360  28.816  1.00 86.78  ? 303 PRO A O   1 
ATOM   2097 C CB  . PRO A 1 309 ? 48.770  13.588  31.420  1.00 83.65  ? 303 PRO A CB  1 
ATOM   2098 C CG  . PRO A 1 309 ? 47.828  12.421  31.392  1.00 84.38  ? 303 PRO A CG  1 
ATOM   2099 C CD  . PRO A 1 309 ? 46.619  13.020  32.065  1.00 85.61  ? 303 PRO A CD  1 
ATOM   2100 N N   . SER A 1 310 ? 48.962  15.508  28.948  1.00 87.78  ? 304 SER A N   1 
ATOM   2101 C CA  . SER A 1 310 ? 49.124  15.627  27.485  1.00 84.19  ? 304 SER A CA  1 
ATOM   2102 C C   . SER A 1 310 ? 49.526  14.277  26.904  1.00 80.96  ? 304 SER A C   1 
ATOM   2103 O O   . SER A 1 310 ? 50.249  13.535  27.578  1.00 75.09  ? 304 SER A O   1 
ATOM   2104 C CB  . SER A 1 310 ? 50.160  16.647  27.141  1.00 83.81  ? 304 SER A CB  1 
ATOM   2105 O OG  . SER A 1 310 ? 51.430  16.266  27.645  1.00 83.48  ? 304 SER A OG  1 
ATOM   2106 N N   . LEU A 1 311 ? 49.078  13.984  25.703  1.00 82.09  ? 305 LEU A N   1 
ATOM   2107 C CA  . LEU A 1 311 ? 49.382  12.662  25.140  1.00 82.12  ? 305 LEU A CA  1 
ATOM   2108 C C   . LEU A 1 311 ? 50.835  12.663  24.687  1.00 80.12  ? 305 LEU A C   1 
ATOM   2109 O O   . LEU A 1 311 ? 51.394  11.583  24.515  1.00 77.84  ? 305 LEU A O   1 
ATOM   2110 C CB  . LEU A 1 311 ? 48.402  12.523  23.982  1.00 82.59  ? 305 LEU A CB  1 
ATOM   2111 C CG  . LEU A 1 311 ? 47.316  11.468  24.166  1.00 82.93  ? 305 LEU A CG  1 
ATOM   2112 C CD1 . LEU A 1 311 ? 47.244  10.633  22.903  1.00 82.86  ? 305 LEU A CD1 1 
ATOM   2113 C CD2 . LEU A 1 311 ? 47.790  10.644  25.342  1.00 83.45  ? 305 LEU A CD2 1 
ATOM   2114 N N   . ALA A 1 312 ? 51.436  13.837  24.569  1.00 80.73  ? 306 ALA A N   1 
ATOM   2115 C CA  . ALA A 1 312 ? 52.784  13.881  23.966  1.00 86.22  ? 306 ALA A CA  1 
ATOM   2116 C C   . ALA A 1 312 ? 53.799  13.109  24.789  1.00 91.33  ? 306 ALA A C   1 
ATOM   2117 O O   . ALA A 1 312 ? 54.640  12.411  24.199  1.00 100.74 ? 306 ALA A O   1 
ATOM   2118 C CB  . ALA A 1 312 ? 53.228  15.306  23.818  1.00 87.17  ? 306 ALA A CB  1 
ATOM   2119 N N   . ALA A 1 313 ? 53.800  13.234  26.100  1.00 88.89  ? 307 ALA A N   1 
ATOM   2120 C CA  . ALA A 1 313 ? 54.715  12.327  26.816  1.00 85.91  ? 307 ALA A CA  1 
ATOM   2121 C C   . ALA A 1 313 ? 54.094  10.956  26.595  1.00 85.10  ? 307 ALA A C   1 
ATOM   2122 O O   . ALA A 1 313 ? 52.857  10.911  26.663  1.00 89.60  ? 307 ALA A O   1 
ATOM   2123 C CB  . ALA A 1 313 ? 54.794  12.674  28.268  1.00 84.92  ? 307 ALA A CB  1 
ATOM   2124 N N   . ASP A 1 314 ? 54.875  9.928   26.296  1.00 79.67  ? 308 ASP A N   1 
ATOM   2125 C CA  . ASP A 1 314 ? 54.379  8.548   26.023  1.00 75.43  ? 308 ASP A CA  1 
ATOM   2126 C C   . ASP A 1 314 ? 53.924  8.342   24.580  1.00 70.91  ? 308 ASP A C   1 
ATOM   2127 O O   . ASP A 1 314 ? 53.623  7.189   24.273  1.00 72.17  ? 308 ASP A O   1 
ATOM   2128 C CB  . ASP A 1 314 ? 53.139  8.172   26.819  1.00 74.74  ? 308 ASP A CB  1 
ATOM   2129 C CG  . ASP A 1 314 ? 53.325  7.228   27.992  1.00 76.56  ? 308 ASP A CG  1 
ATOM   2130 O OD1 . ASP A 1 314 ? 54.462  7.121   28.482  1.00 78.93  ? 308 ASP A OD1 1 
ATOM   2131 O OD2 . ASP A 1 314 ? 52.320  6.622   28.406  1.00 77.76  ? 308 ASP A OD2 1 
ATOM   2132 N N   . PHE A 1 315 ? 53.963  9.336   23.709  1.00 65.22  ? 309 PHE A N   1 
ATOM   2133 C CA  . PHE A 1 315 ? 53.618  9.034   22.296  1.00 62.84  ? 309 PHE A CA  1 
ATOM   2134 C C   . PHE A 1 315 ? 54.525  9.849   21.391  1.00 64.15  ? 309 PHE A C   1 
ATOM   2135 O O   . PHE A 1 315 ? 54.718  9.447   20.242  1.00 61.05  ? 309 PHE A O   1 
ATOM   2136 C CB  . PHE A 1 315 ? 52.116  9.209   22.061  1.00 30.00  ? 309 PHE A CB  1 
ATOM   2137 C CG  . PHE A 1 315 ? 51.205  8.183   22.716  1.00 30.00  ? 309 PHE A CG  1 
ATOM   2138 C CD1 . PHE A 1 315 ? 51.189  6.866   22.284  1.00 30.00  ? 309 PHE A CD1 1 
ATOM   2139 C CD2 . PHE A 1 315 ? 50.363  8.544   23.758  1.00 30.00  ? 309 PHE A CD2 1 
ATOM   2140 C CE1 . PHE A 1 315 ? 50.360  5.937   22.886  1.00 30.00  ? 309 PHE A CE1 1 
ATOM   2141 C CE2 . PHE A 1 315 ? 49.536  7.611   24.355  1.00 30.00  ? 309 PHE A CE2 1 
ATOM   2142 C CZ  . PHE A 1 315 ? 49.536  6.311   23.919  1.00 30.00  ? 309 PHE A CZ  1 
ATOM   2143 N N   . VAL A 1 316 ? 55.097  10.933  21.914  1.00 68.38  ? 310 VAL A N   1 
ATOM   2144 C CA  . VAL A 1 316 ? 56.028  11.790  21.118  1.00 73.55  ? 310 VAL A CA  1 
ATOM   2145 C C   . VAL A 1 316 ? 57.271  12.167  21.945  1.00 77.82  ? 310 VAL A C   1 
ATOM   2146 O O   . VAL A 1 316 ? 58.327  12.387  21.340  1.00 81.73  ? 310 VAL A O   1 
ATOM   2147 C CB  . VAL A 1 316 ? 55.315  13.037  20.562  1.00 75.64  ? 310 VAL A CB  1 
ATOM   2148 C CG1 . VAL A 1 316 ? 53.818  12.984  20.804  1.00 74.76  ? 310 VAL A CG1 1 
ATOM   2149 C CG2 . VAL A 1 316 ? 55.900  14.333  21.102  1.00 76.36  ? 310 VAL A CG2 1 
ATOM   2150 N N   . GLU A 1 317 ? 57.165  12.210  23.269  1.00 80.79  ? 311 GLU A N   1 
ATOM   2151 C CA  . GLU A 1 317 ? 58.311  12.655  24.102  1.00 81.89  ? 311 GLU A CA  1 
ATOM   2152 C C   . GLU A 1 317 ? 59.190  11.506  24.572  1.00 79.80  ? 311 GLU A C   1 
ATOM   2153 O O   . GLU A 1 317 ? 60.274  11.787  25.092  1.00 82.35  ? 311 GLU A O   1 
ATOM   2154 C CB  . GLU A 1 317 ? 57.799  13.355  25.355  1.00 87.67  ? 311 GLU A CB  1 
ATOM   2155 C CG  . GLU A 1 317 ? 57.719  14.871  25.204  1.00 91.46  ? 311 GLU A CG  1 
ATOM   2156 C CD  . GLU A 1 317 ? 57.079  15.595  26.374  1.00 96.09  ? 311 GLU A CD  1 
ATOM   2157 O OE1 . GLU A 1 317 ? 56.456  16.646  26.129  1.00 95.45  ? 311 GLU A OE1 1 
ATOM   2158 O OE2 . GLU A 1 317 ? 57.201  15.120  27.522  1.00 100.86 ? 311 GLU A OE2 1 
ATOM   2159 N N   . SER A 1 318 ? 58.766  10.270  24.356  1.00 78.51  ? 312 SER A N   1 
ATOM   2160 C CA  . SER A 1 318 ? 59.499  9.116   24.932  1.00 74.20  ? 312 SER A CA  1 
ATOM   2161 C C   . SER A 1 318 ? 60.480  8.503   23.939  1.00 75.85  ? 312 SER A C   1 
ATOM   2162 O O   . SER A 1 318 ? 60.148  8.437   22.756  1.00 77.33  ? 312 SER A O   1 
ATOM   2163 C CB  . SER A 1 318 ? 58.547  8.067   25.451  1.00 69.71  ? 312 SER A CB  1 
ATOM   2164 O OG  . SER A 1 318 ? 59.185  6.808   25.576  1.00 68.66  ? 312 SER A OG  1 
ATOM   2165 N N   . LYS A 1 319 ? 61.656  8.130   24.410  1.00 78.16  ? 313 LYS A N   1 
ATOM   2166 C CA  . LYS A 1 319 ? 62.660  7.385   23.601  1.00 80.07  ? 313 LYS A CA  1 
ATOM   2167 C C   . LYS A 1 319 ? 62.057  6.015   23.294  1.00 77.09  ? 313 LYS A C   1 
ATOM   2168 O O   . LYS A 1 319 ? 62.344  5.485   22.217  1.00 77.67  ? 313 LYS A O   1 
ATOM   2169 C CB  . LYS A 1 319 ? 64.002  7.396   24.328  1.00 85.65  ? 313 LYS A CB  1 
ATOM   2170 C CG  . LYS A 1 319 ? 64.558  8.798   24.549  1.00 89.53  ? 313 LYS A CG  1 
ATOM   2171 C CD  . LYS A 1 319 ? 65.569  9.231   23.494  1.00 92.14  ? 313 LYS A CD  1 
ATOM   2172 C CE  . LYS A 1 319 ? 66.299  10.474  23.884  1.00 95.32  ? 313 LYS A CE  1 
ATOM   2173 N NZ  . LYS A 1 319 ? 65.627  11.160  24.989  1.00 97.24  ? 313 LYS A NZ  1 
ATOM   2174 N N   . ASP A 1 320 ? 61.314  5.447   24.226  1.00 74.83  ? 314 ASP A N   1 
ATOM   2175 C CA  . ASP A 1 320 ? 60.778  4.062   24.245  1.00 74.15  ? 314 ASP A CA  1 
ATOM   2176 C C   . ASP A 1 320 ? 59.780  3.717   23.132  1.00 68.36  ? 314 ASP A C   1 
ATOM   2177 O O   . ASP A 1 320 ? 59.584  2.518   22.949  1.00 70.62  ? 314 ASP A O   1 
ATOM   2178 C CB  . ASP A 1 320 ? 60.262  3.754   25.638  1.00 78.41  ? 314 ASP A CB  1 
ATOM   2179 C CG  . ASP A 1 320 ? 61.332  3.674   26.716  1.00 83.94  ? 314 ASP A CG  1 
ATOM   2180 O OD1 . ASP A 1 320 ? 62.486  4.040   26.419  1.00 85.82  ? 314 ASP A OD1 1 
ATOM   2181 O OD2 . ASP A 1 320 ? 61.002  3.247   27.840  1.00 86.05  ? 314 ASP A OD2 1 
ATOM   2182 N N   . VAL A 1 321 ? 59.099  4.635   22.465  1.00 61.16  ? 315 VAL A N   1 
ATOM   2183 C CA  . VAL A 1 321 ? 57.928  4.312   21.605  1.00 60.81  ? 315 VAL A CA  1 
ATOM   2184 C C   . VAL A 1 321 ? 58.228  3.348   20.454  1.00 55.78  ? 315 VAL A C   1 
ATOM   2185 O O   . VAL A 1 321 ? 57.394  2.478   20.239  1.00 55.80  ? 315 VAL A O   1 
ATOM   2186 C CB  . VAL A 1 321 ? 57.646  5.688   20.990  1.00 65.07  ? 315 VAL A CB  1 
ATOM   2187 C CG1 . VAL A 1 321 ? 56.471  5.672   20.026  1.00 67.22  ? 315 VAL A CG1 1 
ATOM   2188 C CG2 . VAL A 1 321 ? 57.501  6.784   22.030  1.00 65.99  ? 315 VAL A CG2 1 
ATOM   2189 N N   . CYS A 1 322 ? 59.344  3.431   19.768  1.00 52.75  ? 316 CYS A N   1 
ATOM   2190 C CA  . CYS A 1 322 ? 59.582  2.437   18.696  1.00 51.49  ? 316 CYS A CA  1 
ATOM   2191 C C   . CYS A 1 322 ? 59.642  1.040   19.337  1.00 48.74  ? 316 CYS A C   1 
ATOM   2192 O O   . CYS A 1 322 ? 59.165  0.102   18.716  1.00 50.52  ? 316 CYS A O   1 
ATOM   2193 C CB  . CYS A 1 322 ? 60.793  2.846   17.873  1.00 52.45  ? 316 CYS A CB  1 
ATOM   2194 S SG  . CYS A 1 322 ? 60.566  4.383   16.949  1.00 57.87  ? 316 CYS A SG  1 
ATOM   2195 N N   . LYS A 1 323 ? 60.257  0.900   20.498  1.00 49.69  ? 317 LYS A N   1 
ATOM   2196 C CA  . LYS A 1 323 ? 60.283  -0.388  21.232  1.00 49.64  ? 317 LYS A CA  1 
ATOM   2197 C C   . LYS A 1 323 ? 58.884  -0.810  21.690  1.00 49.08  ? 317 LYS A C   1 
ATOM   2198 O O   . LYS A 1 323 ? 58.570  -1.996  21.594  1.00 46.42  ? 317 LYS A O   1 
ATOM   2199 C CB  . LYS A 1 323 ? 61.166  -0.214  22.466  1.00 50.85  ? 317 LYS A CB  1 
ATOM   2200 C CG  . LYS A 1 323 ? 61.666  -1.484  23.134  1.00 52.84  ? 317 LYS A CG  1 
ATOM   2201 C CD  . LYS A 1 323 ? 60.888  -1.941  24.362  1.00 54.87  ? 317 LYS A CD  1 
ATOM   2202 C CE  . LYS A 1 323 ? 60.463  -0.832  25.264  1.00 57.11  ? 317 LYS A CE  1 
ATOM   2203 N NZ  . LYS A 1 323 ? 59.641  -1.337  26.364  1.00 59.53  ? 317 LYS A NZ  1 
ATOM   2204 N N   . ASN A 1 324 ? 58.105  0.120   22.229  1.00 50.12  ? 318 ASN A N   1 
ATOM   2205 C CA  . ASN A 1 324 ? 56.749  -0.188  22.643  1.00 49.92  ? 318 ASN A CA  1 
ATOM   2206 C C   . ASN A 1 324 ? 55.927  -0.631  21.434  1.00 45.53  ? 318 ASN A C   1 
ATOM   2207 O O   . ASN A 1 324 ? 55.262  -1.660  21.487  1.00 43.84  ? 318 ASN A O   1 
ATOM   2208 C CB  . ASN A 1 324 ? 56.128  1.033   23.370  1.00 52.25  ? 318 ASN A CB  1 
ATOM   2209 C CG  . ASN A 1 324 ? 56.591  1.218   24.817  1.00 52.57  ? 318 ASN A CG  1 
ATOM   2210 O OD1 . ASN A 1 324 ? 57.023  0.279   25.490  1.00 51.82  ? 318 ASN A OD1 1 
ATOM   2211 N ND2 . ASN A 1 324 ? 56.470  2.438   25.342  1.00 52.31  ? 318 ASN A ND2 1 
ATOM   2212 N N   . TYR A 1 325 ? 56.016  0.127   20.336  1.00 44.06  ? 319 TYR A N   1 
ATOM   2213 C CA  . TYR A 1 325 ? 55.364  -0.249  19.090  1.00 44.46  ? 319 TYR A CA  1 
ATOM   2214 C C   . TYR A 1 325 ? 55.747  -1.636  18.581  1.00 42.60  ? 319 TYR A C   1 
ATOM   2215 O O   . TYR A 1 325 ? 54.896  -2.351  18.074  1.00 44.24  ? 319 TYR A O   1 
ATOM   2216 C CB  . TYR A 1 325 ? 55.673  0.741   17.982  1.00 46.78  ? 319 TYR A CB  1 
ATOM   2217 C CG  . TYR A 1 325 ? 54.849  0.534   16.728  1.00 48.84  ? 319 TYR A CG  1 
ATOM   2218 C CD1 . TYR A 1 325 ? 53.503  0.210   16.803  1.00 50.71  ? 319 TYR A CD1 1 
ATOM   2219 C CD2 . TYR A 1 325 ? 55.397  0.726   15.472  1.00 48.23  ? 319 TYR A CD2 1 
ATOM   2220 C CE1 . TYR A 1 325 ? 52.734  0.050   15.662  1.00 51.40  ? 319 TYR A CE1 1 
ATOM   2221 C CE2 . TYR A 1 325 ? 54.632  0.583   14.321  1.00 49.91  ? 319 TYR A CE2 1 
ATOM   2222 C CZ  . TYR A 1 325 ? 53.300  0.240   14.422  1.00 51.03  ? 319 TYR A CZ  1 
ATOM   2223 O OH  . TYR A 1 325 ? 52.517  0.080   13.306  1.00 55.09  ? 319 TYR A OH  1 
ATOM   2224 N N   . ALA A 1 326 ? 57.019  -2.013  18.716  1.00 41.07  ? 320 ALA A N   1 
ATOM   2225 C CA  . ALA A 1 326 ? 57.488  -3.309  18.255  1.00 42.38  ? 320 ALA A CA  1 
ATOM   2226 C C   . ALA A 1 326 ? 57.071  -4.456  19.168  1.00 44.56  ? 320 ALA A C   1 
ATOM   2227 O O   . ALA A 1 326 ? 56.934  -5.583  18.704  1.00 43.21  ? 320 ALA A O   1 
ATOM   2228 C CB  . ALA A 1 326 ? 58.998  -3.305  18.128  1.00 44.15  ? 320 ALA A CB  1 
ATOM   2229 N N   . GLU A 1 327 ? 56.915  -4.169  20.471  1.00 47.55  ? 321 GLU A N   1 
ATOM   2230 C CA  . GLU A 1 327 ? 56.491  -5.177  21.431  1.00 48.20  ? 321 GLU A CA  1 
ATOM   2231 C C   . GLU A 1 327 ? 54.995  -5.466  21.356  1.00 49.78  ? 321 GLU A C   1 
ATOM   2232 O O   . GLU A 1 327 ? 54.583  -6.606  21.562  1.00 47.32  ? 321 GLU A O   1 
ATOM   2233 C CB  . GLU A 1 327 ? 56.844  -4.747  22.845  1.00 50.78  ? 321 GLU A CB  1 
ATOM   2234 C CG  . GLU A 1 327 ? 58.332  -4.803  23.139  1.00 53.34  ? 321 GLU A CG  1 
ATOM   2235 C CD  . GLU A 1 327 ? 58.934  -6.190  23.098  1.00 54.13  ? 321 GLU A CD  1 
ATOM   2236 O OE1 . GLU A 1 327 ? 58.199  -7.188  23.288  1.00 51.10  ? 321 GLU A OE1 1 
ATOM   2237 O OE2 . GLU A 1 327 ? 60.152  -6.271  22.826  1.00 57.40  ? 321 GLU A OE2 1 
ATOM   2238 N N   . ALA A 1 328 ? 54.189  -4.438  21.052  1.00 50.65  ? 322 ALA A N   1 
ATOM   2239 C CA  . ALA A 1 328 ? 52.744  -4.591  21.099  1.00 55.70  ? 322 ALA A CA  1 
ATOM   2240 C C   . ALA A 1 328 ? 51.980  -3.652  20.169  1.00 56.82  ? 322 ALA A C   1 
ATOM   2241 O O   . ALA A 1 328 ? 51.067  -2.967  20.625  1.00 58.24  ? 322 ALA A O   1 
ATOM   2242 C CB  . ALA A 1 328 ? 52.288  -4.382  22.545  1.00 58.12  ? 322 ALA A CB  1 
ATOM   2243 N N   . LYS A 1 329 ? 52.325  -3.684  18.866  1.00 57.46  ? 323 LYS A N   1 
ATOM   2244 C CA  . LYS A 1 329 ? 51.908  -2.678  17.893  1.00 56.04  ? 323 LYS A CA  1 
ATOM   2245 C C   . LYS A 1 329 ? 50.434  -2.274  17.903  1.00 52.70  ? 323 LYS A C   1 
ATOM   2246 O O   . LYS A 1 329 ? 50.133  -1.110  18.124  1.00 48.09  ? 323 LYS A O   1 
ATOM   2247 C CB  . LYS A 1 329 ? 52.260  -3.088  16.445  1.00 59.16  ? 323 LYS A CB  1 
ATOM   2248 C CG  . LYS A 1 329 ? 51.975  -4.523  16.110  1.00 62.35  ? 323 LYS A CG  1 
ATOM   2249 C CD  . LYS A 1 329 ? 51.597  -4.722  14.672  1.00 64.08  ? 323 LYS A CD  1 
ATOM   2250 C CE  . LYS A 1 329 ? 52.664  -4.314  13.724  1.00 67.73  ? 323 LYS A CE  1 
ATOM   2251 N NZ  . LYS A 1 329 ? 52.688  -5.231  12.543  1.00 69.82  ? 323 LYS A NZ  1 
ATOM   2252 N N   . ASP A 1 330 ? 49.517  -3.211  17.646  1.00 54.28  ? 324 ASP A N   1 
ATOM   2253 C CA  . ASP A 1 330 ? 48.105  -2.864  17.548  1.00 58.60  ? 324 ASP A CA  1 
ATOM   2254 C C   . ASP A 1 330 ? 47.526  -2.426  18.897  1.00 56.12  ? 324 ASP A C   1 
ATOM   2255 O O   . ASP A 1 330 ? 46.698  -1.516  18.955  1.00 52.02  ? 324 ASP A O   1 
ATOM   2256 C CB  . ASP A 1 330 ? 47.282  -4.020  16.924  1.00 59.57  ? 324 ASP A CB  1 
ATOM   2257 C CG  . ASP A 1 330 ? 47.241  -4.036  15.388  1.00 62.67  ? 324 ASP A CG  1 
ATOM   2258 O OD1 . ASP A 1 330 ? 47.935  -3.185  14.751  1.00 60.41  ? 324 ASP A OD1 1 
ATOM   2259 O OD2 . ASP A 1 330 ? 46.498  -4.886  14.817  1.00 67.37  ? 324 ASP A OD2 1 
ATOM   2260 N N   . VAL A 1 331 ? 47.993  -3.044  19.988  1.00 54.36  ? 325 VAL A N   1 
ATOM   2261 C CA  . VAL A 1 331 ? 47.627  -2.586  21.323  1.00 52.51  ? 325 VAL A CA  1 
ATOM   2262 C C   . VAL A 1 331 ? 48.142  -1.166  21.546  1.00 50.79  ? 325 VAL A C   1 
ATOM   2263 O O   . VAL A 1 331 ? 47.414  -0.294  22.011  1.00 55.64  ? 325 VAL A O   1 
ATOM   2264 C CB  . VAL A 1 331 ? 48.145  -3.525  22.427  1.00 50.36  ? 325 VAL A CB  1 
ATOM   2265 C CG1 . VAL A 1 331 ? 47.951  -2.901  23.782  1.00 50.47  ? 325 VAL A CG1 1 
ATOM   2266 C CG2 . VAL A 1 331 ? 47.483  -4.897  22.355  1.00 48.84  ? 325 VAL A CG2 1 
ATOM   2267 N N   . PHE A 1 332 ? 49.414  -0.945  21.223  1.00 48.72  ? 326 PHE A N   1 
ATOM   2268 C CA  . PHE A 1 332 ? 50.011  0.371   21.385  1.00 47.50  ? 326 PHE A CA  1 
ATOM   2269 C C   . PHE A 1 332 ? 49.224  1.416   20.590  1.00 46.42  ? 326 PHE A C   1 
ATOM   2270 O O   . PHE A 1 332 ? 48.846  2.441   21.145  1.00 45.93  ? 326 PHE A O   1 
ATOM   2271 C CB  . PHE A 1 332 ? 51.508  0.329   21.001  1.00 45.36  ? 326 PHE A CB  1 
ATOM   2272 C CG  . PHE A 1 332 ? 52.249  1.608   21.276  1.00 43.86  ? 326 PHE A CG  1 
ATOM   2273 C CD1 . PHE A 1 332 ? 52.472  2.032   22.573  1.00 45.48  ? 326 PHE A CD1 1 
ATOM   2274 C CD2 . PHE A 1 332 ? 52.710  2.394   20.241  1.00 44.02  ? 326 PHE A CD2 1 
ATOM   2275 C CE1 . PHE A 1 332 ? 53.141  3.222   22.827  1.00 44.83  ? 326 PHE A CE1 1 
ATOM   2276 C CE2 . PHE A 1 332 ? 53.374  3.582   20.495  1.00 44.49  ? 326 PHE A CE2 1 
ATOM   2277 C CZ  . PHE A 1 332 ? 53.590  3.986   21.786  1.00 45.42  ? 326 PHE A CZ  1 
ATOM   2278 N N   . LEU A 1 333 ? 48.943  1.136   19.308  1.00 46.63  ? 327 LEU A N   1 
ATOM   2279 C CA  . LEU A 1 333 ? 48.141  2.027   18.476  1.00 46.71  ? 327 LEU A CA  1 
ATOM   2280 C C   . LEU A 1 333 ? 46.712  2.206   19.002  1.00 45.30  ? 327 LEU A C   1 
ATOM   2281 O O   . LEU A 1 333 ? 46.229  3.332   19.087  1.00 44.68  ? 327 LEU A O   1 
ATOM   2282 C CB  . LEU A 1 333 ? 48.081  1.527   17.027  1.00 45.86  ? 327 LEU A CB  1 
ATOM   2283 C CG  . LEU A 1 333 ? 49.405  1.520   16.250  1.00 49.95  ? 327 LEU A CG  1 
ATOM   2284 C CD1 . LEU A 1 333 ? 49.198  1.009   14.814  1.00 50.31  ? 327 LEU A CD1 1 
ATOM   2285 C CD2 . LEU A 1 333 ? 50.078  2.897   16.226  1.00 50.32  ? 327 LEU A CD2 1 
ATOM   2286 N N   . GLY A 1 334 ? 46.043  1.099   19.347  1.00 42.67  ? 328 GLY A N   1 
ATOM   2287 C CA  . GLY A 1 334 ? 44.766  1.146   20.037  1.00 45.59  ? 328 GLY A CA  1 
ATOM   2288 C C   . GLY A 1 334 ? 44.704  2.137   21.207  1.00 47.88  ? 328 GLY A C   1 
ATOM   2289 O O   . GLY A 1 334 ? 43.732  2.879   21.334  1.00 47.41  ? 328 GLY A O   1 
ATOM   2290 N N   . MET A 1 335 ? 45.751  2.155   22.041  1.00 47.98  ? 329 MET A N   1 
ATOM   2291 C CA  . MET A 1 335 ? 45.817  3.024   23.207  1.00 52.12  ? 329 MET A CA  1 
ATOM   2292 C C   . MET A 1 335 ? 46.024  4.498   22.857  1.00 52.13  ? 329 MET A C   1 
ATOM   2293 O O   . MET A 1 335 ? 45.587  5.391   23.579  1.00 52.79  ? 329 MET A O   1 
ATOM   2294 C CB  . MET A 1 335 ? 46.989  2.584   24.116  1.00 54.37  ? 329 MET A CB  1 
ATOM   2295 C CG  . MET A 1 335 ? 46.664  1.392   24.984  1.00 55.17  ? 329 MET A CG  1 
ATOM   2296 S SD  . MET A 1 335 ? 48.144  0.756   25.782  1.00 56.76  ? 329 MET A SD  1 
ATOM   2297 C CE  . MET A 1 335 ? 47.582  -0.867  26.236  1.00 56.30  ? 329 MET A CE  1 
ATOM   2298 N N   . PHE A 1 336 ? 46.762  4.748   21.775  1.00 50.32  ? 330 PHE A N   1 
ATOM   2299 C CA  . PHE A 1 336 ? 46.900  6.089   21.248  1.00 48.21  ? 330 PHE A CA  1 
ATOM   2300 C C   . PHE A 1 336 ? 45.522  6.651   20.911  1.00 48.65  ? 330 PHE A C   1 
ATOM   2301 O O   . PHE A 1 336 ? 45.245  7.830   21.144  1.00 46.22  ? 330 PHE A O   1 
ATOM   2302 C CB  . PHE A 1 336 ? 47.752  6.061   19.993  1.00 46.29  ? 330 PHE A CB  1 
ATOM   2303 C CG  . PHE A 1 336 ? 47.877  7.412   19.368  1.00 46.36  ? 330 PHE A CG  1 
ATOM   2304 C CD1 . PHE A 1 336 ? 48.774  8.341   19.865  1.00 47.20  ? 330 PHE A CD1 1 
ATOM   2305 C CD2 . PHE A 1 336 ? 47.074  7.775   18.304  1.00 45.65  ? 330 PHE A CD2 1 
ATOM   2306 C CE1 . PHE A 1 336 ? 48.886  9.603   19.286  1.00 46.83  ? 330 PHE A CE1 1 
ATOM   2307 C CE2 . PHE A 1 336 ? 47.185  9.034   17.735  1.00 47.43  ? 330 PHE A CE2 1 
ATOM   2308 C CZ  . PHE A 1 336 ? 48.091  9.942   18.229  1.00 47.05  ? 330 PHE A CZ  1 
ATOM   2309 N N   . LEU A 1 337 ? 44.685  5.787   20.320  1.00 46.81  ? 331 LEU A N   1 
ATOM   2310 C CA  . LEU A 1 337 ? 43.385  6.184   19.817  1.00 46.42  ? 331 LEU A CA  1 
ATOM   2311 C C   . LEU A 1 337 ? 42.455  6.393   21.012  1.00 48.64  ? 331 LEU A C   1 
ATOM   2312 O O   . LEU A 1 337 ? 41.735  7.396   21.064  1.00 48.31  ? 331 LEU A O   1 
ATOM   2313 C CB  . LEU A 1 337 ? 42.898  5.109   18.839  1.00 45.19  ? 331 LEU A CB  1 
ATOM   2314 C CG  . LEU A 1 337 ? 41.508  5.278   18.217  1.00 42.82  ? 331 LEU A CG  1 
ATOM   2315 C CD1 . LEU A 1 337 ? 41.464  6.447   17.329  1.00 42.63  ? 331 LEU A CD1 1 
ATOM   2316 C CD2 . LEU A 1 337 ? 41.120  4.029   17.456  1.00 41.79  ? 331 LEU A CD2 1 
ATOM   2317 N N   . TYR A 1 338 ? 42.518  5.462   21.980  1.00 48.39  ? 332 TYR A N   1 
ATOM   2318 C CA  . TYR A 1 338 ? 41.871  5.632   23.274  1.00 52.16  ? 332 TYR A CA  1 
ATOM   2319 C C   . TYR A 1 338 ? 42.141  7.001   23.895  1.00 52.35  ? 332 TYR A C   1 
ATOM   2320 O O   . TYR A 1 338 ? 41.221  7.724   24.264  1.00 53.55  ? 332 TYR A O   1 
ATOM   2321 C CB  . TYR A 1 338 ? 42.332  4.553   24.257  1.00 55.36  ? 332 TYR A CB  1 
ATOM   2322 C CG  . TYR A 1 338 ? 42.001  4.842   25.714  1.00 58.67  ? 332 TYR A CG  1 
ATOM   2323 C CD1 . TYR A 1 338 ? 40.695  4.776   26.177  1.00 59.20  ? 332 TYR A CD1 1 
ATOM   2324 C CD2 . TYR A 1 338 ? 43.000  5.173   26.625  1.00 60.96  ? 332 TYR A CD2 1 
ATOM   2325 C CE1 . TYR A 1 338 ? 40.388  5.027   27.507  1.00 60.67  ? 332 TYR A CE1 1 
ATOM   2326 C CE2 . TYR A 1 338 ? 42.705  5.432   27.957  1.00 60.89  ? 332 TYR A CE2 1 
ATOM   2327 C CZ  . TYR A 1 338 ? 41.395  5.357   28.395  1.00 62.53  ? 332 TYR A CZ  1 
ATOM   2328 O OH  . TYR A 1 338 ? 41.084  5.625   29.708  1.00 62.76  ? 332 TYR A OH  1 
ATOM   2329 N N   . GLU A 1 339 ? 43.419  7.349   24.006  1.00 51.99  ? 333 GLU A N   1 
ATOM   2330 C CA  . GLU A 1 339 ? 43.814  8.581   24.655  1.00 53.50  ? 333 GLU A CA  1 
ATOM   2331 C C   . GLU A 1 339 ? 43.425  9.818   23.858  1.00 53.90  ? 333 GLU A C   1 
ATOM   2332 O O   . GLU A 1 339 ? 43.081  10.829  24.461  1.00 55.77  ? 333 GLU A O   1 
ATOM   2333 C CB  . GLU A 1 339 ? 45.328  8.592   24.908  1.00 54.39  ? 333 GLU A CB  1 
ATOM   2334 C CG  . GLU A 1 339 ? 45.792  7.544   25.905  1.00 55.27  ? 333 GLU A CG  1 
ATOM   2335 C CD  . GLU A 1 339 ? 45.353  7.773   27.332  1.00 55.83  ? 333 GLU A CD  1 
ATOM   2336 O OE1 . GLU A 1 339 ? 44.710  8.811   27.609  1.00 55.34  ? 333 GLU A OE1 1 
ATOM   2337 O OE2 . GLU A 1 339 ? 45.639  6.897   28.176  1.00 60.22  ? 333 GLU A OE2 1 
ATOM   2338 N N   . TYR A 1 340 ? 43.513  9.754   22.522  1.00 54.69  ? 334 TYR A N   1 
ATOM   2339 C CA  . TYR A 1 340 ? 43.160  10.903  21.702  1.00 56.74  ? 334 TYR A CA  1 
ATOM   2340 C C   . TYR A 1 340 ? 41.644  11.087  21.734  1.00 58.78  ? 334 TYR A C   1 
ATOM   2341 O O   . TYR A 1 340 ? 41.158  12.203  21.922  1.00 58.82  ? 334 TYR A O   1 
ATOM   2342 C CB  . TYR A 1 340 ? 43.631  10.766  20.252  1.00 59.44  ? 334 TYR A CB  1 
ATOM   2343 C CG  . TYR A 1 340 ? 44.079  12.082  19.661  1.00 60.82  ? 334 TYR A CG  1 
ATOM   2344 C CD1 . TYR A 1 340 ? 43.239  13.185  19.650  1.00 61.38  ? 334 TYR A CD1 1 
ATOM   2345 C CD2 . TYR A 1 340 ? 45.353  12.232  19.140  1.00 64.49  ? 334 TYR A CD2 1 
ATOM   2346 C CE1 . TYR A 1 340 ? 43.654  14.403  19.128  1.00 62.44  ? 334 TYR A CE1 1 
ATOM   2347 C CE2 . TYR A 1 340 ? 45.777  13.444  18.607  1.00 66.21  ? 334 TYR A CE2 1 
ATOM   2348 C CZ  . TYR A 1 340 ? 44.925  14.529  18.604  1.00 64.27  ? 334 TYR A CZ  1 
ATOM   2349 O OH  . TYR A 1 340 ? 45.344  15.724  18.072  1.00 65.15  ? 334 TYR A OH  1 
ATOM   2350 N N   . ALA A 1 341 ? 40.918  9.970   21.579  1.00 58.39  ? 335 ALA A N   1 
ATOM   2351 C CA  . ALA A 1 341 ? 39.465  9.978   21.514  1.00 61.29  ? 335 ALA A CA  1 
ATOM   2352 C C   . ALA A 1 341 ? 38.802  10.515  22.781  1.00 63.60  ? 335 ALA A C   1 
ATOM   2353 O O   . ALA A 1 341 ? 37.957  11.407  22.713  1.00 65.45  ? 335 ALA A O   1 
ATOM   2354 C CB  . ALA A 1 341 ? 38.963  8.574   21.233  1.00 61.55  ? 335 ALA A CB  1 
ATOM   2355 N N   . ARG A 1 342 ? 39.191  9.964   23.936  1.00 65.14  ? 336 ARG A N   1 
ATOM   2356 C CA  . ARG A 1 342 ? 38.578  10.321  25.207  1.00 66.61  ? 336 ARG A CA  1 
ATOM   2357 C C   . ARG A 1 342 ? 38.704  11.814  25.514  1.00 64.38  ? 336 ARG A C   1 
ATOM   2358 O O   . ARG A 1 342 ? 37.894  12.362  26.249  1.00 64.08  ? 336 ARG A O   1 
ATOM   2359 C CB  . ARG A 1 342 ? 39.205  9.499   26.350  1.00 69.53  ? 336 ARG A CB  1 
ATOM   2360 C CG  . ARG A 1 342 ? 40.559  10.019  26.833  1.00 71.25  ? 336 ARG A CG  1 
ATOM   2361 C CD  . ARG A 1 342 ? 41.302  9.006   27.693  1.00 74.94  ? 336 ARG A CD  1 
ATOM   2362 N NE  . ARG A 1 342 ? 40.798  8.932   29.062  1.00 78.35  ? 336 ARG A NE  1 
ATOM   2363 C CZ  . ARG A 1 342 ? 41.517  8.539   30.110  1.00 79.00  ? 336 ARG A CZ  1 
ATOM   2364 N NH1 . ARG A 1 342 ? 42.834  8.432   30.043  1.00 79.89  ? 336 ARG A NH1 1 
ATOM   2365 N NH2 . ARG A 1 342 ? 40.900  8.273   31.261  1.00 77.86  ? 336 ARG A NH2 1 
ATOM   2366 N N   . ARG A 1 343 ? 39.729  12.458  24.948  1.00 65.27  ? 337 ARG A N   1 
ATOM   2367 C CA  . ARG A 1 343 ? 39.944  13.884  25.121  1.00 66.35  ? 337 ARG A CA  1 
ATOM   2368 C C   . ARG A 1 343 ? 39.144  14.738  24.144  1.00 67.67  ? 337 ARG A C   1 
ATOM   2369 O O   . ARG A 1 343 ? 39.146  15.960  24.257  1.00 68.18  ? 337 ARG A O   1 
ATOM   2370 C CB  . ARG A 1 343 ? 41.430  14.224  24.928  1.00 67.17  ? 337 ARG A CB  1 
ATOM   2371 C CG  . ARG A 1 343 ? 42.320  13.699  26.031  1.00 68.63  ? 337 ARG A CG  1 
ATOM   2372 C CD  . ARG A 1 343 ? 43.782  13.888  25.690  1.00 69.92  ? 337 ARG A CD  1 
ATOM   2373 N NE  . ARG A 1 343 ? 44.648  13.582  26.823  1.00 70.82  ? 337 ARG A NE  1 
ATOM   2374 C CZ  . ARG A 1 343 ? 44.773  12.382  27.379  1.00 69.83  ? 337 ARG A CZ  1 
ATOM   2375 N NH1 . ARG A 1 343 ? 44.030  11.357  26.993  1.00 67.57  ? 337 ARG A NH1 1 
ATOM   2376 N NH2 . ARG A 1 343 ? 45.662  12.208  28.354  1.00 69.74  ? 337 ARG A NH2 1 
ATOM   2377 N N   . HIS A 1 344 ? 38.482  14.097  23.173  1.00 70.06  ? 338 HIS A N   1 
ATOM   2378 C CA  . HIS A 1 344 ? 37.921  14.821  22.044  1.00 68.77  ? 338 HIS A CA  1 
ATOM   2379 C C   . HIS A 1 344 ? 36.569  14.284  21.595  1.00 68.54  ? 338 HIS A C   1 
ATOM   2380 O O   . HIS A 1 344 ? 36.455  13.674  20.529  1.00 69.38  ? 338 HIS A O   1 
ATOM   2381 C CB  . HIS A 1 344 ? 38.914  14.812  20.894  1.00 68.17  ? 338 HIS A CB  1 
ATOM   2382 C CG  . HIS A 1 344 ? 40.047  15.761  21.122  1.00 67.05  ? 338 HIS A CG  1 
ATOM   2383 N ND1 . HIS A 1 344 ? 39.879  17.119  20.965  1.00 66.68  ? 338 HIS A ND1 1 
ATOM   2384 C CD2 . HIS A 1 344 ? 41.319  15.511  21.494  1.00 66.80  ? 338 HIS A CD2 1 
ATOM   2385 C CE1 . HIS A 1 344 ? 41.053  17.662  21.245  1.00 67.93  ? 338 HIS A CE1 1 
ATOM   2386 N NE2 . HIS A 1 344 ? 41.952  16.722  21.571  1.00 68.73  ? 338 HIS A NE2 1 
ATOM   2387 N N   . PRO A 1 345 ? 35.497  14.547  22.381  1.00 68.01  ? 339 PRO A N   1 
ATOM   2388 C CA  . PRO A 1 345 ? 34.137  14.182  21.973  1.00 64.34  ? 339 PRO A CA  1 
ATOM   2389 C C   . PRO A 1 345 ? 33.647  15.063  20.828  1.00 57.70  ? 339 PRO A C   1 
ATOM   2390 O O   . PRO A 1 345 ? 32.686  14.722  20.160  1.00 58.98  ? 339 PRO A O   1 
ATOM   2391 C CB  . PRO A 1 345 ? 33.324  14.367  23.259  1.00 63.12  ? 339 PRO A CB  1 
ATOM   2392 C CG  . PRO A 1 345 ? 34.074  15.418  24.034  1.00 63.20  ? 339 PRO A CG  1 
ATOM   2393 C CD  . PRO A 1 345 ? 35.537  15.240  23.682  1.00 65.11  ? 339 PRO A CD  1 
ATOM   2394 N N   . ASP A 1 346 ? 34.327  16.188  20.602  1.00 56.71  ? 340 ASP A N   1 
ATOM   2395 C CA  . ASP A 1 346 ? 34.014  17.083  19.500  1.00 61.62  ? 340 ASP A CA  1 
ATOM   2396 C C   . ASP A 1 346 ? 34.558  16.655  18.134  1.00 61.51  ? 340 ASP A C   1 
ATOM   2397 O O   . ASP A 1 346 ? 34.572  17.452  17.198  1.00 62.48  ? 340 ASP A O   1 
ATOM   2398 C CB  . ASP A 1 346 ? 34.563  18.482  19.838  1.00 64.20  ? 340 ASP A CB  1 
ATOM   2399 C CG  . ASP A 1 346 ? 36.027  18.464  20.211  1.00 66.98  ? 340 ASP A CG  1 
ATOM   2400 O OD1 . ASP A 1 346 ? 36.415  17.594  21.028  1.00 70.67  ? 340 ASP A OD1 1 
ATOM   2401 O OD2 . ASP A 1 346 ? 36.789  19.330  19.703  1.00 67.55  ? 340 ASP A OD2 1 
ATOM   2402 N N   . TYR A 1 347 ? 35.017  15.404  18.023  1.00 58.22  ? 341 TYR A N   1 
ATOM   2403 C CA  . TYR A 1 347 ? 35.619  14.918  16.796  1.00 55.76  ? 341 TYR A CA  1 
ATOM   2404 C C   . TYR A 1 347 ? 34.759  13.790  16.240  1.00 54.57  ? 341 TYR A C   1 
ATOM   2405 O O   . TYR A 1 347 ? 34.168  13.033  16.999  1.00 52.12  ? 341 TYR A O   1 
ATOM   2406 C CB  . TYR A 1 347 ? 37.048  14.413  17.039  1.00 55.07  ? 341 TYR A CB  1 
ATOM   2407 C CG  . TYR A 1 347 ? 38.140  15.449  17.224  1.00 55.90  ? 341 TYR A CG  1 
ATOM   2408 C CD1 . TYR A 1 347 ? 37.859  16.811  17.209  1.00 57.59  ? 341 TYR A CD1 1 
ATOM   2409 C CD2 . TYR A 1 347 ? 39.461  15.065  17.404  1.00 57.55  ? 341 TYR A CD2 1 
ATOM   2410 C CE1 . TYR A 1 347 ? 38.870  17.758  17.364  1.00 56.84  ? 341 TYR A CE1 1 
ATOM   2411 C CE2 . TYR A 1 347 ? 40.475  15.998  17.563  1.00 57.26  ? 341 TYR A CE2 1 
ATOM   2412 C CZ  . TYR A 1 347 ? 40.177  17.342  17.549  1.00 58.40  ? 341 TYR A CZ  1 
ATOM   2413 O OH  . TYR A 1 347 ? 41.214  18.227  17.706  1.00 61.19  ? 341 TYR A OH  1 
ATOM   2414 N N   . SER A 1 348 ? 34.684  13.691  14.909  1.00 54.44  ? 342 SER A N   1 
ATOM   2415 C CA  . SER A 1 348 ? 34.099  12.514  14.293  1.00 53.67  ? 342 SER A CA  1 
ATOM   2416 C C   . SER A 1 348 ? 35.021  11.321  14.523  1.00 52.47  ? 342 SER A C   1 
ATOM   2417 O O   . SER A 1 348 ? 36.238  11.479  14.598  1.00 53.42  ? 342 SER A O   1 
ATOM   2418 C CB  . SER A 1 348 ? 33.878  12.717  12.801  1.00 52.76  ? 342 SER A CB  1 
ATOM   2419 O OG  . SER A 1 348 ? 35.097  12.809  12.087  1.00 51.19  ? 342 SER A OG  1 
ATOM   2420 N N   . VAL A 1 349 ? 34.423  10.131  14.594  1.00 51.79  ? 343 VAL A N   1 
ATOM   2421 C CA  . VAL A 1 349 ? 35.172  8.891   14.672  1.00 51.57  ? 343 VAL A CA  1 
ATOM   2422 C C   . VAL A 1 349 ? 36.179  8.792   13.526  1.00 54.67  ? 343 VAL A C   1 
ATOM   2423 O O   . VAL A 1 349 ? 37.342  8.467   13.765  1.00 56.86  ? 343 VAL A O   1 
ATOM   2424 C CB  . VAL A 1 349 ? 34.230  7.665   14.680  1.00 51.86  ? 343 VAL A CB  1 
ATOM   2425 C CG1 . VAL A 1 349 ? 35.031  6.372   14.686  1.00 52.79  ? 343 VAL A CG1 1 
ATOM   2426 C CG2 . VAL A 1 349 ? 33.249  7.708   15.853  1.00 50.03  ? 343 VAL A CG2 1 
ATOM   2427 N N   . VAL A 1 350 ? 35.728  9.076   12.288  1.00 55.85  ? 344 VAL A N   1 
ATOM   2428 C CA  . VAL A 1 350 ? 36.580  8.954   11.111  1.00 54.35  ? 344 VAL A CA  1 
ATOM   2429 C C   . VAL A 1 350 ? 37.800  9.867   11.226  1.00 51.77  ? 344 VAL A C   1 
ATOM   2430 O O   . VAL A 1 350 ? 38.898  9.461   10.851  1.00 56.38  ? 344 VAL A O   1 
ATOM   2431 C CB  . VAL A 1 350 ? 35.859  9.180   9.724   1.00 54.93  ? 344 VAL A CB  1 
ATOM   2432 C CG1 . VAL A 1 350 ? 34.920  8.030   9.383   1.00 55.72  ? 344 VAL A CG1 1 
ATOM   2433 C CG2 . VAL A 1 350 ? 35.134  10.512  9.655   1.00 54.79  ? 344 VAL A CG2 1 
ATOM   2434 N N   . LEU A 1 351 ? 37.614  11.092  11.732  1.00 47.64  ? 345 LEU A N   1 
ATOM   2435 C CA  . LEU A 1 351 ? 38.734  11.998  11.956  1.00 49.29  ? 345 LEU A CA  1 
ATOM   2436 C C   . LEU A 1 351 ? 39.804  11.362  12.848  1.00 51.85  ? 345 LEU A C   1 
ATOM   2437 O O   . LEU A 1 351 ? 40.992  11.371  12.509  1.00 48.61  ? 345 LEU A O   1 
ATOM   2438 C CB  . LEU A 1 351 ? 38.268  13.310  12.611  1.00 47.97  ? 345 LEU A CB  1 
ATOM   2439 C CG  . LEU A 1 351 ? 39.375  14.225  13.097  1.00 48.19  ? 345 LEU A CG  1 
ATOM   2440 C CD1 . LEU A 1 351 ? 40.270  14.640  11.948  1.00 49.32  ? 345 LEU A CD1 1 
ATOM   2441 C CD2 . LEU A 1 351 ? 38.814  15.474  13.791  1.00 47.91  ? 345 LEU A CD2 1 
ATOM   2442 N N   . LEU A 1 352 ? 39.356  10.824  13.996  1.00 51.88  ? 346 LEU A N   1 
ATOM   2443 C CA  . LEU A 1 352 ? 40.232  10.158  14.942  1.00 51.30  ? 346 LEU A CA  1 
ATOM   2444 C C   . LEU A 1 352 ? 40.924  8.963   14.292  1.00 50.34  ? 346 LEU A C   1 
ATOM   2445 O O   . LEU A 1 352 ? 42.092  8.701   14.567  1.00 50.54  ? 346 LEU A O   1 
ATOM   2446 C CB  . LEU A 1 352 ? 39.430  9.719   16.175  1.00 53.18  ? 346 LEU A CB  1 
ATOM   2447 C CG  . LEU A 1 352 ? 38.946  10.855  17.100  1.00 54.51  ? 346 LEU A CG  1 
ATOM   2448 C CD1 . LEU A 1 352 ? 37.978  10.337  18.103  1.00 57.02  ? 346 LEU A CD1 1 
ATOM   2449 C CD2 . LEU A 1 352 ? 40.088  11.513  17.822  1.00 54.49  ? 346 LEU A CD2 1 
ATOM   2450 N N   . LEU A 1 353 ? 40.211  8.250   13.415  1.00 49.18  ? 347 LEU A N   1 
ATOM   2451 C CA  . LEU A 1 353 ? 40.842  7.199   12.634  1.00 50.01  ? 347 LEU A CA  1 
ATOM   2452 C C   . LEU A 1 353 ? 41.899  7.755   11.671  1.00 49.88  ? 347 LEU A C   1 
ATOM   2453 O O   . LEU A 1 353 ? 42.916  7.101   11.449  1.00 51.75  ? 347 LEU A O   1 
ATOM   2454 C CB  . LEU A 1 353 ? 39.786  6.353   11.895  1.00 49.12  ? 347 LEU A CB  1 
ATOM   2455 C CG  . LEU A 1 353 ? 38.894  5.489   12.796  1.00 49.28  ? 347 LEU A CG  1 
ATOM   2456 C CD1 . LEU A 1 353 ? 37.939  4.638   11.993  1.00 48.56  ? 347 LEU A CD1 1 
ATOM   2457 C CD2 . LEU A 1 353 ? 39.712  4.582   13.673  1.00 49.30  ? 347 LEU A CD2 1 
ATOM   2458 N N   . ARG A 1 354 ? 41.712  8.964   11.120  1.00 45.99  ? 348 ARG A N   1 
ATOM   2459 C CA  . ARG A 1 354 ? 42.764  9.525   10.284  1.00 45.67  ? 348 ARG A CA  1 
ATOM   2460 C C   . ARG A 1 354 ? 44.014  9.804   11.114  1.00 46.82  ? 348 ARG A C   1 
ATOM   2461 O O   . ARG A 1 354 ? 45.122  9.516   10.678  1.00 47.54  ? 348 ARG A O   1 
ATOM   2462 C CB  . ARG A 1 354 ? 42.354  10.817  9.577   1.00 45.15  ? 348 ARG A CB  1 
ATOM   2463 C CG  . ARG A 1 354 ? 41.356  10.656  8.481   1.00 43.81  ? 348 ARG A CG  1 
ATOM   2464 C CD  . ARG A 1 354 ? 40.801  12.007  8.116   1.00 44.70  ? 348 ARG A CD  1 
ATOM   2465 N NE  . ARG A 1 354 ? 39.592  11.887  7.309   1.00 45.83  ? 348 ARG A NE  1 
ATOM   2466 C CZ  . ARG A 1 354 ? 38.373  12.245  7.694   1.00 46.32  ? 348 ARG A CZ  1 
ATOM   2467 N NH1 . ARG A 1 354 ? 38.173  13.194  8.594   1.00 48.97  ? 348 ARG A NH1 1 
ATOM   2468 N NH2 . ARG A 1 354 ? 37.325  11.647  7.146   1.00 47.10  ? 348 ARG A NH2 1 
ATOM   2469 N N   . LEU A 1 355 ? 43.824  10.377  12.308  1.00 48.98  ? 349 LEU A N   1 
ATOM   2470 C CA  . LEU A 1 355 ? 44.929  10.727  13.192  1.00 50.72  ? 349 LEU A CA  1 
ATOM   2471 C C   . LEU A 1 355 ? 45.737  9.488   13.590  1.00 50.60  ? 349 LEU A C   1 
ATOM   2472 O O   . LEU A 1 355 ? 46.946  9.438   13.401  1.00 50.78  ? 349 LEU A O   1 
ATOM   2473 C CB  . LEU A 1 355 ? 44.384  11.447  14.451  1.00 51.29  ? 349 LEU A CB  1 
ATOM   2474 C CG  . LEU A 1 355 ? 43.598  12.757  14.216  1.00 51.79  ? 349 LEU A CG  1 
ATOM   2475 C CD1 . LEU A 1 355 ? 43.344  13.500  15.529  1.00 52.23  ? 349 LEU A CD1 1 
ATOM   2476 C CD2 . LEU A 1 355 ? 44.305  13.681  13.253  1.00 50.22  ? 349 LEU A CD2 1 
ATOM   2477 N N   . ALA A 1 356 ? 45.054  8.469   14.114  1.00 49.69  ? 350 ALA A N   1 
ATOM   2478 C CA  . ALA A 1 356 ? 45.688  7.195   14.392  1.00 49.45  ? 350 ALA A CA  1 
ATOM   2479 C C   . ALA A 1 356 ? 46.444  6.658   13.176  1.00 50.59  ? 350 ALA A C   1 
ATOM   2480 O O   . ALA A 1 356 ? 47.583  6.230   13.320  1.00 51.30  ? 350 ALA A O   1 
ATOM   2481 C CB  . ALA A 1 356 ? 44.660  6.187   14.880  1.00 47.63  ? 350 ALA A CB  1 
ATOM   2482 N N   . LYS A 1 357 ? 45.827  6.695   11.985  1.00 53.23  ? 351 LYS A N   1 
ATOM   2483 C CA  . LYS A 1 357 ? 46.491  6.264   10.755  1.00 56.43  ? 351 LYS A CA  1 
ATOM   2484 C C   . LYS A 1 357 ? 47.762  7.064   10.479  1.00 53.25  ? 351 LYS A C   1 
ATOM   2485 O O   . LYS A 1 357 ? 48.798  6.491   10.137  1.00 49.94  ? 351 LYS A O   1 
ATOM   2486 C CB  . LYS A 1 357 ? 45.583  6.384   9.512   1.00 59.98  ? 351 LYS A CB  1 
ATOM   2487 C CG  . LYS A 1 357 ? 44.704  5.170   9.251   1.00 66.76  ? 351 LYS A CG  1 
ATOM   2488 C CD  . LYS A 1 357 ? 43.746  5.378   8.052   1.00 74.09  ? 351 LYS A CD  1 
ATOM   2489 C CE  . LYS A 1 357 ? 42.642  4.323   7.950   1.00 80.14  ? 351 LYS A CE  1 
ATOM   2490 N NZ  . LYS A 1 357 ? 43.072  3.094   7.206   1.00 82.63  ? 351 LYS A NZ  1 
ATOM   2491 N N   . THR A 1 358 ? 47.654  8.390   10.620  1.00 50.06  ? 352 THR A N   1 
ATOM   2492 C CA  . THR A 1 358 ? 48.785  9.279   10.439  1.00 51.62  ? 352 THR A CA  1 
ATOM   2493 C C   . THR A 1 358 ? 49.926  8.879   11.373  1.00 55.02  ? 352 THR A C   1 
ATOM   2494 O O   . THR A 1 358 ? 51.074  8.741   10.948  1.00 55.93  ? 352 THR A O   1 
ATOM   2495 C CB  . THR A 1 358 ? 48.320  10.706  10.670  1.00 51.11  ? 352 THR A CB  1 
ATOM   2496 O OG1 . THR A 1 358 ? 47.255  10.981  9.786   1.00 54.18  ? 352 THR A OG1 1 
ATOM   2497 C CG2 . THR A 1 358 ? 49.377  11.702  10.431  1.00 52.10  ? 352 THR A CG2 1 
ATOM   2498 N N   . TYR A 1 359 ? 49.581  8.700   12.655  1.00 54.72  ? 353 TYR A N   1 
ATOM   2499 C CA  . TYR A 1 359 ? 50.538  8.335   13.681  1.00 51.87  ? 353 TYR A CA  1 
ATOM   2500 C C   . TYR A 1 359 ? 51.209  7.013   13.318  1.00 50.50  ? 353 TYR A C   1 
ATOM   2501 O O   . TYR A 1 359 ? 52.428  6.891   13.400  1.00 48.82  ? 353 TYR A O   1 
ATOM   2502 C CB  . TYR A 1 359 ? 49.830  8.223   15.028  1.00 52.59  ? 353 TYR A CB  1 
ATOM   2503 C CG  . TYR A 1 359 ? 50.771  7.962   16.181  1.00 55.28  ? 353 TYR A CG  1 
ATOM   2504 C CD1 . TYR A 1 359 ? 51.770  8.872   16.508  1.00 57.33  ? 353 TYR A CD1 1 
ATOM   2505 C CD2 . TYR A 1 359 ? 50.676  6.803   16.936  1.00 53.87  ? 353 TYR A CD2 1 
ATOM   2506 C CE1 . TYR A 1 359 ? 52.639  8.642   17.561  1.00 56.85  ? 353 TYR A CE1 1 
ATOM   2507 C CE2 . TYR A 1 359 ? 51.542  6.561   17.991  1.00 56.67  ? 353 TYR A CE2 1 
ATOM   2508 C CZ  . TYR A 1 359 ? 52.524  7.487   18.303  1.00 57.27  ? 353 TYR A CZ  1 
ATOM   2509 O OH  . TYR A 1 359 ? 53.407  7.277   19.339  1.00 58.38  ? 353 TYR A OH  1 
ATOM   2510 N N   . GLU A 1 360 ? 50.396  6.029   12.921  1.00 49.39  ? 354 GLU A N   1 
ATOM   2511 C CA  . GLU A 1 360 ? 50.910  4.722   12.543  1.00 51.03  ? 354 GLU A CA  1 
ATOM   2512 C C   . GLU A 1 360 ? 51.896  4.849   11.392  1.00 49.76  ? 354 GLU A C   1 
ATOM   2513 O O   . GLU A 1 360 ? 52.969  4.262   11.451  1.00 51.54  ? 354 GLU A O   1 
ATOM   2514 C CB  . GLU A 1 360 ? 49.820  3.737   12.108  1.00 51.36  ? 354 GLU A CB  1 
ATOM   2515 C CG  . GLU A 1 360 ? 50.404  2.404   11.665  1.00 51.60  ? 354 GLU A CG  1 
ATOM   2516 C CD  . GLU A 1 360 ? 49.392  1.337   11.312  1.00 53.50  ? 354 GLU A CD  1 
ATOM   2517 O OE1 . GLU A 1 360 ? 48.230  1.682   11.015  1.00 55.70  ? 354 GLU A OE1 1 
ATOM   2518 O OE2 . GLU A 1 360 ? 49.757  0.143   11.356  1.00 59.01  ? 354 GLU A OE2 1 
ATOM   2519 N N   . THR A 1 361 ? 51.512  5.607   10.359  1.00 48.49  ? 355 THR A N   1 
ATOM   2520 C CA  . THR A 1 361 ? 52.396  5.857   9.231   1.00 49.75  ? 355 THR A CA  1 
ATOM   2521 C C   . THR A 1 361 ? 53.694  6.538   9.654   1.00 50.91  ? 355 THR A C   1 
ATOM   2522 O O   . THR A 1 361 ? 54.754  6.239   9.117   1.00 51.86  ? 355 THR A O   1 
ATOM   2523 C CB  . THR A 1 361 ? 51.690  6.658   8.184   1.00 49.81  ? 355 THR A CB  1 
ATOM   2524 O OG1 . THR A 1 361 ? 50.586  5.884   7.723   1.00 51.74  ? 355 THR A OG1 1 
ATOM   2525 C CG2 . THR A 1 361 ? 52.575  6.996   7.018   1.00 49.45  ? 355 THR A CG2 1 
ATOM   2526 N N   . THR A 1 362 ? 53.614  7.429   10.642  1.00 52.57  ? 356 THR A N   1 
ATOM   2527 C CA  . THR A 1 362 ? 54.800  8.112   11.125  1.00 53.74  ? 356 THR A CA  1 
ATOM   2528 C C   . THR A 1 362 ? 55.757  7.179   11.872  1.00 55.49  ? 356 THR A C   1 
ATOM   2529 O O   . THR A 1 362 ? 56.967  7.275   11.695  1.00 56.21  ? 356 THR A O   1 
ATOM   2530 C CB  . THR A 1 362 ? 54.373  9.324   11.917  1.00 52.11  ? 356 THR A CB  1 
ATOM   2531 O OG1 . THR A 1 362 ? 53.689  10.179  11.013  1.00 54.31  ? 356 THR A OG1 1 
ATOM   2532 C CG2 . THR A 1 362 ? 55.531  10.065  12.504  1.00 52.24  ? 356 THR A CG2 1 
ATOM   2533 N N   . LEU A 1 363 ? 55.232  6.259   12.687  1.00 54.81  ? 357 LEU A N   1 
ATOM   2534 C CA  . LEU A 1 363 ? 56.100  5.305   13.356  1.00 56.37  ? 357 LEU A CA  1 
ATOM   2535 C C   . LEU A 1 363 ? 56.735  4.314   12.378  1.00 56.50  ? 357 LEU A C   1 
ATOM   2536 O O   . LEU A 1 363 ? 57.884  3.933   12.551  1.00 60.76  ? 357 LEU A O   1 
ATOM   2537 C CB  . LEU A 1 363 ? 55.337  4.560   14.462  1.00 56.72  ? 357 LEU A CB  1 
ATOM   2538 C CG  . LEU A 1 363 ? 54.826  5.430   15.619  1.00 56.01  ? 357 LEU A CG  1 
ATOM   2539 C CD1 . LEU A 1 363 ? 54.511  4.595   16.818  1.00 55.62  ? 357 LEU A CD1 1 
ATOM   2540 C CD2 . LEU A 1 363 ? 55.825  6.507   16.002  1.00 56.44  ? 357 LEU A CD2 1 
ATOM   2541 N N   . GLU A 1 364 ? 56.014  3.921   11.330  1.00 54.89  ? 358 GLU A N   1 
ATOM   2542 C CA  . GLU A 1 364 ? 56.556  2.967   10.379  1.00 60.21  ? 358 GLU A CA  1 
ATOM   2543 C C   . GLU A 1 364 ? 57.771  3.475   9.602   1.00 64.12  ? 358 GLU A C   1 
ATOM   2544 O O   . GLU A 1 364 ? 58.626  2.678   9.226   1.00 65.76  ? 358 GLU A O   1 
ATOM   2545 C CB  . GLU A 1 364 ? 55.470  2.533   9.407   1.00 60.85  ? 358 GLU A CB  1 
ATOM   2546 C CG  . GLU A 1 364 ? 54.495  1.582   10.052  1.00 62.61  ? 358 GLU A CG  1 
ATOM   2547 C CD  . GLU A 1 364 ? 53.363  1.142   9.155   1.00 64.32  ? 358 GLU A CD  1 
ATOM   2548 O OE1 . GLU A 1 364 ? 53.209  1.729   8.058   1.00 63.69  ? 358 GLU A OE1 1 
ATOM   2549 O OE2 . GLU A 1 364 ? 52.643  0.193   9.545   1.00 64.20  ? 358 GLU A OE2 1 
ATOM   2550 N N   . LYS A 1 365 ? 57.831  4.791   9.354   1.00 67.77  ? 359 LYS A N   1 
ATOM   2551 C CA  . LYS A 1 365 ? 58.960  5.400   8.667   1.00 69.37  ? 359 LYS A CA  1 
ATOM   2552 C C   . LYS A 1 365 ? 60.011  5.857   9.679   1.00 67.01  ? 359 LYS A C   1 
ATOM   2553 O O   . LYS A 1 365 ? 61.199  5.621   9.490   1.00 69.05  ? 359 LYS A O   1 
ATOM   2554 C CB  . LYS A 1 365 ? 58.492  6.573   7.761   1.00 74.31  ? 359 LYS A CB  1 
ATOM   2555 C CG  . LYS A 1 365 ? 58.324  7.912   8.485   1.00 81.51  ? 359 LYS A CG  1 
ATOM   2556 C CD  . LYS A 1 365 ? 57.549  9.001   7.708   1.00 86.13  ? 359 LYS A CD  1 
ATOM   2557 C CE  . LYS A 1 365 ? 57.414  10.280  8.539   1.00 88.83  ? 359 LYS A CE  1 
ATOM   2558 N NZ  . LYS A 1 365 ? 56.246  11.118  8.133   1.00 90.46  ? 359 LYS A NZ  1 
ATOM   2559 N N   . CYS A 1 366 ? 59.569  6.480   10.775  1.00 67.66  ? 360 CYS A N   1 
ATOM   2560 C CA  . CYS A 1 366 ? 60.480  7.102   11.724  1.00 68.11  ? 360 CYS A CA  1 
ATOM   2561 C C   . CYS A 1 366 ? 61.315  6.082   12.492  1.00 65.41  ? 360 CYS A C   1 
ATOM   2562 O O   . CYS A 1 366 ? 62.500  6.295   12.734  1.00 62.99  ? 360 CYS A O   1 
ATOM   2563 C CB  . CYS A 1 366 ? 59.722  8.022   12.683  1.00 68.95  ? 360 CYS A CB  1 
ATOM   2564 S SG  . CYS A 1 366 ? 59.180  9.586   11.934  1.00 71.58  ? 360 CYS A SG  1 
ATOM   2565 N N   . CYS A 1 367 ? 60.689  4.965   12.862  1.00 64.16  ? 361 CYS A N   1 
ATOM   2566 C CA  . CYS A 1 367 ? 61.379  3.946   13.629  1.00 64.34  ? 361 CYS A CA  1 
ATOM   2567 C C   . CYS A 1 367 ? 62.426  3.196   12.805  1.00 62.37  ? 361 CYS A C   1 
ATOM   2568 O O   . CYS A 1 367 ? 63.294  2.539   13.374  1.00 66.12  ? 361 CYS A O   1 
ATOM   2569 C CB  . CYS A 1 367 ? 60.364  3.014   14.283  1.00 64.75  ? 361 CYS A CB  1 
ATOM   2570 S SG  . CYS A 1 367 ? 59.286  3.860   15.483  1.00 64.50  ? 361 CYS A SG  1 
ATOM   2571 N N   . ALA A 1 368 ? 62.374  3.349   11.477  1.00 60.50  ? 362 ALA A N   1 
ATOM   2572 C CA  . ALA A 1 368 ? 63.404  2.836   10.588  1.00 60.95  ? 362 ALA A CA  1 
ATOM   2573 C C   . ALA A 1 368 ? 64.516  3.840   10.284  1.00 64.66  ? 362 ALA A C   1 
ATOM   2574 O O   . ALA A 1 368 ? 65.452  3.512   9.564   1.00 68.60  ? 362 ALA A O   1 
ATOM   2575 C CB  . ALA A 1 368 ? 62.765  2.377   9.293   1.00 59.17  ? 362 ALA A CB  1 
ATOM   2576 N N   . ALA A 1 369 ? 64.432  5.053   10.840  1.00 64.93  ? 363 ALA A N   1 
ATOM   2577 C CA  . ALA A 1 369 ? 65.386  6.108   10.531  1.00 67.15  ? 363 ALA A CA  1 
ATOM   2578 C C   . ALA A 1 369 ? 66.520  6.222   11.553  1.00 71.04  ? 363 ALA A C   1 
ATOM   2579 O O   . ALA A 1 369 ? 66.525  5.532   12.573  1.00 73.95  ? 363 ALA A O   1 
ATOM   2580 C CB  . ALA A 1 369 ? 64.646  7.439   10.429  1.00 68.26  ? 363 ALA A CB  1 
ATOM   2581 N N   . ALA A 1 370 ? 67.459  7.133   11.272  1.00 74.01  ? 364 ALA A N   1 
ATOM   2582 C CA  . ALA A 1 370 ? 68.693  7.285   12.029  1.00 77.78  ? 364 ALA A CA  1 
ATOM   2583 C C   . ALA A 1 370 ? 68.498  7.637   13.502  1.00 81.22  ? 364 ALA A C   1 
ATOM   2584 O O   . ALA A 1 370 ? 69.024  6.945   14.373  1.00 84.76  ? 364 ALA A O   1 
ATOM   2585 C CB  . ALA A 1 370 ? 69.562  8.343   11.359  1.00 80.38  ? 364 ALA A CB  1 
ATOM   2586 N N   . ASP A 1 371 ? 67.783  8.739   13.770  1.00 82.83  ? 365 ASP A N   1 
ATOM   2587 C CA  . ASP A 1 371 ? 67.377  9.093   15.122  1.00 80.63  ? 365 ASP A CA  1 
ATOM   2588 C C   . ASP A 1 371 ? 65.853  9.183   15.131  1.00 79.96  ? 365 ASP A C   1 
ATOM   2589 O O   . ASP A 1 371 ? 65.284  10.242  14.855  1.00 72.60  ? 365 ASP A O   1 
ATOM   2590 C CB  . ASP A 1 371 ? 68.021  10.405  15.602  1.00 82.20  ? 365 ASP A CB  1 
ATOM   2591 C CG  . ASP A 1 371 ? 67.726  10.725  17.066  1.00 88.61  ? 365 ASP A CG  1 
ATOM   2592 O OD1 . ASP A 1 371 ? 68.234  9.991   17.958  1.00 90.97  ? 365 ASP A OD1 1 
ATOM   2593 O OD2 . ASP A 1 371 ? 66.981  11.693  17.323  1.00 91.73  ? 365 ASP A OD2 1 
ATOM   2594 N N   . PRO A 1 372 ? 65.147  8.060   15.406  1.00 79.78  ? 366 PRO A N   1 
ATOM   2595 C CA  . PRO A 1 372 ? 63.682  8.051   15.413  1.00 78.49  ? 366 PRO A CA  1 
ATOM   2596 C C   . PRO A 1 372 ? 63.087  9.228   16.179  1.00 76.95  ? 366 PRO A C   1 
ATOM   2597 O O   . PRO A 1 372 ? 62.253  9.953   15.643  1.00 75.08  ? 366 PRO A O   1 
ATOM   2598 C CB  . PRO A 1 372 ? 63.348  6.709   16.065  1.00 76.95  ? 366 PRO A CB  1 
ATOM   2599 C CG  . PRO A 1 372 ? 64.525  5.834   15.752  1.00 76.85  ? 366 PRO A CG  1 
ATOM   2600 C CD  . PRO A 1 372 ? 65.724  6.740   15.714  1.00 76.84  ? 366 PRO A CD  1 
ATOM   2601 N N   . HIS A 1 373 ? 63.566  9.418   17.414  1.00 77.07  ? 367 HIS A N   1 
ATOM   2602 C CA  . HIS A 1 373 ? 63.078  10.448  18.320  1.00 79.45  ? 367 HIS A CA  1 
ATOM   2603 C C   . HIS A 1 373 ? 62.906  11.821  17.671  1.00 81.38  ? 367 HIS A C   1 
ATOM   2604 O O   . HIS A 1 373 ? 61.858  12.450  17.802  1.00 78.50  ? 367 HIS A O   1 
ATOM   2605 C CB  . HIS A 1 373 ? 64.044  10.549  19.501  1.00 81.16  ? 367 HIS A CB  1 
ATOM   2606 C CG  . HIS A 1 373 ? 63.616  11.502  20.569  1.00 80.91  ? 367 HIS A CG  1 
ATOM   2607 N ND1 . HIS A 1 373 ? 62.462  11.296  21.293  1.00 83.26  ? 367 HIS A ND1 1 
ATOM   2608 C CD2 . HIS A 1 373 ? 64.212  12.629  21.002  1.00 82.02  ? 367 HIS A CD2 1 
ATOM   2609 C CE1 . HIS A 1 373 ? 62.385  12.304  22.145  1.00 83.03  ? 367 HIS A CE1 1 
ATOM   2610 N NE2 . HIS A 1 373 ? 63.425  13.133  22.000  1.00 85.01  ? 367 HIS A NE2 1 
ATOM   2611 N N   . GLU A 1 374 ? 63.950  12.273  16.968  1.00 84.93  ? 368 GLU A N   1 
ATOM   2612 C CA  . GLU A 1 374 ? 63.874  13.493  16.181  1.00 86.93  ? 368 GLU A CA  1 
ATOM   2613 C C   . GLU A 1 374 ? 62.769  13.365  15.133  1.00 85.87  ? 368 GLU A C   1 
ATOM   2614 O O   . GLU A 1 374 ? 61.835  14.163  15.127  1.00 90.51  ? 368 GLU A O   1 
ATOM   2615 C CB  . GLU A 1 374 ? 65.245  13.800  15.535  1.00 88.74  ? 368 GLU A CB  1 
ATOM   2616 C CG  . GLU A 1 374 ? 65.318  15.091  14.726  1.00 90.54  ? 368 GLU A CG  1 
ATOM   2617 C CD  . GLU A 1 374 ? 64.922  14.984  13.263  1.00 93.14  ? 368 GLU A CD  1 
ATOM   2618 O OE1 . GLU A 1 374 ? 63.715  14.804  12.980  1.00 95.35  ? 368 GLU A OE1 1 
ATOM   2619 O OE2 . GLU A 1 374 ? 65.822  15.079  12.396  1.00 93.88  ? 368 GLU A OE2 1 
ATOM   2620 N N   . CYS A 1 375 ? 62.872  12.333  14.281  1.00 81.36  ? 369 CYS A N   1 
ATOM   2621 C CA  . CYS A 1 375 ? 62.008  12.153  13.121  1.00 75.69  ? 369 CYS A CA  1 
ATOM   2622 C C   . CYS A 1 375 ? 60.503  12.261  13.368  1.00 72.27  ? 369 CYS A C   1 
ATOM   2623 O O   . CYS A 1 375 ? 59.774  12.709  12.490  1.00 71.30  ? 369 CYS A O   1 
ATOM   2624 C CB  . CYS A 1 375 ? 62.334  10.821  12.460  1.00 74.62  ? 369 CYS A CB  1 
ATOM   2625 S SG  . CYS A 1 375 ? 61.296  10.447  11.028  1.00 76.34  ? 369 CYS A SG  1 
ATOM   2626 N N   . TYR A 1 376 ? 60.036  11.800  14.536  1.00 70.57  ? 370 TYR A N   1 
ATOM   2627 C CA  . TYR A 1 376 ? 58.621  11.842  14.871  1.00 68.68  ? 370 TYR A CA  1 
ATOM   2628 C C   . TYR A 1 376 ? 58.301  12.893  15.930  1.00 71.35  ? 370 TYR A C   1 
ATOM   2629 O O   . TYR A 1 376 ? 57.240  12.839  16.545  1.00 71.08  ? 370 TYR A O   1 
ATOM   2630 C CB  . TYR A 1 376 ? 58.108  10.456  15.344  1.00 65.77  ? 370 TYR A CB  1 
ATOM   2631 C CG  . TYR A 1 376 ? 58.790  9.851   16.560  1.00 63.99  ? 370 TYR A CG  1 
ATOM   2632 C CD1 . TYR A 1 376 ? 58.722  10.466  17.807  1.00 62.97  ? 370 TYR A CD1 1 
ATOM   2633 C CD2 . TYR A 1 376 ? 59.471  8.646   16.471  1.00 62.33  ? 370 TYR A CD2 1 
ATOM   2634 C CE1 . TYR A 1 376 ? 59.337  9.905   18.924  1.00 61.74  ? 370 TYR A CE1 1 
ATOM   2635 C CE2 . TYR A 1 376 ? 60.088  8.078   17.579  1.00 61.15  ? 370 TYR A CE2 1 
ATOM   2636 C CZ  . TYR A 1 376 ? 60.013  8.706   18.807  1.00 61.98  ? 370 TYR A CZ  1 
ATOM   2637 O OH  . TYR A 1 376 ? 60.639  8.140   19.900  1.00 63.63  ? 370 TYR A OH  1 
ATOM   2638 N N   . ALA A 1 377 ? 59.213  13.852  16.130  1.00 75.63  ? 371 ALA A N   1 
ATOM   2639 C CA  . ALA A 1 377 ? 59.021  14.896  17.127  1.00 78.83  ? 371 ALA A CA  1 
ATOM   2640 C C   . ALA A 1 377 ? 57.927  15.883  16.719  1.00 78.64  ? 371 ALA A C   1 
ATOM   2641 O O   . ALA A 1 377 ? 57.293  16.497  17.574  1.00 80.03  ? 371 ALA A O   1 
ATOM   2642 C CB  . ALA A 1 377 ? 60.330  15.639  17.374  1.00 78.38  ? 371 ALA A CB  1 
ATOM   2643 N N   . LYS A 1 378 ? 57.705  16.002  15.406  1.00 78.50  ? 372 LYS A N   1 
ATOM   2644 C CA  . LYS A 1 378 ? 56.817  17.002  14.837  1.00 80.70  ? 372 LYS A CA  1 
ATOM   2645 C C   . LYS A 1 378 ? 55.418  16.490  14.497  1.00 75.79  ? 372 LYS A C   1 
ATOM   2646 O O   . LYS A 1 378 ? 54.665  17.182  13.817  1.00 73.90  ? 372 LYS A O   1 
ATOM   2647 C CB  . LYS A 1 378 ? 57.460  17.572  13.544  1.00 85.46  ? 372 LYS A CB  1 
ATOM   2648 C CG  . LYS A 1 378 ? 57.957  16.522  12.492  1.00 89.70  ? 372 LYS A CG  1 
ATOM   2649 C CD  . LYS A 1 378 ? 56.887  15.523  11.973  1.00 90.60  ? 372 LYS A CD  1 
ATOM   2650 C CE  . LYS A 1 378 ? 57.418  14.630  10.868  1.00 92.81  ? 372 LYS A CE  1 
ATOM   2651 N NZ  . LYS A 1 378 ? 56.431  13.590  10.446  1.00 93.41  ? 372 LYS A NZ  1 
ATOM   2652 N N   . VAL A 1 379 ? 55.073  15.281  14.960  1.00 70.72  ? 373 VAL A N   1 
ATOM   2653 C CA  . VAL A 1 379 ? 53.945  14.557  14.396  1.00 66.49  ? 373 VAL A CA  1 
ATOM   2654 C C   . VAL A 1 379 ? 52.619  15.245  14.708  1.00 65.51  ? 373 VAL A C   1 
ATOM   2655 O O   . VAL A 1 379 ? 51.726  15.257  13.870  1.00 67.11  ? 373 VAL A O   1 
ATOM   2656 C CB  . VAL A 1 379 ? 53.931  13.062  14.805  1.00 64.51  ? 373 VAL A CB  1 
ATOM   2657 C CG1 . VAL A 1 379 ? 53.754  12.875  16.303  1.00 65.59  ? 373 VAL A CG1 1 
ATOM   2658 C CG2 . VAL A 1 379 ? 52.860  12.296  14.030  1.00 63.77  ? 373 VAL A CG2 1 
ATOM   2659 N N   . PHE A 1 380 ? 52.513  15.860  15.887  1.00 67.06  ? 374 PHE A N   1 
ATOM   2660 C CA  . PHE A 1 380 ? 51.322  16.612  16.250  1.00 66.98  ? 374 PHE A CA  1 
ATOM   2661 C C   . PHE A 1 380 ? 51.054  17.788  15.312  1.00 69.69  ? 374 PHE A C   1 
ATOM   2662 O O   . PHE A 1 380 ? 49.905  18.176  15.113  1.00 70.65  ? 374 PHE A O   1 
ATOM   2663 C CB  . PHE A 1 380 ? 51.416  17.085  17.700  1.00 64.93  ? 374 PHE A CB  1 
ATOM   2664 C CG  . PHE A 1 380 ? 51.030  16.014  18.681  1.00 67.49  ? 374 PHE A CG  1 
ATOM   2665 C CD1 . PHE A 1 380 ? 51.422  14.699  18.490  1.00 70.81  ? 374 PHE A CD1 1 
ATOM   2666 C CD2 . PHE A 1 380 ? 50.283  16.317  19.800  1.00 69.47  ? 374 PHE A CD2 1 
ATOM   2667 C CE1 . PHE A 1 380 ? 51.060  13.710  19.400  1.00 72.92  ? 374 PHE A CE1 1 
ATOM   2668 C CE2 . PHE A 1 380 ? 49.938  15.331  20.712  1.00 71.92  ? 374 PHE A CE2 1 
ATOM   2669 C CZ  . PHE A 1 380 ? 50.326  14.034  20.508  1.00 72.54  ? 374 PHE A CZ  1 
ATOM   2670 N N   . ASP A 1 381 ? 52.110  18.335  14.707  1.00 74.67  ? 375 ASP A N   1 
ATOM   2671 C CA  . ASP A 1 381 ? 51.944  19.378  13.709  1.00 79.23  ? 375 ASP A CA  1 
ATOM   2672 C C   . ASP A 1 381 ? 51.258  18.832  12.456  1.00 80.24  ? 375 ASP A C   1 
ATOM   2673 O O   . ASP A 1 381 ? 50.640  19.593  11.718  1.00 80.53  ? 375 ASP A O   1 
ATOM   2674 C CB  . ASP A 1 381 ? 53.301  20.036  13.369  1.00 83.40  ? 375 ASP A CB  1 
ATOM   2675 C CG  . ASP A 1 381 ? 54.002  20.701  14.553  1.00 86.85  ? 375 ASP A CG  1 
ATOM   2676 O OD1 . ASP A 1 381 ? 53.390  20.776  15.646  1.00 89.91  ? 375 ASP A OD1 1 
ATOM   2677 O OD2 . ASP A 1 381 ? 55.163  21.138  14.388  1.00 87.80  ? 375 ASP A OD2 1 
ATOM   2678 N N   . GLU A 1 382 ? 51.368  17.515  12.222  1.00 80.04  ? 376 GLU A N   1 
ATOM   2679 C CA  . GLU A 1 382 ? 50.655  16.868  11.131  1.00 79.79  ? 376 GLU A CA  1 
ATOM   2680 C C   . GLU A 1 382 ? 49.152  16.753  11.373  1.00 77.94  ? 376 GLU A C   1 
ATOM   2681 O O   . GLU A 1 382 ? 48.380  16.740  10.419  1.00 77.61  ? 376 GLU A O   1 
ATOM   2682 C CB  . GLU A 1 382 ? 51.200  15.468  10.863  1.00 81.33  ? 376 GLU A CB  1 
ATOM   2683 C CG  . GLU A 1 382 ? 52.527  15.471  10.142  1.00 85.18  ? 376 GLU A CG  1 
ATOM   2684 C CD  . GLU A 1 382 ? 53.016  14.081  9.807   1.00 89.85  ? 376 GLU A CD  1 
ATOM   2685 O OE1 . GLU A 1 382 ? 53.394  13.339  10.744  1.00 93.02  ? 376 GLU A OE1 1 
ATOM   2686 O OE2 . GLU A 1 382 ? 52.994  13.722  8.608   1.00 93.37  ? 376 GLU A OE2 1 
ATOM   2687 N N   . PHE A 1 383 ? 48.750  16.654  12.645  1.00 75.42  ? 377 PHE A N   1 
ATOM   2688 C CA  . PHE A 1 383 ? 47.347  16.496  12.995  1.00 76.40  ? 377 PHE A CA  1 
ATOM   2689 C C   . PHE A 1 383 ? 46.526  17.776  12.868  1.00 78.74  ? 377 PHE A C   1 
ATOM   2690 O O   . PHE A 1 383 ? 45.302  17.713  12.809  1.00 80.12  ? 377 PHE A O   1 
ATOM   2691 C CB  . PHE A 1 383 ? 47.202  16.011  14.433  1.00 72.56  ? 377 PHE A CB  1 
ATOM   2692 C CG  . PHE A 1 383 ? 47.859  14.706  14.765  1.00 70.37  ? 377 PHE A CG  1 
ATOM   2693 C CD1 . PHE A 1 383 ? 48.331  13.871  13.770  1.00 73.51  ? 377 PHE A CD1 1 
ATOM   2694 C CD2 . PHE A 1 383 ? 48.005  14.309  16.074  1.00 71.80  ? 377 PHE A CD2 1 
ATOM   2695 C CE1 . PHE A 1 383 ? 48.929  12.653  14.087  1.00 74.12  ? 377 PHE A CE1 1 
ATOM   2696 C CE2 . PHE A 1 383 ? 48.612  13.102  16.386  1.00 75.17  ? 377 PHE A CE2 1 
ATOM   2697 C CZ  . PHE A 1 383 ? 49.068  12.280  15.391  1.00 74.50  ? 377 PHE A CZ  1 
ATOM   2698 N N   . LYS A 1 384 ? 47.200  18.932  12.862  1.00 79.54  ? 378 LYS A N   1 
ATOM   2699 C CA  . LYS A 1 384 ? 46.511  20.213  12.836  1.00 80.58  ? 378 LYS A CA  1 
ATOM   2700 C C   . LYS A 1 384 ? 45.673  20.409  11.568  1.00 74.48  ? 378 LYS A C   1 
ATOM   2701 O O   . LYS A 1 384 ? 44.502  20.755  11.671  1.00 72.00  ? 378 LYS A O   1 
ATOM   2702 C CB  . LYS A 1 384 ? 47.521  21.367  13.035  1.00 83.83  ? 378 LYS A CB  1 
ATOM   2703 C CG  . LYS A 1 384 ? 46.857  22.712  13.272  1.00 87.23  ? 378 LYS A CG  1 
ATOM   2704 C CD  . LYS A 1 384 ? 47.815  23.805  13.758  1.00 89.51  ? 378 LYS A CD  1 
ATOM   2705 C CE  . LYS A 1 384 ? 47.081  25.108  14.023  1.00 90.04  ? 378 LYS A CE  1 
ATOM   2706 N NZ  . LYS A 1 384 ? 47.983  26.177  14.519  1.00 92.29  ? 378 LYS A NZ  1 
ATOM   2707 N N   . PRO A 1 385 ? 46.219  20.205  10.342  1.00 68.70  ? 379 PRO A N   1 
ATOM   2708 C CA  . PRO A 1 385 ? 45.428  20.366  9.117   1.00 64.73  ? 379 PRO A CA  1 
ATOM   2709 C C   . PRO A 1 385 ? 44.306  19.351  8.904   1.00 64.00  ? 379 PRO A C   1 
ATOM   2710 O O   . PRO A 1 385 ? 43.305  19.654  8.251   1.00 62.76  ? 379 PRO A O   1 
ATOM   2711 C CB  . PRO A 1 385 ? 46.477  20.245  8.003   1.00 64.80  ? 379 PRO A CB  1 
ATOM   2712 C CG  . PRO A 1 385 ? 47.637  19.535  8.616   1.00 65.52  ? 379 PRO A CG  1 
ATOM   2713 C CD  . PRO A 1 385 ? 47.630  19.877  10.072  1.00 66.08  ? 379 PRO A CD  1 
ATOM   2714 N N   . LEU A 1 386 ? 44.493  18.139  9.433   1.00 62.70  ? 380 LEU A N   1 
ATOM   2715 C CA  . LEU A 1 386 ? 43.484  17.101  9.335   1.00 62.13  ? 380 LEU A CA  1 
ATOM   2716 C C   . LEU A 1 386 ? 42.252  17.485  10.149  1.00 63.86  ? 380 LEU A C   1 
ATOM   2717 O O   . LEU A 1 386 ? 41.127  17.147  9.788   1.00 62.99  ? 380 LEU A O   1 
ATOM   2718 C CB  . LEU A 1 386 ? 44.064  15.772  9.831   1.00 61.26  ? 380 LEU A CB  1 
ATOM   2719 C CG  . LEU A 1 386 ? 45.159  15.176  8.938   1.00 63.60  ? 380 LEU A CG  1 
ATOM   2720 C CD1 . LEU A 1 386 ? 45.823  13.969  9.592   1.00 62.87  ? 380 LEU A CD1 1 
ATOM   2721 C CD2 . LEU A 1 386 ? 44.600  14.781  7.566   1.00 62.41  ? 380 LEU A CD2 1 
ATOM   2722 N N   . VAL A 1 387 ? 42.486  18.191  11.257  1.00 65.30  ? 381 VAL A N   1 
ATOM   2723 C CA  . VAL A 1 387 ? 41.418  18.604  12.148  1.00 67.10  ? 381 VAL A CA  1 
ATOM   2724 C C   . VAL A 1 387 ? 40.704  19.841  11.606  1.00 67.55  ? 381 VAL A C   1 
ATOM   2725 O O   . VAL A 1 387 ? 39.517  20.034  11.850  1.00 72.23  ? 381 VAL A O   1 
ATOM   2726 C CB  . VAL A 1 387 ? 41.991  18.838  13.568  1.00 65.06  ? 381 VAL A CB  1 
ATOM   2727 C CG1 . VAL A 1 387 ? 40.996  19.574  14.465  1.00 65.51  ? 381 VAL A CG1 1 
ATOM   2728 C CG2 . VAL A 1 387 ? 42.421  17.519  14.195  1.00 63.87  ? 381 VAL A CG2 1 
ATOM   2729 N N   . GLU A 1 388 ? 41.433  20.674  10.861  1.00 67.27  ? 382 GLU A N   1 
ATOM   2730 C CA  . GLU A 1 388 ? 40.919  21.969  10.451  1.00 69.12  ? 382 GLU A CA  1 
ATOM   2731 C C   . GLU A 1 388 ? 40.092  21.927  9.170   1.00 66.57  ? 382 GLU A C   1 
ATOM   2732 O O   . GLU A 1 388 ? 39.183  22.736  9.003   1.00 65.30  ? 382 GLU A O   1 
ATOM   2733 C CB  . GLU A 1 388 ? 42.073  22.951  10.316  1.00 70.86  ? 382 GLU A CB  1 
ATOM   2734 C CG  . GLU A 1 388 ? 42.601  23.313  11.679  1.00 75.96  ? 382 GLU A CG  1 
ATOM   2735 C CD  . GLU A 1 388 ? 43.786  24.248  11.699  1.00 83.05  ? 382 GLU A CD  1 
ATOM   2736 O OE1 . GLU A 1 388 ? 44.137  24.813  10.638  1.00 87.20  ? 382 GLU A OE1 1 
ATOM   2737 O OE2 . GLU A 1 388 ? 44.371  24.407  12.794  1.00 91.17  ? 382 GLU A OE2 1 
ATOM   2738 N N   . GLU A 1 389 ? 40.393  20.973  8.286   1.00 63.21  ? 383 GLU A N   1 
ATOM   2739 C CA  . GLU A 1 389 ? 39.634  20.824  7.055   1.00 63.80  ? 383 GLU A CA  1 
ATOM   2740 C C   . GLU A 1 389 ? 38.144  20.578  7.342   1.00 58.72  ? 383 GLU A C   1 
ATOM   2741 O O   . GLU A 1 389 ? 37.311  21.356  6.894   1.00 56.83  ? 383 GLU A O   1 
ATOM   2742 C CB  . GLU A 1 389 ? 40.314  19.745  6.163   1.00 65.28  ? 383 GLU A CB  1 
ATOM   2743 C CG  . GLU A 1 389 ? 39.641  19.498  4.826   1.00 65.75  ? 383 GLU A CG  1 
ATOM   2744 C CD  . GLU A 1 389 ? 38.640  18.363  4.771   1.00 69.58  ? 383 GLU A CD  1 
ATOM   2745 O OE1 . GLU A 1 389 ? 38.490  17.627  5.773   1.00 68.08  ? 383 GLU A OE1 1 
ATOM   2746 O OE2 . GLU A 1 389 ? 38.009  18.203  3.701   1.00 77.47  ? 383 GLU A OE2 1 
ATOM   2747 N N   . PRO A 1 390 ? 37.747  19.549  8.130   1.00 54.35  ? 384 PRO A N   1 
ATOM   2748 C CA  . PRO A 1 390 ? 36.342  19.355  8.486   1.00 53.67  ? 384 PRO A CA  1 
ATOM   2749 C C   . PRO A 1 390 ? 35.699  20.486  9.286   1.00 54.64  ? 384 PRO A C   1 
ATOM   2750 O O   . PRO A 1 390 ? 34.503  20.731  9.141   1.00 52.42  ? 384 PRO A O   1 
ATOM   2751 C CB  . PRO A 1 390 ? 36.353  18.079  9.340   1.00 53.34  ? 384 PRO A CB  1 
ATOM   2752 C CG  . PRO A 1 390 ? 37.660  17.465  9.153   1.00 52.70  ? 384 PRO A CG  1 
ATOM   2753 C CD  . PRO A 1 390 ? 38.617  18.532  8.739   1.00 54.14  ? 384 PRO A CD  1 
ATOM   2754 N N   . GLN A 1 391 ? 36.486  21.144  10.150  1.00 56.98  ? 385 GLN A N   1 
ATOM   2755 C CA  . GLN A 1 391 ? 35.978  22.219  10.994  1.00 56.97  ? 385 GLN A CA  1 
ATOM   2756 C C   . GLN A 1 391 ? 35.614  23.462  10.187  1.00 56.23  ? 385 GLN A C   1 
ATOM   2757 O O   . GLN A 1 391 ? 34.534  24.007  10.370  1.00 56.11  ? 385 GLN A O   1 
ATOM   2758 C CB  . GLN A 1 391 ? 36.979  22.592  12.102  1.00 55.96  ? 385 GLN A CB  1 
ATOM   2759 C CG  . GLN A 1 391 ? 36.881  21.696  13.317  1.00 55.13  ? 385 GLN A CG  1 
ATOM   2760 C CD  . GLN A 1 391 ? 38.056  21.847  14.243  1.00 56.91  ? 385 GLN A CD  1 
ATOM   2761 O OE1 . GLN A 1 391 ? 39.049  22.518  13.934  1.00 61.20  ? 385 GLN A OE1 1 
ATOM   2762 N NE2 . GLN A 1 391 ? 37.992  21.202  15.395  1.00 56.30  ? 385 GLN A NE2 1 
ATOM   2763 N N   . ASN A 1 392 ? 36.512  23.902  9.298   1.00 57.92  ? 386 ASN A N   1 
ATOM   2764 C CA  . ASN A 1 392 ? 36.210  25.000  8.388   1.00 60.19  ? 386 ASN A CA  1 
ATOM   2765 C C   . ASN A 1 392 ? 34.971  24.727  7.537   1.00 59.78  ? 386 ASN A C   1 
ATOM   2766 O O   . ASN A 1 392 ? 34.163  25.624  7.289   1.00 56.26  ? 386 ASN A O   1 
ATOM   2767 C CB  . ASN A 1 392 ? 37.374  25.284  7.457   1.00 61.76  ? 386 ASN A CB  1 
ATOM   2768 C CG  . ASN A 1 392 ? 38.417  26.165  8.072   1.00 70.07  ? 386 ASN A CG  1 
ATOM   2769 O OD1 . ASN A 1 392 ? 39.179  25.750  8.959   1.00 71.06  ? 386 ASN A OD1 1 
ATOM   2770 N ND2 . ASN A 1 392 ? 38.490  27.421  7.600   1.00 77.80  ? 386 ASN A ND2 1 
ATOM   2771 N N   . LEU A 1 393 ? 34.856  23.472  7.088   1.00 57.27  ? 387 LEU A N   1 
ATOM   2772 C CA  . LEU A 1 393 ? 33.812  23.062  6.171   1.00 54.60  ? 387 LEU A CA  1 
ATOM   2773 C C   . LEU A 1 393 ? 32.473  23.109  6.896   1.00 52.79  ? 387 LEU A C   1 
ATOM   2774 O O   . LEU A 1 393 ? 31.479  23.552  6.327   1.00 50.47  ? 387 LEU A O   1 
ATOM   2775 C CB  . LEU A 1 393 ? 34.115  21.650  5.659   1.00 54.67  ? 387 LEU A CB  1 
ATOM   2776 C CG  . LEU A 1 393 ? 33.966  21.431  4.170   1.00 53.60  ? 387 LEU A CG  1 
ATOM   2777 C CD1 . LEU A 1 393 ? 34.731  22.481  3.365   1.00 52.38  ? 387 LEU A CD1 1 
ATOM   2778 C CD2 . LEU A 1 393 ? 34.488  20.075  3.802   1.00 55.17  ? 387 LEU A CD2 1 
ATOM   2779 N N   . ILE A 1 394 ? 32.469  22.674  8.161   1.00 51.75  ? 388 ILE A N   1 
ATOM   2780 C CA  . ILE A 1 394 ? 31.295  22.826  9.003   1.00 52.98  ? 388 ILE A CA  1 
ATOM   2781 C C   . ILE A 1 394 ? 31.006  24.303  9.259   1.00 53.96  ? 388 ILE A C   1 
ATOM   2782 O O   . ILE A 1 394 ? 29.860  24.728  9.179   1.00 53.82  ? 388 ILE A O   1 
ATOM   2783 C CB  . ILE A 1 394 ? 31.424  22.030  10.305  1.00 52.95  ? 388 ILE A CB  1 
ATOM   2784 C CG1 . ILE A 1 394 ? 31.444  20.513  10.002  1.00 53.65  ? 388 ILE A CG1 1 
ATOM   2785 C CG2 . ILE A 1 394 ? 30.300  22.364  11.252  1.00 54.12  ? 388 ILE A CG2 1 
ATOM   2786 C CD1 . ILE A 1 394 ? 31.664  19.644  11.165  1.00 52.73  ? 388 ILE A CD1 1 
ATOM   2787 N N   . LYS A 1 395 ? 32.058  25.083  9.513   1.00 55.66  ? 389 LYS A N   1 
ATOM   2788 C CA  . LYS A 1 395 ? 31.923  26.511  9.751   1.00 59.29  ? 389 LYS A CA  1 
ATOM   2789 C C   . LYS A 1 395 ? 31.306  27.277  8.572   1.00 58.21  ? 389 LYS A C   1 
ATOM   2790 O O   . LYS A 1 395 ? 30.390  28.074  8.759   1.00 55.18  ? 389 LYS A O   1 
ATOM   2791 C CB  . LYS A 1 395 ? 33.311  27.081  10.117  1.00 62.39  ? 389 LYS A CB  1 
ATOM   2792 C CG  . LYS A 1 395 ? 33.310  28.510  10.618  1.00 67.13  ? 389 LYS A CG  1 
ATOM   2793 C CD  . LYS A 1 395 ? 32.569  28.664  11.940  1.00 73.77  ? 389 LYS A CD  1 
ATOM   2794 C CE  . LYS A 1 395 ? 32.632  30.073  12.495  1.00 76.76  ? 389 LYS A CE  1 
ATOM   2795 N NZ  . LYS A 1 395 ? 31.814  30.207  13.733  1.00 78.06  ? 389 LYS A NZ  1 
ATOM   2796 N N   . GLN A 1 396 ? 31.802  27.038  7.353   1.00 57.29  ? 390 GLN A N   1 
ATOM   2797 C CA  . GLN A 1 396 ? 31.311  27.745  6.181   1.00 58.19  ? 390 GLN A CA  1 
ATOM   2798 C C   . GLN A 1 396 ? 29.872  27.375  5.806   1.00 55.41  ? 390 GLN A C   1 
ATOM   2799 O O   . GLN A 1 396 ? 29.096  28.234  5.391   1.00 52.37  ? 390 GLN A O   1 
ATOM   2800 C CB  . GLN A 1 396 ? 32.234  27.470  4.989   1.00 62.63  ? 390 GLN A CB  1 
ATOM   2801 C CG  . GLN A 1 396 ? 33.644  28.006  5.175   1.00 66.78  ? 390 GLN A CG  1 
ATOM   2802 C CD  . GLN A 1 396 ? 34.653  27.225  4.359   1.00 75.22  ? 390 GLN A CD  1 
ATOM   2803 O OE1 . GLN A 1 396 ? 34.658  25.973  4.346   1.00 80.02  ? 390 GLN A OE1 1 
ATOM   2804 N NE2 . GLN A 1 396 ? 35.539  27.933  3.659   1.00 78.03  ? 390 GLN A NE2 1 
ATOM   2805 N N   . ASN A 1 397 ? 29.522  26.093  5.962   1.00 53.28  ? 391 ASN A N   1 
ATOM   2806 C CA  . ASN A 1 397 ? 28.234  25.591  5.514   1.00 51.51  ? 391 ASN A CA  1 
ATOM   2807 C C   . ASN A 1 397 ? 27.118  25.949  6.485   1.00 50.65  ? 391 ASN A C   1 
ATOM   2808 O O   . ASN A 1 397 ? 25.988  26.162  6.054   1.00 48.04  ? 391 ASN A O   1 
ATOM   2809 C CB  . ASN A 1 397 ? 28.271  24.070  5.261   1.00 51.49  ? 391 ASN A CB  1 
ATOM   2810 C CG  . ASN A 1 397 ? 28.877  23.739  3.922   1.00 51.44  ? 391 ASN A CG  1 
ATOM   2811 O OD1 . ASN A 1 397 ? 28.210  23.790  2.880   1.00 52.54  ? 391 ASN A OD1 1 
ATOM   2812 N ND2 . ASN A 1 397 ? 30.160  23.407  3.911   1.00 51.16  ? 391 ASN A ND2 1 
ATOM   2813 N N   . CYS A 1 398 ? 27.444  25.989  7.784   1.00 51.97  ? 392 CYS A N   1 
ATOM   2814 C CA  . CYS A 1 398 ? 26.534  26.500  8.798   1.00 52.04  ? 392 CYS A CA  1 
ATOM   2815 C C   . CYS A 1 398 ? 26.358  28.013  8.699   1.00 52.44  ? 392 CYS A C   1 
ATOM   2816 O O   . CYS A 1 398 ? 25.242  28.513  8.826   1.00 50.37  ? 392 CYS A O   1 
ATOM   2817 C CB  . CYS A 1 398 ? 26.987  26.099  10.189  1.00 52.35  ? 392 CYS A CB  1 
ATOM   2818 S SG  . CYS A 1 398 ? 26.657  24.367  10.585  1.00 56.20  ? 392 CYS A SG  1 
ATOM   2819 N N   . GLU A 1 399 ? 27.452  28.736  8.449   1.00 53.42  ? 393 GLU A N   1 
ATOM   2820 C CA  . GLU A 1 399 ? 27.338  30.158  8.190   1.00 58.35  ? 393 GLU A CA  1 
ATOM   2821 C C   . GLU A 1 399 ? 26.281  30.367  7.102   1.00 59.51  ? 393 GLU A C   1 
ATOM   2822 O O   . GLU A 1 399 ? 25.362  31.167  7.287   1.00 59.78  ? 393 GLU A O   1 
ATOM   2823 C CB  . GLU A 1 399 ? 28.683  30.784  7.807   1.00 64.30  ? 393 GLU A CB  1 
ATOM   2824 C CG  . GLU A 1 399 ? 29.567  31.144  8.994   1.00 71.36  ? 393 GLU A CG  1 
ATOM   2825 C CD  . GLU A 1 399 ? 30.920  31.746  8.628   1.00 81.16  ? 393 GLU A CD  1 
ATOM   2826 O OE1 . GLU A 1 399 ? 31.702  31.070  7.917   1.00 86.06  ? 393 GLU A OE1 1 
ATOM   2827 O OE2 . GLU A 1 399 ? 31.200  32.895  9.050   1.00 86.53  ? 393 GLU A OE2 1 
ATOM   2828 N N   . LEU A 1 400 ? 26.389  29.593  6.008   1.00 56.55  ? 394 LEU A N   1 
ATOM   2829 C CA  . LEU A 1 400 ? 25.518  29.716  4.845   1.00 53.30  ? 394 LEU A CA  1 
ATOM   2830 C C   . LEU A 1 400 ? 24.077  29.282  5.129   1.00 52.14  ? 394 LEU A C   1 
ATOM   2831 O O   . LEU A 1 400 ? 23.126  29.964  4.750   1.00 47.48  ? 394 LEU A O   1 
ATOM   2832 C CB  . LEU A 1 400 ? 26.130  28.866  3.732   1.00 52.37  ? 394 LEU A CB  1 
ATOM   2833 C CG  . LEU A 1 400 ? 25.636  29.053  2.318   1.00 53.50  ? 394 LEU A CG  1 
ATOM   2834 C CD1 . LEU A 1 400 ? 25.974  30.417  1.747   1.00 53.11  ? 394 LEU A CD1 1 
ATOM   2835 C CD2 . LEU A 1 400 ? 26.260  28.023  1.423   1.00 54.82  ? 394 LEU A CD2 1 
ATOM   2836 N N   . PHE A 1 401 ? 23.925  28.142  5.812   1.00 52.59  ? 395 PHE A N   1 
ATOM   2837 C CA  . PHE A 1 401 ? 22.618  27.666  6.235   1.00 54.44  ? 395 PHE A CA  1 
ATOM   2838 C C   . PHE A 1 401 ? 21.917  28.663  7.159   1.00 57.05  ? 395 PHE A C   1 
ATOM   2839 O O   . PHE A 1 401 ? 20.726  28.925  7.011   1.00 56.77  ? 395 PHE A O   1 
ATOM   2840 C CB  . PHE A 1 401 ? 22.720  26.318  6.960   1.00 53.11  ? 395 PHE A CB  1 
ATOM   2841 C CG  . PHE A 1 401 ? 21.443  25.941  7.663   1.00 53.61  ? 395 PHE A CG  1 
ATOM   2842 C CD1 . PHE A 1 401 ? 20.404  25.341  6.972   1.00 56.02  ? 395 PHE A CD1 1 
ATOM   2843 C CD2 . PHE A 1 401 ? 21.253  26.245  9.002   1.00 55.65  ? 395 PHE A CD2 1 
ATOM   2844 C CE1 . PHE A 1 401 ? 19.212  25.004  7.622   1.00 56.79  ? 395 PHE A CE1 1 
ATOM   2845 C CE2 . PHE A 1 401 ? 20.060  25.914  9.651   1.00 56.36  ? 395 PHE A CE2 1 
ATOM   2846 C CZ  . PHE A 1 401 ? 19.045  25.299  8.957   1.00 56.96  ? 395 PHE A CZ  1 
ATOM   2847 N N   . GLU A 1 402 ? 22.660  29.194  8.133   1.00 58.50  ? 396 GLU A N   1 
ATOM   2848 C CA  . GLU A 1 402 ? 22.102  30.175  9.044   1.00 59.76  ? 396 GLU A CA  1 
ATOM   2849 C C   . GLU A 1 402 ? 21.533  31.369  8.285   1.00 56.36  ? 396 GLU A C   1 
ATOM   2850 O O   . GLU A 1 402 ? 20.416  31.798  8.562   1.00 58.03  ? 396 GLU A O   1 
ATOM   2851 C CB  . GLU A 1 402 ? 23.142  30.632  10.099  1.00 63.33  ? 396 GLU A CB  1 
ATOM   2852 C CG  . GLU A 1 402 ? 23.392  29.613  11.218  1.00 64.48  ? 396 GLU A CG  1 
ATOM   2853 C CD  . GLU A 1 402 ? 22.157  29.095  11.944  1.00 69.32  ? 396 GLU A CD  1 
ATOM   2854 O OE1 . GLU A 1 402 ? 21.052  29.657  11.744  1.00 73.69  ? 396 GLU A OE1 1 
ATOM   2855 O OE2 . GLU A 1 402 ? 22.291  28.103  12.701  1.00 73.08  ? 396 GLU A OE2 1 
ATOM   2856 N N   . GLN A 1 403 ? 22.268  31.868  7.293   1.00 55.95  ? 397 GLN A N   1 
ATOM   2857 C CA  . GLN A 1 403 ? 21.839  33.080  6.619   1.00 59.77  ? 397 GLN A CA  1 
ATOM   2858 C C   . GLN A 1 403 ? 20.773  32.870  5.544   1.00 58.24  ? 397 GLN A C   1 
ATOM   2859 O O   . GLN A 1 403 ? 20.103  33.830  5.183   1.00 59.06  ? 397 GLN A O   1 
ATOM   2860 C CB  . GLN A 1 403 ? 23.040  33.862  6.067   1.00 65.99  ? 397 GLN A CB  1 
ATOM   2861 C CG  . GLN A 1 403 ? 23.884  33.143  5.047   1.00 74.49  ? 397 GLN A CG  1 
ATOM   2862 C CD  . GLN A 1 403 ? 25.239  33.814  4.891   1.00 80.82  ? 397 GLN A CD  1 
ATOM   2863 O OE1 . GLN A 1 403 ? 26.003  33.955  5.867   1.00 83.10  ? 397 GLN A OE1 1 
ATOM   2864 N NE2 . GLN A 1 403 ? 25.562  34.237  3.662   1.00 83.60  ? 397 GLN A NE2 1 
ATOM   2865 N N   . LEU A 1 404 ? 20.564  31.622  5.095   1.00 56.66  ? 398 LEU A N   1 
ATOM   2866 C CA  . LEU A 1 404 ? 19.647  31.330  4.003   1.00 50.57  ? 398 LEU A CA  1 
ATOM   2867 C C   . LEU A 1 404 ? 18.358  30.614  4.399   1.00 49.38  ? 398 LEU A C   1 
ATOM   2868 O O   . LEU A 1 404 ? 17.340  30.764  3.720   1.00 53.14  ? 398 LEU A O   1 
ATOM   2869 C CB  . LEU A 1 404 ? 20.377  30.466  2.963   1.00 51.03  ? 398 LEU A CB  1 
ATOM   2870 C CG  . LEU A 1 404 ? 21.377  31.195  2.018   1.00 48.59  ? 398 LEU A CG  1 
ATOM   2871 C CD1 . LEU A 1 404 ? 22.075  30.224  1.135   1.00 48.62  ? 398 LEU A CD1 1 
ATOM   2872 C CD2 . LEU A 1 404 ? 20.690  32.204  1.140   1.00 47.35  ? 398 LEU A CD2 1 
ATOM   2873 N N   . GLY A 1 405 ? 18.400  29.824  5.477   1.00 45.27  ? 399 GLY A N   1 
ATOM   2874 C CA  . GLY A 1 405 ? 17.279  28.969  5.844   1.00 41.87  ? 399 GLY A CA  1 
ATOM   2875 C C   . GLY A 1 405 ? 17.361  27.636  5.105   1.00 43.66  ? 399 GLY A C   1 
ATOM   2876 O O   . GLY A 1 405 ? 18.084  27.523  4.113   1.00 43.88  ? 399 GLY A O   1 
ATOM   2877 N N   . GLU A 1 406 ? 16.614  26.634  5.579   1.00 43.39  ? 400 GLU A N   1 
ATOM   2878 C CA  . GLU A 1 406 ? 16.691  25.310  4.992   1.00 46.01  ? 400 GLU A CA  1 
ATOM   2879 C C   . GLU A 1 406 ? 16.538  25.302  3.472   1.00 46.13  ? 400 GLU A C   1 
ATOM   2880 O O   . GLU A 1 406 ? 17.311  24.636  2.780   1.00 46.55  ? 400 GLU A O   1 
ATOM   2881 C CB  . GLU A 1 406 ? 15.649  24.352  5.562   1.00 48.51  ? 400 GLU A CB  1 
ATOM   2882 C CG  . GLU A 1 406 ? 15.845  22.961  4.972   1.00 54.48  ? 400 GLU A CG  1 
ATOM   2883 C CD  . GLU A 1 406 ? 15.089  21.826  5.621   1.00 61.17  ? 400 GLU A CD  1 
ATOM   2884 O OE1 . GLU A 1 406 ? 13.866  21.718  5.380   1.00 66.38  ? 400 GLU A OE1 1 
ATOM   2885 O OE2 . GLU A 1 406 ? 15.721  21.038  6.365   1.00 68.43  ? 400 GLU A OE2 1 
ATOM   2886 N N   . TYR A 1 407 ? 15.525  26.020  2.971   1.00 46.36  ? 401 TYR A N   1 
ATOM   2887 C CA  . TYR A 1 407 ? 15.055  25.845  1.603   1.00 46.15  ? 401 TYR A CA  1 
ATOM   2888 C C   . TYR A 1 407 ? 16.030  26.424  0.580   1.00 45.37  ? 401 TYR A C   1 
ATOM   2889 O O   . TYR A 1 407 ? 16.363  25.756  -0.390  1.00 45.84  ? 401 TYR A O   1 
ATOM   2890 C CB  . TYR A 1 407 ? 13.651  26.450  1.423   1.00 44.22  ? 401 TYR A CB  1 
ATOM   2891 C CG  . TYR A 1 407 ? 13.175  26.547  -0.011  1.00 44.34  ? 401 TYR A CG  1 
ATOM   2892 C CD1 . TYR A 1 407 ? 13.112  25.425  -0.824  1.00 44.96  ? 401 TYR A CD1 1 
ATOM   2893 C CD2 . TYR A 1 407 ? 12.800  27.761  -0.557  1.00 44.58  ? 401 TYR A CD2 1 
ATOM   2894 C CE1 . TYR A 1 407 ? 12.686  25.511  -2.143  1.00 44.72  ? 401 TYR A CE1 1 
ATOM   2895 C CE2 . TYR A 1 407 ? 12.346  27.856  -1.866  1.00 45.85  ? 401 TYR A CE2 1 
ATOM   2896 C CZ  . TYR A 1 407 ? 12.304  26.732  -2.664  1.00 45.36  ? 401 TYR A CZ  1 
ATOM   2897 O OH  . TYR A 1 407 ? 11.862  26.843  -3.962  1.00 44.73  ? 401 TYR A OH  1 
ATOM   2898 N N   . LYS A 1 408 ? 16.464  27.665  0.800   1.00 45.21  ? 402 LYS A N   1 
ATOM   2899 C CA  . LYS A 1 408 ? 17.467  28.289  -0.045  1.00 46.23  ? 402 LYS A CA  1 
ATOM   2900 C C   . LYS A 1 408 ? 18.855  27.668  0.134   1.00 45.83  ? 402 LYS A C   1 
ATOM   2901 O O   . LYS A 1 408 ? 19.721  27.802  -0.734  1.00 43.63  ? 402 LYS A O   1 
ATOM   2902 C CB  . LYS A 1 408 ? 17.539  29.779  0.262   1.00 46.00  ? 402 LYS A CB  1 
ATOM   2903 C CG  . LYS A 1 408 ? 16.335  30.523  -0.230  1.00 48.32  ? 402 LYS A CG  1 
ATOM   2904 C CD  . LYS A 1 408 ? 16.544  32.008  -0.146  1.00 51.36  ? 402 LYS A CD  1 
ATOM   2905 C CE  . LYS A 1 408 ? 15.397  32.763  -0.699  1.00 54.43  ? 402 LYS A CE  1 
ATOM   2906 N NZ  . LYS A 1 408 ? 15.685  34.213  -0.746  1.00 58.51  ? 402 LYS A NZ  1 
ATOM   2907 N N   . PHE A 1 409 ? 19.069  27.028  1.289   1.00 44.85  ? 403 PHE A N   1 
ATOM   2908 C CA  . PHE A 1 409 ? 20.307  26.311  1.540   1.00 44.32  ? 403 PHE A CA  1 
ATOM   2909 C C   . PHE A 1 409 ? 20.317  25.140  0.567   1.00 42.32  ? 403 PHE A C   1 
ATOM   2910 O O   . PHE A 1 409 ? 21.281  24.974  -0.180  1.00 40.84  ? 403 PHE A O   1 
ATOM   2911 C CB  . PHE A 1 409 ? 20.443  25.842  3.002   1.00 42.51  ? 403 PHE A CB  1 
ATOM   2912 C CG  . PHE A 1 409 ? 21.728  25.125  3.309   1.00 40.30  ? 403 PHE A CG  1 
ATOM   2913 C CD1 . PHE A 1 409 ? 22.937  25.737  3.111   1.00 40.36  ? 403 PHE A CD1 1 
ATOM   2914 C CD2 . PHE A 1 409 ? 21.718  23.835  3.804   1.00 40.22  ? 403 PHE A CD2 1 
ATOM   2915 C CE1 . PHE A 1 409 ? 24.117  25.074  3.395   1.00 41.56  ? 403 PHE A CE1 1 
ATOM   2916 C CE2 . PHE A 1 409 ? 22.889  23.175  4.092   1.00 38.76  ? 403 PHE A CE2 1 
ATOM   2917 C CZ  . PHE A 1 409 ? 24.083  23.789  3.880   1.00 40.89  ? 403 PHE A CZ  1 
ATOM   2918 N N   . GLN A 1 410 ? 19.201  24.397  0.545   1.00 40.42  ? 404 GLN A N   1 
ATOM   2919 C CA  . GLN A 1 410 ? 19.038  23.299  -0.391  1.00 41.34  ? 404 GLN A CA  1 
ATOM   2920 C C   . GLN A 1 410 ? 19.229  23.749  -1.839  1.00 41.49  ? 404 GLN A C   1 
ATOM   2921 O O   . GLN A 1 410 ? 19.748  23.005  -2.667  1.00 41.53  ? 404 GLN A O   1 
ATOM   2922 C CB  . GLN A 1 410 ? 17.678  22.669  -0.251  1.00 41.52  ? 404 GLN A CB  1 
ATOM   2923 C CG  . GLN A 1 410 ? 17.515  21.885  1.024   1.00 43.14  ? 404 GLN A CG  1 
ATOM   2924 C CD  . GLN A 1 410 ? 16.108  21.376  1.189   1.00 42.96  ? 404 GLN A CD  1 
ATOM   2925 O OE1 . GLN A 1 410 ? 15.157  21.868  0.576   1.00 40.08  ? 404 GLN A OE1 1 
ATOM   2926 N NE2 . GLN A 1 410 ? 15.958  20.378  2.033   1.00 44.73  ? 404 GLN A NE2 1 
ATOM   2927 N N   . ASN A 1 411 ? 18.799  24.974  -2.139  1.00 40.52  ? 405 ASN A N   1 
ATOM   2928 C CA  . ASN A 1 411 ? 18.872  25.482  -3.491  1.00 40.23  ? 405 ASN A CA  1 
ATOM   2929 C C   . ASN A 1 411 ? 20.334  25.717  -3.849  1.00 42.01  ? 405 ASN A C   1 
ATOM   2930 O O   . ASN A 1 411 ? 20.742  25.441  -4.981  1.00 42.57  ? 405 ASN A O   1 
ATOM   2931 C CB  . ASN A 1 411 ? 18.030  26.707  -3.639  1.00 37.81  ? 405 ASN A CB  1 
ATOM   2932 C CG  . ASN A 1 411 ? 16.570  26.404  -3.490  1.00 39.12  ? 405 ASN A CG  1 
ATOM   2933 O OD1 . ASN A 1 411 ? 16.118  25.237  -3.368  1.00 36.48  ? 405 ASN A OD1 1 
ATOM   2934 N ND2 . ASN A 1 411 ? 15.785  27.460  -3.488  1.00 40.63  ? 405 ASN A ND2 1 
ATOM   2935 N N   . ALA A 1 412 ? 21.105  26.176  -2.854  1.00 40.89  ? 406 ALA A N   1 
ATOM   2936 C CA  . ALA A 1 412 ? 22.508  26.500  -3.038  1.00 39.37  ? 406 ALA A CA  1 
ATOM   2937 C C   . ALA A 1 412 ? 23.328  25.229  -3.237  1.00 39.59  ? 406 ALA A C   1 
ATOM   2938 O O   . ALA A 1 412 ? 24.224  25.188  -4.068  1.00 41.55  ? 406 ALA A O   1 
ATOM   2939 C CB  . ALA A 1 412 ? 23.011  27.270  -1.842  1.00 38.81  ? 406 ALA A CB  1 
ATOM   2940 N N   . LEU A 1 413 ? 23.015  24.188  -2.466  1.00 38.72  ? 407 LEU A N   1 
ATOM   2941 C CA  . LEU A 1 413 ? 23.662  22.908  -2.657  1.00 40.25  ? 407 LEU A CA  1 
ATOM   2942 C C   . LEU A 1 413 ? 23.307  22.339  -4.035  1.00 41.07  ? 407 LEU A C   1 
ATOM   2943 O O   . LEU A 1 413 ? 24.146  21.723  -4.679  1.00 43.93  ? 407 LEU A O   1 
ATOM   2944 C CB  . LEU A 1 413 ? 23.251  21.921  -1.552  1.00 39.84  ? 407 LEU A CB  1 
ATOM   2945 C CG  . LEU A 1 413 ? 23.712  22.216  -0.148  1.00 41.65  ? 407 LEU A CG  1 
ATOM   2946 C CD1 . LEU A 1 413 ? 23.342  21.102  0.770   1.00 42.20  ? 407 LEU A CD1 1 
ATOM   2947 C CD2 . LEU A 1 413 ? 25.206  22.420  -0.063  1.00 42.21  ? 407 LEU A CD2 1 
ATOM   2948 N N   . LEU A 1 414 ? 22.053  22.512  -4.465  1.00 40.46  ? 408 LEU A N   1 
ATOM   2949 C CA  . LEU A 1 414 ? 21.597  22.016  -5.750  1.00 39.94  ? 408 LEU A CA  1 
ATOM   2950 C C   . LEU A 1 414 ? 22.478  22.569  -6.862  1.00 37.89  ? 408 LEU A C   1 
ATOM   2951 O O   . LEU A 1 414 ? 22.948  21.817  -7.710  1.00 35.14  ? 408 LEU A O   1 
ATOM   2952 C CB  . LEU A 1 414 ? 20.127  22.411  -6.017  1.00 41.50  ? 408 LEU A CB  1 
ATOM   2953 C CG  . LEU A 1 414 ? 19.073  21.519  -5.427  1.00 42.29  ? 408 LEU A CG  1 
ATOM   2954 C CD1 . LEU A 1 414 ? 17.707  22.137  -5.567  1.00 42.25  ? 408 LEU A CD1 1 
ATOM   2955 C CD2 . LEU A 1 414 ? 19.083  20.151  -6.083  1.00 43.95  ? 408 LEU A CD2 1 
ATOM   2956 N N   . VAL A 1 415 ? 22.667  23.890  -6.845  1.00 36.99  ? 409 VAL A N   1 
ATOM   2957 C CA  . VAL A 1 415 ? 23.588  24.538  -7.757  1.00 40.24  ? 409 VAL A CA  1 
ATOM   2958 C C   . VAL A 1 415 ? 25.000  23.963  -7.659  1.00 42.99  ? 409 VAL A C   1 
ATOM   2959 O O   . VAL A 1 415 ? 25.628  23.685  -8.684  1.00 46.59  ? 409 VAL A O   1 
ATOM   2960 C CB  . VAL A 1 415 ? 23.602  26.055  -7.523  1.00 40.14  ? 409 VAL A CB  1 
ATOM   2961 C CG1 . VAL A 1 415 ? 24.735  26.731  -8.308  1.00 39.38  ? 409 VAL A CG1 1 
ATOM   2962 C CG2 . VAL A 1 415 ? 22.236  26.671  -7.875  1.00 39.25  ? 409 VAL A CG2 1 
ATOM   2963 N N   . ARG A 1 416 ? 25.489  23.796  -6.424  1.00 43.19  ? 410 ARG A N   1 
ATOM   2964 C CA  . ARG A 1 416 ? 26.867  23.388  -6.185  1.00 43.76  ? 410 ARG A CA  1 
ATOM   2965 C C   . ARG A 1 416 ? 27.178  21.996  -6.749  1.00 46.15  ? 410 ARG A C   1 
ATOM   2966 O O   . ARG A 1 416 ? 28.162  21.845  -7.464  1.00 50.34  ? 410 ARG A O   1 
ATOM   2967 C CB  . ARG A 1 416 ? 27.172  23.484  -4.671  1.00 43.76  ? 410 ARG A CB  1 
ATOM   2968 C CG  . ARG A 1 416 ? 28.604  23.052  -4.217  1.00 42.97  ? 410 ARG A CG  1 
ATOM   2969 C CD  . ARG A 1 416 ? 28.641  22.610  -2.743  1.00 40.98  ? 410 ARG A CD  1 
ATOM   2970 N NE  . ARG A 1 416 ? 28.614  23.739  -1.815  1.00 39.77  ? 410 ARG A NE  1 
ATOM   2971 C CZ  . ARG A 1 416 ? 28.491  23.630  -0.492  1.00 39.88  ? 410 ARG A CZ  1 
ATOM   2972 N NH1 . ARG A 1 416 ? 28.365  22.451  0.100   1.00 39.12  ? 410 ARG A NH1 1 
ATOM   2973 N NH2 . ARG A 1 416 ? 28.468  24.734  0.251   1.00 38.88  ? 410 ARG A NH2 1 
ATOM   2974 N N   . TYR A 1 417 ? 26.322  20.996  -6.491  1.00 46.14  ? 411 TYR A N   1 
ATOM   2975 C CA  . TYR A 1 417 ? 26.587  19.624  -6.908  1.00 45.57  ? 411 TYR A CA  1 
ATOM   2976 C C   . TYR A 1 417 ? 26.205  19.301  -8.354  1.00 46.71  ? 411 TYR A C   1 
ATOM   2977 O O   . TYR A 1 417 ? 26.778  18.378  -8.934  1.00 49.40  ? 411 TYR A O   1 
ATOM   2978 C CB  . TYR A 1 417 ? 25.917  18.628  -5.932  1.00 44.90  ? 411 TYR A CB  1 
ATOM   2979 C CG  . TYR A 1 417 ? 26.504  18.759  -4.545  1.00 48.03  ? 411 TYR A CG  1 
ATOM   2980 C CD1 . TYR A 1 417 ? 27.886  18.700  -4.341  1.00 47.65  ? 411 TYR A CD1 1 
ATOM   2981 C CD2 . TYR A 1 417 ? 25.690  18.984  -3.439  1.00 48.86  ? 411 TYR A CD2 1 
ATOM   2982 C CE1 . TYR A 1 417 ? 28.436  18.859  -3.078  1.00 47.69  ? 411 TYR A CE1 1 
ATOM   2983 C CE2 . TYR A 1 417 ? 26.229  19.126  -2.164  1.00 48.68  ? 411 TYR A CE2 1 
ATOM   2984 C CZ  . TYR A 1 417 ? 27.605  19.082  -1.990  1.00 50.78  ? 411 TYR A CZ  1 
ATOM   2985 O OH  . TYR A 1 417 ? 28.147  19.240  -0.730  1.00 52.86  ? 411 TYR A OH  1 
ATOM   2986 N N   . THR A 1 418 ? 25.273  20.066  -8.941  1.00 44.98  ? 412 THR A N   1 
ATOM   2987 C CA  . THR A 1 418 ? 24.919  19.894  -10.344 1.00 46.41  ? 412 THR A CA  1 
ATOM   2988 C C   . THR A 1 418 ? 26.131  20.214  -11.220 1.00 47.12  ? 412 THR A C   1 
ATOM   2989 O O   . THR A 1 418 ? 26.531  19.414  -12.065 1.00 48.70  ? 412 THR A O   1 
ATOM   2990 C CB  . THR A 1 418 ? 23.649  20.750  -10.741 1.00 46.13  ? 412 THR A CB  1 
ATOM   2991 O OG1 . THR A 1 418 ? 22.496  20.287  -10.031 1.00 43.92  ? 412 THR A OG1 1 
ATOM   2992 C CG2 . THR A 1 418 ? 23.328  20.682  -12.223 1.00 44.06  ? 412 THR A CG2 1 
ATOM   2993 N N   . LYS A 1 419 ? 26.720  21.390  -11.001 1.00 46.44  ? 413 LYS A N   1 
ATOM   2994 C CA  . LYS A 1 419 ? 27.959  21.759  -11.667 1.00 46.46  ? 413 LYS A CA  1 
ATOM   2995 C C   . LYS A 1 419 ? 29.090  20.747  -11.499 1.00 46.51  ? 413 LYS A C   1 
ATOM   2996 O O   . LYS A 1 419 ? 29.883  20.544  -12.412 1.00 46.96  ? 413 LYS A O   1 
ATOM   2997 C CB  . LYS A 1 419 ? 28.451  23.105  -11.145 1.00 45.36  ? 413 LYS A CB  1 
ATOM   2998 C CG  . LYS A 1 419 ? 27.618  24.254  -11.648 1.00 45.17  ? 413 LYS A CG  1 
ATOM   2999 C CD  . LYS A 1 419 ? 28.019  25.568  -11.019 1.00 45.46  ? 413 LYS A CD  1 
ATOM   3000 C CE  . LYS A 1 419 ? 27.203  26.687  -11.562 1.00 45.44  ? 413 LYS A CE  1 
ATOM   3001 N NZ  . LYS A 1 419 ? 27.942  27.925  -11.535 1.00 45.11  ? 413 LYS A NZ  1 
ATOM   3002 N N   . LYS A 1 420 ? 29.201  20.155  -10.311 1.00 46.48  ? 414 LYS A N   1 
ATOM   3003 C CA  . LYS A 1 420 ? 30.258  19.191  -10.077 1.00 46.47  ? 414 LYS A CA  1 
ATOM   3004 C C   . LYS A 1 420 ? 29.988  17.914  -10.859 1.00 46.83  ? 414 LYS A C   1 
ATOM   3005 O O   . LYS A 1 420 ? 30.897  17.396  -11.492 1.00 48.91  ? 414 LYS A O   1 
ATOM   3006 C CB  . LYS A 1 420 ? 30.431  18.895  -8.595  1.00 46.66  ? 414 LYS A CB  1 
ATOM   3007 C CG  . LYS A 1 420 ? 31.065  20.051  -7.878  1.00 46.55  ? 414 LYS A CG  1 
ATOM   3008 C CD  . LYS A 1 420 ? 31.276  19.797  -6.416  1.00 47.49  ? 414 LYS A CD  1 
ATOM   3009 C CE  . LYS A 1 420 ? 32.110  20.890  -5.806  1.00 49.66  ? 414 LYS A CE  1 
ATOM   3010 N NZ  . LYS A 1 420 ? 32.585  20.518  -4.451  1.00 52.24  ? 414 LYS A NZ  1 
ATOM   3011 N N   . VAL A 1 421 ? 28.745  17.423  -10.826 1.00 47.18  ? 415 VAL A N   1 
ATOM   3012 C CA  . VAL A 1 421 ? 28.407  16.176  -11.496 1.00 47.88  ? 415 VAL A CA  1 
ATOM   3013 C C   . VAL A 1 421 ? 27.145  16.314  -12.354 1.00 47.04  ? 415 VAL A C   1 
ATOM   3014 O O   . VAL A 1 421 ? 26.121  15.700  -12.071 1.00 46.85  ? 415 VAL A O   1 
ATOM   3015 C CB  . VAL A 1 421 ? 28.290  15.052  -10.430 1.00 49.91  ? 415 VAL A CB  1 
ATOM   3016 C CG1 . VAL A 1 421 ? 28.297  13.669  -11.064 1.00 49.95  ? 415 VAL A CG1 1 
ATOM   3017 C CG2 . VAL A 1 421 ? 29.407  15.147  -9.393  1.00 50.07  ? 415 VAL A CG2 1 
ATOM   3018 N N   . PRO A 1 422 ? 27.187  17.080  -13.470 1.00 46.90  ? 416 PRO A N   1 
ATOM   3019 C CA  . PRO A 1 422 ? 25.982  17.343  -14.258 1.00 47.50  ? 416 PRO A CA  1 
ATOM   3020 C C   . PRO A 1 422 ? 25.302  16.149  -14.924 1.00 47.25  ? 416 PRO A C   1 
ATOM   3021 O O   . PRO A 1 422 ? 24.210  16.307  -15.447 1.00 48.41  ? 416 PRO A O   1 
ATOM   3022 C CB  . PRO A 1 422 ? 26.449  18.317  -15.340 1.00 48.38  ? 416 PRO A CB  1 
ATOM   3023 C CG  . PRO A 1 422 ? 27.874  18.655  -15.039 1.00 47.91  ? 416 PRO A CG  1 
ATOM   3024 C CD  . PRO A 1 422 ? 28.395  17.724  -14.010 1.00 47.31  ? 416 PRO A CD  1 
ATOM   3025 N N   . GLN A 1 423 ? 25.936  14.972  -14.889 1.00 48.77  ? 417 GLN A N   1 
ATOM   3026 C CA  . GLN A 1 423 ? 25.442  13.769  -15.544 1.00 48.20  ? 417 GLN A CA  1 
ATOM   3027 C C   . GLN A 1 423 ? 24.455  12.968  -14.694 1.00 47.25  ? 417 GLN A C   1 
ATOM   3028 O O   . GLN A 1 423 ? 23.786  12.068  -15.203 1.00 48.52  ? 417 GLN A O   1 
ATOM   3029 C CB  . GLN A 1 423 ? 26.623  12.823  -15.892 1.00 51.49  ? 417 GLN A CB  1 
ATOM   3030 C CG  . GLN A 1 423 ? 27.773  13.451  -16.677 1.00 55.04  ? 417 GLN A CG  1 
ATOM   3031 C CD  . GLN A 1 423 ? 28.659  14.373  -15.838 1.00 61.01  ? 417 GLN A CD  1 
ATOM   3032 O OE1 . GLN A 1 423 ? 28.537  14.480  -14.626 1.00 58.65  ? 417 GLN A OE1 1 
ATOM   3033 N NE2 . GLN A 1 423 ? 29.595  15.074  -16.471 1.00 66.98  ? 417 GLN A NE2 1 
ATOM   3034 N N   . VAL A 1 424 ? 24.405  13.246  -13.384 1.00 45.72  ? 418 VAL A N   1 
ATOM   3035 C CA  . VAL A 1 424 ? 23.460  12.580  -12.500 1.00 44.18  ? 418 VAL A CA  1 
ATOM   3036 C C   . VAL A 1 424 ? 22.057  12.983  -12.948 1.00 44.22  ? 418 VAL A C   1 
ATOM   3037 O O   . VAL A 1 424 ? 21.870  14.044  -13.544 1.00 43.90  ? 418 VAL A O   1 
ATOM   3038 C CB  . VAL A 1 424 ? 23.751  12.907  -11.004 1.00 45.46  ? 418 VAL A CB  1 
ATOM   3039 C CG1 . VAL A 1 424 ? 22.617  12.468  -10.077 1.00 45.61  ? 418 VAL A CG1 1 
ATOM   3040 C CG2 . VAL A 1 424 ? 25.060  12.271  -10.555 1.00 43.54  ? 418 VAL A CG2 1 
ATOM   3041 N N   . SER A 1 425 ? 21.074  12.114  -12.698 1.00 44.79  ? 419 SER A N   1 
ATOM   3042 C CA  . SER A 1 425 ? 19.712  12.402  -13.110 1.00 46.68  ? 419 SER A CA  1 
ATOM   3043 C C   . SER A 1 425 ? 19.157  13.501  -12.215 1.00 46.98  ? 419 SER A C   1 
ATOM   3044 O O   . SER A 1 425 ? 19.577  13.640  -11.066 1.00 45.09  ? 419 SER A O   1 
ATOM   3045 C CB  . SER A 1 425 ? 18.827  11.166  -13.041 1.00 48.58  ? 419 SER A CB  1 
ATOM   3046 O OG  . SER A 1 425 ? 18.520  10.831  -11.694 1.00 54.33  ? 419 SER A OG  1 
ATOM   3047 N N   . THR A 1 426 ? 18.199  14.258  -12.756 1.00 49.31  ? 420 THR A N   1 
ATOM   3048 C CA  . THR A 1 426 ? 17.614  15.381  -12.041 1.00 49.64  ? 420 THR A CA  1 
ATOM   3049 C C   . THR A 1 426 ? 16.899  14.967  -10.755 1.00 49.62  ? 420 THR A C   1 
ATOM   3050 O O   . THR A 1 426 ? 16.959  15.681  -9.764  1.00 48.83  ? 420 THR A O   1 
ATOM   3051 C CB  . THR A 1 426 ? 16.709  16.159  -12.963 1.00 46.85  ? 420 THR A CB  1 
ATOM   3052 O OG1 . THR A 1 426 ? 17.524  16.714  -13.998 1.00 46.31  ? 420 THR A OG1 1 
ATOM   3053 C CG2 . THR A 1 426 ? 15.975  17.255  -12.245 1.00 45.90  ? 420 THR A CG2 1 
ATOM   3054 N N   . PRO A 1 427 ? 16.167  13.836  -10.711 1.00 51.40  ? 421 PRO A N   1 
ATOM   3055 C CA  . PRO A 1 427 ? 15.538  13.406  -9.457  1.00 50.16  ? 421 PRO A CA  1 
ATOM   3056 C C   . PRO A 1 427 ? 16.559  13.035  -8.388  1.00 49.82  ? 421 PRO A C   1 
ATOM   3057 O O   . PRO A 1 427 ? 16.382  13.360  -7.220  1.00 52.98  ? 421 PRO A O   1 
ATOM   3058 C CB  . PRO A 1 427 ? 14.658  12.229  -9.884  1.00 50.06  ? 421 PRO A CB  1 
ATOM   3059 C CG  . PRO A 1 427 ? 14.457  12.419  -11.380 1.00 50.75  ? 421 PRO A CG  1 
ATOM   3060 C CD  . PRO A 1 427 ? 15.772  13.011  -11.861 1.00 51.13  ? 421 PRO A CD  1 
ATOM   3061 N N   . THR A 1 428 ? 17.648  12.382  -8.793  1.00 49.81  ? 422 THR A N   1 
ATOM   3062 C CA  . THR A 1 428 ? 18.724  12.082  -7.857  1.00 48.72  ? 422 THR A CA  1 
ATOM   3063 C C   . THR A 1 428 ? 19.436  13.305  -7.275  1.00 44.29  ? 422 THR A C   1 
ATOM   3064 O O   . THR A 1 428 ? 19.718  13.333  -6.089  1.00 43.19  ? 422 THR A O   1 
ATOM   3065 C CB  . THR A 1 428 ? 19.698  11.132  -8.525  1.00 49.63  ? 422 THR A CB  1 
ATOM   3066 O OG1 . THR A 1 428 ? 18.955  9.968   -8.891  1.00 50.38  ? 422 THR A OG1 1 
ATOM   3067 C CG2 . THR A 1 428 ? 20.868  10.758  -7.620  1.00 49.02  ? 422 THR A CG2 1 
ATOM   3068 N N   . LEU A 1 429 ? 19.723  14.322  -8.090  1.00 44.71  ? 423 LEU A N   1 
ATOM   3069 C CA  . LEU A 1 429 ? 20.328  15.547  -7.584  1.00 44.96  ? 423 LEU A CA  1 
ATOM   3070 C C   . LEU A 1 429 ? 19.427  16.286  -6.597  1.00 47.23  ? 423 LEU A C   1 
ATOM   3071 O O   . LEU A 1 429 ? 19.922  16.851  -5.624  1.00 48.01  ? 423 LEU A O   1 
ATOM   3072 C CB  . LEU A 1 429 ? 20.700  16.473  -8.745  1.00 44.26  ? 423 LEU A CB  1 
ATOM   3073 C CG  . LEU A 1 429 ? 21.897  16.000  -9.591  1.00 45.12  ? 423 LEU A CG  1 
ATOM   3074 C CD1 . LEU A 1 429 ? 22.081  16.837  -10.832 1.00 45.46  ? 423 LEU A CD1 1 
ATOM   3075 C CD2 . LEU A 1 429 ? 23.173  16.016  -8.785  1.00 44.58  ? 423 LEU A CD2 1 
ATOM   3076 N N   . VAL A 1 430 ? 18.107  16.254  -6.846  1.00 47.92  ? 424 VAL A N   1 
ATOM   3077 C CA  . VAL A 1 430 ? 17.130  16.910  -5.992  1.00 47.25  ? 424 VAL A CA  1 
ATOM   3078 C C   . VAL A 1 430 ? 17.090  16.256  -4.614  1.00 48.12  ? 424 VAL A C   1 
ATOM   3079 O O   . VAL A 1 430 ? 17.102  16.960  -3.607  1.00 45.57  ? 424 VAL A O   1 
ATOM   3080 C CB  . VAL A 1 430 ? 15.707  16.943  -6.637  1.00 47.59  ? 424 VAL A CB  1 
ATOM   3081 C CG1 . VAL A 1 430 ? 14.628  17.368  -5.627  1.00 47.46  ? 424 VAL A CG1 1 
ATOM   3082 C CG2 . VAL A 1 430 ? 15.672  17.857  -7.844  1.00 46.62  ? 424 VAL A CG2 1 
ATOM   3083 N N   . GLU A 1 431 ? 17.026  14.918  -4.581  1.00 50.13  ? 425 GLU A N   1 
ATOM   3084 C CA  . GLU A 1 431 ? 16.886  14.195  -3.327  1.00 56.82  ? 425 GLU A CA  1 
ATOM   3085 C C   . GLU A 1 431 ? 18.153  14.268  -2.463  1.00 56.63  ? 425 GLU A C   1 
ATOM   3086 O O   . GLU A 1 431 ? 18.079  14.489  -1.250  1.00 56.86  ? 425 GLU A O   1 
ATOM   3087 C CB  . GLU A 1 431 ? 16.473  12.732  -3.589  1.00 62.81  ? 425 GLU A CB  1 
ATOM   3088 C CG  . GLU A 1 431 ? 15.179  12.589  -4.401  1.00 73.74  ? 425 GLU A CG  1 
ATOM   3089 C CD  . GLU A 1 431 ? 13.852  12.955  -3.738  1.00 80.58  ? 425 GLU A CD  1 
ATOM   3090 O OE1 . GLU A 1 431 ? 13.330  12.122  -2.957  1.00 84.62  ? 425 GLU A OE1 1 
ATOM   3091 O OE2 . GLU A 1 431 ? 13.323  14.061  -4.015  1.00 79.59  ? 425 GLU A OE2 1 
ATOM   3092 N N   . VAL A 1 432 ? 19.320  14.104  -3.095  1.00 53.42  ? 426 VAL A N   1 
ATOM   3093 C CA  . VAL A 1 432 ? 20.593  14.224  -2.404  1.00 51.20  ? 426 VAL A CA  1 
ATOM   3094 C C   . VAL A 1 432 ? 20.774  15.606  -1.783  1.00 49.97  ? 426 VAL A C   1 
ATOM   3095 O O   . VAL A 1 432 ? 21.154  15.711  -0.621  1.00 51.66  ? 426 VAL A O   1 
ATOM   3096 C CB  . VAL A 1 432 ? 21.758  13.866  -3.356  1.00 50.89  ? 426 VAL A CB  1 
ATOM   3097 C CG1 . VAL A 1 432 ? 23.116  14.366  -2.844  1.00 50.27  ? 426 VAL A CG1 1 
ATOM   3098 C CG2 . VAL A 1 432 ? 21.790  12.364  -3.599  1.00 51.42  ? 426 VAL A CG2 1 
ATOM   3099 N N   . SER A 1 433 ? 20.531  16.655  -2.570  1.00 48.46  ? 427 SER A N   1 
ATOM   3100 C CA  . SER A 1 433 ? 20.664  18.017  -2.085  1.00 48.89  ? 427 SER A CA  1 
ATOM   3101 C C   . SER A 1 433 ? 19.643  18.326  -0.996  1.00 48.13  ? 427 SER A C   1 
ATOM   3102 O O   . SER A 1 433 ? 19.949  19.038  -0.044  1.00 49.34  ? 427 SER A O   1 
ATOM   3103 C CB  . SER A 1 433 ? 20.505  19.010  -3.224  1.00 49.77  ? 427 SER A CB  1 
ATOM   3104 O OG  . SER A 1 433 ? 21.358  18.652  -4.297  1.00 51.07  ? 427 SER A OG  1 
ATOM   3105 N N   . ARG A 1 434 ? 18.430  17.788  -1.155  1.00 47.32  ? 428 ARG A N   1 
ATOM   3106 C CA  . ARG A 1 434 ? 17.364  17.998  -0.196  1.00 47.31  ? 428 ARG A CA  1 
ATOM   3107 C C   . ARG A 1 434 ? 17.788  17.410  1.144   1.00 49.23  ? 428 ARG A C   1 
ATOM   3108 O O   . ARG A 1 434 ? 17.691  18.084  2.173   1.00 50.40  ? 428 ARG A O   1 
ATOM   3109 C CB  . ARG A 1 434 ? 16.014  17.396  -0.695  1.00 45.88  ? 428 ARG A CB  1 
ATOM   3110 C CG  . ARG A 1 434 ? 15.234  18.367  -1.585  1.00 45.45  ? 428 ARG A CG  1 
ATOM   3111 C CD  . ARG A 1 434 ? 13.851  17.877  -1.986  1.00 45.47  ? 428 ARG A CD  1 
ATOM   3112 N NE  . ARG A 1 434 ? 12.890  17.876  -0.887  1.00 44.30  ? 428 ARG A NE  1 
ATOM   3113 C CZ  . ARG A 1 434 ? 12.308  18.959  -0.387  1.00 44.70  ? 428 ARG A CZ  1 
ATOM   3114 N NH1 . ARG A 1 434 ? 12.480  20.155  -0.924  1.00 44.35  ? 428 ARG A NH1 1 
ATOM   3115 N NH2 . ARG A 1 434 ? 11.542  18.842  0.692   1.00 46.19  ? 428 ARG A NH2 1 
ATOM   3116 N N   . ASN A 1 435 ? 18.279  16.165  1.111   1.00 48.61  ? 429 ASN A N   1 
ATOM   3117 C CA  . ASN A 1 435 ? 18.738  15.494  2.316   1.00 51.35  ? 429 ASN A CA  1 
ATOM   3118 C C   . ASN A 1 435 ? 19.959  16.157  2.949   1.00 52.15  ? 429 ASN A C   1 
ATOM   3119 O O   . ASN A 1 435 ? 20.039  16.241  4.169   1.00 57.13  ? 429 ASN A O   1 
ATOM   3120 C CB  . ASN A 1 435 ? 19.050  14.032  2.049   1.00 53.60  ? 429 ASN A CB  1 
ATOM   3121 C CG  . ASN A 1 435 ? 17.841  13.208  1.710   1.00 55.94  ? 429 ASN A CG  1 
ATOM   3122 O OD1 . ASN A 1 435 ? 16.686  13.630  1.868   1.00 58.03  ? 429 ASN A OD1 1 
ATOM   3123 N ND2 . ASN A 1 435 ? 18.085  12.012  1.232   1.00 57.49  ? 429 ASN A ND2 1 
ATOM   3124 N N   . LEU A 1 436 ? 20.906  16.633  2.134   1.00 51.30  ? 430 LEU A N   1 
ATOM   3125 C CA  . LEU A 1 436 ? 22.068  17.315  2.679   1.00 50.76  ? 430 LEU A CA  1 
ATOM   3126 C C   . LEU A 1 436 ? 21.640  18.577  3.421   1.00 50.91  ? 430 LEU A C   1 
ATOM   3127 O O   . LEU A 1 436 ? 22.239  18.935  4.425   1.00 51.60  ? 430 LEU A O   1 
ATOM   3128 C CB  . LEU A 1 436 ? 23.062  17.699  1.605   1.00 49.09  ? 430 LEU A CB  1 
ATOM   3129 C CG  . LEU A 1 436 ? 23.927  16.582  1.075   1.00 50.37  ? 430 LEU A CG  1 
ATOM   3130 C CD1 . LEU A 1 436 ? 24.949  17.132  0.120   1.00 52.22  ? 430 LEU A CD1 1 
ATOM   3131 C CD2 . LEU A 1 436 ? 24.599  15.849  2.163   1.00 49.45  ? 430 LEU A CD2 1 
ATOM   3132 N N   . GLY A 1 437 ? 20.604  19.246  2.916   1.00 50.94  ? 431 GLY A N   1 
ATOM   3133 C CA  . GLY A 1 437 ? 20.112  20.457  3.545   1.00 51.64  ? 431 GLY A CA  1 
ATOM   3134 C C   . GLY A 1 437 ? 19.545  20.206  4.939   1.00 51.74  ? 431 GLY A C   1 
ATOM   3135 O O   . GLY A 1 437 ? 19.732  21.017  5.839   1.00 47.73  ? 431 GLY A O   1 
ATOM   3136 N N   . LYS A 1 438 ? 18.855  19.073  5.097   1.00 54.73  ? 432 LYS A N   1 
ATOM   3137 C CA  . LYS A 1 438 ? 18.263  18.718  6.372   1.00 58.25  ? 432 LYS A CA  1 
ATOM   3138 C C   . LYS A 1 438 ? 19.369  18.443  7.390   1.00 56.60  ? 432 LYS A C   1 
ATOM   3139 O O   . LYS A 1 438 ? 19.260  18.846  8.546   1.00 55.86  ? 432 LYS A O   1 
ATOM   3140 C CB  . LYS A 1 438 ? 17.353  17.502  6.217   1.00 61.99  ? 432 LYS A CB  1 
ATOM   3141 C CG  . LYS A 1 438 ? 16.154  17.733  5.345   1.00 65.14  ? 432 LYS A CG  1 
ATOM   3142 C CD  . LYS A 1 438 ? 15.421  16.433  5.080   1.00 70.87  ? 432 LYS A CD  1 
ATOM   3143 C CE  . LYS A 1 438 ? 14.219  16.598  4.190   1.00 77.00  ? 432 LYS A CE  1 
ATOM   3144 N NZ  . LYS A 1 438 ? 13.876  15.314  3.505   1.00 81.53  ? 432 LYS A NZ  1 
ATOM   3145 N N   . VAL A 1 439 ? 20.437  17.769  6.939   1.00 54.88  ? 433 VAL A N   1 
ATOM   3146 C CA  . VAL A 1 439 ? 21.638  17.595  7.738   1.00 53.32  ? 433 VAL A CA  1 
ATOM   3147 C C   . VAL A 1 439 ? 22.074  18.929  8.331   1.00 52.13  ? 433 VAL A C   1 
ATOM   3148 O O   . VAL A 1 439 ? 22.425  19.008  9.504   1.00 51.20  ? 433 VAL A O   1 
ATOM   3149 C CB  . VAL A 1 439 ? 22.795  16.997  6.940   1.00 52.44  ? 433 VAL A CB  1 
ATOM   3150 C CG1 . VAL A 1 439 ? 24.090  17.019  7.756   1.00 51.98  ? 433 VAL A CG1 1 
ATOM   3151 C CG2 . VAL A 1 439 ? 22.461  15.585  6.486   1.00 54.96  ? 433 VAL A CG2 1 
ATOM   3152 N N   . GLY A 1 440 ? 22.078  19.964  7.495   1.00 52.23  ? 434 GLY A N   1 
ATOM   3153 C CA  . GLY A 1 440 ? 22.294  21.317  7.972   1.00 56.75  ? 434 GLY A CA  1 
ATOM   3154 C C   . GLY A 1 440 ? 21.384  21.730  9.132   1.00 58.18  ? 434 GLY A C   1 
ATOM   3155 O O   . GLY A 1 440 ? 21.846  22.338  10.092  1.00 58.49  ? 434 GLY A O   1 
ATOM   3156 N N   . SER A 1 441 ? 20.088  21.410  9.039   1.00 58.63  ? 435 SER A N   1 
ATOM   3157 C CA  . SER A 1 441 ? 19.134  21.908  10.014  1.00 63.86  ? 435 SER A CA  1 
ATOM   3158 C C   . SER A 1 441 ? 19.204  21.108  11.309  1.00 65.62  ? 435 SER A C   1 
ATOM   3159 O O   . SER A 1 441 ? 18.903  21.630  12.379  1.00 66.72  ? 435 SER A O   1 
ATOM   3160 C CB  . SER A 1 441 ? 17.717  21.930  9.446   1.00 65.51  ? 435 SER A CB  1 
ATOM   3161 O OG  . SER A 1 441 ? 17.372  20.713  8.809   1.00 67.11  ? 435 SER A OG  1 
ATOM   3162 N N   . LYS A 1 442 ? 19.626  19.848  11.206  1.00 67.56  ? 436 LYS A N   1 
ATOM   3163 C CA  . LYS A 1 442 ? 19.714  18.991  12.374  1.00 69.90  ? 436 LYS A CA  1 
ATOM   3164 C C   . LYS A 1 442 ? 20.986  19.277  13.170  1.00 67.33  ? 436 LYS A C   1 
ATOM   3165 O O   . LYS A 1 442 ? 20.957  19.218  14.397  1.00 74.03  ? 436 LYS A O   1 
ATOM   3166 C CB  . LYS A 1 442 ? 19.625  17.508  11.964  1.00 75.10  ? 436 LYS A CB  1 
ATOM   3167 C CG  . LYS A 1 442 ? 19.484  16.522  13.138  1.00 82.54  ? 436 LYS A CG  1 
ATOM   3168 C CD  . LYS A 1 442 ? 18.157  16.689  13.961  1.00 87.38  ? 436 LYS A CD  1 
ATOM   3169 C CE  . LYS A 1 442 ? 18.193  16.017  15.322  1.00 86.83  ? 436 LYS A CE  1 
ATOM   3170 N NZ  . LYS A 1 442 ? 19.245  16.608  16.194  1.00 86.18  ? 436 LYS A NZ  1 
ATOM   3171 N N   . CYS A 1 443 ? 22.081  19.622  12.477  1.00 64.00  ? 437 CYS A N   1 
ATOM   3172 C CA  . CYS A 1 443 ? 23.397  19.740  13.096  1.00 62.64  ? 437 CYS A CA  1 
ATOM   3173 C C   . CYS A 1 443 ? 23.807  21.171  13.439  1.00 61.95  ? 437 CYS A C   1 
ATOM   3174 O O   . CYS A 1 443 ? 24.492  21.400  14.428  1.00 61.66  ? 437 CYS A O   1 
ATOM   3175 C CB  . CYS A 1 443 ? 24.450  19.075  12.212  1.00 61.83  ? 437 CYS A CB  1 
ATOM   3176 S SG  . CYS A 1 443 ? 24.159  17.308  11.947  1.00 64.70  ? 437 CYS A SG  1 
ATOM   3177 N N   . CYS A 1 444 ? 23.456  22.127  12.591  1.00 61.27  ? 438 CYS A N   1 
ATOM   3178 C CA  . CYS A 1 444 ? 23.943  23.513  12.799  1.00 63.89  ? 438 CYS A CA  1 
ATOM   3179 C C   . CYS A 1 444 ? 23.276  24.145  14.030  1.00 65.51  ? 438 CYS A C   1 
ATOM   3180 O O   . CYS A 1 444 ? 23.768  25.176  14.483  1.00 65.59  ? 438 CYS A O   1 
ATOM   3181 C CB  . CYS A 1 444 ? 23.746  24.353  11.541  1.00 63.95  ? 438 CYS A CB  1 
ATOM   3182 S SG  . CYS A 1 444 ? 24.752  23.893  10.108  1.00 62.10  ? 438 CYS A SG  1 
ATOM   3183 N N   . LYS A 1 445 ? 22.175  23.585  14.508  1.00 70.85  ? 439 LYS A N   1 
ATOM   3184 C CA  . LYS A 1 445 ? 21.531  24.074  15.748  1.00 76.31  ? 439 LYS A CA  1 
ATOM   3185 C C   . LYS A 1 445 ? 22.478  23.887  16.928  1.00 76.93  ? 439 LYS A C   1 
ATOM   3186 O O   . LYS A 1 445 ? 22.560  24.788  17.778  1.00 73.65  ? 439 LYS A O   1 
ATOM   3187 C CB  . LYS A 1 445 ? 20.312  23.192  16.014  1.00 80.51  ? 439 LYS A CB  1 
ATOM   3188 C CG  . LYS A 1 445 ? 19.591  23.444  17.332  1.00 88.65  ? 439 LYS A CG  1 
ATOM   3189 C CD  . LYS A 1 445 ? 19.845  22.405  18.419  1.00 93.41  ? 439 LYS A CD  1 
ATOM   3190 C CE  . LYS A 1 445 ? 19.925  22.993  19.795  1.00 94.51  ? 439 LYS A CE  1 
ATOM   3191 N NZ  . LYS A 1 445 ? 20.768  22.198  20.691  1.00 94.40  ? 439 LYS A NZ  1 
ATOM   3192 N N   . HIS A 1 446 ? 23.162  22.750  16.961  1.00 76.58  ? 440 HIS A N   1 
ATOM   3193 C CA  . HIS A 1 446 ? 24.101  22.400  18.053  1.00 72.41  ? 440 HIS A CA  1 
ATOM   3194 C C   . HIS A 1 446 ? 25.346  23.287  18.051  1.00 70.35  ? 440 HIS A C   1 
ATOM   3195 O O   . HIS A 1 446 ? 25.768  23.767  16.990  1.00 67.74  ? 440 HIS A O   1 
ATOM   3196 C CB  . HIS A 1 446 ? 24.457  20.918  17.947  1.00 72.58  ? 440 HIS A CB  1 
ATOM   3197 C CG  . HIS A 1 446 ? 23.303  19.983  18.000  1.00 76.09  ? 440 HIS A CG  1 
ATOM   3198 N ND1 . HIS A 1 446 ? 23.159  18.948  17.105  1.00 78.13  ? 440 HIS A ND1 1 
ATOM   3199 C CD2 . HIS A 1 446 ? 22.264  19.901  18.831  1.00 78.35  ? 440 HIS A CD2 1 
ATOM   3200 C CE1 . HIS A 1 446 ? 22.057  18.275  17.390  1.00 77.06  ? 440 HIS A CE1 1 
ATOM   3201 N NE2 . HIS A 1 446 ? 21.497  18.839  18.433  1.00 78.18  ? 440 HIS A NE2 1 
ATOM   3202 N N   . PRO A 1 447 ? 25.940  23.596  19.231  1.00 69.52  ? 441 PRO A N   1 
ATOM   3203 C CA  . PRO A 1 447 ? 27.186  24.342  19.268  1.00 68.04  ? 441 PRO A CA  1 
ATOM   3204 C C   . PRO A 1 447 ? 28.275  23.604  18.520  1.00 67.65  ? 441 PRO A C   1 
ATOM   3205 O O   . PRO A 1 447 ? 28.079  22.426  18.209  1.00 70.17  ? 441 PRO A O   1 
ATOM   3206 C CB  . PRO A 1 447 ? 27.451  24.413  20.765  1.00 68.21  ? 441 PRO A CB  1 
ATOM   3207 C CG  . PRO A 1 447 ? 26.747  23.215  21.328  1.00 68.12  ? 441 PRO A CG  1 
ATOM   3208 C CD  . PRO A 1 447 ? 25.446  23.279  20.573  1.00 67.85  ? 441 PRO A CD  1 
ATOM   3209 N N   . GLU A 1 448 ? 29.445  24.209  18.354  1.00 67.05  ? 442 GLU A N   1 
ATOM   3210 C CA  . GLU A 1 448 ? 30.485  23.585  17.509  1.00 67.68  ? 442 GLU A CA  1 
ATOM   3211 C C   . GLU A 1 448 ? 30.902  22.248  18.096  1.00 66.44  ? 442 GLU A C   1 
ATOM   3212 O O   . GLU A 1 448 ? 31.098  21.315  17.317  1.00 69.68  ? 442 GLU A O   1 
ATOM   3213 C CB  . GLU A 1 448 ? 31.757  24.413  17.503  1.00 71.75  ? 442 GLU A CB  1 
ATOM   3214 C CG  . GLU A 1 448 ? 32.602  24.220  16.248  1.00 80.05  ? 442 GLU A CG  1 
ATOM   3215 C CD  . GLU A 1 448 ? 33.549  23.032  16.233  1.00 87.93  ? 442 GLU A CD  1 
ATOM   3216 O OE1 . GLU A 1 448 ? 34.277  22.829  17.225  1.00 93.89  ? 442 GLU A OE1 1 
ATOM   3217 O OE2 . GLU A 1 448 ? 33.557  22.309  15.216  1.00 91.69  ? 442 GLU A OE2 1 
ATOM   3218 N N   . ALA A 1 449 ? 31.033  22.166  19.409  1.00 63.69  ? 443 ALA A N   1 
ATOM   3219 C CA  . ALA A 1 449 ? 31.522  20.933  20.055  1.00 62.61  ? 443 ALA A CA  1 
ATOM   3220 C C   . ALA A 1 449 ? 30.678  19.730  19.660  1.00 60.18  ? 443 ALA A C   1 
ATOM   3221 O O   . ALA A 1 449 ? 31.152  18.605  19.794  1.00 60.34  ? 443 ALA A O   1 
ATOM   3222 C CB  . ALA A 1 449 ? 31.495  21.119  21.537  1.00 62.19  ? 443 ALA A CB  1 
ATOM   3223 N N   . LYS A 1 450 ? 29.444  19.958  19.250  1.00 61.13  ? 444 LYS A N   1 
ATOM   3224 C CA  . LYS A 1 450 ? 28.606  18.814  18.927  1.00 61.33  ? 444 LYS A CA  1 
ATOM   3225 C C   . LYS A 1 450 ? 28.441  18.579  17.423  1.00 57.89  ? 444 LYS A C   1 
ATOM   3226 O O   . LYS A 1 450 ? 27.808  17.603  17.027  1.00 57.32  ? 444 LYS A O   1 
ATOM   3227 C CB  . LYS A 1 450 ? 27.239  19.002  19.612  1.00 64.88  ? 444 LYS A CB  1 
ATOM   3228 C CG  . LYS A 1 450 ? 27.259  18.731  21.123  1.00 68.52  ? 444 LYS A CG  1 
ATOM   3229 C CD  . LYS A 1 450 ? 26.206  19.554  21.928  1.00 74.79  ? 444 LYS A CD  1 
ATOM   3230 C CE  . LYS A 1 450 ? 24.766  19.073  21.820  1.00 78.78  ? 444 LYS A CE  1 
ATOM   3231 N NZ  . LYS A 1 450 ? 24.483  17.916  22.724  1.00 80.81  ? 444 LYS A NZ  1 
ATOM   3232 N N   . ARG A 1 451 ? 29.064  19.424  16.587  1.00 54.24  ? 445 ARG A N   1 
ATOM   3233 C CA  . ARG A 1 451 ? 28.740  19.476  15.168  1.00 54.86  ? 445 ARG A CA  1 
ATOM   3234 C C   . ARG A 1 451 ? 29.338  18.372  14.295  1.00 54.42  ? 445 ARG A C   1 
ATOM   3235 O O   . ARG A 1 451 ? 28.640  17.808  13.454  1.00 54.12  ? 445 ARG A O   1 
ATOM   3236 C CB  . ARG A 1 451 ? 29.155  20.833  14.590  1.00 56.12  ? 445 ARG A CB  1 
ATOM   3237 C CG  . ARG A 1 451 ? 28.265  21.962  15.075  1.00 57.04  ? 445 ARG A CG  1 
ATOM   3238 C CD  . ARG A 1 451 ? 28.484  23.264  14.327  1.00 56.90  ? 445 ARG A CD  1 
ATOM   3239 N NE  . ARG A 1 451 ? 27.531  24.271  14.779  1.00 57.60  ? 445 ARG A NE  1 
ATOM   3240 C CZ  . ARG A 1 451 ? 27.312  25.429  14.175  1.00 59.86  ? 445 ARG A CZ  1 
ATOM   3241 N NH1 . ARG A 1 451 ? 28.274  26.069  13.529  1.00 58.48  ? 445 ARG A NH1 1 
ATOM   3242 N NH2 . ARG A 1 451 ? 26.095  25.966  14.225  1.00 63.55  ? 445 ARG A NH2 1 
ATOM   3243 N N   . MET A 1 452 ? 30.630  18.075  14.480  1.00 54.43  ? 446 MET A N   1 
ATOM   3244 C CA  . MET A 1 452 ? 31.313  17.102  13.640  1.00 56.72  ? 446 MET A CA  1 
ATOM   3245 C C   . MET A 1 452 ? 30.733  15.695  13.823  1.00 55.76  ? 446 MET A C   1 
ATOM   3246 O O   . MET A 1 452 ? 30.527  14.986  12.837  1.00 56.33  ? 446 MET A O   1 
ATOM   3247 C CB  . MET A 1 452 ? 32.844  17.141  13.913  1.00 60.82  ? 446 MET A CB  1 
ATOM   3248 C CG  . MET A 1 452 ? 33.713  16.566  12.751  1.00 61.15  ? 446 MET A CG  1 
ATOM   3249 S SD  . MET A 1 452 ? 35.526  16.693  13.009  1.00 59.36  ? 446 MET A SD  1 
ATOM   3250 C CE  . MET A 1 452 ? 35.691  18.400  13.367  1.00 57.65  ? 446 MET A CE  1 
ATOM   3251 N N   . PRO A 1 453 ? 30.414  15.242  15.062  1.00 52.88  ? 447 PRO A N   1 
ATOM   3252 C CA  . PRO A 1 453 ? 29.806  13.930  15.260  1.00 52.96  ? 447 PRO A CA  1 
ATOM   3253 C C   . PRO A 1 453 ? 28.390  13.839  14.701  1.00 53.53  ? 447 PRO A C   1 
ATOM   3254 O O   . PRO A 1 453 ? 27.963  12.779  14.247  1.00 53.22  ? 447 PRO A O   1 
ATOM   3255 C CB  . PRO A 1 453 ? 29.829  13.747  16.790  1.00 52.52  ? 447 PRO A CB  1 
ATOM   3256 C CG  . PRO A 1 453 ? 30.777  14.774  17.301  1.00 52.88  ? 447 PRO A CG  1 
ATOM   3257 C CD  . PRO A 1 453 ? 30.667  15.921  16.342  1.00 54.04  ? 447 PRO A CD  1 
ATOM   3258 N N   . CYS A 1 454 ? 27.659  14.955  14.744  1.00 52.88  ? 448 CYS A N   1 
ATOM   3259 C CA  . CYS A 1 454 ? 26.326  14.974  14.171  1.00 53.55  ? 448 CYS A CA  1 
ATOM   3260 C C   . CYS A 1 454 ? 26.388  14.868  12.644  1.00 48.84  ? 448 CYS A C   1 
ATOM   3261 O O   . CYS A 1 454 ? 25.778  13.980  12.055  1.00 44.68  ? 448 CYS A O   1 
ATOM   3262 C CB  . CYS A 1 454 ? 25.558  16.210  14.630  1.00 55.05  ? 448 CYS A CB  1 
ATOM   3263 S SG  . CYS A 1 454 ? 23.792  16.162  14.217  1.00 62.65  ? 448 CYS A SG  1 
ATOM   3264 N N   . ALA A 1 455 ? 27.120  15.790  12.012  1.00 47.42  ? 449 ALA A N   1 
ATOM   3265 C CA  . ALA A 1 455 ? 27.377  15.711  10.585  1.00 49.82  ? 449 ALA A CA  1 
ATOM   3266 C C   . ALA A 1 455 ? 27.757  14.284  10.199  1.00 50.90  ? 449 ALA A C   1 
ATOM   3267 O O   . ALA A 1 455 ? 27.081  13.668  9.384   1.00 50.08  ? 449 ALA A O   1 
ATOM   3268 C CB  . ALA A 1 455 ? 28.478  16.677  10.191  1.00 50.65  ? 449 ALA A CB  1 
ATOM   3269 N N   . GLU A 1 456 ? 28.809  13.746  10.831  1.00 52.99  ? 450 GLU A N   1 
ATOM   3270 C CA  . GLU A 1 456 ? 29.284  12.408  10.518  1.00 54.73  ? 450 GLU A CA  1 
ATOM   3271 C C   . GLU A 1 456 ? 28.150  11.385  10.563  1.00 55.97  ? 450 GLU A C   1 
ATOM   3272 O O   . GLU A 1 456 ? 28.021  10.579  9.643   1.00 53.84  ? 450 GLU A O   1 
ATOM   3273 C CB  . GLU A 1 456 ? 30.416  11.969  11.458  1.00 55.03  ? 450 GLU A CB  1 
ATOM   3274 C CG  . GLU A 1 456 ? 31.059  10.653  11.043  1.00 56.90  ? 450 GLU A CG  1 
ATOM   3275 C CD  . GLU A 1 456 ? 31.938  9.925   12.060  1.00 60.86  ? 450 GLU A CD  1 
ATOM   3276 O OE1 . GLU A 1 456 ? 31.813  10.160  13.290  1.00 58.74  ? 450 GLU A OE1 1 
ATOM   3277 O OE2 . GLU A 1 456 ? 32.781  9.117   11.601  1.00 61.76  ? 450 GLU A OE2 1 
ATOM   3278 N N   . ASP A 1 457 ? 27.337  11.438  11.629  1.00 61.07  ? 451 ASP A N   1 
ATOM   3279 C CA  . ASP A 1 457 ? 26.217  10.525  11.829  1.00 64.57  ? 451 ASP A CA  1 
ATOM   3280 C C   . ASP A 1 457 ? 25.277  10.459  10.625  1.00 65.10  ? 451 ASP A C   1 
ATOM   3281 O O   . ASP A 1 457 ? 25.011  9.373   10.111  1.00 66.93  ? 451 ASP A O   1 
ATOM   3282 C CB  . ASP A 1 457 ? 25.410  10.932  13.087  1.00 68.69  ? 451 ASP A CB  1 
ATOM   3283 C CG  . ASP A 1 457 ? 24.297  9.971   13.502  1.00 75.09  ? 451 ASP A CG  1 
ATOM   3284 O OD1 . ASP A 1 457 ? 24.261  8.831   12.974  1.00 75.37  ? 451 ASP A OD1 1 
ATOM   3285 O OD2 . ASP A 1 457 ? 23.448  10.366  14.342  1.00 80.42  ? 451 ASP A OD2 1 
ATOM   3286 N N   . TYR A 1 458 ? 24.795  11.628  10.178  1.00 64.54  ? 452 TYR A N   1 
ATOM   3287 C CA  . TYR A 1 458 ? 23.797  11.718  9.121   1.00 65.04  ? 452 TYR A CA  1 
ATOM   3288 C C   . TYR A 1 458 ? 24.382  11.711  7.709   1.00 63.76  ? 452 TYR A C   1 
ATOM   3289 O O   . TYR A 1 458 ? 23.775  11.173  6.788   1.00 61.22  ? 452 TYR A O   1 
ATOM   3290 C CB  . TYR A 1 458 ? 22.938  12.979  9.345   1.00 66.55  ? 452 TYR A CB  1 
ATOM   3291 C CG  . TYR A 1 458 ? 22.064  12.830  10.567  1.00 69.94  ? 452 TYR A CG  1 
ATOM   3292 C CD1 . TYR A 1 458 ? 20.990  11.950  10.572  1.00 72.32  ? 452 TYR A CD1 1 
ATOM   3293 C CD2 . TYR A 1 458 ? 22.356  13.506  11.745  1.00 72.93  ? 452 TYR A CD2 1 
ATOM   3294 C CE1 . TYR A 1 458 ? 20.205  11.773  11.702  1.00 74.48  ? 452 TYR A CE1 1 
ATOM   3295 C CE2 . TYR A 1 458 ? 21.578  13.336  12.886  1.00 76.06  ? 452 TYR A CE2 1 
ATOM   3296 C CZ  . TYR A 1 458 ? 20.500  12.467  12.859  1.00 78.28  ? 452 TYR A CZ  1 
ATOM   3297 O OH  . TYR A 1 458 ? 19.710  12.283  13.971  1.00 81.81  ? 452 TYR A OH  1 
ATOM   3298 N N   . LEU A 1 459 ? 25.568  12.303  7.545   1.00 61.91  ? 453 LEU A N   1 
ATOM   3299 C CA  . LEU A 1 459 ? 26.184  12.406  6.236   1.00 62.16  ? 453 LEU A CA  1 
ATOM   3300 C C   . LEU A 1 459 ? 26.665  11.037  5.761   1.00 62.38  ? 453 LEU A C   1 
ATOM   3301 O O   . LEU A 1 459 ? 26.593  10.718  4.577   1.00 64.11  ? 453 LEU A O   1 
ATOM   3302 C CB  . LEU A 1 459 ? 27.313  13.421  6.299   1.00 64.14  ? 453 LEU A CB  1 
ATOM   3303 C CG  . LEU A 1 459 ? 27.775  13.996  4.979   1.00 68.03  ? 453 LEU A CG  1 
ATOM   3304 C CD1 . LEU A 1 459 ? 26.701  14.842  4.349   1.00 68.03  ? 453 LEU A CD1 1 
ATOM   3305 C CD2 . LEU A 1 459 ? 29.056  14.836  5.158   1.00 67.29  ? 453 LEU A CD2 1 
ATOM   3306 N N   . SER A 1 460 ? 27.105  10.199  6.700   1.00 64.19  ? 454 SER A N   1 
ATOM   3307 C CA  . SER A 1 460 ? 27.550  8.857   6.364   1.00 64.92  ? 454 SER A CA  1 
ATOM   3308 C C   . SER A 1 460 ? 26.434  7.990   5.780   1.00 64.98  ? 454 SER A C   1 
ATOM   3309 O O   . SER A 1 460 ? 26.699  7.144   4.928   1.00 67.07  ? 454 SER A O   1 
ATOM   3310 C CB  . SER A 1 460 ? 28.165  8.167   7.578   1.00 65.56  ? 454 SER A CB  1 
ATOM   3311 O OG  . SER A 1 460 ? 27.172  7.840   8.533   1.00 68.13  ? 454 SER A OG  1 
ATOM   3312 N N   . VAL A 1 461 ? 25.190  8.187   6.234   1.00 65.45  ? 455 VAL A N   1 
ATOM   3313 C CA  . VAL A 1 461 ? 24.074  7.460   5.645   1.00 65.66  ? 455 VAL A CA  1 
ATOM   3314 C C   . VAL A 1 461 ? 23.742  7.986   4.249   1.00 62.59  ? 455 VAL A C   1 
ATOM   3315 O O   . VAL A 1 461 ? 23.450  7.193   3.357   1.00 60.67  ? 455 VAL A O   1 
ATOM   3316 C CB  . VAL A 1 461 ? 22.806  7.417   6.520   1.00 68.08  ? 455 VAL A CB  1 
ATOM   3317 C CG1 . VAL A 1 461 ? 22.317  8.795   6.896   1.00 70.18  ? 455 VAL A CG1 1 
ATOM   3318 C CG2 . VAL A 1 461 ? 21.701  6.646   5.818   1.00 70.31  ? 455 VAL A CG2 1 
ATOM   3319 N N   . VAL A 1 462 ? 23.794  9.313   4.059   1.00 60.68  ? 456 VAL A N   1 
ATOM   3320 C CA  . VAL A 1 462 ? 23.537  9.891   2.750   1.00 58.70  ? 456 VAL A CA  1 
ATOM   3321 C C   . VAL A 1 462 ? 24.550  9.350   1.743   1.00 60.47  ? 456 VAL A C   1 
ATOM   3322 O O   . VAL A 1 462 ? 24.168  8.882   0.675   1.00 63.46  ? 456 VAL A O   1 
ATOM   3323 C CB  . VAL A 1 462 ? 23.548  11.428  2.750   1.00 59.03  ? 456 VAL A CB  1 
ATOM   3324 C CG1 . VAL A 1 462 ? 23.307  11.978  1.358   1.00 59.34  ? 456 VAL A CG1 1 
ATOM   3325 C CG2 . VAL A 1 462 ? 22.517  11.984  3.708   1.00 61.74  ? 456 VAL A CG2 1 
ATOM   3326 N N   . LEU A 1 463 ? 25.842  9.394   2.089   1.00 59.72  ? 457 LEU A N   1 
ATOM   3327 C CA  . LEU A 1 463 ? 26.881  9.008   1.151   1.00 58.43  ? 457 LEU A CA  1 
ATOM   3328 C C   . LEU A 1 463 ? 26.851  7.525   0.791   1.00 60.34  ? 457 LEU A C   1 
ATOM   3329 O O   . LEU A 1 463 ? 27.233  7.142   -0.312  1.00 61.23  ? 457 LEU A O   1 
ATOM   3330 C CB  . LEU A 1 463 ? 28.229  9.404   1.728   1.00 57.37  ? 457 LEU A CB  1 
ATOM   3331 C CG  . LEU A 1 463 ? 28.434  10.907  1.764   1.00 58.92  ? 457 LEU A CG  1 
ATOM   3332 C CD1 . LEU A 1 463 ? 29.824  11.262  2.241   1.00 59.62  ? 457 LEU A CD1 1 
ATOM   3333 C CD2 . LEU A 1 463 ? 28.176  11.540  0.390   1.00 58.79  ? 457 LEU A CD2 1 
ATOM   3334 N N   . ASN A 1 464 ? 26.366  6.692   1.710   1.00 62.58  ? 458 ASN A N   1 
ATOM   3335 C CA  . ASN A 1 464 ? 26.237  5.271   1.442   1.00 67.64  ? 458 ASN A CA  1 
ATOM   3336 C C   . ASN A 1 464 ? 25.040  4.967   0.544   1.00 67.62  ? 458 ASN A C   1 
ATOM   3337 O O   . ASN A 1 464 ? 25.164  4.190   -0.400  1.00 69.43  ? 458 ASN A O   1 
ATOM   3338 C CB  . ASN A 1 464 ? 26.127  4.501   2.740   1.00 72.35  ? 458 ASN A CB  1 
ATOM   3339 C CG  . ASN A 1 464 ? 26.233  3.002   2.555   1.00 76.23  ? 458 ASN A CG  1 
ATOM   3340 O OD1 . ASN A 1 464 ? 25.299  2.245   2.848   1.00 82.27  ? 458 ASN A OD1 1 
ATOM   3341 N ND2 . ASN A 1 464 ? 27.372  2.538   2.068   1.00 76.01  ? 458 ASN A ND2 1 
ATOM   3342 N N   . GLN A 1 465 ? 23.885  5.572   0.847   1.00 65.70  ? 459 GLN A N   1 
ATOM   3343 C CA  . GLN A 1 465 ? 22.716  5.443   -0.006  1.00 67.32  ? 459 GLN A CA  1 
ATOM   3344 C C   . GLN A 1 465 ? 23.053  5.887   -1.426  1.00 67.34  ? 459 GLN A C   1 
ATOM   3345 O O   . GLN A 1 465 ? 22.676  5.232   -2.395  1.00 72.71  ? 459 GLN A O   1 
ATOM   3346 C CB  . GLN A 1 465 ? 21.548  6.267   0.530   1.00 69.52  ? 459 GLN A CB  1 
ATOM   3347 C CG  . GLN A 1 465 ? 20.966  5.693   1.805   1.00 75.16  ? 459 GLN A CG  1 
ATOM   3348 C CD  . GLN A 1 465 ? 19.933  6.593   2.427   1.00 79.08  ? 459 GLN A CD  1 
ATOM   3349 O OE1 . GLN A 1 465 ? 20.079  7.825   2.455   1.00 79.02  ? 459 GLN A OE1 1 
ATOM   3350 N NE2 . GLN A 1 465 ? 18.858  5.994   2.932   1.00 81.36  ? 459 GLN A NE2 1 
ATOM   3351 N N   . LEU A 1 466 ? 23.781  7.001   -1.518  1.00 63.14  ? 460 LEU A N   1 
ATOM   3352 C CA  . LEU A 1 466 ? 24.230  7.561   -2.778  1.00 61.66  ? 460 LEU A CA  1 
ATOM   3353 C C   . LEU A 1 466 ? 25.108  6.586   -3.564  1.00 61.82  ? 460 LEU A C   1 
ATOM   3354 O O   . LEU A 1 466 ? 24.886  6.348   -4.748  1.00 58.50  ? 460 LEU A O   1 
ATOM   3355 C CB  . LEU A 1 466 ? 24.981  8.830   -2.412  1.00 61.64  ? 460 LEU A CB  1 
ATOM   3356 C CG  . LEU A 1 466 ? 25.420  9.688   -3.516  1.00 61.87  ? 460 LEU A CG  1 
ATOM   3357 C CD1 . LEU A 1 466 ? 24.237  10.090  -4.353  1.00 64.34  ? 460 LEU A CD1 1 
ATOM   3358 C CD2 . LEU A 1 466 ? 26.131  10.894  -2.965  1.00 61.74  ? 460 LEU A CD2 1 
ATOM   3359 N N   . CYS A 1 467 ? 26.095  6.002   -2.880  1.00 63.24  ? 461 CYS A N   1 
ATOM   3360 C CA  . CYS A 1 467 ? 26.992  5.032   -3.486  1.00 63.59  ? 461 CYS A CA  1 
ATOM   3361 C C   . CYS A 1 467 ? 26.300  3.741   -3.923  1.00 67.04  ? 461 CYS A C   1 
ATOM   3362 O O   . CYS A 1 467 ? 26.691  3.140   -4.922  1.00 71.52  ? 461 CYS A O   1 
ATOM   3363 C CB  . CYS A 1 467 ? 28.152  4.750   -2.540  1.00 61.89  ? 461 CYS A CB  1 
ATOM   3364 S SG  . CYS A 1 467 ? 29.308  6.136   -2.394  1.00 61.95  ? 461 CYS A SG  1 
ATOM   3365 N N   . VAL A 1 468 ? 25.282  3.310   -3.172  1.00 66.51  ? 462 VAL A N   1 
ATOM   3366 C CA  . VAL A 1 468 ? 24.464  2.179   -3.577  1.00 66.37  ? 462 VAL A CA  1 
ATOM   3367 C C   . VAL A 1 468 ? 23.736  2.469   -4.887  1.00 67.83  ? 462 VAL A C   1 
ATOM   3368 O O   . VAL A 1 468 ? 23.659  1.598   -5.748  1.00 73.18  ? 462 VAL A O   1 
ATOM   3369 C CB  . VAL A 1 468 ? 23.461  1.779   -2.477  1.00 66.89  ? 462 VAL A CB  1 
ATOM   3370 C CG1 . VAL A 1 468 ? 22.322  0.935   -3.039  1.00 66.76  ? 462 VAL A CG1 1 
ATOM   3371 C CG2 . VAL A 1 468 ? 24.161  1.055   -1.339  1.00 66.20  ? 462 VAL A CG2 1 
ATOM   3372 N N   . LEU A 1 469 ? 23.177  3.676   -5.025  1.00 65.37  ? 463 LEU A N   1 
ATOM   3373 C CA  . LEU A 1 469 ? 22.535  4.073   -6.268  1.00 65.87  ? 463 LEU A CA  1 
ATOM   3374 C C   . LEU A 1 469 ? 23.508  4.085   -7.447  1.00 65.65  ? 463 LEU A C   1 
ATOM   3375 O O   . LEU A 1 469 ? 23.170  3.633   -8.536  1.00 65.50  ? 463 LEU A O   1 
ATOM   3376 C CB  . LEU A 1 469 ? 21.906  5.476   -6.148  1.00 64.76  ? 463 LEU A CB  1 
ATOM   3377 C CG  . LEU A 1 469 ? 20.507  5.554   -5.583  1.00 64.36  ? 463 LEU A CG  1 
ATOM   3378 C CD1 . LEU A 1 469 ? 20.046  6.992   -5.512  1.00 64.13  ? 463 LEU A CD1 1 
ATOM   3379 C CD2 . LEU A 1 469 ? 19.522  4.743   -6.414  1.00 62.48  ? 463 LEU A CD2 1 
ATOM   3380 N N   . HIS A 1 470 ? 24.706  4.635   -7.231  1.00 66.44  ? 464 HIS A N   1 
ATOM   3381 C CA  . HIS A 1 470 ? 25.663  4.818   -8.308  1.00 66.36  ? 464 HIS A CA  1 
ATOM   3382 C C   . HIS A 1 470 ? 26.138  3.488   -8.880  1.00 70.22  ? 464 HIS A C   1 
ATOM   3383 O O   . HIS A 1 470 ? 26.373  3.381   -10.077 1.00 71.68  ? 464 HIS A O   1 
ATOM   3384 C CB  . HIS A 1 470 ? 26.875  5.599   -7.827  1.00 62.36  ? 464 HIS A CB  1 
ATOM   3385 C CG  . HIS A 1 470 ? 27.798  6.020   -8.927  1.00 58.33  ? 464 HIS A CG  1 
ATOM   3386 N ND1 . HIS A 1 470 ? 27.514  7.105   -9.712  1.00 59.55  ? 464 HIS A ND1 1 
ATOM   3387 C CD2 . HIS A 1 470 ? 28.987  5.511   -9.306  1.00 59.04  ? 464 HIS A CD2 1 
ATOM   3388 C CE1 . HIS A 1 470 ? 28.528  7.233   -10.556 1.00 59.18  ? 464 HIS A CE1 1 
ATOM   3389 N NE2 . HIS A 1 470 ? 29.443  6.292   -10.350 1.00 56.40  ? 464 HIS A NE2 1 
ATOM   3390 N N   . GLU A 1 471 ? 26.298  2.489   -8.008  1.00 74.78  ? 465 GLU A N   1 
ATOM   3391 C CA  . GLU A 1 471 ? 26.769  1.179   -8.422  1.00 83.32  ? 465 GLU A CA  1 
ATOM   3392 C C   . GLU A 1 471 ? 25.822  0.516   -9.422  1.00 86.11  ? 465 GLU A C   1 
ATOM   3393 O O   . GLU A 1 471 ? 26.281  -0.076  -10.395 1.00 87.49  ? 465 GLU A O   1 
ATOM   3394 C CB  . GLU A 1 471 ? 26.966  0.284   -7.191  1.00 88.43  ? 465 GLU A CB  1 
ATOM   3395 C CG  . GLU A 1 471 ? 27.609  -1.067  -7.482  1.00 94.27  ? 465 GLU A CG  1 
ATOM   3396 C CD  . GLU A 1 471 ? 26.671  -2.204  -7.856  1.00 97.86  ? 465 GLU A CD  1 
ATOM   3397 O OE1 . GLU A 1 471 ? 25.494  -1.934  -8.191  1.00 97.38  ? 465 GLU A OE1 1 
ATOM   3398 O OE2 . GLU A 1 471 ? 27.115  -3.374  -7.788  1.00 101.36 ? 465 GLU A OE2 1 
ATOM   3399 N N   . LYS A 1 472 ? 24.507  0.628   -9.175  1.00 85.96  ? 466 LYS A N   1 
ATOM   3400 C CA  . LYS A 1 472 ? 23.498  -0.009  -10.009 1.00 85.44  ? 466 LYS A CA  1 
ATOM   3401 C C   . LYS A 1 472 ? 23.138  0.785   -11.266 1.00 82.10  ? 466 LYS A C   1 
ATOM   3402 O O   . LYS A 1 472 ? 22.324  0.324   -12.065 1.00 84.35  ? 466 LYS A O   1 
ATOM   3403 C CB  . LYS A 1 472 ? 22.222  -0.312  -9.177  1.00 88.58  ? 466 LYS A CB  1 
ATOM   3404 C CG  . LYS A 1 472 ? 21.452  0.908   -8.658  1.00 94.24  ? 466 LYS A CG  1 
ATOM   3405 C CD  . LYS A 1 472 ? 20.313  1.389   -9.580  1.00 97.50  ? 466 LYS A CD  1 
ATOM   3406 C CE  . LYS A 1 472 ? 19.753  2.728   -9.144  1.00 99.79  ? 466 LYS A CE  1 
ATOM   3407 N NZ  . LYS A 1 472 ? 18.787  3.289   -10.132 1.00 102.74 ? 466 LYS A NZ  1 
ATOM   3408 N N   . THR A 1 473 ? 23.730  1.974   -11.440 1.00 77.09  ? 467 THR A N   1 
ATOM   3409 C CA  . THR A 1 473 ? 23.601  2.715   -12.687 1.00 75.86  ? 467 THR A CA  1 
ATOM   3410 C C   . THR A 1 473 ? 24.683  3.786   -12.822 1.00 72.59  ? 467 THR A C   1 
ATOM   3411 O O   . THR A 1 473 ? 24.393  4.977   -12.861 1.00 73.33  ? 467 THR A O   1 
ATOM   3412 C CB  . THR A 1 473 ? 22.184  3.300   -12.827 1.00 76.35  ? 467 THR A CB  1 
ATOM   3413 O OG1 . THR A 1 473 ? 22.201  4.303   -13.851 1.00 77.04  ? 467 THR A OG1 1 
ATOM   3414 C CG2 . THR A 1 473 ? 21.670  3.903   -11.552 1.00 77.12  ? 467 THR A CG2 1 
ATOM   3415 N N   . PRO A 1 474 ? 25.970  3.394   -12.934 1.00 68.51  ? 468 PRO A N   1 
ATOM   3416 C CA  . PRO A 1 474 ? 27.066  4.359   -12.917 1.00 66.39  ? 468 PRO A CA  1 
ATOM   3417 C C   . PRO A 1 474 ? 26.953  5.418   -14.004 1.00 65.53  ? 468 PRO A C   1 
ATOM   3418 O O   . PRO A 1 474 ? 26.495  5.135   -15.110 1.00 68.75  ? 468 PRO A O   1 
ATOM   3419 C CB  . PRO A 1 474 ? 28.306  3.480   -13.116 1.00 66.86  ? 468 PRO A CB  1 
ATOM   3420 C CG  . PRO A 1 474 ? 27.877  2.104   -12.678 1.00 67.39  ? 468 PRO A CG  1 
ATOM   3421 C CD  . PRO A 1 474 ? 26.435  2.003   -13.052 1.00 67.55  ? 468 PRO A CD  1 
ATOM   3422 N N   . VAL A 1 475 ? 27.369  6.638   -13.656 1.00 62.65  ? 469 VAL A N   1 
ATOM   3423 C CA  . VAL A 1 475 ? 27.418  7.744   -14.598 1.00 60.44  ? 469 VAL A CA  1 
ATOM   3424 C C   . VAL A 1 475 ? 28.706  8.562   -14.510 1.00 57.80  ? 469 VAL A C   1 
ATOM   3425 O O   . VAL A 1 475 ? 29.024  9.285   -15.445 1.00 56.59  ? 469 VAL A O   1 
ATOM   3426 C CB  . VAL A 1 475 ? 26.166  8.626   -14.400 1.00 61.40  ? 469 VAL A CB  1 
ATOM   3427 C CG1 . VAL A 1 475 ? 24.899  7.835   -14.715 1.00 61.05  ? 469 VAL A CG1 1 
ATOM   3428 C CG2 . VAL A 1 475 ? 26.102  9.208   -12.988 1.00 61.90  ? 469 VAL A CG2 1 
ATOM   3429 N N   . SER A 1 476 ? 29.471  8.403   -13.420 1.00 59.02  ? 470 SER A N   1 
ATOM   3430 C CA  . SER A 1 476 ? 30.672  9.191   -13.166 1.00 59.71  ? 470 SER A CA  1 
ATOM   3431 C C   . SER A 1 476 ? 31.786  8.316   -12.606 1.00 61.26  ? 470 SER A C   1 
ATOM   3432 O O   . SER A 1 476 ? 31.579  7.605   -11.628 1.00 67.18  ? 470 SER A O   1 
ATOM   3433 C CB  . SER A 1 476 ? 30.395  10.323  -12.174 1.00 59.68  ? 470 SER A CB  1 
ATOM   3434 O OG  . SER A 1 476 ? 31.586  10.865  -11.606 1.00 57.54  ? 470 SER A OG  1 
ATOM   3435 N N   . ASP A 1 477 ? 32.972  8.404   -13.213 1.00 63.09  ? 471 ASP A N   1 
ATOM   3436 C CA  . ASP A 1 477 ? 34.138  7.688   -12.720 1.00 62.04  ? 471 ASP A CA  1 
ATOM   3437 C C   . ASP A 1 477 ? 34.623  8.240   -11.384 1.00 59.67  ? 471 ASP A C   1 
ATOM   3438 O O   . ASP A 1 477 ? 35.045  7.475   -10.518 1.00 60.36  ? 471 ASP A O   1 
ATOM   3439 C CB  . ASP A 1 477 ? 35.294  7.758   -13.726 1.00 64.10  ? 471 ASP A CB  1 
ATOM   3440 C CG  . ASP A 1 477 ? 35.005  7.118   -15.060 1.00 67.39  ? 471 ASP A CG  1 
ATOM   3441 O OD1 . ASP A 1 477 ? 34.553  5.941   -15.072 1.00 68.05  ? 471 ASP A OD1 1 
ATOM   3442 O OD2 . ASP A 1 477 ? 35.229  7.786   -16.095 1.00 72.41  ? 471 ASP A OD2 1 
ATOM   3443 N N   . ARG A 1 478 ? 34.594  9.574   -11.243 1.00 55.39  ? 472 ARG A N   1 
ATOM   3444 C CA  . ARG A 1 478 ? 34.995  10.216  -10.001 1.00 53.24  ? 472 ARG A CA  1 
ATOM   3445 C C   . ARG A 1 478 ? 34.146  9.702   -8.838  1.00 52.31  ? 472 ARG A C   1 
ATOM   3446 O O   . ARG A 1 478 ? 34.675  9.350   -7.786  1.00 51.75  ? 472 ARG A O   1 
ATOM   3447 C CB  . ARG A 1 478 ? 34.908  11.733  -10.126 1.00 51.55  ? 472 ARG A CB  1 
ATOM   3448 C CG  . ARG A 1 478 ? 35.833  12.298  -11.190 1.00 49.81  ? 472 ARG A CG  1 
ATOM   3449 C CD  . ARG A 1 478 ? 35.582  13.774  -11.443 1.00 49.95  ? 472 ARG A CD  1 
ATOM   3450 N NE  . ARG A 1 478 ? 34.249  14.002  -11.991 1.00 51.02  ? 472 ARG A NE  1 
ATOM   3451 C CZ  . ARG A 1 478 ? 33.597  15.163  -11.958 1.00 49.11  ? 472 ARG A CZ  1 
ATOM   3452 N NH1 . ARG A 1 478 ? 33.931  16.127  -11.121 1.00 48.96  ? 472 ARG A NH1 1 
ATOM   3453 N NH2 . ARG A 1 478 ? 32.553  15.340  -12.757 1.00 49.88  ? 472 ARG A NH2 1 
ATOM   3454 N N   . VAL A 1 479 ? 32.833  9.596   -9.054  1.00 51.23  ? 473 VAL A N   1 
ATOM   3455 C CA  . VAL A 1 479 ? 31.949  9.062   -8.032  1.00 54.09  ? 473 VAL A CA  1 
ATOM   3456 C C   . VAL A 1 479 ? 32.195  7.585   -7.707  1.00 58.25  ? 473 VAL A C   1 
ATOM   3457 O O   . VAL A 1 479 ? 32.188  7.214   -6.535  1.00 59.91  ? 473 VAL A O   1 
ATOM   3458 C CB  . VAL A 1 479 ? 30.478  9.318   -8.407  1.00 52.58  ? 473 VAL A CB  1 
ATOM   3459 C CG1 . VAL A 1 479 ? 29.539  8.579   -7.471  1.00 52.50  ? 473 VAL A CG1 1 
ATOM   3460 C CG2 . VAL A 1 479 ? 30.173  10.812  -8.416  1.00 52.40  ? 473 VAL A CG2 1 
ATOM   3461 N N   . THR A 1 480 ? 32.396  6.730   -8.722  1.00 61.35  ? 474 THR A N   1 
ATOM   3462 C CA  . THR A 1 480 ? 32.736  5.341   -8.441  1.00 64.53  ? 474 THR A CA  1 
ATOM   3463 C C   . THR A 1 480 ? 33.993  5.290   -7.576  1.00 64.09  ? 474 THR A C   1 
ATOM   3464 O O   . THR A 1 480 ? 34.082  4.481   -6.654  1.00 66.21  ? 474 THR A O   1 
ATOM   3465 C CB  . THR A 1 480 ? 32.998  4.442   -9.685  1.00 66.90  ? 474 THR A CB  1 
ATOM   3466 O OG1 . THR A 1 480 ? 34.045  5.024   -10.449 1.00 72.80  ? 474 THR A OG1 1 
ATOM   3467 C CG2 . THR A 1 480 ? 31.780  4.223   -10.543 1.00 64.01  ? 474 THR A CG2 1 
ATOM   3468 N N   . LYS A 1 481 ? 34.945  6.177   -7.833  1.00 61.02  ? 475 LYS A N   1 
ATOM   3469 C CA  . LYS A 1 481 ? 36.216  6.118   -7.075  1.00 63.02  ? 475 LYS A CA  1 
ATOM   3470 C C   . LYS A 1 481 ? 35.983  6.549   -5.628  1.00 62.98  ? 475 LYS A C   1 
ATOM   3471 O O   . LYS A 1 481 ? 36.511  5.890   -4.730  1.00 63.32  ? 475 LYS A O   1 
ATOM   3472 C CB  . LYS A 1 481 ? 37.312  7.002   -7.664  1.00 67.21  ? 475 LYS A CB  1 
ATOM   3473 C CG  . LYS A 1 481 ? 38.593  7.051   -6.854  1.00 70.90  ? 475 LYS A CG  1 
ATOM   3474 C CD  . LYS A 1 481 ? 39.574  8.099   -7.359  1.00 75.44  ? 475 LYS A CD  1 
ATOM   3475 C CE  . LYS A 1 481 ? 40.833  8.108   -6.558  1.00 80.17  ? 475 LYS A CE  1 
ATOM   3476 N NZ  . LYS A 1 481 ? 40.932  9.302   -5.716  1.00 85.33  ? 475 LYS A NZ  1 
ATOM   3477 N N   . CYS A 1 482 ? 35.243  7.631   -5.424  1.00 63.51  ? 476 CYS A N   1 
ATOM   3478 C CA  . CYS A 1 482 ? 35.005  8.157   -4.055  1.00 62.60  ? 476 CYS A CA  1 
ATOM   3479 C C   . CYS A 1 482 ? 34.236  7.062   -3.303  1.00 61.92  ? 476 CYS A C   1 
ATOM   3480 O O   . CYS A 1 482 ? 34.517  6.861   -2.120  1.00 57.96  ? 476 CYS A O   1 
ATOM   3481 C CB  . CYS A 1 482 ? 34.456  9.587   -4.123  1.00 61.61  ? 476 CYS A CB  1 
ATOM   3482 S SG  . CYS A 1 482 ? 35.632  10.800  -4.793  1.00 59.92  ? 476 CYS A SG  1 
ATOM   3483 N N   . CYS A 1 483 ? 33.291  6.408   -3.965  1.00 63.06  ? 477 CYS A N   1 
ATOM   3484 C CA  . CYS A 1 483 ? 32.553  5.262   -3.362  1.00 66.40  ? 477 CYS A CA  1 
ATOM   3485 C C   . CYS A 1 483 ? 33.501  4.073   -3.048  1.00 64.94  ? 477 CYS A C   1 
ATOM   3486 O O   . CYS A 1 483 ? 33.250  3.408   -2.044  1.00 64.74  ? 477 CYS A O   1 
ATOM   3487 C CB  . CYS A 1 483 ? 31.360  4.959   -4.265  1.00 67.10  ? 477 CYS A CB  1 
ATOM   3488 S SG  . CYS A 1 483 ? 30.084  6.241   -4.259  1.00 66.70  ? 477 CYS A SG  1 
ATOM   3489 N N   . THR A 1 484 ? 34.464  3.744   -3.910  1.00 65.61  ? 478 THR A N   1 
ATOM   3490 C CA  . THR A 1 484 ? 35.495  2.664   -3.768  1.00 67.84  ? 478 THR A CA  1 
ATOM   3491 C C   . THR A 1 484 ? 36.451  2.879   -2.616  1.00 69.09  ? 478 THR A C   1 
ATOM   3492 O O   . THR A 1 484 ? 36.870  1.873   -2.024  1.00 68.41  ? 478 THR A O   1 
ATOM   3493 C CB  . THR A 1 484 ? 36.238  2.419   -5.081  1.00 69.23  ? 478 THR A CB  1 
ATOM   3494 O OG1 . THR A 1 484 ? 36.796  3.657   -5.496  1.00 67.93  ? 478 THR A OG1 1 
ATOM   3495 C CG2 . THR A 1 484 ? 35.329  1.834   -6.146  1.00 65.92  ? 478 THR A CG2 1 
ATOM   3496 N N   . GLU A 1 485 ? 36.852  4.107   -2.336  1.00 69.95  ? 479 GLU A N   1 
ATOM   3497 C CA  . GLU A 1 485 ? 37.949  4.466   -1.405  1.00 69.63  ? 479 GLU A CA  1 
ATOM   3498 C C   . GLU A 1 485 ? 37.631  4.197   0.060   1.00 66.11  ? 479 GLU A C   1 
ATOM   3499 O O   . GLU A 1 485 ? 36.461  3.985   0.386   1.00 62.73  ? 479 GLU A O   1 
ATOM   3500 C CB  . GLU A 1 485 ? 38.320  5.946   -1.481  1.00 73.23  ? 479 GLU A CB  1 
ATOM   3501 C CG  . GLU A 1 485 ? 39.732  6.205   -2.001  1.00 78.15  ? 479 GLU A CG  1 
ATOM   3502 C CD  . GLU A 1 485 ? 40.873  5.640   -1.173  1.00 87.35  ? 479 GLU A CD  1 
ATOM   3503 O OE1 . GLU A 1 485 ? 40.817  5.735   0.070   1.00 89.14  ? 479 GLU A OE1 1 
ATOM   3504 O OE2 . GLU A 1 485 ? 41.829  5.104   -1.772  1.00 95.05  ? 479 GLU A OE2 1 
ATOM   3505 N N   . SER A 1 486 ? 38.660  4.147   0.887   1.00 67.47  ? 480 SER A N   1 
ATOM   3506 C CA  . SER A 1 486 ? 38.579  3.760   2.309   1.00 69.31  ? 480 SER A CA  1 
ATOM   3507 C C   . SER A 1 486 ? 37.726  4.740   3.091   1.00 69.33  ? 480 SER A C   1 
ATOM   3508 O O   . SER A 1 486 ? 37.629  5.895   2.676   1.00 71.70  ? 480 SER A O   1 
ATOM   3509 C CB  . SER A 1 486 ? 39.943  3.825   2.892   1.00 69.22  ? 480 SER A CB  1 
ATOM   3510 O OG  . SER A 1 486 ? 40.468  5.140   2.796   1.00 76.99  ? 480 SER A OG  1 
ATOM   3511 N N   . LEU A 1 487 ? 37.107  4.283   4.167   1.00 69.00  ? 481 LEU A N   1 
ATOM   3512 C CA  . LEU A 1 487 ? 36.079  5.074   4.861   1.00 67.88  ? 481 LEU A CA  1 
ATOM   3513 C C   . LEU A 1 487 ? 36.660  6.378   5.362   1.00 64.81  ? 481 LEU A C   1 
ATOM   3514 O O   . LEU A 1 487 ? 35.942  7.378   5.335   1.00 68.86  ? 481 LEU A O   1 
ATOM   3515 C CB  . LEU A 1 487 ? 35.844  4.142   6.036   1.00 71.19  ? 481 LEU A CB  1 
ATOM   3516 C CG  . LEU A 1 487 ? 34.528  4.307   6.796   1.00 74.46  ? 481 LEU A CG  1 
ATOM   3517 C CD1 . LEU A 1 487 ? 33.401  3.666   6.008   1.00 76.13  ? 481 LEU A CD1 1 
ATOM   3518 C CD2 . LEU A 1 487 ? 34.679  3.641   8.149   1.00 75.95  ? 481 LEU A CD2 1 
ATOM   3519 N N   . VAL A 1 488 ? 37.867  6.364   5.865   1.00 62.20  ? 482 VAL A N   1 
ATOM   3520 C CA  . VAL A 1 488 ? 38.470  7.661   6.248   1.00 62.55  ? 482 VAL A CA  1 
ATOM   3521 C C   . VAL A 1 488 ? 38.547  8.591   5.034   1.00 64.47  ? 482 VAL A C   1 
ATOM   3522 O O   . VAL A 1 488 ? 38.689  9.790   5.262   1.00 67.01  ? 482 VAL A O   1 
ATOM   3523 C CB  . VAL A 1 488 ? 39.865  7.413   6.839   1.00 63.43  ? 482 VAL A CB  1 
ATOM   3524 C CG1 . VAL A 1 488 ? 39.789  6.712   8.186   1.00 64.94  ? 482 VAL A CG1 1 
ATOM   3525 C CG2 . VAL A 1 488 ? 40.762  6.653   5.873   1.00 61.78  ? 482 VAL A CG2 1 
ATOM   3526 N N   . ASN A 1 489 ? 38.453  8.086   3.801   1.00 65.09  ? 483 ASN A N   1 
ATOM   3527 C CA  . ASN A 1 489 ? 38.664  8.956   2.654   1.00 65.32  ? 483 ASN A CA  1 
ATOM   3528 C C   . ASN A 1 489 ? 37.422  9.229   1.805   1.00 59.57  ? 483 ASN A C   1 
ATOM   3529 O O   . ASN A 1 489 ? 37.468  10.106  0.951   1.00 60.57  ? 483 ASN A O   1 
ATOM   3530 C CB  . ASN A 1 489 ? 39.780  8.380   1.766   1.00 68.03  ? 483 ASN A CB  1 
ATOM   3531 C CG  . ASN A 1 489 ? 41.160  8.508   2.382   1.00 71.27  ? 483 ASN A CG  1 
ATOM   3532 O OD1 . ASN A 1 489 ? 41.374  9.255   3.349   1.00 75.16  ? 483 ASN A OD1 1 
ATOM   3533 N ND2 . ASN A 1 489 ? 42.137  7.796   1.824   1.00 71.89  ? 483 ASN A ND2 1 
ATOM   3534 N N   . ARG A 1 490 ? 36.328  8.497   2.050   1.00 53.62  ? 484 ARG A N   1 
ATOM   3535 C CA  . ARG A 1 490 ? 35.091  8.683   1.308   1.00 55.35  ? 484 ARG A CA  1 
ATOM   3536 C C   . ARG A 1 490 ? 34.658  10.152  1.240   1.00 53.53  ? 484 ARG A C   1 
ATOM   3537 O O   . ARG A 1 490 ? 34.589  10.728  0.155   1.00 53.46  ? 484 ARG A O   1 
ATOM   3538 C CB  . ARG A 1 490 ? 33.970  7.817   1.928   1.00 57.75  ? 484 ARG A CB  1 
ATOM   3539 C CG  . ARG A 1 490 ? 32.665  7.814   1.137   1.00 61.56  ? 484 ARG A CG  1 
ATOM   3540 C CD  . ARG A 1 490 ? 31.533  7.150   1.903   1.00 64.94  ? 484 ARG A CD  1 
ATOM   3541 N NE  . ARG A 1 490 ? 31.502  5.703   1.717   1.00 69.28  ? 484 ARG A NE  1 
ATOM   3542 C CZ  . ARG A 1 490 ? 30.986  5.097   0.657   1.00 71.99  ? 484 ARG A CZ  1 
ATOM   3543 N NH1 . ARG A 1 490 ? 30.308  5.768   -0.254  1.00 78.07  ? 484 ARG A NH1 1 
ATOM   3544 N NH2 . ARG A 1 490 ? 31.149  3.785   0.508   1.00 71.18  ? 484 ARG A NH2 1 
ATOM   3545 N N   . ARG A 1 491 ? 34.392  10.760  2.405   1.00 49.41  ? 485 ARG A N   1 
ATOM   3546 C CA  . ARG A 1 491 ? 33.892  12.121  2.477   1.00 46.28  ? 485 ARG A CA  1 
ATOM   3547 C C   . ARG A 1 491 ? 34.933  13.091  1.926   1.00 46.20  ? 485 ARG A C   1 
ATOM   3548 O O   . ARG A 1 491 ? 34.586  13.964  1.135   1.00 48.07  ? 485 ARG A O   1 
ATOM   3549 C CB  . ARG A 1 491 ? 33.468  12.466  3.930   1.00 45.01  ? 485 ARG A CB  1 
ATOM   3550 C CG  . ARG A 1 491 ? 32.651  13.765  4.152   1.00 43.77  ? 485 ARG A CG  1 
ATOM   3551 C CD  . ARG A 1 491 ? 33.465  15.042  4.096   1.00 42.90  ? 485 ARG A CD  1 
ATOM   3552 N NE  . ARG A 1 491 ? 34.612  15.018  4.998   1.00 43.11  ? 485 ARG A NE  1 
ATOM   3553 C CZ  . ARG A 1 491 ? 35.647  15.851  4.936   1.00 44.74  ? 485 ARG A CZ  1 
ATOM   3554 N NH1 . ARG A 1 491 ? 35.800  16.694  3.927   1.00 45.58  ? 485 ARG A NH1 1 
ATOM   3555 N NH2 . ARG A 1 491 ? 36.570  15.815  5.894   1.00 44.73  ? 485 ARG A NH2 1 
ATOM   3556 N N   . PRO A 1 492 ? 36.231  12.998  2.303   1.00 46.03  ? 486 PRO A N   1 
ATOM   3557 C CA  . PRO A 1 492 ? 37.243  13.898  1.744   1.00 45.59  ? 486 PRO A CA  1 
ATOM   3558 C C   . PRO A 1 492 ? 37.332  13.847  0.218   1.00 46.76  ? 486 PRO A C   1 
ATOM   3559 O O   . PRO A 1 492 ? 37.547  14.879  -0.414  1.00 47.97  ? 486 PRO A O   1 
ATOM   3560 C CB  . PRO A 1 492 ? 38.555  13.445  2.431   1.00 44.03  ? 486 PRO A CB  1 
ATOM   3561 C CG  . PRO A 1 492 ? 38.133  12.763  3.654   1.00 43.83  ? 486 PRO A CG  1 
ATOM   3562 C CD  . PRO A 1 492 ? 36.789  12.105  3.333   1.00 45.58  ? 486 PRO A CD  1 
ATOM   3563 N N   . CYS A 1 493 ? 37.161  12.650  -0.362  1.00 48.18  ? 487 CYS A N   1 
ATOM   3564 C CA  . CYS A 1 493 ? 37.156  12.462  -1.807  1.00 50.03  ? 487 CYS A CA  1 
ATOM   3565 C C   . CYS A 1 493 ? 35.972  13.181  -2.450  1.00 47.26  ? 487 CYS A C   1 
ATOM   3566 O O   . CYS A 1 493 ? 36.151  13.955  -3.388  1.00 48.07  ? 487 CYS A O   1 
ATOM   3567 C CB  . CYS A 1 493 ? 37.157  10.971  -2.163  1.00 55.86  ? 487 CYS A CB  1 
ATOM   3568 S SG  . CYS A 1 493 ? 37.507  10.609  -3.916  1.00 61.90  ? 487 CYS A SG  1 
ATOM   3569 N N   . PHE A 1 494 ? 34.768  12.950  -1.917  1.00 44.21  ? 488 PHE A N   1 
ATOM   3570 C CA  . PHE A 1 494 ? 33.602  13.742  -2.292  1.00 43.83  ? 488 PHE A CA  1 
ATOM   3571 C C   . PHE A 1 494 ? 33.811  15.248  -2.137  1.00 43.77  ? 488 PHE A C   1 
ATOM   3572 O O   . PHE A 1 494 ? 33.447  16.014  -3.029  1.00 43.16  ? 488 PHE A O   1 
ATOM   3573 C CB  . PHE A 1 494 ? 32.385  13.324  -1.487  1.00 42.64  ? 488 PHE A CB  1 
ATOM   3574 C CG  . PHE A 1 494 ? 31.685  12.120  -2.045  1.00 43.58  ? 488 PHE A CG  1 
ATOM   3575 C CD1 . PHE A 1 494 ? 30.964  12.205  -3.219  1.00 44.51  ? 488 PHE A CD1 1 
ATOM   3576 C CD2 . PHE A 1 494 ? 31.758  10.897  -1.404  1.00 44.77  ? 488 PHE A CD2 1 
ATOM   3577 C CE1 . PHE A 1 494 ? 30.292  11.092  -3.723  1.00 46.83  ? 488 PHE A CE1 1 
ATOM   3578 C CE2 . PHE A 1 494 ? 31.090  9.785   -1.908  1.00 47.20  ? 488 PHE A CE2 1 
ATOM   3579 C CZ  . PHE A 1 494 ? 30.363  9.886   -3.066  1.00 47.36  ? 488 PHE A CZ  1 
ATOM   3580 N N   . SER A 1 495 ? 34.419  15.663  -1.017  1.00 42.13  ? 489 SER A N   1 
ATOM   3581 C CA  . SER A 1 495 ? 34.793  17.053  -0.841  1.00 42.89  ? 489 SER A CA  1 
ATOM   3582 C C   . SER A 1 495 ? 35.773  17.535  -1.913  1.00 44.22  ? 489 SER A C   1 
ATOM   3583 O O   . SER A 1 495 ? 35.872  18.725  -2.158  1.00 45.46  ? 489 SER A O   1 
ATOM   3584 C CB  . SER A 1 495 ? 35.408  17.291  0.542   1.00 43.26  ? 489 SER A CB  1 
ATOM   3585 O OG  . SER A 1 495 ? 34.489  17.180  1.616   1.00 42.26  ? 489 SER A OG  1 
ATOM   3586 N N   . ALA A 1 496 ? 36.512  16.621  -2.549  1.00 44.29  ? 490 ALA A N   1 
ATOM   3587 C CA  . ALA A 1 496 ? 37.537  17.015  -3.500  1.00 44.97  ? 490 ALA A CA  1 
ATOM   3588 C C   . ALA A 1 496 ? 37.038  17.178  -4.936  1.00 45.58  ? 490 ALA A C   1 
ATOM   3589 O O   . ALA A 1 496 ? 37.797  17.608  -5.796  1.00 45.14  ? 490 ALA A O   1 
ATOM   3590 C CB  . ALA A 1 496 ? 38.675  16.010  -3.467  1.00 44.91  ? 490 ALA A CB  1 
ATOM   3591 N N   . LEU A 1 497 ? 35.768  16.843  -5.186  1.00 45.91  ? 491 LEU A N   1 
ATOM   3592 C CA  . LEU A 1 497 ? 35.172  16.989  -6.502  1.00 44.70  ? 491 LEU A CA  1 
ATOM   3593 C C   . LEU A 1 497 ? 35.171  18.448  -6.962  1.00 46.54  ? 491 LEU A C   1 
ATOM   3594 O O   . LEU A 1 497 ? 34.818  19.340  -6.197  1.00 43.10  ? 491 LEU A O   1 
ATOM   3595 C CB  . LEU A 1 497 ? 33.729  16.469  -6.462  1.00 45.17  ? 491 LEU A CB  1 
ATOM   3596 C CG  . LEU A 1 497 ? 33.539  14.981  -6.152  1.00 46.32  ? 491 LEU A CG  1 
ATOM   3597 C CD1 . LEU A 1 497 ? 32.086  14.622  -6.113  1.00 45.56  ? 491 LEU A CD1 1 
ATOM   3598 C CD2 . LEU A 1 497 ? 34.240  14.102  -7.169  1.00 47.14  ? 491 LEU A CD2 1 
ATOM   3599 N N   . GLU A 1 498 ? 35.533  18.654  -8.235  1.00 49.73  ? 492 GLU A N   1 
ATOM   3600 C CA  . GLU A 1 498 ? 35.532  19.950  -8.894  1.00 51.82  ? 492 GLU A CA  1 
ATOM   3601 C C   . GLU A 1 498 ? 34.380  20.067  -9.895  1.00 49.95  ? 492 GLU A C   1 
ATOM   3602 O O   . GLU A 1 498 ? 33.771  19.058  -10.232 1.00 48.20  ? 492 GLU A O   1 
ATOM   3603 C CB  . GLU A 1 498 ? 36.838  20.083  -9.647  1.00 56.11  ? 492 GLU A CB  1 
ATOM   3604 C CG  . GLU A 1 498 ? 38.082  19.760  -8.839  1.00 60.62  ? 492 GLU A CG  1 
ATOM   3605 C CD  . GLU A 1 498 ? 38.932  20.946  -8.438  1.00 67.35  ? 492 GLU A CD  1 
ATOM   3606 O OE1 . GLU A 1 498 ? 38.473  22.105  -8.576  1.00 74.80  ? 492 GLU A OE1 1 
ATOM   3607 O OE2 . GLU A 1 498 ? 40.083  20.709  -8.010  1.00 70.93  ? 492 GLU A OE2 1 
ATOM   3608 N N   . VAL A 1 499 ? 34.096  21.286  -10.390 1.00 48.87  ? 493 VAL A N   1 
ATOM   3609 C CA  . VAL A 1 499 ? 33.137  21.446  -11.471 1.00 49.75  ? 493 VAL A CA  1 
ATOM   3610 C C   . VAL A 1 499 ? 33.642  20.708  -12.705 1.00 52.41  ? 493 VAL A C   1 
ATOM   3611 O O   . VAL A 1 499 ? 34.844  20.635  -12.961 1.00 52.06  ? 493 VAL A O   1 
ATOM   3612 C CB  . VAL A 1 499 ? 32.796  22.884  -11.911 1.00 49.23  ? 493 VAL A CB  1 
ATOM   3613 C CG1 . VAL A 1 499 ? 32.378  23.747  -10.733 1.00 49.47  ? 493 VAL A CG1 1 
ATOM   3614 C CG2 . VAL A 1 499 ? 33.939  23.500  -12.673 1.00 49.28  ? 493 VAL A CG2 1 
ATOM   3615 N N   . ASP A 1 500 ? 32.688  20.182  -13.472 1.00 54.39  ? 494 ASP A N   1 
ATOM   3616 C CA  . ASP A 1 500 ? 32.987  19.484  -14.701 1.00 56.46  ? 494 ASP A CA  1 
ATOM   3617 C C   . ASP A 1 500 ? 32.978  20.498  -15.838 1.00 56.72  ? 494 ASP A C   1 
ATOM   3618 O O   . ASP A 1 500 ? 31.918  20.897  -16.299 1.00 56.84  ? 494 ASP A O   1 
ATOM   3619 C CB  . ASP A 1 500 ? 31.975  18.385  -14.936 1.00 57.82  ? 494 ASP A CB  1 
ATOM   3620 C CG  . ASP A 1 500 ? 32.200  17.711  -16.255 1.00 62.36  ? 494 ASP A CG  1 
ATOM   3621 O OD1 . ASP A 1 500 ? 32.946  18.276  -17.084 1.00 64.86  ? 494 ASP A OD1 1 
ATOM   3622 O OD2 . ASP A 1 500 ? 31.665  16.593  -16.451 1.00 66.66  ? 494 ASP A OD2 1 
ATOM   3623 N N   . GLU A 1 501 ? 34.175  20.881  -16.292 1.00 59.70  ? 495 GLU A N   1 
ATOM   3624 C CA  . GLU A 1 501 ? 34.332  21.898  -17.318 1.00 59.63  ? 495 GLU A CA  1 
ATOM   3625 C C   . GLU A 1 501 ? 34.097  21.360  -18.731 1.00 56.39  ? 495 GLU A C   1 
ATOM   3626 O O   . GLU A 1 501 ? 33.899  22.141  -19.659 1.00 54.25  ? 495 GLU A O   1 
ATOM   3627 C CB  . GLU A 1 501 ? 35.733  22.526  -17.238 1.00 63.09  ? 495 GLU A CB  1 
ATOM   3628 C CG  . GLU A 1 501 ? 36.101  23.148  -15.900 1.00 64.29  ? 495 GLU A CG  1 
ATOM   3629 C CD  . GLU A 1 501 ? 35.501  24.513  -15.611 1.00 68.26  ? 495 GLU A CD  1 
ATOM   3630 O OE1 . GLU A 1 501 ? 34.602  24.952  -16.363 1.00 74.96  ? 495 GLU A OE1 1 
ATOM   3631 O OE2 . GLU A 1 501 ? 35.938  25.150  -14.625 1.00 67.89  ? 495 GLU A OE2 1 
ATOM   3632 N N   . THR A 1 502 ? 34.093  20.034  -18.896 1.00 54.50  ? 496 THR A N   1 
ATOM   3633 C CA  . THR A 1 502 ? 33.803  19.444  -20.196 1.00 56.56  ? 496 THR A CA  1 
ATOM   3634 C C   . THR A 1 502 ? 32.320  19.452  -20.591 1.00 55.70  ? 496 THR A C   1 
ATOM   3635 O O   . THR A 1 502 ? 31.990  19.417  -21.778 1.00 54.16  ? 496 THR A O   1 
ATOM   3636 C CB  . THR A 1 502 ? 34.298  17.984  -20.269 1.00 57.53  ? 496 THR A CB  1 
ATOM   3637 O OG1 . THR A 1 502 ? 33.376  17.146  -19.575 1.00 58.32  ? 496 THR A OG1 1 
ATOM   3638 C CG2 . THR A 1 502 ? 35.697  17.800  -19.705 1.00 59.09  ? 496 THR A CG2 1 
ATOM   3639 N N   . TYR A 1 503 ? 31.430  19.451  -19.591 1.00 54.50  ? 497 TYR A N   1 
ATOM   3640 C CA  . TYR A 1 503 ? 30.003  19.241  -19.800 1.00 50.37  ? 497 TYR A CA  1 
ATOM   3641 C C   . TYR A 1 503 ? 29.456  20.234  -20.815 1.00 48.43  ? 497 TYR A C   1 
ATOM   3642 O O   . TYR A 1 503 ? 29.718  21.429  -20.700 1.00 51.65  ? 497 TYR A O   1 
ATOM   3643 C CB  . TYR A 1 503 ? 29.268  19.407  -18.466 1.00 47.53  ? 497 TYR A CB  1 
ATOM   3644 C CG  . TYR A 1 503 ? 27.769  19.301  -18.549 1.00 44.64  ? 497 TYR A CG  1 
ATOM   3645 C CD1 . TYR A 1 503 ? 27.147  18.071  -18.713 1.00 42.66  ? 497 TYR A CD1 1 
ATOM   3646 C CD2 . TYR A 1 503 ? 26.969  20.429  -18.462 1.00 43.11  ? 497 TYR A CD2 1 
ATOM   3647 C CE1 . TYR A 1 503 ? 25.771  17.966  -18.780 1.00 40.70  ? 497 TYR A CE1 1 
ATOM   3648 C CE2 . TYR A 1 503 ? 25.587  20.336  -18.533 1.00 41.46  ? 497 TYR A CE2 1 
ATOM   3649 C CZ  . TYR A 1 503 ? 24.992  19.103  -18.684 1.00 42.02  ? 497 TYR A CZ  1 
ATOM   3650 O OH  . TYR A 1 503 ? 23.619  19.012  -18.766 1.00 45.28  ? 497 TYR A OH  1 
ATOM   3651 N N   . VAL A 1 504 ? 28.714  19.744  -21.810 1.00 45.14  ? 498 VAL A N   1 
ATOM   3652 C CA  . VAL A 1 504 ? 28.124  20.648  -22.790 1.00 44.12  ? 498 VAL A CA  1 
ATOM   3653 C C   . VAL A 1 504 ? 26.713  20.988  -22.316 1.00 41.18  ? 498 VAL A C   1 
ATOM   3654 O O   . VAL A 1 504 ? 25.963  20.105  -21.904 1.00 39.36  ? 498 VAL A O   1 
ATOM   3655 C CB  . VAL A 1 504 ? 28.141  20.060  -24.247 1.00 45.89  ? 498 VAL A CB  1 
ATOM   3656 C CG1 . VAL A 1 504 ? 27.570  21.059  -25.264 1.00 45.05  ? 498 VAL A CG1 1 
ATOM   3657 C CG2 . VAL A 1 504 ? 29.555  19.627  -24.656 1.00 44.78  ? 498 VAL A CG2 1 
ATOM   3658 N N   . PRO A 1 505 ? 26.302  22.268  -22.366 1.00 41.09  ? 499 PRO A N   1 
ATOM   3659 C CA  . PRO A 1 505 ? 24.952  22.658  -21.955 1.00 42.89  ? 499 PRO A CA  1 
ATOM   3660 C C   . PRO A 1 505 ? 23.830  21.871  -22.620 1.00 46.14  ? 499 PRO A C   1 
ATOM   3661 O O   . PRO A 1 505 ? 23.881  21.628  -23.826 1.00 47.63  ? 499 PRO A O   1 
ATOM   3662 C CB  . PRO A 1 505 ? 24.846  24.132  -22.391 1.00 42.90  ? 499 PRO A CB  1 
ATOM   3663 C CG  . PRO A 1 505 ? 26.286  24.631  -22.439 1.00 43.75  ? 499 PRO A CG  1 
ATOM   3664 C CD  . PRO A 1 505 ? 27.121  23.404  -22.816 1.00 43.10  ? 499 PRO A CD  1 
ATOM   3665 N N   . LYS A 1 506 ? 22.825  21.489  -21.818 1.00 47.67  ? 500 LYS A N   1 
ATOM   3666 C CA  . LYS A 1 506 ? 21.534  21.052  -22.329 1.00 48.78  ? 500 LYS A CA  1 
ATOM   3667 C C   . LYS A 1 506 ? 20.835  22.133  -23.150 1.00 50.73  ? 500 LYS A C   1 
ATOM   3668 O O   . LYS A 1 506 ? 20.749  23.288  -22.723 1.00 50.29  ? 500 LYS A O   1 
ATOM   3669 C CB  . LYS A 1 506 ? 20.571  20.687  -21.197 1.00 49.18  ? 500 LYS A CB  1 
ATOM   3670 C CG  . LYS A 1 506 ? 20.447  19.226  -20.884 1.00 49.09  ? 500 LYS A CG  1 
ATOM   3671 C CD  . LYS A 1 506 ? 19.073  18.920  -20.440 1.00 50.05  ? 500 LYS A CD  1 
ATOM   3672 C CE  . LYS A 1 506 ? 18.958  17.572  -19.828 1.00 53.68  ? 500 LYS A CE  1 
ATOM   3673 N NZ  . LYS A 1 506 ? 17.558  17.343  -19.399 1.00 57.00  ? 500 LYS A NZ  1 
ATOM   3674 N N   . GLU A 1 507 ? 20.291  21.724  -24.303 1.00 50.86  ? 501 GLU A N   1 
ATOM   3675 C CA  . GLU A 1 507 ? 19.491  22.609  -25.129 1.00 52.57  ? 501 GLU A CA  1 
ATOM   3676 C C   . GLU A 1 507 ? 18.281  23.116  -24.345 1.00 54.44  ? 501 GLU A C   1 
ATOM   3677 O O   . GLU A 1 507 ? 17.669  22.361  -23.586 1.00 52.81  ? 501 GLU A O   1 
ATOM   3678 C CB  . GLU A 1 507 ? 19.043  21.858  -26.386 1.00 53.38  ? 501 GLU A CB  1 
ATOM   3679 C CG  . GLU A 1 507 ? 18.016  22.594  -27.213 1.00 53.37  ? 501 GLU A CG  1 
ATOM   3680 C CD  . GLU A 1 507 ? 17.509  21.825  -28.412 1.00 56.24  ? 501 GLU A CD  1 
ATOM   3681 O OE1 . GLU A 1 507 ? 17.119  20.645  -28.253 1.00 56.01  ? 501 GLU A OE1 1 
ATOM   3682 O OE2 . GLU A 1 507 ? 17.454  22.427  -29.509 1.00 62.59  ? 501 GLU A OE2 1 
ATOM   3683 N N   . PHE A 1 508 ? 17.938  24.394  -24.549 1.00 56.84  ? 502 PHE A N   1 
ATOM   3684 C CA  . PHE A 1 508 ? 16.725  24.961  -23.986 1.00 62.55  ? 502 PHE A CA  1 
ATOM   3685 C C   . PHE A 1 508 ? 15.488  24.116  -24.268 1.00 63.19  ? 502 PHE A C   1 
ATOM   3686 O O   . PHE A 1 508 ? 15.183  23.830  -25.425 1.00 68.54  ? 502 PHE A O   1 
ATOM   3687 C CB  . PHE A 1 508 ? 16.442  26.345  -24.569 1.00 69.96  ? 502 PHE A CB  1 
ATOM   3688 C CG  . PHE A 1 508 ? 15.031  26.800  -24.279 1.00 78.57  ? 502 PHE A CG  1 
ATOM   3689 C CD1 . PHE A 1 508 ? 14.648  27.151  -22.993 1.00 83.78  ? 502 PHE A CD1 1 
ATOM   3690 C CD2 . PHE A 1 508 ? 14.069  26.815  -25.278 1.00 82.57  ? 502 PHE A CD2 1 
ATOM   3691 C CE1 . PHE A 1 508 ? 13.342  27.548  -22.724 1.00 85.67  ? 502 PHE A CE1 1 
ATOM   3692 C CE2 . PHE A 1 508 ? 12.764  27.213  -25.003 1.00 83.82  ? 502 PHE A CE2 1 
ATOM   3693 C CZ  . PHE A 1 508 ? 12.409  27.578  -23.732 1.00 84.11  ? 502 PHE A CZ  1 
ATOM   3694 N N   . ASN A 1 509 ? 14.756  23.755  -23.214 1.00 60.92  ? 503 ASN A N   1 
ATOM   3695 C CA  . ASN A 1 509 ? 13.400  23.272  -23.394 1.00 62.59  ? 503 ASN A CA  1 
ATOM   3696 C C   . ASN A 1 509 ? 12.417  24.103  -22.570 1.00 65.45  ? 503 ASN A C   1 
ATOM   3697 O O   . ASN A 1 509 ? 12.677  24.416  -21.409 1.00 68.07  ? 503 ASN A O   1 
ATOM   3698 C CB  . ASN A 1 509 ? 13.289  21.807  -23.081 1.00 60.80  ? 503 ASN A CB  1 
ATOM   3699 C CG  . ASN A 1 509 ? 11.902  21.325  -23.356 1.00 62.40  ? 503 ASN A CG  1 
ATOM   3700 O OD1 . ASN A 1 509 ? 11.011  22.120  -23.659 1.00 65.00  ? 503 ASN A OD1 1 
ATOM   3701 N ND2 . ASN A 1 509 ? 11.668  20.038  -23.269 1.00 64.86  ? 503 ASN A ND2 1 
ATOM   3702 N N   . ALA A 1 510 ? 11.273  24.423  -23.191 1.00 64.93  ? 504 ALA A N   1 
ATOM   3703 C CA  . ALA A 1 510 ? 10.311  25.372  -22.652 1.00 65.40  ? 504 ALA A CA  1 
ATOM   3704 C C   . ALA A 1 510 ? 9.466   24.779  -21.534 1.00 64.94  ? 504 ALA A C   1 
ATOM   3705 O O   . ALA A 1 510 ? 9.204   25.444  -20.538 1.00 62.29  ? 504 ALA A O   1 
ATOM   3706 C CB  . ALA A 1 510 ? 9.391   25.866  -23.752 1.00 64.40  ? 504 ALA A CB  1 
ATOM   3707 N N   . GLU A 1 511 ? 9.022   23.539  -21.733 1.00 67.06  ? 505 GLU A N   1 
ATOM   3708 C CA  . GLU A 1 511 ? 8.144   22.890  -20.778 1.00 70.80  ? 505 GLU A CA  1 
ATOM   3709 C C   . GLU A 1 511 ? 8.759   22.881  -19.378 1.00 68.73  ? 505 GLU A C   1 
ATOM   3710 O O   . GLU A 1 511 ? 8.094   23.271  -18.419 1.00 73.15  ? 505 GLU A O   1 
ATOM   3711 C CB  . GLU A 1 511 ? 7.797   21.472  -21.249 1.00 72.75  ? 505 GLU A CB  1 
ATOM   3712 C CG  . GLU A 1 511 ? 6.925   20.710  -20.268 1.00 75.59  ? 505 GLU A CG  1 
ATOM   3713 C CD  . GLU A 1 511 ? 5.646   21.403  -19.834 1.00 78.29  ? 505 GLU A CD  1 
ATOM   3714 O OE1 . GLU A 1 511 ? 5.131   22.270  -20.581 1.00 80.45  ? 505 GLU A OE1 1 
ATOM   3715 O OE2 . GLU A 1 511 ? 5.172   21.084  -18.719 1.00 79.66  ? 505 GLU A OE2 1 
ATOM   3716 N N   . THR A 1 512 ? 10.036  22.483  -19.282 1.00 64.80  ? 506 THR A N   1 
ATOM   3717 C CA  . THR A 1 512 ? 10.707  22.303  -18.001 1.00 62.91  ? 506 THR A CA  1 
ATOM   3718 C C   . THR A 1 512 ? 10.724  23.569  -17.141 1.00 57.48  ? 506 THR A C   1 
ATOM   3719 O O   . THR A 1 512 ? 10.708  23.463  -15.921 1.00 58.99  ? 506 THR A O   1 
ATOM   3720 C CB  . THR A 1 512 ? 12.158  21.722  -18.164 1.00 64.57  ? 506 THR A CB  1 
ATOM   3721 O OG1 . THR A 1 512 ? 13.057  22.754  -18.589 1.00 66.95  ? 506 THR A OG1 1 
ATOM   3722 C CG2 . THR A 1 512 ? 12.222  20.516  -19.132 1.00 63.23  ? 506 THR A CG2 1 
ATOM   3723 N N   . PHE A 1 513 ? 10.717  24.756  -17.760 1.00 51.89  ? 507 PHE A N   1 
ATOM   3724 C CA  . PHE A 1 513 ? 10.632  25.997  -17.005 1.00 52.53  ? 507 PHE A CA  1 
ATOM   3725 C C   . PHE A 1 513 ? 9.252   26.667  -17.010 1.00 53.04  ? 507 PHE A C   1 
ATOM   3726 O O   . PHE A 1 513 ? 9.130   27.858  -16.729 1.00 50.79  ? 507 PHE A O   1 
ATOM   3727 C CB  . PHE A 1 513 ? 11.710  26.934  -17.531 1.00 55.50  ? 507 PHE A CB  1 
ATOM   3728 C CG  . PHE A 1 513 ? 13.039  26.233  -17.538 1.00 60.21  ? 507 PHE A CG  1 
ATOM   3729 C CD1 . PHE A 1 513 ? 13.664  25.886  -16.347 1.00 59.41  ? 507 PHE A CD1 1 
ATOM   3730 C CD2 . PHE A 1 513 ? 13.633  25.850  -18.732 1.00 62.66  ? 507 PHE A CD2 1 
ATOM   3731 C CE1 . PHE A 1 513 ? 14.875  25.212  -16.352 1.00 59.66  ? 507 PHE A CE1 1 
ATOM   3732 C CE2 . PHE A 1 513 ? 14.857  25.177  -18.735 1.00 61.98  ? 507 PHE A CE2 1 
ATOM   3733 C CZ  . PHE A 1 513 ? 15.463  24.857  -17.548 1.00 61.98  ? 507 PHE A CZ  1 
ATOM   3734 N N   . THR A 1 514 ? 8.199   25.896  -17.306 1.00 53.48  ? 508 THR A N   1 
ATOM   3735 C CA  . THR A 1 514 ? 6.844   26.396  -17.183 1.00 55.98  ? 508 THR A CA  1 
ATOM   3736 C C   . THR A 1 514 ? 6.113   25.675  -16.056 1.00 55.52  ? 508 THR A C   1 
ATOM   3737 O O   . THR A 1 514 ? 6.113   24.449  -16.006 1.00 52.76  ? 508 THR A O   1 
ATOM   3738 C CB  . THR A 1 514 ? 6.042   26.216  -18.465 1.00 57.46  ? 508 THR A CB  1 
ATOM   3739 O OG1 . THR A 1 514 ? 5.926   24.821  -18.698 1.00 59.78  ? 508 THR A OG1 1 
ATOM   3740 C CG2 . THR A 1 514 ? 6.660   26.921  -19.665 1.00 57.49  ? 508 THR A CG2 1 
ATOM   3741 N N   . PHE A 1 515 ? 5.461   26.457  -15.190 1.00 56.38  ? 509 PHE A N   1 
ATOM   3742 C CA  . PHE A 1 515 ? 4.625   25.920  -14.131 1.00 59.59  ? 509 PHE A CA  1 
ATOM   3743 C C   . PHE A 1 515 ? 3.149   25.937  -14.533 1.00 65.32  ? 509 PHE A C   1 
ATOM   3744 O O   . PHE A 1 515 ? 2.757   26.722  -15.392 1.00 70.40  ? 509 PHE A O   1 
ATOM   3745 C CB  . PHE A 1 515 ? 4.884   26.734  -12.874 1.00 56.82  ? 509 PHE A CB  1 
ATOM   3746 C CG  . PHE A 1 515 ? 6.345   26.741  -12.498 1.00 54.37  ? 509 PHE A CG  1 
ATOM   3747 C CD1 . PHE A 1 515 ? 6.922   25.652  -11.872 1.00 52.65  ? 509 PHE A CD1 1 
ATOM   3748 C CD2 . PHE A 1 515 ? 7.146   27.823  -12.797 1.00 53.93  ? 509 PHE A CD2 1 
ATOM   3749 C CE1 . PHE A 1 515 ? 8.268   25.663  -11.527 1.00 52.76  ? 509 PHE A CE1 1 
ATOM   3750 C CE2 . PHE A 1 515 ? 8.493   27.824  -12.462 1.00 54.79  ? 509 PHE A CE2 1 
ATOM   3751 C CZ  . PHE A 1 515 ? 9.049   26.741  -11.838 1.00 53.05  ? 509 PHE A CZ  1 
ATOM   3752 N N   . HIS A 1 516 ? 2.350   25.047  -13.922 1.00 65.67  ? 510 HIS A N   1 
ATOM   3753 C CA  . HIS A 1 516 ? 0.919   24.937  -14.179 1.00 62.03  ? 510 HIS A CA  1 
ATOM   3754 C C   . HIS A 1 516 ? 0.123   25.232  -12.906 1.00 61.71  ? 510 HIS A C   1 
ATOM   3755 O O   . HIS A 1 516 ? 0.668   25.185  -11.808 1.00 61.61  ? 510 HIS A O   1 
ATOM   3756 C CB  . HIS A 1 516 ? 0.572   23.531  -14.692 1.00 62.41  ? 510 HIS A CB  1 
ATOM   3757 C CG  . HIS A 1 516 ? 1.322   23.108  -15.920 1.00 66.93  ? 510 HIS A CG  1 
ATOM   3758 N ND1 . HIS A 1 516 ? 2.343   22.164  -15.856 1.00 70.68  ? 510 HIS A ND1 1 
ATOM   3759 C CD2 . HIS A 1 516 ? 1.199   23.516  -17.203 1.00 66.87  ? 510 HIS A CD2 1 
ATOM   3760 C CE1 . HIS A 1 516 ? 2.795   22.022  -17.094 1.00 67.57  ? 510 HIS A CE1 1 
ATOM   3761 N NE2 . HIS A 1 516 ? 2.133   22.812  -17.940 1.00 66.92  ? 510 HIS A NE2 1 
ATOM   3762 N N   . ALA A 1 517 ? -1.178  25.515  -13.056 1.00 58.61  ? 511 ALA A N   1 
ATOM   3763 C CA  . ALA A 1 517 ? -2.018  25.903  -11.933 1.00 56.31  ? 511 ALA A CA  1 
ATOM   3764 C C   . ALA A 1 517 ? -2.191  24.799  -10.895 1.00 53.44  ? 511 ALA A C   1 
ATOM   3765 O O   . ALA A 1 517 ? -2.433  25.079  -9.724  1.00 53.70  ? 511 ALA A O   1 
ATOM   3766 C CB  . ALA A 1 517 ? -3.375  26.327  -12.431 1.00 58.39  ? 511 ALA A CB  1 
ATOM   3767 N N   . ASP A 1 518 ? -2.055  23.546  -11.328 1.00 52.61  ? 512 ASP A N   1 
ATOM   3768 C CA  . ASP A 1 518 ? -2.184  22.405  -10.440 1.00 54.90  ? 512 ASP A CA  1 
ATOM   3769 C C   . ASP A 1 518 ? -1.175  22.442  -9.290  1.00 54.50  ? 512 ASP A C   1 
ATOM   3770 O O   . ASP A 1 518 ? -1.414  21.850  -8.241  1.00 52.33  ? 512 ASP A O   1 
ATOM   3771 C CB  . ASP A 1 518 ? -2.058  21.113  -11.262 1.00 59.62  ? 512 ASP A CB  1 
ATOM   3772 C CG  . ASP A 1 518 ? -1.801  19.866  -10.443 1.00 68.92  ? 512 ASP A CG  1 
ATOM   3773 O OD1 . ASP A 1 518 ? -0.596  19.549  -10.201 1.00 73.73  ? 512 ASP A OD1 1 
ATOM   3774 O OD2 . ASP A 1 518 ? -2.801  19.211  -10.014 1.00 72.91  ? 512 ASP A OD2 1 
ATOM   3775 N N   . ILE A 1 519 ? -0.046  23.139  -9.498  1.00 53.23  ? 513 ILE A N   1 
ATOM   3776 C CA  . ILE A 1 519 ? 1.007   23.235  -8.503  1.00 48.90  ? 513 ILE A CA  1 
ATOM   3777 C C   . ILE A 1 519 ? 0.471   23.846  -7.207  1.00 48.42  ? 513 ILE A C   1 
ATOM   3778 O O   . ILE A 1 519 ? 0.993   23.553  -6.132  1.00 45.27  ? 513 ILE A O   1 
ATOM   3779 C CB  . ILE A 1 519 ? 2.222   24.043  -9.044  1.00 47.46  ? 513 ILE A CB  1 
ATOM   3780 C CG1 . ILE A 1 519 ? 3.521   23.722  -8.245  1.00 46.98  ? 513 ILE A CG1 1 
ATOM   3781 C CG2 . ILE A 1 519 ? 1.927   25.549  -9.091  1.00 47.11  ? 513 ILE A CG2 1 
ATOM   3782 C CD1 . ILE A 1 519 ? 4.639   24.727  -8.401  1.00 47.01  ? 513 ILE A CD1 1 
ATOM   3783 N N   . CYS A 1 520 ? -0.567  24.689  -7.318  1.00 47.02  ? 514 CYS A N   1 
ATOM   3784 C CA  . CYS A 1 520 ? -1.169  25.323  -6.153  1.00 46.72  ? 514 CYS A CA  1 
ATOM   3785 C C   . CYS A 1 520 ? -1.905  24.354  -5.230  1.00 42.64  ? 514 CYS A C   1 
ATOM   3786 O O   . CYS A 1 520 ? -2.117  24.667  -4.066  1.00 42.07  ? 514 CYS A O   1 
ATOM   3787 C CB  . CYS A 1 520 ? -2.072  26.465  -6.583  1.00 50.20  ? 514 CYS A CB  1 
ATOM   3788 S SG  . CYS A 1 520 ? -1.282  27.632  -7.735  1.00 57.61  ? 514 CYS A SG  1 
ATOM   3789 N N   . THR A 1 521 ? -2.230  23.156  -5.723  1.00 42.93  ? 515 THR A N   1 
ATOM   3790 C CA  . THR A 1 521 ? -2.904  22.153  -4.914  1.00 44.21  ? 515 THR A CA  1 
ATOM   3791 C C   . THR A 1 521 ? -1.950  21.318  -4.060  1.00 48.09  ? 515 THR A C   1 
ATOM   3792 O O   . THR A 1 521 ? -2.370  20.707  -3.082  1.00 54.50  ? 515 THR A O   1 
ATOM   3793 C CB  . THR A 1 521 ? -3.768  21.213  -5.794  1.00 43.33  ? 515 THR A CB  1 
ATOM   3794 O OG1 . THR A 1 521 ? -2.974  20.225  -6.451  1.00 41.16  ? 515 THR A OG1 1 
ATOM   3795 C CG2 . THR A 1 521 ? -4.573  21.961  -6.802  1.00 41.95  ? 515 THR A CG2 1 
ATOM   3796 N N   . LEU A 1 522 ? -0.668  21.289  -4.438  1.00 49.89  ? 516 LEU A N   1 
ATOM   3797 C CA  . LEU A 1 522 ? 0.320   20.403  -3.839  1.00 46.37  ? 516 LEU A CA  1 
ATOM   3798 C C   . LEU A 1 522 ? 0.686   20.764  -2.401  1.00 43.76  ? 516 LEU A C   1 
ATOM   3799 O O   . LEU A 1 522 ? 0.561   21.914  -2.007  1.00 43.00  ? 516 LEU A O   1 
ATOM   3800 C CB  . LEU A 1 522 ? 1.593   20.479  -4.687  1.00 45.48  ? 516 LEU A CB  1 
ATOM   3801 C CG  . LEU A 1 522 ? 1.489   19.960  -6.116  1.00 45.11  ? 516 LEU A CG  1 
ATOM   3802 C CD1 . LEU A 1 522 ? 2.840   20.036  -6.806  1.00 44.58  ? 516 LEU A CD1 1 
ATOM   3803 C CD2 . LEU A 1 522 ? 0.952   18.504  -6.161  1.00 42.90  ? 516 LEU A CD2 1 
ATOM   3804 N N   . SER A 1 523 ? 1.166   19.777  -1.635  1.00 43.47  ? 517 SER A N   1 
ATOM   3805 C CA  . SER A 1 523 ? 1.852   20.052  -0.378  1.00 46.64  ? 517 SER A CA  1 
ATOM   3806 C C   . SER A 1 523 ? 3.112   20.897  -0.582  1.00 48.15  ? 517 SER A C   1 
ATOM   3807 O O   . SER A 1 523 ? 3.584   21.070  -1.709  1.00 47.96  ? 517 SER A O   1 
ATOM   3808 C CB  . SER A 1 523 ? 2.258   18.764  0.315   1.00 44.51  ? 517 SER A CB  1 
ATOM   3809 O OG  . SER A 1 523 ? 3.346   18.226  -0.409  1.00 44.48  ? 517 SER A OG  1 
ATOM   3810 N N   . GLU A 1 524 ? 3.655   21.415  0.524   1.00 49.75  ? 518 GLU A N   1 
ATOM   3811 C CA  . GLU A 1 524 ? 4.821   22.283  0.458   1.00 51.25  ? 518 GLU A CA  1 
ATOM   3812 C C   . GLU A 1 524 ? 6.016   21.519  -0.102  1.00 48.45  ? 518 GLU A C   1 
ATOM   3813 O O   . GLU A 1 524 ? 6.761   22.046  -0.922  1.00 47.89  ? 518 GLU A O   1 
ATOM   3814 C CB  . GLU A 1 524 ? 5.167   22.865  1.822   1.00 52.13  ? 518 GLU A CB  1 
ATOM   3815 C CG  . GLU A 1 524 ? 6.132   24.047  1.762   1.00 55.56  ? 518 GLU A CG  1 
ATOM   3816 C CD  . GLU A 1 524 ? 6.468   24.623  3.135   1.00 59.50  ? 518 GLU A CD  1 
ATOM   3817 O OE1 . GLU A 1 524 ? 6.013   24.028  4.140   1.00 62.41  ? 518 GLU A OE1 1 
ATOM   3818 O OE2 . GLU A 1 524 ? 7.174   25.659  3.213   1.00 58.72  ? 518 GLU A OE2 1 
ATOM   3819 N N   . LYS A 1 525 ? 6.166   20.269  0.323   1.00 47.04  ? 519 LYS A N   1 
ATOM   3820 C CA  . LYS A 1 525 ? 7.270   19.437  -0.118  1.00 49.69  ? 519 LYS A CA  1 
ATOM   3821 C C   . LYS A 1 525 ? 7.261   19.312  -1.641  1.00 51.02  ? 519 LYS A C   1 
ATOM   3822 O O   . LYS A 1 525 ? 8.245   19.618  -2.302  1.00 46.65  ? 519 LYS A O   1 
ATOM   3823 C CB  . LYS A 1 525 ? 7.175   18.072  0.559   1.00 50.50  ? 519 LYS A CB  1 
ATOM   3824 C CG  . LYS A 1 525 ? 8.213   17.080  0.100   1.00 53.86  ? 519 LYS A CG  1 
ATOM   3825 C CD  . LYS A 1 525 ? 8.125   15.734  0.811   1.00 54.42  ? 519 LYS A CD  1 
ATOM   3826 C CE  . LYS A 1 525 ? 8.992   14.716  0.111   1.00 57.08  ? 519 LYS A CE  1 
ATOM   3827 N NZ  . LYS A 1 525 ? 8.944   13.390  0.777   1.00 58.89  ? 519 LYS A NZ  1 
ATOM   3828 N N   . GLU A 1 526 ? 6.117   18.895  -2.190  1.00 56.37  ? 520 GLU A N   1 
ATOM   3829 C CA  . GLU A 1 526 ? 5.984   18.639  -3.616  1.00 56.42  ? 520 GLU A CA  1 
ATOM   3830 C C   . GLU A 1 526 ? 6.018   19.878  -4.509  1.00 52.21  ? 520 GLU A C   1 
ATOM   3831 O O   . GLU A 1 526 ? 6.486   19.815  -5.640  1.00 48.86  ? 520 GLU A O   1 
ATOM   3832 C CB  . GLU A 1 526 ? 4.686   17.856  -3.873  1.00 60.26  ? 520 GLU A CB  1 
ATOM   3833 C CG  . GLU A 1 526 ? 4.837   16.364  -3.643  1.00 66.43  ? 520 GLU A CG  1 
ATOM   3834 C CD  . GLU A 1 526 ? 6.194   15.788  -4.035  1.00 77.22  ? 520 GLU A CD  1 
ATOM   3835 O OE1 . GLU A 1 526 ? 6.645   16.008  -5.189  1.00 82.48  ? 520 GLU A OE1 1 
ATOM   3836 O OE2 . GLU A 1 526 ? 6.814   15.121  -3.171  1.00 84.03  ? 520 GLU A OE2 1 
ATOM   3837 N N   . ARG A 1 527 ? 5.477   20.994  -4.016  1.00 53.77  ? 521 ARG A N   1 
ATOM   3838 C CA  . ARG A 1 527 ? 5.608   22.275  -4.692  1.00 50.80  ? 521 ARG A CA  1 
ATOM   3839 C C   . ARG A 1 527 ? 7.097   22.623  -4.754  1.00 47.50  ? 521 ARG A C   1 
ATOM   3840 O O   . ARG A 1 527 ? 7.617   22.926  -5.827  1.00 47.74  ? 521 ARG A O   1 
ATOM   3841 C CB  . ARG A 1 527 ? 4.797   23.363  -3.949  1.00 50.25  ? 521 ARG A CB  1 
ATOM   3842 C CG  . ARG A 1 527 ? 4.945   24.785  -4.501  1.00 52.39  ? 521 ARG A CG  1 
ATOM   3843 C CD  . ARG A 1 527 ? 4.826   25.842  -3.409  1.00 54.53  ? 521 ARG A CD  1 
ATOM   3844 N NE  . ARG A 1 527 ? 3.512   25.784  -2.783  1.00 58.46  ? 521 ARG A NE  1 
ATOM   3845 C CZ  . ARG A 1 527 ? 3.280   25.478  -1.512  1.00 55.87  ? 521 ARG A CZ  1 
ATOM   3846 N NH1 . ARG A 1 527 ? 3.927   26.077  -0.522  1.00 53.96  ? 521 ARG A NH1 1 
ATOM   3847 N NH2 . ARG A 1 527 ? 2.324   24.598  -1.231  1.00 55.93  ? 521 ARG A NH2 1 
ATOM   3848 N N   . GLN A 1 528 ? 7.766   22.562  -3.595  1.00 42.66  ? 522 GLN A N   1 
ATOM   3849 C CA  . GLN A 1 528 ? 9.193   22.826  -3.499  1.00 43.27  ? 522 GLN A CA  1 
ATOM   3850 C C   . GLN A 1 528 ? 10.035  22.009  -4.475  1.00 43.26  ? 522 GLN A C   1 
ATOM   3851 O O   . GLN A 1 528 ? 10.889  22.567  -5.164  1.00 42.37  ? 522 GLN A O   1 
ATOM   3852 C CB  . GLN A 1 528 ? 9.700   22.574  -2.074  1.00 42.80  ? 522 GLN A CB  1 
ATOM   3853 C CG  . GLN A 1 528 ? 9.451   23.774  -1.179  1.00 42.84  ? 522 GLN A CG  1 
ATOM   3854 C CD  . GLN A 1 528 ? 9.954   23.554  0.205   1.00 42.54  ? 522 GLN A CD  1 
ATOM   3855 O OE1 . GLN A 1 528 ? 10.366  22.448  0.565   1.00 45.81  ? 522 GLN A OE1 1 
ATOM   3856 N NE2 . GLN A 1 528 ? 9.962   24.610  0.995   1.00 41.19  ? 522 GLN A NE2 1 
ATOM   3857 N N   . ILE A 1 529 ? 9.766   20.701  -4.526  1.00 42.26  ? 523 ILE A N   1 
ATOM   3858 C CA  . ILE A 1 529 ? 10.456  19.802  -5.427  1.00 43.16  ? 523 ILE A CA  1 
ATOM   3859 C C   . ILE A 1 529 ? 10.270  20.234  -6.873  1.00 46.29  ? 523 ILE A C   1 
ATOM   3860 O O   . ILE A 1 529 ? 11.197  20.163  -7.681  1.00 47.54  ? 523 ILE A O   1 
ATOM   3861 C CB  . ILE A 1 529 ? 9.986   18.378  -5.175  1.00 44.31  ? 523 ILE A CB  1 
ATOM   3862 C CG1 . ILE A 1 529 ? 10.720  17.810  -3.939  1.00 44.66  ? 523 ILE A CG1 1 
ATOM   3863 C CG2 . ILE A 1 529 ? 10.207  17.493  -6.407  1.00 45.50  ? 523 ILE A CG2 1 
ATOM   3864 C CD1 . ILE A 1 529 ? 10.096  16.665  -3.325  1.00 45.66  ? 523 ILE A CD1 1 
ATOM   3865 N N   . LYS A 1 530 ? 9.063   20.708  -7.174  1.00 49.05  ? 524 LYS A N   1 
ATOM   3866 C CA  . LYS A 1 530 ? 8.736   21.186  -8.503  1.00 49.15  ? 524 LYS A CA  1 
ATOM   3867 C C   . LYS A 1 530 ? 9.722   22.264  -8.931  1.00 46.44  ? 524 LYS A C   1 
ATOM   3868 O O   . LYS A 1 530 ? 10.320  22.170  -9.998  1.00 48.28  ? 524 LYS A O   1 
ATOM   3869 C CB  . LYS A 1 530 ? 7.317   21.749  -8.535  1.00 52.09  ? 524 LYS A CB  1 
ATOM   3870 C CG  . LYS A 1 530 ? 6.511   21.260  -9.692  1.00 53.10  ? 524 LYS A CG  1 
ATOM   3871 C CD  . LYS A 1 530 ? 6.066   19.837  -9.467  1.00 53.63  ? 524 LYS A CD  1 
ATOM   3872 C CE  . LYS A 1 530 ? 5.168   19.367  -10.560 1.00 57.02  ? 524 LYS A CE  1 
ATOM   3873 N NZ  . LYS A 1 530 ? 5.445   17.945  -10.879 1.00 60.35  ? 524 LYS A NZ  1 
ATOM   3874 N N   . LYS A 1 531 ? 9.887   23.287  -8.094  1.00 42.93  ? 525 LYS A N   1 
ATOM   3875 C CA  . LYS A 1 531 ? 10.831  24.351  -8.405  1.00 43.53  ? 525 LYS A CA  1 
ATOM   3876 C C   . LYS A 1 531 ? 12.292  23.879  -8.348  1.00 42.50  ? 525 LYS A C   1 
ATOM   3877 O O   . LYS A 1 531 ? 13.145  24.370  -9.086  1.00 41.27  ? 525 LYS A O   1 
ATOM   3878 C CB  . LYS A 1 531 ? 10.611  25.553  -7.462  1.00 41.24  ? 525 LYS A CB  1 
ATOM   3879 C CG  . LYS A 1 531 ? 9.289   26.257  -7.679  1.00 42.05  ? 525 LYS A CG  1 
ATOM   3880 C CD  . LYS A 1 531 ? 8.982   27.360  -6.574  1.00 44.41  ? 525 LYS A CD  1 
ATOM   3881 C CE  . LYS A 1 531 ? 8.497   26.768  -5.246  1.00 44.72  ? 525 LYS A CE  1 
ATOM   3882 N NZ  . LYS A 1 531 ? 8.710   27.717  -4.118  1.00 45.63  ? 525 LYS A NZ  1 
ATOM   3883 N N   . GLN A 1 532 ? 12.591  22.918  -7.473  1.00 39.64  ? 526 GLN A N   1 
ATOM   3884 C CA  . GLN A 1 532 ? 13.959  22.445  -7.362  1.00 41.03  ? 526 GLN A CA  1 
ATOM   3885 C C   . GLN A 1 532 ? 14.353  21.602  -8.577  1.00 42.58  ? 526 GLN A C   1 
ATOM   3886 O O   . GLN A 1 532 ? 15.530  21.511  -8.923  1.00 40.26  ? 526 GLN A O   1 
ATOM   3887 C CB  . GLN A 1 532 ? 14.146  21.700  -6.048  1.00 39.46  ? 526 GLN A CB  1 
ATOM   3888 C CG  . GLN A 1 532 ? 14.318  22.702  -4.885  1.00 39.50  ? 526 GLN A CG  1 
ATOM   3889 C CD  . GLN A 1 532 ? 14.226  22.062  -3.529  1.00 39.25  ? 526 GLN A CD  1 
ATOM   3890 O OE1 . GLN A 1 532 ? 13.747  20.944  -3.344  1.00 38.93  ? 526 GLN A OE1 1 
ATOM   3891 N NE2 . GLN A 1 532 ? 14.675  22.767  -2.539  1.00 41.64  ? 526 GLN A NE2 1 
ATOM   3892 N N   . THR A 1 533 ? 13.351  21.003  -9.227  1.00 42.72  ? 527 THR A N   1 
ATOM   3893 C CA  . THR A 1 533 ? 13.568  20.311  -10.479 1.00 42.51  ? 527 THR A CA  1 
ATOM   3894 C C   . THR A 1 533 ? 13.909  21.299  -11.582 1.00 42.91  ? 527 THR A C   1 
ATOM   3895 O O   . THR A 1 533 ? 14.720  21.006  -12.451 1.00 46.31  ? 527 THR A O   1 
ATOM   3896 C CB  . THR A 1 533 ? 12.356  19.526  -10.843 1.00 41.22  ? 527 THR A CB  1 
ATOM   3897 O OG1 . THR A 1 533 ? 12.095  18.641  -9.754  1.00 44.08  ? 527 THR A OG1 1 
ATOM   3898 C CG2 . THR A 1 533 ? 12.544  18.756  -12.104 1.00 39.97  ? 527 THR A CG2 1 
ATOM   3899 N N   . ALA A 1 534 ? 13.284  22.471  -11.533 1.00 41.44  ? 528 ALA A N   1 
ATOM   3900 C CA  . ALA A 1 534 ? 13.493  23.457  -12.568 1.00 41.91  ? 528 ALA A CA  1 
ATOM   3901 C C   . ALA A 1 534 ? 14.920  23.978  -12.424 1.00 44.18  ? 528 ALA A C   1 
ATOM   3902 O O   . ALA A 1 534 ? 15.645  24.135  -13.405 1.00 50.31  ? 528 ALA A O   1 
ATOM   3903 C CB  . ALA A 1 534 ? 12.465  24.565  -12.468 1.00 40.96  ? 528 ALA A CB  1 
ATOM   3904 N N   . LEU A 1 535 ? 15.327  24.217  -11.183 1.00 44.23  ? 529 LEU A N   1 
ATOM   3905 C CA  . LEU A 1 535 ? 16.623  24.810  -10.913 1.00 44.51  ? 529 LEU A CA  1 
ATOM   3906 C C   . LEU A 1 535 ? 17.743  23.909  -11.424 1.00 42.81  ? 529 LEU A C   1 
ATOM   3907 O O   . LEU A 1 535 ? 18.663  24.392  -12.082 1.00 42.49  ? 529 LEU A O   1 
ATOM   3908 C CB  . LEU A 1 535 ? 16.754  25.071  -9.418  1.00 45.26  ? 529 LEU A CB  1 
ATOM   3909 C CG  . LEU A 1 535 ? 18.125  25.461  -8.915  1.00 46.07  ? 529 LEU A CG  1 
ATOM   3910 C CD1 . LEU A 1 535 ? 18.604  26.723  -9.579  1.00 45.18  ? 529 LEU A CD1 1 
ATOM   3911 C CD2 . LEU A 1 535 ? 18.101  25.588  -7.379  1.00 45.42  ? 529 LEU A CD2 1 
ATOM   3912 N N   . VAL A 1 536 ? 17.658  22.607  -11.123 1.00 41.40  ? 530 VAL A N   1 
ATOM   3913 C CA  . VAL A 1 536 ? 18.670  21.658  -11.560 1.00 42.70  ? 530 VAL A CA  1 
ATOM   3914 C C   . VAL A 1 536 ? 18.764  21.685  -13.089 1.00 43.52  ? 530 VAL A C   1 
ATOM   3915 O O   . VAL A 1 536 ? 19.858  21.647  -13.658 1.00 42.78  ? 530 VAL A O   1 
ATOM   3916 C CB  . VAL A 1 536 ? 18.411  20.217  -11.033 1.00 43.54  ? 530 VAL A CB  1 
ATOM   3917 C CG1 . VAL A 1 536 ? 19.368  19.210  -11.663 1.00 44.73  ? 530 VAL A CG1 1 
ATOM   3918 C CG2 . VAL A 1 536 ? 18.511  20.133  -9.517  1.00 43.42  ? 530 VAL A CG2 1 
ATOM   3919 N N   . GLU A 1 537 ? 17.598  21.771  -13.741 1.00 44.49  ? 531 GLU A N   1 
ATOM   3920 C CA  . GLU A 1 537 ? 17.506  21.810  -15.192 1.00 43.12  ? 531 GLU A CA  1 
ATOM   3921 C C   . GLU A 1 537 ? 18.048  23.132  -15.723 1.00 41.80  ? 531 GLU A C   1 
ATOM   3922 O O   . GLU A 1 537 ? 18.697  23.172  -16.756 1.00 44.01  ? 531 GLU A O   1 
ATOM   3923 C CB  . GLU A 1 537 ? 16.058  21.576  -15.616 1.00 44.39  ? 531 GLU A CB  1 
ATOM   3924 C CG  . GLU A 1 537 ? 15.580  20.150  -15.388 1.00 45.83  ? 531 GLU A CG  1 
ATOM   3925 C CD  . GLU A 1 537 ? 16.154  19.095  -16.325 1.00 52.27  ? 531 GLU A CD  1 
ATOM   3926 O OE1 . GLU A 1 537 ? 16.600  19.456  -17.446 1.00 56.15  ? 531 GLU A OE1 1 
ATOM   3927 O OE2 . GLU A 1 537 ? 16.193  17.905  -15.922 1.00 55.44  ? 531 GLU A OE2 1 
ATOM   3928 N N   . LEU A 1 538 ? 17.810  24.216  -14.994 1.00 40.98  ? 532 LEU A N   1 
ATOM   3929 C CA  . LEU A 1 538 ? 18.389  25.497  -15.352 1.00 41.60  ? 532 LEU A CA  1 
ATOM   3930 C C   . LEU A 1 538 ? 19.914  25.424  -15.345 1.00 42.28  ? 532 LEU A C   1 
ATOM   3931 O O   . LEU A 1 538 ? 20.578  26.005  -16.201 1.00 42.71  ? 532 LEU A O   1 
ATOM   3932 C CB  . LEU A 1 538 ? 17.885  26.590  -14.370 1.00 40.92  ? 532 LEU A CB  1 
ATOM   3933 C CG  . LEU A 1 538 ? 18.354  27.997  -14.658 1.00 42.41  ? 532 LEU A CG  1 
ATOM   3934 C CD1 . LEU A 1 538 ? 17.732  28.552  -15.919 1.00 41.91  ? 532 LEU A CD1 1 
ATOM   3935 C CD2 . LEU A 1 538 ? 18.067  28.931  -13.452 1.00 44.88  ? 532 LEU A CD2 1 
ATOM   3936 N N   . VAL A 1 539 ? 20.475  24.722  -14.355 1.00 44.66  ? 533 VAL A N   1 
ATOM   3937 C CA  . VAL A 1 539 ? 21.921  24.679  -14.207 1.00 43.87  ? 533 VAL A CA  1 
ATOM   3938 C C   . VAL A 1 539 ? 22.522  23.850  -15.341 1.00 42.18  ? 533 VAL A C   1 
ATOM   3939 O O   . VAL A 1 539 ? 23.540  24.253  -15.893 1.00 42.64  ? 533 VAL A O   1 
ATOM   3940 C CB  . VAL A 1 539 ? 22.361  24.169  -12.835 1.00 43.25  ? 533 VAL A CB  1 
ATOM   3941 C CG1 . VAL A 1 539 ? 23.877  24.012  -12.778 1.00 43.08  ? 533 VAL A CG1 1 
ATOM   3942 C CG2 . VAL A 1 539 ? 21.868  25.100  -11.725 1.00 45.31  ? 533 VAL A CG2 1 
ATOM   3943 N N   . LYS A 1 540 ? 21.874  22.726  -15.683 1.00 38.94  ? 534 LYS A N   1 
ATOM   3944 C CA  . LYS A 1 540 ? 22.283  21.895  -16.807 1.00 40.32  ? 534 LYS A CA  1 
ATOM   3945 C C   . LYS A 1 540 ? 22.244  22.628  -18.149 1.00 43.49  ? 534 LYS A C   1 
ATOM   3946 O O   . LYS A 1 540 ? 22.915  22.205  -19.087 1.00 44.62  ? 534 LYS A O   1 
ATOM   3947 C CB  . LYS A 1 540 ? 21.421  20.633  -16.910 1.00 38.00  ? 534 LYS A CB  1 
ATOM   3948 C CG  . LYS A 1 540 ? 21.761  19.597  -15.854 1.00 38.12  ? 534 LYS A CG  1 
ATOM   3949 C CD  . LYS A 1 540 ? 20.907  18.386  -15.932 1.00 37.56  ? 534 LYS A CD  1 
ATOM   3950 C CE  . LYS A 1 540 ? 21.141  17.521  -14.759 1.00 37.63  ? 534 LYS A CE  1 
ATOM   3951 N NZ  . LYS A 1 540 ? 20.367  16.261  -14.863 1.00 38.56  ? 534 LYS A NZ  1 
ATOM   3952 N N   . HIS A 1 541 ? 21.465  23.719  -18.209 1.00 43.30  ? 535 HIS A N   1 
ATOM   3953 C CA  . HIS A 1 541 ? 21.294  24.533  -19.400 1.00 44.32  ? 535 HIS A CA  1 
ATOM   3954 C C   . HIS A 1 541 ? 22.156  25.793  -19.387 1.00 45.33  ? 535 HIS A C   1 
ATOM   3955 O O   . HIS A 1 541 ? 22.415  26.377  -20.441 1.00 44.58  ? 535 HIS A O   1 
ATOM   3956 C CB  . HIS A 1 541 ? 19.793  24.912  -19.517 1.00 43.74  ? 535 HIS A CB  1 
ATOM   3957 C CG  . HIS A 1 541 ? 19.466  25.949  -20.548 1.00 42.69  ? 535 HIS A CG  1 
ATOM   3958 N ND1 . HIS A 1 541 ? 19.758  25.758  -21.891 1.00 42.62  ? 535 HIS A ND1 1 
ATOM   3959 C CD2 . HIS A 1 541 ? 18.876  27.154  -20.398 1.00 43.12  ? 535 HIS A CD2 1 
ATOM   3960 C CE1 . HIS A 1 541 ? 19.339  26.850  -22.518 1.00 41.92  ? 535 HIS A CE1 1 
ATOM   3961 N NE2 . HIS A 1 541 ? 18.783  27.714  -21.651 1.00 43.46  ? 535 HIS A NE2 1 
ATOM   3962 N N   . LYS A 1 542 ? 22.558  26.220  -18.178 1.00 46.06  ? 536 LYS A N   1 
ATOM   3963 C CA  . LYS A 1 542 ? 23.462  27.344  -17.992 1.00 44.70  ? 536 LYS A CA  1 
ATOM   3964 C C   . LYS A 1 542 ? 24.543  27.008  -16.967 1.00 44.82  ? 536 LYS A C   1 
ATOM   3965 O O   . LYS A 1 542 ? 24.598  27.608  -15.897 1.00 44.76  ? 536 LYS A O   1 
ATOM   3966 C CB  . LYS A 1 542 ? 22.665  28.550  -17.520 1.00 44.49  ? 536 LYS A CB  1 
ATOM   3967 C CG  . LYS A 1 542 ? 21.662  29.056  -18.512 1.00 45.01  ? 536 LYS A CG  1 
ATOM   3968 C CD  . LYS A 1 542 ? 22.290  29.955  -19.516 1.00 45.24  ? 536 LYS A CD  1 
ATOM   3969 C CE  . LYS A 1 542 ? 21.296  30.494  -20.495 1.00 45.24  ? 536 LYS A CE  1 
ATOM   3970 N NZ  . LYS A 1 542 ? 21.816  31.710  -21.140 1.00 45.33  ? 536 LYS A NZ  1 
ATOM   3971 N N   . PRO A 1 543 ? 25.473  26.075  -17.258 1.00 46.96  ? 537 PRO A N   1 
ATOM   3972 C CA  . PRO A 1 543 ? 26.344  25.529  -16.206 1.00 46.97  ? 537 PRO A CA  1 
ATOM   3973 C C   . PRO A 1 543 ? 27.515  26.424  -15.796 1.00 45.22  ? 537 PRO A C   1 
ATOM   3974 O O   . PRO A 1 543 ? 28.111  26.203  -14.746 1.00 47.01  ? 537 PRO A O   1 
ATOM   3975 C CB  . PRO A 1 543 ? 26.818  24.198  -16.790 1.00 47.38  ? 537 PRO A CB  1 
ATOM   3976 C CG  . PRO A 1 543 ? 26.749  24.414  -18.348 1.00 50.07  ? 537 PRO A CG  1 
ATOM   3977 C CD  . PRO A 1 543 ? 25.767  25.556  -18.605 1.00 48.69  ? 537 PRO A CD  1 
ATOM   3978 N N   . LYS A 1 544 ? 27.822  27.454  -16.590 1.00 44.75  ? 538 LYS A N   1 
ATOM   3979 C CA  . LYS A 1 544 ? 28.849  28.417  -16.223 1.00 45.99  ? 538 LYS A CA  1 
ATOM   3980 C C   . LYS A 1 544 ? 28.285  29.734  -15.694 1.00 45.43  ? 538 LYS A C   1 
ATOM   3981 O O   . LYS A 1 544 ? 29.044  30.666  -15.416 1.00 46.80  ? 538 LYS A O   1 
ATOM   3982 C CB  . LYS A 1 544 ? 29.775  28.706  -17.428 1.00 49.72  ? 538 LYS A CB  1 
ATOM   3983 C CG  . LYS A 1 544 ? 30.193  27.449  -18.179 1.00 53.76  ? 538 LYS A CG  1 
ATOM   3984 C CD  . LYS A 1 544 ? 31.629  27.463  -18.703 1.00 57.53  ? 538 LYS A CD  1 
ATOM   3985 C CE  . LYS A 1 544 ? 32.116  26.030  -18.913 1.00 62.90  ? 538 LYS A CE  1 
ATOM   3986 N NZ  . LYS A 1 544 ? 33.611  25.912  -18.823 1.00 64.61  ? 538 LYS A NZ  1 
ATOM   3987 N N   . ALA A 1 545 ? 26.956  29.835  -15.575 1.00 44.04  ? 539 ALA A N   1 
ATOM   3988 C CA  . ALA A 1 545 ? 26.354  31.026  -14.993 1.00 46.09  ? 539 ALA A CA  1 
ATOM   3989 C C   . ALA A 1 545 ? 26.703  31.144  -13.507 1.00 43.71  ? 539 ALA A C   1 
ATOM   3990 O O   . ALA A 1 545 ? 26.816  30.150  -12.801 1.00 41.39  ? 539 ALA A O   1 
ATOM   3991 C CB  . ALA A 1 545 ? 24.851  31.011  -15.170 1.00 47.78  ? 539 ALA A CB  1 
ATOM   3992 N N   . THR A 1 546 ? 26.873  32.371  -13.027 1.00 43.12  ? 540 THR A N   1 
ATOM   3993 C CA  . THR A 1 546 ? 27.195  32.565  -11.627 1.00 46.36  ? 540 THR A CA  1 
ATOM   3994 C C   . THR A 1 546 ? 26.042  32.107  -10.736 1.00 48.59  ? 540 THR A C   1 
ATOM   3995 O O   . THR A 1 546 ? 24.883  32.082  -11.157 1.00 47.27  ? 540 THR A O   1 
ATOM   3996 C CB  . THR A 1 546 ? 27.538  34.007  -11.360 1.00 46.85  ? 540 THR A CB  1 
ATOM   3997 O OG1 . THR A 1 546 ? 26.378  34.809  -11.646 1.00 45.66  ? 540 THR A OG1 1 
ATOM   3998 C CG2 . THR A 1 546 ? 28.775  34.454  -12.170 1.00 46.94  ? 540 THR A CG2 1 
ATOM   3999 N N   . LYS A 1 547 ? 26.381  31.758  -9.489  1.00 49.36  ? 541 LYS A N   1 
ATOM   4000 C CA  . LYS A 1 547 ? 25.374  31.398  -8.504  1.00 49.06  ? 541 LYS A CA  1 
ATOM   4001 C C   . LYS A 1 547 ? 24.509  32.588  -8.097  1.00 48.81  ? 541 LYS A C   1 
ATOM   4002 O O   . LYS A 1 547 ? 23.394  32.391  -7.616  1.00 49.83  ? 541 LYS A O   1 
ATOM   4003 C CB  . LYS A 1 547 ? 26.011  30.759  -7.284  1.00 49.36  ? 541 LYS A CB  1 
ATOM   4004 C CG  . LYS A 1 547 ? 26.915  31.651  -6.492  1.00 50.35  ? 541 LYS A CG  1 
ATOM   4005 C CD  . LYS A 1 547 ? 27.828  30.793  -5.619  1.00 52.59  ? 541 LYS A CD  1 
ATOM   4006 C CE  . LYS A 1 547 ? 28.933  31.569  -4.989  1.00 56.70  ? 541 LYS A CE  1 
ATOM   4007 N NZ  . LYS A 1 547 ? 29.739  30.674  -4.132  1.00 61.88  ? 541 LYS A NZ  1 
ATOM   4008 N N   . GLU A 1 548 ? 25.012  33.808  -8.333  1.00 48.63  ? 542 GLU A N   1 
ATOM   4009 C CA  . GLU A 1 548 ? 24.212  35.015  -8.225  1.00 48.64  ? 542 GLU A CA  1 
ATOM   4010 C C   . GLU A 1 548 ? 23.085  35.072  -9.257  1.00 48.92  ? 542 GLU A C   1 
ATOM   4011 O O   . GLU A 1 548 ? 21.944  35.366  -8.904  1.00 46.81  ? 542 GLU A O   1 
ATOM   4012 C CB  . GLU A 1 548 ? 25.091  36.271  -8.370  1.00 52.03  ? 542 GLU A CB  1 
ATOM   4013 C CG  . GLU A 1 548 ? 25.988  36.566  -7.170  1.00 54.90  ? 542 GLU A CG  1 
ATOM   4014 C CD  . GLU A 1 548 ? 27.400  35.984  -7.184  1.00 57.11  ? 542 GLU A CD  1 
ATOM   4015 O OE1 . GLU A 1 548 ? 27.648  34.964  -7.868  1.00 56.20  ? 542 GLU A OE1 1 
ATOM   4016 O OE2 . GLU A 1 548 ? 28.276  36.586  -6.519  1.00 62.61  ? 542 GLU A OE2 1 
ATOM   4017 N N   . GLN A 1 549 ? 23.402  34.801  -10.533 1.00 49.30  ? 543 GLN A N   1 
ATOM   4018 C CA  . GLN A 1 549 ? 22.406  34.902  -11.591 1.00 48.66  ? 543 GLN A CA  1 
ATOM   4019 C C   . GLN A 1 549 ? 21.401  33.761  -11.434 1.00 46.61  ? 543 GLN A C   1 
ATOM   4020 O O   . GLN A 1 549 ? 20.198  33.976  -11.570 1.00 43.75  ? 543 GLN A O   1 
ATOM   4021 C CB  . GLN A 1 549 ? 23.038  34.867  -13.001 1.00 49.24  ? 543 GLN A CB  1 
ATOM   4022 C CG  . GLN A 1 549 ? 23.877  36.070  -13.373 1.00 51.97  ? 543 GLN A CG  1 
ATOM   4023 C CD  . GLN A 1 549 ? 24.816  35.786  -14.538 1.00 55.57  ? 543 GLN A CD  1 
ATOM   4024 O OE1 . GLN A 1 549 ? 25.885  35.160  -14.379 1.00 63.86  ? 543 GLN A OE1 1 
ATOM   4025 N NE2 . GLN A 1 549 ? 24.469  36.252  -15.735 1.00 53.53  ? 543 GLN A NE2 1 
ATOM   4026 N N   . LEU A 1 550 ? 21.925  32.560  -11.148 1.00 44.53  ? 544 LEU A N   1 
ATOM   4027 C CA  . LEU A 1 550 ? 21.126  31.368  -10.929 1.00 46.43  ? 544 LEU A CA  1 
ATOM   4028 C C   . LEU A 1 550 ? 20.119  31.485  -9.783  1.00 48.96  ? 544 LEU A C   1 
ATOM   4029 O O   . LEU A 1 550 ? 19.012  30.959  -9.885  1.00 50.97  ? 544 LEU A O   1 
ATOM   4030 C CB  . LEU A 1 550 ? 22.065  30.168  -10.655 1.00 46.41  ? 544 LEU A CB  1 
ATOM   4031 C CG  . LEU A 1 550 ? 22.869  29.673  -11.848 1.00 46.51  ? 544 LEU A CG  1 
ATOM   4032 C CD1 . LEU A 1 550 ? 23.990  28.741  -11.427 1.00 46.52  ? 544 LEU A CD1 1 
ATOM   4033 C CD2 . LEU A 1 550 ? 21.986  28.975  -12.834 1.00 46.99  ? 544 LEU A CD2 1 
ATOM   4034 N N   . LYS A 1 551 ? 20.517  32.145  -8.688  1.00 50.86  ? 545 LYS A N   1 
ATOM   4035 C CA  . LYS A 1 551 ? 19.654  32.344  -7.532  1.00 52.04  ? 545 LYS A CA  1 
ATOM   4036 C C   . LYS A 1 551 ? 18.581  33.414  -7.752  1.00 50.21  ? 545 LYS A C   1 
ATOM   4037 O O   . LYS A 1 551 ? 17.473  33.306  -7.228  1.00 48.98  ? 545 LYS A O   1 
ATOM   4038 C CB  . LYS A 1 551 ? 20.504  32.775  -6.329  1.00 56.29  ? 545 LYS A CB  1 
ATOM   4039 C CG  . LYS A 1 551 ? 19.760  32.686  -5.009  1.00 57.79  ? 545 LYS A CG  1 
ATOM   4040 C CD  . LYS A 1 551 ? 20.283  33.648  -4.011  1.00 59.73  ? 545 LYS A CD  1 
ATOM   4041 C CE  . LYS A 1 551 ? 19.543  33.547  -2.712  1.00 61.78  ? 545 LYS A CE  1 
ATOM   4042 N NZ  . LYS A 1 551 ? 19.377  34.882  -2.120  1.00 66.60  ? 545 LYS A NZ  1 
ATOM   4043 N N   . ALA A 1 552 ? 18.940  34.473  -8.489  1.00 46.45  ? 546 ALA A N   1 
ATOM   4044 C CA  . ALA A 1 552 ? 17.977  35.484  -8.893  1.00 46.71  ? 546 ALA A CA  1 
ATOM   4045 C C   . ALA A 1 552 ? 16.823  34.895  -9.710  1.00 47.19  ? 546 ALA A C   1 
ATOM   4046 O O   . ALA A 1 552 ? 15.676  35.275  -9.520  1.00 50.31  ? 546 ALA A O   1 
ATOM   4047 C CB  . ALA A 1 552 ? 18.664  36.591  -9.676  1.00 45.79  ? 546 ALA A CB  1 
ATOM   4048 N N   . VAL A 1 553 ? 17.122  33.954  -10.607 1.00 46.21  ? 547 VAL A N   1 
ATOM   4049 C CA  . VAL A 1 553 ? 16.083  33.274  -11.355 1.00 45.64  ? 547 VAL A CA  1 
ATOM   4050 C C   . VAL A 1 553 ? 15.254  32.385  -10.418 1.00 45.40  ? 547 VAL A C   1 
ATOM   4051 O O   . VAL A 1 553 ? 14.031  32.410  -10.456 1.00 46.34  ? 547 VAL A O   1 
ATOM   4052 C CB  . VAL A 1 553 ? 16.703  32.501  -12.563 1.00 43.38  ? 547 VAL A CB  1 
ATOM   4053 C CG1 . VAL A 1 553 ? 15.685  31.568  -13.203 1.00 43.60  ? 547 VAL A CG1 1 
ATOM   4054 C CG2 . VAL A 1 553 ? 17.281  33.457  -13.592 1.00 41.81  ? 547 VAL A CG2 1 
ATOM   4055 N N   . MET A 1 554 ? 15.909  31.592  -9.568  1.00 45.74  ? 548 MET A N   1 
ATOM   4056 C CA  . MET A 1 554 ? 15.196  30.662  -8.701  1.00 47.68  ? 548 MET A CA  1 
ATOM   4057 C C   . MET A 1 554 ? 14.215  31.383  -7.776  1.00 48.52  ? 548 MET A C   1 
ATOM   4058 O O   . MET A 1 554 ? 13.145  30.852  -7.469  1.00 44.81  ? 548 MET A O   1 
ATOM   4059 C CB  . MET A 1 554 ? 16.186  29.850  -7.847  1.00 47.55  ? 548 MET A CB  1 
ATOM   4060 C CG  . MET A 1 554 ? 15.535  28.882  -6.823  1.00 47.57  ? 548 MET A CG  1 
ATOM   4061 S SD  . MET A 1 554 ? 14.464  27.663  -7.597  1.00 47.95  ? 548 MET A SD  1 
ATOM   4062 C CE  . MET A 1 554 ? 14.403  26.440  -6.409  1.00 49.50  ? 548 MET A CE  1 
ATOM   4063 N N   . ASP A 1 555 ? 14.601  32.585  -7.324  1.00 48.98  ? 549 ASP A N   1 
ATOM   4064 C CA  . ASP A 1 555 ? 13.722  33.414  -6.517  1.00 50.68  ? 549 ASP A CA  1 
ATOM   4065 C C   . ASP A 1 555 ? 12.560  33.910  -7.388  1.00 52.88  ? 549 ASP A C   1 
ATOM   4066 O O   . ASP A 1 555 ? 11.419  33.987  -6.928  1.00 50.21  ? 549 ASP A O   1 
ATOM   4067 C CB  . ASP A 1 555 ? 14.527  34.564  -5.865  1.00 50.68  ? 549 ASP A CB  1 
ATOM   4068 C CG  . ASP A 1 555 ? 15.581  34.163  -4.813  1.00 55.29  ? 549 ASP A CG  1 
ATOM   4069 O OD1 . ASP A 1 555 ? 15.497  33.030  -4.259  1.00 53.27  ? 549 ASP A OD1 1 
ATOM   4070 O OD2 . ASP A 1 555 ? 16.493  34.969  -4.555  1.00 60.89  ? 549 ASP A OD2 1 
ATOM   4071 N N   . ASP A 1 556 ? 12.851  34.218  -8.662  1.00 52.55  ? 550 ASP A N   1 
ATOM   4072 C CA  . ASP A 1 556 ? 11.817  34.548  -9.629  1.00 53.17  ? 550 ASP A CA  1 
ATOM   4073 C C   . ASP A 1 556 ? 10.806  33.409  -9.777  1.00 52.85  ? 550 ASP A C   1 
ATOM   4074 O O   . ASP A 1 556 ? 9.601   33.644  -9.772  1.00 53.22  ? 550 ASP A O   1 
ATOM   4075 C CB  . ASP A 1 556 ? 12.417  34.903  -10.999 1.00 53.53  ? 550 ASP A CB  1 
ATOM   4076 C CG  . ASP A 1 556 ? 13.156  36.214  -11.048 1.00 56.69  ? 550 ASP A CG  1 
ATOM   4077 O OD1 . ASP A 1 556 ? 13.176  36.917  -10.028 1.00 60.57  ? 550 ASP A OD1 1 
ATOM   4078 O OD2 . ASP A 1 556 ? 13.722  36.541  -12.120 1.00 62.47  ? 550 ASP A OD2 1 
ATOM   4079 N N   . PHE A 1 557 ? 11.286  32.169  -9.904  1.00 49.80  ? 551 PHE A N   1 
ATOM   4080 C CA  . PHE A 1 557 ? 10.375  31.039  -9.900  1.00 48.52  ? 551 PHE A CA  1 
ATOM   4081 C C   . PHE A 1 557 ? 9.505   31.103  -8.650  1.00 48.61  ? 551 PHE A C   1 
ATOM   4082 O O   . PHE A 1 557 ? 8.304   30.885  -8.728  1.00 48.44  ? 551 PHE A O   1 
ATOM   4083 C CB  . PHE A 1 557 ? 11.102  29.691  -9.973  1.00 47.22  ? 551 PHE A CB  1 
ATOM   4084 C CG  . PHE A 1 557 ? 11.812  29.395  -11.269 1.00 46.70  ? 551 PHE A CG  1 
ATOM   4085 C CD1 . PHE A 1 557 ? 11.762  30.280  -12.328 1.00 47.18  ? 551 PHE A CD1 1 
ATOM   4086 C CD2 . PHE A 1 557 ? 12.545  28.235  -11.424 1.00 48.03  ? 551 PHE A CD2 1 
ATOM   4087 C CE1 . PHE A 1 557 ? 12.406  29.996  -13.523 1.00 45.92  ? 551 PHE A CE1 1 
ATOM   4088 C CE2 . PHE A 1 557 ? 13.194  27.959  -12.619 1.00 47.10  ? 551 PHE A CE2 1 
ATOM   4089 C CZ  . PHE A 1 557 ? 13.112  28.840  -13.660 1.00 46.61  ? 551 PHE A CZ  1 
ATOM   4090 N N   . ALA A 1 558 ? 10.110  31.424  -7.502  1.00 50.29  ? 552 ALA A N   1 
ATOM   4091 C CA  . ALA A 1 558 ? 9.394   31.430  -6.230  1.00 47.84  ? 552 ALA A CA  1 
ATOM   4092 C C   . ALA A 1 558 ? 8.345   32.543  -6.180  1.00 45.92  ? 552 ALA A C   1 
ATOM   4093 O O   . ALA A 1 558 ? 7.192   32.296  -5.852  1.00 43.88  ? 552 ALA A O   1 
ATOM   4094 C CB  . ALA A 1 558 ? 10.377  31.555  -5.060  1.00 44.69  ? 552 ALA A CB  1 
ATOM   4095 N N   . ALA A 1 559 ? 8.759   33.767  -6.521  1.00 47.20  ? 553 ALA A N   1 
ATOM   4096 C CA  . ALA A 1 559 ? 7.873   34.920  -6.533  1.00 47.99  ? 553 ALA A CA  1 
ATOM   4097 C C   . ALA A 1 559 ? 6.684   34.707  -7.471  1.00 52.43  ? 553 ALA A C   1 
ATOM   4098 O O   . ALA A 1 559 ? 5.567   35.122  -7.175  1.00 57.55  ? 553 ALA A O   1 
ATOM   4099 C CB  . ALA A 1 559 ? 8.653   36.161  -6.947  1.00 44.71  ? 553 ALA A CB  1 
ATOM   4100 N N   . PHE A 1 560 ? 6.949   34.039  -8.599  1.00 53.19  ? 554 PHE A N   1 
ATOM   4101 C CA  . PHE A 1 560 ? 5.952   33.745  -9.606  1.00 52.40  ? 554 PHE A CA  1 
ATOM   4102 C C   . PHE A 1 560 ? 4.866   32.803  -9.101  1.00 52.68  ? 554 PHE A C   1 
ATOM   4103 O O   . PHE A 1 560 ? 3.688   33.097  -9.264  1.00 50.44  ? 554 PHE A O   1 
ATOM   4104 C CB  . PHE A 1 560 ? 6.639   33.137  -10.822 1.00 53.37  ? 554 PHE A CB  1 
ATOM   4105 C CG  . PHE A 1 560 ? 5.692   32.688  -11.904 1.00 56.41  ? 554 PHE A CG  1 
ATOM   4106 C CD1 . PHE A 1 560 ? 4.693   33.527  -12.367 1.00 56.66  ? 554 PHE A CD1 1 
ATOM   4107 C CD2 . PHE A 1 560 ? 5.809   31.431  -12.470 1.00 57.98  ? 554 PHE A CD2 1 
ATOM   4108 C CE1 . PHE A 1 560 ? 3.837   33.117  -13.379 1.00 58.26  ? 554 PHE A CE1 1 
ATOM   4109 C CE2 . PHE A 1 560 ? 4.953   31.029  -13.487 1.00 58.92  ? 554 PHE A CE2 1 
ATOM   4110 C CZ  . PHE A 1 560 ? 3.970   31.870  -13.931 1.00 58.56  ? 554 PHE A CZ  1 
ATOM   4111 N N   . VAL A 1 561 ? 5.278   31.663  -8.530  1.00 54.14  ? 555 VAL A N   1 
ATOM   4112 C CA  . VAL A 1 561 ? 4.354   30.695  -7.960  1.00 54.62  ? 555 VAL A CA  1 
ATOM   4113 C C   . VAL A 1 561 ? 3.591   31.294  -6.777  1.00 58.39  ? 555 VAL A C   1 
ATOM   4114 O O   . VAL A 1 561 ? 2.402   31.039  -6.624  1.00 61.33  ? 555 VAL A O   1 
ATOM   4115 C CB  . VAL A 1 561 ? 5.065   29.380  -7.569  1.00 52.76  ? 555 VAL A CB  1 
ATOM   4116 C CG1 . VAL A 1 561 ? 4.158   28.478  -6.748  1.00 53.44  ? 555 VAL A CG1 1 
ATOM   4117 C CG2 . VAL A 1 561 ? 5.551   28.640  -8.793  1.00 54.75  ? 555 VAL A CG2 1 
ATOM   4118 N N   . GLU A 1 562 ? 4.278   32.093  -5.953  1.00 61.98  ? 556 GLU A N   1 
ATOM   4119 C CA  . GLU A 1 562 ? 3.661   32.788  -4.833  1.00 64.09  ? 556 GLU A CA  1 
ATOM   4120 C C   . GLU A 1 562 ? 2.493   33.670  -5.271  1.00 66.20  ? 556 GLU A C   1 
ATOM   4121 O O   . GLU A 1 562 ? 1.446   33.693  -4.621  1.00 63.16  ? 556 GLU A O   1 
ATOM   4122 C CB  . GLU A 1 562 ? 4.725   33.644  -4.133  1.00 68.06  ? 556 GLU A CB  1 
ATOM   4123 C CG  . GLU A 1 562 ? 4.238   34.527  -3.000  1.00 73.80  ? 556 GLU A CG  1 
ATOM   4124 C CD  . GLU A 1 562 ? 3.477   33.820  -1.890  1.00 82.36  ? 556 GLU A CD  1 
ATOM   4125 O OE1 . GLU A 1 562 ? 3.989   32.804  -1.362  1.00 86.01  ? 556 GLU A OE1 1 
ATOM   4126 O OE2 . GLU A 1 562 ? 2.368   34.292  -1.539  1.00 88.21  ? 556 GLU A OE2 1 
ATOM   4127 N N   . LYS A 1 563 ? 2.695   34.391  -6.381  1.00 68.01  ? 557 LYS A N   1 
ATOM   4128 C CA  . LYS A 1 563 ? 1.798   35.454  -6.809  1.00 70.30  ? 557 LYS A CA  1 
ATOM   4129 C C   . LYS A 1 563 ? 0.519   34.925  -7.458  1.00 72.72  ? 557 LYS A C   1 
ATOM   4130 O O   . LYS A 1 563 ? -0.576  35.421  -7.192  1.00 72.49  ? 557 LYS A O   1 
ATOM   4131 C CB  . LYS A 1 563 ? 2.557   36.352  -7.788  1.00 70.83  ? 557 LYS A CB  1 
ATOM   4132 C CG  . LYS A 1 563 ? 1.922   37.693  -8.051  1.00 72.97  ? 557 LYS A CG  1 
ATOM   4133 C CD  . LYS A 1 563 ? 2.833   38.561  -8.901  1.00 75.21  ? 557 LYS A CD  1 
ATOM   4134 C CE  . LYS A 1 563 ? 2.258   39.916  -9.160  1.00 78.32  ? 557 LYS A CE  1 
ATOM   4135 N NZ  . LYS A 1 563 ? 0.982   39.818  -9.909  1.00 81.07  ? 557 LYS A NZ  1 
ATOM   4136 N N   . CYS A 1 564 ? 0.680   33.909  -8.310  1.00 72.08  ? 558 CYS A N   1 
ATOM   4137 C CA  . CYS A 1 564 ? -0.415  33.346  -9.078  1.00 72.49  ? 558 CYS A CA  1 
ATOM   4138 C C   . CYS A 1 564 ? -1.276  32.399  -8.248  1.00 72.07  ? 558 CYS A C   1 
ATOM   4139 O O   . CYS A 1 564 ? -2.439  32.183  -8.575  1.00 71.31  ? 558 CYS A O   1 
ATOM   4140 C CB  . CYS A 1 564 ? 0.123   32.651  -10.326 1.00 72.95  ? 558 CYS A CB  1 
ATOM   4141 S SG  . CYS A 1 564 ? 1.010   33.747  -11.464 1.00 75.91  ? 558 CYS A SG  1 
ATOM   4142 N N   . CYS A 1 565 ? -0.694  31.822  -7.191  1.00 70.84  ? 559 CYS A N   1 
ATOM   4143 C CA  . CYS A 1 565 ? -1.455  31.007  -6.254  1.00 72.63  ? 559 CYS A CA  1 
ATOM   4144 C C   . CYS A 1 565 ? -2.342  31.839  -5.319  1.00 71.80  ? 559 CYS A C   1 
ATOM   4145 O O   . CYS A 1 565 ? -3.225  31.291  -4.671  1.00 73.44  ? 559 CYS A O   1 
ATOM   4146 C CB  . CYS A 1 565 ? -0.522  30.087  -5.464  1.00 69.24  ? 559 CYS A CB  1 
ATOM   4147 S SG  . CYS A 1 565 ? 0.201   28.739  -6.441  1.00 64.44  ? 559 CYS A SG  1 
ATOM   4148 N N   . LYS A 1 566 ? -2.087  33.152  -5.231  1.00 71.00  ? 560 LYS A N   1 
ATOM   4149 C CA  . LYS A 1 566 ? -2.980  34.085  -4.558  1.00 72.25  ? 560 LYS A CA  1 
ATOM   4150 C C   . LYS A 1 566 ? -4.066  34.665  -5.461  1.00 74.91  ? 560 LYS A C   1 
ATOM   4151 O O   . LYS A 1 566 ? -5.025  35.240  -4.962  1.00 79.64  ? 560 LYS A O   1 
ATOM   4152 C CB  . LYS A 1 566 ? -2.219  35.297  -4.042  1.00 70.66  ? 560 LYS A CB  1 
ATOM   4153 C CG  . LYS A 1 566 ? -1.356  35.074  -2.844  1.00 71.20  ? 560 LYS A CG  1 
ATOM   4154 C CD  . LYS A 1 566 ? -0.776  36.395  -2.365  1.00 73.81  ? 560 LYS A CD  1 
ATOM   4155 C CE  . LYS A 1 566 ? 0.098   37.064  -3.413  1.00 77.97  ? 560 LYS A CE  1 
ATOM   4156 N NZ  . LYS A 1 566 ? 0.351   38.494  -3.103  1.00 80.69  ? 560 LYS A NZ  1 
ATOM   4157 N N   . ALA A 1 567 ? -3.871  34.571  -6.783  1.00 75.88  ? 561 ALA A N   1 
ATOM   4158 C CA  . ALA A 1 567 ? -4.742  35.225  -7.746  1.00 74.51  ? 561 ALA A CA  1 
ATOM   4159 C C   . ALA A 1 567 ? -6.111  34.559  -7.790  1.00 76.33  ? 561 ALA A C   1 
ATOM   4160 O O   . ALA A 1 567 ? -6.214  33.351  -7.582  1.00 76.92  ? 561 ALA A O   1 
ATOM   4161 C CB  . ALA A 1 567 ? -4.122  35.193  -9.131  1.00 73.14  ? 561 ALA A CB  1 
ATOM   4162 N N   . ASP A 1 568 ? -7.142  35.359  -8.090  1.00 79.10  ? 562 ASP A N   1 
ATOM   4163 C CA  . ASP A 1 568 ? -8.492  34.844  -8.248  1.00 81.79  ? 562 ASP A CA  1 
ATOM   4164 C C   . ASP A 1 568 ? -8.545  33.901  -9.451  1.00 79.67  ? 562 ASP A C   1 
ATOM   4165 O O   . ASP A 1 568 ? -8.842  32.720  -9.284  1.00 74.67  ? 562 ASP A O   1 
ATOM   4166 C CB  . ASP A 1 568 ? -9.517  35.991  -8.354  1.00 86.94  ? 562 ASP A CB  1 
ATOM   4167 C CG  . ASP A 1 568 ? -9.501  36.950  -7.164  1.00 89.86  ? 562 ASP A CG  1 
ATOM   4168 O OD1 . ASP A 1 568 ? -8.539  36.886  -6.360  1.00 90.28  ? 562 ASP A OD1 1 
ATOM   4169 O OD2 . ASP A 1 568 ? -10.453 37.761  -7.037  1.00 89.00  ? 562 ASP A OD2 1 
ATOM   4170 N N   . ASP A 1 569 ? -8.221  34.409  -10.651 1.00 80.60  ? 563 ASP A N   1 
ATOM   4171 C CA  . ASP A 1 569 ? -8.118  33.554  -11.826 1.00 80.63  ? 563 ASP A CA  1 
ATOM   4172 C C   . ASP A 1 569 ? -6.677  33.079  -11.984 1.00 78.65  ? 563 ASP A C   1 
ATOM   4173 O O   . ASP A 1 569 ? -5.827  33.801  -12.496 1.00 79.79  ? 563 ASP A O   1 
ATOM   4174 C CB  . ASP A 1 569 ? -8.598  34.245  -13.117 1.00 81.41  ? 563 ASP A CB  1 
ATOM   4175 C CG  . ASP A 1 569 ? -8.794  33.303  -14.310 1.00 83.51  ? 563 ASP A CG  1 
ATOM   4176 O OD1 . ASP A 1 569 ? -8.696  32.056  -14.121 1.00 83.18  ? 563 ASP A OD1 1 
ATOM   4177 O OD2 . ASP A 1 569 ? -9.047  33.807  -15.429 1.00 86.07  ? 563 ASP A OD2 1 
ATOM   4178 N N   . LYS A 1 570 ? -6.424  31.845  -11.542 1.00 79.20  ? 564 LYS A N   1 
ATOM   4179 C CA  . LYS A 1 570 ? -5.087  31.284  -11.529 1.00 79.60  ? 564 LYS A CA  1 
ATOM   4180 C C   . LYS A 1 570 ? -4.604  30.995  -12.946 1.00 80.05  ? 564 LYS A C   1 
ATOM   4181 O O   . LYS A 1 570 ? -3.495  31.380  -13.305 1.00 75.85  ? 564 LYS A O   1 
ATOM   4182 C CB  . LYS A 1 570 ? -5.049  29.995  -10.689 1.00 78.41  ? 564 LYS A CB  1 
ATOM   4183 C CG  . LYS A 1 570 ? -5.363  30.198  -9.211  1.00 77.99  ? 564 LYS A CG  1 
ATOM   4184 C CD  . LYS A 1 570 ? -5.202  28.891  -8.419  1.00 79.75  ? 564 LYS A CD  1 
ATOM   4185 C CE  . LYS A 1 570 ? -5.778  28.953  -7.022  1.00 80.05  ? 564 LYS A CE  1 
ATOM   4186 N NZ  . LYS A 1 570 ? -5.200  30.075  -6.242  1.00 81.53  ? 564 LYS A NZ  1 
ATOM   4187 N N   . GLU A 1 571 ? -5.456  30.319  -13.730 1.00 82.50  ? 565 GLU A N   1 
ATOM   4188 C CA  . GLU A 1 571 ? -5.126  29.869  -15.076 1.00 82.45  ? 565 GLU A CA  1 
ATOM   4189 C C   . GLU A 1 571 ? -4.610  31.036  -15.917 1.00 81.87  ? 565 GLU A C   1 
ATOM   4190 O O   . GLU A 1 571 ? -3.653  30.900  -16.679 1.00 82.96  ? 565 GLU A O   1 
ATOM   4191 C CB  . GLU A 1 571 ? -6.355  29.261  -15.785 1.00 84.88  ? 565 GLU A CB  1 
ATOM   4192 C CG  . GLU A 1 571 ? -7.291  28.396  -14.933 1.00 88.77  ? 565 GLU A CG  1 
ATOM   4193 C CD  . GLU A 1 571 ? -6.849  26.985  -14.580 1.00 89.43  ? 565 GLU A CD  1 
ATOM   4194 O OE1 . GLU A 1 571 ? -5.813  26.518  -15.110 1.00 89.91  ? 565 GLU A OE1 1 
ATOM   4195 O OE2 . GLU A 1 571 ? -7.557  26.339  -13.771 1.00 87.32  ? 565 GLU A OE2 1 
ATOM   4196 N N   . THR A 1 572 ? -5.264  32.189  -15.755 1.00 78.58  ? 566 THR A N   1 
ATOM   4197 C CA  . THR A 1 572 ? -4.892  33.404  -16.459 1.00 78.85  ? 566 THR A CA  1 
ATOM   4198 C C   . THR A 1 572 ? -3.611  34.038  -15.916 1.00 73.87  ? 566 THR A C   1 
ATOM   4199 O O   . THR A 1 572 ? -2.809  34.580  -16.674 1.00 73.45  ? 566 THR A O   1 
ATOM   4200 C CB  . THR A 1 572 ? -6.097  34.361  -16.440 1.00 78.66  ? 566 THR A CB  1 
ATOM   4201 O OG1 . THR A 1 572 ? -7.052  33.857  -17.387 1.00 78.07  ? 566 THR A OG1 1 
ATOM   4202 C CG2 . THR A 1 572 ? -5.724  35.812  -16.773 1.00 77.66  ? 566 THR A CG2 1 
ATOM   4203 N N   . CYS A 1 573 ? -3.416  33.987  -14.600 1.00 70.90  ? 567 CYS A N   1 
ATOM   4204 C CA  . CYS A 1 573 ? -2.180  34.493  -14.032 1.00 69.37  ? 567 CYS A CA  1 
ATOM   4205 C C   . CYS A 1 573 ? -0.994  33.693  -14.573 1.00 67.92  ? 567 CYS A C   1 
ATOM   4206 O O   . CYS A 1 573 ? -0.026  34.268  -15.057 1.00 65.65  ? 567 CYS A O   1 
ATOM   4207 C CB  . CYS A 1 573 ? -2.234  34.480  -12.512 1.00 67.99  ? 567 CYS A CB  1 
ATOM   4208 S SG  . CYS A 1 573 ? -1.098  35.651  -11.739 1.00 72.77  ? 567 CYS A SG  1 
ATOM   4209 N N   . PHE A 1 574 ? -1.110  32.361  -14.538 1.00 68.17  ? 568 PHE A N   1 
ATOM   4210 C CA  . PHE A 1 574 ? -0.038  31.472  -14.955 1.00 73.75  ? 568 PHE A CA  1 
ATOM   4211 C C   . PHE A 1 574 ? 0.376   31.640  -16.419 1.00 74.63  ? 568 PHE A C   1 
ATOM   4212 O O   . PHE A 1 574 ? 1.536   31.419  -16.760 1.00 73.32  ? 568 PHE A O   1 
ATOM   4213 C CB  . PHE A 1 574 ? -0.420  29.993  -14.675 1.00 77.89  ? 568 PHE A CB  1 
ATOM   4214 C CG  . PHE A 1 574 ? -0.081  29.505  -13.275 1.00 82.36  ? 568 PHE A CG  1 
ATOM   4215 C CD1 . PHE A 1 574 ? -0.774  29.974  -12.168 1.00 83.45  ? 568 PHE A CD1 1 
ATOM   4216 C CD2 . PHE A 1 574 ? 0.941   28.594  -13.068 1.00 83.79  ? 568 PHE A CD2 1 
ATOM   4217 C CE1 . PHE A 1 574 ? -0.458  29.530  -10.890 1.00 81.59  ? 568 PHE A CE1 1 
ATOM   4218 C CE2 . PHE A 1 574 ? 1.256   28.162  -11.788 1.00 83.91  ? 568 PHE A CE2 1 
ATOM   4219 C CZ  . PHE A 1 574 ? 0.556   28.632  -10.708 1.00 82.14  ? 568 PHE A CZ  1 
ATOM   4220 N N   . ALA A 1 575 ? -0.571  32.032  -17.279 1.00 76.64  ? 569 ALA A N   1 
ATOM   4221 C CA  . ALA A 1 575 ? -0.271  32.296  -18.678 1.00 75.81  ? 569 ALA A CA  1 
ATOM   4222 C C   . ALA A 1 575 ? 0.351   33.681  -18.869 1.00 76.37  ? 569 ALA A C   1 
ATOM   4223 O O   . ALA A 1 575 ? 1.391   33.809  -19.509 1.00 81.09  ? 569 ALA A O   1 
ATOM   4224 C CB  . ALA A 1 575 ? -1.523  32.143  -19.520 1.00 75.06  ? 569 ALA A CB  1 
ATOM   4225 N N   . GLU A 1 576 ? -0.270  34.716  -18.298 1.00 76.04  ? 570 GLU A N   1 
ATOM   4226 C CA  . GLU A 1 576 ? 0.214   36.075  -18.475 1.00 80.58  ? 570 GLU A CA  1 
ATOM   4227 C C   . GLU A 1 576 ? 1.561   36.295  -17.789 1.00 83.35  ? 570 GLU A C   1 
ATOM   4228 O O   . GLU A 1 576 ? 2.565   36.505  -18.465 1.00 86.33  ? 570 GLU A O   1 
ATOM   4229 C CB  . GLU A 1 576 ? -0.814  37.097  -17.960 1.00 84.42  ? 570 GLU A CB  1 
ATOM   4230 C CG  . GLU A 1 576 ? -2.113  37.116  -18.749 1.00 89.64  ? 570 GLU A CG  1 
ATOM   4231 C CD  . GLU A 1 576 ? -1.942  37.108  -20.258 1.00 94.80  ? 570 GLU A CD  1 
ATOM   4232 O OE1 . GLU A 1 576 ? -1.223  37.992  -20.785 1.00 93.65  ? 570 GLU A OE1 1 
ATOM   4233 O OE2 . GLU A 1 576 ? -2.526  36.211  -20.914 1.00 97.05  ? 570 GLU A OE2 1 
ATOM   4234 N N   . GLU A 1 577 ? 1.575   36.238  -16.450 1.00 80.31  ? 571 GLU A N   1 
ATOM   4235 C CA  . GLU A 1 577 ? 2.788   36.436  -15.670 1.00 78.58  ? 571 GLU A CA  1 
ATOM   4236 C C   . GLU A 1 577 ? 3.910   35.472  -16.050 1.00 74.06  ? 571 GLU A C   1 
ATOM   4237 O O   . GLU A 1 577 ? 5.080   35.771  -15.819 1.00 65.72  ? 571 GLU A O   1 
ATOM   4238 C CB  . GLU A 1 577 ? 2.474   36.284  -14.179 1.00 84.71  ? 571 GLU A CB  1 
ATOM   4239 C CG  . GLU A 1 577 ? 1.783   37.484  -13.570 1.00 88.37  ? 571 GLU A CG  1 
ATOM   4240 C CD  . GLU A 1 577 ? 2.707   38.657  -13.331 1.00 94.25  ? 571 GLU A CD  1 
ATOM   4241 O OE1 . GLU A 1 577 ? 3.871   38.593  -13.788 1.00 98.22  ? 571 GLU A OE1 1 
ATOM   4242 O OE2 . GLU A 1 577 ? 2.279   39.631  -12.670 1.00 99.75  ? 571 GLU A OE2 1 
ATOM   4243 N N   . GLY A 1 578 ? 3.531   34.319  -16.621 1.00 74.32  ? 572 GLY A N   1 
ATOM   4244 C CA  . GLY A 1 578 ? 4.462   33.388  -17.238 1.00 75.40  ? 572 GLY A CA  1 
ATOM   4245 C C   . GLY A 1 578 ? 5.372   34.008  -18.298 1.00 77.79  ? 572 GLY A C   1 
ATOM   4246 O O   . GLY A 1 578 ? 6.494   33.547  -18.503 1.00 76.58  ? 572 GLY A O   1 
ATOM   4247 N N   . LYS A 1 579 ? 4.874   35.046  -18.978 1.00 80.04  ? 573 LYS A N   1 
ATOM   4248 C CA  . LYS A 1 579 ? 5.664   35.780  -19.953 1.00 79.56  ? 573 LYS A CA  1 
ATOM   4249 C C   . LYS A 1 579 ? 6.687   36.673  -19.263 1.00 75.26  ? 573 LYS A C   1 
ATOM   4250 O O   . LYS A 1 579 ? 7.836   36.724  -19.692 1.00 78.63  ? 573 LYS A O   1 
ATOM   4251 C CB  . LYS A 1 579 ? 4.776   36.624  -20.890 1.00 80.97  ? 573 LYS A CB  1 
ATOM   4252 C CG  . LYS A 1 579 ? 4.175   35.812  -22.006 1.00 82.97  ? 573 LYS A CG  1 
ATOM   4253 C CD  . LYS A 1 579 ? 3.259   36.617  -22.888 1.00 86.04  ? 573 LYS A CD  1 
ATOM   4254 C CE  . LYS A 1 579 ? 1.924   36.874  -22.247 1.00 87.40  ? 573 LYS A CE  1 
ATOM   4255 N NZ  . LYS A 1 579 ? 0.928   37.344  -23.251 1.00 89.07  ? 573 LYS A NZ  1 
ATOM   4256 N N   . LYS A 1 580 ? 6.267   37.374  -18.202 1.00 70.79  ? 574 LYS A N   1 
ATOM   4257 C CA  . LYS A 1 580 ? 7.189   38.201  -17.437 1.00 68.93  ? 574 LYS A CA  1 
ATOM   4258 C C   . LYS A 1 580 ? 8.309   37.403  -16.756 1.00 63.95  ? 574 LYS A C   1 
ATOM   4259 O O   . LYS A 1 580 ? 9.388   37.938  -16.515 1.00 66.27  ? 574 LYS A O   1 
ATOM   4260 C CB  . LYS A 1 580 ? 6.416   39.044  -16.416 1.00 70.17  ? 574 LYS A CB  1 
ATOM   4261 C CG  . LYS A 1 580 ? 5.512   40.090  -17.071 1.00 73.88  ? 574 LYS A CG  1 
ATOM   4262 C CD  . LYS A 1 580 ? 4.903   41.104  -16.064 1.00 77.34  ? 574 LYS A CD  1 
ATOM   4263 C CE  . LYS A 1 580 ? 4.125   42.226  -16.742 1.00 80.67  ? 574 LYS A CE  1 
ATOM   4264 N NZ  . LYS A 1 580 ? 5.007   43.112  -17.575 1.00 81.30  ? 574 LYS A NZ  1 
ATOM   4265 N N   . LEU A 1 581 ? 8.066   36.121  -16.461 1.00 56.21  ? 575 LEU A N   1 
ATOM   4266 C CA  . LEU A 1 581 ? 9.094   35.267  -15.899 1.00 55.74  ? 575 LEU A CA  1 
ATOM   4267 C C   . LEU A 1 581 ? 10.141  34.966  -16.973 1.00 56.41  ? 575 LEU A C   1 
ATOM   4268 O O   . LEU A 1 581 ? 11.344  35.109  -16.739 1.00 53.92  ? 575 LEU A O   1 
ATOM   4269 C CB  . LEU A 1 581 ? 8.489   33.958  -15.315 1.00 53.72  ? 575 LEU A CB  1 
ATOM   4270 C CG  . LEU A 1 581 ? 9.528   32.892  -14.874 1.00 52.80  ? 575 LEU A CG  1 
ATOM   4271 C CD1 . LEU A 1 581 ? 10.356  33.376  -13.710 1.00 53.02  ? 575 LEU A CD1 1 
ATOM   4272 C CD2 . LEU A 1 581 ? 8.874   31.567  -14.506 1.00 51.40  ? 575 LEU A CD2 1 
ATOM   4273 N N   . VAL A 1 582 ? 9.668   34.547  -18.153 1.00 55.26  ? 576 VAL A N   1 
ATOM   4274 C CA  . VAL A 1 582 ? 10.535  34.277  -19.290 1.00 53.34  ? 576 VAL A CA  1 
ATOM   4275 C C   . VAL A 1 582 ? 11.396  35.487  -19.647 1.00 52.22  ? 576 VAL A C   1 
ATOM   4276 O O   . VAL A 1 582 ? 12.568  35.335  -19.981 1.00 49.90  ? 576 VAL A O   1 
ATOM   4277 C CB  . VAL A 1 582 ? 9.709   33.773  -20.501 1.00 52.38  ? 576 VAL A CB  1 
ATOM   4278 C CG1 . VAL A 1 582 ? 10.408  34.064  -21.841 1.00 52.68  ? 576 VAL A CG1 1 
ATOM   4279 C CG2 . VAL A 1 582 ? 9.387   32.278  -20.351 1.00 50.47  ? 576 VAL A CG2 1 
ATOM   4280 N N   . ALA A 1 583 ? 10.824  36.689  -19.535 1.00 52.16  ? 577 ALA A N   1 
ATOM   4281 C CA  . ALA A 1 583 ? 11.575  37.905  -19.807 1.00 53.08  ? 577 ALA A CA  1 
ATOM   4282 C C   . ALA A 1 583 ? 12.531  38.263  -18.666 1.00 53.27  ? 577 ALA A C   1 
ATOM   4283 O O   . ALA A 1 583 ? 13.528  38.949  -18.886 1.00 53.39  ? 577 ALA A O   1 
ATOM   4284 C CB  . ALA A 1 583 ? 10.619  39.065  -20.093 1.00 51.47  ? 577 ALA A CB  1 
ATOM   4285 N N   . ALA A 1 584 ? 12.224  37.810  -17.441 1.00 52.84  ? 578 ALA A N   1 
ATOM   4286 C CA  . ALA A 1 584 ? 13.085  38.063  -16.291 1.00 50.92  ? 578 ALA A CA  1 
ATOM   4287 C C   . ALA A 1 584 ? 14.352  37.201  -16.311 1.00 49.91  ? 578 ALA A C   1 
ATOM   4288 O O   . ALA A 1 584 ? 15.444  37.698  -16.031 1.00 45.48  ? 578 ALA A O   1 
ATOM   4289 C CB  . ALA A 1 584 ? 12.309  37.845  -14.985 1.00 49.11  ? 578 ALA A CB  1 
ATOM   4290 N N   . SER A 1 585 ? 14.180  35.905  -16.619 1.00 49.84  ? 579 SER A N   1 
ATOM   4291 C CA  . SER A 1 585 ? 15.287  34.970  -16.742 1.00 51.99  ? 579 SER A CA  1 
ATOM   4292 C C   . SER A 1 585 ? 16.197  35.327  -17.915 1.00 53.32  ? 579 SER A C   1 
ATOM   4293 O O   . SER A 1 585 ? 17.408  35.123  -17.861 1.00 52.97  ? 579 SER A O   1 
ATOM   4294 C CB  . SER A 1 585 ? 14.777  33.548  -16.940 1.00 50.82  ? 579 SER A CB  1 
ATOM   4295 O OG  . SER A 1 585 ? 13.589  33.323  -16.208 1.00 54.42  ? 579 SER A OG  1 
ATOM   4296 N N   . GLN A 1 586 ? 15.570  35.815  -18.985 1.00 55.06  ? 580 GLN A N   1 
ATOM   4297 C CA  . GLN A 1 586 ? 16.262  36.242  -20.185 1.00 59.83  ? 580 GLN A CA  1 
ATOM   4298 C C   . GLN A 1 586 ? 17.080  37.490  -19.885 1.00 57.00  ? 580 GLN A C   1 
ATOM   4299 O O   . GLN A 1 586 ? 18.174  37.654  -20.418 1.00 57.10  ? 580 GLN A O   1 
ATOM   4300 C CB  . GLN A 1 586 ? 15.218  36.489  -21.289 1.00 66.28  ? 580 GLN A CB  1 
ATOM   4301 C CG  . GLN A 1 586 ? 15.634  37.391  -22.435 1.00 71.32  ? 580 GLN A CG  1 
ATOM   4302 C CD  . GLN A 1 586 ? 14.445  37.581  -23.351 1.00 77.44  ? 580 GLN A CD  1 
ATOM   4303 O OE1 . GLN A 1 586 ? 14.087  36.689  -24.132 1.00 79.74  ? 580 GLN A OE1 1 
ATOM   4304 N NE2 . GLN A 1 586 ? 13.785  38.738  -23.253 1.00 79.49  ? 580 GLN A NE2 1 
ATOM   4305 N N   . ALA A 1 587 ? 16.523  38.367  -19.042 1.00 55.14  ? 581 ALA A N   1 
ATOM   4306 C CA  . ALA A 1 587 ? 17.227  39.554  -18.587 1.00 54.58  ? 581 ALA A CA  1 
ATOM   4307 C C   . ALA A 1 587 ? 18.473  39.174  -17.791 1.00 53.36  ? 581 ALA A C   1 
ATOM   4308 O O   . ALA A 1 587 ? 19.520  39.789  -17.971 1.00 56.70  ? 581 ALA A O   1 
ATOM   4309 C CB  . ALA A 1 587 ? 16.317  40.433  -17.746 1.00 53.79  ? 581 ALA A CB  1 
ATOM   4310 N N   . ALA A 1 588 ? 18.340  38.142  -16.950 1.00 50.03  ? 582 ALA A N   1 
ATOM   4311 C CA  . ALA A 1 588 ? 19.381  37.712  -16.032 1.00 51.64  ? 582 ALA A CA  1 
ATOM   4312 C C   . ALA A 1 588 ? 20.435  36.810  -16.673 1.00 51.42  ? 582 ALA A C   1 
ATOM   4313 O O   . ALA A 1 588 ? 21.629  36.971  -16.441 1.00 48.79  ? 582 ALA A O   1 
ATOM   4314 C CB  . ALA A 1 588 ? 18.739  36.968  -14.853 1.00 50.20  ? 582 ALA A CB  1 
ATOM   4315 N N   . LEU A 1 589 ? 19.963  35.822  -17.430 1.00 52.88  ? 583 LEU A N   1 
ATOM   4316 C CA  . LEU A 1 589 ? 20.780  34.708  -17.875 1.00 53.42  ? 583 LEU A CA  1 
ATOM   4317 C C   . LEU A 1 589 ? 20.777  34.492  -19.386 1.00 54.48  ? 583 LEU A C   1 
ATOM   4318 O O   . LEU A 1 589 ? 21.572  33.687  -19.876 1.00 49.57  ? 583 LEU A O   1 
ATOM   4319 C CB  . LEU A 1 589 ? 20.228  33.438  -17.207 1.00 55.75  ? 583 LEU A CB  1 
ATOM   4320 C CG  . LEU A 1 589 ? 20.737  33.197  -15.824 1.00 59.92  ? 583 LEU A CG  1 
ATOM   4321 C CD1 . LEU A 1 589 ? 20.380  31.811  -15.326 1.00 60.07  ? 583 LEU A CD1 1 
ATOM   4322 C CD2 . LEU A 1 589 ? 22.236  33.362  -15.778 1.00 63.94  ? 583 LEU A CD2 1 
ATOM   4323 N N   . GLY A 1 590 ? 19.856  35.182  -20.089 1.00 53.10  ? 584 GLY A N   1 
ATOM   4324 C CA  . GLY A 1 590 ? 19.570  34.928  -21.489 1.00 53.70  ? 584 GLY A CA  1 
ATOM   4325 C C   . GLY A 1 590 ? 18.890  33.597  -21.762 1.00 56.59  ? 584 GLY A C   1 
ATOM   4326 O O   . GLY A 1 590 ? 18.698  32.796  -20.853 1.00 54.64  ? 584 GLY A O   1 
ATOM   4327 N N   . GLU B 2 1   ? 54.415  6.159   44.325  1.00 98.17  ? 1   GLU B N   1 
ATOM   4328 C CA  . GLU B 2 1   ? 53.367  5.734   45.257  1.00 98.73  ? 1   GLU B CA  1 
ATOM   4329 C C   . GLU B 2 1   ? 52.790  4.359   44.917  1.00 92.49  ? 1   GLU B C   1 
ATOM   4330 O O   . GLU B 2 1   ? 52.493  3.576   45.817  1.00 87.72  ? 1   GLU B O   1 
ATOM   4331 C CB  . GLU B 2 1   ? 52.219  6.767   45.308  1.00 104.42 ? 1   GLU B CB  1 
ATOM   4332 C CG  . GLU B 2 1   ? 52.629  8.162   45.767  1.00 110.11 ? 1   GLU B CG  1 
ATOM   4333 C CD  . GLU B 2 1   ? 52.939  9.186   44.684  1.00 115.27 ? 1   GLU B CD  1 
ATOM   4334 O OE1 . GLU B 2 1   ? 52.768  8.875   43.482  1.00 118.39 ? 1   GLU B OE1 1 
ATOM   4335 O OE2 . GLU B 2 1   ? 53.340  10.317  45.044  1.00 115.70 ? 1   GLU B OE2 1 
ATOM   4336 N N   . VAL B 2 2   ? 52.607  4.078   43.618  1.00 89.20  ? 2   VAL B N   1 
ATOM   4337 C CA  . VAL B 2 2   ? 52.095  2.786   43.185  1.00 87.57  ? 2   VAL B CA  1 
ATOM   4338 C C   . VAL B 2 2   ? 53.137  1.721   43.519  1.00 86.16  ? 2   VAL B C   1 
ATOM   4339 O O   . VAL B 2 2   ? 54.312  1.879   43.193  1.00 87.67  ? 2   VAL B O   1 
ATOM   4340 C CB  . VAL B 2 2   ? 51.701  2.735   41.679  1.00 85.92  ? 2   VAL B CB  1 
ATOM   4341 C CG1 . VAL B 2 2   ? 51.132  1.360   41.301  1.00 82.15  ? 2   VAL B CG1 1 
ATOM   4342 C CG2 . VAL B 2 2   ? 50.715  3.850   41.319  1.00 85.33  ? 2   VAL B CG2 1 
ATOM   4343 N N   . GLN B 2 3   ? 52.690  0.648   44.183  1.00 83.88  ? 3   GLN B N   1 
ATOM   4344 C CA  . GLN B 2 3   ? 53.565  -0.418  44.639  1.00 80.72  ? 3   GLN B CA  1 
ATOM   4345 C C   . GLN B 2 3   ? 52.842  -1.753  44.501  1.00 72.29  ? 3   GLN B C   1 
ATOM   4346 O O   . GLN B 2 3   ? 51.756  -1.922  45.042  1.00 70.18  ? 3   GLN B O   1 
ATOM   4347 C CB  . GLN B 2 3   ? 53.965  -0.223  46.112  1.00 85.56  ? 3   GLN B CB  1 
ATOM   4348 C CG  . GLN B 2 3   ? 54.692  1.083   46.416  1.00 87.49  ? 3   GLN B CG  1 
ATOM   4349 C CD  . GLN B 2 3   ? 56.186  0.951   46.336  1.00 89.71  ? 3   GLN B CD  1 
ATOM   4350 O OE1 . GLN B 2 3   ? 56.809  1.248   45.303  1.00 95.27  ? 3   GLN B OE1 1 
ATOM   4351 N NE2 . GLN B 2 3   ? 56.792  0.492   47.425  1.00 86.22  ? 3   GLN B NE2 1 
ATOM   4352 N N   . LEU B 2 4   ? 53.468  -2.684  43.778  1.00 69.16  ? 4   LEU B N   1 
ATOM   4353 C CA  . LEU B 2 4   ? 52.976  -4.042  43.627  1.00 67.87  ? 4   LEU B CA  1 
ATOM   4354 C C   . LEU B 2 4   ? 54.049  -4.962  44.183  1.00 64.91  ? 4   LEU B C   1 
ATOM   4355 O O   . LEU B 2 4   ? 55.231  -4.692  44.009  1.00 64.23  ? 4   LEU B O   1 
ATOM   4356 C CB  . LEU B 2 4   ? 52.735  -4.368  42.143  1.00 70.11  ? 4   LEU B CB  1 
ATOM   4357 C CG  . LEU B 2 4   ? 51.727  -3.481  41.413  1.00 70.92  ? 4   LEU B CG  1 
ATOM   4358 C CD1 . LEU B 2 4   ? 51.622  -3.875  39.950  1.00 72.68  ? 4   LEU B CD1 1 
ATOM   4359 C CD2 . LEU B 2 4   ? 50.361  -3.525  42.084  1.00 68.71  ? 4   LEU B CD2 1 
ATOM   4360 N N   . GLN B 2 5   ? 53.647  -6.052  44.836  1.00 65.59  ? 5   GLN B N   1 
ATOM   4361 C CA  . GLN B 2 5   ? 54.631  -6.949  45.414  1.00 68.26  ? 5   GLN B CA  1 
ATOM   4362 C C   . GLN B 2 5   ? 54.105  -8.376  45.450  1.00 64.45  ? 5   GLN B C   1 
ATOM   4363 O O   . GLN B 2 5   ? 53.149  -8.660  46.153  1.00 65.30  ? 5   GLN B O   1 
ATOM   4364 C CB  . GLN B 2 5   ? 55.041  -6.440  46.807  1.00 74.79  ? 5   GLN B CB  1 
ATOM   4365 C CG  . GLN B 2 5   ? 53.889  -6.342  47.798  1.00 83.01  ? 5   GLN B CG  1 
ATOM   4366 C CD  . GLN B 2 5   ? 54.069  -5.245  48.836  1.00 90.12  ? 5   GLN B CD  1 
ATOM   4367 O OE1 . GLN B 2 5   ? 54.216  -5.519  50.040  1.00 90.48  ? 5   GLN B OE1 1 
ATOM   4368 N NE2 . GLN B 2 5   ? 54.031  -3.975  48.392  1.00 92.93  ? 5   GLN B NE2 1 
ATOM   4369 N N   . GLU B 2 6   ? 54.748  -9.259  44.675  1.00 64.78  ? 6   GLU B N   1 
ATOM   4370 C CA  . GLU B 2 6   ? 54.330  -10.647 44.554  1.00 65.05  ? 6   GLU B CA  1 
ATOM   4371 C C   . GLU B 2 6   ? 54.764  -11.426 45.793  1.00 63.08  ? 6   GLU B C   1 
ATOM   4372 O O   . GLU B 2 6   ? 55.778  -11.097 46.401  1.00 59.98  ? 6   GLU B O   1 
ATOM   4373 C CB  . GLU B 2 6   ? 54.940  -11.347 43.299  1.00 64.43  ? 6   GLU B CB  1 
ATOM   4374 C CG  . GLU B 2 6   ? 54.613  -10.735 41.942  1.00 64.54  ? 6   GLU B CG  1 
ATOM   4375 C CD  . GLU B 2 6   ? 55.366  -9.456  41.612  1.00 64.17  ? 6   GLU B CD  1 
ATOM   4376 O OE1 . GLU B 2 6   ? 56.043  -8.931  42.521  1.00 70.26  ? 6   GLU B OE1 1 
ATOM   4377 O OE2 . GLU B 2 6   ? 55.319  -8.991  40.451  1.00 60.13  ? 6   GLU B OE2 1 
ATOM   4378 N N   . SER B 2 7   ? 53.994  -12.465 46.139  1.00 62.36  ? 7   SER B N   1 
ATOM   4379 C CA  . SER B 2 7   ? 54.433  -13.477 47.085  1.00 62.79  ? 7   SER B CA  1 
ATOM   4380 C C   . SER B 2 7   ? 54.012  -14.881 46.656  1.00 65.89  ? 7   SER B C   1 
ATOM   4381 O O   . SER B 2 7   ? 53.219  -15.049 45.728  1.00 65.09  ? 7   SER B O   1 
ATOM   4382 C CB  . SER B 2 7   ? 53.876  -13.200 48.480  1.00 62.48  ? 7   SER B CB  1 
ATOM   4383 O OG  . SER B 2 7   ? 54.231  -11.907 48.943  1.00 63.12  ? 7   SER B OG  1 
ATOM   4384 N N   . GLY B 2 8   ? 54.572  -15.883 47.346  1.00 66.15  ? 8   GLY B N   1 
ATOM   4385 C CA  . GLY B 2 8   ? 54.005  -17.221 47.368  1.00 67.69  ? 8   GLY B CA  1 
ATOM   4386 C C   . GLY B 2 8   ? 54.724  -18.283 46.542  1.00 67.61  ? 8   GLY B C   1 
ATOM   4387 O O   . GLY B 2 8   ? 54.175  -19.366 46.331  1.00 71.64  ? 8   GLY B O   1 
ATOM   4388 N N   . GLY B 2 9   ? 55.949  -17.972 46.102  1.00 67.84  ? 9   GLY B N   1 
ATOM   4389 C CA  . GLY B 2 9   ? 56.702  -18.835 45.204  1.00 70.15  ? 9   GLY B CA  1 
ATOM   4390 C C   . GLY B 2 9   ? 57.778  -19.672 45.893  1.00 71.98  ? 9   GLY B C   1 
ATOM   4391 O O   . GLY B 2 9   ? 58.107  -19.452 47.059  1.00 73.93  ? 9   GLY B O   1 
ATOM   4392 N N   . GLY B 2 10  ? 58.344  -20.609 45.127  1.00 70.83  ? 10  GLY B N   1 
ATOM   4393 C CA  . GLY B 2 10  ? 59.249  -21.620 45.646  1.00 68.97  ? 10  GLY B CA  1 
ATOM   4394 C C   . GLY B 2 10  ? 59.201  -22.836 44.730  1.00 67.35  ? 10  GLY B C   1 
ATOM   4395 O O   . GLY B 2 10  ? 58.627  -22.760 43.649  1.00 67.94  ? 10  GLY B O   1 
ATOM   4396 N N   . LEU B 2 11  ? 59.802  -23.947 45.164  1.00 68.43  ? 11  LEU B N   1 
ATOM   4397 C CA  . LEU B 2 11  ? 59.846  -25.149 44.346  1.00 70.48  ? 11  LEU B CA  1 
ATOM   4398 C C   . LEU B 2 11  ? 58.601  -25.994 44.598  1.00 70.57  ? 11  LEU B C   1 
ATOM   4399 O O   . LEU B 2 11  ? 58.172  -26.153 45.737  1.00 73.21  ? 11  LEU B O   1 
ATOM   4400 C CB  . LEU B 2 11  ? 61.140  -25.944 44.618  1.00 70.00  ? 11  LEU B CB  1 
ATOM   4401 C CG  . LEU B 2 11  ? 61.211  -27.395 44.084  1.00 70.23  ? 11  LEU B CG  1 
ATOM   4402 C CD1 . LEU B 2 11  ? 60.946  -27.494 42.608  1.00 70.38  ? 11  LEU B CD1 1 
ATOM   4403 C CD2 . LEU B 2 11  ? 62.564  -27.989 44.349  1.00 69.57  ? 11  LEU B CD2 1 
ATOM   4404 N N   . VAL B 2 12  ? 58.012  -26.489 43.508  1.00 72.72  ? 12  VAL B N   1 
ATOM   4405 C CA  . VAL B 2 12  ? 56.917  -27.441 43.564  1.00 76.62  ? 12  VAL B CA  1 
ATOM   4406 C C   . VAL B 2 12  ? 57.141  -28.471 42.457  1.00 77.50  ? 12  VAL B C   1 
ATOM   4407 O O   . VAL B 2 12  ? 58.106  -28.365 41.707  1.00 81.63  ? 12  VAL B O   1 
ATOM   4408 C CB  . VAL B 2 12  ? 55.584  -26.676 43.444  1.00 77.88  ? 12  VAL B CB  1 
ATOM   4409 C CG1 . VAL B 2 12  ? 55.335  -26.228 41.999  1.00 78.41  ? 12  VAL B CG1 1 
ATOM   4410 C CG2 . VAL B 2 12  ? 54.414  -27.488 43.992  1.00 77.22  ? 12  VAL B CG2 1 
ATOM   4411 N N   . GLN B 2 13  ? 56.256  -29.466 42.346  1.00 76.86  ? 13  GLN B N   1 
ATOM   4412 C CA  . GLN B 2 13  ? 56.489  -30.570 41.429  1.00 80.04  ? 13  GLN B CA  1 
ATOM   4413 C C   . GLN B 2 13  ? 55.276  -30.914 40.567  1.00 79.55  ? 13  GLN B C   1 
ATOM   4414 O O   . GLN B 2 13  ? 54.159  -30.502 40.880  1.00 79.84  ? 13  GLN B O   1 
ATOM   4415 C CB  . GLN B 2 13  ? 56.930  -31.785 42.248  1.00 84.44  ? 13  GLN B CB  1 
ATOM   4416 C CG  . GLN B 2 13  ? 55.847  -32.344 43.162  1.00 86.55  ? 13  GLN B CG  1 
ATOM   4417 C CD  . GLN B 2 13  ? 56.382  -33.462 43.999  1.00 85.93  ? 13  GLN B CD  1 
ATOM   4418 O OE1 . GLN B 2 13  ? 57.597  -33.659 44.095  1.00 82.58  ? 13  GLN B OE1 1 
ATOM   4419 N NE2 . GLN B 2 13  ? 55.481  -34.209 44.630  1.00 88.87  ? 13  GLN B NE2 1 
ATOM   4420 N N   . PRO B 2 14  ? 55.461  -31.679 39.462  1.00 77.55  ? 14  PRO B N   1 
ATOM   4421 C CA  . PRO B 2 14  ? 54.358  -32.031 38.562  1.00 77.54  ? 14  PRO B CA  1 
ATOM   4422 C C   . PRO B 2 14  ? 53.115  -32.555 39.279  1.00 75.62  ? 14  PRO B C   1 
ATOM   4423 O O   . PRO B 2 14  ? 53.231  -33.282 40.263  1.00 80.13  ? 14  PRO B O   1 
ATOM   4424 C CB  . PRO B 2 14  ? 54.970  -33.110 37.649  1.00 77.59  ? 14  PRO B CB  1 
ATOM   4425 C CG  . PRO B 2 14  ? 56.438  -32.819 37.653  1.00 77.88  ? 14  PRO B CG  1 
ATOM   4426 C CD  . PRO B 2 14  ? 56.749  -32.236 39.019  1.00 77.58  ? 14  PRO B CD  1 
ATOM   4427 N N   . GLY B 2 15  ? 51.935  -32.153 38.778  1.00 74.01  ? 15  GLY B N   1 
ATOM   4428 C CA  . GLY B 2 15  ? 50.647  -32.542 39.330  1.00 70.24  ? 15  GLY B CA  1 
ATOM   4429 C C   . GLY B 2 15  ? 50.159  -31.600 40.425  1.00 68.62  ? 15  GLY B C   1 
ATOM   4430 O O   . GLY B 2 15  ? 48.959  -31.400 40.578  1.00 70.82  ? 15  GLY B O   1 
ATOM   4431 N N   . GLY B 2 16  ? 51.109  -31.023 41.170  1.00 68.87  ? 16  GLY B N   1 
ATOM   4432 C CA  . GLY B 2 16  ? 50.816  -30.205 42.334  1.00 68.29  ? 16  GLY B CA  1 
ATOM   4433 C C   . GLY B 2 16  ? 50.187  -28.849 42.028  1.00 67.75  ? 16  GLY B C   1 
ATOM   4434 O O   . GLY B 2 16  ? 49.741  -28.606 40.906  1.00 70.52  ? 16  GLY B O   1 
ATOM   4435 N N   . SER B 2 17  ? 50.181  -27.979 43.048  1.00 67.34  ? 17  SER B N   1 
ATOM   4436 C CA  A SER B 2 17  ? 49.446  -26.725 43.012  0.25 69.80  ? 17  SER B CA  1 
ATOM   4437 C CA  B SER B 2 17  ? 49.448  -26.726 43.010  0.75 69.46  ? 17  SER B CA  1 
ATOM   4438 C C   . SER B 2 17  ? 50.114  -25.648 43.866  1.00 72.30  ? 17  SER B C   1 
ATOM   4439 O O   . SER B 2 17  ? 50.916  -25.960 44.747  1.00 72.20  ? 17  SER B O   1 
ATOM   4440 C CB  A SER B 2 17  ? 48.018  -26.952 43.497  0.25 70.30  ? 17  SER B CB  1 
ATOM   4441 C CB  B SER B 2 17  ? 48.019  -26.963 43.488  0.75 70.24  ? 17  SER B CB  1 
ATOM   4442 O OG  A SER B 2 17  ? 47.372  -27.975 42.757  0.25 70.64  ? 17  SER B OG  1 
ATOM   4443 O OG  B SER B 2 17  ? 47.998  -27.482 44.808  0.75 69.85  ? 17  SER B OG  1 
ATOM   4444 N N   . LEU B 2 18  ? 49.766  -24.373 43.608  1.00 70.66  ? 18  LEU B N   1 
ATOM   4445 C CA  . LEU B 2 18  ? 50.321  -23.253 44.358  1.00 71.19  ? 18  LEU B CA  1 
ATOM   4446 C C   . LEU B 2 18  ? 49.495  -21.977 44.171  1.00 69.84  ? 18  LEU B C   1 
ATOM   4447 O O   . LEU B 2 18  ? 48.902  -21.756 43.116  1.00 70.47  ? 18  LEU B O   1 
ATOM   4448 C CB  . LEU B 2 18  ? 51.807  -23.026 43.919  1.00 75.18  ? 18  LEU B CB  1 
ATOM   4449 C CG  . LEU B 2 18  ? 52.660  -22.017 44.726  1.00 74.92  ? 18  LEU B CG  1 
ATOM   4450 C CD1 . LEU B 2 18  ? 52.776  -22.414 46.162  1.00 75.34  ? 18  LEU B CD1 1 
ATOM   4451 C CD2 . LEU B 2 18  ? 54.055  -21.893 44.150  1.00 74.87  ? 18  LEU B CD2 1 
ATOM   4452 N N   . ARG B 2 19  ? 49.453  -21.137 45.210  1.00 67.61  ? 19  ARG B N   1 
ATOM   4453 C CA  . ARG B 2 19  ? 48.765  -19.858 45.131  1.00 71.27  ? 19  ARG B CA  1 
ATOM   4454 C C   . ARG B 2 19  ? 49.762  -18.701 45.189  1.00 70.81  ? 19  ARG B C   1 
ATOM   4455 O O   . ARG B 2 19  ? 50.672  -18.720 46.011  1.00 73.68  ? 19  ARG B O   1 
ATOM   4456 C CB  . ARG B 2 19  ? 47.755  -19.722 46.274  1.00 72.03  ? 19  ARG B CB  1 
ATOM   4457 C CG  . ARG B 2 19  ? 47.029  -18.378 46.278  1.00 72.86  ? 19  ARG B CG  1 
ATOM   4458 C CD  . ARG B 2 19  ? 46.590  -17.952 47.658  1.00 74.51  ? 19  ARG B CD  1 
ATOM   4459 N NE  . ARG B 2 19  ? 45.171  -18.150 47.906  1.00 75.70  ? 19  ARG B NE  1 
ATOM   4460 C CZ  . ARG B 2 19  ? 44.526  -17.594 48.922  1.00 79.04  ? 19  ARG B CZ  1 
ATOM   4461 N NH1 . ARG B 2 19  ? 45.179  -17.014 49.919  1.00 75.34  ? 19  ARG B NH1 1 
ATOM   4462 N NH2 . ARG B 2 19  ? 43.195  -17.611 48.934  1.00 81.30  ? 19  ARG B NH2 1 
ATOM   4463 N N   . LEU B 2 20  ? 49.578  -17.696 44.321  1.00 66.41  ? 20  LEU B N   1 
ATOM   4464 C CA  . LEU B 2 20  ? 50.383  -16.483 44.352  1.00 63.04  ? 20  LEU B CA  1 
ATOM   4465 C C   . LEU B 2 20  ? 49.528  -15.330 44.863  1.00 57.97  ? 20  LEU B C   1 
ATOM   4466 O O   . LEU B 2 20  ? 48.308  -15.373 44.743  1.00 54.21  ? 20  LEU B O   1 
ATOM   4467 C CB  . LEU B 2 20  ? 50.912  -16.101 42.949  1.00 66.99  ? 20  LEU B CB  1 
ATOM   4468 C CG  . LEU B 2 20  ? 51.948  -17.013 42.291  1.00 69.77  ? 20  LEU B CG  1 
ATOM   4469 C CD1 . LEU B 2 20  ? 52.497  -16.376 41.020  1.00 68.88  ? 20  LEU B CD1 1 
ATOM   4470 C CD2 . LEU B 2 20  ? 53.112  -17.360 43.221  1.00 71.90  ? 20  LEU B CD2 1 
ATOM   4471 N N   . SER B 2 21  ? 50.179  -14.297 45.413  1.00 58.03  ? 21  SER B N   1 
ATOM   4472 C CA  A SER B 2 21  ? 49.484  -13.109 45.879  0.36 59.20  ? 21  SER B CA  1 
ATOM   4473 C CA  B SER B 2 21  ? 49.479  -13.108 45.870  0.64 59.56  ? 21  SER B CA  1 
ATOM   4474 C C   . SER B 2 21  ? 50.254  -11.831 45.563  1.00 59.06  ? 21  SER B C   1 
ATOM   4475 O O   . SER B 2 21  ? 51.464  -11.862 45.331  1.00 58.51  ? 21  SER B O   1 
ATOM   4476 C CB  A SER B 2 21  ? 49.213  -13.176 47.383  0.36 59.46  ? 21  SER B CB  1 
ATOM   4477 C CB  B SER B 2 21  ? 49.181  -13.168 47.373  0.64 59.84  ? 21  SER B CB  1 
ATOM   4478 O OG  A SER B 2 21  ? 50.410  -13.159 48.142  0.36 58.50  ? 21  SER B OG  1 
ATOM   4479 O OG  B SER B 2 21  ? 50.321  -12.905 48.175  0.64 57.89  ? 21  SER B OG  1 
ATOM   4480 N N   . CYS B 2 22  ? 49.528  -10.711 45.594  1.00 58.71  ? 22  CYS B N   1 
ATOM   4481 C CA  . CYS B 2 22  ? 50.091  -9.409  45.298  1.00 60.71  ? 22  CYS B CA  1 
ATOM   4482 C C   . CYS B 2 22  ? 49.353  -8.371  46.141  1.00 60.47  ? 22  CYS B C   1 
ATOM   4483 O O   . CYS B 2 22  ? 48.120  -8.345  46.156  1.00 58.77  ? 22  CYS B O   1 
ATOM   4484 C CB  . CYS B 2 22  ? 49.987  -9.124  43.798  1.00 64.34  ? 22  CYS B CB  1 
ATOM   4485 S SG  . CYS B 2 22  ? 50.590  -7.488  43.296  1.00 72.87  ? 22  CYS B SG  1 
ATOM   4486 N N   . ALA B 2 23  ? 50.123  -7.547  46.861  1.00 61.03  ? 23  ALA B N   1 
ATOM   4487 C CA  . ALA B 2 23  ? 49.582  -6.422  47.607  1.00 66.51  ? 23  ALA B CA  1 
ATOM   4488 C C   . ALA B 2 23  ? 49.773  -5.114  46.837  1.00 70.55  ? 23  ALA B C   1 
ATOM   4489 O O   . ALA B 2 23  ? 50.788  -4.917  46.169  1.00 70.18  ? 23  ALA B O   1 
ATOM   4490 C CB  . ALA B 2 23  ? 50.246  -6.328  48.967  1.00 66.29  ? 23  ALA B CB  1 
ATOM   4491 N N   . ALA B 2 24  ? 48.815  -4.201  47.028  1.00 73.49  ? 24  ALA B N   1 
ATOM   4492 C CA  . ALA B 2 24  ? 48.837  -2.924  46.282  1.00 75.67  ? 24  ALA B CA  1 
ATOM   4493 C C   . ALA B 2 24  ? 49.038  -1.716  47.187  1.00 76.73  ? 24  ALA B C   1 
ATOM   4494 O O   . ALA B 2 24  ? 48.520  -1.745  48.308  1.00 80.43  ? 24  ALA B O   1 
ATOM   4495 C CB  . ALA B 2 24  ? 47.568  -2.786  45.516  1.00 77.97  ? 24  ALA B CB  1 
ATOM   4496 N N   . SER B 2 25  ? 49.741  -0.704  46.694  1.00 76.50  ? 25  SER B N   1 
ATOM   4497 C CA  . SER B 2 25  ? 49.889  0.569   47.431  1.00 75.93  ? 25  SER B CA  1 
ATOM   4498 C C   . SER B 2 25  ? 49.610  1.671   46.408  1.00 77.82  ? 25  SER B C   1 
ATOM   4499 O O   . SER B 2 25  ? 49.150  1.329   45.315  1.00 74.99  ? 25  SER B O   1 
ATOM   4500 C CB  . SER B 2 25  ? 51.234  0.683   48.065  1.00 76.32  ? 25  SER B CB  1 
ATOM   4501 O OG  . SER B 2 25  ? 51.637  -0.563  48.615  1.00 75.97  ? 25  SER B OG  1 
ATOM   4502 N N   . GLY B 2 26  ? 49.972  2.917   46.682  1.00 79.11  ? 26  GLY B N   1 
ATOM   4503 C CA  . GLY B 2 26  ? 49.573  4.007   45.779  1.00 79.91  ? 26  GLY B CA  1 
ATOM   4504 C C   . GLY B 2 26  ? 48.070  4.126   45.647  1.00 82.23  ? 26  GLY B C   1 
ATOM   4505 O O   . GLY B 2 26  ? 47.411  4.206   46.695  1.00 90.44  ? 26  GLY B O   1 
ATOM   4506 N N   . PHE B 2 27  ? 47.535  4.178   44.433  1.00 81.13  ? 27  PHE B N   1 
ATOM   4507 C CA  . PHE B 2 27  ? 46.083  4.400   44.146  1.00 80.06  ? 27  PHE B CA  1 
ATOM   4508 C C   . PHE B 2 27  ? 45.212  3.196   44.485  1.00 73.50  ? 27  PHE B C   1 
ATOM   4509 O O   . PHE B 2 27  ? 45.749  2.104   44.721  1.00 68.47  ? 27  PHE B O   1 
ATOM   4510 C CB  . PHE B 2 27  ? 45.769  4.860   42.719  1.00 83.27  ? 27  PHE B CB  1 
ATOM   4511 C CG  . PHE B 2 27  ? 44.535  5.750   42.612  1.00 82.64  ? 27  PHE B CG  1 
ATOM   4512 C CD1 . PHE B 2 27  ? 44.576  7.083   42.996  1.00 83.18  ? 27  PHE B CD1 1 
ATOM   4513 C CD2 . PHE B 2 27  ? 43.332  5.249   42.132  1.00 82.84  ? 27  PHE B CD2 1 
ATOM   4514 C CE1 . PHE B 2 27  ? 43.452  7.887   42.896  1.00 82.03  ? 27  PHE B CE1 1 
ATOM   4515 C CE2 . PHE B 2 27  ? 42.212  6.057   42.035  1.00 83.22  ? 27  PHE B CE2 1 
ATOM   4516 C CZ  . PHE B 2 27  ? 42.274  7.372   42.417  1.00 83.54  ? 27  PHE B CZ  1 
ATOM   4517 N N   . THR B 2 28  ? 43.909  3.430   44.643  1.00 70.02  ? 28  THR B N   1 
ATOM   4518 C CA  . THR B 2 28  ? 43.006  2.367   45.097  1.00 69.18  ? 28  THR B CA  1 
ATOM   4519 C C   . THR B 2 28  ? 42.916  1.189   44.177  1.00 67.92  ? 28  THR B C   1 
ATOM   4520 O O   . THR B 2 28  ? 42.690  1.403   42.993  1.00 69.84  ? 28  THR B O   1 
ATOM   4521 C CB  . THR B 2 28  ? 41.653  3.056   45.028  1.00 69.24  ? 28  THR B CB  1 
ATOM   4522 O OG1 . THR B 2 28  ? 41.372  3.130   43.637  1.00 67.39  ? 28  THR B OG1 1 
ATOM   4523 C CG2 . THR B 2 28  ? 41.678  4.466   45.585  1.00 68.40  ? 28  THR B CG2 1 
ATOM   4524 N N   . PHE B 2 29  ? 42.957  -0.015  44.737  1.00 64.97  ? 29  PHE B N   1 
ATOM   4525 C CA  . PHE B 2 29  ? 42.845  -1.312  44.019  1.00 66.71  ? 29  PHE B CA  1 
ATOM   4526 C C   . PHE B 2 29  ? 41.516  -1.518  43.351  1.00 69.20  ? 29  PHE B C   1 
ATOM   4527 O O   . PHE B 2 29  ? 41.447  -2.116  42.268  1.00 72.45  ? 29  PHE B O   1 
ATOM   4528 C CB  . PHE B 2 29  ? 43.093  -2.388  45.076  1.00 62.14  ? 29  PHE B CB  1 
ATOM   4529 C CG  . PHE B 2 29  ? 43.320  -3.815  44.602  1.00 59.64  ? 29  PHE B CG  1 
ATOM   4530 C CD1 . PHE B 2 29  ? 44.424  -4.145  43.831  1.00 59.99  ? 29  PHE B CD1 1 
ATOM   4531 C CD2 . PHE B 2 29  ? 42.442  -4.828  44.964  1.00 58.08  ? 29  PHE B CD2 1 
ATOM   4532 C CE1 . PHE B 2 29  ? 44.628  -5.450  43.418  1.00 60.08  ? 29  PHE B CE1 1 
ATOM   4533 C CE2 . PHE B 2 29  ? 42.650  -6.129  44.547  1.00 57.91  ? 29  PHE B CE2 1 
ATOM   4534 C CZ  . PHE B 2 29  ? 43.742  -6.435  43.775  1.00 59.87  ? 29  PHE B CZ  1 
ATOM   4535 N N   . SER B 2 30  ? 40.453  -1.105  44.007  1.00 69.55  ? 30  SER B N   1 
ATOM   4536 C CA  . SER B 2 30  ? 39.100  -1.462  43.539  1.00 70.57  ? 30  SER B CA  1 
ATOM   4537 C C   . SER B 2 30  ? 38.823  -0.899  42.147  1.00 71.44  ? 30  SER B C   1 
ATOM   4538 O O   . SER B 2 30  ? 38.097  -1.557  41.406  1.00 70.63  ? 30  SER B O   1 
ATOM   4539 C CB  . SER B 2 30  ? 38.107  -0.965  44.528  1.00 68.25  ? 30  SER B CB  1 
ATOM   4540 O OG  . SER B 2 30  ? 38.548  0.256   45.101  1.00 67.47  ? 30  SER B OG  1 
ATOM   4541 N N   . ARG B 2 31  ? 39.266  0.312   41.863  1.00 71.93  ? 31  ARG B N   1 
ATOM   4542 C CA  . ARG B 2 31  ? 38.910  0.963   40.582  1.00 75.58  ? 31  ARG B CA  1 
ATOM   4543 C C   . ARG B 2 31  ? 39.660  0.422   39.348  1.00 73.24  ? 31  ARG B C   1 
ATOM   4544 O O   . ARG B 2 31  ? 39.225  0.783   38.245  1.00 76.15  ? 31  ARG B O   1 
ATOM   4545 C CB  . ARG B 2 31  ? 39.166  2.460   40.774  1.00 80.41  ? 31  ARG B CB  1 
ATOM   4546 C CG  . ARG B 2 31  ? 38.528  3.061   42.018  1.00 84.42  ? 31  ARG B CG  1 
ATOM   4547 C CD  . ARG B 2 31  ? 37.086  2.629   42.218  1.00 87.59  ? 31  ARG B CD  1 
ATOM   4548 N NE  . ARG B 2 31  ? 36.531  3.148   43.473  1.00 92.36  ? 31  ARG B NE  1 
ATOM   4549 C CZ  . ARG B 2 31  ? 35.889  2.422   44.378  1.00 90.92  ? 31  ARG B CZ  1 
ATOM   4550 N NH1 . ARG B 2 31  ? 35.431  1.225   44.064  1.00 89.11  ? 31  ARG B NH1 1 
ATOM   4551 N NH2 . ARG B 2 31  ? 35.707  2.898   45.595  1.00 90.88  ? 31  ARG B NH2 1 
ATOM   4552 N N   . TYR B 2 32  ? 40.728  -0.371  39.477  1.00 66.57  ? 32  TYR B N   1 
ATOM   4553 C CA  . TYR B 2 32  ? 41.424  -0.796  38.245  1.00 61.22  ? 32  TYR B CA  1 
ATOM   4554 C C   . TYR B 2 32  ? 41.569  -2.266  37.974  1.00 60.36  ? 32  TYR B C   1 
ATOM   4555 O O   . TYR B 2 32  ? 41.317  -3.093  38.846  1.00 57.77  ? 32  TYR B O   1 
ATOM   4556 C CB  . TYR B 2 32  ? 42.748  -0.095  38.520  1.00 60.87  ? 32  TYR B CB  1 
ATOM   4557 C CG  . TYR B 2 32  ? 42.724  1.425   38.438  1.00 61.91  ? 32  TYR B CG  1 
ATOM   4558 C CD1 . TYR B 2 32  ? 42.845  2.082   37.221  1.00 64.05  ? 32  TYR B CD1 1 
ATOM   4559 C CD2 . TYR B 2 32  ? 42.632  2.201   39.582  1.00 62.40  ? 32  TYR B CD2 1 
ATOM   4560 C CE1 . TYR B 2 32  ? 42.846  3.463   37.142  1.00 62.89  ? 32  TYR B CE1 1 
ATOM   4561 C CE2 . TYR B 2 32  ? 42.628  3.582   39.516  1.00 64.69  ? 32  TYR B CE2 1 
ATOM   4562 C CZ  . TYR B 2 32  ? 42.736  4.216   38.294  1.00 65.25  ? 32  TYR B CZ  1 
ATOM   4563 O OH  . TYR B 2 32  ? 42.734  5.578   38.236  1.00 63.64  ? 32  TYR B OH  1 
ATOM   4564 N N   . TRP B 2 33  ? 41.950  -2.570  36.730  1.00 60.81  ? 33  TRP B N   1 
ATOM   4565 C CA  . TRP B 2 33  ? 42.234  -3.932  36.296  1.00 60.07  ? 33  TRP B CA  1 
ATOM   4566 C C   . TRP B 2 33  ? 43.559  -4.444  36.862  1.00 58.25  ? 33  TRP B C   1 
ATOM   4567 O O   . TRP B 2 33  ? 44.432  -3.654  37.226  1.00 60.91  ? 33  TRP B O   1 
ATOM   4568 C CB  . TRP B 2 33  ? 42.264  -4.016  34.732  1.00 62.67  ? 33  TRP B CB  1 
ATOM   4569 C CG  . TRP B 2 33  ? 40.906  -4.031  34.048  1.00 59.66  ? 33  TRP B CG  1 
ATOM   4570 C CD1 . TRP B 2 33  ? 39.934  -3.077  34.122  1.00 55.97  ? 33  TRP B CD1 1 
ATOM   4571 C CD2 . TRP B 2 33  ? 40.384  -5.068  33.193  1.00 55.37  ? 33  TRP B CD2 1 
ATOM   4572 N NE1 . TRP B 2 33  ? 38.845  -3.451  33.364  1.00 56.80  ? 33  TRP B NE1 1 
ATOM   4573 C CE2 . TRP B 2 33  ? 39.093  -4.669  32.789  1.00 54.61  ? 33  TRP B CE2 1 
ATOM   4574 C CE3 . TRP B 2 33  ? 40.880  -6.291  32.737  1.00 53.60  ? 33  TRP B CE3 1 
ATOM   4575 C CZ2 . TRP B 2 33  ? 38.302  -5.445  31.948  1.00 54.76  ? 33  TRP B CZ2 1 
ATOM   4576 C CZ3 . TRP B 2 33  ? 40.092  -7.061  31.896  1.00 54.71  ? 33  TRP B CZ3 1 
ATOM   4577 C CH2 . TRP B 2 33  ? 38.824  -6.638  31.508  1.00 54.72  ? 33  TRP B CH2 1 
ATOM   4578 N N   . MET B 2 34  ? 43.714  -5.772  36.922  1.00 54.32  ? 34  MET B N   1 
ATOM   4579 C CA  . MET B 2 34  ? 44.961  -6.369  37.369  1.00 55.23  ? 34  MET B CA  1 
ATOM   4580 C C   . MET B 2 34  ? 45.303  -7.551  36.470  1.00 54.43  ? 34  MET B C   1 
ATOM   4581 O O   . MET B 2 34  ? 44.408  -8.192  35.928  1.00 50.75  ? 34  MET B O   1 
ATOM   4582 C CB  . MET B 2 34  ? 44.885  -6.851  38.836  1.00 55.60  ? 34  MET B CB  1 
ATOM   4583 C CG  . MET B 2 34  ? 44.781  -5.713  39.832  1.00 57.91  ? 34  MET B CG  1 
ATOM   4584 S SD  . MET B 2 34  ? 46.181  -4.531  39.870  1.00 57.83  ? 34  MET B SD  1 
ATOM   4585 C CE  . MET B 2 34  ? 47.544  -5.626  40.268  1.00 57.12  ? 34  MET B CE  1 
ATOM   4586 N N   . PHE B 2 35  ? 46.608  -7.839  36.366  1.00 53.58  ? 35  PHE B N   1 
ATOM   4587 C CA  . PHE B 2 35  ? 47.134  -8.759  35.373  1.00 55.88  ? 35  PHE B CA  1 
ATOM   4588 C C   . PHE B 2 35  ? 48.260  -9.603  35.969  1.00 56.22  ? 35  PHE B C   1 
ATOM   4589 O O   . PHE B 2 35  ? 49.075  -9.068  36.722  1.00 56.37  ? 35  PHE B O   1 
ATOM   4590 C CB  . PHE B 2 35  ? 47.672  -7.953  34.159  1.00 54.94  ? 35  PHE B CB  1 
ATOM   4591 C CG  . PHE B 2 35  ? 46.661  -7.023  33.535  1.00 53.10  ? 35  PHE B CG  1 
ATOM   4592 C CD1 . PHE B 2 35  ? 45.823  -7.462  32.524  1.00 52.61  ? 35  PHE B CD1 1 
ATOM   4593 C CD2 . PHE B 2 35  ? 46.521  -5.719  33.989  1.00 53.06  ? 35  PHE B CD2 1 
ATOM   4594 C CE1 . PHE B 2 35  ? 44.891  -6.605  31.952  1.00 54.27  ? 35  PHE B CE1 1 
ATOM   4595 C CE2 . PHE B 2 35  ? 45.580  -4.864  33.425  1.00 53.56  ? 35  PHE B CE2 1 
ATOM   4596 C CZ  . PHE B 2 35  ? 44.782  -5.306  32.401  1.00 55.54  ? 35  PHE B CZ  1 
ATOM   4597 N N   . TRP B 2 36  ? 48.272  -10.903 35.622  1.00 53.32  ? 36  TRP B N   1 
ATOM   4598 C CA  . TRP B 2 36  ? 49.377  -11.805 35.901  1.00 56.27  ? 36  TRP B CA  1 
ATOM   4599 C C   . TRP B 2 36  ? 50.092  -12.207 34.614  1.00 54.29  ? 36  TRP B C   1 
ATOM   4600 O O   . TRP B 2 36  ? 49.497  -12.829 33.741  1.00 54.47  ? 36  TRP B O   1 
ATOM   4601 C CB  . TRP B 2 36  ? 48.909  -13.105 36.581  1.00 61.29  ? 36  TRP B CB  1 
ATOM   4602 C CG  . TRP B 2 36  ? 48.494  -12.967 38.009  1.00 66.09  ? 36  TRP B CG  1 
ATOM   4603 C CD1 . TRP B 2 36  ? 47.228  -13.042 38.503  1.00 67.96  ? 36  TRP B CD1 1 
ATOM   4604 C CD2 . TRP B 2 36  ? 49.354  -12.769 39.135  1.00 69.44  ? 36  TRP B CD2 1 
ATOM   4605 N NE1 . TRP B 2 36  ? 47.240  -12.876 39.866  1.00 69.99  ? 36  TRP B NE1 1 
ATOM   4606 C CE2 . TRP B 2 36  ? 48.534  -12.712 40.284  1.00 71.07  ? 36  TRP B CE2 1 
ATOM   4607 C CE3 . TRP B 2 36  ? 50.737  -12.625 39.285  1.00 69.18  ? 36  TRP B CE3 1 
ATOM   4608 C CZ2 . TRP B 2 36  ? 49.056  -12.519 41.569  1.00 72.69  ? 36  TRP B CZ2 1 
ATOM   4609 C CZ3 . TRP B 2 36  ? 51.255  -12.439 40.557  1.00 72.80  ? 36  TRP B CZ3 1 
ATOM   4610 C CH2 . TRP B 2 36  ? 50.419  -12.380 41.682  1.00 72.59  ? 36  TRP B CH2 1 
ATOM   4611 N N   . VAL B 2 37  ? 51.391  -11.910 34.548  1.00 55.06  ? 37  VAL B N   1 
ATOM   4612 C CA  . VAL B 2 37  ? 52.212  -12.205 33.389  1.00 55.03  ? 37  VAL B CA  1 
ATOM   4613 C C   . VAL B 2 37  ? 53.494  -12.914 33.827  1.00 55.58  ? 37  VAL B C   1 
ATOM   4614 O O   . VAL B 2 37  ? 54.060  -12.591 34.871  1.00 56.18  ? 37  VAL B O   1 
ATOM   4615 C CB  . VAL B 2 37  ? 52.464  -10.900 32.620  1.00 55.32  ? 37  VAL B CB  1 
ATOM   4616 C CG1 . VAL B 2 37  ? 53.120  -9.856  33.490  1.00 56.55  ? 37  VAL B CG1 1 
ATOM   4617 C CG2 . VAL B 2 37  ? 53.283  -11.145 31.367  1.00 58.90  ? 37  VAL B CG2 1 
ATOM   4618 N N   . ARG B 2 38  ? 53.934  -13.887 33.017  1.00 55.91  ? 38  ARG B N   1 
ATOM   4619 C CA  . ARG B 2 38  ? 55.028  -14.774 33.374  1.00 54.52  ? 38  ARG B CA  1 
ATOM   4620 C C   . ARG B 2 38  ? 56.144  -14.825 32.328  1.00 56.75  ? 38  ARG B C   1 
ATOM   4621 O O   . ARG B 2 38  ? 55.952  -14.469 31.166  1.00 54.91  ? 38  ARG B O   1 
ATOM   4622 C CB  . ARG B 2 38  ? 54.484  -16.184 33.592  1.00 55.81  ? 38  ARG B CB  1 
ATOM   4623 C CG  . ARG B 2 38  ? 54.156  -16.966 32.319  1.00 55.78  ? 38  ARG B CG  1 
ATOM   4624 C CD  . ARG B 2 38  ? 53.503  -18.302 32.674  1.00 55.67  ? 38  ARG B CD  1 
ATOM   4625 N NE  . ARG B 2 38  ? 53.289  -19.196 31.536  1.00 54.33  ? 38  ARG B NE  1 
ATOM   4626 C CZ  . ARG B 2 38  ? 52.691  -20.377 31.634  1.00 56.79  ? 38  ARG B CZ  1 
ATOM   4627 N NH1 . ARG B 2 38  ? 52.385  -20.901 32.811  1.00 58.39  ? 38  ARG B NH1 1 
ATOM   4628 N NH2 . ARG B 2 38  ? 52.388  -21.049 30.527  1.00 57.96  ? 38  ARG B NH2 1 
ATOM   4629 N N   . GLN B 2 39  ? 57.308  -15.312 32.776  1.00 58.24  ? 39  GLN B N   1 
ATOM   4630 C CA  . GLN B 2 39  ? 58.534  -15.338 31.998  1.00 55.79  ? 39  GLN B CA  1 
ATOM   4631 C C   . GLN B 2 39  ? 59.238  -16.677 32.159  1.00 52.83  ? 39  GLN B C   1 
ATOM   4632 O O   . GLN B 2 39  ? 59.911  -16.893 33.164  1.00 54.86  ? 39  GLN B O   1 
ATOM   4633 C CB  . GLN B 2 39  ? 59.431  -14.212 32.474  1.00 56.93  ? 39  GLN B CB  1 
ATOM   4634 C CG  . GLN B 2 39  ? 60.740  -14.059 31.735  1.00 57.25  ? 39  GLN B CG  1 
ATOM   4635 C CD  . GLN B 2 39  ? 61.354  -12.795 32.241  1.00 63.85  ? 39  GLN B CD  1 
ATOM   4636 O OE1 . GLN B 2 39  ? 61.330  -11.747 31.581  1.00 63.89  ? 39  GLN B OE1 1 
ATOM   4637 N NE2 . GLN B 2 39  ? 61.852  -12.835 33.483  1.00 69.73  ? 39  GLN B NE2 1 
ATOM   4638 N N   . ALA B 2 40  ? 59.070  -17.564 31.171  1.00 49.67  ? 40  ALA B N   1 
ATOM   4639 C CA  . ALA B 2 40  ? 59.671  -18.888 31.202  1.00 49.34  ? 40  ALA B CA  1 
ATOM   4640 C C   . ALA B 2 40  ? 61.142  -18.856 30.789  1.00 52.41  ? 40  ALA B C   1 
ATOM   4641 O O   . ALA B 2 40  ? 61.579  -17.891 30.161  1.00 51.04  ? 40  ALA B O   1 
ATOM   4642 C CB  . ALA B 2 40  ? 58.902  -19.819 30.308  1.00 48.15  ? 40  ALA B CB  1 
ATOM   4643 N N   . PRO B 2 41  ? 61.926  -19.915 31.118  1.00 54.43  ? 41  PRO B N   1 
ATOM   4644 C CA  . PRO B 2 41  ? 63.388  -19.905 31.013  1.00 57.52  ? 41  PRO B CA  1 
ATOM   4645 C C   . PRO B 2 41  ? 64.057  -19.253 29.802  1.00 61.31  ? 41  PRO B C   1 
ATOM   4646 O O   . PRO B 2 41  ? 65.045  -18.529 29.971  1.00 72.03  ? 41  PRO B O   1 
ATOM   4647 C CB  . PRO B 2 41  ? 63.732  -21.403 31.087  1.00 53.86  ? 41  PRO B CB  1 
ATOM   4648 C CG  . PRO B 2 41  ? 62.704  -21.944 32.006  1.00 52.38  ? 41  PRO B CG  1 
ATOM   4649 C CD  . PRO B 2 41  ? 61.444  -21.187 31.691  1.00 53.53  ? 41  PRO B CD  1 
ATOM   4650 N N   . GLY B 2 42  ? 63.555  -19.516 28.594  1.00 54.65  ? 42  GLY B N   1 
ATOM   4651 C CA  . GLY B 2 42  ? 64.218  -19.021 27.392  1.00 53.54  ? 42  GLY B CA  1 
ATOM   4652 C C   . GLY B 2 42  ? 63.376  -18.047 26.567  1.00 53.04  ? 42  GLY B C   1 
ATOM   4653 O O   . GLY B 2 42  ? 63.631  -17.855 25.380  1.00 52.25  ? 42  GLY B O   1 
ATOM   4654 N N   . LYS B 2 43  ? 62.405  -17.405 27.226  1.00 51.17  ? 43  LYS B N   1 
ATOM   4655 C CA  . LYS B 2 43  ? 61.345  -16.678 26.555  1.00 51.32  ? 43  LYS B CA  1 
ATOM   4656 C C   . LYS B 2 43  ? 61.224  -15.276 27.134  1.00 46.48  ? 43  LYS B C   1 
ATOM   4657 O O   . LYS B 2 43  ? 61.888  -14.957 28.110  1.00 47.80  ? 43  LYS B O   1 
ATOM   4658 C CB  . LYS B 2 43  ? 59.994  -17.421 26.719  1.00 56.80  ? 43  LYS B CB  1 
ATOM   4659 C CG  . LYS B 2 43  ? 59.996  -18.899 26.303  1.00 59.06  ? 43  LYS B CG  1 
ATOM   4660 C CD  . LYS B 2 43  ? 60.195  -19.113 24.790  1.00 63.54  ? 43  LYS B CD  1 
ATOM   4661 C CE  . LYS B 2 43  ? 58.954  -18.818 23.953  1.00 66.98  ? 43  LYS B CE  1 
ATOM   4662 N NZ  . LYS B 2 43  ? 59.222  -18.934 22.467  1.00 66.17  ? 43  LYS B NZ  1 
ATOM   4663 N N   . GLY B 2 44  ? 60.393  -14.450 26.492  1.00 44.24  ? 44  GLY B N   1 
ATOM   4664 C CA  . GLY B 2 44  ? 59.894  -13.220 27.082  1.00 44.18  ? 44  GLY B CA  1 
ATOM   4665 C C   . GLY B 2 44  ? 58.556  -13.450 27.782  1.00 47.33  ? 44  GLY B C   1 
ATOM   4666 O O   . GLY B 2 44  ? 58.165  -14.598 28.028  1.00 48.32  ? 44  GLY B O   1 
ATOM   4667 N N   . LEU B 2 45  ? 57.851  -12.345 28.065  1.00 49.11  ? 45  LEU B N   1 
ATOM   4668 C CA  . LEU B 2 45  ? 56.617  -12.371 28.838  1.00 50.67  ? 45  LEU B CA  1 
ATOM   4669 C C   . LEU B 2 45  ? 55.453  -13.047 28.118  1.00 51.40  ? 45  LEU B C   1 
ATOM   4670 O O   . LEU B 2 45  ? 55.174  -12.719 26.977  1.00 54.43  ? 45  LEU B O   1 
ATOM   4671 C CB  . LEU B 2 45  ? 56.160  -10.952 29.153  1.00 50.47  ? 45  LEU B CB  1 
ATOM   4672 C CG  . LEU B 2 45  ? 57.074  -10.124 30.002  1.00 53.09  ? 45  LEU B CG  1 
ATOM   4673 C CD1 . LEU B 2 45  ? 56.462  -8.786  30.244  1.00 54.51  ? 45  LEU B CD1 1 
ATOM   4674 C CD2 . LEU B 2 45  ? 57.398  -10.808 31.336  1.00 54.04  ? 45  LEU B CD2 1 
ATOM   4675 N N   . GLU B 2 46  ? 54.782  -13.977 28.808  1.00 52.76  ? 46  GLU B N   1 
ATOM   4676 C CA  . GLU B 2 46  ? 53.488  -14.499 28.400  1.00 50.90  ? 46  GLU B CA  1 
ATOM   4677 C C   . GLU B 2 46  ? 52.421  -13.889 29.308  1.00 51.91  ? 46  GLU B C   1 
ATOM   4678 O O   . GLU B 2 46  ? 52.552  -13.896 30.536  1.00 47.47  ? 46  GLU B O   1 
ATOM   4679 C CB  . GLU B 2 46  ? 53.497  -16.016 28.482  1.00 50.38  ? 46  GLU B CB  1 
ATOM   4680 C CG  . GLU B 2 46  ? 52.259  -16.721 27.970  1.00 52.03  ? 46  GLU B CG  1 
ATOM   4681 C CD  . GLU B 2 46  ? 52.407  -18.242 27.974  1.00 54.75  ? 46  GLU B CD  1 
ATOM   4682 O OE1 . GLU B 2 46  ? 53.337  -18.752 28.645  1.00 58.32  ? 46  GLU B OE1 1 
ATOM   4683 O OE2 . GLU B 2 46  ? 51.615  -18.929 27.293  1.00 52.21  ? 46  GLU B OE2 1 
ATOM   4684 N N   . TRP B 2 47  ? 51.381  -13.313 28.688  1.00 53.51  ? 47  TRP B N   1 
ATOM   4685 C CA  . TRP B 2 47  ? 50.281  -12.730 29.439  1.00 49.94  ? 47  TRP B CA  1 
ATOM   4686 C C   . TRP B 2 47  ? 49.229  -13.820 29.594  1.00 51.38  ? 47  TRP B C   1 
ATOM   4687 O O   . TRP B 2 47  ? 48.751  -14.357 28.598  1.00 46.68  ? 47  TRP B O   1 
ATOM   4688 C CB  . TRP B 2 47  ? 49.723  -11.505 28.777  1.00 45.47  ? 47  TRP B CB  1 
ATOM   4689 C CG  . TRP B 2 47  ? 50.713  -10.402 28.703  1.00 44.77  ? 47  TRP B CG  1 
ATOM   4690 C CD1 . TRP B 2 47  ? 51.738  -10.276 27.812  1.00 43.80  ? 47  TRP B CD1 1 
ATOM   4691 C CD2 . TRP B 2 47  ? 50.767  -9.245  29.549  1.00 44.26  ? 47  TRP B CD2 1 
ATOM   4692 N NE1 . TRP B 2 47  ? 52.427  -9.108  28.050  1.00 44.29  ? 47  TRP B NE1 1 
ATOM   4693 C CE2 . TRP B 2 47  ? 51.856  -8.463  29.121  1.00 42.96  ? 47  TRP B CE2 1 
ATOM   4694 C CE3 . TRP B 2 47  ? 49.999  -8.801  30.632  1.00 45.21  ? 47  TRP B CE3 1 
ATOM   4695 C CZ2 . TRP B 2 47  ? 52.202  -7.268  29.740  1.00 45.23  ? 47  TRP B CZ2 1 
ATOM   4696 C CZ3 . TRP B 2 47  ? 50.343  -7.622  31.253  1.00 46.78  ? 47  TRP B CZ3 1 
ATOM   4697 C CH2 . TRP B 2 47  ? 51.438  -6.867  30.813  1.00 47.77  ? 47  TRP B CH2 1 
ATOM   4698 N N   . ILE B 2 48  ? 48.910  -14.152 30.856  1.00 54.36  ? 48  ILE B N   1 
ATOM   4699 C CA  . ILE B 2 48  ? 48.233  -15.402 31.154  1.00 56.47  ? 48  ILE B CA  1 
ATOM   4700 C C   . ILE B 2 48  ? 46.855  -15.270 31.794  1.00 54.45  ? 48  ILE B C   1 
ATOM   4701 O O   . ILE B 2 48  ? 46.049  -16.184 31.642  1.00 51.15  ? 48  ILE B O   1 
ATOM   4702 C CB  . ILE B 2 48  ? 49.145  -16.304 31.999  1.00 59.30  ? 48  ILE B CB  1 
ATOM   4703 C CG1 . ILE B 2 48  ? 49.546  -15.641 33.323  1.00 60.28  ? 48  ILE B CG1 1 
ATOM   4704 C CG2 . ILE B 2 48  ? 50.374  -16.721 31.180  1.00 59.93  ? 48  ILE B CG2 1 
ATOM   4705 C CD1 . ILE B 2 48  ? 50.283  -16.609 34.296  1.00 60.11  ? 48  ILE B CD1 1 
ATOM   4706 N N   . SER B 2 49  ? 46.592  -14.159 32.499  1.00 54.20  ? 49  SER B N   1 
ATOM   4707 C CA  . SER B 2 49  ? 45.278  -13.935 33.079  1.00 53.16  ? 49  SER B CA  1 
ATOM   4708 C C   . SER B 2 49  ? 45.012  -12.465 33.377  1.00 52.65  ? 49  SER B C   1 
ATOM   4709 O O   . SER B 2 49  ? 45.908  -11.751 33.827  1.00 53.59  ? 49  SER B O   1 
ATOM   4710 C CB  . SER B 2 49  ? 45.120  -14.732 34.377  1.00 57.63  ? 49  SER B CB  1 
ATOM   4711 O OG  . SER B 2 49  ? 45.682  -16.034 34.277  1.00 61.28  ? 49  SER B OG  1 
ATOM   4712 N N   . ASP B 2 50  ? 43.757  -12.044 33.185  1.00 53.85  ? 50  ASP B N   1 
ATOM   4713 C CA  . ASP B 2 50  ? 43.350  -10.673 33.452  1.00 57.86  ? 50  ASP B CA  1 
ATOM   4714 C C   . ASP B 2 50  ? 42.111  -10.657 34.340  1.00 57.73  ? 50  ASP B C   1 
ATOM   4715 O O   . ASP B 2 50  ? 41.328  -11.609 34.321  1.00 59.67  ? 50  ASP B O   1 
ATOM   4716 C CB  . ASP B 2 50  ? 43.027  -9.905  32.140  1.00 61.59  ? 50  ASP B CB  1 
ATOM   4717 C CG  . ASP B 2 50  ? 43.942  -10.205 30.967  1.00 65.82  ? 50  ASP B CG  1 
ATOM   4718 O OD1 . ASP B 2 50  ? 44.028  -11.390 30.559  1.00 68.65  ? 50  ASP B OD1 1 
ATOM   4719 O OD2 . ASP B 2 50  ? 44.547  -9.270  30.446  1.00 71.91  ? 50  ASP B OD2 1 
ATOM   4720 N N   . ILE B 2 51  ? 41.932  -9.548  35.073  1.00 55.91  ? 51  ILE B N   1 
ATOM   4721 C CA  . ILE B 2 51  ? 40.760  -9.346  35.909  1.00 57.21  ? 51  ILE B CA  1 
ATOM   4722 C C   . ILE B 2 51  ? 40.355  -7.874  35.926  1.00 57.97  ? 51  ILE B C   1 
ATOM   4723 O O   . ILE B 2 51  ? 41.198  -6.988  36.069  1.00 51.96  ? 51  ILE B O   1 
ATOM   4724 C CB  . ILE B 2 51  ? 40.980  -9.875  37.362  1.00 59.04  ? 51  ILE B CB  1 
ATOM   4725 C CG1 . ILE B 2 51  ? 39.660  -9.876  38.154  1.00 59.71  ? 51  ILE B CG1 1 
ATOM   4726 C CG2 . ILE B 2 51  ? 42.066  -9.071  38.121  1.00 58.81  ? 51  ILE B CG2 1 
ATOM   4727 C CD1 . ILE B 2 51  ? 39.679  -10.739 39.367  1.00 60.81  ? 51  ILE B CD1 1 
ATOM   4728 N N   . ASN B 2 52  ? 39.043  -7.633  35.787  1.00 62.95  ? 52  ASN B N   1 
ATOM   4729 C CA  . ASN B 2 52  ? 38.488  -6.291  35.897  1.00 65.84  ? 52  ASN B CA  1 
ATOM   4730 C C   . ASN B 2 52  ? 38.411  -5.862  37.362  1.00 68.46  ? 52  ASN B C   1 
ATOM   4731 O O   . ASN B 2 52  ? 38.676  -6.657  38.263  1.00 68.43  ? 52  ASN B O   1 
ATOM   4732 C CB  . ASN B 2 52  ? 37.104  -6.185  35.215  1.00 64.89  ? 52  ASN B CB  1 
ATOM   4733 C CG  . ASN B 2 52  ? 36.015  -6.990  35.879  1.00 63.52  ? 52  ASN B CG  1 
ATOM   4734 O OD1 . ASN B 2 52  ? 36.269  -7.871  36.714  1.00 59.11  ? 52  ASN B OD1 1 
ATOM   4735 N ND2 . ASN B 2 52  ? 34.777  -6.714  35.487  1.00 63.36  ? 52  ASN B ND2 1 
ATOM   4736 N N   . SER B 2 53  ? 38.046  -4.592  37.577  1.00 67.42  ? 53  SER B N   1 
ATOM   4737 C CA  . SER B 2 53  ? 38.229  -3.941  38.862  1.00 66.07  ? 53  SER B CA  1 
ATOM   4738 C C   . SER B 2 53  ? 37.277  -4.512  39.912  1.00 68.48  ? 53  SER B C   1 
ATOM   4739 O O   . SER B 2 53  ? 37.675  -4.766  41.049  1.00 65.90  ? 53  SER B O   1 
ATOM   4740 C CB  . SER B 2 53  ? 38.069  -2.435  38.698  1.00 62.36  ? 53  SER B CB  1 
ATOM   4741 O OG  . SER B 2 53  ? 36.769  -2.124  38.241  1.00 62.80  ? 53  SER B OG  1 
ATOM   4742 N N   . GLY B 2 54  ? 36.031  -4.756  39.498  1.00 69.45  ? 54  GLY B N   1 
ATOM   4743 C CA  . GLY B 2 54  ? 35.037  -5.353  40.372  1.00 70.06  ? 54  GLY B CA  1 
ATOM   4744 C C   . GLY B 2 54  ? 35.153  -6.865  40.562  1.00 68.94  ? 54  GLY B C   1 
ATOM   4745 O O   . GLY B 2 54  ? 34.514  -7.410  41.458  1.00 77.38  ? 54  GLY B O   1 
ATOM   4746 N N   . GLY B 2 55  ? 35.948  -7.538  39.721  1.00 63.61  ? 55  GLY B N   1 
ATOM   4747 C CA  . GLY B 2 55  ? 36.093  -8.986  39.789  1.00 63.23  ? 55  GLY B CA  1 
ATOM   4748 C C   . GLY B 2 55  ? 35.054  -9.761  38.973  1.00 64.17  ? 55  GLY B C   1 
ATOM   4749 O O   . GLY B 2 55  ? 35.036  -10.991 38.982  1.00 61.77  ? 55  GLY B O   1 
ATOM   4750 N N   . THR B 2 56  ? 34.219  -9.034  38.225  1.00 62.84  ? 56  THR B N   1 
ATOM   4751 C CA  . THR B 2 56  ? 33.130  -9.639  37.481  1.00 64.31  ? 56  THR B CA  1 
ATOM   4752 C C   . THR B 2 56  ? 33.507  -10.267 36.142  1.00 62.82  ? 56  THR B C   1 
ATOM   4753 O O   . THR B 2 56  ? 32.683  -10.990 35.586  1.00 63.72  ? 56  THR B O   1 
ATOM   4754 C CB  . THR B 2 56  ? 32.038  -8.593  37.274  1.00 68.30  ? 56  THR B CB  1 
ATOM   4755 O OG1 . THR B 2 56  ? 32.602  -7.435  36.660  1.00 67.09  ? 56  THR B OG1 1 
ATOM   4756 C CG2 . THR B 2 56  ? 31.371  -8.197  38.591  1.00 69.72  ? 56  THR B CG2 1 
ATOM   4757 N N   . TYR B 2 57  ? 34.728  -9.987  35.641  1.00 61.25  ? 57  TYR B N   1 
ATOM   4758 C CA  . TYR B 2 57  ? 35.252  -10.579 34.412  1.00 58.68  ? 57  TYR B CA  1 
ATOM   4759 C C   . TYR B 2 57  ? 36.704  -11.059 34.534  1.00 58.88  ? 57  TYR B C   1 
ATOM   4760 O O   . TYR B 2 57  ? 37.555  -10.338 35.065  1.00 55.25  ? 57  TYR B O   1 
ATOM   4761 C CB  . TYR B 2 57  ? 35.187  -9.579  33.230  1.00 59.30  ? 57  TYR B CB  1 
ATOM   4762 C CG  . TYR B 2 57  ? 35.799  -10.123 31.941  1.00 60.46  ? 57  TYR B CG  1 
ATOM   4763 C CD1 . TYR B 2 57  ? 35.143  -11.090 31.187  1.00 58.29  ? 57  TYR B CD1 1 
ATOM   4764 C CD2 . TYR B 2 57  ? 37.052  -9.700  31.504  1.00 62.13  ? 57  TYR B CD2 1 
ATOM   4765 C CE1 . TYR B 2 57  ? 35.704  -11.608 30.025  1.00 58.01  ? 57  TYR B CE1 1 
ATOM   4766 C CE2 . TYR B 2 57  ? 37.625  -10.213 30.338  1.00 61.39  ? 57  TYR B CE2 1 
ATOM   4767 C CZ  . TYR B 2 57  ? 36.945  -11.168 29.600  1.00 59.78  ? 57  TYR B CZ  1 
ATOM   4768 O OH  . TYR B 2 57  ? 37.484  -11.694 28.445  1.00 58.03  ? 57  TYR B OH  1 
ATOM   4769 N N   . THR B 2 58  ? 36.971  -12.259 33.981  1.00 58.23  ? 58  THR B N   1 
ATOM   4770 C CA  . THR B 2 58  ? 38.302  -12.839 33.887  1.00 61.43  ? 58  THR B CA  1 
ATOM   4771 C C   . THR B 2 58  ? 38.627  -13.438 32.514  1.00 63.74  ? 58  THR B C   1 
ATOM   4772 O O   . THR B 2 58  ? 37.747  -13.987 31.847  1.00 61.92  ? 58  THR B O   1 
ATOM   4773 C CB  . THR B 2 58  ? 38.498  -13.967 34.952  1.00 62.48  ? 58  THR B CB  1 
ATOM   4774 O OG1 . THR B 2 58  ? 37.735  -15.124 34.576  1.00 60.00  ? 58  THR B OG1 1 
ATOM   4775 C CG2 . THR B 2 58  ? 38.140  -13.516 36.376  1.00 60.44  ? 58  THR B CG2 1 
ATOM   4776 N N   . ARG B 2 59  ? 39.919  -13.387 32.140  1.00 64.68  ? 59  ARG B N   1 
ATOM   4777 C CA  . ARG B 2 59  ? 40.409  -13.878 30.856  1.00 64.45  ? 59  ARG B CA  1 
ATOM   4778 C C   . ARG B 2 59  ? 41.662  -14.729 31.074  1.00 62.62  ? 59  ARG B C   1 
ATOM   4779 O O   . ARG B 2 59  ? 42.478  -14.402 31.935  1.00 61.47  ? 59  ARG B O   1 
ATOM   4780 C CB  . ARG B 2 59  ? 40.699  -12.683 29.914  1.00 64.06  ? 59  ARG B CB  1 
ATOM   4781 C CG  . ARG B 2 59  ? 41.493  -13.013 28.635  1.00 67.93  ? 59  ARG B CG  1 
ATOM   4782 C CD  . ARG B 2 59  ? 42.052  -11.730 28.002  1.00 70.85  ? 59  ARG B CD  1 
ATOM   4783 N NE  . ARG B 2 59  ? 43.267  -11.917 27.209  1.00 71.97  ? 59  ARG B NE  1 
ATOM   4784 C CZ  . ARG B 2 59  ? 44.502  -11.721 27.660  1.00 71.89  ? 59  ARG B CZ  1 
ATOM   4785 N NH1 . ARG B 2 59  ? 45.110  -12.623 28.417  1.00 68.84  ? 59  ARG B NH1 1 
ATOM   4786 N NH2 . ARG B 2 59  ? 45.165  -10.624 27.288  1.00 69.05  ? 59  ARG B NH2 1 
ATOM   4787 N N   . TYR B 2 60  ? 41.802  -15.806 30.283  1.00 58.31  ? 60  TYR B N   1 
ATOM   4788 C CA  . TYR B 2 60  ? 42.908  -16.739 30.418  1.00 58.97  ? 60  TYR B CA  1 
ATOM   4789 C C   . TYR B 2 60  ? 43.483  -17.172 29.073  1.00 61.40  ? 60  TYR B C   1 
ATOM   4790 O O   . TYR B 2 60  ? 42.781  -17.775 28.260  1.00 66.20  ? 60  TYR B O   1 
ATOM   4791 C CB  . TYR B 2 60  ? 42.483  -18.025 31.136  1.00 59.51  ? 60  TYR B CB  1 
ATOM   4792 C CG  . TYR B 2 60  ? 41.968  -17.831 32.538  1.00 60.95  ? 60  TYR B CG  1 
ATOM   4793 C CD1 . TYR B 2 60  ? 42.843  -17.680 33.609  1.00 59.68  ? 60  TYR B CD1 1 
ATOM   4794 C CD2 . TYR B 2 60  ? 40.600  -17.794 32.800  1.00 59.22  ? 60  TYR B CD2 1 
ATOM   4795 C CE1 . TYR B 2 60  ? 42.372  -17.507 34.907  1.00 58.58  ? 60  TYR B CE1 1 
ATOM   4796 C CE2 . TYR B 2 60  ? 40.117  -17.616 34.095  1.00 59.33  ? 60  TYR B CE2 1 
ATOM   4797 C CZ  . TYR B 2 60  ? 41.007  -17.479 35.147  1.00 58.82  ? 60  TYR B CZ  1 
ATOM   4798 O OH  . TYR B 2 60  ? 40.543  -17.307 36.428  1.00 57.96  ? 60  TYR B OH  1 
ATOM   4799 N N   . ALA B 2 61  ? 44.783  -16.918 28.881  1.00 57.62  ? 61  ALA B N   1 
ATOM   4800 C CA  . ALA B 2 61  ? 45.540  -17.538 27.810  1.00 55.66  ? 61  ALA B CA  1 
ATOM   4801 C C   . ALA B 2 61  ? 45.252  -19.036 27.769  1.00 56.12  ? 61  ALA B C   1 
ATOM   4802 O O   . ALA B 2 61  ? 45.088  -19.650 28.819  1.00 59.17  ? 61  ALA B O   1 
ATOM   4803 C CB  . ALA B 2 61  ? 47.026  -17.282 28.017  1.00 54.27  ? 61  ALA B CB  1 
ATOM   4804 N N   . ASP B 2 62  ? 45.202  -19.605 26.556  1.00 56.79  ? 62  ASP B N   1 
ATOM   4805 C CA  . ASP B 2 62  ? 44.891  -21.013 26.347  1.00 58.31  ? 62  ASP B CA  1 
ATOM   4806 C C   . ASP B 2 62  ? 45.791  -21.934 27.157  1.00 61.34  ? 62  ASP B C   1 
ATOM   4807 O O   . ASP B 2 62  ? 45.339  -22.948 27.671  1.00 69.39  ? 62  ASP B O   1 
ATOM   4808 C CB  . ASP B 2 62  ? 45.013  -21.411 24.861  1.00 59.51  ? 62  ASP B CB  1 
ATOM   4809 C CG  . ASP B 2 62  ? 43.880  -20.947 23.926  1.00 65.69  ? 62  ASP B CG  1 
ATOM   4810 O OD1 . ASP B 2 62  ? 42.964  -20.199 24.396  1.00 61.31  ? 62  ASP B OD1 1 
ATOM   4811 O OD2 . ASP B 2 62  ? 43.899  -21.337 22.728  1.00 74.07  ? 62  ASP B OD2 1 
ATOM   4812 N N   . SER B 2 63  ? 47.066  -21.565 27.280  1.00 64.31  ? 63  SER B N   1 
ATOM   4813 C CA  . SER B 2 63  ? 48.057  -22.420 27.912  1.00 62.16  ? 63  SER B CA  1 
ATOM   4814 C C   . SER B 2 63  ? 47.892  -22.613 29.422  1.00 63.31  ? 63  SER B C   1 
ATOM   4815 O O   . SER B 2 63  ? 48.555  -23.472 29.998  1.00 62.80  ? 63  SER B O   1 
ATOM   4816 C CB  . SER B 2 63  ? 49.437  -21.852 27.628  1.00 58.41  ? 63  SER B CB  1 
ATOM   4817 O OG  . SER B 2 63  ? 49.473  -20.538 28.149  1.00 60.02  ? 63  SER B OG  1 
ATOM   4818 N N   . VAL B 2 64  ? 47.033  -21.811 30.069  1.00 62.72  ? 64  VAL B N   1 
ATOM   4819 C CA  . VAL B 2 64  ? 46.743  -22.006 31.482  1.00 65.39  ? 64  VAL B CA  1 
ATOM   4820 C C   . VAL B 2 64  ? 45.260  -22.205 31.809  1.00 70.44  ? 64  VAL B C   1 
ATOM   4821 O O   . VAL B 2 64  ? 44.922  -22.461 32.966  1.00 69.51  ? 64  VAL B O   1 
ATOM   4822 C CB  . VAL B 2 64  ? 47.330  -20.844 32.339  1.00 64.88  ? 64  VAL B CB  1 
ATOM   4823 C CG1 . VAL B 2 64  ? 48.856  -20.756 32.202  1.00 64.76  ? 64  VAL B CG1 1 
ATOM   4824 C CG2 . VAL B 2 64  ? 46.676  -19.501 32.019  1.00 63.62  ? 64  VAL B CG2 1 
ATOM   4825 N N   . LYS B 2 65  ? 44.382  -22.099 30.800  1.00 75.01  ? 65  LYS B N   1 
ATOM   4826 C CA  . LYS B 2 65  ? 42.943  -22.181 31.015  1.00 77.44  ? 65  LYS B CA  1 
ATOM   4827 C C   . LYS B 2 65  ? 42.537  -23.563 31.514  1.00 72.49  ? 65  LYS B C   1 
ATOM   4828 O O   . LYS B 2 65  ? 43.165  -24.560 31.167  1.00 69.64  ? 65  LYS B O   1 
ATOM   4829 C CB  . LYS B 2 65  ? 42.143  -21.854 29.734  1.00 82.19  ? 65  LYS B CB  1 
ATOM   4830 C CG  . LYS B 2 65  ? 42.372  -22.831 28.573  1.00 87.23  ? 65  LYS B CG  1 
ATOM   4831 C CD  . LYS B 2 65  ? 41.532  -24.117 28.613  1.00 90.12  ? 65  LYS B CD  1 
ATOM   4832 C CE  . LYS B 2 65  ? 42.246  -25.268 27.937  1.00 91.81  ? 65  LYS B CE  1 
ATOM   4833 N NZ  . LYS B 2 65  ? 41.743  -26.580 28.416  1.00 94.28  ? 65  LYS B NZ  1 
ATOM   4834 N N   . GLY B 2 66  ? 41.476  -23.595 32.327  1.00 72.14  ? 66  GLY B N   1 
ATOM   4835 C CA  . GLY B 2 66  ? 41.017  -24.817 32.968  1.00 74.84  ? 66  GLY B CA  1 
ATOM   4836 C C   . GLY B 2 66  ? 41.742  -25.125 34.276  1.00 76.52  ? 66  GLY B C   1 
ATOM   4837 O O   . GLY B 2 66  ? 41.117  -25.603 35.223  1.00 78.06  ? 66  GLY B O   1 
ATOM   4838 N N   . ARG B 2 67  ? 43.052  -24.825 34.310  1.00 74.17  ? 67  ARG B N   1 
ATOM   4839 C CA  . ARG B 2 67  ? 43.926  -25.168 35.421  1.00 71.43  ? 67  ARG B CA  1 
ATOM   4840 C C   . ARG B 2 67  ? 44.174  -24.027 36.400  1.00 69.51  ? 67  ARG B C   1 
ATOM   4841 O O   . ARG B 2 67  ? 44.558  -24.262 37.549  1.00 68.83  ? 67  ARG B O   1 
ATOM   4842 C CB  . ARG B 2 67  ? 45.282  -25.607 34.891  1.00 71.38  ? 67  ARG B CB  1 
ATOM   4843 C CG  . ARG B 2 67  ? 45.191  -26.682 33.852  1.00 72.43  ? 67  ARG B CG  1 
ATOM   4844 C CD  . ARG B 2 67  ? 46.562  -27.131 33.422  1.00 75.59  ? 67  ARG B CD  1 
ATOM   4845 N NE  . ARG B 2 67  ? 47.331  -26.058 32.796  1.00 78.01  ? 67  ARG B NE  1 
ATOM   4846 C CZ  . ARG B 2 67  ? 48.431  -25.513 33.307  1.00 79.09  ? 67  ARG B CZ  1 
ATOM   4847 N NH1 . ARG B 2 67  ? 48.715  -25.602 34.595  1.00 79.57  ? 67  ARG B NH1 1 
ATOM   4848 N NH2 . ARG B 2 67  ? 49.255  -24.844 32.506  1.00 78.84  ? 67  ARG B NH2 1 
ATOM   4849 N N   . PHE B 2 68  ? 44.003  -22.791 35.930  1.00 66.39  ? 68  PHE B N   1 
ATOM   4850 C CA  . PHE B 2 68  ? 44.331  -21.641 36.753  1.00 67.71  ? 68  PHE B CA  1 
ATOM   4851 C C   . PHE B 2 68  ? 43.056  -20.913 37.153  1.00 66.40  ? 68  PHE B C   1 
ATOM   4852 O O   . PHE B 2 68  ? 41.995  -21.152 36.590  1.00 72.87  ? 68  PHE B O   1 
ATOM   4853 C CB  . PHE B 2 68  ? 45.280  -20.675 36.024  1.00 70.29  ? 68  PHE B CB  1 
ATOM   4854 C CG  . PHE B 2 68  ? 46.762  -21.000 36.025  1.00 71.74  ? 68  PHE B CG  1 
ATOM   4855 C CD1 . PHE B 2 68  ? 47.209  -22.304 35.853  1.00 73.40  ? 68  PHE B CD1 1 
ATOM   4856 C CD2 . PHE B 2 68  ? 47.712  -19.986 36.115  1.00 72.00  ? 68  PHE B CD2 1 
ATOM   4857 C CE1 . PHE B 2 68  ? 48.579  -22.590 35.823  1.00 75.11  ? 68  PHE B CE1 1 
ATOM   4858 C CE2 . PHE B 2 68  ? 49.077  -20.274 36.070  1.00 70.84  ? 68  PHE B CE2 1 
ATOM   4859 C CZ  . PHE B 2 68  ? 49.503  -21.572 35.928  1.00 73.50  ? 68  PHE B CZ  1 
ATOM   4860 N N   . THR B 2 69  ? 43.183  -20.040 38.151  1.00 64.96  ? 69  THR B N   1 
ATOM   4861 C CA  . THR B 2 69  ? 42.111  -19.145 38.534  1.00 65.13  ? 69  THR B CA  1 
ATOM   4862 C C   . THR B 2 69  ? 42.714  -17.836 39.038  1.00 65.44  ? 69  THR B C   1 
ATOM   4863 O O   . THR B 2 69  ? 43.651  -17.824 39.841  1.00 62.63  ? 69  THR B O   1 
ATOM   4864 C CB  . THR B 2 69  ? 41.179  -19.801 39.575  1.00 64.12  ? 69  THR B CB  1 
ATOM   4865 O OG1 . THR B 2 69  ? 40.573  -20.966 38.989  1.00 62.94  ? 69  THR B OG1 1 
ATOM   4866 C CG2 . THR B 2 69  ? 40.101  -18.824 40.075  1.00 61.44  ? 69  THR B CG2 1 
ATOM   4867 N N   . ILE B 2 70  ? 42.151  -16.734 38.544  1.00 66.70  ? 70  ILE B N   1 
ATOM   4868 C CA  . ILE B 2 70  ? 42.495  -15.411 39.024  1.00 67.03  ? 70  ILE B CA  1 
ATOM   4869 C C   . ILE B 2 70  ? 41.292  -14.897 39.807  1.00 67.11  ? 70  ILE B C   1 
ATOM   4870 O O   . ILE B 2 70  ? 40.159  -15.227 39.474  1.00 69.95  ? 70  ILE B O   1 
ATOM   4871 C CB  . ILE B 2 70  ? 42.928  -14.488 37.868  1.00 65.43  ? 70  ILE B CB  1 
ATOM   4872 C CG1 . ILE B 2 70  ? 43.398  -13.116 38.432  1.00 68.99  ? 70  ILE B CG1 1 
ATOM   4873 C CG2 . ILE B 2 70  ? 41.839  -14.340 36.803  1.00 64.36  ? 70  ILE B CG2 1 
ATOM   4874 C CD1 . ILE B 2 70  ? 44.079  -12.176 37.379  1.00 70.75  ? 70  ILE B CD1 1 
ATOM   4875 N N   . SER B 2 71  ? 41.563  -14.120 40.860  1.00 66.43  ? 71  SER B N   1 
ATOM   4876 C CA  . SER B 2 71  ? 40.533  -13.545 41.710  1.00 68.99  ? 71  SER B CA  1 
ATOM   4877 C C   . SER B 2 71  ? 41.192  -12.492 42.595  1.00 69.71  ? 71  SER B C   1 
ATOM   4878 O O   . SER B 2 71  ? 42.419  -12.391 42.613  1.00 68.04  ? 71  SER B O   1 
ATOM   4879 C CB  . SER B 2 71  ? 39.843  -14.610 42.559  1.00 67.43  ? 71  SER B CB  1 
ATOM   4880 O OG  . SER B 2 71  ? 40.780  -15.305 43.360  1.00 67.50  ? 71  SER B OG  1 
ATOM   4881 N N   . ARG B 2 72  ? 40.374  -11.731 43.329  1.00 70.03  ? 72  ARG B N   1 
ATOM   4882 C CA  . ARG B 2 72  ? 40.882  -10.639 44.144  1.00 71.87  ? 72  ARG B CA  1 
ATOM   4883 C C   . ARG B 2 72  ? 40.076  -10.395 45.421  1.00 73.92  ? 72  ARG B C   1 
ATOM   4884 O O   . ARG B 2 72  ? 39.002  -10.963 45.628  1.00 73.38  ? 72  ARG B O   1 
ATOM   4885 C CB  . ARG B 2 72  ? 40.935  -9.354  43.298  1.00 70.85  ? 72  ARG B CB  1 
ATOM   4886 C CG  . ARG B 2 72  ? 39.569  -8.944  42.725  1.00 70.40  ? 72  ARG B CG  1 
ATOM   4887 C CD  . ARG B 2 72  ? 39.691  -7.981  41.560  1.00 65.45  ? 72  ARG B CD  1 
ATOM   4888 N NE  . ARG B 2 72  ? 40.312  -6.736  41.979  1.00 62.71  ? 72  ARG B NE  1 
ATOM   4889 C CZ  . ARG B 2 72  ? 40.672  -5.752  41.168  1.00 62.72  ? 72  ARG B CZ  1 
ATOM   4890 N NH1 . ARG B 2 72  ? 40.814  -5.945  39.863  1.00 66.60  ? 72  ARG B NH1 1 
ATOM   4891 N NH2 . ARG B 2 72  ? 40.947  -4.556  41.684  1.00 56.70  ? 72  ARG B NH2 1 
ATOM   4892 N N   . ASP B 2 73  ? 40.646  -9.546  46.283  1.00 74.47  ? 73  ASP B N   1 
ATOM   4893 C CA  . ASP B 2 73  ? 40.043  -9.144  47.541  1.00 72.64  ? 73  ASP B CA  1 
ATOM   4894 C C   . ASP B 2 73  ? 40.290  -7.643  47.679  1.00 71.98  ? 73  ASP B C   1 
ATOM   4895 O O   . ASP B 2 73  ? 41.370  -7.223  48.108  1.00 65.77  ? 73  ASP B O   1 
ATOM   4896 C CB  . ASP B 2 73  ? 40.648  -9.955  48.699  1.00 72.92  ? 73  ASP B CB  1 
ATOM   4897 C CG  . ASP B 2 73  ? 40.125  -9.685  50.110  1.00 73.94  ? 73  ASP B CG  1 
ATOM   4898 O OD1 . ASP B 2 73  ? 39.511  -8.610  50.331  1.00 70.31  ? 73  ASP B OD1 1 
ATOM   4899 O OD2 . ASP B 2 73  ? 40.327  -10.560 50.994  1.00 75.80  ? 73  ASP B OD2 1 
ATOM   4900 N N   . ASN B 2 74  ? 39.276  -6.856  47.285  1.00 71.34  ? 74  ASN B N   1 
ATOM   4901 C CA  . ASN B 2 74  ? 39.382  -5.407  47.207  1.00 72.42  ? 74  ASN B CA  1 
ATOM   4902 C C   . ASN B 2 74  ? 39.569  -4.729  48.563  1.00 74.54  ? 74  ASN B C   1 
ATOM   4903 O O   . ASN B 2 74  ? 40.103  -3.621  48.626  1.00 75.61  ? 74  ASN B O   1 
ATOM   4904 C CB  . ASN B 2 74  ? 38.143  -4.812  46.486  1.00 73.11  ? 74  ASN B CB  1 
ATOM   4905 C CG  . ASN B 2 74  ? 38.215  -4.817  44.973  1.00 73.56  ? 74  ASN B CG  1 
ATOM   4906 O OD1 . ASN B 2 74  ? 37.281  -4.398  44.281  1.00 74.65  ? 74  ASN B OD1 1 
ATOM   4907 N ND2 . ASN B 2 74  ? 39.320  -5.263  44.421  1.00 72.16  ? 74  ASN B ND2 1 
ATOM   4908 N N   . ALA B 2 75  ? 39.107  -5.392  49.633  1.00 74.91  ? 75  ALA B N   1 
ATOM   4909 C CA  . ALA B 2 75  ? 39.303  -4.911  50.993  1.00 78.51  ? 75  ALA B CA  1 
ATOM   4910 C C   . ALA B 2 75  ? 40.778  -4.930  51.395  1.00 77.96  ? 75  ALA B C   1 
ATOM   4911 O O   . ALA B 2 75  ? 41.282  -3.965  51.969  1.00 76.01  ? 75  ALA B O   1 
ATOM   4912 C CB  . ALA B 2 75  ? 38.484  -5.749  51.970  1.00 79.18  ? 75  ALA B CB  1 
ATOM   4913 N N   . LYS B 2 76  ? 41.459  -6.035  51.065  1.00 77.54  ? 76  LYS B N   1 
ATOM   4914 C CA  . LYS B 2 76  ? 42.844  -6.249  51.450  1.00 77.63  ? 76  LYS B CA  1 
ATOM   4915 C C   . LYS B 2 76  ? 43.880  -5.722  50.454  1.00 74.76  ? 76  LYS B C   1 
ATOM   4916 O O   . LYS B 2 76  ? 45.079  -5.852  50.706  1.00 70.14  ? 76  LYS B O   1 
ATOM   4917 C CB  . LYS B 2 76  ? 43.063  -7.757  51.666  1.00 81.64  ? 76  LYS B CB  1 
ATOM   4918 C CG  . LYS B 2 76  ? 42.116  -8.354  52.710  1.00 86.60  ? 76  LYS B CG  1 
ATOM   4919 C CD  . LYS B 2 76  ? 42.483  -9.776  53.112  1.00 90.24  ? 76  LYS B CD  1 
ATOM   4920 C CE  . LYS B 2 76  ? 41.624  -10.283 54.248  1.00 92.15  ? 76  LYS B CE  1 
ATOM   4921 N NZ  . LYS B 2 76  ? 42.092  -11.609 54.740  1.00 94.29  ? 76  LYS B NZ  1 
ATOM   4922 N N   . ASN B 2 77  ? 43.419  -5.115  49.343  1.00 71.01  ? 77  ASN B N   1 
ATOM   4923 C CA  . ASN B 2 77  ? 44.299  -4.673  48.270  1.00 67.68  ? 77  ASN B CA  1 
ATOM   4924 C C   . ASN B 2 77  ? 45.193  -5.826  47.806  1.00 70.25  ? 77  ASN B C   1 
ATOM   4925 O O   . ASN B 2 77  ? 46.410  -5.673  47.650  1.00 69.86  ? 77  ASN B O   1 
ATOM   4926 C CB  . ASN B 2 77  ? 45.131  -3.458  48.704  1.00 68.42  ? 77  ASN B CB  1 
ATOM   4927 C CG  . ASN B 2 77  ? 44.441  -2.124  48.531  1.00 70.43  ? 77  ASN B CG  1 
ATOM   4928 O OD1 . ASN B 2 77  ? 45.078  -1.091  48.254  1.00 71.14  ? 77  ASN B OD1 1 
ATOM   4929 N ND2 . ASN B 2 77  ? 43.140  -2.094  48.727  1.00 72.80  ? 77  ASN B ND2 1 
ATOM   4930 N N   . THR B 2 78  ? 44.564  -6.989  47.577  1.00 67.94  ? 78  THR B N   1 
ATOM   4931 C CA  . THR B 2 78  ? 45.303  -8.215  47.327  1.00 67.38  ? 78  THR B CA  1 
ATOM   4932 C C   . THR B 2 78  ? 44.740  -9.031  46.164  1.00 65.77  ? 78  THR B C   1 
ATOM   4933 O O   . THR B 2 78  ? 43.584  -9.453  46.191  1.00 57.72  ? 78  THR B O   1 
ATOM   4934 C CB  . THR B 2 78  ? 45.373  -9.031  48.614  1.00 68.24  ? 78  THR B CB  1 
ATOM   4935 O OG1 . THR B 2 78  ? 45.929  -8.191  49.632  1.00 68.26  ? 78  THR B OG1 1 
ATOM   4936 C CG2 . THR B 2 78  ? 46.207  -10.303 48.459  1.00 67.81  ? 78  THR B CG2 1 
ATOM   4937 N N   . LEU B 2 79  ? 45.607  -9.249  45.162  1.00 65.66  ? 79  LEU B N   1 
ATOM   4938 C CA  . LEU B 2 79  ? 45.309  -10.060 43.995  1.00 64.54  ? 79  LEU B CA  1 
ATOM   4939 C C   . LEU B 2 79  ? 45.825  -11.472 44.248  1.00 62.65  ? 79  LEU B C   1 
ATOM   4940 O O   . LEU B 2 79  ? 46.883  -11.630 44.854  1.00 61.76  ? 79  LEU B O   1 
ATOM   4941 C CB  . LEU B 2 79  ? 45.984  -9.435  42.750  1.00 63.89  ? 79  LEU B CB  1 
ATOM   4942 C CG  . LEU B 2 79  ? 45.746  -10.141 41.413  1.00 64.17  ? 79  LEU B CG  1 
ATOM   4943 C CD1 . LEU B 2 79  ? 44.338  -9.931  40.917  1.00 64.23  ? 79  LEU B CD1 1 
ATOM   4944 C CD2 . LEU B 2 79  ? 46.725  -9.659  40.367  1.00 67.14  ? 79  LEU B CD2 1 
ATOM   4945 N N   . TYR B 2 80  ? 45.070  -12.476 43.774  1.00 62.93  ? 80  TYR B N   1 
ATOM   4946 C CA  . TYR B 2 80  ? 45.424  -13.879 43.944  1.00 66.22  ? 80  TYR B CA  1 
ATOM   4947 C C   . TYR B 2 80  ? 45.512  -14.566 42.590  1.00 64.48  ? 80  TYR B C   1 
ATOM   4948 O O   . TYR B 2 80  ? 44.814  -14.190 41.654  1.00 67.91  ? 80  TYR B O   1 
ATOM   4949 C CB  . TYR B 2 80  ? 44.397  -14.624 44.819  1.00 69.24  ? 80  TYR B CB  1 
ATOM   4950 C CG  . TYR B 2 80  ? 44.271  -14.034 46.203  1.00 73.10  ? 80  TYR B CG  1 
ATOM   4951 C CD1 . TYR B 2 80  ? 45.139  -14.407 47.222  1.00 74.73  ? 80  TYR B CD1 1 
ATOM   4952 C CD2 . TYR B 2 80  ? 43.330  -13.051 46.478  1.00 75.77  ? 80  TYR B CD2 1 
ATOM   4953 C CE1 . TYR B 2 80  ? 45.045  -13.845 48.492  1.00 76.15  ? 80  TYR B CE1 1 
ATOM   4954 C CE2 . TYR B 2 80  ? 43.232  -12.476 47.741  1.00 77.21  ? 80  TYR B CE2 1 
ATOM   4955 C CZ  . TYR B 2 80  ? 44.090  -12.879 48.746  1.00 76.69  ? 80  TYR B CZ  1 
ATOM   4956 O OH  . TYR B 2 80  ? 43.995  -12.311 49.988  1.00 81.67  ? 80  TYR B OH  1 
ATOM   4957 N N   . LEU B 2 81  ? 46.400  -15.554 42.498  1.00 62.44  ? 81  LEU B N   1 
ATOM   4958 C CA  . LEU B 2 81  ? 46.437  -16.457 41.365  1.00 63.14  ? 81  LEU B CA  1 
ATOM   4959 C C   . LEU B 2 81  ? 46.545  -17.848 41.976  1.00 64.29  ? 81  LEU B C   1 
ATOM   4960 O O   . LEU B 2 81  ? 47.475  -18.138 42.728  1.00 65.24  ? 81  LEU B O   1 
ATOM   4961 C CB  . LEU B 2 81  ? 47.611  -16.156 40.426  1.00 63.40  ? 81  LEU B CB  1 
ATOM   4962 C CG  . LEU B 2 81  ? 47.631  -16.874 39.068  1.00 61.04  ? 81  LEU B CG  1 
ATOM   4963 C CD1 . LEU B 2 81  ? 46.516  -16.371 38.139  1.00 59.01  ? 81  LEU B CD1 1 
ATOM   4964 C CD2 . LEU B 2 81  ? 48.998  -16.698 38.396  1.00 60.87  ? 81  LEU B CD2 1 
ATOM   4965 N N   . GLN B 2 82  ? 45.537  -18.674 41.694  1.00 64.90  ? 82  GLN B N   1 
ATOM   4966 C CA  . GLN B 2 82  ? 45.488  -20.030 42.206  1.00 63.28  ? 82  GLN B CA  1 
ATOM   4967 C C   . GLN B 2 82  ? 45.884  -20.921 41.034  1.00 59.23  ? 82  GLN B C   1 
ATOM   4968 O O   . GLN B 2 82  ? 45.218  -20.904 40.005  1.00 54.74  ? 82  GLN B O   1 
ATOM   4969 C CB  . GLN B 2 82  ? 44.073  -20.332 42.768  1.00 63.33  ? 82  GLN B CB  1 
ATOM   4970 C CG  . GLN B 2 82  ? 43.874  -21.761 43.299  1.00 63.08  ? 82  GLN B CG  1 
ATOM   4971 C CD  . GLN B 2 82  ? 44.882  -22.144 44.359  1.00 60.55  ? 82  GLN B CD  1 
ATOM   4972 O OE1 . GLN B 2 82  ? 44.937  -21.546 45.441  1.00 58.66  ? 82  GLN B OE1 1 
ATOM   4973 N NE2 . GLN B 2 82  ? 45.703  -23.144 44.065  1.00 58.57  ? 82  GLN B NE2 1 
ATOM   4974 N N   . MET B 2 83  ? 46.996  -21.649 41.188  1.00 61.00  ? 83  MET B N   1 
ATOM   4975 C CA  . MET B 2 83  ? 47.506  -22.525 40.141  1.00 65.72  ? 83  MET B CA  1 
ATOM   4976 C C   . MET B 2 83  ? 47.344  -24.000 40.518  1.00 66.28  ? 83  MET B C   1 
ATOM   4977 O O   . MET B 2 83  ? 47.873  -24.435 41.542  1.00 67.70  ? 83  MET B O   1 
ATOM   4978 C CB  . MET B 2 83  ? 49.011  -22.256 39.883  1.00 67.61  ? 83  MET B CB  1 
ATOM   4979 C CG  . MET B 2 83  ? 49.358  -20.813 39.553  1.00 71.22  ? 83  MET B CG  1 
ATOM   4980 S SD  . MET B 2 83  ? 51.139  -20.586 39.178  1.00 76.02  ? 83  MET B SD  1 
ATOM   4981 C CE  . MET B 2 83  ? 51.511  -19.505 40.370  1.00 73.78  ? 83  MET B CE  1 
ATOM   4982 N N   . ASN B 2 84  ? 46.631  -24.774 39.684  1.00 64.90  ? 84  ASN B N   1 
ATOM   4983 C CA  . ASN B 2 84  ? 46.513  -26.208 39.894  1.00 62.79  ? 84  ASN B CA  1 
ATOM   4984 C C   . ASN B 2 84  ? 47.163  -26.919 38.717  1.00 63.98  ? 84  ASN B C   1 
ATOM   4985 O O   . ASN B 2 84  ? 47.633  -26.265 37.789  1.00 65.20  ? 84  ASN B O   1 
ATOM   4986 C CB  . ASN B 2 84  ? 45.055  -26.652 40.077  1.00 60.40  ? 84  ASN B CB  1 
ATOM   4987 C CG  . ASN B 2 84  ? 44.357  -25.945 41.207  1.00 59.59  ? 84  ASN B CG  1 
ATOM   4988 O OD1 . ASN B 2 84  ? 44.851  -25.863 42.321  1.00 63.13  ? 84  ASN B OD1 1 
ATOM   4989 N ND2 . ASN B 2 84  ? 43.203  -25.380 40.957  1.00 60.53  ? 84  ASN B ND2 1 
ATOM   4990 N N   . SER B 2 85  ? 47.213  -28.252 38.807  1.00 67.47  ? 85  SER B N   1 
ATOM   4991 C CA  . SER B 2 85  ? 47.716  -29.122 37.755  1.00 69.92  ? 85  SER B CA  1 
ATOM   4992 C C   . SER B 2 85  ? 48.950  -28.552 37.058  1.00 69.57  ? 85  SER B C   1 
ATOM   4993 O O   . SER B 2 85  ? 48.954  -28.358 35.843  1.00 66.06  ? 85  SER B O   1 
ATOM   4994 C CB  . SER B 2 85  ? 46.611  -29.421 36.748  1.00 71.68  ? 85  SER B CB  1 
ATOM   4995 O OG  . SER B 2 85  ? 46.987  -30.502 35.909  1.00 74.82  ? 85  SER B OG  1 
ATOM   4996 N N   . LEU B 2 86  ? 49.994  -28.301 37.860  1.00 69.92  ? 86  LEU B N   1 
ATOM   4997 C CA  . LEU B 2 86  ? 51.219  -27.665 37.400  1.00 67.29  ? 86  LEU B CA  1 
ATOM   4998 C C   . LEU B 2 86  ? 52.031  -28.619 36.535  1.00 66.76  ? 86  LEU B C   1 
ATOM   4999 O O   . LEU B 2 86  ? 52.048  -29.816 36.792  1.00 65.84  ? 86  LEU B O   1 
ATOM   5000 C CB  . LEU B 2 86  ? 52.033  -27.207 38.616  1.00 67.98  ? 86  LEU B CB  1 
ATOM   5001 C CG  . LEU B 2 86  ? 51.432  -26.013 39.373  1.00 69.20  ? 86  LEU B CG  1 
ATOM   5002 C CD1 . LEU B 2 86  ? 52.169  -25.722 40.659  1.00 70.21  ? 86  LEU B CD1 1 
ATOM   5003 C CD2 . LEU B 2 86  ? 51.443  -24.753 38.512  1.00 71.51  ? 86  LEU B CD2 1 
ATOM   5004 N N   . ARG B 2 87  ? 52.665  -28.077 35.488  1.00 68.81  ? 87  ARG B N   1 
ATOM   5005 C CA  . ARG B 2 87  ? 53.500  -28.854 34.584  1.00 68.87  ? 87  ARG B CA  1 
ATOM   5006 C C   . ARG B 2 87  ? 54.899  -28.244 34.546  1.00 68.23  ? 87  ARG B C   1 
ATOM   5007 O O   . ARG B 2 87  ? 55.140  -27.206 35.154  1.00 66.34  ? 87  ARG B O   1 
ATOM   5008 C CB  . ARG B 2 87  ? 52.900  -28.880 33.179  1.00 72.06  ? 87  ARG B CB  1 
ATOM   5009 C CG  . ARG B 2 87  ? 51.449  -29.335 33.116  1.00 77.54  ? 87  ARG B CG  1 
ATOM   5010 C CD  . ARG B 2 87  ? 50.732  -28.764 31.898  1.00 81.40  ? 87  ARG B CD  1 
ATOM   5011 N NE  . ARG B 2 87  ? 49.327  -29.163 31.829  1.00 86.34  ? 87  ARG B NE  1 
ATOM   5012 C CZ  . ARG B 2 87  ? 48.433  -28.663 30.979  1.00 84.22  ? 87  ARG B CZ  1 
ATOM   5013 N NH1 . ARG B 2 87  ? 48.628  -27.505 30.368  1.00 82.73  ? 87  ARG B NH1 1 
ATOM   5014 N NH2 . ARG B 2 87  ? 47.301  -29.328 30.762  1.00 81.97  ? 87  ARG B NH2 1 
ATOM   5015 N N   . ALA B 2 88  ? 55.812  -28.894 33.815  1.00 70.83  ? 88  ALA B N   1 
ATOM   5016 C CA  . ALA B 2 88  ? 57.173  -28.405 33.640  1.00 69.42  ? 88  ALA B CA  1 
ATOM   5017 C C   . ALA B 2 88  ? 57.207  -26.978 33.090  1.00 66.37  ? 88  ALA B C   1 
ATOM   5018 O O   . ALA B 2 88  ? 58.014  -26.153 33.526  1.00 61.64  ? 88  ALA B O   1 
ATOM   5019 C CB  . ALA B 2 88  ? 57.936  -29.340 32.711  1.00 67.08  ? 88  ALA B CB  1 
ATOM   5020 N N   . GLU B 2 89  ? 56.270  -26.705 32.174  1.00 64.69  ? 89  GLU B N   1 
ATOM   5021 C CA  . GLU B 2 89  ? 56.248  -25.500 31.364  1.00 63.40  ? 89  GLU B CA  1 
ATOM   5022 C C   . GLU B 2 89  ? 55.749  -24.284 32.139  1.00 62.15  ? 89  GLU B C   1 
ATOM   5023 O O   . GLU B 2 89  ? 55.820  -23.160 31.638  1.00 58.61  ? 89  GLU B O   1 
ATOM   5024 C CB  . GLU B 2 89  ? 55.358  -25.734 30.142  1.00 64.86  ? 89  GLU B CB  1 
ATOM   5025 C CG  . GLU B 2 89  ? 55.903  -26.762 29.160  1.00 69.85  ? 89  GLU B CG  1 
ATOM   5026 C CD  . GLU B 2 89  ? 55.968  -28.211 29.622  1.00 77.06  ? 89  GLU B CD  1 
ATOM   5027 O OE1 . GLU B 2 89  ? 55.415  -28.544 30.698  1.00 80.81  ? 89  GLU B OE1 1 
ATOM   5028 O OE2 . GLU B 2 89  ? 56.593  -29.018 28.896  1.00 83.33  ? 89  GLU B OE2 1 
ATOM   5029 N N   . ASP B 2 90  ? 55.252  -24.515 33.361  1.00 58.16  ? 90  ASP B N   1 
ATOM   5030 C CA  . ASP B 2 90  ? 54.791  -23.428 34.204  1.00 61.75  ? 90  ASP B CA  1 
ATOM   5031 C C   . ASP B 2 90  ? 55.918  -22.776 35.004  1.00 59.25  ? 90  ASP B C   1 
ATOM   5032 O O   . ASP B 2 90  ? 55.696  -21.760 35.670  1.00 56.41  ? 90  ASP B O   1 
ATOM   5033 C CB  . ASP B 2 90  ? 53.690  -23.925 35.131  1.00 69.63  ? 90  ASP B CB  1 
ATOM   5034 C CG  . ASP B 2 90  ? 52.454  -24.349 34.374  1.00 75.88  ? 90  ASP B CG  1 
ATOM   5035 O OD1 . ASP B 2 90  ? 51.819  -23.470 33.737  1.00 79.86  ? 90  ASP B OD1 1 
ATOM   5036 O OD2 . ASP B 2 90  ? 52.129  -25.569 34.397  1.00 80.08  ? 90  ASP B OD2 1 
ATOM   5037 N N   . THR B 2 91  ? 57.126  -23.349 34.907  1.00 55.63  ? 91  THR B N   1 
ATOM   5038 C CA  . THR B 2 91  ? 58.319  -22.713 35.438  1.00 55.39  ? 91  THR B CA  1 
ATOM   5039 C C   . THR B 2 91  ? 58.462  -21.315 34.842  1.00 51.74  ? 91  THR B C   1 
ATOM   5040 O O   . THR B 2 91  ? 58.472  -21.160 33.629  1.00 54.89  ? 91  THR B O   1 
ATOM   5041 C CB  . THR B 2 91  ? 59.569  -23.549 35.156  1.00 58.63  ? 91  THR B CB  1 
ATOM   5042 O OG1 . THR B 2 91  ? 59.331  -24.913 35.537  1.00 65.18  ? 91  THR B OG1 1 
ATOM   5043 C CG2 . THR B 2 91  ? 60.809  -23.011 35.878  1.00 57.54  ? 91  THR B CG2 1 
ATOM   5044 N N   . ALA B 2 92  ? 58.577  -20.309 35.711  1.00 50.14  ? 92  ALA B N   1 
ATOM   5045 C CA  . ALA B 2 92  ? 58.740  -18.932 35.287  1.00 50.84  ? 92  ALA B CA  1 
ATOM   5046 C C   . ALA B 2 92  ? 58.771  -18.016 36.502  1.00 50.32  ? 92  ALA B C   1 
ATOM   5047 O O   . ALA B 2 92  ? 58.280  -18.375 37.563  1.00 54.64  ? 92  ALA B O   1 
ATOM   5048 C CB  . ALA B 2 92  ? 57.589  -18.521 34.382  1.00 52.94  ? 92  ALA B CB  1 
ATOM   5049 N N   . VAL B 2 93  ? 59.323  -16.821 36.328  1.00 48.98  ? 93  VAL B N   1 
ATOM   5050 C CA  . VAL B 2 93  ? 59.111  -15.737 37.264  1.00 49.68  ? 93  VAL B CA  1 
ATOM   5051 C C   . VAL B 2 93  ? 57.730  -15.141 36.986  1.00 52.70  ? 93  VAL B C   1 
ATOM   5052 O O   . VAL B 2 93  ? 57.512  -14.560 35.922  1.00 53.75  ? 93  VAL B O   1 
ATOM   5053 C CB  . VAL B 2 93  ? 60.226  -14.680 37.096  1.00 52.12  ? 93  VAL B CB  1 
ATOM   5054 C CG1 . VAL B 2 93  ? 60.012  -13.487 38.035  1.00 53.40  ? 93  VAL B CG1 1 
ATOM   5055 C CG2 . VAL B 2 93  ? 61.608  -15.301 37.291  1.00 50.79  ? 93  VAL B CG2 1 
ATOM   5056 N N   . TYR B 2 94  ? 56.797  -15.276 37.940  1.00 52.37  ? 94  TYR B N   1 
ATOM   5057 C CA  . TYR B 2 94  ? 55.473  -14.699 37.783  1.00 50.15  ? 94  TYR B CA  1 
ATOM   5058 C C   . TYR B 2 94  ? 55.500  -13.269 38.307  1.00 54.52  ? 94  TYR B C   1 
ATOM   5059 O O   . TYR B 2 94  ? 56.074  -13.003 39.361  1.00 57.41  ? 94  TYR B O   1 
ATOM   5060 C CB  . TYR B 2 94  ? 54.421  -15.526 38.473  1.00 46.34  ? 94  TYR B CB  1 
ATOM   5061 C CG  . TYR B 2 94  ? 54.162  -16.839 37.776  1.00 44.61  ? 94  TYR B CG  1 
ATOM   5062 C CD1 . TYR B 2 94  ? 55.144  -17.805 37.686  1.00 45.82  ? 94  TYR B CD1 1 
ATOM   5063 C CD2 . TYR B 2 94  ? 52.930  -17.119 37.218  1.00 44.83  ? 94  TYR B CD2 1 
ATOM   5064 C CE1 . TYR B 2 94  ? 54.906  -19.023 37.060  1.00 47.31  ? 94  TYR B CE1 1 
ATOM   5065 C CE2 . TYR B 2 94  ? 52.677  -18.331 36.591  1.00 46.05  ? 94  TYR B CE2 1 
ATOM   5066 C CZ  . TYR B 2 94  ? 53.669  -19.280 36.508  1.00 47.20  ? 94  TYR B CZ  1 
ATOM   5067 O OH  . TYR B 2 94  ? 53.422  -20.466 35.861  1.00 50.36  ? 94  TYR B OH  1 
ATOM   5068 N N   . TYR B 2 95  ? 54.921  -12.346 37.534  1.00 56.55  ? 95  TYR B N   1 
ATOM   5069 C CA  . TYR B 2 95  ? 54.747  -10.981 37.993  1.00 59.47  ? 95  TYR B CA  1 
ATOM   5070 C C   . TYR B 2 95  ? 53.261  -10.629 37.964  1.00 60.48  ? 95  TYR B C   1 
ATOM   5071 O O   . TYR B 2 95  ? 52.439  -11.382 37.446  1.00 61.89  ? 95  TYR B O   1 
ATOM   5072 C CB  . TYR B 2 95  ? 55.533  -9.958  37.151  1.00 61.75  ? 95  TYR B CB  1 
ATOM   5073 C CG  . TYR B 2 95  ? 56.987  -10.268 36.812  1.00 63.14  ? 95  TYR B CG  1 
ATOM   5074 C CD1 . TYR B 2 95  ? 57.323  -11.370 36.026  1.00 63.52  ? 95  TYR B CD1 1 
ATOM   5075 C CD2 . TYR B 2 95  ? 58.013  -9.407  37.195  1.00 60.67  ? 95  TYR B CD2 1 
ATOM   5076 C CE1 . TYR B 2 95  ? 58.641  -11.624 35.661  1.00 63.11  ? 95  TYR B CE1 1 
ATOM   5077 C CE2 . TYR B 2 95  ? 59.335  -9.652  36.837  1.00 61.66  ? 95  TYR B CE2 1 
ATOM   5078 C CZ  . TYR B 2 95  ? 59.646  -10.763 36.069  1.00 63.92  ? 95  TYR B CZ  1 
ATOM   5079 O OH  . TYR B 2 95  ? 60.949  -11.015 35.699  1.00 64.37  ? 95  TYR B OH  1 
ATOM   5080 N N   . CYS B 2 96  ? 52.928  -9.483  38.558  1.00 61.03  ? 96  CYS B N   1 
ATOM   5081 C CA  . CYS B 2 96  ? 51.589  -8.937  38.482  1.00 62.54  ? 96  CYS B CA  1 
ATOM   5082 C C   . CYS B 2 96  ? 51.755  -7.469  38.111  1.00 61.53  ? 96  CYS B C   1 
ATOM   5083 O O   . CYS B 2 96  ? 52.768  -6.844  38.450  1.00 58.36  ? 96  CYS B O   1 
ATOM   5084 C CB  . CYS B 2 96  ? 50.812  -9.108  39.786  1.00 68.94  ? 96  CYS B CB  1 
ATOM   5085 S SG  . CYS B 2 96  ? 50.811  -7.638  40.856  1.00 78.72  ? 96  CYS B SG  1 
ATOM   5086 N N   . ALA B 2 97  ? 50.736  -6.944  37.419  1.00 57.28  ? 97  ALA B N   1 
ATOM   5087 C CA  . ALA B 2 97  ? 50.819  -5.637  36.805  1.00 53.31  ? 97  ALA B CA  1 
ATOM   5088 C C   . ALA B 2 97  ? 49.443  -4.995  36.715  1.00 54.82  ? 97  ALA B C   1 
ATOM   5089 O O   . ALA B 2 97  ? 48.422  -5.669  36.871  1.00 55.58  ? 97  ALA B O   1 
ATOM   5090 C CB  . ALA B 2 97  ? 51.415  -5.773  35.436  1.00 53.86  ? 97  ALA B CB  1 
ATOM   5091 N N   . THR B 2 98  ? 49.451  -3.692  36.422  1.00 54.70  ? 98  THR B N   1 
ATOM   5092 C CA  . THR B 2 98  ? 48.247  -2.890  36.319  1.00 56.72  ? 98  THR B CA  1 
ATOM   5093 C C   . THR B 2 98  ? 48.553  -1.672  35.457  1.00 57.07  ? 98  THR B C   1 
ATOM   5094 O O   . THR B 2 98  ? 49.722  -1.370  35.198  1.00 54.39  ? 98  THR B O   1 
ATOM   5095 C CB  . THR B 2 98  ? 47.776  -2.485  37.723  1.00 60.18  ? 98  THR B CB  1 
ATOM   5096 O OG1 . THR B 2 98  ? 46.528  -1.780  37.642  1.00 62.54  ? 98  THR B OG1 1 
ATOM   5097 C CG2 . THR B 2 98  ? 48.792  -1.613  38.444  1.00 60.67  ? 98  THR B CG2 1 
ATOM   5098 N N   . ASN B 2 99  ? 47.496  -0.964  35.039  1.00 60.24  ? 99  ASN B N   1 
ATOM   5099 C CA  . ASN B 2 99  ? 47.672  0.290   34.319  1.00 65.11  ? 99  ASN B CA  1 
ATOM   5100 C C   . ASN B 2 99  ? 47.185  1.512   35.090  1.00 67.13  ? 99  ASN B C   1 
ATOM   5101 O O   . ASN B 2 99  ? 47.019  2.577   34.499  1.00 70.38  ? 99  ASN B O   1 
ATOM   5102 C CB  . ASN B 2 99  ? 47.003  0.216   32.942  1.00 66.23  ? 99  ASN B CB  1 
ATOM   5103 C CG  . ASN B 2 99  ? 47.829  -0.586  31.981  1.00 65.01  ? 99  ASN B CG  1 
ATOM   5104 O OD1 . ASN B 2 99  ? 48.852  -0.107  31.510  1.00 67.88  ? 99  ASN B OD1 1 
ATOM   5105 N ND2 . ASN B 2 99  ? 47.422  -1.823  31.687  1.00 64.88  ? 99  ASN B ND2 1 
ATOM   5106 N N   . SER B 2 100 ? 46.990  1.354   36.408  1.00 69.98  ? 100 SER B N   1 
ATOM   5107 C CA  . SER B 2 100 ? 46.715  2.479   37.288  1.00 70.61  ? 100 SER B CA  1 
ATOM   5108 C C   . SER B 2 100 ? 47.826  3.521   37.267  1.00 71.93  ? 100 SER B C   1 
ATOM   5109 O O   . SER B 2 100 ? 49.002  3.192   37.110  1.00 70.02  ? 100 SER B O   1 
ATOM   5110 C CB  . SER B 2 100 ? 46.541  2.017   38.723  1.00 71.23  ? 100 SER B CB  1 
ATOM   5111 O OG  . SER B 2 100 ? 45.412  1.176   38.834  1.00 74.73  ? 100 SER B OG  1 
ATOM   5112 N N   . GLY B 2 101 ? 47.424  4.776   37.465  1.00 76.18  ? 101 GLY B N   1 
ATOM   5113 C CA  . GLY B 2 101 ? 48.358  5.878   37.577  1.00 80.69  ? 101 GLY B CA  1 
ATOM   5114 C C   . GLY B 2 101 ? 48.525  6.585   36.240  1.00 85.33  ? 101 GLY B C   1 
ATOM   5115 O O   . GLY B 2 101 ? 47.925  6.184   35.246  1.00 85.95  ? 101 GLY B O   1 
ATOM   5116 N N   . ASP B 2 102 ? 49.322  7.658   36.254  1.00 92.86  ? 102 ASP B N   1 
ATOM   5117 C CA  . ASP B 2 102 ? 49.706  8.371   35.047  1.00 96.84  ? 102 ASP B CA  1 
ATOM   5118 C C   . ASP B 2 102 ? 51.204  8.201   34.821  1.00 91.52  ? 102 ASP B C   1 
ATOM   5119 O O   . ASP B 2 102 ? 51.846  9.064   34.224  1.00 85.79  ? 102 ASP B O   1 
ATOM   5120 C CB  . ASP B 2 102 ? 49.339  9.855   35.150  1.00 103.96 ? 102 ASP B CB  1 
ATOM   5121 C CG  . ASP B 2 102 ? 47.874  10.079  35.442  1.00 110.79 ? 102 ASP B CG  1 
ATOM   5122 O OD1 . ASP B 2 102 ? 47.382  9.533   36.458  1.00 115.75 ? 102 ASP B OD1 1 
ATOM   5123 O OD2 . ASP B 2 102 ? 47.213  10.795  34.650  1.00 116.05 ? 102 ASP B OD2 1 
ATOM   5124 N N   . GLY B 2 103 ? 51.741  7.079   35.318  1.00 87.83  ? 103 GLY B N   1 
ATOM   5125 C CA  . GLY B 2 103 ? 53.112  6.700   35.040  1.00 84.20  ? 103 GLY B CA  1 
ATOM   5126 C C   . GLY B 2 103 ? 53.313  6.418   33.555  1.00 80.07  ? 103 GLY B C   1 
ATOM   5127 O O   . GLY B 2 103 ? 52.360  6.375   32.787  1.00 79.45  ? 103 GLY B O   1 
ATOM   5128 N N   . LYS B 2 104 ? 54.575  6.239   33.170  1.00 79.74  ? 104 LYS B N   1 
ATOM   5129 C CA  . LYS B 2 104 ? 54.945  5.853   31.822  1.00 78.01  ? 104 LYS B CA  1 
ATOM   5130 C C   . LYS B 2 104 ? 54.342  4.484   31.512  1.00 71.88  ? 104 LYS B C   1 
ATOM   5131 O O   . LYS B 2 104 ? 54.139  3.684   32.420  1.00 67.89  ? 104 LYS B O   1 
ATOM   5132 C CB  . LYS B 2 104 ? 56.487  5.838   31.730  1.00 85.00  ? 104 LYS B CB  1 
ATOM   5133 C CG  . LYS B 2 104 ? 57.059  5.891   30.327  1.00 93.52  ? 104 LYS B CG  1 
ATOM   5134 C CD  . LYS B 2 104 ? 58.594  5.977   30.325  1.00 98.52  ? 104 LYS B CD  1 
ATOM   5135 C CE  . LYS B 2 104 ? 59.187  5.773   28.942  1.00 100.90 ? 104 LYS B CE  1 
ATOM   5136 N NZ  . LYS B 2 104 ? 60.671  5.911   28.946  1.00 102.27 ? 104 LYS B NZ  1 
ATOM   5137 N N   . ARG B 2 105 ? 54.039  4.236   30.229  1.00 70.00  ? 105 ARG B N   1 
ATOM   5138 C CA  . ARG B 2 105 ? 53.649  2.915   29.764  1.00 67.65  ? 105 ARG B CA  1 
ATOM   5139 C C   . ARG B 2 105 ? 54.896  2.109   29.427  1.00 62.99  ? 105 ARG B C   1 
ATOM   5140 O O   . ARG B 2 105 ? 55.911  2.673   29.033  1.00 65.26  ? 105 ARG B O   1 
ATOM   5141 C CB  . ARG B 2 105 ? 52.743  2.983   28.524  1.00 68.80  ? 105 ARG B CB  1 
ATOM   5142 C CG  . ARG B 2 105 ? 51.400  3.616   28.805  1.00 71.35  ? 105 ARG B CG  1 
ATOM   5143 C CD  . ARG B 2 105 ? 50.336  3.178   27.816  1.00 73.29  ? 105 ARG B CD  1 
ATOM   5144 N NE  . ARG B 2 105 ? 49.141  4.010   27.923  1.00 73.37  ? 105 ARG B NE  1 
ATOM   5145 C CZ  . ARG B 2 105 ? 47.910  3.564   28.148  1.00 74.33  ? 105 ARG B CZ  1 
ATOM   5146 N NH1 . ARG B 2 105 ? 47.686  2.370   28.679  1.00 73.66  ? 105 ARG B NH1 1 
ATOM   5147 N NH2 . ARG B 2 105 ? 46.875  4.344   27.843  1.00 74.81  ? 105 ARG B NH2 1 
ATOM   5148 N N   . TYR B 2 106 ? 54.792  0.787   29.575  1.00 57.87  ? 106 TYR B N   1 
ATOM   5149 C CA  . TYR B 2 106 ? 55.877  -0.118  29.254  1.00 58.10  ? 106 TYR B CA  1 
ATOM   5150 C C   . TYR B 2 106 ? 55.274  -1.311  28.519  1.00 57.98  ? 106 TYR B C   1 
ATOM   5151 O O   . TYR B 2 106 ? 54.509  -2.080  29.096  1.00 57.33  ? 106 TYR B O   1 
ATOM   5152 C CB  . TYR B 2 106 ? 56.621  -0.576  30.526  1.00 60.95  ? 106 TYR B CB  1 
ATOM   5153 C CG  . TYR B 2 106 ? 57.247  0.546   31.328  1.00 66.44  ? 106 TYR B CG  1 
ATOM   5154 C CD1 . TYR B 2 106 ? 58.426  1.155   30.911  1.00 68.77  ? 106 TYR B CD1 1 
ATOM   5155 C CD2 . TYR B 2 106 ? 56.650  1.011   32.497  1.00 69.46  ? 106 TYR B CD2 1 
ATOM   5156 C CE1 . TYR B 2 106 ? 59.003  2.194   31.641  1.00 70.67  ? 106 TYR B CE1 1 
ATOM   5157 C CE2 . TYR B 2 106 ? 57.216  2.049   33.236  1.00 70.78  ? 106 TYR B CE2 1 
ATOM   5158 C CZ  . TYR B 2 106 ? 58.391  2.641   32.804  1.00 74.71  ? 106 TYR B CZ  1 
ATOM   5159 O OH  . TYR B 2 106 ? 58.949  3.666   33.533  1.00 79.63  ? 106 TYR B OH  1 
ATOM   5160 N N   . CYS B 2 107 ? 55.627  -1.466  27.240  1.00 54.52  ? 107 CYS B N   1 
ATOM   5161 C CA  . CYS B 2 107 ? 55.074  -2.549  26.451  1.00 53.21  ? 107 CYS B CA  1 
ATOM   5162 C C   . CYS B 2 107 ? 56.099  -3.669  26.386  1.00 51.48  ? 107 CYS B C   1 
ATOM   5163 O O   . CYS B 2 107 ? 57.296  -3.415  26.253  1.00 52.41  ? 107 CYS B O   1 
ATOM   5164 C CB  . CYS B 2 107 ? 54.662  -2.076  25.061  1.00 53.80  ? 107 CYS B CB  1 
ATOM   5165 S SG  . CYS B 2 107 ? 53.595  -0.605  25.070  1.00 53.94  ? 107 CYS B SG  1 
ATOM   5166 N N   . SER B 2 108 ? 55.601  -4.903  26.471  1.00 48.43  ? 108 SER B N   1 
ATOM   5167 C CA  . SER B 2 108 ? 56.445  -6.077  26.386  1.00 47.68  ? 108 SER B CA  1 
ATOM   5168 C C   . SER B 2 108 ? 55.545  -7.295  26.238  1.00 48.24  ? 108 SER B C   1 
ATOM   5169 O O   . SER B 2 108 ? 54.564  -7.413  26.964  1.00 49.44  ? 108 SER B O   1 
ATOM   5170 C CB  . SER B 2 108 ? 57.320  -6.209  27.622  1.00 48.16  ? 108 SER B CB  1 
ATOM   5171 O OG  . SER B 2 108 ? 57.997  -7.457  27.627  1.00 49.17  ? 108 SER B OG  1 
ATOM   5172 N N   . GLY B 2 109 ? 55.874  -8.168  25.275  1.00 46.74  ? 109 GLY B N   1 
ATOM   5173 C CA  . GLY B 2 109 ? 55.159  -9.416  25.084  1.00 46.26  ? 109 GLY B CA  1 
ATOM   5174 C C   . GLY B 2 109 ? 53.780  -9.299  24.429  1.00 47.83  ? 109 GLY B C   1 
ATOM   5175 O O   . GLY B 2 109 ? 53.032  -10.275 24.395  1.00 49.60  ? 109 GLY B O   1 
ATOM   5176 N N   . GLY B 2 110 ? 53.458  -8.123  23.882  1.00 47.22  ? 110 GLY B N   1 
ATOM   5177 C CA  . GLY B 2 110 ? 52.193  -7.920  23.196  1.00 49.19  ? 110 GLY B CA  1 
ATOM   5178 C C   . GLY B 2 110 ? 51.123  -7.169  23.989  1.00 50.63  ? 110 GLY B C   1 
ATOM   5179 O O   . GLY B 2 110 ? 49.990  -7.065  23.539  1.00 51.33  ? 110 GLY B O   1 
ATOM   5180 N N   . TYR B 2 111 ? 51.483  -6.649  25.169  1.00 54.45  ? 111 TYR B N   1 
ATOM   5181 C CA  . TYR B 2 111 ? 50.602  -5.777  25.929  1.00 53.71  ? 111 TYR B CA  1 
ATOM   5182 C C   . TYR B 2 111 ? 51.423  -4.682  26.607  1.00 52.20  ? 111 TYR B C   1 
ATOM   5183 O O   . TYR B 2 111 ? 52.642  -4.680  26.489  1.00 53.24  ? 111 TYR B O   1 
ATOM   5184 C CB  . TYR B 2 111 ? 49.793  -6.589  26.945  1.00 53.28  ? 111 TYR B CB  1 
ATOM   5185 C CG  . TYR B 2 111 ? 48.545  -5.868  27.394  1.00 54.74  ? 111 TYR B CG  1 
ATOM   5186 C CD1 . TYR B 2 111 ? 47.473  -5.687  26.528  1.00 54.88  ? 111 TYR B CD1 1 
ATOM   5187 C CD2 . TYR B 2 111 ? 48.447  -5.334  28.674  1.00 54.96  ? 111 TYR B CD2 1 
ATOM   5188 C CE1 . TYR B 2 111 ? 46.332  -5.003  26.924  1.00 54.57  ? 111 TYR B CE1 1 
ATOM   5189 C CE2 . TYR B 2 111 ? 47.300  -4.662  29.088  1.00 57.17  ? 111 TYR B CE2 1 
ATOM   5190 C CZ  . TYR B 2 111 ? 46.242  -4.500  28.209  1.00 55.87  ? 111 TYR B CZ  1 
ATOM   5191 O OH  . TYR B 2 111 ? 45.105  -3.832  28.596  1.00 53.83  ? 111 TYR B OH  1 
ATOM   5192 N N   . CYS B 2 112 ? 50.745  -3.741  27.276  1.00 52.22  ? 112 CYS B N   1 
ATOM   5193 C CA  . CYS B 2 112 ? 51.402  -2.687  28.028  1.00 55.65  ? 112 CYS B CA  1 
ATOM   5194 C C   . CYS B 2 112 ? 50.863  -2.474  29.443  1.00 59.62  ? 112 CYS B C   1 
ATOM   5195 O O   . CYS B 2 112 ? 49.646  -2.411  29.641  1.00 57.53  ? 112 CYS B O   1 
ATOM   5196 C CB  . CYS B 2 112 ? 51.305  -1.410  27.223  1.00 58.19  ? 112 CYS B CB  1 
ATOM   5197 S SG  . CYS B 2 112 ? 51.688  -1.655  25.480  1.00 61.94  ? 112 CYS B SG  1 
ATOM   5198 N N   . TYR B 2 113 ? 51.804  -2.352  30.403  1.00 63.01  ? 113 TYR B N   1 
ATOM   5199 C CA  . TYR B 2 113 ? 51.533  -2.023  31.796  1.00 62.95  ? 113 TYR B CA  1 
ATOM   5200 C C   . TYR B 2 113 ? 52.175  -0.684  32.143  1.00 61.52  ? 113 TYR B C   1 
ATOM   5201 O O   . TYR B 2 113 ? 53.040  -0.210  31.414  1.00 61.54  ? 113 TYR B O   1 
ATOM   5202 C CB  . TYR B 2 113 ? 52.032  -3.127  32.755  1.00 66.01  ? 113 TYR B CB  1 
ATOM   5203 C CG  . TYR B 2 113 ? 53.520  -3.428  32.704  1.00 70.99  ? 113 TYR B CG  1 
ATOM   5204 C CD1 . TYR B 2 113 ? 54.449  -2.560  33.266  1.00 73.31  ? 113 TYR B CD1 1 
ATOM   5205 C CD2 . TYR B 2 113 ? 53.996  -4.592  32.113  1.00 75.33  ? 113 TYR B CD2 1 
ATOM   5206 C CE1 . TYR B 2 113 ? 55.814  -2.835  33.225  1.00 72.81  ? 113 TYR B CE1 1 
ATOM   5207 C CE2 . TYR B 2 113 ? 55.356  -4.876  32.063  1.00 75.99  ? 113 TYR B CE2 1 
ATOM   5208 C CZ  . TYR B 2 113 ? 56.263  -3.993  32.618  1.00 74.40  ? 113 TYR B CZ  1 
ATOM   5209 O OH  . TYR B 2 113 ? 57.600  -4.292  32.570  1.00 72.32  ? 113 TYR B OH  1 
ATOM   5210 N N   . ARG B 2 114 ? 51.705  -0.064  33.234  1.00 62.44  ? 114 ARG B N   1 
ATOM   5211 C CA  . ARG B 2 114 ? 52.337  1.115   33.809  1.00 61.52  ? 114 ARG B CA  1 
ATOM   5212 C C   . ARG B 2 114 ? 53.170  0.751   35.032  1.00 60.50  ? 114 ARG B C   1 
ATOM   5213 O O   . ARG B 2 114 ? 54.154  1.420   35.300  1.00 60.17  ? 114 ARG B O   1 
ATOM   5214 C CB  . ARG B 2 114 ? 51.312  2.192   34.215  1.00 63.73  ? 114 ARG B CB  1 
ATOM   5215 C CG  . ARG B 2 114 ? 51.223  3.360   33.244  1.00 66.05  ? 114 ARG B CG  1 
ATOM   5216 C CD  . ARG B 2 114 ? 50.186  4.398   33.637  1.00 66.29  ? 114 ARG B CD  1 
ATOM   5217 N NE  . ARG B 2 114 ? 48.992  4.314   32.806  1.00 71.79  ? 114 ARG B NE  1 
ATOM   5218 C CZ  . ARG B 2 114 ? 48.715  5.133   31.792  1.00 76.08  ? 114 ARG B CZ  1 
ATOM   5219 N NH1 . ARG B 2 114 ? 49.613  5.985   31.318  1.00 76.87  ? 114 ARG B NH1 1 
ATOM   5220 N NH2 . ARG B 2 114 ? 47.515  5.075   31.221  1.00 76.00  ? 114 ARG B NH2 1 
ATOM   5221 N N   . SER B 2 115 ? 52.755  -0.285  35.777  1.00 59.66  ? 115 SER B N   1 
ATOM   5222 C CA  . SER B 2 115 ? 53.486  -0.746  36.947  1.00 59.93  ? 115 SER B CA  1 
ATOM   5223 C C   . SER B 2 115 ? 53.495  -2.268  37.069  1.00 60.81  ? 115 SER B C   1 
ATOM   5224 O O   . SER B 2 115 ? 52.521  -2.948  36.743  1.00 54.48  ? 115 SER B O   1 
ATOM   5225 C CB  . SER B 2 115 ? 52.919  -0.152  38.242  1.00 60.45  ? 115 SER B CB  1 
ATOM   5226 O OG  . SER B 2 115 ? 53.411  1.156   38.492  1.00 59.37  ? 115 SER B OG  1 
ATOM   5227 N N   . ARG B 2 116 ? 54.626  -2.771  37.573  1.00 61.63  ? 116 ARG B N   1 
ATOM   5228 C CA  . ARG B 2 116 ? 54.828  -4.189  37.781  1.00 62.82  ? 116 ARG B CA  1 
ATOM   5229 C C   . ARG B 2 116 ? 55.519  -4.365  39.129  1.00 63.43  ? 116 ARG B C   1 
ATOM   5230 O O   . ARG B 2 116 ? 56.248  -3.476  39.573  1.00 58.52  ? 116 ARG B O   1 
ATOM   5231 C CB  . ARG B 2 116 ? 55.684  -4.773  36.659  1.00 63.32  ? 116 ARG B CB  1 
ATOM   5232 C CG  . ARG B 2 116 ? 55.790  -6.282  36.712  1.00 65.98  ? 116 ARG B CG  1 
ATOM   5233 C CD  . ARG B 2 116 ? 56.418  -6.823  35.457  1.00 69.37  ? 116 ARG B CD  1 
ATOM   5234 N NE  . ARG B 2 116 ? 57.783  -6.349  35.262  1.00 70.53  ? 116 ARG B NE  1 
ATOM   5235 C CZ  . ARG B 2 116 ? 58.561  -6.725  34.255  1.00 70.26  ? 116 ARG B CZ  1 
ATOM   5236 N NH1 . ARG B 2 116 ? 58.057  -7.259  33.156  1.00 70.25  ? 116 ARG B NH1 1 
ATOM   5237 N NH2 . ARG B 2 116 ? 59.875  -6.545  34.347  1.00 69.05  ? 116 ARG B NH2 1 
ATOM   5238 N N   . GLY B 2 117 ? 55.257  -5.513  39.770  1.00 62.01  ? 117 GLY B N   1 
ATOM   5239 C CA  . GLY B 2 117 ? 55.981  -5.908  40.962  1.00 61.18  ? 117 GLY B CA  1 
ATOM   5240 C C   . GLY B 2 117 ? 57.398  -6.325  40.594  1.00 60.18  ? 117 GLY B C   1 
ATOM   5241 O O   . GLY B 2 117 ? 57.821  -6.133  39.460  1.00 62.88  ? 117 GLY B O   1 
ATOM   5242 N N   . GLN B 2 118 ? 58.126  -6.860  41.577  1.00 61.54  ? 118 GLN B N   1 
ATOM   5243 C CA  . GLN B 2 118 ? 59.499  -7.305  41.389  1.00 62.74  ? 118 GLN B CA  1 
ATOM   5244 C C   . GLN B 2 118 ? 59.522  -8.763  40.934  1.00 61.82  ? 118 GLN B C   1 
ATOM   5245 O O   . GLN B 2 118 ? 60.532  -9.238  40.419  1.00 59.14  ? 118 GLN B O   1 
ATOM   5246 C CB  . GLN B 2 118 ? 60.300  -7.113  42.690  1.00 66.39  ? 118 GLN B CB  1 
ATOM   5247 C CG  . GLN B 2 118 ? 59.981  -8.120  43.827  1.00 70.50  ? 118 GLN B CG  1 
ATOM   5248 C CD  . GLN B 2 118 ? 58.588  -7.990  44.443  1.00 75.21  ? 118 GLN B CD  1 
ATOM   5249 O OE1 . GLN B 2 118 ? 57.850  -6.997  44.248  1.00 75.65  ? 118 GLN B OE1 1 
ATOM   5250 N NE2 . GLN B 2 118 ? 58.206  -8.997  45.228  1.00 76.01  ? 118 GLN B NE2 1 
ATOM   5251 N N   . GLY B 2 119 ? 58.409  -9.470  41.187  1.00 60.86  ? 119 GLY B N   1 
ATOM   5252 C CA  . GLY B 2 119 ? 58.137  -10.763 40.584  1.00 62.60  ? 119 GLY B CA  1 
ATOM   5253 C C   . GLY B 2 119 ? 58.729  -11.919 41.375  1.00 64.65  ? 119 GLY B C   1 
ATOM   5254 O O   . GLY B 2 119 ? 59.881  -11.844 41.785  1.00 70.98  ? 119 GLY B O   1 
ATOM   5255 N N   . THR B 2 120 ? 57.931  -12.977 41.573  1.00 68.00  ? 120 THR B N   1 
ATOM   5256 C CA  . THR B 2 120 ? 58.332  -14.116 42.385  1.00 68.58  ? 120 THR B CA  1 
ATOM   5257 C C   . THR B 2 120 ? 58.588  -15.315 41.483  1.00 65.57  ? 120 THR B C   1 
ATOM   5258 O O   . THR B 2 120 ? 57.814  -15.557 40.561  1.00 69.39  ? 120 THR B O   1 
ATOM   5259 C CB  . THR B 2 120 ? 57.266  -14.465 43.442  1.00 72.61  ? 120 THR B CB  1 
ATOM   5260 O OG1 . THR B 2 120 ? 57.831  -15.410 44.370  1.00 72.70  ? 120 THR B OG1 1 
ATOM   5261 C CG2 . THR B 2 120 ? 55.965  -15.031 42.818  1.00 71.97  ? 120 THR B CG2 1 
ATOM   5262 N N   . LEU B 2 121 ? 59.660  -16.056 41.784  1.00 60.15  ? 121 LEU B N   1 
ATOM   5263 C CA  . LEU B 2 121 ? 60.051  -17.219 41.008  1.00 59.53  ? 121 LEU B CA  1 
ATOM   5264 C C   . LEU B 2 121 ? 59.346  -18.480 41.503  1.00 61.48  ? 121 LEU B C   1 
ATOM   5265 O O   . LEU B 2 121 ? 59.345  -18.758 42.699  1.00 69.01  ? 121 LEU B O   1 
ATOM   5266 C CB  . LEU B 2 121 ? 61.580  -17.380 41.065  1.00 57.23  ? 121 LEU B CB  1 
ATOM   5267 C CG  . LEU B 2 121 ? 62.177  -18.659 40.466  1.00 59.02  ? 121 LEU B CG  1 
ATOM   5268 C CD1 . LEU B 2 121 ? 61.773  -18.871 39.009  1.00 58.22  ? 121 LEU B CD1 1 
ATOM   5269 C CD2 . LEU B 2 121 ? 63.694  -18.629 40.534  1.00 59.95  ? 121 LEU B CD2 1 
ATOM   5270 N N   . VAL B 2 122 ? 58.743  -19.216 40.561  1.00 61.73  ? 122 VAL B N   1 
ATOM   5271 C CA  . VAL B 2 122 ? 58.185  -20.544 40.775  1.00 63.84  ? 122 VAL B CA  1 
ATOM   5272 C C   . VAL B 2 122 ? 58.931  -21.541 39.895  1.00 64.85  ? 122 VAL B C   1 
ATOM   5273 O O   . VAL B 2 122 ? 59.066  -21.328 38.695  1.00 66.11  ? 122 VAL B O   1 
ATOM   5274 C CB  . VAL B 2 122 ? 56.673  -20.599 40.413  1.00 66.58  ? 122 VAL B CB  1 
ATOM   5275 C CG1 . VAL B 2 122 ? 56.163  -22.044 40.338  1.00 66.08  ? 122 VAL B CG1 1 
ATOM   5276 C CG2 . VAL B 2 122 ? 55.826  -19.754 41.367  1.00 67.15  ? 122 VAL B CG2 1 
ATOM   5277 N N   . THR B 2 123 ? 59.384  -22.649 40.483  1.00 68.26  ? 123 THR B N   1 
ATOM   5278 C CA  . THR B 2 123 ? 60.035  -23.700 39.719  1.00 67.83  ? 123 THR B CA  1 
ATOM   5279 C C   . THR B 2 123 ? 59.214  -24.979 39.850  1.00 67.44  ? 123 THR B C   1 
ATOM   5280 O O   . THR B 2 123 ? 58.884  -25.392 40.966  1.00 61.98  ? 123 THR B O   1 
ATOM   5281 C CB  . THR B 2 123 ? 61.492  -23.848 40.173  1.00 68.72  ? 123 THR B CB  1 
ATOM   5282 O OG1 . THR B 2 123 ? 62.130  -22.570 40.026  1.00 68.17  ? 123 THR B OG1 1 
ATOM   5283 C CG2 . THR B 2 123 ? 62.250  -24.924 39.378  1.00 67.97  ? 123 THR B CG2 1 
ATOM   5284 N N   . VAL B 2 124 ? 58.874  -25.576 38.697  1.00 68.04  ? 124 VAL B N   1 
ATOM   5285 C CA  . VAL B 2 124 ? 58.108  -26.812 38.662  1.00 68.90  ? 124 VAL B CA  1 
ATOM   5286 C C   . VAL B 2 124 ? 58.975  -27.932 38.104  1.00 69.43  ? 124 VAL B C   1 
ATOM   5287 O O   . VAL B 2 124 ? 58.884  -28.259 36.928  1.00 65.60  ? 124 VAL B O   1 
ATOM   5288 C CB  . VAL B 2 124 ? 56.796  -26.655 37.861  1.00 68.74  ? 124 VAL B CB  1 
ATOM   5289 C CG1 . VAL B 2 124 ? 56.021  -27.969 37.801  1.00 69.27  ? 124 VAL B CG1 1 
ATOM   5290 C CG2 . VAL B 2 124 ? 55.926  -25.544 38.439  1.00 68.45  ? 124 VAL B CG2 1 
ATOM   5291 N N   . SER B 2 125 ? 59.813  -28.510 38.972  1.00 81.05  ? 125 SER B N   1 
ATOM   5292 C CA  . SER B 2 125 ? 60.727  -29.578 38.587  1.00 88.76  ? 125 SER B CA  1 
ATOM   5293 C C   . SER B 2 125 ? 60.235  -30.944 39.057  1.00 89.02  ? 125 SER B C   1 
ATOM   5294 O O   . SER B 2 125 ? 59.876  -31.108 40.223  1.00 85.11  ? 125 SER B O   1 
ATOM   5295 C CB  . SER B 2 125 ? 62.124  -29.328 39.151  1.00 90.87  ? 125 SER B CB  1 
ATOM   5296 O OG  . SER B 2 125 ? 62.991  -30.427 38.907  1.00 91.16  ? 125 SER B OG  1 
ATOM   5297 N N   . SER B 2 126 ? 60.236  -31.914 38.136  1.00 91.11  ? 126 SER B N   1 
ATOM   5298 C CA  . SER B 2 126 ? 59.892  -33.285 38.471  1.00 94.57  ? 126 SER B CA  1 
ATOM   5299 C C   . SER B 2 126 ? 60.820  -33.801 39.564  1.00 96.81  ? 126 SER B C   1 
ATOM   5300 O O   . SER B 2 126 ? 60.347  -34.240 40.604  1.00 96.15  ? 126 SER B O   1 
ATOM   5301 C CB  . SER B 2 126 ? 59.954  -34.181 37.242  1.00 93.96  ? 126 SER B CB  1 
ATOM   5302 O OG  . SER B 2 126 ? 59.344  -35.432 37.512  1.00 93.03  ? 126 SER B OG  1 
ATOM   5303 O OXT . SER B 2 126 ? 62.041  -33.744 39.422  1.00 100.11 ? 126 SER B OXT 1 
HETATM 5304 O O   . HOH C 3 .   ? 15.366  1.684   3.084   1.00 82.65  ? 601 HOH A O   1 
HETATM 5305 O O   . HOH C 3 .   ? 57.512  -7.883  18.678  1.00 42.52  ? 602 HOH A O   1 
HETATM 5306 O O   . HOH C 3 .   ? 12.210  28.931  -5.076  1.00 57.10  ? 603 HOH A O   1 
HETATM 5307 O O   . HOH C 3 .   ? 28.665  7.982   29.028  1.00 54.74  ? 604 HOH A O   1 
HETATM 5308 O O   . HOH C 3 .   ? 23.127  2.737   3.904   1.00 63.81  ? 605 HOH A O   1 
HETATM 5309 O O   . HOH C 3 .   ? -2.966  17.680  -6.293  1.00 52.37  ? 606 HOH A O   1 
HETATM 5310 O O   . HOH C 3 .   ? 40.203  -6.156  27.891  1.00 48.29  ? 607 HOH A O   1 
HETATM 5311 O O   . HOH C 3 .   ? -6.683  23.928  -13.513 1.00 72.82  ? 608 HOH A O   1 
HETATM 5312 O O   . HOH C 3 .   ? 36.590  20.020  -16.021 1.00 68.29  ? 609 HOH A O   1 
HETATM 5313 O O   . HOH C 3 .   ? 0.674   31.801  -3.040  1.00 59.77  ? 610 HOH A O   1 
HETATM 5314 O O   . HOH C 3 .   ? 36.450  16.847  -9.854  1.00 46.16  ? 611 HOH A O   1 
HETATM 5315 O O   . HOH C 3 .   ? 32.558  18.996  16.616  1.00 55.55  ? 612 HOH A O   1 
HETATM 5316 O O   . HOH C 3 .   ? 7.884   -11.073 3.995   1.00 88.76  ? 613 HOH A O   1 
HETATM 5317 O O   . HOH C 3 .   ? 32.009  18.350  -3.081  1.00 47.05  ? 614 HOH A O   1 
HETATM 5318 O O   . HOH C 3 .   ? 50.719  0.592   7.782   1.00 64.47  ? 615 HOH A O   1 
HETATM 5319 O O   . HOH C 3 .   ? 48.951  7.792   6.875   1.00 60.23  ? 616 HOH A O   1 
HETATM 5320 O O   . HOH C 3 .   ? 47.908  16.266  34.633  1.00 69.15  ? 617 HOH A O   1 
HETATM 5321 O O   . HOH C 3 .   ? 1.364   -3.491  29.950  1.00 80.86  ? 618 HOH A O   1 
HETATM 5322 O O   . HOH C 3 .   ? 37.172  11.865  37.316  1.00 78.95  ? 619 HOH A O   1 
HETATM 5323 O O   . HOH C 3 .   ? 12.344  41.035  -17.567 1.00 57.14  ? 620 HOH A O   1 
HETATM 5324 O O   . HOH C 3 .   ? -1.297  24.427  -1.460  1.00 53.12  ? 621 HOH A O   1 
HETATM 5325 O O   . HOH C 3 .   ? 21.582  8.447   12.517  1.00 75.58  ? 622 HOH A O   1 
HETATM 5326 O O   . HOH C 3 .   ? 21.007  11.177  7.037   1.00 54.29  ? 623 HOH A O   1 
HETATM 5327 O O   . HOH C 3 .   ? 26.614  0.653   23.607  1.00 65.11  ? 624 HOH A O   1 
HETATM 5328 O O   . HOH C 3 .   ? 67.839  11.166  20.459  1.00 74.80  ? 625 HOH A O   1 
HETATM 5329 O O   . HOH C 3 .   ? 23.854  27.252  16.347  1.00 57.78  ? 626 HOH A O   1 
HETATM 5330 O O   . HOH C 3 .   ? 6.870   44.317  -15.823 1.00 68.81  ? 627 HOH A O   1 
HETATM 5331 O O   . HOH C 3 .   ? 9.744   20.945  2.881   1.00 58.67  ? 628 HOH A O   1 
HETATM 5332 O O   . HOH C 3 .   ? 66.342  8.183   19.070  1.00 61.52  ? 629 HOH A O   1 
HETATM 5333 O O   . HOH C 3 .   ? 19.181  38.710  -22.868 1.00 64.67  ? 630 HOH A O   1 
HETATM 5334 O O   . HOH C 3 .   ? 19.135  10.053  -0.595  1.00 64.25  ? 631 HOH A O   1 
HETATM 5335 O O   . HOH C 3 .   ? 33.455  33.927  7.554   1.00 76.09  ? 632 HOH A O   1 
HETATM 5336 O O   . HOH C 3 .   ? 5.222   15.080  -10.484 1.00 67.57  ? 633 HOH A O   1 
HETATM 5337 O O   . HOH C 3 .   ? 12.512  -3.200  34.496  1.00 86.33  ? 634 HOH A O   1 
HETATM 5338 O O   . HOH C 3 .   ? 41.491  26.228  10.997  1.00 72.42  ? 635 HOH A O   1 
HETATM 5339 O O   . HOH C 3 .   ? 18.486  29.739  9.988   1.00 55.52  ? 636 HOH A O   1 
HETATM 5340 O O   . HOH C 3 .   ? 11.588  -5.530  29.035  1.00 73.69  ? 637 HOH A O   1 
HETATM 5341 O O   . HOH C 3 .   ? 20.966  -23.012 -6.272  1.00 88.38  ? 638 HOH A O   1 
HETATM 5342 O O   . HOH C 3 .   ? 34.734  -2.111  -3.746  1.00 76.65  ? 639 HOH A O   1 
HETATM 5343 O O   . HOH C 3 .   ? 41.992  6.684   34.042  1.00 71.63  ? 640 HOH A O   1 
HETATM 5344 O O   . HOH C 3 .   ? -9.384  -4.845  14.547  1.00 91.23  ? 641 HOH A O   1 
HETATM 5345 O O   . HOH C 3 .   ? 3.126   4.253   11.037  1.00 84.12  ? 642 HOH A O   1 
HETATM 5346 O O   . HOH C 3 .   ? 45.694  15.897  22.726  1.00 87.81  ? 643 HOH A O   1 
HETATM 5347 O O   . HOH C 3 .   ? 30.402  -32.452 21.190  1.00 89.08  ? 644 HOH A O   1 
HETATM 5348 O O   . HOH C 3 .   ? 1.606   -1.630  3.798   1.00 91.09  ? 645 HOH A O   1 
HETATM 5349 O O   . HOH C 3 .   ? 4.507   -23.266 -1.577  1.00 86.49  ? 646 HOH A O   1 
HETATM 5350 O O   . HOH C 3 .   ? 15.372  -6.123  -4.735  1.00 73.86  ? 647 HOH A O   1 
HETATM 5351 O O   . HOH C 3 .   ? 1.761   -5.698  -2.196  1.00 70.80  ? 648 HOH A O   1 
HETATM 5352 O O   . HOH D 3 .   ? 62.451  -21.400 28.357  1.00 80.30  ? 201 HOH B O   1 
HETATM 5353 O O   . HOH D 3 .   ? 63.290  -35.364 37.721  0.50 72.42  ? 202 HOH B O   1 
HETATM 5354 O O   . HOH D 3 .   ? 56.985  -1.145  37.722  1.00 57.99  ? 203 HOH B O   1 
HETATM 5355 O O   . HOH D 3 .   ? 53.718  9.881   36.454  1.00 83.91  ? 204 HOH B O   1 
HETATM 5356 O O   . HOH D 3 .   ? 45.712  -32.675 34.192  1.00 74.74  ? 205 HOH B O   1 
# 
